CNRS Nantes University US2B US2B
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Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.


***  6GHV  ***

elNémo ID: 2602120904031230012

Job options:

ID        	=	 2602120904031230012
JOBID     	=	 6GHV
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 6GHV

data_6GHV
# 
_entry.id   6GHV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   6GHV         pdb_00006ghv 10.2210/pdb6ghv/pdb 
WWPDB D_1200009734 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2019-09-11 
2 'Structure model' 1 1 2019-11-27 
3 'Structure model' 1 2 2024-01-17 
4 'Structure model' 1 3 2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Derived calculations'   
5 3 'Structure model' 'Refinement description' 
6 4 'Structure model' 'Structure summary'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation                      
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' pdbx_initial_refinement_model 
6 3 'Structure model' pdbx_struct_conn_angle        
7 3 'Structure model' struct_conn                   
8 4 'Structure model' pdbx_entry_details            
9 4 'Structure model' pdbx_modification_feature     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.journal_volume'                    
2  2 'Structure model' '_citation.page_first'                        
3  2 'Structure model' '_citation.page_last'                         
4  2 'Structure model' '_citation.title'                             
5  3 'Structure model' '_database_2.pdbx_DOI'                        
6  3 'Structure model' '_database_2.pdbx_database_accession'         
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_symmetry'      
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
19 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
20 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
21 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
22 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
23 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
24 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_symmetry'      
25 3 'Structure model' '_pdbx_struct_conn_angle.value'               
26 3 'Structure model' '_struct_conn.pdbx_dist_value'                
27 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
28 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
29 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
30 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
31 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
32 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
33 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
34 3 'Structure model' '_struct_conn.ptnr1_symmetry'                 
35 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
36 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
37 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
38 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
39 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
40 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
41 3 'Structure model' '_struct_conn.ptnr2_symmetry'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6GHV 
_pdbx_database_status.recvd_initial_deposition_date   2018-05-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thepaut, M.'  1 ? 
'Achilli, S.'  2 ? 
'Medve, L.'    3 ? 
'Bernardi, A.' 4 ? 
'Fieschi, F.'  5 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistry 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           0947-6539 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            25 
_citation.language                  ? 
_citation.page_first                14659 
_citation.page_last                 14668 
_citation.title                     
'Enhancing Potency and Selectivity of a DC-SIGN Glycomimetic Ligand by Fragment-Based Design: Structural Basis.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/chem.201903391 
_citation.pdbx_database_id_PubMed   31469191 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Medve, L.'             1  ? 
primary 'Achilli, S.'           2  ? 
primary 'Guzman-Caldentey, J.'  3  ? 
primary 'Thepaut, M.'           4  ? 
primary 'Senaldi, L.'           5  ? 
primary 'Le Roy, A.'            6  ? 
primary 'Sattin, S.'            7  ? 
primary 'Ebel, C.'              8  ? 
primary 'Vives, C.'             9  ? 
primary 'Martin-Santamaria, S.' 10 ? 
primary 'Bernardi, A.'          11 ? 
primary 'Fieschi, F.'           12 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'CD209 antigen' 17746.582 6   ? ? ? ? 
2 non-polymer syn 
;[1-[(2~{S},3~{S},4~{R},5~{S},6~{R})-2-[(1~{S},2~{S},4~{S},5~{S})-2-(2-chloroethyloxy)-4,5-bis[[4-(hydroxymethyl)phenyl]methylcarbamoyl]cyclohexyl]oxy-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-3-yl]-1,2,3-triazol-4-yl]methylazanium
;
748.243   6   ? ? ? ? 
3 non-polymer nat 'CALCIUM ION' 40.078    18  ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION' 35.453    14  ? ? ? ? 
5 water       nat water 18.015    660 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'C-type lectin domain family 4 member L,Dendritic cell-specific ICAM-3-grabbing non-integrin 1,DC-SIGN1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQW
VDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQW
VDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;[1-[(2~{S},3~{S},4~{R},5~{S},6~{R})-2-[(1~{S},2~{S},4~{S},5~{S})-2-(2-chloroethyloxy)-4,5-bis[[4-(hydroxymethyl)phenyl]methylcarbamoyl]cyclohexyl]oxy-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-3-yl]-1,2,3-triazol-4-yl]methylazanium
;
EZ8 
3 'CALCIUM ION' CA  
4 'CHLORIDE ION' CL  
5 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   ARG n 
1 3   LEU n 
1 4   CYS n 
1 5   HIS n 
1 6   PRO n 
1 7   CYS n 
1 8   PRO n 
1 9   TRP n 
1 10  GLU n 
1 11  TRP n 
1 12  THR n 
1 13  PHE n 
1 14  PHE n 
1 15  GLN n 
1 16  GLY n 
1 17  ASN n 
1 18  CYS n 
1 19  TYR n 
1 20  PHE n 
1 21  MET n 
1 22  SER n 
1 23  ASN n 
1 24  SER n 
1 25  GLN n 
1 26  ARG n 
1 27  ASN n 
1 28  TRP n 
1 29  HIS n 
1 30  ASP n 
1 31  SER n 
1 32  ILE n 
1 33  THR n 
1 34  ALA n 
1 35  CYS n 
1 36  LYS n 
1 37  GLU n 
1 38  VAL n 
1 39  GLY n 
1 40  ALA n 
1 41  GLN n 
1 42  LEU n 
1 43  VAL n 
1 44  VAL n 
1 45  ILE n 
1 46  LYS n 
1 47  SER n 
1 48  ALA n 
1 49  GLU n 
1 50  GLU n 
1 51  GLN n 
1 52  ASN n 
1 53  PHE n 
1 54  LEU n 
1 55  GLN n 
1 56  LEU n 
1 57  GLN n 
1 58  SER n 
1 59  SER n 
1 60  ARG n 
1 61  SER n 
1 62  ASN n 
1 63  ARG n 
1 64  PHE n 
1 65  THR n 
1 66  TRP n 
1 67  MET n 
1 68  GLY n 
1 69  LEU n 
1 70  SER n 
1 71  ASP n 
1 72  LEU n 
1 73  ASN n 
1 74  GLN n 
1 75  GLU n 
1 76  GLY n 
1 77  THR n 
1 78  TRP n 
1 79  GLN n 
1 80  TRP n 
1 81  VAL n 
1 82  ASP n 
1 83  GLY n 
1 84  SER n 
1 85  PRO n 
1 86  LEU n 
1 87  LEU n 
1 88  PRO n 
1 89  SER n 
1 90  PHE n 
1 91  LYS n 
1 92  GLN n 
1 93  TYR n 
1 94  TRP n 
1 95  ASN n 
1 96  ARG n 
1 97  GLY n 
1 98  GLU n 
1 99  PRO n 
1 100 ASN n 
1 101 ASN n 
1 102 VAL n 
1 103 GLY n 
1 104 GLU n 
1 105 GLU n 
1 106 ASP n 
1 107 CYS n 
1 108 ALA n 
1 109 GLU n 
1 110 PHE n 
1 111 SER n 
1 112 GLY n 
1 113 ASN n 
1 114 GLY n 
1 115 TRP n 
1 116 ASN n 
1 117 ASP n 
1 118 ASP n 
1 119 LYS n 
1 120 CYS n 
1 121 ASN n 
1 122 LEU n 
1 123 ALA n 
1 124 LYS n 
1 125 PHE n 
1 126 TRP n 
1 127 ILE n 
1 128 CYS n 
1 129 LYS n 
1 130 LYS n 
1 131 SER n 
1 132 ALA n 
1 133 ALA n 
1 134 SER n 
1 135 CYS n 
1 136 SER n 
1 137 ARG n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 GLN n 
1 142 PHE n 
1 143 LEU n 
1 144 SER n 
1 145 PRO n 
1 146 ALA n 
1 147 PRO n 
1 148 ALA n 
1 149 THR n 
1 150 PRO n 
1 151 ASN n 
1 152 PRO n 
1 153 PRO n 
1 154 PRO n 
1 155 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   155 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CD209, CLEC4L' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET30 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'          133.103 
CA  non-polymer         . 'CALCIUM ION' ? 'Ca 2'                40.078  
CL  non-polymer         . 'CHLORIDE ION' ? 'Cl -1'               35.453  
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
EZ8 non-polymer         . 
;[1-[(2~{S},3~{S},4~{R},5~{S},6~{R})-2-[(1~{S},2~{S},4~{S},5~{S})-2-(2-chloroethyloxy)-4,5-bis[[4-(hydroxymethyl)phenyl]methylcarbamoyl]cyclohexyl]oxy-6-(hydroxymethyl)-4,5-bis(oxidanyl)oxan-3-yl]-1,2,3-triazol-4-yl]methylazanium
;
? 'C35 H48 Cl N6 O10 1' 748.243 
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLU 1   250 ?   ?   ?   A . n 
A 1 2   ARG 2   251 ?   ?   ?   A . n 
A 1 3   LEU 3   252 ?   ?   ?   A . n 
A 1 4   CYS 4   253 253 CYS CYS A . n 
A 1 5   HIS 5   254 254 HIS HIS A . n 
A 1 6   PRO 6   255 255 PRO PRO A . n 
A 1 7   CYS 7   256 256 CYS CYS A . n 
A 1 8   PRO 8   257 257 PRO PRO A . n 
A 1 9   TRP 9   258 258 TRP TRP A . n 
A 1 10  GLU 10  259 259 GLU GLU A . n 
A 1 11  TRP 11  260 260 TRP TRP A . n 
A 1 12  THR 12  261 261 THR THR A . n 
A 1 13  PHE 13  262 262 PHE PHE A . n 
A 1 14  PHE 14  263 263 PHE PHE A . n 
A 1 15  GLN 15  264 264 GLN GLN A . n 
A 1 16  GLY 16  265 265 GLY GLY A . n 
A 1 17  ASN 17  266 266 ASN ASN A . n 
A 1 18  CYS 18  267 267 CYS CYS A . n 
A 1 19  TYR 19  268 268 TYR TYR A . n 
A 1 20  PHE 20  269 269 PHE PHE A . n 
A 1 21  MET 21  270 270 MET MET A . n 
A 1 22  SER 22  271 271 SER SER A . n 
A 1 23  ASN 23  272 272 ASN ASN A . n 
A 1 24  SER 24  273 273 SER SER A . n 
A 1 25  GLN 25  274 274 GLN GLN A . n 
A 1 26  ARG 26  275 275 ARG ARG A . n 
A 1 27  ASN 27  276 276 ASN ASN A . n 
A 1 28  TRP 28  277 277 TRP TRP A . n 
A 1 29  HIS 29  278 278 HIS HIS A . n 
A 1 30  ASP 30  279 279 ASP ASP A . n 
A 1 31  SER 31  280 280 SER SER A . n 
A 1 32  ILE 32  281 281 ILE ILE A . n 
A 1 33  THR 33  282 282 THR THR A . n 
A 1 34  ALA 34  283 283 ALA ALA A . n 
A 1 35  CYS 35  284 284 CYS CYS A . n 
A 1 36  LYS 36  285 285 LYS LYS A . n 
A 1 37  GLU 37  286 286 GLU GLU A . n 
A 1 38  VAL 38  287 287 VAL VAL A . n 
A 1 39  GLY 39  288 288 GLY GLY A . n 
A 1 40  ALA 40  289 289 ALA ALA A . n 
A 1 41  GLN 41  290 290 GLN GLN A . n 
A 1 42  LEU 42  291 291 LEU LEU A . n 
A 1 43  VAL 43  292 292 VAL VAL A . n 
A 1 44  VAL 44  293 293 VAL VAL A . n 
A 1 45  ILE 45  294 294 ILE ILE A . n 
A 1 46  LYS 46  295 295 LYS LYS A . n 
A 1 47  SER 47  296 296 SER SER A . n 
A 1 48  ALA 48  297 297 ALA ALA A . n 
A 1 49  GLU 49  298 298 GLU GLU A . n 
A 1 50  GLU 50  299 299 GLU GLU A . n 
A 1 51  GLN 51  300 300 GLN GLN A . n 
A 1 52  ASN 52  301 301 ASN ASN A . n 
A 1 53  PHE 53  302 302 PHE PHE A . n 
A 1 54  LEU 54  303 303 LEU LEU A . n 
A 1 55  GLN 55  304 304 GLN GLN A . n 
A 1 56  LEU 56  305 305 LEU LEU A . n 
A 1 57  GLN 57  306 306 GLN GLN A . n 
A 1 58  SER 58  307 307 SER SER A . n 
A 1 59  SER 59  308 308 SER SER A . n 
A 1 60  ARG 60  309 309 ARG ARG A . n 
A 1 61  SER 61  310 310 SER SER A . n 
A 1 62  ASN 62  311 311 ASN ASN A . n 
A 1 63  ARG 63  312 312 ARG ARG A . n 
A 1 64  PHE 64  313 313 PHE PHE A . n 
A 1 65  THR 65  314 314 THR THR A . n 
A 1 66  TRP 66  315 315 TRP TRP A . n 
A 1 67  MET 67  316 316 MET MET A . n 
A 1 68  GLY 68  317 317 GLY GLY A . n 
A 1 69  LEU 69  318 318 LEU LEU A . n 
A 1 70  SER 70  319 319 SER SER A . n 
A 1 71  ASP 71  320 320 ASP ASP A . n 
A 1 72  LEU 72  321 321 LEU LEU A . n 
A 1 73  ASN 73  322 322 ASN ASN A . n 
A 1 74  GLN 74  323 323 GLN GLN A . n 
A 1 75  GLU 75  324 324 GLU GLU A . n 
A 1 76  GLY 76  325 325 GLY GLY A . n 
A 1 77  THR 77  326 326 THR THR A . n 
A 1 78  TRP 78  327 327 TRP TRP A . n 
A 1 79  GLN 79  328 328 GLN GLN A . n 
A 1 80  TRP 80  329 329 TRP TRP A . n 
A 1 81  VAL 81  330 330 VAL VAL A . n 
A 1 82  ASP 82  331 331 ASP ASP A . n 
A 1 83  GLY 83  332 332 GLY GLY A . n 
A 1 84  SER 84  333 333 SER SER A . n 
A 1 85  PRO 85  334 334 PRO PRO A . n 
A 1 86  LEU 86  335 335 LEU LEU A . n 
A 1 87  LEU 87  336 336 LEU LEU A . n 
A 1 88  PRO 88  337 337 PRO PRO A . n 
A 1 89  SER 89  338 338 SER SER A . n 
A 1 90  PHE 90  339 339 PHE PHE A . n 
A 1 91  LYS 91  340 340 LYS LYS A . n 
A 1 92  GLN 92  341 341 GLN GLN A . n 
A 1 93  TYR 93  342 342 TYR TYR A . n 
A 1 94  TRP 94  343 343 TRP TRP A . n 
A 1 95  ASN 95  344 344 ASN ASN A . n 
A 1 96  ARG 96  345 345 ARG ARG A . n 
A 1 97  GLY 97  346 346 GLY GLY A . n 
A 1 98  GLU 98  347 347 GLU GLU A . n 
A 1 99  PRO 99  348 348 PRO PRO A . n 
A 1 100 ASN 100 349 349 ASN ASN A . n 
A 1 101 ASN 101 350 350 ASN ASN A . n 
A 1 102 VAL 102 351 351 VAL VAL A . n 
A 1 103 GLY 103 352 352 GLY GLY A . n 
A 1 104 GLU 104 353 353 GLU GLU A . n 
A 1 105 GLU 105 354 354 GLU GLU A . n 
A 1 106 ASP 106 355 355 ASP ASP A . n 
A 1 107 CYS 107 356 356 CYS CYS A . n 
A 1 108 ALA 108 357 357 ALA ALA A . n 
A 1 109 GLU 109 358 358 GLU GLU A . n 
A 1 110 PHE 110 359 359 PHE PHE A . n 
A 1 111 SER 111 360 360 SER SER A . n 
A 1 112 GLY 112 361 361 GLY GLY A . n 
A 1 113 ASN 113 362 362 ASN ASN A . n 
A 1 114 GLY 114 363 363 GLY GLY A . n 
A 1 115 TRP 115 364 364 TRP TRP A . n 
A 1 116 ASN 116 365 365 ASN ASN A . n 
A 1 117 ASP 117 366 366 ASP ASP A . n 
A 1 118 ASP 118 367 367 ASP ASP A . n 
A 1 119 LYS 119 368 368 LYS LYS A . n 
A 1 120 CYS 120 369 369 CYS CYS A . n 
A 1 121 ASN 121 370 370 ASN ASN A . n 
A 1 122 LEU 122 371 371 LEU LEU A . n 
A 1 123 ALA 123 372 372 ALA ALA A . n 
A 1 124 LYS 124 373 373 LYS LYS A . n 
A 1 125 PHE 125 374 374 PHE PHE A . n 
A 1 126 TRP 126 375 375 TRP TRP A . n 
A 1 127 ILE 127 376 376 ILE ILE A . n 
A 1 128 CYS 128 377 377 CYS CYS A . n 
A 1 129 LYS 129 378 378 LYS LYS A . n 
A 1 130 LYS 130 379 379 LYS LYS A . n 
A 1 131 SER 131 380 380 SER SER A . n 
A 1 132 ALA 132 381 381 ALA ALA A . n 
A 1 133 ALA 133 382 382 ALA ALA A . n 
A 1 134 SER 134 383 383 SER SER A . n 
A 1 135 CYS 135 384 384 CYS CYS A . n 
A 1 136 SER 136 385 ?   ?   ?   A . n 
A 1 137 ARG 137 386 ?   ?   ?   A . n 
A 1 138 ASP 138 387 ?   ?   ?   A . n 
A 1 139 GLU 139 388 ?   ?   ?   A . n 
A 1 140 GLU 140 389 ?   ?   ?   A . n 
A 1 141 GLN 141 390 ?   ?   ?   A . n 
A 1 142 PHE 142 391 ?   ?   ?   A . n 
A 1 143 LEU 143 392 ?   ?   ?   A . n 
A 1 144 SER 144 393 ?   ?   ?   A . n 
A 1 145 PRO 145 394 ?   ?   ?   A . n 
A 1 146 ALA 146 395 ?   ?   ?   A . n 
A 1 147 PRO 147 396 ?   ?   ?   A . n 
A 1 148 ALA 148 397 ?   ?   ?   A . n 
A 1 149 THR 149 398 ?   ?   ?   A . n 
A 1 150 PRO 150 399 ?   ?   ?   A . n 
A 1 151 ASN 151 400 ?   ?   ?   A . n 
A 1 152 PRO 152 401 ?   ?   ?   A . n 
A 1 153 PRO 153 402 ?   ?   ?   A . n 
A 1 154 PRO 154 403 ?   ?   ?   A . n 
A 1 155 ALA 155 404 ?   ?   ?   A . n 
B 1 1   GLU 1   250 ?   ?   ?   B . n 
B 1 2   ARG 2   251 ?   ?   ?   B . n 
B 1 3   LEU 3   252 ?   ?   ?   B . n 
B 1 4   CYS 4   253 253 CYS CYS B . n 
B 1 5   HIS 5   254 254 HIS HIS B . n 
B 1 6   PRO 6   255 255 PRO PRO B . n 
B 1 7   CYS 7   256 256 CYS CYS B . n 
B 1 8   PRO 8   257 257 PRO PRO B . n 
B 1 9   TRP 9   258 258 TRP TRP B . n 
B 1 10  GLU 10  259 259 GLU GLU B . n 
B 1 11  TRP 11  260 260 TRP TRP B . n 
B 1 12  THR 12  261 261 THR THR B . n 
B 1 13  PHE 13  262 262 PHE PHE B . n 
B 1 14  PHE 14  263 263 PHE PHE B . n 
B 1 15  GLN 15  264 264 GLN GLN B . n 
B 1 16  GLY 16  265 265 GLY GLY B . n 
B 1 17  ASN 17  266 266 ASN ASN B . n 
B 1 18  CYS 18  267 267 CYS CYS B . n 
B 1 19  TYR 19  268 268 TYR TYR B . n 
B 1 20  PHE 20  269 269 PHE PHE B . n 
B 1 21  MET 21  270 270 MET MET B . n 
B 1 22  SER 22  271 271 SER SER B . n 
B 1 23  ASN 23  272 272 ASN ASN B . n 
B 1 24  SER 24  273 273 SER SER B . n 
B 1 25  GLN 25  274 274 GLN GLN B . n 
B 1 26  ARG 26  275 275 ARG ARG B . n 
B 1 27  ASN 27  276 276 ASN ASN B . n 
B 1 28  TRP 28  277 277 TRP TRP B . n 
B 1 29  HIS 29  278 278 HIS HIS B . n 
B 1 30  ASP 30  279 279 ASP ASP B . n 
B 1 31  SER 31  280 280 SER SER B . n 
B 1 32  ILE 32  281 281 ILE ILE B . n 
B 1 33  THR 33  282 282 THR THR B . n 
B 1 34  ALA 34  283 283 ALA ALA B . n 
B 1 35  CYS 35  284 284 CYS CYS B . n 
B 1 36  LYS 36  285 285 LYS LYS B . n 
B 1 37  GLU 37  286 286 GLU GLU B . n 
B 1 38  VAL 38  287 287 VAL VAL B . n 
B 1 39  GLY 39  288 288 GLY GLY B . n 
B 1 40  ALA 40  289 289 ALA ALA B . n 
B 1 41  GLN 41  290 290 GLN GLN B . n 
B 1 42  LEU 42  291 291 LEU LEU B . n 
B 1 43  VAL 43  292 292 VAL VAL B . n 
B 1 44  VAL 44  293 293 VAL VAL B . n 
B 1 45  ILE 45  294 294 ILE ILE B . n 
B 1 46  LYS 46  295 295 LYS LYS B . n 
B 1 47  SER 47  296 296 SER SER B . n 
B 1 48  ALA 48  297 297 ALA ALA B . n 
B 1 49  GLU 49  298 298 GLU GLU B . n 
B 1 50  GLU 50  299 299 GLU GLU B . n 
B 1 51  GLN 51  300 300 GLN GLN B . n 
B 1 52  ASN 52  301 301 ASN ASN B . n 
B 1 53  PHE 53  302 302 PHE PHE B . n 
B 1 54  LEU 54  303 303 LEU LEU B . n 
B 1 55  GLN 55  304 304 GLN GLN B . n 
B 1 56  LEU 56  305 305 LEU LEU B . n 
B 1 57  GLN 57  306 306 GLN GLN B . n 
B 1 58  SER 58  307 307 SER SER B . n 
B 1 59  SER 59  308 308 SER SER B . n 
B 1 60  ARG 60  309 309 ARG ARG B . n 
B 1 61  SER 61  310 310 SER SER B . n 
B 1 62  ASN 62  311 311 ASN ASN B . n 
B 1 63  ARG 63  312 312 ARG ARG B . n 
B 1 64  PHE 64  313 313 PHE PHE B . n 
B 1 65  THR 65  314 314 THR THR B . n 
B 1 66  TRP 66  315 315 TRP TRP B . n 
B 1 67  MET 67  316 316 MET MET B . n 
B 1 68  GLY 68  317 317 GLY GLY B . n 
B 1 69  LEU 69  318 318 LEU LEU B . n 
B 1 70  SER 70  319 319 SER SER B . n 
B 1 71  ASP 71  320 320 ASP ASP B . n 
B 1 72  LEU 72  321 321 LEU LEU B . n 
B 1 73  ASN 73  322 322 ASN ASN B . n 
B 1 74  GLN 74  323 323 GLN GLN B . n 
B 1 75  GLU 75  324 324 GLU GLU B . n 
B 1 76  GLY 76  325 325 GLY GLY B . n 
B 1 77  THR 77  326 326 THR THR B . n 
B 1 78  TRP 78  327 327 TRP TRP B . n 
B 1 79  GLN 79  328 328 GLN GLN B . n 
B 1 80  TRP 80  329 329 TRP TRP B . n 
B 1 81  VAL 81  330 330 VAL VAL B . n 
B 1 82  ASP 82  331 331 ASP ASP B . n 
B 1 83  GLY 83  332 332 GLY GLY B . n 
B 1 84  SER 84  333 333 SER SER B . n 
B 1 85  PRO 85  334 334 PRO PRO B . n 
B 1 86  LEU 86  335 335 LEU LEU B . n 
B 1 87  LEU 87  336 336 LEU LEU B . n 
B 1 88  PRO 88  337 337 PRO PRO B . n 
B 1 89  SER 89  338 338 SER SER B . n 
B 1 90  PHE 90  339 339 PHE PHE B . n 
B 1 91  LYS 91  340 340 LYS LYS B . n 
B 1 92  GLN 92  341 341 GLN GLN B . n 
B 1 93  TYR 93  342 342 TYR TYR B . n 
B 1 94  TRP 94  343 343 TRP TRP B . n 
B 1 95  ASN 95  344 344 ASN ASN B . n 
B 1 96  ARG 96  345 345 ARG ARG B . n 
B 1 97  GLY 97  346 346 GLY GLY B . n 
B 1 98  GLU 98  347 347 GLU GLU B . n 
B 1 99  PRO 99  348 348 PRO PRO B . n 
B 1 100 ASN 100 349 349 ASN ASN B . n 
B 1 101 ASN 101 350 350 ASN ASN B . n 
B 1 102 VAL 102 351 351 VAL VAL B . n 
B 1 103 GLY 103 352 352 GLY GLY B . n 
B 1 104 GLU 104 353 353 GLU GLU B . n 
B 1 105 GLU 105 354 354 GLU GLU B . n 
B 1 106 ASP 106 355 355 ASP ASP B . n 
B 1 107 CYS 107 356 356 CYS CYS B . n 
B 1 108 ALA 108 357 357 ALA ALA B . n 
B 1 109 GLU 109 358 358 GLU GLU B . n 
B 1 110 PHE 110 359 359 PHE PHE B . n 
B 1 111 SER 111 360 360 SER SER B . n 
B 1 112 GLY 112 361 361 GLY GLY B . n 
B 1 113 ASN 113 362 362 ASN ASN B . n 
B 1 114 GLY 114 363 363 GLY GLY B . n 
B 1 115 TRP 115 364 364 TRP TRP B . n 
B 1 116 ASN 116 365 365 ASN ASN B . n 
B 1 117 ASP 117 366 366 ASP ASP B . n 
B 1 118 ASP 118 367 367 ASP ASP B . n 
B 1 119 LYS 119 368 368 LYS LYS B . n 
B 1 120 CYS 120 369 369 CYS CYS B . n 
B 1 121 ASN 121 370 370 ASN ASN B . n 
B 1 122 LEU 122 371 371 LEU LEU B . n 
B 1 123 ALA 123 372 372 ALA ALA B . n 
B 1 124 LYS 124 373 373 LYS LYS B . n 
B 1 125 PHE 125 374 374 PHE PHE B . n 
B 1 126 TRP 126 375 375 TRP TRP B . n 
B 1 127 ILE 127 376 376 ILE ILE B . n 
B 1 128 CYS 128 377 377 CYS CYS B . n 
B 1 129 LYS 129 378 378 LYS LYS B . n 
B 1 130 LYS 130 379 379 LYS LYS B . n 
B 1 131 SER 131 380 380 SER SER B . n 
B 1 132 ALA 132 381 381 ALA ALA B . n 
B 1 133 ALA 133 382 382 ALA ALA B . n 
B 1 134 SER 134 383 383 SER SER B . n 
B 1 135 CYS 135 384 384 CYS CYS B . n 
B 1 136 SER 136 385 ?   ?   ?   B . n 
B 1 137 ARG 137 386 ?   ?   ?   B . n 
B 1 138 ASP 138 387 ?   ?   ?   B . n 
B 1 139 GLU 139 388 ?   ?   ?   B . n 
B 1 140 GLU 140 389 ?   ?   ?   B . n 
B 1 141 GLN 141 390 ?   ?   ?   B . n 
B 1 142 PHE 142 391 ?   ?   ?   B . n 
B 1 143 LEU 143 392 ?   ?   ?   B . n 
B 1 144 SER 144 393 ?   ?   ?   B . n 
B 1 145 PRO 145 394 ?   ?   ?   B . n 
B 1 146 ALA 146 395 ?   ?   ?   B . n 
B 1 147 PRO 147 396 ?   ?   ?   B . n 
B 1 148 ALA 148 397 ?   ?   ?   B . n 
B 1 149 THR 149 398 ?   ?   ?   B . n 
B 1 150 PRO 150 399 ?   ?   ?   B . n 
B 1 151 ASN 151 400 ?   ?   ?   B . n 
B 1 152 PRO 152 401 ?   ?   ?   B . n 
B 1 153 PRO 153 402 ?   ?   ?   B . n 
B 1 154 PRO 154 403 ?   ?   ?   B . n 
B 1 155 ALA 155 404 ?   ?   ?   B . n 
C 1 1   GLU 1   250 ?   ?   ?   C . n 
C 1 2   ARG 2   251 ?   ?   ?   C . n 
C 1 3   LEU 3   252 252 LEU LEU C . n 
C 1 4   CYS 4   253 253 CYS CYS C . n 
C 1 5   HIS 5   254 254 HIS HIS C . n 
C 1 6   PRO 6   255 255 PRO PRO C . n 
C 1 7   CYS 7   256 256 CYS CYS C . n 
C 1 8   PRO 8   257 257 PRO PRO C . n 
C 1 9   TRP 9   258 258 TRP TRP C . n 
C 1 10  GLU 10  259 259 GLU GLU C . n 
C 1 11  TRP 11  260 260 TRP TRP C . n 
C 1 12  THR 12  261 261 THR THR C . n 
C 1 13  PHE 13  262 262 PHE PHE C . n 
C 1 14  PHE 14  263 263 PHE PHE C . n 
C 1 15  GLN 15  264 264 GLN GLN C . n 
C 1 16  GLY 16  265 265 GLY GLY C . n 
C 1 17  ASN 17  266 266 ASN ASN C . n 
C 1 18  CYS 18  267 267 CYS CYS C . n 
C 1 19  TYR 19  268 268 TYR TYR C . n 
C 1 20  PHE 20  269 269 PHE PHE C . n 
C 1 21  MET 21  270 270 MET MET C . n 
C 1 22  SER 22  271 271 SER SER C . n 
C 1 23  ASN 23  272 272 ASN ASN C . n 
C 1 24  SER 24  273 273 SER SER C . n 
C 1 25  GLN 25  274 274 GLN GLN C . n 
C 1 26  ARG 26  275 275 ARG ARG C . n 
C 1 27  ASN 27  276 276 ASN ASN C . n 
C 1 28  TRP 28  277 277 TRP TRP C . n 
C 1 29  HIS 29  278 278 HIS HIS C . n 
C 1 30  ASP 30  279 279 ASP ASP C . n 
C 1 31  SER 31  280 280 SER SER C . n 
C 1 32  ILE 32  281 281 ILE ILE C . n 
C 1 33  THR 33  282 282 THR THR C . n 
C 1 34  ALA 34  283 283 ALA ALA C . n 
C 1 35  CYS 35  284 284 CYS CYS C . n 
C 1 36  LYS 36  285 285 LYS LYS C . n 
C 1 37  GLU 37  286 286 GLU GLU C . n 
C 1 38  VAL 38  287 287 VAL VAL C . n 
C 1 39  GLY 39  288 288 GLY GLY C . n 
C 1 40  ALA 40  289 289 ALA ALA C . n 
C 1 41  GLN 41  290 290 GLN GLN C . n 
C 1 42  LEU 42  291 291 LEU LEU C . n 
C 1 43  VAL 43  292 292 VAL VAL C . n 
C 1 44  VAL 44  293 293 VAL VAL C . n 
C 1 45  ILE 45  294 294 ILE ILE C . n 
C 1 46  LYS 46  295 295 LYS LYS C . n 
C 1 47  SER 47  296 296 SER SER C . n 
C 1 48  ALA 48  297 297 ALA ALA C . n 
C 1 49  GLU 49  298 298 GLU GLU C . n 
C 1 50  GLU 50  299 299 GLU GLU C . n 
C 1 51  GLN 51  300 300 GLN GLN C . n 
C 1 52  ASN 52  301 301 ASN ASN C . n 
C 1 53  PHE 53  302 302 PHE PHE C . n 
C 1 54  LEU 54  303 303 LEU LEU C . n 
C 1 55  GLN 55  304 304 GLN GLN C . n 
C 1 56  LEU 56  305 305 LEU LEU C . n 
C 1 57  GLN 57  306 306 GLN GLN C . n 
C 1 58  SER 58  307 307 SER SER C . n 
C 1 59  SER 59  308 308 SER SER C . n 
C 1 60  ARG 60  309 309 ARG ARG C . n 
C 1 61  SER 61  310 310 SER SER C . n 
C 1 62  ASN 62  311 311 ASN ASN C . n 
C 1 63  ARG 63  312 312 ARG ARG C . n 
C 1 64  PHE 64  313 313 PHE PHE C . n 
C 1 65  THR 65  314 314 THR THR C . n 
C 1 66  TRP 66  315 315 TRP TRP C . n 
C 1 67  MET 67  316 316 MET MET C . n 
C 1 68  GLY 68  317 317 GLY GLY C . n 
C 1 69  LEU 69  318 318 LEU LEU C . n 
C 1 70  SER 70  319 319 SER SER C . n 
C 1 71  ASP 71  320 320 ASP ASP C . n 
C 1 72  LEU 72  321 321 LEU LEU C . n 
C 1 73  ASN 73  322 322 ASN ASN C . n 
C 1 74  GLN 74  323 323 GLN GLN C . n 
C 1 75  GLU 75  324 324 GLU GLU C . n 
C 1 76  GLY 76  325 325 GLY GLY C . n 
C 1 77  THR 77  326 326 THR THR C . n 
C 1 78  TRP 78  327 327 TRP TRP C . n 
C 1 79  GLN 79  328 328 GLN GLN C . n 
C 1 80  TRP 80  329 329 TRP TRP C . n 
C 1 81  VAL 81  330 330 VAL VAL C . n 
C 1 82  ASP 82  331 331 ASP ASP C . n 
C 1 83  GLY 83  332 332 GLY GLY C . n 
C 1 84  SER 84  333 333 SER SER C . n 
C 1 85  PRO 85  334 334 PRO PRO C . n 
C 1 86  LEU 86  335 335 LEU LEU C . n 
C 1 87  LEU 87  336 336 LEU LEU C . n 
C 1 88  PRO 88  337 337 PRO PRO C . n 
C 1 89  SER 89  338 338 SER SER C . n 
C 1 90  PHE 90  339 339 PHE PHE C . n 
C 1 91  LYS 91  340 340 LYS LYS C . n 
C 1 92  GLN 92  341 341 GLN GLN C . n 
C 1 93  TYR 93  342 342 TYR TYR C . n 
C 1 94  TRP 94  343 343 TRP TRP C . n 
C 1 95  ASN 95  344 344 ASN ASN C . n 
C 1 96  ARG 96  345 345 ARG ARG C . n 
C 1 97  GLY 97  346 346 GLY GLY C . n 
C 1 98  GLU 98  347 347 GLU GLU C . n 
C 1 99  PRO 99  348 348 PRO PRO C . n 
C 1 100 ASN 100 349 349 ASN ASN C . n 
C 1 101 ASN 101 350 350 ASN ASN C . n 
C 1 102 VAL 102 351 351 VAL VAL C . n 
C 1 103 GLY 103 352 352 GLY GLY C . n 
C 1 104 GLU 104 353 353 GLU GLU C . n 
C 1 105 GLU 105 354 354 GLU GLU C . n 
C 1 106 ASP 106 355 355 ASP ASP C . n 
C 1 107 CYS 107 356 356 CYS CYS C . n 
C 1 108 ALA 108 357 357 ALA ALA C . n 
C 1 109 GLU 109 358 358 GLU GLU C . n 
C 1 110 PHE 110 359 359 PHE PHE C . n 
C 1 111 SER 111 360 360 SER SER C . n 
C 1 112 GLY 112 361 361 GLY GLY C . n 
C 1 113 ASN 113 362 362 ASN ASN C . n 
C 1 114 GLY 114 363 363 GLY GLY C . n 
C 1 115 TRP 115 364 364 TRP TRP C . n 
C 1 116 ASN 116 365 365 ASN ASN C . n 
C 1 117 ASP 117 366 366 ASP ASP C . n 
C 1 118 ASP 118 367 367 ASP ASP C . n 
C 1 119 LYS 119 368 368 LYS LYS C . n 
C 1 120 CYS 120 369 369 CYS CYS C . n 
C 1 121 ASN 121 370 370 ASN ASN C . n 
C 1 122 LEU 122 371 371 LEU LEU C . n 
C 1 123 ALA 123 372 372 ALA ALA C . n 
C 1 124 LYS 124 373 373 LYS LYS C . n 
C 1 125 PHE 125 374 374 PHE PHE C . n 
C 1 126 TRP 126 375 375 TRP TRP C . n 
C 1 127 ILE 127 376 376 ILE ILE C . n 
C 1 128 CYS 128 377 377 CYS CYS C . n 
C 1 129 LYS 129 378 378 LYS LYS C . n 
C 1 130 LYS 130 379 379 LYS LYS C . n 
C 1 131 SER 131 380 380 SER SER C . n 
C 1 132 ALA 132 381 381 ALA ALA C . n 
C 1 133 ALA 133 382 382 ALA ALA C . n 
C 1 134 SER 134 383 383 SER SER C . n 
C 1 135 CYS 135 384 384 CYS CYS C . n 
C 1 136 SER 136 385 ?   ?   ?   C . n 
C 1 137 ARG 137 386 ?   ?   ?   C . n 
C 1 138 ASP 138 387 ?   ?   ?   C . n 
C 1 139 GLU 139 388 ?   ?   ?   C . n 
C 1 140 GLU 140 389 ?   ?   ?   C . n 
C 1 141 GLN 141 390 ?   ?   ?   C . n 
C 1 142 PHE 142 391 ?   ?   ?   C . n 
C 1 143 LEU 143 392 ?   ?   ?   C . n 
C 1 144 SER 144 393 ?   ?   ?   C . n 
C 1 145 PRO 145 394 ?   ?   ?   C . n 
C 1 146 ALA 146 395 ?   ?   ?   C . n 
C 1 147 PRO 147 396 ?   ?   ?   C . n 
C 1 148 ALA 148 397 ?   ?   ?   C . n 
C 1 149 THR 149 398 ?   ?   ?   C . n 
C 1 150 PRO 150 399 ?   ?   ?   C . n 
C 1 151 ASN 151 400 ?   ?   ?   C . n 
C 1 152 PRO 152 401 ?   ?   ?   C . n 
C 1 153 PRO 153 402 ?   ?   ?   C . n 
C 1 154 PRO 154 403 ?   ?   ?   C . n 
C 1 155 ALA 155 404 ?   ?   ?   C . n 
D 1 1   GLU 1   250 ?   ?   ?   D . n 
D 1 2   ARG 2   251 ?   ?   ?   D . n 
D 1 3   LEU 3   252 252 LEU LEU D . n 
D 1 4   CYS 4   253 253 CYS CYS D . n 
D 1 5   HIS 5   254 254 HIS HIS D . n 
D 1 6   PRO 6   255 255 PRO PRO D . n 
D 1 7   CYS 7   256 256 CYS CYS D . n 
D 1 8   PRO 8   257 257 PRO PRO D . n 
D 1 9   TRP 9   258 258 TRP TRP D . n 
D 1 10  GLU 10  259 259 GLU GLU D . n 
D 1 11  TRP 11  260 260 TRP TRP D . n 
D 1 12  THR 12  261 261 THR THR D . n 
D 1 13  PHE 13  262 262 PHE PHE D . n 
D 1 14  PHE 14  263 263 PHE PHE D . n 
D 1 15  GLN 15  264 264 GLN GLN D . n 
D 1 16  GLY 16  265 265 GLY GLY D . n 
D 1 17  ASN 17  266 266 ASN ASN D . n 
D 1 18  CYS 18  267 267 CYS CYS D . n 
D 1 19  TYR 19  268 268 TYR TYR D . n 
D 1 20  PHE 20  269 269 PHE PHE D . n 
D 1 21  MET 21  270 270 MET MET D . n 
D 1 22  SER 22  271 271 SER SER D . n 
D 1 23  ASN 23  272 272 ASN ASN D . n 
D 1 24  SER 24  273 273 SER SER D . n 
D 1 25  GLN 25  274 274 GLN GLN D . n 
D 1 26  ARG 26  275 275 ARG ARG D . n 
D 1 27  ASN 27  276 276 ASN ASN D . n 
D 1 28  TRP 28  277 277 TRP TRP D . n 
D 1 29  HIS 29  278 278 HIS HIS D . n 
D 1 30  ASP 30  279 279 ASP ASP D . n 
D 1 31  SER 31  280 280 SER SER D . n 
D 1 32  ILE 32  281 281 ILE ILE D . n 
D 1 33  THR 33  282 282 THR THR D . n 
D 1 34  ALA 34  283 283 ALA ALA D . n 
D 1 35  CYS 35  284 284 CYS CYS D . n 
D 1 36  LYS 36  285 285 LYS LYS D . n 
D 1 37  GLU 37  286 286 GLU GLU D . n 
D 1 38  VAL 38  287 287 VAL VAL D . n 
D 1 39  GLY 39  288 288 GLY GLY D . n 
D 1 40  ALA 40  289 289 ALA ALA D . n 
D 1 41  GLN 41  290 290 GLN GLN D . n 
D 1 42  LEU 42  291 291 LEU LEU D . n 
D 1 43  VAL 43  292 292 VAL VAL D . n 
D 1 44  VAL 44  293 293 VAL VAL D . n 
D 1 45  ILE 45  294 294 ILE ILE D . n 
D 1 46  LYS 46  295 295 LYS LYS D . n 
D 1 47  SER 47  296 296 SER SER D . n 
D 1 48  ALA 48  297 297 ALA ALA D . n 
D 1 49  GLU 49  298 298 GLU GLU D . n 
D 1 50  GLU 50  299 299 GLU GLU D . n 
D 1 51  GLN 51  300 300 GLN GLN D . n 
D 1 52  ASN 52  301 301 ASN ASN D . n 
D 1 53  PHE 53  302 302 PHE PHE D . n 
D 1 54  LEU 54  303 303 LEU LEU D . n 
D 1 55  GLN 55  304 304 GLN GLN D . n 
D 1 56  LEU 56  305 305 LEU LEU D . n 
D 1 57  GLN 57  306 306 GLN GLN D . n 
D 1 58  SER 58  307 307 SER SER D . n 
D 1 59  SER 59  308 308 SER SER D . n 
D 1 60  ARG 60  309 309 ARG ARG D . n 
D 1 61  SER 61  310 310 SER SER D . n 
D 1 62  ASN 62  311 311 ASN ASN D . n 
D 1 63  ARG 63  312 312 ARG ARG D . n 
D 1 64  PHE 64  313 313 PHE PHE D . n 
D 1 65  THR 65  314 314 THR THR D . n 
D 1 66  TRP 66  315 315 TRP TRP D . n 
D 1 67  MET 67  316 316 MET MET D . n 
D 1 68  GLY 68  317 317 GLY GLY D . n 
D 1 69  LEU 69  318 318 LEU LEU D . n 
D 1 70  SER 70  319 319 SER SER D . n 
D 1 71  ASP 71  320 320 ASP ASP D . n 
D 1 72  LEU 72  321 321 LEU LEU D . n 
D 1 73  ASN 73  322 322 ASN ASN D . n 
D 1 74  GLN 74  323 323 GLN GLN D . n 
D 1 75  GLU 75  324 324 GLU GLU D . n 
D 1 76  GLY 76  325 325 GLY GLY D . n 
D 1 77  THR 77  326 326 THR THR D . n 
D 1 78  TRP 78  327 327 TRP TRP D . n 
D 1 79  GLN 79  328 328 GLN GLN D . n 
D 1 80  TRP 80  329 329 TRP TRP D . n 
D 1 81  VAL 81  330 330 VAL VAL D . n 
D 1 82  ASP 82  331 331 ASP ASP D . n 
D 1 83  GLY 83  332 332 GLY GLY D . n 
D 1 84  SER 84  333 333 SER SER D . n 
D 1 85  PRO 85  334 334 PRO PRO D . n 
D 1 86  LEU 86  335 335 LEU LEU D . n 
D 1 87  LEU 87  336 336 LEU LEU D . n 
D 1 88  PRO 88  337 337 PRO PRO D . n 
D 1 89  SER 89  338 338 SER SER D . n 
D 1 90  PHE 90  339 339 PHE PHE D . n 
D 1 91  LYS 91  340 340 LYS LYS D . n 
D 1 92  GLN 92  341 341 GLN GLN D . n 
D 1 93  TYR 93  342 342 TYR TYR D . n 
D 1 94  TRP 94  343 343 TRP TRP D . n 
D 1 95  ASN 95  344 344 ASN ASN D . n 
D 1 96  ARG 96  345 345 ARG ARG D . n 
D 1 97  GLY 97  346 346 GLY GLY D . n 
D 1 98  GLU 98  347 347 GLU GLU D . n 
D 1 99  PRO 99  348 348 PRO PRO D . n 
D 1 100 ASN 100 349 349 ASN ASN D . n 
D 1 101 ASN 101 350 350 ASN ASN D . n 
D 1 102 VAL 102 351 351 VAL VAL D . n 
D 1 103 GLY 103 352 352 GLY GLY D . n 
D 1 104 GLU 104 353 353 GLU GLU D . n 
D 1 105 GLU 105 354 354 GLU GLU D . n 
D 1 106 ASP 106 355 355 ASP ASP D . n 
D 1 107 CYS 107 356 356 CYS CYS D . n 
D 1 108 ALA 108 357 357 ALA ALA D . n 
D 1 109 GLU 109 358 358 GLU GLU D . n 
D 1 110 PHE 110 359 359 PHE PHE D . n 
D 1 111 SER 111 360 360 SER SER D . n 
D 1 112 GLY 112 361 361 GLY GLY D . n 
D 1 113 ASN 113 362 362 ASN ASN D . n 
D 1 114 GLY 114 363 363 GLY GLY D . n 
D 1 115 TRP 115 364 364 TRP TRP D . n 
D 1 116 ASN 116 365 365 ASN ASN D . n 
D 1 117 ASP 117 366 366 ASP ASP D . n 
D 1 118 ASP 118 367 367 ASP ASP D . n 
D 1 119 LYS 119 368 368 LYS LYS D . n 
D 1 120 CYS 120 369 369 CYS CYS D . n 
D 1 121 ASN 121 370 370 ASN ASN D . n 
D 1 122 LEU 122 371 371 LEU LEU D . n 
D 1 123 ALA 123 372 372 ALA ALA D . n 
D 1 124 LYS 124 373 373 LYS LYS D . n 
D 1 125 PHE 125 374 374 PHE PHE D . n 
D 1 126 TRP 126 375 375 TRP TRP D . n 
D 1 127 ILE 127 376 376 ILE ILE D . n 
D 1 128 CYS 128 377 377 CYS CYS D . n 
D 1 129 LYS 129 378 378 LYS LYS D . n 
D 1 130 LYS 130 379 379 LYS LYS D . n 
D 1 131 SER 131 380 380 SER SER D . n 
D 1 132 ALA 132 381 381 ALA ALA D . n 
D 1 133 ALA 133 382 382 ALA ALA D . n 
D 1 134 SER 134 383 383 SER SER D . n 
D 1 135 CYS 135 384 384 CYS CYS D . n 
D 1 136 SER 136 385 ?   ?   ?   D . n 
D 1 137 ARG 137 386 ?   ?   ?   D . n 
D 1 138 ASP 138 387 ?   ?   ?   D . n 
D 1 139 GLU 139 388 ?   ?   ?   D . n 
D 1 140 GLU 140 389 ?   ?   ?   D . n 
D 1 141 GLN 141 390 ?   ?   ?   D . n 
D 1 142 PHE 142 391 ?   ?   ?   D . n 
D 1 143 LEU 143 392 ?   ?   ?   D . n 
D 1 144 SER 144 393 ?   ?   ?   D . n 
D 1 145 PRO 145 394 ?   ?   ?   D . n 
D 1 146 ALA 146 395 ?   ?   ?   D . n 
D 1 147 PRO 147 396 ?   ?   ?   D . n 
D 1 148 ALA 148 397 ?   ?   ?   D . n 
D 1 149 THR 149 398 ?   ?   ?   D . n 
D 1 150 PRO 150 399 ?   ?   ?   D . n 
D 1 151 ASN 151 400 ?   ?   ?   D . n 
D 1 152 PRO 152 401 ?   ?   ?   D . n 
D 1 153 PRO 153 402 ?   ?   ?   D . n 
D 1 154 PRO 154 403 ?   ?   ?   D . n 
D 1 155 ALA 155 404 ?   ?   ?   D . n 
E 1 1   GLU 1   250 ?   ?   ?   E . n 
E 1 2   ARG 2   251 ?   ?   ?   E . n 
E 1 3   LEU 3   252 252 LEU LEU E . n 
E 1 4   CYS 4   253 253 CYS CYS E . n 
E 1 5   HIS 5   254 254 HIS HIS E . n 
E 1 6   PRO 6   255 255 PRO PRO E . n 
E 1 7   CYS 7   256 256 CYS CYS E . n 
E 1 8   PRO 8   257 257 PRO PRO E . n 
E 1 9   TRP 9   258 258 TRP TRP E . n 
E 1 10  GLU 10  259 259 GLU GLU E . n 
E 1 11  TRP 11  260 260 TRP TRP E . n 
E 1 12  THR 12  261 261 THR THR E . n 
E 1 13  PHE 13  262 262 PHE PHE E . n 
E 1 14  PHE 14  263 263 PHE PHE E . n 
E 1 15  GLN 15  264 264 GLN GLN E . n 
E 1 16  GLY 16  265 265 GLY GLY E . n 
E 1 17  ASN 17  266 266 ASN ASN E . n 
E 1 18  CYS 18  267 267 CYS CYS E . n 
E 1 19  TYR 19  268 268 TYR TYR E . n 
E 1 20  PHE 20  269 269 PHE PHE E . n 
E 1 21  MET 21  270 270 MET MET E . n 
E 1 22  SER 22  271 271 SER SER E . n 
E 1 23  ASN 23  272 272 ASN ASN E . n 
E 1 24  SER 24  273 273 SER SER E . n 
E 1 25  GLN 25  274 274 GLN GLN E . n 
E 1 26  ARG 26  275 275 ARG ARG E . n 
E 1 27  ASN 27  276 276 ASN ASN E . n 
E 1 28  TRP 28  277 277 TRP TRP E . n 
E 1 29  HIS 29  278 278 HIS HIS E . n 
E 1 30  ASP 30  279 279 ASP ASP E . n 
E 1 31  SER 31  280 280 SER SER E . n 
E 1 32  ILE 32  281 281 ILE ILE E . n 
E 1 33  THR 33  282 282 THR THR E . n 
E 1 34  ALA 34  283 283 ALA ALA E . n 
E 1 35  CYS 35  284 284 CYS CYS E . n 
E 1 36  LYS 36  285 285 LYS LYS E . n 
E 1 37  GLU 37  286 286 GLU GLU E . n 
E 1 38  VAL 38  287 287 VAL VAL E . n 
E 1 39  GLY 39  288 288 GLY GLY E . n 
E 1 40  ALA 40  289 289 ALA ALA E . n 
E 1 41  GLN 41  290 290 GLN GLN E . n 
E 1 42  LEU 42  291 291 LEU LEU E . n 
E 1 43  VAL 43  292 292 VAL VAL E . n 
E 1 44  VAL 44  293 293 VAL VAL E . n 
E 1 45  ILE 45  294 294 ILE ILE E . n 
E 1 46  LYS 46  295 295 LYS LYS E . n 
E 1 47  SER 47  296 296 SER SER E . n 
E 1 48  ALA 48  297 297 ALA ALA E . n 
E 1 49  GLU 49  298 298 GLU GLU E . n 
E 1 50  GLU 50  299 299 GLU GLU E . n 
E 1 51  GLN 51  300 300 GLN GLN E . n 
E 1 52  ASN 52  301 301 ASN ASN E . n 
E 1 53  PHE 53  302 302 PHE PHE E . n 
E 1 54  LEU 54  303 303 LEU LEU E . n 
E 1 55  GLN 55  304 304 GLN GLN E . n 
E 1 56  LEU 56  305 305 LEU LEU E . n 
E 1 57  GLN 57  306 306 GLN GLN E . n 
E 1 58  SER 58  307 307 SER SER E . n 
E 1 59  SER 59  308 308 SER SER E . n 
E 1 60  ARG 60  309 309 ARG ARG E . n 
E 1 61  SER 61  310 310 SER SER E . n 
E 1 62  ASN 62  311 311 ASN ASN E . n 
E 1 63  ARG 63  312 312 ARG ARG E . n 
E 1 64  PHE 64  313 313 PHE PHE E . n 
E 1 65  THR 65  314 314 THR THR E . n 
E 1 66  TRP 66  315 315 TRP TRP E . n 
E 1 67  MET 67  316 316 MET MET E . n 
E 1 68  GLY 68  317 317 GLY GLY E . n 
E 1 69  LEU 69  318 318 LEU LEU E . n 
E 1 70  SER 70  319 319 SER SER E . n 
E 1 71  ASP 71  320 320 ASP ASP E . n 
E 1 72  LEU 72  321 321 LEU LEU E . n 
E 1 73  ASN 73  322 322 ASN ASN E . n 
E 1 74  GLN 74  323 323 GLN GLN E . n 
E 1 75  GLU 75  324 324 GLU GLU E . n 
E 1 76  GLY 76  325 325 GLY GLY E . n 
E 1 77  THR 77  326 326 THR THR E . n 
E 1 78  TRP 78  327 327 TRP TRP E . n 
E 1 79  GLN 79  328 328 GLN GLN E . n 
E 1 80  TRP 80  329 329 TRP TRP E . n 
E 1 81  VAL 81  330 330 VAL VAL E . n 
E 1 82  ASP 82  331 331 ASP ASP E . n 
E 1 83  GLY 83  332 332 GLY GLY E . n 
E 1 84  SER 84  333 333 SER SER E . n 
E 1 85  PRO 85  334 334 PRO PRO E . n 
E 1 86  LEU 86  335 335 LEU LEU E . n 
E 1 87  LEU 87  336 336 LEU LEU E . n 
E 1 88  PRO 88  337 337 PRO PRO E . n 
E 1 89  SER 89  338 338 SER SER E . n 
E 1 90  PHE 90  339 339 PHE PHE E . n 
E 1 91  LYS 91  340 340 LYS LYS E . n 
E 1 92  GLN 92  341 341 GLN GLN E . n 
E 1 93  TYR 93  342 342 TYR TYR E . n 
E 1 94  TRP 94  343 343 TRP TRP E . n 
E 1 95  ASN 95  344 344 ASN ASN E . n 
E 1 96  ARG 96  345 345 ARG ARG E . n 
E 1 97  GLY 97  346 346 GLY GLY E . n 
E 1 98  GLU 98  347 347 GLU GLU E . n 
E 1 99  PRO 99  348 348 PRO PRO E . n 
E 1 100 ASN 100 349 349 ASN ASN E . n 
E 1 101 ASN 101 350 350 ASN ASN E . n 
E 1 102 VAL 102 351 351 VAL VAL E . n 
E 1 103 GLY 103 352 352 GLY GLY E . n 
E 1 104 GLU 104 353 353 GLU GLU E . n 
E 1 105 GLU 105 354 354 GLU GLU E . n 
E 1 106 ASP 106 355 355 ASP ASP E . n 
E 1 107 CYS 107 356 356 CYS CYS E . n 
E 1 108 ALA 108 357 357 ALA ALA E . n 
E 1 109 GLU 109 358 358 GLU GLU E . n 
E 1 110 PHE 110 359 359 PHE PHE E . n 
E 1 111 SER 111 360 360 SER SER E . n 
E 1 112 GLY 112 361 361 GLY GLY E . n 
E 1 113 ASN 113 362 362 ASN ASN E . n 
E 1 114 GLY 114 363 363 GLY GLY E . n 
E 1 115 TRP 115 364 364 TRP TRP E . n 
E 1 116 ASN 116 365 365 ASN ASN E . n 
E 1 117 ASP 117 366 366 ASP ASP E . n 
E 1 118 ASP 118 367 367 ASP ASP E . n 
E 1 119 LYS 119 368 368 LYS LYS E . n 
E 1 120 CYS 120 369 369 CYS CYS E . n 
E 1 121 ASN 121 370 370 ASN ASN E . n 
E 1 122 LEU 122 371 371 LEU LEU E . n 
E 1 123 ALA 123 372 372 ALA ALA E . n 
E 1 124 LYS 124 373 373 LYS LYS E . n 
E 1 125 PHE 125 374 374 PHE PHE E . n 
E 1 126 TRP 126 375 375 TRP TRP E . n 
E 1 127 ILE 127 376 376 ILE ILE E . n 
E 1 128 CYS 128 377 377 CYS CYS E . n 
E 1 129 LYS 129 378 378 LYS LYS E . n 
E 1 130 LYS 130 379 379 LYS LYS E . n 
E 1 131 SER 131 380 380 SER SER E . n 
E 1 132 ALA 132 381 381 ALA ALA E . n 
E 1 133 ALA 133 382 382 ALA ALA E . n 
E 1 134 SER 134 383 383 SER SER E . n 
E 1 135 CYS 135 384 384 CYS CYS E . n 
E 1 136 SER 136 385 ?   ?   ?   E . n 
E 1 137 ARG 137 386 ?   ?   ?   E . n 
E 1 138 ASP 138 387 ?   ?   ?   E . n 
E 1 139 GLU 139 388 ?   ?   ?   E . n 
E 1 140 GLU 140 389 ?   ?   ?   E . n 
E 1 141 GLN 141 390 ?   ?   ?   E . n 
E 1 142 PHE 142 391 ?   ?   ?   E . n 
E 1 143 LEU 143 392 ?   ?   ?   E . n 
E 1 144 SER 144 393 ?   ?   ?   E . n 
E 1 145 PRO 145 394 ?   ?   ?   E . n 
E 1 146 ALA 146 395 ?   ?   ?   E . n 
E 1 147 PRO 147 396 ?   ?   ?   E . n 
E 1 148 ALA 148 397 ?   ?   ?   E . n 
E 1 149 THR 149 398 ?   ?   ?   E . n 
E 1 150 PRO 150 399 ?   ?   ?   E . n 
E 1 151 ASN 151 400 ?   ?   ?   E . n 
E 1 152 PRO 152 401 ?   ?   ?   E . n 
E 1 153 PRO 153 402 ?   ?   ?   E . n 
E 1 154 PRO 154 403 ?   ?   ?   E . n 
E 1 155 ALA 155 404 ?   ?   ?   E . n 
F 1 1   GLU 1   250 ?   ?   ?   F . n 
F 1 2   ARG 2   251 ?   ?   ?   F . n 
F 1 3   LEU 3   252 ?   ?   ?   F . n 
F 1 4   CYS 4   253 253 CYS CYS F . n 
F 1 5   HIS 5   254 254 HIS HIS F . n 
F 1 6   PRO 6   255 255 PRO PRO F . n 
F 1 7   CYS 7   256 256 CYS CYS F . n 
F 1 8   PRO 8   257 257 PRO PRO F . n 
F 1 9   TRP 9   258 258 TRP TRP F . n 
F 1 10  GLU 10  259 259 GLU GLU F . n 
F 1 11  TRP 11  260 260 TRP TRP F . n 
F 1 12  THR 12  261 261 THR THR F . n 
F 1 13  PHE 13  262 262 PHE PHE F . n 
F 1 14  PHE 14  263 263 PHE PHE F . n 
F 1 15  GLN 15  264 264 GLN GLN F . n 
F 1 16  GLY 16  265 265 GLY GLY F . n 
F 1 17  ASN 17  266 266 ASN ASN F . n 
F 1 18  CYS 18  267 267 CYS CYS F . n 
F 1 19  TYR 19  268 268 TYR TYR F . n 
F 1 20  PHE 20  269 269 PHE PHE F . n 
F 1 21  MET 21  270 270 MET MET F . n 
F 1 22  SER 22  271 271 SER SER F . n 
F 1 23  ASN 23  272 272 ASN ASN F . n 
F 1 24  SER 24  273 273 SER SER F . n 
F 1 25  GLN 25  274 274 GLN GLN F . n 
F 1 26  ARG 26  275 275 ARG ARG F . n 
F 1 27  ASN 27  276 276 ASN ASN F . n 
F 1 28  TRP 28  277 277 TRP TRP F . n 
F 1 29  HIS 29  278 278 HIS HIS F . n 
F 1 30  ASP 30  279 279 ASP ASP F . n 
F 1 31  SER 31  280 280 SER SER F . n 
F 1 32  ILE 32  281 281 ILE ILE F . n 
F 1 33  THR 33  282 282 THR THR F . n 
F 1 34  ALA 34  283 283 ALA ALA F . n 
F 1 35  CYS 35  284 284 CYS CYS F . n 
F 1 36  LYS 36  285 285 LYS LYS F . n 
F 1 37  GLU 37  286 286 GLU GLU F . n 
F 1 38  VAL 38  287 287 VAL VAL F . n 
F 1 39  GLY 39  288 288 GLY GLY F . n 
F 1 40  ALA 40  289 289 ALA ALA F . n 
F 1 41  GLN 41  290 290 GLN GLN F . n 
F 1 42  LEU 42  291 291 LEU LEU F . n 
F 1 43  VAL 43  292 292 VAL VAL F . n 
F 1 44  VAL 44  293 293 VAL VAL F . n 
F 1 45  ILE 45  294 294 ILE ILE F . n 
F 1 46  LYS 46  295 295 LYS LYS F . n 
F 1 47  SER 47  296 296 SER SER F . n 
F 1 48  ALA 48  297 297 ALA ALA F . n 
F 1 49  GLU 49  298 298 GLU GLU F . n 
F 1 50  GLU 50  299 299 GLU GLU F . n 
F 1 51  GLN 51  300 300 GLN GLN F . n 
F 1 52  ASN 52  301 301 ASN ASN F . n 
F 1 53  PHE 53  302 302 PHE PHE F . n 
F 1 54  LEU 54  303 303 LEU LEU F . n 
F 1 55  GLN 55  304 304 GLN GLN F . n 
F 1 56  LEU 56  305 305 LEU LEU F . n 
F 1 57  GLN 57  306 306 GLN GLN F . n 
F 1 58  SER 58  307 307 SER SER F . n 
F 1 59  SER 59  308 308 SER SER F . n 
F 1 60  ARG 60  309 309 ARG ARG F . n 
F 1 61  SER 61  310 310 SER SER F . n 
F 1 62  ASN 62  311 311 ASN ASN F . n 
F 1 63  ARG 63  312 312 ARG ARG F . n 
F 1 64  PHE 64  313 313 PHE PHE F . n 
F 1 65  THR 65  314 314 THR THR F . n 
F 1 66  TRP 66  315 315 TRP TRP F . n 
F 1 67  MET 67  316 316 MET MET F . n 
F 1 68  GLY 68  317 317 GLY GLY F . n 
F 1 69  LEU 69  318 318 LEU LEU F . n 
F 1 70  SER 70  319 319 SER SER F . n 
F 1 71  ASP 71  320 320 ASP ASP F . n 
F 1 72  LEU 72  321 321 LEU LEU F . n 
F 1 73  ASN 73  322 322 ASN ASN F . n 
F 1 74  GLN 74  323 323 GLN GLN F . n 
F 1 75  GLU 75  324 324 GLU GLU F . n 
F 1 76  GLY 76  325 325 GLY GLY F . n 
F 1 77  THR 77  326 326 THR THR F . n 
F 1 78  TRP 78  327 327 TRP TRP F . n 
F 1 79  GLN 79  328 328 GLN GLN F . n 
F 1 80  TRP 80  329 329 TRP TRP F . n 
F 1 81  VAL 81  330 330 VAL VAL F . n 
F 1 82  ASP 82  331 331 ASP ASP F . n 
F 1 83  GLY 83  332 332 GLY GLY F . n 
F 1 84  SER 84  333 333 SER SER F . n 
F 1 85  PRO 85  334 334 PRO PRO F . n 
F 1 86  LEU 86  335 335 LEU LEU F . n 
F 1 87  LEU 87  336 336 LEU LEU F . n 
F 1 88  PRO 88  337 337 PRO PRO F . n 
F 1 89  SER 89  338 338 SER SER F . n 
F 1 90  PHE 90  339 339 PHE PHE F . n 
F 1 91  LYS 91  340 340 LYS LYS F . n 
F 1 92  GLN 92  341 341 GLN GLN F . n 
F 1 93  TYR 93  342 342 TYR TYR F . n 
F 1 94  TRP 94  343 343 TRP TRP F . n 
F 1 95  ASN 95  344 344 ASN ASN F . n 
F 1 96  ARG 96  345 345 ARG ARG F . n 
F 1 97  GLY 97  346 346 GLY GLY F . n 
F 1 98  GLU 98  347 347 GLU GLU F . n 
F 1 99  PRO 99  348 348 PRO PRO F . n 
F 1 100 ASN 100 349 349 ASN ASN F . n 
F 1 101 ASN 101 350 350 ASN ASN F . n 
F 1 102 VAL 102 351 351 VAL VAL F . n 
F 1 103 GLY 103 352 352 GLY GLY F . n 
F 1 104 GLU 104 353 353 GLU GLU F . n 
F 1 105 GLU 105 354 354 GLU GLU F . n 
F 1 106 ASP 106 355 355 ASP ASP F . n 
F 1 107 CYS 107 356 356 CYS CYS F . n 
F 1 108 ALA 108 357 357 ALA ALA F . n 
F 1 109 GLU 109 358 358 GLU GLU F . n 
F 1 110 PHE 110 359 359 PHE PHE F . n 
F 1 111 SER 111 360 360 SER SER F . n 
F 1 112 GLY 112 361 361 GLY GLY F . n 
F 1 113 ASN 113 362 362 ASN ASN F . n 
F 1 114 GLY 114 363 363 GLY GLY F . n 
F 1 115 TRP 115 364 364 TRP TRP F . n 
F 1 116 ASN 116 365 365 ASN ASN F . n 
F 1 117 ASP 117 366 366 ASP ASP F . n 
F 1 118 ASP 118 367 367 ASP ASP F . n 
F 1 119 LYS 119 368 368 LYS LYS F . n 
F 1 120 CYS 120 369 369 CYS CYS F . n 
F 1 121 ASN 121 370 370 ASN ASN F . n 
F 1 122 LEU 122 371 371 LEU LEU F . n 
F 1 123 ALA 123 372 372 ALA ALA F . n 
F 1 124 LYS 124 373 373 LYS LYS F . n 
F 1 125 PHE 125 374 374 PHE PHE F . n 
F 1 126 TRP 126 375 375 TRP TRP F . n 
F 1 127 ILE 127 376 376 ILE ILE F . n 
F 1 128 CYS 128 377 377 CYS CYS F . n 
F 1 129 LYS 129 378 378 LYS LYS F . n 
F 1 130 LYS 130 379 379 LYS LYS F . n 
F 1 131 SER 131 380 380 SER SER F . n 
F 1 132 ALA 132 381 381 ALA ALA F . n 
F 1 133 ALA 133 382 382 ALA ALA F . n 
F 1 134 SER 134 383 383 SER SER F . n 
F 1 135 CYS 135 384 384 CYS CYS F . n 
F 1 136 SER 136 385 ?   ?   ?   F . n 
F 1 137 ARG 137 386 ?   ?   ?   F . n 
F 1 138 ASP 138 387 ?   ?   ?   F . n 
F 1 139 GLU 139 388 ?   ?   ?   F . n 
F 1 140 GLU 140 389 ?   ?   ?   F . n 
F 1 141 GLN 141 390 ?   ?   ?   F . n 
F 1 142 PHE 142 391 ?   ?   ?   F . n 
F 1 143 LEU 143 392 ?   ?   ?   F . n 
F 1 144 SER 144 393 ?   ?   ?   F . n 
F 1 145 PRO 145 394 ?   ?   ?   F . n 
F 1 146 ALA 146 395 ?   ?   ?   F . n 
F 1 147 PRO 147 396 ?   ?   ?   F . n 
F 1 148 ALA 148 397 ?   ?   ?   F . n 
F 1 149 THR 149 398 ?   ?   ?   F . n 
F 1 150 PRO 150 399 ?   ?   ?   F . n 
F 1 151 ASN 151 400 ?   ?   ?   F . n 
F 1 152 PRO 152 401 ?   ?   ?   F . n 
F 1 153 PRO 153 402 ?   ?   ?   F . n 
F 1 154 PRO 154 403 ?   ?   ?   F . n 
F 1 155 ALA 155 404 ?   ?   ?   F . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        EZ8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   EZ8 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G  2 EZ8 1   1001 1001 EZ8 DRG A . 
H  3 CA  1   1002 1002 CA  CA  A . 
I  3 CA  1   1003 1003 CA  CA  A . 
J  3 CA  1   1004 1004 CA  CA  A . 
K  4 CL  1   1005 1006 CL  CL  A . 
L  4 CL  1   1006 1007 CL  CL  A . 
M  4 CL  1   1007 1005 CL  CL  A . 
N  2 EZ8 1   1001 1001 EZ8 DRG B . 
O  3 CA  1   1002 1002 CA  CA  B . 
P  3 CA  1   1003 1003 CA  CA  B . 
Q  3 CA  1   1004 1004 CA  CA  B . 
R  4 CL  1   1005 1006 CL  CL  B . 
S  4 CL  1   1006 1005 CL  CL  B . 
T  2 EZ8 1   1001 1001 EZ8 DRG C . 
U  3 CA  1   1002 1002 CA  CA  C . 
V  3 CA  1   1003 1003 CA  CA  C . 
W  3 CA  1   1004 1004 CA  CA  C . 
X  4 CL  1   1005 1006 CL  CL  C . 
Y  4 CL  1   1006 1005 CL  CL  C . 
Z  4 CL  1   501  1005 CL  CL  D . 
AA 2 EZ8 1   502  1001 EZ8 DRG D . 
BA 3 CA  1   503  1002 CA  CA  D . 
CA 3 CA  1   504  1003 CA  CA  D . 
DA 3 CA  1   505  1004 CA  CA  D . 
EA 4 CL  1   506  1006 CL  CL  D . 
FA 4 CL  1   501  1007 CL  CL  E . 
GA 4 CL  1   502  1005 CL  CL  E . 
HA 2 EZ8 1   503  1001 EZ8 DRG E . 
IA 3 CA  1   504  1002 CA  CA  E . 
JA 3 CA  1   505  1003 CA  CA  E . 
KA 3 CA  1   506  1004 CA  CA  E . 
LA 4 CL  1   507  1006 CL  CL  E . 
MA 4 CL  1   501  1005 CL  CL  F . 
NA 2 EZ8 1   502  1001 EZ8 DRG F . 
OA 3 CA  1   503  1002 CA  CA  F . 
PA 3 CA  1   504  1003 CA  CA  F . 
QA 3 CA  1   505  1004 CA  CA  F . 
RA 4 CL  1   506  1006 CL  CL  F . 
SA 5 HOH 1   1101 470  HOH HOH A . 
SA 5 HOH 2   1102 2    HOH HOH A . 
SA 5 HOH 3   1103 360  HOH HOH A . 
SA 5 HOH 4   1104 545  HOH HOH A . 
SA 5 HOH 5   1105 483  HOH HOH A . 
SA 5 HOH 6   1106 135  HOH HOH A . 
SA 5 HOH 7   1107 520  HOH HOH A . 
SA 5 HOH 8   1108 509  HOH HOH A . 
SA 5 HOH 9   1109 617  HOH HOH A . 
SA 5 HOH 10  1110 660  HOH HOH A . 
SA 5 HOH 11  1111 143  HOH HOH A . 
SA 5 HOH 12  1112 365  HOH HOH A . 
SA 5 HOH 13  1113 315  HOH HOH A . 
SA 5 HOH 14  1114 83   HOH HOH A . 
SA 5 HOH 15  1115 356  HOH HOH A . 
SA 5 HOH 16  1116 136  HOH HOH A . 
SA 5 HOH 17  1117 139  HOH HOH A . 
SA 5 HOH 18  1118 1    HOH HOH A . 
SA 5 HOH 19  1119 362  HOH HOH A . 
SA 5 HOH 20  1120 145  HOH HOH A . 
SA 5 HOH 21  1121 78   HOH HOH A . 
SA 5 HOH 22  1122 355  HOH HOH A . 
SA 5 HOH 23  1123 84   HOH HOH A . 
SA 5 HOH 24  1124 502  HOH HOH A . 
SA 5 HOH 25  1125 323  HOH HOH A . 
SA 5 HOH 26  1126 97   HOH HOH A . 
SA 5 HOH 27  1127 134  HOH HOH A . 
SA 5 HOH 28  1128 508  HOH HOH A . 
SA 5 HOH 29  1129 71   HOH HOH A . 
SA 5 HOH 30  1130 73   HOH HOH A . 
SA 5 HOH 31  1131 37   HOH HOH A . 
SA 5 HOH 32  1132 578  HOH HOH A . 
SA 5 HOH 33  1133 319  HOH HOH A . 
SA 5 HOH 34  1134 507  HOH HOH A . 
SA 5 HOH 35  1135 547  HOH HOH A . 
SA 5 HOH 36  1136 263  HOH HOH A . 
SA 5 HOH 37  1137 144  HOH HOH A . 
SA 5 HOH 38  1138 546  HOH HOH A . 
SA 5 HOH 39  1139 4    HOH HOH A . 
SA 5 HOH 40  1140 604  HOH HOH A . 
SA 5 HOH 41  1141 56   HOH HOH A . 
SA 5 HOH 42  1142 303  HOH HOH A . 
SA 5 HOH 43  1143 146  HOH HOH A . 
SA 5 HOH 44  1144 261  HOH HOH A . 
SA 5 HOH 45  1145 364  HOH HOH A . 
SA 5 HOH 46  1146 125  HOH HOH A . 
SA 5 HOH 47  1147 142  HOH HOH A . 
SA 5 HOH 48  1148 504  HOH HOH A . 
SA 5 HOH 49  1149 89   HOH HOH A . 
SA 5 HOH 50  1150 137  HOH HOH A . 
SA 5 HOH 51  1151 399  HOH HOH A . 
SA 5 HOH 52  1152 568  HOH HOH A . 
SA 5 HOH 53  1153 359  HOH HOH A . 
SA 5 HOH 54  1154 81   HOH HOH A . 
SA 5 HOH 55  1155 287  HOH HOH A . 
SA 5 HOH 56  1156 131  HOH HOH A . 
SA 5 HOH 57  1157 426  HOH HOH A . 
SA 5 HOH 58  1158 148  HOH HOH A . 
SA 5 HOH 59  1159 549  HOH HOH A . 
SA 5 HOH 60  1160 591  HOH HOH A . 
SA 5 HOH 61  1161 650  HOH HOH A . 
SA 5 HOH 62  1162 626  HOH HOH A . 
SA 5 HOH 63  1163 130  HOH HOH A . 
SA 5 HOH 64  1164 485  HOH HOH A . 
SA 5 HOH 65  1165 357  HOH HOH A . 
SA 5 HOH 66  1166 111  HOH HOH A . 
SA 5 HOH 67  1167 346  HOH HOH A . 
SA 5 HOH 68  1168 280  HOH HOH A . 
SA 5 HOH 69  1169 149  HOH HOH A . 
SA 5 HOH 70  1170 320  HOH HOH A . 
SA 5 HOH 71  1171 544  HOH HOH A . 
SA 5 HOH 72  1172 147  HOH HOH A . 
SA 5 HOH 73  1173 358  HOH HOH A . 
SA 5 HOH 74  1174 503  HOH HOH A . 
SA 5 HOH 75  1175 262  HOH HOH A . 
SA 5 HOH 76  1176 580  HOH HOH A . 
SA 5 HOH 77  1177 284  HOH HOH A . 
SA 5 HOH 78  1178 140  HOH HOH A . 
SA 5 HOH 79  1179 625  HOH HOH A . 
SA 5 HOH 80  1180 141  HOH HOH A . 
SA 5 HOH 81  1181 290  HOH HOH A . 
SA 5 HOH 82  1182 603  HOH HOH A . 
SA 5 HOH 83  1183 63   HOH HOH A . 
SA 5 HOH 84  1184 585  HOH HOH A . 
SA 5 HOH 85  1185 459  HOH HOH A . 
SA 5 HOH 86  1186 279  HOH HOH A . 
SA 5 HOH 87  1187 656  HOH HOH A . 
SA 5 HOH 88  1188 138  HOH HOH A . 
SA 5 HOH 89  1189 505  HOH HOH A . 
SA 5 HOH 90  1190 133  HOH HOH A . 
SA 5 HOH 91  1191 351  HOH HOH A . 
SA 5 HOH 92  1192 472  HOH HOH A . 
SA 5 HOH 93  1193 363  HOH HOH A . 
SA 5 HOH 94  1194 352  HOH HOH A . 
SA 5 HOH 95  1195 655  HOH HOH A . 
TA 5 HOH 1   1101 615  HOH HOH B . 
TA 5 HOH 2   1102 349  HOH HOH B . 
TA 5 HOH 3   1103 371  HOH HOH B . 
TA 5 HOH 4   1104 652  HOH HOH B . 
TA 5 HOH 5   1105 348  HOH HOH B . 
TA 5 HOH 6   1106 658  HOH HOH B . 
TA 5 HOH 7   1107 283  HOH HOH B . 
TA 5 HOH 8   1108 7    HOH HOH B . 
TA 5 HOH 9   1109 382  HOH HOH B . 
TA 5 HOH 10  1110 376  HOH HOH B . 
TA 5 HOH 11  1111 326  HOH HOH B . 
TA 5 HOH 12  1112 480  HOH HOH B . 
TA 5 HOH 13  1113 76   HOH HOH B . 
TA 5 HOH 14  1114 268  HOH HOH B . 
TA 5 HOH 15  1115 394  HOH HOH B . 
TA 5 HOH 16  1116 271  HOH HOH B . 
TA 5 HOH 17  1117 373  HOH HOH B . 
TA 5 HOH 18  1118 574  HOH HOH B . 
TA 5 HOH 19  1119 310  HOH HOH B . 
TA 5 HOH 20  1120 152  HOH HOH B . 
TA 5 HOH 21  1121 559  HOH HOH B . 
TA 5 HOH 22  1122 93   HOH HOH B . 
TA 5 HOH 23  1123 270  HOH HOH B . 
TA 5 HOH 24  1124 50   HOH HOH B . 
TA 5 HOH 25  1125 587  HOH HOH B . 
TA 5 HOH 26  1126 10   HOH HOH B . 
TA 5 HOH 27  1127 327  HOH HOH B . 
TA 5 HOH 28  1128 395  HOH HOH B . 
TA 5 HOH 29  1129 328  HOH HOH B . 
TA 5 HOH 30  1130 107  HOH HOH B . 
TA 5 HOH 31  1131 39   HOH HOH B . 
TA 5 HOH 32  1132 72   HOH HOH B . 
TA 5 HOH 33  1133 34   HOH HOH B . 
TA 5 HOH 34  1134 535  HOH HOH B . 
TA 5 HOH 35  1135 106  HOH HOH B . 
TA 5 HOH 36  1136 116  HOH HOH B . 
TA 5 HOH 37  1137 265  HOH HOH B . 
TA 5 HOH 38  1138 329  HOH HOH B . 
TA 5 HOH 39  1139 387  HOH HOH B . 
TA 5 HOH 40  1140 566  HOH HOH B . 
TA 5 HOH 41  1141 180  HOH HOH B . 
TA 5 HOH 42  1142 45   HOH HOH B . 
TA 5 HOH 43  1143 384  HOH HOH B . 
TA 5 HOH 44  1144 58   HOH HOH B . 
TA 5 HOH 45  1145 150  HOH HOH B . 
TA 5 HOH 46  1146 103  HOH HOH B . 
TA 5 HOH 47  1147 393  HOH HOH B . 
TA 5 HOH 48  1148 9    HOH HOH B . 
TA 5 HOH 49  1149 309  HOH HOH B . 
TA 5 HOH 50  1150 467  HOH HOH B . 
TA 5 HOH 51  1151 305  HOH HOH B . 
TA 5 HOH 52  1152 370  HOH HOH B . 
TA 5 HOH 53  1153 88   HOH HOH B . 
TA 5 HOH 54  1154 623  HOH HOH B . 
TA 5 HOH 55  1155 8    HOH HOH B . 
TA 5 HOH 56  1156 366  HOH HOH B . 
TA 5 HOH 57  1157 233  HOH HOH B . 
TA 5 HOH 58  1158 381  HOH HOH B . 
TA 5 HOH 59  1159 481  HOH HOH B . 
TA 5 HOH 60  1160 155  HOH HOH B . 
TA 5 HOH 61  1161 484  HOH HOH B . 
TA 5 HOH 62  1162 469  HOH HOH B . 
TA 5 HOH 63  1163 590  HOH HOH B . 
TA 5 HOH 64  1164 122  HOH HOH B . 
TA 5 HOH 65  1165 325  HOH HOH B . 
TA 5 HOH 66  1166 372  HOH HOH B . 
TA 5 HOH 67  1167 468  HOH HOH B . 
TA 5 HOH 68  1168 536  HOH HOH B . 
TA 5 HOH 69  1169 594  HOH HOH B . 
TA 5 HOH 70  1170 52   HOH HOH B . 
TA 5 HOH 71  1171 490  HOH HOH B . 
TA 5 HOH 72  1172 496  HOH HOH B . 
TA 5 HOH 73  1173 375  HOH HOH B . 
TA 5 HOH 74  1174 397  HOH HOH B . 
TA 5 HOH 75  1175 269  HOH HOH B . 
TA 5 HOH 76  1176 158  HOH HOH B . 
TA 5 HOH 77  1177 109  HOH HOH B . 
TA 5 HOH 78  1178 159  HOH HOH B . 
TA 5 HOH 79  1179 68   HOH HOH B . 
TA 5 HOH 80  1180 592  HOH HOH B . 
TA 5 HOH 81  1181 495  HOH HOH B . 
TA 5 HOH 82  1182 266  HOH HOH B . 
TA 5 HOH 83  1183 474  HOH HOH B . 
TA 5 HOH 84  1184 156  HOH HOH B . 
TA 5 HOH 85  1185 367  HOH HOH B . 
TA 5 HOH 86  1186 377  HOH HOH B . 
TA 5 HOH 87  1187 529  HOH HOH B . 
TA 5 HOH 88  1188 635  HOH HOH B . 
TA 5 HOH 89  1189 392  HOH HOH B . 
TA 5 HOH 90  1190 608  HOH HOH B . 
TA 5 HOH 91  1191 36   HOH HOH B . 
TA 5 HOH 92  1192 396  HOH HOH B . 
TA 5 HOH 93  1193 388  HOH HOH B . 
TA 5 HOH 94  1194 632  HOH HOH B . 
TA 5 HOH 95  1195 441  HOH HOH B . 
TA 5 HOH 96  1196 308  HOH HOH B . 
TA 5 HOH 97  1197 311  HOH HOH B . 
TA 5 HOH 98  1198 564  HOH HOH B . 
TA 5 HOH 99  1199 157  HOH HOH B . 
TA 5 HOH 100 1200 378  HOH HOH B . 
TA 5 HOH 101 1201 512  HOH HOH B . 
TA 5 HOH 102 1202 631  HOH HOH B . 
TA 5 HOH 103 1203 380  HOH HOH B . 
TA 5 HOH 104 1204 333  HOH HOH B . 
TA 5 HOH 105 1205 151  HOH HOH B . 
TA 5 HOH 106 1206 350  HOH HOH B . 
TA 5 HOH 107 1207 102  HOH HOH B . 
TA 5 HOH 108 1208 510  HOH HOH B . 
TA 5 HOH 109 1209 644  HOH HOH B . 
TA 5 HOH 110 1210 565  HOH HOH B . 
TA 5 HOH 111 1211 531  HOH HOH B . 
TA 5 HOH 112 1212 6    HOH HOH B . 
TA 5 HOH 113 1213 654  HOH HOH B . 
TA 5 HOH 114 1214 153  HOH HOH B . 
TA 5 HOH 115 1215 386  HOH HOH B . 
TA 5 HOH 116 1216 383  HOH HOH B . 
TA 5 HOH 117 1217 337  HOH HOH B . 
TA 5 HOH 118 1218 267  HOH HOH B . 
TA 5 HOH 119 1219 576  HOH HOH B . 
TA 5 HOH 120 1220 369  HOH HOH B . 
TA 5 HOH 121 1221 209  HOH HOH B . 
TA 5 HOH 122 1222 154  HOH HOH B . 
TA 5 HOH 123 1223 374  HOH HOH B . 
TA 5 HOH 124 1224 205  HOH HOH B . 
TA 5 HOH 125 1225 633  HOH HOH B . 
UA 5 HOH 1   1101 408  HOH HOH C . 
UA 5 HOH 2   1102 165  HOH HOH C . 
UA 5 HOH 3   1103 127  HOH HOH C . 
UA 5 HOH 4   1104 581  HOH HOH C . 
UA 5 HOH 5   1105 330  HOH HOH C . 
UA 5 HOH 6   1106 402  HOH HOH C . 
UA 5 HOH 7   1107 128  HOH HOH C . 
UA 5 HOH 8   1108 511  HOH HOH C . 
UA 5 HOH 9   1109 282  HOH HOH C . 
UA 5 HOH 10  1110 298  HOH HOH C . 
UA 5 HOH 11  1111 321  HOH HOH C . 
UA 5 HOH 12  1112 12   HOH HOH C . 
UA 5 HOH 13  1113 77   HOH HOH C . 
UA 5 HOH 14  1114 299  HOH HOH C . 
UA 5 HOH 15  1115 47   HOH HOH C . 
UA 5 HOH 16  1116 313  HOH HOH C . 
UA 5 HOH 17  1117 38   HOH HOH C . 
UA 5 HOH 18  1118 515  HOH HOH C . 
UA 5 HOH 19  1119 331  HOH HOH C . 
UA 5 HOH 20  1120 404  HOH HOH C . 
UA 5 HOH 21  1121 32   HOH HOH C . 
UA 5 HOH 22  1122 285  HOH HOH C . 
UA 5 HOH 23  1123 573  HOH HOH C . 
UA 5 HOH 24  1124 49   HOH HOH C . 
UA 5 HOH 25  1125 124  HOH HOH C . 
UA 5 HOH 26  1126 14   HOH HOH C . 
UA 5 HOH 27  1127 123  HOH HOH C . 
UA 5 HOH 28  1128 15   HOH HOH C . 
UA 5 HOH 29  1129 548  HOH HOH C . 
UA 5 HOH 30  1130 13   HOH HOH C . 
UA 5 HOH 31  1131 173  HOH HOH C . 
UA 5 HOH 32  1132 160  HOH HOH C . 
UA 5 HOH 33  1133 391  HOH HOH C . 
UA 5 HOH 34  1134 301  HOH HOH C . 
UA 5 HOH 35  1135 405  HOH HOH C . 
UA 5 HOH 36  1136 62   HOH HOH C . 
UA 5 HOH 37  1137 74   HOH HOH C . 
UA 5 HOH 38  1138 588  HOH HOH C . 
UA 5 HOH 39  1139 179  HOH HOH C . 
UA 5 HOH 40  1140 477  HOH HOH C . 
UA 5 HOH 41  1141 401  HOH HOH C . 
UA 5 HOH 42  1142 164  HOH HOH C . 
UA 5 HOH 43  1143 42   HOH HOH C . 
UA 5 HOH 44  1144 163  HOH HOH C . 
UA 5 HOH 45  1145 582  HOH HOH C . 
UA 5 HOH 46  1146 176  HOH HOH C . 
UA 5 HOH 47  1147 607  HOH HOH C . 
UA 5 HOH 48  1148 479  HOH HOH C . 
UA 5 HOH 49  1149 82   HOH HOH C . 
UA 5 HOH 50  1150 338  HOH HOH C . 
UA 5 HOH 51  1151 40   HOH HOH C . 
UA 5 HOH 52  1152 60   HOH HOH C . 
UA 5 HOH 53  1153 487  HOH HOH C . 
UA 5 HOH 54  1154 302  HOH HOH C . 
UA 5 HOH 55  1155 161  HOH HOH C . 
UA 5 HOH 56  1156 593  HOH HOH C . 
UA 5 HOH 57  1157 390  HOH HOH C . 
UA 5 HOH 58  1158 166  HOH HOH C . 
UA 5 HOH 59  1159 162  HOH HOH C . 
UA 5 HOH 60  1160 304  HOH HOH C . 
UA 5 HOH 61  1161 332  HOH HOH C . 
UA 5 HOH 62  1162 466  HOH HOH C . 
UA 5 HOH 63  1163 44   HOH HOH C . 
UA 5 HOH 64  1164 48   HOH HOH C . 
UA 5 HOH 65  1165 579  HOH HOH C . 
UA 5 HOH 66  1166 532  HOH HOH C . 
UA 5 HOH 67  1167 297  HOH HOH C . 
UA 5 HOH 68  1168 86   HOH HOH C . 
UA 5 HOH 69  1169 606  HOH HOH C . 
UA 5 HOH 70  1170 108  HOH HOH C . 
UA 5 HOH 71  1171 353  HOH HOH C . 
UA 5 HOH 72  1172 659  HOH HOH C . 
UA 5 HOH 73  1173 70   HOH HOH C . 
UA 5 HOH 74  1174 264  HOH HOH C . 
UA 5 HOH 75  1175 174  HOH HOH C . 
UA 5 HOH 76  1176 595  HOH HOH C . 
UA 5 HOH 77  1177 516  HOH HOH C . 
UA 5 HOH 78  1178 482  HOH HOH C . 
UA 5 HOH 79  1179 170  HOH HOH C . 
UA 5 HOH 80  1180 43   HOH HOH C . 
UA 5 HOH 81  1181 406  HOH HOH C . 
UA 5 HOH 82  1182 167  HOH HOH C . 
UA 5 HOH 83  1183 79   HOH HOH C . 
UA 5 HOH 84  1184 518  HOH HOH C . 
UA 5 HOH 85  1185 339  HOH HOH C . 
UA 5 HOH 86  1186 324  HOH HOH C . 
UA 5 HOH 87  1187 398  HOH HOH C . 
UA 5 HOH 88  1188 168  HOH HOH C . 
UA 5 HOH 89  1189 175  HOH HOH C . 
UA 5 HOH 90  1190 281  HOH HOH C . 
UA 5 HOH 91  1191 181  HOH HOH C . 
UA 5 HOH 92  1192 400  HOH HOH C . 
UA 5 HOH 93  1193 533  HOH HOH C . 
UA 5 HOH 94  1194 637  HOH HOH C . 
UA 5 HOH 95  1195 473  HOH HOH C . 
UA 5 HOH 96  1196 110  HOH HOH C . 
UA 5 HOH 97  1197 307  HOH HOH C . 
UA 5 HOH 98  1198 619  HOH HOH C . 
UA 5 HOH 99  1199 589  HOH HOH C . 
UA 5 HOH 100 1200 514  HOH HOH C . 
UA 5 HOH 101 1201 336  HOH HOH C . 
UA 5 HOH 102 1202 171  HOH HOH C . 
UA 5 HOH 103 1203 379  HOH HOH C . 
UA 5 HOH 104 1204 177  HOH HOH C . 
UA 5 HOH 105 1205 616  HOH HOH C . 
UA 5 HOH 106 1206 465  HOH HOH C . 
UA 5 HOH 107 1207 513  HOH HOH C . 
UA 5 HOH 108 1208 599  HOH HOH C . 
UA 5 HOH 109 1209 389  HOH HOH C . 
UA 5 HOH 110 1210 334  HOH HOH C . 
UA 5 HOH 111 1211 172  HOH HOH C . 
UA 5 HOH 112 1212 178  HOH HOH C . 
UA 5 HOH 113 1213 634  HOH HOH C . 
UA 5 HOH 114 1214 534  HOH HOH C . 
UA 5 HOH 115 1215 639  HOH HOH C . 
UA 5 HOH 116 1216 66   HOH HOH C . 
UA 5 HOH 117 1217 636  HOH HOH C . 
UA 5 HOH 118 1218 129  HOH HOH C . 
UA 5 HOH 119 1219 340  HOH HOH C . 
UA 5 HOH 120 1220 517  HOH HOH C . 
UA 5 HOH 121 1221 11   HOH HOH C . 
UA 5 HOH 122 1222 335  HOH HOH C . 
UA 5 HOH 123 1223 475  HOH HOH C . 
UA 5 HOH 124 1224 169  HOH HOH C . 
UA 5 HOH 125 1225 403  HOH HOH C . 
UA 5 HOH 126 1226 182  HOH HOH C . 
UA 5 HOH 127 1227 638  HOH HOH C . 
UA 5 HOH 128 1228 286  HOH HOH C . 
UA 5 HOH 129 1229 463  HOH HOH C . 
UA 5 HOH 130 1230 464  HOH HOH C . 
UA 5 HOH 131 1231 272  HOH HOH C . 
UA 5 HOH 132 1232 345  HOH HOH C . 
UA 5 HOH 133 1233 407  HOH HOH C . 
UA 5 HOH 134 1234 132  HOH HOH C . 
UA 5 HOH 135 1235 586  HOH HOH C . 
VA 5 HOH 1   601  96   HOH HOH D . 
VA 5 HOH 2   602  427  HOH HOH D . 
VA 5 HOH 3   603  99   HOH HOH D . 
VA 5 HOH 4   604  488  HOH HOH D . 
VA 5 HOH 5   605  414  HOH HOH D . 
VA 5 HOH 6   606  59   HOH HOH D . 
VA 5 HOH 7   607  3    HOH HOH D . 
VA 5 HOH 8   608  424  HOH HOH D . 
VA 5 HOH 9   609  361  HOH HOH D . 
VA 5 HOH 10  610  16   HOH HOH D . 
VA 5 HOH 11  611  193  HOH HOH D . 
VA 5 HOH 12  612  91   HOH HOH D . 
VA 5 HOH 13  613  289  HOH HOH D . 
VA 5 HOH 14  614  425  HOH HOH D . 
VA 5 HOH 15  615  600  HOH HOH D . 
VA 5 HOH 16  616  300  HOH HOH D . 
VA 5 HOH 17  617  18   HOH HOH D . 
VA 5 HOH 18  618  555  HOH HOH D . 
VA 5 HOH 19  619  431  HOH HOH D . 
VA 5 HOH 20  620  64   HOH HOH D . 
VA 5 HOH 21  621  292  HOH HOH D . 
VA 5 HOH 22  622  19   HOH HOH D . 
VA 5 HOH 23  623  35   HOH HOH D . 
VA 5 HOH 24  624  478  HOH HOH D . 
VA 5 HOH 25  625  187  HOH HOH D . 
VA 5 HOH 26  626  530  HOH HOH D . 
VA 5 HOH 27  627  188  HOH HOH D . 
VA 5 HOH 28  628  354  HOH HOH D . 
VA 5 HOH 29  629  46   HOH HOH D . 
VA 5 HOH 30  630  605  HOH HOH D . 
VA 5 HOH 31  631  415  HOH HOH D . 
VA 5 HOH 32  632  61   HOH HOH D . 
VA 5 HOH 33  633  192  HOH HOH D . 
VA 5 HOH 34  634  471  HOH HOH D . 
VA 5 HOH 35  635  419  HOH HOH D . 
VA 5 HOH 36  636  322  HOH HOH D . 
VA 5 HOH 37  637  552  HOH HOH D . 
VA 5 HOH 38  638  196  HOH HOH D . 
VA 5 HOH 39  639  189  HOH HOH D . 
VA 5 HOH 40  640  67   HOH HOH D . 
VA 5 HOH 41  641  613  HOH HOH D . 
VA 5 HOH 42  642  75   HOH HOH D . 
VA 5 HOH 43  643  201  HOH HOH D . 
VA 5 HOH 44  644  199  HOH HOH D . 
VA 5 HOH 45  645  312  HOH HOH D . 
VA 5 HOH 46  646  523  HOH HOH D . 
VA 5 HOH 47  647  121  HOH HOH D . 
VA 5 HOH 48  648  291  HOH HOH D . 
VA 5 HOH 49  649  20   HOH HOH D . 
VA 5 HOH 50  650  551  HOH HOH D . 
VA 5 HOH 51  651  413  HOH HOH D . 
VA 5 HOH 52  652  197  HOH HOH D . 
VA 5 HOH 53  653  416  HOH HOH D . 
VA 5 HOH 54  654  202  HOH HOH D . 
VA 5 HOH 55  655  506  HOH HOH D . 
VA 5 HOH 56  656  497  HOH HOH D . 
VA 5 HOH 57  657  191  HOH HOH D . 
VA 5 HOH 58  658  621  HOH HOH D . 
VA 5 HOH 59  659  411  HOH HOH D . 
VA 5 HOH 60  660  293  HOH HOH D . 
VA 5 HOH 61  661  553  HOH HOH D . 
VA 5 HOH 62  662  556  HOH HOH D . 
VA 5 HOH 63  663  200  HOH HOH D . 
VA 5 HOH 64  664  294  HOH HOH D . 
VA 5 HOH 65  665  296  HOH HOH D . 
VA 5 HOH 66  666  612  HOH HOH D . 
VA 5 HOH 67  667  428  HOH HOH D . 
VA 5 HOH 68  668  421  HOH HOH D . 
VA 5 HOH 69  669  554  HOH HOH D . 
VA 5 HOH 70  670  104  HOH HOH D . 
VA 5 HOH 71  671  295  HOH HOH D . 
VA 5 HOH 72  672  550  HOH HOH D . 
VA 5 HOH 73  673  423  HOH HOH D . 
VA 5 HOH 74  674  198  HOH HOH D . 
VA 5 HOH 75  675  184  HOH HOH D . 
VA 5 HOH 76  676  183  HOH HOH D . 
VA 5 HOH 77  677  640  HOH HOH D . 
VA 5 HOH 78  678  641  HOH HOH D . 
VA 5 HOH 79  679  601  HOH HOH D . 
VA 5 HOH 80  680  418  HOH HOH D . 
VA 5 HOH 81  681  461  HOH HOH D . 
VA 5 HOH 82  682  627  HOH HOH D . 
VA 5 HOH 83  683  412  HOH HOH D . 
VA 5 HOH 84  684  430  HOH HOH D . 
VA 5 HOH 85  685  185  HOH HOH D . 
VA 5 HOH 86  686  422  HOH HOH D . 
VA 5 HOH 87  687  420  HOH HOH D . 
VA 5 HOH 88  688  288  HOH HOH D . 
VA 5 HOH 89  689  417  HOH HOH D . 
VA 5 HOH 90  690  525  HOH HOH D . 
VA 5 HOH 91  691  347  HOH HOH D . 
VA 5 HOH 92  692  190  HOH HOH D . 
VA 5 HOH 93  693  429  HOH HOH D . 
VA 5 HOH 94  694  557  HOH HOH D . 
VA 5 HOH 95  695  5    HOH HOH D . 
VA 5 HOH 96  696  409  HOH HOH D . 
VA 5 HOH 97  697  17   HOH HOH D . 
VA 5 HOH 98  698  194  HOH HOH D . 
VA 5 HOH 99  699  195  HOH HOH D . 
WA 5 HOH 1   601  435  HOH HOH E . 
WA 5 HOH 2   602  492  HOH HOH E . 
WA 5 HOH 3   603  443  HOH HOH E . 
WA 5 HOH 4   604  445  HOH HOH E . 
WA 5 HOH 5   605  434  HOH HOH E . 
WA 5 HOH 6   606  41   HOH HOH E . 
WA 5 HOH 7   607  236  HOH HOH E . 
WA 5 HOH 8   608  24   HOH HOH E . 
WA 5 HOH 9   609  98   HOH HOH E . 
WA 5 HOH 10  610  439  HOH HOH E . 
WA 5 HOH 11  611  225  HOH HOH E . 
WA 5 HOH 12  612  206  HOH HOH E . 
WA 5 HOH 13  613  23   HOH HOH E . 
WA 5 HOH 14  614  26   HOH HOH E . 
WA 5 HOH 15  615  316  HOH HOH E . 
WA 5 HOH 16  616  28   HOH HOH E . 
WA 5 HOH 17  617  226  HOH HOH E . 
WA 5 HOH 18  618  222  HOH HOH E . 
WA 5 HOH 19  619  541  HOH HOH E . 
WA 5 HOH 20  620  242  HOH HOH E . 
WA 5 HOH 21  621  218  HOH HOH E . 
WA 5 HOH 22  622  22   HOH HOH E . 
WA 5 HOH 23  623  560  HOH HOH E . 
WA 5 HOH 24  624  524  HOH HOH E . 
WA 5 HOH 25  625  648  HOH HOH E . 
WA 5 HOH 26  626  444  HOH HOH E . 
WA 5 HOH 27  627  432  HOH HOH E . 
WA 5 HOH 28  628  210  HOH HOH E . 
WA 5 HOH 29  629  21   HOH HOH E . 
WA 5 HOH 30  630  216  HOH HOH E . 
WA 5 HOH 31  631  231  HOH HOH E . 
WA 5 HOH 32  632  342  HOH HOH E . 
WA 5 HOH 33  633  539  HOH HOH E . 
WA 5 HOH 34  634  314  HOH HOH E . 
WA 5 HOH 35  635  567  HOH HOH E . 
WA 5 HOH 36  636  438  HOH HOH E . 
WA 5 HOH 37  637  219  HOH HOH E . 
WA 5 HOH 38  638  33   HOH HOH E . 
WA 5 HOH 39  639  277  HOH HOH E . 
WA 5 HOH 40  640  117  HOH HOH E . 
WA 5 HOH 41  641  57   HOH HOH E . 
WA 5 HOH 42  642  208  HOH HOH E . 
WA 5 HOH 43  643  341  HOH HOH E . 
WA 5 HOH 44  644  238  HOH HOH E . 
WA 5 HOH 45  645  120  HOH HOH E . 
WA 5 HOH 46  646  598  HOH HOH E . 
WA 5 HOH 47  647  213  HOH HOH E . 
WA 5 HOH 48  648  317  HOH HOH E . 
WA 5 HOH 49  649  240  HOH HOH E . 
WA 5 HOH 50  650  476  HOH HOH E . 
WA 5 HOH 51  651  230  HOH HOH E . 
WA 5 HOH 52  652  572  HOH HOH E . 
WA 5 HOH 53  653  611  HOH HOH E . 
WA 5 HOH 54  654  437  HOH HOH E . 
WA 5 HOH 55  655  499  HOH HOH E . 
WA 5 HOH 56  656  234  HOH HOH E . 
WA 5 HOH 57  657  204  HOH HOH E . 
WA 5 HOH 58  658  442  HOH HOH E . 
WA 5 HOH 59  659  80   HOH HOH E . 
WA 5 HOH 60  660  69   HOH HOH E . 
WA 5 HOH 61  661  224  HOH HOH E . 
WA 5 HOH 62  662  51   HOH HOH E . 
WA 5 HOH 63  663  245  HOH HOH E . 
WA 5 HOH 64  664  498  HOH HOH E . 
WA 5 HOH 65  665  609  HOH HOH E . 
WA 5 HOH 66  666  232  HOH HOH E . 
WA 5 HOH 67  667  521  HOH HOH E . 
WA 5 HOH 68  668  436  HOH HOH E . 
WA 5 HOH 69  669  440  HOH HOH E . 
WA 5 HOH 70  670  53   HOH HOH E . 
WA 5 HOH 71  671  569  HOH HOH E . 
WA 5 HOH 72  672  55   HOH HOH E . 
WA 5 HOH 73  673  118  HOH HOH E . 
WA 5 HOH 74  674  643  HOH HOH E . 
WA 5 HOH 75  675  215  HOH HOH E . 
WA 5 HOH 76  676  446  HOH HOH E . 
WA 5 HOH 77  677  228  HOH HOH E . 
WA 5 HOH 78  678  214  HOH HOH E . 
WA 5 HOH 79  679  645  HOH HOH E . 
WA 5 HOH 80  680  119  HOH HOH E . 
WA 5 HOH 81  681  570  HOH HOH E . 
WA 5 HOH 82  682  542  HOH HOH E . 
WA 5 HOH 83  683  491  HOH HOH E . 
WA 5 HOH 84  684  229  HOH HOH E . 
WA 5 HOH 85  685  628  HOH HOH E . 
WA 5 HOH 86  686  278  HOH HOH E . 
WA 5 HOH 87  687  227  HOH HOH E . 
WA 5 HOH 88  688  540  HOH HOH E . 
WA 5 HOH 89  689  239  HOH HOH E . 
WA 5 HOH 90  690  618  HOH HOH E . 
WA 5 HOH 91  691  235  HOH HOH E . 
WA 5 HOH 92  692  653  HOH HOH E . 
WA 5 HOH 93  693  203  HOH HOH E . 
WA 5 HOH 94  694  237  HOH HOH E . 
WA 5 HOH 95  695  647  HOH HOH E . 
WA 5 HOH 96  696  584  HOH HOH E . 
WA 5 HOH 97  697  522  HOH HOH E . 
WA 5 HOH 98  698  211  HOH HOH E . 
WA 5 HOH 99  699  657  HOH HOH E . 
WA 5 HOH 100 700  220  HOH HOH E . 
WA 5 HOH 101 701  433  HOH HOH E . 
WA 5 HOH 102 702  212  HOH HOH E . 
WA 5 HOH 103 703  571  HOH HOH E . 
WA 5 HOH 104 704  368  HOH HOH E . 
WA 5 HOH 105 705  646  HOH HOH E . 
WA 5 HOH 106 706  207  HOH HOH E . 
WA 5 HOH 107 707  25   HOH HOH E . 
WA 5 HOH 108 708  223  HOH HOH E . 
WA 5 HOH 109 709  410  HOH HOH E . 
WA 5 HOH 110 710  462  HOH HOH E . 
WA 5 HOH 111 711  126  HOH HOH E . 
WA 5 HOH 112 712  558  HOH HOH E . 
XA 5 HOH 1   601  453  HOH HOH F . 
XA 5 HOH 2   602  306  HOH HOH F . 
XA 5 HOH 3   603  87   HOH HOH F . 
XA 5 HOH 4   604  27   HOH HOH F . 
XA 5 HOH 5   605  29   HOH HOH F . 
XA 5 HOH 6   606  248  HOH HOH F . 
XA 5 HOH 7   607  90   HOH HOH F . 
XA 5 HOH 8   608  543  HOH HOH F . 
XA 5 HOH 9   609  318  HOH HOH F . 
XA 5 HOH 10  610  114  HOH HOH F . 
XA 5 HOH 11  611  244  HOH HOH F . 
XA 5 HOH 12  612  519  HOH HOH F . 
XA 5 HOH 13  613  602  HOH HOH F . 
XA 5 HOH 14  614  251  HOH HOH F . 
XA 5 HOH 15  615  260  HOH HOH F . 
XA 5 HOH 16  616  486  HOH HOH F . 
XA 5 HOH 17  617  65   HOH HOH F . 
XA 5 HOH 18  618  31   HOH HOH F . 
XA 5 HOH 19  619  54   HOH HOH F . 
XA 5 HOH 20  620  256  HOH HOH F . 
XA 5 HOH 21  621  561  HOH HOH F . 
XA 5 HOH 22  622  95   HOH HOH F . 
XA 5 HOH 23  623  186  HOH HOH F . 
XA 5 HOH 24  624  577  HOH HOH F . 
XA 5 HOH 25  625  456  HOH HOH F . 
XA 5 HOH 26  626  273  HOH HOH F . 
XA 5 HOH 27  627  457  HOH HOH F . 
XA 5 HOH 28  628  247  HOH HOH F . 
XA 5 HOH 29  629  241  HOH HOH F . 
XA 5 HOH 30  630  500  HOH HOH F . 
XA 5 HOH 31  631  501  HOH HOH F . 
XA 5 HOH 32  632  562  HOH HOH F . 
XA 5 HOH 33  633  105  HOH HOH F . 
XA 5 HOH 34  634  92   HOH HOH F . 
XA 5 HOH 35  635  249  HOH HOH F . 
XA 5 HOH 36  636  113  HOH HOH F . 
XA 5 HOH 37  637  583  HOH HOH F . 
XA 5 HOH 38  638  274  HOH HOH F . 
XA 5 HOH 39  639  221  HOH HOH F . 
XA 5 HOH 40  640  629  HOH HOH F . 
XA 5 HOH 41  641  537  HOH HOH F . 
XA 5 HOH 42  642  624  HOH HOH F . 
XA 5 HOH 43  643  460  HOH HOH F . 
XA 5 HOH 44  644  276  HOH HOH F . 
XA 5 HOH 45  645  100  HOH HOH F . 
XA 5 HOH 46  646  597  HOH HOH F . 
XA 5 HOH 47  647  451  HOH HOH F . 
XA 5 HOH 48  648  614  HOH HOH F . 
XA 5 HOH 49  649  85   HOH HOH F . 
XA 5 HOH 50  650  94   HOH HOH F . 
XA 5 HOH 51  651  493  HOH HOH F . 
XA 5 HOH 52  652  101  HOH HOH F . 
XA 5 HOH 53  653  452  HOH HOH F . 
XA 5 HOH 54  654  246  HOH HOH F . 
XA 5 HOH 55  655  448  HOH HOH F . 
XA 5 HOH 56  656  610  HOH HOH F . 
XA 5 HOH 57  657  259  HOH HOH F . 
XA 5 HOH 58  658  526  HOH HOH F . 
XA 5 HOH 59  659  596  HOH HOH F . 
XA 5 HOH 60  660  489  HOH HOH F . 
XA 5 HOH 61  661  454  HOH HOH F . 
XA 5 HOH 62  662  651  HOH HOH F . 
XA 5 HOH 63  663  447  HOH HOH F . 
XA 5 HOH 64  664  575  HOH HOH F . 
XA 5 HOH 65  665  450  HOH HOH F . 
XA 5 HOH 66  666  528  HOH HOH F . 
XA 5 HOH 67  667  254  HOH HOH F . 
XA 5 HOH 68  668  385  HOH HOH F . 
XA 5 HOH 69  669  630  HOH HOH F . 
XA 5 HOH 70  670  494  HOH HOH F . 
XA 5 HOH 71  671  115  HOH HOH F . 
XA 5 HOH 72  672  253  HOH HOH F . 
XA 5 HOH 73  673  563  HOH HOH F . 
XA 5 HOH 74  674  527  HOH HOH F . 
XA 5 HOH 75  675  642  HOH HOH F . 
XA 5 HOH 76  676  252  HOH HOH F . 
XA 5 HOH 77  677  258  HOH HOH F . 
XA 5 HOH 78  678  217  HOH HOH F . 
XA 5 HOH 79  679  538  HOH HOH F . 
XA 5 HOH 80  680  275  HOH HOH F . 
XA 5 HOH 81  681  344  HOH HOH F . 
XA 5 HOH 82  682  255  HOH HOH F . 
XA 5 HOH 83  683  620  HOH HOH F . 
XA 5 HOH 84  684  250  HOH HOH F . 
XA 5 HOH 85  685  449  HOH HOH F . 
XA 5 HOH 86  686  243  HOH HOH F . 
XA 5 HOH 87  687  257  HOH HOH F . 
XA 5 HOH 88  688  455  HOH HOH F . 
XA 5 HOH 89  689  649  HOH HOH F . 
XA 5 HOH 90  690  622  HOH HOH F . 
XA 5 HOH 91  691  343  HOH HOH F . 
XA 5 HOH 92  692  112  HOH HOH F . 
XA 5 HOH 93  693  30   HOH HOH F . 
XA 5 HOH 94  694  458  HOH HOH F . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0218 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? 20180126 2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? 20180126 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? 11.6.02  4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.24     5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   118.67 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6GHV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     105.612 
_cell.length_a_esd                 ? 
_cell.length_b                     57.507 
_cell.length_b_esd                 ? 
_cell.length_c                     107.247 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         6GHV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   6GHV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            3.15 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         60.90 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;20% PEG 3350, 200mM Mg(NO3)2, 100mM MES pH6. Protein sample: 150mM NaCl, 4mM CaCl2, 25mM Tris pH8, 2% DMSO, 3.25 mM ligand and 5.54mg/mL protein.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-02-27 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.966 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.966 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate            34.771 
_reflns.entry_id                         6GHV 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.100 
_reflns.d_resolution_low                 40.000 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       65455 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             98.400 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.087 
_reflns.pdbx_Rmerge_I_obs                0.099 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            8.470 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 1.005 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.120 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.993 
_reflns.pdbx_R_split                     ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_R_split 
2.100  2.200  ? 2.010  ? ? ? ? 8427  97.900 ? ? ? ? 0.545 ? ? ? ? ? ? ? ? 2.807 ? ? ? ? 0.668 ? ? 1  1 0.769 ? 
2.200  2.400  ? 3.000  ? ? ? ? 13028 98.700 ? ? ? ? 0.397 ? ? ? ? ? ? ? ? 3.139 ? ? ? ? 0.478 ? ? 2  1 0.868 ? 
2.400  2.900  ? 6.140  ? ? ? ? 19053 99.300 ? ? ? ? 0.198 ? ? ? ? ? ? ? ? 3.221 ? ? ? ? 0.238 ? ? 3  1 0.956 ? 
2.900  3.500  ? 11.540 ? ? ? ? 10721 98.500 ? ? ? ? 0.090 ? ? ? ? ? ? ? ? 3.059 ? ? ? ? 0.110 ? ? 4  1 0.987 ? 
3.500  4.500  ? 16.770 ? ? ? ? 7446  97.200 ? ? ? ? 0.056 ? ? ? ? ? ? ? ? 2.812 ? ? ? ? 0.069 ? ? 5  1 0.993 ? 
4.500  6.000  ? 18.970 ? ? ? ? 3909  98.100 ? ? ? ? 0.054 ? ? ? ? ? ? ? ? 3.358 ? ? ? ? 0.065 ? ? 6  1 0.994 ? 
6.000  8.000  ? 18.620 ? ? ? ? 1649  97.100 ? ? ? ? 0.056 ? ? ? ? ? ? ? ? 3.317 ? ? ? ? 0.066 ? ? 7  1 0.993 ? 
8.000  11.000 ? 22.170 ? ? ? ? 750   95.400 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? 3.215 ? ? ? ? 0.052 ? ? 8  1 0.997 ? 
11.000 15.000 ? 23.830 ? ? ? ? 287   95.700 ? ? ? ? 0.039 ? ? ? ? ? ? ? ? 3.084 ? ? ? ? 0.047 ? ? 9  1 0.996 ? 
15.000 20.000 ? 24.520 ? ? ? ? 110   91.700 ? ? ? ? 0.036 ? ? ? ? ? ? ? ? 2.955 ? ? ? ? 0.044 ? ? 10 1 0.996 ? 
20.000 26.000 ? 22.170 ? ? ? ? 46    93.900 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 2.565 ? ? ? ? 0.050 ? ? 11 1 0.994 ? 
26.000 35.000 ? 23.490 ? ? ? ? 20    87.000 ? ? ? ? 0.042 ? ? ? ? ? ? ? ? 2.300 ? ? ? ? 0.056 ? ? 12 1 0.987 ? 
35.000 45.000 ? 20.180 ? ? ? ? 9     90.000 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 1.667 ? ? ? ? 0.046 ? ? 13 1 0.995 ? 
40.000 45.000 ? ?      ? ? ? ? ?     ?      ? ? ? ? ?     ? ? ? ? ? ? ? ? ?     ? ? ? ? ?     ? ? 14 1 ?     ? 
# 
_refine.aniso_B[1][1]                            1.48 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.55 
_refine.aniso_B[2][2]                            -2.31 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.14 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               33.681 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.925 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 6GHV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             40.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     62185 
_refine.ls_number_reflns_R_free                  3261 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.55 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17879 
_refine.ls_R_factor_R_free                       0.23357 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17592 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1K9I 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.184 
_refine.pdbx_overall_ESU_R_Free                  0.175 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             5.856 
_refine.overall_SU_ML                            0.145 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        6444 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         344 
_refine_hist.number_atoms_solvent             660 
_refine_hist.number_atoms_total               7448 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        40.00 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.017  0.020  7139  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  5793  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.625  1.932  9737  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.113  3.019  13637 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.758  5.000  829   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.877 25.466 386   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.447 15.000 1072  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.049 15.000 24    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.099  0.200  938   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  7977  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1579  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.538  3.251  3214  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.534  3.249  3213  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.727  4.847  4017  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.727  4.849  4018  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.901  3.477  3925  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.901  3.476  3926  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.379  5.104  5701  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.114  37.375 8791  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.059  37.159 8707  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             235 
_refine_ls_shell.number_reflns_R_work             4508 
_refine_ls_shell.percent_reflns_obs               97.81 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.332 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.296 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     6GHV 
_struct.title                        'Structure of a DC-SIGN CRD in complex with high affinity glycomimetic.' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6GHV 
_struct_keywords.text            'DC-SIGN, Inhibitor, SUGAR BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'SUGAR BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 2 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 4 ? 
L  N N 4 ? 
M  N N 4 ? 
N  N N 2 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 4 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 4 ? 
Y  N N 4 ? 
Z  N N 4 ? 
AA N N 2 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 4 ? 
FA N N 4 ? 
GA N N 4 ? 
HA N N 2 ? 
IA N N 3 ? 
JA N N 3 ? 
KA N N 3 ? 
LA N N 4 ? 
MA N N 4 ? 
NA N N 2 ? 
OA N N 3 ? 
PA N N 3 ? 
QA N N 3 ? 
RA N N 4 ? 
SA N N 5 ? 
TA N N 5 ? 
UA N N 5 ? 
VA N N 5 ? 
WA N N 5 ? 
XA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CD209_HUMAN 
_struct_ref.pdbx_db_accession          Q9NNX6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQW
VDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA
;
_struct_ref.pdbx_align_begin           250 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 6GHV A 1 ? 155 ? Q9NNX6 250 ? 404 ? 250 404 
2 1 6GHV B 1 ? 155 ? Q9NNX6 250 ? 404 ? 250 404 
3 1 6GHV C 1 ? 155 ? Q9NNX6 250 ? 404 ? 250 404 
4 1 6GHV D 1 ? 155 ? Q9NNX6 250 ? 404 ? 250 404 
5 1 6GHV E 1 ? 155 ? Q9NNX6 250 ? 404 ? 250 404 
6 1 6GHV F 1 ? 155 ? Q9NNX6 250 ? 404 ? 250 404 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
5 author_defined_assembly ? monomeric 1 
6 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,G,H,I,J,K,L,M,SA        
2 1 B,N,O,P,Q,R,S,TA          
3 1 C,T,U,V,W,X,Y,UA          
4 1 D,Z,AA,BA,CA,DA,EA,VA     
5 1 E,FA,GA,HA,IA,JA,KA,LA,WA 
6 1 F,MA,NA,OA,PA,QA,RA,XA    
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 27 ? GLU A 37 ? ASN A 276 GLU A 286 1 ? 11 
HELX_P HELX_P2  AA2 SER A 47 ? ASN A 62 ? SER A 296 ASN A 311 1 ? 16 
HELX_P HELX_P3  AA3 LEU A 87 ? TRP A 94 ? LEU A 336 TRP A 343 5 ? 8  
HELX_P HELX_P4  AA4 ASN B 27 ? VAL B 38 ? ASN B 276 VAL B 287 1 ? 12 
HELX_P HELX_P5  AA5 SER B 47 ? ASN B 62 ? SER B 296 ASN B 311 1 ? 16 
HELX_P HELX_P6  AA6 LEU B 87 ? TRP B 94 ? LEU B 336 TRP B 343 5 ? 8  
HELX_P HELX_P7  AA7 ASN C 27 ? VAL C 38 ? ASN C 276 VAL C 287 1 ? 12 
HELX_P HELX_P8  AA8 SER C 47 ? ASN C 62 ? SER C 296 ASN C 311 1 ? 16 
HELX_P HELX_P9  AA9 LEU C 87 ? TRP C 94 ? LEU C 336 TRP C 343 5 ? 8  
HELX_P HELX_P10 AB1 ASN D 27 ? GLU D 37 ? ASN D 276 GLU D 286 1 ? 11 
HELX_P HELX_P11 AB2 SER D 47 ? ASN D 62 ? SER D 296 ASN D 311 1 ? 16 
HELX_P HELX_P12 AB3 LEU D 87 ? TRP D 94 ? LEU D 336 TRP D 343 5 ? 8  
HELX_P HELX_P13 AB4 ASN E 27 ? GLU E 37 ? ASN E 276 GLU E 286 1 ? 11 
HELX_P HELX_P14 AB5 SER E 47 ? ASN E 62 ? SER E 296 ASN E 311 1 ? 16 
HELX_P HELX_P15 AB6 LEU E 87 ? TRP E 94 ? LEU E 336 TRP E 343 5 ? 8  
HELX_P HELX_P16 AB7 ASN F 27 ? GLU F 37 ? ASN F 276 GLU F 286 1 ? 11 
HELX_P HELX_P17 AB8 SER F 47 ? ASN F 62 ? SER F 296 ASN F 311 1 ? 16 
HELX_P HELX_P18 AB9 LEU F 87 ? TRP F 94 ? LEU F 336 TRP F 343 5 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1   disulf ? ? A  CYS 4   SG  ? ? ? 1_555 A  CYS 135 SG ? ? A CYS 253  A CYS 384  1_555 ? ? ? ? ? ? ? 2.060 ? ? 
disulf2   disulf ? ? A  CYS 7   SG  ? ? ? 1_555 A  CYS 18  SG ? ? A CYS 256  A CYS 267  1_555 ? ? ? ? ? ? ? 2.067 ? ? 
disulf3   disulf ? ? A  CYS 35  SG  ? ? ? 1_555 A  CYS 128 SG ? ? A CYS 284  A CYS 377  1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf4   disulf ? ? A  CYS 107 SG  ? ? ? 1_555 A  CYS 120 SG ? ? A CYS 356  A CYS 369  1_555 ? ? ? ? ? ? ? 2.099 ? ? 
disulf5   disulf ? ? B  CYS 4   SG  ? ? ? 1_555 B  CYS 135 SG ? ? B CYS 253  B CYS 384  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf6   disulf ? ? B  CYS 7   SG  ? ? ? 1_555 B  CYS 18  SG ? ? B CYS 256  B CYS 267  1_555 ? ? ? ? ? ? ? 2.056 ? ? 
disulf7   disulf ? ? B  CYS 35  SG  ? ? ? 1_555 B  CYS 128 SG ? ? B CYS 284  B CYS 377  1_555 ? ? ? ? ? ? ? 2.078 ? ? 
disulf8   disulf ? ? B  CYS 107 SG  ? ? ? 1_555 B  CYS 120 SG ? ? B CYS 356  B CYS 369  1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf9   disulf ? ? C  CYS 4   SG  ? ? ? 1_555 C  CYS 135 SG ? ? C CYS 253  C CYS 384  1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf10  disulf ? ? C  CYS 7   SG  ? ? ? 1_555 C  CYS 18  SG ? ? C CYS 256  C CYS 267  1_555 ? ? ? ? ? ? ? 2.069 ? ? 
disulf11  disulf ? ? C  CYS 35  SG  ? ? ? 1_555 C  CYS 128 SG ? ? C CYS 284  C CYS 377  1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf12  disulf ? ? C  CYS 107 SG  ? ? ? 1_555 C  CYS 120 SG ? ? C CYS 356  C CYS 369  1_555 ? ? ? ? ? ? ? 1.999 ? ? 
disulf13  disulf ? ? D  CYS 4   SG  ? ? ? 1_555 D  CYS 135 SG ? ? D CYS 253  D CYS 384  1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf14  disulf ? ? D  CYS 7   SG  ? ? ? 1_555 D  CYS 18  SG ? ? D CYS 256  D CYS 267  1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf15  disulf ? ? D  CYS 35  SG  ? ? ? 1_555 D  CYS 128 SG ? ? D CYS 284  D CYS 377  1_555 ? ? ? ? ? ? ? 2.060 ? ? 
disulf16  disulf ? ? D  CYS 107 SG  ? ? ? 1_555 D  CYS 120 SG ? ? D CYS 356  D CYS 369  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf17  disulf ? ? E  CYS 4   SG  ? ? ? 1_555 E  CYS 135 SG ? ? E CYS 253  E CYS 384  1_555 ? ? ? ? ? ? ? 2.045 ? ? 
disulf18  disulf ? ? E  CYS 7   SG  ? ? ? 1_555 E  CYS 18  SG ? ? E CYS 256  E CYS 267  1_555 ? ? ? ? ? ? ? 2.066 ? ? 
disulf19  disulf ? ? E  CYS 35  SG  ? ? ? 1_555 E  CYS 128 SG ? ? E CYS 284  E CYS 377  1_555 ? ? ? ? ? ? ? 2.090 ? ? 
disulf20  disulf ? ? E  CYS 107 SG  ? ? ? 1_555 E  CYS 120 SG ? ? E CYS 356  E CYS 369  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf21  disulf ? ? F  CYS 4   SG  ? ? ? 1_555 F  CYS 135 SG ? ? F CYS 253  F CYS 384  1_555 ? ? ? ? ? ? ? 2.050 ? ? 
disulf22  disulf ? ? F  CYS 7   SG  ? ? ? 1_555 F  CYS 18  SG ? ? F CYS 256  F CYS 267  1_555 ? ? ? ? ? ? ? 2.057 ? ? 
disulf23  disulf ? ? F  CYS 35  SG  ? ? ? 1_555 F  CYS 128 SG ? ? F CYS 284  F CYS 377  1_555 ? ? ? ? ? ? ? 2.075 ? ? 
disulf24  disulf ? ? F  CYS 107 SG  ? ? ? 1_555 F  CYS 120 SG ? ? F CYS 356  F CYS 369  1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc1   metalc ? ? A  ASP 71  OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 320  A CA  1003 1_555 ? ? ? ? ? ? ? 2.526 ? ? 
metalc2   metalc ? ? A  ASP 71  OD2 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 320  A CA  1003 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc3   metalc ? ? A  GLU 75  OE1 ? ? ? 1_555 I  CA  .   CA ? ? A GLU 324  A CA  1003 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc4   metalc ? ? A  GLU 75  OE2 ? ? ? 1_555 I  CA  .   CA ? ? A GLU 324  A CA  1003 1_555 ? ? ? ? ? ? ? 2.551 ? ? 
metalc5   metalc ? ? A  GLU 98  OE1 ? ? ? 1_555 H  CA  .   CA ? ? A GLU 347  A CA  1002 1_555 ? ? ? ? ? ? ? 2.399 ? ? 
metalc6   metalc ? ? A  ASN 100 OD1 ? ? ? 1_555 H  CA  .   CA ? ? A ASN 349  A CA  1002 1_555 ? ? ? ? ? ? ? 2.481 ? ? 
metalc7   metalc ? ? A  ASN 101 OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASN 350  A CA  1003 1_555 ? ? ? ? ? ? ? 2.537 ? ? 
metalc8   metalc ? ? A  GLU 105 OE1 ? ? ? 1_555 H  CA  .   CA ? ? A GLU 354  A CA  1002 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc9   metalc ? ? A  GLU 105 O   ? ? ? 1_555 I  CA  .   CA ? ? A GLU 354  A CA  1003 1_555 ? ? ? ? ? ? ? 2.543 ? ? 
metalc10  metalc ? ? A  ASP 106 OD1 ? ? ? 1_555 I  CA  .   CA ? ? A ASP 355  A CA  1003 1_555 ? ? ? ? ? ? ? 2.196 ? ? 
metalc11  metalc ? ? A  ASP 106 OD2 ? ? ? 1_555 J  CA  .   CA ? ? A ASP 355  A CA  1004 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc12  metalc ? ? A  ASN 116 OD1 ? ? ? 1_555 H  CA  .   CA ? ? A ASN 365  A CA  1002 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc13  metalc ? ? A  ASP 117 O   ? ? ? 1_555 H  CA  .   CA ? ? A ASP 366  A CA  1002 1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc14  metalc ? ? A  ASP 117 OD1 ? ? ? 1_555 H  CA  .   CA ? ? A ASP 366  A CA  1002 1_555 ? ? ? ? ? ? ? 2.207 ? ? 
metalc15  metalc ? ? G  EZ8 .   O4  ? ? ? 1_555 H  CA  .   CA ? ? A EZ8 1001 A CA  1002 1_555 ? ? ? ? ? ? ? 2.650 ? ? 
metalc16  metalc ? ? G  EZ8 .   O3  ? ? ? 1_555 H  CA  .   CA ? ? A EZ8 1001 A CA  1002 1_555 ? ? ? ? ? ? ? 2.574 ? ? 
metalc17  metalc ? ? I  CA  .   CA  ? ? ? 1_555 SA HOH .   O  ? ? A CA  1003 A HOH 1129 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc18  metalc ? ? J  CA  .   CA  ? ? ? 1_555 SA HOH .   O  ? ? A CA  1004 A HOH 1102 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc19  metalc ? ? J  CA  .   CA  ? ? ? 1_555 SA HOH .   O  ? ? A CA  1004 A HOH 1118 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc20  metalc ? ? J  CA  .   CA  ? ? ? 1_555 SA HOH .   O  ? ? A CA  1004 A HOH 1139 1_555 ? ? ? ? ? ? ? 1.916 ? ? 
metalc21  metalc ? ? J  CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? A CA  1004 D HOH 607  2_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc22  metalc ? ? J  CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? A CA  1004 D HOH 695  2_555 ? ? ? ? ? ? ? 2.121 ? ? 
metalc23  metalc ? ? B  ASP 71  OD1 ? ? ? 1_555 P  CA  .   CA ? ? B ASP 320  B CA  1003 1_555 ? ? ? ? ? ? ? 2.504 ? ? 
metalc24  metalc ? ? B  ASP 71  OD2 ? ? ? 1_555 P  CA  .   CA ? ? B ASP 320  B CA  1003 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc25  metalc ? ? B  GLU 75  OE1 ? ? ? 1_555 P  CA  .   CA ? ? B GLU 324  B CA  1003 1_555 ? ? ? ? ? ? ? 2.555 ? ? 
metalc26  metalc ? ? B  GLU 75  OE2 ? ? ? 1_555 P  CA  .   CA ? ? B GLU 324  B CA  1003 1_555 ? ? ? ? ? ? ? 2.754 ? ? 
metalc27  metalc ? ? B  GLU 98  OE1 ? ? ? 1_555 O  CA  .   CA ? ? B GLU 347  B CA  1002 1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc28  metalc ? ? B  ASN 100 OD1 ? ? ? 1_555 O  CA  .   CA ? ? B ASN 349  B CA  1002 1_555 ? ? ? ? ? ? ? 2.385 ? ? 
metalc29  metalc ? ? B  ASN 101 OD1 ? ? ? 1_555 P  CA  .   CA ? ? B ASN 350  B CA  1003 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc30  metalc ? ? B  GLU 105 OE1 ? ? ? 1_555 O  CA  .   CA ? ? B GLU 354  B CA  1002 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
metalc31  metalc ? ? B  GLU 105 O   ? ? ? 1_555 P  CA  .   CA ? ? B GLU 354  B CA  1003 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc32  metalc ? ? B  ASP 106 OD1 ? ? ? 1_555 P  CA  .   CA ? ? B ASP 355  B CA  1003 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc33  metalc ? ? B  ASP 106 OD2 ? ? ? 1_555 Q  CA  .   CA ? ? B ASP 355  B CA  1004 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc34  metalc ? ? B  ASN 116 OD1 ? ? ? 1_555 O  CA  .   CA ? ? B ASN 365  B CA  1002 1_555 ? ? ? ? ? ? ? 2.512 ? ? 
metalc35  metalc ? ? B  ASP 117 O   ? ? ? 1_555 O  CA  .   CA ? ? B ASP 366  B CA  1002 1_555 ? ? ? ? ? ? ? 2.529 ? ? 
metalc36  metalc ? ? B  ASP 117 OD1 ? ? ? 1_555 O  CA  .   CA ? ? B ASP 366  B CA  1002 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc37  metalc ? ? N  EZ8 .   O4  ? ? ? 1_555 O  CA  .   CA ? ? B EZ8 1001 B CA  1002 1_555 ? ? ? ? ? ? ? 2.512 ? ? 
metalc38  metalc ? ? N  EZ8 .   O3  ? ? ? 1_555 O  CA  .   CA ? ? B EZ8 1001 B CA  1002 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc39  metalc ? ? P  CA  .   CA  ? ? ? 1_555 TA HOH .   O  ? ? B CA  1003 B HOH 1133 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc40  metalc ? ? Q  CA  .   CA  ? ? ? 1_555 TA HOH .   O  ? ? B CA  1004 B HOH 1108 1_555 ? ? ? ? ? ? ? 2.241 ? ? 
metalc41  metalc ? ? Q  CA  .   CA  ? ? ? 1_555 TA HOH .   O  ? ? B CA  1004 B HOH 1126 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc42  metalc ? ? Q  CA  .   CA  ? ? ? 1_555 TA HOH .   O  ? ? B CA  1004 B HOH 1148 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc43  metalc ? ? Q  CA  .   CA  ? ? ? 1_555 TA HOH .   O  ? ? B CA  1004 B HOH 1155 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc44  metalc ? ? Q  CA  .   CA  ? ? ? 1_555 TA HOH .   O  ? ? B CA  1004 B HOH 1212 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc45  metalc ? ? C  ASP 71  OD1 ? ? ? 1_555 V  CA  .   CA ? ? C ASP 320  C CA  1003 1_555 ? ? ? ? ? ? ? 2.535 ? ? 
metalc46  metalc ? ? C  ASP 71  OD2 ? ? ? 1_555 V  CA  .   CA ? ? C ASP 320  C CA  1003 1_555 ? ? ? ? ? ? ? 2.542 ? ? 
metalc47  metalc ? ? C  GLU 75  OE1 ? ? ? 1_555 V  CA  .   CA ? ? C GLU 324  C CA  1003 1_555 ? ? ? ? ? ? ? 2.519 ? ? 
metalc48  metalc ? ? C  GLU 75  OE2 ? ? ? 1_555 V  CA  .   CA ? ? C GLU 324  C CA  1003 1_555 ? ? ? ? ? ? ? 2.846 ? ? 
metalc49  metalc ? ? C  GLU 98  OE1 ? ? ? 1_555 U  CA  .   CA ? ? C GLU 347  C CA  1002 1_555 ? ? ? ? ? ? ? 2.540 ? ? 
metalc50  metalc ? ? C  ASN 100 OD1 ? ? ? 1_555 U  CA  .   CA ? ? C ASN 349  C CA  1002 1_555 ? ? ? ? ? ? ? 2.652 ? ? 
metalc51  metalc ? ? C  ASN 101 OD1 ? ? ? 1_555 V  CA  .   CA ? ? C ASN 350  C CA  1003 1_555 ? ? ? ? ? ? ? 2.488 ? ? 
metalc52  metalc ? ? C  GLU 105 OE1 ? ? ? 1_555 U  CA  .   CA ? ? C GLU 354  C CA  1002 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc53  metalc ? ? C  GLU 105 O   ? ? ? 1_555 V  CA  .   CA ? ? C GLU 354  C CA  1003 1_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc54  metalc ? ? C  ASP 106 OD1 ? ? ? 1_555 V  CA  .   CA ? ? C ASP 355  C CA  1003 1_555 ? ? ? ? ? ? ? 2.402 ? ? 
metalc55  metalc ? ? C  ASP 106 OD2 ? ? ? 1_555 W  CA  .   CA ? ? C ASP 355  C CA  1004 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc56  metalc ? ? C  ASN 116 OD1 ? ? ? 1_555 U  CA  .   CA ? ? C ASN 365  C CA  1002 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc57  metalc ? ? C  ASP 117 O   ? ? ? 1_555 U  CA  .   CA ? ? C ASP 366  C CA  1002 1_555 ? ? ? ? ? ? ? 2.365 ? ? 
metalc58  metalc ? ? C  ASP 117 OD1 ? ? ? 1_555 U  CA  .   CA ? ? C ASP 366  C CA  1002 1_555 ? ? ? ? ? ? ? 2.448 ? ? 
metalc59  metalc ? ? T  EZ8 .   O4  ? ? ? 1_555 U  CA  .   CA ? ? C EZ8 1001 C CA  1002 1_555 ? ? ? ? ? ? ? 2.531 ? ? 
metalc60  metalc ? ? T  EZ8 .   O3  ? ? ? 1_555 U  CA  .   CA ? ? C EZ8 1001 C CA  1002 1_555 ? ? ? ? ? ? ? 2.482 ? ? 
metalc61  metalc ? ? V  CA  .   CA  ? ? ? 1_555 UA HOH .   O  ? ? C CA  1003 C HOH 1121 1_555 ? ? ? ? ? ? ? 2.181 ? ? 
metalc62  metalc ? ? W  CA  .   CA  ? ? ? 1_555 UA HOH .   O  ? ? C CA  1004 C HOH 1112 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc63  metalc ? ? W  CA  .   CA  ? ? ? 1_555 UA HOH .   O  ? ? C CA  1004 C HOH 1126 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc64  metalc ? ? W  CA  .   CA  ? ? ? 1_555 UA HOH .   O  ? ? C CA  1004 C HOH 1128 1_555 ? ? ? ? ? ? ? 2.281 ? ? 
metalc65  metalc ? ? W  CA  .   CA  ? ? ? 1_555 UA HOH .   O  ? ? C CA  1004 C HOH 1130 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc66  metalc ? ? W  CA  .   CA  ? ? ? 1_555 UA HOH .   O  ? ? C CA  1004 C HOH 1221 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc67  metalc ? ? D  ASP 71  OD1 ? ? ? 1_555 CA CA  .   CA ? ? D ASP 320  D CA  504  1_555 ? ? ? ? ? ? ? 2.615 ? ? 
metalc68  metalc ? ? D  ASP 71  OD2 ? ? ? 1_555 CA CA  .   CA ? ? D ASP 320  D CA  504  1_555 ? ? ? ? ? ? ? 2.384 ? ? 
metalc69  metalc ? ? D  GLU 75  OE1 ? ? ? 1_555 CA CA  .   CA ? ? D GLU 324  D CA  504  1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc70  metalc ? ? D  GLU 75  OE2 ? ? ? 1_555 CA CA  .   CA ? ? D GLU 324  D CA  504  1_555 ? ? ? ? ? ? ? 2.469 ? ? 
metalc71  metalc ? ? D  GLU 98  OE1 ? ? ? 1_555 BA CA  .   CA ? ? D GLU 347  D CA  503  1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc72  metalc ? ? D  ASN 100 OD1 ? ? ? 1_555 BA CA  .   CA ? ? D ASN 349  D CA  503  1_555 ? ? ? ? ? ? ? 2.492 ? ? 
metalc73  metalc ? ? D  ASN 101 OD1 ? ? ? 1_555 CA CA  .   CA ? ? D ASN 350  D CA  504  1_555 ? ? ? ? ? ? ? 2.417 ? ? 
metalc74  metalc ? ? D  GLU 105 OE1 ? ? ? 1_555 BA CA  .   CA ? ? D GLU 354  D CA  503  1_555 ? ? ? ? ? ? ? 2.212 ? ? 
metalc75  metalc ? ? D  GLU 105 O   ? ? ? 1_555 CA CA  .   CA ? ? D GLU 354  D CA  504  1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc76  metalc ? ? D  ASP 106 OD1 ? ? ? 1_555 CA CA  .   CA ? ? D ASP 355  D CA  504  1_555 ? ? ? ? ? ? ? 2.188 ? ? 
metalc77  metalc ? ? D  ASP 106 OD2 ? ? ? 1_555 DA CA  .   CA ? ? D ASP 355  D CA  505  1_555 ? ? ? ? ? ? ? 2.382 ? ? 
metalc78  metalc ? ? D  ASN 116 OD1 ? ? ? 1_555 BA CA  .   CA ? ? D ASN 365  D CA  503  1_555 ? ? ? ? ? ? ? 2.651 ? ? 
metalc79  metalc ? ? D  ASP 117 O   ? ? ? 1_555 BA CA  .   CA ? ? D ASP 366  D CA  503  1_555 ? ? ? ? ? ? ? 2.485 ? ? 
metalc80  metalc ? ? D  ASP 117 OD1 ? ? ? 1_555 BA CA  .   CA ? ? D ASP 366  D CA  503  1_555 ? ? ? ? ? ? ? 2.412 ? ? 
metalc81  metalc ? ? AA EZ8 .   O4  ? ? ? 1_555 BA CA  .   CA ? ? D EZ8 502  D CA  503  1_555 ? ? ? ? ? ? ? 2.508 ? ? 
metalc82  metalc ? ? AA EZ8 .   O3  ? ? ? 1_555 BA CA  .   CA ? ? D EZ8 502  D CA  503  1_555 ? ? ? ? ? ? ? 2.490 ? ? 
metalc83  metalc ? ? CA CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? D CA  504  D HOH 623  1_555 ? ? ? ? ? ? ? 2.159 ? ? 
metalc84  metalc ? ? DA CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? D CA  505  D HOH 610  1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc85  metalc ? ? DA CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? D CA  505  D HOH 617  1_555 ? ? ? ? ? ? ? 2.158 ? ? 
metalc86  metalc ? ? DA CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? D CA  505  D HOH 622  1_555 ? ? ? ? ? ? ? 2.111 ? ? 
metalc87  metalc ? ? DA CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? D CA  505  D HOH 649  1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc88  metalc ? ? DA CA  .   CA  ? ? ? 1_555 VA HOH .   O  ? ? D CA  505  D HOH 697  1_555 ? ? ? ? ? ? ? 2.262 ? ? 
metalc89  metalc ? ? E  ASP 71  OD1 ? ? ? 1_555 JA CA  .   CA ? ? E ASP 320  E CA  505  1_555 ? ? ? ? ? ? ? 2.544 ? ? 
metalc90  metalc ? ? E  ASP 71  OD2 ? ? ? 1_555 JA CA  .   CA ? ? E ASP 320  E CA  505  1_555 ? ? ? ? ? ? ? 2.642 ? ? 
metalc91  metalc ? ? E  GLU 75  OE1 ? ? ? 1_555 JA CA  .   CA ? ? E GLU 324  E CA  505  1_555 ? ? ? ? ? ? ? 2.475 ? ? 
metalc92  metalc ? ? E  GLU 75  OE2 ? ? ? 1_555 JA CA  .   CA ? ? E GLU 324  E CA  505  1_555 ? ? ? ? ? ? ? 2.611 ? ? 
metalc93  metalc ? ? E  GLU 98  OE1 ? ? ? 1_555 IA CA  .   CA ? ? E GLU 347  E CA  504  1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc94  metalc ? ? E  ASN 100 OD1 ? ? ? 1_555 IA CA  .   CA ? ? E ASN 349  E CA  504  1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc95  metalc ? ? E  ASN 101 OD1 ? ? ? 1_555 JA CA  .   CA ? ? E ASN 350  E CA  505  1_555 ? ? ? ? ? ? ? 2.521 ? ? 
metalc96  metalc ? ? E  GLU 105 OE1 ? ? ? 1_555 IA CA  .   CA ? ? E GLU 354  E CA  504  1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc97  metalc ? ? E  GLU 105 O   ? ? ? 1_555 JA CA  .   CA ? ? E GLU 354  E CA  505  1_555 ? ? ? ? ? ? ? 2.452 ? ? 
metalc98  metalc ? ? E  ASP 106 OD1 ? ? ? 1_555 JA CA  .   CA ? ? E ASP 355  E CA  505  1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc99  metalc ? ? E  ASP 106 OD1 ? ? ? 1_555 KA CA  .   CA ? ? E ASP 355  E CA  506  1_555 ? ? ? ? ? ? ? 2.985 ? ? 
metalc100 metalc ? ? E  ASP 106 OD2 ? ? ? 1_555 KA CA  .   CA ? ? E ASP 355  E CA  506  1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc101 metalc ? ? E  ASN 116 OD1 ? ? ? 1_555 IA CA  .   CA ? ? E ASN 365  E CA  504  1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc102 metalc ? ? E  ASP 117 O   ? ? ? 1_555 IA CA  .   CA ? ? E ASP 366  E CA  504  1_555 ? ? ? ? ? ? ? 2.469 ? ? 
metalc103 metalc ? ? E  ASP 117 OD1 ? ? ? 1_555 IA CA  .   CA ? ? E ASP 366  E CA  504  1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc104 metalc ? ? HA EZ8 .   O4  ? ? ? 1_555 IA CA  .   CA ? ? E EZ8 503  E CA  504  1_555 ? ? ? ? ? ? ? 2.592 ? ? 
metalc105 metalc ? ? HA EZ8 .   O3  ? ? ? 1_555 IA CA  .   CA ? ? E EZ8 503  E CA  504  1_555 ? ? ? ? ? ? ? 2.559 ? ? 
metalc106 metalc ? ? JA CA  .   CA  ? ? ? 1_555 WA HOH .   O  ? ? E CA  505  E HOH 638  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc107 metalc ? ? KA CA  .   CA  ? ? ? 1_555 WA HOH .   O  ? ? E CA  506  E HOH 608  1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc108 metalc ? ? KA CA  .   CA  ? ? ? 1_555 WA HOH .   O  ? ? E CA  506  E HOH 613  1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc109 metalc ? ? KA CA  .   CA  ? ? ? 1_555 WA HOH .   O  ? ? E CA  506  E HOH 622  1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc110 metalc ? ? KA CA  .   CA  ? ? ? 1_555 WA HOH .   O  ? ? E CA  506  E HOH 629  1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc111 metalc ? ? KA CA  .   CA  ? ? ? 1_555 WA HOH .   O  ? ? E CA  506  E HOH 707  1_555 ? ? ? ? ? ? ? 2.164 ? ? 
metalc112 metalc ? ? WA HOH .   O   ? ? ? 2_657 QA CA  .   CA ? ? E HOH 614  F CA  505  1_555 ? ? ? ? ? ? ? 2.127 ? ? 
metalc113 metalc ? ? WA HOH .   O   ? ? ? 2_657 QA CA  .   CA ? ? E HOH 616  F CA  505  1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc114 metalc ? ? F  ASP 71  OD1 ? ? ? 1_555 PA CA  .   CA ? ? F ASP 320  F CA  504  1_555 ? ? ? ? ? ? ? 2.424 ? ? 
metalc115 metalc ? ? F  ASP 71  OD2 ? ? ? 1_555 PA CA  .   CA ? ? F ASP 320  F CA  504  1_555 ? ? ? ? ? ? ? 2.638 ? ? 
metalc116 metalc ? ? F  GLU 75  OE1 ? ? ? 1_555 PA CA  .   CA ? ? F GLU 324  F CA  504  1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc117 metalc ? ? F  GLU 75  OE2 ? ? ? 1_555 PA CA  .   CA ? ? F GLU 324  F CA  504  1_555 ? ? ? ? ? ? ? 2.649 ? ? 
metalc118 metalc ? ? F  GLU 98  OE1 ? ? ? 1_555 OA CA  .   CA ? ? F GLU 347  F CA  503  1_555 ? ? ? ? ? ? ? 2.317 ? ? 
metalc119 metalc ? ? F  ASN 100 OD1 ? ? ? 1_555 OA CA  .   CA ? ? F ASN 349  F CA  503  1_555 ? ? ? ? ? ? ? 2.428 ? ? 
metalc120 metalc ? ? F  ASN 101 OD1 ? ? ? 1_555 PA CA  .   CA ? ? F ASN 350  F CA  504  1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc121 metalc ? ? F  GLU 105 OE1 ? ? ? 1_555 OA CA  .   CA ? ? F GLU 354  F CA  503  1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc122 metalc ? ? F  GLU 105 O   ? ? ? 1_555 PA CA  .   CA ? ? F GLU 354  F CA  504  1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc123 metalc ? ? F  ASP 106 OD1 ? ? ? 1_555 PA CA  .   CA ? ? F ASP 355  F CA  504  1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc124 metalc ? ? F  ASP 106 OD2 ? ? ? 1_555 QA CA  .   CA ? ? F ASP 355  F CA  505  1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc125 metalc ? ? F  ASN 116 OD1 ? ? ? 1_555 OA CA  .   CA ? ? F ASN 365  F CA  503  1_555 ? ? ? ? ? ? ? 2.362 ? ? 
metalc126 metalc ? ? F  ASP 117 O   ? ? ? 1_555 OA CA  .   CA ? ? F ASP 366  F CA  503  1_555 ? ? ? ? ? ? ? 2.446 ? ? 
metalc127 metalc ? ? F  ASP 117 OD1 ? ? ? 1_555 OA CA  .   CA ? ? F ASP 366  F CA  503  1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc128 metalc ? ? NA EZ8 .   O4  ? ? ? 1_555 OA CA  .   CA ? ? F EZ8 502  F CA  503  1_555 ? ? ? ? ? ? ? 2.507 ? ? 
metalc129 metalc ? ? NA EZ8 .   O3  ? ? ? 1_555 OA CA  .   CA ? ? F EZ8 502  F CA  503  1_555 ? ? ? ? ? ? ? 2.450 ? ? 
metalc130 metalc ? ? PA CA  .   CA  ? ? ? 1_555 XA HOH .   O  ? ? F CA  504  F HOH 618  1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc131 metalc ? ? QA CA  .   CA  ? ? ? 1_555 XA HOH .   O  ? ? F CA  505  F HOH 604  1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc132 metalc ? ? QA CA  .   CA  ? ? ? 1_555 XA HOH .   O  ? ? F CA  505  F HOH 605  1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc133 metalc ? ? QA CA  .   CA  ? ? ? 1_555 XA HOH .   O  ? ? F CA  505  F HOH 693  1_555 ? ? ? ? ? ? ? 2.294 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 51.3  ? 
2   OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 90.9  ? 
3   OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 82.8  ? 
4   OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 116.4 ? 
5   OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 71.6  ? 
6   OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 53.0  ? 
7   OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 158.3 ? 
8   OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 147.8 ? 
9   OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 84.3  ? 
10  OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 77.1  ? 
11  OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? A  GLU 105 ? A GLU 354  ? 1_555 95.6  ? 
12  OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? A  GLU 105 ? A GLU 354  ? 1_555 122.9 ? 
13  OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? A  GLU 105 ? A GLU 354  ? 1_555 150.9 ? 
14  OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? A  GLU 105 ? A GLU 354  ? 1_555 142.6 ? 
15  OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? A  GLU 105 ? A GLU 354  ? 1_555 79.2  ? 
16  OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 72.6  ? 
17  OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 119.0 ? 
18  OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 75.4  ? 
19  OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 126.5 ? 
20  OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 85.8  ? 
21  O   ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 79.6  ? 
22  OD1 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 111.2 ? 
23  OD2 ? A  ASP 71  ? A ASP 320  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 79.1  ? 
24  OE1 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 131.1 ? 
25  OE2 ? A  GLU 75  ? A GLU 324  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 78.2  ? 
26  OD1 ? A  ASN 101 ? A ASN 350  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 87.4  ? 
27  O   ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 72.2  ? 
28  OD1 ? A  ASP 106 ? A ASP 355  ? 1_555 CA ? I  CA . ? A CA 1003 ? 1_555 O   ? SA HOH .   ? A HOH 1129 ? 1_555 151.8 ? 
29  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 71.4  ? 
30  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 139.3 ? 
31  OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 68.6  ? 
32  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 70.6  ? 
33  OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 141.1 ? 
34  OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 150.1 ? 
35  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O   ? A  ASP 117 ? A ASP 366  ? 1_555 138.2 ? 
36  OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O   ? A  ASP 117 ? A ASP 366  ? 1_555 136.7 ? 
37  OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O   ? A  ASP 117 ? A ASP 366  ? 1_555 73.5  ? 
38  OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O   ? A  ASP 117 ? A ASP 366  ? 1_555 79.8  ? 
39  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 76.4  ? 
40  OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 84.8  ? 
41  OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 92.8  ? 
42  OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 94.1  ? 
43  O   ? A  ASP 117 ? A ASP 366  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 77.0  ? 
44  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 72.9  ? 
45  OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 75.8  ? 
46  OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 103.6 ? 
47  OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 85.5  ? 
48  O   ? A  ASP 117 ? A ASP 366  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 134.3 ? 
49  OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 147.6 ? 
50  OE1 ? A  GLU 98  ? A GLU 347  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 129.5 ? 
51  OD1 ? A  ASN 100 ? A ASN 349  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 118.7 ? 
52  OE1 ? A  GLU 105 ? A GLU 354  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 78.0  ? 
53  OD1 ? A  ASN 116 ? A ASN 365  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 80.8  ? 
54  O   ? A  ASP 117 ? A ASP 366  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 71.0  ? 
55  OD1 ? A  ASP 117 ? A ASP 366  ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 148.0 ? 
56  O4  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 CA ? H  CA . ? A CA 1002 ? 1_555 O3  ? G  EZ8 .   ? A EZ8 1001 ? 1_555 63.9  ? 
57  OD2 ? A  ASP 106 ? A ASP 355  ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? SA HOH .   ? A HOH 1102 ? 1_555 84.1  ? 
58  OD2 ? A  ASP 106 ? A ASP 355  ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? SA HOH .   ? A HOH 1118 ? 1_555 76.9  ? 
59  O   ? SA HOH .   ? A HOH 1102 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? SA HOH .   ? A HOH 1118 ? 1_555 85.0  ? 
60  OD2 ? A  ASP 106 ? A ASP 355  ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? SA HOH .   ? A HOH 1139 ? 1_555 89.1  ? 
61  O   ? SA HOH .   ? A HOH 1102 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? SA HOH .   ? A HOH 1139 ? 1_555 166.2 ? 
62  O   ? SA HOH .   ? A HOH 1118 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? SA HOH .   ? A HOH 1139 ? 1_555 81.7  ? 
63  OD2 ? A  ASP 106 ? A ASP 355  ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 607  ? 2_555 95.1  ? 
64  O   ? SA HOH .   ? A HOH 1102 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 607  ? 2_555 96.7  ? 
65  O   ? SA HOH .   ? A HOH 1118 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 607  ? 2_555 171.6 ? 
66  O   ? SA HOH .   ? A HOH 1139 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 607  ? 2_555 95.9  ? 
67  OD2 ? A  ASP 106 ? A ASP 355  ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 695  ? 2_555 167.8 ? 
68  O   ? SA HOH .   ? A HOH 1102 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 695  ? 2_555 88.1  ? 
69  O   ? SA HOH .   ? A HOH 1118 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 695  ? 2_555 93.2  ? 
70  O   ? SA HOH .   ? A HOH 1139 ? 1_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 695  ? 2_555 96.4  ? 
71  O   ? VA HOH .   ? D HOH 607  ? 2_555 CA ? J  CA . ? A CA 1004 ? 1_555 O   ? VA HOH .   ? D HOH 695  ? 2_555 95.1  ? 
72  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 53.7  ? 
73  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 99.5  ? 
74  OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 79.7  ? 
75  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 121.2 ? 
76  OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 70.7  ? 
77  OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 49.0  ? 
78  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 159.5 ? 
79  OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 142.2 ? 
80  OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 76.6  ? 
81  OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 71.5  ? 
82  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? B  GLU 105 ? B GLU 354  ? 1_555 93.8  ? 
83  OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? B  GLU 105 ? B GLU 354  ? 1_555 134.5 ? 
84  OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? B  GLU 105 ? B GLU 354  ? 1_555 142.6 ? 
85  OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? B  GLU 105 ? B GLU 354  ? 1_555 143.0 ? 
86  OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? B  GLU 105 ? B GLU 354  ? 1_555 78.8  ? 
87  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 75.9  ? 
88  OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 116.7 ? 
89  OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 73.0  ? 
90  OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 120.3 ? 
91  OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 83.8  ? 
92  O   ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 76.7  ? 
93  OD1 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 106.1 ? 
94  OD2 ? B  ASP 71  ? B ASP 320  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 80.6  ? 
95  OE1 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 128.4 ? 
96  OE2 ? B  GLU 75  ? B GLU 324  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 79.5  ? 
97  OD1 ? B  ASN 101 ? B ASN 350  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 91.5  ? 
98  O   ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 79.7  ? 
99  OD1 ? B  ASP 106 ? B ASP 355  ? 1_555 CA ? P  CA . ? B CA 1003 ? 1_555 O   ? TA HOH .   ? B HOH 1133 ? 1_555 156.3 ? 
100 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 68.1  ? 
101 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 141.7 ? 
102 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 75.6  ? 
103 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 72.5  ? 
104 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 140.1 ? 
105 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 144.2 ? 
106 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O   ? B  ASP 117 ? B ASP 366  ? 1_555 130.5 ? 
107 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O   ? B  ASP 117 ? B ASP 366  ? 1_555 140.5 ? 
108 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O   ? B  ASP 117 ? B ASP 366  ? 1_555 73.8  ? 
109 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O   ? B  ASP 117 ? B ASP 366  ? 1_555 72.9  ? 
110 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 71.3  ? 
111 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 82.9  ? 
112 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 93.1  ? 
113 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 90.3  ? 
114 O   ? B  ASP 117 ? B ASP 366  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 74.6  ? 
115 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 74.1  ? 
116 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 76.6  ? 
117 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 109.3 ? 
118 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 87.3  ? 
119 O   ? B  ASP 117 ? B ASP 366  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 137.4 ? 
120 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 144.3 ? 
121 OE1 ? B  GLU 98  ? B GLU 347  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 133.2 ? 
122 OD1 ? B  ASN 100 ? B ASN 349  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 123.9 ? 
123 OE1 ? B  GLU 105 ? B GLU 354  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 77.8  ? 
124 OD1 ? B  ASN 116 ? B ASN 365  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 80.2  ? 
125 O   ? B  ASP 117 ? B ASP 366  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 72.4  ? 
126 OD1 ? B  ASP 117 ? B ASP 366  ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 147.1 ? 
127 O4  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 CA ? O  CA . ? B CA 1002 ? 1_555 O3  ? N  EZ8 .   ? B EZ8 1001 ? 1_555 67.2  ? 
128 OD2 ? B  ASP 106 ? B ASP 355  ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1108 ? 1_555 92.4  ? 
129 OD2 ? B  ASP 106 ? B ASP 355  ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1126 ? 1_555 86.9  ? 
130 O   ? TA HOH .   ? B HOH 1108 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1126 ? 1_555 83.0  ? 
131 OD2 ? B  ASP 106 ? B ASP 355  ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1148 ? 1_555 90.6  ? 
132 O   ? TA HOH .   ? B HOH 1108 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1148 ? 1_555 93.7  ? 
133 O   ? TA HOH .   ? B HOH 1126 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1148 ? 1_555 175.8 ? 
134 OD2 ? B  ASP 106 ? B ASP 355  ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1155 ? 1_555 85.0  ? 
135 O   ? TA HOH .   ? B HOH 1108 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1155 ? 1_555 174.6 ? 
136 O   ? TA HOH .   ? B HOH 1126 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1155 ? 1_555 92.1  ? 
137 O   ? TA HOH .   ? B HOH 1148 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1155 ? 1_555 91.1  ? 
138 OD2 ? B  ASP 106 ? B ASP 355  ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1212 ? 1_555 165.6 ? 
139 O   ? TA HOH .   ? B HOH 1108 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1212 ? 1_555 99.4  ? 
140 O   ? TA HOH .   ? B HOH 1126 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1212 ? 1_555 86.4  ? 
141 O   ? TA HOH .   ? B HOH 1148 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1212 ? 1_555 96.7  ? 
142 O   ? TA HOH .   ? B HOH 1155 ? 1_555 CA ? Q  CA . ? B CA 1004 ? 1_555 O   ? TA HOH .   ? B HOH 1212 ? 1_555 82.5  ? 
143 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 51.7  ? 
144 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 93.0  ? 
145 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 80.5  ? 
146 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 116.4 ? 
147 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 71.1  ? 
148 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 48.2  ? 
149 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 156.9 ? 
150 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 149.8 ? 
151 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 86.1  ? 
152 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 79.8  ? 
153 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? C  GLU 105 ? C GLU 354  ? 1_555 91.0  ? 
154 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? C  GLU 105 ? C GLU 354  ? 1_555 123.2 ? 
155 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? C  GLU 105 ? C GLU 354  ? 1_555 151.3 ? 
156 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? C  GLU 105 ? C GLU 354  ? 1_555 148.7 ? 
157 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? C  GLU 105 ? C GLU 354  ? 1_555 79.2  ? 
158 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 72.3  ? 
159 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 118.9 ? 
160 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 80.1  ? 
161 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 126.5 ? 
162 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 84.8  ? 
163 O   ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 74.2  ? 
164 OD1 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 108.5 ? 
165 OD2 ? C  ASP 71  ? C ASP 320  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 81.7  ? 
166 OE1 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 133.4 ? 
167 OE2 ? C  GLU 75  ? C GLU 324  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 85.3  ? 
168 OD1 ? C  ASN 101 ? C ASN 350  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 88.3  ? 
169 O   ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 71.1  ? 
170 OD1 ? C  ASP 106 ? C ASP 355  ? 1_555 CA ? V  CA . ? C CA 1003 ? 1_555 O   ? UA HOH .   ? C HOH 1121 ? 1_555 145.3 ? 
171 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 72.6  ? 
172 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 140.4 ? 
173 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 68.8  ? 
174 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 68.3  ? 
175 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 140.6 ? 
176 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 150.6 ? 
177 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O   ? C  ASP 117 ? C ASP 366  ? 1_555 136.5 ? 
178 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O   ? C  ASP 117 ? C ASP 366  ? 1_555 129.4 ? 
179 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O   ? C  ASP 117 ? C ASP 366  ? 1_555 68.7  ? 
180 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O   ? C  ASP 117 ? C ASP 366  ? 1_555 84.5  ? 
181 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 73.8  ? 
182 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 81.6  ? 
183 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 92.0  ? 
184 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 92.0  ? 
185 O   ? C  ASP 117 ? C ASP 366  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 73.8  ? 
186 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 71.4  ? 
187 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 78.6  ? 
188 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 108.4 ? 
189 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 84.6  ? 
190 O   ? C  ASP 117 ? C ASP 366  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 141.1 ? 
191 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 143.7 ? 
192 OE1 ? C  GLU 98  ? C GLU 347  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 131.9 ? 
193 OD1 ? C  ASN 100 ? C ASN 349  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 120.8 ? 
194 OE1 ? C  GLU 105 ? C GLU 354  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 77.6  ? 
195 OD1 ? C  ASN 116 ? C ASN 365  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 83.8  ? 
196 O   ? C  ASP 117 ? C ASP 366  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 74.1  ? 
197 OD1 ? C  ASP 117 ? C ASP 366  ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 148.0 ? 
198 O4  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 CA ? U  CA . ? C CA 1002 ? 1_555 O3  ? T  EZ8 .   ? C EZ8 1001 ? 1_555 67.6  ? 
199 OD2 ? C  ASP 106 ? C ASP 355  ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1112 ? 1_555 104.4 ? 
200 OD2 ? C  ASP 106 ? C ASP 355  ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1126 ? 1_555 87.9  ? 
201 O   ? UA HOH .   ? C HOH 1112 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1126 ? 1_555 90.1  ? 
202 OD2 ? C  ASP 106 ? C ASP 355  ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1128 ? 1_555 91.1  ? 
203 O   ? UA HOH .   ? C HOH 1112 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1128 ? 1_555 95.3  ? 
204 O   ? UA HOH .   ? C HOH 1126 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1128 ? 1_555 174.6 ? 
205 OD2 ? C  ASP 106 ? C ASP 355  ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1130 ? 1_555 83.1  ? 
206 O   ? UA HOH .   ? C HOH 1112 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1130 ? 1_555 169.8 ? 
207 O   ? UA HOH .   ? C HOH 1126 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1130 ? 1_555 97.1  ? 
208 O   ? UA HOH .   ? C HOH 1128 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1130 ? 1_555 77.5  ? 
209 OD2 ? C  ASP 106 ? C ASP 355  ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1221 ? 1_555 164.0 ? 
210 O   ? UA HOH .   ? C HOH 1112 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1221 ? 1_555 90.9  ? 
211 O   ? UA HOH .   ? C HOH 1126 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1221 ? 1_555 96.9  ? 
212 O   ? UA HOH .   ? C HOH 1128 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1221 ? 1_555 82.8  ? 
213 O   ? UA HOH .   ? C HOH 1130 ? 1_555 CA ? W  CA . ? C CA 1004 ? 1_555 O   ? UA HOH .   ? C HOH 1221 ? 1_555 81.1  ? 
214 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 51.6  ? 
215 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 94.9  ? 
216 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 78.7  ? 
217 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 119.4 ? 
218 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 70.7  ? 
219 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 52.9  ? 
220 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 156.3 ? 
221 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 149.0 ? 
222 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 83.5  ? 
223 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 78.3  ? 
224 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? D  GLU 105 ? D GLU 354  ? 1_555 91.5  ? 
225 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? D  GLU 105 ? D GLU 354  ? 1_555 129.1 ? 
226 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? D  GLU 105 ? D GLU 354  ? 1_555 146.3 ? 
227 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? D  GLU 105 ? D GLU 354  ? 1_555 145.3 ? 
228 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? D  GLU 105 ? D GLU 354  ? 1_555 77.8  ? 
229 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 71.8  ? 
230 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 112.9 ? 
231 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 72.8  ? 
232 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 124.4 ? 
233 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 85.3  ? 
234 O   ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 78.0  ? 
235 OD1 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 106.2 ? 
236 OD2 ? D  ASP 71  ? D ASP 320  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 84.8  ? 
237 OE1 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 135.9 ? 
238 OE2 ? D  GLU 75  ? D GLU 324  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 83.1  ? 
239 OD1 ? D  ASN 101 ? D ASN 350  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 90.7  ? 
240 O   ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 72.5  ? 
241 OD1 ? D  ASP 106 ? D ASP 355  ? 1_555 CA ? CA CA . ? D CA 504  ? 1_555 O   ? VA HOH .   ? D HOH 623  ? 1_555 150.4 ? 
242 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 74.3  ? 
243 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 150.7 ? 
244 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 76.4  ? 
245 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 65.8  ? 
246 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 140.1 ? 
247 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 143.5 ? 
248 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O   ? D  ASP 117 ? D ASP 366  ? 1_555 131.6 ? 
249 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O   ? D  ASP 117 ? D ASP 366  ? 1_555 140.2 ? 
250 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O   ? D  ASP 117 ? D ASP 366  ? 1_555 73.0  ? 
251 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O   ? D  ASP 117 ? D ASP 366  ? 1_555 74.1  ? 
252 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 74.7  ? 
253 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 84.2  ? 
254 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 100.8 ? 
255 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 86.8  ? 
256 O   ? D  ASP 117 ? D ASP 366  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 77.2  ? 
257 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 66.0  ? 
258 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 78.5  ? 
259 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 109.6 ? 
260 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 84.0  ? 
261 O   ? D  ASP 117 ? D ASP 366  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 136.0 ? 
262 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 140.0 ? 
263 OE1 ? D  GLU 98  ? D GLU 347  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 123.6 ? 
264 OD1 ? D  ASN 100 ? D ASN 349  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 126.6 ? 
265 OE1 ? D  GLU 105 ? D GLU 354  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 76.4  ? 
266 OD1 ? D  ASN 116 ? D ASN 365  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 77.6  ? 
267 O   ? D  ASP 117 ? D ASP 366  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 69.4  ? 
268 OD1 ? D  ASP 117 ? D ASP 366  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 145.8 ? 
269 O4  ? AA EZ8 .   ? D EZ8 502  ? 1_555 CA ? BA CA . ? D CA 503  ? 1_555 O3  ? AA EZ8 .   ? D EZ8 502  ? 1_555 68.9  ? 
270 OD2 ? D  ASP 106 ? D ASP 355  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 610  ? 1_555 84.7  ? 
271 OD2 ? D  ASP 106 ? D ASP 355  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 617  ? 1_555 88.7  ? 
272 O   ? VA HOH .   ? D HOH 610  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 617  ? 1_555 94.1  ? 
273 OD2 ? D  ASP 106 ? D ASP 355  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 622  ? 1_555 73.5  ? 
274 O   ? VA HOH .   ? D HOH 610  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 622  ? 1_555 83.6  ? 
275 O   ? VA HOH .   ? D HOH 617  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 622  ? 1_555 162.2 ? 
276 OD2 ? D  ASP 106 ? D ASP 355  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 649  ? 1_555 83.7  ? 
277 O   ? VA HOH .   ? D HOH 610  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 649  ? 1_555 168.3 ? 
278 O   ? VA HOH .   ? D HOH 617  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 649  ? 1_555 86.6  ? 
279 O   ? VA HOH .   ? D HOH 622  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 649  ? 1_555 92.2  ? 
280 OD2 ? D  ASP 106 ? D ASP 355  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 697  ? 1_555 161.8 ? 
281 O   ? VA HOH .   ? D HOH 610  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 697  ? 1_555 92.0  ? 
282 O   ? VA HOH .   ? D HOH 617  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 697  ? 1_555 109.3 ? 
283 O   ? VA HOH .   ? D HOH 622  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 697  ? 1_555 88.4  ? 
284 O   ? VA HOH .   ? D HOH 649  ? 1_555 CA ? DA CA . ? D CA 505  ? 1_555 O   ? VA HOH .   ? D HOH 697  ? 1_555 98.8  ? 
285 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 50.4  ? 
286 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 92.9  ? 
287 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 82.9  ? 
288 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 111.5 ? 
289 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 66.5  ? 
290 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 52.2  ? 
291 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 164.0 ? 
292 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 143.2 ? 
293 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 82.8  ? 
294 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 78.0  ? 
295 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? E  GLU 105 ? E GLU 354  ? 1_555 94.8  ? 
296 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? E  GLU 105 ? E GLU 354  ? 1_555 121.5 ? 
297 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? E  GLU 105 ? E GLU 354  ? 1_555 153.0 ? 
298 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? E  GLU 105 ? E GLU 354  ? 1_555 144.5 ? 
299 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? E  GLU 105 ? E GLU 354  ? 1_555 82.6  ? 
300 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 71.9  ? 
301 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 116.6 ? 
302 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 75.4  ? 
303 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 127.4 ? 
304 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 92.1  ? 
305 O   ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 82.5  ? 
306 OD1 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 106.8 ? 
307 OD2 ? E  ASP 71  ? E ASP 320  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 72.5  ? 
308 OE1 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 124.3 ? 
309 OE2 ? E  GLU 75  ? E GLU 324  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 72.0  ? 
310 OD1 ? E  ASN 101 ? E ASN 350  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 88.2  ? 
311 O   ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 77.9  ? 
312 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? JA CA . ? E CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 638  ? 1_555 160.2 ? 
313 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 70.9  ? 
314 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 137.9 ? 
315 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 67.9  ? 
316 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 74.7  ? 
317 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 145.5 ? 
318 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 145.6 ? 
319 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O   ? E  ASP 117 ? E ASP 366  ? 1_555 138.5 ? 
320 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O   ? E  ASP 117 ? E ASP 366  ? 1_555 132.8 ? 
321 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O   ? E  ASP 117 ? E ASP 366  ? 1_555 71.3  ? 
322 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O   ? E  ASP 117 ? E ASP 366  ? 1_555 75.2  ? 
323 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 77.3  ? 
324 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 81.8  ? 
325 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 88.9  ? 
326 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 89.5  ? 
327 O   ? E  ASP 117 ? E ASP 366  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 74.6  ? 
328 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 71.2  ? 
329 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 83.1  ? 
330 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 111.1 ? 
331 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 87.2  ? 
332 O   ? E  ASP 117 ? E ASP 366  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 134.4 ? 
333 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 148.0 ? 
334 OE1 ? E  GLU 98  ? E GLU 347  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 132.6 ? 
335 OD1 ? E  ASN 100 ? E ASN 349  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 119.7 ? 
336 OE1 ? E  GLU 105 ? E GLU 354  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 77.3  ? 
337 OD1 ? E  ASN 116 ? E ASN 365  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 85.2  ? 
338 O   ? E  ASP 117 ? E ASP 366  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 71.5  ? 
339 OD1 ? E  ASP 117 ? E ASP 366  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 146.0 ? 
340 O4  ? HA EZ8 .   ? E EZ8 503  ? 1_555 CA ? IA CA . ? E CA 504  ? 1_555 O3  ? HA EZ8 .   ? E EZ8 503  ? 1_555 65.3  ? 
341 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 OD2 ? E  ASP 106 ? E ASP 355  ? 1_555 47.8  ? 
342 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 608  ? 1_555 71.0  ? 
343 OD2 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 608  ? 1_555 98.0  ? 
344 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 613  ? 1_555 113.8 ? 
345 OD2 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 613  ? 1_555 72.1  ? 
346 O   ? WA HOH .   ? E HOH 608  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 613  ? 1_555 153.9 ? 
347 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 622  ? 1_555 106.2 ? 
348 OD2 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 622  ? 1_555 76.2  ? 
349 O   ? WA HOH .   ? E HOH 608  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 622  ? 1_555 75.3  ? 
350 O   ? WA HOH .   ? E HOH 613  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 622  ? 1_555 78.8  ? 
351 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 629  ? 1_555 62.3  ? 
352 OD2 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 629  ? 1_555 95.4  ? 
353 O   ? WA HOH .   ? E HOH 608  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 629  ? 1_555 98.5  ? 
354 O   ? WA HOH .   ? E HOH 613  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 629  ? 1_555 106.4 ? 
355 O   ? WA HOH .   ? E HOH 622  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 629  ? 1_555 168.5 ? 
356 OD1 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 707  ? 1_555 152.3 ? 
357 OD2 ? E  ASP 106 ? E ASP 355  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 707  ? 1_555 158.2 ? 
358 O   ? WA HOH .   ? E HOH 608  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 707  ? 1_555 88.7  ? 
359 O   ? WA HOH .   ? E HOH 613  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 707  ? 1_555 92.9  ? 
360 O   ? WA HOH .   ? E HOH 622  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 707  ? 1_555 85.7  ? 
361 O   ? WA HOH .   ? E HOH 629  ? 1_555 CA ? KA CA . ? E CA 506  ? 1_555 O   ? WA HOH .   ? E HOH 707  ? 1_555 104.1 ? 
362 O   ? WA HOH .   ? E HOH 614  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? WA HOH .   ? E HOH 616  ? 2_657 77.5  ? 
363 O   ? WA HOH .   ? E HOH 614  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 OD2 ? F  ASP 106 ? F ASP 355  ? 1_555 88.1  ? 
364 O   ? WA HOH .   ? E HOH 616  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 OD2 ? F  ASP 106 ? F ASP 355  ? 1_555 83.1  ? 
365 O   ? WA HOH .   ? E HOH 614  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 604  ? 1_555 158.7 ? 
366 O   ? WA HOH .   ? E HOH 616  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 604  ? 1_555 82.6  ? 
367 OD2 ? F  ASP 106 ? F ASP 355  ? 1_555 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 604  ? 1_555 82.2  ? 
368 O   ? WA HOH .   ? E HOH 614  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 605  ? 1_555 96.1  ? 
369 O   ? WA HOH .   ? E HOH 616  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 605  ? 1_555 172.9 ? 
370 OD2 ? F  ASP 106 ? F ASP 355  ? 1_555 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 605  ? 1_555 93.6  ? 
371 O   ? XA HOH .   ? F HOH 604  ? 1_555 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 605  ? 1_555 103.3 ? 
372 O   ? WA HOH .   ? E HOH 614  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 693  ? 1_555 96.5  ? 
373 O   ? WA HOH .   ? E HOH 616  ? 2_657 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 693  ? 1_555 80.5  ? 
374 OD2 ? F  ASP 106 ? F ASP 355  ? 1_555 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 693  ? 1_555 161.5 ? 
375 O   ? XA HOH .   ? F HOH 604  ? 1_555 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 693  ? 1_555 87.4  ? 
376 O   ? XA HOH .   ? F HOH 605  ? 1_555 CA ? QA CA . ? F CA 505  ? 1_555 O   ? XA HOH .   ? F HOH 693  ? 1_555 103.6 ? 
377 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 49.9  ? 
378 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 94.3  ? 
379 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 76.5  ? 
380 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 114.4 ? 
381 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 66.8  ? 
382 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 51.3  ? 
383 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 161.4 ? 
384 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 141.0 ? 
385 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 78.1  ? 
386 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 74.2  ? 
387 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? F  GLU 105 ? F GLU 354  ? 1_555 98.5  ? 
388 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? F  GLU 105 ? F GLU 354  ? 1_555 133.4 ? 
389 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? F  GLU 105 ? F GLU 354  ? 1_555 147.6 ? 
390 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? F  GLU 105 ? F GLU 354  ? 1_555 142.1 ? 
391 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? F  GLU 105 ? F GLU 354  ? 1_555 80.4  ? 
392 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 76.5  ? 
393 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 115.7 ? 
394 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 74.9  ? 
395 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 124.9 ? 
396 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 85.1  ? 
397 O   ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 79.3  ? 
398 OD1 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 109.0 ? 
399 OD2 ? F  ASP 71  ? F ASP 320  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 84.4  ? 
400 OE1 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 128.4 ? 
401 OE2 ? F  GLU 75  ? F GLU 324  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 77.1  ? 
402 OD1 ? F  ASN 101 ? F ASN 350  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 88.7  ? 
403 O   ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 74.7  ? 
404 OD1 ? F  ASP 106 ? F ASP 355  ? 1_555 CA ? PA CA . ? F CA 504  ? 1_555 O   ? XA HOH .   ? F HOH 618  ? 1_555 154.0 ? 
405 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 74.6  ? 
406 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 148.1 ? 
407 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 75.6  ? 
408 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 69.6  ? 
409 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 144.2 ? 
410 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 138.8 ? 
411 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O   ? F  ASP 117 ? F ASP 366  ? 1_555 129.5 ? 
412 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O   ? F  ASP 117 ? F ASP 366  ? 1_555 136.9 ? 
413 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O   ? F  ASP 117 ? F ASP 366  ? 1_555 69.4  ? 
414 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O   ? F  ASP 117 ? F ASP 366  ? 1_555 70.4  ? 
415 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 74.6  ? 
416 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 81.3  ? 
417 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 89.8  ? 
418 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 88.0  ? 
419 O   ? F  ASP 117 ? F ASP 366  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 74.5  ? 
420 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 75.6  ? 
421 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 79.1  ? 
422 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 109.6 ? 
423 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 93.1  ? 
424 O   ? F  ASP 117 ? F ASP 366  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 135.9 ? 
425 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 147.7 ? 
426 OE1 ? F  GLU 98  ? F GLU 347  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 134.0 ? 
427 OD1 ? F  ASN 100 ? F ASN 349  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 123.5 ? 
428 OE1 ? F  GLU 105 ? F GLU 354  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 73.5  ? 
429 OD1 ? F  ASN 116 ? F ASN 365  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 84.2  ? 
430 O   ? F  ASP 117 ? F ASP 366  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 69.2  ? 
431 OD1 ? F  ASP 117 ? F ASP 366  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 143.3 ? 
432 O4  ? NA EZ8 .   ? F EZ8 502  ? 1_555 CA ? OA CA . ? F CA 503  ? 1_555 O3  ? NA EZ8 .   ? F EZ8 502  ? 1_555 68.7  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 4   ? CYS A 135 ? CYS A 253 ? 1_555 CYS A 384 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 7   ? CYS A 18  ? CYS A 256 ? 1_555 CYS A 267 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 35  ? CYS A 128 ? CYS A 284 ? 1_555 CYS A 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 107 ? CYS A 120 ? CYS A 356 ? 1_555 CYS A 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS B 4   ? CYS B 135 ? CYS B 253 ? 1_555 CYS B 384 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS B 7   ? CYS B 18  ? CYS B 256 ? 1_555 CYS B 267 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS B 35  ? CYS B 128 ? CYS B 284 ? 1_555 CYS B 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS B 107 ? CYS B 120 ? CYS B 356 ? 1_555 CYS B 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS C 4   ? CYS C 135 ? CYS C 253 ? 1_555 CYS C 384 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS C 7   ? CYS C 18  ? CYS C 256 ? 1_555 CYS C 267 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS C 35  ? CYS C 128 ? CYS C 284 ? 1_555 CYS C 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS C 107 ? CYS C 120 ? CYS C 356 ? 1_555 CYS C 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS D 4   ? CYS D 135 ? CYS D 253 ? 1_555 CYS D 384 ? 1_555 SG SG . . . None 'Disulfide bridge' 
14 CYS D 7   ? CYS D 18  ? CYS D 256 ? 1_555 CYS D 267 ? 1_555 SG SG . . . None 'Disulfide bridge' 
15 CYS D 35  ? CYS D 128 ? CYS D 284 ? 1_555 CYS D 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
16 CYS D 107 ? CYS D 120 ? CYS D 356 ? 1_555 CYS D 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
17 CYS E 4   ? CYS E 135 ? CYS E 253 ? 1_555 CYS E 384 ? 1_555 SG SG . . . None 'Disulfide bridge' 
18 CYS E 7   ? CYS E 18  ? CYS E 256 ? 1_555 CYS E 267 ? 1_555 SG SG . . . None 'Disulfide bridge' 
19 CYS E 35  ? CYS E 128 ? CYS E 284 ? 1_555 CYS E 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
20 CYS E 107 ? CYS E 120 ? CYS E 356 ? 1_555 CYS E 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
21 CYS F 4   ? CYS F 135 ? CYS F 253 ? 1_555 CYS F 384 ? 1_555 SG SG . . . None 'Disulfide bridge' 
22 CYS F 7   ? CYS F 18  ? CYS F 256 ? 1_555 CYS F 267 ? 1_555 SG SG . . . None 'Disulfide bridge' 
23 CYS F 35  ? CYS F 128 ? CYS F 284 ? 1_555 CYS F 377 ? 1_555 SG SG . . . None 'Disulfide bridge' 
24 CYS F 107 ? CYS F 120 ? CYS F 356 ? 1_555 CYS F 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 98 A . ? GLU 347 A PRO 99 A ? PRO 348 A 1 2.28   
2 GLU 98 B . ? GLU 347 B PRO 99 B ? PRO 348 B 1 -11.02 
3 GLU 98 C . ? GLU 347 C PRO 99 C ? PRO 348 C 1 4.23   
4 GLU 98 D . ? GLU 347 D PRO 99 D ? PRO 348 D 1 -3.43  
5 GLU 98 E . ? GLU 347 E PRO 99 E ? PRO 348 E 1 -6.96  
6 GLU 98 F . ? GLU 347 F PRO 99 F ? PRO 348 F 1 -6.57  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
AA4 ? 5 ? 
AA5 ? 5 ? 
AA6 ? 5 ? 
AA7 ? 5 ? 
AA8 ? 5 ? 
AA9 ? 5 ? 
AB1 ? 5 ? 
AB2 ? 5 ? 
AB3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA7 4 5 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? parallel      
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? parallel      
AB1 3 4 ? anti-parallel 
AB1 4 5 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? parallel      
AB2 4 5 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? parallel      
AB3 3 4 ? anti-parallel 
AB3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 12  ? PHE A 14  ? THR A 261 PHE A 263 
AA1 2 ASN A 17  ? MET A 21  ? ASN A 266 MET A 270 
AA1 3 PHE A 125 ? SER A 131 ? PHE A 374 SER A 380 
AA1 4 THR A 65  ? SER A 70  ? THR A 314 SER A 319 
AA1 5 GLN A 79  ? TRP A 80  ? GLN A 328 TRP A 329 
AA2 1 GLN A 41  ? LEU A 42  ? GLN A 290 LEU A 291 
AA2 2 PHE A 125 ? SER A 131 ? PHE A 374 SER A 380 
AA2 3 THR A 65  ? SER A 70  ? THR A 314 SER A 319 
AA2 4 CYS A 107 ? SER A 111 ? CYS A 356 SER A 360 
AA2 5 GLY A 114 ? ASP A 118 ? GLY A 363 ASP A 367 
AA3 1 THR B 12  ? PHE B 14  ? THR B 261 PHE B 263 
AA3 2 ASN B 17  ? MET B 21  ? ASN B 266 MET B 270 
AA3 3 PHE B 125 ? SER B 131 ? PHE B 374 SER B 380 
AA3 4 THR B 65  ? SER B 70  ? THR B 314 SER B 319 
AA3 5 GLN B 79  ? TRP B 80  ? GLN B 328 TRP B 329 
AA4 1 GLN B 41  ? LEU B 42  ? GLN B 290 LEU B 291 
AA4 2 PHE B 125 ? SER B 131 ? PHE B 374 SER B 380 
AA4 3 THR B 65  ? SER B 70  ? THR B 314 SER B 319 
AA4 4 CYS B 107 ? SER B 111 ? CYS B 356 SER B 360 
AA4 5 GLY B 114 ? ASP B 118 ? GLY B 363 ASP B 367 
AA5 1 THR C 12  ? PHE C 14  ? THR C 261 PHE C 263 
AA5 2 ASN C 17  ? MET C 21  ? ASN C 266 MET C 270 
AA5 3 PHE C 125 ? SER C 131 ? PHE C 374 SER C 380 
AA5 4 THR C 65  ? GLN C 74  ? THR C 314 GLN C 323 
AA5 5 THR C 77  ? TRP C 80  ? THR C 326 TRP C 329 
AA6 1 GLN C 41  ? LEU C 42  ? GLN C 290 LEU C 291 
AA6 2 PHE C 125 ? SER C 131 ? PHE C 374 SER C 380 
AA6 3 THR C 65  ? GLN C 74  ? THR C 314 GLN C 323 
AA6 4 CYS C 107 ? SER C 111 ? CYS C 356 SER C 360 
AA6 5 GLY C 114 ? ASP C 118 ? GLY C 363 ASP C 367 
AA7 1 THR D 12  ? PHE D 14  ? THR D 261 PHE D 263 
AA7 2 ASN D 17  ? MET D 21  ? ASN D 266 MET D 270 
AA7 3 PHE D 125 ? SER D 131 ? PHE D 374 SER D 380 
AA7 4 THR D 65  ? SER D 70  ? THR D 314 SER D 319 
AA7 5 GLN D 79  ? TRP D 80  ? GLN D 328 TRP D 329 
AA8 1 GLN D 41  ? LEU D 42  ? GLN D 290 LEU D 291 
AA8 2 PHE D 125 ? SER D 131 ? PHE D 374 SER D 380 
AA8 3 THR D 65  ? SER D 70  ? THR D 314 SER D 319 
AA8 4 CYS D 107 ? SER D 111 ? CYS D 356 SER D 360 
AA8 5 GLY D 114 ? ASP D 118 ? GLY D 363 ASP D 367 
AA9 1 THR E 12  ? PHE E 14  ? THR E 261 PHE E 263 
AA9 2 ASN E 17  ? MET E 21  ? ASN E 266 MET E 270 
AA9 3 PHE E 125 ? SER E 131 ? PHE E 374 SER E 380 
AA9 4 THR E 65  ? GLN E 74  ? THR E 314 GLN E 323 
AA9 5 THR E 77  ? TRP E 80  ? THR E 326 TRP E 329 
AB1 1 GLN E 41  ? LEU E 42  ? GLN E 290 LEU E 291 
AB1 2 PHE E 125 ? SER E 131 ? PHE E 374 SER E 380 
AB1 3 THR E 65  ? GLN E 74  ? THR E 314 GLN E 323 
AB1 4 CYS E 107 ? SER E 111 ? CYS E 356 SER E 360 
AB1 5 GLY E 114 ? ASP E 118 ? GLY E 363 ASP E 367 
AB2 1 THR F 12  ? PHE F 14  ? THR F 261 PHE F 263 
AB2 2 ASN F 17  ? MET F 21  ? ASN F 266 MET F 270 
AB2 3 PHE F 125 ? SER F 131 ? PHE F 374 SER F 380 
AB2 4 THR F 65  ? SER F 70  ? THR F 314 SER F 319 
AB2 5 GLN F 79  ? TRP F 80  ? GLN F 328 TRP F 329 
AB3 1 GLN F 41  ? LEU F 42  ? GLN F 290 LEU F 291 
AB3 2 PHE F 125 ? SER F 131 ? PHE F 374 SER F 380 
AB3 3 THR F 65  ? SER F 70  ? THR F 314 SER F 319 
AB3 4 CYS F 107 ? SER F 111 ? CYS F 356 SER F 360 
AB3 5 GLY F 114 ? ASP F 118 ? GLY F 363 ASP F 367 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 14  ? N PHE A 263 O ASN A 17  ? O ASN A 266 
AA1 2 3 N CYS A 18  ? N CYS A 267 O LYS A 130 ? O LYS A 379 
AA1 3 4 O PHE A 125 ? O PHE A 374 N TRP A 66  ? N TRP A 315 
AA1 4 5 N SER A 70  ? N SER A 319 O GLN A 79  ? O GLN A 328 
AA2 1 2 N GLN A 41  ? N GLN A 290 O LYS A 129 ? O LYS A 378 
AA2 2 3 O PHE A 125 ? O PHE A 374 N TRP A 66  ? N TRP A 315 
AA2 3 4 N THR A 65  ? N THR A 314 O PHE A 110 ? O PHE A 359 
AA2 4 5 N SER A 111 ? N SER A 360 O GLY A 114 ? O GLY A 363 
AA3 1 2 N THR B 12  ? N THR B 261 O TYR B 19  ? O TYR B 268 
AA3 2 3 N CYS B 18  ? N CYS B 267 O LYS B 130 ? O LYS B 379 
AA3 3 4 O PHE B 125 ? O PHE B 374 N TRP B 66  ? N TRP B 315 
AA3 4 5 N SER B 70  ? N SER B 319 O GLN B 79  ? O GLN B 328 
AA4 1 2 N GLN B 41  ? N GLN B 290 O LYS B 129 ? O LYS B 378 
AA4 2 3 O PHE B 125 ? O PHE B 374 N TRP B 66  ? N TRP B 315 
AA4 3 4 N THR B 65  ? N THR B 314 O PHE B 110 ? O PHE B 359 
AA4 4 5 N SER B 111 ? N SER B 360 O GLY B 114 ? O GLY B 363 
AA5 1 2 N PHE C 14  ? N PHE C 263 O ASN C 17  ? O ASN C 266 
AA5 2 3 N CYS C 18  ? N CYS C 267 O LYS C 130 ? O LYS C 379 
AA5 3 4 O PHE C 125 ? O PHE C 374 N TRP C 66  ? N TRP C 315 
AA5 4 5 N GLN C 74  ? N GLN C 323 O THR C 77  ? O THR C 326 
AA6 1 2 N GLN C 41  ? N GLN C 290 O LYS C 129 ? O LYS C 378 
AA6 2 3 O PHE C 125 ? O PHE C 374 N TRP C 66  ? N TRP C 315 
AA6 3 4 N THR C 65  ? N THR C 314 O PHE C 110 ? O PHE C 359 
AA6 4 5 N GLU C 109 ? N GLU C 358 O ASN C 116 ? O ASN C 365 
AA7 1 2 N THR D 12  ? N THR D 261 O TYR D 19  ? O TYR D 268 
AA7 2 3 N CYS D 18  ? N CYS D 267 O LYS D 130 ? O LYS D 379 
AA7 3 4 O PHE D 125 ? O PHE D 374 N TRP D 66  ? N TRP D 315 
AA7 4 5 N SER D 70  ? N SER D 319 O GLN D 79  ? O GLN D 328 
AA8 1 2 N GLN D 41  ? N GLN D 290 O LYS D 129 ? O LYS D 378 
AA8 2 3 O PHE D 125 ? O PHE D 374 N TRP D 66  ? N TRP D 315 
AA8 3 4 N THR D 65  ? N THR D 314 O PHE D 110 ? O PHE D 359 
AA8 4 5 N CYS D 107 ? N CYS D 356 O ASP D 118 ? O ASP D 367 
AA9 1 2 N THR E 12  ? N THR E 261 O TYR E 19  ? O TYR E 268 
AA9 2 3 N CYS E 18  ? N CYS E 267 O LYS E 130 ? O LYS E 379 
AA9 3 4 O PHE E 125 ? O PHE E 374 N TRP E 66  ? N TRP E 315 
AA9 4 5 N SER E 70  ? N SER E 319 O GLN E 79  ? O GLN E 328 
AB1 1 2 N GLN E 41  ? N GLN E 290 O LYS E 129 ? O LYS E 378 
AB1 2 3 O PHE E 125 ? O PHE E 374 N TRP E 66  ? N TRP E 315 
AB1 3 4 N THR E 65  ? N THR E 314 O PHE E 110 ? O PHE E 359 
AB1 4 5 N SER E 111 ? N SER E 360 O GLY E 114 ? O GLY E 363 
AB2 1 2 N THR F 12  ? N THR F 261 O TYR F 19  ? O TYR F 268 
AB2 2 3 N CYS F 18  ? N CYS F 267 O LYS F 130 ? O LYS F 379 
AB2 3 4 O PHE F 125 ? O PHE F 374 N TRP F 66  ? N TRP F 315 
AB2 4 5 N SER F 70  ? N SER F 319 O GLN F 79  ? O GLN F 328 
AB3 1 2 N GLN F 41  ? N GLN F 290 O LYS F 129 ? O LYS F 378 
AB3 2 3 O PHE F 125 ? O PHE F 374 N TRP F 66  ? N TRP F 315 
AB3 3 4 N THR F 65  ? N THR F 314 O PHE F 110 ? O PHE F 359 
AB3 4 5 N SER F 111 ? N SER F 360 O GLY F 114 ? O GLY F 363 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A EZ8 1001 ? 21 'binding site for residue EZ8 A 1001' 
AC2 Software A CA  1002 ? 6  'binding site for residue CA A 1002'  
AC3 Software A CA  1003 ? 6  'binding site for residue CA A 1003'  
AC4 Software A CA  1004 ? 4  'binding site for residue CA A 1004'  
AC5 Software A CL  1005 ? 2  'binding site for residue CL A 1005'  
AC6 Software A CL  1006 ? 1  'binding site for residue CL A 1006'  
AC7 Software A CL  1007 ? 2  'binding site for residue CL A 1007'  
AC8 Software B EZ8 1001 ? 29 'binding site for residue EZ8 B 1001' 
AC9 Software B CA  1002 ? 6  'binding site for residue CA B 1002'  
AD1 Software B CA  1003 ? 6  'binding site for residue CA B 1003'  
AD2 Software B CA  1004 ? 6  'binding site for residue CA B 1004'  
AD3 Software B CL  1005 ? 1  'binding site for residue CL B 1005'  
AD4 Software B CL  1006 ? 2  'binding site for residue CL B 1006'  
AD5 Software C EZ8 1001 ? 28 'binding site for residue EZ8 C 1001' 
AD6 Software C CA  1002 ? 6  'binding site for residue CA C 1002'  
AD7 Software C CA  1003 ? 6  'binding site for residue CA C 1003'  
AD8 Software C CA  1004 ? 6  'binding site for residue CA C 1004'  
AD9 Software C CL  1005 ? 2  'binding site for residue CL C 1005'  
AE1 Software C CL  1006 ? 2  'binding site for residue CL C 1006'  
AE2 Software D CL  501  ? 1  'binding site for residue CL D 501'   
AE3 Software D EZ8 502  ? 27 'binding site for residue EZ8 D 502'  
AE4 Software D CA  503  ? 6  'binding site for residue CA D 503'   
AE5 Software D CA  504  ? 6  'binding site for residue CA D 504'   
AE6 Software D CA  505  ? 6  'binding site for residue CA D 505'   
AE7 Software D CL  506  ? 2  'binding site for residue CL D 506'   
AE8 Software E CL  501  ? 2  'binding site for residue CL E 501'   
AE9 Software E CL  502  ? 2  'binding site for residue CL E 502'   
AF1 Software E EZ8 503  ? 25 'binding site for residue EZ8 E 503'  
AF2 Software E CA  504  ? 6  'binding site for residue CA E 504'   
AF3 Software E CA  505  ? 6  'binding site for residue CA E 505'   
AF4 Software E CA  506  ? 7  'binding site for residue CA E 506'   
AF5 Software E CL  507  ? 2  'binding site for residue CL E 507'   
AF6 Software F CL  501  ? 1  'binding site for residue CL F 501'   
AF7 Software F EZ8 502  ? 26 'binding site for residue EZ8 F 502'  
AF8 Software F CA  503  ? 6  'binding site for residue CA F 503'   
AF9 Software F CA  504  ? 6  'binding site for residue CA F 504'   
AG1 Software F CA  505  ? 4  'binding site for residue CA F 505'   
AG2 Software F CL  506  ? 3  'binding site for residue CL F 506'   
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 21 PHE A  64  ? PHE A 313  . ? 1_555 ? 
2   AC1 21 GLU A  98  ? GLU A 347  . ? 1_555 ? 
3   AC1 21 ASN A  100 ? ASN A 349  . ? 1_555 ? 
4   AC1 21 GLY A  103 ? GLY A 352  . ? 1_555 ? 
5   AC1 21 GLU A  105 ? GLU A 354  . ? 1_555 ? 
6   AC1 21 GLU A  109 ? GLU A 358  . ? 1_555 ? 
7   AC1 21 SER A  111 ? SER A 360  . ? 1_555 ? 
8   AC1 21 ASN A  116 ? ASN A 365  . ? 1_555 ? 
9   AC1 21 ASP A  117 ? ASP A 366  . ? 1_555 ? 
10  AC1 21 ASP A  118 ? ASP A 367  . ? 1_555 ? 
11  AC1 21 LYS A  119 ? LYS A 368  . ? 1_555 ? 
12  AC1 21 CA  H  .   ? CA  A 1002 . ? 1_555 ? 
13  AC1 21 HOH SA .   ? HOH A 1108 . ? 1_555 ? 
14  AC1 21 HOH SA .   ? HOH A 1113 . ? 1_555 ? 
15  AC1 21 ASN D  23  ? ASN D 272  . ? 1_555 ? 
16  AC1 21 ARG D  60  ? ARG D 309  . ? 1_555 ? 
17  AC1 21 SER D  61  ? SER D 310  . ? 1_555 ? 
18  AC1 21 ASN D  62  ? ASN D 311  . ? 1_555 ? 
19  AC1 21 ARG D  63  ? ARG D 312  . ? 1_555 ? 
20  AC1 21 THR D  65  ? THR D 314  . ? 1_555 ? 
21  AC1 21 CL  Z  .   ? CL  D 501  . ? 1_555 ? 
22  AC2 6  GLU A  98  ? GLU A 347  . ? 1_555 ? 
23  AC2 6  ASN A  100 ? ASN A 349  . ? 1_555 ? 
24  AC2 6  GLU A  105 ? GLU A 354  . ? 1_555 ? 
25  AC2 6  ASN A  116 ? ASN A 365  . ? 1_555 ? 
26  AC2 6  ASP A  117 ? ASP A 366  . ? 1_555 ? 
27  AC2 6  EZ8 G  .   ? EZ8 A 1001 . ? 1_555 ? 
28  AC3 6  ASP A  71  ? ASP A 320  . ? 1_555 ? 
29  AC3 6  GLU A  75  ? GLU A 324  . ? 1_555 ? 
30  AC3 6  ASN A  101 ? ASN A 350  . ? 1_555 ? 
31  AC3 6  GLU A  105 ? GLU A 354  . ? 1_555 ? 
32  AC3 6  ASP A  106 ? ASP A 355  . ? 1_555 ? 
33  AC3 6  HOH SA .   ? HOH A 1129 . ? 1_555 ? 
34  AC4 4  ASP A  106 ? ASP A 355  . ? 1_555 ? 
35  AC4 4  HOH SA .   ? HOH A 1102 . ? 1_555 ? 
36  AC4 4  HOH SA .   ? HOH A 1118 . ? 1_555 ? 
37  AC4 4  HOH SA .   ? HOH A 1139 . ? 1_555 ? 
38  AC5 2  ASN A  23  ? ASN A 272  . ? 1_555 ? 
39  AC5 2  SER A  24  ? SER A 273  . ? 1_555 ? 
40  AC6 1  ARG A  60  ? ARG A 309  . ? 1_555 ? 
41  AC7 2  GLN A  15  ? GLN A 264  . ? 1_555 ? 
42  AC7 2  EZ8 N  .   ? EZ8 B 1001 . ? 1_555 ? 
43  AC8 29 GLN A  15  ? GLN A 264  . ? 1_555 ? 
44  AC8 29 GLY A  16  ? GLY A 265  . ? 1_555 ? 
45  AC8 29 CL  M  .   ? CL  A 1007 . ? 1_555 ? 
46  AC8 29 PHE B  64  ? PHE B 313  . ? 1_555 ? 
47  AC8 29 GLU B  98  ? GLU B 347  . ? 1_555 ? 
48  AC8 29 ASN B  100 ? ASN B 349  . ? 1_555 ? 
49  AC8 29 VAL B  102 ? VAL B 351  . ? 1_555 ? 
50  AC8 29 GLY B  103 ? GLY B 352  . ? 1_555 ? 
51  AC8 29 GLU B  105 ? GLU B 354  . ? 1_555 ? 
52  AC8 29 GLU B  109 ? GLU B 358  . ? 1_555 ? 
53  AC8 29 SER B  111 ? SER B 360  . ? 1_555 ? 
54  AC8 29 ASN B  116 ? ASN B 365  . ? 1_555 ? 
55  AC8 29 ASP B  117 ? ASP B 366  . ? 1_555 ? 
56  AC8 29 ASP B  118 ? ASP B 367  . ? 1_555 ? 
57  AC8 29 LYS B  119 ? LYS B 368  . ? 1_555 ? 
58  AC8 29 CA  O  .   ? CA  B 1002 . ? 1_555 ? 
59  AC8 29 HOH TA .   ? HOH B 1105 . ? 1_555 ? 
60  AC8 29 HOH TA .   ? HOH B 1111 . ? 1_555 ? 
61  AC8 29 HOH TA .   ? HOH B 1116 . ? 1_555 ? 
62  AC8 29 HOH TA .   ? HOH B 1151 . ? 1_555 ? 
63  AC8 29 ASN C  23  ? ASN C 272  . ? 1_555 ? 
64  AC8 29 GLN C  57  ? GLN C 306  . ? 1_555 ? 
65  AC8 29 ARG C  60  ? ARG C 309  . ? 1_555 ? 
66  AC8 29 SER C  61  ? SER C 310  . ? 1_555 ? 
67  AC8 29 ASN C  62  ? ASN C 311  . ? 1_555 ? 
68  AC8 29 ARG C  63  ? ARG C 312  . ? 1_555 ? 
69  AC8 29 THR C  65  ? THR C 314  . ? 1_555 ? 
70  AC8 29 PHE C  125 ? PHE C 374  . ? 1_555 ? 
71  AC8 29 HOH UA .   ? HOH C 1139 . ? 1_555 ? 
72  AC9 6  GLU B  98  ? GLU B 347  . ? 1_555 ? 
73  AC9 6  ASN B  100 ? ASN B 349  . ? 1_555 ? 
74  AC9 6  GLU B  105 ? GLU B 354  . ? 1_555 ? 
75  AC9 6  ASN B  116 ? ASN B 365  . ? 1_555 ? 
76  AC9 6  ASP B  117 ? ASP B 366  . ? 1_555 ? 
77  AC9 6  EZ8 N  .   ? EZ8 B 1001 . ? 1_555 ? 
78  AD1 6  ASP B  71  ? ASP B 320  . ? 1_555 ? 
79  AD1 6  GLU B  75  ? GLU B 324  . ? 1_555 ? 
80  AD1 6  ASN B  101 ? ASN B 350  . ? 1_555 ? 
81  AD1 6  GLU B  105 ? GLU B 354  . ? 1_555 ? 
82  AD1 6  ASP B  106 ? ASP B 355  . ? 1_555 ? 
83  AD1 6  HOH TA .   ? HOH B 1133 . ? 1_555 ? 
84  AD2 6  ASP B  106 ? ASP B 355  . ? 1_555 ? 
85  AD2 6  HOH TA .   ? HOH B 1108 . ? 1_555 ? 
86  AD2 6  HOH TA .   ? HOH B 1126 . ? 1_555 ? 
87  AD2 6  HOH TA .   ? HOH B 1148 . ? 1_555 ? 
88  AD2 6  HOH TA .   ? HOH B 1155 . ? 1_555 ? 
89  AD2 6  HOH TA .   ? HOH B 1212 . ? 1_555 ? 
90  AD3 1  SER B  24  ? SER B 273  . ? 1_555 ? 
91  AD4 2  GLN B  15  ? GLN B 264  . ? 1_555 ? 
92  AD4 2  EZ8 NA .   ? EZ8 F 502  . ? 1_555 ? 
93  AD5 28 ASN B  23  ? ASN B 272  . ? 1_555 ? 
94  AD5 28 GLN B  57  ? GLN B 306  . ? 1_555 ? 
95  AD5 28 ARG B  60  ? ARG B 309  . ? 1_555 ? 
96  AD5 28 SER B  61  ? SER B 310  . ? 1_555 ? 
97  AD5 28 ASN B  62  ? ASN B 311  . ? 1_555 ? 
98  AD5 28 ARG B  63  ? ARG B 312  . ? 1_555 ? 
99  AD5 28 THR B  65  ? THR B 314  . ? 1_555 ? 
100 AD5 28 PHE B  125 ? PHE B 374  . ? 1_555 ? 
101 AD5 28 PHE C  64  ? PHE C 313  . ? 1_555 ? 
102 AD5 28 GLU C  98  ? GLU C 347  . ? 1_555 ? 
103 AD5 28 ASN C  100 ? ASN C 349  . ? 1_555 ? 
104 AD5 28 VAL C  102 ? VAL C 351  . ? 1_555 ? 
105 AD5 28 GLY C  103 ? GLY C 352  . ? 1_555 ? 
106 AD5 28 GLU C  105 ? GLU C 354  . ? 1_555 ? 
107 AD5 28 GLU C  109 ? GLU C 358  . ? 1_555 ? 
108 AD5 28 SER C  111 ? SER C 360  . ? 1_555 ? 
109 AD5 28 ASN C  116 ? ASN C 365  . ? 1_555 ? 
110 AD5 28 ASP C  117 ? ASP C 366  . ? 1_555 ? 
111 AD5 28 ASP C  118 ? ASP C 367  . ? 1_555 ? 
112 AD5 28 LYS C  119 ? LYS C 368  . ? 1_555 ? 
113 AD5 28 CA  U  .   ? CA  C 1002 . ? 1_555 ? 
114 AD5 28 HOH UA .   ? HOH C 1105 . ? 1_555 ? 
115 AD5 28 HOH UA .   ? HOH C 1111 . ? 1_555 ? 
116 AD5 28 HOH UA .   ? HOH C 1124 . ? 1_555 ? 
117 AD5 28 GLN E  15  ? GLN E 264  . ? 1_555 ? 
118 AD5 28 GLY E  16  ? GLY E 265  . ? 1_555 ? 
119 AD5 28 GLU E  49  ? GLU E 298  . ? 1_555 ? 
120 AD5 28 CL  GA .   ? CL  E 502  . ? 1_555 ? 
121 AD6 6  GLU C  98  ? GLU C 347  . ? 1_555 ? 
122 AD6 6  ASN C  100 ? ASN C 349  . ? 1_555 ? 
123 AD6 6  GLU C  105 ? GLU C 354  . ? 1_555 ? 
124 AD6 6  ASN C  116 ? ASN C 365  . ? 1_555 ? 
125 AD6 6  ASP C  117 ? ASP C 366  . ? 1_555 ? 
126 AD6 6  EZ8 T  .   ? EZ8 C 1001 . ? 1_555 ? 
127 AD7 6  ASP C  71  ? ASP C 320  . ? 1_555 ? 
128 AD7 6  GLU C  75  ? GLU C 324  . ? 1_555 ? 
129 AD7 6  ASN C  101 ? ASN C 350  . ? 1_555 ? 
130 AD7 6  GLU C  105 ? GLU C 354  . ? 1_555 ? 
131 AD7 6  ASP C  106 ? ASP C 355  . ? 1_555 ? 
132 AD7 6  HOH UA .   ? HOH C 1121 . ? 1_555 ? 
133 AD8 6  ASP C  106 ? ASP C 355  . ? 1_555 ? 
134 AD8 6  HOH UA .   ? HOH C 1112 . ? 1_555 ? 
135 AD8 6  HOH UA .   ? HOH C 1126 . ? 1_555 ? 
136 AD8 6  HOH UA .   ? HOH C 1128 . ? 1_555 ? 
137 AD8 6  HOH UA .   ? HOH C 1130 . ? 1_555 ? 
138 AD8 6  HOH UA .   ? HOH C 1221 . ? 1_555 ? 
139 AD9 2  ASN C  23  ? ASN C 272  . ? 1_555 ? 
140 AD9 2  SER C  24  ? SER C 273  . ? 1_555 ? 
141 AE1 2  GLN C  15  ? GLN C 264  . ? 1_555 ? 
142 AE1 2  EZ8 AA .   ? EZ8 D 502  . ? 1_555 ? 
143 AE2 1  EZ8 G  .   ? EZ8 A 1001 . ? 1_555 ? 
144 AE3 27 SER A  22  ? SER A 271  . ? 1_555 ? 
145 AE3 27 ASN A  23  ? ASN A 272  . ? 1_555 ? 
146 AE3 27 ARG A  60  ? ARG A 309  . ? 1_555 ? 
147 AE3 27 SER A  61  ? SER A 310  . ? 1_555 ? 
148 AE3 27 ASN A  62  ? ASN A 311  . ? 1_555 ? 
149 AE3 27 ARG A  63  ? ARG A 312  . ? 1_555 ? 
150 AE3 27 THR A  65  ? THR A 314  . ? 1_555 ? 
151 AE3 27 PHE A  125 ? PHE A 374  . ? 1_555 ? 
152 AE3 27 PHE C  14  ? PHE C 263  . ? 1_555 ? 
153 AE3 27 GLN C  15  ? GLN C 264  . ? 1_555 ? 
154 AE3 27 GLY C  16  ? GLY C 265  . ? 1_555 ? 
155 AE3 27 GLU C  49  ? GLU C 298  . ? 1_555 ? 
156 AE3 27 CL  Y  .   ? CL  C 1006 . ? 1_555 ? 
157 AE3 27 PHE D  64  ? PHE D 313  . ? 1_555 ? 
158 AE3 27 GLU D  98  ? GLU D 347  . ? 1_555 ? 
159 AE3 27 ASN D  100 ? ASN D 349  . ? 1_555 ? 
160 AE3 27 VAL D  102 ? VAL D 351  . ? 1_555 ? 
161 AE3 27 GLU D  105 ? GLU D 354  . ? 1_555 ? 
162 AE3 27 GLU D  109 ? GLU D 358  . ? 1_555 ? 
163 AE3 27 SER D  111 ? SER D 360  . ? 1_555 ? 
164 AE3 27 ASN D  116 ? ASN D 365  . ? 1_555 ? 
165 AE3 27 ASP D  117 ? ASP D 366  . ? 1_555 ? 
166 AE3 27 ASP D  118 ? ASP D 367  . ? 1_555 ? 
167 AE3 27 LYS D  119 ? LYS D 368  . ? 1_555 ? 
168 AE3 27 CA  BA .   ? CA  D 503  . ? 1_555 ? 
169 AE3 27 HOH VA .   ? HOH D 601  . ? 1_555 ? 
170 AE3 27 HOH VA .   ? HOH D 628  . ? 1_555 ? 
171 AE4 6  GLU D  98  ? GLU D 347  . ? 1_555 ? 
172 AE4 6  ASN D  100 ? ASN D 349  . ? 1_555 ? 
173 AE4 6  GLU D  105 ? GLU D 354  . ? 1_555 ? 
174 AE4 6  ASN D  116 ? ASN D 365  . ? 1_555 ? 
175 AE4 6  ASP D  117 ? ASP D 366  . ? 1_555 ? 
176 AE4 6  EZ8 AA .   ? EZ8 D 502  . ? 1_555 ? 
177 AE5 6  ASP D  71  ? ASP D 320  . ? 1_555 ? 
178 AE5 6  GLU D  75  ? GLU D 324  . ? 1_555 ? 
179 AE5 6  ASN D  101 ? ASN D 350  . ? 1_555 ? 
180 AE5 6  GLU D  105 ? GLU D 354  . ? 1_555 ? 
181 AE5 6  ASP D  106 ? ASP D 355  . ? 1_555 ? 
182 AE5 6  HOH VA .   ? HOH D 623  . ? 1_555 ? 
183 AE6 6  ASP D  106 ? ASP D 355  . ? 1_555 ? 
184 AE6 6  HOH VA .   ? HOH D 610  . ? 1_555 ? 
185 AE6 6  HOH VA .   ? HOH D 617  . ? 1_555 ? 
186 AE6 6  HOH VA .   ? HOH D 622  . ? 1_555 ? 
187 AE6 6  HOH VA .   ? HOH D 649  . ? 1_555 ? 
188 AE6 6  HOH VA .   ? HOH D 697  . ? 1_555 ? 
189 AE7 2  ASN D  23  ? ASN D 272  . ? 1_555 ? 
190 AE7 2  SER D  24  ? SER D 273  . ? 1_555 ? 
191 AE8 2  ARG B  60  ? ARG B 309  . ? 1_555 ? 
192 AE8 2  ARG E  60  ? ARG E 309  . ? 1_555 ? 
193 AE9 2  EZ8 T  .   ? EZ8 C 1001 . ? 1_555 ? 
194 AE9 2  GLN E  15  ? GLN E 264  . ? 1_555 ? 
195 AF1 25 PHE E  64  ? PHE E 313  . ? 1_555 ? 
196 AF1 25 GLU E  98  ? GLU E 347  . ? 1_555 ? 
197 AF1 25 ASN E  100 ? ASN E 349  . ? 1_555 ? 
198 AF1 25 VAL E  102 ? VAL E 351  . ? 1_555 ? 
199 AF1 25 GLY E  103 ? GLY E 352  . ? 1_555 ? 
200 AF1 25 GLU E  105 ? GLU E 354  . ? 1_555 ? 
201 AF1 25 GLU E  109 ? GLU E 358  . ? 1_555 ? 
202 AF1 25 SER E  111 ? SER E 360  . ? 1_555 ? 
203 AF1 25 ASN E  116 ? ASN E 365  . ? 1_555 ? 
204 AF1 25 ASP E  117 ? ASP E 366  . ? 1_555 ? 
205 AF1 25 ASP E  118 ? ASP E 367  . ? 1_555 ? 
206 AF1 25 LYS E  119 ? LYS E 368  . ? 1_555 ? 
207 AF1 25 CA  IA .   ? CA  E 504  . ? 1_555 ? 
208 AF1 25 HOH WA .   ? HOH E 615  . ? 1_555 ? 
209 AF1 25 HOH WA .   ? HOH E 620  . ? 1_555 ? 
210 AF1 25 HOH WA .   ? HOH E 648  . ? 1_555 ? 
211 AF1 25 HOH WA .   ? HOH E 650  . ? 1_555 ? 
212 AF1 25 ASN F  23  ? ASN F 272  . ? 1_555 ? 
213 AF1 25 ARG F  60  ? ARG F 309  . ? 1_555 ? 
214 AF1 25 SER F  61  ? SER F 310  . ? 1_555 ? 
215 AF1 25 ASN F  62  ? ASN F 311  . ? 1_555 ? 
216 AF1 25 ARG F  63  ? ARG F 312  . ? 1_555 ? 
217 AF1 25 THR F  65  ? THR F 314  . ? 1_555 ? 
218 AF1 25 PHE F  125 ? PHE F 374  . ? 1_555 ? 
219 AF1 25 CL  MA .   ? CL  F 501  . ? 1_555 ? 
220 AF2 6  GLU E  98  ? GLU E 347  . ? 1_555 ? 
221 AF2 6  ASN E  100 ? ASN E 349  . ? 1_555 ? 
222 AF2 6  GLU E  105 ? GLU E 354  . ? 1_555 ? 
223 AF2 6  ASN E  116 ? ASN E 365  . ? 1_555 ? 
224 AF2 6  ASP E  117 ? ASP E 366  . ? 1_555 ? 
225 AF2 6  EZ8 HA .   ? EZ8 E 503  . ? 1_555 ? 
226 AF3 6  ASP E  71  ? ASP E 320  . ? 1_555 ? 
227 AF3 6  GLU E  75  ? GLU E 324  . ? 1_555 ? 
228 AF3 6  ASN E  101 ? ASN E 350  . ? 1_555 ? 
229 AF3 6  GLU E  105 ? GLU E 354  . ? 1_555 ? 
230 AF3 6  ASP E  106 ? ASP E 355  . ? 1_555 ? 
231 AF3 6  HOH WA .   ? HOH E 638  . ? 1_555 ? 
232 AF4 7  GLU E  75  ? GLU E 324  . ? 1_555 ? 
233 AF4 7  ASP E  106 ? ASP E 355  . ? 1_555 ? 
234 AF4 7  HOH WA .   ? HOH E 608  . ? 1_555 ? 
235 AF4 7  HOH WA .   ? HOH E 613  . ? 1_555 ? 
236 AF4 7  HOH WA .   ? HOH E 622  . ? 1_555 ? 
237 AF4 7  HOH WA .   ? HOH E 629  . ? 1_555 ? 
238 AF4 7  HOH WA .   ? HOH E 707  . ? 1_555 ? 
239 AF5 2  ASN E  23  ? ASN E 272  . ? 1_555 ? 
240 AF5 2  SER E  24  ? SER E 273  . ? 1_555 ? 
241 AF6 1  EZ8 HA .   ? EZ8 E 503  . ? 1_555 ? 
242 AF7 26 GLN B  15  ? GLN B 264  . ? 1_555 ? 
243 AF7 26 GLY B  16  ? GLY B 265  . ? 1_555 ? 
244 AF7 26 CL  S  .   ? CL  B 1006 . ? 1_555 ? 
245 AF7 26 ASN E  23  ? ASN E 272  . ? 1_555 ? 
246 AF7 26 ARG E  60  ? ARG E 309  . ? 1_555 ? 
247 AF7 26 SER E  61  ? SER E 310  . ? 1_555 ? 
248 AF7 26 ASN E  62  ? ASN E 311  . ? 1_555 ? 
249 AF7 26 ARG E  63  ? ARG E 312  . ? 1_555 ? 
250 AF7 26 THR E  65  ? THR E 314  . ? 1_555 ? 
251 AF7 26 PHE E  125 ? PHE E 374  . ? 1_555 ? 
252 AF7 26 PHE F  64  ? PHE F 313  . ? 1_555 ? 
253 AF7 26 GLU F  98  ? GLU F 347  . ? 1_555 ? 
254 AF7 26 ASN F  100 ? ASN F 349  . ? 1_555 ? 
255 AF7 26 VAL F  102 ? VAL F 351  . ? 1_555 ? 
256 AF7 26 GLY F  103 ? GLY F 352  . ? 1_555 ? 
257 AF7 26 GLU F  105 ? GLU F 354  . ? 1_555 ? 
258 AF7 26 GLU F  109 ? GLU F 358  . ? 1_555 ? 
259 AF7 26 SER F  111 ? SER F 360  . ? 1_555 ? 
260 AF7 26 ASN F  116 ? ASN F 365  . ? 1_555 ? 
261 AF7 26 ASP F  117 ? ASP F 366  . ? 1_555 ? 
262 AF7 26 ASP F  118 ? ASP F 367  . ? 1_555 ? 
263 AF7 26 LYS F  119 ? LYS F 368  . ? 1_555 ? 
264 AF7 26 CA  OA .   ? CA  F 503  . ? 1_555 ? 
265 AF7 26 HOH XA .   ? HOH F 602  . ? 1_555 ? 
266 AF7 26 HOH XA .   ? HOH F 615  . ? 1_555 ? 
267 AF7 26 HOH XA .   ? HOH F 622  . ? 1_555 ? 
268 AF8 6  GLU F  98  ? GLU F 347  . ? 1_555 ? 
269 AF8 6  ASN F  100 ? ASN F 349  . ? 1_555 ? 
270 AF8 6  GLU F  105 ? GLU F 354  . ? 1_555 ? 
271 AF8 6  ASN F  116 ? ASN F 365  . ? 1_555 ? 
272 AF8 6  ASP F  117 ? ASP F 366  . ? 1_555 ? 
273 AF8 6  EZ8 NA .   ? EZ8 F 502  . ? 1_555 ? 
274 AF9 6  ASP F  71  ? ASP F 320  . ? 1_555 ? 
275 AF9 6  GLU F  75  ? GLU F 324  . ? 1_555 ? 
276 AF9 6  ASN F  101 ? ASN F 350  . ? 1_555 ? 
277 AF9 6  GLU F  105 ? GLU F 354  . ? 1_555 ? 
278 AF9 6  ASP F  106 ? ASP F 355  . ? 1_555 ? 
279 AF9 6  HOH XA .   ? HOH F 618  . ? 1_555 ? 
280 AG1 4  ASP F  106 ? ASP F 355  . ? 1_555 ? 
281 AG1 4  HOH XA .   ? HOH F 604  . ? 1_555 ? 
282 AG1 4  HOH XA .   ? HOH F 605  . ? 1_555 ? 
283 AG1 4  HOH XA .   ? HOH F 693  . ? 1_555 ? 
284 AG2 3  SER F  22  ? SER F 271  . ? 1_555 ? 
285 AG2 3  ASN F  23  ? ASN F 272  . ? 1_555 ? 
286 AG2 3  SER F  24  ? SER F 273  . ? 1_555 ? 
# 
_pdbx_entry_details.entry_id                   6GHV 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 259 ? ? 88.08 -9.19  
2  1 GLU A 353 ? ? 63.86 95.07  
3  1 GLU B 259 ? ? 87.58 -10.31 
4  1 GLN B 264 ? ? 38.98 52.45  
5  1 GLU B 353 ? ? 76.19 97.74  
6  1 GLU C 259 ? ? 82.94 -14.16 
7  1 GLU C 353 ? ? 70.67 92.18  
8  1 GLU D 259 ? ? 89.61 -12.06 
9  1 ASN D 311 ? ? 34.04 47.70  
10 1 GLU D 353 ? ? 75.04 95.22  
11 1 GLU E 259 ? ? 84.19 -9.01  
12 1 GLN E 264 ? ? 32.95 53.29  
13 1 GLU E 353 ? ? 63.51 101.18 
14 1 GLU F 259 ? ? 90.44 -15.11 
15 1 GLU F 353 ? ? 79.78 105.04 
# 
_pdbx_phasing_MR.entry_id                     6GHV 
_pdbx_phasing_MR.method_rotation              ? 
_pdbx_phasing_MR.method_translation           ? 
_pdbx_phasing_MR.model_details                ? 
_pdbx_phasing_MR.R_factor                     ? 
_pdbx_phasing_MR.R_rigid_body                 0.583 
_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc   ? 
_pdbx_phasing_MR.correlation_coeff_Io_to_Ic   ? 
_pdbx_phasing_MR.d_res_high_rotation          92.670 
_pdbx_phasing_MR.d_res_low_rotation           3.500 
_pdbx_phasing_MR.d_res_high_translation       ? 
_pdbx_phasing_MR.d_res_low_translation        ? 
_pdbx_phasing_MR.packing                      ? 
_pdbx_phasing_MR.reflns_percent_rotation      ? 
_pdbx_phasing_MR.reflns_percent_translation   ? 
_pdbx_phasing_MR.sigma_F_rotation             ? 
_pdbx_phasing_MR.sigma_F_translation          ? 
_pdbx_phasing_MR.sigma_I_rotation             ? 
_pdbx_phasing_MR.sigma_I_translation          ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1195 ? 6.43 . 
2 1 O ? B HOH 1225 ? 7.06 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A GLU 250 ? A GLU 1   
2   1 Y 1 A ARG 251 ? A ARG 2   
3   1 Y 1 A LEU 252 ? A LEU 3   
4   1 Y 1 A SER 385 ? A SER 136 
5   1 Y 1 A ARG 386 ? A ARG 137 
6   1 Y 1 A ASP 387 ? A ASP 138 
7   1 Y 1 A GLU 388 ? A GLU 139 
8   1 Y 1 A GLU 389 ? A GLU 140 
9   1 Y 1 A GLN 390 ? A GLN 141 
10  1 Y 1 A PHE 391 ? A PHE 142 
11  1 Y 1 A LEU 392 ? A LEU 143 
12  1 Y 1 A SER 393 ? A SER 144 
13  1 Y 1 A PRO 394 ? A PRO 145 
14  1 Y 1 A ALA 395 ? A ALA 146 
15  1 Y 1 A PRO 396 ? A PRO 147 
16  1 Y 1 A ALA 397 ? A ALA 148 
17  1 Y 1 A THR 398 ? A THR 149 
18  1 Y 1 A PRO 399 ? A PRO 150 
19  1 Y 1 A ASN 400 ? A ASN 151 
20  1 Y 1 A PRO 401 ? A PRO 152 
21  1 Y 1 A PRO 402 ? A PRO 153 
22  1 Y 1 A PRO 403 ? A PRO 154 
23  1 Y 1 A ALA 404 ? A ALA 155 
24  1 Y 1 B GLU 250 ? B GLU 1   
25  1 Y 1 B ARG 251 ? B ARG 2   
26  1 Y 1 B LEU 252 ? B LEU 3   
27  1 Y 1 B SER 385 ? B SER 136 
28  1 Y 1 B ARG 386 ? B ARG 137 
29  1 Y 1 B ASP 387 ? B ASP 138 
30  1 Y 1 B GLU 388 ? B GLU 139 
31  1 Y 1 B GLU 389 ? B GLU 140 
32  1 Y 1 B GLN 390 ? B GLN 141 
33  1 Y 1 B PHE 391 ? B PHE 142 
34  1 Y 1 B LEU 392 ? B LEU 143 
35  1 Y 1 B SER 393 ? B SER 144 
36  1 Y 1 B PRO 394 ? B PRO 145 
37  1 Y 1 B ALA 395 ? B ALA 146 
38  1 Y 1 B PRO 396 ? B PRO 147 
39  1 Y 1 B ALA 397 ? B ALA 148 
40  1 Y 1 B THR 398 ? B THR 149 
41  1 Y 1 B PRO 399 ? B PRO 150 
42  1 Y 1 B ASN 400 ? B ASN 151 
43  1 Y 1 B PRO 401 ? B PRO 152 
44  1 Y 1 B PRO 402 ? B PRO 153 
45  1 Y 1 B PRO 403 ? B PRO 154 
46  1 Y 1 B ALA 404 ? B ALA 155 
47  1 Y 1 C GLU 250 ? C GLU 1   
48  1 Y 1 C ARG 251 ? C ARG 2   
49  1 Y 1 C SER 385 ? C SER 136 
50  1 Y 1 C ARG 386 ? C ARG 137 
51  1 Y 1 C ASP 387 ? C ASP 138 
52  1 Y 1 C GLU 388 ? C GLU 139 
53  1 Y 1 C GLU 389 ? C GLU 140 
54  1 Y 1 C GLN 390 ? C GLN 141 
55  1 Y 1 C PHE 391 ? C PHE 142 
56  1 Y 1 C LEU 392 ? C LEU 143 
57  1 Y 1 C SER 393 ? C SER 144 
58  1 Y 1 C PRO 394 ? C PRO 145 
59  1 Y 1 C ALA 395 ? C ALA 146 
60  1 Y 1 C PRO 396 ? C PRO 147 
61  1 Y 1 C ALA 397 ? C ALA 148 
62  1 Y 1 C THR 398 ? C THR 149 
63  1 Y 1 C PRO 399 ? C PRO 150 
64  1 Y 1 C ASN 400 ? C ASN 151 
65  1 Y 1 C PRO 401 ? C PRO 152 
66  1 Y 1 C PRO 402 ? C PRO 153 
67  1 Y 1 C PRO 403 ? C PRO 154 
68  1 Y 1 C ALA 404 ? C ALA 155 
69  1 Y 1 D GLU 250 ? D GLU 1   
70  1 Y 1 D ARG 251 ? D ARG 2   
71  1 Y 1 D SER 385 ? D SER 136 
72  1 Y 1 D ARG 386 ? D ARG 137 
73  1 Y 1 D ASP 387 ? D ASP 138 
74  1 Y 1 D GLU 388 ? D GLU 139 
75  1 Y 1 D GLU 389 ? D GLU 140 
76  1 Y 1 D GLN 390 ? D GLN 141 
77  1 Y 1 D PHE 391 ? D PHE 142 
78  1 Y 1 D LEU 392 ? D LEU 143 
79  1 Y 1 D SER 393 ? D SER 144 
80  1 Y 1 D PRO 394 ? D PRO 145 
81  1 Y 1 D ALA 395 ? D ALA 146 
82  1 Y 1 D PRO 396 ? D PRO 147 
83  1 Y 1 D ALA 397 ? D ALA 148 
84  1 Y 1 D THR 398 ? D THR 149 
85  1 Y 1 D PRO 399 ? D PRO 150 
86  1 Y 1 D ASN 400 ? D ASN 151 
87  1 Y 1 D PRO 401 ? D PRO 152 
88  1 Y 1 D PRO 402 ? D PRO 153 
89  1 Y 1 D PRO 403 ? D PRO 154 
90  1 Y 1 D ALA 404 ? D ALA 155 
91  1 Y 1 E GLU 250 ? E GLU 1   
92  1 Y 1 E ARG 251 ? E ARG 2   
93  1 Y 1 E SER 385 ? E SER 136 
94  1 Y 1 E ARG 386 ? E ARG 137 
95  1 Y 1 E ASP 387 ? E ASP 138 
96  1 Y 1 E GLU 388 ? E GLU 139 
97  1 Y 1 E GLU 389 ? E GLU 140 
98  1 Y 1 E GLN 390 ? E GLN 141 
99  1 Y 1 E PHE 391 ? E PHE 142 
100 1 Y 1 E LEU 392 ? E LEU 143 
101 1 Y 1 E SER 393 ? E SER 144 
102 1 Y 1 E PRO 394 ? E PRO 145 
103 1 Y 1 E ALA 395 ? E ALA 146 
104 1 Y 1 E PRO 396 ? E PRO 147 
105 1 Y 1 E ALA 397 ? E ALA 148 
106 1 Y 1 E THR 398 ? E THR 149 
107 1 Y 1 E PRO 399 ? E PRO 150 
108 1 Y 1 E ASN 400 ? E ASN 151 
109 1 Y 1 E PRO 401 ? E PRO 152 
110 1 Y 1 E PRO 402 ? E PRO 153 
111 1 Y 1 E PRO 403 ? E PRO 154 
112 1 Y 1 E ALA 404 ? E ALA 155 
113 1 Y 1 F GLU 250 ? F GLU 1   
114 1 Y 1 F ARG 251 ? F ARG 2   
115 1 Y 1 F LEU 252 ? F LEU 3   
116 1 Y 1 F SER 385 ? F SER 136 
117 1 Y 1 F ARG 386 ? F ARG 137 
118 1 Y 1 F ASP 387 ? F ASP 138 
119 1 Y 1 F GLU 388 ? F GLU 139 
120 1 Y 1 F GLU 389 ? F GLU 140 
121 1 Y 1 F GLN 390 ? F GLN 141 
122 1 Y 1 F PHE 391 ? F PHE 142 
123 1 Y 1 F LEU 392 ? F LEU 143 
124 1 Y 1 F SER 393 ? F SER 144 
125 1 Y 1 F PRO 394 ? F PRO 145 
126 1 Y 1 F ALA 395 ? F ALA 146 
127 1 Y 1 F PRO 396 ? F PRO 147 
128 1 Y 1 F ALA 397 ? F ALA 148 
129 1 Y 1 F THR 398 ? F THR 149 
130 1 Y 1 F PRO 399 ? F PRO 150 
131 1 Y 1 F ASN 400 ? F ASN 151 
132 1 Y 1 F PRO 401 ? F PRO 152 
133 1 Y 1 F PRO 402 ? F PRO 153 
134 1 Y 1 F PRO 403 ? F PRO 154 
135 1 Y 1 F ALA 404 ? F ALA 155 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CL  CL   CL N N 75  
CYS N    N  N N 76  
CYS CA   C  N R 77  
CYS C    C  N N 78  
CYS O    O  N N 79  
CYS CB   C  N N 80  
CYS SG   S  N N 81  
CYS OXT  O  N N 82  
CYS H    H  N N 83  
CYS H2   H  N N 84  
CYS HA   H  N N 85  
CYS HB2  H  N N 86  
CYS HB3  H  N N 87  
CYS HG   H  N N 88  
CYS HXT  H  N N 89  
EZ8 C4   C  N S 90  
EZ8 C5   C  N R 91  
EZ8 C6   C  N N 92  
EZ8 N2   N  Y N 93  
EZ8 C3   C  N R 94  
EZ8 CAP  C  Y N 95  
EZ8 CAL  C  Y N 96  
EZ8 CBM  C  Y N 97  
EZ8 CAV  C  N N 98  
EZ8 OAE  O  N N 99  
EZ8 CAM  C  Y N 100 
EZ8 CAQ  C  Y N 101 
EZ8 CBO  C  Y N 102 
EZ8 CAZ  C  N N 103 
EZ8 NBF  N  N N 104 
EZ8 CBK  C  N N 105 
EZ8 OAC  O  N N 106 
EZ8 CBW  C  N S 107 
EZ8 CBB  C  N N 108 
EZ8 CBV  C  N S 109 
EZ8 CBJ  C  N N 110 
EZ8 OAB  O  N N 111 
EZ8 NBE  N  N N 112 
EZ8 CAY  C  N N 113 
EZ8 CBN  C  Y N 114 
EZ8 CAN  C  Y N 115 
EZ8 CAJ  C  Y N 116 
EZ8 CBL  C  Y N 117 
EZ8 CAU  C  N N 118 
EZ8 OAD  O  N N 119 
EZ8 CAK  C  Y N 120 
EZ8 CAO  C  Y N 121 
EZ8 CBA  C  N N 122 
EZ8 CBT  C  N S 123 
EZ8 OBG  O  N N 124 
EZ8 CAX  C  N N 125 
EZ8 CAT  C  N N 126 
EZ8 CL1  CL N N 127 
EZ8 CBU  C  N S 128 
EZ8 O1   O  N N 129 
EZ8 C1   C  N S 130 
EZ8 O5   O  N N 131 
EZ8 O6   O  N N 132 
EZ8 O4   O  N N 133 
EZ8 O3   O  N N 134 
EZ8 C2   C  N S 135 
EZ8 CAR  C  Y N 136 
EZ8 NBD  N  Y N 137 
EZ8 NBC  N  Y N 138 
EZ8 CBP  C  Y N 139 
EZ8 CAS  C  N N 140 
EZ8 NAA  N  N N 141 
EZ8 H1   H  N N 142 
EZ8 H2   H  N N 143 
EZ8 H3   H  N N 144 
EZ8 H4   H  N N 145 
EZ8 H5   H  N N 146 
EZ8 H6   H  N N 147 
EZ8 H7   H  N N 148 
EZ8 H8   H  N N 149 
EZ8 H9   H  N N 150 
EZ8 H10  H  N N 151 
EZ8 H11  H  N N 152 
EZ8 H12  H  N N 153 
EZ8 H13  H  N N 154 
EZ8 H14  H  N N 155 
EZ8 H15  H  N N 156 
EZ8 H16  H  N N 157 
EZ8 H17  H  N N 158 
EZ8 H18  H  N N 159 
EZ8 H19  H  N N 160 
EZ8 H20  H  N N 161 
EZ8 H21  H  N N 162 
EZ8 H22  H  N N 163 
EZ8 H23  H  N N 164 
EZ8 H24  H  N N 165 
EZ8 H25  H  N N 166 
EZ8 H26  H  N N 167 
EZ8 H27  H  N N 168 
EZ8 H28  H  N N 169 
EZ8 H29  H  N N 170 
EZ8 H30  H  N N 171 
EZ8 H31  H  N N 172 
EZ8 H32  H  N N 173 
EZ8 H33  H  N N 174 
EZ8 H34  H  N N 175 
EZ8 H35  H  N N 176 
EZ8 H36  H  N N 177 
EZ8 H37  H  N N 178 
EZ8 H38  H  N N 179 
EZ8 H39  H  N N 180 
EZ8 H40  H  N N 181 
EZ8 H41  H  N N 182 
EZ8 H42  H  N N 183 
EZ8 H43  H  N N 184 
EZ8 H44  H  N N 185 
EZ8 H45  H  N N 186 
EZ8 H46  H  N N 187 
EZ8 H47  H  N N 188 
EZ8 H48  H  N N 189 
GLN N    N  N N 190 
GLN CA   C  N S 191 
GLN C    C  N N 192 
GLN O    O  N N 193 
GLN CB   C  N N 194 
GLN CG   C  N N 195 
GLN CD   C  N N 196 
GLN OE1  O  N N 197 
GLN NE2  N  N N 198 
GLN OXT  O  N N 199 
GLN H    H  N N 200 
GLN H2   H  N N 201 
GLN HA   H  N N 202 
GLN HB2  H  N N 203 
GLN HB3  H  N N 204 
GLN HG2  H  N N 205 
GLN HG3  H  N N 206 
GLN HE21 H  N N 207 
GLN HE22 H  N N 208 
GLN HXT  H  N N 209 
GLU N    N  N N 210 
GLU CA   C  N S 211 
GLU C    C  N N 212 
GLU O    O  N N 213 
GLU CB   C  N N 214 
GLU CG   C  N N 215 
GLU CD   C  N N 216 
GLU OE1  O  N N 217 
GLU OE2  O  N N 218 
GLU OXT  O  N N 219 
GLU H    H  N N 220 
GLU H2   H  N N 221 
GLU HA   H  N N 222 
GLU HB2  H  N N 223 
GLU HB3  H  N N 224 
GLU HG2  H  N N 225 
GLU HG3  H  N N 226 
GLU HE2  H  N N 227 
GLU HXT  H  N N 228 
GLY N    N  N N 229 
GLY CA   C  N N 230 
GLY C    C  N N 231 
GLY O    O  N N 232 
GLY OXT  O  N N 233 
GLY H    H  N N 234 
GLY H2   H  N N 235 
GLY HA2  H  N N 236 
GLY HA3  H  N N 237 
GLY HXT  H  N N 238 
HIS N    N  N N 239 
HIS CA   C  N S 240 
HIS C    C  N N 241 
HIS O    O  N N 242 
HIS CB   C  N N 243 
HIS CG   C  Y N 244 
HIS ND1  N  Y N 245 
HIS CD2  C  Y N 246 
HIS CE1  C  Y N 247 
HIS NE2  N  Y N 248 
HIS OXT  O  N N 249 
HIS H    H  N N 250 
HIS H2   H  N N 251 
HIS HA   H  N N 252 
HIS HB2  H  N N 253 
HIS HB3  H  N N 254 
HIS HD1  H  N N 255 
HIS HD2  H  N N 256 
HIS HE1  H  N N 257 
HIS HE2  H  N N 258 
HIS HXT  H  N N 259 
HOH O    O  N N 260 
HOH H1   H  N N 261 
HOH H2   H  N N 262 
ILE N    N  N N 263 
ILE CA   C  N S 264 
ILE C    C  N N 265 
ILE O    O  N N 266 
ILE CB   C  N S 267 
ILE CG1  C  N N 268 
ILE CG2  C  N N 269 
ILE CD1  C  N N 270 
ILE OXT  O  N N 271 
ILE H    H  N N 272 
ILE H2   H  N N 273 
ILE HA   H  N N 274 
ILE HB   H  N N 275 
ILE HG12 H  N N 276 
ILE HG13 H  N N 277 
ILE HG21 H  N N 278 
ILE HG22 H  N N 279 
ILE HG23 H  N N 280 
ILE HD11 H  N N 281 
ILE HD12 H  N N 282 
ILE HD13 H  N N 283 
ILE HXT  H  N N 284 
LEU N    N  N N 285 
LEU CA   C  N S 286 
LEU C    C  N N 287 
LEU O    O  N N 288 
LEU CB   C  N N 289 
LEU CG   C  N N 290 
LEU CD1  C  N N 291 
LEU CD2  C  N N 292 
LEU OXT  O  N N 293 
LEU H    H  N N 294 
LEU H2   H  N N 295 
LEU HA   H  N N 296 
LEU HB2  H  N N 297 
LEU HB3  H  N N 298 
LEU HG   H  N N 299 
LEU HD11 H  N N 300 
LEU HD12 H  N N 301 
LEU HD13 H  N N 302 
LEU HD21 H  N N 303 
LEU HD22 H  N N 304 
LEU HD23 H  N N 305 
LEU HXT  H  N N 306 
LYS N    N  N N 307 
LYS CA   C  N S 308 
LYS C    C  N N 309 
LYS O    O  N N 310 
LYS CB   C  N N 311 
LYS CG   C  N N 312 
LYS CD   C  N N 313 
LYS CE   C  N N 314 
LYS NZ   N  N N 315 
LYS OXT  O  N N 316 
LYS H    H  N N 317 
LYS H2   H  N N 318 
LYS HA   H  N N 319 
LYS HB2  H  N N 320 
LYS HB3  H  N N 321 
LYS HG2  H  N N 322 
LYS HG3  H  N N 323 
LYS HD2  H  N N 324 
LYS HD3  H  N N 325 
LYS HE2  H  N N 326 
LYS HE3  H  N N 327 
LYS HZ1  H  N N 328 
LYS HZ2  H  N N 329 
LYS HZ3  H  N N 330 
LYS HXT  H  N N 331 
MET N    N  N N 332 
MET CA   C  N S 333 
MET C    C  N N 334 
MET O    O  N N 335 
MET CB   C  N N 336 
MET CG   C  N N 337 
MET SD   S  N N 338 
MET CE   C  N N 339 
MET OXT  O  N N 340 
MET H    H  N N 341 
MET H2   H  N N 342 
MET HA   H  N N 343 
MET HB2  H  N N 344 
MET HB3  H  N N 345 
MET HG2  H  N N 346 
MET HG3  H  N N 347 
MET HE1  H  N N 348 
MET HE2  H  N N 349 
MET HE3  H  N N 350 
MET HXT  H  N N 351 
PHE N    N  N N 352 
PHE CA   C  N S 353 
PHE C    C  N N 354 
PHE O    O  N N 355 
PHE CB   C  N N 356 
PHE CG   C  Y N 357 
PHE CD1  C  Y N 358 
PHE CD2  C  Y N 359 
PHE CE1  C  Y N 360 
PHE CE2  C  Y N 361 
PHE CZ   C  Y N 362 
PHE OXT  O  N N 363 
PHE H    H  N N 364 
PHE H2   H  N N 365 
PHE HA   H  N N 366 
PHE HB2  H  N N 367 
PHE HB3  H  N N 368 
PHE HD1  H  N N 369 
PHE HD2  H  N N 370 
PHE HE1  H  N N 371 
PHE HE2  H  N N 372 
PHE HZ   H  N N 373 
PHE HXT  H  N N 374 
PRO N    N  N N 375 
PRO CA   C  N S 376 
PRO C    C  N N 377 
PRO O    O  N N 378 
PRO CB   C  N N 379 
PRO CG   C  N N 380 
PRO CD   C  N N 381 
PRO OXT  O  N N 382 
PRO H    H  N N 383 
PRO HA   H  N N 384 
PRO HB2  H  N N 385 
PRO HB3  H  N N 386 
PRO HG2  H  N N 387 
PRO HG3  H  N N 388 
PRO HD2  H  N N 389 
PRO HD3  H  N N 390 
PRO HXT  H  N N 391 
SER N    N  N N 392 
SER CA   C  N S 393 
SER C    C  N N 394 
SER O    O  N N 395 
SER CB   C  N N 396 
SER OG   O  N N 397 
SER OXT  O  N N 398 
SER H    H  N N 399 
SER H2   H  N N 400 
SER HA   H  N N 401 
SER HB2  H  N N 402 
SER HB3  H  N N 403 
SER HG   H  N N 404 
SER HXT  H  N N 405 
THR N    N  N N 406 
THR CA   C  N S 407 
THR C    C  N N 408 
THR O    O  N N 409 
THR CB   C  N R 410 
THR OG1  O  N N 411 
THR CG2  C  N N 412 
THR OXT  O  N N 413 
THR H    H  N N 414 
THR H2   H  N N 415 
THR HA   H  N N 416 
THR HB   H  N N 417 
THR HG1  H  N N 418 
THR HG21 H  N N 419 
THR HG22 H  N N 420 
THR HG23 H  N N 421 
THR HXT  H  N N 422 
TRP N    N  N N 423 
TRP CA   C  N S 424 
TRP C    C  N N 425 
TRP O    O  N N 426 
TRP CB   C  N N 427 
TRP CG   C  Y N 428 
TRP CD1  C  Y N 429 
TRP CD2  C  Y N 430 
TRP NE1  N  Y N 431 
TRP CE2  C  Y N 432 
TRP CE3  C  Y N 433 
TRP CZ2  C  Y N 434 
TRP CZ3  C  Y N 435 
TRP CH2  C  Y N 436 
TRP OXT  O  N N 437 
TRP H    H  N N 438 
TRP H2   H  N N 439 
TRP HA   H  N N 440 
TRP HB2  H  N N 441 
TRP HB3  H  N N 442 
TRP HD1  H  N N 443 
TRP HE1  H  N N 444 
TRP HE3  H  N N 445 
TRP HZ2  H  N N 446 
TRP HZ3  H  N N 447 
TRP HH2  H  N N 448 
TRP HXT  H  N N 449 
TYR N    N  N N 450 
TYR CA   C  N S 451 
TYR C    C  N N 452 
TYR O    O  N N 453 
TYR CB   C  N N 454 
TYR CG   C  Y N 455 
TYR CD1  C  Y N 456 
TYR CD2  C  Y N 457 
TYR CE1  C  Y N 458 
TYR CE2  C  Y N 459 
TYR CZ   C  Y N 460 
TYR OH   O  N N 461 
TYR OXT  O  N N 462 
TYR H    H  N N 463 
TYR H2   H  N N 464 
TYR HA   H  N N 465 
TYR HB2  H  N N 466 
TYR HB3  H  N N 467 
TYR HD1  H  N N 468 
TYR HD2  H  N N 469 
TYR HE1  H  N N 470 
TYR HE2  H  N N 471 
TYR HH   H  N N 472 
TYR HXT  H  N N 473 
VAL N    N  N N 474 
VAL CA   C  N S 475 
VAL C    C  N N 476 
VAL O    O  N N 477 
VAL CB   C  N N 478 
VAL CG1  C  N N 479 
VAL CG2  C  N N 480 
VAL OXT  O  N N 481 
VAL H    H  N N 482 
VAL H2   H  N N 483 
VAL HA   H  N N 484 
VAL HB   H  N N 485 
VAL HG11 H  N N 486 
VAL HG12 H  N N 487 
VAL HG13 H  N N 488 
VAL HG21 H  N N 489 
VAL HG22 H  N N 490 
VAL HG23 H  N N 491 
VAL HXT  H  N N 492 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EZ8 CAK CAO  doub Y N 83  
EZ8 CAK CBL  sing Y N 84  
EZ8 OAD CAU  sing N N 85  
EZ8 CAO CBN  sing Y N 86  
EZ8 CAU CBL  sing N N 87  
EZ8 CBL CAJ  doub Y N 88  
EZ8 CBN CAY  sing N N 89  
EZ8 CBN CAN  doub Y N 90  
EZ8 CAY NBE  sing N N 91  
EZ8 CAJ CAN  sing Y N 92  
EZ8 NBE CBJ  sing N N 93  
EZ8 CAZ CBO  sing N N 94  
EZ8 CAZ NBF  sing N N 95  
EZ8 CBJ OAB  doub N N 96  
EZ8 CBJ CBV  sing N N 97  
EZ8 CBO CAP  doub Y N 98  
EZ8 CBO CAQ  sing Y N 99  
EZ8 NBF CBK  sing N N 100 
EZ8 CAP CAL  sing Y N 101 
EZ8 CAQ CAM  doub Y N 102 
EZ8 OAC CBK  doub N N 103 
EZ8 CBK CBW  sing N N 104 
EZ8 CAL CBM  doub Y N 105 
EZ8 CBV CBW  sing N N 106 
EZ8 CBV CBA  sing N N 107 
EZ8 CAM CBM  sing Y N 108 
EZ8 CBM CAV  sing N N 109 
EZ8 OAE CAV  sing N N 110 
EZ8 CBW CBB  sing N N 111 
EZ8 CBA CBT  sing N N 112 
EZ8 OBG CBT  sing N N 113 
EZ8 OBG CAX  sing N N 114 
EZ8 CBB CBU  sing N N 115 
EZ8 CBT CBU  sing N N 116 
EZ8 CL1 CAT  sing N N 117 
EZ8 CBU O1   sing N N 118 
EZ8 CAT CAX  sing N N 119 
EZ8 O1  C1   sing N N 120 
EZ8 C1  C2   sing N N 121 
EZ8 C1  O5   sing N N 122 
EZ8 C2  C3   sing N N 123 
EZ8 C2  N2   sing N N 124 
EZ8 C3  O3   sing N N 125 
EZ8 C3  C4   sing N N 126 
EZ8 CAR N2   sing Y N 127 
EZ8 CAR CBP  doub Y N 128 
EZ8 O5  C5   sing N N 129 
EZ8 N2  NBD  sing Y N 130 
EZ8 C5  C4   sing N N 131 
EZ8 C5  C6   sing N N 132 
EZ8 C4  O4   sing N N 133 
EZ8 CBP CAS  sing N N 134 
EZ8 CBP NBC  sing Y N 135 
EZ8 CAS NAA  sing N N 136 
EZ8 O6  C6   sing N N 137 
EZ8 NBD NBC  doub Y N 138 
EZ8 C4  H1   sing N N 139 
EZ8 C5  H2   sing N N 140 
EZ8 C6  H3   sing N N 141 
EZ8 C6  H4   sing N N 142 
EZ8 C3  H5   sing N N 143 
EZ8 CAP H6   sing N N 144 
EZ8 CAL H7   sing N N 145 
EZ8 CAV H8   sing N N 146 
EZ8 CAV H9   sing N N 147 
EZ8 OAE H10  sing N N 148 
EZ8 CAM H11  sing N N 149 
EZ8 CAQ H12  sing N N 150 
EZ8 CAZ H13  sing N N 151 
EZ8 CAZ H14  sing N N 152 
EZ8 NBF H15  sing N N 153 
EZ8 CBW H16  sing N N 154 
EZ8 CBB H17  sing N N 155 
EZ8 CBB H18  sing N N 156 
EZ8 CBV H19  sing N N 157 
EZ8 NBE H20  sing N N 158 
EZ8 CAY H21  sing N N 159 
EZ8 CAY H22  sing N N 160 
EZ8 CAN H23  sing N N 161 
EZ8 CAJ H24  sing N N 162 
EZ8 CAU H25  sing N N 163 
EZ8 CAU H26  sing N N 164 
EZ8 OAD H27  sing N N 165 
EZ8 CAK H28  sing N N 166 
EZ8 CAO H29  sing N N 167 
EZ8 CBA H30  sing N N 168 
EZ8 CBA H31  sing N N 169 
EZ8 CBT H32  sing N N 170 
EZ8 CAX H33  sing N N 171 
EZ8 CAX H34  sing N N 172 
EZ8 CAT H35  sing N N 173 
EZ8 CAT H36  sing N N 174 
EZ8 CBU H37  sing N N 175 
EZ8 C1  H38  sing N N 176 
EZ8 O6  H39  sing N N 177 
EZ8 O4  H40  sing N N 178 
EZ8 O3  H41  sing N N 179 
EZ8 C2  H42  sing N N 180 
EZ8 CAR H43  sing N N 181 
EZ8 CAS H44  sing N N 182 
EZ8 CAS H45  sing N N 183 
EZ8 NAA H46  sing N N 184 
EZ8 NAA H47  sing N N 185 
EZ8 NAA H48  sing N N 186 
GLN N   CA   sing N N 187 
GLN N   H    sing N N 188 
GLN N   H2   sing N N 189 
GLN CA  C    sing N N 190 
GLN CA  CB   sing N N 191 
GLN CA  HA   sing N N 192 
GLN C   O    doub N N 193 
GLN C   OXT  sing N N 194 
GLN CB  CG   sing N N 195 
GLN CB  HB2  sing N N 196 
GLN CB  HB3  sing N N 197 
GLN CG  CD   sing N N 198 
GLN CG  HG2  sing N N 199 
GLN CG  HG3  sing N N 200 
GLN CD  OE1  doub N N 201 
GLN CD  NE2  sing N N 202 
GLN NE2 HE21 sing N N 203 
GLN NE2 HE22 sing N N 204 
GLN OXT HXT  sing N N 205 
GLU N   CA   sing N N 206 
GLU N   H    sing N N 207 
GLU N   H2   sing N N 208 
GLU CA  C    sing N N 209 
GLU CA  CB   sing N N 210 
GLU CA  HA   sing N N 211 
GLU C   O    doub N N 212 
GLU C   OXT  sing N N 213 
GLU CB  CG   sing N N 214 
GLU CB  HB2  sing N N 215 
GLU CB  HB3  sing N N 216 
GLU CG  CD   sing N N 217 
GLU CG  HG2  sing N N 218 
GLU CG  HG3  sing N N 219 
GLU CD  OE1  doub N N 220 
GLU CD  OE2  sing N N 221 
GLU OE2 HE2  sing N N 222 
GLU OXT HXT  sing N N 223 
GLY N   CA   sing N N 224 
GLY N   H    sing N N 225 
GLY N   H2   sing N N 226 
GLY CA  C    sing N N 227 
GLY CA  HA2  sing N N 228 
GLY CA  HA3  sing N N 229 
GLY C   O    doub N N 230 
GLY C   OXT  sing N N 231 
GLY OXT HXT  sing N N 232 
HIS N   CA   sing N N 233 
HIS N   H    sing N N 234 
HIS N   H2   sing N N 235 
HIS CA  C    sing N N 236 
HIS CA  CB   sing N N 237 
HIS CA  HA   sing N N 238 
HIS C   O    doub N N 239 
HIS C   OXT  sing N N 240 
HIS CB  CG   sing N N 241 
HIS CB  HB2  sing N N 242 
HIS CB  HB3  sing N N 243 
HIS CG  ND1  sing Y N 244 
HIS CG  CD2  doub Y N 245 
HIS ND1 CE1  doub Y N 246 
HIS ND1 HD1  sing N N 247 
HIS CD2 NE2  sing Y N 248 
HIS CD2 HD2  sing N N 249 
HIS CE1 NE2  sing Y N 250 
HIS CE1 HE1  sing N N 251 
HIS NE2 HE2  sing N N 252 
HIS OXT HXT  sing N N 253 
HOH O   H1   sing N N 254 
HOH O   H2   sing N N 255 
ILE N   CA   sing N N 256 
ILE N   H    sing N N 257 
ILE N   H2   sing N N 258 
ILE CA  C    sing N N 259 
ILE CA  CB   sing N N 260 
ILE CA  HA   sing N N 261 
ILE C   O    doub N N 262 
ILE C   OXT  sing N N 263 
ILE CB  CG1  sing N N 264 
ILE CB  CG2  sing N N 265 
ILE CB  HB   sing N N 266 
ILE CG1 CD1  sing N N 267 
ILE CG1 HG12 sing N N 268 
ILE CG1 HG13 sing N N 269 
ILE CG2 HG21 sing N N 270 
ILE CG2 HG22 sing N N 271 
ILE CG2 HG23 sing N N 272 
ILE CD1 HD11 sing N N 273 
ILE CD1 HD12 sing N N 274 
ILE CD1 HD13 sing N N 275 
ILE OXT HXT  sing N N 276 
LEU N   CA   sing N N 277 
LEU N   H    sing N N 278 
LEU N   H2   sing N N 279 
LEU CA  C    sing N N 280 
LEU CA  CB   sing N N 281 
LEU CA  HA   sing N N 282 
LEU C   O    doub N N 283 
LEU C   OXT  sing N N 284 
LEU CB  CG   sing N N 285 
LEU CB  HB2  sing N N 286 
LEU CB  HB3  sing N N 287 
LEU CG  CD1  sing N N 288 
LEU CG  CD2  sing N N 289 
LEU CG  HG   sing N N 290 
LEU CD1 HD11 sing N N 291 
LEU CD1 HD12 sing N N 292 
LEU CD1 HD13 sing N N 293 
LEU CD2 HD21 sing N N 294 
LEU CD2 HD22 sing N N 295 
LEU CD2 HD23 sing N N 296 
LEU OXT HXT  sing N N 297 
LYS N   CA   sing N N 298 
LYS N   H    sing N N 299 
LYS N   H2   sing N N 300 
LYS CA  C    sing N N 301 
LYS CA  CB   sing N N 302 
LYS CA  HA   sing N N 303 
LYS C   O    doub N N 304 
LYS C   OXT  sing N N 305 
LYS CB  CG   sing N N 306 
LYS CB  HB2  sing N N 307 
LYS CB  HB3  sing N N 308 
LYS CG  CD   sing N N 309 
LYS CG  HG2  sing N N 310 
LYS CG  HG3  sing N N 311 
LYS CD  CE   sing N N 312 
LYS CD  HD2  sing N N 313 
LYS CD  HD3  sing N N 314 
LYS CE  NZ   sing N N 315 
LYS CE  HE2  sing N N 316 
LYS CE  HE3  sing N N 317 
LYS NZ  HZ1  sing N N 318 
LYS NZ  HZ2  sing N N 319 
LYS NZ  HZ3  sing N N 320 
LYS OXT HXT  sing N N 321 
MET N   CA   sing N N 322 
MET N   H    sing N N 323 
MET N   H2   sing N N 324 
MET CA  C    sing N N 325 
MET CA  CB   sing N N 326 
MET CA  HA   sing N N 327 
MET C   O    doub N N 328 
MET C   OXT  sing N N 329 
MET CB  CG   sing N N 330 
MET CB  HB2  sing N N 331 
MET CB  HB3  sing N N 332 
MET CG  SD   sing N N 333 
MET CG  HG2  sing N N 334 
MET CG  HG3  sing N N 335 
MET SD  CE   sing N N 336 
MET CE  HE1  sing N N 337 
MET CE  HE2  sing N N 338 
MET CE  HE3  sing N N 339 
MET OXT HXT  sing N N 340 
PHE N   CA   sing N N 341 
PHE N   H    sing N N 342 
PHE N   H2   sing N N 343 
PHE CA  C    sing N N 344 
PHE CA  CB   sing N N 345 
PHE CA  HA   sing N N 346 
PHE C   O    doub N N 347 
PHE C   OXT  sing N N 348 
PHE CB  CG   sing N N 349 
PHE CB  HB2  sing N N 350 
PHE CB  HB3  sing N N 351 
PHE CG  CD1  doub Y N 352 
PHE CG  CD2  sing Y N 353 
PHE CD1 CE1  sing Y N 354 
PHE CD1 HD1  sing N N 355 
PHE CD2 CE2  doub Y N 356 
PHE CD2 HD2  sing N N 357 
PHE CE1 CZ   doub Y N 358 
PHE CE1 HE1  sing N N 359 
PHE CE2 CZ   sing Y N 360 
PHE CE2 HE2  sing N N 361 
PHE CZ  HZ   sing N N 362 
PHE OXT HXT  sing N N 363 
PRO N   CA   sing N N 364 
PRO N   CD   sing N N 365 
PRO N   H    sing N N 366 
PRO CA  C    sing N N 367 
PRO CA  CB   sing N N 368 
PRO CA  HA   sing N N 369 
PRO C   O    doub N N 370 
PRO C   OXT  sing N N 371 
PRO CB  CG   sing N N 372 
PRO CB  HB2  sing N N 373 
PRO CB  HB3  sing N N 374 
PRO CG  CD   sing N N 375 
PRO CG  HG2  sing N N 376 
PRO CG  HG3  sing N N 377 
PRO CD  HD2  sing N N 378 
PRO CD  HD3  sing N N 379 
PRO OXT HXT  sing N N 380 
SER N   CA   sing N N 381 
SER N   H    sing N N 382 
SER N   H2   sing N N 383 
SER CA  C    sing N N 384 
SER CA  CB   sing N N 385 
SER CA  HA   sing N N 386 
SER C   O    doub N N 387 
SER C   OXT  sing N N 388 
SER CB  OG   sing N N 389 
SER CB  HB2  sing N N 390 
SER CB  HB3  sing N N 391 
SER OG  HG   sing N N 392 
SER OXT HXT  sing N N 393 
THR N   CA   sing N N 394 
THR N   H    sing N N 395 
THR N   H2   sing N N 396 
THR CA  C    sing N N 397 
THR CA  CB   sing N N 398 
THR CA  HA   sing N N 399 
THR C   O    doub N N 400 
THR C   OXT  sing N N 401 
THR CB  OG1  sing N N 402 
THR CB  CG2  sing N N 403 
THR CB  HB   sing N N 404 
THR OG1 HG1  sing N N 405 
THR CG2 HG21 sing N N 406 
THR CG2 HG22 sing N N 407 
THR CG2 HG23 sing N N 408 
THR OXT HXT  sing N N 409 
TRP N   CA   sing N N 410 
TRP N   H    sing N N 411 
TRP N   H2   sing N N 412 
TRP CA  C    sing N N 413 
TRP CA  CB   sing N N 414 
TRP CA  HA   sing N N 415 
TRP C   O    doub N N 416 
TRP C   OXT  sing N N 417 
TRP CB  CG   sing N N 418 
TRP CB  HB2  sing N N 419 
TRP CB  HB3  sing N N 420 
TRP CG  CD1  doub Y N 421 
TRP CG  CD2  sing Y N 422 
TRP CD1 NE1  sing Y N 423 
TRP CD1 HD1  sing N N 424 
TRP CD2 CE2  doub Y N 425 
TRP CD2 CE3  sing Y N 426 
TRP NE1 CE2  sing Y N 427 
TRP NE1 HE1  sing N N 428 
TRP CE2 CZ2  sing Y N 429 
TRP CE3 CZ3  doub Y N 430 
TRP CE3 HE3  sing N N 431 
TRP CZ2 CH2  doub Y N 432 
TRP CZ2 HZ2  sing N N 433 
TRP CZ3 CH2  sing Y N 434 
TRP CZ3 HZ3  sing N N 435 
TRP CH2 HH2  sing N N 436 
TRP OXT HXT  sing N N 437 
TYR N   CA   sing N N 438 
TYR N   H    sing N N 439 
TYR N   H2   sing N N 440 
TYR CA  C    sing N N 441 
TYR CA  CB   sing N N 442 
TYR CA  HA   sing N N 443 
TYR C   O    doub N N 444 
TYR C   OXT  sing N N 445 
TYR CB  CG   sing N N 446 
TYR CB  HB2  sing N N 447 
TYR CB  HB3  sing N N 448 
TYR CG  CD1  doub Y N 449 
TYR CG  CD2  sing Y N 450 
TYR CD1 CE1  sing Y N 451 
TYR CD1 HD1  sing N N 452 
TYR CD2 CE2  doub Y N 453 
TYR CD2 HD2  sing N N 454 
TYR CE1 CZ   doub Y N 455 
TYR CE1 HE1  sing N N 456 
TYR CE2 CZ   sing Y N 457 
TYR CE2 HE2  sing N N 458 
TYR CZ  OH   sing N N 459 
TYR OH  HH   sing N N 460 
TYR OXT HXT  sing N N 461 
VAL N   CA   sing N N 462 
VAL N   H    sing N N 463 
VAL N   H2   sing N N 464 
VAL CA  C    sing N N 465 
VAL CA  CB   sing N N 466 
VAL CA  HA   sing N N 467 
VAL C   O    doub N N 468 
VAL C   OXT  sing N N 469 
VAL CB  CG1  sing N N 470 
VAL CB  CG2  sing N N 471 
VAL CB  HB   sing N N 472 
VAL CG1 HG11 sing N N 473 
VAL CG1 HG12 sing N N 474 
VAL CG1 HG13 sing N N 475 
VAL CG2 HG21 sing N N 476 
VAL CG2 HG22 sing N N 477 
VAL CG2 HG23 sing N N 478 
VAL OXT HXT  sing N N 479 
# 
_pdbx_audit_support.funding_organization   'European Commission' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           'ITN 642870' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1K9I 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6GHV 
_atom_sites.fract_transf_matrix[1][1]   0.009469 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005177 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017389 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.010627 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . CYS A  1 4   ? -28.471 1.709   33.406  1.00 83.64  ? 253  CYS A N   1 
ATOM   2    C  CA  . CYS A  1 4   ? -27.226 2.492   33.116  1.00 86.10  ? 253  CYS A CA  1 
ATOM   3    C  C   . CYS A  1 4   ? -25.968 1.659   33.376  1.00 74.44  ? 253  CYS A C   1 
ATOM   4    O  O   . CYS A  1 4   ? -25.479 1.575   34.513  1.00 68.79  ? 253  CYS A O   1 
ATOM   5    C  CB  . CYS A  1 4   ? -27.147 3.790   33.945  1.00 91.58  ? 253  CYS A CB  1 
ATOM   6    S  SG  . CYS A  1 4   ? -25.738 4.864   33.497  1.00 96.83  ? 253  CYS A SG  1 
ATOM   7    N  N   . HIS A  1 5   ? -25.454 1.063   32.306  1.00 59.58  ? 254  HIS A N   1 
ATOM   8    C  CA  . HIS A  1 5   ? -24.186 0.358   32.335  1.00 48.45  ? 254  HIS A CA  1 
ATOM   9    C  C   . HIS A  1 5   ? -23.056 1.302   31.911  1.00 40.66  ? 254  HIS A C   1 
ATOM   10   O  O   . HIS A  1 5   ? -23.182 1.988   30.931  1.00 40.06  ? 254  HIS A O   1 
ATOM   11   C  CB  . HIS A  1 5   ? -24.274 -0.825  31.390  1.00 45.73  ? 254  HIS A CB  1 
ATOM   12   C  CG  . HIS A  1 5   ? -25.386 -1.773  31.710  1.00 43.38  ? 254  HIS A CG  1 
ATOM   13   N  ND1 . HIS A  1 5   ? -25.329 -2.659  32.767  1.00 43.45  ? 254  HIS A ND1 1 
ATOM   14   C  CD2 . HIS A  1 5   ? -26.564 -2.003  31.088  1.00 42.88  ? 254  HIS A CD2 1 
ATOM   15   C  CE1 . HIS A  1 5   ? -26.435 -3.380  32.789  1.00 45.53  ? 254  HIS A CE1 1 
ATOM   16   N  NE2 . HIS A  1 5   ? -27.192 -3.015  31.769  1.00 45.27  ? 254  HIS A NE2 1 
ATOM   17   N  N   . PRO A  1 6   ? -21.953 1.356   32.658  1.00 39.91  ? 255  PRO A N   1 
ATOM   18   C  CA  . PRO A  1 6   ? -20.904 2.290   32.224  1.00 39.31  ? 255  PRO A CA  1 
ATOM   19   C  C   . PRO A  1 6   ? -20.341 1.971   30.813  1.00 39.47  ? 255  PRO A C   1 
ATOM   20   O  O   . PRO A  1 6   ? -19.856 2.850   30.130  1.00 39.36  ? 255  PRO A O   1 
ATOM   21   C  CB  . PRO A  1 6   ? -19.813 2.111   33.294  1.00 41.76  ? 255  PRO A CB  1 
ATOM   22   C  CG  . PRO A  1 6   ? -20.523 1.591   34.509  1.00 42.79  ? 255  PRO A CG  1 
ATOM   23   C  CD  . PRO A  1 6   ? -21.689 0.792   34.000  1.00 41.73  ? 255  PRO A CD  1 
ATOM   24   N  N   . CYS A  1 7   ? -20.407 0.720   30.395  1.00 34.96  ? 256  CYS A N   1 
ATOM   25   C  CA  . CYS A  1 7   ? -19.863 0.330   29.128  1.00 35.47  ? 256  CYS A CA  1 
ATOM   26   C  C   . CYS A  1 7   ? -20.828 -0.552  28.398  1.00 38.01  ? 256  CYS A C   1 
ATOM   27   O  O   . CYS A  1 7   ? -21.737 -1.145  29.010  1.00 38.18  ? 256  CYS A O   1 
ATOM   28   C  CB  . CYS A  1 7   ? -18.596 -0.477  29.327  1.00 34.75  ? 256  CYS A CB  1 
ATOM   29   S  SG  . CYS A  1 7   ? -17.256 0.452   30.020  1.00 36.97  ? 256  CYS A SG  1 
ATOM   30   N  N   . PRO A  1 8   ? -20.622 -0.669  27.080  1.00 35.78  ? 257  PRO A N   1 
ATOM   31   C  CA  . PRO A  1 8   ? -21.353 -1.650  26.295  1.00 33.86  ? 257  PRO A CA  1 
ATOM   32   C  C   . PRO A  1 8   ? -21.035 -3.060  26.744  1.00 31.78  ? 257  PRO A C   1 
ATOM   33   O  O   . PRO A  1 8   ? -19.961 -3.324  27.233  1.00 31.47  ? 257  PRO A O   1 
ATOM   34   C  CB  . PRO A  1 8   ? -20.870 -1.428  24.844  1.00 36.01  ? 257  PRO A CB  1 
ATOM   35   C  CG  . PRO A  1 8   ? -20.150 -0.095  24.855  1.00 39.44  ? 257  PRO A CG  1 
ATOM   36   C  CD  . PRO A  1 8   ? -19.729 0.187   26.275  1.00 37.44  ? 257  PRO A CD  1 
ATOM   37   N  N   . TRP A  1 9   ? -22.008 -3.936  26.590  1.00 31.63  ? 258  TRP A N   1 
ATOM   38   C  CA  . TRP A  1 9   ? -21.910 -5.332  26.931  1.00 35.24  ? 258  TRP A CA  1 
ATOM   39   C  C   . TRP A  1 9   ? -20.646 -5.995  26.361  1.00 36.61  ? 258  TRP A C   1 
ATOM   40   O  O   . TRP A  1 9   ? -20.355 -5.926  25.159  1.00 41.16  ? 258  TRP A O   1 
ATOM   41   C  CB  . TRP A  1 9   ? -23.165 -6.058  26.386  1.00 37.62  ? 258  TRP A CB  1 
ATOM   42   C  CG  . TRP A  1 9   ? -23.576 -7.333  27.115  1.00 38.69  ? 258  TRP A CG  1 
ATOM   43   C  CD1 . TRP A  1 9   ? -22.757 -8.285  27.659  1.00 40.83  ? 258  TRP A CD1 1 
ATOM   44   C  CD2 . TRP A  1 9   ? -24.914 -7.776  27.349  1.00 38.53  ? 258  TRP A CD2 1 
ATOM   45   N  NE1 . TRP A  1 9   ? -23.504 -9.288  28.221  1.00 39.24  ? 258  TRP A NE1 1 
ATOM   46   C  CE2 . TRP A  1 9   ? -24.832 -8.999  28.050  1.00 38.29  ? 258  TRP A CE2 1 
ATOM   47   C  CE3 . TRP A  1 9   ? -26.175 -7.248  27.046  1.00 37.58  ? 258  TRP A CE3 1 
ATOM   48   C  CZ2 . TRP A  1 9   ? -25.963 -9.716  28.445  1.00 40.57  ? 258  TRP A CZ2 1 
ATOM   49   C  CZ3 . TRP A  1 9   ? -27.301 -7.958  27.436  1.00 42.28  ? 258  TRP A CZ3 1 
ATOM   50   C  CH2 . TRP A  1 9   ? -27.188 -9.192  28.123  1.00 42.19  ? 258  TRP A CH2 1 
ATOM   51   N  N   . GLU A  1 10  ? -19.902 -6.643  27.244  1.00 36.63  ? 259  GLU A N   1 
ATOM   52   C  CA  . GLU A  1 10  ? -18.721 -7.410  26.888  1.00 38.66  ? 259  GLU A CA  1 
ATOM   53   C  C   . GLU A  1 10  ? -17.479 -6.573  26.871  1.00 37.90  ? 259  GLU A C   1 
ATOM   54   O  O   . GLU A  1 10  ? -16.417 -7.121  26.724  1.00 39.66  ? 259  GLU A O   1 
ATOM   55   C  CB  . GLU A  1 10  ? -18.860 -8.080  25.511  1.00 40.79  ? 259  GLU A CB  1 
ATOM   56   C  CG  . GLU A  1 10  ? -20.057 -9.003  25.399  1.00 41.75  ? 259  GLU A CG  1 
ATOM   57   C  CD  . GLU A  1 10  ? -19.844 -10.095 24.386  1.00 43.29  ? 259  GLU A CD  1 
ATOM   58   O  OE1 . GLU A  1 10  ? -18.685 -10.516 24.208  1.00 43.21  ? 259  GLU A OE1 1 
ATOM   59   O  OE2 . GLU A  1 10  ? -20.844 -10.551 23.794  1.00 47.40  ? 259  GLU A OE2 1 
ATOM   60   N  N   . TRP A  1 11  ? -17.615 -5.255  26.985  1.00 35.20  ? 260  TRP A N   1 
ATOM   61   C  CA  . TRP A  1 11  ? -16.477 -4.359  27.139  1.00 34.25  ? 260  TRP A CA  1 
ATOM   62   C  C   . TRP A  1 11  ? -16.080 -4.306  28.594  1.00 35.54  ? 260  TRP A C   1 
ATOM   63   O  O   . TRP A  1 11  ? -16.897 -4.528  29.485  1.00 36.75  ? 260  TRP A O   1 
ATOM   64   C  CB  . TRP A  1 11  ? -16.828 -2.951  26.679  1.00 33.97  ? 260  TRP A CB  1 
ATOM   65   C  CG  . TRP A  1 11  ? -17.094 -2.814  25.213  1.00 36.45  ? 260  TRP A CG  1 
ATOM   66   C  CD1 . TRP A  1 11  ? -17.970 -3.548  24.459  1.00 34.99  ? 260  TRP A CD1 1 
ATOM   67   C  CD2 . TRP A  1 11  ? -16.522 -1.838  24.325  1.00 33.32  ? 260  TRP A CD2 1 
ATOM   68   N  NE1 . TRP A  1 11  ? -17.946 -3.111  23.176  1.00 33.55  ? 260  TRP A NE1 1 
ATOM   69   C  CE2 . TRP A  1 11  ? -17.096 -2.043  23.064  1.00 33.65  ? 260  TRP A CE2 1 
ATOM   70   C  CE3 . TRP A  1 11  ? -15.599 -0.812  24.485  1.00 33.59  ? 260  TRP A CE3 1 
ATOM   71   C  CZ2 . TRP A  1 11  ? -16.753 -1.278  21.940  1.00 32.92  ? 260  TRP A CZ2 1 
ATOM   72   C  CZ3 . TRP A  1 11  ? -15.259 -0.048  23.369  1.00 36.22  ? 260  TRP A CZ3 1 
ATOM   73   C  CH2 . TRP A  1 11  ? -15.845 -0.286  22.117  1.00 33.27  ? 260  TRP A CH2 1 
ATOM   74   N  N   . THR A  1 12  ? -14.817 -3.985  28.816  1.00 34.49  ? 261  THR A N   1 
ATOM   75   C  CA  . THR A  1 12  ? -14.199 -3.960  30.127  1.00 33.38  ? 261  THR A CA  1 
ATOM   76   C  C   . THR A  1 12  ? -14.097 -2.510  30.558  1.00 29.85  ? 261  THR A C   1 
ATOM   77   O  O   . THR A  1 12  ? -13.548 -1.685  29.827  1.00 25.44  ? 261  THR A O   1 
ATOM   78   C  CB  . THR A  1 12  ? -12.780 -4.554  30.079  1.00 36.92  ? 261  THR A CB  1 
ATOM   79   O  OG1 . THR A  1 12  ? -12.846 -5.927  29.650  1.00 38.64  ? 261  THR A OG1 1 
ATOM   80   C  CG2 . THR A  1 12  ? -12.098 -4.480  31.463  1.00 38.39  ? 261  THR A CG2 1 
ATOM   81   N  N   . PHE A  1 13  ? -14.667 -2.210  31.718  1.00 28.86  ? 262  PHE A N   1 
ATOM   82   C  CA  . PHE A  1 13  ? -14.498 -0.917  32.373  1.00 31.29  ? 262  PHE A CA  1 
ATOM   83   C  C   . PHE A  1 13  ? -13.116 -0.842  33.037  1.00 30.45  ? 262  PHE A C   1 
ATOM   84   O  O   . PHE A  1 13  ? -12.701 -1.762  33.747  1.00 30.33  ? 262  PHE A O   1 
ATOM   85   C  CB  . PHE A  1 13  ? -15.581 -0.741  33.443  1.00 31.68  ? 262  PHE A CB  1 
ATOM   86   C  CG  . PHE A  1 13  ? -15.531 0.586   34.141  1.00 30.63  ? 262  PHE A CG  1 
ATOM   87   C  CD1 . PHE A  1 13  ? -16.221 1.663   33.635  1.00 33.90  ? 262  PHE A CD1 1 
ATOM   88   C  CD2 . PHE A  1 13  ? -14.754 0.766   35.268  1.00 32.98  ? 262  PHE A CD2 1 
ATOM   89   C  CE1 . PHE A  1 13  ? -16.174 2.892   34.262  1.00 32.64  ? 262  PHE A CE1 1 
ATOM   90   C  CE2 . PHE A  1 13  ? -14.704 1.990   35.916  1.00 33.80  ? 262  PHE A CE2 1 
ATOM   91   C  CZ  . PHE A  1 13  ? -15.401 3.060   35.396  1.00 33.67  ? 262  PHE A CZ  1 
ATOM   92   N  N   . PHE A  1 14  ? -12.396 0.246   32.812  1.00 30.86  ? 263  PHE A N   1 
ATOM   93   C  CA  . PHE A  1 14  ? -11.190 0.514   33.589  1.00 29.87  ? 263  PHE A CA  1 
ATOM   94   C  C   . PHE A  1 14  ? -11.015 2.028   33.659  1.00 33.56  ? 263  PHE A C   1 
ATOM   95   O  O   . PHE A  1 14  ? -10.889 2.702   32.605  1.00 27.81  ? 263  PHE A O   1 
ATOM   96   C  CB  . PHE A  1 14  ? -9.996  -0.168  32.965  1.00 30.39  ? 263  PHE A CB  1 
ATOM   97   C  CG  . PHE A  1 14  ? -8.680  0.175   33.606  1.00 31.37  ? 263  PHE A CG  1 
ATOM   98   C  CD1 . PHE A  1 14  ? -7.953  1.284   33.162  1.00 29.61  ? 263  PHE A CD1 1 
ATOM   99   C  CD2 . PHE A  1 14  ? -8.153  -0.616  34.623  1.00 31.13  ? 263  PHE A CD2 1 
ATOM   100  C  CE1 . PHE A  1 14  ? -6.748  1.614   33.731  1.00 30.34  ? 263  PHE A CE1 1 
ATOM   101  C  CE2 . PHE A  1 14  ? -6.932  -0.295  35.193  1.00 35.35  ? 263  PHE A CE2 1 
ATOM   102  C  CZ  . PHE A  1 14  ? -6.225  0.826   34.739  1.00 33.34  ? 263  PHE A CZ  1 
ATOM   103  N  N   . GLN A  1 15  ? -11.074 2.535   34.902  1.00 32.46  ? 264  GLN A N   1 
ATOM   104  C  CA  . GLN A  1 15  ? -10.778 3.935   35.256  1.00 31.17  ? 264  GLN A CA  1 
ATOM   105  C  C   . GLN A  1 15  ? -11.456 4.942   34.365  1.00 30.93  ? 264  GLN A C   1 
ATOM   106  O  O   . GLN A  1 15  ? -10.803 5.850   33.822  1.00 27.83  ? 264  GLN A O   1 
ATOM   107  C  CB  . GLN A  1 15  ? -9.263  4.211   35.305  1.00 30.45  ? 264  GLN A CB  1 
ATOM   108  C  CG  . GLN A  1 15  ? -8.520  3.260   36.232  1.00 34.54  ? 264  GLN A CG  1 
ATOM   109  C  CD  . GLN A  1 15  ? -7.195  3.812   36.718  1.00 35.07  ? 264  GLN A CD  1 
ATOM   110  O  OE1 . GLN A  1 15  ? -6.587  4.604   36.042  1.00 41.66  ? 264  GLN A OE1 1 
ATOM   111  N  NE2 . GLN A  1 15  ? -6.762  3.406   37.881  1.00 36.12  ? 264  GLN A NE2 1 
ATOM   112  N  N   . GLY A  1 16  ? -12.765 4.770   34.204  1.00 29.97  ? 265  GLY A N   1 
ATOM   113  C  CA  . GLY A  1 16  ? -13.581 5.753   33.494  1.00 31.41  ? 265  GLY A CA  1 
ATOM   114  C  C   . GLY A  1 16  ? -13.610 5.575   32.005  1.00 33.21  ? 265  GLY A C   1 
ATOM   115  O  O   . GLY A  1 16  ? -14.210 6.378   31.307  1.00 33.70  ? 265  GLY A O   1 
ATOM   116  N  N   . ASN A  1 17  ? -12.973 4.519   31.492  1.00 32.08  ? 266  ASN A N   1 
ATOM   117  C  CA  . ASN A  1 17  ? -13.110 4.190   30.066  1.00 32.26  ? 266  ASN A CA  1 
ATOM   118  C  C   . ASN A  1 17  ? -13.496 2.721   29.873  1.00 31.88  ? 266  ASN A C   1 
ATOM   119  O  O   . ASN A  1 17  ? -13.340 1.899   30.773  1.00 33.54  ? 266  ASN A O   1 
ATOM   120  C  CB  . ASN A  1 17  ? -11.837 4.536   29.309  1.00 30.50  ? 266  ASN A CB  1 
ATOM   121  C  CG  . ASN A  1 17  ? -11.510 6.023   29.362  1.00 29.62  ? 266  ASN A CG  1 
ATOM   122  O  OD1 . ASN A  1 17  ? -12.194 6.834   28.777  1.00 32.80  ? 266  ASN A OD1 1 
ATOM   123  N  ND2 . ASN A  1 17  ? -10.426 6.354   29.982  1.00 29.45  ? 266  ASN A ND2 1 
ATOM   124  N  N   . CYS A  1 18  ? -13.996 2.442   28.682  1.00 30.80  ? 267  CYS A N   1 
ATOM   125  C  CA  . CYS A  1 18  ? -14.450 1.154   28.240  1.00 29.40  ? 267  CYS A CA  1 
ATOM   126  C  C   . CYS A  1 18  ? -13.470 0.661   27.186  1.00 32.34  ? 267  CYS A C   1 
ATOM   127  O  O   . CYS A  1 18  ? -13.050 1.444   26.293  1.00 32.58  ? 267  CYS A O   1 
ATOM   128  C  CB  . CYS A  1 18  ? -15.809 1.324   27.585  1.00 32.35  ? 267  CYS A CB  1 
ATOM   129  S  SG  . CYS A  1 18  ? -17.015 2.038   28.717  1.00 38.22  ? 267  CYS A SG  1 
ATOM   130  N  N   . TYR A  1 19  ? -13.123 -0.621  27.275  1.00 29.03  ? 268  TYR A N   1 
ATOM   131  C  CA  . TYR A  1 19  ? -12.189 -1.242  26.358  1.00 30.43  ? 268  TYR A CA  1 
ATOM   132  C  C   . TYR A  1 19  ? -12.762 -2.475  25.758  1.00 31.34  ? 268  TYR A C   1 
ATOM   133  O  O   . TYR A  1 19  ? -13.357 -3.304  26.447  1.00 29.76  ? 268  TYR A O   1 
ATOM   134  C  CB  . TYR A  1 19  ? -10.913 -1.645  27.084  1.00 28.98  ? 268  TYR A CB  1 
ATOM   135  C  CG  . TYR A  1 19  ? -10.208 -0.456  27.653  1.00 28.35  ? 268  TYR A CG  1 
ATOM   136  C  CD1 . TYR A  1 19  ? -10.635 0.107   28.864  1.00 28.27  ? 268  TYR A CD1 1 
ATOM   137  C  CD2 . TYR A  1 19  ? -9.185  0.161   26.965  1.00 25.78  ? 268  TYR A CD2 1 
ATOM   138  C  CE1 . TYR A  1 19  ? -10.012 1.209   29.401  1.00 27.13  ? 268  TYR A CE1 1 
ATOM   139  C  CE2 . TYR A  1 19  ? -8.536  1.279   27.492  1.00 26.57  ? 268  TYR A CE2 1 
ATOM   140  C  CZ  . TYR A  1 19  ? -8.960  1.810   28.711  1.00 29.06  ? 268  TYR A CZ  1 
ATOM   141  O  OH  . TYR A  1 19  ? -8.340  2.925   29.274  1.00 27.40  ? 268  TYR A OH  1 
ATOM   142  N  N   . PHE A  1 20  ? -12.560 -2.619  24.460  1.00 30.36  ? 269  PHE A N   1 
ATOM   143  C  CA  . PHE A  1 20  ? -12.896 -3.842  23.789  1.00 30.34  ? 269  PHE A CA  1 
ATOM   144  C  C   . PHE A  1 20  ? -11.650 -4.596  23.366  1.00 29.54  ? 269  PHE A C   1 
ATOM   145  O  O   . PHE A  1 20  ? -10.797 -4.037  22.689  1.00 24.37  ? 269  PHE A O   1 
ATOM   146  C  CB  . PHE A  1 20  ? -13.761 -3.510  22.574  1.00 36.36  ? 269  PHE A CB  1 
ATOM   147  C  CG  . PHE A  1 20  ? -14.158 -4.705  21.792  1.00 38.75  ? 269  PHE A CG  1 
ATOM   148  C  CD1 . PHE A  1 20  ? -15.200 -5.524  22.239  1.00 39.90  ? 269  PHE A CD1 1 
ATOM   149  C  CD2 . PHE A  1 20  ? -13.484 -5.028  20.615  1.00 39.95  ? 269  PHE A CD2 1 
ATOM   150  C  CE1 . PHE A  1 20  ? -15.552 -6.669  21.553  1.00 38.62  ? 269  PHE A CE1 1 
ATOM   151  C  CE2 . PHE A  1 20  ? -13.851 -6.161  19.917  1.00 43.12  ? 269  PHE A CE2 1 
ATOM   152  C  CZ  . PHE A  1 20  ? -14.886 -6.984  20.397  1.00 40.88  ? 269  PHE A CZ  1 
ATOM   153  N  N   . MET A  1 21  ? -11.571 -5.878  23.725  1.00 30.47  ? 270  MET A N   1 
ATOM   154  C  CA  . MET A  1 21  ? -10.424 -6.697  23.409  1.00 32.55  ? 270  MET A CA  1 
ATOM   155  C  C   . MET A  1 21  ? -10.888 -7.611  22.305  1.00 32.18  ? 270  MET A C   1 
ATOM   156  O  O   . MET A  1 21  ? -11.827 -8.386  22.466  1.00 30.44  ? 270  MET A O   1 
ATOM   157  C  CB  . MET A  1 21  ? -9.989  -7.544  24.598  1.00 39.59  ? 270  MET A CB  1 
ATOM   158  C  CG  . MET A  1 21  ? -10.139 -6.898  25.960  1.00 49.83  ? 270  MET A CG  1 
ATOM   159  S  SD  . MET A  1 21  ? -9.128  -5.447  26.243  1.00 51.03  ? 270  MET A SD  1 
ATOM   160  C  CE  . MET A  1 21  ? -9.776  -4.985  27.850  1.00 50.74  ? 270  MET A CE  1 
ATOM   161  N  N   . SER A  1 22  ? -10.282 -7.520  21.135  1.00 29.49  ? 271  SER A N   1 
ATOM   162  C  CA  . SER A  1 22  ? -10.792 -8.316  20.048  1.00 26.91  ? 271  SER A CA  1 
ATOM   163  C  C   . SER A  1 22  ? -10.465 -9.779  20.307  1.00 26.55  ? 271  SER A C   1 
ATOM   164  O  O   . SER A  1 22  ? -9.476  -10.094 20.993  1.00 26.15  ? 271  SER A O   1 
ATOM   165  C  CB  . SER A  1 22  ? -10.177 -7.841  18.721  1.00 27.26  ? 271  SER A CB  1 
ATOM   166  O  OG  . SER A  1 22  ? -8.938  -8.436  18.534  1.00 23.86  ? 271  SER A OG  1 
ATOM   167  N  N   . ASN A  1 23  ? -11.293 -10.676 19.785  1.00 29.02  ? 272  ASN A N   1 
ATOM   168  C  CA  A ASN A  1 23  ? -10.964 -12.092 19.761  0.50 31.40  ? 272  ASN A CA  1 
ATOM   169  C  CA  B ASN A  1 23  ? -10.912 -12.096 19.764  0.50 32.71  ? 272  ASN A CA  1 
ATOM   170  C  C   . ASN A  1 23  ? -10.601 -12.570 18.344  1.00 32.11  ? 272  ASN A C   1 
ATOM   171  O  O   . ASN A  1 23  ? -10.615 -13.772 18.061  1.00 32.53  ? 272  ASN A O   1 
ATOM   172  C  CB  A ASN A  1 23  ? -12.100 -12.916 20.384  0.50 32.17  ? 272  ASN A CB  1 
ATOM   173  C  CB  B ASN A  1 23  ? -11.944 -13.026 20.426  0.50 35.24  ? 272  ASN A CB  1 
ATOM   174  C  CG  A ASN A  1 23  ? -12.149 -12.764 21.897  0.50 31.28  ? 272  ASN A CG  1 
ATOM   175  C  CG  B ASN A  1 23  ? -11.324 -14.349 20.879  0.50 36.14  ? 272  ASN A CG  1 
ATOM   176  O  OD1 A ASN A  1 23  ? -11.132 -12.894 22.565  0.50 30.71  ? 272  ASN A OD1 1 
ATOM   177  O  OD1 B ASN A  1 23  ? -10.403 -14.372 21.696  0.50 39.32  ? 272  ASN A OD1 1 
ATOM   178  N  ND2 A ASN A  1 23  ? -13.313 -12.438 22.429  0.50 31.10  ? 272  ASN A ND2 1 
ATOM   179  N  ND2 B ASN A  1 23  ? -11.817 -15.453 20.337  0.50 37.07  ? 272  ASN A ND2 1 
ATOM   180  N  N   . SER A  1 24  ? -10.262 -11.638 17.472  1.00 33.89  ? 273  SER A N   1 
ATOM   181  C  CA  . SER A  1 24  ? -9.802  -11.970 16.107  1.00 36.56  ? 273  SER A CA  1 
ATOM   182  C  C   . SER A  1 24  ? -8.745  -10.980 15.646  1.00 34.99  ? 273  SER A C   1 
ATOM   183  O  O   . SER A  1 24  ? -8.472  -9.967  16.316  1.00 29.35  ? 273  SER A O   1 
ATOM   184  C  CB  . SER A  1 24  ? -10.973 -11.994 15.109  1.00 40.18  ? 273  SER A CB  1 
ATOM   185  O  OG  . SER A  1 24  ? -11.502 -10.697 14.892  1.00 45.00  ? 273  SER A OG  1 
ATOM   186  N  N   . GLN A  1 25  ? -8.154  -11.267 14.486  1.00 34.93  ? 274  GLN A N   1 
ATOM   187  C  CA  . GLN A  1 25  ? -6.973  -10.531 14.067  1.00 34.09  ? 274  GLN A CA  1 
ATOM   188  C  C   . GLN A  1 25  ? -7.232  -9.755  12.793  1.00 32.35  ? 274  GLN A C   1 
ATOM   189  O  O   . GLN A  1 25  ? -7.962  -10.190 11.922  1.00 34.08  ? 274  GLN A O   1 
ATOM   190  C  CB  . GLN A  1 25  ? -5.781  -11.466 13.894  1.00 33.86  ? 274  GLN A CB  1 
ATOM   191  C  CG  . GLN A  1 25  ? -5.542  -12.442 15.039  1.00 32.70  ? 274  GLN A CG  1 
ATOM   192  C  CD  . GLN A  1 25  ? -4.885  -13.735 14.574  1.00 30.00  ? 274  GLN A CD  1 
ATOM   193  O  OE1 . GLN A  1 25  ? -3.689  -13.918 14.727  1.00 32.58  ? 274  GLN A OE1 1 
ATOM   194  N  NE2 . GLN A  1 25  ? -5.655  -14.606 13.986  1.00 27.01  ? 274  GLN A NE2 1 
ATOM   195  N  N   . ARG A  1 26  ? -6.646  -8.568  12.742  1.00 31.83  ? 275  ARG A N   1 
ATOM   196  C  CA  . ARG A  1 26  ? -6.814  -7.606  11.664  1.00 30.89  ? 275  ARG A CA  1 
ATOM   197  C  C   . ARG A  1 26  ? -5.542  -6.801  11.528  1.00 30.47  ? 275  ARG A C   1 
ATOM   198  O  O   . ARG A  1 26  ? -4.820  -6.617  12.519  1.00 29.79  ? 275  ARG A O   1 
ATOM   199  C  CB  . ARG A  1 26  ? -7.911  -6.642  12.001  1.00 33.05  ? 275  ARG A CB  1 
ATOM   200  C  CG  . ARG A  1 26  ? -9.277  -7.246  11.795  1.00 36.10  ? 275  ARG A CG  1 
ATOM   201  C  CD  . ARG A  1 26  ? -10.286 -6.157  11.959  1.00 38.40  ? 275  ARG A CD  1 
ATOM   202  N  NE  . ARG A  1 26  ? -11.644 -6.630  11.716  1.00 41.82  ? 275  ARG A NE  1 
ATOM   203  C  CZ  . ARG A  1 26  ? -12.582 -5.919  11.090  1.00 41.82  ? 275  ARG A CZ  1 
ATOM   204  N  NH1 . ARG A  1 26  ? -12.335 -4.680  10.611  1.00 39.11  ? 275  ARG A NH1 1 
ATOM   205  N  NH2 . ARG A  1 26  ? -13.775 -6.466  10.938  1.00 43.47  ? 275  ARG A NH2 1 
ATOM   206  N  N   . ASN A  1 27  ? -5.236  -6.348  10.315  1.00 28.68  ? 276  ASN A N   1 
ATOM   207  C  CA  . ASN A  1 27  ? -4.154  -5.420  10.165  1.00 29.23  ? 276  ASN A CA  1 
ATOM   208  C  C   . ASN A  1 27  ? -4.560  -4.125  10.871  1.00 29.75  ? 276  ASN A C   1 
ATOM   209  O  O   . ASN A  1 27  ? -5.684  -3.993  11.369  1.00 24.56  ? 276  ASN A O   1 
ATOM   210  C  CB  . ASN A  1 27  ? -3.713  -5.209  8.690   1.00 34.22  ? 276  ASN A CB  1 
ATOM   211  C  CG  . ASN A  1 27  ? -4.807  -4.672  7.793   1.00 32.97  ? 276  ASN A CG  1 
ATOM   212  O  OD1 . ASN A  1 27  ? -5.451  -3.671  8.094   1.00 35.56  ? 276  ASN A OD1 1 
ATOM   213  N  ND2 . ASN A  1 27  ? -5.014  -5.342  6.669   1.00 38.65  ? 276  ASN A ND2 1 
ATOM   214  N  N   . TRP A  1 28  ? -3.599  -3.214  10.971  1.00 29.43  ? 277  TRP A N   1 
ATOM   215  C  CA  . TRP A  1 28  ? -3.732  -2.037  11.804  1.00 29.72  ? 277  TRP A CA  1 
ATOM   216  C  C   . TRP A  1 28  ? -4.810  -1.096  11.233  1.00 29.66  ? 277  TRP A C   1 
ATOM   217  O  O   . TRP A  1 28  ? -5.641  -0.576  11.981  1.00 29.35  ? 277  TRP A O   1 
ATOM   218  C  CB  . TRP A  1 28  ? -2.352  -1.363  11.928  1.00 30.11  ? 277  TRP A CB  1 
ATOM   219  C  CG  . TRP A  1 28  ? -2.269  -0.194  12.894  1.00 31.36  ? 277  TRP A CG  1 
ATOM   220  C  CD1 . TRP A  1 28  ? -2.006  -0.259  14.225  1.00 31.37  ? 277  TRP A CD1 1 
ATOM   221  C  CD2 . TRP A  1 28  ? -2.405  1.207   12.588  1.00 31.92  ? 277  TRP A CD2 1 
ATOM   222  N  NE1 . TRP A  1 28  ? -1.976  0.988   14.763  1.00 32.06  ? 277  TRP A NE1 1 
ATOM   223  C  CE2 . TRP A  1 28  ? -2.230  1.909   13.793  1.00 31.77  ? 277  TRP A CE2 1 
ATOM   224  C  CE3 . TRP A  1 28  ? -2.671  1.925   11.421  1.00 31.81  ? 277  TRP A CE3 1 
ATOM   225  C  CZ2 . TRP A  1 28  ? -2.312  3.300   13.876  1.00 33.06  ? 277  TRP A CZ2 1 
ATOM   226  C  CZ3 . TRP A  1 28  ? -2.740  3.317   11.497  1.00 33.56  ? 277  TRP A CZ3 1 
ATOM   227  C  CH2 . TRP A  1 28  ? -2.558  3.987   12.711  1.00 32.89  ? 277  TRP A CH2 1 
ATOM   228  N  N   . HIS A  1 29  ? -4.791  -0.854  9.920   1.00 29.30  ? 278  HIS A N   1 
ATOM   229  C  CA  . HIS A  1 29  ? -5.771  0.051   9.315   1.00 27.39  ? 278  HIS A CA  1 
ATOM   230  C  C   . HIS A  1 29  ? -7.152  -0.541  9.441   1.00 28.91  ? 278  HIS A C   1 
ATOM   231  O  O   . HIS A  1 29  ? -8.118  0.194   9.691   1.00 27.74  ? 278  HIS A O   1 
ATOM   232  C  CB  . HIS A  1 29  ? -5.485  0.318   7.840   1.00 30.61  ? 278  HIS A CB  1 
ATOM   233  C  CG  . HIS A  1 29  ? -4.054  0.581   7.558   1.00 28.98  ? 278  HIS A CG  1 
ATOM   234  N  ND1 . HIS A  1 29  ? -3.514  1.843   7.615   1.00 30.40  ? 278  HIS A ND1 1 
ATOM   235  C  CD2 . HIS A  1 29  ? -3.042  -0.261  7.248   1.00 33.63  ? 278  HIS A CD2 1 
ATOM   236  C  CE1 . HIS A  1 29  ? -2.221  1.763   7.365   1.00 33.15  ? 278  HIS A CE1 1 
ATOM   237  N  NE2 . HIS A  1 29  ? -1.914  0.502   7.120   1.00 33.09  ? 278  HIS A NE2 1 
ATOM   238  N  N   . ASP A  1 30  ? -7.294  -1.856  9.285   1.00 26.63  ? 279  ASP A N   1 
ATOM   239  C  CA  . ASP A  1 30  ? -8.667  -2.425  9.471   1.00 29.91  ? 279  ASP A CA  1 
ATOM   240  C  C   . ASP A  1 30  ? -9.124  -2.456  10.962  1.00 30.69  ? 279  ASP A C   1 
ATOM   241  O  O   . ASP A  1 30  ? -10.345 -2.529  11.248  1.00 27.28  ? 279  ASP A O   1 
ATOM   242  C  CB  . ASP A  1 30  ? -8.807  -3.807  8.811   1.00 35.05  ? 279  ASP A CB  1 
ATOM   243  C  CG  . ASP A  1 30  ? -8.744  -3.735  7.288   1.00 36.32  ? 279  ASP A CG  1 
ATOM   244  O  OD1 . ASP A  1 30  ? -8.972  -2.654  6.705   1.00 49.61  ? 279  ASP A OD1 1 
ATOM   245  O  OD2 . ASP A  1 30  ? -8.502  -4.760  6.654   1.00 42.68  ? 279  ASP A OD2 1 
ATOM   246  N  N   . SER A  1 31  ? -8.147  -2.368  11.886  1.00 27.95  ? 280  SER A N   1 
ATOM   247  C  CA  . SER A  1 31  ? -8.410  -2.316  13.344  1.00 29.48  ? 280  SER A CA  1 
ATOM   248  C  C   . SER A  1 31  ? -8.910  -0.907  13.742  1.00 32.15  ? 280  SER A C   1 
ATOM   249  O  O   . SER A  1 31  ? -9.779  -0.754  14.641  1.00 31.58  ? 280  SER A O   1 
ATOM   250  C  CB  . SER A  1 31  ? -7.149  -2.667  14.128  1.00 26.19  ? 280  SER A CB  1 
ATOM   251  O  OG  . SER A  1 31  ? -6.772  -4.014  13.940  1.00 23.89  ? 280  SER A OG  1 
ATOM   252  N  N   . ILE A  1 32  ? -8.350  0.100   13.067  1.00 32.01  ? 281  ILE A N   1 
ATOM   253  C  CA  . ILE A  1 32  ? -8.836  1.465   13.142  1.00 34.69  ? 281  ILE A CA  1 
ATOM   254  C  C   . ILE A  1 32  ? -10.310 1.519   12.737  1.00 37.10  ? 281  ILE A C   1 
ATOM   255  O  O   . ILE A  1 32  ? -11.138 2.114   13.432  1.00 39.93  ? 281  ILE A O   1 
ATOM   256  C  CB  . ILE A  1 32  ? -8.097  2.449   12.199  1.00 35.78  ? 281  ILE A CB  1 
ATOM   257  C  CG1 . ILE A  1 32  ? -6.617  2.609   12.578  1.00 37.80  ? 281  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A  1 32  ? -8.783  3.821   12.221  1.00 32.72  ? 281  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A  1 32  ? -6.344  3.620   13.672  1.00 40.24  ? 281  ILE A CD1 1 
ATOM   260  N  N   . THR A  1 33  ? -10.607 0.937   11.593  1.00 34.76  ? 282  THR A N   1 
ATOM   261  C  CA  . THR A  1 33  ? -11.972 0.877   11.073  1.00 35.30  ? 282  THR A CA  1 
ATOM   262  C  C   . THR A  1 33  ? -12.941 0.185   12.050  1.00 33.39  ? 282  THR A C   1 
ATOM   263  O  O   . THR A  1 33  ? -14.006 0.714   12.326  1.00 37.22  ? 282  THR A O   1 
ATOM   264  C  CB  . THR A  1 33  ? -11.991 0.204   9.678   1.00 37.69  ? 282  THR A CB  1 
ATOM   265  O  OG1 . THR A  1 33  ? -11.420 1.100   8.726   1.00 38.86  ? 282  THR A OG1 1 
ATOM   266  C  CG2 . THR A  1 33  ? -13.391 -0.113  9.215   1.00 37.25  ? 282  THR A CG2 1 
ATOM   267  N  N   . ALA A  1 34  ? -12.585 -0.997  12.535  1.00 29.22  ? 283  ALA A N   1 
ATOM   268  C  CA  . ALA A  1 34  ? -13.410 -1.719  13.483  1.00 29.64  ? 283  ALA A CA  1 
ATOM   269  C  C   . ALA A  1 34  ? -13.746 -0.874  14.738  1.00 31.69  ? 283  ALA A C   1 
ATOM   270  O  O   . ALA A  1 34  ? -14.907 -0.803  15.143  1.00 34.09  ? 283  ALA A O   1 
ATOM   271  C  CB  . ALA A  1 34  ? -12.747 -3.024  13.884  1.00 27.15  ? 283  ALA A CB  1 
ATOM   272  N  N   . CYS A  1 35  ? -12.757 -0.185  15.301  1.00 29.89  ? 284  CYS A N   1 
ATOM   273  C  CA  . CYS A  1 35  ? -12.979 0.615   16.478  1.00 31.76  ? 284  CYS A CA  1 
ATOM   274  C  C   . CYS A  1 35  ? -13.959 1.738   16.190  1.00 36.91  ? 284  CYS A C   1 
ATOM   275  O  O   . CYS A  1 35  ? -14.899 1.918   16.972  1.00 33.72  ? 284  CYS A O   1 
ATOM   276  C  CB  . CYS A  1 35  ? -11.669 1.148   17.063  1.00 31.55  ? 284  CYS A CB  1 
ATOM   277  S  SG  . CYS A  1 35  ? -10.663 -0.171  17.755  1.00 27.37  ? 284  CYS A SG  1 
ATOM   278  N  N   . LYS A  1 36  ? -13.773 2.442   15.062  1.00 36.71  ? 285  LYS A N   1 
ATOM   279  C  CA  . LYS A  1 36  ? -14.707 3.508   14.620  1.00 42.42  ? 285  LYS A CA  1 
ATOM   280  C  C   . LYS A  1 36  ? -16.132 3.080   14.290  1.00 39.03  ? 285  LYS A C   1 
ATOM   281  O  O   . LYS A  1 36  ? -17.033 3.857   14.442  1.00 48.48  ? 285  LYS A O   1 
ATOM   282  C  CB  . LYS A  1 36  ? -14.157 4.241   13.408  1.00 44.95  ? 285  LYS A CB  1 
ATOM   283  C  CG  . LYS A  1 36  ? -13.220 5.386   13.735  1.00 45.99  ? 285  LYS A CG  1 
ATOM   284  C  CD  . LYS A  1 36  ? -12.371 5.651   12.507  1.00 52.93  ? 285  LYS A CD  1 
ATOM   285  C  CE  . LYS A  1 36  ? -11.644 6.976   12.564  1.00 53.14  ? 285  LYS A CE  1 
ATOM   286  N  NZ  . LYS A  1 36  ? -10.728 7.000   11.388  1.00 56.56  ? 285  LYS A NZ  1 
ATOM   287  N  N   . GLU A  1 37  ? -16.328 1.849   13.854  1.00 44.02  ? 286  GLU A N   1 
ATOM   288  C  CA  . GLU A  1 37  ? -17.674 1.306   13.638  1.00 51.30  ? 286  GLU A CA  1 
ATOM   289  C  C   . GLU A  1 37  ? -18.457 1.032   14.939  1.00 52.94  ? 286  GLU A C   1 
ATOM   290  O  O   . GLU A  1 37  ? -19.653 0.703   14.909  1.00 51.59  ? 286  GLU A O   1 
ATOM   291  C  CB  . GLU A  1 37  ? -17.603 0.046   12.769  1.00 56.15  ? 286  GLU A CB  1 
ATOM   292  C  CG  . GLU A  1 37  ? -17.452 0.414   11.301  1.00 66.76  ? 286  GLU A CG  1 
ATOM   293  C  CD  . GLU A  1 37  ? -17.137 -0.756  10.408  1.00 73.50  ? 286  GLU A CD  1 
ATOM   294  O  OE1 . GLU A  1 37  ? -17.068 -0.541  9.181   1.00 84.98  ? 286  GLU A OE1 1 
ATOM   295  O  OE2 . GLU A  1 37  ? -16.935 -1.875  10.922  1.00 78.96  ? 286  GLU A OE2 1 
ATOM   296  N  N   . VAL A  1 38  ? -17.788 1.168   16.078  1.00 47.73  ? 287  VAL A N   1 
ATOM   297  C  CA  . VAL A  1 38  ? -18.455 1.017   17.370  1.00 43.24  ? 287  VAL A CA  1 
ATOM   298  C  C   . VAL A  1 38  ? -18.253 2.260   18.221  1.00 40.18  ? 287  VAL A C   1 
ATOM   299  O  O   . VAL A  1 38  ? -18.301 2.186   19.423  1.00 40.99  ? 287  VAL A O   1 
ATOM   300  C  CB  . VAL A  1 38  ? -18.021 -0.288  18.096  1.00 42.83  ? 287  VAL A CB  1 
ATOM   301  C  CG1 . VAL A  1 38  ? -18.548 -1.499  17.351  1.00 41.95  ? 287  VAL A CG1 1 
ATOM   302  C  CG2 . VAL A  1 38  ? -16.501 -0.402  18.253  1.00 42.01  ? 287  VAL A CG2 1 
ATOM   303  N  N   . GLY A  1 39  ? -18.045 3.406   17.570  1.00 37.85  ? 288  GLY A N   1 
ATOM   304  C  CA  . GLY A  1 39  ? -17.878 4.685   18.254  1.00 35.72  ? 288  GLY A CA  1 
ATOM   305  C  C   . GLY A  1 39  ? -16.678 4.749   19.168  1.00 34.34  ? 288  GLY A C   1 
ATOM   306  O  O   . GLY A  1 39  ? -16.714 5.374   20.231  1.00 34.98  ? 288  GLY A O   1 
ATOM   307  N  N   . ALA A  1 40  ? -15.599 4.084   18.781  1.00 31.98  ? 289  ALA A N   1 
ATOM   308  C  CA  . ALA A  1 40  ? -14.407 4.045   19.628  1.00 29.37  ? 289  ALA A CA  1 
ATOM   309  C  C   . ALA A  1 40  ? -13.140 4.316   18.820  1.00 30.06  ? 289  ALA A C   1 
ATOM   310  O  O   . ALA A  1 40  ? -13.178 4.496   17.601  1.00 33.53  ? 289  ALA A O   1 
ATOM   311  C  CB  . ALA A  1 40  ? -14.304 2.692   20.328  1.00 29.41  ? 289  ALA A CB  1 
ATOM   312  N  N   . GLN A  1 41  ? -12.019 4.257   19.514  1.00 28.28  ? 290  GLN A N   1 
ATOM   313  C  CA  A GLN A  1 41  ? -10.743 4.533   18.930  0.50 28.42  ? 290  GLN A CA  1 
ATOM   314  C  CA  B GLN A  1 41  ? -10.744 4.546   18.916  0.50 30.94  ? 290  GLN A CA  1 
ATOM   315  C  C   . GLN A  1 41  ? -9.763  3.419   19.238  1.00 28.80  ? 290  GLN A C   1 
ATOM   316  O  O   . GLN A  1 41  ? -9.776  2.874   20.327  1.00 29.85  ? 290  GLN A O   1 
ATOM   317  C  CB  A GLN A  1 41  ? -10.227 5.829   19.526  0.50 27.72  ? 290  GLN A CB  1 
ATOM   318  C  CB  B GLN A  1 41  ? -10.281 5.949   19.384  0.50 33.62  ? 290  GLN A CB  1 
ATOM   319  C  CG  A GLN A  1 41  ? -9.371  6.633   18.585  0.50 25.13  ? 290  GLN A CG  1 
ATOM   320  C  CG  B GLN A  1 41  ? -8.828  6.124   19.812  0.50 35.18  ? 290  GLN A CG  1 
ATOM   321  C  CD  A GLN A  1 41  ? -9.207  8.035   19.099  0.50 23.90  ? 290  GLN A CD  1 
ATOM   322  C  CD  B GLN A  1 41  ? -8.681  6.471   21.291  0.50 35.51  ? 290  GLN A CD  1 
ATOM   323  O  OE1 A GLN A  1 41  ? -8.779  8.238   20.222  0.50 22.59  ? 290  GLN A OE1 1 
ATOM   324  O  OE1 B GLN A  1 41  ? -8.584  5.594   22.153  0.50 29.70  ? 290  GLN A OE1 1 
ATOM   325  N  NE2 A GLN A  1 41  ? -9.558  9.002   18.286  0.50 24.07  ? 290  GLN A NE2 1 
ATOM   326  N  NE2 B GLN A  1 41  ? -8.619  7.774   21.579  0.50 34.28  ? 290  GLN A NE2 1 
ATOM   327  N  N   . LEU A  1 42  ? -8.921  3.073   18.268  1.00 27.59  ? 291  LEU A N   1 
ATOM   328  C  CA  . LEU A  1 42  ? -7.882  2.092   18.474  1.00 27.99  ? 291  LEU A CA  1 
ATOM   329  C  C   . LEU A  1 42  ? -7.023  2.684   19.582  1.00 28.47  ? 291  LEU A C   1 
ATOM   330  O  O   . LEU A  1 42  ? -6.686  3.872   19.544  1.00 26.52  ? 291  LEU A O   1 
ATOM   331  C  CB  . LEU A  1 42  ? -7.094  1.848   17.194  1.00 29.53  ? 291  LEU A CB  1 
ATOM   332  C  CG  . LEU A  1 42  ? -5.971  0.799   17.257  1.00 28.19  ? 291  LEU A CG  1 
ATOM   333  C  CD1 . LEU A  1 42  ? -6.521  -0.576  17.533  1.00 27.00  ? 291  LEU A CD1 1 
ATOM   334  C  CD2 . LEU A  1 42  ? -5.161  0.827   15.958  1.00 26.14  ? 291  LEU A CD2 1 
ATOM   335  N  N   . VAL A  1 43  ? -6.719  1.865   20.581  1.00 27.09  ? 292  VAL A N   1 
ATOM   336  C  CA  . VAL A  1 43  ? -6.429  2.386   21.922  1.00 31.08  ? 292  VAL A CA  1 
ATOM   337  C  C   . VAL A  1 43  ? -5.233  3.361   22.053  1.00 30.34  ? 292  VAL A C   1 
ATOM   338  O  O   . VAL A  1 43  ? -4.082  3.039   21.750  1.00 29.65  ? 292  VAL A O   1 
ATOM   339  C  CB  . VAL A  1 43  ? -6.314  1.256   22.975  1.00 29.75  ? 292  VAL A CB  1 
ATOM   340  C  CG1 . VAL A  1 43  ? -5.131  0.357   22.709  1.00 27.50  ? 292  VAL A CG1 1 
ATOM   341  C  CG2 . VAL A  1 43  ? -6.231  1.848   24.381  1.00 31.05  ? 292  VAL A CG2 1 
ATOM   342  N  N   . VAL A  1 44  ? -5.563  4.555   22.518  1.00 28.09  ? 293  VAL A N   1 
ATOM   343  C  CA  . VAL A  1 44  ? -4.611  5.608   22.805  1.00 27.59  ? 293  VAL A CA  1 
ATOM   344  C  C   . VAL A  1 44  ? -4.379  5.586   24.314  1.00 28.88  ? 293  VAL A C   1 
ATOM   345  O  O   . VAL A  1 44  ? -5.333  5.671   25.108  1.00 25.07  ? 293  VAL A O   1 
ATOM   346  C  CB  . VAL A  1 44  ? -5.144  7.000   22.336  1.00 29.32  ? 293  VAL A CB  1 
ATOM   347  C  CG1 . VAL A  1 44  ? -4.145  8.121   22.644  1.00 29.96  ? 293  VAL A CG1 1 
ATOM   348  C  CG2 . VAL A  1 44  ? -5.433  6.966   20.833  1.00 29.92  ? 293  VAL A CG2 1 
ATOM   349  N  N   . ILE A  1 45  ? -3.115  5.440   24.702  1.00 28.27  ? 294  ILE A N   1 
ATOM   350  C  CA  . ILE A  1 45  ? -2.760  5.363   26.087  1.00 30.35  ? 294  ILE A CA  1 
ATOM   351  C  C   . ILE A  1 45  ? -2.376  6.731   26.642  1.00 35.61  ? 294  ILE A C   1 
ATOM   352  O  O   . ILE A  1 45  ? -1.528  7.421   26.074  1.00 31.12  ? 294  ILE A O   1 
ATOM   353  C  CB  . ILE A  1 45  ? -1.589  4.403   26.291  1.00 29.68  ? 294  ILE A CB  1 
ATOM   354  C  CG1 . ILE A  1 45  ? -1.925  3.064   25.650  1.00 27.74  ? 294  ILE A CG1 1 
ATOM   355  C  CG2 . ILE A  1 45  ? -1.325  4.237   27.777  1.00 29.74  ? 294  ILE A CG2 1 
ATOM   356  C  CD1 . ILE A  1 45  ? -0.798  2.091   25.637  1.00 27.22  ? 294  ILE A CD1 1 
ATOM   357  N  N   . LYS A  1 46  ? -3.001  7.083   27.769  1.00 38.52  ? 295  LYS A N   1 
ATOM   358  C  CA  . LYS A  1 46  ? -2.867  8.388   28.412  1.00 37.07  ? 295  LYS A CA  1 
ATOM   359  C  C   . LYS A  1 46  ? -2.155  8.336   29.763  1.00 37.90  ? 295  LYS A C   1 
ATOM   360  O  O   . LYS A  1 46  ? -1.765  9.365   30.227  1.00 37.35  ? 295  LYS A O   1 
ATOM   361  C  CB  . LYS A  1 46  ? -4.256  9.027   28.632  1.00 38.95  ? 295  LYS A CB  1 
ATOM   362  C  CG  . LYS A  1 46  ? -5.071  9.370   27.389  1.00 38.77  ? 295  LYS A CG  1 
ATOM   363  C  CD  . LYS A  1 46  ? -4.310  10.342  26.516  1.00 42.42  ? 295  LYS A CD  1 
ATOM   364  C  CE  . LYS A  1 46  ? -5.116  10.846  25.335  1.00 43.81  ? 295  LYS A CE  1 
ATOM   365  N  NZ  . LYS A  1 46  ? -4.182  11.427  24.311  1.00 48.45  ? 295  LYS A NZ  1 
ATOM   366  N  N   . SER A  1 47  ? -2.006  7.169   30.409  1.00 36.33  ? 296  SER A N   1 
ATOM   367  C  CA  . SER A  1 47  ? -1.362  7.103   31.724  1.00 35.30  ? 296  SER A CA  1 
ATOM   368  C  C   . SER A  1 47  ? -0.594  5.807   31.981  1.00 37.71  ? 296  SER A C   1 
ATOM   369  O  O   . SER A  1 47  ? -0.852  4.786   31.334  1.00 37.68  ? 296  SER A O   1 
ATOM   370  C  CB  . SER A  1 47  ? -2.413  7.279   32.814  1.00 35.57  ? 296  SER A CB  1 
ATOM   371  O  OG  . SER A  1 47  ? -3.243  6.138   32.888  1.00 33.31  ? 296  SER A OG  1 
ATOM   372  N  N   . ALA A  1 48  ? 0.315   5.840   32.961  1.00 34.25  ? 297  ALA A N   1 
ATOM   373  C  CA  . ALA A  1 48  ? 1.051   4.644   33.358  1.00 32.65  ? 297  ALA A CA  1 
ATOM   374  C  C   . ALA A  1 48  ? 0.156   3.521   33.821  1.00 32.84  ? 297  ALA A C   1 
ATOM   375  O  O   . ALA A  1 48  ? 0.445   2.380   33.534  1.00 34.23  ? 297  ALA A O   1 
ATOM   376  C  CB  . ALA A  1 48  ? 2.094   4.947   34.425  1.00 31.54  ? 297  ALA A CB  1 
ATOM   377  N  N   . GLU A  1 49  ? -0.926  3.832   34.517  1.00 35.15  ? 298  GLU A N   1 
ATOM   378  C  CA  A GLU A  1 49  ? -1.807  2.793   35.078  0.70 39.36  ? 298  GLU A CA  1 
ATOM   379  C  CA  B GLU A  1 49  ? -1.784  2.787   35.069  0.30 36.62  ? 298  GLU A CA  1 
ATOM   380  C  C   . GLU A  1 49  ? -2.550  2.109   33.924  1.00 37.53  ? 298  GLU A C   1 
ATOM   381  O  O   . GLU A  1 49  ? -2.781  0.911   33.947  1.00 34.64  ? 298  GLU A O   1 
ATOM   382  C  CB  A GLU A  1 49  ? -2.829  3.346   36.102  0.70 42.78  ? 298  GLU A CB  1 
ATOM   383  C  CB  B GLU A  1 49  ? -2.733  3.370   36.121  0.30 37.33  ? 298  GLU A CB  1 
ATOM   384  C  CG  A GLU A  1 49  ? -2.378  4.521   36.971  0.70 49.04  ? 298  GLU A CG  1 
ATOM   385  C  CG  B GLU A  1 49  ? -2.037  4.230   37.172  0.30 38.93  ? 298  GLU A CG  1 
ATOM   386  C  CD  A GLU A  1 49  ? -2.604  5.887   36.312  0.70 49.86  ? 298  GLU A CD  1 
ATOM   387  C  CD  B GLU A  1 49  ? -1.816  3.504   38.473  0.30 38.08  ? 298  GLU A CD  1 
ATOM   388  O  OE1 A GLU A  1 49  ? -1.601  6.649   36.214  0.70 45.63  ? 298  GLU A OE1 1 
ATOM   389  O  OE1 B GLU A  1 49  ? -0.665  3.483   38.969  0.30 37.50  ? 298  GLU A OE1 1 
ATOM   390  O  OE2 A GLU A  1 49  ? -3.766  6.175   35.873  0.70 45.58  ? 298  GLU A OE2 1 
ATOM   391  O  OE2 B GLU A  1 49  ? -2.806  2.959   38.990  0.30 38.01  ? 298  GLU A OE2 1 
ATOM   392  N  N   . GLU A  1 50  ? -2.897  2.903   32.907  1.00 35.39  ? 299  GLU A N   1 
ATOM   393  C  CA  . GLU A  1 50  ? -3.606  2.424   31.753  1.00 35.83  ? 299  GLU A CA  1 
ATOM   394  C  C   . GLU A  1 50  ? -2.699  1.507   30.923  1.00 33.41  ? 299  GLU A C   1 
ATOM   395  O  O   . GLU A  1 50  ? -3.079  0.385   30.577  1.00 28.00  ? 299  GLU A O   1 
ATOM   396  C  CB  . GLU A  1 50  ? -4.108  3.570   30.920  1.00 35.91  ? 299  GLU A CB  1 
ATOM   397  C  CG  . GLU A  1 50  ? -5.065  3.102   29.832  1.00 37.11  ? 299  GLU A CG  1 
ATOM   398  C  CD  . GLU A  1 50  ? -5.509  4.227   28.913  1.00 35.59  ? 299  GLU A CD  1 
ATOM   399  O  OE1 . GLU A  1 50  ? -6.475  4.037   28.149  1.00 37.55  ? 299  GLU A OE1 1 
ATOM   400  O  OE2 . GLU A  1 50  ? -4.919  5.321   28.970  1.00 35.27  ? 299  GLU A OE2 1 
ATOM   401  N  N   . GLN A  1 51  ? -1.483  1.969   30.709  1.00 32.73  ? 300  GLN A N   1 
ATOM   402  C  CA  . GLN A  1 51  ? -0.452  1.168   30.050  1.00 34.25  ? 300  GLN A CA  1 
ATOM   403  C  C   . GLN A  1 51  ? -0.246  -0.168  30.747  1.00 35.83  ? 300  GLN A C   1 
ATOM   404  O  O   . GLN A  1 51  ? -0.058  -1.194  30.090  1.00 36.63  ? 300  GLN A O   1 
ATOM   405  C  CB  . GLN A  1 51  ? 0.844   1.933   30.016  1.00 32.00  ? 300  GLN A CB  1 
ATOM   406  C  CG  . GLN A  1 51  ? 2.106   1.101   29.955  1.00 32.84  ? 300  GLN A CG  1 
ATOM   407  C  CD  . GLN A  1 51  ? 2.228   0.224   28.743  1.00 31.25  ? 300  GLN A CD  1 
ATOM   408  O  OE1 . GLN A  1 51  ? 1.448   0.299   27.796  1.00 30.85  ? 300  GLN A OE1 1 
ATOM   409  N  NE2 . GLN A  1 51  ? 3.210   -0.642  28.781  1.00 33.28  ? 300  GLN A NE2 1 
ATOM   410  N  N   . ASN A  1 52  ? -0.261  -0.149  32.074  1.00 35.76  ? 301  ASN A N   1 
ATOM   411  C  CA  . ASN A  1 52  ? 0.010   -1.360  32.849  1.00 36.50  ? 301  ASN A CA  1 
ATOM   412  C  C   . ASN A  1 52  ? -1.111  -2.373  32.659  1.00 34.40  ? 301  ASN A C   1 
ATOM   413  O  O   . ASN A  1 52  ? -0.843  -3.572  32.490  1.00 33.60  ? 301  ASN A O   1 
ATOM   414  C  CB  . ASN A  1 52  ? 0.162   -1.053  34.329  1.00 38.81  ? 301  ASN A CB  1 
ATOM   415  C  CG  . ASN A  1 52  ? 1.486   -0.396  34.664  1.00 42.68  ? 301  ASN A CG  1 
ATOM   416  O  OD1 . ASN A  1 52  ? 2.453   -0.425  33.892  1.00 41.66  ? 301  ASN A OD1 1 
ATOM   417  N  ND2 . ASN A  1 52  ? 1.526   0.218   35.834  1.00 41.40  ? 301  ASN A ND2 1 
ATOM   418  N  N   . PHE A  1 53  ? -2.342  -1.856  32.705  1.00 28.32  ? 302  PHE A N   1 
ATOM   419  C  CA  . PHE A  1 53  ? -3.530  -2.615  32.422  1.00 29.46  ? 302  PHE A CA  1 
ATOM   420  C  C   . PHE A  1 53  ? -3.532  -3.233  31.007  1.00 30.77  ? 302  PHE A C   1 
ATOM   421  O  O   . PHE A  1 53  ? -3.800  -4.422  30.859  1.00 34.56  ? 302  PHE A O   1 
ATOM   422  C  CB  . PHE A  1 53  ? -4.734  -1.710  32.641  1.00 31.37  ? 302  PHE A CB  1 
ATOM   423  C  CG  . PHE A  1 53  ? -6.017  -2.244  32.129  1.00 29.02  ? 302  PHE A CG  1 
ATOM   424  C  CD1 . PHE A  1 53  ? -6.643  -3.293  32.770  1.00 30.59  ? 302  PHE A CD1 1 
ATOM   425  C  CD2 . PHE A  1 53  ? -6.624  -1.679  31.026  1.00 32.89  ? 302  PHE A CD2 1 
ATOM   426  C  CE1 . PHE A  1 53  ? -7.862  -3.789  32.312  1.00 29.07  ? 302  PHE A CE1 1 
ATOM   427  C  CE2 . PHE A  1 53  ? -7.842  -2.189  30.548  1.00 33.54  ? 302  PHE A CE2 1 
ATOM   428  C  CZ  . PHE A  1 53  ? -8.445  -3.256  31.200  1.00 29.35  ? 302  PHE A CZ  1 
ATOM   429  N  N   . LEU A  1 54  ? -3.242  -2.430  29.985  1.00 27.42  ? 303  LEU A N   1 
ATOM   430  C  CA  . LEU A  1 54  ? -3.304  -2.880  28.605  1.00 27.19  ? 303  LEU A CA  1 
ATOM   431  C  C   . LEU A  1 54  ? -2.226  -3.928  28.336  1.00 24.48  ? 303  LEU A C   1 
ATOM   432  O  O   . LEU A  1 54  ? -2.503  -4.962  27.768  1.00 28.63  ? 303  LEU A O   1 
ATOM   433  C  CB  . LEU A  1 54  ? -3.233  -1.671  27.636  1.00 26.62  ? 303  LEU A CB  1 
ATOM   434  C  CG  . LEU A  1 54  ? -4.434  -0.724  27.793  1.00 26.25  ? 303  LEU A CG  1 
ATOM   435  C  CD1 . LEU A  1 54  ? -4.100  0.638   27.235  1.00 27.63  ? 303  LEU A CD1 1 
ATOM   436  C  CD2 . LEU A  1 54  ? -5.700  -1.266  27.147  1.00 27.56  ? 303  LEU A CD2 1 
ATOM   437  N  N   . GLN A  1 55  ? -1.003  -3.636  28.763  1.00 24.37  ? 304  GLN A N   1 
ATOM   438  C  CA  . GLN A  1 55  ? 0.126   -4.510  28.608  1.00 23.29  ? 304  GLN A CA  1 
ATOM   439  C  C   . GLN A  1 55  ? -0.123  -5.892  29.212  1.00 26.14  ? 304  GLN A C   1 
ATOM   440  O  O   . GLN A  1 55  ? 0.261   -6.900  28.627  1.00 24.64  ? 304  GLN A O   1 
ATOM   441  C  CB  . GLN A  1 55  ? 1.371   -3.912  29.232  1.00 21.89  ? 304  GLN A CB  1 
ATOM   442  C  CG  . GLN A  1 55  ? 2.612   -4.603  28.751  1.00 23.18  ? 304  GLN A CG  1 
ATOM   443  C  CD  . GLN A  1 55  ? 2.986   -4.281  27.306  1.00 25.53  ? 304  GLN A CD  1 
ATOM   444  O  OE1 . GLN A  1 55  ? 3.032   -3.117  26.941  1.00 29.64  ? 304  GLN A OE1 1 
ATOM   445  N  NE2 . GLN A  1 55  ? 3.309   -5.310  26.494  1.00 25.15  ? 304  GLN A NE2 1 
ATOM   446  N  N   . LEU A  1 56  ? -0.751  -5.909  30.377  1.00 26.42  ? 305  LEU A N   1 
ATOM   447  C  CA  . LEU A  1 56  ? -1.109  -7.131  31.037  1.00 30.32  ? 305  LEU A CA  1 
ATOM   448  C  C   . LEU A  1 56  ? -1.944  -8.045  30.178  1.00 30.56  ? 305  LEU A C   1 
ATOM   449  O  O   . LEU A  1 56  ? -1.643  -9.222  30.104  1.00 32.00  ? 305  LEU A O   1 
ATOM   450  C  CB  . LEU A  1 56  ? -1.904  -6.800  32.298  1.00 36.52  ? 305  LEU A CB  1 
ATOM   451  C  CG  . LEU A  1 56  ? -2.420  -8.011  33.063  1.00 41.28  ? 305  LEU A CG  1 
ATOM   452  C  CD1 . LEU A  1 56  ? -1.243  -8.705  33.731  1.00 45.05  ? 305  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A  1 56  ? -3.466  -7.565  34.065  1.00 43.72  ? 305  LEU A CD2 1 
ATOM   454  N  N   . GLN A  1 57  ? -2.990  -7.490  29.546  1.00 32.43  ? 306  GLN A N   1 
ATOM   455  C  CA  . GLN A  1 57  ? -3.848  -8.222  28.625  1.00 34.37  ? 306  GLN A CA  1 
ATOM   456  C  C   . GLN A  1 57  ? -3.052  -9.063  27.649  1.00 35.79  ? 306  GLN A C   1 
ATOM   457  O  O   . GLN A  1 57  ? -3.436  -10.194 27.390  1.00 28.99  ? 306  GLN A O   1 
ATOM   458  C  CB  . GLN A  1 57  ? -4.772  -7.317  27.791  1.00 36.18  ? 306  GLN A CB  1 
ATOM   459  C  CG  . GLN A  1 57  ? -5.570  -6.283  28.559  1.00 38.50  ? 306  GLN A CG  1 
ATOM   460  C  CD  . GLN A  1 57  ? -6.268  -6.868  29.764  1.00 41.30  ? 306  GLN A CD  1 
ATOM   461  O  OE1 . GLN A  1 57  ? -7.134  -7.697  29.617  1.00 40.21  ? 306  GLN A OE1 1 
ATOM   462  N  NE2 . GLN A  1 57  ? -5.900  -6.420  30.962  1.00 45.44  ? 306  GLN A NE2 1 
ATOM   463  N  N   . SER A  1 58  ? -1.978  -8.481  27.091  1.00 34.80  ? 307  SER A N   1 
ATOM   464  C  CA  . SER A  1 58  ? -1.151  -9.142  26.088  1.00 35.39  ? 307  SER A CA  1 
ATOM   465  C  C   . SER A  1 58  ? -0.049  -10.009 26.697  1.00 32.24  ? 307  SER A C   1 
ATOM   466  O  O   . SER A  1 58  ? 0.233   -11.072 26.207  1.00 31.87  ? 307  SER A O   1 
ATOM   467  C  CB  . SER A  1 58  ? -0.499  -8.095  25.157  1.00 39.07  ? 307  SER A CB  1 
ATOM   468  O  OG  . SER A  1 58  ? -1.414  -7.696  24.157  1.00 46.44  ? 307  SER A OG  1 
ATOM   469  N  N   . SER A  1 59  ? 0.595   -9.565  27.746  1.00 32.19  ? 308  SER A N   1 
ATOM   470  C  CA  . SER A  1 59  ? 1.668   -10.376 28.315  1.00 37.72  ? 308  SER A CA  1 
ATOM   471  C  C   . SER A  1 59  ? 1.076   -11.686 28.863  1.00 37.81  ? 308  SER A C   1 
ATOM   472  O  O   . SER A  1 59  ? 1.669   -12.724 28.754  1.00 39.45  ? 308  SER A O   1 
ATOM   473  C  CB  . SER A  1 59  ? 2.450   -9.623  29.401  1.00 38.31  ? 308  SER A CB  1 
ATOM   474  O  OG  . SER A  1 59  ? 1.635   -9.308  30.521  1.00 40.31  ? 308  SER A OG  1 
ATOM   475  N  N   . ARG A  1 60  ? -0.129  -11.626 29.396  1.00 39.52  ? 309  ARG A N   1 
ATOM   476  C  CA  . ARG A  1 60  ? -0.766  -12.793 30.011  1.00 42.16  ? 309  ARG A CA  1 
ATOM   477  C  C   . ARG A  1 60  ? -1.410  -13.748 28.974  1.00 40.28  ? 309  ARG A C   1 
ATOM   478  O  O   . ARG A  1 60  ? -1.428  -14.953 29.138  1.00 41.20  ? 309  ARG A O   1 
ATOM   479  C  CB  . ARG A  1 60  ? -1.806  -12.287 31.005  1.00 43.10  ? 309  ARG A CB  1 
ATOM   480  C  CG  . ARG A  1 60  ? -2.635  -13.346 31.678  1.00 46.37  ? 309  ARG A CG  1 
ATOM   481  C  CD  . ARG A  1 60  ? -3.604  -12.690 32.652  1.00 49.33  ? 309  ARG A CD  1 
ATOM   482  N  NE  . ARG A  1 60  ? -4.555  -11.814 31.965  1.00 50.16  ? 309  ARG A NE  1 
ATOM   483  C  CZ  . ARG A  1 60  ? -5.431  -11.015 32.571  1.00 53.87  ? 309  ARG A CZ  1 
ATOM   484  N  NH1 . ARG A  1 60  ? -5.486  -10.956 33.906  1.00 61.30  ? 309  ARG A NH1 1 
ATOM   485  N  NH2 . ARG A  1 60  ? -6.246  -10.258 31.842  1.00 52.57  ? 309  ARG A NH2 1 
ATOM   486  N  N   . SER A  1 61  ? -1.975  -13.192 27.925  1.00 36.94  ? 310  SER A N   1 
ATOM   487  C  CA  . SER A  1 61  ? -2.597  -13.974 26.921  1.00 33.64  ? 310  SER A CA  1 
ATOM   488  C  C   . SER A  1 61  ? -1.571  -14.442 25.879  1.00 34.08  ? 310  SER A C   1 
ATOM   489  O  O   . SER A  1 61  ? -1.864  -15.314 25.118  1.00 31.57  ? 310  SER A O   1 
ATOM   490  C  CB  . SER A  1 61  ? -3.609  -13.129 26.217  1.00 35.73  ? 310  SER A CB  1 
ATOM   491  O  OG  . SER A  1 61  ? -2.885  -12.197 25.463  1.00 38.20  ? 310  SER A OG  1 
ATOM   492  N  N   . ASN A  1 62  ? -0.368  -13.880 25.903  1.00 36.10  ? 311  ASN A N   1 
ATOM   493  C  CA  . ASN A  1 62  ? 0.660   -14.094 24.880  1.00 37.77  ? 311  ASN A CA  1 
ATOM   494  C  C   . ASN A  1 62  ? 0.215   -13.730 23.469  1.00 34.19  ? 311  ASN A C   1 
ATOM   495  O  O   . ASN A  1 62  ? 0.667   -14.363 22.505  1.00 38.17  ? 311  ASN A O   1 
ATOM   496  C  CB  . ASN A  1 62  ? 1.148   -15.551 24.909  1.00 42.57  ? 311  ASN A CB  1 
ATOM   497  C  CG  . ASN A  1 62  ? 1.576   -15.994 26.286  1.00 44.23  ? 311  ASN A CG  1 
ATOM   498  O  OD1 . ASN A  1 62  ? 2.623   -15.575 26.779  1.00 51.39  ? 311  ASN A OD1 1 
ATOM   499  N  ND2 . ASN A  1 62  ? 0.772   -16.868 26.920  1.00 50.21  ? 311  ASN A ND2 1 
ATOM   500  N  N   . ARG A  1 63  ? -0.671  -12.747 23.349  1.00 29.36  ? 312  ARG A N   1 
ATOM   501  C  CA  . ARG A  1 63  ? -1.136  -12.253 22.079  1.00 32.90  ? 312  ARG A CA  1 
ATOM   502  C  C   . ARG A  1 63  ? -0.486  -10.909 21.643  1.00 31.33  ? 312  ARG A C   1 
ATOM   503  O  O   . ARG A  1 63  ? -0.237  -10.013 22.428  1.00 35.20  ? 312  ARG A O   1 
ATOM   504  C  CB  . ARG A  1 63  ? -2.658  -12.091 22.087  1.00 37.57  ? 312  ARG A CB  1 
ATOM   505  C  CG  . ARG A  1 63  ? -3.497  -13.301 22.506  1.00 40.84  ? 312  ARG A CG  1 
ATOM   506  C  CD  . ARG A  1 63  ? -3.295  -14.517 21.634  1.00 43.36  ? 312  ARG A CD  1 
ATOM   507  N  NE  . ARG A  1 63  ? -4.095  -15.721 21.990  1.00 43.36  ? 312  ARG A NE  1 
ATOM   508  C  CZ  . ARG A  1 63  ? -4.092  -16.845 21.263  1.00 40.52  ? 312  ARG A CZ  1 
ATOM   509  N  NH1 . ARG A  1 63  ? -3.359  -16.886 20.142  1.00 36.29  ? 312  ARG A NH1 1 
ATOM   510  N  NH2 . ARG A  1 63  ? -4.802  -17.928 21.652  1.00 40.14  ? 312  ARG A NH2 1 
ATOM   511  N  N   . PHE A  1 64  ? -0.198  -10.790 20.365  1.00 28.51  ? 313  PHE A N   1 
ATOM   512  C  CA  . PHE A  1 64  ? 0.246   -9.533  19.798  1.00 25.87  ? 313  PHE A CA  1 
ATOM   513  C  C   . PHE A  1 64  ? -0.976  -8.689  19.447  1.00 24.71  ? 313  PHE A C   1 
ATOM   514  O  O   . PHE A  1 64  ? -1.889  -9.156  18.762  1.00 26.69  ? 313  PHE A O   1 
ATOM   515  C  CB  . PHE A  1 64  ? 1.055   -9.848  18.560  1.00 28.23  ? 313  PHE A CB  1 
ATOM   516  C  CG  . PHE A  1 64  ? 2.285   -10.668 18.849  1.00 29.16  ? 313  PHE A CG  1 
ATOM   517  C  CD1 . PHE A  1 64  ? 3.061   -10.416 19.987  1.00 29.00  ? 313  PHE A CD1 1 
ATOM   518  C  CD2 . PHE A  1 64  ? 2.700   -11.662 17.963  1.00 30.76  ? 313  PHE A CD2 1 
ATOM   519  C  CE1 . PHE A  1 64  ? 4.209   -11.160 20.252  1.00 31.50  ? 313  PHE A CE1 1 
ATOM   520  C  CE2 . PHE A  1 64  ? 3.845   -12.404 18.223  1.00 30.07  ? 313  PHE A CE2 1 
ATOM   521  C  CZ  . PHE A  1 64  ? 4.606   -12.156 19.363  1.00 30.24  ? 313  PHE A CZ  1 
ATOM   522  N  N   . THR A  1 65  ? -0.985  -7.451  19.929  1.00 23.25  ? 314  THR A N   1 
ATOM   523  C  CA  . THR A  1 65  ? -2.161  -6.605  19.953  1.00 23.67  ? 314  THR A CA  1 
ATOM   524  C  C   . THR A  1 65  ? -1.828  -5.173  19.521  1.00 23.64  ? 314  THR A C   1 
ATOM   525  O  O   . THR A  1 65  ? -0.888  -4.570  20.042  1.00 22.29  ? 314  THR A O   1 
ATOM   526  C  CB  . THR A  1 65  ? -2.698  -6.563  21.405  1.00 24.65  ? 314  THR A CB  1 
ATOM   527  O  OG1 . THR A  1 65  ? -2.841  -7.921  21.877  1.00 28.77  ? 314  THR A OG1 1 
ATOM   528  C  CG2 . THR A  1 65  ? -3.978  -5.788  21.499  1.00 23.14  ? 314  THR A CG2 1 
ATOM   529  N  N   . TRP A  1 66  ? -2.579  -4.633  18.568  1.00 22.93  ? 315  TRP A N   1 
ATOM   530  C  CA  . TRP A  1 66  ? -2.288  -3.299  18.009  1.00 23.08  ? 315  TRP A CA  1 
ATOM   531  C  C   . TRP A  1 66  ? -2.745  -2.269  19.012  1.00 25.97  ? 315  TRP A C   1 
ATOM   532  O  O   . TRP A  1 66  ? -3.764  -2.498  19.708  1.00 23.78  ? 315  TRP A O   1 
ATOM   533  C  CB  . TRP A  1 66  ? -3.116  -3.013  16.731  1.00 23.81  ? 315  TRP A CB  1 
ATOM   534  C  CG  . TRP A  1 66  ? -2.692  -3.754  15.469  1.00 25.13  ? 315  TRP A CG  1 
ATOM   535  C  CD1 . TRP A  1 66  ? -3.455  -4.586  14.679  1.00 25.15  ? 315  TRP A CD1 1 
ATOM   536  C  CD2 . TRP A  1 66  ? -1.418  -3.699  14.876  1.00 23.78  ? 315  TRP A CD2 1 
ATOM   537  N  NE1 . TRP A  1 66  ? -2.686  -5.086  13.625  1.00 24.52  ? 315  TRP A NE1 1 
ATOM   538  C  CE2 . TRP A  1 66  ? -1.444  -4.523  13.718  1.00 24.79  ? 315  TRP A CE2 1 
ATOM   539  C  CE3 . TRP A  1 66  ? -0.220  -3.072  15.233  1.00 25.08  ? 315  TRP A CE3 1 
ATOM   540  C  CZ2 . TRP A  1 66  ? -0.328  -4.691  12.914  1.00 24.98  ? 315  TRP A CZ2 1 
ATOM   541  C  CZ3 . TRP A  1 66  ? 0.885   -3.235  14.425  1.00 24.67  ? 315  TRP A CZ3 1 
ATOM   542  C  CH2 . TRP A  1 66  ? 0.821   -4.033  13.282  1.00 24.17  ? 315  TRP A CH2 1 
ATOM   543  N  N   . MET A  1 67  ? -2.049  -1.140  19.053  1.00 22.96  ? 316  MET A N   1 
ATOM   544  C  CA  . MET A  1 67  ? -2.558  0.042   19.757  1.00 26.89  ? 316  MET A CA  1 
ATOM   545  C  C   . MET A  1 67  ? -2.605  1.164   18.727  1.00 26.57  ? 316  MET A C   1 
ATOM   546  O  O   . MET A  1 67  ? -2.121  1.018   17.608  1.00 24.82  ? 316  MET A O   1 
ATOM   547  C  CB  . MET A  1 67  ? -1.704  0.450   20.992  1.00 26.71  ? 316  MET A CB  1 
ATOM   548  C  CG  . MET A  1 67  ? -0.407  1.127   20.639  1.00 27.08  ? 316  MET A CG  1 
ATOM   549  S  SD  . MET A  1 67  ? 0.870   1.244   21.912  1.00 27.55  ? 316  MET A SD  1 
ATOM   550  C  CE  . MET A  1 67  ? 1.314   -0.464  22.188  1.00 29.47  ? 316  MET A CE  1 
ATOM   551  N  N   . GLY A  1 68  ? -3.188  2.288   19.127  1.00 26.53  ? 317  GLY A N   1 
ATOM   552  C  CA  . GLY A  1 68  ? -3.419  3.401   18.240  1.00 26.66  ? 317  GLY A CA  1 
ATOM   553  C  C   . GLY A  1 68  ? -2.229  4.319   18.097  1.00 24.48  ? 317  GLY A C   1 
ATOM   554  O  O   . GLY A  1 68  ? -2.335  5.530   18.280  1.00 21.98  ? 317  GLY A O   1 
ATOM   555  N  N   . LEU A  1 69  ? -1.102  3.757   17.734  1.00 22.81  ? 318  LEU A N   1 
ATOM   556  C  CA  . LEU A  1 69  ? 0.108   4.531   17.696  1.00 22.53  ? 318  LEU A CA  1 
ATOM   557  C  C   . LEU A  1 69  ? 0.849   4.172   16.418  1.00 23.01  ? 318  LEU A C   1 
ATOM   558  O  O   . LEU A  1 69  ? 0.954   2.993   16.082  1.00 25.40  ? 318  LEU A O   1 
ATOM   559  C  CB  . LEU A  1 69  ? 0.914   4.229   18.954  1.00 22.95  ? 318  LEU A CB  1 
ATOM   560  C  CG  . LEU A  1 69  ? 2.276   4.933   19.048  1.00 23.79  ? 318  LEU A CG  1 
ATOM   561  C  CD1 . LEU A  1 69  ? 2.071   6.418   19.283  1.00 25.82  ? 318  LEU A CD1 1 
ATOM   562  C  CD2 . LEU A  1 69  ? 3.159   4.317   20.122  1.00 24.01  ? 318  LEU A CD2 1 
ATOM   563  N  N   . SER A  1 70  ? 1.370   5.174   15.716  1.00 22.49  ? 319  SER A N   1 
ATOM   564  C  CA  . SER A  1 70  ? 2.043   4.969   14.424  1.00 25.69  ? 319  SER A CA  1 
ATOM   565  C  C   . SER A  1 70  ? 3.004   6.071   14.049  1.00 25.74  ? 319  SER A C   1 
ATOM   566  O  O   . SER A  1 70  ? 3.025   7.154   14.651  1.00 24.68  ? 319  SER A O   1 
ATOM   567  C  CB  . SER A  1 70  ? 1.029   4.795   13.240  1.00 27.43  ? 319  SER A CB  1 
ATOM   568  O  OG  . SER A  1 70  ? 0.691   6.045   12.696  1.00 29.05  ? 319  SER A OG  1 
ATOM   569  N  N   . ASP A  1 71  ? 3.833   5.756   13.054  1.00 26.19  ? 320  ASP A N   1 
ATOM   570  C  CA  . ASP A  1 71  ? 4.796   6.708   12.509  1.00 26.06  ? 320  ASP A CA  1 
ATOM   571  C  C   . ASP A  1 71  ? 4.749   6.591   11.007  1.00 29.97  ? 320  ASP A C   1 
ATOM   572  O  O   . ASP A  1 71  ? 5.724   6.874   10.295  1.00 26.03  ? 320  ASP A O   1 
ATOM   573  C  CB  . ASP A  1 71  ? 6.234   6.549   13.135  1.00 26.02  ? 320  ASP A CB  1 
ATOM   574  C  CG  . ASP A  1 71  ? 7.091   5.435   12.472  1.00 27.61  ? 320  ASP A CG  1 
ATOM   575  O  OD1 . ASP A  1 71  ? 6.508   4.586   11.783  1.00 29.26  ? 320  ASP A OD1 1 
ATOM   576  O  OD2 . ASP A  1 71  ? 8.353   5.383   12.634  1.00 27.75  ? 320  ASP A OD2 1 
ATOM   577  N  N   . LEU A  1 72  ? 3.562   6.189   10.545  1.00 32.94  ? 321  LEU A N   1 
ATOM   578  C  CA  . LEU A  1 72  ? 3.226   6.139   9.150   1.00 32.82  ? 321  LEU A CA  1 
ATOM   579  C  C   . LEU A  1 72  ? 3.397   7.524   8.510   1.00 37.40  ? 321  LEU A C   1 
ATOM   580  O  O   . LEU A  1 72  ? 3.895   7.641   7.384   1.00 35.52  ? 321  LEU A O   1 
ATOM   581  C  CB  . LEU A  1 72  ? 1.762   5.752   8.983   1.00 30.87  ? 321  LEU A CB  1 
ATOM   582  C  CG  . LEU A  1 72  ? 1.383   4.287   8.963   1.00 30.75  ? 321  LEU A CG  1 
ATOM   583  C  CD1 . LEU A  1 72  ? -0.124  4.159   9.058   1.00 30.74  ? 321  LEU A CD1 1 
ATOM   584  C  CD2 . LEU A  1 72  ? 1.911   3.632   7.711   1.00 32.00  ? 321  LEU A CD2 1 
ATOM   585  N  N   . ASN A  1 73  ? 2.934   8.567   9.181   1.00 33.78  ? 322  ASN A N   1 
ATOM   586  C  CA  A ASN A  1 73  ? 2.939   9.886   8.564   0.70 37.22  ? 322  ASN A CA  1 
ATOM   587  C  CA  B ASN A  1 73  ? 2.937   9.868   8.538   0.30 35.94  ? 322  ASN A CA  1 
ATOM   588  C  C   . ASN A  1 73  ? 4.375   10.357  8.374   1.00 36.55  ? 322  ASN A C   1 
ATOM   589  O  O   . ASN A  1 73  ? 4.754   10.781  7.310   1.00 36.68  ? 322  ASN A O   1 
ATOM   590  C  CB  A ASN A  1 73  ? 2.154   10.910  9.392   0.70 35.71  ? 322  ASN A CB  1 
ATOM   591  C  CB  B ASN A  1 73  ? 2.035   10.862  9.273   0.30 34.71  ? 322  ASN A CB  1 
ATOM   592  C  CG  A ASN A  1 73  ? 1.991   12.238  8.671   0.70 37.60  ? 322  ASN A CG  1 
ATOM   593  C  CG  B ASN A  1 73  ? 0.563   10.623  8.978   0.30 34.84  ? 322  ASN A CG  1 
ATOM   594  O  OD1 A ASN A  1 73  ? 2.233   13.314  9.243   0.70 40.24  ? 322  ASN A OD1 1 
ATOM   595  O  OD1 B ASN A  1 73  ? 0.208   9.684   8.263   0.30 34.80  ? 322  ASN A OD1 1 
ATOM   596  N  ND2 A ASN A  1 73  ? 1.564   12.176  7.410   0.70 37.24  ? 322  ASN A ND2 1 
ATOM   597  N  ND2 B ASN A  1 73  ? -0.300  11.468  9.523   0.30 35.29  ? 322  ASN A ND2 1 
ATOM   598  N  N   . GLN A  1 74  ? 5.176   10.259  9.419   1.00 37.01  ? 323  GLN A N   1 
ATOM   599  C  CA  . GLN A  1 74  ? 6.550   10.726  9.338   1.00 39.77  ? 323  GLN A CA  1 
ATOM   600  C  C   . GLN A  1 74  ? 7.416   9.787   10.140  1.00 35.92  ? 323  GLN A C   1 
ATOM   601  O  O   . GLN A  1 74  ? 7.265   9.656   11.384  1.00 36.23  ? 323  GLN A O   1 
ATOM   602  C  CB  . GLN A  1 74  ? 6.679   12.174  9.851   1.00 39.80  ? 323  GLN A CB  1 
ATOM   603  C  CG  . GLN A  1 74  ? 8.112   12.726  9.957   1.00 45.23  ? 323  GLN A CG  1 
ATOM   604  C  CD  . GLN A  1 74  ? 8.947   12.659  8.656   1.00 54.46  ? 323  GLN A CD  1 
ATOM   605  O  OE1 . GLN A  1 74  ? 8.503   13.075  7.563   1.00 55.98  ? 323  GLN A OE1 1 
ATOM   606  N  NE2 . GLN A  1 74  ? 10.180  12.141  8.782   1.00 55.90  ? 323  GLN A NE2 1 
ATOM   607  N  N   . GLU A  1 75  ? 8.318   9.131   9.420   1.00 33.86  ? 324  GLU A N   1 
ATOM   608  C  CA  . GLU A  1 75  ? 9.173   8.095   10.000  1.00 34.14  ? 324  GLU A CA  1 
ATOM   609  C  C   . GLU A  1 75  ? 9.929   8.624   11.205  1.00 32.87  ? 324  GLU A C   1 
ATOM   610  O  O   . GLU A  1 75  ? 10.573  9.641   11.138  1.00 35.72  ? 324  GLU A O   1 
ATOM   611  C  CB  . GLU A  1 75  ? 10.139  7.538   8.940   1.00 32.55  ? 324  GLU A CB  1 
ATOM   612  C  CG  . GLU A  1 75  ? 11.029  6.402   9.458   1.00 34.25  ? 324  GLU A CG  1 
ATOM   613  C  CD  . GLU A  1 75  ? 10.261  5.235   10.074  1.00 32.57  ? 324  GLU A CD  1 
ATOM   614  O  OE1 . GLU A  1 75  ? 9.183   4.863   9.542   1.00 34.72  ? 324  GLU A OE1 1 
ATOM   615  O  OE2 . GLU A  1 75  ? 10.763  4.661   11.067  1.00 30.84  ? 324  GLU A OE2 1 
ATOM   616  N  N   . GLY A  1 76  ? 9.826   7.948   12.331  1.00 32.56  ? 325  GLY A N   1 
ATOM   617  C  CA  . GLY A  1 76  ? 10.486  8.431   13.524  1.00 30.65  ? 325  GLY A CA  1 
ATOM   618  C  C   . GLY A  1 76  ? 9.618   9.314   14.398  1.00 32.46  ? 325  GLY A C   1 
ATOM   619  O  O   . GLY A  1 76  ? 9.947   9.558   15.562  1.00 38.18  ? 325  GLY A O   1 
ATOM   620  N  N   . THR A  1 77  ? 8.504   9.791   13.877  1.00 30.76  ? 326  THR A N   1 
ATOM   621  C  CA  . THR A  1 77  ? 7.627   10.575  14.701  1.00 32.35  ? 326  THR A CA  1 
ATOM   622  C  C   . THR A  1 77  ? 6.427   9.740   15.062  1.00 30.35  ? 326  THR A C   1 
ATOM   623  O  O   . THR A  1 77  ? 5.517   9.532   14.243  1.00 29.84  ? 326  THR A O   1 
ATOM   624  C  CB  . THR A  1 77  ? 7.132   11.866  13.997  1.00 35.16  ? 326  THR A CB  1 
ATOM   625  O  OG1 . THR A  1 77  ? 8.252   12.687  13.651  1.00 38.50  ? 326  THR A OG1 1 
ATOM   626  C  CG2 . THR A  1 77  ? 6.205   12.643  14.924  1.00 33.60  ? 326  THR A CG2 1 
ATOM   627  N  N   . TRP A  1 78  ? 6.405   9.307   16.310  1.00 31.85  ? 327  TRP A N   1 
ATOM   628  C  CA  . TRP A  1 78  ? 5.323   8.466   16.798  1.00 32.65  ? 327  TRP A CA  1 
ATOM   629  C  C   . TRP A  1 78  ? 4.175   9.313   17.297  1.00 31.86  ? 327  TRP A C   1 
ATOM   630  O  O   . TRP A  1 78  ? 4.314   10.148  18.158  1.00 30.88  ? 327  TRP A O   1 
ATOM   631  C  CB  . TRP A  1 78  ? 5.831   7.489   17.831  1.00 32.50  ? 327  TRP A CB  1 
ATOM   632  C  CG  . TRP A  1 78  ? 6.648   6.488   17.138  1.00 31.18  ? 327  TRP A CG  1 
ATOM   633  C  CD1 . TRP A  1 78  ? 7.966   6.588   16.830  1.00 32.42  ? 327  TRP A CD1 1 
ATOM   634  C  CD2 . TRP A  1 78  ? 6.192   5.263   16.577  1.00 30.50  ? 327  TRP A CD2 1 
ATOM   635  N  NE1 . TRP A  1 78  ? 8.371   5.475   16.129  1.00 33.28  ? 327  TRP A NE1 1 
ATOM   636  C  CE2 . TRP A  1 78  ? 7.288   4.660   15.943  1.00 31.91  ? 327  TRP A CE2 1 
ATOM   637  C  CE3 . TRP A  1 78  ? 4.965   4.610   16.548  1.00 27.58  ? 327  TRP A CE3 1 
ATOM   638  C  CZ2 . TRP A  1 78  ? 7.183   3.447   15.311  1.00 31.93  ? 327  TRP A CZ2 1 
ATOM   639  C  CZ3 . TRP A  1 78  ? 4.868   3.418   15.917  1.00 26.77  ? 327  TRP A CZ3 1 
ATOM   640  C  CH2 . TRP A  1 78  ? 5.957   2.832   15.340  1.00 29.27  ? 327  TRP A CH2 1 
ATOM   641  N  N   . GLN A  1 79  ? 3.021   9.050   16.729  1.00 33.54  ? 328  GLN A N   1 
ATOM   642  C  CA  . GLN A  1 79  ? 1.872   9.885   16.937  1.00 34.00  ? 328  GLN A CA  1 
ATOM   643  C  C   . GLN A  1 79  ? 0.685   8.968   17.233  1.00 28.24  ? 328  GLN A C   1 
ATOM   644  O  O   . GLN A  1 79  ? 0.487   8.012   16.529  1.00 26.63  ? 328  GLN A O   1 
ATOM   645  C  CB  . GLN A  1 79  ? 1.665   10.675  15.662  1.00 32.99  ? 328  GLN A CB  1 
ATOM   646  C  CG  . GLN A  1 79  ? 0.661   11.796  15.798  1.00 39.80  ? 328  GLN A CG  1 
ATOM   647  C  CD  . GLN A  1 79  ? 0.570   12.638  14.546  1.00 41.24  ? 328  GLN A CD  1 
ATOM   648  O  OE1 . GLN A  1 79  ? 1.425   12.544  13.657  1.00 42.54  ? 328  GLN A OE1 1 
ATOM   649  N  NE2 . GLN A  1 79  ? -0.468  13.459  14.467  1.00 47.89  ? 328  GLN A NE2 1 
ATOM   650  N  N   . TRP A  1 80  ? -0.055  9.233   18.302  1.00 28.72  ? 329  TRP A N   1 
ATOM   651  C  CA  . TRP A  1 80  ? -1.311  8.502   18.598  1.00 26.90  ? 329  TRP A CA  1 
ATOM   652  C  C   . TRP A  1 80  ? -2.369  8.884   17.540  1.00 27.08  ? 329  TRP A C   1 
ATOM   653  O  O   . TRP A  1 80  ? -2.288  9.946   16.956  1.00 23.80  ? 329  TRP A O   1 
ATOM   654  C  CB  . TRP A  1 80  ? -1.837  8.848   19.992  1.00 27.89  ? 329  TRP A CB  1 
ATOM   655  C  CG  . TRP A  1 80  ? -0.900  8.490   21.057  1.00 29.95  ? 329  TRP A CG  1 
ATOM   656  C  CD1 . TRP A  1 80  ? -0.069  9.324   21.707  1.00 31.12  ? 329  TRP A CD1 1 
ATOM   657  C  CD2 . TRP A  1 80  ? -0.684  7.187   21.619  1.00 30.62  ? 329  TRP A CD2 1 
ATOM   658  N  NE1 . TRP A  1 80  ? 0.678   8.635   22.614  1.00 31.52  ? 329  TRP A NE1 1 
ATOM   659  C  CE2 . TRP A  1 80  ? 0.306   7.321   22.598  1.00 30.50  ? 329  TRP A CE2 1 
ATOM   660  C  CE3 . TRP A  1 80  ? -1.238  5.931   21.391  1.00 31.30  ? 329  TRP A CE3 1 
ATOM   661  C  CZ2 . TRP A  1 80  ? 0.771   6.245   23.354  1.00 30.08  ? 329  TRP A CZ2 1 
ATOM   662  C  CZ3 . TRP A  1 80  ? -0.772  4.854   22.137  1.00 32.00  ? 329  TRP A CZ3 1 
ATOM   663  C  CH2 . TRP A  1 80  ? 0.226   5.022   23.104  1.00 31.88  ? 329  TRP A CH2 1 
ATOM   664  N  N   . VAL A  1 81  ? -3.338  8.013   17.291  1.00 25.07  ? 330  VAL A N   1 
ATOM   665  C  CA  . VAL A  1 81  ? -4.370  8.307   16.341  1.00 26.48  ? 330  VAL A CA  1 
ATOM   666  C  C   . VAL A  1 81  ? -5.276  9.491   16.709  1.00 30.45  ? 330  VAL A C   1 
ATOM   667  O  O   . VAL A  1 81  ? -6.087  9.899   15.875  1.00 33.56  ? 330  VAL A O   1 
ATOM   668  C  CB  . VAL A  1 81  ? -5.293  7.097   16.069  1.00 27.23  ? 330  VAL A CB  1 
ATOM   669  C  CG1 . VAL A  1 81  ? -4.513  5.913   15.532  1.00 28.23  ? 330  VAL A CG1 1 
ATOM   670  C  CG2 . VAL A  1 81  ? -6.096  6.714   17.316  1.00 25.81  ? 330  VAL A CG2 1 
ATOM   671  N  N   . ASP A  1 82  ? -5.182  10.022  17.927  1.00 29.93  ? 331  ASP A N   1 
ATOM   672  C  CA  . ASP A  1 82  ? -5.928  11.222  18.265  1.00 32.07  ? 331  ASP A CA  1 
ATOM   673  C  C   . ASP A  1 82  ? -5.135  12.476  17.964  1.00 36.44  ? 331  ASP A C   1 
ATOM   674  O  O   . ASP A  1 82  ? -5.525  13.571  18.379  1.00 39.43  ? 331  ASP A O   1 
ATOM   675  C  CB  . ASP A  1 82  ? -6.430  11.215  19.732  1.00 31.95  ? 331  ASP A CB  1 
ATOM   676  C  CG  . ASP A  1 82  ? -5.325  11.368  20.744  1.00 32.55  ? 331  ASP A CG  1 
ATOM   677  O  OD1 . ASP A  1 82  ? -4.133  11.447  20.370  1.00 35.35  ? 331  ASP A OD1 1 
ATOM   678  O  OD2 . ASP A  1 82  ? -5.649  11.423  21.944  1.00 32.93  ? 331  ASP A OD2 1 
ATOM   679  N  N   . GLY A  1 83  ? -4.031  12.334  17.239  1.00 34.63  ? 332  GLY A N   1 
ATOM   680  C  CA  . GLY A  1 83  ? -3.224  13.474  16.848  1.00 34.31  ? 332  GLY A CA  1 
ATOM   681  C  C   . GLY A  1 83  ? -2.090  13.804  17.800  1.00 35.59  ? 332  GLY A C   1 
ATOM   682  O  O   . GLY A  1 83  ? -1.154  14.491  17.434  1.00 36.92  ? 332  GLY A O   1 
ATOM   683  N  N   . SER A  1 84  ? -2.161  13.339  19.034  1.00 36.02  ? 333  SER A N   1 
ATOM   684  C  CA  . SER A  1 84  ? -1.175  13.734  20.019  1.00 35.29  ? 333  SER A CA  1 
ATOM   685  C  C   . SER A  1 84  ? 0.130   12.941  19.821  1.00 34.49  ? 333  SER A C   1 
ATOM   686  O  O   . SER A  1 84  ? 0.119   11.805  19.354  1.00 31.29  ? 333  SER A O   1 
ATOM   687  C  CB  . SER A  1 84  ? -1.740  13.536  21.430  1.00 37.40  ? 333  SER A CB  1 
ATOM   688  O  OG  . SER A  1 84  ? -1.780  12.164  21.758  1.00 40.84  ? 333  SER A OG  1 
ATOM   689  N  N   . PRO A  1 85  ? 1.264   13.562  20.145  1.00 36.10  ? 334  PRO A N   1 
ATOM   690  C  CA  . PRO A  1 85  ? 2.561   12.923  20.027  1.00 34.15  ? 334  PRO A CA  1 
ATOM   691  C  C   . PRO A  1 85  ? 2.924   12.046  21.216  1.00 34.50  ? 334  PRO A C   1 
ATOM   692  O  O   . PRO A  1 85  ? 2.411   12.215  22.321  1.00 32.77  ? 334  PRO A O   1 
ATOM   693  C  CB  . PRO A  1 85  ? 3.524   14.103  19.938  1.00 36.53  ? 334  PRO A CB  1 
ATOM   694  C  CG  . PRO A  1 85  ? 2.827   15.214  20.656  1.00 36.50  ? 334  PRO A CG  1 
ATOM   695  C  CD  . PRO A  1 85  ? 1.377   15.014  20.390  1.00 34.73  ? 334  PRO A CD  1 
ATOM   696  N  N   . LEU A  1 86  ? 3.801   11.091  20.971  1.00 33.22  ? 335  LEU A N   1 
ATOM   697  C  CA  . LEU A  1 86  ? 4.258   10.225  22.029  1.00 33.90  ? 335  LEU A CA  1 
ATOM   698  C  C   . LEU A  1 86  ? 5.108   11.011  23.002  1.00 32.89  ? 335  LEU A C   1 
ATOM   699  O  O   . LEU A  1 86  ? 6.194   11.465  22.650  1.00 31.59  ? 335  LEU A O   1 
ATOM   700  C  CB  . LEU A  1 86  ? 5.072   9.070   21.467  1.00 31.89  ? 335  LEU A CB  1 
ATOM   701  C  CG  . LEU A  1 86  ? 5.508   8.008   22.455  1.00 33.24  ? 335  LEU A CG  1 
ATOM   702  C  CD1 . LEU A  1 86  ? 4.326   7.367   23.160  1.00 32.93  ? 335  LEU A CD1 1 
ATOM   703  C  CD2 . LEU A  1 86  ? 6.310   6.963   21.687  1.00 33.08  ? 335  LEU A CD2 1 
ATOM   704  N  N   . LEU A  1 87  ? 4.631   11.126  24.238  1.00 32.84  ? 336  LEU A N   1 
ATOM   705  C  CA  . LEU A  1 87  ? 5.374   11.835  25.268  1.00 33.89  ? 336  LEU A CA  1 
ATOM   706  C  C   . LEU A  1 87  ? 6.664   11.118  25.619  1.00 34.10  ? 336  LEU A C   1 
ATOM   707  O  O   . LEU A  1 87  ? 6.688   9.883   25.650  1.00 33.75  ? 336  LEU A O   1 
ATOM   708  C  CB  . LEU A  1 87  ? 4.530   11.978  26.539  1.00 35.47  ? 336  LEU A CB  1 
ATOM   709  C  CG  . LEU A  1 87  ? 3.207   12.728  26.427  1.00 37.74  ? 336  LEU A CG  1 
ATOM   710  C  CD1 . LEU A  1 87  ? 2.496   12.758  27.774  1.00 37.38  ? 336  LEU A CD1 1 
ATOM   711  C  CD2 . LEU A  1 87  ? 3.428   14.148  25.930  1.00 41.30  ? 336  LEU A CD2 1 
ATOM   712  N  N   . PRO A  1 88  ? 7.740   11.883  25.912  1.00 36.74  ? 337  PRO A N   1 
ATOM   713  C  CA  . PRO A  1 88  ? 8.995   11.308  26.395  1.00 36.93  ? 337  PRO A CA  1 
ATOM   714  C  C   . PRO A  1 88  ? 8.862   10.352  27.571  1.00 36.19  ? 337  PRO A C   1 
ATOM   715  O  O   . PRO A  1 88  ? 9.522   9.335   27.599  1.00 35.14  ? 337  PRO A O   1 
ATOM   716  C  CB  . PRO A  1 88  ? 9.781   12.529  26.827  1.00 39.27  ? 337  PRO A CB  1 
ATOM   717  C  CG  . PRO A  1 88  ? 9.305   13.601  25.912  1.00 39.96  ? 337  PRO A CG  1 
ATOM   718  C  CD  . PRO A  1 88  ? 7.838   13.349  25.779  1.00 37.98  ? 337  PRO A CD  1 
ATOM   719  N  N   . SER A  1 89  ? 8.010   10.654  28.542  1.00 37.99  ? 338  SER A N   1 
ATOM   720  C  CA  . SER A  1 89  ? 7.845   9.740   29.660  1.00 39.19  ? 338  SER A CA  1 
ATOM   721  C  C   . SER A  1 89  ? 7.353   8.339   29.267  1.00 43.12  ? 338  SER A C   1 
ATOM   722  O  O   . SER A  1 89  ? 7.443   7.414   30.093  1.00 47.05  ? 338  SER A O   1 
ATOM   723  C  CB  . SER A  1 89  ? 6.866   10.314  30.663  1.00 39.51  ? 338  SER A CB  1 
ATOM   724  O  OG  . SER A  1 89  ? 5.595   10.410  30.052  1.00 42.42  ? 338  SER A OG  1 
ATOM   725  N  N   . PHE A  1 90  ? 6.817   8.184   28.050  1.00 40.15  ? 339  PHE A N   1 
ATOM   726  C  CA  . PHE A  1 90  ? 6.286   6.887   27.595  1.00 41.16  ? 339  PHE A CA  1 
ATOM   727  C  C   . PHE A  1 90  ? 7.264   6.029   26.795  1.00 39.17  ? 339  PHE A C   1 
ATOM   728  O  O   . PHE A  1 90  ? 7.052   4.811   26.638  1.00 40.08  ? 339  PHE A O   1 
ATOM   729  C  CB  . PHE A  1 90  ? 5.018   7.070   26.778  1.00 39.26  ? 339  PHE A CB  1 
ATOM   730  C  CG  . PHE A  1 90  ? 3.804   7.309   27.604  1.00 43.80  ? 339  PHE A CG  1 
ATOM   731  C  CD1 . PHE A  1 90  ? 3.598   8.543   28.208  1.00 50.03  ? 339  PHE A CD1 1 
ATOM   732  C  CD2 . PHE A  1 90  ? 2.854   6.319   27.775  1.00 44.79  ? 339  PHE A CD2 1 
ATOM   733  C  CE1 . PHE A  1 90  ? 2.471   8.788   28.984  1.00 51.20  ? 339  PHE A CE1 1 
ATOM   734  C  CE2 . PHE A  1 90  ? 1.720   6.551   28.540  1.00 48.23  ? 339  PHE A CE2 1 
ATOM   735  C  CZ  . PHE A  1 90  ? 1.528   7.786   29.156  1.00 49.99  ? 339  PHE A CZ  1 
ATOM   736  N  N   . LYS A  1 91  ? 8.344   6.639   26.316  1.00 37.06  ? 340  LYS A N   1 
ATOM   737  C  CA  . LYS A  1 91  ? 9.313   5.926   25.494  1.00 37.81  ? 340  LYS A CA  1 
ATOM   738  C  C   . LYS A  1 91  ? 9.956   4.757   26.258  1.00 33.73  ? 340  LYS A C   1 
ATOM   739  O  O   . LYS A  1 91  ? 10.468  3.819   25.671  1.00 36.80  ? 340  LYS A O   1 
ATOM   740  C  CB  . LYS A  1 91  ? 10.356  6.900   24.942  1.00 39.12  ? 340  LYS A CB  1 
ATOM   741  C  CG  . LYS A  1 91  ? 9.788   7.876   23.901  1.00 42.86  ? 340  LYS A CG  1 
ATOM   742  C  CD  . LYS A  1 91  ? 10.778  9.002   23.572  1.00 46.82  ? 340  LYS A CD  1 
ATOM   743  C  CE  . LYS A  1 91  ? 10.500  9.710   22.229  1.00 49.56  ? 340  LYS A CE  1 
ATOM   744  N  NZ  . LYS A  1 91  ? 9.309   10.600  22.275  1.00 50.88  ? 340  LYS A NZ  1 
ATOM   745  N  N   . GLN A  1 92  ? 9.883   4.798   27.575  1.00 33.30  ? 341  GLN A N   1 
ATOM   746  C  CA  . GLN A  1 92  ? 10.377  3.711   28.394  1.00 34.31  ? 341  GLN A CA  1 
ATOM   747  C  C   . GLN A  1 92  ? 9.669   2.377   28.093  1.00 33.94  ? 341  GLN A C   1 
ATOM   748  O  O   . GLN A  1 92  ? 10.255  1.297   28.267  1.00 35.03  ? 341  GLN A O   1 
ATOM   749  C  CB  . GLN A  1 92  ? 10.250  4.078   29.884  1.00 35.12  ? 341  GLN A CB  1 
ATOM   750  C  CG  . GLN A  1 92  ? 8.826   4.266   30.371  1.00 37.80  ? 341  GLN A CG  1 
ATOM   751  C  CD  . GLN A  1 92  ? 8.727   4.544   31.868  1.00 40.83  ? 341  GLN A CD  1 
ATOM   752  O  OE1 . GLN A  1 92  ? 8.506   5.679   32.294  1.00 41.89  ? 341  GLN A OE1 1 
ATOM   753  N  NE2 . GLN A  1 92  ? 8.844   3.498   32.664  1.00 43.30  ? 341  GLN A NE2 1 
ATOM   754  N  N   . TYR A  1 93  ? 8.415   2.447   27.646  1.00 32.43  ? 342  TYR A N   1 
ATOM   755  C  CA  . TYR A  1 93  ? 7.655   1.225   27.390  1.00 31.23  ? 342  TYR A CA  1 
ATOM   756  C  C   . TYR A  1 93  ? 8.035   0.457   26.131  1.00 29.28  ? 342  TYR A C   1 
ATOM   757  O  O   . TYR A  1 93  ? 7.667   -0.698  25.985  1.00 29.54  ? 342  TYR A O   1 
ATOM   758  C  CB  . TYR A  1 93  ? 6.188   1.523   27.364  1.00 31.51  ? 342  TYR A CB  1 
ATOM   759  C  CG  . TYR A  1 93  ? 5.709   2.140   28.645  1.00 34.62  ? 342  TYR A CG  1 
ATOM   760  C  CD1 . TYR A  1 93  ? 5.901   1.488   29.876  1.00 32.77  ? 342  TYR A CD1 1 
ATOM   761  C  CD2 . TYR A  1 93  ? 5.062   3.386   28.629  1.00 31.71  ? 342  TYR A CD2 1 
ATOM   762  C  CE1 . TYR A  1 93  ? 5.440   2.053   31.044  1.00 33.45  ? 342  TYR A CE1 1 
ATOM   763  C  CE2 . TYR A  1 93  ? 4.603   3.946   29.781  1.00 33.54  ? 342  TYR A CE2 1 
ATOM   764  C  CZ  . TYR A  1 93  ? 4.795   3.289   30.985  1.00 34.26  ? 342  TYR A CZ  1 
ATOM   765  O  OH  . TYR A  1 93  ? 4.309   3.890   32.118  1.00 35.24  ? 342  TYR A OH  1 
ATOM   766  N  N   . TRP A  1 94  ? 8.784   1.065   25.229  1.00 29.11  ? 343  TRP A N   1 
ATOM   767  C  CA  . TRP A  1 94  ? 9.329   0.309   24.122  1.00 29.35  ? 343  TRP A CA  1 
ATOM   768  C  C   . TRP A  1 94  ? 10.101  -0.909  24.661  1.00 32.48  ? 343  TRP A C   1 
ATOM   769  O  O   . TRP A  1 94  ? 10.809  -0.813  25.667  1.00 36.88  ? 343  TRP A O   1 
ATOM   770  C  CB  . TRP A  1 94  ? 10.247  1.179   23.251  1.00 28.88  ? 343  TRP A CB  1 
ATOM   771  C  CG  . TRP A  1 94  ? 9.575   2.240   22.417  1.00 28.95  ? 343  TRP A CG  1 
ATOM   772  C  CD1 . TRP A  1 94  ? 9.753   3.594   22.542  1.00 28.48  ? 343  TRP A CD1 1 
ATOM   773  C  CD2 . TRP A  1 94  ? 8.643   2.059   21.302  1.00 29.47  ? 343  TRP A CD2 1 
ATOM   774  N  NE1 . TRP A  1 94  ? 8.963   4.263   21.636  1.00 29.35  ? 343  TRP A NE1 1 
ATOM   775  C  CE2 . TRP A  1 94  ? 8.290   3.354   20.846  1.00 30.28  ? 343  TRP A CE2 1 
ATOM   776  C  CE3 . TRP A  1 94  ? 8.069   0.939   20.667  1.00 28.96  ? 343  TRP A CE3 1 
ATOM   777  C  CZ2 . TRP A  1 94  ? 7.412   3.563   19.743  1.00 28.18  ? 343  TRP A CZ2 1 
ATOM   778  C  CZ3 . TRP A  1 94  ? 7.176   1.138   19.596  1.00 28.29  ? 343  TRP A CZ3 1 
ATOM   779  C  CH2 . TRP A  1 94  ? 6.854   2.452   19.141  1.00 27.61  ? 343  TRP A CH2 1 
ATOM   780  N  N   . ASN A  1 95  ? 9.979   -2.057  24.009  1.00 34.00  ? 344  ASN A N   1 
ATOM   781  C  CA  . ASN A  1 95  ? 10.904  -3.152  24.300  1.00 34.34  ? 344  ASN A CA  1 
ATOM   782  C  C   . ASN A  1 95  ? 12.314  -2.685  23.983  1.00 35.24  ? 344  ASN A C   1 
ATOM   783  O  O   . ASN A  1 95  ? 12.517  -1.730  23.220  1.00 32.68  ? 344  ASN A O   1 
ATOM   784  C  CB  . ASN A  1 95  ? 10.601  -4.411  23.486  1.00 32.97  ? 344  ASN A CB  1 
ATOM   785  C  CG  . ASN A  1 95  ? 9.295   -5.080  23.898  1.00 34.67  ? 344  ASN A CG  1 
ATOM   786  O  OD1 . ASN A  1 95  ? 8.873   -4.988  25.044  1.00 32.00  ? 344  ASN A OD1 1 
ATOM   787  N  ND2 . ASN A  1 95  ? 8.663   -5.766  22.965  1.00 31.86  ? 344  ASN A ND2 1 
ATOM   788  N  N   . ARG A  1 96  ? 13.284  -3.374  24.569  1.00 39.92  ? 345  ARG A N   1 
ATOM   789  C  CA  . ARG A  1 96  ? 14.702  -3.054  24.356  1.00 44.76  ? 345  ARG A CA  1 
ATOM   790  C  C   . ARG A  1 96  ? 15.038  -3.128  22.863  1.00 39.58  ? 345  ARG A C   1 
ATOM   791  O  O   . ARG A  1 96  ? 14.618  -4.042  22.172  1.00 40.84  ? 345  ARG A O   1 
ATOM   792  C  CB  . ARG A  1 96  ? 15.594  -3.982  25.204  1.00 52.60  ? 345  ARG A CB  1 
ATOM   793  C  CG  . ARG A  1 96  ? 16.983  -3.434  25.516  1.00 66.17  ? 345  ARG A CG  1 
ATOM   794  C  CD  . ARG A  1 96  ? 17.820  -4.391  26.378  1.00 81.64  ? 345  ARG A CD  1 
ATOM   795  N  NE  . ARG A  1 96  ? 18.360  -5.531  25.617  1.00 90.32  ? 345  ARG A NE  1 
ATOM   796  C  CZ  . ARG A  1 96  ? 17.785  -6.736  25.504  1.00 97.71  ? 345  ARG A CZ  1 
ATOM   797  N  NH1 . ARG A  1 96  ? 16.628  -7.022  26.108  1.00 95.44  ? 345  ARG A NH1 1 
ATOM   798  N  NH2 . ARG A  1 96  ? 18.380  -7.674  24.771  1.00 98.89  ? 345  ARG A NH2 1 
ATOM   799  N  N   . GLY A  1 97  ? 15.754  -2.133  22.358  1.00 36.03  ? 346  GLY A N   1 
ATOM   800  C  CA  . GLY A  1 97  ? 16.084  -2.052  20.914  1.00 34.85  ? 346  GLY A CA  1 
ATOM   801  C  C   . GLY A  1 97  ? 14.973  -1.509  20.017  1.00 37.92  ? 346  GLY A C   1 
ATOM   802  O  O   . GLY A  1 97  ? 15.172  -1.368  18.807  1.00 36.39  ? 346  GLY A O   1 
ATOM   803  N  N   . GLU A  1 98  ? 13.797  -1.232  20.584  1.00 32.53  ? 347  GLU A N   1 
ATOM   804  C  CA  . GLU A  1 98  ? 12.683  -0.771  19.779  1.00 36.19  ? 347  GLU A CA  1 
ATOM   805  C  C   . GLU A  1 98  ? 12.436  0.725   20.052  1.00 33.13  ? 347  GLU A C   1 
ATOM   806  O  O   . GLU A  1 98  ? 12.773  1.191   21.137  1.00 34.23  ? 347  GLU A O   1 
ATOM   807  C  CB  . GLU A  1 98  ? 11.428  -1.610  20.067  1.00 33.97  ? 347  GLU A CB  1 
ATOM   808  C  CG  . GLU A  1 98  ? 11.633  -3.101  19.932  1.00 35.58  ? 347  GLU A CG  1 
ATOM   809  C  CD  . GLU A  1 98  ? 11.861  -3.597  18.506  1.00 38.49  ? 347  GLU A CD  1 
ATOM   810  O  OE1 . GLU A  1 98  ? 11.695  -2.806  17.514  1.00 34.71  ? 347  GLU A OE1 1 
ATOM   811  O  OE2 . GLU A  1 98  ? 12.160  -4.842  18.377  1.00 41.34  ? 347  GLU A OE2 1 
ATOM   812  N  N   . PRO A  1 99  ? 11.857  1.466   19.095  1.00 32.38  ? 348  PRO A N   1 
ATOM   813  C  CA  . PRO A  1 99  ? 11.393  0.931   17.805  1.00 31.62  ? 348  PRO A CA  1 
ATOM   814  C  C   . PRO A  1 99  ? 12.518  0.993   16.823  1.00 32.62  ? 348  PRO A C   1 
ATOM   815  O  O   . PRO A  1 99  ? 13.273  1.921   16.874  1.00 30.10  ? 348  PRO A O   1 
ATOM   816  C  CB  . PRO A  1 99  ? 10.358  1.953   17.366  1.00 30.96  ? 348  PRO A CB  1 
ATOM   817  C  CG  . PRO A  1 99  ? 10.843  3.276   17.960  1.00 32.27  ? 348  PRO A CG  1 
ATOM   818  C  CD  . PRO A  1 99  ? 11.721  2.947   19.141  1.00 32.65  ? 348  PRO A CD  1 
ATOM   819  N  N   . ASN A  1 100 ? 12.611  0.033   15.927  1.00 31.46  ? 349  ASN A N   1 
ATOM   820  C  CA  . ASN A  1 100 ? 13.804  -0.108  15.112  1.00 32.59  ? 349  ASN A CA  1 
ATOM   821  C  C   . ASN A  1 100 ? 13.495  -0.048  13.620  1.00 34.05  ? 349  ASN A C   1 
ATOM   822  O  O   . ASN A  1 100 ? 14.398  -0.093  12.823  1.00 35.30  ? 349  ASN A O   1 
ATOM   823  C  CB  . ASN A  1 100 ? 14.512  -1.433  15.477  1.00 31.86  ? 349  ASN A CB  1 
ATOM   824  C  CG  . ASN A  1 100 ? 13.635  -2.672  15.226  1.00 28.36  ? 349  ASN A CG  1 
ATOM   825  O  OD1 . ASN A  1 100 ? 12.491  -2.577  14.790  1.00 26.90  ? 349  ASN A OD1 1 
ATOM   826  N  ND2 . ASN A  1 100 ? 14.195  -3.828  15.468  1.00 28.01  ? 349  ASN A ND2 1 
ATOM   827  N  N   . ASN A  1 101 ? 12.211  0.031   13.262  1.00 34.15  ? 350  ASN A N   1 
ATOM   828  C  CA  . ASN A  1 101 ? 11.762  0.224   11.891  1.00 34.94  ? 350  ASN A CA  1 
ATOM   829  C  C   . ASN A  1 101 ? 12.264  -0.837  10.931  1.00 36.10  ? 350  ASN A C   1 
ATOM   830  O  O   . ASN A  1 101 ? 12.297  -0.605  9.717   1.00 32.31  ? 350  ASN A O   1 
ATOM   831  C  CB  . ASN A  1 101 ? 12.141  1.615   11.359  1.00 34.29  ? 350  ASN A CB  1 
ATOM   832  C  CG  . ASN A  1 101 ? 11.373  1.976   10.100  1.00 35.84  ? 350  ASN A CG  1 
ATOM   833  O  OD1 . ASN A  1 101 ? 10.168  1.739   9.985   1.00 35.87  ? 350  ASN A OD1 1 
ATOM   834  N  ND2 . ASN A  1 101 ? 12.068  2.544   9.137   1.00 37.31  ? 350  ASN A ND2 1 
ATOM   835  N  N   . VAL A  1 102 ? 12.599  -2.026  11.449  1.00 37.17  ? 351  VAL A N   1 
ATOM   836  C  CA  . VAL A  1 102 ? 13.209  -3.051  10.575  1.00 36.54  ? 351  VAL A CA  1 
ATOM   837  C  C   . VAL A  1 102 ? 12.215  -3.606  9.549   1.00 36.09  ? 351  VAL A C   1 
ATOM   838  O  O   . VAL A  1 102 ? 11.150  -4.151  9.892   1.00 34.70  ? 351  VAL A O   1 
ATOM   839  C  CB  . VAL A  1 102 ? 13.899  -4.157  11.378  1.00 37.68  ? 351  VAL A CB  1 
ATOM   840  C  CG1 . VAL A  1 102 ? 12.877  -5.049  12.113  1.00 40.14  ? 351  VAL A CG1 1 
ATOM   841  C  CG2 . VAL A  1 102 ? 14.805  -4.962  10.452  1.00 37.85  ? 351  VAL A CG2 1 
ATOM   842  N  N   . GLY A  1 103 ? 12.557  -3.452  8.276   1.00 34.78  ? 352  GLY A N   1 
ATOM   843  C  CA  . GLY A  1 103 ? 11.652  -3.841  7.205   1.00 35.78  ? 352  GLY A CA  1 
ATOM   844  C  C   . GLY A  1 103 ? 10.492  -2.876  6.993   1.00 38.04  ? 352  GLY A C   1 
ATOM   845  O  O   . GLY A  1 103 ? 9.484   -3.234  6.342   1.00 36.38  ? 352  GLY A O   1 
ATOM   846  N  N   . GLU A  1 104 ? 10.647  -1.656  7.532   1.00 38.32  ? 353  GLU A N   1 
ATOM   847  C  CA  . GLU A  1 104 ? 9.580   -0.658  7.602   1.00 36.33  ? 353  GLU A CA  1 
ATOM   848  C  C   . GLU A  1 104 ? 8.417   -1.097  8.471   1.00 33.28  ? 353  GLU A C   1 
ATOM   849  O  O   . GLU A  1 104 ? 7.511   -1.757  7.979   1.00 31.30  ? 353  GLU A O   1 
ATOM   850  C  CB  . GLU A  1 104 ? 9.118   -0.263  6.206   1.00 37.43  ? 353  GLU A CB  1 
ATOM   851  C  CG  . GLU A  1 104 ? 10.337  0.195   5.423   1.00 44.39  ? 353  GLU A CG  1 
ATOM   852  C  CD  . GLU A  1 104 ? 10.025  1.181   4.340   1.00 48.55  ? 353  GLU A CD  1 
ATOM   853  O  OE1 . GLU A  1 104 ? 8.914   1.117   3.772   1.00 51.91  ? 353  GLU A OE1 1 
ATOM   854  O  OE2 . GLU A  1 104 ? 10.899  2.031   4.073   1.00 59.01  ? 353  GLU A OE2 1 
ATOM   855  N  N   . GLU A  1 105 ? 8.461   -0.669  9.741   1.00 30.73  ? 354  GLU A N   1 
ATOM   856  C  CA  . GLU A  1 105 ? 7.472   -1.005  10.780  1.00 28.71  ? 354  GLU A CA  1 
ATOM   857  C  C   . GLU A  1 105 ? 6.989   0.335   11.292  1.00 25.26  ? 354  GLU A C   1 
ATOM   858  O  O   . GLU A  1 105 ? 7.713   1.034   11.975  1.00 23.98  ? 354  GLU A O   1 
ATOM   859  C  CB  . GLU A  1 105 ? 8.117   -1.806  11.924  1.00 29.70  ? 354  GLU A CB  1 
ATOM   860  C  CG  . GLU A  1 105 ? 8.748   -3.099  11.445  1.00 30.63  ? 354  GLU A CG  1 
ATOM   861  C  CD  . GLU A  1 105 ? 9.469   -3.861  12.506  1.00 32.81  ? 354  GLU A CD  1 
ATOM   862  O  OE1 . GLU A  1 105 ? 10.312  -3.258  13.249  1.00 32.52  ? 354  GLU A OE1 1 
ATOM   863  O  OE2 . GLU A  1 105 ? 9.216   -5.107  12.569  1.00 37.11  ? 354  GLU A OE2 1 
ATOM   864  N  N   . ASP A  1 106 ? 5.775   0.692   10.922  1.00 23.99  ? 355  ASP A N   1 
ATOM   865  C  CA  . ASP A  1 106 ? 5.188   1.956   11.305  1.00 24.77  ? 355  ASP A CA  1 
ATOM   866  C  C   . ASP A  1 106 ? 3.974   1.849   12.244  1.00 28.07  ? 355  ASP A C   1 
ATOM   867  O  O   . ASP A  1 106 ? 3.262   2.838   12.460  1.00 25.56  ? 355  ASP A O   1 
ATOM   868  C  CB  . ASP A  1 106 ? 4.792   2.712   10.057  1.00 24.05  ? 355  ASP A CB  1 
ATOM   869  C  CG  . ASP A  1 106 ? 5.993   3.000   9.157   1.00 22.15  ? 355  ASP A CG  1 
ATOM   870  O  OD1 . ASP A  1 106 ? 7.176   2.906   9.634   1.00 19.93  ? 355  ASP A OD1 1 
ATOM   871  O  OD2 . ASP A  1 106 ? 5.726   3.331   8.036   1.00 22.13  ? 355  ASP A OD2 1 
ATOM   872  N  N   . CYS A  1 107 ? 3.745   0.666   12.795  1.00 28.70  ? 356  CYS A N   1 
ATOM   873  C  CA  . CYS A  1 107 ? 2.600   0.485   13.698  1.00 29.44  ? 356  CYS A CA  1 
ATOM   874  C  C   . CYS A  1 107 ? 3.013   -0.172  14.993  1.00 28.28  ? 356  CYS A C   1 
ATOM   875  O  O   . CYS A  1 107 ? 3.848   -1.067  15.011  1.00 26.38  ? 356  CYS A O   1 
ATOM   876  C  CB  . CYS A  1 107 ? 1.526   -0.325  12.994  1.00 29.65  ? 356  CYS A CB  1 
ATOM   877  S  SG  . CYS A  1 107 ? 0.699   0.563   11.673  1.00 31.65  ? 356  CYS A SG  1 
ATOM   878  N  N   . ALA A  1 108 ? 2.438   0.302   16.089  1.00 28.96  ? 357  ALA A N   1 
ATOM   879  C  CA  . ALA A  1 108 ? 2.860   -0.116  17.410  1.00 28.94  ? 357  ALA A CA  1 
ATOM   880  C  C   . ALA A  1 108 ? 1.934   -1.191  17.956  1.00 26.86  ? 357  ALA A C   1 
ATOM   881  O  O   . ALA A  1 108 ? 0.730   -1.130  17.768  1.00 26.17  ? 357  ALA A O   1 
ATOM   882  C  CB  . ALA A  1 108 ? 2.931   1.064   18.365  1.00 29.29  ? 357  ALA A CB  1 
ATOM   883  N  N   . GLU A  1 109 ? 2.524   -2.171  18.627  1.00 26.65  ? 358  GLU A N   1 
ATOM   884  C  CA  . GLU A  1 109 ? 1.809   -3.308  19.157  1.00 25.47  ? 358  GLU A CA  1 
ATOM   885  C  C   . GLU A  1 109 ? 2.280   -3.597  20.569  1.00 24.90  ? 358  GLU A C   1 
ATOM   886  O  O   . GLU A  1 109 ? 3.425   -3.331  20.943  1.00 25.18  ? 358  GLU A O   1 
ATOM   887  C  CB  . GLU A  1 109 ? 2.050   -4.553  18.283  1.00 27.54  ? 358  GLU A CB  1 
ATOM   888  C  CG  . GLU A  1 109 ? 3.508   -5.020  18.351  1.00 30.28  ? 358  GLU A CG  1 
ATOM   889  C  CD  . GLU A  1 109 ? 3.797   -6.437  17.877  1.00 30.18  ? 358  GLU A CD  1 
ATOM   890  O  OE1 . GLU A  1 109 ? 5.002   -6.722  17.694  1.00 31.28  ? 358  GLU A OE1 1 
ATOM   891  O  OE2 . GLU A  1 109 ? 2.880   -7.274  17.725  1.00 29.53  ? 358  GLU A OE2 1 
ATOM   892  N  N   . PHE A  1 110 ? 1.409   -4.202  21.358  1.00 23.89  ? 359  PHE A N   1 
ATOM   893  C  CA  . PHE A  1 110 ? 1.824   -4.795  22.587  1.00 22.99  ? 359  PHE A CA  1 
ATOM   894  C  C   . PHE A  1 110 ? 2.467   -6.124  22.267  1.00 25.22  ? 359  PHE A C   1 
ATOM   895  O  O   . PHE A  1 110 ? 1.846   -6.983  21.625  1.00 26.29  ? 359  PHE A O   1 
ATOM   896  C  CB  . PHE A  1 110 ? 0.609   -5.040  23.479  1.00 22.54  ? 359  PHE A CB  1 
ATOM   897  C  CG  . PHE A  1 110 ? -0.107  -3.791  23.879  1.00 21.13  ? 359  PHE A CG  1 
ATOM   898  C  CD1 . PHE A  1 110 ? 0.362   -3.005  24.895  1.00 23.40  ? 359  PHE A CD1 1 
ATOM   899  C  CD2 . PHE A  1 110 ? -1.220  -3.373  23.190  1.00 22.72  ? 359  PHE A CD2 1 
ATOM   900  C  CE1 . PHE A  1 110 ? -0.295  -1.841  25.269  1.00 21.70  ? 359  PHE A CE1 1 
ATOM   901  C  CE2 . PHE A  1 110 ? -1.874  -2.220  23.563  1.00 23.94  ? 359  PHE A CE2 1 
ATOM   902  C  CZ  . PHE A  1 110 ? -1.409  -1.454  24.607  1.00 21.91  ? 359  PHE A CZ  1 
ATOM   903  N  N   . SER A  1 111 ? 3.685   -6.318  22.777  1.00 27.30  ? 360  SER A N   1 
ATOM   904  C  CA  . SER A  1 111 ? 4.429   -7.502  22.508  1.00 30.03  ? 360  SER A CA  1 
ATOM   905  C  C   . SER A  1 111 ? 5.364   -7.910  23.628  1.00 34.52  ? 360  SER A C   1 
ATOM   906  O  O   . SER A  1 111 ? 6.431   -7.315  23.793  1.00 34.92  ? 360  SER A O   1 
ATOM   907  C  CB  . SER A  1 111 ? 5.248   -7.250  21.283  1.00 32.98  ? 360  SER A CB  1 
ATOM   908  O  OG  . SER A  1 111 ? 5.962   -8.419  20.978  1.00 40.68  ? 360  SER A OG  1 
ATOM   909  N  N   . GLY A  1 112 ? 4.991   -8.972  24.349  1.00 35.88  ? 361  GLY A N   1 
ATOM   910  C  CA  . GLY A  1 112 ? 5.689   -9.364  25.562  1.00 34.56  ? 361  GLY A CA  1 
ATOM   911  C  C   . GLY A  1 112 ? 5.371   -8.395  26.698  1.00 36.67  ? 361  GLY A C   1 
ATOM   912  O  O   . GLY A  1 112 ? 4.215   -8.177  27.045  1.00 36.59  ? 361  GLY A O   1 
ATOM   913  N  N   . ASN A  1 113 ? 6.411   -7.830  27.292  1.00 37.22  ? 362  ASN A N   1 
ATOM   914  C  CA  . ASN A  1 113 ? 6.261   -6.886  28.397  1.00 38.63  ? 362  ASN A CA  1 
ATOM   915  C  C   . ASN A  1 113 ? 6.253   -5.413  27.982  1.00 35.07  ? 362  ASN A C   1 
ATOM   916  O  O   . ASN A  1 113 ? 6.003   -4.545  28.798  1.00 34.05  ? 362  ASN A O   1 
ATOM   917  C  CB  . ASN A  1 113 ? 7.400   -7.110  29.387  1.00 41.76  ? 362  ASN A CB  1 
ATOM   918  C  CG  . ASN A  1 113 ? 7.355   -8.498  30.007  1.00 48.28  ? 362  ASN A CG  1 
ATOM   919  O  OD1 . ASN A  1 113 ? 6.278   -9.069  30.273  1.00 48.40  ? 362  ASN A OD1 1 
ATOM   920  N  ND2 . ASN A  1 113 ? 8.531   -9.061  30.222  1.00 55.91  ? 362  ASN A ND2 1 
ATOM   921  N  N   . GLY A  1 114 ? 6.553   -5.139  26.725  1.00 35.30  ? 363  GLY A N   1 
ATOM   922  C  CA  . GLY A  1 114 ? 6.527   -3.754  26.208  1.00 34.44  ? 363  GLY A CA  1 
ATOM   923  C  C   . GLY A  1 114 ? 5.913   -3.609  24.814  1.00 32.67  ? 363  GLY A C   1 
ATOM   924  O  O   . GLY A  1 114 ? 5.101   -4.440  24.366  1.00 28.62  ? 363  GLY A O   1 
ATOM   925  N  N   . TRP A  1 115 ? 6.323   -2.532  24.138  1.00 30.61  ? 364  TRP A N   1 
ATOM   926  C  CA  . TRP A  1 115 ? 5.824   -2.183  22.844  1.00 27.30  ? 364  TRP A CA  1 
ATOM   927  C  C   . TRP A  1 115 ? 6.875   -2.509  21.811  1.00 27.44  ? 364  TRP A C   1 
ATOM   928  O  O   . TRP A  1 115 ? 8.074   -2.461  22.075  1.00 26.70  ? 364  TRP A O   1 
ATOM   929  C  CB  . TRP A  1 115 ? 5.510   -0.695  22.736  1.00 27.20  ? 364  TRP A CB  1 
ATOM   930  C  CG  . TRP A  1 115 ? 4.627   -0.131  23.737  1.00 27.02  ? 364  TRP A CG  1 
ATOM   931  C  CD1 . TRP A  1 115 ? 3.886   -0.788  24.684  1.00 26.54  ? 364  TRP A CD1 1 
ATOM   932  C  CD2 . TRP A  1 115 ? 4.342   1.242   23.882  1.00 27.75  ? 364  TRP A CD2 1 
ATOM   933  N  NE1 . TRP A  1 115 ? 3.198   0.128   25.456  1.00 24.81  ? 364  TRP A NE1 1 
ATOM   934  C  CE2 . TRP A  1 115 ? 3.464   1.382   24.982  1.00 25.73  ? 364  TRP A CE2 1 
ATOM   935  C  CE3 . TRP A  1 115 ? 4.799   2.394   23.233  1.00 28.44  ? 364  TRP A CE3 1 
ATOM   936  C  CZ2 . TRP A  1 115 ? 2.979   2.631   25.405  1.00 26.27  ? 364  TRP A CZ2 1 
ATOM   937  C  CZ3 . TRP A  1 115 ? 4.320   3.637   23.668  1.00 27.35  ? 364  TRP A CZ3 1 
ATOM   938  C  CH2 . TRP A  1 115 ? 3.403   3.734   24.739  1.00 26.32  ? 364  TRP A CH2 1 
ATOM   939  N  N   . ASN A  1 116 ? 6.403   -2.819  20.621  1.00 25.86  ? 365  ASN A N   1 
ATOM   940  C  CA  . ASN A  1 116 ? 7.284   -3.037  19.484  1.00 27.73  ? 365  ASN A CA  1 
ATOM   941  C  C   . ASN A  1 116 ? 6.687   -2.353  18.258  1.00 26.46  ? 365  ASN A C   1 
ATOM   942  O  O   . ASN A  1 116 ? 5.487   -2.239  18.141  1.00 28.42  ? 365  ASN A O   1 
ATOM   943  C  CB  . ASN A  1 116 ? 7.446   -4.538  19.210  1.00 25.15  ? 365  ASN A CB  1 
ATOM   944  C  CG  . ASN A  1 116 ? 8.230   -4.801  17.915  1.00 27.41  ? 365  ASN A CG  1 
ATOM   945  O  OD1 . ASN A  1 116 ? 9.296   -4.191  17.688  1.00 22.88  ? 365  ASN A OD1 1 
ATOM   946  N  ND2 . ASN A  1 116 ? 7.694   -5.671  17.049  1.00 22.61  ? 365  ASN A ND2 1 
ATOM   947  N  N   . ASP A  1 117 ? 7.521   -1.898  17.342  1.00 28.82  ? 366  ASP A N   1 
ATOM   948  C  CA  . ASP A  1 117 ? 7.017   -1.488  16.043  1.00 25.71  ? 366  ASP A CA  1 
ATOM   949  C  C   . ASP A  1 117 ? 7.025   -2.669  15.076  1.00 27.17  ? 366  ASP A C   1 
ATOM   950  O  O   . ASP A  1 117 ? 8.004   -3.384  14.990  1.00 25.71  ? 366  ASP A O   1 
ATOM   951  C  CB  . ASP A  1 117 ? 7.753   -0.272  15.492  1.00 28.37  ? 366  ASP A CB  1 
ATOM   952  C  CG  . ASP A  1 117 ? 9.221   -0.481  15.281  1.00 28.05  ? 366  ASP A CG  1 
ATOM   953  O  OD1 . ASP A  1 117 ? 9.813   -1.344  15.948  1.00 27.12  ? 366  ASP A OD1 1 
ATOM   954  O  OD2 . ASP A  1 117 ? 9.784   0.275   14.457  1.00 32.28  ? 366  ASP A OD2 1 
ATOM   955  N  N   . ASP A  1 118 ? 5.905   -2.914  14.403  1.00 26.56  ? 367  ASP A N   1 
ATOM   956  C  CA  . ASP A  1 118 ? 5.806   -4.019  13.469  1.00 29.24  ? 367  ASP A CA  1 
ATOM   957  C  C   . ASP A  1 118 ? 5.167   -3.480  12.241  1.00 27.96  ? 367  ASP A C   1 
ATOM   958  O  O   . ASP A  1 118 ? 4.806   -2.304  12.196  1.00 26.23  ? 367  ASP A O   1 
ATOM   959  C  CB  . ASP A  1 118 ? 4.984   -5.187  14.024  1.00 30.43  ? 367  ASP A CB  1 
ATOM   960  C  CG  . ASP A  1 118 ? 5.426   -6.565  13.470  1.00 32.22  ? 367  ASP A CG  1 
ATOM   961  O  OD1 . ASP A  1 118 ? 6.045   -6.661  12.378  1.00 31.15  ? 367  ASP A OD1 1 
ATOM   962  O  OD2 . ASP A  1 118 ? 5.142   -7.576  14.144  1.00 32.34  ? 367  ASP A OD2 1 
ATOM   963  N  N   . LYS A  1 119 ? 5.056   -4.354  11.243  1.00 29.64  ? 368  LYS A N   1 
ATOM   964  C  CA  . LYS A  1 119 ? 4.512   -4.022  9.938   1.00 32.05  ? 368  LYS A CA  1 
ATOM   965  C  C   . LYS A  1 119 ? 2.984   -3.990  9.990   1.00 30.08  ? 368  LYS A C   1 
ATOM   966  O  O   . LYS A  1 119 ? 2.351   -4.912  10.480  1.00 25.31  ? 368  LYS A O   1 
ATOM   967  C  CB  . LYS A  1 119 ? 4.948   -5.041  8.883   1.00 36.44  ? 368  LYS A CB  1 
ATOM   968  C  CG  . LYS A  1 119 ? 6.381   -5.526  9.008   1.00 40.08  ? 368  LYS A CG  1 
ATOM   969  C  CD  . LYS A  1 119 ? 6.834   -6.158  7.712   1.00 48.43  ? 368  LYS A CD  1 
ATOM   970  C  CE  . LYS A  1 119 ? 8.260   -6.667  7.854   1.00 55.12  ? 368  LYS A CE  1 
ATOM   971  N  NZ  . LYS A  1 119 ? 8.315   -7.960  8.603   1.00 54.90  ? 368  LYS A NZ  1 
ATOM   972  N  N   . CYS A  1 120 ? 2.442   -2.937  9.403   1.00 29.41  ? 369  CYS A N   1 
ATOM   973  C  CA  . CYS A  1 120 ? 1.066   -2.528  9.582   1.00 28.75  ? 369  CYS A CA  1 
ATOM   974  C  C   . CYS A  1 120 ? 0.103   -3.426  8.899   1.00 28.97  ? 369  CYS A C   1 
ATOM   975  O  O   . CYS A  1 120 ? -1.068  -3.422  9.266   1.00 28.38  ? 369  CYS A O   1 
ATOM   976  C  CB  . CYS A  1 120 ? 0.847   -1.096  9.059   1.00 29.62  ? 369  CYS A CB  1 
ATOM   977  S  SG  . CYS A  1 120 ? 1.787   0.196   9.916   1.00 30.26  ? 369  CYS A SG  1 
ATOM   978  N  N   . ASN A  1 121 ? 0.565   -4.165  7.882   1.00 28.00  ? 370  ASN A N   1 
ATOM   979  C  CA  . ASN A  1 121 ? -0.302  -5.047  7.130   1.00 30.72  ? 370  ASN A CA  1 
ATOM   980  C  C   . ASN A  1 121 ? -0.407  -6.450  7.697   1.00 28.39  ? 370  ASN A C   1 
ATOM   981  O  O   . ASN A  1 121 ? -1.135  -7.250  7.161   1.00 31.03  ? 370  ASN A O   1 
ATOM   982  C  CB  . ASN A  1 121 ? 0.136   -5.129  5.668   1.00 35.84  ? 370  ASN A CB  1 
ATOM   983  C  CG  . ASN A  1 121 ? 1.412   -5.909  5.468   1.00 39.28  ? 370  ASN A CG  1 
ATOM   984  O  OD1 . ASN A  1 121 ? 2.407   -5.703  6.163   1.00 43.84  ? 370  ASN A OD1 1 
ATOM   985  N  ND2 . ASN A  1 121 ? 1.403   -6.790  4.466   1.00 49.44  ? 370  ASN A ND2 1 
ATOM   986  N  N   . LEU A  1 122 ? 0.322   -6.750  8.764   1.00 29.49  ? 371  LEU A N   1 
ATOM   987  C  CA  . LEU A  1 122 ? 0.133   -8.021  9.488   1.00 29.38  ? 371  LEU A CA  1 
ATOM   988  C  C   . LEU A  1 122 ? -1.114  -7.978  10.323  1.00 30.08  ? 371  LEU A C   1 
ATOM   989  O  O   . LEU A  1 122 ? -1.583  -6.919  10.706  1.00 30.00  ? 371  LEU A O   1 
ATOM   990  C  CB  . LEU A  1 122 ? 1.314   -8.369  10.406  1.00 27.70  ? 371  LEU A CB  1 
ATOM   991  C  CG  . LEU A  1 122 ? 2.658   -8.479  9.709   1.00 29.29  ? 371  LEU A CG  1 
ATOM   992  C  CD1 . LEU A  1 122 ? 3.802   -8.734  10.678  1.00 27.68  ? 371  LEU A CD1 1 
ATOM   993  C  CD2 . LEU A  1 122 ? 2.558   -9.578  8.671   1.00 28.59  ? 371  LEU A CD2 1 
ATOM   994  N  N   . ALA A  1 123 ? -1.597  -9.172  10.634  1.00 30.55  ? 372  ALA A N   1 
ATOM   995  C  CA  . ALA A  1 123 ? -2.853  -9.402  11.310  1.00 29.64  ? 372  ALA A CA  1 
ATOM   996  C  C   . ALA A  1 123 ? -2.555  -9.603  12.796  1.00 29.22  ? 372  ALA A C   1 
ATOM   997  O  O   . ALA A  1 123 ? -1.763  -10.458 13.164  1.00 29.43  ? 372  ALA A O   1 
ATOM   998  C  CB  . ALA A  1 123 ? -3.551  -10.626 10.705  1.00 31.84  ? 372  ALA A CB  1 
ATOM   999  N  N   . LYS A  1 124 ? -3.148  -8.760  13.639  1.00 27.52  ? 373  LYS A N   1 
ATOM   1000 C  CA  . LYS A  1 124 ? -2.979  -8.856  15.078  1.00 25.70  ? 373  LYS A CA  1 
ATOM   1001 C  C   . LYS A  1 124 ? -4.290  -8.651  15.776  1.00 23.97  ? 373  LYS A C   1 
ATOM   1002 O  O   . LYS A  1 124 ? -5.214  -8.104  15.196  1.00 25.16  ? 373  LYS A O   1 
ATOM   1003 C  CB  . LYS A  1 124 ? -2.014  -7.763  15.560  1.00 26.72  ? 373  LYS A CB  1 
ATOM   1004 C  CG  . LYS A  1 124 ? -0.517  -8.045  15.308  1.00 27.78  ? 373  LYS A CG  1 
ATOM   1005 C  CD  . LYS A  1 124 ? 0.364   -6.855  15.648  1.00 28.23  ? 373  LYS A CD  1 
ATOM   1006 C  CE  . LYS A  1 124 ? 1.661   -6.801  14.864  1.00 31.74  ? 373  LYS A CE  1 
ATOM   1007 N  NZ  . LYS A  1 124 ? 2.577   -7.888  15.260  1.00 35.02  ? 373  LYS A NZ  1 
ATOM   1008 N  N   . PHE A  1 125 ? -4.360  -9.021  17.055  1.00 24.96  ? 374  PHE A N   1 
ATOM   1009 C  CA  . PHE A  1 125 ? -5.517  -8.638  17.872  1.00 24.48  ? 374  PHE A CA  1 
ATOM   1010 C  C   . PHE A  1 125 ? -5.482  -7.137  18.087  1.00 24.47  ? 374  PHE A C   1 
ATOM   1011 O  O   . PHE A  1 125 ? -4.463  -6.490  17.819  1.00 24.62  ? 374  PHE A O   1 
ATOM   1012 C  CB  . PHE A  1 125 ? -5.527  -9.370  19.192  1.00 25.48  ? 374  PHE A CB  1 
ATOM   1013 C  CG  . PHE A  1 125 ? -5.618  -10.850 19.047  1.00 28.75  ? 374  PHE A CG  1 
ATOM   1014 C  CD1 . PHE A  1 125 ? -6.845  -11.471 18.979  1.00 31.43  ? 374  PHE A CD1 1 
ATOM   1015 C  CD2 . PHE A  1 125 ? -4.473  -11.623 18.947  1.00 30.41  ? 374  PHE A CD2 1 
ATOM   1016 C  CE1 . PHE A  1 125 ? -6.940  -12.842 18.797  1.00 32.81  ? 374  PHE A CE1 1 
ATOM   1017 C  CE2 . PHE A  1 125 ? -4.553  -12.987 18.801  1.00 32.23  ? 374  PHE A CE2 1 
ATOM   1018 C  CZ  . PHE A  1 125 ? -5.790  -13.607 18.708  1.00 31.97  ? 374  PHE A CZ  1 
ATOM   1019 N  N   . TRP A  1 126 ? -6.581  -6.571  18.563  1.00 25.25  ? 375  TRP A N   1 
ATOM   1020 C  CA  . TRP A  1 126 ? -6.657  -5.119  18.775  1.00 26.15  ? 375  TRP A CA  1 
ATOM   1021 C  C   . TRP A  1 126 ? -7.570  -4.752  19.952  1.00 27.30  ? 375  TRP A C   1 
ATOM   1022 O  O   . TRP A  1 126 ? -8.383  -5.556  20.445  1.00 26.45  ? 375  TRP A O   1 
ATOM   1023 C  CB  . TRP A  1 126 ? -7.072  -4.363  17.490  1.00 26.62  ? 375  TRP A CB  1 
ATOM   1024 C  CG  . TRP A  1 126 ? -8.558  -4.455  17.223  1.00 27.26  ? 375  TRP A CG  1 
ATOM   1025 C  CD1 . TRP A  1 126 ? -9.555  -3.606  17.702  1.00 27.41  ? 375  TRP A CD1 1 
ATOM   1026 C  CD2 . TRP A  1 126 ? -9.218  -5.463  16.494  1.00 25.78  ? 375  TRP A CD2 1 
ATOM   1027 N  NE1 . TRP A  1 126 ? -10.781 -4.036  17.285  1.00 27.87  ? 375  TRP A NE1 1 
ATOM   1028 C  CE2 . TRP A  1 126 ? -10.608 -5.185  16.552  1.00 28.54  ? 375  TRP A CE2 1 
ATOM   1029 C  CE3 . TRP A  1 126 ? -8.780  -6.549  15.758  1.00 27.43  ? 375  TRP A CE3 1 
ATOM   1030 C  CZ2 . TRP A  1 126 ? -11.544 -5.984  15.925  1.00 27.32  ? 375  TRP A CZ2 1 
ATOM   1031 C  CZ3 . TRP A  1 126 ? -9.701  -7.351  15.169  1.00 29.85  ? 375  TRP A CZ3 1 
ATOM   1032 C  CH2 . TRP A  1 126 ? -11.064 -7.074  15.247  1.00 28.50  ? 375  TRP A CH2 1 
ATOM   1033 N  N   . ILE A  1 127 ? -7.405  -3.530  20.417  1.00 25.86  ? 376  ILE A N   1 
ATOM   1034 C  CA  . ILE A  1 127 ? -8.195  -3.019  21.546  1.00 27.97  ? 376  ILE A CA  1 
ATOM   1035 C  C   . ILE A  1 127 ? -8.756  -1.646  21.205  1.00 27.75  ? 376  ILE A C   1 
ATOM   1036 O  O   . ILE A  1 127 ? -8.048  -0.742  20.786  1.00 26.08  ? 376  ILE A O   1 
ATOM   1037 C  CB  . ILE A  1 127 ? -7.369  -2.939  22.826  1.00 26.82  ? 376  ILE A CB  1 
ATOM   1038 C  CG1 . ILE A  1 127 ? -6.988  -4.359  23.269  1.00 28.88  ? 376  ILE A CG1 1 
ATOM   1039 C  CG2 . ILE A  1 127 ? -8.149  -2.219  23.922  1.00 27.56  ? 376  ILE A CG2 1 
ATOM   1040 C  CD1 . ILE A  1 127 ? -5.871  -4.420  24.281  1.00 30.49  ? 376  ILE A CD1 1 
ATOM   1041 N  N   . CYS A  1 128 ? -10.052 -1.523  21.331  1.00 28.89  ? 377  CYS A N   1 
ATOM   1042 C  CA  . CYS A  1 128 ? -10.686 -0.228  21.176  1.00 30.17  ? 377  CYS A CA  1 
ATOM   1043 C  C   . CYS A  1 128 ? -10.943 0.378   22.544  1.00 29.24  ? 377  CYS A C   1 
ATOM   1044 O  O   . CYS A  1 128 ? -11.166 -0.341  23.540  1.00 26.96  ? 377  CYS A O   1 
ATOM   1045 C  CB  . CYS A  1 128 ? -12.036 -0.364  20.451  1.00 30.04  ? 377  CYS A CB  1 
ATOM   1046 S  SG  . CYS A  1 128 ? -11.977 -1.263  18.909  1.00 33.93  ? 377  CYS A SG  1 
ATOM   1047 N  N   . LYS A  1 129 ? -10.971 1.709   22.559  1.00 28.53  ? 378  LYS A N   1 
ATOM   1048 C  CA  . LYS A  1 129 ? -11.220 2.475   23.754  1.00 29.01  ? 378  LYS A CA  1 
ATOM   1049 C  C   . LYS A  1 129 ? -12.276 3.549   23.479  1.00 29.40  ? 378  LYS A C   1 
ATOM   1050 O  O   . LYS A  1 129 ? -12.225 4.206   22.438  1.00 26.95  ? 378  LYS A O   1 
ATOM   1051 C  CB  . LYS A  1 129 ? -9.915  3.131   24.227  1.00 27.89  ? 378  LYS A CB  1 
ATOM   1052 C  CG  . LYS A  1 129 ? -10.039 3.972   25.496  1.00 26.85  ? 378  LYS A CG  1 
ATOM   1053 C  CD  . LYS A  1 129 ? -8.894  4.964   25.576  1.00 27.69  ? 378  LYS A CD  1 
ATOM   1054 C  CE  . LYS A  1 129 ? -8.831  5.744   26.839  1.00 28.90  ? 378  LYS A CE  1 
ATOM   1055 N  NZ  . LYS A  1 129 ? -7.439  6.268   27.094  1.00 29.95  ? 378  LYS A NZ  1 
ATOM   1056 N  N   . LYS A  1 130 ? -13.211 3.723   24.417  1.00 28.91  ? 379  LYS A N   1 
ATOM   1057 C  CA  . LYS A  1 130 ? -14.072 4.920   24.459  1.00 31.93  ? 379  LYS A CA  1 
ATOM   1058 C  C   . LYS A  1 130 ? -14.538 5.228   25.883  1.00 32.47  ? 379  LYS A C   1 
ATOM   1059 O  O   . LYS A  1 130 ? -14.463 4.362   26.738  1.00 31.49  ? 379  LYS A O   1 
ATOM   1060 C  CB  . LYS A  1 130 ? -15.308 4.757   23.559  1.00 33.74  ? 379  LYS A CB  1 
ATOM   1061 C  CG  . LYS A  1 130 ? -16.099 3.502   23.783  1.00 36.52  ? 379  LYS A CG  1 
ATOM   1062 C  CD  . LYS A  1 130 ? -17.520 3.691   23.321  1.00 38.92  ? 379  LYS A CD  1 
ATOM   1063 C  CE  . LYS A  1 130 ? -18.283 2.400   23.430  1.00 43.69  ? 379  LYS A CE  1 
ATOM   1064 N  NZ  . LYS A  1 130 ? -19.211 2.316   22.267  1.00 45.84  ? 379  LYS A NZ  1 
ATOM   1065 N  N   . SER A  1 131 ? -15.064 6.442   26.105  1.00 32.60  ? 380  SER A N   1 
ATOM   1066 C  CA  . SER A  1 131 ? -15.494 6.896   27.448  1.00 36.42  ? 380  SER A CA  1 
ATOM   1067 C  C   . SER A  1 131 ? -16.603 6.057   28.024  1.00 33.33  ? 380  SER A C   1 
ATOM   1068 O  O   . SER A  1 131 ? -17.476 5.624   27.302  1.00 37.71  ? 380  SER A O   1 
ATOM   1069 C  CB  . SER A  1 131 ? -15.987 8.331   27.417  1.00 36.01  ? 380  SER A CB  1 
ATOM   1070 O  OG  . SER A  1 131 ? -14.852 9.152   27.381  1.00 45.06  ? 380  SER A OG  1 
ATOM   1071 N  N   . ALA A  1 132 ? -16.552 5.808   29.316  1.00 36.30  ? 381  ALA A N   1 
ATOM   1072 C  CA  . ALA A  1 132 ? -17.699 5.228   29.986  1.00 39.03  ? 381  ALA A CA  1 
ATOM   1073 C  C   . ALA A  1 132 ? -18.837 6.223   29.858  1.00 42.07  ? 381  ALA A C   1 
ATOM   1074 O  O   . ALA A  1 132 ? -18.622 7.400   29.569  1.00 42.80  ? 381  ALA A O   1 
ATOM   1075 C  CB  . ALA A  1 132 ? -17.383 4.936   31.436  1.00 41.28  ? 381  ALA A CB  1 
ATOM   1076 N  N   . ALA A  1 133 ? -20.058 5.746   29.983  1.00 48.00  ? 382  ALA A N   1 
ATOM   1077 C  CA  . ALA A  1 133 ? -21.218 6.639   30.059  1.00 57.00  ? 382  ALA A CA  1 
ATOM   1078 C  C   . ALA A  1 133 ? -21.327 7.062   31.513  1.00 58.08  ? 382  ALA A C   1 
ATOM   1079 O  O   . ALA A  1 133 ? -20.787 6.385   32.394  1.00 51.66  ? 382  ALA A O   1 
ATOM   1080 C  CB  . ALA A  1 133 ? -22.484 5.932   29.596  1.00 57.25  ? 382  ALA A CB  1 
ATOM   1081 N  N   . SER A  1 134 ? -21.983 8.185   31.778  1.00 68.68  ? 383  SER A N   1 
ATOM   1082 C  CA  . SER A  1 134 ? -22.168 8.589   33.183  1.00 78.14  ? 383  SER A CA  1 
ATOM   1083 C  C   . SER A  1 134 ? -23.357 7.879   33.837  1.00 79.21  ? 383  SER A C   1 
ATOM   1084 O  O   . SER A  1 134 ? -24.414 7.713   33.205  1.00 70.13  ? 383  SER A O   1 
ATOM   1085 C  CB  . SER A  1 134 ? -22.270 10.100  33.334  1.00 75.92  ? 383  SER A CB  1 
ATOM   1086 O  OG  . SER A  1 134 ? -21.002 10.598  33.735  1.00 76.03  ? 383  SER A OG  1 
ATOM   1087 N  N   . CYS A  1 135 ? -23.142 7.431   35.077  1.00 84.34  ? 384  CYS A N   1 
ATOM   1088 C  CA  . CYS A  1 135 ? -24.177 6.763   35.881  1.00 96.18  ? 384  CYS A CA  1 
ATOM   1089 C  C   . CYS A  1 135 ? -24.277 7.407   37.279  1.00 98.40  ? 384  CYS A C   1 
ATOM   1090 O  O   . CYS A  1 135 ? -25.375 7.653   37.800  1.00 84.38  ? 384  CYS A O   1 
ATOM   1091 C  CB  . CYS A  1 135 ? -23.888 5.258   36.020  1.00 95.03  ? 384  CYS A CB  1 
ATOM   1092 S  SG  . CYS A  1 135 ? -24.109 4.188   34.561  1.00 100.23 ? 384  CYS A SG  1 
ATOM   1093 N  N   . CYS B  1 4   ? -11.582 7.688   90.114  1.00 81.16  ? 253  CYS B N   1 
ATOM   1094 C  CA  . CYS B  1 4   ? -11.575 8.480   88.848  1.00 75.60  ? 253  CYS B CA  1 
ATOM   1095 C  C   . CYS B  1 4   ? -10.837 7.737   87.741  1.00 70.65  ? 253  CYS B C   1 
ATOM   1096 O  O   . CYS B  1 4   ? -9.655  7.409   87.886  1.00 70.83  ? 253  CYS B O   1 
ATOM   1097 C  CB  . CYS B  1 4   ? -10.909 9.847   89.060  1.00 79.60  ? 253  CYS B CB  1 
ATOM   1098 S  SG  . CYS B  1 4   ? -10.644 10.830  87.546  1.00 86.94  ? 253  CYS B SG  1 
ATOM   1099 N  N   . HIS B  1 5   ? -11.530 7.492   86.630  1.00 62.49  ? 254  HIS B N   1 
ATOM   1100 C  CA  . HIS B  1 5   ? -10.897 6.938   85.423  1.00 49.05  ? 254  HIS B CA  1 
ATOM   1101 C  C   . HIS B  1 5   ? -10.770 8.019   84.375  1.00 42.23  ? 254  HIS B C   1 
ATOM   1102 O  O   . HIS B  1 5   ? -11.740 8.689   84.090  1.00 40.45  ? 254  HIS B O   1 
ATOM   1103 C  CB  . HIS B  1 5   ? -11.735 5.797   84.878  1.00 47.07  ? 254  HIS B CB  1 
ATOM   1104 C  CG  . HIS B  1 5   ? -11.937 4.708   85.868  1.00 46.05  ? 254  HIS B CG  1 
ATOM   1105 N  ND1 . HIS B  1 5   ? -10.921 3.847   86.238  1.00 47.82  ? 254  HIS B ND1 1 
ATOM   1106 C  CD2 . HIS B  1 5   ? -13.008 4.381   86.623  1.00 45.16  ? 254  HIS B CD2 1 
ATOM   1107 C  CE1 . HIS B  1 5   ? -11.373 3.016   87.159  1.00 47.66  ? 254  HIS B CE1 1 
ATOM   1108 N  NE2 . HIS B  1 5   ? -12.634 3.324   87.415  1.00 49.23  ? 254  HIS B NE2 1 
ATOM   1109 N  N   . PRO B  1 6   ? -9.571  8.198   83.808  1.00 37.14  ? 255  PRO B N   1 
ATOM   1110 C  CA  . PRO B  1 6   ? -9.445  9.194   82.743  1.00 38.68  ? 255  PRO B CA  1 
ATOM   1111 C  C   . PRO B  1 6   ? -10.379 8.962   81.538  1.00 35.93  ? 255  PRO B C   1 
ATOM   1112 O  O   . PRO B  1 6   ? -10.836 9.914   80.941  1.00 41.36  ? 255  PRO B O   1 
ATOM   1113 C  CB  . PRO B  1 6   ? -7.968  9.093   82.332  1.00 40.35  ? 255  PRO B CB  1 
ATOM   1114 C  CG  . PRO B  1 6   ? -7.257  8.448   83.506  1.00 40.82  ? 255  PRO B CG  1 
ATOM   1115 C  CD  . PRO B  1 6   ? -8.282  7.554   84.142  1.00 38.62  ? 255  PRO B CD  1 
ATOM   1116 N  N   . CYS B  1 7   ? -10.672 7.713   81.205  1.00 34.81  ? 256  CYS B N   1 
ATOM   1117 C  CA  . CYS B  1 7   ? -11.433 7.380   80.017  1.00 34.69  ? 256  CYS B CA  1 
ATOM   1118 C  C   . CYS B  1 7   ? -12.497 6.391   80.354  1.00 35.24  ? 256  CYS B C   1 
ATOM   1119 O  O   . CYS B  1 7   ? -12.339 5.652   81.310  1.00 34.95  ? 256  CYS B O   1 
ATOM   1120 C  CB  . CYS B  1 7   ? -10.495 6.732   78.977  1.00 34.23  ? 256  CYS B CB  1 
ATOM   1121 S  SG  . CYS B  1 7   ? -9.316  7.950   78.399  1.00 39.50  ? 256  CYS B SG  1 
ATOM   1122 N  N   . PRO B  1 8   ? -13.565 6.328   79.531  1.00 33.35  ? 257  PRO B N   1 
ATOM   1123 C  CA  . PRO B  1 8   ? -14.508 5.245   79.717  1.00 34.28  ? 257  PRO B CA  1 
ATOM   1124 C  C   . PRO B  1 8   ? -13.882 3.865   79.518  1.00 35.65  ? 257  PRO B C   1 
ATOM   1125 O  O   . PRO B  1 8   ? -12.907 3.718   78.767  1.00 31.66  ? 257  PRO B O   1 
ATOM   1126 C  CB  . PRO B  1 8   ? -15.588 5.502   78.626  1.00 33.22  ? 257  PRO B CB  1 
ATOM   1127 C  CG  . PRO B  1 8   ? -15.495 6.974   78.352  1.00 35.80  ? 257  PRO B CG  1 
ATOM   1128 C  CD  . PRO B  1 8   ? -13.999 7.254   78.471  1.00 34.17  ? 257  PRO B CD  1 
ATOM   1129 N  N   . TRP B  1 9   ? -14.494 2.867   80.159  1.00 33.85  ? 258  TRP B N   1 
ATOM   1130 C  CA  . TRP B  1 9   ? -14.044 1.493   80.092  1.00 36.29  ? 258  TRP B CA  1 
ATOM   1131 C  C   . TRP B  1 9   ? -13.920 1.022   78.647  1.00 36.04  ? 258  TRP B C   1 
ATOM   1132 O  O   . TRP B  1 9   ? -14.847 1.154   77.842  1.00 36.20  ? 258  TRP B O   1 
ATOM   1133 C  CB  . TRP B  1 9   ? -15.012 0.593   80.876  1.00 37.88  ? 258  TRP B CB  1 
ATOM   1134 C  CG  . TRP B  1 9   ? -14.435 -0.718  81.410  1.00 39.22  ? 258  TRP B CG  1 
ATOM   1135 C  CD1 . TRP B  1 9   ? -13.490 -1.527  80.827  1.00 39.74  ? 258  TRP B CD1 1 
ATOM   1136 C  CD2 . TRP B  1 9   ? -14.839 -1.382  82.609  1.00 40.58  ? 258  TRP B CD2 1 
ATOM   1137 N  NE1 . TRP B  1 9   ? -13.264 -2.628  81.607  1.00 38.27  ? 258  TRP B NE1 1 
ATOM   1138 C  CE2 . TRP B  1 9   ? -14.078 -2.566  82.708  1.00 40.53  ? 258  TRP B CE2 1 
ATOM   1139 C  CE3 . TRP B  1 9   ? -15.754 -1.066  83.636  1.00 43.12  ? 258  TRP B CE3 1 
ATOM   1140 C  CZ2 . TRP B  1 9   ? -14.216 -3.454  83.778  1.00 40.46  ? 258  TRP B CZ2 1 
ATOM   1141 C  CZ3 . TRP B  1 9   ? -15.885 -1.937  84.706  1.00 41.50  ? 258  TRP B CZ3 1 
ATOM   1142 C  CH2 . TRP B  1 9   ? -15.129 -3.129  84.762  1.00 43.49  ? 258  TRP B CH2 1 
ATOM   1143 N  N   . GLU B  1 10  ? -12.760 0.459   78.331  1.00 38.08  ? 259  GLU B N   1 
ATOM   1144 C  CA  . GLU B  1 10  ? -12.472 -0.079  77.007  1.00 38.04  ? 259  GLU B CA  1 
ATOM   1145 C  C   . GLU B  1 10  ? -11.911 0.947   76.034  1.00 35.68  ? 259  GLU B C   1 
ATOM   1146 O  O   . GLU B  1 10  ? -11.432 0.565   74.975  1.00 35.50  ? 259  GLU B O   1 
ATOM   1147 C  CB  . GLU B  1 10  ? -13.687 -0.767  76.369  1.00 40.72  ? 259  GLU B CB  1 
ATOM   1148 C  CG  . GLU B  1 10  ? -14.282 -1.867  77.222  1.00 43.95  ? 259  GLU B CG  1 
ATOM   1149 C  CD  . GLU B  1 10  ? -14.839 -3.009  76.400  1.00 47.42  ? 259  GLU B CD  1 
ATOM   1150 O  OE1 . GLU B  1 10  ? -15.727 -3.710  76.900  1.00 51.79  ? 259  GLU B OE1 1 
ATOM   1151 O  OE2 . GLU B  1 10  ? -14.392 -3.219  75.259  1.00 52.86  ? 259  GLU B OE2 1 
ATOM   1152 N  N   . TRP B  1 11  ? -11.933 2.227   76.385  1.00 32.95  ? 260  TRP B N   1 
ATOM   1153 C  CA  . TRP B  1 11  ? -11.235 3.224   75.581  1.00 33.34  ? 260  TRP B CA  1 
ATOM   1154 C  C   . TRP B  1 11  ? -9.766  3.323   76.032  1.00 33.27  ? 260  TRP B C   1 
ATOM   1155 O  O   . TRP B  1 11  ? -9.443  3.103   77.211  1.00 34.28  ? 260  TRP B O   1 
ATOM   1156 C  CB  . TRP B  1 11  ? -11.873 4.582   75.765  1.00 31.28  ? 260  TRP B CB  1 
ATOM   1157 C  CG  . TRP B  1 11  ? -13.285 4.720   75.289  1.00 31.32  ? 260  TRP B CG  1 
ATOM   1158 C  CD1 . TRP B  1 11  ? -14.332 3.910   75.574  1.00 31.57  ? 260  TRP B CD1 1 
ATOM   1159 C  CD2 . TRP B  1 11  ? -13.808 5.768   74.439  1.00 29.90  ? 260  TRP B CD2 1 
ATOM   1160 N  NE1 . TRP B  1 11  ? -15.475 4.390   74.984  1.00 31.60  ? 260  TRP B NE1 1 
ATOM   1161 C  CE2 . TRP B  1 11  ? -15.176 5.516   74.268  1.00 28.74  ? 260  TRP B CE2 1 
ATOM   1162 C  CE3 . TRP B  1 11  ? -13.237 6.877   73.796  1.00 28.16  ? 260  TRP B CE3 1 
ATOM   1163 C  CZ2 . TRP B  1 11  ? -15.995 6.339   73.512  1.00 27.63  ? 260  TRP B CZ2 1 
ATOM   1164 C  CZ3 . TRP B  1 11  ? -14.048 7.697   73.064  1.00 28.49  ? 260  TRP B CZ3 1 
ATOM   1165 C  CH2 . TRP B  1 11  ? -15.413 7.411   72.902  1.00 27.05  ? 260  TRP B CH2 1 
ATOM   1166 N  N   . THR B  1 12  ? -8.903  3.690   75.095  1.00 33.17  ? 261  THR B N   1 
ATOM   1167 C  CA  . THR B  1 12  ? -7.488  3.863   75.324  1.00 32.72  ? 261  THR B CA  1 
ATOM   1168 C  C   . THR B  1 12  ? -7.206  5.326   75.600  1.00 34.87  ? 261  THR B C   1 
ATOM   1169 O  O   . THR B  1 12  ? -7.570  6.215   74.837  1.00 34.04  ? 261  THR B O   1 
ATOM   1170 C  CB  . THR B  1 12  ? -6.649  3.517   74.078  1.00 33.19  ? 261  THR B CB  1 
ATOM   1171 O  OG1 . THR B  1 12  ? -6.924  2.204   73.664  1.00 32.80  ? 261  THR B OG1 1 
ATOM   1172 C  CG2 . THR B  1 12  ? -5.134  3.635   74.339  1.00 33.06  ? 261  THR B CG2 1 
ATOM   1173 N  N   . PHE B  1 13  ? -6.435  5.540   76.644  1.00 35.14  ? 262  PHE B N   1 
ATOM   1174 C  CA  . PHE B  1 13  ? -5.907  6.836   76.974  1.00 34.15  ? 262  PHE B CA  1 
ATOM   1175 C  C   . PHE B  1 13  ? -4.606  7.075   76.242  1.00 30.41  ? 262  PHE B C   1 
ATOM   1176 O  O   . PHE B  1 13  ? -3.721  6.262   76.291  1.00 28.76  ? 262  PHE B O   1 
ATOM   1177 C  CB  . PHE B  1 13  ? -5.679  6.891   78.474  1.00 32.74  ? 262  PHE B CB  1 
ATOM   1178 C  CG  . PHE B  1 13  ? -5.004  8.129   78.939  1.00 33.67  ? 262  PHE B CG  1 
ATOM   1179 C  CD1 . PHE B  1 13  ? -3.609  8.196   78.984  1.00 35.84  ? 262  PHE B CD1 1 
ATOM   1180 C  CD2 . PHE B  1 13  ? -5.746  9.192   79.405  1.00 32.89  ? 262  PHE B CD2 1 
ATOM   1181 C  CE1 . PHE B  1 13  ? -2.978  9.342   79.440  1.00 37.05  ? 262  PHE B CE1 1 
ATOM   1182 C  CE2 . PHE B  1 13  ? -5.124  10.335  79.858  1.00 34.91  ? 262  PHE B CE2 1 
ATOM   1183 C  CZ  . PHE B  1 13  ? -3.744  10.407  79.890  1.00 34.44  ? 262  PHE B CZ  1 
ATOM   1184 N  N   . PHE B  1 14  ? -4.484  8.207   75.581  1.00 28.52  ? 263  PHE B N   1 
ATOM   1185 C  CA  . PHE B  1 14  ? -3.192  8.596   75.034  1.00 30.96  ? 263  PHE B CA  1 
ATOM   1186 C  C   . PHE B  1 14  ? -3.115  10.090  75.133  1.00 29.92  ? 263  PHE B C   1 
ATOM   1187 O  O   . PHE B  1 14  ? -4.001  10.794  74.629  1.00 30.90  ? 263  PHE B O   1 
ATOM   1188 C  CB  . PHE B  1 14  ? -3.061  8.166   73.570  1.00 32.68  ? 263  PHE B CB  1 
ATOM   1189 C  CG  . PHE B  1 14  ? -1.789  8.606   72.921  1.00 33.19  ? 263  PHE B CG  1 
ATOM   1190 C  CD1 . PHE B  1 14  ? -0.655  7.828   73.021  1.00 33.28  ? 263  PHE B CD1 1 
ATOM   1191 C  CD2 . PHE B  1 14  ? -1.728  9.800   72.197  1.00 36.04  ? 263  PHE B CD2 1 
ATOM   1192 C  CE1 . PHE B  1 14  ? 0.534   8.225   72.425  1.00 35.37  ? 263  PHE B CE1 1 
ATOM   1193 C  CE2 . PHE B  1 14  ? -0.548  10.191  71.561  1.00 35.96  ? 263  PHE B CE2 1 
ATOM   1194 C  CZ  . PHE B  1 14  ? 0.588   9.409   71.696  1.00 34.17  ? 263  PHE B CZ  1 
ATOM   1195 N  N   . GLN B  1 15  ? -2.084  10.547  75.833  1.00 29.64  ? 264  GLN B N   1 
ATOM   1196 C  CA  . GLN B  1 15  ? -1.777  11.968  76.024  1.00 28.84  ? 264  GLN B CA  1 
ATOM   1197 C  C   . GLN B  1 15  ? -2.932  12.877  76.232  1.00 27.26  ? 264  GLN B C   1 
ATOM   1198 O  O   . GLN B  1 15  ? -3.040  13.861  75.560  1.00 28.30  ? 264  GLN B O   1 
ATOM   1199 C  CB  . GLN B  1 15  ? -0.910  12.502  74.879  1.00 31.45  ? 264  GLN B CB  1 
ATOM   1200 C  CG  . GLN B  1 15  ? 0.366   11.696  74.660  1.00 31.63  ? 264  GLN B CG  1 
ATOM   1201 C  CD  . GLN B  1 15  ? 1.316   12.358  73.687  1.00 33.47  ? 264  GLN B CD  1 
ATOM   1202 O  OE1 . GLN B  1 15  ? 0.900   13.201  72.894  1.00 35.76  ? 264  GLN B OE1 1 
ATOM   1203 N  NE2 . GLN B  1 15  ? 2.605   11.970  73.731  1.00 28.32  ? 264  GLN B NE2 1 
ATOM   1204 N  N   . GLY B  1 16  ? -3.788  12.549  77.184  1.00 29.12  ? 265  GLY B N   1 
ATOM   1205 C  CA  . GLY B  1 16  ? -4.806  13.463  77.645  1.00 29.07  ? 265  GLY B CA  1 
ATOM   1206 C  C   . GLY B  1 16  ? -6.139  13.239  76.956  1.00 33.22  ? 265  GLY B C   1 
ATOM   1207 O  O   . GLY B  1 16  ? -7.100  13.973  77.232  1.00 32.51  ? 265  GLY B O   1 
ATOM   1208 N  N   . ASN B  1 17  ? -6.200  12.268  76.029  1.00 31.71  ? 266  ASN B N   1 
ATOM   1209 C  CA  . ASN B  1 17  ? -7.443  12.036  75.266  1.00 32.43  ? 266  ASN B CA  1 
ATOM   1210 C  C   . ASN B  1 17  ? -7.820  10.572  75.314  1.00 31.78  ? 266  ASN B C   1 
ATOM   1211 O  O   . ASN B  1 17  ? -6.975  9.733   75.662  1.00 30.97  ? 266  ASN B O   1 
ATOM   1212 C  CB  . ASN B  1 17  ? -7.299  12.522  73.816  1.00 32.90  ? 266  ASN B CB  1 
ATOM   1213 C  CG  . ASN B  1 17  ? -7.226  14.045  73.721  1.00 31.58  ? 266  ASN B CG  1 
ATOM   1214 O  OD1 . ASN B  1 17  ? -8.165  14.713  74.035  1.00 33.70  ? 266  ASN B OD1 1 
ATOM   1215 N  ND2 . ASN B  1 17  ? -6.126  14.565  73.263  1.00 31.25  ? 266  ASN B ND2 1 
ATOM   1216 N  N   . CYS B  1 18  ? -9.084  10.289  75.012  1.00 26.30  ? 267  CYS B N   1 
ATOM   1217 C  CA  . CYS B  1 18  ? -9.590  8.952   75.009  1.00 28.30  ? 267  CYS B CA  1 
ATOM   1218 C  C   . CYS B  1 18  ? -9.927  8.548   73.567  1.00 29.56  ? 267  CYS B C   1 
ATOM   1219 O  O   . CYS B  1 18  ? -10.584 9.292   72.821  1.00 29.88  ? 267  CYS B O   1 
ATOM   1220 C  CB  . CYS B  1 18  ? -10.819 8.826   75.883  1.00 30.60  ? 267  CYS B CB  1 
ATOM   1221 S  SG  . CYS B  1 18  ? -10.571 9.364   77.592  1.00 34.79  ? 267  CYS B SG  1 
ATOM   1222 N  N   . TYR B  1 19  ? -9.507  7.353   73.202  1.00 27.67  ? 268  TYR B N   1 
ATOM   1223 C  CA  . TYR B  1 19  ? -9.749  6.825   71.861  1.00 28.56  ? 268  TYR B CA  1 
ATOM   1224 C  C   . TYR B  1 19  ? -10.487 5.518   71.889  1.00 28.29  ? 268  TYR B C   1 
ATOM   1225 O  O   . TYR B  1 19  ? -10.206 4.619   72.695  1.00 27.90  ? 268  TYR B O   1 
ATOM   1226 C  CB  . TYR B  1 19  ? -8.478  6.687   71.101  1.00 25.98  ? 268  TYR B CB  1 
ATOM   1227 C  CG  . TYR B  1 19  ? -7.707  7.983   71.020  1.00 26.71  ? 268  TYR B CG  1 
ATOM   1228 C  CD1 . TYR B  1 19  ? -6.954  8.433   72.101  1.00 27.73  ? 268  TYR B CD1 1 
ATOM   1229 C  CD2 . TYR B  1 19  ? -7.692  8.716   69.859  1.00 26.81  ? 268  TYR B CD2 1 
ATOM   1230 C  CE1 . TYR B  1 19  ? -6.202  9.602   72.023  1.00 28.20  ? 268  TYR B CE1 1 
ATOM   1231 C  CE2 . TYR B  1 19  ? -6.987  9.875   69.763  1.00 27.45  ? 268  TYR B CE2 1 
ATOM   1232 C  CZ  . TYR B  1 19  ? -6.215  10.314  70.828  1.00 29.39  ? 268  TYR B CZ  1 
ATOM   1233 O  OH  . TYR B  1 19  ? -5.515  11.477  70.676  1.00 27.54  ? 268  TYR B OH  1 
ATOM   1234 N  N   . PHE B  1 20  ? -11.496 5.470   71.026  1.00 30.70  ? 269  PHE B N   1 
ATOM   1235 C  CA  . PHE B  1 20  ? -12.295 4.282   70.810  1.00 31.43  ? 269  PHE B CA  1 
ATOM   1236 C  C   . PHE B  1 20  ? -11.913 3.693   69.456  1.00 27.91  ? 269  PHE B C   1 
ATOM   1237 O  O   . PHE B  1 20  ? -12.070 4.372   68.434  1.00 26.55  ? 269  PHE B O   1 
ATOM   1238 C  CB  . PHE B  1 20  ? -13.789 4.633   70.791  1.00 34.67  ? 269  PHE B CB  1 
ATOM   1239 C  CG  . PHE B  1 20  ? -14.651 3.412   70.632  1.00 40.37  ? 269  PHE B CG  1 
ATOM   1240 C  CD1 . PHE B  1 20  ? -14.695 2.467   71.653  1.00 46.01  ? 269  PHE B CD1 1 
ATOM   1241 C  CD2 . PHE B  1 20  ? -15.347 3.165   69.458  1.00 42.56  ? 269  PHE B CD2 1 
ATOM   1242 C  CE1 . PHE B  1 20  ? -15.458 1.311   71.518  1.00 49.89  ? 269  PHE B CE1 1 
ATOM   1243 C  CE2 . PHE B  1 20  ? -16.126 2.014   69.321  1.00 45.94  ? 269  PHE B CE2 1 
ATOM   1244 C  CZ  . PHE B  1 20  ? -16.177 1.084   70.348  1.00 43.58  ? 269  PHE B CZ  1 
ATOM   1245 N  N   . MET B  1 21  ? -11.403 2.466   69.449  1.00 27.22  ? 270  MET B N   1 
ATOM   1246 C  CA  . MET B  1 21  ? -11.058 1.754   68.213  1.00 30.94  ? 270  MET B CA  1 
ATOM   1247 C  C   . MET B  1 21  ? -12.221 0.823   67.932  1.00 31.92  ? 270  MET B C   1 
ATOM   1248 O  O   . MET B  1 21  ? -12.455 -0.102  68.716  1.00 30.78  ? 270  MET B O   1 
ATOM   1249 C  CB  . MET B  1 21  ? -9.784  0.927   68.335  1.00 34.30  ? 270  MET B CB  1 
ATOM   1250 C  CG  . MET B  1 21  ? -8.694  1.448   69.276  1.00 41.76  ? 270  MET B CG  1 
ATOM   1251 S  SD  . MET B  1 21  ? -8.088  3.099   68.935  1.00 46.67  ? 270  MET B SD  1 
ATOM   1252 C  CE  . MET B  1 21  ? -6.535  3.089   69.829  1.00 48.15  ? 270  MET B CE  1 
ATOM   1253 N  N   . SER B  1 22  ? -12.971 1.083   66.854  1.00 29.28  ? 271  SER B N   1 
ATOM   1254 C  CA  . SER B  1 22  ? -14.121 0.221   66.494  1.00 28.15  ? 271  SER B CA  1 
ATOM   1255 C  C   . SER B  1 22  ? -13.641 -1.205  66.197  1.00 28.95  ? 271  SER B C   1 
ATOM   1256 O  O   . SER B  1 22  ? -12.530 -1.390  65.778  1.00 29.59  ? 271  SER B O   1 
ATOM   1257 C  CB  . SER B  1 22  ? -14.854 0.772   65.275  1.00 25.08  ? 271  SER B CB  1 
ATOM   1258 O  OG  . SER B  1 22  ? -14.176 0.436   64.021  1.00 24.81  ? 271  SER B OG  1 
ATOM   1259 N  N   . ASN B  1 23  ? -14.485 -2.189  66.415  1.00 31.15  ? 272  ASN B N   1 
ATOM   1260 C  CA  A ASN B  1 23  ? -14.208 -3.566  65.934  0.30 32.33  ? 272  ASN B CA  1 
ATOM   1261 C  CA  B ASN B  1 23  ? -14.218 -3.541  65.967  0.70 36.69  ? 272  ASN B CA  1 
ATOM   1262 C  C   . ASN B  1 23  ? -15.209 -3.986  64.858  1.00 33.99  ? 272  ASN B C   1 
ATOM   1263 O  O   . ASN B  1 23  ? -15.350 -5.171  64.567  1.00 35.78  ? 272  ASN B O   1 
ATOM   1264 C  CB  A ASN B  1 23  ? -14.201 -4.619  67.065  0.30 31.58  ? 272  ASN B CB  1 
ATOM   1265 C  CB  B ASN B  1 23  ? -14.202 -4.438  67.214  0.70 39.46  ? 272  ASN B CB  1 
ATOM   1266 C  CG  A ASN B  1 23  ? -13.542 -5.940  66.633  0.30 30.69  ? 272  ASN B CG  1 
ATOM   1267 C  CG  B ASN B  1 23  ? -13.002 -4.120  68.110  0.70 45.64  ? 272  ASN B CG  1 
ATOM   1268 O  OD1 A ASN B  1 23  ? -12.856 -6.007  65.611  0.30 28.33  ? 272  ASN B OD1 1 
ATOM   1269 O  OD1 B ASN B  1 23  ? -13.158 -3.550  69.198  0.70 46.33  ? 272  ASN B OD1 1 
ATOM   1270 N  ND2 A ASN B  1 23  ? -13.760 -6.995  67.411  0.30 30.83  ? 272  ASN B ND2 1 
ATOM   1271 N  ND2 B ASN B  1 23  ? -11.775 -4.417  67.608  0.70 39.98  ? 272  ASN B ND2 1 
ATOM   1272 N  N   . SER B  1 24  ? -15.900 -3.006  64.282  1.00 29.89  ? 273  SER B N   1 
ATOM   1273 C  CA  . SER B  1 24  ? -16.723 -3.192  63.108  1.00 30.19  ? 273  SER B CA  1 
ATOM   1274 C  C   . SER B  1 24  ? -16.473 -2.031  62.158  1.00 26.62  ? 273  SER B C   1 
ATOM   1275 O  O   . SER B  1 24  ? -15.755 -1.091  62.517  1.00 27.96  ? 273  SER B O   1 
ATOM   1276 C  CB  . SER B  1 24  ? -18.198 -3.247  63.458  1.00 29.25  ? 273  SER B CB  1 
ATOM   1277 O  OG  . SER B  1 24  ? -18.603 -2.000  63.919  1.00 32.98  ? 273  SER B OG  1 
ATOM   1278 N  N   . GLN B  1 25  ? -17.104 -2.102  60.994  1.00 22.32  ? 274  GLN B N   1 
ATOM   1279 C  CA  . GLN B  1 25  ? -16.851 -1.205  59.874  1.00 24.05  ? 274  GLN B CA  1 
ATOM   1280 C  C   . GLN B  1 25  ? -18.109 -0.428  59.454  1.00 22.89  ? 274  GLN B C   1 
ATOM   1281 O  O   . GLN B  1 25  ? -19.196 -0.983  59.434  1.00 21.08  ? 274  GLN B O   1 
ATOM   1282 C  CB  . GLN B  1 25  ? -16.403 -2.013  58.666  1.00 22.36  ? 274  GLN B CB  1 
ATOM   1283 C  CG  . GLN B  1 25  ? -15.119 -2.767  58.820  1.00 24.26  ? 274  GLN B CG  1 
ATOM   1284 C  CD  . GLN B  1 25  ? -15.126 -4.038  58.004  1.00 25.06  ? 274  GLN B CD  1 
ATOM   1285 O  OE1 . GLN B  1 25  ? -15.857 -4.968  58.341  1.00 24.91  ? 274  GLN B OE1 1 
ATOM   1286 N  NE2 . GLN B  1 25  ? -14.338 -4.068  56.890  1.00 24.91  ? 274  GLN B NE2 1 
ATOM   1287 N  N   . ARG B  1 26  ? -17.925 0.842   59.090  1.00 22.82  ? 275  ARG B N   1 
ATOM   1288 C  CA  . ARG B  1 26  ? -18.979 1.669   58.602  1.00 21.37  ? 275  ARG B CA  1 
ATOM   1289 C  C   . ARG B  1 26  ? -18.430 2.670   57.597  1.00 20.28  ? 275  ARG B C   1 
ATOM   1290 O  O   . ARG B  1 26  ? -17.233 2.906   57.487  1.00 16.48  ? 275  ARG B O   1 
ATOM   1291 C  CB  . ARG B  1 26  ? -19.584 2.439   59.760  1.00 24.89  ? 275  ARG B CB  1 
ATOM   1292 C  CG  . ARG B  1 26  ? -20.438 1.616   60.725  1.00 27.18  ? 275  ARG B CG  1 
ATOM   1293 C  CD  . ARG B  1 26  ? -20.835 2.600   61.794  1.00 30.19  ? 275  ARG B CD  1 
ATOM   1294 N  NE  . ARG B  1 26  ? -21.663 2.071   62.849  1.00 34.30  ? 275  ARG B NE  1 
ATOM   1295 C  CZ  . ARG B  1 26  ? -22.625 2.771   63.467  1.00 38.21  ? 275  ARG B CZ  1 
ATOM   1296 N  NH1 . ARG B  1 26  ? -22.990 4.018   63.069  1.00 39.04  ? 275  ARG B NH1 1 
ATOM   1297 N  NH2 . ARG B  1 26  ? -23.281 2.185   64.445  1.00 42.27  ? 275  ARG B NH2 1 
ATOM   1298 N  N   . ASN B  1 27  ? -19.335 3.306   56.887  1.00 19.80  ? 276  ASN B N   1 
ATOM   1299 C  CA  . ASN B  1 27  ? -18.919 4.310   55.921  1.00 21.10  ? 276  ASN B CA  1 
ATOM   1300 C  C   . ASN B  1 27  ? -18.547 5.558   56.704  1.00 19.03  ? 276  ASN B C   1 
ATOM   1301 O  O   . ASN B  1 27  ? -18.815 5.618   57.914  1.00 17.92  ? 276  ASN B O   1 
ATOM   1302 C  CB  . ASN B  1 27  ? -19.955 4.499   54.813  1.00 22.16  ? 276  ASN B CB  1 
ATOM   1303 C  CG  . ASN B  1 27  ? -21.229 5.128   55.270  1.00 24.01  ? 276  ASN B CG  1 
ATOM   1304 O  OD1 . ASN B  1 27  ? -21.230 6.015   56.100  1.00 28.87  ? 276  ASN B OD1 1 
ATOM   1305 N  ND2 . ASN B  1 27  ? -22.336 4.703   54.677  1.00 24.09  ? 276  ASN B ND2 1 
ATOM   1306 N  N   . TRP B  1 28  ? -17.929 6.524   56.041  1.00 17.80  ? 277  TRP B N   1 
ATOM   1307 C  CA  . TRP B  1 28  ? -17.336 7.655   56.691  1.00 18.81  ? 277  TRP B CA  1 
ATOM   1308 C  C   . TRP B  1 28  ? -18.387 8.423   57.535  1.00 21.47  ? 277  TRP B C   1 
ATOM   1309 O  O   . TRP B  1 28  ? -18.139 8.725   58.686  1.00 22.00  ? 277  TRP B O   1 
ATOM   1310 C  CB  . TRP B  1 28  ? -16.663 8.566   55.662  1.00 20.28  ? 277  TRP B CB  1 
ATOM   1311 C  CG  . TRP B  1 28  ? -15.776 9.628   56.283  1.00 20.51  ? 277  TRP B CG  1 
ATOM   1312 C  CD1 . TRP B  1 28  ? -14.519 9.455   56.778  1.00 19.30  ? 277  TRP B CD1 1 
ATOM   1313 C  CD2 . TRP B  1 28  ? -16.065 11.032  56.435  1.00 21.12  ? 277  TRP B CD2 1 
ATOM   1314 N  NE1 . TRP B  1 28  ? -14.025 10.643  57.247  1.00 18.41  ? 277  TRP B NE1 1 
ATOM   1315 C  CE2 . TRP B  1 28  ? -14.955 11.622  57.052  1.00 18.90  ? 277  TRP B CE2 1 
ATOM   1316 C  CE3 . TRP B  1 28  ? -17.152 11.830  56.117  1.00 23.22  ? 277  TRP B CE3 1 
ATOM   1317 C  CZ2 . TRP B  1 28  ? -14.908 12.965  57.374  1.00 20.98  ? 277  TRP B CZ2 1 
ATOM   1318 C  CZ3 . TRP B  1 28  ? -17.099 13.192  56.413  1.00 23.19  ? 277  TRP B CZ3 1 
ATOM   1319 C  CH2 . TRP B  1 28  ? -15.965 13.759  56.991  1.00 20.97  ? 277  TRP B CH2 1 
ATOM   1320 N  N   . HIS B  1 29  ? -19.555 8.696   56.937  1.00 21.98  ? 278  HIS B N   1 
ATOM   1321 C  CA  . HIS B  1 29  ? -20.612 9.444   57.542  1.00 21.44  ? 278  HIS B CA  1 
ATOM   1322 C  C   . HIS B  1 29  ? -21.302 8.693   58.663  1.00 22.34  ? 278  HIS B C   1 
ATOM   1323 O  O   . HIS B  1 29  ? -21.680 9.307   59.625  1.00 22.52  ? 278  HIS B O   1 
ATOM   1324 C  CB  . HIS B  1 29  ? -21.668 9.830   56.467  1.00 22.98  ? 278  HIS B CB  1 
ATOM   1325 C  CG  . HIS B  1 29  ? -21.270 11.005  55.645  1.00 22.72  ? 278  HIS B CG  1 
ATOM   1326 N  ND1 . HIS B  1 29  ? -20.753 10.879  54.363  1.00 21.17  ? 278  HIS B ND1 1 
ATOM   1327 C  CD2 . HIS B  1 29  ? -21.283 12.326  55.935  1.00 22.96  ? 278  HIS B CD2 1 
ATOM   1328 C  CE1 . HIS B  1 29  ? -20.415 12.075  53.932  1.00 23.56  ? 278  HIS B CE1 1 
ATOM   1329 N  NE2 . HIS B  1 29  ? -20.750 12.972  54.852  1.00 24.61  ? 278  HIS B NE2 1 
ATOM   1330 N  N   . ASP B  1 30  ? -21.514 7.386   58.518  1.00 22.62  ? 279  ASP B N   1 
ATOM   1331 C  CA  . ASP B  1 30  ? -22.047 6.600   59.608  1.00 25.02  ? 279  ASP B CA  1 
ATOM   1332 C  C   . ASP B  1 30  ? -20.997 6.481   60.741  1.00 25.69  ? 279  ASP B C   1 
ATOM   1333 O  O   . ASP B  1 30  ? -21.341 6.422   61.932  1.00 26.17  ? 279  ASP B O   1 
ATOM   1334 C  CB  . ASP B  1 30  ? -22.481 5.210   59.144  1.00 27.35  ? 279  ASP B CB  1 
ATOM   1335 C  CG  . ASP B  1 30  ? -23.689 5.223   58.228  1.00 29.37  ? 279  ASP B CG  1 
ATOM   1336 O  OD1 . ASP B  1 30  ? -24.294 6.289   58.031  1.00 30.90  ? 279  ASP B OD1 1 
ATOM   1337 O  OD2 . ASP B  1 30  ? -24.003 4.152   57.634  1.00 31.14  ? 279  ASP B OD2 1 
ATOM   1338 N  N   . SER B  1 31  ? -19.721 6.507   60.392  1.00 24.16  ? 280  SER B N   1 
ATOM   1339 C  CA  . SER B  1 31  ? -18.674 6.578   61.432  1.00 25.94  ? 280  SER B CA  1 
ATOM   1340 C  C   . SER B  1 31  ? -18.720 7.856   62.315  1.00 26.97  ? 280  SER B C   1 
ATOM   1341 O  O   . SER B  1 31  ? -18.559 7.799   63.546  1.00 26.18  ? 280  SER B O   1 
ATOM   1342 C  CB  . SER B  1 31  ? -17.275 6.379   60.843  1.00 24.17  ? 280  SER B CB  1 
ATOM   1343 O  OG  . SER B  1 31  ? -17.149 5.058   60.285  1.00 22.54  ? 280  SER B OG  1 
ATOM   1344 N  N   . ILE B  1 32  ? -18.951 8.987   61.677  1.00 27.65  ? 281  ILE B N   1 
ATOM   1345 C  CA  . ILE B  1 32  ? -19.151 10.260  62.410  1.00 26.84  ? 281  ILE B CA  1 
ATOM   1346 C  C   . ILE B  1 32  ? -20.303 10.128  63.424  1.00 27.77  ? 281  ILE B C   1 
ATOM   1347 O  O   . ILE B  1 32  ? -20.202 10.570  64.564  1.00 27.16  ? 281  ILE B O   1 
ATOM   1348 C  CB  . ILE B  1 32  ? -19.445 11.385  61.409  1.00 27.15  ? 281  ILE B CB  1 
ATOM   1349 C  CG1 . ILE B  1 32  ? -18.162 11.855  60.715  1.00 31.40  ? 281  ILE B CG1 1 
ATOM   1350 C  CG2 . ILE B  1 32  ? -20.135 12.582  62.024  1.00 27.49  ? 281  ILE B CG2 1 
ATOM   1351 C  CD1 . ILE B  1 32  ? -18.422 12.395  59.336  1.00 33.08  ? 281  ILE B CD1 1 
ATOM   1352 N  N   . THR B  1 33  ? -21.407 9.576   62.965  1.00 26.76  ? 282  THR B N   1 
ATOM   1353 C  CA  . THR B  1 33  ? -22.583 9.410   63.784  1.00 30.06  ? 282  THR B CA  1 
ATOM   1354 C  C   . THR B  1 33  ? -22.326 8.474   64.927  1.00 28.99  ? 282  THR B C   1 
ATOM   1355 O  O   . THR B  1 33  ? -22.740 8.742   66.043  1.00 25.02  ? 282  THR B O   1 
ATOM   1356 C  CB  . THR B  1 33  ? -23.721 8.820   62.926  1.00 28.51  ? 282  THR B CB  1 
ATOM   1357 O  OG1 . THR B  1 33  ? -23.951 9.736   61.880  1.00 27.53  ? 282  THR B OG1 1 
ATOM   1358 C  CG2 . THR B  1 33  ? -24.996 8.609   63.709  1.00 29.70  ? 282  THR B CG2 1 
ATOM   1359 N  N   . ALA B  1 34  ? -21.676 7.350   64.632  1.00 27.64  ? 283  ALA B N   1 
ATOM   1360 C  CA  . ALA B  1 34  ? -21.245 6.428   65.721  1.00 27.81  ? 283  ALA B CA  1 
ATOM   1361 C  C   . ALA B  1 34  ? -20.433 7.141   66.807  1.00 28.37  ? 283  ALA B C   1 
ATOM   1362 O  O   . ALA B  1 34  ? -20.707 6.972   68.011  1.00 27.55  ? 283  ALA B O   1 
ATOM   1363 C  CB  . ALA B  1 34  ? -20.466 5.265   65.155  1.00 27.25  ? 283  ALA B CB  1 
ATOM   1364 N  N   . CYS B  1 35  ? -19.504 8.009   66.404  1.00 27.61  ? 284  CYS B N   1 
ATOM   1365 C  CA  . CYS B  1 35  ? -18.722 8.766   67.404  1.00 28.18  ? 284  CYS B CA  1 
ATOM   1366 C  C   . CYS B  1 35  ? -19.630 9.738   68.180  1.00 29.77  ? 284  CYS B C   1 
ATOM   1367 O  O   . CYS B  1 35  ? -19.491 9.830   69.417  1.00 27.18  ? 284  CYS B O   1 
ATOM   1368 C  CB  . CYS B  1 35  ? -17.534 9.498   66.768  1.00 27.41  ? 284  CYS B CB  1 
ATOM   1369 S  SG  . CYS B  1 35  ? -16.336 8.307   66.063  1.00 28.11  ? 284  CYS B SG  1 
ATOM   1370 N  N   . LYS B  1 36  ? -20.586 10.401  67.495  1.00 30.51  ? 285  LYS B N   1 
ATOM   1371 C  CA  . LYS B  1 36  ? -21.498 11.351  68.181  1.00 30.66  ? 285  LYS B CA  1 
ATOM   1372 C  C   . LYS B  1 36  ? -22.291 10.596  69.238  1.00 29.69  ? 285  LYS B C   1 
ATOM   1373 O  O   . LYS B  1 36  ? -22.605 11.101  70.311  1.00 29.77  ? 285  LYS B O   1 
ATOM   1374 C  CB  . LYS B  1 36  ? -22.476 12.021  67.232  1.00 33.41  ? 285  LYS B CB  1 
ATOM   1375 C  CG  . LYS B  1 36  ? -21.856 12.983  66.249  1.00 40.31  ? 285  LYS B CG  1 
ATOM   1376 C  CD  . LYS B  1 36  ? -22.937 13.602  65.374  1.00 44.62  ? 285  LYS B CD  1 
ATOM   1377 C  CE  . LYS B  1 36  ? -22.323 14.286  64.160  1.00 50.17  ? 285  LYS B CE  1 
ATOM   1378 N  NZ  . LYS B  1 36  ? -21.386 15.412  64.440  1.00 51.02  ? 285  LYS B NZ  1 
ATOM   1379 N  N   . GLU B  1 37  ? -22.608 9.363   68.950  1.00 30.54  ? 286  GLU B N   1 
ATOM   1380 C  CA  . GLU B  1 37  ? -23.417 8.622   69.864  1.00 34.74  ? 286  GLU B CA  1 
ATOM   1381 C  C   . GLU B  1 37  ? -22.722 8.359   71.180  1.00 35.86  ? 286  GLU B C   1 
ATOM   1382 O  O   . GLU B  1 37  ? -23.382 8.166   72.172  1.00 36.01  ? 286  GLU B O   1 
ATOM   1383 C  CB  . GLU B  1 37  ? -23.906 7.342   69.203  1.00 35.42  ? 286  GLU B CB  1 
ATOM   1384 C  CG  . GLU B  1 37  ? -24.969 7.639   68.160  1.00 36.80  ? 286  GLU B CG  1 
ATOM   1385 C  CD  . GLU B  1 37  ? -25.440 6.422   67.407  1.00 40.19  ? 286  GLU B CD  1 
ATOM   1386 O  OE1 . GLU B  1 37  ? -26.588 6.446   66.881  1.00 44.62  ? 286  GLU B OE1 1 
ATOM   1387 O  OE2 . GLU B  1 37  ? -24.683 5.430   67.377  1.00 38.07  ? 286  GLU B OE2 1 
ATOM   1388 N  N   . VAL B  1 38  ? -21.388 8.409   71.201  1.00 36.67  ? 287  VAL B N   1 
ATOM   1389 C  CA  . VAL B  1 38  ? -20.630 8.217   72.443  1.00 30.83  ? 287  VAL B CA  1 
ATOM   1390 C  C   . VAL B  1 38  ? -19.921 9.452   72.861  1.00 31.20  ? 287  VAL B C   1 
ATOM   1391 O  O   . VAL B  1 38  ? -18.886 9.377   73.501  1.00 37.01  ? 287  VAL B O   1 
ATOM   1392 C  CB  . VAL B  1 38  ? -19.648 7.043   72.352  1.00 30.18  ? 287  VAL B CB  1 
ATOM   1393 C  CG1 . VAL B  1 38  ? -20.444 5.735   72.303  1.00 30.15  ? 287  VAL B CG1 1 
ATOM   1394 C  CG2 . VAL B  1 38  ? -18.736 7.139   71.110  1.00 30.07  ? 287  VAL B CG2 1 
ATOM   1395 N  N   . GLY B  1 39  ? -20.483 10.593  72.513  1.00 27.22  ? 288  GLY B N   1 
ATOM   1396 C  CA  . GLY B  1 39  ? -19.993 11.868  72.965  1.00 26.80  ? 288  GLY B CA  1 
ATOM   1397 C  C   . GLY B  1 39  ? -18.643 12.226  72.388  1.00 29.99  ? 288  GLY B C   1 
ATOM   1398 O  O   . GLY B  1 39  ? -17.861 12.977  72.988  1.00 32.63  ? 288  GLY B O   1 
ATOM   1399 N  N   . ALA B  1 40  ? -18.364 11.745  71.193  1.00 29.06  ? 289  ALA B N   1 
ATOM   1400 C  CA  . ALA B  1 40  ? -17.012 11.850  70.693  1.00 27.89  ? 289  ALA B CA  1 
ATOM   1401 C  C   . ALA B  1 40  ? -16.980 12.323  69.264  1.00 26.40  ? 289  ALA B C   1 
ATOM   1402 O  O   . ALA B  1 40  ? -17.996 12.595  68.666  1.00 28.72  ? 289  ALA B O   1 
ATOM   1403 C  CB  . ALA B  1 40  ? -16.310 10.496  70.845  1.00 29.14  ? 289  ALA B CB  1 
ATOM   1404 N  N   . GLN B  1 41  ? -15.794 12.396  68.715  1.00 25.24  ? 290  GLN B N   1 
ATOM   1405 C  CA  A GLN B  1 41  ? -15.632 12.871  67.367  0.50 25.90  ? 290  GLN B CA  1 
ATOM   1406 C  CA  B GLN B  1 41  ? -15.557 12.935  67.381  0.50 26.51  ? 290  GLN B CA  1 
ATOM   1407 C  C   . GLN B  1 41  ? -14.771 11.906  66.561  1.00 25.77  ? 290  GLN B C   1 
ATOM   1408 O  O   . GLN B  1 41  ? -13.852 11.298  67.075  1.00 27.07  ? 290  GLN B O   1 
ATOM   1409 C  CB  A GLN B  1 41  ? -14.991 14.242  67.418  0.50 25.58  ? 290  GLN B CB  1 
ATOM   1410 C  CB  B GLN B  1 41  ? -14.764 14.254  67.534  0.50 27.01  ? 290  GLN B CB  1 
ATOM   1411 C  CG  A GLN B  1 41  ? -15.214 15.047  66.167  0.50 25.58  ? 290  GLN B CG  1 
ATOM   1412 C  CG  B GLN B  1 41  ? -13.587 14.454  66.577  0.50 27.10  ? 290  GLN B CG  1 
ATOM   1413 C  CD  A GLN B  1 41  ? -14.706 16.454  66.306  0.50 23.65  ? 290  GLN B CD  1 
ATOM   1414 C  CD  B GLN B  1 41  ? -12.370 15.136  67.197  0.50 27.13  ? 290  GLN B CD  1 
ATOM   1415 O  OE1 A GLN B  1 41  ? -15.449 17.393  66.069  0.50 22.05  ? 290  GLN B OE1 1 
ATOM   1416 O  OE1 B GLN B  1 41  ? -11.349 14.478  67.459  0.50 26.27  ? 290  GLN B OE1 1 
ATOM   1417 N  NE2 A GLN B  1 41  ? -13.438 16.602  66.693  0.50 21.54  ? 290  GLN B NE2 1 
ATOM   1418 N  NE2 B GLN B  1 41  ? -12.456 16.454  67.403  0.50 25.16  ? 290  GLN B NE2 1 
ATOM   1419 N  N   . LEU B  1 42  ? -15.106 11.729  65.289  1.00 27.90  ? 291  LEU B N   1 
ATOM   1420 C  CA  . LEU B  1 42  ? -14.267 10.926  64.411  1.00 25.51  ? 291  LEU B CA  1 
ATOM   1421 C  C   . LEU B  1 42  ? -12.916 11.616  64.409  1.00 23.70  ? 291  LEU B C   1 
ATOM   1422 O  O   . LEU B  1 42  ? -12.834 12.840  64.267  1.00 24.86  ? 291  LEU B O   1 
ATOM   1423 C  CB  . LEU B  1 42  ? -14.862 10.818  63.003  1.00 27.96  ? 291  LEU B CB  1 
ATOM   1424 C  CG  . LEU B  1 42  ? -14.126 9.946   61.975  1.00 27.27  ? 291  LEU B CG  1 
ATOM   1425 C  CD1 . LEU B  1 42  ? -14.073 8.503   62.435  1.00 27.89  ? 291  LEU B CD1 1 
ATOM   1426 C  CD2 . LEU B  1 42  ? -14.791 10.092  60.591  1.00 29.77  ? 291  LEU B CD2 1 
ATOM   1427 N  N   . VAL B  1 43  ? -11.867 10.832  64.597  1.00 22.37  ? 292  VAL B N   1 
ATOM   1428 C  CA  . VAL B  1 43  ? -10.572 11.319  65.111  1.00 21.94  ? 292  VAL B CA  1 
ATOM   1429 C  C   . VAL B  1 43  ? -9.964  12.433  64.278  1.00 24.71  ? 292  VAL B C   1 
ATOM   1430 O  O   . VAL B  1 43  ? -9.727  12.268  63.079  1.00 23.08  ? 292  VAL B O   1 
ATOM   1431 C  CB  . VAL B  1 43  ? -9.548  10.163  65.329  1.00 23.26  ? 292  VAL B CB  1 
ATOM   1432 C  CG1 . VAL B  1 43  ? -9.194  9.431   64.018  1.00 23.81  ? 292  VAL B CG1 1 
ATOM   1433 C  CG2 . VAL B  1 43  ? -8.284  10.657  66.068  1.00 23.41  ? 292  VAL B CG2 1 
ATOM   1434 N  N   . VAL B  1 44  ? -9.698  13.549  64.958  1.00 26.26  ? 293  VAL B N   1 
ATOM   1435 C  CA  . VAL B  1 44  ? -8.974  14.709  64.430  1.00 25.07  ? 293  VAL B CA  1 
ATOM   1436 C  C   . VAL B  1 44  ? -7.582  14.677  65.051  1.00 24.61  ? 293  VAL B C   1 
ATOM   1437 O  O   . VAL B  1 44  ? -7.446  14.707  66.232  1.00 25.86  ? 293  VAL B O   1 
ATOM   1438 C  CB  . VAL B  1 44  ? -9.647  16.039  64.838  1.00 25.54  ? 293  VAL B CB  1 
ATOM   1439 C  CG1 . VAL B  1 44  ? -8.862  17.246  64.336  1.00 24.75  ? 293  VAL B CG1 1 
ATOM   1440 C  CG2 . VAL B  1 44  ? -11.092 16.102  64.350  1.00 27.87  ? 293  VAL B CG2 1 
ATOM   1441 N  N   . ILE B  1 45  ? -6.554  14.618  64.231  1.00 25.12  ? 294  ILE B N   1 
ATOM   1442 C  CA  . ILE B  1 45  ? -5.207  14.501  64.673  1.00 26.68  ? 294  ILE B CA  1 
ATOM   1443 C  C   . ILE B  1 45  ? -4.610  15.921  64.816  1.00 31.40  ? 294  ILE B C   1 
ATOM   1444 O  O   . ILE B  1 45  ? -4.711  16.753  63.910  1.00 32.68  ? 294  ILE B O   1 
ATOM   1445 C  CB  . ILE B  1 45  ? -4.371  13.711  63.655  1.00 27.24  ? 294  ILE B CB  1 
ATOM   1446 C  CG1 . ILE B  1 45  ? -5.046  12.343  63.327  1.00 26.30  ? 294  ILE B CG1 1 
ATOM   1447 C  CG2 . ILE B  1 45  ? -2.954  13.523  64.220  1.00 28.17  ? 294  ILE B CG2 1 
ATOM   1448 C  CD1 . ILE B  1 45  ? -4.306  11.554  62.251  1.00 27.42  ? 294  ILE B CD1 1 
ATOM   1449 N  N   . LYS B  1 46  ? -3.967  16.175  65.942  1.00 31.07  ? 295  LYS B N   1 
ATOM   1450 C  CA  . LYS B  1 46  ? -3.487  17.503  66.256  1.00 33.79  ? 295  LYS B CA  1 
ATOM   1451 C  C   . LYS B  1 46  ? -1.966  17.573  66.388  1.00 33.75  ? 295  LYS B C   1 
ATOM   1452 O  O   . LYS B  1 46  ? -1.436  18.664  66.419  1.00 32.87  ? 295  LYS B O   1 
ATOM   1453 C  CB  . LYS B  1 46  ? -4.106  17.954  67.573  1.00 36.06  ? 295  LYS B CB  1 
ATOM   1454 C  CG  . LYS B  1 46  ? -5.617  18.079  67.569  1.00 36.20  ? 295  LYS B CG  1 
ATOM   1455 C  CD  . LYS B  1 46  ? -6.050  19.464  67.189  1.00 36.82  ? 295  LYS B CD  1 
ATOM   1456 C  CE  . LYS B  1 46  ? -7.548  19.527  66.974  1.00 36.56  ? 295  LYS B CE  1 
ATOM   1457 N  NZ  . LYS B  1 46  ? -7.890  20.251  65.722  1.00 33.96  ? 295  LYS B NZ  1 
ATOM   1458 N  N   . SER B  1 47  ? -1.290  16.426  66.479  1.00 32.79  ? 296  SER B N   1 
ATOM   1459 C  CA  . SER B  1 47  ? 0.166   16.359  66.647  1.00 34.10  ? 296  SER B CA  1 
ATOM   1460 C  C   . SER B  1 47  ? 0.776   15.098  66.068  1.00 33.94  ? 296  SER B C   1 
ATOM   1461 O  O   . SER B  1 47  ? 0.080   14.136  65.728  1.00 35.20  ? 296  SER B O   1 
ATOM   1462 C  CB  . SER B  1 47  ? 0.540   16.381  68.124  1.00 34.38  ? 296  SER B CB  1 
ATOM   1463 O  OG  . SER B  1 47  ? 0.393   15.082  68.662  1.00 33.96  ? 296  SER B OG  1 
ATOM   1464 N  N   . ALA B  1 48  ? 2.096   15.092  66.031  1.00 31.74  ? 297  ALA B N   1 
ATOM   1465 C  CA  . ALA B  1 48  ? 2.839   14.098  65.280  1.00 34.65  ? 297  ALA B CA  1 
ATOM   1466 C  C   . ALA B  1 48  ? 2.852   12.774  66.014  1.00 33.47  ? 297  ALA B C   1 
ATOM   1467 O  O   . ALA B  1 48  ? 2.799   11.711  65.418  1.00 30.63  ? 297  ALA B O   1 
ATOM   1468 C  CB  . ALA B  1 48  ? 4.260   14.577  65.061  1.00 35.11  ? 297  ALA B CB  1 
ATOM   1469 N  N   . GLU B  1 49  ? 2.980   12.885  67.327  1.00 34.19  ? 298  GLU B N   1 
ATOM   1470 C  CA  A GLU B  1 49  ? 3.002   11.774  68.242  0.70 31.83  ? 298  GLU B CA  1 
ATOM   1471 C  CA  B GLU B  1 49  ? 3.043   11.717  68.181  0.30 31.80  ? 298  GLU B CA  1 
ATOM   1472 C  C   . GLU B  1 49  ? 1.645   11.097  68.256  1.00 29.52  ? 298  GLU B C   1 
ATOM   1473 O  O   . GLU B  1 49  ? 1.518   9.876   68.347  1.00 30.80  ? 298  GLU B O   1 
ATOM   1474 C  CB  A GLU B  1 49  ? 3.359   12.289  69.640  0.70 34.29  ? 298  GLU B CB  1 
ATOM   1475 C  CB  B GLU B  1 49  ? 3.678   12.036  69.555  0.30 33.10  ? 298  GLU B CB  1 
ATOM   1476 C  CG  A GLU B  1 49  ? 4.752   12.938  69.716  0.70 37.09  ? 298  GLU B CG  1 
ATOM   1477 C  CG  B GLU B  1 49  ? 5.177   11.669  69.630  0.30 34.09  ? 298  GLU B CG  1 
ATOM   1478 C  CD  A GLU B  1 49  ? 4.814   14.407  69.260  0.70 37.46  ? 298  GLU B CD  1 
ATOM   1479 C  CD  B GLU B  1 49  ? 6.039   12.680  70.374  0.30 34.54  ? 298  GLU B CD  1 
ATOM   1480 O  OE1 A GLU B  1 49  ? 5.950   14.906  69.049  0.70 42.86  ? 298  GLU B OE1 1 
ATOM   1481 O  OE1 B GLU B  1 49  ? 5.492   13.686  70.858  0.30 38.76  ? 298  GLU B OE1 1 
ATOM   1482 O  OE2 A GLU B  1 49  ? 3.768   15.071  69.114  0.70 33.45  ? 298  GLU B OE2 1 
ATOM   1483 O  OE2 B GLU B  1 49  ? 7.271   12.483  70.478  0.30 34.36  ? 298  GLU B OE2 1 
ATOM   1484 N  N   . GLU B  1 50  ? 0.614   11.907  68.185  1.00 27.44  ? 299  GLU B N   1 
ATOM   1485 C  CA  . GLU B  1 50  ? -0.742  11.371  68.002  1.00 28.27  ? 299  GLU B CA  1 
ATOM   1486 C  C   . GLU B  1 50  ? -0.920  10.581  66.697  1.00 29.10  ? 299  GLU B C   1 
ATOM   1487 O  O   . GLU B  1 50  ? -1.404  9.446   66.695  1.00 28.12  ? 299  GLU B O   1 
ATOM   1488 C  CB  . GLU B  1 50  ? -1.766  12.459  68.101  1.00 28.30  ? 299  GLU B CB  1 
ATOM   1489 C  CG  . GLU B  1 50  ? -3.158  11.911  68.246  1.00 31.17  ? 299  GLU B CG  1 
ATOM   1490 C  CD  . GLU B  1 50  ? -4.174  13.032  68.321  1.00 31.81  ? 299  GLU B CD  1 
ATOM   1491 O  OE1 . GLU B  1 50  ? -5.376  12.749  68.519  1.00 30.57  ? 299  GLU B OE1 1 
ATOM   1492 O  OE2 . GLU B  1 50  ? -3.751  14.191  68.193  1.00 32.05  ? 299  GLU B OE2 1 
ATOM   1493 N  N   . GLN B  1 51  ? -0.475  11.160  65.599  1.00 26.15  ? 300  GLN B N   1 
ATOM   1494 C  CA  . GLN B  1 51  ? -0.408  10.439  64.344  1.00 24.62  ? 300  GLN B CA  1 
ATOM   1495 C  C   . GLN B  1 51  ? 0.315   9.111   64.428  1.00 25.87  ? 300  GLN B C   1 
ATOM   1496 O  O   . GLN B  1 51  ? -0.225  8.111   63.989  1.00 25.74  ? 300  GLN B O   1 
ATOM   1497 C  CB  . GLN B  1 51  ? 0.182   11.316  63.244  1.00 24.68  ? 300  GLN B CB  1 
ATOM   1498 C  CG  . GLN B  1 51  ? 0.886   10.576  62.121  1.00 25.37  ? 300  GLN B CG  1 
ATOM   1499 C  CD  . GLN B  1 51  ? -0.016  9.748   61.205  1.00 26.79  ? 300  GLN B CD  1 
ATOM   1500 O  OE1 . GLN B  1 51  ? 0.492   8.996   60.367  1.00 26.30  ? 300  GLN B OE1 1 
ATOM   1501 N  NE2 . GLN B  1 51  ? -1.316  9.921   61.305  1.00 23.01  ? 300  GLN B NE2 1 
ATOM   1502 N  N   . ASN B  1 52  ? 1.524   9.066   64.995  1.00 27.68  ? 301  ASN B N   1 
ATOM   1503 C  CA  . ASN B  1 52  ? 2.279   7.801   65.080  1.00 24.99  ? 301  ASN B CA  1 
ATOM   1504 C  C   . ASN B  1 52  ? 1.514   6.801   65.908  1.00 22.91  ? 301  ASN B C   1 
ATOM   1505 O  O   . ASN B  1 52  ? 1.470   5.633   65.565  1.00 24.64  ? 301  ASN B O   1 
ATOM   1506 C  CB  . ASN B  1 52  ? 3.644   7.999   65.711  1.00 29.79  ? 301  ASN B CB  1 
ATOM   1507 C  CG  . ASN B  1 52  ? 4.492   9.022   64.984  1.00 30.31  ? 301  ASN B CG  1 
ATOM   1508 O  OD1 . ASN B  1 52  ? 4.337   9.239   63.800  1.00 34.68  ? 301  ASN B OD1 1 
ATOM   1509 N  ND2 . ASN B  1 52  ? 5.416   9.647   65.711  1.00 35.17  ? 301  ASN B ND2 1 
ATOM   1510 N  N   . PHE B  1 53  ? 0.866   7.249   66.974  1.00 22.50  ? 302  PHE B N   1 
ATOM   1511 C  CA  . PHE B  1 53  ? 0.086   6.348   67.795  1.00 24.37  ? 302  PHE B CA  1 
ATOM   1512 C  C   . PHE B  1 53  ? -1.064  5.745   66.981  1.00 27.32  ? 302  PHE B C   1 
ATOM   1513 O  O   . PHE B  1 53  ? -1.224  4.483   66.932  1.00 29.63  ? 302  PHE B O   1 
ATOM   1514 C  CB  . PHE B  1 53  ? -0.409  7.058   69.034  1.00 24.78  ? 302  PHE B CB  1 
ATOM   1515 C  CG  . PHE B  1 53  ? -1.609  6.434   69.697  1.00 28.41  ? 302  PHE B CG  1 
ATOM   1516 C  CD1 . PHE B  1 53  ? -1.492  5.268   70.435  1.00 30.35  ? 302  PHE B CD1 1 
ATOM   1517 C  CD2 . PHE B  1 53  ? -2.856  7.082   69.667  1.00 32.09  ? 302  PHE B CD2 1 
ATOM   1518 C  CE1 . PHE B  1 53  ? -2.592  4.713   71.089  1.00 29.91  ? 302  PHE B CE1 1 
ATOM   1519 C  CE2 . PHE B  1 53  ? -3.959  6.543   70.337  1.00 32.19  ? 302  PHE B CE2 1 
ATOM   1520 C  CZ  . PHE B  1 53  ? -3.821  5.340   71.027  1.00 30.91  ? 302  PHE B CZ  1 
ATOM   1521 N  N   . LEU B  1 54  ? -1.834  6.613   66.324  1.00 25.46  ? 303  LEU B N   1 
ATOM   1522 C  CA  . LEU B  1 54  ? -2.991  6.167   65.514  1.00 26.83  ? 303  LEU B CA  1 
ATOM   1523 C  C   . LEU B  1 54  ? -2.609  5.350   64.251  1.00 26.02  ? 303  LEU B C   1 
ATOM   1524 O  O   . LEU B  1 54  ? -3.281  4.360   63.913  1.00 27.46  ? 303  LEU B O   1 
ATOM   1525 C  CB  . LEU B  1 54  ? -3.809  7.354   65.084  1.00 25.06  ? 303  LEU B CB  1 
ATOM   1526 C  CG  . LEU B  1 54  ? -4.539  8.059   66.218  1.00 26.72  ? 303  LEU B CG  1 
ATOM   1527 C  CD1 . LEU B  1 54  ? -4.920  9.415   65.694  1.00 27.13  ? 303  LEU B CD1 1 
ATOM   1528 C  CD2 . LEU B  1 54  ? -5.771  7.325   66.710  1.00 28.62  ? 303  LEU B CD2 1 
ATOM   1529 N  N   . GLN B  1 55  ? -1.554  5.762   63.565  1.00 23.94  ? 304  GLN B N   1 
ATOM   1530 C  CA  . GLN B  1 55  ? -1.128  5.050   62.350  1.00 27.41  ? 304  GLN B CA  1 
ATOM   1531 C  C   . GLN B  1 55  ? -0.817  3.600   62.717  1.00 30.57  ? 304  GLN B C   1 
ATOM   1532 O  O   . GLN B  1 55  ? -1.231  2.628   62.026  1.00 30.97  ? 304  GLN B O   1 
ATOM   1533 C  CB  . GLN B  1 55  ? 0.117   5.683   61.756  1.00 28.37  ? 304  GLN B CB  1 
ATOM   1534 C  CG  . GLN B  1 55  ? 0.495   5.148   60.385  1.00 28.93  ? 304  GLN B CG  1 
ATOM   1535 C  CD  . GLN B  1 55  ? -0.564  5.449   59.357  1.00 31.39  ? 304  GLN B CD  1 
ATOM   1536 O  OE1 . GLN B  1 55  ? -1.112  4.519   58.709  1.00 29.03  ? 304  GLN B OE1 1 
ATOM   1537 N  NE2 . GLN B  1 55  ? -0.858  6.755   59.179  1.00 25.90  ? 304  GLN B NE2 1 
ATOM   1538 N  N   . LEU B  1 56  ? -0.085  3.494   63.817  1.00 37.41  ? 305  LEU B N   1 
ATOM   1539 C  CA  . LEU B  1 56  ? 0.331   2.239   64.405  1.00 37.96  ? 305  LEU B CA  1 
ATOM   1540 C  C   . LEU B  1 56  ? -0.851  1.294   64.609  1.00 36.53  ? 305  LEU B C   1 
ATOM   1541 O  O   . LEU B  1 56  ? -0.742  0.123   64.305  1.00 35.09  ? 305  LEU B O   1 
ATOM   1542 C  CB  . LEU B  1 56  ? 1.045   2.502   65.732  1.00 42.60  ? 305  LEU B CB  1 
ATOM   1543 C  CG  . LEU B  1 56  ? 1.497   1.179   66.366  1.00 47.80  ? 305  LEU B CG  1 
ATOM   1544 C  CD1 . LEU B  1 56  ? 2.883   0.837   65.860  1.00 48.65  ? 305  LEU B CD1 1 
ATOM   1545 C  CD2 . LEU B  1 56  ? 1.387   1.179   67.884  1.00 49.13  ? 305  LEU B CD2 1 
ATOM   1546 N  N   . GLN B  1 57  ? -1.987  1.799   65.068  1.00 36.49  ? 306  GLN B N   1 
ATOM   1547 C  CA  . GLN B  1 57  ? -3.187  0.938   65.229  1.00 38.99  ? 306  GLN B CA  1 
ATOM   1548 C  C   . GLN B  1 57  ? -3.529  0.224   63.935  1.00 34.47  ? 306  GLN B C   1 
ATOM   1549 O  O   . GLN B  1 57  ? -3.920  -0.926  63.964  1.00 38.04  ? 306  GLN B O   1 
ATOM   1550 C  CB  . GLN B  1 57  ? -4.442  1.693   65.717  1.00 35.84  ? 306  GLN B CB  1 
ATOM   1551 C  CG  . GLN B  1 57  ? -4.272  2.477   67.009  1.00 38.39  ? 306  GLN B CG  1 
ATOM   1552 C  CD  . GLN B  1 57  ? -3.481  1.741   68.079  1.00 38.79  ? 306  GLN B CD  1 
ATOM   1553 O  OE1 . GLN B  1 57  ? -3.831  0.621   68.461  1.00 38.14  ? 306  GLN B OE1 1 
ATOM   1554 N  NE2 . GLN B  1 57  ? -2.389  2.371   68.567  1.00 38.33  ? 306  GLN B NE2 1 
ATOM   1555 N  N   . SER B  1 58  ? -3.353  0.895   62.816  1.00 35.10  ? 307  SER B N   1 
ATOM   1556 C  CA  . SER B  1 58  ? -3.697  0.336   61.522  1.00 35.03  ? 307  SER B CA  1 
ATOM   1557 C  C   . SER B  1 58  ? -2.579  -0.431  60.826  1.00 34.50  ? 307  SER B C   1 
ATOM   1558 O  O   . SER B  1 58  ? -2.859  -1.417  60.157  1.00 33.66  ? 307  SER B O   1 
ATOM   1559 C  CB  . SER B  1 58  ? -4.222  1.434   60.592  1.00 35.41  ? 307  SER B CB  1 
ATOM   1560 O  OG  . SER B  1 58  ? -5.615  1.601   60.783  1.00 35.53  ? 307  SER B OG  1 
ATOM   1561 N  N   . SER B  1 59  ? -1.341  0.059   60.910  1.00 33.00  ? 308  SER B N   1 
ATOM   1562 C  CA  . SER B  1 59  ? -0.214  -0.626  60.258  1.00 36.33  ? 308  SER B CA  1 
ATOM   1563 C  C   . SER B  1 59  ? -0.019  -2.014  60.859  1.00 36.89  ? 308  SER B C   1 
ATOM   1564 O  O   . SER B  1 59  ? 0.227   -2.963  60.142  1.00 39.62  ? 308  SER B O   1 
ATOM   1565 C  CB  . SER B  1 59  ? 1.084   0.148   60.373  1.00 34.08  ? 308  SER B CB  1 
ATOM   1566 O  OG  . SER B  1 59  ? 1.372   0.411   61.728  1.00 33.71  ? 308  SER B OG  1 
ATOM   1567 N  N   . ARG B  1 60  ? -0.180  -2.099  62.172  1.00 35.16  ? 309  ARG B N   1 
ATOM   1568 C  CA  . ARG B  1 60  ? 0.014   -3.319  62.933  1.00 37.83  ? 309  ARG B CA  1 
ATOM   1569 C  C   . ARG B  1 60  ? -1.157  -4.276  62.700  1.00 34.13  ? 309  ARG B C   1 
ATOM   1570 O  O   . ARG B  1 60  ? -0.986  -5.467  62.642  1.00 31.54  ? 309  ARG B O   1 
ATOM   1571 C  CB  . ARG B  1 60  ? 0.165   -2.939  64.408  1.00 40.90  ? 309  ARG B CB  1 
ATOM   1572 C  CG  . ARG B  1 60  ? 0.513   -4.054  65.360  1.00 47.32  ? 309  ARG B CG  1 
ATOM   1573 C  CD  . ARG B  1 60  ? 0.506   -3.556  66.810  1.00 51.87  ? 309  ARG B CD  1 
ATOM   1574 N  NE  . ARG B  1 60  ? -0.694  -2.792  67.194  1.00 49.37  ? 309  ARG B NE  1 
ATOM   1575 C  CZ  . ARG B  1 60  ? -0.801  -2.066  68.310  1.00 47.13  ? 309  ARG B CZ  1 
ATOM   1576 N  NH1 . ARG B  1 60  ? 0.210   -1.996  69.162  1.00 49.97  ? 309  ARG B NH1 1 
ATOM   1577 N  NH2 . ARG B  1 60  ? -1.913  -1.390  68.568  1.00 46.36  ? 309  ARG B NH2 1 
ATOM   1578 N  N   . SER B  1 61  ? -2.361  -3.752  62.550  1.00 33.81  ? 310  SER B N   1 
ATOM   1579 C  CA  . SER B  1 61  ? -3.520  -4.636  62.337  1.00 30.19  ? 310  SER B CA  1 
ATOM   1580 C  C   . SER B  1 61  ? -3.765  -5.042  60.883  1.00 30.54  ? 310  SER B C   1 
ATOM   1581 O  O   . SER B  1 61  ? -4.603  -5.913  60.620  1.00 32.03  ? 310  SER B O   1 
ATOM   1582 C  CB  . SER B  1 61  ? -4.749  -3.960  62.870  1.00 29.28  ? 310  SER B CB  1 
ATOM   1583 O  OG  . SER B  1 61  ? -4.965  -2.776  62.126  1.00 28.43  ? 310  SER B OG  1 
ATOM   1584 N  N   . ASN B  1 62  ? -3.062  -4.410  59.957  1.00 29.39  ? 311  ASN B N   1 
ATOM   1585 C  CA  . ASN B  1 62  ? -3.340  -4.519  58.534  1.00 32.54  ? 311  ASN B CA  1 
ATOM   1586 C  C   . ASN B  1 62  ? -4.783  -4.106  58.142  1.00 32.20  ? 311  ASN B C   1 
ATOM   1587 O  O   . ASN B  1 62  ? -5.300  -4.557  57.147  1.00 31.20  ? 311  ASN B O   1 
ATOM   1588 C  CB  . ASN B  1 62  ? -3.050  -5.923  58.081  1.00 34.63  ? 311  ASN B CB  1 
ATOM   1589 C  CG  . ASN B  1 62  ? -1.650  -6.338  58.442  1.00 37.66  ? 311  ASN B CG  1 
ATOM   1590 O  OD1 . ASN B  1 62  ? -0.691  -5.710  57.973  1.00 38.77  ? 311  ASN B OD1 1 
ATOM   1591 N  ND2 . ASN B  1 62  ? -1.511  -7.383  59.279  1.00 34.91  ? 311  ASN B ND2 1 
ATOM   1592 N  N   . ARG B  1 63  ? -5.397  -3.243  58.938  1.00 29.67  ? 312  ARG B N   1 
ATOM   1593 C  CA  . ARG B  1 63  ? -6.747  -2.822  58.708  1.00 30.67  ? 312  ARG B CA  1 
ATOM   1594 C  C   . ARG B  1 63  ? -6.820  -1.374  58.236  1.00 29.28  ? 312  ARG B C   1 
ATOM   1595 O  O   . ARG B  1 63  ? -5.897  -0.623  58.416  1.00 30.49  ? 312  ARG B O   1 
ATOM   1596 C  CB  . ARG B  1 63  ? -7.531  -3.068  59.975  1.00 34.66  ? 312  ARG B CB  1 
ATOM   1597 C  CG  . ARG B  1 63  ? -7.511  -4.571  60.252  1.00 38.41  ? 312  ARG B CG  1 
ATOM   1598 C  CD  . ARG B  1 63  ? -8.762  -5.087  60.904  1.00 39.29  ? 312  ARG B CD  1 
ATOM   1599 N  NE  . ARG B  1 63  ? -8.645  -6.498  61.341  1.00 40.11  ? 312  ARG B NE  1 
ATOM   1600 C  CZ  . ARG B  1 63  ? -9.049  -7.576  60.651  1.00 36.13  ? 312  ARG B CZ  1 
ATOM   1601 N  NH1 . ARG B  1 63  ? -8.912  -8.783  61.223  1.00 34.35  ? 312  ARG B NH1 1 
ATOM   1602 N  NH2 . ARG B  1 63  ? -9.560  -7.477  59.406  1.00 33.52  ? 312  ARG B NH2 1 
ATOM   1603 N  N   . PHE B  1 64  ? -7.896  -1.038  57.540  1.00 26.39  ? 313  PHE B N   1 
ATOM   1604 C  CA  . PHE B  1 64  ? -8.155  0.306   57.019  1.00 25.55  ? 313  PHE B CA  1 
ATOM   1605 C  C   . PHE B  1 64  ? -9.132  1.000   57.905  1.00 25.98  ? 313  PHE B C   1 
ATOM   1606 O  O   . PHE B  1 64  ? -10.146 0.396   58.275  1.00 24.20  ? 313  PHE B O   1 
ATOM   1607 C  CB  . PHE B  1 64  ? -8.769  0.202   55.636  1.00 26.07  ? 313  PHE B CB  1 
ATOM   1608 C  CG  . PHE B  1 64  ? -7.909  -0.552  54.663  1.00 26.67  ? 313  PHE B CG  1 
ATOM   1609 C  CD1 . PHE B  1 64  ? -6.528  -0.492  54.756  1.00 26.35  ? 313  PHE B CD1 1 
ATOM   1610 C  CD2 . PHE B  1 64  ? -8.484  -1.292  53.641  1.00 26.92  ? 313  PHE B CD2 1 
ATOM   1611 C  CE1 . PHE B  1 64  ? -5.720  -1.139  53.822  1.00 29.95  ? 313  PHE B CE1 1 
ATOM   1612 C  CE2 . PHE B  1 64  ? -7.681  -1.959  52.720  1.00 28.61  ? 313  PHE B CE2 1 
ATOM   1613 C  CZ  . PHE B  1 64  ? -6.297  -1.876  52.815  1.00 27.71  ? 313  PHE B CZ  1 
ATOM   1614 N  N   . THR B  1 65  ? -8.839  2.271   58.229  1.00 26.31  ? 314  THR B N   1 
ATOM   1615 C  CA  . THR B  1 65  ? -9.456  2.959   59.373  1.00 26.49  ? 314  THR B CA  1 
ATOM   1616 C  C   . THR B  1 65  ? -9.719  4.428   58.994  1.00 24.25  ? 314  THR B C   1 
ATOM   1617 O  O   . THR B  1 65  ? -8.799  5.165   58.648  1.00 24.12  ? 314  THR B O   1 
ATOM   1618 C  CB  . THR B  1 65  ? -8.564  2.836   60.656  1.00 25.79  ? 314  THR B CB  1 
ATOM   1619 O  OG1 . THR B  1 65  ? -8.250  1.453   60.905  1.00 28.48  ? 314  THR B OG1 1 
ATOM   1620 C  CG2 . THR B  1 65  ? -9.226  3.418   61.902  1.00 24.68  ? 314  THR B CG2 1 
ATOM   1621 N  N   . TRP B  1 66  ? -10.986 4.827   59.051  1.00 21.50  ? 315  TRP B N   1 
ATOM   1622 C  CA  . TRP B  1 66  ? -11.323 6.216   58.815  1.00 23.09  ? 315  TRP B CA  1 
ATOM   1623 C  C   . TRP B  1 66  ? -10.711 7.137   59.851  1.00 23.48  ? 315  TRP B C   1 
ATOM   1624 O  O   . TRP B  1 66  ? -10.701 6.830   61.030  1.00 23.08  ? 315  TRP B O   1 
ATOM   1625 C  CB  . TRP B  1 66  ? -12.852 6.467   58.858  1.00 20.88  ? 315  TRP B CB  1 
ATOM   1626 C  CG  . TRP B  1 66  ? -13.618 5.898   57.792  1.00 18.37  ? 315  TRP B CG  1 
ATOM   1627 C  CD1 . TRP B  1 66  ? -14.700 5.065   57.915  1.00 19.52  ? 315  TRP B CD1 1 
ATOM   1628 C  CD2 . TRP B  1 66  ? -13.401 6.064   56.376  1.00 18.76  ? 315  TRP B CD2 1 
ATOM   1629 N  NE1 . TRP B  1 66  ? -15.148 4.685   56.659  1.00 19.71  ? 315  TRP B NE1 1 
ATOM   1630 C  CE2 . TRP B  1 66  ? -14.389 5.316   55.706  1.00 19.03  ? 315  TRP B CE2 1 
ATOM   1631 C  CE3 . TRP B  1 66  ? -12.480 6.788   55.611  1.00 20.08  ? 315  TRP B CE3 1 
ATOM   1632 C  CZ2 . TRP B  1 66  ? -14.460 5.251   54.299  1.00 19.57  ? 315  TRP B CZ2 1 
ATOM   1633 C  CZ3 . TRP B  1 66  ? -12.549 6.716   54.232  1.00 19.29  ? 315  TRP B CZ3 1 
ATOM   1634 C  CH2 . TRP B  1 66  ? -13.539 5.953   53.598  1.00 18.69  ? 315  TRP B CH2 1 
ATOM   1635 N  N   . MET B  1 67  ? -10.256 8.304   59.396  1.00 26.75  ? 316  MET B N   1 
ATOM   1636 C  CA  . MET B  1 67  ? -10.068 9.460   60.293  1.00 25.60  ? 316  MET B CA  1 
ATOM   1637 C  C   . MET B  1 67  ? -11.066 10.590  59.930  1.00 26.09  ? 316  MET B C   1 
ATOM   1638 O  O   . MET B  1 67  ? -11.709 10.533  58.919  1.00 25.26  ? 316  MET B O   1 
ATOM   1639 C  CB  . MET B  1 67  ? -8.639  9.983   60.215  1.00 25.24  ? 316  MET B CB  1 
ATOM   1640 C  CG  . MET B  1 67  ? -8.319  10.718  58.904  1.00 27.11  ? 316  MET B CG  1 
ATOM   1641 S  SD  . MET B  1 67  ? -6.562  11.044  58.775  1.00 25.09  ? 316  MET B SD  1 
ATOM   1642 C  CE  . MET B  1 67  ? -5.990  9.416   58.286  1.00 25.34  ? 316  MET B CE  1 
ATOM   1643 N  N   . GLY B  1 68  ? -11.168 11.624  60.770  1.00 26.60  ? 317  GLY B N   1 
ATOM   1644 C  CA  . GLY B  1 68  ? -12.147 12.711  60.593  1.00 23.19  ? 317  GLY B CA  1 
ATOM   1645 C  C   . GLY B  1 68  ? -11.642 13.789  59.669  1.00 23.22  ? 317  GLY B C   1 
ATOM   1646 O  O   . GLY B  1 68  ? -11.632 14.974  60.016  1.00 22.22  ? 317  GLY B O   1 
ATOM   1647 N  N   . LEU B  1 69  ? -11.245 13.392  58.471  1.00 22.44  ? 318  LEU B N   1 
ATOM   1648 C  CA  . LEU B  1 69  ? -10.640 14.314  57.511  1.00 23.53  ? 318  LEU B CA  1 
ATOM   1649 C  C   . LEU B  1 69  ? -11.232 14.067  56.099  1.00 25.04  ? 318  LEU B C   1 
ATOM   1650 O  O   . LEU B  1 69  ? -11.362 12.903  55.665  1.00 23.53  ? 318  LEU B O   1 
ATOM   1651 C  CB  . LEU B  1 69  ? -9.143  14.094  57.543  1.00 22.37  ? 318  LEU B CB  1 
ATOM   1652 C  CG  . LEU B  1 69  ? -8.346  14.886  56.559  1.00 24.03  ? 318  LEU B CG  1 
ATOM   1653 C  CD1 . LEU B  1 69  ? -8.321  16.339  57.043  1.00 24.11  ? 318  LEU B CD1 1 
ATOM   1654 C  CD2 . LEU B  1 69  ? -6.943  14.316  56.453  1.00 23.79  ? 318  LEU B CD2 1 
ATOM   1655 N  N   . SER B  1 70  ? -11.635 15.139  55.412  1.00 25.54  ? 319  SER B N   1 
ATOM   1656 C  CA  . SER B  1 70  ? -12.242 15.037  54.080  1.00 26.45  ? 319  SER B CA  1 
ATOM   1657 C  C   . SER B  1 70  ? -12.026 16.249  53.161  1.00 28.86  ? 319  SER B C   1 
ATOM   1658 O  O   . SER B  1 70  ? -11.783 17.373  53.624  1.00 27.48  ? 319  SER B O   1 
ATOM   1659 C  CB  . SER B  1 70  ? -13.726 14.760  54.173  1.00 25.87  ? 319  SER B CB  1 
ATOM   1660 O  OG  . SER B  1 70  ? -14.460 15.878  54.569  1.00 23.45  ? 319  SER B OG  1 
ATOM   1661 N  N   . ASP B  1 71  ? -12.112 16.002  51.859  1.00 25.87  ? 320  ASP B N   1 
ATOM   1662 C  CA  . ASP B  1 71  ? -12.199 17.084  50.887  1.00 27.16  ? 320  ASP B CA  1 
ATOM   1663 C  C   . ASP B  1 71  ? -13.542 17.092  50.139  1.00 26.80  ? 320  ASP B C   1 
ATOM   1664 O  O   . ASP B  1 71  ? -13.631 17.598  49.009  1.00 24.69  ? 320  ASP B O   1 
ATOM   1665 C  CB  . ASP B  1 71  ? -11.001 17.127  49.935  1.00 25.19  ? 320  ASP B CB  1 
ATOM   1666 C  CG  . ASP B  1 71  ? -11.007 16.031  48.915  1.00 26.07  ? 320  ASP B CG  1 
ATOM   1667 O  OD1 . ASP B  1 71  ? -11.758 15.026  49.066  1.00 21.25  ? 320  ASP B OD1 1 
ATOM   1668 O  OD2 . ASP B  1 71  ? -10.271 16.210  47.894  1.00 28.13  ? 320  ASP B OD2 1 
ATOM   1669 N  N   . LEU B  1 72  ? -14.567 16.530  50.783  1.00 24.57  ? 321  LEU B N   1 
ATOM   1670 C  CA  . LEU B  1 72  ? -15.922 16.554  50.270  1.00 25.85  ? 321  LEU B CA  1 
ATOM   1671 C  C   . LEU B  1 72  ? -16.402 17.971  49.909  1.00 28.54  ? 321  LEU B C   1 
ATOM   1672 O  O   . LEU B  1 72  ? -16.971 18.191  48.842  1.00 34.03  ? 321  LEU B O   1 
ATOM   1673 C  CB  . LEU B  1 72  ? -16.901 16.001  51.302  1.00 25.14  ? 321  LEU B CB  1 
ATOM   1674 C  CG  . LEU B  1 72  ? -16.962 14.465  51.416  1.00 26.79  ? 321  LEU B CG  1 
ATOM   1675 C  CD1 . LEU B  1 72  ? -17.528 14.049  52.767  1.00 25.99  ? 321  LEU B CD1 1 
ATOM   1676 C  CD2 . LEU B  1 72  ? -17.801 13.918  50.285  1.00 26.40  ? 321  LEU B CD2 1 
ATOM   1677 N  N   . ASN B  1 73  ? -16.198 18.901  50.826  1.00 28.50  ? 322  ASN B N   1 
ATOM   1678 C  CA  A ASN B  1 73  ? -16.688 20.264  50.674  0.30 28.76  ? 322  ASN B CA  1 
ATOM   1679 C  CA  B ASN B  1 73  ? -16.680 20.254  50.653  0.70 32.16  ? 322  ASN B CA  1 
ATOM   1680 C  C   . ASN B  1 73  ? -15.924 20.961  49.534  1.00 30.63  ? 322  ASN B C   1 
ATOM   1681 O  O   . ASN B  1 73  ? -16.544 21.486  48.643  1.00 31.26  ? 322  ASN B O   1 
ATOM   1682 C  CB  A ASN B  1 73  ? -16.605 21.047  52.006  0.30 27.42  ? 322  ASN B CB  1 
ATOM   1683 C  CB  B ASN B  1 73  ? -16.588 21.029  51.962  0.70 34.59  ? 322  ASN B CB  1 
ATOM   1684 C  CG  A ASN B  1 73  ? -17.638 20.583  53.049  0.30 26.17  ? 322  ASN B CG  1 
ATOM   1685 C  CG  B ASN B  1 73  ? -17.226 22.392  51.868  0.70 39.47  ? 322  ASN B CG  1 
ATOM   1686 O  OD1 A ASN B  1 73  ? -18.176 19.480  52.978  0.30 25.40  ? 322  ASN B OD1 1 
ATOM   1687 O  OD1 B ASN B  1 73  ? -16.670 23.373  52.378  0.70 40.22  ? 322  ASN B OD1 1 
ATOM   1688 N  ND2 A ASN B  1 73  ? -17.898 21.432  54.034  0.30 25.60  ? 322  ASN B ND2 1 
ATOM   1689 N  ND2 B ASN B  1 73  ? -18.391 22.476  51.191  0.70 38.50  ? 322  ASN B ND2 1 
ATOM   1690 N  N   . GLN B  1 74  ? -14.590 20.891  49.554  1.00 29.80  ? 323  GLN B N   1 
ATOM   1691 C  CA  . GLN B  1 74  ? -13.708 21.534  48.550  1.00 28.73  ? 323  GLN B CA  1 
ATOM   1692 C  C   . GLN B  1 74  ? -12.645 20.591  48.032  1.00 24.44  ? 323  GLN B C   1 
ATOM   1693 O  O   . GLN B  1 74  ? -11.668 20.345  48.710  1.00 24.82  ? 323  GLN B O   1 
ATOM   1694 C  CB  . GLN B  1 74  ? -13.001 22.777  49.167  1.00 30.37  ? 323  GLN B CB  1 
ATOM   1695 C  CG  . GLN B  1 74  ? -13.956 23.771  49.874  1.00 36.06  ? 323  GLN B CG  1 
ATOM   1696 C  CD  . GLN B  1 74  ? -13.241 24.820  50.775  1.00 38.32  ? 323  GLN B CD  1 
ATOM   1697 O  OE1 . GLN B  1 74  ? -12.272 24.491  51.449  1.00 37.03  ? 323  GLN B OE1 1 
ATOM   1698 N  NE2 . GLN B  1 74  ? -13.730 26.096  50.765  1.00 36.47  ? 323  GLN B NE2 1 
ATOM   1699 N  N   . GLU B  1 75  ? -12.800 20.086  46.810  1.00 27.63  ? 324  GLU B N   1 
ATOM   1700 C  CA  . GLU B  1 75  ? -11.873 19.098  46.256  1.00 26.82  ? 324  GLU B CA  1 
ATOM   1701 C  C   . GLU B  1 75  ? -10.455 19.623  46.374  1.00 27.53  ? 324  GLU B C   1 
ATOM   1702 O  O   . GLU B  1 75  ? -10.169 20.750  45.979  1.00 28.67  ? 324  GLU B O   1 
ATOM   1703 C  CB  . GLU B  1 75  ? -12.208 18.763  44.798  1.00 27.33  ? 324  GLU B CB  1 
ATOM   1704 C  CG  . GLU B  1 75  ? -11.186 17.810  44.156  1.00 27.81  ? 324  GLU B CG  1 
ATOM   1705 C  CD  . GLU B  1 75  ? -11.123 16.435  44.841  1.00 29.64  ? 324  GLU B CD  1 
ATOM   1706 O  OE1 . GLU B  1 75  ? -12.176 15.927  45.335  1.00 32.59  ? 324  GLU B OE1 1 
ATOM   1707 O  OE2 . GLU B  1 75  ? -10.011 15.853  44.910  1.00 29.49  ? 324  GLU B OE2 1 
ATOM   1708 N  N   . GLY B  1 76  ? -9.561  18.815  46.932  1.00 30.25  ? 325  GLY B N   1 
ATOM   1709 C  CA  . GLY B  1 76  ? -8.134  19.185  46.999  1.00 28.89  ? 325  GLY B CA  1 
ATOM   1710 C  C   . GLY B  1 76  ? -7.734  19.939  48.261  1.00 29.25  ? 325  GLY B C   1 
ATOM   1711 O  O   . GLY B  1 76  ? -6.559  20.007  48.544  1.00 28.56  ? 325  GLY B O   1 
ATOM   1712 N  N   . THR B  1 77  ? -8.718  20.471  48.999  1.00 25.38  ? 326  THR B N   1 
ATOM   1713 C  CA  . THR B  1 77  ? -8.492  21.183  50.228  1.00 29.71  ? 326  THR B CA  1 
ATOM   1714 C  C   . THR B  1 77  ? -9.119  20.375  51.370  1.00 27.01  ? 326  THR B C   1 
ATOM   1715 O  O   . THR B  1 77  ? -10.328 20.283  51.475  1.00 23.71  ? 326  THR B O   1 
ATOM   1716 C  CB  . THR B  1 77  ? -9.075  22.612  50.165  1.00 30.24  ? 326  THR B CB  1 
ATOM   1717 O  OG1 . THR B  1 77  ? -8.285  23.399  49.263  1.00 32.61  ? 326  THR B OG1 1 
ATOM   1718 C  CG2 . THR B  1 77  ? -9.042  23.242  51.547  1.00 29.03  ? 326  THR B CG2 1 
ATOM   1719 N  N   . TRP B  1 78  ? -8.252  19.736  52.155  1.00 26.27  ? 327  TRP B N   1 
ATOM   1720 C  CA  . TRP B  1 78  ? -8.661  18.772  53.185  1.00 25.43  ? 327  TRP B CA  1 
ATOM   1721 C  C   . TRP B  1 78  ? -8.859  19.501  54.508  1.00 25.20  ? 327  TRP B C   1 
ATOM   1722 O  O   . TRP B  1 78  ? -8.059  20.354  54.886  1.00 25.88  ? 327  TRP B O   1 
ATOM   1723 C  CB  . TRP B  1 78  ? -7.622  17.659  53.342  1.00 23.86  ? 327  TRP B CB  1 
ATOM   1724 C  CG  . TRP B  1 78  ? -7.532  16.841  52.126  1.00 24.98  ? 327  TRP B CG  1 
ATOM   1725 C  CD1 . TRP B  1 78  ? -6.862  17.130  50.969  1.00 25.33  ? 327  TRP B CD1 1 
ATOM   1726 C  CD2 . TRP B  1 78  ? -8.210  15.592  51.906  1.00 24.49  ? 327  TRP B CD2 1 
ATOM   1727 N  NE1 . TRP B  1 78  ? -7.068  16.116  50.049  1.00 26.05  ? 327  TRP B NE1 1 
ATOM   1728 C  CE2 . TRP B  1 78  ? -7.897  15.169  50.603  1.00 24.61  ? 327  TRP B CE2 1 
ATOM   1729 C  CE3 . TRP B  1 78  ? -9.071  14.814  52.687  1.00 26.52  ? 327  TRP B CE3 1 
ATOM   1730 C  CZ2 . TRP B  1 78  ? -8.397  14.000  50.065  1.00 25.81  ? 327  TRP B CZ2 1 
ATOM   1731 C  CZ3 . TRP B  1 78  ? -9.564  13.622  52.168  1.00 29.81  ? 327  TRP B CZ3 1 
ATOM   1732 C  CH2 . TRP B  1 78  ? -9.217  13.229  50.849  1.00 26.99  ? 327  TRP B CH2 1 
ATOM   1733 N  N   . GLN B  1 79  ? -9.917  19.115  55.192  1.00 24.25  ? 328  GLN B N   1 
ATOM   1734 C  CA  . GLN B  1 79  ? -10.389 19.754  56.371  1.00 29.08  ? 328  GLN B CA  1 
ATOM   1735 C  C   . GLN B  1 79  ? -10.799 18.705  57.387  1.00 25.97  ? 328  GLN B C   1 
ATOM   1736 O  O   . GLN B  1 79  ? -11.478 17.727  57.060  1.00 25.83  ? 328  GLN B O   1 
ATOM   1737 C  CB  . GLN B  1 79  ? -11.619 20.507  55.934  1.00 36.30  ? 328  GLN B CB  1 
ATOM   1738 C  CG  . GLN B  1 79  ? -12.208 21.465  56.914  1.00 45.35  ? 328  GLN B CG  1 
ATOM   1739 C  CD  . GLN B  1 79  ? -13.341 22.226  56.275  1.00 49.57  ? 328  GLN B CD  1 
ATOM   1740 O  OE1 . GLN B  1 79  ? -14.325 22.547  56.943  1.00 57.93  ? 328  GLN B OE1 1 
ATOM   1741 N  NE2 . GLN B  1 79  ? -13.214 22.512  54.954  1.00 49.81  ? 328  GLN B NE2 1 
ATOM   1742 N  N   . TRP B  1 80  ? -10.439 18.940  58.630  1.00 26.20  ? 329  TRP B N   1 
ATOM   1743 C  CA  . TRP B  1 80  ? -10.834 18.064  59.724  1.00 26.34  ? 329  TRP B CA  1 
ATOM   1744 C  C   . TRP B  1 80  ? -12.269 18.319  60.075  1.00 25.90  ? 329  TRP B C   1 
ATOM   1745 O  O   . TRP B  1 80  ? -12.767 19.396  59.871  1.00 27.99  ? 329  TRP B O   1 
ATOM   1746 C  CB  . TRP B  1 80  ? -9.940  18.246  60.948  1.00 25.42  ? 329  TRP B CB  1 
ATOM   1747 C  CG  . TRP B  1 80  ? -8.543  17.925  60.705  1.00 24.68  ? 329  TRP B CG  1 
ATOM   1748 C  CD1 . TRP B  1 80  ? -7.545  18.798  60.408  1.00 24.70  ? 329  TRP B CD1 1 
ATOM   1749 C  CD2 . TRP B  1 80  ? -7.949  16.612  60.700  1.00 26.08  ? 329  TRP B CD2 1 
ATOM   1750 N  NE1 . TRP B  1 80  ? -6.365  18.119  60.240  1.00 26.06  ? 329  TRP B NE1 1 
ATOM   1751 C  CE2 . TRP B  1 80  ? -6.590  16.774  60.403  1.00 25.19  ? 329  TRP B CE2 1 
ATOM   1752 C  CE3 . TRP B  1 80  ? -8.450  15.321  60.895  1.00 24.22  ? 329  TRP B CE3 1 
ATOM   1753 C  CZ2 . TRP B  1 80  ? -5.717  15.687  60.295  1.00 28.51  ? 329  TRP B CZ2 1 
ATOM   1754 C  CZ3 . TRP B  1 80  ? -7.594  14.255  60.794  1.00 24.53  ? 329  TRP B CZ3 1 
ATOM   1755 C  CH2 . TRP B  1 80  ? -6.241  14.427  60.522  1.00 24.23  ? 329  TRP B CH2 1 
ATOM   1756 N  N   . VAL B  1 81  ? -12.944 17.322  60.624  1.00 28.41  ? 330  VAL B N   1 
ATOM   1757 C  CA  . VAL B  1 81  ? -14.363 17.477  60.895  1.00 30.47  ? 330  VAL B CA  1 
ATOM   1758 C  C   . VAL B  1 81  ? -14.677 18.504  62.002  1.00 30.09  ? 330  VAL B C   1 
ATOM   1759 O  O   . VAL B  1 81  ? -15.826 18.853  62.166  1.00 28.73  ? 330  VAL B O   1 
ATOM   1760 C  CB  . VAL B  1 81  ? -15.054 16.178  61.284  1.00 31.47  ? 330  VAL B CB  1 
ATOM   1761 C  CG1 . VAL B  1 81  ? -15.005 15.208  60.128  1.00 33.13  ? 330  VAL B CG1 1 
ATOM   1762 C  CG2 . VAL B  1 81  ? -14.441 15.621  62.555  1.00 30.57  ? 330  VAL B CG2 1 
ATOM   1763 N  N   . ASP B  1 82  ? -13.678 18.960  62.748  1.00 29.10  ? 331  ASP B N   1 
ATOM   1764 C  CA  . ASP B  1 82  ? -13.867 20.091  63.657  1.00 30.07  ? 331  ASP B CA  1 
ATOM   1765 C  C   . ASP B  1 82  ? -13.699 21.438  62.928  1.00 30.68  ? 331  ASP B C   1 
ATOM   1766 O  O   . ASP B  1 82  ? -13.845 22.474  63.531  1.00 33.39  ? 331  ASP B O   1 
ATOM   1767 C  CB  . ASP B  1 82  ? -12.904 20.020  64.844  1.00 28.54  ? 331  ASP B CB  1 
ATOM   1768 C  CG  . ASP B  1 82  ? -11.469 20.237  64.438  1.00 31.65  ? 331  ASP B CG  1 
ATOM   1769 O  OD1 . ASP B  1 82  ? -11.234 20.359  63.203  1.00 36.23  ? 331  ASP B OD1 1 
ATOM   1770 O  OD2 . ASP B  1 82  ? -10.549 20.238  65.312  1.00 29.69  ? 331  ASP B OD2 1 
ATOM   1771 N  N   . GLY B  1 83  ? -13.354 21.431  61.649  1.00 27.95  ? 332  GLY B N   1 
ATOM   1772 C  CA  . GLY B  1 83  ? -13.269 22.660  60.898  1.00 26.85  ? 332  GLY B CA  1 
ATOM   1773 C  C   . GLY B  1 83  ? -11.848 23.066  60.642  1.00 28.46  ? 332  GLY B C   1 
ATOM   1774 O  O   . GLY B  1 83  ? -11.573 23.959  59.782  1.00 32.13  ? 332  GLY B O   1 
ATOM   1775 N  N   . SER B  1 84  ? -10.918 22.463  61.372  1.00 26.57  ? 333  SER B N   1 
ATOM   1776 C  CA  . SER B  1 84  ? -9.528  22.921  61.277  1.00 28.23  ? 333  SER B CA  1 
ATOM   1777 C  C   . SER B  1 84  ? -8.973  22.485  59.889  1.00 27.85  ? 333  SER B C   1 
ATOM   1778 O  O   . SER B  1 84  ? -9.498  21.599  59.268  1.00 29.36  ? 333  SER B O   1 
ATOM   1779 C  CB  . SER B  1 84  ? -8.688  22.417  62.471  1.00 28.70  ? 333  SER B CB  1 
ATOM   1780 O  OG  . SER B  1 84  ? -8.748  20.982  62.653  1.00 31.22  ? 333  SER B OG  1 
ATOM   1781 N  N   . PRO B  1 85  ? -7.978  23.174  59.383  1.00 28.71  ? 334  PRO B N   1 
ATOM   1782 C  CA  . PRO B  1 85  ? -7.333  22.834  58.124  1.00 27.11  ? 334  PRO B CA  1 
ATOM   1783 C  C   . PRO B  1 85  ? -6.306  21.720  58.278  1.00 29.32  ? 334  PRO B C   1 
ATOM   1784 O  O   . PRO B  1 85  ? -5.820  21.438  59.384  1.00 28.85  ? 334  PRO B O   1 
ATOM   1785 C  CB  . PRO B  1 85  ? -6.633  24.152  57.729  1.00 29.82  ? 334  PRO B CB  1 
ATOM   1786 C  CG  . PRO B  1 85  ? -6.390  24.862  59.028  1.00 30.10  ? 334  PRO B CG  1 
ATOM   1787 C  CD  . PRO B  1 85  ? -7.558  24.488  59.919  1.00 29.87  ? 334  PRO B CD  1 
ATOM   1788 N  N   . LEU B  1 86  ? -5.994  21.051  57.175  1.00 30.05  ? 335  LEU B N   1 
ATOM   1789 C  CA  . LEU B  1 86  ? -4.854  20.192  57.143  1.00 29.79  ? 335  LEU B CA  1 
ATOM   1790 C  C   . LEU B  1 86  ? -3.627  21.063  57.045  1.00 32.28  ? 335  LEU B C   1 
ATOM   1791 O  O   . LEU B  1 86  ? -3.409  21.725  56.029  1.00 36.20  ? 335  LEU B O   1 
ATOM   1792 C  CB  . LEU B  1 86  ? -4.891  19.234  55.943  1.00 30.58  ? 335  LEU B CB  1 
ATOM   1793 C  CG  . LEU B  1 86  ? -3.832  18.130  55.901  1.00 28.44  ? 335  LEU B CG  1 
ATOM   1794 C  CD1 . LEU B  1 86  ? -3.855  17.312  57.170  1.00 30.60  ? 335  LEU B CD1 1 
ATOM   1795 C  CD2 . LEU B  1 86  ? -4.079  17.227  54.716  1.00 30.96  ? 335  LEU B CD2 1 
ATOM   1796 N  N   . LEU B  1 87  ? -2.791  21.015  58.063  1.00 34.70  ? 336  LEU B N   1 
ATOM   1797 C  CA  . LEU B  1 87  ? -1.560  21.818  58.088  1.00 36.54  ? 336  LEU B CA  1 
ATOM   1798 C  C   . LEU B  1 87  ? -0.472  21.227  57.206  1.00 39.53  ? 336  LEU B C   1 
ATOM   1799 O  O   . LEU B  1 87  ? -0.396  19.991  57.055  1.00 37.00  ? 336  LEU B O   1 
ATOM   1800 C  CB  . LEU B  1 87  ? -1.009  21.899  59.504  1.00 35.78  ? 336  LEU B CB  1 
ATOM   1801 C  CG  . LEU B  1 87  ? -1.933  22.501  60.548  1.00 36.80  ? 336  LEU B CG  1 
ATOM   1802 C  CD1 . LEU B  1 87  ? -1.287  22.263  61.901  1.00 37.60  ? 336  LEU B CD1 1 
ATOM   1803 C  CD2 . LEU B  1 87  ? -2.188  23.991  60.307  1.00 37.57  ? 336  LEU B CD2 1 
ATOM   1804 N  N   . PRO B  1 88  ? 0.398   22.094  56.646  1.00 39.37  ? 337  PRO B N   1 
ATOM   1805 C  CA  . PRO B  1 88  ? 1.389   21.614  55.696  1.00 38.70  ? 337  PRO B CA  1 
ATOM   1806 C  C   . PRO B  1 88  ? 2.320   20.612  56.282  1.00 36.19  ? 337  PRO B C   1 
ATOM   1807 O  O   . PRO B  1 88  ? 2.745   19.694  55.586  1.00 36.15  ? 337  PRO B O   1 
ATOM   1808 C  CB  . PRO B  1 88  ? 2.143   22.887  55.290  1.00 41.78  ? 337  PRO B CB  1 
ATOM   1809 C  CG  . PRO B  1 88  ? 1.121   23.970  55.415  1.00 42.66  ? 337  PRO B CG  1 
ATOM   1810 C  CD  . PRO B  1 88  ? 0.299   23.569  56.620  1.00 43.62  ? 337  PRO B CD  1 
ATOM   1811 N  N   . SER B  1 89  ? 2.593   20.726  57.567  1.00 38.73  ? 338  SER B N   1 
ATOM   1812 C  CA  . SER B  1 89  ? 3.489   19.764  58.222  1.00 40.69  ? 338  SER B CA  1 
ATOM   1813 C  C   . SER B  1 89  ? 2.880   18.341  58.289  1.00 41.97  ? 338  SER B C   1 
ATOM   1814 O  O   . SER B  1 89  ? 3.603   17.408  58.557  1.00 44.32  ? 338  SER B O   1 
ATOM   1815 C  CB  . SER B  1 89  ? 3.874   20.236  59.619  1.00 39.18  ? 338  SER B CB  1 
ATOM   1816 O  OG  . SER B  1 89  ? 2.742   20.301  60.464  1.00 45.18  ? 338  SER B OG  1 
ATOM   1817 N  N   . PHE B  1 90  ? 1.568   18.190  58.067  1.00 39.26  ? 339  PHE B N   1 
ATOM   1818 C  CA  . PHE B  1 90  ? 0.912   16.859  58.098  1.00 38.19  ? 339  PHE B CA  1 
ATOM   1819 C  C   . PHE B  1 90  ? 0.871   16.183  56.723  1.00 38.03  ? 339  PHE B C   1 
ATOM   1820 O  O   . PHE B  1 90  ? 0.584   14.987  56.623  1.00 34.17  ? 339  PHE B O   1 
ATOM   1821 C  CB  . PHE B  1 90  ? -0.499  16.956  58.687  1.00 36.31  ? 339  PHE B CB  1 
ATOM   1822 C  CG  . PHE B  1 90  ? -0.508  17.163  60.167  1.00 40.23  ? 339  PHE B CG  1 
ATOM   1823 C  CD1 . PHE B  1 90  ? 0.050   18.307  60.730  1.00 41.06  ? 339  PHE B CD1 1 
ATOM   1824 C  CD2 . PHE B  1 90  ? -1.054  16.216  61.010  1.00 43.59  ? 339  PHE B CD2 1 
ATOM   1825 C  CE1 . PHE B  1 90  ? 0.054   18.503  62.097  1.00 42.02  ? 339  PHE B CE1 1 
ATOM   1826 C  CE2 . PHE B  1 90  ? -1.049  16.404  62.389  1.00 44.50  ? 339  PHE B CE2 1 
ATOM   1827 C  CZ  . PHE B  1 90  ? -0.494  17.549  62.931  1.00 42.30  ? 339  PHE B CZ  1 
ATOM   1828 N  N   . LYS B  1 91  ? 1.168   16.929  55.660  1.00 34.86  ? 340  LYS B N   1 
ATOM   1829 C  CA  . LYS B  1 91  ? 1.004   16.389  54.313  1.00 34.25  ? 340  LYS B CA  1 
ATOM   1830 C  C   . LYS B  1 91  ? 1.969   15.260  54.077  1.00 32.67  ? 340  LYS B C   1 
ATOM   1831 O  O   . LYS B  1 91  ? 1.725   14.377  53.242  1.00 34.37  ? 340  LYS B O   1 
ATOM   1832 C  CB  . LYS B  1 91  ? 1.188   17.481  53.242  1.00 37.96  ? 340  LYS B CB  1 
ATOM   1833 C  CG  . LYS B  1 91  ? 0.036   18.478  53.156  1.00 43.21  ? 340  LYS B CG  1 
ATOM   1834 C  CD  . LYS B  1 91  ? 0.300   19.558  52.107  1.00 50.48  ? 340  LYS B CD  1 
ATOM   1835 C  CE  . LYS B  1 91  ? -0.910  20.495  51.908  1.00 60.03  ? 340  LYS B CE  1 
ATOM   1836 N  NZ  . LYS B  1 91  ? -1.489  21.089  53.160  1.00 58.85  ? 340  LYS B NZ  1 
ATOM   1837 N  N   . GLN B  1 92  ? 3.092   15.291  54.780  1.00 29.15  ? 341  GLN B N   1 
ATOM   1838 C  CA  . GLN B  1 92  ? 4.047   14.214  54.724  1.00 31.50  ? 341  GLN B CA  1 
ATOM   1839 C  C   . GLN B  1 92  ? 3.444   12.816  55.040  1.00 32.22  ? 341  GLN B C   1 
ATOM   1840 O  O   . GLN B  1 92  ? 3.999   11.806  54.623  1.00 29.98  ? 341  GLN B O   1 
ATOM   1841 C  CB  . GLN B  1 92  ? 5.191   14.489  55.700  1.00 33.45  ? 341  GLN B CB  1 
ATOM   1842 C  CG  . GLN B  1 92  ? 4.773   14.452  57.171  1.00 36.03  ? 341  GLN B CG  1 
ATOM   1843 C  CD  . GLN B  1 92  ? 5.973   14.629  58.100  1.00 40.35  ? 341  GLN B CD  1 
ATOM   1844 O  OE1 . GLN B  1 92  ? 6.803   13.732  58.197  1.00 39.47  ? 341  GLN B OE1 1 
ATOM   1845 N  NE2 . GLN B  1 92  ? 6.062   15.788  58.791  1.00 37.00  ? 341  GLN B NE2 1 
ATOM   1846 N  N   . TYR B  1 93  ? 2.335   12.756  55.794  1.00 31.86  ? 342  TYR B N   1 
ATOM   1847 C  CA  . TYR B  1 93  ? 1.724   11.452  56.130  1.00 32.24  ? 342  TYR B CA  1 
ATOM   1848 C  C   . TYR B  1 93  ? 0.922   10.746  55.014  1.00 31.03  ? 342  TYR B C   1 
ATOM   1849 O  O   . TYR B  1 93  ? 0.697   9.532   55.094  1.00 34.05  ? 342  TYR B O   1 
ATOM   1850 C  CB  . TYR B  1 93  ? 0.889   11.538  57.415  1.00 30.80  ? 342  TYR B CB  1 
ATOM   1851 C  CG  . TYR B  1 93  ? 1.667   12.061  58.580  1.00 29.88  ? 342  TYR B CG  1 
ATOM   1852 C  CD1 . TYR B  1 93  ? 2.848   11.457  58.985  1.00 32.01  ? 342  TYR B CD1 1 
ATOM   1853 C  CD2 . TYR B  1 93  ? 1.258   13.207  59.232  1.00 28.90  ? 342  TYR B CD2 1 
ATOM   1854 C  CE1 . TYR B  1 93  ? 3.589   11.981  60.032  1.00 32.26  ? 342  TYR B CE1 1 
ATOM   1855 C  CE2 . TYR B  1 93  ? 1.961   13.727  60.260  1.00 30.46  ? 342  TYR B CE2 1 
ATOM   1856 C  CZ  . TYR B  1 93  ? 3.135   13.122  60.676  1.00 32.40  ? 342  TYR B CZ  1 
ATOM   1857 O  OH  . TYR B  1 93  ? 3.791   13.669  61.769  1.00 29.92  ? 342  TYR B OH  1 
ATOM   1858 N  N   . TRP B  1 94  ? 0.495   11.464  53.993  1.00 27.71  ? 343  TRP B N   1 
ATOM   1859 C  CA  . TRP B  1 94  ? -0.093  10.823  52.839  1.00 30.01  ? 343  TRP B CA  1 
ATOM   1860 C  C   . TRP B  1 94  ? 0.864   9.776   52.305  1.00 29.72  ? 343  TRP B C   1 
ATOM   1861 O  O   . TRP B  1 94  ? 2.039   10.072  52.187  1.00 29.13  ? 343  TRP B O   1 
ATOM   1862 C  CB  . TRP B  1 94  ? -0.348  11.824  51.709  1.00 29.01  ? 343  TRP B CB  1 
ATOM   1863 C  CG  . TRP B  1 94  ? -1.460  12.803  51.971  1.00 29.61  ? 343  TRP B CG  1 
ATOM   1864 C  CD1 . TRP B  1 94  ? -1.349  14.161  52.094  1.00 28.78  ? 343  TRP B CD1 1 
ATOM   1865 C  CD2 . TRP B  1 94  ? -2.846  12.502  52.095  1.00 26.44  ? 343  TRP B CD2 1 
ATOM   1866 N  NE1 . TRP B  1 94  ? -2.583  14.713  52.304  1.00 27.33  ? 343  TRP B NE1 1 
ATOM   1867 C  CE2 . TRP B  1 94  ? -3.515  13.712  52.306  1.00 26.10  ? 343  TRP B CE2 1 
ATOM   1868 C  CE3 . TRP B  1 94  ? -3.588  11.308  52.066  1.00 27.33  ? 343  TRP B CE3 1 
ATOM   1869 C  CZ2 . TRP B  1 94  ? -4.893  13.784  52.471  1.00 26.54  ? 343  TRP B CZ2 1 
ATOM   1870 C  CZ3 . TRP B  1 94  ? -4.949  11.381  52.246  1.00 26.36  ? 343  TRP B CZ3 1 
ATOM   1871 C  CH2 . TRP B  1 94  ? -5.586  12.620  52.438  1.00 28.30  ? 343  TRP B CH2 1 
ATOM   1872 N  N   . ASN B  1 95  ? 0.372   8.571   52.008  1.00 27.28  ? 344  ASN B N   1 
ATOM   1873 C  CA  . ASN B  1 95  ? 1.172   7.586   51.297  1.00 30.60  ? 344  ASN B CA  1 
ATOM   1874 C  C   . ASN B  1 95  ? 1.626   8.198   49.952  1.00 32.24  ? 344  ASN B C   1 
ATOM   1875 O  O   . ASN B  1 95  ? 1.026   9.169   49.432  1.00 31.87  ? 344  ASN B O   1 
ATOM   1876 C  CB  . ASN B  1 95  ? 0.440   6.245   51.027  1.00 30.10  ? 344  ASN B CB  1 
ATOM   1877 C  CG  . ASN B  1 95  ? 0.039   5.508   52.290  1.00 29.93  ? 344  ASN B CG  1 
ATOM   1878 O  OD1 . ASN B  1 95  ? 0.748   5.544   53.305  1.00 31.39  ? 344  ASN B OD1 1 
ATOM   1879 N  ND2 . ASN B  1 95  ? -1.083  4.797   52.224  1.00 25.03  ? 344  ASN B ND2 1 
ATOM   1880 N  N   . ARG B  1 96  ? 2.698   7.630   49.421  1.00 33.51  ? 345  ARG B N   1 
ATOM   1881 C  CA  . ARG B  1 96  ? 3.258   8.068   48.149  1.00 37.97  ? 345  ARG B CA  1 
ATOM   1882 C  C   . ARG B  1 96  ? 2.185   7.997   47.057  1.00 33.77  ? 345  ARG B C   1 
ATOM   1883 O  O   . ARG B  1 96  ? 1.489   6.989   46.889  1.00 34.63  ? 345  ARG B O   1 
ATOM   1884 C  CB  . ARG B  1 96  ? 4.511   7.241   47.789  1.00 46.02  ? 345  ARG B CB  1 
ATOM   1885 C  CG  . ARG B  1 96  ? 5.016   7.423   46.347  1.00 56.96  ? 345  ARG B CG  1 
ATOM   1886 C  CD  . ARG B  1 96  ? 6.066   6.397   45.901  1.00 62.98  ? 345  ARG B CD  1 
ATOM   1887 N  NE  . ARG B  1 96  ? 7.425   6.889   46.157  1.00 73.94  ? 345  ARG B NE  1 
ATOM   1888 C  CZ  . ARG B  1 96  ? 8.056   6.841   47.335  1.00 77.58  ? 345  ARG B CZ  1 
ATOM   1889 N  NH1 . ARG B  1 96  ? 7.476   6.306   48.413  1.00 80.99  ? 345  ARG B NH1 1 
ATOM   1890 N  NH2 . ARG B  1 96  ? 9.293   7.325   47.440  1.00 76.48  ? 345  ARG B NH2 1 
ATOM   1891 N  N   . GLY B  1 97  ? 2.052   9.101   46.335  1.00 30.07  ? 346  GLY B N   1 
ATOM   1892 C  CA  . GLY B  1 97  ? 1.076   9.253   45.275  1.00 29.53  ? 346  GLY B CA  1 
ATOM   1893 C  C   . GLY B  1 97  ? -0.292  9.706   45.765  1.00 30.25  ? 346  GLY B C   1 
ATOM   1894 O  O   . GLY B  1 97  ? -1.204  9.849   44.960  1.00 35.58  ? 346  GLY B O   1 
ATOM   1895 N  N   . GLU B  1 98  ? -0.460  9.933   47.067  1.00 28.34  ? 347  GLU B N   1 
ATOM   1896 C  CA  . GLU B  1 98  ? -1.771  10.324  47.573  1.00 27.71  ? 347  GLU B CA  1 
ATOM   1897 C  C   . GLU B  1 98  ? -1.751  11.783  47.966  1.00 27.68  ? 347  GLU B C   1 
ATOM   1898 O  O   . GLU B  1 98  ? -0.683  12.345  48.145  1.00 28.34  ? 347  GLU B O   1 
ATOM   1899 C  CB  . GLU B  1 98  ? -2.174  9.431   48.747  1.00 25.42  ? 347  GLU B CB  1 
ATOM   1900 C  CG  . GLU B  1 98  ? -2.144  7.933   48.368  1.00 25.73  ? 347  GLU B CG  1 
ATOM   1901 C  CD  . GLU B  1 98  ? -3.145  7.497   47.271  1.00 26.30  ? 347  GLU B CD  1 
ATOM   1902 O  OE1 . GLU B  1 98  ? -4.041  8.272   46.878  1.00 26.24  ? 347  GLU B OE1 1 
ATOM   1903 O  OE2 . GLU B  1 98  ? -3.072  6.318   46.810  1.00 24.30  ? 347  GLU B OE2 1 
ATOM   1904 N  N   . PRO B  1 99  ? -2.896  12.444  48.081  1.00 28.01  ? 348  PRO B N   1 
ATOM   1905 C  CA  . PRO B  1 99  ? -4.219  11.979  47.650  1.00 27.06  ? 348  PRO B CA  1 
ATOM   1906 C  C   . PRO B  1 99  ? -4.347  12.090  46.142  1.00 29.33  ? 348  PRO B C   1 
ATOM   1907 O  O   . PRO B  1 99  ? -3.897  13.052  45.589  1.00 31.53  ? 348  PRO B O   1 
ATOM   1908 C  CB  . PRO B  1 99  ? -5.162  12.973  48.340  1.00 27.70  ? 348  PRO B CB  1 
ATOM   1909 C  CG  . PRO B  1 99  ? -4.354  14.211  48.596  1.00 27.85  ? 348  PRO B CG  1 
ATOM   1910 C  CD  . PRO B  1 99  ? -2.892  13.831  48.586  1.00 26.69  ? 348  PRO B CD  1 
ATOM   1911 N  N   . ASN B  1 100 ? -4.942  11.106  45.490  1.00 27.71  ? 349  ASN B N   1 
ATOM   1912 C  CA  . ASN B  1 100 ? -5.015  11.085  44.043  1.00 26.25  ? 349  ASN B CA  1 
ATOM   1913 C  C   . ASN B  1 100 ? -6.463  11.288  43.550  1.00 26.54  ? 349  ASN B C   1 
ATOM   1914 O  O   . ASN B  1 100 ? -6.676  11.470  42.393  1.00 22.31  ? 349  ASN B O   1 
ATOM   1915 C  CB  . ASN B  1 100 ? -4.378  9.820   43.469  1.00 25.25  ? 349  ASN B CB  1 
ATOM   1916 C  CG  . ASN B  1 100 ? -4.997  8.545   44.016  1.00 26.92  ? 349  ASN B CG  1 
ATOM   1917 O  OD1 . ASN B  1 100 ? -5.884  8.577   44.870  1.00 22.47  ? 349  ASN B OD1 1 
ATOM   1918 N  ND2 . ASN B  1 100 ? -4.509  7.405   43.537  1.00 25.90  ? 349  ASN B ND2 1 
ATOM   1919 N  N   . ASN B  1 101 ? -7.458  11.280  44.432  1.00 25.19  ? 350  ASN B N   1 
ATOM   1920 C  CA  . ASN B  1 101 ? -8.849  11.466  43.988  1.00 25.12  ? 350  ASN B CA  1 
ATOM   1921 C  C   . ASN B  1 101 ? -9.314  10.465  42.926  1.00 25.59  ? 350  ASN B C   1 
ATOM   1922 O  O   . ASN B  1 101 ? -10.309 10.667  42.238  1.00 29.22  ? 350  ASN B O   1 
ATOM   1923 C  CB  . ASN B  1 101 ? -9.066  12.899  43.472  1.00 25.55  ? 350  ASN B CB  1 
ATOM   1924 C  CG  . ASN B  1 101 ? -10.531 13.303  43.534  1.00 26.89  ? 350  ASN B CG  1 
ATOM   1925 O  OD1 . ASN B  1 101 ? -11.219 12.998  44.514  1.00 28.45  ? 350  ASN B OD1 1 
ATOM   1926 N  ND2 . ASN B  1 101 ? -11.016 13.964  42.504  1.00 23.12  ? 350  ASN B ND2 1 
ATOM   1927 N  N   . VAL B  1 102 ? -8.641  9.333   42.830  1.00 26.99  ? 351  VAL B N   1 
ATOM   1928 C  CA  . VAL B  1 102 ? -8.948  8.411   41.772  1.00 25.29  ? 351  VAL B CA  1 
ATOM   1929 C  C   . VAL B  1 102 ? -10.391 7.865   41.839  1.00 26.85  ? 351  VAL B C   1 
ATOM   1930 O  O   . VAL B  1 102 ? -10.765 7.190   42.757  1.00 26.38  ? 351  VAL B O   1 
ATOM   1931 C  CB  . VAL B  1 102 ? -7.876  7.322   41.667  1.00 25.53  ? 351  VAL B CB  1 
ATOM   1932 C  CG1 . VAL B  1 102 ? -7.834  6.440   42.922  1.00 25.57  ? 351  VAL B CG1 1 
ATOM   1933 C  CG2 . VAL B  1 102 ? -8.102  6.554   40.369  1.00 28.70  ? 351  VAL B CG2 1 
ATOM   1934 N  N   . GLY B  1 103 ? -11.193 8.185   40.834  1.00 28.47  ? 352  GLY B N   1 
ATOM   1935 C  CA  . GLY B  1 103 ? -12.598 7.821   40.825  1.00 30.13  ? 352  GLY B CA  1 
ATOM   1936 C  C   . GLY B  1 103 ? -13.450 8.647   41.805  1.00 33.03  ? 352  GLY B C   1 
ATOM   1937 O  O   . GLY B  1 103 ? -14.585 8.255   42.126  1.00 30.13  ? 352  GLY B O   1 
ATOM   1938 N  N   . GLU B  1 104 ? -12.898 9.777   42.274  1.00 30.46  ? 353  GLU B N   1 
ATOM   1939 C  CA  . GLU B  1 104 ? -13.540 10.604  43.328  1.00 33.41  ? 353  GLU B CA  1 
ATOM   1940 C  C   . GLU B  1 104 ? -13.376 9.966   44.697  1.00 27.97  ? 353  GLU B C   1 
ATOM   1941 O  O   . GLU B  1 104 ? -14.080 9.064   45.061  1.00 32.28  ? 353  GLU B O   1 
ATOM   1942 C  CB  . GLU B  1 104 ? -15.022 10.976  43.019  1.00 31.38  ? 353  GLU B CB  1 
ATOM   1943 C  CG  . GLU B  1 104 ? -15.112 12.106  42.009  1.00 36.41  ? 353  GLU B CG  1 
ATOM   1944 C  CD  . GLU B  1 104 ? -16.536 12.620  41.742  1.00 39.17  ? 353  GLU B CD  1 
ATOM   1945 O  OE1 . GLU B  1 104 ? -16.739 13.164  40.647  1.00 45.25  ? 353  GLU B OE1 1 
ATOM   1946 O  OE2 . GLU B  1 104 ? -17.442 12.502  42.605  1.00 39.59  ? 353  GLU B OE2 1 
ATOM   1947 N  N   . GLU B  1 105 ? -12.382 10.434  45.440  1.00 28.87  ? 354  GLU B N   1 
ATOM   1948 C  CA  . GLU B  1 105 ? -12.113 9.910   46.773  1.00 25.18  ? 354  GLU B CA  1 
ATOM   1949 C  C   . GLU B  1 105 ? -12.072 11.101  47.628  1.00 27.07  ? 354  GLU B C   1 
ATOM   1950 O  O   . GLU B  1 105 ? -11.196 11.960  47.449  1.00 26.89  ? 354  GLU B O   1 
ATOM   1951 C  CB  . GLU B  1 105 ? -10.786 9.140   46.842  1.00 24.55  ? 354  GLU B CB  1 
ATOM   1952 C  CG  . GLU B  1 105 ? -10.749 7.939   45.871  1.00 24.60  ? 354  GLU B CG  1 
ATOM   1953 C  CD  . GLU B  1 105 ? -9.484  7.102   45.939  1.00 23.81  ? 354  GLU B CD  1 
ATOM   1954 O  OE1 . GLU B  1 105 ? -8.361  7.696   45.899  1.00 18.90  ? 354  GLU B OE1 1 
ATOM   1955 O  OE2 . GLU B  1 105 ? -9.621  5.836   46.040  1.00 23.34  ? 354  GLU B OE2 1 
ATOM   1956 N  N   . ASP B  1 106 ? -12.990 11.180  48.590  1.00 27.56  ? 355  ASP B N   1 
ATOM   1957 C  CA  . ASP B  1 106 ? -13.058 12.417  49.416  1.00 28.40  ? 355  ASP B CA  1 
ATOM   1958 C  C   . ASP B  1 106 ? -12.908 12.227  50.949  1.00 28.90  ? 355  ASP B C   1 
ATOM   1959 O  O   . ASP B  1 106 ? -12.947 13.221  51.686  1.00 28.10  ? 355  ASP B O   1 
ATOM   1960 C  CB  . ASP B  1 106 ? -14.343 13.213  49.056  1.00 27.90  ? 355  ASP B CB  1 
ATOM   1961 C  CG  . ASP B  1 106 ? -14.378 13.696  47.603  1.00 28.71  ? 355  ASP B CG  1 
ATOM   1962 O  OD1 . ASP B  1 106 ? -13.328 13.774  46.894  1.00 28.71  ? 355  ASP B OD1 1 
ATOM   1963 O  OD2 . ASP B  1 106 ? -15.513 13.992  47.114  1.00 32.32  ? 355  ASP B OD2 1 
ATOM   1964 N  N   . CYS B  1 107 ? -12.720 10.978  51.436  1.00 24.58  ? 356  CYS B N   1 
ATOM   1965 C  CA  . CYS B  1 107 ? -12.499 10.745  52.860  1.00 25.02  ? 356  CYS B CA  1 
ATOM   1966 C  C   . CYS B  1 107 ? -11.160 10.086  53.143  1.00 23.12  ? 356  CYS B C   1 
ATOM   1967 O  O   . CYS B  1 107 ? -10.707 9.210   52.387  1.00 23.91  ? 356  CYS B O   1 
ATOM   1968 C  CB  . CYS B  1 107 ? -13.649 9.961   53.499  1.00 25.13  ? 356  CYS B CB  1 
ATOM   1969 S  SG  . CYS B  1 107 ? -15.224 10.807  53.302  1.00 27.75  ? 356  CYS B SG  1 
ATOM   1970 N  N   . ALA B  1 108 ? -10.500 10.536  54.205  1.00 20.26  ? 357  ALA B N   1 
ATOM   1971 C  CA  . ALA B  1 108 ? -9.142  10.023  54.537  1.00 21.13  ? 357  ALA B CA  1 
ATOM   1972 C  C   . ALA B  1 108 ? -9.128  8.792   55.441  1.00 21.40  ? 357  ALA B C   1 
ATOM   1973 O  O   . ALA B  1 108 ? -9.829  8.719   56.467  1.00 23.07  ? 357  ALA B O   1 
ATOM   1974 C  CB  . ALA B  1 108 ? -8.288  11.113  55.159  1.00 20.32  ? 357  ALA B CB  1 
ATOM   1975 N  N   . GLU B  1 109 ? -8.295  7.852   55.069  1.00 19.85  ? 358  GLU B N   1 
ATOM   1976 C  CA  . GLU B  1 109 ? -8.079  6.591   55.852  1.00 22.47  ? 358  GLU B CA  1 
ATOM   1977 C  C   . GLU B  1 109 ? -6.596  6.392   56.259  1.00 22.31  ? 358  GLU B C   1 
ATOM   1978 O  O   . GLU B  1 109 ? -5.699  6.852   55.557  1.00 21.76  ? 358  GLU B O   1 
ATOM   1979 C  CB  . GLU B  1 109 ? -8.514  5.376   55.037  1.00 23.86  ? 358  GLU B CB  1 
ATOM   1980 C  CG  . GLU B  1 109 ? -7.709  5.158   53.768  1.00 26.11  ? 358  GLU B CG  1 
ATOM   1981 C  CD  . GLU B  1 109 ? -7.922  3.793   53.147  1.00 27.52  ? 358  GLU B CD  1 
ATOM   1982 O  OE1 . GLU B  1 109 ? -7.566  3.635   51.955  1.00 29.38  ? 358  GLU B OE1 1 
ATOM   1983 O  OE2 . GLU B  1 109 ? -8.469  2.891   53.818  1.00 23.85  ? 358  GLU B OE2 1 
ATOM   1984 N  N   . PHE B  1 110 ? -6.364  5.748   57.397  1.00 24.37  ? 359  PHE B N   1 
ATOM   1985 C  CA  . PHE B  1 110 ? -5.065  5.099   57.731  1.00 24.61  ? 359  PHE B CA  1 
ATOM   1986 C  C   . PHE B  1 110 ? -4.977  3.846   56.895  1.00 25.17  ? 359  PHE B C   1 
ATOM   1987 O  O   . PHE B  1 110 ? -5.868  3.020   56.966  1.00 23.53  ? 359  PHE B O   1 
ATOM   1988 C  CB  . PHE B  1 110 ? -4.971  4.688   59.193  1.00 25.77  ? 359  PHE B CB  1 
ATOM   1989 C  CG  . PHE B  1 110 ? -5.151  5.819   60.140  1.00 25.94  ? 359  PHE B CG  1 
ATOM   1990 C  CD1 . PHE B  1 110 ? -4.111  6.722   60.355  1.00 25.84  ? 359  PHE B CD1 1 
ATOM   1991 C  CD2 . PHE B  1 110 ? -6.351  6.000   60.801  1.00 25.71  ? 359  PHE B CD2 1 
ATOM   1992 C  CE1 . PHE B  1 110 ? -4.268  7.791   61.215  1.00 28.55  ? 359  PHE B CE1 1 
ATOM   1993 C  CE2 . PHE B  1 110 ? -6.522  7.071   61.665  1.00 29.73  ? 359  PHE B CE2 1 
ATOM   1994 C  CZ  . PHE B  1 110 ? -5.469  7.965   61.894  1.00 28.94  ? 359  PHE B CZ  1 
ATOM   1995 N  N   . SER B  1 111 ? -3.936  3.739   56.077  1.00 24.83  ? 360  SER B N   1 
ATOM   1996 C  CA  . SER B  1 111 ? -3.738  2.613   55.190  1.00 28.51  ? 360  SER B CA  1 
ATOM   1997 C  C   . SER B  1 111 ? -2.247  2.261   55.097  1.00 28.84  ? 360  SER B C   1 
ATOM   1998 O  O   . SER B  1 111 ? -1.488  2.969   54.477  1.00 31.95  ? 360  SER B O   1 
ATOM   1999 C  CB  . SER B  1 111 ? -4.267  2.944   53.827  1.00 30.31  ? 360  SER B CB  1 
ATOM   2000 O  OG  . SER B  1 111 ? -4.087  1.855   52.959  1.00 36.19  ? 360  SER B OG  1 
ATOM   2001 N  N   . GLY B  1 112 ? -1.844  1.156   55.702  1.00 30.55  ? 361  GLY B N   1 
ATOM   2002 C  CA  . GLY B  1 112 ? -0.423  0.797   55.778  1.00 30.93  ? 361  GLY B CA  1 
ATOM   2003 C  C   . GLY B  1 112 ? 0.324   1.729   56.699  1.00 30.62  ? 361  GLY B C   1 
ATOM   2004 O  O   . GLY B  1 112 ? -0.038  1.913   57.882  1.00 28.13  ? 361  GLY B O   1 
ATOM   2005 N  N   . ASN B  1 113 ? 1.329   2.393   56.159  1.00 31.44  ? 362  ASN B N   1 
ATOM   2006 C  CA  . ASN B  1 113 ? 2.170   3.252   56.993  1.00 33.10  ? 362  ASN B CA  1 
ATOM   2007 C  C   . ASN B  1 113 ? 1.776   4.712   57.030  1.00 33.32  ? 362  ASN B C   1 
ATOM   2008 O  O   . ASN B  1 113 ? 2.316   5.460   57.820  1.00 33.54  ? 362  ASN B O   1 
ATOM   2009 C  CB  . ASN B  1 113 ? 3.620   3.068   56.558  1.00 36.83  ? 362  ASN B CB  1 
ATOM   2010 C  CG  . ASN B  1 113 ? 4.066   1.629   56.756  1.00 40.39  ? 362  ASN B CG  1 
ATOM   2011 O  OD1 . ASN B  1 113 ? 4.591   1.005   55.852  1.00 43.01  ? 362  ASN B OD1 1 
ATOM   2012 N  ND2 . ASN B  1 113 ? 3.743   1.064   57.924  1.00 41.29  ? 362  ASN B ND2 1 
ATOM   2013 N  N   . GLY B  1 114 ? 0.815   5.095   56.193  1.00 32.09  ? 363  GLY B N   1 
ATOM   2014 C  CA  . GLY B  1 114 ? 0.347   6.462   56.088  1.00 30.58  ? 363  GLY B CA  1 
ATOM   2015 C  C   . GLY B  1 114 ? -1.127  6.538   55.687  1.00 27.29  ? 363  GLY B C   1 
ATOM   2016 O  O   . GLY B  1 114 ? -1.907  5.609   55.877  1.00 25.88  ? 363  GLY B O   1 
ATOM   2017 N  N   . TRP B  1 115 ? -1.483  7.670   55.123  1.00 28.79  ? 364  TRP B N   1 
ATOM   2018 C  CA  . TRP B  1 115 ? -2.867  7.994   54.775  1.00 26.68  ? 364  TRP B CA  1 
ATOM   2019 C  C   . TRP B  1 115 ? -3.207  7.783   53.329  1.00 25.02  ? 364  TRP B C   1 
ATOM   2020 O  O   . TRP B  1 115 ? -2.374  7.979   52.454  1.00 23.95  ? 364  TRP B O   1 
ATOM   2021 C  CB  . TRP B  1 115 ? -3.093  9.449   55.026  1.00 28.99  ? 364  TRP B CB  1 
ATOM   2022 C  CG  . TRP B  1 115 ? -2.811  9.923   56.372  1.00 30.19  ? 364  TRP B CG  1 
ATOM   2023 C  CD1 . TRP B  1 115 ? -2.473  9.195   57.460  1.00 29.17  ? 364  TRP B CD1 1 
ATOM   2024 C  CD2 . TRP B  1 115 ? -2.950  11.271  56.804  1.00 31.19  ? 364  TRP B CD2 1 
ATOM   2025 N  NE1 . TRP B  1 115 ? -2.371  10.012  58.545  1.00 31.12  ? 364  TRP B NE1 1 
ATOM   2026 C  CE2 . TRP B  1 115 ? -2.654  11.296  58.169  1.00 30.46  ? 364  TRP B CE2 1 
ATOM   2027 C  CE3 . TRP B  1 115 ? -3.282  12.466  56.154  1.00 32.65  ? 364  TRP B CE3 1 
ATOM   2028 C  CZ2 . TRP B  1 115 ? -2.639  12.471  58.906  1.00 32.19  ? 364  TRP B CZ2 1 
ATOM   2029 C  CZ3 . TRP B  1 115 ? -3.297  13.638  56.893  1.00 34.23  ? 364  TRP B CZ3 1 
ATOM   2030 C  CH2 . TRP B  1 115 ? -2.965  13.630  58.258  1.00 31.97  ? 364  TRP B CH2 1 
ATOM   2031 N  N   . ASN B  1 116 ? -4.472  7.479   53.063  1.00 24.53  ? 365  ASN B N   1 
ATOM   2032 C  CA  . ASN B  1 116 ? -4.960  7.474   51.686  1.00 25.34  ? 365  ASN B CA  1 
ATOM   2033 C  C   . ASN B  1 116 ? -6.277  8.167   51.616  1.00 22.88  ? 365  ASN B C   1 
ATOM   2034 O  O   . ASN B  1 116 ? -7.071  8.092   52.553  1.00 20.42  ? 365  ASN B O   1 
ATOM   2035 C  CB  . ASN B  1 116 ? -5.166  5.998   51.280  1.00 26.71  ? 365  ASN B CB  1 
ATOM   2036 C  CG  . ASN B  1 116 ? -5.673  5.813   49.877  1.00 26.66  ? 365  ASN B CG  1 
ATOM   2037 O  OD1 . ASN B  1 116 ? -5.257  6.512   48.937  1.00 27.39  ? 365  ASN B OD1 1 
ATOM   2038 N  ND2 . ASN B  1 116 ? -6.585  4.845   49.712  1.00 25.75  ? 365  ASN B ND2 1 
ATOM   2039 N  N   . ASP B  1 117 ? -6.587  8.736   50.462  1.00 20.95  ? 366  ASP B N   1 
ATOM   2040 C  CA  . ASP B  1 117 ? -7.973  9.160   50.231  1.00 20.45  ? 366  ASP B CA  1 
ATOM   2041 C  C   . ASP B  1 117 ? -8.693  7.986   49.593  1.00 21.99  ? 366  ASP B C   1 
ATOM   2042 O  O   . ASP B  1 117 ? -8.123  7.350   48.728  1.00 16.92  ? 366  ASP B O   1 
ATOM   2043 C  CB  . ASP B  1 117 ? -8.051  10.427  49.407  1.00 19.77  ? 366  ASP B CB  1 
ATOM   2044 C  CG  . ASP B  1 117 ? -7.324  10.326  48.006  1.00 21.82  ? 366  ASP B CG  1 
ATOM   2045 O  OD1 . ASP B  1 117 ? -6.389  9.527   47.785  1.00 20.58  ? 366  ASP B OD1 1 
ATOM   2046 O  OD2 . ASP B  1 117 ? -7.744  11.085  47.130  1.00 23.37  ? 366  ASP B OD2 1 
ATOM   2047 N  N   . ASP B  1 118 ? -9.905  7.668   50.075  1.00 21.04  ? 367  ASP B N   1 
ATOM   2048 C  CA  . ASP B  1 118 ? -10.677 6.581   49.527  1.00 22.94  ? 367  ASP B CA  1 
ATOM   2049 C  C   . ASP B  1 118 ? -12.131 7.020   49.404  1.00 23.14  ? 367  ASP B C   1 
ATOM   2050 O  O   . ASP B  1 118 ? -12.485 8.120   49.835  1.00 17.60  ? 367  ASP B O   1 
ATOM   2051 C  CB  . ASP B  1 118 ? -10.537 5.313   50.383  1.00 25.34  ? 367  ASP B CB  1 
ATOM   2052 C  CG  . ASP B  1 118 ? -10.850 4.019   49.586  1.00 27.21  ? 367  ASP B CG  1 
ATOM   2053 O  OD1 . ASP B  1 118 ? -11.297 4.125   48.429  1.00 26.44  ? 367  ASP B OD1 1 
ATOM   2054 O  OD2 . ASP B  1 118 ? -10.656 2.907   50.131  1.00 28.09  ? 367  ASP B OD2 1 
ATOM   2055 N  N   . LYS B  1 119 ? -12.965 6.158   48.823  1.00 22.09  ? 368  LYS B N   1 
ATOM   2056 C  CA  . LYS B  1 119 ? -14.387 6.486   48.634  1.00 24.24  ? 368  LYS B CA  1 
ATOM   2057 C  C   . LYS B  1 119 ? -15.149 6.494   49.958  1.00 23.42  ? 368  LYS B C   1 
ATOM   2058 O  O   . LYS B  1 119 ? -15.190 5.500   50.675  1.00 20.85  ? 368  LYS B O   1 
ATOM   2059 C  CB  . LYS B  1 119 ? -15.084 5.560   47.639  1.00 25.90  ? 368  LYS B CB  1 
ATOM   2060 C  CG  . LYS B  1 119 ? -14.431 5.436   46.236  1.00 30.79  ? 368  LYS B CG  1 
ATOM   2061 C  CD  . LYS B  1 119 ? -15.074 4.208   45.633  1.00 38.91  ? 368  LYS B CD  1 
ATOM   2062 C  CE  . LYS B  1 119 ? -14.782 3.955   44.174  1.00 47.06  ? 368  LYS B CE  1 
ATOM   2063 N  NZ  . LYS B  1 119 ? -13.370 3.525   44.029  1.00 50.74  ? 368  LYS B NZ  1 
ATOM   2064 N  N   . CYS B  1 120 ? -15.790 7.632   50.227  1.00 24.43  ? 369  CYS B N   1 
ATOM   2065 C  CA  . CYS B  1 120 ? -16.533 7.869   51.462  1.00 22.21  ? 369  CYS B CA  1 
ATOM   2066 C  C   . CYS B  1 120 ? -17.611 6.807   51.788  1.00 22.75  ? 369  CYS B C   1 
ATOM   2067 O  O   . CYS B  1 120 ? -17.945 6.575   52.934  1.00 21.30  ? 369  CYS B O   1 
ATOM   2068 C  CB  . CYS B  1 120 ? -17.120 9.267   51.390  1.00 25.54  ? 369  CYS B CB  1 
ATOM   2069 S  SG  . CYS B  1 120 ? -15.841 10.590  51.357  1.00 28.56  ? 369  CYS B SG  1 
ATOM   2070 N  N   . ASN B  1 121 ? -18.129 6.135   50.779  1.00 21.23  ? 370  ASN B N   1 
ATOM   2071 C  CA  . ASN B  1 121 ? -19.243 5.253   50.949  1.00 24.52  ? 370  ASN B CA  1 
ATOM   2072 C  C   . ASN B  1 121 ? -18.784 3.811   51.247  1.00 23.43  ? 370  ASN B C   1 
ATOM   2073 O  O   . ASN B  1 121 ? -19.591 2.954   51.487  1.00 24.84  ? 370  ASN B O   1 
ATOM   2074 C  CB  . ASN B  1 121 ? -20.175 5.347   49.729  1.00 27.62  ? 370  ASN B CB  1 
ATOM   2075 C  CG  . ASN B  1 121 ? -19.409 5.199   48.409  1.00 33.88  ? 370  ASN B CG  1 
ATOM   2076 O  OD1 . ASN B  1 121 ? -18.750 6.144   47.927  1.00 46.73  ? 370  ASN B OD1 1 
ATOM   2077 N  ND2 . ASN B  1 121 ? -19.408 4.016   47.887  1.00 34.05  ? 370  ASN B ND2 1 
ATOM   2078 N  N   . LEU B  1 122 ? -17.480 3.564   51.280  1.00 24.67  ? 371  LEU B N   1 
ATOM   2079 C  CA  . LEU B  1 122 ? -16.960 2.261   51.713  1.00 25.40  ? 371  LEU B CA  1 
ATOM   2080 C  C   . LEU B  1 122 ? -16.979 2.089   53.228  1.00 21.58  ? 371  LEU B C   1 
ATOM   2081 O  O   . LEU B  1 122 ? -16.983 3.045   54.010  1.00 21.68  ? 371  LEU B O   1 
ATOM   2082 C  CB  . LEU B  1 122 ? -15.560 1.968   51.102  1.00 26.64  ? 371  LEU B CB  1 
ATOM   2083 C  CG  . LEU B  1 122 ? -15.533 1.980   49.555  1.00 27.15  ? 371  LEU B CG  1 
ATOM   2084 C  CD1 . LEU B  1 122 ? -14.104 1.805   49.039  1.00 27.97  ? 371  LEU B CD1 1 
ATOM   2085 C  CD2 . LEU B  1 122 ? -16.476 0.958   48.871  1.00 29.94  ? 371  LEU B CD2 1 
ATOM   2086 N  N   . ALA B  1 123 ? -17.053 0.846   53.633  1.00 22.34  ? 372  ALA B N   1 
ATOM   2087 C  CA  . ALA B  1 123 ? -17.048 0.481   55.040  1.00 24.74  ? 372  ALA B CA  1 
ATOM   2088 C  C   . ALA B  1 123 ? -15.590 0.258   55.525  1.00 22.99  ? 372  ALA B C   1 
ATOM   2089 O  O   . ALA B  1 123 ? -14.804 -0.417  54.875  1.00 24.81  ? 372  ALA B O   1 
ATOM   2090 C  CB  . ALA B  1 123 ? -17.882 -0.778  55.229  1.00 26.76  ? 372  ALA B CB  1 
ATOM   2091 N  N   . LYS B  1 124 ? -15.229 0.912   56.623  1.00 23.86  ? 373  LYS B N   1 
ATOM   2092 C  CA  . LYS B  1 124 ? -13.921 0.769   57.215  1.00 22.59  ? 373  LYS B CA  1 
ATOM   2093 C  C   . LYS B  1 124 ? -14.096 0.813   58.705  1.00 23.18  ? 373  LYS B C   1 
ATOM   2094 O  O   . LYS B  1 124 ? -15.118 1.229   59.190  1.00 24.81  ? 373  LYS B O   1 
ATOM   2095 C  CB  . LYS B  1 124 ? -13.043 1.917   56.773  1.00 24.01  ? 373  LYS B CB  1 
ATOM   2096 C  CG  . LYS B  1 124 ? -12.689 1.890   55.309  1.00 23.51  ? 373  LYS B CG  1 
ATOM   2097 C  CD  . LYS B  1 124 ? -11.848 3.049   54.880  1.00 24.20  ? 373  LYS B CD  1 
ATOM   2098 C  CE  . LYS B  1 124 ? -11.794 3.159   53.347  1.00 24.82  ? 373  LYS B CE  1 
ATOM   2099 N  NZ  . LYS B  1 124 ? -10.880 2.122   52.859  1.00 25.22  ? 373  LYS B NZ  1 
ATOM   2100 N  N   . PHE B  1 125 ? -13.051 0.458   59.432  1.00 24.59  ? 374  PHE B N   1 
ATOM   2101 C  CA  . PHE B  1 125 ? -12.995 0.635   60.875  1.00 23.56  ? 374  PHE B CA  1 
ATOM   2102 C  C   . PHE B  1 125 ? -12.918 2.119   61.134  1.00 21.88  ? 374  PHE B C   1 
ATOM   2103 O  O   . PHE B  1 125 ? -12.583 2.866   60.264  1.00 20.44  ? 374  PHE B O   1 
ATOM   2104 C  CB  . PHE B  1 125 ? -11.790 -0.112  61.451  1.00 23.80  ? 374  PHE B CB  1 
ATOM   2105 C  CG  . PHE B  1 125 ? -11.947 -1.591  61.360  1.00 23.70  ? 374  PHE B CG  1 
ATOM   2106 C  CD1 . PHE B  1 125 ? -11.552 -2.251  60.227  1.00 25.94  ? 374  PHE B CD1 1 
ATOM   2107 C  CD2 . PHE B  1 125 ? -12.606 -2.265  62.334  1.00 22.47  ? 374  PHE B CD2 1 
ATOM   2108 C  CE1 . PHE B  1 125 ? -11.757 -3.608  60.083  1.00 27.68  ? 374  PHE B CE1 1 
ATOM   2109 C  CE2 . PHE B  1 125 ? -12.831 -3.599  62.225  1.00 25.12  ? 374  PHE B CE2 1 
ATOM   2110 C  CZ  . PHE B  1 125 ? -12.416 -4.279  61.087  1.00 26.11  ? 374  PHE B CZ  1 
ATOM   2111 N  N   . TRP B  1 126 ? -13.285 2.553   62.321  1.00 21.11  ? 375  TRP B N   1 
ATOM   2112 C  CA  . TRP B  1 126 ? -13.155 3.964   62.605  1.00 23.72  ? 375  TRP B CA  1 
ATOM   2113 C  C   . TRP B  1 126 ? -12.539 4.146   64.000  1.00 23.14  ? 375  TRP B C   1 
ATOM   2114 O  O   . TRP B  1 126 ? -12.546 3.213   64.839  1.00 20.32  ? 375  TRP B O   1 
ATOM   2115 C  CB  . TRP B  1 126 ? -14.511 4.686   62.453  1.00 22.15  ? 375  TRP B CB  1 
ATOM   2116 C  CG  . TRP B  1 126 ? -15.525 4.328   63.524  1.00 22.23  ? 375  TRP B CG  1 
ATOM   2117 C  CD1 . TRP B  1 126 ? -15.731 4.975   64.708  1.00 24.33  ? 375  TRP B CD1 1 
ATOM   2118 C  CD2 . TRP B  1 126 ? -16.438 3.236   63.509  1.00 22.68  ? 375  TRP B CD2 1 
ATOM   2119 N  NE1 . TRP B  1 126 ? -16.720 4.335   65.458  1.00 23.71  ? 375  TRP B NE1 1 
ATOM   2120 C  CE2 . TRP B  1 126 ? -17.171 3.269   64.733  1.00 24.02  ? 375  TRP B CE2 1 
ATOM   2121 C  CE3 . TRP B  1 126 ? -16.702 2.232   62.603  1.00 22.69  ? 375  TRP B CE3 1 
ATOM   2122 C  CZ2 . TRP B  1 126 ? -18.144 2.339   65.049  1.00 23.36  ? 375  TRP B CZ2 1 
ATOM   2123 C  CZ3 . TRP B  1 126 ? -17.690 1.313   62.906  1.00 25.64  ? 375  TRP B CZ3 1 
ATOM   2124 C  CH2 . TRP B  1 126 ? -18.386 1.358   64.132  1.00 25.35  ? 375  TRP B CH2 1 
ATOM   2125 N  N   . ILE B  1 127 ? -12.025 5.348   64.236  1.00 23.54  ? 376  ILE B N   1 
ATOM   2126 C  CA  . ILE B  1 127 ? -11.605 5.750   65.589  1.00 23.84  ? 376  ILE B CA  1 
ATOM   2127 C  C   . ILE B  1 127 ? -12.230 7.030   66.056  1.00 22.98  ? 376  ILE B C   1 
ATOM   2128 O  O   . ILE B  1 127 ? -12.134 8.031   65.363  1.00 22.87  ? 376  ILE B O   1 
ATOM   2129 C  CB  . ILE B  1 127 ? -10.060 5.908   65.643  1.00 26.35  ? 376  ILE B CB  1 
ATOM   2130 C  CG1 . ILE B  1 127 ? -9.366  4.569   65.311  1.00 26.33  ? 376  ILE B CG1 1 
ATOM   2131 C  CG2 . ILE B  1 127 ? -9.595  6.370   67.024  1.00 28.08  ? 376  ILE B CG2 1 
ATOM   2132 C  CD1 . ILE B  1 127 ? -7.880  4.725   65.090  1.00 27.94  ? 376  ILE B CD1 1 
ATOM   2133 N  N   . CYS B  1 128 ? -12.776 7.019   67.274  1.00 24.65  ? 377  CYS B N   1 
ATOM   2134 C  CA  . CYS B  1 128 ? -13.362 8.193   67.920  1.00 25.50  ? 377  CYS B CA  1 
ATOM   2135 C  C   . CYS B  1 128 ? -12.399 8.754   69.002  1.00 27.78  ? 377  CYS B C   1 
ATOM   2136 O  O   . CYS B  1 128 ? -11.662 7.997   69.647  1.00 28.17  ? 377  CYS B O   1 
ATOM   2137 C  CB  . CYS B  1 128 ? -14.656 7.829   68.613  1.00 27.20  ? 377  CYS B CB  1 
ATOM   2138 S  SG  . CYS B  1 128 ? -15.946 7.034   67.659  1.00 30.65  ? 377  CYS B SG  1 
ATOM   2139 N  N   . LYS B  1 129 ? -12.437 10.071  69.184  1.00 26.18  ? 378  LYS B N   1 
ATOM   2140 C  CA  . LYS B  1 129 ? -11.613 10.776  70.154  1.00 27.80  ? 378  LYS B CA  1 
ATOM   2141 C  C   . LYS B  1 129 ? -12.464 11.711  70.978  1.00 26.30  ? 378  LYS B C   1 
ATOM   2142 O  O   . LYS B  1 129 ? -13.334 12.375  70.453  1.00 25.29  ? 378  LYS B O   1 
ATOM   2143 C  CB  . LYS B  1 129 ? -10.552 11.621  69.471  1.00 28.77  ? 378  LYS B CB  1 
ATOM   2144 C  CG  . LYS B  1 129 ? -9.683  12.474  70.375  1.00 30.04  ? 378  LYS B CG  1 
ATOM   2145 C  CD  . LYS B  1 129 ? -8.731  13.241  69.482  1.00 33.34  ? 378  LYS B CD  1 
ATOM   2146 C  CE  . LYS B  1 129 ? -7.841  14.194  70.246  1.00 30.72  ? 378  LYS B CE  1 
ATOM   2147 N  NZ  . LYS B  1 129 ? -6.806  14.754  69.341  1.00 31.82  ? 378  LYS B NZ  1 
ATOM   2148 N  N   . LYS B  1 130 ? -12.208 11.709  72.274  1.00 26.99  ? 379  LYS B N   1 
ATOM   2149 C  CA  . LYS B  1 130 ? -12.716 12.727  73.184  1.00 29.35  ? 379  LYS B CA  1 
ATOM   2150 C  C   . LYS B  1 130 ? -11.785 12.989  74.337  1.00 31.04  ? 379  LYS B C   1 
ATOM   2151 O  O   . LYS B  1 130 ? -10.858 12.214  74.594  1.00 29.58  ? 379  LYS B O   1 
ATOM   2152 C  CB  . LYS B  1 130 ? -14.086 12.348  73.705  1.00 28.82  ? 379  LYS B CB  1 
ATOM   2153 C  CG  . LYS B  1 130 ? -14.148 11.239  74.721  1.00 29.52  ? 379  LYS B CG  1 
ATOM   2154 C  CD  . LYS B  1 130 ? -15.615 10.999  74.960  1.00 32.34  ? 379  LYS B CD  1 
ATOM   2155 C  CE  . LYS B  1 130 ? -15.816 9.925   75.971  1.00 36.87  ? 379  LYS B CE  1 
ATOM   2156 N  NZ  . LYS B  1 130 ? -17.192 9.400   75.825  1.00 41.90  ? 379  LYS B NZ  1 
ATOM   2157 N  N   . SER B  1 131 ? -12.072 14.077  75.057  1.00 34.05  ? 380  SER B N   1 
ATOM   2158 C  CA  . SER B  1 131 ? -11.275 14.494  76.220  1.00 35.94  ? 380  SER B CA  1 
ATOM   2159 C  C   . SER B  1 131 ? -11.253 13.482  77.330  1.00 34.87  ? 380  SER B C   1 
ATOM   2160 O  O   . SER B  1 131 ? -12.263 12.845  77.613  1.00 32.56  ? 380  SER B O   1 
ATOM   2161 C  CB  . SER B  1 131 ? -11.799 15.812  76.799  1.00 38.11  ? 380  SER B CB  1 
ATOM   2162 O  OG  . SER B  1 131 ? -11.107 16.857  76.173  1.00 43.52  ? 380  SER B OG  1 
ATOM   2163 N  N   . ALA B  1 132 ? -10.083 13.334  77.951  1.00 35.91  ? 381  ALA B N   1 
ATOM   2164 C  CA  . ALA B  1 132 ? -9.972  12.563  79.197  1.00 40.06  ? 381  ALA B CA  1 
ATOM   2165 C  C   . ALA B  1 132 ? -10.526 13.388  80.331  1.00 39.06  ? 381  ALA B C   1 
ATOM   2166 O  O   . ALA B  1 132 ? -10.366 14.602  80.326  1.00 38.28  ? 381  ALA B O   1 
ATOM   2167 C  CB  . ALA B  1 132 ? -8.525  12.225  79.495  1.00 38.66  ? 381  ALA B CB  1 
ATOM   2168 N  N   . ALA B  1 133 ? -11.149 12.725  81.300  1.00 42.44  ? 382  ALA B N   1 
ATOM   2169 C  CA  . ALA B  1 133 ? -11.501 13.342  82.591  1.00 50.31  ? 382  ALA B CA  1 
ATOM   2170 C  C   . ALA B  1 133 ? -10.259 13.695  83.420  1.00 60.22  ? 382  ALA B C   1 
ATOM   2171 O  O   . ALA B  1 133 ? -9.204  13.025  83.317  1.00 61.38  ? 382  ALA B O   1 
ATOM   2172 C  CB  . ALA B  1 133 ? -12.396 12.416  83.398  1.00 48.19  ? 382  ALA B CB  1 
ATOM   2173 N  N   . SER B  1 134 ? -10.407 14.745  84.237  1.00 73.89  ? 383  SER B N   1 
ATOM   2174 C  CA  . SER B  1 134 ? -9.406  15.147  85.247  1.00 81.94  ? 383  SER B CA  1 
ATOM   2175 C  C   . SER B  1 134 ? -9.464  14.205  86.454  1.00 86.58  ? 383  SER B C   1 
ATOM   2176 O  O   . SER B  1 134 ? -10.551 13.946  87.003  1.00 84.07  ? 383  SER B O   1 
ATOM   2177 C  CB  . SER B  1 134 ? -9.661  16.582  85.741  1.00 82.33  ? 383  SER B CB  1 
ATOM   2178 O  OG  . SER B  1 134 ? -9.567  17.530  84.690  1.00 79.90  ? 383  SER B OG  1 
ATOM   2179 N  N   . CYS B  1 135 ? -8.294  13.707  86.849  1.00 86.14  ? 384  CYS B N   1 
ATOM   2180 C  CA  . CYS B  1 135 ? -8.154  12.859  88.032  1.00 97.70  ? 384  CYS B CA  1 
ATOM   2181 C  C   . CYS B  1 135 ? -7.267  13.538  89.089  1.00 103.19 ? 384  CYS B C   1 
ATOM   2182 O  O   . CYS B  1 135 ? -6.068  13.264  89.193  1.00 108.84 ? 384  CYS B O   1 
ATOM   2183 C  CB  . CYS B  1 135 ? -7.592  11.482  87.642  1.00 96.02  ? 384  CYS B CB  1 
ATOM   2184 S  SG  . CYS B  1 135 ? -8.770  10.284  86.935  1.00 92.28  ? 384  CYS B SG  1 
ATOM   2185 N  N   . LEU C  1 3   ? -29.118 -11.127 20.479  1.00 68.74  ? 252  LEU C N   1 
ATOM   2186 C  CA  . LEU C  1 3   ? -27.729 -11.680 20.521  1.00 66.36  ? 252  LEU C CA  1 
ATOM   2187 C  C   . LEU C  1 3   ? -27.462 -12.380 21.863  1.00 65.89  ? 252  LEU C C   1 
ATOM   2188 O  O   . LEU C  1 3   ? -27.884 -11.898 22.920  1.00 71.43  ? 252  LEU C O   1 
ATOM   2189 C  CB  . LEU C  1 3   ? -26.692 -10.569 20.301  1.00 65.39  ? 252  LEU C CB  1 
ATOM   2190 C  CG  . LEU C  1 3   ? -25.307 -11.072 19.849  1.00 69.06  ? 252  LEU C CG  1 
ATOM   2191 C  CD1 . LEU C  1 3   ? -25.360 -11.516 18.385  1.00 67.88  ? 252  LEU C CD1 1 
ATOM   2192 C  CD2 . LEU C  1 3   ? -24.210 -10.025 20.061  1.00 66.96  ? 252  LEU C CD2 1 
ATOM   2193 N  N   . CYS C  1 4   ? -26.770 -13.517 21.806  1.00 60.18  ? 253  CYS C N   1 
ATOM   2194 C  CA  . CYS C  1 4   ? -26.334 -14.261 22.994  1.00 52.49  ? 253  CYS C CA  1 
ATOM   2195 C  C   . CYS C  1 4   ? -24.956 -13.736 23.457  1.00 47.74  ? 253  CYS C C   1 
ATOM   2196 O  O   . CYS C  1 4   ? -24.056 -13.542 22.634  1.00 44.62  ? 253  CYS C O   1 
ATOM   2197 C  CB  . CYS C  1 4   ? -26.246 -15.733 22.618  1.00 49.88  ? 253  CYS C CB  1 
ATOM   2198 S  SG  . CYS C  1 4   ? -25.583 -16.872 23.859  1.00 44.89  ? 253  CYS C SG  1 
ATOM   2199 N  N   . HIS C  1 5   ? -24.786 -13.520 24.756  1.00 39.39  ? 254  HIS C N   1 
ATOM   2200 C  CA  . HIS C  1 5   ? -23.457 -13.162 25.293  1.00 36.10  ? 254  HIS C CA  1 
ATOM   2201 C  C   . HIS C  1 5   ? -23.005 -14.242 26.237  1.00 35.49  ? 254  HIS C C   1 
ATOM   2202 O  O   . HIS C  1 5   ? -23.838 -14.835 26.951  1.00 33.08  ? 254  HIS C O   1 
ATOM   2203 C  CB  . HIS C  1 5   ? -23.466 -11.801 26.008  1.00 37.55  ? 254  HIS C CB  1 
ATOM   2204 C  CG  . HIS C  1 5   ? -24.049 -10.683 25.191  1.00 39.73  ? 254  HIS C CG  1 
ATOM   2205 N  ND1 . HIS C  1 5   ? -23.280 -9.850  24.404  1.00 41.14  ? 254  HIS C ND1 1 
ATOM   2206 C  CD2 . HIS C  1 5   ? -25.331 -10.264 25.037  1.00 40.27  ? 254  HIS C CD2 1 
ATOM   2207 C  CE1 . HIS C  1 5   ? -24.062 -8.970  23.800  1.00 39.56  ? 254  HIS C CE1 1 
ATOM   2208 N  NE2 . HIS C  1 5   ? -25.309 -9.195  24.172  1.00 37.91  ? 254  HIS C NE2 1 
ATOM   2209 N  N   . PRO C  1 6   ? -21.673 -14.518 26.257  1.00 30.93  ? 255  PRO C N   1 
ATOM   2210 C  CA  . PRO C  1 6   ? -21.168 -15.519 27.181  1.00 28.15  ? 255  PRO C CA  1 
ATOM   2211 C  C   . PRO C  1 6   ? -21.536 -15.223 28.612  1.00 26.91  ? 255  PRO C C   1 
ATOM   2212 O  O   . PRO C  1 6   ? -21.913 -16.124 29.353  1.00 23.00  ? 255  PRO C O   1 
ATOM   2213 C  CB  . PRO C  1 6   ? -19.660 -15.425 26.994  1.00 31.22  ? 255  PRO C CB  1 
ATOM   2214 C  CG  . PRO C  1 6   ? -19.501 -14.973 25.574  1.00 31.48  ? 255  PRO C CG  1 
ATOM   2215 C  CD  . PRO C  1 6   ? -20.588 -13.956 25.432  1.00 30.92  ? 255  PRO C CD  1 
ATOM   2216 N  N   . CYS C  1 7   ? -21.425 -13.965 28.999  1.00 26.32  ? 256  CYS C N   1 
ATOM   2217 C  CA  . CYS C  1 7   ? -21.693 -13.581 30.383  1.00 27.51  ? 256  CYS C CA  1 
ATOM   2218 C  C   . CYS C  1 7   ? -22.772 -12.498 30.480  1.00 29.78  ? 256  CYS C C   1 
ATOM   2219 O  O   . CYS C  1 7   ? -23.051 -11.794 29.504  1.00 28.78  ? 256  CYS C O   1 
ATOM   2220 C  CB  . CYS C  1 7   ? -20.421 -13.018 31.010  1.00 28.02  ? 256  CYS C CB  1 
ATOM   2221 S  SG  . CYS C  1 7   ? -19.110 -14.204 31.112  1.00 31.38  ? 256  CYS C SG  1 
ATOM   2222 N  N   . PRO C  1 8   ? -23.337 -12.311 31.681  1.00 33.01  ? 257  PRO C N   1 
ATOM   2223 C  CA  . PRO C  1 8   ? -24.219 -11.189 31.844  1.00 31.49  ? 257  PRO C CA  1 
ATOM   2224 C  C   . PRO C  1 8   ? -23.450 -9.888  31.789  1.00 30.36  ? 257  PRO C C   1 
ATOM   2225 O  O   . PRO C  1 8   ? -22.202 -9.845  31.939  1.00 29.30  ? 257  PRO C O   1 
ATOM   2226 C  CB  . PRO C  1 8   ? -24.819 -11.409 33.247  1.00 34.15  ? 257  PRO C CB  1 
ATOM   2227 C  CG  . PRO C  1 8   ? -24.663 -12.879 33.493  1.00 36.60  ? 257  PRO C CG  1 
ATOM   2228 C  CD  . PRO C  1 8   ? -23.305 -13.145 32.897  1.00 36.41  ? 257  PRO C CD  1 
ATOM   2229 N  N   . TRP C  1 9   ? -24.209 -8.829  31.572  1.00 32.59  ? 258  TRP C N   1 
ATOM   2230 C  CA  . TRP C  1 9   ? -23.658 -7.503  31.341  1.00 34.87  ? 258  TRP C CA  1 
ATOM   2231 C  C   . TRP C  1 9   ? -22.903 -7.092  32.601  1.00 35.94  ? 258  TRP C C   1 
ATOM   2232 O  O   . TRP C  1 9   ? -23.415 -7.237  33.740  1.00 36.41  ? 258  TRP C O   1 
ATOM   2233 C  CB  . TRP C  1 9   ? -24.804 -6.547  31.010  1.00 35.95  ? 258  TRP C CB  1 
ATOM   2234 C  CG  . TRP C  1 9   ? -24.440 -5.252  30.285  1.00 39.09  ? 258  TRP C CG  1 
ATOM   2235 C  CD1 . TRP C  1 9   ? -23.273 -4.554  30.375  1.00 39.58  ? 258  TRP C CD1 1 
ATOM   2236 C  CD2 . TRP C  1 9   ? -25.298 -4.477  29.436  1.00 39.11  ? 258  TRP C CD2 1 
ATOM   2237 N  NE1 . TRP C  1 9   ? -23.332 -3.424  29.605  1.00 39.96  ? 258  TRP C NE1 1 
ATOM   2238 C  CE2 . TRP C  1 9   ? -24.567 -3.340  29.030  1.00 38.78  ? 258  TRP C CE2 1 
ATOM   2239 C  CE3 . TRP C  1 9   ? -26.614 -4.633  28.987  1.00 40.88  ? 258  TRP C CE3 1 
ATOM   2240 C  CZ2 . TRP C  1 9   ? -25.101 -2.358  28.194  1.00 41.13  ? 258  TRP C CZ2 1 
ATOM   2241 C  CZ3 . TRP C  1 9   ? -27.146 -3.665  28.155  1.00 43.22  ? 258  TRP C CZ3 1 
ATOM   2242 C  CH2 . TRP C  1 9   ? -26.381 -2.537  27.757  1.00 44.02  ? 258  TRP C CH2 1 
ATOM   2243 N  N   . GLU C  1 10  ? -21.680 -6.619  32.391  1.00 35.39  ? 259  GLU C N   1 
ATOM   2244 C  CA  . GLU C  1 10  ? -20.747 -6.209  33.459  1.00 39.35  ? 259  GLU C CA  1 
ATOM   2245 C  C   . GLU C  1 10  ? -19.937 -7.320  34.116  1.00 38.70  ? 259  GLU C C   1 
ATOM   2246 O  O   . GLU C  1 10  ? -18.952 -7.018  34.793  1.00 45.38  ? 259  GLU C O   1 
ATOM   2247 C  CB  . GLU C  1 10  ? -21.421 -5.356  34.549  1.00 42.94  ? 259  GLU C CB  1 
ATOM   2248 C  CG  . GLU C  1 10  ? -22.247 -4.232  33.947  1.00 47.40  ? 259  GLU C CG  1 
ATOM   2249 C  CD  . GLU C  1 10  ? -22.541 -3.104  34.900  1.00 49.70  ? 259  GLU C CD  1 
ATOM   2250 O  OE1 . GLU C  1 10  ? -22.036 -3.150  36.031  1.00 54.78  ? 259  GLU C OE1 1 
ATOM   2251 O  OE2 . GLU C  1 10  ? -23.275 -2.173  34.504  1.00 50.31  ? 259  GLU C OE2 1 
ATOM   2252 N  N   . TRP C  1 11  ? -20.306 -8.586  33.912  1.00 33.22  ? 260  TRP C N   1 
ATOM   2253 C  CA  . TRP C  1 11  ? -19.502 -9.682  34.407  1.00 30.39  ? 260  TRP C CA  1 
ATOM   2254 C  C   . TRP C  1 11  ? -18.304 -9.763  33.490  1.00 30.21  ? 260  TRP C C   1 
ATOM   2255 O  O   . TRP C  1 11  ? -18.396 -9.372  32.334  1.00 27.77  ? 260  TRP C O   1 
ATOM   2256 C  CB  . TRP C  1 11  ? -20.259 -10.998 34.399  1.00 28.77  ? 260  TRP C CB  1 
ATOM   2257 C  CG  . TRP C  1 11  ? -21.359 -11.042 35.399  1.00 28.87  ? 260  TRP C CG  1 
ATOM   2258 C  CD1 . TRP C  1 11  ? -22.317 -10.107 35.574  1.00 31.75  ? 260  TRP C CD1 1 
ATOM   2259 C  CD2 . TRP C  1 11  ? -21.624 -12.071 36.370  1.00 28.11  ? 260  TRP C CD2 1 
ATOM   2260 N  NE1 . TRP C  1 11  ? -23.167 -10.484 36.584  1.00 31.95  ? 260  TRP C NE1 1 
ATOM   2261 C  CE2 . TRP C  1 11  ? -22.748 -11.677 37.097  1.00 29.49  ? 260  TRP C CE2 1 
ATOM   2262 C  CE3 . TRP C  1 11  ? -20.995 -13.262 36.715  1.00 29.35  ? 260  TRP C CE3 1 
ATOM   2263 C  CZ2 . TRP C  1 11  ? -23.278 -12.433 38.111  1.00 30.58  ? 260  TRP C CZ2 1 
ATOM   2264 C  CZ3 . TRP C  1 11  ? -21.514 -14.007 37.741  1.00 29.34  ? 260  TRP C CZ3 1 
ATOM   2265 C  CH2 . TRP C  1 11  ? -22.649 -13.588 38.427  1.00 29.17  ? 260  TRP C CH2 1 
ATOM   2266 N  N   . THR C  1 12  ? -17.187 -10.268 34.019  1.00 29.02  ? 261  THR C N   1 
ATOM   2267 C  CA  . THR C  1 12  ? -15.978 -10.500 33.235  1.00 29.20  ? 261  THR C CA  1 
ATOM   2268 C  C   . THR C  1 12  ? -15.877 -11.941 32.797  1.00 28.70  ? 261  THR C C   1 
ATOM   2269 O  O   . THR C  1 12  ? -16.023 -12.855 33.607  1.00 30.78  ? 261  THR C O   1 
ATOM   2270 C  CB  . THR C  1 12  ? -14.770 -10.225 34.114  1.00 27.61  ? 261  THR C CB  1 
ATOM   2271 O  OG1 . THR C  1 12  ? -14.845 -8.900  34.566  1.00 30.55  ? 261  THR C OG1 1 
ATOM   2272 C  CG2 . THR C  1 12  ? -13.475 -10.420 33.367  1.00 29.81  ? 261  THR C CG2 1 
ATOM   2273 N  N   . PHE C  1 13  ? -15.593 -12.151 31.522  1.00 30.86  ? 262  PHE C N   1 
ATOM   2274 C  CA  . PHE C  1 13  ? -15.430 -13.489 30.976  1.00 27.19  ? 262  PHE C CA  1 
ATOM   2275 C  C   . PHE C  1 13  ? -14.016 -13.892 31.270  1.00 26.84  ? 262  PHE C C   1 
ATOM   2276 O  O   . PHE C  1 13  ? -13.123 -13.124 30.953  1.00 29.48  ? 262  PHE C O   1 
ATOM   2277 C  CB  . PHE C  1 13  ? -15.597 -13.493 29.450  1.00 29.33  ? 262  PHE C CB  1 
ATOM   2278 C  CG  . PHE C  1 13  ? -15.366 -14.858 28.831  1.00 27.68  ? 262  PHE C CG  1 
ATOM   2279 C  CD1 . PHE C  1 13  ? -16.394 -15.771 28.762  1.00 28.12  ? 262  PHE C CD1 1 
ATOM   2280 C  CD2 . PHE C  1 13  ? -14.116 -15.231 28.360  1.00 28.00  ? 262  PHE C CD2 1 
ATOM   2281 C  CE1 . PHE C  1 13  ? -16.196 -17.034 28.202  1.00 29.67  ? 262  PHE C CE1 1 
ATOM   2282 C  CE2 . PHE C  1 13  ? -13.896 -16.504 27.843  1.00 28.03  ? 262  PHE C CE2 1 
ATOM   2283 C  CZ  . PHE C  1 13  ? -14.940 -17.404 27.760  1.00 29.89  ? 262  PHE C CZ  1 
ATOM   2284 N  N   . PHE C  1 14  ? -13.784 -15.068 31.834  1.00 23.91  ? 263  PHE C N   1 
ATOM   2285 C  CA  . PHE C  1 14  ? -12.411 -15.582 31.953  1.00 26.83  ? 263  PHE C CA  1 
ATOM   2286 C  C   . PHE C  1 14  ? -12.420 -17.125 31.857  1.00 28.90  ? 263  PHE C C   1 
ATOM   2287 O  O   . PHE C  1 14  ? -13.034 -17.843 32.713  1.00 26.03  ? 263  PHE C O   1 
ATOM   2288 C  CB  . PHE C  1 14  ? -11.729 -15.087 33.238  1.00 28.52  ? 263  PHE C CB  1 
ATOM   2289 C  CG  . PHE C  1 14  ? -10.336 -15.606 33.442  1.00 29.35  ? 263  PHE C CG  1 
ATOM   2290 C  CD1 . PHE C  1 14  ? -10.120 -16.793 34.106  1.00 31.01  ? 263  PHE C CD1 1 
ATOM   2291 C  CD2 . PHE C  1 14  ? -9.257  -14.923 32.952  1.00 31.58  ? 263  PHE C CD2 1 
ATOM   2292 C  CE1 . PHE C  1 14  ? -8.846  -17.287 34.292  1.00 32.46  ? 263  PHE C CE1 1 
ATOM   2293 C  CE2 . PHE C  1 14  ? -7.980  -15.404 33.146  1.00 32.91  ? 263  PHE C CE2 1 
ATOM   2294 C  CZ  . PHE C  1 14  ? -7.774  -16.585 33.815  1.00 31.55  ? 263  PHE C CZ  1 
ATOM   2295 N  N   . GLN C  1 15  ? -11.746 -17.612 30.802  1.00 24.96  ? 264  GLN C N   1 
ATOM   2296 C  CA  . GLN C  1 15  ? -11.581 -19.047 30.534  1.00 26.16  ? 264  GLN C CA  1 
ATOM   2297 C  C   . GLN C  1 15  ? -12.859 -19.850 30.719  1.00 25.19  ? 264  GLN C C   1 
ATOM   2298 O  O   . GLN C  1 15  ? -12.875 -20.864 31.398  1.00 26.58  ? 264  GLN C O   1 
ATOM   2299 C  CB  . GLN C  1 15  ? -10.466 -19.667 31.401  1.00 25.50  ? 264  GLN C CB  1 
ATOM   2300 C  CG  . GLN C  1 15  ? -9.187  -18.898 31.340  1.00 26.07  ? 264  GLN C CG  1 
ATOM   2301 C  CD  . GLN C  1 15  ? -7.969  -19.726 31.692  1.00 30.34  ? 264  GLN C CD  1 
ATOM   2302 O  OE1 . GLN C  1 15  ? -8.028  -20.659 32.504  1.00 28.97  ? 264  GLN C OE1 1 
ATOM   2303 N  NE2 . GLN C  1 15  ? -6.832  -19.377 31.075  1.00 28.56  ? 264  GLN C NE2 1 
ATOM   2304 N  N   . GLY C  1 16  ? -13.923 -19.372 30.102  1.00 27.65  ? 265  GLY C N   1 
ATOM   2305 C  CA  . GLY C  1 16  ? -15.196 -20.082 30.059  1.00 29.66  ? 265  GLY C CA  1 
ATOM   2306 C  C   . GLY C  1 16  ? -16.116 -19.868 31.248  1.00 29.17  ? 265  GLY C C   1 
ATOM   2307 O  O   . GLY C  1 16  ? -17.150 -20.550 31.374  1.00 27.88  ? 265  GLY C O   1 
ATOM   2308 N  N   . ASN C  1 17  ? -15.728 -18.977 32.154  1.00 28.69  ? 266  ASN C N   1 
ATOM   2309 C  CA  . ASN C  1 17  ? -16.584 -18.646 33.294  1.00 26.57  ? 266  ASN C CA  1 
ATOM   2310 C  C   . ASN C  1 17  ? -16.748 -17.127 33.328  1.00 28.80  ? 266  ASN C C   1 
ATOM   2311 O  O   . ASN C  1 17  ? -16.017 -16.363 32.657  1.00 27.54  ? 266  ASN C O   1 
ATOM   2312 C  CB  . ASN C  1 17  ? -16.001 -19.193 34.610  1.00 26.31  ? 266  ASN C CB  1 
ATOM   2313 C  CG  . ASN C  1 17  ? -15.937 -20.751 34.657  1.00 28.55  ? 266  ASN C CG  1 
ATOM   2314 O  OD1 . ASN C  1 17  ? -16.945 -21.412 34.839  1.00 28.93  ? 266  ASN C OD1 1 
ATOM   2315 N  ND2 . ASN C  1 17  ? -14.728 -21.315 34.565  1.00 24.94  ? 266  ASN C ND2 1 
ATOM   2316 N  N   . CYS C  1 18  ? -17.742 -16.718 34.092  1.00 27.65  ? 267  CYS C N   1 
ATOM   2317 C  CA  . CYS C  1 18  ? -18.127 -15.354 34.248  1.00 29.47  ? 267  CYS C CA  1 
ATOM   2318 C  C   . CYS C  1 18  ? -17.934 -15.002 35.693  1.00 29.99  ? 267  CYS C C   1 
ATOM   2319 O  O   . CYS C  1 18  ? -18.440 -15.734 36.576  1.00 26.67  ? 267  CYS C O   1 
ATOM   2320 C  CB  . CYS C  1 18  ? -19.622 -15.211 33.899  1.00 31.00  ? 267  CYS C CB  1 
ATOM   2321 S  SG  . CYS C  1 18  ? -19.969 -15.730 32.213  1.00 30.36  ? 267  CYS C SG  1 
ATOM   2322 N  N   . TYR C  1 19  ? -17.274 -13.866 35.920  1.00 27.72  ? 268  TYR C N   1 
ATOM   2323 C  CA  . TYR C  1 19  ? -17.003 -13.365 37.243  1.00 27.75  ? 268  TYR C CA  1 
ATOM   2324 C  C   . TYR C  1 19  ? -17.654 -11.997 37.481  1.00 27.16  ? 268  TYR C C   1 
ATOM   2325 O  O   . TYR C  1 19  ? -17.553 -11.056 36.650  1.00 27.39  ? 268  TYR C O   1 
ATOM   2326 C  CB  . TYR C  1 19  ? -15.485 -13.311 37.502  1.00 28.40  ? 268  TYR C CB  1 
ATOM   2327 C  CG  . TYR C  1 19  ? -14.803 -14.654 37.334  1.00 28.61  ? 268  TYR C CG  1 
ATOM   2328 C  CD1 . TYR C  1 19  ? -14.495 -15.142 36.070  1.00 27.27  ? 268  TYR C CD1 1 
ATOM   2329 C  CD2 . TYR C  1 19  ? -14.478 -15.447 38.430  1.00 28.12  ? 268  TYR C CD2 1 
ATOM   2330 C  CE1 . TYR C  1 19  ? -13.877 -16.376 35.899  1.00 29.66  ? 268  TYR C CE1 1 
ATOM   2331 C  CE2 . TYR C  1 19  ? -13.869 -16.681 38.264  1.00 28.29  ? 268  TYR C CE2 1 
ATOM   2332 C  CZ  . TYR C  1 19  ? -13.551 -17.126 36.985  1.00 27.89  ? 268  TYR C CZ  1 
ATOM   2333 O  OH  . TYR C  1 19  ? -12.971 -18.353 36.794  1.00 29.71  ? 268  TYR C OH  1 
ATOM   2334 N  N   . PHE C  1 20  ? -18.362 -11.916 38.605  1.00 26.07  ? 269  PHE C N   1 
ATOM   2335 C  CA  . PHE C  1 20  ? -18.873 -10.675 39.133  1.00 26.73  ? 269  PHE C CA  1 
ATOM   2336 C  C   . PHE C  1 20  ? -17.933 -10.163 40.223  1.00 26.26  ? 269  PHE C C   1 
ATOM   2337 O  O   . PHE C  1 20  ? -17.733 -10.834 41.222  1.00 26.50  ? 269  PHE C O   1 
ATOM   2338 C  CB  . PHE C  1 20  ? -20.240 -10.885 39.730  1.00 28.84  ? 269  PHE C CB  1 
ATOM   2339 C  CG  . PHE C  1 20  ? -20.858 -9.618  40.256  1.00 31.35  ? 269  PHE C CG  1 
ATOM   2340 C  CD1 . PHE C  1 20  ? -21.165 -8.578  39.384  1.00 34.90  ? 269  PHE C CD1 1 
ATOM   2341 C  CD2 . PHE C  1 20  ? -21.086 -9.445  41.618  1.00 33.18  ? 269  PHE C CD2 1 
ATOM   2342 C  CE1 . PHE C  1 20  ? -21.724 -7.377  39.855  1.00 36.70  ? 269  PHE C CE1 1 
ATOM   2343 C  CE2 . PHE C  1 20  ? -21.637 -8.252  42.105  1.00 34.31  ? 269  PHE C CE2 1 
ATOM   2344 C  CZ  . PHE C  1 20  ? -21.964 -7.221  41.220  1.00 35.64  ? 269  PHE C CZ  1 
ATOM   2345 N  N   . MET C  1 21  ? -17.354 -8.992  40.010  1.00 28.08  ? 270  MET C N   1 
ATOM   2346 C  CA  . MET C  1 21  ? -16.534 -8.334  41.012  1.00 27.74  ? 270  MET C CA  1 
ATOM   2347 C  C   . MET C  1 21  ? -17.440 -7.320  41.691  1.00 25.64  ? 270  MET C C   1 
ATOM   2348 O  O   . MET C  1 21  ? -17.881 -6.405  41.044  1.00 24.80  ? 270  MET C O   1 
ATOM   2349 C  CB  . MET C  1 21  ? -15.344 -7.598  40.370  1.00 31.89  ? 270  MET C CB  1 
ATOM   2350 C  CG  . MET C  1 21  ? -14.688 -8.277  39.169  1.00 39.62  ? 270  MET C CG  1 
ATOM   2351 S  SD  . MET C  1 21  ? -14.141 -9.929  39.503  1.00 46.97  ? 270  MET C SD  1 
ATOM   2352 C  CE  . MET C  1 21  ? -12.841 -10.162 38.298  1.00 48.86  ? 270  MET C CE  1 
ATOM   2353 N  N   . SER C  1 22  ? -17.743 -7.482  42.972  1.00 24.65  ? 271  SER C N   1 
ATOM   2354 C  CA  . SER C  1 22  ? -18.640 -6.523  43.662  1.00 26.55  ? 271  SER C CA  1 
ATOM   2355 C  C   . SER C  1 22  ? -17.985 -5.139  43.772  1.00 26.66  ? 271  SER C C   1 
ATOM   2356 O  O   . SER C  1 22  ? -16.767 -5.046  43.837  1.00 25.32  ? 271  SER C O   1 
ATOM   2357 C  CB  . SER C  1 22  ? -18.960 -7.027  45.082  1.00 22.62  ? 271  SER C CB  1 
ATOM   2358 O  OG  . SER C  1 22  ? -17.849 -6.777  45.935  1.00 24.31  ? 271  SER C OG  1 
ATOM   2359 N  N   . ASN C  1 23  ? -18.764 -4.079  43.886  1.00 29.43  ? 272  ASN C N   1 
ATOM   2360 C  CA  A ASN C  1 23  ? -18.207 -2.770  44.178  0.50 29.80  ? 272  ASN C CA  1 
ATOM   2361 C  CA  B ASN C  1 23  ? -18.159 -2.763  44.235  0.50 30.39  ? 272  ASN C CA  1 
ATOM   2362 C  C   . ASN C  1 23  ? -18.696 -2.308  45.563  1.00 30.10  ? 272  ASN C C   1 
ATOM   2363 O  O   . ASN C  1 23  ? -18.531 -1.152  45.917  1.00 29.82  ? 272  ASN C O   1 
ATOM   2364 C  CB  A ASN C  1 23  ? -18.536 -1.768  43.046  0.50 31.63  ? 272  ASN C CB  1 
ATOM   2365 C  CB  B ASN C  1 23  ? -18.351 -1.657  43.169  0.50 33.18  ? 272  ASN C CB  1 
ATOM   2366 C  CG  A ASN C  1 23  ? -17.700 -1.996  41.762  0.50 31.66  ? 272  ASN C CG  1 
ATOM   2367 C  CG  B ASN C  1 23  ? -17.274 -0.529  43.238  0.50 34.59  ? 272  ASN C CG  1 
ATOM   2368 O  OD1 A ASN C  1 23  ? -16.493 -2.313  41.805  0.50 30.89  ? 272  ASN C OD1 1 
ATOM   2369 O  OD1 B ASN C  1 23  ? -16.752 -0.155  44.313  0.50 36.43  ? 272  ASN C OD1 1 
ATOM   2370 N  ND2 A ASN C  1 23  ? -18.346 -1.799  40.608  0.50 30.93  ? 272  ASN C ND2 1 
ATOM   2371 N  ND2 B ASN C  1 23  ? -16.975 0.047   42.074  0.50 34.10  ? 272  ASN C ND2 1 
ATOM   2372 N  N   . SER C  1 24  ? -19.276 -3.229  46.336  1.00 28.07  ? 273  SER C N   1 
ATOM   2373 C  CA  . SER C  1 24  ? -19.546 -2.957  47.754  1.00 27.93  ? 273  SER C CA  1 
ATOM   2374 C  C   . SER C  1 24  ? -19.106 -4.162  48.624  1.00 27.46  ? 273  SER C C   1 
ATOM   2375 O  O   . SER C  1 24  ? -18.477 -5.131  48.116  1.00 25.90  ? 273  SER C O   1 
ATOM   2376 C  CB  . SER C  1 24  ? -21.032 -2.632  47.951  1.00 31.25  ? 273  SER C CB  1 
ATOM   2377 O  OG  . SER C  1 24  ? -21.808 -3.786  47.659  1.00 33.61  ? 273  SER C OG  1 
ATOM   2378 N  N   . GLN C  1 25  ? -19.387 -4.103  49.920  1.00 23.65  ? 274  GLN C N   1 
ATOM   2379 C  CA  . GLN C  1 25  ? -18.796 -5.056  50.849  1.00 26.64  ? 274  GLN C CA  1 
ATOM   2380 C  C   . GLN C  1 25  ? -19.841 -5.789  51.694  1.00 26.39  ? 274  GLN C C   1 
ATOM   2381 O  O   . GLN C  1 25  ? -20.825 -5.218  52.093  1.00 25.46  ? 274  GLN C O   1 
ATOM   2382 C  CB  . GLN C  1 25  ? -17.776 -4.365  51.767  1.00 26.10  ? 274  GLN C CB  1 
ATOM   2383 C  CG  . GLN C  1 25  ? -16.703 -3.532  51.041  1.00 27.47  ? 274  GLN C CG  1 
ATOM   2384 C  CD  . GLN C  1 25  ? -16.321 -2.274  51.837  1.00 28.83  ? 274  GLN C CD  1 
ATOM   2385 O  OE1 . GLN C  1 25  ? -17.106 -1.315  51.912  1.00 28.11  ? 274  GLN C OE1 1 
ATOM   2386 N  NE2 . GLN C  1 25  ? -15.132 -2.284  52.448  1.00 26.38  ? 274  GLN C NE2 1 
ATOM   2387 N  N   . ARG C  1 26  ? -19.588 -7.056  51.951  1.00 24.80  ? 275  ARG C N   1 
ATOM   2388 C  CA  . ARG C  1 26  ? -20.497 -7.911  52.706  1.00 26.00  ? 275  ARG C CA  1 
ATOM   2389 C  C   . ARG C  1 26  ? -19.677 -8.894  53.499  1.00 25.07  ? 275  ARG C C   1 
ATOM   2390 O  O   . ARG C  1 26  ? -18.547 -9.235  53.126  1.00 22.00  ? 275  ARG C O   1 
ATOM   2391 C  CB  . ARG C  1 26  ? -21.420 -8.687  51.767  1.00 28.84  ? 275  ARG C CB  1 
ATOM   2392 C  CG  . ARG C  1 26  ? -22.585 -7.915  51.233  1.00 28.98  ? 275  ARG C CG  1 
ATOM   2393 C  CD  . ARG C  1 26  ? -23.371 -8.768  50.289  1.00 34.31  ? 275  ARG C CD  1 
ATOM   2394 N  NE  . ARG C  1 26  ? -24.540 -8.053  49.796  1.00 40.38  ? 275  ARG C NE  1 
ATOM   2395 C  CZ  . ARG C  1 26  ? -25.787 -8.534  49.769  1.00 44.79  ? 275  ARG C CZ  1 
ATOM   2396 N  NH1 . ARG C  1 26  ? -26.080 -9.795  50.153  1.00 43.60  ? 275  ARG C NH1 1 
ATOM   2397 N  NH2 . ARG C  1 26  ? -26.753 -7.746  49.323  1.00 43.84  ? 275  ARG C NH2 1 
ATOM   2398 N  N   . ASN C  1 27  ? -20.243 -9.370  54.593  1.00 26.13  ? 276  ASN C N   1 
ATOM   2399 C  CA  . ASN C  1 27  ? -19.614 -10.439 55.302  1.00 25.05  ? 276  ASN C CA  1 
ATOM   2400 C  C   . ASN C  1 27  ? -19.651 -11.680 54.419  1.00 23.10  ? 276  ASN C C   1 
ATOM   2401 O  O   . ASN C  1 27  ? -20.314 -11.726 53.385  1.00 26.16  ? 276  ASN C O   1 
ATOM   2402 C  CB  . ASN C  1 27  ? -20.204 -10.638 56.730  1.00 24.33  ? 276  ASN C CB  1 
ATOM   2403 C  CG  . ASN C  1 27  ? -21.638 -11.182 56.735  1.00 26.28  ? 276  ASN C CG  1 
ATOM   2404 O  OD1 . ASN C  1 27  ? -22.030 -11.927 55.856  1.00 22.82  ? 276  ASN C OD1 1 
ATOM   2405 N  ND2 . ASN C  1 27  ? -22.410 -10.821 57.758  1.00 23.04  ? 276  ASN C ND2 1 
ATOM   2406 N  N   . TRP C  1 28  ? -18.937 -12.696 54.839  1.00 23.05  ? 277  TRP C N   1 
ATOM   2407 C  CA  . TRP C  1 28  ? -18.762 -13.895 54.025  1.00 22.29  ? 277  TRP C CA  1 
ATOM   2408 C  C   . TRP C  1 28  ? -20.096 -14.587 53.694  1.00 22.51  ? 277  TRP C C   1 
ATOM   2409 O  O   . TRP C  1 28  ? -20.327 -14.988 52.565  1.00 21.11  ? 277  TRP C O   1 
ATOM   2410 C  CB  . TRP C  1 28  ? -17.786 -14.824 54.717  1.00 20.37  ? 277  TRP C CB  1 
ATOM   2411 C  CG  . TRP C  1 28  ? -17.254 -15.933 53.878  1.00 20.38  ? 277  TRP C CG  1 
ATOM   2412 C  CD1 . TRP C  1 28  ? -16.241 -15.877 52.995  1.00 18.82  ? 277  TRP C CD1 1 
ATOM   2413 C  CD2 . TRP C  1 28  ? -17.684 -17.293 53.913  1.00 20.90  ? 277  TRP C CD2 1 
ATOM   2414 N  NE1 . TRP C  1 28  ? -16.016 -17.117 52.444  1.00 17.83  ? 277  TRP C NE1 1 
ATOM   2415 C  CE2 . TRP C  1 28  ? -16.889 -18.004 53.007  1.00 20.12  ? 277  TRP C CE2 1 
ATOM   2416 C  CE3 . TRP C  1 28  ? -18.674 -17.976 54.628  1.00 23.18  ? 277  TRP C CE3 1 
ATOM   2417 C  CZ2 . TRP C  1 28  ? -17.055 -19.349 52.778  1.00 20.85  ? 277  TRP C CZ2 1 
ATOM   2418 C  CZ3 . TRP C  1 28  ? -18.836 -19.325 54.399  1.00 23.75  ? 277  TRP C CZ3 1 
ATOM   2419 C  CH2 . TRP C  1 28  ? -18.029 -19.991 53.473  1.00 23.79  ? 277  TRP C CH2 1 
ATOM   2420 N  N   . HIS C  1 29  ? -21.002 -14.651 54.660  1.00 22.48  ? 278  HIS C N   1 
ATOM   2421 C  CA  . HIS C  1 29  ? -22.168 -15.445 54.545  1.00 24.58  ? 278  HIS C CA  1 
ATOM   2422 C  C   . HIS C  1 29  ? -23.139 -14.733 53.652  1.00 24.28  ? 278  HIS C C   1 
ATOM   2423 O  O   . HIS C  1 29  ? -23.762 -15.343 52.764  1.00 27.61  ? 278  HIS C O   1 
ATOM   2424 C  CB  . HIS C  1 29  ? -22.767 -15.784 55.958  1.00 27.51  ? 278  HIS C CB  1 
ATOM   2425 C  CG  . HIS C  1 29  ? -22.160 -17.003 56.578  1.00 33.72  ? 278  HIS C CG  1 
ATOM   2426 N  ND1 . HIS C  1 29  ? -21.226 -16.947 57.602  1.00 37.73  ? 278  HIS C ND1 1 
ATOM   2427 C  CD2 . HIS C  1 29  ? -22.341 -18.324 56.304  1.00 38.26  ? 278  HIS C CD2 1 
ATOM   2428 C  CE1 . HIS C  1 29  ? -20.863 -18.176 57.922  1.00 37.39  ? 278  HIS C CE1 1 
ATOM   2429 N  NE2 . HIS C  1 29  ? -21.538 -19.030 57.164  1.00 36.89  ? 278  HIS C NE2 1 
ATOM   2430 N  N   . ASP C  1 30  ? -23.228 -13.425 53.813  1.00 23.02  ? 279  ASP C N   1 
ATOM   2431 C  CA  . ASP C  1 30  ? -24.003 -12.629 52.911  1.00 22.25  ? 279  ASP C CA  1 
ATOM   2432 C  C   . ASP C  1 30  ? -23.419 -12.577 51.483  1.00 24.13  ? 279  ASP C C   1 
ATOM   2433 O  O   . ASP C  1 30  ? -24.177 -12.344 50.515  1.00 22.02  ? 279  ASP C O   1 
ATOM   2434 C  CB  . ASP C  1 30  ? -24.102 -11.233 53.448  1.00 25.50  ? 279  ASP C CB  1 
ATOM   2435 C  CG  . ASP C  1 30  ? -24.943 -11.170 54.725  1.00 28.82  ? 279  ASP C CG  1 
ATOM   2436 O  OD1 . ASP C  1 30  ? -25.581 -12.191 55.069  1.00 30.43  ? 279  ASP C OD1 1 
ATOM   2437 O  OD2 . ASP C  1 30  ? -24.956 -10.103 55.366  1.00 30.47  ? 279  ASP C OD2 1 
ATOM   2438 N  N   . SER C  1 31  ? -22.097 -12.719 51.345  1.00 21.89  ? 280  SER C N   1 
ATOM   2439 C  CA  . SER C  1 31  ? -21.502 -12.774 50.001  1.00 21.85  ? 280  SER C CA  1 
ATOM   2440 C  C   . SER C  1 31  ? -21.957 -14.077 49.327  1.00 22.44  ? 280  SER C C   1 
ATOM   2441 O  O   . SER C  1 31  ? -22.295 -14.092 48.175  1.00 25.02  ? 280  SER C O   1 
ATOM   2442 C  CB  . SER C  1 31  ? -19.993 -12.715 50.067  1.00 21.18  ? 280  SER C CB  1 
ATOM   2443 O  OG  . SER C  1 31  ? -19.534 -11.489 50.613  1.00 20.81  ? 280  SER C OG  1 
ATOM   2444 N  N   . ILE C  1 32  ? -21.991 -15.164 50.071  1.00 23.74  ? 281  ILE C N   1 
ATOM   2445 C  CA  . ILE C  1 32  ? -22.445 -16.397 49.536  1.00 23.24  ? 281  ILE C CA  1 
ATOM   2446 C  C   . ILE C  1 32  ? -23.895 -16.241 49.007  1.00 26.92  ? 281  ILE C C   1 
ATOM   2447 O  O   . ILE C  1 32  ? -24.235 -16.699 47.893  1.00 24.07  ? 281  ILE C O   1 
ATOM   2448 C  CB  . ILE C  1 32  ? -22.351 -17.493 50.610  1.00 25.14  ? 281  ILE C CB  1 
ATOM   2449 C  CG1 . ILE C  1 32  ? -20.895 -17.880 50.686  1.00 28.26  ? 281  ILE C CG1 1 
ATOM   2450 C  CG2 . ILE C  1 32  ? -23.248 -18.694 50.297  1.00 23.84  ? 281  ILE C CG2 1 
ATOM   2451 C  CD1 . ILE C  1 32  ? -20.610 -18.989 51.613  1.00 33.07  ? 281  ILE C CD1 1 
ATOM   2452 N  N   . THR C  1 33  ? -24.734 -15.591 49.801  1.00 23.92  ? 282  THR C N   1 
ATOM   2453 C  CA  . THR C  1 33  ? -26.109 -15.412 49.437  1.00 24.34  ? 282  THR C CA  1 
ATOM   2454 C  C   . THR C  1 33  ? -26.219 -14.582 48.181  1.00 24.95  ? 282  THR C C   1 
ATOM   2455 O  O   . THR C  1 33  ? -27.013 -14.878 47.298  1.00 26.89  ? 282  THR C O   1 
ATOM   2456 C  CB  . THR C  1 33  ? -26.859 -14.670 50.547  1.00 26.06  ? 282  THR C CB  1 
ATOM   2457 O  OG1 . THR C  1 33  ? -26.824 -15.458 51.744  1.00 25.80  ? 282  THR C OG1 1 
ATOM   2458 C  CG2 . THR C  1 33  ? -28.296 -14.424 50.122  1.00 28.17  ? 282  THR C CG2 1 
ATOM   2459 N  N   . ALA C  1 34  ? -25.466 -13.500 48.142  1.00 23.88  ? 283  ALA C N   1 
ATOM   2460 C  CA  . ALA C  1 34  ? -25.519 -12.580 47.072  1.00 25.25  ? 283  ALA C CA  1 
ATOM   2461 C  C   . ALA C  1 34  ? -25.185 -13.317 45.761  1.00 25.16  ? 283  ALA C C   1 
ATOM   2462 O  O   . ALA C  1 34  ? -25.874 -13.181 44.774  1.00 26.34  ? 283  ALA C O   1 
ATOM   2463 C  CB  . ALA C  1 34  ? -24.549 -11.424 47.324  1.00 26.33  ? 283  ALA C CB  1 
ATOM   2464 N  N   . CYS C  1 35  ? -24.167 -14.140 45.790  1.00 24.46  ? 284  CYS C N   1 
ATOM   2465 C  CA  . CYS C  1 35  ? -23.796 -14.945 44.613  1.00 25.87  ? 284  CYS C CA  1 
ATOM   2466 C  C   . CYS C  1 35  ? -24.931 -15.944 44.226  1.00 27.85  ? 284  CYS C C   1 
ATOM   2467 O  O   . CYS C  1 35  ? -25.267 -16.029 43.046  1.00 24.37  ? 284  CYS C O   1 
ATOM   2468 C  CB  . CYS C  1 35  ? -22.468 -15.669 44.847  1.00 24.79  ? 284  CYS C CB  1 
ATOM   2469 S  SG  . CYS C  1 35  ? -21.074 -14.532 44.912  1.00 24.03  ? 284  CYS C SG  1 
ATOM   2470 N  N   . LYS C  1 36  ? -25.536 -16.640 45.203  1.00 28.25  ? 285  LYS C N   1 
ATOM   2471 C  CA  . LYS C  1 36  ? -26.614 -17.590 44.906  1.00 31.31  ? 285  LYS C CA  1 
ATOM   2472 C  C   . LYS C  1 36  ? -27.768 -16.930 44.152  1.00 29.57  ? 285  LYS C C   1 
ATOM   2473 O  O   . LYS C  1 36  ? -28.268 -17.465 43.167  1.00 28.67  ? 285  LYS C O   1 
ATOM   2474 C  CB  . LYS C  1 36  ? -27.145 -18.229 46.176  1.00 34.43  ? 285  LYS C CB  1 
ATOM   2475 C  CG  . LYS C  1 36  ? -26.268 -19.372 46.616  1.00 38.20  ? 285  LYS C CG  1 
ATOM   2476 C  CD  . LYS C  1 36  ? -26.676 -19.907 47.976  1.00 41.61  ? 285  LYS C CD  1 
ATOM   2477 C  CE  . LYS C  1 36  ? -25.765 -21.089 48.266  1.00 46.90  ? 285  LYS C CE  1 
ATOM   2478 N  NZ  . LYS C  1 36  ? -25.918 -21.605 49.647  1.00 52.01  ? 285  LYS C NZ  1 
ATOM   2479 N  N   . GLU C  1 37  ? -28.124 -15.733 44.587  1.00 28.74  ? 286  GLU C N   1 
ATOM   2480 C  CA  . GLU C  1 37  ? -29.258 -15.027 44.070  1.00 30.05  ? 286  GLU C CA  1 
ATOM   2481 C  C   . GLU C  1 37  ? -29.063 -14.568 42.623  1.00 30.43  ? 286  GLU C C   1 
ATOM   2482 O  O   . GLU C  1 37  ? -30.048 -14.278 41.942  1.00 29.60  ? 286  GLU C O   1 
ATOM   2483 C  CB  . GLU C  1 37  ? -29.633 -13.870 44.982  1.00 30.90  ? 286  GLU C CB  1 
ATOM   2484 C  CG  . GLU C  1 37  ? -30.276 -14.398 46.261  1.00 37.92  ? 286  GLU C CG  1 
ATOM   2485 C  CD  . GLU C  1 37  ? -30.690 -13.305 47.222  1.00 46.37  ? 286  GLU C CD  1 
ATOM   2486 O  OE1 . GLU C  1 37  ? -30.462 -12.096 46.923  1.00 53.77  ? 286  GLU C OE1 1 
ATOM   2487 O  OE2 . GLU C  1 37  ? -31.229 -13.678 48.288  1.00 53.75  ? 286  GLU C OE2 1 
ATOM   2488 N  N   . VAL C  1 38  ? -27.825 -14.546 42.135  1.00 29.20  ? 287  VAL C N   1 
ATOM   2489 C  CA  . VAL C  1 38  ? -27.610 -14.284 40.689  1.00 28.29  ? 287  VAL C CA  1 
ATOM   2490 C  C   . VAL C  1 38  ? -27.181 -15.538 39.948  1.00 30.40  ? 287  VAL C C   1 
ATOM   2491 O  O   . VAL C  1 38  ? -26.611 -15.466 38.840  1.00 32.40  ? 287  VAL C O   1 
ATOM   2492 C  CB  . VAL C  1 38  ? -26.624 -13.122 40.441  1.00 27.45  ? 287  VAL C CB  1 
ATOM   2493 C  CG1 . VAL C  1 38  ? -27.199 -11.816 40.939  1.00 28.48  ? 287  VAL C CG1 1 
ATOM   2494 C  CG2 . VAL C  1 38  ? -25.287 -13.383 41.093  1.00 27.90  ? 287  VAL C CG2 1 
ATOM   2495 N  N   . GLY C  1 39  ? -27.481 -16.687 40.552  1.00 29.44  ? 288  GLY C N   1 
ATOM   2496 C  CA  . GLY C  1 39  ? -27.163 -17.976 39.980  1.00 27.20  ? 288  GLY C CA  1 
ATOM   2497 C  C   . GLY C  1 39  ? -25.693 -18.335 39.909  1.00 28.14  ? 288  GLY C C   1 
ATOM   2498 O  O   . GLY C  1 39  ? -25.281 -19.081 39.040  1.00 28.00  ? 288  GLY C O   1 
ATOM   2499 N  N   . ALA C  1 40  ? -24.901 -17.831 40.850  1.00 29.37  ? 289  ALA C N   1 
ATOM   2500 C  CA  . ALA C  1 40  ? -23.463 -18.050 40.848  1.00 26.60  ? 289  ALA C CA  1 
ATOM   2501 C  C   . ALA C  1 40  ? -23.064 -18.538 42.199  1.00 27.59  ? 289  ALA C C   1 
ATOM   2502 O  O   . ALA C  1 40  ? -23.921 -18.741 43.071  1.00 26.77  ? 289  ALA C O   1 
ATOM   2503 C  CB  . ALA C  1 40  ? -22.736 -16.751 40.519  1.00 28.07  ? 289  ALA C CB  1 
ATOM   2504 N  N   . GLN C  1 41  ? -21.744 -18.666 42.382  1.00 27.93  ? 290  GLN C N   1 
ATOM   2505 C  CA  . GLN C  1 41  ? -21.171 -19.137 43.606  1.00 28.20  ? 290  GLN C CA  1 
ATOM   2506 C  C   . GLN C  1 41  ? -19.959 -18.293 44.033  1.00 26.90  ? 290  GLN C C   1 
ATOM   2507 O  O   . GLN C  1 41  ? -19.144 -17.904 43.190  1.00 22.81  ? 290  GLN C O   1 
ATOM   2508 C  CB  . GLN C  1 41  ? -20.720 -20.544 43.352  1.00 29.64  ? 290  GLN C CB  1 
ATOM   2509 C  CG  . GLN C  1 41  ? -20.249 -21.285 44.572  1.00 32.18  ? 290  GLN C CG  1 
ATOM   2510 C  CD  . GLN C  1 41  ? -19.959 -22.732 44.226  1.00 36.13  ? 290  GLN C CD  1 
ATOM   2511 O  OE1 . GLN C  1 41  ? -19.125 -23.030 43.328  1.00 38.61  ? 290  GLN C OE1 1 
ATOM   2512 N  NE2 . GLN C  1 41  ? -20.663 -23.636 44.892  1.00 30.74  ? 290  GLN C NE2 1 
ATOM   2513 N  N   . LEU C  1 42  ? -19.854 -18.029 45.334  1.00 22.86  ? 291  LEU C N   1 
ATOM   2514 C  CA  . LEU C  1 42  ? -18.697 -17.305 45.899  1.00 22.46  ? 291  LEU C CA  1 
ATOM   2515 C  C   . LEU C  1 42  ? -17.446 -18.070 45.468  1.00 20.88  ? 291  LEU C C   1 
ATOM   2516 O  O   . LEU C  1 42  ? -17.352 -19.296 45.599  1.00 18.96  ? 291  LEU C O   1 
ATOM   2517 C  CB  . LEU C  1 42  ? -18.810 -17.147 47.409  1.00 22.35  ? 291  LEU C CB  1 
ATOM   2518 C  CG  . LEU C  1 42  ? -17.685 -16.300 48.012  1.00 23.67  ? 291  LEU C CG  1 
ATOM   2519 C  CD1 . LEU C  1 42  ? -17.846 -14.853 47.612  1.00 22.78  ? 291  LEU C CD1 1 
ATOM   2520 C  CD2 . LEU C  1 42  ? -17.695 -16.456 49.520  1.00 22.74  ? 291  LEU C CD2 1 
ATOM   2521 N  N   . VAL C  1 43  ? -16.565 -17.355 44.800  1.00 20.75  ? 292  VAL C N   1 
ATOM   2522 C  CA  . VAL C  1 43  ? -15.615 -17.967 43.911  1.00 21.57  ? 292  VAL C CA  1 
ATOM   2523 C  C   . VAL C  1 43  ? -14.777 -19.145 44.469  1.00 24.39  ? 292  VAL C C   1 
ATOM   2524 O  O   . VAL C  1 43  ? -14.096 -19.047 45.506  1.00 23.59  ? 292  VAL C O   1 
ATOM   2525 C  CB  . VAL C  1 43  ? -14.757 -16.910 43.200  1.00 22.22  ? 292  VAL C CB  1 
ATOM   2526 C  CG1 . VAL C  1 43  ? -13.944 -16.096 44.172  1.00 22.41  ? 292  VAL C CG1 1 
ATOM   2527 C  CG2 . VAL C  1 43  ? -13.886 -17.577 42.115  1.00 22.08  ? 292  VAL C CG2 1 
ATOM   2528 N  N   . VAL C  1 44  ? -14.848 -20.245 43.724  1.00 24.27  ? 293  VAL C N   1 
ATOM   2529 C  CA  . VAL C  1 44  ? -14.068 -21.427 43.975  1.00 26.70  ? 293  VAL C CA  1 
ATOM   2530 C  C   . VAL C  1 44  ? -12.967 -21.529 42.933  1.00 26.08  ? 293  VAL C C   1 
ATOM   2531 O  O   . VAL C  1 44  ? -13.247 -21.525 41.755  1.00 26.01  ? 293  VAL C O   1 
ATOM   2532 C  CB  . VAL C  1 44  ? -14.956 -22.675 43.917  1.00 26.74  ? 293  VAL C CB  1 
ATOM   2533 C  CG1 . VAL C  1 44  ? -14.129 -23.946 44.102  1.00 28.20  ? 293  VAL C CG1 1 
ATOM   2534 C  CG2 . VAL C  1 44  ? -16.040 -22.603 44.996  1.00 28.37  ? 293  VAL C CG2 1 
ATOM   2535 N  N   . ILE C  1 45  ? -11.723 -21.645 43.376  1.00 25.81  ? 294  ILE C N   1 
ATOM   2536 C  CA  . ILE C  1 45  ? -10.564 -21.596 42.478  1.00 26.46  ? 294  ILE C CA  1 
ATOM   2537 C  C   . ILE C  1 45  ? -10.133 -23.040 42.115  1.00 28.25  ? 294  ILE C C   1 
ATOM   2538 O  O   . ILE C  1 45  ? -10.037 -23.914 42.986  1.00 28.14  ? 294  ILE C O   1 
ATOM   2539 C  CB  . ILE C  1 45  ? -9.389  -20.828 43.126  1.00 27.60  ? 294  ILE C CB  1 
ATOM   2540 C  CG1 . ILE C  1 45  ? -9.903  -19.471 43.672  1.00 28.48  ? 294  ILE C CG1 1 
ATOM   2541 C  CG2 . ILE C  1 45  ? -8.274  -20.583 42.115  1.00 27.19  ? 294  ILE C CG2 1 
ATOM   2542 C  CD1 . ILE C  1 45  ? -8.834  -18.621 44.313  1.00 27.76  ? 294  ILE C CD1 1 
ATOM   2543 N  N   . LYS C  1 46  ? -9.916  -23.270 40.812  1.00 29.51  ? 295  LYS C N   1 
ATOM   2544 C  CA  . LYS C  1 46  ? -9.578  -24.596 40.264  1.00 29.56  ? 295  LYS C CA  1 
ATOM   2545 C  C   . LYS C  1 46  ? -8.202  -24.676 39.601  1.00 33.28  ? 295  LYS C C   1 
ATOM   2546 O  O   . LYS C  1 46  ? -7.692  -25.777 39.410  1.00 37.13  ? 295  LYS C O   1 
ATOM   2547 C  CB  . LYS C  1 46  ? -10.591 -24.997 39.226  1.00 29.52  ? 295  LYS C CB  1 
ATOM   2548 C  CG  . LYS C  1 46  ? -12.015 -25.122 39.707  1.00 31.36  ? 295  LYS C CG  1 
ATOM   2549 C  CD  . LYS C  1 46  ? -12.238 -26.295 40.633  1.00 30.82  ? 295  LYS C CD  1 
ATOM   2550 C  CE  . LYS C  1 46  ? -13.737 -26.437 40.932  1.00 30.28  ? 295  LYS C CE  1 
ATOM   2551 N  NZ  . LYS C  1 46  ? -13.965 -27.013 42.264  1.00 30.80  ? 295  LYS C NZ  1 
ATOM   2552 N  N   . SER C  1 47  ? -7.630  -23.534 39.207  1.00 29.81  ? 296  SER C N   1 
ATOM   2553 C  CA  . SER C  1 47  ? -6.297  -23.519 38.647  1.00 31.60  ? 296  SER C CA  1 
ATOM   2554 C  C   . SER C  1 47  ? -5.463  -22.312 39.043  1.00 30.30  ? 296  SER C C   1 
ATOM   2555 O  O   . SER C  1 47  ? -5.934  -21.270 39.583  1.00 26.38  ? 296  SER C O   1 
ATOM   2556 C  CB  . SER C  1 47  ? -6.368  -23.587 37.112  1.00 31.91  ? 296  SER C CB  1 
ATOM   2557 O  OG  . SER C  1 47  ? -6.962  -22.417 36.582  1.00 29.87  ? 296  SER C OG  1 
ATOM   2558 N  N   . ALA C  1 48  ? -4.186  -22.496 38.787  1.00 32.19  ? 297  ALA C N   1 
ATOM   2559 C  CA  . ALA C  1 48  ? -3.182  -21.510 39.077  1.00 33.54  ? 297  ALA C CA  1 
ATOM   2560 C  C   . ALA C  1 48  ? -3.460  -20.196 38.319  1.00 34.95  ? 297  ALA C C   1 
ATOM   2561 O  O   . ALA C  1 48  ? -3.427  -19.101 38.932  1.00 36.91  ? 297  ALA C O   1 
ATOM   2562 C  CB  . ALA C  1 48  ? -1.812  -22.067 38.720  1.00 35.37  ? 297  ALA C CB  1 
ATOM   2563 N  N   . GLU C  1 49  ? -3.760  -20.315 37.016  1.00 33.67  ? 298  GLU C N   1 
ATOM   2564 C  CA  A GLU C  1 49  ? -4.056  -19.172 36.155  0.70 35.01  ? 298  GLU C CA  1 
ATOM   2565 C  CA  B GLU C  1 49  ? -4.035  -19.134 36.186  0.30 33.10  ? 298  GLU C CA  1 
ATOM   2566 C  C   . GLU C  1 49  ? -5.284  -18.402 36.669  1.00 32.37  ? 298  GLU C C   1 
ATOM   2567 O  O   . GLU C  1 49  ? -5.360  -17.209 36.548  1.00 27.39  ? 298  GLU C O   1 
ATOM   2568 C  CB  A GLU C  1 49  ? -4.371  -19.623 34.720  0.70 35.45  ? 298  GLU C CB  1 
ATOM   2569 C  CB  B GLU C  1 49  ? -4.231  -19.479 34.703  0.30 32.67  ? 298  GLU C CB  1 
ATOM   2570 C  CG  A GLU C  1 49  ? -3.270  -20.340 33.945  0.70 40.32  ? 298  GLU C CG  1 
ATOM   2571 C  CG  B GLU C  1 49  ? -2.974  -19.832 33.928  0.30 34.11  ? 298  GLU C CG  1 
ATOM   2572 C  CD  A GLU C  1 49  ? -2.988  -21.781 34.406  0.70 40.49  ? 298  GLU C CD  1 
ATOM   2573 C  CD  B GLU C  1 49  ? -2.107  -18.646 33.564  0.30 34.17  ? 298  GLU C CD  1 
ATOM   2574 O  OE1 A GLU C  1 49  ? -3.901  -22.494 34.870  0.70 36.51  ? 298  GLU C OE1 1 
ATOM   2575 O  OE1 B GLU C  1 49  ? -2.314  -17.537 34.105  0.30 35.42  ? 298  GLU C OE1 1 
ATOM   2576 O  OE2 A GLU C  1 49  ? -1.810  -22.194 34.312  0.70 42.47  ? 298  GLU C OE2 1 
ATOM   2577 O  OE2 B GLU C  1 49  ? -1.195  -18.844 32.729  0.30 35.92  ? 298  GLU C OE2 1 
ATOM   2578 N  N   . GLU C  1 50  ? -6.278  -19.138 37.156  1.00 31.11  ? 299  GLU C N   1 
ATOM   2579 C  CA  . GLU C  1 50  ? -7.469  -18.524 37.713  1.00 31.36  ? 299  GLU C CA  1 
ATOM   2580 C  C   . GLU C  1 50  ? -7.087  -17.807 39.005  1.00 31.66  ? 299  GLU C C   1 
ATOM   2581 O  O   . GLU C  1 50  ? -7.528  -16.706 39.223  1.00 30.97  ? 299  GLU C O   1 
ATOM   2582 C  CB  . GLU C  1 50  ? -8.537  -19.559 38.011  1.00 31.77  ? 299  GLU C CB  1 
ATOM   2583 C  CG  . GLU C  1 50  ? -9.961  -19.030 38.177  1.00 32.14  ? 299  GLU C CG  1 
ATOM   2584 C  CD  . GLU C  1 50  ? -10.920 -20.061 38.766  1.00 32.16  ? 299  GLU C CD  1 
ATOM   2585 O  OE1 . GLU C  1 50  ? -12.068 -19.685 39.093  1.00 33.45  ? 299  GLU C OE1 1 
ATOM   2586 O  OE2 . GLU C  1 50  ? -10.557 -21.252 38.909  1.00 31.79  ? 299  GLU C OE2 1 
ATOM   2587 N  N   . GLN C  1 51  ? -6.283  -18.459 39.855  1.00 30.37  ? 300  GLN C N   1 
ATOM   2588 C  CA  . GLN C  1 51  ? -5.713  -17.837 41.056  1.00 26.59  ? 300  GLN C CA  1 
ATOM   2589 C  C   . GLN C  1 51  ? -5.007  -16.559 40.708  1.00 25.93  ? 300  GLN C C   1 
ATOM   2590 O  O   . GLN C  1 51  ? -5.191  -15.568 41.401  1.00 22.16  ? 300  GLN C O   1 
ATOM   2591 C  CB  . GLN C  1 51  ? -4.762  -18.790 41.794  1.00 24.95  ? 300  GLN C CB  1 
ATOM   2592 C  CG  . GLN C  1 51  ? -3.707  -18.160 42.700  1.00 24.83  ? 300  GLN C CG  1 
ATOM   2593 C  CD  . GLN C  1 51  ? -4.271  -17.249 43.802  1.00 27.61  ? 300  GLN C CD  1 
ATOM   2594 O  OE1 . GLN C  1 51  ? -5.455  -17.330 44.176  1.00 28.43  ? 300  GLN C OE1 1 
ATOM   2595 N  NE2 . GLN C  1 51  ? -3.434  -16.322 44.273  1.00 25.01  ? 300  GLN C NE2 1 
ATOM   2596 N  N   . ASN C  1 52  ? -4.210  -16.578 39.638  1.00 23.71  ? 301  ASN C N   1 
ATOM   2597 C  CA  . ASN C  1 52  ? -3.475  -15.374 39.219  1.00 25.47  ? 301  ASN C CA  1 
ATOM   2598 C  C   . ASN C  1 52  ? -4.401  -14.247 38.749  1.00 23.96  ? 301  ASN C C   1 
ATOM   2599 O  O   . ASN C  1 52  ? -4.149  -13.106 38.994  1.00 25.97  ? 301  ASN C O   1 
ATOM   2600 C  CB  . ASN C  1 52  ? -2.423  -15.684 38.112  1.00 27.88  ? 301  ASN C CB  1 
ATOM   2601 C  CG  . ASN C  1 52  ? -1.278  -16.575 38.605  1.00 32.46  ? 301  ASN C CG  1 
ATOM   2602 O  OD1 . ASN C  1 52  ? -1.088  -16.815 39.809  1.00 34.45  ? 301  ASN C OD1 1 
ATOM   2603 N  ND2 . ASN C  1 52  ? -0.516  -17.094 37.651  1.00 36.91  ? 301  ASN C ND2 1 
ATOM   2604 N  N   . PHE C  1 53  ? -5.441  -14.567 38.015  1.00 25.16  ? 302  PHE C N   1 
ATOM   2605 C  CA  . PHE C  1 53  ? -6.358  -13.574 37.564  1.00 25.50  ? 302  PHE C CA  1 
ATOM   2606 C  C   . PHE C  1 53  ? -7.107  -12.939 38.757  1.00 25.93  ? 302  PHE C C   1 
ATOM   2607 O  O   . PHE C  1 53  ? -7.290  -11.704 38.833  1.00 25.49  ? 302  PHE C O   1 
ATOM   2608 C  CB  . PHE C  1 53  ? -7.314  -14.272 36.607  1.00 27.92  ? 302  PHE C CB  1 
ATOM   2609 C  CG  . PHE C  1 53  ? -8.569  -13.528 36.344  1.00 28.49  ? 302  PHE C CG  1 
ATOM   2610 C  CD1 . PHE C  1 53  ? -8.554  -12.367 35.593  1.00 31.47  ? 302  PHE C CD1 1 
ATOM   2611 C  CD2 . PHE C  1 53  ? -9.764  -14.012 36.813  1.00 30.84  ? 302  PHE C CD2 1 
ATOM   2612 C  CE1 . PHE C  1 53  ? -9.715  -11.693 35.319  1.00 29.80  ? 302  PHE C CE1 1 
ATOM   2613 C  CE2 . PHE C  1 53  ? -10.940 -13.341 36.538  1.00 32.07  ? 302  PHE C CE2 1 
ATOM   2614 C  CZ  . PHE C  1 53  ? -10.902 -12.175 35.819  1.00 32.58  ? 302  PHE C CZ  1 
ATOM   2615 N  N   . LEU C  1 54  ? -7.548  -13.787 39.672  1.00 22.13  ? 303  LEU C N   1 
ATOM   2616 C  CA  . LEU C  1 54  ? -8.294  -13.339 40.837  1.00 23.53  ? 303  LEU C CA  1 
ATOM   2617 C  C   . LEU C  1 54  ? -7.477  -12.520 41.847  1.00 25.63  ? 303  LEU C C   1 
ATOM   2618 O  O   . LEU C  1 54  ? -7.919  -11.444 42.296  1.00 24.52  ? 303  LEU C O   1 
ATOM   2619 C  CB  . LEU C  1 54  ? -8.918  -14.549 41.522  1.00 23.34  ? 303  LEU C CB  1 
ATOM   2620 C  CG  . LEU C  1 54  ? -9.907  -15.353 40.696  1.00 22.21  ? 303  LEU C CG  1 
ATOM   2621 C  CD1 . LEU C  1 54  ? -10.220 -16.612 41.456  1.00 24.78  ? 303  LEU C CD1 1 
ATOM   2622 C  CD2 . LEU C  1 54  ? -11.171 -14.551 40.397  1.00 23.66  ? 303  LEU C CD2 1 
ATOM   2623 N  N   . GLN C  1 55  ? -6.278  -13.014 42.176  1.00 24.95  ? 304  GLN C N   1 
ATOM   2624 C  CA  . GLN C  1 55  ? -5.383  -12.333 43.087  1.00 24.37  ? 304  GLN C CA  1 
ATOM   2625 C  C   . GLN C  1 55  ? -5.073  -10.923 42.608  1.00 27.55  ? 304  GLN C C   1 
ATOM   2626 O  O   . GLN C  1 55  ? -4.992  -9.966  43.421  1.00 27.66  ? 304  GLN C O   1 
ATOM   2627 C  CB  . GLN C  1 55  ? -4.080  -13.140 43.260  1.00 25.04  ? 304  GLN C CB  1 
ATOM   2628 C  CG  . GLN C  1 55  ? -3.160  -12.707 44.403  1.00 22.44  ? 304  GLN C CG  1 
ATOM   2629 C  CD  . GLN C  1 55  ? -3.795  -12.950 45.732  1.00 23.68  ? 304  GLN C CD  1 
ATOM   2630 O  OE1 . GLN C  1 55  ? -4.136  -14.121 46.060  1.00 23.33  ? 304  GLN C OE1 1 
ATOM   2631 N  NE2 . GLN C  1 55  ? -3.980  -11.867 46.526  1.00 21.12  ? 304  GLN C NE2 1 
ATOM   2632 N  N   . LEU C  1 56  ? -4.896  -10.793 41.297  1.00 27.17  ? 305  LEU C N   1 
ATOM   2633 C  CA  . LEU C  1 56  ? -4.578  -9.533  40.695  1.00 28.17  ? 305  LEU C CA  1 
ATOM   2634 C  C   . LEU C  1 56  ? -5.665  -8.488  40.952  1.00 27.71  ? 305  LEU C C   1 
ATOM   2635 O  O   . LEU C  1 56  ? -5.355  -7.338  41.100  1.00 31.43  ? 305  LEU C O   1 
ATOM   2636 C  CB  . LEU C  1 56  ? -4.364  -9.696  39.174  1.00 29.89  ? 305  LEU C CB  1 
ATOM   2637 C  CG  . LEU C  1 56  ? -4.012  -8.382  38.480  1.00 33.98  ? 305  LEU C CG  1 
ATOM   2638 C  CD1 . LEU C  1 56  ? -2.561  -7.981  38.757  1.00 33.34  ? 305  LEU C CD1 1 
ATOM   2639 C  CD2 . LEU C  1 56  ? -4.294  -8.434  36.981  1.00 36.97  ? 305  LEU C CD2 1 
ATOM   2640 N  N   . GLN C  1 57  ? -6.933  -8.883  40.993  1.00 27.26  ? 306  GLN C N   1 
ATOM   2641 C  CA  . GLN C  1 57  ? -8.006  -7.907  41.172  1.00 29.74  ? 306  GLN C CA  1 
ATOM   2642 C  C   . GLN C  1 57  ? -7.825  -7.251  42.523  1.00 29.66  ? 306  GLN C C   1 
ATOM   2643 O  O   . GLN C  1 57  ? -8.025  -6.048  42.650  1.00 35.50  ? 306  GLN C O   1 
ATOM   2644 C  CB  . GLN C  1 57  ? -9.416  -8.523  41.076  1.00 28.84  ? 306  GLN C CB  1 
ATOM   2645 C  CG  . GLN C  1 57  ? -9.628  -9.480  39.925  1.00 30.00  ? 306  GLN C CG  1 
ATOM   2646 C  CD  . GLN C  1 57  ? -9.328  -8.855  38.584  1.00 32.36  ? 306  GLN C CD  1 
ATOM   2647 O  OE1 . GLN C  1 57  ? -9.880  -7.823  38.256  1.00 35.66  ? 306  GLN C OE1 1 
ATOM   2648 N  NE2 . GLN C  1 57  ? -8.462  -9.479  37.806  1.00 33.29  ? 306  GLN C NE2 1 
ATOM   2649 N  N   . SER C  1 58  ? -7.386  -8.016  43.515  1.00 27.26  ? 307  SER C N   1 
ATOM   2650 C  CA  . SER C  1 58  ? -7.156  -7.448  44.833  1.00 28.02  ? 307  SER C CA  1 
ATOM   2651 C  C   . SER C  1 58  ? -5.776  -6.807  45.021  1.00 28.51  ? 307  SER C C   1 
ATOM   2652 O  O   . SER C  1 58  ? -5.661  -5.799  45.733  1.00 28.71  ? 307  SER C O   1 
ATOM   2653 C  CB  . SER C  1 58  ? -7.397  -8.524  45.919  1.00 29.58  ? 307  SER C CB  1 
ATOM   2654 O  OG  . SER C  1 58  ? -8.767  -8.922  45.871  1.00 29.91  ? 307  SER C OG  1 
ATOM   2655 N  N   . SER C  1 59  ? -4.730  -7.383  44.444  1.00 27.07  ? 308  SER C N   1 
ATOM   2656 C  CA  . SER C  1 59  ? -3.387  -6.879  44.726  1.00 32.94  ? 308  SER C CA  1 
ATOM   2657 C  C   . SER C  1 59  ? -3.237  -5.484  44.100  1.00 32.71  ? 308  SER C C   1 
ATOM   2658 O  O   . SER C  1 59  ? -2.652  -4.584  44.695  1.00 37.89  ? 308  SER C O   1 
ATOM   2659 C  CB  . SER C  1 59  ? -2.290  -7.793  44.184  1.00 31.34  ? 308  SER C CB  1 
ATOM   2660 O  OG  . SER C  1 59  ? -2.408  -7.904  42.784  1.00 35.40  ? 308  SER C OG  1 
ATOM   2661 N  N   . ARG C  1 60  ? -3.787  -5.346  42.915  1.00 31.21  ? 309  ARG C N   1 
ATOM   2662 C  CA  . ARG C  1 60  ? -3.747  -4.110  42.157  1.00 37.26  ? 309  ARG C CA  1 
ATOM   2663 C  C   . ARG C  1 60  ? -4.688  -3.041  42.718  1.00 36.32  ? 309  ARG C C   1 
ATOM   2664 O  O   . ARG C  1 60  ? -4.359  -1.878  42.712  1.00 33.15  ? 309  ARG C O   1 
ATOM   2665 C  CB  . ARG C  1 60  ? -4.153  -4.426  40.746  1.00 39.48  ? 309  ARG C CB  1 
ATOM   2666 C  CG  . ARG C  1 60  ? -4.123  -3.280  39.784  1.00 44.71  ? 309  ARG C CG  1 
ATOM   2667 C  CD  . ARG C  1 60  ? -4.467  -3.817  38.402  1.00 49.17  ? 309  ARG C CD  1 
ATOM   2668 N  NE  . ARG C  1 60  ? -5.820  -4.375  38.345  1.00 51.20  ? 309  ARG C NE  1 
ATOM   2669 C  CZ  . ARG C  1 60  ? -6.305  -5.096  37.339  1.00 54.57  ? 309  ARG C CZ  1 
ATOM   2670 N  NH1 . ARG C  1 60  ? -5.552  -5.368  36.266  1.00 55.05  ? 309  ARG C NH1 1 
ATOM   2671 N  NH2 . ARG C  1 60  ? -7.559  -5.547  37.403  1.00 55.87  ? 309  ARG C NH2 1 
ATOM   2672 N  N   . SER C  1 61  ? -5.869  -3.447  43.172  1.00 34.57  ? 310  SER C N   1 
ATOM   2673 C  CA  . SER C  1 61  ? -6.806  -2.515  43.759  1.00 33.77  ? 310  SER C CA  1 
ATOM   2674 C  C   . SER C  1 61  ? -6.498  -2.164  45.221  1.00 34.75  ? 310  SER C C   1 
ATOM   2675 O  O   . SER C  1 61  ? -7.070  -1.215  45.755  1.00 33.43  ? 310  SER C O   1 
ATOM   2676 C  CB  . SER C  1 61  ? -8.221  -3.080  43.647  1.00 32.87  ? 310  SER C CB  1 
ATOM   2677 O  OG  . SER C  1 61  ? -8.376  -4.172  44.521  1.00 30.14  ? 310  SER C OG  1 
ATOM   2678 N  N   . ASN C  1 62  ? -5.605  -2.925  45.861  1.00 34.63  ? 311  ASN C N   1 
ATOM   2679 C  CA  . ASN C  1 62  ? -5.348  -2.810  47.306  1.00 35.96  ? 311  ASN C CA  1 
ATOM   2680 C  C   . ASN C  1 62  ? -6.580  -3.101  48.200  1.00 34.32  ? 311  ASN C C   1 
ATOM   2681 O  O   . ASN C  1 62  ? -6.613  -2.665  49.369  1.00 36.80  ? 311  ASN C O   1 
ATOM   2682 C  CB  . ASN C  1 62  ? -4.784  -1.416  47.645  1.00 36.07  ? 311  ASN C CB  1 
ATOM   2683 C  CG  . ASN C  1 62  ? -3.605  -1.063  46.787  1.00 41.05  ? 311  ASN C CG  1 
ATOM   2684 O  OD1 . ASN C  1 62  ? -2.558  -1.709  46.890  1.00 43.89  ? 311  ASN C OD1 1 
ATOM   2685 N  ND2 . ASN C  1 62  ? -3.770  -0.057  45.890  1.00 36.58  ? 311  ASN C ND2 1 
ATOM   2686 N  N   . ARG C  1 63  ? -7.563  -3.812  47.651  1.00 29.38  ? 312  ARG C N   1 
ATOM   2687 C  CA  . ARG C  1 63  ? -8.820  -4.142  48.306  1.00 29.77  ? 312  ARG C CA  1 
ATOM   2688 C  C   . ARG C  1 63  ? -8.819  -5.593  48.833  1.00 28.78  ? 312  ARG C C   1 
ATOM   2689 O  O   . ARG C  1 63  ? -8.152  -6.425  48.262  1.00 30.09  ? 312  ARG C O   1 
ATOM   2690 C  CB  . ARG C  1 63  ? -9.940  -4.076  47.265  1.00 31.82  ? 312  ARG C CB  1 
ATOM   2691 C  CG  . ARG C  1 63  ? -10.050 -2.759  46.540  1.00 36.46  ? 312  ARG C CG  1 
ATOM   2692 C  CD  . ARG C  1 63  ? -10.932 -1.766  47.233  1.00 36.51  ? 312  ARG C CD  1 
ATOM   2693 N  NE  . ARG C  1 63  ? -10.964 -0.424  46.599  1.00 36.17  ? 312  ARG C NE  1 
ATOM   2694 C  CZ  . ARG C  1 63  ? -11.099 0.710   47.294  1.00 35.94  ? 312  ARG C CZ  1 
ATOM   2695 N  NH1 . ARG C  1 63  ? -11.155 1.894   46.655  1.00 34.67  ? 312  ARG C NH1 1 
ATOM   2696 N  NH2 . ARG C  1 63  ? -11.170 0.660   48.649  1.00 32.29  ? 312  ARG C NH2 1 
ATOM   2697 N  N   . PHE C  1 64  ? -9.631  -5.884  49.848  1.00 24.24  ? 313  PHE C N   1 
ATOM   2698 C  CA  . PHE C  1 64  ? -9.714  -7.184  50.467  1.00 23.49  ? 313  PHE C CA  1 
ATOM   2699 C  C   . PHE C  1 64  ? -10.987 -7.833  49.980  1.00 24.76  ? 313  PHE C C   1 
ATOM   2700 O  O   . PHE C  1 64  ? -12.073 -7.224  50.014  1.00 20.00  ? 313  PHE C O   1 
ATOM   2701 C  CB  . PHE C  1 64  ? -9.772  -7.053  51.981  1.00 27.42  ? 313  PHE C CB  1 
ATOM   2702 C  CG  . PHE C  1 64  ? -8.566  -6.390  52.594  1.00 27.78  ? 313  PHE C CG  1 
ATOM   2703 C  CD1 . PHE C  1 64  ? -7.278  -6.724  52.201  1.00 28.13  ? 313  PHE C CD1 1 
ATOM   2704 C  CD2 . PHE C  1 64  ? -8.725  -5.465  53.625  1.00 26.26  ? 313  PHE C CD2 1 
ATOM   2705 C  CE1 . PHE C  1 64  ? -6.165  -6.092  52.797  1.00 28.30  ? 313  PHE C CE1 1 
ATOM   2706 C  CE2 . PHE C  1 64  ? -7.631  -4.904  54.255  1.00 27.28  ? 313  PHE C CE2 1 
ATOM   2707 C  CZ  . PHE C  1 64  ? -6.353  -5.197  53.833  1.00 26.89  ? 313  PHE C CZ  1 
ATOM   2708 N  N   . THR C  1 65  ? -10.849 -9.068  49.497  1.00 23.92  ? 314  THR C N   1 
ATOM   2709 C  CA  . THR C  1 65  ? -11.911 -9.714  48.783  1.00 23.59  ? 314  THR C CA  1 
ATOM   2710 C  C   . THR C  1 65  ? -12.131 -11.182 49.220  1.00 23.36  ? 314  THR C C   1 
ATOM   2711 O  O   . THR C  1 65  ? -11.200 -11.997 49.280  1.00 20.54  ? 314  THR C O   1 
ATOM   2712 C  CB  . THR C  1 65  ? -11.583 -9.660  47.257  1.00 24.88  ? 314  THR C CB  1 
ATOM   2713 O  OG1 . THR C  1 65  ? -11.315 -8.290  46.853  1.00 25.34  ? 314  THR C OG1 1 
ATOM   2714 C  CG2 . THR C  1 65  ? -12.724 -10.163 46.487  1.00 22.35  ? 314  THR C CG2 1 
ATOM   2715 N  N   . TRP C  1 66  ? -13.377 -11.564 49.442  1.00 23.92  ? 315  TRP C N   1 
ATOM   2716 C  CA  . TRP C  1 66  ? -13.624 -12.935 49.897  1.00 24.85  ? 315  TRP C CA  1 
ATOM   2717 C  C   . TRP C  1 66  ? -13.577 -13.914 48.730  1.00 24.57  ? 315  TRP C C   1 
ATOM   2718 O  O   . TRP C  1 66  ? -13.930 -13.557 47.613  1.00 22.34  ? 315  TRP C O   1 
ATOM   2719 C  CB  . TRP C  1 66  ? -15.003 -13.124 50.503  1.00 25.76  ? 315  TRP C CB  1 
ATOM   2720 C  CG  . TRP C  1 66  ? -15.345 -12.436 51.799  1.00 24.55  ? 315  TRP C CG  1 
ATOM   2721 C  CD1 . TRP C  1 66  ? -16.395 -11.578 52.009  1.00 26.08  ? 315  TRP C CD1 1 
ATOM   2722 C  CD2 . TRP C  1 66  ? -14.729 -12.617 53.062  1.00 25.28  ? 315  TRP C CD2 1 
ATOM   2723 N  NE1 . TRP C  1 66  ? -16.473 -11.221 53.319  1.00 23.58  ? 315  TRP C NE1 1 
ATOM   2724 C  CE2 . TRP C  1 66  ? -15.440 -11.833 53.986  1.00 24.25  ? 315  TRP C CE2 1 
ATOM   2725 C  CE3 . TRP C  1 66  ? -13.648 -13.371 53.506  1.00 24.07  ? 315  TRP C CE3 1 
ATOM   2726 C  CZ2 . TRP C  1 66  ? -15.103 -11.789 55.298  1.00 24.40  ? 315  TRP C CZ2 1 
ATOM   2727 C  CZ3 . TRP C  1 66  ? -13.307 -13.312 54.792  1.00 28.34  ? 315  TRP C CZ3 1 
ATOM   2728 C  CH2 . TRP C  1 66  ? -14.024 -12.537 55.701  1.00 25.87  ? 315  TRP C CH2 1 
ATOM   2729 N  N   . MET C  1 67  ? -13.222 -15.162 49.045  1.00 22.33  ? 316  MET C N   1 
ATOM   2730 C  CA  . MET C  1 67  ? -13.363 -16.262 48.119  1.00 23.43  ? 316  MET C CA  1 
ATOM   2731 C  C   . MET C  1 67  ? -14.220 -17.293 48.849  1.00 21.92  ? 316  MET C C   1 
ATOM   2732 O  O   . MET C  1 67  ? -14.435 -17.139 50.073  1.00 20.78  ? 316  MET C O   1 
ATOM   2733 C  CB  . MET C  1 67  ? -12.001 -16.776 47.715  1.00 23.80  ? 316  MET C CB  1 
ATOM   2734 C  CG  . MET C  1 67  ? -11.246 -17.426 48.827  1.00 26.58  ? 316  MET C CG  1 
ATOM   2735 S  SD  . MET C  1 67  ? -9.617  -18.025 48.373  1.00 26.92  ? 316  MET C SD  1 
ATOM   2736 C  CE  . MET C  1 67  ? -8.662  -16.510 48.478  1.00 27.93  ? 316  MET C CE  1 
ATOM   2737 N  N   . GLY C  1 68  ? -14.731 -18.291 48.115  1.00 21.35  ? 317  GLY C N   1 
ATOM   2738 C  CA  . GLY C  1 68  ? -15.592 -19.351 48.685  1.00 22.95  ? 317  GLY C CA  1 
ATOM   2739 C  C   . GLY C  1 68  ? -14.788 -20.496 49.339  1.00 23.17  ? 317  GLY C C   1 
ATOM   2740 O  O   . GLY C  1 68  ? -14.860 -21.665 48.882  1.00 27.26  ? 317  GLY C O   1 
ATOM   2741 N  N   . LEU C  1 69  ? -13.969 -20.141 50.333  1.00 23.74  ? 318  LEU C N   1 
ATOM   2742 C  CA  . LEU C  1 69  ? -13.063 -21.057 51.052  1.00 24.37  ? 318  LEU C CA  1 
ATOM   2743 C  C   . LEU C  1 69  ? -13.146 -20.744 52.535  1.00 24.82  ? 318  LEU C C   1 
ATOM   2744 O  O   . LEU C  1 69  ? -12.984 -19.604 52.907  1.00 27.13  ? 318  LEU C O   1 
ATOM   2745 C  CB  . LEU C  1 69  ? -11.661 -20.843 50.584  1.00 25.39  ? 318  LEU C CB  1 
ATOM   2746 C  CG  . LEU C  1 69  ? -10.571 -21.736 51.167  1.00 25.68  ? 318  LEU C CG  1 
ATOM   2747 C  CD1 . LEU C  1 69  ? -10.720 -23.187 50.778  1.00 26.29  ? 318  LEU C CD1 1 
ATOM   2748 C  CD2 . LEU C  1 69  ? -9.217  -21.232 50.734  1.00 26.55  ? 318  LEU C CD2 1 
ATOM   2749 N  N   . SER C  1 70  ? -13.451 -21.754 53.352  1.00 23.61  ? 319  SER C N   1 
ATOM   2750 C  CA  . SER C  1 70  ? -13.536 -21.634 54.772  1.00 26.21  ? 319  SER C CA  1 
ATOM   2751 C  C   . SER C  1 70  ? -13.031 -22.891 55.526  1.00 28.54  ? 319  SER C C   1 
ATOM   2752 O  O   . SER C  1 70  ? -12.872 -23.987 54.940  1.00 29.57  ? 319  SER C O   1 
ATOM   2753 C  CB  . SER C  1 70  ? -14.967 -21.355 55.170  1.00 26.63  ? 319  SER C CB  1 
ATOM   2754 O  OG  . SER C  1 70  ? -15.675 -22.570 55.212  1.00 28.31  ? 319  SER C OG  1 
ATOM   2755 N  N   . ASP C  1 71  ? -12.756 -22.723 56.823  1.00 28.11  ? 320  ASP C N   1 
ATOM   2756 C  CA  . ASP C  1 71  ? -12.512 -23.864 57.747  1.00 27.60  ? 320  ASP C CA  1 
ATOM   2757 C  C   . ASP C  1 71  ? -13.456 -23.796 58.922  1.00 30.71  ? 320  ASP C C   1 
ATOM   2758 O  O   . ASP C  1 71  ? -13.110 -24.209 60.039  1.00 28.79  ? 320  ASP C O   1 
ATOM   2759 C  CB  . ASP C  1 71  ? -11.063 -23.956 58.222  1.00 27.68  ? 320  ASP C CB  1 
ATOM   2760 C  CG  . ASP C  1 71  ? -10.653 -22.864 59.288  1.00 29.41  ? 320  ASP C CG  1 
ATOM   2761 O  OD1 . ASP C  1 71  ? -11.376 -21.844 59.514  1.00 29.73  ? 320  ASP C OD1 1 
ATOM   2762 O  OD2 . ASP C  1 71  ? -9.541  -23.023 59.885  1.00 27.72  ? 320  ASP C OD2 1 
ATOM   2763 N  N   . LEU C  1 72  ? -14.640 -23.257 58.658  1.00 28.09  ? 321  LEU C N   1 
ATOM   2764 C  CA  . LEU C  1 72  ? -15.726 -23.229 59.620  1.00 29.60  ? 321  LEU C CA  1 
ATOM   2765 C  C   . LEU C  1 72  ? -16.134 -24.593 60.140  1.00 32.58  ? 321  LEU C C   1 
ATOM   2766 O  O   . LEU C  1 72  ? -16.485 -24.711 61.316  1.00 34.65  ? 321  LEU C O   1 
ATOM   2767 C  CB  . LEU C  1 72  ? -16.992 -22.625 58.982  1.00 29.76  ? 321  LEU C CB  1 
ATOM   2768 C  CG  . LEU C  1 72  ? -16.967 -21.093 58.822  1.00 31.85  ? 321  LEU C CG  1 
ATOM   2769 C  CD1 . LEU C  1 72  ? -17.996 -20.610 57.798  1.00 31.56  ? 321  LEU C CD1 1 
ATOM   2770 C  CD2 . LEU C  1 72  ? -17.165 -20.466 60.188  1.00 32.45  ? 321  LEU C CD2 1 
ATOM   2771 N  N   . ASN C  1 73  ? -16.155 -25.601 59.267  1.00 33.20  ? 322  ASN C N   1 
ATOM   2772 C  CA  A ASN C  1 73  ? -16.649 -26.910 59.661  0.70 37.44  ? 322  ASN C CA  1 
ATOM   2773 C  CA  B ASN C  1 73  ? -16.647 -26.929 59.641  0.30 34.98  ? 322  ASN C CA  1 
ATOM   2774 C  C   . ASN C  1 73  ? -15.636 -27.661 60.498  1.00 37.55  ? 322  ASN C C   1 
ATOM   2775 O  O   . ASN C  1 73  ? -15.993 -28.265 61.501  1.00 37.91  ? 322  ASN C O   1 
ATOM   2776 C  CB  A ASN C  1 73  ? -17.019 -27.721 58.442  0.70 41.34  ? 322  ASN C CB  1 
ATOM   2777 C  CB  B ASN C  1 73  ? -16.952 -27.796 58.423  0.30 35.28  ? 322  ASN C CB  1 
ATOM   2778 C  CG  A ASN C  1 73  ? -18.262 -27.207 57.775  0.70 41.78  ? 322  ASN C CG  1 
ATOM   2779 C  CG  B ASN C  1 73  ? -17.313 -29.225 58.814  0.30 34.37  ? 322  ASN C CG  1 
ATOM   2780 O  OD1 A ASN C  1 73  ? -19.087 -26.530 58.404  0.70 45.68  ? 322  ASN C OD1 1 
ATOM   2781 O  OD1 B ASN C  1 73  ? -18.111 -29.434 59.725  0.30 33.66  ? 322  ASN C OD1 1 
ATOM   2782 N  ND2 A ASN C  1 73  ? -18.406 -27.512 56.495  0.70 42.59  ? 322  ASN C ND2 1 
ATOM   2783 N  ND2 B ASN C  1 73  ? -16.708 -30.208 58.144  0.30 32.12  ? 322  ASN C ND2 1 
ATOM   2784 N  N   . GLN C  1 74  ? -14.379 -27.601 60.088  1.00 34.32  ? 323  GLN C N   1 
ATOM   2785 C  CA  . GLN C  1 74  ? -13.329 -28.313 60.785  1.00 34.45  ? 323  GLN C CA  1 
ATOM   2786 C  C   . GLN C  1 74  ? -12.094 -27.412 60.846  1.00 32.09  ? 323  GLN C C   1 
ATOM   2787 O  O   . GLN C  1 74  ? -11.347 -27.235 59.836  1.00 32.08  ? 323  GLN C O   1 
ATOM   2788 C  CB  . GLN C  1 74  ? -13.037 -29.621 60.059  1.00 31.93  ? 323  GLN C CB  1 
ATOM   2789 C  CG  . GLN C  1 74  ? -11.846 -30.392 60.601  1.00 34.69  ? 323  GLN C CG  1 
ATOM   2790 C  CD  . GLN C  1 74  ? -12.168 -31.144 61.882  1.00 40.35  ? 323  GLN C CD  1 
ATOM   2791 O  OE1 . GLN C  1 74  ? -13.337 -31.362 62.217  1.00 46.47  ? 323  GLN C OE1 1 
ATOM   2792 N  NE2 . GLN C  1 74  ? -11.126 -31.562 62.600  1.00 42.33  ? 323  GLN C NE2 1 
ATOM   2793 N  N   . GLU C  1 75  ? -11.895 -26.841 62.020  1.00 30.19  ? 324  GLU C N   1 
ATOM   2794 C  CA  . GLU C  1 75  ? -10.814 -25.912 62.255  1.00 31.42  ? 324  GLU C CA  1 
ATOM   2795 C  C   . GLU C  1 75  ? -9.534  -26.458 61.696  1.00 30.28  ? 324  GLU C C   1 
ATOM   2796 O  O   . GLU C  1 75  ? -9.182  -27.578 61.991  1.00 31.06  ? 324  GLU C O   1 
ATOM   2797 C  CB  . GLU C  1 75  ? -10.658 -25.558 63.748  1.00 31.52  ? 324  GLU C CB  1 
ATOM   2798 C  CG  . GLU C  1 75  ? -9.465  -24.629 64.052  1.00 30.70  ? 324  GLU C CG  1 
ATOM   2799 C  CD  . GLU C  1 75  ? -9.477  -23.340 63.214  1.00 30.84  ? 324  GLU C CD  1 
ATOM   2800 O  OE1 . GLU C  1 75  ? -10.576 -22.758 62.974  1.00 29.82  ? 324  GLU C OE1 1 
ATOM   2801 O  OE2 . GLU C  1 75  ? -8.378  -22.916 62.803  1.00 29.47  ? 324  GLU C OE2 1 
ATOM   2802 N  N   . GLY C  1 76  ? -8.894  -25.694 60.806  1.00 30.15  ? 325  GLY C N   1 
ATOM   2803 C  CA  . GLY C  1 76  ? -7.605  -26.090 60.197  1.00 29.79  ? 325  GLY C CA  1 
ATOM   2804 C  C   . GLY C  1 76  ? -7.728  -26.858 58.899  1.00 32.45  ? 325  GLY C C   1 
ATOM   2805 O  O   . GLY C  1 76  ? -6.712  -27.061 58.178  1.00 32.02  ? 325  GLY C O   1 
ATOM   2806 N  N   . THR C  1 77  ? -8.966  -27.276 58.568  1.00 31.50  ? 326  THR C N   1 
ATOM   2807 C  CA  . THR C  1 77  ? -9.219  -27.896 57.283  1.00 28.06  ? 326  THR C CA  1 
ATOM   2808 C  C   . THR C  1 77  ? -10.045 -26.990 56.346  1.00 29.69  ? 326  THR C C   1 
ATOM   2809 O  O   . THR C  1 77  ? -11.250 -26.792 56.571  1.00 26.60  ? 326  THR C O   1 
ATOM   2810 C  CB  . THR C  1 77  ? -9.844  -29.294 57.440  1.00 29.84  ? 326  THR C CB  1 
ATOM   2811 O  OG1 . THR C  1 77  ? -8.867  -30.146 58.044  1.00 32.83  ? 326  THR C OG1 1 
ATOM   2812 C  CG2 . THR C  1 77  ? -10.200 -29.881 56.080  1.00 27.69  ? 326  THR C CG2 1 
ATOM   2813 N  N   . TRP C  1 78  ? -9.386  -26.504 55.270  1.00 27.46  ? 327  TRP C N   1 
ATOM   2814 C  CA  . TRP C  1 78  ? -10.009 -25.571 54.338  1.00 29.87  ? 327  TRP C CA  1 
ATOM   2815 C  C   . TRP C  1 78  ? -10.763 -26.261 53.220  1.00 28.64  ? 327  TRP C C   1 
ATOM   2816 O  O   . TRP C  1 78  ? -10.262 -27.148 52.517  1.00 30.61  ? 327  TRP C O   1 
ATOM   2817 C  CB  . TRP C  1 78  ? -8.993  -24.568 53.813  1.00 29.99  ? 327  TRP C CB  1 
ATOM   2818 C  CG  . TRP C  1 78  ? -8.522  -23.741 54.926  1.00 31.85  ? 327  TRP C CG  1 
ATOM   2819 C  CD1 . TRP C  1 78  ? -7.531  -24.056 55.825  1.00 32.21  ? 327  TRP C CD1 1 
ATOM   2820 C  CD2 . TRP C  1 78  ? -9.062  -22.485 55.345  1.00 30.53  ? 327  TRP C CD2 1 
ATOM   2821 N  NE1 . TRP C  1 78  ? -7.413  -23.061 56.759  1.00 29.73  ? 327  TRP C NE1 1 
ATOM   2822 C  CE2 . TRP C  1 78  ? -8.329  -22.083 56.490  1.00 30.08  ? 327  TRP C CE2 1 
ATOM   2823 C  CE3 . TRP C  1 78  ? -10.087 -21.649 54.859  1.00 28.52  ? 327  TRP C CE3 1 
ATOM   2824 C  CZ2 . TRP C  1 78  ? -8.578  -20.882 57.157  1.00 28.98  ? 327  TRP C CZ2 1 
ATOM   2825 C  CZ3 . TRP C  1 78  ? -10.323 -20.438 55.517  1.00 30.47  ? 327  TRP C CZ3 1 
ATOM   2826 C  CH2 . TRP C  1 78  ? -9.573  -20.076 56.666  1.00 31.34  ? 327  TRP C CH2 1 
ATOM   2827 N  N   . GLN C  1 79  ? -11.985 -25.806 53.055  1.00 29.24  ? 328  GLN C N   1 
ATOM   2828 C  CA  . GLN C  1 79  ? -12.936 -26.392 52.146  1.00 29.88  ? 328  GLN C CA  1 
ATOM   2829 C  C   . GLN C  1 79  ? -13.577 -25.330 51.292  1.00 26.63  ? 328  GLN C C   1 
ATOM   2830 O  O   . GLN C  1 79  ? -14.053 -24.323 51.791  1.00 26.36  ? 328  GLN C O   1 
ATOM   2831 C  CB  . GLN C  1 79  ? -14.028 -27.089 52.949  1.00 36.09  ? 328  GLN C CB  1 
ATOM   2832 C  CG  . GLN C  1 79  ? -14.887 -28.005 52.099  1.00 43.50  ? 328  GLN C CG  1 
ATOM   2833 C  CD  . GLN C  1 79  ? -15.733 -28.977 52.928  1.00 50.91  ? 328  GLN C CD  1 
ATOM   2834 O  OE1 . GLN C  1 79  ? -16.043 -30.078 52.467  1.00 57.48  ? 328  GLN C OE1 1 
ATOM   2835 N  NE2 . GLN C  1 79  ? -16.107 -28.576 54.148  1.00 56.30  ? 328  GLN C NE2 1 
ATOM   2836 N  N   . TRP C  1 80  ? -13.626 -25.583 49.988  1.00 26.72  ? 329  TRP C N   1 
ATOM   2837 C  CA  . TRP C  1 80  ? -14.296 -24.715 49.067  1.00 24.07  ? 329  TRP C CA  1 
ATOM   2838 C  C   . TRP C  1 80  ? -15.771 -24.938 49.257  1.00 24.23  ? 329  TRP C C   1 
ATOM   2839 O  O   . TRP C  1 80  ? -16.177 -26.009 49.701  1.00 24.39  ? 329  TRP C O   1 
ATOM   2840 C  CB  . TRP C  1 80  ? -13.889 -25.010 47.628  1.00 25.15  ? 329  TRP C CB  1 
ATOM   2841 C  CG  . TRP C  1 80  ? -12.462 -24.770 47.311  1.00 23.63  ? 329  TRP C CG  1 
ATOM   2842 C  CD1 . TRP C  1 80  ? -11.514 -25.691 47.210  1.00 24.31  ? 329  TRP C CD1 1 
ATOM   2843 C  CD2 . TRP C  1 80  ? -11.817 -23.494 47.084  1.00 24.81  ? 329  TRP C CD2 1 
ATOM   2844 N  NE1 . TRP C  1 80  ? -10.297 -25.108 46.910  1.00 25.80  ? 329  TRP C NE1 1 
ATOM   2845 C  CE2 . TRP C  1 80  ? -10.465 -23.754 46.824  1.00 23.28  ? 329  TRP C CE2 1 
ATOM   2846 C  CE3 . TRP C  1 80  ? -12.256 -22.162 47.107  1.00 25.19  ? 329  TRP C CE3 1 
ATOM   2847 C  CZ2 . TRP C  1 80  ? -9.542  -22.747 46.579  1.00 23.64  ? 329  TRP C CZ2 1 
ATOM   2848 C  CZ3 . TRP C  1 80  ? -11.327 -21.150 46.861  1.00 23.77  ? 329  TRP C CZ3 1 
ATOM   2849 C  CH2 . TRP C  1 80  ? -9.995  -21.448 46.600  1.00 23.95  ? 329  TRP C CH2 1 
ATOM   2850 N  N   . VAL C  1 81  ? -16.574 -23.935 48.920  1.00 25.07  ? 330  VAL C N   1 
ATOM   2851 C  CA  . VAL C  1 81  ? -18.039 -23.982 49.115  1.00 26.78  ? 330  VAL C CA  1 
ATOM   2852 C  C   . VAL C  1 81  ? -18.734 -24.978 48.217  1.00 28.03  ? 330  VAL C C   1 
ATOM   2853 O  O   . VAL C  1 81  ? -19.860 -25.331 48.488  1.00 27.67  ? 330  VAL C O   1 
ATOM   2854 C  CB  . VAL C  1 81  ? -18.742 -22.590 48.937  1.00 28.02  ? 330  VAL C CB  1 
ATOM   2855 C  CG1 . VAL C  1 81  ? -18.348 -21.669 50.062  1.00 28.29  ? 330  VAL C CG1 1 
ATOM   2856 C  CG2 . VAL C  1 81  ? -18.375 -21.896 47.647  1.00 28.64  ? 330  VAL C CG2 1 
ATOM   2857 N  N   . ASP C  1 82  ? -18.087 -25.391 47.121  1.00 29.12  ? 331  ASP C N   1 
ATOM   2858 C  CA  . ASP C  1 82  ? -18.645 -26.428 46.280  1.00 29.82  ? 331  ASP C CA  1 
ATOM   2859 C  C   . ASP C  1 82  ? -18.334 -27.800 46.853  1.00 32.29  ? 331  ASP C C   1 
ATOM   2860 O  O   . ASP C  1 82  ? -18.602 -28.790 46.190  1.00 34.16  ? 331  ASP C O   1 
ATOM   2861 C  CB  . ASP C  1 82  ? -18.108 -26.369 44.837  1.00 28.81  ? 331  ASP C CB  1 
ATOM   2862 C  CG  . ASP C  1 82  ? -16.671 -26.743 44.753  1.00 29.06  ? 331  ASP C CG  1 
ATOM   2863 O  OD1 . ASP C  1 82  ? -16.068 -26.898 45.818  1.00 30.05  ? 331  ASP C OD1 1 
ATOM   2864 O  OD2 . ASP C  1 82  ? -16.108 -26.851 43.649  1.00 34.76  ? 331  ASP C OD2 1 
ATOM   2865 N  N   . GLY C  1 83  ? -17.711 -27.867 48.020  1.00 30.41  ? 332  GLY C N   1 
ATOM   2866 C  CA  . GLY C  1 83  ? -17.430 -29.157 48.675  1.00 35.00  ? 332  GLY C CA  1 
ATOM   2867 C  C   . GLY C  1 83  ? -16.004 -29.693 48.444  1.00 35.09  ? 332  GLY C C   1 
ATOM   2868 O  O   . GLY C  1 83  ? -15.544 -30.584 49.156  1.00 37.93  ? 332  GLY C O   1 
ATOM   2869 N  N   . SER C  1 84  ? -15.301 -29.135 47.465  1.00 31.43  ? 333  SER C N   1 
ATOM   2870 C  CA  . SER C  1 84  ? -14.024 -29.662 47.055  1.00 31.48  ? 333  SER C CA  1 
ATOM   2871 C  C   . SER C  1 84  ? -13.013 -29.237 48.104  1.00 32.91  ? 333  SER C C   1 
ATOM   2872 O  O   . SER C  1 84  ? -13.227 -28.246 48.821  1.00 33.00  ? 333  SER C O   1 
ATOM   2873 C  CB  . SER C  1 84  ? -13.629 -29.165 45.641  1.00 32.27  ? 333  SER C CB  1 
ATOM   2874 O  OG  . SER C  1 84  ? -13.560 -27.743 45.582  1.00 36.38  ? 333  SER C OG  1 
ATOM   2875 N  N   . PRO C  1 85  ? -11.919 -29.992 48.209  1.00 33.63  ? 334  PRO C N   1 
ATOM   2876 C  CA  . PRO C  1 85  ? -10.908 -29.784 49.224  1.00 32.01  ? 334  PRO C CA  1 
ATOM   2877 C  C   . PRO C  1 85  ? -9.885  -28.781 48.763  1.00 33.49  ? 334  PRO C C   1 
ATOM   2878 O  O   . PRO C  1 85  ? -9.677  -28.640 47.568  1.00 33.32  ? 334  PRO C O   1 
ATOM   2879 C  CB  . PRO C  1 85  ? -10.252 -31.175 49.332  1.00 34.12  ? 334  PRO C CB  1 
ATOM   2880 C  CG  . PRO C  1 85  ? -10.376 -31.762 47.953  1.00 33.29  ? 334  PRO C CG  1 
ATOM   2881 C  CD  . PRO C  1 85  ? -11.676 -31.232 47.423  1.00 34.73  ? 334  PRO C CD  1 
ATOM   2882 N  N   . LEU C  1 86  ? -9.222  -28.107 49.695  1.00 34.10  ? 335  LEU C N   1 
ATOM   2883 C  CA  . LEU C  1 86  ? -8.097  -27.303 49.313  1.00 33.04  ? 335  LEU C CA  1 
ATOM   2884 C  C   . LEU C  1 86  ? -6.917  -28.225 49.058  1.00 36.36  ? 335  LEU C C   1 
ATOM   2885 O  O   . LEU C  1 86  ? -6.380  -28.822 49.993  1.00 38.42  ? 335  LEU C O   1 
ATOM   2886 C  CB  . LEU C  1 86  ? -7.741  -26.309 50.398  1.00 34.14  ? 335  LEU C CB  1 
ATOM   2887 C  CG  . LEU C  1 86  ? -6.539  -25.406 50.035  1.00 33.91  ? 335  LEU C CG  1 
ATOM   2888 C  CD1 . LEU C  1 86  ? -6.811  -24.475 48.849  1.00 31.59  ? 335  LEU C CD1 1 
ATOM   2889 C  CD2 . LEU C  1 86  ? -6.191  -24.605 51.272  1.00 33.61  ? 335  LEU C CD2 1 
ATOM   2890 N  N   . LEU C  1 87  ? -6.476  -28.290 47.808  1.00 35.66  ? 336  LEU C N   1 
ATOM   2891 C  CA  . LEU C  1 87  ? -5.397  -29.185 47.405  1.00 33.63  ? 336  LEU C CA  1 
ATOM   2892 C  C   . LEU C  1 87  ? -4.049  -28.688 47.922  1.00 35.03  ? 336  LEU C C   1 
ATOM   2893 O  O   . LEU C  1 87  ? -3.841  -27.470 48.055  1.00 36.26  ? 336  LEU C O   1 
ATOM   2894 C  CB  . LEU C  1 87  ? -5.355  -29.340 45.882  1.00 33.24  ? 336  LEU C CB  1 
ATOM   2895 C  CG  . LEU C  1 87  ? -6.598  -29.996 45.250  1.00 37.38  ? 336  LEU C CG  1 
ATOM   2896 C  CD1 . LEU C  1 87  ? -6.496  -29.945 43.723  1.00 38.30  ? 336  LEU C CD1 1 
ATOM   2897 C  CD2 . LEU C  1 87  ? -6.805  -31.430 45.699  1.00 36.97  ? 336  LEU C CD2 1 
ATOM   2898 N  N   . PRO C  1 88  ? -3.115  -29.620 48.200  1.00 35.94  ? 337  PRO C N   1 
ATOM   2899 C  CA  . PRO C  1 88  ? -1.790  -29.227 48.713  1.00 37.73  ? 337  PRO C CA  1 
ATOM   2900 C  C   . PRO C  1 88  ? -1.037  -28.222 47.845  1.00 34.22  ? 337  PRO C C   1 
ATOM   2901 O  O   . PRO C  1 88  ? -0.326  -27.381 48.383  1.00 33.04  ? 337  PRO C O   1 
ATOM   2902 C  CB  . PRO C  1 88  ? -1.024  -30.563 48.771  1.00 40.37  ? 337  PRO C CB  1 
ATOM   2903 C  CG  . PRO C  1 88  ? -2.110  -31.603 48.968  1.00 39.13  ? 337  PRO C CG  1 
ATOM   2904 C  CD  . PRO C  1 88  ? -3.248  -31.092 48.120  1.00 39.53  ? 337  PRO C CD  1 
ATOM   2905 N  N   . SER C  1 89  ? -1.209  -28.302 46.528  1.00 34.87  ? 338  SER C N   1 
ATOM   2906 C  CA  . SER C  1 89  ? -0.563  -27.381 45.570  1.00 36.72  ? 338  SER C CA  1 
ATOM   2907 C  C   . SER C  1 89  ? -1.050  -25.927 45.623  1.00 36.27  ? 338  SER C C   1 
ATOM   2908 O  O   . SER C  1 89  ? -0.473  -25.070 44.938  1.00 35.37  ? 338  SER C O   1 
ATOM   2909 C  CB  . SER C  1 89  ? -0.824  -27.882 44.154  1.00 38.58  ? 338  SER C CB  1 
ATOM   2910 O  OG  . SER C  1 89  ? -2.225  -28.065 43.999  1.00 41.56  ? 338  SER C OG  1 
ATOM   2911 N  N   . PHE C  1 90  ? -2.141  -25.685 46.368  1.00 34.54  ? 339  PHE C N   1 
ATOM   2912 C  CA  . PHE C  1 90  ? -2.728  -24.340 46.583  1.00 34.79  ? 339  PHE C CA  1 
ATOM   2913 C  C   . PHE C  1 90  ? -2.291  -23.743 47.899  1.00 35.74  ? 339  PHE C C   1 
ATOM   2914 O  O   . PHE C  1 90  ? -2.580  -22.587 48.160  1.00 34.68  ? 339  PHE C O   1 
ATOM   2915 C  CB  . PHE C  1 90  ? -4.272  -24.381 46.522  1.00 34.41  ? 339  PHE C CB  1 
ATOM   2916 C  CG  . PHE C  1 90  ? -4.794  -24.548 45.129  1.00 38.40  ? 339  PHE C CG  1 
ATOM   2917 C  CD1 . PHE C  1 90  ? -4.604  -25.731 44.448  1.00 40.18  ? 339  PHE C CD1 1 
ATOM   2918 C  CD2 . PHE C  1 90  ? -5.400  -23.491 44.458  1.00 43.31  ? 339  PHE C CD2 1 
ATOM   2919 C  CE1 . PHE C  1 90  ? -5.018  -25.883 43.131  1.00 41.33  ? 339  PHE C CE1 1 
ATOM   2920 C  CE2 . PHE C  1 90  ? -5.824  -23.637 43.136  1.00 45.82  ? 339  PHE C CE2 1 
ATOM   2921 C  CZ  . PHE C  1 90  ? -5.628  -24.838 42.469  1.00 40.69  ? 339  PHE C CZ  1 
ATOM   2922 N  N   . LYS C  1 91  ? -1.575  -24.506 48.727  1.00 33.98  ? 340  LYS C N   1 
ATOM   2923 C  CA  . LYS C  1 91  ? -1.211  -24.006 50.041  1.00 35.97  ? 340  LYS C CA  1 
ATOM   2924 C  C   . LYS C  1 91  ? -0.156  -22.905 50.005  1.00 32.50  ? 340  LYS C C   1 
ATOM   2925 O  O   . LYS C  1 91  ? -0.111  -22.040 50.874  1.00 31.99  ? 340  LYS C O   1 
ATOM   2926 C  CB  . LYS C  1 91  ? -0.879  -25.158 50.943  1.00 39.77  ? 340  LYS C CB  1 
ATOM   2927 C  CG  . LYS C  1 91  ? -2.180  -25.808 51.322  1.00 44.24  ? 340  LYS C CG  1 
ATOM   2928 C  CD  . LYS C  1 91  ? -2.061  -27.115 52.077  1.00 47.59  ? 340  LYS C CD  1 
ATOM   2929 C  CE  . LYS C  1 91  ? -3.373  -27.372 52.807  1.00 51.09  ? 340  LYS C CE  1 
ATOM   2930 N  NZ  . LYS C  1 91  ? -3.910  -28.726 52.520  1.00 56.90  ? 340  LYS C NZ  1 
ATOM   2931 N  N   . GLN C  1 92  ? 0.592   -22.885 48.919  1.00 28.65  ? 341  GLN C N   1 
ATOM   2932 C  CA  . GLN C  1 92  ? 1.531   -21.842 48.597  1.00 30.11  ? 341  GLN C CA  1 
ATOM   2933 C  C   . GLN C  1 92  ? 0.924   -20.451 48.434  1.00 29.89  ? 341  GLN C C   1 
ATOM   2934 O  O   . GLN C  1 92  ? 1.639   -19.464 48.489  1.00 28.88  ? 341  GLN C O   1 
ATOM   2935 C  CB  . GLN C  1 92  ? 2.242   -22.189 47.285  1.00 31.98  ? 341  GLN C CB  1 
ATOM   2936 C  CG  . GLN C  1 92  ? 1.350   -22.219 46.062  1.00 32.34  ? 341  GLN C CG  1 
ATOM   2937 C  CD  . GLN C  1 92  ? 2.112   -22.590 44.801  1.00 37.37  ? 341  GLN C CD  1 
ATOM   2938 O  OE1 . GLN C  1 92  ? 2.883   -21.800 44.280  1.00 36.65  ? 341  GLN C OE1 1 
ATOM   2939 N  NE2 . GLN C  1 92  ? 1.862   -23.787 44.280  1.00 37.17  ? 341  GLN C NE2 1 
ATOM   2940 N  N   . TYR C  1 93  ? -0.381  -20.352 48.205  1.00 27.10  ? 342  TYR C N   1 
ATOM   2941 C  CA  . TYR C  1 93  ? -0.944  -19.045 47.932  1.00 29.03  ? 342  TYR C CA  1 
ATOM   2942 C  C   . TYR C  1 93  ? -1.239  -18.257 49.214  1.00 27.26  ? 342  TYR C C   1 
ATOM   2943 O  O   . TYR C  1 93  ? -1.503  -17.059 49.145  1.00 29.50  ? 342  TYR C O   1 
ATOM   2944 C  CB  . TYR C  1 93  ? -2.220  -19.155 47.011  1.00 27.93  ? 342  TYR C CB  1 
ATOM   2945 C  CG  . TYR C  1 93  ? -1.908  -19.697 45.635  1.00 26.40  ? 342  TYR C CG  1 
ATOM   2946 C  CD1 . TYR C  1 93  ? -0.948  -19.116 44.860  1.00 26.60  ? 342  TYR C CD1 1 
ATOM   2947 C  CD2 . TYR C  1 93  ? -2.551  -20.838 45.142  1.00 28.76  ? 342  TYR C CD2 1 
ATOM   2948 C  CE1 . TYR C  1 93  ? -0.628  -19.621 43.618  1.00 28.13  ? 342  TYR C CE1 1 
ATOM   2949 C  CE2 . TYR C  1 93  ? -2.235  -21.353 43.889  1.00 27.47  ? 342  TYR C CE2 1 
ATOM   2950 C  CZ  . TYR C  1 93  ? -1.278  -20.721 43.136  1.00 26.97  ? 342  TYR C CZ  1 
ATOM   2951 O  OH  . TYR C  1 93  ? -0.965  -21.172 41.893  1.00 29.91  ? 342  TYR C OH  1 
ATOM   2952 N  N   . TRP C  1 94  ? -1.238  -18.923 50.358  1.00 29.89  ? 343  TRP C N   1 
ATOM   2953 C  CA  . TRP C  1 94  ? -1.420  -18.246 51.646  1.00 30.48  ? 343  TRP C CA  1 
ATOM   2954 C  C   . TRP C  1 94  ? -0.262  -17.309 51.826  1.00 32.32  ? 343  TRP C C   1 
ATOM   2955 O  O   . TRP C  1 94  ? 0.849   -17.733 51.545  1.00 27.49  ? 343  TRP C O   1 
ATOM   2956 C  CB  . TRP C  1 94  ? -1.343  -19.225 52.810  1.00 28.72  ? 343  TRP C CB  1 
ATOM   2957 C  CG  . TRP C  1 94  ? -2.504  -20.173 52.966  1.00 31.52  ? 343  TRP C CG  1 
ATOM   2958 C  CD1 . TRP C  1 94  ? -2.476  -21.546 52.844  1.00 29.60  ? 343  TRP C CD1 1 
ATOM   2959 C  CD2 . TRP C  1 94  ? -3.842  -19.836 53.344  1.00 29.88  ? 343  TRP C CD2 1 
ATOM   2960 N  NE1 . TRP C  1 94  ? -3.717  -22.073 53.133  1.00 28.33  ? 343  TRP C NE1 1 
ATOM   2961 C  CE2 . TRP C  1 94  ? -4.568  -21.053 53.450  1.00 29.46  ? 343  TRP C CE2 1 
ATOM   2962 C  CE3 . TRP C  1 94  ? -4.494  -18.627 53.649  1.00 27.35  ? 343  TRP C CE3 1 
ATOM   2963 C  CZ2 . TRP C  1 94  ? -5.932  -21.091 53.793  1.00 30.72  ? 343  TRP C CZ2 1 
ATOM   2964 C  CZ3 . TRP C  1 94  ? -5.854  -18.672 53.996  1.00 29.85  ? 343  TRP C CZ3 1 
ATOM   2965 C  CH2 . TRP C  1 94  ? -6.567  -19.901 54.032  1.00 27.62  ? 343  TRP C CH2 1 
ATOM   2966 N  N   . ASN C  1 95  ? -0.519  -16.082 52.296  1.00 29.31  ? 344  ASN C N   1 
ATOM   2967 C  CA  . ASN C  1 95  ? 0.540   -15.155 52.744  1.00 32.16  ? 344  ASN C CA  1 
ATOM   2968 C  C   . ASN C  1 95  ? 1.412   -15.794 53.816  1.00 30.54  ? 344  ASN C C   1 
ATOM   2969 O  O   . ASN C  1 95  ? 0.932   -16.644 54.603  1.00 30.57  ? 344  ASN C O   1 
ATOM   2970 C  CB  . ASN C  1 95  ? -0.066  -13.865 53.360  1.00 32.86  ? 344  ASN C CB  1 
ATOM   2971 C  CG  . ASN C  1 95  ? -0.866  -13.039 52.346  1.00 31.35  ? 344  ASN C CG  1 
ATOM   2972 O  OD1 . ASN C  1 95  ? -0.560  -13.074 51.169  1.00 27.58  ? 344  ASN C OD1 1 
ATOM   2973 N  ND2 . ASN C  1 95  ? -1.929  -12.340 52.804  1.00 27.72  ? 344  ASN C ND2 1 
ATOM   2974 N  N   . ARG C  1 96  ? 2.654   -15.328 53.918  1.00 33.66  ? 345  ARG C N   1 
ATOM   2975 C  CA  . ARG C  1 96  ? 3.578   -15.810 54.975  1.00 35.83  ? 345  ARG C CA  1 
ATOM   2976 C  C   . ARG C  1 96  ? 2.857   -15.787 56.313  1.00 31.43  ? 345  ARG C C   1 
ATOM   2977 O  O   . ARG C  1 96  ? 2.215   -14.817 56.620  1.00 28.78  ? 345  ARG C O   1 
ATOM   2978 C  CB  . ARG C  1 96  ? 4.840   -14.953 55.078  1.00 43.76  ? 345  ARG C CB  1 
ATOM   2979 C  CG  . ARG C  1 96  ? 5.967   -15.648 55.873  1.00 55.08  ? 345  ARG C CG  1 
ATOM   2980 C  CD  . ARG C  1 96  ? 6.743   -14.776 56.888  1.00 62.02  ? 345  ARG C CD  1 
ATOM   2981 N  NE  . ARG C  1 96  ? 5.905   -14.245 57.999  1.00 73.42  ? 345  ARG C NE  1 
ATOM   2982 C  CZ  . ARG C  1 96  ? 5.515   -14.904 59.107  1.00 67.94  ? 345  ARG C CZ  1 
ATOM   2983 N  NH1 . ARG C  1 96  ? 5.863   -16.174 59.347  1.00 68.08  ? 345  ARG C NH1 1 
ATOM   2984 N  NH2 . ARG C  1 96  ? 4.750   -14.280 59.993  1.00 65.10  ? 345  ARG C NH2 1 
ATOM   2985 N  N   . GLY C  1 97  ? 2.897   -16.879 57.065  1.00 27.71  ? 346  GLY C N   1 
ATOM   2986 C  CA  . GLY C  1 97  ? 2.319   -16.918 58.385  1.00 27.21  ? 346  GLY C CA  1 
ATOM   2987 C  C   . GLY C  1 97  ? 0.852   -17.256 58.417  1.00 28.20  ? 346  GLY C C   1 
ATOM   2988 O  O   . GLY C  1 97  ? 0.300   -17.436 59.497  1.00 29.94  ? 346  GLY C O   1 
ATOM   2989 N  N   . GLU C  1 98  ? 0.218   -17.357 57.246  1.00 30.07  ? 347  GLU C N   1 
ATOM   2990 C  CA  . GLU C  1 98  ? -1.191  -17.708 57.176  1.00 30.63  ? 347  GLU C CA  1 
ATOM   2991 C  C   . GLU C  1 98  ? -1.380  -19.167 56.690  1.00 32.46  ? 347  GLU C C   1 
ATOM   2992 O  O   . GLU C  1 98  ? -0.577  -19.640 55.891  1.00 32.56  ? 347  GLU C O   1 
ATOM   2993 C  CB  . GLU C  1 98  ? -1.901  -16.715 56.254  1.00 31.03  ? 347  GLU C CB  1 
ATOM   2994 C  CG  . GLU C  1 98  ? -1.577  -15.216 56.515  1.00 31.97  ? 347  GLU C CG  1 
ATOM   2995 C  CD  . GLU C  1 98  ? -2.092  -14.705 57.860  1.00 33.19  ? 347  GLU C CD  1 
ATOM   2996 O  OE1 . GLU C  1 98  ? -2.847  -15.474 58.527  1.00 33.41  ? 347  GLU C OE1 1 
ATOM   2997 O  OE2 . GLU C  1 98  ? -1.772  -13.520 58.237  1.00 31.34  ? 347  GLU C OE2 1 
ATOM   2998 N  N   . PRO C  1 99  ? -2.460  -19.842 57.084  1.00 29.71  ? 348  PRO C N   1 
ATOM   2999 C  CA  . PRO C  1 99  ? -3.532  -19.240 57.888  1.00 32.11  ? 348  PRO C CA  1 
ATOM   3000 C  C   . PRO C  1 99  ? -3.216  -19.405 59.363  1.00 32.42  ? 348  PRO C C   1 
ATOM   3001 O  O   . PRO C  1 99  ? -2.594  -20.401 59.720  1.00 35.93  ? 348  PRO C O   1 
ATOM   3002 C  CB  . PRO C  1 99  ? -4.769  -20.049 57.498  1.00 30.71  ? 348  PRO C CB  1 
ATOM   3003 C  CG  . PRO C  1 99  ? -4.226  -21.421 57.127  1.00 30.87  ? 348  PRO C CG  1 
ATOM   3004 C  CD  . PRO C  1 99  ? -2.789  -21.227 56.677  1.00 30.76  ? 348  PRO C CD  1 
ATOM   3005 N  N   . ASN C  1 100 ? -3.628  -18.469 60.220  1.00 28.85  ? 349  ASN C N   1 
ATOM   3006 C  CA  . ASN C  1 100 ? -3.156  -18.531 61.611  1.00 30.65  ? 349  ASN C CA  1 
ATOM   3007 C  C   . ASN C  1 100 ? -4.295  -18.561 62.618  1.00 32.72  ? 349  ASN C C   1 
ATOM   3008 O  O   . ASN C  1 100 ? -4.058  -18.717 63.815  1.00 33.07  ? 349  ASN C O   1 
ATOM   3009 C  CB  . ASN C  1 100 ? -2.191  -17.373 61.934  1.00 28.51  ? 349  ASN C CB  1 
ATOM   3010 C  CG  . ASN C  1 100 ? -2.827  -15.999 61.699  1.00 27.80  ? 349  ASN C CG  1 
ATOM   3011 O  OD1 . ASN C  1 100 ? -4.005  -15.915 61.343  1.00 25.42  ? 349  ASN C OD1 1 
ATOM   3012 N  ND2 . ASN C  1 100 ? -2.038  -14.926 61.840  1.00 26.69  ? 349  ASN C ND2 1 
ATOM   3013 N  N   . ASN C  1 101 ? -5.513  -18.357 62.159  1.00 26.80  ? 350  ASN C N   1 
ATOM   3014 C  CA  . ASN C  1 101 ? -6.660  -18.427 63.035  1.00 27.69  ? 350  ASN C CA  1 
ATOM   3015 C  C   . ASN C  1 101 ? -6.600  -17.454 64.191  1.00 28.45  ? 350  ASN C C   1 
ATOM   3016 O  O   . ASN C  1 101 ? -7.180  -17.707 65.236  1.00 27.19  ? 350  ASN C O   1 
ATOM   3017 C  CB  . ASN C  1 101 ? -6.853  -19.828 63.605  1.00 26.57  ? 350  ASN C CB  1 
ATOM   3018 C  CG  . ASN C  1 101 ? -8.264  -20.076 64.020  1.00 26.44  ? 350  ASN C CG  1 
ATOM   3019 O  OD1 . ASN C  1 101 ? -9.230  -19.638 63.354  1.00 28.48  ? 350  ASN C OD1 1 
ATOM   3020 N  ND2 . ASN C  1 101 ? -8.426  -20.811 65.081  1.00 28.69  ? 350  ASN C ND2 1 
ATOM   3021 N  N   . VAL C  1 102 ? -5.918  -16.337 63.990  1.00 28.11  ? 351  VAL C N   1 
ATOM   3022 C  CA  . VAL C  1 102 ? -5.714  -15.435 65.083  1.00 32.27  ? 351  VAL C CA  1 
ATOM   3023 C  C   . VAL C  1 102 ? -7.008  -14.681 65.430  1.00 30.54  ? 351  VAL C C   1 
ATOM   3024 O  O   . VAL C  1 102 ? -7.569  -13.969 64.598  1.00 30.20  ? 351  VAL C O   1 
ATOM   3025 C  CB  . VAL C  1 102 ? -4.512  -14.516 64.833  1.00 32.26  ? 351  VAL C CB  1 
ATOM   3026 C  CG1 . VAL C  1 102 ? -4.783  -13.542 63.705  1.00 33.73  ? 351  VAL C CG1 1 
ATOM   3027 C  CG2 . VAL C  1 102 ? -4.168  -13.793 66.129  1.00 34.15  ? 351  VAL C CG2 1 
ATOM   3028 N  N   . GLY C  1 103 ? -7.498  -14.911 66.646  1.00 32.30  ? 352  GLY C N   1 
ATOM   3029 C  CA  . GLY C  1 103 ? -8.789  -14.386 67.075  1.00 33.54  ? 352  GLY C CA  1 
ATOM   3030 C  C   . GLY C  1 103 ? -9.997  -15.123 66.483  1.00 36.13  ? 352  GLY C C   1 
ATOM   3031 O  O   . GLY C  1 103 ? -11.109 -14.566 66.430  1.00 36.75  ? 352  GLY C O   1 
ATOM   3032 N  N   . GLU C  1 104 ? -9.780  -16.355 66.015  1.00 34.12  ? 353  GLU C N   1 
ATOM   3033 C  CA  . GLU C  1 104 ? -10.806 -17.146 65.276  1.00 34.87  ? 353  GLU C CA  1 
ATOM   3034 C  C   . GLU C  1 104 ? -11.084 -16.603 63.889  1.00 28.92  ? 353  GLU C C   1 
ATOM   3035 O  O   . GLU C  1 104 ? -11.917 -15.727 63.691  1.00 26.00  ? 353  GLU C O   1 
ATOM   3036 C  CB  . GLU C  1 104 ? -12.112 -17.271 66.052  1.00 39.26  ? 353  GLU C CB  1 
ATOM   3037 C  CG  . GLU C  1 104 ? -11.894 -17.762 67.472  1.00 47.91  ? 353  GLU C CG  1 
ATOM   3038 C  CD  . GLU C  1 104 ? -11.867 -19.276 67.598  1.00 59.42  ? 353  GLU C CD  1 
ATOM   3039 O  OE1 . GLU C  1 104 ? -12.695 -19.773 68.392  1.00 70.48  ? 353  GLU C OE1 1 
ATOM   3040 O  OE2 . GLU C  1 104 ? -11.042 -19.966 66.926  1.00 66.69  ? 353  GLU C OE2 1 
ATOM   3041 N  N   . GLU C  1 105 ? -10.365 -17.125 62.915  1.00 28.46  ? 354  GLU C N   1 
ATOM   3042 C  CA  . GLU C  1 105 ? -10.498 -16.649 61.566  1.00 26.36  ? 354  GLU C CA  1 
ATOM   3043 C  C   . GLU C  1 105 ? -10.849 -17.813 60.690  1.00 26.15  ? 354  GLU C C   1 
ATOM   3044 O  O   . GLU C  1 105 ? -10.015 -18.682 60.449  1.00 23.02  ? 354  GLU C O   1 
ATOM   3045 C  CB  . GLU C  1 105 ? -9.185  -16.028 61.108  1.00 27.89  ? 354  GLU C CB  1 
ATOM   3046 C  CG  . GLU C  1 105 ? -8.826  -14.725 61.817  1.00 27.29  ? 354  GLU C CG  1 
ATOM   3047 C  CD  . GLU C  1 105 ? -7.577  -14.048 61.276  1.00 26.88  ? 354  GLU C CD  1 
ATOM   3048 O  OE1 . GLU C  1 105 ? -6.551  -14.753 61.077  1.00 24.84  ? 354  GLU C OE1 1 
ATOM   3049 O  OE2 . GLU C  1 105 ? -7.606  -12.785 61.078  1.00 25.06  ? 354  GLU C OE2 1 
ATOM   3050 N  N   . ASP C  1 106 ? -12.061 -17.830 60.152  1.00 27.71  ? 355  ASP C N   1 
ATOM   3051 C  CA  . ASP C  1 106 ? -12.496 -19.032 59.406  1.00 26.77  ? 355  ASP C CA  1 
ATOM   3052 C  C   . ASP C  1 106 ? -12.822 -18.875 57.915  1.00 27.09  ? 355  ASP C C   1 
ATOM   3053 O  O   . ASP C  1 106 ? -13.169 -19.848 57.280  1.00 27.47  ? 355  ASP C O   1 
ATOM   3054 C  CB  . ASP C  1 106 ? -13.661 -19.699 60.118  1.00 26.00  ? 355  ASP C CB  1 
ATOM   3055 C  CG  . ASP C  1 106 ? -13.301 -20.172 61.513  1.00 26.34  ? 355  ASP C CG  1 
ATOM   3056 O  OD1 . ASP C  1 106 ? -12.095 -20.226 61.831  1.00 28.36  ? 355  ASP C OD1 1 
ATOM   3057 O  OD2 . ASP C  1 106 ? -14.225 -20.489 62.291  1.00 28.30  ? 355  ASP C OD2 1 
ATOM   3058 N  N   . CYS C  1 107 ? -12.659 -17.673 57.375  1.00 25.93  ? 356  CYS C N   1 
ATOM   3059 C  CA  . CYS C  1 107 ? -12.958 -17.366 56.014  1.00 26.39  ? 356  CYS C CA  1 
ATOM   3060 C  C   . CYS C  1 107 ? -11.757 -16.761 55.270  1.00 26.71  ? 356  CYS C C   1 
ATOM   3061 O  O   . CYS C  1 107 ? -11.085 -15.852 55.788  1.00 30.78  ? 356  CYS C O   1 
ATOM   3062 C  CB  . CYS C  1 107 ? -14.138 -16.394 55.997  1.00 26.95  ? 356  CYS C CB  1 
ATOM   3063 S  SG  . CYS C  1 107 ? -15.647 -17.170 56.576  1.00 28.59  ? 356  CYS C SG  1 
ATOM   3064 N  N   . ALA C  1 108 ? -11.527 -17.220 54.040  1.00 25.21  ? 357  ALA C N   1 
ATOM   3065 C  CA  . ALA C  1 108 ? -10.332 -16.857 53.297  1.00 23.22  ? 357  ALA C CA  1 
ATOM   3066 C  C   . ALA C  1 108 ? -10.588 -15.643 52.440  1.00 23.32  ? 357  ALA C C   1 
ATOM   3067 O  O   . ALA C  1 108 ? -11.646 -15.517 51.815  1.00 25.17  ? 357  ALA C O   1 
ATOM   3068 C  CB  . ALA C  1 108 ? -9.853  -18.023 52.439  1.00 22.14  ? 357  ALA C CB  1 
ATOM   3069 N  N   . GLU C  1 109 ? -9.636  -14.725 52.445  1.00 24.84  ? 358  GLU C N   1 
ATOM   3070 C  CA  . GLU C  1 109 ? -9.693  -13.544 51.574  1.00 24.66  ? 358  GLU C CA  1 
ATOM   3071 C  C   . GLU C  1 109 ? -8.468  -13.451 50.711  1.00 23.74  ? 358  GLU C C   1 
ATOM   3072 O  O   . GLU C  1 109 ? -7.428  -14.037 51.044  1.00 27.37  ? 358  GLU C O   1 
ATOM   3073 C  CB  . GLU C  1 109 ? -9.821  -12.269 52.383  1.00 24.90  ? 358  GLU C CB  1 
ATOM   3074 C  CG  . GLU C  1 109 ? -8.637  -12.062 53.338  1.00 29.88  ? 358  GLU C CG  1 
ATOM   3075 C  CD  . GLU C  1 109 ? -8.587  -10.721 54.040  1.00 29.65  ? 358  GLU C CD  1 
ATOM   3076 O  OE1 . GLU C  1 109 ? -7.736  -10.574 54.935  1.00 30.62  ? 358  GLU C OE1 1 
ATOM   3077 O  OE2 . GLU C  1 109 ? -9.327  -9.804  53.638  1.00 34.18  ? 358  GLU C OE2 1 
ATOM   3078 N  N   . PHE C  1 110 ? -8.577  -12.702 49.614  1.00 20.75  ? 359  PHE C N   1 
ATOM   3079 C  CA  . PHE C  1 110 ? -7.402  -12.256 48.903  1.00 22.94  ? 359  PHE C CA  1 
ATOM   3080 C  C   . PHE C  1 110 ? -6.934  -11.007 49.607  1.00 23.78  ? 359  PHE C C   1 
ATOM   3081 O  O   . PHE C  1 110 ? -7.697  -10.070 49.760  1.00 26.83  ? 359  PHE C O   1 
ATOM   3082 C  CB  . PHE C  1 110 ? -7.668  -11.932 47.421  1.00 22.12  ? 359  PHE C CB  1 
ATOM   3083 C  CG  . PHE C  1 110 ? -8.351  -13.024 46.649  1.00 21.90  ? 359  PHE C CG  1 
ATOM   3084 C  CD1 . PHE C  1 110 ? -7.620  -14.015 46.006  1.00 21.98  ? 359  PHE C CD1 1 
ATOM   3085 C  CD2 . PHE C  1 110 ? -9.737  -13.010 46.472  1.00 22.47  ? 359  PHE C CD2 1 
ATOM   3086 C  CE1 . PHE C  1 110 ? -8.245  -14.988 45.264  1.00 22.02  ? 359  PHE C CE1 1 
ATOM   3087 C  CE2 . PHE C  1 110 ? -10.364 -13.999 45.756  1.00 22.78  ? 359  PHE C CE2 1 
ATOM   3088 C  CZ  . PHE C  1 110 ? -9.613  -14.989 45.127  1.00 22.30  ? 359  PHE C CZ  1 
ATOM   3089 N  N   . SER C  1 111 ? -5.678  -11.002 50.035  1.00 25.74  ? 360  SER C N   1 
ATOM   3090 C  CA  . SER C  1 111 ? -5.130  -9.923  50.820  1.00 28.24  ? 360  SER C CA  1 
ATOM   3091 C  C   . SER C  1 111 ? -3.707  -9.616  50.390  1.00 29.49  ? 360  SER C C   1 
ATOM   3092 O  O   . SER C  1 111 ? -2.769  -10.333 50.717  1.00 31.90  ? 360  SER C O   1 
ATOM   3093 C  CB  . SER C  1 111 ? -5.215  -10.282 52.317  1.00 30.95  ? 360  SER C CB  1 
ATOM   3094 O  OG  . SER C  1 111 ? -4.713  -9.251  53.110  1.00 30.83  ? 360  SER C OG  1 
ATOM   3095 N  N   . GLY C  1 112 ? -3.570  -8.552  49.602  1.00 31.74  ? 361  GLY C N   1 
ATOM   3096 C  CA  . GLY C  1 112 ? -2.315  -8.228  48.929  1.00 30.59  ? 361  GLY C CA  1 
ATOM   3097 C  C   . GLY C  1 112 ? -1.957  -9.253  47.861  1.00 29.71  ? 361  GLY C C   1 
ATOM   3098 O  O   . GLY C  1 112 ? -2.669  -9.404  46.866  1.00 33.40  ? 361  GLY C O   1 
ATOM   3099 N  N   . ASN C  1 113 ? -0.838  -9.951  48.054  1.00 29.71  ? 362  ASN C N   1 
ATOM   3100 C  CA  . ASN C  1 113 ? -0.301  -10.853 47.022  1.00 30.66  ? 362  ASN C CA  1 
ATOM   3101 C  C   . ASN C  1 113 ? -0.727  -12.292 47.163  1.00 25.83  ? 362  ASN C C   1 
ATOM   3102 O  O   . ASN C  1 113 ? -0.454  -13.086 46.305  1.00 25.58  ? 362  ASN C O   1 
ATOM   3103 C  CB  . ASN C  1 113 ? 1.235   -10.767 46.975  1.00 33.78  ? 362  ASN C CB  1 
ATOM   3104 C  CG  . ASN C  1 113 ? 1.722   -9.380  46.548  1.00 39.81  ? 362  ASN C CG  1 
ATOM   3105 O  OD1 . ASN C  1 113 ? 2.779   -8.935  46.998  1.00 46.64  ? 362  ASN C OD1 1 
ATOM   3106 N  ND2 . ASN C  1 113 ? 0.931   -8.673  45.716  1.00 36.61  ? 362  ASN C ND2 1 
ATOM   3107 N  N   . GLY C  1 114 ? -1.410  -12.623 48.230  1.00 25.60  ? 363  GLY C N   1 
ATOM   3108 C  CA  . GLY C  1 114 ? -1.844  -13.990 48.470  1.00 27.58  ? 363  GLY C CA  1 
ATOM   3109 C  C   . GLY C  1 114 ? -3.069  -14.024 49.365  1.00 28.97  ? 363  GLY C C   1 
ATOM   3110 O  O   . GLY C  1 114 ? -3.819  -13.027 49.398  1.00 27.45  ? 363  GLY C O   1 
ATOM   3111 N  N   . TRP C  1 115 ? -3.291  -15.156 50.058  1.00 27.53  ? 364  TRP C N   1 
ATOM   3112 C  CA  . TRP C  1 115 ? -4.488  -15.319 50.869  1.00 26.98  ? 364  TRP C CA  1 
ATOM   3113 C  C   . TRP C  1 115 ? -4.263  -15.139 52.334  1.00 27.07  ? 364  TRP C C   1 
ATOM   3114 O  O   . TRP C  1 115 ? -3.177  -15.373 52.847  1.00 29.10  ? 364  TRP C O   1 
ATOM   3115 C  CB  . TRP C  1 115 ? -5.139  -16.676 50.711  1.00 26.80  ? 364  TRP C CB  1 
ATOM   3116 C  CG  . TRP C  1 115 ? -5.286  -17.189 49.318  1.00 28.17  ? 364  TRP C CG  1 
ATOM   3117 C  CD1 . TRP C  1 115 ? -5.230  -16.484 48.157  1.00 27.16  ? 364  TRP C CD1 1 
ATOM   3118 C  CD2 . TRP C  1 115 ? -5.603  -18.520 48.965  1.00 28.90  ? 364  TRP C CD2 1 
ATOM   3119 N  NE1 . TRP C  1 115 ? -5.446  -17.299 47.104  1.00 25.83  ? 364  TRP C NE1 1 
ATOM   3120 C  CE2 . TRP C  1 115 ? -5.691  -18.563 47.563  1.00 27.93  ? 364  TRP C CE2 1 
ATOM   3121 C  CE3 . TRP C  1 115 ? -5.771  -19.709 49.702  1.00 30.54  ? 364  TRP C CE3 1 
ATOM   3122 C  CZ2 . TRP C  1 115 ? -5.954  -19.746 46.862  1.00 28.53  ? 364  TRP C CZ2 1 
ATOM   3123 C  CZ3 . TRP C  1 115 ? -6.047  -20.889 49.010  1.00 32.19  ? 364  TRP C CZ3 1 
ATOM   3124 C  CH2 . TRP C  1 115 ? -6.145  -20.892 47.596  1.00 29.39  ? 364  TRP C CH2 1 
ATOM   3125 N  N   . ASN C  1 116 ? -5.339  -14.775 53.020  1.00 26.37  ? 365  ASN C N   1 
ATOM   3126 C  CA  . ASN C  1 116 ? -5.319  -14.658 54.465  1.00 25.13  ? 365  ASN C CA  1 
ATOM   3127 C  C   . ASN C  1 116 ? -6.611  -15.213 54.989  1.00 25.63  ? 365  ASN C C   1 
ATOM   3128 O  O   . ASN C  1 116 ? -7.654  -15.042 54.339  1.00 27.82  ? 365  ASN C O   1 
ATOM   3129 C  CB  . ASN C  1 116 ? -5.143  -13.182 54.903  1.00 24.62  ? 365  ASN C CB  1 
ATOM   3130 C  CG  . ASN C  1 116 ? -5.198  -13.008 56.425  1.00 23.65  ? 365  ASN C CG  1 
ATOM   3131 O  OD1 . ASN C  1 116 ? -4.524  -13.757 57.190  1.00 21.08  ? 365  ASN C OD1 1 
ATOM   3132 N  ND2 . ASN C  1 116 ? -6.046  -12.054 56.893  1.00 20.67  ? 365  ASN C ND2 1 
ATOM   3133 N  N   . ASP C  1 117 ? -6.570  -15.875 56.145  1.00 25.10  ? 366  ASP C N   1 
ATOM   3134 C  CA  . ASP C  1 117 ? -7.803  -16.109 56.906  1.00 24.66  ? 366  ASP C CA  1 
ATOM   3135 C  C   . ASP C  1 117 ? -8.141  -14.939 57.796  1.00 23.91  ? 366  ASP C C   1 
ATOM   3136 O  O   . ASP C  1 117 ? -7.290  -14.467 58.567  1.00 23.24  ? 366  ASP C O   1 
ATOM   3137 C  CB  . ASP C  1 117 ? -7.768  -17.376 57.766  1.00 25.29  ? 366  ASP C CB  1 
ATOM   3138 C  CG  . ASP C  1 117 ? -6.598  -17.423 58.735  1.00 25.52  ? 366  ASP C CG  1 
ATOM   3139 O  OD1 . ASP C  1 117 ? -5.547  -16.774 58.512  1.00 24.51  ? 366  ASP C OD1 1 
ATOM   3140 O  OD2 . ASP C  1 117 ? -6.734  -18.188 59.692  1.00 30.51  ? 366  ASP C OD2 1 
ATOM   3141 N  N   . ASP C  1 118 ? -9.412  -14.541 57.750  1.00 23.29  ? 367  ASP C N   1 
ATOM   3142 C  CA  . ASP C  1 118 ? -9.914  -13.407 58.507  1.00 23.31  ? 367  ASP C CA  1 
ATOM   3143 C  C   . ASP C  1 118 ? -11.270 -13.747 59.073  1.00 24.66  ? 367  ASP C C   1 
ATOM   3144 O  O   . ASP C  1 118 ? -11.777 -14.841 58.858  1.00 25.53  ? 367  ASP C O   1 
ATOM   3145 C  CB  . ASP C  1 118 ? -9.994  -12.137 57.645  1.00 22.40  ? 367  ASP C CB  1 
ATOM   3146 C  CG  . ASP C  1 118 ? -9.870  -10.835 58.468  1.00 26.18  ? 367  ASP C CG  1 
ATOM   3147 O  OD1 . ASP C  1 118 ? -9.873  -10.891 59.732  1.00 24.18  ? 367  ASP C OD1 1 
ATOM   3148 O  OD2 . ASP C  1 118 ? -9.777  -9.726  57.852  1.00 28.53  ? 367  ASP C OD2 1 
ATOM   3149 N  N   . LYS C  1 119 ? -11.814 -12.825 59.862  1.00 24.79  ? 368  LYS C N   1 
ATOM   3150 C  CA  . LYS C  1 119 ? -13.032 -13.067 60.585  1.00 27.98  ? 368  LYS C CA  1 
ATOM   3151 C  C   . LYS C  1 119 ? -14.195 -12.962 59.609  1.00 27.78  ? 368  LYS C C   1 
ATOM   3152 O  O   . LYS C  1 119 ? -14.318 -11.984 58.831  1.00 27.53  ? 368  LYS C O   1 
ATOM   3153 C  CB  . LYS C  1 119 ? -13.177 -12.109 61.785  1.00 31.10  ? 368  LYS C CB  1 
ATOM   3154 C  CG  . LYS C  1 119 ? -11.936 -12.010 62.652  1.00 35.95  ? 368  LYS C CG  1 
ATOM   3155 C  CD  . LYS C  1 119 ? -12.305 -11.644 64.085  1.00 43.96  ? 368  LYS C CD  1 
ATOM   3156 C  CE  . LYS C  1 119 ? -11.095 -11.180 64.897  1.00 51.46  ? 368  LYS C CE  1 
ATOM   3157 N  NZ  . LYS C  1 119 ? -10.814 -9.731  64.675  1.00 53.89  ? 368  LYS C NZ  1 
ATOM   3158 N  N   . CYS C  1 120 ? -15.044 -13.988 59.651  1.00 26.87  ? 369  CYS C N   1 
ATOM   3159 C  CA  . CYS C  1 120 ? -16.142 -14.164 58.716  1.00 25.73  ? 369  CYS C CA  1 
ATOM   3160 C  C   . CYS C  1 120 ? -17.193 -13.090 58.815  1.00 28.43  ? 369  CYS C C   1 
ATOM   3161 O  O   . CYS C  1 120 ? -17.893 -12.842 57.850  1.00 29.33  ? 369  CYS C O   1 
ATOM   3162 C  CB  . CYS C  1 120 ? -16.815 -15.519 58.927  1.00 29.66  ? 369  CYS C CB  1 
ATOM   3163 S  SG  . CYS C  1 120 ? -15.770 -16.952 58.559  1.00 31.71  ? 369  CYS C SG  1 
ATOM   3164 N  N   . ASN C  1 121 ? -17.327 -12.469 59.980  1.00 28.22  ? 370  ASN C N   1 
ATOM   3165 C  CA  . ASN C  1 121 ? -18.368 -11.466 60.190  1.00 30.23  ? 370  ASN C CA  1 
ATOM   3166 C  C   . ASN C  1 121 ? -17.939 -10.082 59.677  1.00 28.52  ? 370  ASN C C   1 
ATOM   3167 O  O   . ASN C  1 121 ? -18.712 -9.159  59.743  1.00 26.60  ? 370  ASN C O   1 
ATOM   3168 C  CB  . ASN C  1 121 ? -18.814 -11.412 61.668  1.00 31.39  ? 370  ASN C CB  1 
ATOM   3169 C  CG  . ASN C  1 121 ? -17.673 -11.029 62.619  1.00 37.00  ? 370  ASN C CG  1 
ATOM   3170 O  OD1 . ASN C  1 121 ? -16.491 -11.325 62.376  1.00 41.54  ? 370  ASN C OD1 1 
ATOM   3171 N  ND2 . ASN C  1 121 ? -18.023 -10.375 63.713  1.00 44.06  ? 370  ASN C ND2 1 
ATOM   3172 N  N   . LEU C  1 122 ? -16.722 -9.957  59.169  1.00 26.98  ? 371  LEU C N   1 
ATOM   3173 C  CA  . LEU C  1 122 ? -16.301 -8.723  58.576  1.00 26.50  ? 371  LEU C CA  1 
ATOM   3174 C  C   . LEU C  1 122 ? -16.732 -8.536  57.127  1.00 26.17  ? 371  LEU C C   1 
ATOM   3175 O  O   . LEU C  1 122 ? -16.958 -9.493  56.414  1.00 28.68  ? 371  LEU C O   1 
ATOM   3176 C  CB  . LEU C  1 122 ? -14.811 -8.593  58.675  1.00 27.00  ? 371  LEU C CB  1 
ATOM   3177 C  CG  . LEU C  1 122 ? -14.209 -8.502  60.063  1.00 29.44  ? 371  LEU C CG  1 
ATOM   3178 C  CD1 . LEU C  1 122 ? -12.679 -8.458  59.966  1.00 29.70  ? 371  LEU C CD1 1 
ATOM   3179 C  CD2 . LEU C  1 122 ? -14.779 -7.371  60.927  1.00 28.84  ? 371  LEU C CD2 1 
ATOM   3180 N  N   . ALA C  1 123 ? -16.829 -7.273  56.701  1.00 25.89  ? 372  ALA C N   1 
ATOM   3181 C  CA  . ALA C  1 123 ? -17.321 -6.902  55.393  1.00 25.42  ? 372  ALA C CA  1 
ATOM   3182 C  C   . ALA C  1 123 ? -16.135 -6.691  54.433  1.00 26.03  ? 372  ALA C C   1 
ATOM   3183 O  O   . ALA C  1 123 ? -15.197 -5.959  54.720  1.00 29.13  ? 372  ALA C O   1 
ATOM   3184 C  CB  . ALA C  1 123 ? -18.176 -5.647  55.484  1.00 25.11  ? 372  ALA C CB  1 
ATOM   3185 N  N   . LYS C  1 124 ? -16.188 -7.359  53.297  1.00 25.36  ? 373  LYS C N   1 
ATOM   3186 C  CA  . LYS C  1 124 ? -15.153 -7.262  52.291  1.00 23.34  ? 373  LYS C CA  1 
ATOM   3187 C  C   . LYS C  1 124 ? -15.822 -7.279  50.960  1.00 23.06  ? 373  LYS C C   1 
ATOM   3188 O  O   . LYS C  1 124 ? -17.011 -7.592  50.823  1.00 25.76  ? 373  LYS C O   1 
ATOM   3189 C  CB  . LYS C  1 124 ? -14.158 -8.424  52.399  1.00 24.74  ? 373  LYS C CB  1 
ATOM   3190 C  CG  . LYS C  1 124 ? -13.574 -8.640  53.793  1.00 25.78  ? 373  LYS C CG  1 
ATOM   3191 C  CD  . LYS C  1 124 ? -12.627 -9.813  53.780  1.00 27.18  ? 373  LYS C CD  1 
ATOM   3192 C  CE  . LYS C  1 124 ? -11.928 -10.032 55.097  1.00 28.48  ? 373  LYS C CE  1 
ATOM   3193 N  NZ  . LYS C  1 124 ? -11.020 -8.932  55.526  1.00 29.34  ? 373  LYS C NZ  1 
ATOM   3194 N  N   . PHE C  1 125 ? -15.055 -6.962  49.936  1.00 20.54  ? 374  PHE C N   1 
ATOM   3195 C  CA  . PHE C  1 125 ? -15.517 -7.183  48.606  1.00 20.62  ? 374  PHE C CA  1 
ATOM   3196 C  C   . PHE C  1 125 ? -15.749 -8.687  48.343  1.00 19.71  ? 374  PHE C C   1 
ATOM   3197 O  O   . PHE C  1 125 ? -15.225 -9.477  49.044  1.00 21.44  ? 374  PHE C O   1 
ATOM   3198 C  CB  . PHE C  1 125 ? -14.527 -6.531  47.611  1.00 20.07  ? 374  PHE C CB  1 
ATOM   3199 C  CG  . PHE C  1 125 ? -14.566 -5.031  47.694  1.00 21.01  ? 374  PHE C CG  1 
ATOM   3200 C  CD1 . PHE C  1 125 ? -13.752 -4.348  48.596  1.00 22.55  ? 374  PHE C CD1 1 
ATOM   3201 C  CD2 . PHE C  1 125 ? -15.493 -4.323  46.984  1.00 20.48  ? 374  PHE C CD2 1 
ATOM   3202 C  CE1 . PHE C  1 125 ? -13.831 -2.959  48.715  1.00 22.70  ? 374  PHE C CE1 1 
ATOM   3203 C  CE2 . PHE C  1 125 ? -15.587 -2.965  47.106  1.00 22.68  ? 374  PHE C CE2 1 
ATOM   3204 C  CZ  . PHE C  1 125 ? -14.766 -2.289  47.983  1.00 21.85  ? 374  PHE C CZ  1 
ATOM   3205 N  N   . TRP C  1 126 ? -16.501 -9.048  47.301  1.00 22.72  ? 375  TRP C N   1 
ATOM   3206 C  CA  . TRP C  1 126 ? -16.676 -10.445 46.919  1.00 22.96  ? 375  TRP C CA  1 
ATOM   3207 C  C   . TRP C  1 126 ? -16.629 -10.671 45.401  1.00 22.00  ? 375  TRP C C   1 
ATOM   3208 O  O   . TRP C  1 126 ? -16.759 -9.755  44.599  1.00 23.34  ? 375  TRP C O   1 
ATOM   3209 C  CB  . TRP C  1 126 ? -17.902 -11.073 47.558  1.00 22.87  ? 375  TRP C CB  1 
ATOM   3210 C  CG  . TRP C  1 126 ? -19.202 -10.638 46.938  1.00 24.94  ? 375  TRP C CG  1 
ATOM   3211 C  CD1 . TRP C  1 126 ? -19.888 -11.273 45.953  1.00 25.94  ? 375  TRP C CD1 1 
ATOM   3212 C  CD2 . TRP C  1 126 ? -19.972 -9.495  47.277  1.00 25.46  ? 375  TRP C CD2 1 
ATOM   3213 N  NE1 . TRP C  1 126 ? -21.013 -10.580 45.615  1.00 25.03  ? 375  TRP C NE1 1 
ATOM   3214 C  CE2 . TRP C  1 126 ? -21.111 -9.497  46.429  1.00 24.63  ? 375  TRP C CE2 1 
ATOM   3215 C  CE3 . TRP C  1 126 ? -19.797 -8.442  48.189  1.00 26.17  ? 375  TRP C CE3 1 
ATOM   3216 C  CZ2 . TRP C  1 126 ? -22.071 -8.521  46.467  1.00 25.34  ? 375  TRP C CZ2 1 
ATOM   3217 C  CZ3 . TRP C  1 126 ? -20.759 -7.461  48.233  1.00 27.71  ? 375  TRP C CZ3 1 
ATOM   3218 C  CH2 . TRP C  1 126 ? -21.902 -7.521  47.400  1.00 28.69  ? 375  TRP C CH2 1 
ATOM   3219 N  N   . ILE C  1 127 ? -16.326 -11.901 45.035  1.00 21.50  ? 376  ILE C N   1 
ATOM   3220 C  CA  . ILE C  1 127 ? -16.338 -12.299 43.687  1.00 25.01  ? 376  ILE C CA  1 
ATOM   3221 C  C   . ILE C  1 127 ? -17.178 -13.557 43.548  1.00 24.55  ? 376  ILE C C   1 
ATOM   3222 O  O   . ILE C  1 127 ? -17.013 -14.489 44.307  1.00 26.89  ? 376  ILE C O   1 
ATOM   3223 C  CB  . ILE C  1 127 ? -14.945 -12.503 43.111  1.00 27.65  ? 376  ILE C CB  1 
ATOM   3224 C  CG1 . ILE C  1 127 ? -14.207 -11.168 43.073  1.00 28.05  ? 376  ILE C CG1 1 
ATOM   3225 C  CG2 . ILE C  1 127 ? -15.057 -13.007 41.650  1.00 29.21  ? 376  ILE C CG2 1 
ATOM   3226 C  CD1 . ILE C  1 127 ? -12.750 -11.318 42.668  1.00 30.63  ? 376  ILE C CD1 1 
ATOM   3227 N  N   . CYS C  1 128 ? -18.084 -13.519 42.578  1.00 22.66  ? 377  CYS C N   1 
ATOM   3228 C  CA  . CYS C  1 128 ? -18.949 -14.605 42.188  1.00 23.92  ? 377  CYS C CA  1 
ATOM   3229 C  C   . CYS C  1 128 ? -18.426 -15.164 40.851  1.00 23.72  ? 377  CYS C C   1 
ATOM   3230 O  O   . CYS C  1 128 ? -17.845 -14.450 40.040  1.00 22.26  ? 377  CYS C O   1 
ATOM   3231 C  CB  . CYS C  1 128 ? -20.382 -14.133 41.921  1.00 24.88  ? 377  CYS C CB  1 
ATOM   3232 S  SG  . CYS C  1 128 ? -21.258 -13.288 43.246  1.00 29.64  ? 377  CYS C SG  1 
ATOM   3233 N  N   . LYS C  1 129 ? -18.697 -16.435 40.643  1.00 23.68  ? 378  LYS C N   1 
ATOM   3234 C  CA  . LYS C  1 129 ? -18.316 -17.160 39.430  1.00 24.79  ? 378  LYS C CA  1 
ATOM   3235 C  C   . LYS C  1 129 ? -19.473 -18.062 39.025  1.00 26.50  ? 378  LYS C C   1 
ATOM   3236 O  O   . LYS C  1 129 ? -20.182 -18.647 39.888  1.00 22.48  ? 378  LYS C O   1 
ATOM   3237 C  CB  . LYS C  1 129 ? -17.137 -18.043 39.752  1.00 24.44  ? 378  LYS C CB  1 
ATOM   3238 C  CG  . LYS C  1 129 ? -16.758 -19.074 38.708  1.00 25.70  ? 378  LYS C CG  1 
ATOM   3239 C  CD  . LYS C  1 129 ? -15.529 -19.818 39.186  1.00 25.93  ? 378  LYS C CD  1 
ATOM   3240 C  CE  . LYS C  1 129 ? -15.114 -20.936 38.242  1.00 27.37  ? 378  LYS C CE  1 
ATOM   3241 N  NZ  . LYS C  1 129 ? -13.976 -21.728 38.779  1.00 27.06  ? 378  LYS C NZ  1 
ATOM   3242 N  N   . LYS C  1 130 ? -19.684 -18.134 37.722  1.00 26.61  ? 379  LYS C N   1 
ATOM   3243 C  CA  . LYS C  1 130 ? -20.586 -19.109 37.141  1.00 29.10  ? 379  LYS C CA  1 
ATOM   3244 C  C   . LYS C  1 130 ? -20.155 -19.396 35.714  1.00 29.88  ? 379  LYS C C   1 
ATOM   3245 O  O   . LYS C  1 130 ? -19.354 -18.651 35.135  1.00 26.70  ? 379  LYS C O   1 
ATOM   3246 C  CB  . LYS C  1 130 ? -22.016 -18.602 37.168  1.00 31.41  ? 379  LYS C CB  1 
ATOM   3247 C  CG  . LYS C  1 130 ? -22.314 -17.484 36.212  1.00 32.85  ? 379  LYS C CG  1 
ATOM   3248 C  CD  . LYS C  1 130 ? -23.627 -16.833 36.557  1.00 35.14  ? 379  LYS C CD  1 
ATOM   3249 C  CE  . LYS C  1 130 ? -24.394 -16.367 35.344  1.00 41.35  ? 379  LYS C CE  1 
ATOM   3250 N  NZ  . LYS C  1 130 ? -25.695 -15.791 35.816  1.00 44.50  ? 379  LYS C NZ  1 
ATOM   3251 N  N   . SER C  1 131 ? -20.726 -20.446 35.131  1.00 31.32  ? 380  SER C N   1 
ATOM   3252 C  CA  . SER C  1 131 ? -20.370 -20.850 33.774  1.00 33.29  ? 380  SER C CA  1 
ATOM   3253 C  C   . SER C  1 131 ? -20.807 -19.869 32.710  1.00 30.71  ? 380  SER C C   1 
ATOM   3254 O  O   . SER C  1 131 ? -21.869 -19.286 32.778  1.00 28.43  ? 380  SER C O   1 
ATOM   3255 C  CB  . SER C  1 131 ? -20.977 -22.225 33.475  1.00 37.71  ? 380  SER C CB  1 
ATOM   3256 O  OG  . SER C  1 131 ? -20.307 -23.176 34.279  1.00 37.50  ? 380  SER C OG  1 
ATOM   3257 N  N   . ALA C  1 132 ? -19.969 -19.690 31.705  1.00 30.99  ? 381  ALA C N   1 
ATOM   3258 C  CA  . ALA C  1 132 ? -20.381 -18.925 30.532  1.00 29.22  ? 381  ALA C CA  1 
ATOM   3259 C  C   . ALA C  1 132 ? -21.471 -19.669 29.750  1.00 28.40  ? 381  ALA C C   1 
ATOM   3260 O  O   . ALA C  1 132 ? -21.598 -20.895 29.834  1.00 23.49  ? 381  ALA C O   1 
ATOM   3261 C  CB  . ALA C  1 132 ? -19.193 -18.674 29.650  1.00 30.86  ? 381  ALA C CB  1 
ATOM   3262 N  N   . ALA C  1 133 ? -22.308 -18.909 29.065  1.00 29.48  ? 382  ALA C N   1 
ATOM   3263 C  CA  . ALA C  1 133 ? -23.225 -19.469 28.114  1.00 31.42  ? 382  ALA C CA  1 
ATOM   3264 C  C   . ALA C  1 133 ? -22.397 -19.742 26.875  1.00 36.68  ? 382  ALA C C   1 
ATOM   3265 O  O   . ALA C  1 133 ? -21.486 -18.983 26.575  1.00 37.45  ? 382  ALA C O   1 
ATOM   3266 C  CB  . ALA C  1 133 ? -24.285 -18.465 27.781  1.00 30.09  ? 382  ALA C CB  1 
ATOM   3267 N  N   . SER C  1 134 ? -22.673 -20.827 26.171  1.00 40.08  ? 383  SER C N   1 
ATOM   3268 C  CA  . SER C  1 134 ? -22.075 -21.017 24.848  1.00 44.28  ? 383  SER C CA  1 
ATOM   3269 C  C   . SER C  1 134 ? -22.958 -20.350 23.805  1.00 42.12  ? 383  SER C C   1 
ATOM   3270 O  O   . SER C  1 134 ? -24.082 -20.781 23.587  1.00 40.50  ? 383  SER C O   1 
ATOM   3271 C  CB  . SER C  1 134 ? -21.968 -22.511 24.516  1.00 50.38  ? 383  SER C CB  1 
ATOM   3272 O  OG  . SER C  1 134 ? -21.594 -23.273 25.653  1.00 57.90  ? 383  SER C OG  1 
ATOM   3273 N  N   . CYS C  1 135 ? -22.446 -19.349 23.104  1.00 45.94  ? 384  CYS C N   1 
ATOM   3274 C  CA  . CYS C  1 135 ? -23.263 -18.678 22.097  1.00 53.95  ? 384  CYS C CA  1 
ATOM   3275 C  C   . CYS C  1 135 ? -23.067 -19.214 20.652  1.00 58.19  ? 384  CYS C C   1 
ATOM   3276 O  O   . CYS C  1 135 ? -21.946 -19.295 20.149  1.00 70.81  ? 384  CYS C O   1 
ATOM   3277 C  CB  . CYS C  1 135 ? -23.054 -17.171 22.212  1.00 53.80  ? 384  CYS C CB  1 
ATOM   3278 S  SG  . CYS C  1 135 ? -23.567 -16.579 23.849  1.00 49.63  ? 384  CYS C SG  1 
ATOM   3279 N  N   . LEU D  1 3   ? 23.520  -27.943 -13.789 1.00 82.46  ? 252  LEU D N   1 
ATOM   3280 C  CA  . LEU D  1 3   ? 22.901  -26.764 -13.102 1.00 84.27  ? 252  LEU D CA  1 
ATOM   3281 C  C   . LEU D  1 3   ? 21.861  -27.242 -12.074 1.00 79.16  ? 252  LEU D C   1 
ATOM   3282 O  O   . LEU D  1 3   ? 20.756  -26.709 -11.998 1.00 77.17  ? 252  LEU D O   1 
ATOM   3283 C  CB  . LEU D  1 3   ? 22.279  -25.803 -14.141 1.00 88.67  ? 252  LEU D CB  1 
ATOM   3284 C  CG  . LEU D  1 3   ? 21.759  -24.418 -13.696 1.00 92.81  ? 252  LEU D CG  1 
ATOM   3285 C  CD1 . LEU D  1 3   ? 22.882  -23.546 -13.132 1.00 90.14  ? 252  LEU D CD1 1 
ATOM   3286 C  CD2 . LEU D  1 3   ? 21.035  -23.707 -14.845 1.00 89.05  ? 252  LEU D CD2 1 
ATOM   3287 N  N   . CYS D  1 4   ? 22.240  -28.241 -11.275 1.00 75.12  ? 253  CYS D N   1 
ATOM   3288 C  CA  . CYS D  1 4   ? 21.347  -28.834 -10.278 1.00 76.51  ? 253  CYS D CA  1 
ATOM   3289 C  C   . CYS D  1 4   ? 21.380  -28.076 -8.939  1.00 70.77  ? 253  CYS D C   1 
ATOM   3290 O  O   . CYS D  1 4   ? 22.436  -27.915 -8.312  1.00 63.86  ? 253  CYS D O   1 
ATOM   3291 C  CB  . CYS D  1 4   ? 21.675  -30.311 -10.044 1.00 80.10  ? 253  CYS D CB  1 
ATOM   3292 S  SG  . CYS D  1 4   ? 20.654  -31.105 -8.770  1.00 87.25  ? 253  CYS D SG  1 
ATOM   3293 N  N   . HIS D  1 5   ? 20.198  -27.622 -8.527  1.00 62.17  ? 254  HIS D N   1 
ATOM   3294 C  CA  . HIS D  1 5   ? 19.985  -26.962 -7.242  1.00 52.60  ? 254  HIS D CA  1 
ATOM   3295 C  C   . HIS D  1 5   ? 19.228  -27.899 -6.303  1.00 43.56  ? 254  HIS D C   1 
ATOM   3296 O  O   . HIS D  1 5   ? 18.273  -28.511 -6.685  1.00 41.86  ? 254  HIS D O   1 
ATOM   3297 C  CB  . HIS D  1 5   ? 19.192  -25.704 -7.465  1.00 51.22  ? 254  HIS D CB  1 
ATOM   3298 C  CG  . HIS D  1 5   ? 19.834  -24.767 -8.430  1.00 52.89  ? 254  HIS D CG  1 
ATOM   3299 N  ND1 . HIS D  1 5   ? 20.792  -23.855 -8.048  1.00 56.25  ? 254  HIS D ND1 1 
ATOM   3300 C  CD2 . HIS D  1 5   ? 19.652  -24.591 -9.760  1.00 55.49  ? 254  HIS D CD2 1 
ATOM   3301 C  CE1 . HIS D  1 5   ? 21.162  -23.141 -9.097  1.00 56.34  ? 254  HIS D CE1 1 
ATOM   3302 N  NE2 . HIS D  1 5   ? 20.483  -23.569 -10.149 1.00 58.89  ? 254  HIS D NE2 1 
ATOM   3303 N  N   . PRO D  1 6   ? 19.673  -28.034 -5.064  1.00 42.45  ? 255  PRO D N   1 
ATOM   3304 C  CA  . PRO D  1 6   ? 18.900  -28.900 -4.167  1.00 40.89  ? 255  PRO D CA  1 
ATOM   3305 C  C   . PRO D  1 6   ? 17.469  -28.386 -3.849  1.00 36.21  ? 255  PRO D C   1 
ATOM   3306 O  O   . PRO D  1 6   ? 16.585  -29.184 -3.642  1.00 36.90  ? 255  PRO D O   1 
ATOM   3307 C  CB  . PRO D  1 6   ? 19.760  -28.927 -2.888  1.00 39.66  ? 255  PRO D CB  1 
ATOM   3308 C  CG  . PRO D  1 6   ? 21.098  -28.373 -3.275  1.00 39.98  ? 255  PRO D CG  1 
ATOM   3309 C  CD  . PRO D  1 6   ? 20.830  -27.424 -4.385  1.00 42.54  ? 255  PRO D CD  1 
ATOM   3310 N  N   . CYS D  1 7   ? 17.260  -27.075 -3.796  1.00 36.64  ? 256  CYS D N   1 
ATOM   3311 C  CA  . CYS D  1 7   ? 15.960  -26.535 -3.408  1.00 39.91  ? 256  CYS D CA  1 
ATOM   3312 C  C   . CYS D  1 7   ? 15.380  -25.634 -4.474  1.00 44.43  ? 256  CYS D C   1 
ATOM   3313 O  O   . CYS D  1 7   ? 16.130  -25.030 -5.237  1.00 48.39  ? 256  CYS D O   1 
ATOM   3314 C  CB  . CYS D  1 7   ? 16.091  -25.747 -2.093  1.00 37.89  ? 256  CYS D CB  1 
ATOM   3315 S  SG  . CYS D  1 7   ? 16.498  -26.844 -0.729  1.00 36.57  ? 256  CYS D SG  1 
ATOM   3316 N  N   . PRO D  1 8   ? 14.041  -25.533 -4.525  1.00 39.70  ? 257  PRO D N   1 
ATOM   3317 C  CA  . PRO D  1 8   ? 13.485  -24.485 -5.308  1.00 38.62  ? 257  PRO D CA  1 
ATOM   3318 C  C   . PRO D  1 8   ? 14.042  -23.125 -4.948  1.00 39.51  ? 257  PRO D C   1 
ATOM   3319 O  O   . PRO D  1 8   ? 14.440  -22.841 -3.781  1.00 33.30  ? 257  PRO D O   1 
ATOM   3320 C  CB  . PRO D  1 8   ? 11.998  -24.529 -4.949  1.00 44.27  ? 257  PRO D CB  1 
ATOM   3321 C  CG  . PRO D  1 8   ? 11.743  -25.935 -4.603  1.00 42.63  ? 257  PRO D CG  1 
ATOM   3322 C  CD  . PRO D  1 8   ? 13.003  -26.385 -3.929  1.00 42.23  ? 257  PRO D CD  1 
ATOM   3323 N  N   . TRP D  1 9   ? 14.027  -22.286 -5.973  1.00 37.06  ? 258  TRP D N   1 
ATOM   3324 C  CA  . TRP D  1 9   ? 14.453  -20.925 -5.883  1.00 39.96  ? 258  TRP D CA  1 
ATOM   3325 C  C   . TRP D  1 9   ? 13.752  -20.206 -4.723  1.00 40.30  ? 258  TRP D C   1 
ATOM   3326 O  O   . TRP D  1 9   ? 12.541  -20.214 -4.632  1.00 38.97  ? 258  TRP D O   1 
ATOM   3327 C  CB  . TRP D  1 9   ? 14.151  -20.232 -7.203  1.00 40.76  ? 258  TRP D CB  1 
ATOM   3328 C  CG  . TRP D  1 9   ? 14.920  -18.966 -7.452  1.00 43.46  ? 258  TRP D CG  1 
ATOM   3329 C  CD1 . TRP D  1 9   ? 15.210  -17.976 -6.559  1.00 42.82  ? 258  TRP D CD1 1 
ATOM   3330 C  CD2 . TRP D  1 9   ? 15.464  -18.545 -8.708  1.00 46.26  ? 258  TRP D CD2 1 
ATOM   3331 N  NE1 . TRP D  1 9   ? 15.921  -16.976 -7.179  1.00 44.26  ? 258  TRP D NE1 1 
ATOM   3332 C  CE2 . TRP D  1 9   ? 16.091  -17.307 -8.498  1.00 44.98  ? 258  TRP D CE2 1 
ATOM   3333 C  CE3 . TRP D  1 9   ? 15.500  -19.114 -9.992  1.00 48.75  ? 258  TRP D CE3 1 
ATOM   3334 C  CZ2 . TRP D  1 9   ? 16.726  -16.603 -9.532  1.00 47.61  ? 258  TRP D CZ2 1 
ATOM   3335 C  CZ3 . TRP D  1 9   ? 16.142  -18.422 -11.009 1.00 49.21  ? 258  TRP D CZ3 1 
ATOM   3336 C  CH2 . TRP D  1 9   ? 16.750  -17.183 -10.770 1.00 46.05  ? 258  TRP D CH2 1 
ATOM   3337 N  N   . GLU D  1 10  ? 14.536  -19.593 -3.841  1.00 40.36  ? 259  GLU D N   1 
ATOM   3338 C  CA  . GLU D  1 10  ? 14.026  -18.789 -2.701  1.00 40.39  ? 259  GLU D CA  1 
ATOM   3339 C  C   . GLU D  1 10  ? 13.813  -19.629 -1.463  1.00 37.63  ? 259  GLU D C   1 
ATOM   3340 O  O   . GLU D  1 10  ? 13.589  -19.080 -0.395  1.00 43.66  ? 259  GLU D O   1 
ATOM   3341 C  CB  . GLU D  1 10  ? 12.720  -18.010 -3.034  1.00 42.67  ? 259  GLU D CB  1 
ATOM   3342 C  CG  . GLU D  1 10  ? 12.847  -17.131 -4.261  1.00 45.90  ? 259  GLU D CG  1 
ATOM   3343 C  CD  . GLU D  1 10  ? 11.782  -16.036 -4.411  1.00 50.77  ? 259  GLU D CD  1 
ATOM   3344 O  OE1 . GLU D  1 10  ? 11.415  -15.375 -3.415  1.00 46.45  ? 259  GLU D OE1 1 
ATOM   3345 O  OE2 . GLU D  1 10  ? 11.366  -15.803 -5.572  1.00 49.92  ? 259  GLU D OE2 1 
ATOM   3346 N  N   . TRP D  1 11  ? 13.856  -20.954 -1.600  1.00 35.85  ? 260  TRP D N   1 
ATOM   3347 C  CA  . TRP D  1 11  ? 13.709  -21.844 -0.471  1.00 34.37  ? 260  TRP D CA  1 
ATOM   3348 C  C   . TRP D  1 11  ? 15.038  -22.062 0.258   1.00 38.42  ? 260  TRP D C   1 
ATOM   3349 O  O   . TRP D  1 11  ? 16.109  -21.968 -0.345  1.00 36.08  ? 260  TRP D O   1 
ATOM   3350 C  CB  . TRP D  1 11  ? 13.187  -23.197 -0.917  1.00 33.64  ? 260  TRP D CB  1 
ATOM   3351 C  CG  . TRP D  1 11  ? 11.735  -23.192 -1.380  1.00 34.10  ? 260  TRP D CG  1 
ATOM   3352 C  CD1 . TRP D  1 11  ? 11.164  -22.349 -2.289  1.00 34.40  ? 260  TRP D CD1 1 
ATOM   3353 C  CD2 . TRP D  1 11  ? 10.699  -24.094 -0.970  1.00 31.63  ? 260  TRP D CD2 1 
ATOM   3354 N  NE1 . TRP D  1 11  ? 9.857   -22.683 -2.481  1.00 32.95  ? 260  TRP D NE1 1 
ATOM   3355 C  CE2 . TRP D  1 11  ? 9.545   -23.751 -1.683  1.00 31.60  ? 260  TRP D CE2 1 
ATOM   3356 C  CE3 . TRP D  1 11  ? 10.643  -25.152 -0.079  1.00 29.79  ? 260  TRP D CE3 1 
ATOM   3357 C  CZ2 . TRP D  1 11  ? 8.351   -24.385 -1.498  1.00 29.91  ? 260  TRP D CZ2 1 
ATOM   3358 C  CZ3 . TRP D  1 11  ? 9.455   -25.804 0.079   1.00 32.53  ? 260  TRP D CZ3 1 
ATOM   3359 C  CH2 . TRP D  1 11  ? 8.322   -25.419 -0.634  1.00 31.42  ? 260  TRP D CH2 1 
ATOM   3360 N  N   . THR D  1 12  ? 14.947  -22.410 1.545   1.00 37.58  ? 261  THR D N   1 
ATOM   3361 C  CA  . THR D  1 12  ? 16.128  -22.634 2.407   1.00 35.37  ? 261  THR D CA  1 
ATOM   3362 C  C   . THR D  1 12  ? 16.444  -24.112 2.572   1.00 33.75  ? 261  THR D C   1 
ATOM   3363 O  O   . THR D  1 12  ? 15.593  -24.897 2.970   1.00 34.67  ? 261  THR D O   1 
ATOM   3364 C  CB  . THR D  1 12  ? 15.920  -22.027 3.814   1.00 34.86  ? 261  THR D CB  1 
ATOM   3365 O  OG1 . THR D  1 12  ? 15.836  -20.613 3.696   1.00 32.59  ? 261  THR D OG1 1 
ATOM   3366 C  CG2 . THR D  1 12  ? 17.089  -22.369 4.752   1.00 35.35  ? 261  THR D CG2 1 
ATOM   3367 N  N   . PHE D  1 13  ? 17.692  -24.468 2.289   1.00 36.70  ? 262  PHE D N   1 
ATOM   3368 C  CA  . PHE D  1 13  ? 18.213  -25.836 2.440   1.00 35.04  ? 262  PHE D CA  1 
ATOM   3369 C  C   . PHE D  1 13  ? 18.661  -26.069 3.863   1.00 32.76  ? 262  PHE D C   1 
ATOM   3370 O  O   . PHE D  1 13  ? 19.370  -25.274 4.441   1.00 32.70  ? 262  PHE D O   1 
ATOM   3371 C  CB  . PHE D  1 13  ? 19.409  -26.080 1.506   1.00 35.34  ? 262  PHE D CB  1 
ATOM   3372 C  CG  . PHE D  1 13  ? 20.033  -27.448 1.644   1.00 37.17  ? 262  PHE D CG  1 
ATOM   3373 C  CD1 . PHE D  1 13  ? 21.071  -27.674 2.540   1.00 38.42  ? 262  PHE D CD1 1 
ATOM   3374 C  CD2 . PHE D  1 13  ? 19.611  -28.506 0.853   1.00 38.91  ? 262  PHE D CD2 1 
ATOM   3375 C  CE1 . PHE D  1 13  ? 21.650  -28.931 2.666   1.00 36.58  ? 262  PHE D CE1 1 
ATOM   3376 C  CE2 . PHE D  1 13  ? 20.193  -29.757 0.969   1.00 40.17  ? 262  PHE D CE2 1 
ATOM   3377 C  CZ  . PHE D  1 13  ? 21.224  -29.967 1.878   1.00 38.00  ? 262  PHE D CZ  1 
ATOM   3378 N  N   . PHE D  1 14  ? 18.254  -27.187 4.427   1.00 34.04  ? 263  PHE D N   1 
ATOM   3379 C  CA  . PHE D  1 14  ? 18.774  -27.584 5.711   1.00 33.90  ? 263  PHE D CA  1 
ATOM   3380 C  C   . PHE D  1 14  ? 18.759  -29.082 5.772   1.00 33.16  ? 263  PHE D C   1 
ATOM   3381 O  O   . PHE D  1 14  ? 17.713  -29.713 5.679   1.00 29.29  ? 263  PHE D O   1 
ATOM   3382 C  CB  . PHE D  1 14  ? 17.955  -27.010 6.866   1.00 34.04  ? 263  PHE D CB  1 
ATOM   3383 C  CG  . PHE D  1 14  ? 18.377  -27.550 8.204   1.00 36.55  ? 263  PHE D CG  1 
ATOM   3384 C  CD1 . PHE D  1 14  ? 19.421  -26.957 8.913   1.00 35.24  ? 263  PHE D CD1 1 
ATOM   3385 C  CD2 . PHE D  1 14  ? 17.760  -28.673 8.731   1.00 35.63  ? 263  PHE D CD2 1 
ATOM   3386 C  CE1 . PHE D  1 14  ? 19.814  -27.459 10.126  1.00 34.07  ? 263  PHE D CE1 1 
ATOM   3387 C  CE2 . PHE D  1 14  ? 18.177  -29.208 9.930   1.00 37.54  ? 263  PHE D CE2 1 
ATOM   3388 C  CZ  . PHE D  1 14  ? 19.198  -28.590 10.642  1.00 37.67  ? 263  PHE D CZ  1 
ATOM   3389 N  N   . GLN D  1 15  ? 19.955  -29.629 5.923   1.00 36.18  ? 264  GLN D N   1 
ATOM   3390 C  CA  . GLN D  1 15  ? 20.189  -31.055 6.141   1.00 36.75  ? 264  GLN D CA  1 
ATOM   3391 C  C   . GLN D  1 15  ? 19.322  -31.934 5.275   1.00 35.38  ? 264  GLN D C   1 
ATOM   3392 O  O   . GLN D  1 15  ? 18.683  -32.850 5.751   1.00 33.65  ? 264  GLN D O   1 
ATOM   3393 C  CB  . GLN D  1 15  ? 20.092  -31.406 7.634   1.00 36.68  ? 264  GLN D CB  1 
ATOM   3394 C  CG  . GLN D  1 15  ? 21.250  -30.772 8.419   1.00 39.03  ? 264  GLN D CG  1 
ATOM   3395 C  CD  . GLN D  1 15  ? 21.418  -31.240 9.862   1.00 40.38  ? 264  GLN D CD  1 
ATOM   3396 O  OE1 . GLN D  1 15  ? 20.936  -32.298 10.251  1.00 47.47  ? 264  GLN D OE1 1 
ATOM   3397 N  NE2 . GLN D  1 15  ? 22.147  -30.452 10.661  1.00 42.67  ? 264  GLN D NE2 1 
ATOM   3398 N  N   . GLY D  1 16  ? 19.334  -31.637 3.985   1.00 34.48  ? 265  GLY D N   1 
ATOM   3399 C  CA  . GLY D  1 16  ? 18.737  -32.512 2.986   1.00 36.42  ? 265  GLY D CA  1 
ATOM   3400 C  C   . GLY D  1 16  ? 17.260  -32.283 2.717   1.00 34.49  ? 265  GLY D C   1 
ATOM   3401 O  O   . GLY D  1 16  ? 16.618  -33.117 2.115   1.00 36.01  ? 265  GLY D O   1 
ATOM   3402 N  N   . ASN D  1 17  ? 16.725  -31.155 3.176   1.00 33.01  ? 266  ASN D N   1 
ATOM   3403 C  CA  . ASN D  1 17  ? 15.347  -30.761 2.865   1.00 30.22  ? 266  ASN D CA  1 
ATOM   3404 C  C   . ASN D  1 17  ? 15.288  -29.293 2.616   1.00 28.76  ? 266  ASN D C   1 
ATOM   3405 O  O   . ASN D  1 17  ? 16.222  -28.562 2.924   1.00 30.26  ? 266  ASN D O   1 
ATOM   3406 C  CB  . ASN D  1 17  ? 14.429  -31.134 4.029   1.00 34.48  ? 266  ASN D CB  1 
ATOM   3407 C  CG  . ASN D  1 17  ? 14.337  -32.637 4.231   1.00 30.34  ? 266  ASN D CG  1 
ATOM   3408 O  OD1 . ASN D  1 17  ? 13.702  -33.313 3.465   1.00 33.03  ? 266  ASN D OD1 1 
ATOM   3409 N  ND2 . ASN D  1 17  ? 14.971  -33.142 5.244   1.00 29.05  ? 266  ASN D ND2 1 
ATOM   3410 N  N   . CYS D  1 18  ? 14.180  -28.859 2.045   1.00 29.15  ? 267  CYS D N   1 
ATOM   3411 C  CA  . CYS D  1 18  ? 13.991  -27.478 1.624   1.00 30.85  ? 267  CYS D CA  1 
ATOM   3412 C  C   . CYS D  1 18  ? 12.806  -26.899 2.381   1.00 30.37  ? 267  CYS D C   1 
ATOM   3413 O  O   . CYS D  1 18  ? 11.810  -27.597 2.606   1.00 30.51  ? 267  CYS D O   1 
ATOM   3414 C  CB  . CYS D  1 18  ? 13.692  -27.433 0.129   1.00 33.67  ? 267  CYS D CB  1 
ATOM   3415 S  SG  . CYS D  1 18  ? 14.999  -28.248 -0.794  1.00 36.12  ? 267  CYS D SG  1 
ATOM   3416 N  N   . TYR D  1 19  ? 12.920  -25.638 2.746   1.00 28.77  ? 268  TYR D N   1 
ATOM   3417 C  CA  . TYR D  1 19  ? 12.017  -25.037 3.695   1.00 31.17  ? 268  TYR D CA  1 
ATOM   3418 C  C   . TYR D  1 19  ? 11.622  -23.695 3.151   1.00 32.50  ? 268  TYR D C   1 
ATOM   3419 O  O   . TYR D  1 19  ? 12.469  -22.925 2.690   1.00 30.17  ? 268  TYR D O   1 
ATOM   3420 C  CB  . TYR D  1 19  ? 12.661  -24.908 5.089   1.00 31.07  ? 268  TYR D CB  1 
ATOM   3421 C  CG  . TYR D  1 19  ? 12.955  -26.225 5.746   1.00 31.54  ? 268  TYR D CG  1 
ATOM   3422 C  CD1 . TYR D  1 19  ? 14.144  -26.894 5.508   1.00 32.57  ? 268  TYR D CD1 1 
ATOM   3423 C  CD2 . TYR D  1 19  ? 12.046  -26.809 6.597   1.00 31.76  ? 268  TYR D CD2 1 
ATOM   3424 C  CE1 . TYR D  1 19  ? 14.406  -28.110 6.089   1.00 31.34  ? 268  TYR D CE1 1 
ATOM   3425 C  CE2 . TYR D  1 19  ? 12.300  -28.025 7.191   1.00 28.51  ? 268  TYR D CE2 1 
ATOM   3426 C  CZ  . TYR D  1 19  ? 13.480  -28.674 6.937   1.00 29.71  ? 268  TYR D CZ  1 
ATOM   3427 O  OH  . TYR D  1 19  ? 13.742  -29.901 7.539   1.00 26.57  ? 268  TYR D OH  1 
ATOM   3428 N  N   . PHE D  1 20  ? 10.320  -23.442 3.162   1.00 32.15  ? 269  PHE D N   1 
ATOM   3429 C  CA  . PHE D  1 20  ? 9.809   -22.158 2.799   1.00 30.38  ? 269  PHE D CA  1 
ATOM   3430 C  C   . PHE D  1 20  ? 9.186   -21.515 4.028   1.00 30.05  ? 269  PHE D C   1 
ATOM   3431 O  O   . PHE D  1 20  ? 8.321   -22.139 4.697   1.00 27.84  ? 269  PHE D O   1 
ATOM   3432 C  CB  . PHE D  1 20  ? 8.766   -22.348 1.734   1.00 33.18  ? 269  PHE D CB  1 
ATOM   3433 C  CG  . PHE D  1 20  ? 8.096   -21.081 1.348   1.00 33.72  ? 269  PHE D CG  1 
ATOM   3434 C  CD1 . PHE D  1 20  ? 8.741   -20.177 0.515   1.00 38.60  ? 269  PHE D CD1 1 
ATOM   3435 C  CD2 . PHE D  1 20  ? 6.857   -20.757 1.868   1.00 34.77  ? 269  PHE D CD2 1 
ATOM   3436 C  CE1 . PHE D  1 20  ? 8.149   -18.977 0.190   1.00 36.83  ? 269  PHE D CE1 1 
ATOM   3437 C  CE2 . PHE D  1 20  ? 6.243   -19.562 1.534   1.00 37.35  ? 269  PHE D CE2 1 
ATOM   3438 C  CZ  . PHE D  1 20  ? 6.893   -18.678 0.693   1.00 36.68  ? 269  PHE D CZ  1 
ATOM   3439 N  N   . MET D  1 21  ? 9.608   -20.292 4.328   1.00 30.42  ? 270  MET D N   1 
ATOM   3440 C  CA  . MET D  1 21  ? 9.052   -19.548 5.461   1.00 33.92  ? 270  MET D CA  1 
ATOM   3441 C  C   . MET D  1 21  ? 8.096   -18.510 4.921   1.00 32.22  ? 270  MET D C   1 
ATOM   3442 O  O   . MET D  1 21  ? 8.477   -17.641 4.142   1.00 32.35  ? 270  MET D O   1 
ATOM   3443 C  CB  . MET D  1 21  ? 10.108  -18.838 6.295   1.00 38.55  ? 270  MET D CB  1 
ATOM   3444 C  CG  . MET D  1 21  ? 11.476  -19.490 6.318   1.00 45.10  ? 270  MET D CG  1 
ATOM   3445 S  SD  . MET D  1 21  ? 11.562  -21.167 6.934   1.00 47.95  ? 270  MET D SD  1 
ATOM   3446 C  CE  . MET D  1 21  ? 13.328  -21.438 6.784   1.00 50.66  ? 270  MET D CE  1 
ATOM   3447 N  N   . SER D  1 22  ? 6.850   -18.584 5.339   1.00 28.94  ? 271  SER D N   1 
ATOM   3448 C  CA  . SER D  1 22  ? 5.877   -17.640 4.849   1.00 30.61  ? 271  SER D CA  1 
ATOM   3449 C  C   . SER D  1 22  ? 6.231   -16.234 5.305   1.00 30.79  ? 271  SER D C   1 
ATOM   3450 O  O   . SER D  1 22  ? 6.858   -16.064 6.332   1.00 34.12  ? 271  SER D O   1 
ATOM   3451 C  CB  . SER D  1 22  ? 4.474   -18.013 5.340   1.00 31.36  ? 271  SER D CB  1 
ATOM   3452 O  OG  . SER D  1 22  ? 4.265   -17.637 6.693   1.00 29.69  ? 271  SER D OG  1 
ATOM   3453 N  N   . ASN D  1 23  ? 5.828   -15.243 4.519   1.00 34.05  ? 272  ASN D N   1 
ATOM   3454 C  CA  A ASN D  1 23  ? 5.915   -13.835 4.867   0.70 40.30  ? 272  ASN D CA  1 
ATOM   3455 C  CA  B ASN D  1 23  ? 5.926   -13.852 4.975   0.30 34.61  ? 272  ASN D CA  1 
ATOM   3456 C  C   . ASN D  1 23  ? 4.531   -13.255 5.210   1.00 37.48  ? 272  ASN D C   1 
ATOM   3457 O  O   . ASN D  1 23  ? 4.391   -12.071 5.425   1.00 42.95  ? 272  ASN D O   1 
ATOM   3458 C  CB  A ASN D  1 23  ? 6.519   -13.059 3.688   0.70 47.53  ? 272  ASN D CB  1 
ATOM   3459 C  CB  B ASN D  1 23  ? 6.762   -12.989 4.020   0.30 33.60  ? 272  ASN D CB  1 
ATOM   3460 C  CG  A ASN D  1 23  ? 7.051   -11.700 4.092   0.70 51.53  ? 272  ASN D CG  1 
ATOM   3461 C  CG  B ASN D  1 23  ? 8.255   -13.295 4.100   0.30 31.00  ? 272  ASN D CG  1 
ATOM   3462 O  OD1 A ASN D  1 23  ? 7.151   -11.391 5.283   0.70 56.22  ? 272  ASN D OD1 1 
ATOM   3463 O  OD1 B ASN D  1 23  ? 8.820   -13.522 5.183   0.30 28.02  ? 272  ASN D OD1 1 
ATOM   3464 N  ND2 A ASN D  1 23  ? 7.391   -10.873 3.098   0.70 52.63  ? 272  ASN D ND2 1 
ATOM   3465 N  ND2 B ASN D  1 23  ? 8.898   -13.303 2.942   0.30 29.18  ? 272  ASN D ND2 1 
ATOM   3466 N  N   . SER D  1 24  ? 3.506   -14.096 5.232   1.00 34.88  ? 273  SER D N   1 
ATOM   3467 C  CA  . SER D  1 24  ? 2.174   -13.662 5.619   1.00 34.94  ? 273  SER D CA  1 
ATOM   3468 C  C   . SER D  1 24  ? 1.568   -14.709 6.575   1.00 33.83  ? 273  SER D C   1 
ATOM   3469 O  O   . SER D  1 24  ? 2.233   -15.692 6.916   1.00 30.77  ? 273  SER D O   1 
ATOM   3470 C  CB  . SER D  1 24  ? 1.319   -13.520 4.391   1.00 33.11  ? 273  SER D CB  1 
ATOM   3471 O  OG  . SER D  1 24  ? 1.293   -14.764 3.746   1.00 39.73  ? 273  SER D OG  1 
ATOM   3472 N  N   . GLN D  1 25  ? 0.325   -14.475 7.007   1.00 30.80  ? 274  GLN D N   1 
ATOM   3473 C  CA  . GLN D  1 25  ? -0.344  -15.323 7.985   1.00 29.31  ? 274  GLN D CA  1 
ATOM   3474 C  C   . GLN D  1 25  ? -1.622  -15.986 7.447   1.00 28.74  ? 274  GLN D C   1 
ATOM   3475 O  O   . GLN D  1 25  ? -2.344  -15.412 6.649   1.00 34.15  ? 274  GLN D O   1 
ATOM   3476 C  CB  . GLN D  1 25  ? -0.683  -14.503 9.240   1.00 31.10  ? 274  GLN D CB  1 
ATOM   3477 C  CG  . GLN D  1 25  ? 0.507   -13.888 9.973   1.00 29.30  ? 274  GLN D CG  1 
ATOM   3478 C  CD  . GLN D  1 25  ? 0.102   -12.596 10.670  1.00 33.48  ? 274  GLN D CD  1 
ATOM   3479 O  OE1 . GLN D  1 25  ? 0.055   -12.508 11.918  1.00 36.57  ? 274  GLN D OE1 1 
ATOM   3480 N  NE2 . GLN D  1 25  ? -0.273  -11.621 9.873   1.00 29.99  ? 274  GLN D NE2 1 
ATOM   3481 N  N   . ARG D  1 26  ? -1.890  -17.193 7.925   1.00 27.24  ? 275  ARG D N   1 
ATOM   3482 C  CA  . ARG D  1 26  ? -3.045  -17.971 7.558   1.00 29.03  ? 275  ARG D CA  1 
ATOM   3483 C  C   . ARG D  1 26  ? -3.412  -18.895 8.731   1.00 25.47  ? 275  ARG D C   1 
ATOM   3484 O  O   . ARG D  1 26  ? -2.601  -19.225 9.584   1.00 24.36  ? 275  ARG D O   1 
ATOM   3485 C  CB  . ARG D  1 26  ? -2.703  -18.903 6.382   1.00 33.07  ? 275  ARG D CB  1 
ATOM   3486 C  CG  . ARG D  1 26  ? -2.583  -18.228 5.032   1.00 37.53  ? 275  ARG D CG  1 
ATOM   3487 C  CD  . ARG D  1 26  ? -2.084  -19.217 3.995   1.00 40.71  ? 275  ARG D CD  1 
ATOM   3488 N  NE  . ARG D  1 26  ? -2.195  -18.615 2.687   1.00 42.91  ? 275  ARG D NE  1 
ATOM   3489 C  CZ  . ARG D  1 26  ? -2.904  -19.094 1.677   1.00 45.17  ? 275  ARG D CZ  1 
ATOM   3490 N  NH1 . ARG D  1 26  ? -3.538  -20.268 1.744   1.00 49.10  ? 275  ARG D NH1 1 
ATOM   3491 N  NH2 . ARG D  1 26  ? -2.931  -18.403 0.561   1.00 45.48  ? 275  ARG D NH2 1 
ATOM   3492 N  N   . ASN D  1 27  ? -4.624  -19.377 8.729   1.00 25.02  ? 276  ASN D N   1 
ATOM   3493 C  CA  . ASN D  1 27  ? -4.996  -20.373 9.716   1.00 25.84  ? 276  ASN D CA  1 
ATOM   3494 C  C   . ASN D  1 27  ? -4.366  -21.713 9.313   1.00 25.82  ? 276  ASN D C   1 
ATOM   3495 O  O   . ASN D  1 27  ? -3.708  -21.828 8.281   1.00 22.69  ? 276  ASN D O   1 
ATOM   3496 C  CB  . ASN D  1 27  ? -6.520  -20.417 9.897   1.00 26.51  ? 276  ASN D CB  1 
ATOM   3497 C  CG  . ASN D  1 27  ? -7.257  -20.827 8.655   1.00 28.20  ? 276  ASN D CG  1 
ATOM   3498 O  OD1 . ASN D  1 27  ? -6.835  -21.726 7.893   1.00 29.63  ? 276  ASN D OD1 1 
ATOM   3499 N  ND2 . ASN D  1 27  ? -8.397  -20.197 8.451   1.00 28.57  ? 276  ASN D ND2 1 
ATOM   3500 N  N   . TRP D  1 28  ? -4.526  -22.693 10.171  1.00 26.44  ? 277  TRP D N   1 
ATOM   3501 C  CA  . TRP D  1 28  ? -3.827  -23.944 10.036  1.00 27.36  ? 277  TRP D CA  1 
ATOM   3502 C  C   . TRP D  1 28  ? -4.204  -24.669 8.737   1.00 29.84  ? 277  TRP D C   1 
ATOM   3503 O  O   . TRP D  1 28  ? -3.339  -25.010 7.914   1.00 27.92  ? 277  TRP D O   1 
ATOM   3504 C  CB  . TRP D  1 28  ? -4.087  -24.790 11.261  1.00 27.23  ? 277  TRP D CB  1 
ATOM   3505 C  CG  . TRP D  1 28  ? -3.205  -25.915 11.358  1.00 25.79  ? 277  TRP D CG  1 
ATOM   3506 C  CD1 . TRP D  1 28  ? -1.897  -25.894 11.747  1.00 26.51  ? 277  TRP D CD1 1 
ATOM   3507 C  CD2 . TRP D  1 28  ? -3.520  -27.280 11.058  1.00 25.17  ? 277  TRP D CD2 1 
ATOM   3508 N  NE1 . TRP D  1 28  ? -1.380  -27.157 11.706  1.00 25.22  ? 277  TRP D NE1 1 
ATOM   3509 C  CE2 . TRP D  1 28  ? -2.341  -28.028 11.269  1.00 26.00  ? 277  TRP D CE2 1 
ATOM   3510 C  CE3 . TRP D  1 28  ? -4.667  -27.931 10.589  1.00 26.81  ? 277  TRP D CE3 1 
ATOM   3511 C  CZ2 . TRP D  1 28  ? -2.283  -29.422 11.090  1.00 27.51  ? 277  TRP D CZ2 1 
ATOM   3512 C  CZ3 . TRP D  1 28  ? -4.616  -29.301 10.358  1.00 28.40  ? 277  TRP D CZ3 1 
ATOM   3513 C  CH2 . TRP D  1 28  ? -3.430  -30.044 10.628  1.00 28.73  ? 277  TRP D CH2 1 
ATOM   3514 N  N   . HIS D  1 29  ? -5.498  -24.820 8.521   1.00 31.28  ? 278  HIS D N   1 
ATOM   3515 C  CA  . HIS D  1 29  ? -6.002  -25.397 7.289   1.00 32.33  ? 278  HIS D CA  1 
ATOM   3516 C  C   . HIS D  1 29  ? -5.561  -24.662 6.012   1.00 31.54  ? 278  HIS D C   1 
ATOM   3517 O  O   . HIS D  1 29  ? -5.172  -25.313 5.048   1.00 27.58  ? 278  HIS D O   1 
ATOM   3518 C  CB  . HIS D  1 29  ? -7.520  -25.575 7.370   1.00 36.13  ? 278  HIS D CB  1 
ATOM   3519 C  CG  . HIS D  1 29  ? -7.933  -26.615 8.382   1.00 39.64  ? 278  HIS D CG  1 
ATOM   3520 N  ND1 . HIS D  1 29  ? -8.359  -26.296 9.661   1.00 39.86  ? 278  HIS D ND1 1 
ATOM   3521 C  CD2 . HIS D  1 29  ? -7.921  -27.973 8.318   1.00 39.93  ? 278  HIS D CD2 1 
ATOM   3522 C  CE1 . HIS D  1 29  ? -8.622  -27.410 10.323  1.00 44.69  ? 278  HIS D CE1 1 
ATOM   3523 N  NE2 . HIS D  1 29  ? -8.375  -28.440 9.527   1.00 39.65  ? 278  HIS D NE2 1 
ATOM   3524 N  N   . ASP D  1 30  ? -5.569  -23.331 5.997   1.00 28.76  ? 279  ASP D N   1 
ATOM   3525 C  CA  . ASP D  1 30  ? -5.106  -22.605 4.816   1.00 29.26  ? 279  ASP D CA  1 
ATOM   3526 C  C   . ASP D  1 30  ? -3.591  -22.711 4.617   1.00 29.49  ? 279  ASP D C   1 
ATOM   3527 O  O   . ASP D  1 30  ? -3.110  -22.610 3.498   1.00 31.48  ? 279  ASP D O   1 
ATOM   3528 C  CB  . ASP D  1 30  ? -5.499  -21.148 4.891   1.00 32.46  ? 279  ASP D CB  1 
ATOM   3529 C  CG  . ASP D  1 30  ? -7.013  -20.947 4.794   1.00 34.53  ? 279  ASP D CG  1 
ATOM   3530 O  OD1 . ASP D  1 30  ? -7.699  -21.884 4.368   1.00 29.34  ? 279  ASP D OD1 1 
ATOM   3531 O  OD2 . ASP D  1 30  ? -7.503  -19.866 5.205   1.00 32.86  ? 279  ASP D OD2 1 
ATOM   3532 N  N   . SER D  1 31  ? -2.860  -22.879 5.715   1.00 27.94  ? 280  SER D N   1 
ATOM   3533 C  CA  . SER D  1 31  ? -1.428  -23.205 5.671   1.00 27.55  ? 280  SER D CA  1 
ATOM   3534 C  C   . SER D  1 31  ? -1.167  -24.567 5.033   1.00 26.99  ? 280  SER D C   1 
ATOM   3535 O  O   . SER D  1 31  ? -0.325  -24.687 4.135   1.00 24.66  ? 280  SER D O   1 
ATOM   3536 C  CB  . SER D  1 31  ? -0.797  -23.078 7.047   1.00 26.79  ? 280  SER D CB  1 
ATOM   3537 O  OG  . SER D  1 31  ? -0.866  -21.721 7.426   1.00 25.52  ? 280  SER D OG  1 
ATOM   3538 N  N   . ILE D  1 32  ? -1.918  -25.584 5.414   1.00 29.83  ? 281  ILE D N   1 
ATOM   3539 C  CA  . ILE D  1 32  ? -1.816  -26.877 4.693   1.00 29.84  ? 281  ILE D CA  1 
ATOM   3540 C  C   . ILE D  1 32  ? -1.973  -26.724 3.184   1.00 30.58  ? 281  ILE D C   1 
ATOM   3541 O  O   . ILE D  1 32  ? -1.180  -27.219 2.361   1.00 29.46  ? 281  ILE D O   1 
ATOM   3542 C  CB  . ILE D  1 32  ? -2.852  -27.849 5.200   1.00 31.04  ? 281  ILE D CB  1 
ATOM   3543 C  CG1 . ILE D  1 32  ? -2.383  -28.291 6.588   1.00 34.81  ? 281  ILE D CG1 1 
ATOM   3544 C  CG2 . ILE D  1 32  ? -3.025  -29.014 4.206   1.00 28.96  ? 281  ILE D CG2 1 
ATOM   3545 C  CD1 . ILE D  1 32  ? -3.313  -29.223 7.309   1.00 37.53  ? 281  ILE D CD1 1 
ATOM   3546 N  N   . THR D  1 33  ? -3.013  -26.007 2.834   1.00 30.39  ? 282  THR D N   1 
ATOM   3547 C  CA  . THR D  1 33  ? -3.337  -25.755 1.478   1.00 29.83  ? 282  THR D CA  1 
ATOM   3548 C  C   . THR D  1 33  ? -2.244  -25.003 0.768   1.00 28.92  ? 282  THR D C   1 
ATOM   3549 O  O   . THR D  1 33  ? -1.861  -25.364 -0.361  1.00 29.78  ? 282  THR D O   1 
ATOM   3550 C  CB  . THR D  1 33  ? -4.679  -24.987 1.409   1.00 30.28  ? 282  THR D CB  1 
ATOM   3551 O  OG1 . THR D  1 33  ? -5.717  -25.913 1.741   1.00 33.49  ? 282  THR D OG1 1 
ATOM   3552 C  CG2 . THR D  1 33  ? -4.914  -24.458 0.051   1.00 30.53  ? 282  THR D CG2 1 
ATOM   3553 N  N   . ALA D  1 34  ? -1.772  -23.927 1.384   1.00 28.86  ? 283  ALA D N   1 
ATOM   3554 C  CA  . ALA D  1 34  ? -0.715  -23.111 0.758   1.00 29.95  ? 283  ALA D CA  1 
ATOM   3555 C  C   . ALA D  1 34  ? 0.540   -23.924 0.455   1.00 32.35  ? 283  ALA D C   1 
ATOM   3556 O  O   . ALA D  1 34  ? 1.248   -23.645 -0.534  1.00 34.30  ? 283  ALA D O   1 
ATOM   3557 C  CB  . ALA D  1 34  ? -0.352  -21.944 1.656   1.00 30.57  ? 283  ALA D CB  1 
ATOM   3558 N  N   . CYS D  1 35  ? 0.830   -24.889 1.328   1.00 30.35  ? 284  CYS D N   1 
ATOM   3559 C  CA  . CYS D  1 35  ? 2.006   -25.721 1.173   1.00 33.49  ? 284  CYS D CA  1 
ATOM   3560 C  C   . CYS D  1 35  ? 1.796   -26.741 0.082   1.00 34.38  ? 284  CYS D C   1 
ATOM   3561 O  O   . CYS D  1 35  ? 2.715   -26.996 -0.727  1.00 33.20  ? 284  CYS D O   1 
ATOM   3562 C  CB  . CYS D  1 35  ? 2.374   -26.418 2.500   1.00 32.65  ? 284  CYS D CB  1 
ATOM   3563 S  SG  . CYS D  1 35  ? 3.192   -25.353 3.714   1.00 28.37  ? 284  CYS D SG  1 
ATOM   3564 N  N   . LYS D  1 36  ? 0.585   -27.312 0.028   1.00 34.11  ? 285  LYS D N   1 
ATOM   3565 C  CA  . LYS D  1 36  ? 0.250   -28.231 -1.062  1.00 34.16  ? 285  LYS D CA  1 
ATOM   3566 C  C   . LYS D  1 36  ? 0.360   -27.591 -2.436  1.00 33.85  ? 285  LYS D C   1 
ATOM   3567 O  O   . LYS D  1 36  ? 0.772   -28.250 -3.370  1.00 32.82  ? 285  LYS D O   1 
ATOM   3568 C  CB  . LYS D  1 36  ? -1.125  -28.813 -0.902  1.00 36.35  ? 285  LYS D CB  1 
ATOM   3569 C  CG  . LYS D  1 36  ? -1.150  -29.966 0.060   1.00 39.82  ? 285  LYS D CG  1 
ATOM   3570 C  CD  . LYS D  1 36  ? -2.524  -30.592 0.079   1.00 43.10  ? 285  LYS D CD  1 
ATOM   3571 C  CE  . LYS D  1 36  ? -2.507  -31.873 0.883   1.00 49.17  ? 285  LYS D CE  1 
ATOM   3572 N  NZ  . LYS D  1 36  ? -3.776  -32.040 1.654   1.00 53.73  ? 285  LYS D NZ  1 
ATOM   3573 N  N   . GLU D  1 37  ? 0.042   -26.300 -2.528  1.00 31.60  ? 286  GLU D N   1 
ATOM   3574 C  CA  . GLU D  1 37  ? -0.019  -25.596 -3.789  1.00 35.87  ? 286  GLU D CA  1 
ATOM   3575 C  C   . GLU D  1 37  ? 1.330   -25.305 -4.425  1.00 37.47  ? 286  GLU D C   1 
ATOM   3576 O  O   . GLU D  1 37  ? 1.385   -24.936 -5.598  1.00 36.08  ? 286  GLU D O   1 
ATOM   3577 C  CB  . GLU D  1 37  ? -0.890  -24.335 -3.669  1.00 39.22  ? 286  GLU D CB  1 
ATOM   3578 C  CG  . GLU D  1 37  ? -2.371  -24.768 -3.696  1.00 46.46  ? 286  GLU D CG  1 
ATOM   3579 C  CD  . GLU D  1 37  ? -3.396  -23.640 -3.570  1.00 51.44  ? 286  GLU D CD  1 
ATOM   3580 O  OE1 . GLU D  1 37  ? -4.615  -23.960 -3.637  1.00 55.99  ? 286  GLU D OE1 1 
ATOM   3581 O  OE2 . GLU D  1 37  ? -3.006  -22.468 -3.412  1.00 49.14  ? 286  GLU D OE2 1 
ATOM   3582 N  N   . VAL D  1 38  ? 2.393   -25.468 -3.645  1.00 35.48  ? 287  VAL D N   1 
ATOM   3583 C  CA  . VAL D  1 38  ? 3.756   -25.430 -4.129  1.00 37.10  ? 287  VAL D CA  1 
ATOM   3584 C  C   . VAL D  1 38  ? 4.442   -26.823 -4.019  1.00 35.78  ? 287  VAL D C   1 
ATOM   3585 O  O   . VAL D  1 38  ? 5.662   -26.915 -3.957  1.00 37.30  ? 287  VAL D O   1 
ATOM   3586 C  CB  . VAL D  1 38  ? 4.584   -24.336 -3.378  1.00 37.70  ? 287  VAL D CB  1 
ATOM   3587 C  CG1 . VAL D  1 38  ? 3.917   -22.976 -3.514  1.00 34.42  ? 287  VAL D CG1 1 
ATOM   3588 C  CG2 . VAL D  1 38  ? 4.737   -24.665 -1.884  1.00 40.80  ? 287  VAL D CG2 1 
ATOM   3589 N  N   . GLY D  1 39  ? 3.666   -27.897 -4.009  1.00 35.12  ? 288  GLY D N   1 
ATOM   3590 C  CA  . GLY D  1 39  ? 4.241   -29.264 -3.987  1.00 35.25  ? 288  GLY D CA  1 
ATOM   3591 C  C   . GLY D  1 39  ? 5.003   -29.656 -2.728  1.00 34.09  ? 288  GLY D C   1 
ATOM   3592 O  O   . GLY D  1 39  ? 6.016   -30.349 -2.781  1.00 34.14  ? 288  GLY D O   1 
ATOM   3593 N  N   . ALA D  1 40  ? 4.501   -29.244 -1.573  1.00 32.02  ? 289  ALA D N   1 
ATOM   3594 C  CA  . ALA D  1 40  ? 5.215   -29.426 -0.348  1.00 30.20  ? 289  ALA D CA  1 
ATOM   3595 C  C   . ALA D  1 40  ? 4.226   -29.664 0.788   1.00 31.26  ? 289  ALA D C   1 
ATOM   3596 O  O   . ALA D  1 40  ? 3.027   -29.800 0.591   1.00 29.62  ? 289  ALA D O   1 
ATOM   3597 C  CB  . ALA D  1 40  ? 6.080   -28.195 -0.077  1.00 29.73  ? 289  ALA D CB  1 
ATOM   3598 N  N   . GLN D  1 41  ? 4.727   -29.667 1.995   1.00 29.71  ? 290  GLN D N   1 
ATOM   3599 C  CA  . GLN D  1 41  ? 3.890   -30.068 3.098   1.00 31.46  ? 290  GLN D CA  1 
ATOM   3600 C  C   . GLN D  1 41  ? 4.117   -29.185 4.314   1.00 28.64  ? 290  GLN D C   1 
ATOM   3601 O  O   . GLN D  1 41  ? 5.259   -28.904 4.665   1.00 28.95  ? 290  GLN D O   1 
ATOM   3602 C  CB  . GLN D  1 41  ? 4.214   -31.515 3.404   1.00 30.65  ? 290  GLN D CB  1 
ATOM   3603 C  CG  . GLN D  1 41  ? 3.277   -32.178 4.399   1.00 33.69  ? 290  GLN D CG  1 
ATOM   3604 C  CD  . GLN D  1 41  ? 3.680   -33.632 4.594   1.00 34.85  ? 290  GLN D CD  1 
ATOM   3605 O  OE1 . GLN D  1 41  ? 4.766   -33.918 5.143   1.00 34.65  ? 290  GLN D OE1 1 
ATOM   3606 N  NE2 . GLN D  1 41  ? 2.857   -34.553 4.089   1.00 31.82  ? 290  GLN D NE2 1 
ATOM   3607 N  N   . LEU D  1 42  ? 3.039   -28.793 4.997   1.00 27.88  ? 291  LEU D N   1 
ATOM   3608 C  CA  . LEU D  1 42  ? 3.175   -28.045 6.271   1.00 26.21  ? 291  LEU D CA  1 
ATOM   3609 C  C   . LEU D  1 42  ? 4.124   -28.829 7.132   1.00 24.38  ? 291  LEU D C   1 
ATOM   3610 O  O   . LEU D  1 42  ? 3.954   -30.022 7.272   1.00 22.54  ? 291  LEU D O   1 
ATOM   3611 C  CB  . LEU D  1 42  ? 1.812   -27.857 6.977   1.00 26.66  ? 291  LEU D CB  1 
ATOM   3612 C  CG  . LEU D  1 42  ? 1.760   -26.966 8.227   1.00 28.23  ? 291  LEU D CG  1 
ATOM   3613 C  CD1 . LEU D  1 42  ? 2.349   -25.597 7.904   1.00 28.88  ? 291  LEU D CD1 1 
ATOM   3614 C  CD2 . LEU D  1 42  ? 0.324   -26.801 8.766   1.00 27.19  ? 291  LEU D CD2 1 
ATOM   3615 N  N   . VAL D  1 43  ? 5.128   -28.168 7.694   1.00 26.55  ? 292  VAL D N   1 
ATOM   3616 C  CA  . VAL D  1 43  ? 6.352   -28.879 8.132   1.00 26.15  ? 292  VAL D CA  1 
ATOM   3617 C  C   . VAL D  1 43  ? 6.125   -30.047 9.121   1.00 28.28  ? 292  VAL D C   1 
ATOM   3618 O  O   . VAL D  1 43  ? 5.486   -29.905 10.198  1.00 27.01  ? 292  VAL D O   1 
ATOM   3619 C  CB  . VAL D  1 43  ? 7.420   -27.877 8.667   1.00 26.81  ? 292  VAL D CB  1 
ATOM   3620 C  CG1 . VAL D  1 43  ? 6.953   -27.209 9.959   1.00 28.14  ? 292  VAL D CG1 1 
ATOM   3621 C  CG2 . VAL D  1 43  ? 8.740   -28.600 8.931   1.00 25.17  ? 292  VAL D CG2 1 
ATOM   3622 N  N   . VAL D  1 44  ? 6.658   -31.210 8.756   1.00 27.04  ? 293  VAL D N   1 
ATOM   3623 C  CA  . VAL D  1 44  ? 6.691   -32.367 9.631   1.00 27.02  ? 293  VAL D CA  1 
ATOM   3624 C  C   . VAL D  1 44  ? 8.119   -32.539 10.116  1.00 27.85  ? 293  VAL D C   1 
ATOM   3625 O  O   . VAL D  1 44  ? 9.046   -32.636 9.329   1.00 27.33  ? 293  VAL D O   1 
ATOM   3626 C  CB  . VAL D  1 44  ? 6.152   -33.602 8.892   1.00 28.65  ? 293  VAL D CB  1 
ATOM   3627 C  CG1 . VAL D  1 44  ? 6.313   -34.872 9.703   1.00 29.66  ? 293  VAL D CG1 1 
ATOM   3628 C  CG2 . VAL D  1 44  ? 4.690   -33.383 8.584   1.00 28.28  ? 293  VAL D CG2 1 
ATOM   3629 N  N   . ILE D  1 45  ? 8.297   -32.531 11.429  1.00 28.47  ? 294  ILE D N   1 
ATOM   3630 C  CA  . ILE D  1 45  ? 9.618   -32.582 12.034  1.00 29.74  ? 294  ILE D CA  1 
ATOM   3631 C  C   . ILE D  1 45  ? 10.025  -34.032 12.298  1.00 33.35  ? 294  ILE D C   1 
ATOM   3632 O  O   . ILE D  1 45  ? 9.339   -34.749 13.011  1.00 35.60  ? 294  ILE D O   1 
ATOM   3633 C  CB  . ILE D  1 45  ? 9.661   -31.804 13.371  1.00 28.03  ? 294  ILE D CB  1 
ATOM   3634 C  CG1 . ILE D  1 45  ? 9.233   -30.351 13.158  1.00 26.73  ? 294  ILE D CG1 1 
ATOM   3635 C  CG2 . ILE D  1 45  ? 11.068  -31.815 13.935  1.00 31.59  ? 294  ILE D CG2 1 
ATOM   3636 C  CD1 . ILE D  1 45  ? 9.084   -29.562 14.422  1.00 25.98  ? 294  ILE D CD1 1 
ATOM   3637 N  N   . LYS D  1 46  ? 11.163  -34.445 11.768  1.00 34.63  ? 295  LYS D N   1 
ATOM   3638 C  CA  . LYS D  1 46  ? 11.605  -35.847 11.926  1.00 38.18  ? 295  LYS D CA  1 
ATOM   3639 C  C   . LYS D  1 46  ? 12.802  -36.055 12.830  1.00 35.20  ? 295  LYS D C   1 
ATOM   3640 O  O   . LYS D  1 46  ? 13.083  -37.181 13.179  1.00 42.31  ? 295  LYS D O   1 
ATOM   3641 C  CB  . LYS D  1 46  ? 11.975  -36.435 10.587  1.00 38.14  ? 295  LYS D CB  1 
ATOM   3642 C  CG  . LYS D  1 46  ? 10.852  -36.461 9.589   1.00 39.30  ? 295  LYS D CG  1 
ATOM   3643 C  CD  . LYS D  1 46  ? 9.918   -37.601 9.876   1.00 38.74  ? 295  LYS D CD  1 
ATOM   3644 C  CE  . LYS D  1 46  ? 8.829   -37.604 8.809   1.00 37.57  ? 295  LYS D CE  1 
ATOM   3645 N  NZ  . LYS D  1 46  ? 7.546   -38.025 9.415   1.00 34.93  ? 295  LYS D NZ  1 
ATOM   3646 N  N   . SER D  1 47  ? 13.519  -35.002 13.184  1.00 32.00  ? 296  SER D N   1 
ATOM   3647 C  CA  . SER D  1 47  ? 14.674  -35.133 14.061  1.00 32.76  ? 296  SER D CA  1 
ATOM   3648 C  C   . SER D  1 47  ? 14.897  -33.906 14.973  1.00 32.70  ? 296  SER D C   1 
ATOM   3649 O  O   . SER D  1 47  ? 14.425  -32.817 14.701  1.00 32.96  ? 296  SER D O   1 
ATOM   3650 C  CB  . SER D  1 47  ? 15.924  -35.343 13.217  1.00 31.48  ? 296  SER D CB  1 
ATOM   3651 O  OG  . SER D  1 47  ? 16.226  -34.118 12.561  1.00 31.70  ? 296  SER D OG  1 
ATOM   3652 N  N   . ALA D  1 48  ? 15.686  -34.127 16.022  1.00 33.58  ? 297  ALA D N   1 
ATOM   3653 C  CA  . ALA D  1 48  ? 16.137  -33.105 16.983  1.00 33.87  ? 297  ALA D CA  1 
ATOM   3654 C  C   . ALA D  1 48  ? 16.853  -31.910 16.348  1.00 32.58  ? 297  ALA D C   1 
ATOM   3655 O  O   . ALA D  1 48  ? 16.631  -30.820 16.766  1.00 28.04  ? 297  ALA D O   1 
ATOM   3656 C  CB  . ALA D  1 48  ? 17.057  -33.741 18.047  1.00 32.32  ? 297  ALA D CB  1 
ATOM   3657 N  N   . GLU D  1 49  ? 17.715  -32.157 15.352  1.00 33.92  ? 298  GLU D N   1 
ATOM   3658 C  CA  A GLU D  1 49  ? 18.450  -31.134 14.644  0.70 34.70  ? 298  GLU D CA  1 
ATOM   3659 C  CA  B GLU D  1 49  ? 18.449  -31.088 14.691  0.30 34.26  ? 298  GLU D CA  1 
ATOM   3660 C  C   . GLU D  1 49  ? 17.502  -30.211 13.882  1.00 33.04  ? 298  GLU D C   1 
ATOM   3661 O  O   . GLU D  1 49  ? 17.684  -28.960 13.827  1.00 30.01  ? 298  GLU D O   1 
ATOM   3662 C  CB  A GLU D  1 49  ? 19.400  -31.804 13.617  0.70 40.12  ? 298  GLU D CB  1 
ATOM   3663 C  CB  B GLU D  1 49  ? 19.539  -31.645 13.760  0.30 37.64  ? 298  GLU D CB  1 
ATOM   3664 C  CG  A GLU D  1 49  ? 20.629  -32.539 14.198  0.70 47.20  ? 298  GLU D CG  1 
ATOM   3665 C  CG  B GLU D  1 49  ? 20.631  -32.463 14.450  0.30 41.25  ? 298  GLU D CG  1 
ATOM   3666 C  CD  A GLU D  1 49  ? 20.313  -33.796 15.035  0.70 45.88  ? 298  GLU D CD  1 
ATOM   3667 C  CD  B GLU D  1 49  ? 21.207  -31.794 15.684  0.30 41.69  ? 298  GLU D CD  1 
ATOM   3668 O  OE1 A GLU D  1 49  ? 19.307  -34.496 14.779  0.70 42.42  ? 298  GLU D OE1 1 
ATOM   3669 O  OE1 B GLU D  1 49  ? 22.414  -31.481 15.682  0.30 43.04  ? 298  GLU D OE1 1 
ATOM   3670 O  OE2 A GLU D  1 49  ? 21.094  -34.075 15.961  0.70 44.47  ? 298  GLU D OE2 1 
ATOM   3671 O  OE2 B GLU D  1 49  ? 20.450  -31.584 16.658  0.30 41.77  ? 298  GLU D OE2 1 
ATOM   3672 N  N   . GLU D  1 50  ? 16.533  -30.855 13.226  1.00 30.76  ? 299  GLU D N   1 
ATOM   3673 C  CA  . GLU D  1 50  ? 15.484  -30.171 12.448  1.00 29.92  ? 299  GLU D CA  1 
ATOM   3674 C  C   . GLU D  1 50  ? 14.574  -29.318 13.371  1.00 28.29  ? 299  GLU D C   1 
ATOM   3675 O  O   . GLU D  1 50  ? 14.277  -28.146 13.068  1.00 28.83  ? 299  GLU D O   1 
ATOM   3676 C  CB  . GLU D  1 50  ? 14.673  -31.182 11.646  1.00 30.51  ? 299  GLU D CB  1 
ATOM   3677 C  CG  . GLU D  1 50  ? 13.716  -30.523 10.675  1.00 32.85  ? 299  GLU D CG  1 
ATOM   3678 C  CD  . GLU D  1 50  ? 12.876  -31.522 9.935   1.00 33.66  ? 299  GLU D CD  1 
ATOM   3679 O  OE1 . GLU D  1 50  ? 12.269  -31.130 8.929   1.00 32.03  ? 299  GLU D OE1 1 
ATOM   3680 O  OE2 . GLU D  1 50  ? 12.847  -32.699 10.359  1.00 33.62  ? 299  GLU D OE2 1 
ATOM   3681 N  N   . GLN D  1 51  ? 14.189  -29.878 14.505  1.00 27.25  ? 300  GLN D N   1 
ATOM   3682 C  CA  . GLN D  1 51  ? 13.494  -29.090 15.532  1.00 29.70  ? 300  GLN D CA  1 
ATOM   3683 C  C   . GLN D  1 51  ? 14.332  -27.903 15.956  1.00 30.21  ? 300  GLN D C   1 
ATOM   3684 O  O   . GLN D  1 51  ? 13.836  -26.806 16.124  1.00 28.78  ? 300  GLN D O   1 
ATOM   3685 C  CB  . GLN D  1 51  ? 13.159  -29.962 16.758  1.00 29.58  ? 300  GLN D CB  1 
ATOM   3686 C  CG  . GLN D  1 51  ? 12.966  -29.247 18.114  1.00 30.17  ? 300  GLN D CG  1 
ATOM   3687 C  CD  . GLN D  1 51  ? 11.880  -28.203 18.112  1.00 31.46  ? 300  GLN D CD  1 
ATOM   3688 O  OE1 . GLN D  1 51  ? 11.011  -28.204 17.248  1.00 36.68  ? 300  GLN D OE1 1 
ATOM   3689 N  NE2 . GLN D  1 51  ? 11.928  -27.292 19.067  1.00 33.15  ? 300  GLN D NE2 1 
ATOM   3690 N  N   . ASN D  1 52  ? 15.613  -28.118 16.194  1.00 31.66  ? 301  ASN D N   1 
ATOM   3691 C  CA  A ASN D  1 52  ? 16.451  -27.035 16.705  0.50 31.34  ? 301  ASN D CA  1 
ATOM   3692 C  CA  B ASN D  1 52  ? 16.439  -27.037 16.684  0.50 31.71  ? 301  ASN D CA  1 
ATOM   3693 C  C   . ASN D  1 52  ? 16.486  -25.903 15.671  1.00 30.73  ? 301  ASN D C   1 
ATOM   3694 O  O   . ASN D  1 52  ? 16.336  -24.734 16.007  1.00 29.72  ? 301  ASN D O   1 
ATOM   3695 C  CB  A ASN D  1 52  ? 17.868  -27.536 17.067  0.50 33.85  ? 301  ASN D CB  1 
ATOM   3696 C  CB  B ASN D  1 52  ? 17.846  -27.532 16.976  0.50 34.81  ? 301  ASN D CB  1 
ATOM   3697 C  CG  A ASN D  1 52  ? 17.870  -28.539 18.221  0.50 33.89  ? 301  ASN D CG  1 
ATOM   3698 C  CG  B ASN D  1 52  ? 18.700  -26.454 17.561  0.50 35.84  ? 301  ASN D CG  1 
ATOM   3699 O  OD1 A ASN D  1 52  ? 16.921  -28.596 19.015  0.50 36.22  ? 301  ASN D OD1 1 
ATOM   3700 O  OD1 B ASN D  1 52  ? 19.620  -25.956 16.910  0.50 38.59  ? 301  ASN D OD1 1 
ATOM   3701 N  ND2 A ASN D  1 52  ? 18.941  -29.343 18.315  0.50 33.16  ? 301  ASN D ND2 1 
ATOM   3702 N  ND2 B ASN D  1 52  ? 18.351  -26.029 18.770  0.50 32.47  ? 301  ASN D ND2 1 
ATOM   3703 N  N   . PHE D  1 53  ? 16.662  -26.259 14.412  1.00 29.41  ? 302  PHE D N   1 
ATOM   3704 C  CA  . PHE D  1 53  ? 16.752  -25.291 13.347  1.00 28.95  ? 302  PHE D CA  1 
ATOM   3705 C  C   . PHE D  1 53  ? 15.457  -24.509 13.190  1.00 29.00  ? 302  PHE D C   1 
ATOM   3706 O  O   . PHE D  1 53  ? 15.483  -23.296 13.063  1.00 27.16  ? 302  PHE D O   1 
ATOM   3707 C  CB  . PHE D  1 53  ? 17.077  -26.030 12.057  1.00 31.34  ? 302  PHE D CB  1 
ATOM   3708 C  CG  . PHE D  1 53  ? 16.828  -25.241 10.823  1.00 32.40  ? 302  PHE D CG  1 
ATOM   3709 C  CD1 . PHE D  1 53  ? 17.650  -24.178 10.498  1.00 34.27  ? 302  PHE D CD1 1 
ATOM   3710 C  CD2 . PHE D  1 53  ? 15.794  -25.587 9.963   1.00 34.40  ? 302  PHE D CD2 1 
ATOM   3711 C  CE1 . PHE D  1 53  ? 17.440  -23.464 9.326   1.00 35.85  ? 302  PHE D CE1 1 
ATOM   3712 C  CE2 . PHE D  1 53  ? 15.578  -24.877 8.785   1.00 34.76  ? 302  PHE D CE2 1 
ATOM   3713 C  CZ  . PHE D  1 53  ? 16.411  -23.812 8.471   1.00 33.46  ? 302  PHE D CZ  1 
ATOM   3714 N  N   . LEU D  1 54  ? 14.329  -25.199 13.244  1.00 25.53  ? 303  LEU D N   1 
ATOM   3715 C  CA  . LEU D  1 54  ? 13.055  -24.558 13.025  1.00 28.58  ? 303  LEU D CA  1 
ATOM   3716 C  C   . LEU D  1 54  ? 12.648  -23.668 14.187  1.00 28.83  ? 303  LEU D C   1 
ATOM   3717 O  O   . LEU D  1 54  ? 12.151  -22.554 13.957  1.00 29.78  ? 303  LEU D O   1 
ATOM   3718 C  CB  . LEU D  1 54  ? 11.960  -25.582 12.744  1.00 28.77  ? 303  LEU D CB  1 
ATOM   3719 C  CG  . LEU D  1 54  ? 12.179  -26.392 11.458  1.00 30.96  ? 303  LEU D CG  1 
ATOM   3720 C  CD1 . LEU D  1 54  ? 11.253  -27.605 11.455  1.00 31.64  ? 303  LEU D CD1 1 
ATOM   3721 C  CD2 . LEU D  1 54  ? 11.976  -25.538 10.217  1.00 30.69  ? 303  LEU D CD2 1 
ATOM   3722 N  N   . GLN D  1 55  ? 12.829  -24.184 15.408  1.00 30.47  ? 304  GLN D N   1 
ATOM   3723 C  CA  . GLN D  1 55  ? 12.559  -23.442 16.635  1.00 31.26  ? 304  GLN D CA  1 
ATOM   3724 C  C   . GLN D  1 55  ? 13.339  -22.130 16.655  1.00 35.68  ? 304  GLN D C   1 
ATOM   3725 O  O   . GLN D  1 55  ? 12.807  -21.098 17.072  1.00 32.34  ? 304  GLN D O   1 
ATOM   3726 C  CB  . GLN D  1 55  ? 12.941  -24.236 17.860  1.00 28.91  ? 304  GLN D CB  1 
ATOM   3727 C  CG  . GLN D  1 55  ? 12.381  -23.630 19.142  1.00 27.75  ? 304  GLN D CG  1 
ATOM   3728 C  CD  . GLN D  1 55  ? 10.876  -23.739 19.185  1.00 27.12  ? 304  GLN D CD  1 
ATOM   3729 O  OE1 . GLN D  1 55  ? 10.346  -24.828 19.109  1.00 27.35  ? 304  GLN D OE1 1 
ATOM   3730 N  NE2 . GLN D  1 55  ? 10.188  -22.620 19.352  1.00 28.64  ? 304  GLN D NE2 1 
ATOM   3731 N  N   . LEU D  1 56  ? 14.576  -22.179 16.168  1.00 39.16  ? 305  LEU D N   1 
ATOM   3732 C  CA  . LEU D  1 56  ? 15.416  -20.995 16.116  1.00 46.10  ? 305  LEU D CA  1 
ATOM   3733 C  C   . LEU D  1 56  ? 14.965  -19.972 15.075  1.00 40.85  ? 305  LEU D C   1 
ATOM   3734 O  O   . LEU D  1 56  ? 14.952  -18.800 15.395  1.00 45.33  ? 305  LEU D O   1 
ATOM   3735 C  CB  . LEU D  1 56  ? 16.920  -21.355 16.053  1.00 52.60  ? 305  LEU D CB  1 
ATOM   3736 C  CG  . LEU D  1 56  ? 17.311  -22.120 17.354  1.00 60.37  ? 305  LEU D CG  1 
ATOM   3737 C  CD1 . LEU D  1 56  ? 18.722  -22.704 17.277  1.00 65.93  ? 305  LEU D CD1 1 
ATOM   3738 C  CD2 . LEU D  1 56  ? 17.127  -21.327 18.665  1.00 59.83  ? 305  LEU D CD2 1 
ATOM   3739 N  N   . GLN D  1 57  ? 14.509  -20.387 13.898  1.00 42.38  ? 306  GLN D N   1 
ATOM   3740 C  CA  . GLN D  1 57  ? 13.849  -19.438 12.966  1.00 44.09  ? 306  GLN D CA  1 
ATOM   3741 C  C   . GLN D  1 57  ? 12.758  -18.652 13.681  1.00 41.96  ? 306  GLN D C   1 
ATOM   3742 O  O   . GLN D  1 57  ? 12.679  -17.435 13.543  1.00 36.99  ? 306  GLN D O   1 
ATOM   3743 C  CB  . GLN D  1 57  ? 13.152  -20.105 11.783  1.00 47.52  ? 306  GLN D CB  1 
ATOM   3744 C  CG  . GLN D  1 57  ? 14.004  -20.996 10.906  1.00 55.01  ? 306  GLN D CG  1 
ATOM   3745 C  CD  . GLN D  1 57  ? 15.029  -20.234 10.092  1.00 61.02  ? 306  GLN D CD  1 
ATOM   3746 O  OE1 . GLN D  1 57  ? 14.678  -19.406 9.242   1.00 71.10  ? 306  GLN D OE1 1 
ATOM   3747 N  NE2 . GLN D  1 57  ? 16.307  -20.519 10.334  1.00 60.63  ? 306  GLN D NE2 1 
ATOM   3748 N  N   . SER D  1 58  ? 11.907  -19.357 14.427  1.00 37.88  ? 307  SER D N   1 
ATOM   3749 C  CA  . SER D  1 58  ? 10.724  -18.721 15.023  1.00 41.59  ? 307  SER D CA  1 
ATOM   3750 C  C   . SER D  1 58  ? 11.073  -17.850 16.181  1.00 34.91  ? 307  SER D C   1 
ATOM   3751 O  O   . SER D  1 58  ? 10.552  -16.766 16.272  1.00 37.27  ? 307  SER D O   1 
ATOM   3752 C  CB  . SER D  1 58  ? 9.671   -19.728 15.481  1.00 44.50  ? 307  SER D CB  1 
ATOM   3753 O  OG  . SER D  1 58  ? 9.170   -20.408 14.361  1.00 58.91  ? 307  SER D OG  1 
ATOM   3754 N  N   . SER D  1 59  ? 11.956  -18.315 17.052  1.00 35.43  ? 308  SER D N   1 
ATOM   3755 C  CA  . SER D  1 59  ? 12.344  -17.542 18.216  1.00 39.84  ? 308  SER D CA  1 
ATOM   3756 C  C   . SER D  1 59  ? 13.106  -16.255 17.801  1.00 41.55  ? 308  SER D C   1 
ATOM   3757 O  O   . SER D  1 59  ? 12.808  -15.171 18.289  1.00 40.78  ? 308  SER D O   1 
ATOM   3758 C  CB  . SER D  1 59  ? 13.173  -18.400 19.173  1.00 39.15  ? 308  SER D CB  1 
ATOM   3759 O  OG  . SER D  1 59  ? 14.436  -18.711 18.619  1.00 40.66  ? 308  SER D OG  1 
ATOM   3760 N  N   . ARG D  1 60  ? 14.039  -16.387 16.868  1.00 42.16  ? 309  ARG D N   1 
ATOM   3761 C  CA  . ARG D  1 60  ? 14.825  -15.240 16.336  1.00 46.11  ? 309  ARG D CA  1 
ATOM   3762 C  C   . ARG D  1 60  ? 13.930  -14.214 15.620  1.00 42.66  ? 309  ARG D C   1 
ATOM   3763 O  O   . ARG D  1 60  ? 14.099  -13.009 15.737  1.00 45.34  ? 309  ARG D O   1 
ATOM   3764 C  CB  . ARG D  1 60  ? 15.910  -15.765 15.358  1.00 49.31  ? 309  ARG D CB  1 
ATOM   3765 C  CG  . ARG D  1 60  ? 17.144  -14.895 15.260  1.00 61.80  ? 309  ARG D CG  1 
ATOM   3766 C  CD  . ARG D  1 60  ? 18.306  -15.596 14.554  1.00 64.30  ? 309  ARG D CD  1 
ATOM   3767 N  NE  . ARG D  1 60  ? 18.387  -15.236 13.130  1.00 68.90  ? 309  ARG D NE  1 
ATOM   3768 C  CZ  . ARG D  1 60  ? 19.126  -14.237 12.606  1.00 66.00  ? 309  ARG D CZ  1 
ATOM   3769 N  NH1 . ARG D  1 60  ? 19.888  -13.435 13.356  1.00 59.54  ? 309  ARG D NH1 1 
ATOM   3770 N  NH2 . ARG D  1 60  ? 19.097  -14.031 11.296  1.00 66.11  ? 309  ARG D NH2 1 
ATOM   3771 N  N   . SER D  1 61  ? 12.980  -14.714 14.849  1.00 42.72  ? 310  SER D N   1 
ATOM   3772 C  CA  . SER D  1 61  ? 12.085  -13.857 14.118  1.00 39.58  ? 310  SER D CA  1 
ATOM   3773 C  C   . SER D  1 61  ? 10.885  -13.421 14.954  1.00 38.04  ? 310  SER D C   1 
ATOM   3774 O  O   . SER D  1 61  ? 10.096  -12.637 14.459  1.00 37.68  ? 310  SER D O   1 
ATOM   3775 C  CB  . SER D  1 61  ? 11.598  -14.572 12.860  1.00 42.44  ? 310  SER D CB  1 
ATOM   3776 O  OG  . SER D  1 61  ? 10.601  -15.545 13.156  1.00 45.08  ? 310  SER D OG  1 
ATOM   3777 N  N   . ASN D  1 62  ? 10.774  -13.922 16.199  1.00 37.25  ? 311  ASN D N   1 
ATOM   3778 C  CA  A ASN D  1 62  ? 9.608   -13.654 17.028  0.50 36.68  ? 311  ASN D CA  1 
ATOM   3779 C  CA  B ASN D  1 62  ? 9.590   -13.791 17.090  0.50 37.46  ? 311  ASN D CA  1 
ATOM   3780 C  C   . ASN D  1 62  ? 8.269   -13.800 16.285  1.00 37.44  ? 311  ASN D C   1 
ATOM   3781 O  O   . ASN D  1 62  ? 7.352   -13.021 16.486  1.00 43.21  ? 311  ASN D O   1 
ATOM   3782 C  CB  A ASN D  1 62  ? 9.748   -12.251 17.601  0.50 34.80  ? 311  ASN D CB  1 
ATOM   3783 C  CB  B ASN D  1 62  ? 9.713   -12.612 18.093  0.50 36.17  ? 311  ASN D CB  1 
ATOM   3784 C  CG  A ASN D  1 62  ? 11.006  -12.104 18.399  0.50 33.04  ? 311  ASN D CG  1 
ATOM   3785 C  CG  B ASN D  1 62  ? 8.821   -12.781 19.348  0.50 36.37  ? 311  ASN D CG  1 
ATOM   3786 O  OD1 A ASN D  1 62  ? 11.237  -12.879 19.307  0.50 32.67  ? 311  ASN D OD1 1 
ATOM   3787 O  OD1 B ASN D  1 62  ? 8.722   -13.857 19.926  0.50 37.16  ? 311  ASN D OD1 1 
ATOM   3788 N  ND2 A ASN D  1 62  ? 11.851  -11.148 18.034  0.50 32.73  ? 311  ASN D ND2 1 
ATOM   3789 N  ND2 B ASN D  1 62  ? 8.190   -11.702 19.772  0.50 36.38  ? 311  ASN D ND2 1 
ATOM   3790 N  N   . ARG D  1 63  ? 8.165   -14.757 15.388  1.00 37.84  ? 312  ARG D N   1 
ATOM   3791 C  CA  . ARG D  1 63  ? 6.906   -15.035 14.742  1.00 40.97  ? 312  ARG D CA  1 
ATOM   3792 C  C   . ARG D  1 63  ? 6.360   -16.365 15.299  1.00 39.72  ? 312  ARG D C   1 
ATOM   3793 O  O   . ARG D  1 63  ? 7.118   -17.341 15.473  1.00 41.12  ? 312  ARG D O   1 
ATOM   3794 C  CB  . ARG D  1 63  ? 7.091   -15.135 13.226  1.00 47.58  ? 312  ARG D CB  1 
ATOM   3795 C  CG  . ARG D  1 63  ? 7.593   -13.852 12.535  1.00 52.70  ? 312  ARG D CG  1 
ATOM   3796 C  CD  . ARG D  1 63  ? 6.889   -12.572 12.999  1.00 55.78  ? 312  ARG D CD  1 
ATOM   3797 N  NE  . ARG D  1 63  ? 7.264   -11.365 12.240  1.00 51.95  ? 312  ARG D NE  1 
ATOM   3798 C  CZ  . ARG D  1 63  ? 6.633   -10.184 12.319  1.00 53.54  ? 312  ARG D CZ  1 
ATOM   3799 N  NH1 . ARG D  1 63  ? 7.075   -9.137  11.597  1.00 51.94  ? 312  ARG D NH1 1 
ATOM   3800 N  NH2 . ARG D  1 63  ? 5.577   -10.023 13.132  1.00 47.48  ? 312  ARG D NH2 1 
ATOM   3801 N  N   . PHE D  1 64  ? 5.061   -16.380 15.594  1.00 32.10  ? 313  PHE D N   1 
ATOM   3802 C  CA  . PHE D  1 64  ? 4.325   -17.625 15.810  1.00 32.27  ? 313  PHE D CA  1 
ATOM   3803 C  C   . PHE D  1 64  ? 4.090   -18.342 14.492  1.00 27.97  ? 313  PHE D C   1 
ATOM   3804 O  O   . PHE D  1 64  ? 3.626   -17.757 13.524  1.00 28.10  ? 313  PHE D O   1 
ATOM   3805 C  CB  . PHE D  1 64  ? 2.958   -17.387 16.474  1.00 32.09  ? 313  PHE D CB  1 
ATOM   3806 C  CG  . PHE D  1 64  ? 3.024   -16.621 17.759  1.00 30.03  ? 313  PHE D CG  1 
ATOM   3807 C  CD1 . PHE D  1 64  ? 4.065   -16.815 18.646  1.00 30.67  ? 313  PHE D CD1 1 
ATOM   3808 C  CD2 . PHE D  1 64  ? 2.031   -15.678 18.071  1.00 31.51  ? 313  PHE D CD2 1 
ATOM   3809 C  CE1 . PHE D  1 64  ? 4.131   -16.098 19.838  1.00 32.11  ? 313  PHE D CE1 1 
ATOM   3810 C  CE2 . PHE D  1 64  ? 2.110   -14.946 19.251  1.00 30.75  ? 313  PHE D CE2 1 
ATOM   3811 C  CZ  . PHE D  1 64  ? 3.160   -15.162 20.128  1.00 28.92  ? 313  PHE D CZ  1 
ATOM   3812 N  N   . THR D  1 65  ? 4.373   -19.629 14.468  1.00 27.83  ? 314  THR D N   1 
ATOM   3813 C  CA  . THR D  1 65  ? 4.417   -20.337 13.202  1.00 27.34  ? 314  THR D CA  1 
ATOM   3814 C  C   . THR D  1 65  ? 3.827   -21.718 13.373  1.00 24.46  ? 314  THR D C   1 
ATOM   3815 O  O   . THR D  1 65  ? 4.230   -22.442 14.212  1.00 23.94  ? 314  THR D O   1 
ATOM   3816 C  CB  . THR D  1 65  ? 5.887   -20.466 12.708  1.00 30.28  ? 314  THR D CB  1 
ATOM   3817 O  OG1 . THR D  1 65  ? 6.484   -19.178 12.637  1.00 27.71  ? 314  THR D OG1 1 
ATOM   3818 C  CG2 . THR D  1 65  ? 5.989   -21.170 11.283  1.00 28.47  ? 314  THR D CG2 1 
ATOM   3819 N  N   . TRP D  1 66  ? 2.876   -22.061 12.515  1.00 25.84  ? 315  TRP D N   1 
ATOM   3820 C  CA  . TRP D  1 66  ? 2.289   -23.387 12.437  1.00 24.30  ? 315  TRP D CA  1 
ATOM   3821 C  C   . TRP D  1 66  ? 3.272   -24.448 11.959  1.00 24.93  ? 315  TRP D C   1 
ATOM   3822 O  O   . TRP D  1 66  ? 4.060   -24.209 11.058  1.00 25.19  ? 315  TRP D O   1 
ATOM   3823 C  CB  . TRP D  1 66  ? 1.175   -23.382 11.384  1.00 24.76  ? 315  TRP D CB  1 
ATOM   3824 C  CG  . TRP D  1 66  ? -0.042  -22.630 11.680  1.00 23.82  ? 315  TRP D CG  1 
ATOM   3825 C  CD1 . TRP D  1 66  ? -0.646  -21.735 10.890  1.00 23.00  ? 315  TRP D CD1 1 
ATOM   3826 C  CD2 . TRP D  1 66  ? -0.824  -22.720 12.862  1.00 23.81  ? 315  TRP D CD2 1 
ATOM   3827 N  NE1 . TRP D  1 66  ? -1.772  -21.241 11.482  1.00 23.47  ? 315  TRP D NE1 1 
ATOM   3828 C  CE2 . TRP D  1 66  ? -1.907  -21.836 12.711  1.00 23.90  ? 315  TRP D CE2 1 
ATOM   3829 C  CE3 . TRP D  1 66  ? -0.700  -23.431 14.041  1.00 23.38  ? 315  TRP D CE3 1 
ATOM   3830 C  CZ2 . TRP D  1 66  ? -2.894  -21.675 13.696  1.00 23.54  ? 315  TRP D CZ2 1 
ATOM   3831 C  CZ3 . TRP D  1 66  ? -1.699  -23.282 15.020  1.00 25.74  ? 315  TRP D CZ3 1 
ATOM   3832 C  CH2 . TRP D  1 66  ? -2.774  -22.392 14.827  1.00 23.77  ? 315  TRP D CH2 1 
ATOM   3833 N  N   . MET D  1 67  ? 3.133   -25.643 12.502  1.00 25.60  ? 316  MET D N   1 
ATOM   3834 C  CA  . MET D  1 67  ? 3.790   -26.826 11.954  1.00 25.61  ? 316  MET D CA  1 
ATOM   3835 C  C   . MET D  1 67  ? 2.691   -27.840 11.647  1.00 26.88  ? 316  MET D C   1 
ATOM   3836 O  O   . MET D  1 67  ? 1.527   -27.658 12.015  1.00 27.37  ? 316  MET D O   1 
ATOM   3837 C  CB  . MET D  1 67  ? 4.823   -27.380 12.953  1.00 25.64  ? 316  MET D CB  1 
ATOM   3838 C  CG  . MET D  1 67  ? 4.227   -28.088 14.181  1.00 26.00  ? 316  MET D CG  1 
ATOM   3839 S  SD  . MET D  1 67  ? 5.404   -28.476 15.503  1.00 28.56  ? 316  MET D SD  1 
ATOM   3840 C  CE  . MET D  1 67  ? 5.689   -26.843 16.219  1.00 26.67  ? 316  MET D CE  1 
ATOM   3841 N  N   . GLY D  1 68  ? 3.049   -28.923 10.988  1.00 24.47  ? 317  GLY D N   1 
ATOM   3842 C  CA  . GLY D  1 68  ? 2.060   -29.808 10.439  1.00 23.91  ? 317  GLY D CA  1 
ATOM   3843 C  C   . GLY D  1 68  ? 1.715   -30.836 11.482  1.00 23.71  ? 317  GLY D C   1 
ATOM   3844 O  O   . GLY D  1 68  ? 1.946   -32.031 11.281  1.00 22.36  ? 317  GLY D O   1 
ATOM   3845 N  N   . LEU D  1 69  ? 1.160   -30.362 12.602  1.00 23.95  ? 318  LEU D N   1 
ATOM   3846 C  CA  . LEU D  1 69  ? 0.903   -31.224 13.729  1.00 24.36  ? 318  LEU D CA  1 
ATOM   3847 C  C   . LEU D  1 69  ? -0.389  -30.828 14.373  1.00 25.68  ? 318  LEU D C   1 
ATOM   3848 O  O   . LEU D  1 69  ? -0.570  -29.648 14.702  1.00 21.73  ? 318  LEU D O   1 
ATOM   3849 C  CB  . LEU D  1 69  ? 2.038   -31.114 14.712  1.00 25.78  ? 318  LEU D CB  1 
ATOM   3850 C  CG  . LEU D  1 69  ? 1.979   -31.904 16.024  1.00 28.77  ? 318  LEU D CG  1 
ATOM   3851 C  CD1 . LEU D  1 69  ? 1.992   -33.424 15.800  1.00 28.37  ? 318  LEU D CD1 1 
ATOM   3852 C  CD2 . LEU D  1 69  ? 3.178   -31.495 16.899  1.00 28.88  ? 318  LEU D CD2 1 
ATOM   3853 N  N   . SER D  1 70  ? -1.292  -31.807 14.538  1.00 27.79  ? 319  SER D N   1 
ATOM   3854 C  CA  . SER D  1 70  ? -2.590  -31.577 15.166  1.00 27.06  ? 319  SER D CA  1 
ATOM   3855 C  C   . SER D  1 70  ? -3.076  -32.693 16.091  1.00 30.50  ? 319  SER D C   1 
ATOM   3856 O  O   . SER D  1 70  ? -2.650  -33.847 15.957  1.00 27.62  ? 319  SER D O   1 
ATOM   3857 C  CB  . SER D  1 70  ? -3.656  -31.234 14.098  1.00 28.29  ? 319  SER D CB  1 
ATOM   3858 O  OG  . SER D  1 70  ? -4.267  -32.366 13.524  1.00 29.12  ? 319  SER D OG  1 
ATOM   3859 N  N   . ASP D  1 71  ? -3.970  -32.353 17.053  1.00 28.97  ? 320  ASP D N   1 
ATOM   3860 C  CA  . ASP D  1 71  ? -4.831  -33.410 17.660  1.00 29.78  ? 320  ASP D CA  1 
ATOM   3861 C  C   . ASP D  1 71  ? -6.342  -33.257 17.278  1.00 31.57  ? 320  ASP D C   1 
ATOM   3862 O  O   . ASP D  1 71  ? -7.264  -33.518 18.099  1.00 29.48  ? 320  ASP D O   1 
ATOM   3863 C  CB  . ASP D  1 71  ? -4.636  -33.491 19.167  1.00 29.64  ? 320  ASP D CB  1 
ATOM   3864 C  CG  . ASP D  1 71  ? -5.307  -32.342 19.894  1.00 27.78  ? 320  ASP D CG  1 
ATOM   3865 O  OD1 . ASP D  1 71  ? -5.636  -31.318 19.249  1.00 25.44  ? 320  ASP D OD1 1 
ATOM   3866 O  OD2 . ASP D  1 71  ? -5.538  -32.479 21.099  1.00 29.82  ? 320  ASP D OD2 1 
ATOM   3867 N  N   . LEU D  1 72  ? -6.561  -32.819 16.035  1.00 29.19  ? 321  LEU D N   1 
ATOM   3868 C  CA  . LEU D  1 72  ? -7.902  -32.535 15.491  1.00 32.22  ? 321  LEU D CA  1 
ATOM   3869 C  C   . LEU D  1 72  ? -8.737  -33.806 15.393  1.00 37.08  ? 321  LEU D C   1 
ATOM   3870 O  O   . LEU D  1 72  ? -9.850  -33.850 15.857  1.00 34.94  ? 321  LEU D O   1 
ATOM   3871 C  CB  . LEU D  1 72  ? -7.811  -31.930 14.076  1.00 31.35  ? 321  LEU D CB  1 
ATOM   3872 C  CG  . LEU D  1 72  ? -7.643  -30.424 13.962  1.00 31.25  ? 321  LEU D CG  1 
ATOM   3873 C  CD1 . LEU D  1 72  ? -7.167  -30.018 12.571  1.00 30.01  ? 321  LEU D CD1 1 
ATOM   3874 C  CD2 . LEU D  1 72  ? -8.931  -29.695 14.339  1.00 31.87  ? 321  LEU D CD2 1 
ATOM   3875 N  N   . ASN D  1 73  ? -8.199  -34.836 14.748  1.00 38.73  ? 322  ASN D N   1 
ATOM   3876 C  CA  A ASN D  1 73  ? -9.003  -36.034 14.528  0.70 39.39  ? 322  ASN D CA  1 
ATOM   3877 C  CA  B ASN D  1 73  ? -8.909  -36.100 14.560  0.30 38.64  ? 322  ASN D CA  1 
ATOM   3878 C  C   . ASN D  1 73  ? -9.339  -36.704 15.888  1.00 39.68  ? 322  ASN D C   1 
ATOM   3879 O  O   . ASN D  1 73  ? -10.431 -37.187 16.033  1.00 37.99  ? 322  ASN D O   1 
ATOM   3880 C  CB  A ASN D  1 73  ? -8.373  -36.992 13.478  0.70 38.38  ? 322  ASN D CB  1 
ATOM   3881 C  CB  B ASN D  1 73  ? -8.022  -37.116 13.837  0.30 37.78  ? 322  ASN D CB  1 
ATOM   3882 C  CG  A ASN D  1 73  ? -8.336  -36.392 12.045  0.70 39.35  ? 322  ASN D CG  1 
ATOM   3883 C  CG  B ASN D  1 73  ? -8.733  -38.425 13.607  0.30 36.77  ? 322  ASN D CG  1 
ATOM   3884 O  OD1 A ASN D  1 73  ? -8.854  -35.290 11.774  0.70 39.98  ? 322  ASN D OD1 1 
ATOM   3885 O  OD1 B ASN D  1 73  ? -9.933  -38.434 13.376  0.30 38.68  ? 322  ASN D OD1 1 
ATOM   3886 N  ND2 A ASN D  1 73  ? -7.720  -37.127 11.120  0.70 36.87  ? 322  ASN D ND2 1 
ATOM   3887 N  ND2 B ASN D  1 73  ? -8.008  -39.534 13.689  0.30 36.79  ? 322  ASN D ND2 1 
ATOM   3888 N  N   . GLN D  1 74  ? -8.438  -36.672 16.868  1.00 38.99  ? 323  GLN D N   1 
ATOM   3889 C  CA  . GLN D  1 74  ? -8.692  -37.280 18.175  1.00 40.54  ? 323  GLN D CA  1 
ATOM   3890 C  C   . GLN D  1 74  ? -7.968  -36.563 19.357  1.00 38.50  ? 323  GLN D C   1 
ATOM   3891 O  O   . GLN D  1 74  ? -6.733  -36.652 19.522  1.00 34.53  ? 323  GLN D O   1 
ATOM   3892 C  CB  . GLN D  1 74  ? -8.306  -38.762 18.083  1.00 44.90  ? 323  GLN D CB  1 
ATOM   3893 C  CG  . GLN D  1 74  ? -8.428  -39.626 19.333  1.00 51.93  ? 323  GLN D CG  1 
ATOM   3894 C  CD  . GLN D  1 74  ? -7.934  -41.057 19.049  1.00 57.50  ? 323  GLN D CD  1 
ATOM   3895 O  OE1 . GLN D  1 74  ? -8.496  -41.750 18.200  1.00 61.25  ? 323  GLN D OE1 1 
ATOM   3896 N  NE2 . GLN D  1 74  ? -6.869  -41.487 19.738  1.00 54.73  ? 323  GLN D NE2 1 
ATOM   3897 N  N   . GLU D  1 75  ? -8.756  -35.892 20.204  1.00 34.22  ? 324  GLU D N   1 
ATOM   3898 C  CA  . GLU D  1 75  ? -8.215  -35.038 21.270  1.00 34.27  ? 324  GLU D CA  1 
ATOM   3899 C  C   . GLU D  1 75  ? -7.207  -35.735 22.112  1.00 33.25  ? 324  GLU D C   1 
ATOM   3900 O  O   . GLU D  1 75  ? -7.432  -36.865 22.527  1.00 40.52  ? 324  GLU D O   1 
ATOM   3901 C  CB  . GLU D  1 75  ? -9.339  -34.505 22.196  1.00 32.78  ? 324  GLU D CB  1 
ATOM   3902 C  CG  . GLU D  1 75  ? -8.859  -33.518 23.260  1.00 32.13  ? 324  GLU D CG  1 
ATOM   3903 C  CD  . GLU D  1 75  ? -8.090  -32.298 22.699  1.00 29.15  ? 324  GLU D CD  1 
ATOM   3904 O  OE1 . GLU D  1 75  ? -8.435  -31.752 21.626  1.00 29.86  ? 324  GLU D OE1 1 
ATOM   3905 O  OE2 . GLU D  1 75  ? -7.115  -31.876 23.344  1.00 29.07  ? 324  GLU D OE2 1 
ATOM   3906 N  N   . GLY D  1 76  ? -6.072  -35.080 22.362  1.00 33.97  ? 325  GLY D N   1 
ATOM   3907 C  CA  . GLY D  1 76  ? -4.948  -35.713 23.088  1.00 30.92  ? 325  GLY D CA  1 
ATOM   3908 C  C   . GLY D  1 76  ? -4.012  -36.648 22.318  1.00 31.99  ? 325  GLY D C   1 
ATOM   3909 O  O   . GLY D  1 76  ? -2.905  -36.924 22.772  1.00 34.67  ? 325  GLY D O   1 
ATOM   3910 N  N   . THR D  1 77  ? -4.426  -37.134 21.156  1.00 32.48  ? 326  THR D N   1 
ATOM   3911 C  CA  . THR D  1 77  ? -3.534  -37.918 20.307  1.00 31.76  ? 326  THR D CA  1 
ATOM   3912 C  C   . THR D  1 77  ? -2.983  -37.056 19.163  1.00 29.50  ? 326  THR D C   1 
ATOM   3913 O  O   . THR D  1 77  ? -3.682  -36.779 18.181  1.00 29.73  ? 326  THR D O   1 
ATOM   3914 C  CB  . THR D  1 77  ? -4.287  -39.162 19.760  1.00 32.74  ? 326  THR D CB  1 
ATOM   3915 O  OG1 . THR D  1 77  ? -4.612  -39.996 20.877  1.00 34.50  ? 326  THR D OG1 1 
ATOM   3916 C  CG2 . THR D  1 77  ? -3.427  -39.988 18.760  1.00 33.79  ? 326  THR D CG2 1 
ATOM   3917 N  N   . TRP D  1 78  ? -1.724  -36.660 19.289  1.00 29.67  ? 327  TRP D N   1 
ATOM   3918 C  CA  . TRP D  1 78  ? -1.114  -35.713 18.365  1.00 31.55  ? 327  TRP D CA  1 
ATOM   3919 C  C   . TRP D  1 78  ? -0.511  -36.444 17.179  1.00 31.63  ? 327  TRP D C   1 
ATOM   3920 O  O   . TRP D  1 78  ? 0.285   -37.363 17.360  1.00 30.57  ? 327  TRP D O   1 
ATOM   3921 C  CB  . TRP D  1 78  ? -0.057  -34.859 19.077  1.00 31.44  ? 327  TRP D CB  1 
ATOM   3922 C  CG  . TRP D  1 78  ? -0.698  -33.847 19.897  1.00 31.20  ? 327  TRP D CG  1 
ATOM   3923 C  CD1 . TRP D  1 78  ? -1.136  -33.998 21.158  1.00 32.50  ? 327  TRP D CD1 1 
ATOM   3924 C  CD2 . TRP D  1 78  ? -1.039  -32.520 19.497  1.00 31.58  ? 327  TRP D CD2 1 
ATOM   3925 N  NE1 . TRP D  1 78  ? -1.727  -32.844 21.591  1.00 33.60  ? 327  TRP D NE1 1 
ATOM   3926 C  CE2 . TRP D  1 78  ? -1.691  -31.917 20.588  1.00 31.66  ? 327  TRP D CE2 1 
ATOM   3927 C  CE3 . TRP D  1 78  ? -0.851  -31.785 18.324  1.00 29.68  ? 327  TRP D CE3 1 
ATOM   3928 C  CZ2 . TRP D  1 78  ? -2.173  -30.601 20.552  1.00 34.55  ? 327  TRP D CZ2 1 
ATOM   3929 C  CZ3 . TRP D  1 78  ? -1.332  -30.478 18.275  1.00 33.37  ? 327  TRP D CZ3 1 
ATOM   3930 C  CH2 . TRP D  1 78  ? -1.982  -29.895 19.387  1.00 32.67  ? 327  TRP D CH2 1 
ATOM   3931 N  N   . GLN D  1 79  ? -0.854  -35.964 15.991  1.00 30.75  ? 328  GLN D N   1 
ATOM   3932 C  CA  . GLN D  1 79  ? -0.529  -36.597 14.751  1.00 34.15  ? 328  GLN D CA  1 
ATOM   3933 C  C   . GLN D  1 79  ? 0.075   -35.583 13.793  1.00 32.29  ? 328  GLN D C   1 
ATOM   3934 O  O   . GLN D  1 79  ? -0.476  -34.479 13.613  1.00 29.44  ? 328  GLN D O   1 
ATOM   3935 C  CB  . GLN D  1 79  ? -1.825  -37.135 14.174  1.00 39.13  ? 328  GLN D CB  1 
ATOM   3936 C  CG  . GLN D  1 79  ? -1.675  -38.255 13.175  1.00 51.65  ? 328  GLN D CG  1 
ATOM   3937 C  CD  . GLN D  1 79  ? -3.039  -38.753 12.701  1.00 61.14  ? 328  GLN D CD  1 
ATOM   3938 O  OE1 . GLN D  1 79  ? -4.002  -38.780 13.476  1.00 69.20  ? 328  GLN D OE1 1 
ATOM   3939 N  NE2 . GLN D  1 79  ? -3.131  -39.134 11.428  1.00 59.32  ? 328  GLN D NE2 1 
ATOM   3940 N  N   . TRP D  1 80  ? 1.175   -35.951 13.150  1.00 27.67  ? 329  TRP D N   1 
ATOM   3941 C  CA  . TRP D  1 80  ? 1.719   -35.113 12.076  1.00 29.02  ? 329  TRP D CA  1 
ATOM   3942 C  C   . TRP D  1 80  ? 0.887   -35.249 10.843  1.00 29.99  ? 329  TRP D C   1 
ATOM   3943 O  O   . TRP D  1 80  ? 0.249   -36.276 10.637  1.00 33.05  ? 329  TRP D O   1 
ATOM   3944 C  CB  . TRP D  1 80  ? 3.150   -35.506 11.728  1.00 29.99  ? 329  TRP D CB  1 
ATOM   3945 C  CG  . TRP D  1 80  ? 4.098   -35.332 12.818  1.00 28.60  ? 329  TRP D CG  1 
ATOM   3946 C  CD1 . TRP D  1 80  ? 4.569   -36.311 13.652  1.00 29.63  ? 329  TRP D CD1 1 
ATOM   3947 C  CD2 . TRP D  1 80  ? 4.726   -34.112 13.226  1.00 29.52  ? 329  TRP D CD2 1 
ATOM   3948 N  NE1 . TRP D  1 80  ? 5.457   -35.782 14.548  1.00 30.45  ? 329  TRP D NE1 1 
ATOM   3949 C  CE2 . TRP D  1 80  ? 5.576   -34.430 14.318  1.00 29.31  ? 329  TRP D CE2 1 
ATOM   3950 C  CE3 . TRP D  1 80  ? 4.684   -32.797 12.762  1.00 29.95  ? 329  TRP D CE3 1 
ATOM   3951 C  CZ2 . TRP D  1 80  ? 6.377   -33.464 14.971  1.00 30.33  ? 329  TRP D CZ2 1 
ATOM   3952 C  CZ3 . TRP D  1 80  ? 5.480   -31.810 13.418  1.00 29.83  ? 329  TRP D CZ3 1 
ATOM   3953 C  CH2 . TRP D  1 80  ? 6.314   -32.157 14.510  1.00 32.31  ? 329  TRP D CH2 1 
ATOM   3954 N  N   . VAL D  1 81  ? 0.895   -34.238 9.988   1.00 30.14  ? 330  VAL D N   1 
ATOM   3955 C  CA  . VAL D  1 81  ? 0.013   -34.287 8.795   1.00 31.02  ? 330  VAL D CA  1 
ATOM   3956 C  C   . VAL D  1 81  ? 0.393   -35.362 7.781   1.00 34.21  ? 330  VAL D C   1 
ATOM   3957 O  O   . VAL D  1 81  ? -0.405  -35.678 6.912   1.00 29.18  ? 330  VAL D O   1 
ATOM   3958 C  CB  . VAL D  1 81  ? -0.074  -32.969 8.043   1.00 28.59  ? 330  VAL D CB  1 
ATOM   3959 C  CG1 . VAL D  1 81  ? -0.779  -31.917 8.892   1.00 28.42  ? 330  VAL D CG1 1 
ATOM   3960 C  CG2 . VAL D  1 81  ? 1.303   -32.522 7.582   1.00 29.37  ? 330  VAL D CG2 1 
ATOM   3961 N  N   . ASP D  1 82  ? 1.580   -35.947 7.903   1.00 34.47  ? 331  ASP D N   1 
ATOM   3962 C  CA  . ASP D  1 82  ? 1.963   -37.045 6.989   1.00 36.78  ? 331  ASP D CA  1 
ATOM   3963 C  C   . ASP D  1 82  ? 1.496   -38.391 7.498   1.00 36.58  ? 331  ASP D C   1 
ATOM   3964 O  O   . ASP D  1 82  ? 1.793   -39.382 6.886   1.00 37.71  ? 331  ASP D O   1 
ATOM   3965 C  CB  . ASP D  1 82  ? 3.477   -37.117 6.801   1.00 32.83  ? 331  ASP D CB  1 
ATOM   3966 C  CG  . ASP D  1 82  ? 4.187   -37.538 8.058   1.00 33.38  ? 331  ASP D CG  1 
ATOM   3967 O  OD1 . ASP D  1 82  ? 3.599   -37.495 9.175   1.00 36.30  ? 331  ASP D OD1 1 
ATOM   3968 O  OD2 . ASP D  1 82  ? 5.365   -37.883 7.962   1.00 35.24  ? 331  ASP D OD2 1 
ATOM   3969 N  N   . GLY D  1 83  ? 0.828   -38.443 8.644   1.00 35.01  ? 332  GLY D N   1 
ATOM   3970 C  CA  . GLY D  1 83  ? 0.383   -39.722 9.182   1.00 34.72  ? 332  GLY D CA  1 
ATOM   3971 C  C   . GLY D  1 83  ? 1.193   -40.323 10.327  1.00 37.55  ? 332  GLY D C   1 
ATOM   3972 O  O   . GLY D  1 83  ? 0.731   -41.242 10.987  1.00 40.20  ? 332  GLY D O   1 
ATOM   3973 N  N   . SER D  1 84  ? 2.388   -39.816 10.592  1.00 36.54  ? 333  SER D N   1 
ATOM   3974 C  CA  . SER D  1 84  ? 3.165   -40.311 11.716  1.00 35.86  ? 333  SER D CA  1 
ATOM   3975 C  C   . SER D  1 84  ? 2.659   -39.745 13.062  1.00 34.08  ? 333  SER D C   1 
ATOM   3976 O  O   . SER D  1 84  ? 2.172   -38.648 13.135  1.00 37.70  ? 333  SER D O   1 
ATOM   3977 C  CB  . SER D  1 84  ? 4.638   -40.000 11.505  1.00 36.65  ? 333  SER D CB  1 
ATOM   3978 O  OG  . SER D  1 84  ? 4.812   -38.698 10.986  1.00 44.25  ? 333  SER D OG  1 
ATOM   3979 N  N   . PRO D  1 85  ? 2.755   -40.533 14.127  1.00 32.93  ? 334  PRO D N   1 
ATOM   3980 C  CA  . PRO D  1 85  ? 2.381   -40.125 15.476  1.00 31.75  ? 334  PRO D CA  1 
ATOM   3981 C  C   . PRO D  1 85  ? 3.486   -39.259 16.061  1.00 34.84  ? 334  PRO D C   1 
ATOM   3982 O  O   . PRO D  1 85  ? 4.658   -39.404 15.668  1.00 31.09  ? 334  PRO D O   1 
ATOM   3983 C  CB  . PRO D  1 85  ? 2.307   -41.462 16.234  1.00 30.84  ? 334  PRO D CB  1 
ATOM   3984 C  CG  . PRO D  1 85  ? 3.307   -42.333 15.537  1.00 32.18  ? 334  PRO D CG  1 
ATOM   3985 C  CD  . PRO D  1 85  ? 3.395   -41.865 14.100  1.00 31.26  ? 334  PRO D CD  1 
ATOM   3986 N  N   . LEU D  1 86  ? 3.117   -38.355 16.970  1.00 33.94  ? 335  LEU D N   1 
ATOM   3987 C  CA  . LEU D  1 86  ? 4.087   -37.613 17.704  1.00 33.70  ? 335  LEU D CA  1 
ATOM   3988 C  C   . LEU D  1 86  ? 4.835   -38.559 18.618  1.00 35.37  ? 335  LEU D C   1 
ATOM   3989 O  O   . LEU D  1 86  ? 4.269   -39.115 19.568  1.00 39.57  ? 335  LEU D O   1 
ATOM   3990 C  CB  . LEU D  1 86  ? 3.434   -36.504 18.534  1.00 33.63  ? 335  LEU D CB  1 
ATOM   3991 C  CG  . LEU D  1 86  ? 4.410   -35.696 19.382  1.00 31.45  ? 335  LEU D CG  1 
ATOM   3992 C  CD1 . LEU D  1 86  ? 5.371   -34.960 18.469  1.00 32.61  ? 335  LEU D CD1 1 
ATOM   3993 C  CD2 . LEU D  1 86  ? 3.679   -34.742 20.318  1.00 31.02  ? 335  LEU D CD2 1 
ATOM   3994 N  N   . LEU D  1 87  ? 6.129   -38.720 18.362  1.00 34.70  ? 336  LEU D N   1 
ATOM   3995 C  CA  . LEU D  1 87  ? 6.926   -39.613 19.187  1.00 32.14  ? 336  LEU D CA  1 
ATOM   3996 C  C   . LEU D  1 87  ? 7.078   -39.077 20.613  1.00 33.66  ? 336  LEU D C   1 
ATOM   3997 O  O   . LEU D  1 87  ? 7.123   -37.866 20.818  1.00 30.70  ? 336  LEU D O   1 
ATOM   3998 C  CB  . LEU D  1 87  ? 8.275   -39.863 18.550  1.00 33.90  ? 336  LEU D CB  1 
ATOM   3999 C  CG  . LEU D  1 87  ? 8.178   -40.542 17.176  1.00 33.52  ? 336  LEU D CG  1 
ATOM   4000 C  CD1 . LEU D  1 87  ? 9.552   -40.576 16.530  1.00 32.66  ? 336  LEU D CD1 1 
ATOM   4001 C  CD2 . LEU D  1 87  ? 7.562   -41.950 17.225  1.00 35.37  ? 336  LEU D CD2 1 
ATOM   4002 N  N   . PRO D  1 88  ? 7.107   -39.982 21.618  1.00 34.73  ? 337  PRO D N   1 
ATOM   4003 C  CA  . PRO D  1 88  ? 7.406   -39.634 23.011  1.00 35.02  ? 337  PRO D CA  1 
ATOM   4004 C  C   . PRO D  1 88  ? 8.696   -38.832 23.216  1.00 32.08  ? 337  PRO D C   1 
ATOM   4005 O  O   . PRO D  1 88  ? 8.743   -37.952 24.051  1.00 32.04  ? 337  PRO D O   1 
ATOM   4006 C  CB  . PRO D  1 88  ? 7.519   -41.019 23.696  1.00 37.80  ? 337  PRO D CB  1 
ATOM   4007 C  CG  . PRO D  1 88  ? 6.615   -41.886 22.920  1.00 36.13  ? 337  PRO D CG  1 
ATOM   4008 C  CD  . PRO D  1 88  ? 6.747   -41.413 21.493  1.00 37.60  ? 337  PRO D CD  1 
ATOM   4009 N  N   . SER D  1 89  ? 9.723   -39.113 22.442  1.00 32.62  ? 338  SER D N   1 
ATOM   4010 C  CA  . SER D  1 89  ? 10.979  -38.385 22.526  1.00 35.67  ? 338  SER D CA  1 
ATOM   4011 C  C   . SER D  1 89  ? 10.834  -36.921 22.107  1.00 35.95  ? 338  SER D C   1 
ATOM   4012 O  O   . SER D  1 89  ? 11.740  -36.115 22.359  1.00 34.27  ? 338  SER D O   1 
ATOM   4013 C  CB  . SER D  1 89  ? 12.036  -39.059 21.639  1.00 36.99  ? 338  SER D CB  1 
ATOM   4014 O  OG  . SER D  1 89  ? 11.638  -39.070 20.282  1.00 38.30  ? 338  SER D OG  1 
ATOM   4015 N  N   . PHE D  1 90  ? 9.716   -36.599 21.444  1.00 33.84  ? 339  PHE D N   1 
ATOM   4016 C  CA  . PHE D  1 90  ? 9.445   -35.227 20.975  1.00 33.62  ? 339  PHE D CA  1 
ATOM   4017 C  C   . PHE D  1 90  ? 8.642   -34.420 21.962  1.00 32.36  ? 339  PHE D C   1 
ATOM   4018 O  O   . PHE D  1 90  ? 8.613   -33.202 21.851  1.00 31.44  ? 339  PHE D O   1 
ATOM   4019 C  CB  . PHE D  1 90  ? 8.753   -35.208 19.622  1.00 35.23  ? 339  PHE D CB  1 
ATOM   4020 C  CG  . PHE D  1 90  ? 9.676   -35.448 18.488  1.00 38.13  ? 339  PHE D CG  1 
ATOM   4021 C  CD1 . PHE D  1 90  ? 10.237  -36.700 18.304  1.00 41.40  ? 339  PHE D CD1 1 
ATOM   4022 C  CD2 . PHE D  1 90  ? 9.982   -34.443 17.591  1.00 39.32  ? 339  PHE D CD2 1 
ATOM   4023 C  CE1 . PHE D  1 90  ? 11.091  -36.955 17.245  1.00 41.12  ? 339  PHE D CE1 1 
ATOM   4024 C  CE2 . PHE D  1 90  ? 10.843  -34.686 16.543  1.00 40.75  ? 339  PHE D CE2 1 
ATOM   4025 C  CZ  . PHE D  1 90  ? 11.414  -35.939 16.379  1.00 40.42  ? 339  PHE D CZ  1 
ATOM   4026 N  N   . LYS D  1 91  ? 8.054   -35.070 22.957  1.00 29.96  ? 340  LYS D N   1 
ATOM   4027 C  CA  . LYS D  1 91  ? 7.261   -34.354 23.962  1.00 33.42  ? 340  LYS D CA  1 
ATOM   4028 C  C   . LYS D  1 91  ? 8.047   -33.302 24.775  1.00 30.69  ? 340  LYS D C   1 
ATOM   4029 O  O   . LYS D  1 91  ? 7.488   -32.322 25.270  1.00 31.56  ? 340  LYS D O   1 
ATOM   4030 C  CB  . LYS D  1 91  ? 6.500   -35.357 24.856  1.00 39.22  ? 340  LYS D CB  1 
ATOM   4031 C  CG  . LYS D  1 91  ? 5.299   -35.942 24.113  1.00 49.12  ? 340  LYS D CG  1 
ATOM   4032 C  CD  . LYS D  1 91  ? 4.732   -37.218 24.728  1.00 54.64  ? 340  LYS D CD  1 
ATOM   4033 C  CE  . LYS D  1 91  ? 3.883   -37.951 23.689  1.00 63.79  ? 340  LYS D CE  1 
ATOM   4034 N  NZ  . LYS D  1 91  ? 3.466   -39.314 24.150  1.00 71.96  ? 340  LYS D NZ  1 
ATOM   4035 N  N   . GLN D  1 92  ? 9.347   -33.489 24.900  1.00 31.54  ? 341  GLN D N   1 
ATOM   4036 C  CA  . GLN D  1 92  ? 10.191  -32.501 25.526  1.00 32.20  ? 341  GLN D CA  1 
ATOM   4037 C  C   . GLN D  1 92  ? 10.102  -31.110 24.873  1.00 33.66  ? 341  GLN D C   1 
ATOM   4038 O  O   . GLN D  1 92  ? 10.479  -30.109 25.497  1.00 36.04  ? 341  GLN D O   1 
ATOM   4039 C  CB  . GLN D  1 92  ? 11.643  -32.987 25.514  1.00 34.50  ? 341  GLN D CB  1 
ATOM   4040 C  CG  . GLN D  1 92  ? 12.257  -33.039 24.131  1.00 38.41  ? 341  GLN D CG  1 
ATOM   4041 C  CD  . GLN D  1 92  ? 13.666  -33.580 24.153  1.00 40.57  ? 341  GLN D CD  1 
ATOM   4042 O  OE1 . GLN D  1 92  ? 14.513  -33.080 24.856  1.00 42.41  ? 341  GLN D OE1 1 
ATOM   4043 N  NE2 . GLN D  1 92  ? 13.907  -34.623 23.383  1.00 46.28  ? 341  GLN D NE2 1 
ATOM   4044 N  N   . TYR D  1 93  ? 9.625   -31.032 23.630  1.00 32.82  ? 342  TYR D N   1 
ATOM   4045 C  CA  . TYR D  1 93  ? 9.610   -29.736 22.921  1.00 32.75  ? 342  TYR D CA  1 
ATOM   4046 C  C   . TYR D  1 93  ? 8.422   -28.840 23.224  1.00 28.28  ? 342  TYR D C   1 
ATOM   4047 O  O   . TYR D  1 93  ? 8.503   -27.641 23.047  1.00 30.96  ? 342  TYR D O   1 
ATOM   4048 C  CB  . TYR D  1 93  ? 9.781   -29.938 21.426  1.00 31.03  ? 342  TYR D CB  1 
ATOM   4049 C  CG  . TYR D  1 93  ? 11.050  -30.685 21.105  1.00 29.40  ? 342  TYR D CG  1 
ATOM   4050 C  CD1 . TYR D  1 93  ? 12.268  -30.256 21.594  1.00 28.58  ? 342  TYR D CD1 1 
ATOM   4051 C  CD2 . TYR D  1 93  ? 11.033  -31.822 20.294  1.00 31.32  ? 342  TYR D CD2 1 
ATOM   4052 C  CE1 . TYR D  1 93  ? 13.446  -30.918 21.281  1.00 29.77  ? 342  TYR D CE1 1 
ATOM   4053 C  CE2 . TYR D  1 93  ? 12.208  -32.514 20.012  1.00 31.22  ? 342  TYR D CE2 1 
ATOM   4054 C  CZ  . TYR D  1 93  ? 13.404  -32.057 20.531  1.00 30.40  ? 342  TYR D CZ  1 
ATOM   4055 O  OH  . TYR D  1 93  ? 14.566  -32.702 20.231  1.00 38.48  ? 342  TYR D OH  1 
ATOM   4056 N  N   . TRP D  1 94  ? 7.343   -29.408 23.719  1.00 27.97  ? 343  TRP D N   1 
ATOM   4057 C  CA  . TRP D  1 94  ? 6.256   -28.588 24.286  1.00 30.28  ? 343  TRP D CA  1 
ATOM   4058 C  C   . TRP D  1 94  ? 6.729   -27.632 25.388  1.00 28.83  ? 343  TRP D C   1 
ATOM   4059 O  O   . TRP D  1 94  ? 7.456   -28.034 26.274  1.00 32.25  ? 343  TRP D O   1 
ATOM   4060 C  CB  . TRP D  1 94  ? 5.199   -29.453 24.918  1.00 29.06  ? 343  TRP D CB  1 
ATOM   4061 C  CG  . TRP D  1 94  ? 4.445   -30.311 24.027  1.00 29.27  ? 343  TRP D CG  1 
ATOM   4062 C  CD1 . TRP D  1 94  ? 4.420   -31.665 24.059  1.00 29.67  ? 343  TRP D CD1 1 
ATOM   4063 C  CD2 . TRP D  1 94  ? 3.526   -29.918 22.988  1.00 30.63  ? 343  TRP D CD2 1 
ATOM   4064 N  NE1 . TRP D  1 94  ? 3.571   -32.141 23.097  1.00 29.47  ? 343  TRP D NE1 1 
ATOM   4065 C  CE2 . TRP D  1 94  ? 3.009   -31.097 22.428  1.00 29.11  ? 343  TRP D CE2 1 
ATOM   4066 C  CE3 . TRP D  1 94  ? 3.108   -28.698 22.473  1.00 29.65  ? 343  TRP D CE3 1 
ATOM   4067 C  CZ2 . TRP D  1 94  ? 2.081   -31.090 21.412  1.00 30.45  ? 343  TRP D CZ2 1 
ATOM   4068 C  CZ3 . TRP D  1 94  ? 2.213   -28.695 21.449  1.00 31.44  ? 343  TRP D CZ3 1 
ATOM   4069 C  CH2 . TRP D  1 94  ? 1.705   -29.884 20.921  1.00 32.15  ? 343  TRP D CH2 1 
ATOM   4070 N  N   . ASN D  1 95  ? 6.353   -26.356 25.304  1.00 30.10  ? 344  ASN D N   1 
ATOM   4071 C  CA  . ASN D  1 95  ? 6.543   -25.434 26.415  1.00 30.25  ? 344  ASN D CA  1 
ATOM   4072 C  C   . ASN D  1 95  ? 5.898   -25.990 27.701  1.00 33.64  ? 344  ASN D C   1 
ATOM   4073 O  O   . ASN D  1 95  ? 5.008   -26.823 27.653  1.00 31.41  ? 344  ASN D O   1 
ATOM   4074 C  CB  . ASN D  1 95  ? 5.843   -24.089 26.142  1.00 30.44  ? 344  ASN D CB  1 
ATOM   4075 C  CG  . ASN D  1 95  ? 6.455   -23.330 24.993  1.00 28.89  ? 344  ASN D CG  1 
ATOM   4076 O  OD1 . ASN D  1 95  ? 7.629   -23.503 24.718  1.00 27.22  ? 344  ASN D OD1 1 
ATOM   4077 N  ND2 . ASN D  1 95  ? 5.656   -22.464 24.325  1.00 27.80  ? 344  ASN D ND2 1 
ATOM   4078 N  N   . ARG D  1 96  ? 6.321   -25.459 28.838  1.00 37.50  ? 345  ARG D N   1 
ATOM   4079 C  CA  . ARG D  1 96  ? 5.825   -25.910 30.144  1.00 40.46  ? 345  ARG D CA  1 
ATOM   4080 C  C   . ARG D  1 96  ? 4.323   -25.796 30.153  1.00 36.18  ? 345  ARG D C   1 
ATOM   4081 O  O   . ARG D  1 96  ? 3.758   -24.802 29.705  1.00 39.05  ? 345  ARG D O   1 
ATOM   4082 C  CB  . ARG D  1 96  ? 6.485   -25.093 31.252  1.00 47.66  ? 345  ARG D CB  1 
ATOM   4083 C  CG  . ARG D  1 96  ? 5.909   -25.245 32.663  1.00 59.04  ? 345  ARG D CG  1 
ATOM   4084 C  CD  . ARG D  1 96  ? 6.721   -24.461 33.696  1.00 63.88  ? 345  ARG D CD  1 
ATOM   4085 N  NE  . ARG D  1 96  ? 7.933   -25.177 34.127  1.00 70.02  ? 345  ARG D NE  1 
ATOM   4086 C  CZ  . ARG D  1 96  ? 9.133   -25.124 33.532  1.00 75.74  ? 345  ARG D CZ  1 
ATOM   4087 N  NH1 . ARG D  1 96  ? 9.345   -24.387 32.438  1.00 77.09  ? 345  ARG D NH1 1 
ATOM   4088 N  NH2 . ARG D  1 96  ? 10.146  -25.823 34.041  1.00 77.41  ? 345  ARG D NH2 1 
ATOM   4089 N  N   . GLY D  1 97  ? 3.663   -26.847 30.593  1.00 38.27  ? 346  GLY D N   1 
ATOM   4090 C  CA  . GLY D  1 97  ? 2.208   -26.856 30.698  1.00 36.37  ? 346  GLY D CA  1 
ATOM   4091 C  C   . GLY D  1 97  ? 1.430   -27.047 29.409  1.00 36.40  ? 346  GLY D C   1 
ATOM   4092 O  O   . GLY D  1 97  ? 0.208   -27.025 29.419  1.00 33.33  ? 346  GLY D O   1 
ATOM   4093 N  N   . GLU D  1 98  ? 2.113   -27.275 28.294  1.00 33.86  ? 347  GLU D N   1 
ATOM   4094 C  CA  . GLU D  1 98  ? 1.415   -27.580 27.084  1.00 35.84  ? 347  GLU D CA  1 
ATOM   4095 C  C   . GLU D  1 98  ? 1.679   -29.068 26.749  1.00 32.50  ? 347  GLU D C   1 
ATOM   4096 O  O   . GLU D  1 98  ? 2.661   -29.634 27.186  1.00 32.71  ? 347  GLU D O   1 
ATOM   4097 C  CB  . GLU D  1 98  ? 1.938   -26.680 25.963  1.00 37.22  ? 347  GLU D CB  1 
ATOM   4098 C  CG  . GLU D  1 98  ? 2.086   -25.233 26.366  1.00 34.41  ? 347  GLU D CG  1 
ATOM   4099 C  CD  . GLU D  1 98  ? 0.786   -24.514 26.501  1.00 33.50  ? 347  GLU D CD  1 
ATOM   4100 O  OE1 . GLU D  1 98  ? -0.275  -24.983 26.058  1.00 32.87  ? 347  GLU D OE1 1 
ATOM   4101 O  OE2 . GLU D  1 98  ? 0.849   -23.389 27.001  1.00 40.43  ? 347  GLU D OE2 1 
ATOM   4102 N  N   . PRO D  1 99  ? 0.862   -29.678 25.924  1.00 31.42  ? 348  PRO D N   1 
ATOM   4103 C  CA  . PRO D  1 99  ? -0.340  -29.078 25.338  1.00 32.68  ? 348  PRO D CA  1 
ATOM   4104 C  C   . PRO D  1 99  ? -1.479  -29.078 26.350  1.00 32.66  ? 348  PRO D C   1 
ATOM   4105 O  O   . PRO D  1 99  ? -1.656  -30.055 27.033  1.00 33.38  ? 348  PRO D O   1 
ATOM   4106 C  CB  . PRO D  1 99  ? -0.690  -30.034 24.202  1.00 31.99  ? 348  PRO D CB  1 
ATOM   4107 C  CG  . PRO D  1 99  ? -0.085  -31.346 24.576  1.00 31.33  ? 348  PRO D CG  1 
ATOM   4108 C  CD  . PRO D  1 99  ? 1.120   -31.051 25.425  1.00 32.62  ? 348  PRO D CD  1 
ATOM   4109 N  N   . ASN D  1 100 ? -2.244  -28.000 26.428  1.00 31.25  ? 349  ASN D N   1 
ATOM   4110 C  CA  . ASN D  1 100 ? -3.244  -27.872 27.502  1.00 31.51  ? 349  ASN D CA  1 
ATOM   4111 C  C   . ASN D  1 100 ? -4.663  -27.787 26.947  1.00 30.14  ? 349  ASN D C   1 
ATOM   4112 O  O   . ASN D  1 100 ? -5.614  -27.858 27.693  1.00 30.71  ? 349  ASN D O   1 
ATOM   4113 C  CB  . ASN D  1 100 ? -2.909  -26.683 28.373  1.00 29.72  ? 349  ASN D CB  1 
ATOM   4114 C  CG  . ASN D  1 100 ? -2.890  -25.377 27.600  1.00 29.70  ? 349  ASN D CG  1 
ATOM   4115 O  OD1 . ASN D  1 100 ? -3.224  -25.315 26.412  1.00 30.20  ? 349  ASN D OD1 1 
ATOM   4116 N  ND2 . ASN D  1 100 ? -2.496  -24.335 28.264  1.00 27.10  ? 349  ASN D ND2 1 
ATOM   4117 N  N   . ASN D  1 101 ? -4.794  -27.699 25.630  1.00 26.81  ? 350  ASN D N   1 
ATOM   4118 C  CA  . ASN D  1 101 ? -6.092  -27.659 25.000  1.00 31.04  ? 350  ASN D CA  1 
ATOM   4119 C  C   . ASN D  1 101 ? -7.014  -26.531 25.530  1.00 32.49  ? 350  ASN D C   1 
ATOM   4120 O  O   . ASN D  1 101 ? -8.211  -26.603 25.364  1.00 33.27  ? 350  ASN D O   1 
ATOM   4121 C  CB  . ASN D  1 101 ? -6.797  -29.019 25.133  1.00 31.54  ? 350  ASN D CB  1 
ATOM   4122 C  CG  . ASN D  1 101 ? -7.951  -29.171 24.157  1.00 34.19  ? 350  ASN D CG  1 
ATOM   4123 O  OD1 . ASN D  1 101 ? -7.811  -28.898 22.947  1.00 29.31  ? 350  ASN D OD1 1 
ATOM   4124 N  ND2 . ASN D  1 101 ? -9.114  -29.578 24.676  1.00 30.37  ? 350  ASN D ND2 1 
ATOM   4125 N  N   . VAL D  1 102 ? -6.453  -25.454 26.070  1.00 38.04  ? 351  VAL D N   1 
ATOM   4126 C  CA  . VAL D  1 102 ? -7.265  -24.389 26.690  1.00 39.57  ? 351  VAL D CA  1 
ATOM   4127 C  C   . VAL D  1 102 ? -8.125  -23.607 25.664  1.00 41.59  ? 351  VAL D C   1 
ATOM   4128 O  O   . VAL D  1 102 ? -7.627  -22.868 24.823  1.00 40.90  ? 351  VAL D O   1 
ATOM   4129 C  CB  . VAL D  1 102 ? -6.392  -23.485 27.594  1.00 42.51  ? 351  VAL D CB  1 
ATOM   4130 C  CG1 . VAL D  1 102 ? -5.416  -22.637 26.782  1.00 46.32  ? 351  VAL D CG1 1 
ATOM   4131 C  CG2 . VAL D  1 102 ? -7.256  -22.616 28.486  1.00 43.13  ? 351  VAL D CG2 1 
ATOM   4132 N  N   . GLY D  1 103 ? -9.438  -23.783 25.757  1.00 41.29  ? 352  GLY D N   1 
ATOM   4133 C  CA  . GLY D  1 103 ? -10.369 -23.228 24.783  1.00 40.50  ? 352  GLY D CA  1 
ATOM   4134 C  C   . GLY D  1 103 ? -10.541 -24.031 23.492  1.00 41.61  ? 352  GLY D C   1 
ATOM   4135 O  O   . GLY D  1 103 ? -11.135 -23.521 22.517  1.00 42.21  ? 352  GLY D O   1 
ATOM   4136 N  N   . GLU D  1 104 ? -10.063 -25.283 23.511  1.00 38.28  ? 353  GLU D N   1 
ATOM   4137 C  CA  . GLU D  1 104 ? -10.036 -26.179 22.370  1.00 38.40  ? 353  GLU D CA  1 
ATOM   4138 C  C   . GLU D  1 104 ? -8.914  -25.715 21.452  1.00 34.36  ? 353  GLU D C   1 
ATOM   4139 O  O   . GLU D  1 104 ? -9.094  -24.790 20.674  1.00 34.94  ? 353  GLU D O   1 
ATOM   4140 C  CB  . GLU D  1 104 ? -11.360 -26.217 21.603  1.00 43.73  ? 353  GLU D CB  1 
ATOM   4141 C  CG  . GLU D  1 104 ? -12.478 -27.067 22.201  1.00 51.13  ? 353  GLU D CG  1 
ATOM   4142 C  CD  . GLU D  1 104 ? -13.663 -27.193 21.231  1.00 61.72  ? 353  GLU D CD  1 
ATOM   4143 O  OE1 . GLU D  1 104 ? -13.462 -27.148 19.982  1.00 65.77  ? 353  GLU D OE1 1 
ATOM   4144 O  OE2 . GLU D  1 104 ? -14.816 -27.328 21.706  1.00 70.41  ? 353  GLU D OE2 1 
ATOM   4145 N  N   . GLU D  1 105 ? -7.746  -26.327 21.607  1.00 30.22  ? 354  GLU D N   1 
ATOM   4146 C  CA  . GLU D  1 105 ? -6.573  -25.944 20.849  1.00 28.37  ? 354  GLU D CA  1 
ATOM   4147 C  C   . GLU D  1 105 ? -6.060  -27.246 20.254  1.00 27.18  ? 354  GLU D C   1 
ATOM   4148 O  O   . GLU D  1 105 ? -5.650  -28.173 20.971  1.00 23.48  ? 354  GLU D O   1 
ATOM   4149 C  CB  . GLU D  1 105 ? -5.535  -25.266 21.733  1.00 28.54  ? 354  GLU D CB  1 
ATOM   4150 C  CG  . GLU D  1 105 ? -6.051  -24.027 22.505  1.00 28.12  ? 354  GLU D CG  1 
ATOM   4151 C  CD  . GLU D  1 105 ? -4.927  -23.326 23.229  1.00 27.80  ? 354  GLU D CD  1 
ATOM   4152 O  OE1 . GLU D  1 105 ? -4.165  -24.004 23.981  1.00 21.97  ? 354  GLU D OE1 1 
ATOM   4153 O  OE2 . GLU D  1 105 ? -4.747  -22.100 23.001  1.00 30.63  ? 354  GLU D OE2 1 
ATOM   4154 N  N   . ASP D  1 106 ? -6.098  -27.330 18.937  1.00 28.16  ? 355  ASP D N   1 
ATOM   4155 C  CA  . ASP D  1 106 ? -5.780  -28.599 18.271  1.00 28.28  ? 355  ASP D CA  1 
ATOM   4156 C  C   . ASP D  1 106 ? -4.705  -28.506 17.180  1.00 31.19  ? 355  ASP D C   1 
ATOM   4157 O  O   . ASP D  1 106 ? -4.474  -29.504 16.473  1.00 27.89  ? 355  ASP D O   1 
ATOM   4158 C  CB  . ASP D  1 106 ? -7.054  -29.182 17.647  1.00 30.24  ? 355  ASP D CB  1 
ATOM   4159 C  CG  . ASP D  1 106 ? -8.149  -29.529 18.690  1.00 29.87  ? 355  ASP D CG  1 
ATOM   4160 O  OD1 . ASP D  1 106 ? -7.864  -29.696 19.928  1.00 25.98  ? 355  ASP D OD1 1 
ATOM   4161 O  OD2 . ASP D  1 106 ? -9.300  -29.621 18.206  1.00 31.58  ? 355  ASP D OD2 1 
ATOM   4162 N  N   . CYS D  1 107 ? -4.064  -27.343 17.034  1.00 27.38  ? 356  CYS D N   1 
ATOM   4163 C  CA  . CYS D  1 107 ? -2.978  -27.212 16.075  1.00 28.72  ? 356  CYS D CA  1 
ATOM   4164 C  C   . CYS D  1 107 ? -1.711  -26.701 16.765  1.00 27.86  ? 356  CYS D C   1 
ATOM   4165 O  O   . CYS D  1 107 ? -1.769  -25.885 17.702  1.00 27.45  ? 356  CYS D O   1 
ATOM   4166 C  CB  . CYS D  1 107 ? -3.394  -26.302 14.947  1.00 29.60  ? 356  CYS D CB  1 
ATOM   4167 S  SG  . CYS D  1 107 ? -4.776  -26.907 13.994  1.00 31.82  ? 356  CYS D SG  1 
ATOM   4168 N  N   . ALA D  1 108 ? -0.564  -27.205 16.328  1.00 25.03  ? 357  ALA D N   1 
ATOM   4169 C  CA  . ALA D  1 108 ? 0.694   -26.859 16.969  1.00 25.82  ? 357  ALA D CA  1 
ATOM   4170 C  C   . ALA D  1 108 ? 1.481   -25.770 16.242  1.00 28.79  ? 357  ALA D C   1 
ATOM   4171 O  O   . ALA D  1 108 ? 1.523   -25.728 15.017  1.00 29.10  ? 357  ALA D O   1 
ATOM   4172 C  CB  . ALA D  1 108 ? 1.548   -28.088 17.180  1.00 27.31  ? 357  ALA D CB  1 
ATOM   4173 N  N   . GLU D  1 109 ? 2.102   -24.891 17.042  1.00 28.98  ? 358  GLU D N   1 
ATOM   4174 C  CA  . GLU D  1 109 ? 2.918   -23.790 16.562  1.00 28.07  ? 358  GLU D CA  1 
ATOM   4175 C  C   . GLU D  1 109 ? 4.237   -23.756 17.313  1.00 27.20  ? 358  GLU D C   1 
ATOM   4176 O  O   . GLU D  1 109 ? 4.341   -24.254 18.430  1.00 23.96  ? 358  GLU D O   1 
ATOM   4177 C  CB  . GLU D  1 109 ? 2.250   -22.444 16.824  1.00 28.63  ? 358  GLU D CB  1 
ATOM   4178 C  CG  . GLU D  1 109 ? 1.830   -22.290 18.281  1.00 28.56  ? 358  GLU D CG  1 
ATOM   4179 C  CD  . GLU D  1 109 ? 1.413   -20.899 18.664  1.00 29.36  ? 358  GLU D CD  1 
ATOM   4180 O  OE1 . GLU D  1 109 ? 0.862   -20.772 19.786  1.00 28.95  ? 358  GLU D OE1 1 
ATOM   4181 O  OE2 . GLU D  1 109 ? 1.623   -19.935 17.891  1.00 27.79  ? 358  GLU D OE2 1 
ATOM   4182 N  N   . PHE D  1 110 ? 5.228   -23.105 16.706  1.00 24.61  ? 359  PHE D N   1 
ATOM   4183 C  CA  . PHE D  1 110 ? 6.447   -22.776 17.385  1.00 26.16  ? 359  PHE D CA  1 
ATOM   4184 C  C   . PHE D  1 110 ? 6.100   -21.483 18.113  1.00 27.44  ? 359  PHE D C   1 
ATOM   4185 O  O   . PHE D  1 110 ? 5.650   -20.564 17.509  1.00 28.70  ? 359  PHE D O   1 
ATOM   4186 C  CB  . PHE D  1 110 ? 7.576   -22.504 16.397  1.00 25.80  ? 359  PHE D CB  1 
ATOM   4187 C  CG  . PHE D  1 110 ? 7.905   -23.674 15.504  1.00 25.15  ? 359  PHE D CG  1 
ATOM   4188 C  CD1 . PHE D  1 110 ? 8.825   -24.619 15.905  1.00 25.93  ? 359  PHE D CD1 1 
ATOM   4189 C  CD2 . PHE D  1 110 ? 7.298   -23.801 14.266  1.00 25.14  ? 359  PHE D CD2 1 
ATOM   4190 C  CE1 . PHE D  1 110 ? 9.137   -25.705 15.088  1.00 27.13  ? 359  PHE D CE1 1 
ATOM   4191 C  CE2 . PHE D  1 110 ? 7.625   -24.868 13.404  1.00 28.30  ? 359  PHE D CE2 1 
ATOM   4192 C  CZ  . PHE D  1 110 ? 8.542   -25.822 13.825  1.00 28.90  ? 359  PHE D CZ  1 
ATOM   4193 N  N   . SER D  1 111 ? 6.268   -21.450 19.412  1.00 30.44  ? 360  SER D N   1 
ATOM   4194 C  CA  . SER D  1 111 ? 5.930   -20.280 20.188  1.00 33.86  ? 360  SER D CA  1 
ATOM   4195 C  C   . SER D  1 111 ? 6.948   -20.135 21.297  1.00 32.52  ? 360  SER D C   1 
ATOM   4196 O  O   . SER D  1 111 ? 7.013   -20.938 22.204  1.00 27.97  ? 360  SER D O   1 
ATOM   4197 C  CB  . SER D  1 111 ? 4.547   -20.436 20.759  1.00 36.56  ? 360  SER D CB  1 
ATOM   4198 O  OG  . SER D  1 111 ? 4.350   -19.481 21.761  1.00 37.82  ? 360  SER D OG  1 
ATOM   4199 N  N   . GLY D  1 112 ? 7.772   -19.116 21.189  1.00 35.89  ? 361  GLY D N   1 
ATOM   4200 C  CA  . GLY D  1 112 ? 8.786   -18.874 22.203  1.00 39.22  ? 361  GLY D CA  1 
ATOM   4201 C  C   . GLY D  1 112 ? 9.918   -19.865 22.047  1.00 37.83  ? 361  GLY D C   1 
ATOM   4202 O  O   . GLY D  1 112 ? 10.469  -20.001 20.959  1.00 38.61  ? 361  GLY D O   1 
ATOM   4203 N  N   . ASN D  1 113 ? 10.261  -20.573 23.121  1.00 36.87  ? 362  ASN D N   1 
ATOM   4204 C  CA  . ASN D  1 113 ? 11.373  -21.526 23.047  1.00 41.65  ? 362  ASN D CA  1 
ATOM   4205 C  C   . ASN D  1 113 ? 10.989  -22.951 22.662  1.00 39.61  ? 362  ASN D C   1 
ATOM   4206 O  O   . ASN D  1 113 ? 11.869  -23.789 22.485  1.00 40.84  ? 362  ASN D O   1 
ATOM   4207 C  CB  . ASN D  1 113 ? 12.167  -21.522 24.360  1.00 45.80  ? 362  ASN D CB  1 
ATOM   4208 C  CG  . ASN D  1 113 ? 13.003  -20.255 24.516  1.00 49.92  ? 362  ASN D CG  1 
ATOM   4209 O  OD1 . ASN D  1 113 ? 13.210  -19.797 25.633  1.00 57.41  ? 362  ASN D OD1 1 
ATOM   4210 N  ND2 . ASN D  1 113 ? 13.466  -19.669 23.391  1.00 45.31  ? 362  ASN D ND2 1 
ATOM   4211 N  N   . GLY D  1 114 ? 9.692   -23.210 22.502  1.00 35.75  ? 363  GLY D N   1 
ATOM   4212 C  CA  . GLY D  1 114 ? 9.192   -24.554 22.262  1.00 34.21  ? 363  GLY D CA  1 
ATOM   4213 C  C   . GLY D  1 114 ? 7.875   -24.499 21.556  1.00 30.79  ? 363  GLY D C   1 
ATOM   4214 O  O   . GLY D  1 114 ? 7.632   -23.566 20.819  1.00 33.71  ? 363  GLY D O   1 
ATOM   4215 N  N   . TRP D  1 115 ? 7.048   -25.518 21.780  1.00 28.65  ? 364  TRP D N   1 
ATOM   4216 C  CA  . TRP D  1 115 ? 5.808   -25.676 21.075  1.00 26.85  ? 364  TRP D CA  1 
ATOM   4217 C  C   . TRP D  1 115 ? 4.613   -25.351 21.922  1.00 25.71  ? 364  TRP D C   1 
ATOM   4218 O  O   . TRP D  1 115 ? 4.615   -25.557 23.136  1.00 26.91  ? 364  TRP D O   1 
ATOM   4219 C  CB  . TRP D  1 115 ? 5.611   -27.113 20.585  1.00 26.88  ? 364  TRP D CB  1 
ATOM   4220 C  CG  . TRP D  1 115 ? 6.667   -27.708 19.685  1.00 26.68  ? 364  TRP D CG  1 
ATOM   4221 C  CD1 . TRP D  1 115 ? 7.749   -27.084 19.113  1.00 27.17  ? 364  TRP D CD1 1 
ATOM   4222 C  CD2 . TRP D  1 115 ? 6.720   -29.050 19.254  1.00 27.64  ? 364  TRP D CD2 1 
ATOM   4223 N  NE1 . TRP D  1 115 ? 8.472   -27.964 18.372  1.00 25.42  ? 364  TRP D NE1 1 
ATOM   4224 C  CE2 . TRP D  1 115 ? 7.848   -29.181 18.414  1.00 27.99  ? 364  TRP D CE2 1 
ATOM   4225 C  CE3 . TRP D  1 115 ? 5.926   -30.172 19.493  1.00 29.06  ? 364  TRP D CE3 1 
ATOM   4226 C  CZ2 . TRP D  1 115 ? 8.200   -30.404 17.824  1.00 26.66  ? 364  TRP D CZ2 1 
ATOM   4227 C  CZ3 . TRP D  1 115 ? 6.265   -31.390 18.878  1.00 26.97  ? 364  TRP D CZ3 1 
ATOM   4228 C  CH2 . TRP D  1 115 ? 7.383   -31.488 18.062  1.00 26.93  ? 364  TRP D CH2 1 
ATOM   4229 N  N   . ASN D  1 116 ? 3.537   -24.947 21.248  1.00 25.41  ? 365  ASN D N   1 
ATOM   4230 C  CA  . ASN D  1 116 ? 2.324   -24.660 21.942  1.00 26.69  ? 365  ASN D CA  1 
ATOM   4231 C  C   . ASN D  1 116 ? 1.190   -25.209 21.096  1.00 26.28  ? 365  ASN D C   1 
ATOM   4232 O  O   . ASN D  1 116 ? 1.235   -25.104 19.886  1.00 25.91  ? 365  ASN D O   1 
ATOM   4233 C  CB  . ASN D  1 116 ? 2.128   -23.137 22.176  1.00 25.22  ? 365  ASN D CB  1 
ATOM   4234 C  CG  . ASN D  1 116 ? 0.799   -22.841 22.840  1.00 28.57  ? 365  ASN D CG  1 
ATOM   4235 O  OD1 . ASN D  1 116 ? 0.427   -23.539 23.788  1.00 25.64  ? 365  ASN D OD1 1 
ATOM   4236 N  ND2 . ASN D  1 116 ? 0.047   -21.868 22.311  1.00 30.21  ? 365  ASN D ND2 1 
ATOM   4237 N  N   . ASP D  1 117 ? 0.139   -25.739 21.737  1.00 25.87  ? 366  ASP D N   1 
ATOM   4238 C  CA  . ASP D  1 117 ? -1.119  -25.897 21.035  1.00 24.52  ? 366  ASP D CA  1 
ATOM   4239 C  C   . ASP D  1 117 ? -1.963  -24.618 21.045  1.00 26.25  ? 366  ASP D C   1 
ATOM   4240 O  O   . ASP D  1 117 ? -2.114  -23.964 22.072  1.00 27.40  ? 366  ASP D O   1 
ATOM   4241 C  CB  . ASP D  1 117 ? -1.891  -27.123 21.530  1.00 25.54  ? 366  ASP D CB  1 
ATOM   4242 C  CG  . ASP D  1 117 ? -2.267  -27.067 23.022  1.00 25.54  ? 366  ASP D CG  1 
ATOM   4243 O  OD1 . ASP D  1 117 ? -1.543  -26.413 23.807  1.00 23.61  ? 366  ASP D OD1 1 
ATOM   4244 O  OD2 . ASP D  1 117 ? -3.250  -27.777 23.402  1.00 25.24  ? 366  ASP D OD2 1 
ATOM   4245 N  N   . ASP D  1 118 ? -2.477  -24.219 19.891  1.00 27.50  ? 367  ASP D N   1 
ATOM   4246 C  CA  . ASP D  1 118 ? -3.279  -22.990 19.840  1.00 27.57  ? 367  ASP D CA  1 
ATOM   4247 C  C   . ASP D  1 118 ? -4.473  -23.340 19.014  1.00 25.18  ? 367  ASP D C   1 
ATOM   4248 O  O   . ASP D  1 118 ? -4.577  -24.467 18.529  1.00 27.03  ? 367  ASP D O   1 
ATOM   4249 C  CB  . ASP D  1 118 ? -2.505  -21.793 19.242  1.00 27.69  ? 367  ASP D CB  1 
ATOM   4250 C  CG  . ASP D  1 118 ? -3.037  -20.392 19.750  1.00 31.55  ? 367  ASP D CG  1 
ATOM   4251 O  OD1 . ASP D  1 118 ? -4.094  -20.345 20.430  1.00 29.46  ? 367  ASP D OD1 1 
ATOM   4252 O  OD2 . ASP D  1 118 ? -2.363  -19.346 19.513  1.00 30.08  ? 367  ASP D OD2 1 
ATOM   4253 N  N   . LYS D  1 119 ? -5.354  -22.382 18.847  1.00 24.75  ? 368  LYS D N   1 
ATOM   4254 C  CA  . LYS D  1 119 ? -6.578  -22.527 18.104  1.00 27.94  ? 368  LYS D CA  1 
ATOM   4255 C  C   . LYS D  1 119 ? -6.293  -22.499 16.616  1.00 30.86  ? 368  LYS D C   1 
ATOM   4256 O  O   . LYS D  1 119 ? -5.638  -21.562 16.116  1.00 26.18  ? 368  LYS D O   1 
ATOM   4257 C  CB  . LYS D  1 119 ? -7.561  -21.416 18.442  1.00 29.84  ? 368  LYS D CB  1 
ATOM   4258 C  CG  . LYS D  1 119 ? -7.949  -21.397 19.918  1.00 33.93  ? 368  LYS D CG  1 
ATOM   4259 C  CD  . LYS D  1 119 ? -8.735  -20.165 20.266  1.00 42.20  ? 368  LYS D CD  1 
ATOM   4260 C  CE  . LYS D  1 119 ? -8.993  -20.097 21.774  1.00 53.22  ? 368  LYS D CE  1 
ATOM   4261 N  NZ  . LYS D  1 119 ? -8.124  -19.106 22.464  1.00 56.60  ? 368  LYS D NZ  1 
ATOM   4262 N  N   . CYS D  1 120 ? -6.892  -23.476 15.926  1.00 28.73  ? 369  CYS D N   1 
ATOM   4263 C  CA  . CYS D  1 120 ? -6.644  -23.732 14.496  1.00 30.35  ? 369  CYS D CA  1 
ATOM   4264 C  C   . CYS D  1 120 ? -7.137  -22.620 13.588  1.00 30.63  ? 369  CYS D C   1 
ATOM   4265 O  O   . CYS D  1 120 ? -6.655  -22.476 12.456  1.00 27.86  ? 369  CYS D O   1 
ATOM   4266 C  CB  . CYS D  1 120 ? -7.239  -25.081 14.108  1.00 30.61  ? 369  CYS D CB  1 
ATOM   4267 S  SG  . CYS D  1 120 ? -6.464  -26.403 15.058  1.00 35.15  ? 369  CYS D SG  1 
ATOM   4268 N  N   . ASN D  1 121 ? -8.048  -21.789 14.096  1.00 29.14  ? 370  ASN D N   1 
ATOM   4269 C  CA  . ASN D  1 121 ? -8.647  -20.749 13.264  1.00 30.35  ? 370  ASN D CA  1 
ATOM   4270 C  C   . ASN D  1 121 ? -7.898  -19.426 13.333  1.00 29.07  ? 370  ASN D C   1 
ATOM   4271 O  O   . ASN D  1 121 ? -8.267  -18.465 12.656  1.00 27.92  ? 370  ASN D O   1 
ATOM   4272 C  CB  . ASN D  1 121 ? -10.145 -20.584 13.571  1.00 33.67  ? 370  ASN D CB  1 
ATOM   4273 C  CG  . ASN D  1 121 ? -10.404 -20.009 14.973  1.00 39.41  ? 370  ASN D CG  1 
ATOM   4274 O  OD1 . ASN D  1 121 ? -9.524  -20.013 15.826  1.00 41.40  ? 370  ASN D OD1 1 
ATOM   4275 N  ND2 . ASN D  1 121 ? -11.621 -19.512 15.200  1.00 42.07  ? 370  ASN D ND2 1 
ATOM   4276 N  N   . LEU D  1 122 ? -6.821  -19.372 14.105  1.00 28.56  ? 371  LEU D N   1 
ATOM   4277 C  CA  . LEU D  1 122 ? -6.031  -18.146 14.145  1.00 28.86  ? 371  LEU D CA  1 
ATOM   4278 C  C   . LEU D  1 122 ? -5.012  -18.084 12.996  1.00 30.72  ? 371  LEU D C   1 
ATOM   4279 O  O   . LEU D  1 122 ? -4.641  -19.079 12.409  1.00 31.15  ? 371  LEU D O   1 
ATOM   4280 C  CB  . LEU D  1 122 ? -5.355  -18.013 15.469  1.00 29.28  ? 371  LEU D CB  1 
ATOM   4281 C  CG  . LEU D  1 122 ? -6.296  -17.848 16.670  1.00 30.74  ? 371  LEU D CG  1 
ATOM   4282 C  CD1 . LEU D  1 122 ? -5.469  -17.848 17.935  1.00 29.20  ? 371  LEU D CD1 1 
ATOM   4283 C  CD2 . LEU D  1 122 ? -7.146  -16.600 16.579  1.00 28.09  ? 371  LEU D CD2 1 
ATOM   4284 N  N   . ALA D  1 123 ? -4.572  -16.890 12.694  1.00 30.02  ? 372  ALA D N   1 
ATOM   4285 C  CA  . ALA D  1 123 ? -3.689  -16.661 11.596  1.00 27.79  ? 372  ALA D CA  1 
ATOM   4286 C  C   . ALA D  1 123 ? -2.296  -16.632 12.223  1.00 29.40  ? 372  ALA D C   1 
ATOM   4287 O  O   . ALA D  1 123 ? -2.068  -15.887 13.179  1.00 28.79  ? 372  ALA D O   1 
ATOM   4288 C  CB  . ALA D  1 123 ? -4.028  -15.330 10.935  1.00 30.13  ? 372  ALA D CB  1 
ATOM   4289 N  N   . LYS D  1 124 ? -1.395  -17.476 11.710  1.00 25.10  ? 373  LYS D N   1 
ATOM   4290 C  CA  . LYS D  1 124 ? -0.002  -17.525 12.111  1.00 25.05  ? 373  LYS D CA  1 
ATOM   4291 C  C   . LYS D  1 124 ? 0.859   -17.676 10.842  1.00 26.58  ? 373  LYS D C   1 
ATOM   4292 O  O   . LYS D  1 124 ? 0.341   -17.949 9.748   1.00 25.16  ? 373  LYS D O   1 
ATOM   4293 C  CB  . LYS D  1 124 ? 0.273   -18.703 13.018  1.00 26.57  ? 373  LYS D CB  1 
ATOM   4294 C  CG  . LYS D  1 124 ? -0.504  -18.706 14.340  1.00 26.23  ? 373  LYS D CG  1 
ATOM   4295 C  CD  . LYS D  1 124 ? -0.154  -19.911 15.167  1.00 26.18  ? 373  LYS D CD  1 
ATOM   4296 C  CE  . LYS D  1 124 ? -1.005  -19.991 16.436  1.00 29.81  ? 373  LYS D CE  1 
ATOM   4297 N  NZ  . LYS D  1 124 ? -0.816  -18.799 17.298  1.00 30.00  ? 373  LYS D NZ  1 
ATOM   4298 N  N   . PHE D  1 125 ? 2.171   -17.551 10.999  1.00 25.03  ? 374  PHE D N   1 
ATOM   4299 C  CA  . PHE D  1 125 ? 3.056   -17.758 9.864   1.00 25.51  ? 374  PHE D CA  1 
ATOM   4300 C  C   . PHE D  1 125 ? 3.072   -19.250 9.716   1.00 25.31  ? 374  PHE D C   1 
ATOM   4301 O  O   . PHE D  1 125 ? 2.449   -19.934 10.517  1.00 23.82  ? 374  PHE D O   1 
ATOM   4302 C  CB  . PHE D  1 125 ? 4.425   -17.160 10.128  1.00 26.43  ? 374  PHE D CB  1 
ATOM   4303 C  CG  . PHE D  1 125 ? 4.402   -15.652 10.166  1.00 28.84  ? 374  PHE D CG  1 
ATOM   4304 C  CD1 . PHE D  1 125 ? 4.063   -14.975 11.351  1.00 29.47  ? 374  PHE D CD1 1 
ATOM   4305 C  CD2 . PHE D  1 125 ? 4.702   -14.913 9.034   1.00 28.33  ? 374  PHE D CD2 1 
ATOM   4306 C  CE1 . PHE D  1 125 ? 4.031   -13.582 11.388  1.00 32.68  ? 374  PHE D CE1 1 
ATOM   4307 C  CE2 . PHE D  1 125 ? 4.639   -13.526 9.063   1.00 29.63  ? 374  PHE D CE2 1 
ATOM   4308 C  CZ  . PHE D  1 125 ? 4.281   -12.859 10.222  1.00 31.13  ? 374  PHE D CZ  1 
ATOM   4309 N  N   . TRP D  1 126 ? 3.708   -19.757 8.673   1.00 23.58  ? 375  TRP D N   1 
ATOM   4310 C  CA  . TRP D  1 126 ? 3.793   -21.188 8.498   1.00 23.84  ? 375  TRP D CA  1 
ATOM   4311 C  C   . TRP D  1 126 ? 5.105   -21.523 7.747   1.00 25.50  ? 375  TRP D C   1 
ATOM   4312 O  O   . TRP D  1 126 ? 5.732   -20.669 7.071   1.00 22.78  ? 375  TRP D O   1 
ATOM   4313 C  CB  . TRP D  1 126 ? 2.535   -21.743 7.761   1.00 26.55  ? 375  TRP D CB  1 
ATOM   4314 C  CG  . TRP D  1 126 ? 2.519   -21.438 6.294   1.00 26.39  ? 375  TRP D CG  1 
ATOM   4315 C  CD1 . TRP D  1 126 ? 3.143   -22.166 5.287   1.00 26.54  ? 375  TRP D CD1 1 
ATOM   4316 C  CD2 . TRP D  1 126 ? 1.943   -20.286 5.652   1.00 27.73  ? 375  TRP D CD2 1 
ATOM   4317 N  NE1 . TRP D  1 126 ? 2.995   -21.519 4.087   1.00 26.40  ? 375  TRP D NE1 1 
ATOM   4318 C  CE2 . TRP D  1 126 ? 2.264   -20.375 4.269   1.00 28.37  ? 375  TRP D CE2 1 
ATOM   4319 C  CE3 . TRP D  1 126 ? 1.212   -19.182 6.107   1.00 28.42  ? 375  TRP D CE3 1 
ATOM   4320 C  CZ2 . TRP D  1 126 ? 1.845   -19.412 3.336   1.00 29.02  ? 375  TRP D CZ2 1 
ATOM   4321 C  CZ3 . TRP D  1 126 ? 0.813   -18.208 5.186   1.00 30.53  ? 375  TRP D CZ3 1 
ATOM   4322 C  CH2 . TRP D  1 126 ? 1.125   -18.334 3.811   1.00 30.22  ? 375  TRP D CH2 1 
ATOM   4323 N  N   . ILE D  1 127 ? 5.490   -22.782 7.847   1.00 25.15  ? 376  ILE D N   1 
ATOM   4324 C  CA  . ILE D  1 127 ? 6.647   -23.277 7.172   1.00 25.98  ? 376  ILE D CA  1 
ATOM   4325 C  C   . ILE D  1 127 ? 6.297   -24.516 6.373   1.00 26.16  ? 376  ILE D C   1 
ATOM   4326 O  O   . ILE D  1 127 ? 5.642   -25.413 6.889   1.00 24.00  ? 376  ILE D O   1 
ATOM   4327 C  CB  . ILE D  1 127 ? 7.740   -23.604 8.185   1.00 25.53  ? 376  ILE D CB  1 
ATOM   4328 C  CG1 . ILE D  1 127 ? 8.256   -22.303 8.804   1.00 27.49  ? 376  ILE D CG1 1 
ATOM   4329 C  CG2 . ILE D  1 127 ? 8.855   -24.373 7.503   1.00 27.00  ? 376  ILE D CG2 1 
ATOM   4330 C  CD1 . ILE D  1 127 ? 9.223   -22.468 9.960   1.00 30.03  ? 376  ILE D CD1 1 
ATOM   4331 N  N   . CYS D  1 128 ? 6.690   -24.522 5.092   1.00 27.41  ? 377  CYS D N   1 
ATOM   4332 C  CA  . CYS D  1 128 ? 6.504   -25.662 4.215   1.00 29.97  ? 377  CYS D CA  1 
ATOM   4333 C  C   . CYS D  1 128 ? 7.833   -26.411 4.090   1.00 32.52  ? 377  CYS D C   1 
ATOM   4334 O  O   . CYS D  1 128 ? 8.902   -25.819 4.180   1.00 28.30  ? 377  CYS D O   1 
ATOM   4335 C  CB  . CYS D  1 128 ? 6.074   -25.246 2.807   1.00 31.28  ? 377  CYS D CB  1 
ATOM   4336 S  SG  . CYS D  1 128 ? 4.596   -24.258 2.677   1.00 33.74  ? 377  CYS D SG  1 
ATOM   4337 N  N   . LYS D  1 129 ? 7.743   -27.715 3.843   1.00 33.21  ? 378  LYS D N   1 
ATOM   4338 C  CA  . LYS D  1 129 ? 8.913   -28.574 3.750   1.00 32.10  ? 378  LYS D CA  1 
ATOM   4339 C  C   . LYS D  1 129 ? 8.727   -29.498 2.560   1.00 32.69  ? 378  LYS D C   1 
ATOM   4340 O  O   . LYS D  1 129 ? 7.615   -29.955 2.326   1.00 27.12  ? 378  LYS D O   1 
ATOM   4341 C  CB  . LYS D  1 129 ? 9.052   -29.432 4.988   1.00 30.73  ? 378  LYS D CB  1 
ATOM   4342 C  CG  . LYS D  1 129 ? 10.296  -30.335 5.016   1.00 29.54  ? 378  LYS D CG  1 
ATOM   4343 C  CD  . LYS D  1 129 ? 10.103  -31.448 6.026   1.00 31.30  ? 378  LYS D CD  1 
ATOM   4344 C  CE  . LYS D  1 129 ? 11.291  -32.392 6.117   1.00 32.47  ? 378  LYS D CE  1 
ATOM   4345 N  NZ  . LYS D  1 129 ? 11.124  -33.268 7.299   1.00 32.33  ? 378  LYS D NZ  1 
ATOM   4346 N  N   . LYS D  1 130 ? 9.828   -29.750 1.846   1.00 32.18  ? 379  LYS D N   1 
ATOM   4347 C  CA  . LYS D  1 130 ? 9.919   -30.813 0.868   1.00 33.65  ? 379  LYS D CA  1 
ATOM   4348 C  C   . LYS D  1 130 ? 11.370  -31.352 0.748   1.00 32.03  ? 379  LYS D C   1 
ATOM   4349 O  O   . LYS D  1 130 ? 12.282  -30.671 1.087   1.00 32.58  ? 379  LYS D O   1 
ATOM   4350 C  CB  . LYS D  1 130 ? 9.377   -30.339 -0.469  1.00 36.98  ? 379  LYS D CB  1 
ATOM   4351 C  CG  . LYS D  1 130 ? 10.273  -29.387 -1.222  1.00 40.71  ? 379  LYS D CG  1 
ATOM   4352 C  CD  . LYS D  1 130 ? 9.861   -29.298 -2.676  1.00 46.32  ? 379  LYS D CD  1 
ATOM   4353 C  CE  . LYS D  1 130 ? 8.996   -28.079 -2.904  1.00 50.76  ? 379  LYS D CE  1 
ATOM   4354 N  NZ  . LYS D  1 130 ? 8.304   -28.166 -4.207  1.00 52.58  ? 379  LYS D NZ  1 
ATOM   4355 N  N   . SER D  1 131 ? 11.545  -32.603 0.338   1.00 33.79  ? 380  SER D N   1 
ATOM   4356 C  CA  . SER D  1 131 ? 12.862  -33.177 0.014   1.00 38.12  ? 380  SER D CA  1 
ATOM   4357 C  C   . SER D  1 131 ? 13.710  -32.334 -0.921  1.00 37.05  ? 380  SER D C   1 
ATOM   4358 O  O   . SER D  1 131 ? 13.190  -31.707 -1.859  1.00 31.34  ? 380  SER D O   1 
ATOM   4359 C  CB  . SER D  1 131 ? 12.682  -34.503 -0.697  1.00 40.21  ? 380  SER D CB  1 
ATOM   4360 O  OG  . SER D  1 131 ? 11.998  -35.375 0.150   1.00 45.50  ? 380  SER D OG  1 
ATOM   4361 N  N   . ALA D  1 132 ? 15.010  -32.298 -0.651  1.00 37.93  ? 381  ALA D N   1 
ATOM   4362 C  CA  . ALA D  1 132 ? 15.942  -31.708 -1.613  1.00 43.93  ? 381  ALA D CA  1 
ATOM   4363 C  C   . ALA D  1 132 ? 16.081  -32.704 -2.756  1.00 42.59  ? 381  ALA D C   1 
ATOM   4364 O  O   . ALA D  1 132 ? 15.859  -33.873 -2.549  1.00 41.39  ? 381  ALA D O   1 
ATOM   4365 C  CB  . ALA D  1 132 ? 17.281  -31.445 -0.963  1.00 44.33  ? 381  ALA D CB  1 
ATOM   4366 N  N   . ALA D  1 133 ? 16.390  -32.239 -3.959  1.00 49.86  ? 382  ALA D N   1 
ATOM   4367 C  CA  . ALA D  1 133 ? 16.644  -33.164 -5.085  1.00 57.24  ? 382  ALA D CA  1 
ATOM   4368 C  C   . ALA D  1 133 ? 18.094  -33.628 -5.011  1.00 60.47  ? 382  ALA D C   1 
ATOM   4369 O  O   . ALA D  1 133 ? 18.873  -33.108 -4.210  1.00 58.35  ? 382  ALA D O   1 
ATOM   4370 C  CB  . ALA D  1 133 ? 16.352  -32.487 -6.417  1.00 55.27  ? 382  ALA D CB  1 
ATOM   4371 N  N   . SER D  1 134 ? 18.463  -34.597 -5.842  1.00 78.16  ? 383  SER D N   1 
ATOM   4372 C  CA  . SER D  1 134 ? 19.858  -35.090 -5.885  1.00 87.08  ? 383  SER D CA  1 
ATOM   4373 C  C   . SER D  1 134 ? 20.742  -34.250 -6.807  1.00 84.72  ? 383  SER D C   1 
ATOM   4374 O  O   . SER D  1 134 ? 20.397  -34.062 -7.964  1.00 88.46  ? 383  SER D O   1 
ATOM   4375 C  CB  . SER D  1 134 ? 19.871  -36.537 -6.368  1.00 93.36  ? 383  SER D CB  1 
ATOM   4376 O  OG  . SER D  1 134 ? 18.977  -37.321 -5.602  1.00 99.26  ? 383  SER D OG  1 
ATOM   4377 N  N   . CYS D  1 135 ? 21.868  -33.746 -6.308  1.00 88.02  ? 384  CYS D N   1 
ATOM   4378 C  CA  . CYS D  1 135 ? 22.822  -33.004 -7.170  1.00 101.05 ? 384  CYS D CA  1 
ATOM   4379 C  C   . CYS D  1 135 ? 24.229  -33.613 -7.228  1.00 108.93 ? 384  CYS D C   1 
ATOM   4380 O  O   . CYS D  1 135 ? 24.533  -34.590 -6.547  1.00 126.24 ? 384  CYS D O   1 
ATOM   4381 C  CB  . CYS D  1 135 ? 22.952  -31.541 -6.741  1.00 96.48  ? 384  CYS D CB  1 
ATOM   4382 S  SG  . CYS D  1 135 ? 21.524  -30.483 -7.040  1.00 79.77  ? 384  CYS D SG  1 
ATOM   4383 N  N   . LEU E  1 3   ? -22.634 -5.459  83.053  1.00 63.39  ? 252  LEU E N   1 
ATOM   4384 C  CA  . LEU E  1 3   ? -21.940 -5.481  81.721  1.00 67.61  ? 252  LEU E CA  1 
ATOM   4385 C  C   . LEU E  1 3   ? -20.531 -6.078  81.836  1.00 63.96  ? 252  LEU E C   1 
ATOM   4386 O  O   . LEU E  1 3   ? -19.698 -5.606  82.606  1.00 60.88  ? 252  LEU E O   1 
ATOM   4387 C  CB  . LEU E  1 3   ? -21.890 -4.075  81.108  1.00 67.53  ? 252  LEU E CB  1 
ATOM   4388 C  CG  . LEU E  1 3   ? -21.200 -3.863  79.747  1.00 75.52  ? 252  LEU E CG  1 
ATOM   4389 C  CD1 . LEU E  1 3   ? -21.454 -4.978  78.730  1.00 74.96  ? 252  LEU E CD1 1 
ATOM   4390 C  CD2 . LEU E  1 3   ? -21.630 -2.510  79.176  1.00 75.17  ? 252  LEU E CD2 1 
ATOM   4391 N  N   . CYS E  1 4   ? -20.270 -7.143  81.090  1.00 63.08  ? 253  CYS E N   1 
ATOM   4392 C  CA  . CYS E  1 4   ? -18.959 -7.782  81.152  1.00 58.26  ? 253  CYS E CA  1 
ATOM   4393 C  C   . CYS E  1 4   ? -18.014 -7.094  80.177  1.00 50.80  ? 253  CYS E C   1 
ATOM   4394 O  O   . CYS E  1 4   ? -18.378 -6.832  79.031  1.00 50.27  ? 253  CYS E O   1 
ATOM   4395 C  CB  . CYS E  1 4   ? -19.072 -9.278  80.852  1.00 59.46  ? 253  CYS E CB  1 
ATOM   4396 S  SG  . CYS E  1 4   ? -17.519 -10.202 80.999  1.00 59.31  ? 253  CYS E SG  1 
ATOM   4397 N  N   . HIS E  1 5   ? -16.814 -6.783  80.657  1.00 44.63  ? 254  HIS E N   1 
ATOM   4398 C  CA  . HIS E  1 5   ? -15.713 -6.392  79.792  1.00 42.22  ? 254  HIS E CA  1 
ATOM   4399 C  C   . HIS E  1 5   ? -14.562 -7.393  79.881  1.00 40.31  ? 254  HIS E C   1 
ATOM   4400 O  O   . HIS E  1 5   ? -14.301 -7.978  80.944  1.00 40.87  ? 254  HIS E O   1 
ATOM   4401 C  CB  . HIS E  1 5   ? -15.187 -5.040  80.199  1.00 42.14  ? 254  HIS E CB  1 
ATOM   4402 C  CG  . HIS E  1 5   ? -16.240 -4.006  80.376  1.00 40.86  ? 254  HIS E CG  1 
ATOM   4403 N  ND1 . HIS E  1 5   ? -16.573 -3.108  79.381  1.00 37.62  ? 254  HIS E ND1 1 
ATOM   4404 C  CD2 . HIS E  1 5   ? -17.011 -3.696  81.448  1.00 40.18  ? 254  HIS E CD2 1 
ATOM   4405 C  CE1 . HIS E  1 5   ? -17.493 -2.273  79.844  1.00 40.29  ? 254  HIS E CE1 1 
ATOM   4406 N  NE2 . HIS E  1 5   ? -17.788 -2.619  81.089  1.00 40.49  ? 254  HIS E NE2 1 
ATOM   4407 N  N   . PRO E  1 6   ? -13.840 -7.579  78.774  1.00 35.11  ? 255  PRO E N   1 
ATOM   4408 C  CA  . PRO E  1 6   ? -12.761 -8.583  78.739  1.00 35.64  ? 255  PRO E CA  1 
ATOM   4409 C  C   . PRO E  1 6   ? -11.617 -8.295  79.718  1.00 32.82  ? 255  PRO E C   1 
ATOM   4410 O  O   . PRO E  1 6   ? -11.040 -9.221  80.236  1.00 36.47  ? 255  PRO E O   1 
ATOM   4411 C  CB  . PRO E  1 6   ? -12.241 -8.534  77.300  1.00 34.26  ? 255  PRO E CB  1 
ATOM   4412 C  CG  . PRO E  1 6   ? -13.014 -7.495  76.585  1.00 35.75  ? 255  PRO E CG  1 
ATOM   4413 C  CD  . PRO E  1 6   ? -14.069 -6.916  77.496  1.00 36.00  ? 255  PRO E CD  1 
ATOM   4414 N  N   . CYS E  1 7   ? -11.329 -7.020  79.973  1.00 31.60  ? 256  CYS E N   1 
ATOM   4415 C  CA  . CYS E  1 7   ? -10.247 -6.611  80.855  1.00 30.20  ? 256  CYS E CA  1 
ATOM   4416 C  C   . CYS E  1 7   ? -10.737 -5.685  81.945  1.00 30.39  ? 256  CYS E C   1 
ATOM   4417 O  O   . CYS E  1 7   ? -11.758 -5.016  81.780  1.00 29.60  ? 256  CYS E O   1 
ATOM   4418 C  CB  . CYS E  1 7   ? -9.224  -5.863  80.036  1.00 30.25  ? 256  CYS E CB  1 
ATOM   4419 S  SG  . CYS E  1 7   ? -8.413  -6.912  78.829  1.00 33.51  ? 256  CYS E SG  1 
ATOM   4420 N  N   . PRO E  1 8   ? -9.988  -5.598  83.041  1.00 32.02  ? 257  PRO E N   1 
ATOM   4421 C  CA  . PRO E  1 8   ? -10.365 -4.564  83.984  1.00 33.05  ? 257  PRO E CA  1 
ATOM   4422 C  C   . PRO E  1 8   ? -10.190 -3.145  83.407  1.00 34.61  ? 257  PRO E C   1 
ATOM   4423 O  O   . PRO E  1 8   ? -9.507  -2.931  82.391  1.00 33.01  ? 257  PRO E O   1 
ATOM   4424 C  CB  . PRO E  1 8   ? -9.450  -4.842  85.206  1.00 32.41  ? 257  PRO E CB  1 
ATOM   4425 C  CG  . PRO E  1 8   ? -8.962  -6.228  85.027  1.00 31.64  ? 257  PRO E CG  1 
ATOM   4426 C  CD  . PRO E  1 8   ? -8.837  -6.383  83.539  1.00 32.21  ? 257  PRO E CD  1 
ATOM   4427 N  N   . TRP E  1 9   ? -10.843 -2.194  84.048  1.00 31.79  ? 258  TRP E N   1 
ATOM   4428 C  CA  . TRP E  1 9   ? -10.894 -0.863  83.542  1.00 34.93  ? 258  TRP E CA  1 
ATOM   4429 C  C   . TRP E  1 9   ? -9.493  -0.257  83.536  1.00 36.36  ? 258  TRP E C   1 
ATOM   4430 O  O   . TRP E  1 9   ? -8.743  -0.349  84.510  1.00 34.73  ? 258  TRP E O   1 
ATOM   4431 C  CB  . TRP E  1 9   ? -11.825 -0.059  84.418  1.00 37.64  ? 258  TRP E CB  1 
ATOM   4432 C  CG  . TRP E  1 9   ? -12.322 1.278   83.877  1.00 40.09  ? 258  TRP E CG  1 
ATOM   4433 C  CD1 . TRP E  1 9   ? -11.707 2.125   82.978  1.00 40.91  ? 258  TRP E CD1 1 
ATOM   4434 C  CD2 . TRP E  1 9   ? -13.519 1.929   84.276  1.00 39.17  ? 258  TRP E CD2 1 
ATOM   4435 N  NE1 . TRP E  1 9   ? -12.466 3.239   82.789  1.00 38.17  ? 258  TRP E NE1 1 
ATOM   4436 C  CE2 . TRP E  1 9   ? -13.584 3.150   83.578  1.00 38.74  ? 258  TRP E CE2 1 
ATOM   4437 C  CE3 . TRP E  1 9   ? -14.546 1.597   85.164  1.00 40.34  ? 258  TRP E CE3 1 
ATOM   4438 C  CZ2 . TRP E  1 9   ? -14.648 4.042   83.734  1.00 39.77  ? 258  TRP E CZ2 1 
ATOM   4439 C  CZ3 . TRP E  1 9   ? -15.597 2.485   85.327  1.00 40.09  ? 258  TRP E CZ3 1 
ATOM   4440 C  CH2 . TRP E  1 9   ? -15.649 3.688   84.600  1.00 40.12  ? 258  TRP E CH2 1 
ATOM   4441 N  N   . GLU E  1 10  ? -9.131  0.316   82.402  1.00 36.40  ? 259  GLU E N   1 
ATOM   4442 C  CA  . GLU E  1 10  ? -7.809  0.914   82.216  1.00 39.32  ? 259  GLU E CA  1 
ATOM   4443 C  C   . GLU E  1 10  ? -6.726  -0.050  81.815  1.00 36.49  ? 259  GLU E C   1 
ATOM   4444 O  O   . GLU E  1 10  ? -5.639  0.400   81.505  1.00 39.97  ? 259  GLU E O   1 
ATOM   4445 C  CB  . GLU E  1 10  ? -7.314  1.681   83.455  1.00 38.95  ? 259  GLU E CB  1 
ATOM   4446 C  CG  . GLU E  1 10  ? -8.311  2.692   83.981  1.00 43.45  ? 259  GLU E CG  1 
ATOM   4447 C  CD  . GLU E  1 10  ? -7.695  3.713   84.882  1.00 43.51  ? 259  GLU E CD  1 
ATOM   4448 O  OE1 . GLU E  1 10  ? -8.447  4.271   85.700  1.00 47.50  ? 259  GLU E OE1 1 
ATOM   4449 O  OE2 . GLU E  1 10  ? -6.483  3.974   84.748  1.00 48.94  ? 259  GLU E OE2 1 
ATOM   4450 N  N   . TRP E  1 11  ? -6.977  -1.352  81.835  1.00 34.85  ? 260  TRP E N   1 
ATOM   4451 C  CA  . TRP E  1 11  ? -5.992  -2.282  81.288  1.00 33.43  ? 260  TRP E CA  1 
ATOM   4452 C  C   . TRP E  1 11  ? -6.138  -2.354  79.784  1.00 33.94  ? 260  TRP E C   1 
ATOM   4453 O  O   . TRP E  1 11  ? -7.181  -2.067  79.247  1.00 36.70  ? 260  TRP E O   1 
ATOM   4454 C  CB  . TRP E  1 11  ? -6.160  -3.682  81.852  1.00 33.26  ? 260  TRP E CB  1 
ATOM   4455 C  CG  . TRP E  1 11  ? -5.929  -3.821  83.290  1.00 31.12  ? 260  TRP E CG  1 
ATOM   4456 C  CD1 . TRP E  1 11  ? -6.375  -3.002  84.248  1.00 32.37  ? 260  TRP E CD1 1 
ATOM   4457 C  CD2 . TRP E  1 11  ? -5.225  -4.882  83.956  1.00 29.39  ? 260  TRP E CD2 1 
ATOM   4458 N  NE1 . TRP E  1 11  ? -5.995  -3.459  85.476  1.00 31.84  ? 260  TRP E NE1 1 
ATOM   4459 C  CE2 . TRP E  1 11  ? -5.298  -4.624  85.327  1.00 30.44  ? 260  TRP E CE2 1 
ATOM   4460 C  CE3 . TRP E  1 11  ? -4.555  -6.028  83.520  1.00 29.95  ? 260  TRP E CE3 1 
ATOM   4461 C  CZ2 . TRP E  1 11  ? -4.724  -5.458  86.283  1.00 28.59  ? 260  TRP E CZ2 1 
ATOM   4462 C  CZ3 . TRP E  1 11  ? -3.970  -6.859  84.466  1.00 27.86  ? 260  TRP E CZ3 1 
ATOM   4463 C  CH2 . TRP E  1 11  ? -4.081  -6.581  85.823  1.00 28.63  ? 260  TRP E CH2 1 
ATOM   4464 N  N   . THR E  1 12  ? -5.110  -2.826  79.108  1.00 31.16  ? 261  THR E N   1 
ATOM   4465 C  CA  . THR E  1 12  ? -5.114  -2.873  77.646  1.00 30.94  ? 261  THR E CA  1 
ATOM   4466 C  C   . THR E  1 12  ? -5.377  -4.310  77.212  1.00 29.52  ? 261  THR E C   1 
ATOM   4467 O  O   . THR E  1 12  ? -4.746  -5.221  77.705  1.00 27.24  ? 261  THR E O   1 
ATOM   4468 C  CB  . THR E  1 12  ? -3.757  -2.399  77.074  1.00 30.82  ? 261  THR E CB  1 
ATOM   4469 O  OG1 . THR E  1 12  ? -3.565  -1.016  77.409  1.00 31.15  ? 261  THR E OG1 1 
ATOM   4470 C  CG2 . THR E  1 12  ? -3.699  -2.529  75.558  1.00 31.25  ? 261  THR E CG2 1 
ATOM   4471 N  N   . PHE E  1 13  ? -6.322  -4.483  76.300  1.00 27.42  ? 262  PHE E N   1 
ATOM   4472 C  CA  . PHE E  1 13  ? -6.626  -5.757  75.748  1.00 31.33  ? 262  PHE E CA  1 
ATOM   4473 C  C   . PHE E  1 13  ? -5.672  -5.966  74.600  1.00 29.51  ? 262  PHE E C   1 
ATOM   4474 O  O   . PHE E  1 13  ? -5.491  -5.068  73.823  1.00 27.32  ? 262  PHE E O   1 
ATOM   4475 C  CB  . PHE E  1 13  ? -8.027  -5.782  75.172  1.00 32.40  ? 262  PHE E CB  1 
ATOM   4476 C  CG  . PHE E  1 13  ? -8.361  -7.078  74.495  1.00 32.34  ? 262  PHE E CG  1 
ATOM   4477 C  CD1 . PHE E  1 13  ? -8.887  -8.131  75.223  1.00 33.19  ? 262  PHE E CD1 1 
ATOM   4478 C  CD2 . PHE E  1 13  ? -8.113  -7.251  73.134  1.00 35.37  ? 262  PHE E CD2 1 
ATOM   4479 C  CE1 . PHE E  1 13  ? -9.199  -9.337  74.611  1.00 36.14  ? 262  PHE E CE1 1 
ATOM   4480 C  CE2 . PHE E  1 13  ? -8.425  -8.457  72.508  1.00 36.52  ? 262  PHE E CE2 1 
ATOM   4481 C  CZ  . PHE E  1 13  ? -8.975  -9.496  73.252  1.00 35.69  ? 262  PHE E CZ  1 
ATOM   4482 N  N   . PHE E  1 14  ? -5.040  -7.124  74.536  1.00 27.28  ? 263  PHE E N   1 
ATOM   4483 C  CA  . PHE E  1 14  ? -4.233  -7.470  73.377  1.00 29.85  ? 263  PHE E CA  1 
ATOM   4484 C  C   . PHE E  1 14  ? -4.178  -8.991  73.243  1.00 30.12  ? 263  PHE E C   1 
ATOM   4485 O  O   . PHE E  1 14  ? -3.832  -9.702  74.209  1.00 29.65  ? 263  PHE E O   1 
ATOM   4486 C  CB  . PHE E  1 14  ? -2.830  -6.873  73.495  1.00 32.42  ? 263  PHE E CB  1 
ATOM   4487 C  CG  . PHE E  1 14  ? -1.907  -7.247  72.371  1.00 32.42  ? 263  PHE E CG  1 
ATOM   4488 C  CD1 . PHE E  1 14  ? -1.139  -8.420  72.438  1.00 32.31  ? 263  PHE E CD1 1 
ATOM   4489 C  CD2 . PHE E  1 14  ? -1.758  -6.427  71.275  1.00 32.69  ? 263  PHE E CD2 1 
ATOM   4490 C  CE1 . PHE E  1 14  ? -0.286  -8.788  71.408  1.00 31.22  ? 263  PHE E CE1 1 
ATOM   4491 C  CE2 . PHE E  1 14  ? -0.876  -6.776  70.247  1.00 32.81  ? 263  PHE E CE2 1 
ATOM   4492 C  CZ  . PHE E  1 14  ? -0.140  -7.954  70.307  1.00 29.82  ? 263  PHE E CZ  1 
ATOM   4493 N  N   . GLN E  1 15  ? -4.576  -9.450  72.050  1.00 29.79  ? 264  GLN E N   1 
ATOM   4494 C  CA  . GLN E  1 15  ? -4.688  -10.864 71.636  1.00 28.63  ? 264  GLN E CA  1 
ATOM   4495 C  C   . GLN E  1 15  ? -5.075  -11.827 72.715  1.00 30.20  ? 264  GLN E C   1 
ATOM   4496 O  O   . GLN E  1 15  ? -4.370  -12.796 72.944  1.00 31.15  ? 264  GLN E O   1 
ATOM   4497 C  CB  . GLN E  1 15  ? -3.384  -11.313 70.979  1.00 29.61  ? 264  GLN E CB  1 
ATOM   4498 C  CG  . GLN E  1 15  ? -3.081  -10.450 69.759  1.00 30.57  ? 264  GLN E CG  1 
ATOM   4499 C  CD  . GLN E  1 15  ? -2.052  -11.036 68.822  1.00 31.80  ? 264  GLN E CD  1 
ATOM   4500 O  OE1 . GLN E  1 15  ? -1.787  -10.502 67.734  1.00 32.11  ? 264  GLN E OE1 1 
ATOM   4501 N  NE2 . GLN E  1 15  ? -1.454  -12.111 69.237  1.00 33.08  ? 264  GLN E NE2 1 
ATOM   4502 N  N   . GLY E  1 16  ? -6.182  -11.523 73.391  1.00 30.86  ? 265  GLY E N   1 
ATOM   4503 C  CA  . GLY E  1 16  ? -6.776  -12.418 74.393  1.00 32.20  ? 265  GLY E CA  1 
ATOM   4504 C  C   . GLY E  1 16  ? -6.281  -12.265 75.807  1.00 36.39  ? 265  GLY E C   1 
ATOM   4505 O  O   . GLY E  1 16  ? -6.782  -12.937 76.725  1.00 39.58  ? 265  GLY E O   1 
ATOM   4506 N  N   . ASN E  1 17  ? -5.315  -11.371 76.025  1.00 35.37  ? 266  ASN E N   1 
ATOM   4507 C  CA  . ASN E  1 17  ? -4.877  -11.086 77.378  1.00 32.60  ? 266  ASN E CA  1 
ATOM   4508 C  C   . ASN E  1 17  ? -5.011  -9.617  77.742  1.00 31.46  ? 266  ASN E C   1 
ATOM   4509 O  O   . ASN E  1 17  ? -5.130  -8.760  76.853  1.00 28.89  ? 266  ASN E O   1 
ATOM   4510 C  CB  . ASN E  1 17  ? -3.451  -11.568 77.557  1.00 31.59  ? 266  ASN E CB  1 
ATOM   4511 C  CG  . ASN E  1 17  ? -3.340  -13.055 77.380  1.00 30.47  ? 266  ASN E CG  1 
ATOM   4512 O  OD1 . ASN E  1 17  ? -3.888  -13.816 78.169  1.00 32.74  ? 266  ASN E OD1 1 
ATOM   4513 N  ND2 . ASN E  1 17  ? -2.630  -13.478 76.361  1.00 27.91  ? 266  ASN E ND2 1 
ATOM   4514 N  N   . CYS E  1 18  ? -4.996  -9.367  79.054  1.00 29.36  ? 267  CYS E N   1 
ATOM   4515 C  CA  . CYS E  1 18  ? -5.095  -8.030  79.626  1.00 29.57  ? 267  CYS E CA  1 
ATOM   4516 C  C   . CYS E  1 18  ? -3.748  -7.628  80.215  1.00 30.59  ? 267  CYS E C   1 
ATOM   4517 O  O   . CYS E  1 18  ? -3.103  -8.428  80.851  1.00 32.31  ? 267  CYS E O   1 
ATOM   4518 C  CB  . CYS E  1 18  ? -6.168  -8.002  80.691  1.00 31.07  ? 267  CYS E CB  1 
ATOM   4519 S  SG  . CYS E  1 18  ? -7.792  -8.480  80.023  1.00 36.55  ? 267  CYS E SG  1 
ATOM   4520 N  N   . TYR E  1 19  ? -3.345  -6.387  79.961  1.00 27.57  ? 268  TYR E N   1 
ATOM   4521 C  CA  . TYR E  1 19  ? -2.047  -5.889  80.288  1.00 27.57  ? 268  TYR E CA  1 
ATOM   4522 C  C   . TYR E  1 19  ? -2.199  -4.607  81.095  1.00 28.48  ? 268  TYR E C   1 
ATOM   4523 O  O   . TYR E  1 19  ? -2.908  -3.723  80.671  1.00 27.49  ? 268  TYR E O   1 
ATOM   4524 C  CB  . TYR E  1 19  ? -1.278  -5.595  78.999  1.00 26.73  ? 268  TYR E CB  1 
ATOM   4525 C  CG  . TYR E  1 19  ? -0.934  -6.872  78.260  1.00 26.82  ? 268  TYR E CG  1 
ATOM   4526 C  CD1 . TYR E  1 19  ? -1.835  -7.430  77.320  1.00 27.67  ? 268  TYR E CD1 1 
ATOM   4527 C  CD2 . TYR E  1 19  ? 0.254   -7.544  78.508  1.00 24.24  ? 268  TYR E CD2 1 
ATOM   4528 C  CE1 . TYR E  1 19  ? -1.514  -8.604  76.640  1.00 25.91  ? 268  TYR E CE1 1 
ATOM   4529 C  CE2 . TYR E  1 19  ? 0.576   -8.703  77.833  1.00 26.09  ? 268  TYR E CE2 1 
ATOM   4530 C  CZ  . TYR E  1 19  ? -0.309  -9.241  76.913  1.00 25.64  ? 268  TYR E CZ  1 
ATOM   4531 O  OH  . TYR E  1 19  ? 0.004   -10.406 76.250  1.00 24.87  ? 268  TYR E OH  1 
ATOM   4532 N  N   . PHE E  1 20  ? -1.546  -4.549  82.258  1.00 27.83  ? 269  PHE E N   1 
ATOM   4533 C  CA  . PHE E  1 20  ? -1.505  -3.383  83.101  1.00 30.00  ? 269  PHE E CA  1 
ATOM   4534 C  C   . PHE E  1 20  ? -0.123  -2.760  82.958  1.00 30.34  ? 269  PHE E C   1 
ATOM   4535 O  O   . PHE E  1 20  ? 0.865   -3.428  83.214  1.00 28.92  ? 269  PHE E O   1 
ATOM   4536 C  CB  . PHE E  1 20  ? -1.742  -3.764  84.561  1.00 31.46  ? 269  PHE E CB  1 
ATOM   4537 C  CG  . PHE E  1 20  ? -1.601  -2.606  85.516  1.00 35.52  ? 269  PHE E CG  1 
ATOM   4538 C  CD1 . PHE E  1 20  ? -2.582  -1.622  85.581  1.00 37.35  ? 269  PHE E CD1 1 
ATOM   4539 C  CD2 . PHE E  1 20  ? -0.470  -2.480  86.325  1.00 34.98  ? 269  PHE E CD2 1 
ATOM   4540 C  CE1 . PHE E  1 20  ? -2.461  -0.543  86.455  1.00 38.13  ? 269  PHE E CE1 1 
ATOM   4541 C  CE2 . PHE E  1 20  ? -0.343  -1.406  87.186  1.00 38.70  ? 269  PHE E CE2 1 
ATOM   4542 C  CZ  . PHE E  1 20  ? -1.340  -0.447  87.262  1.00 37.62  ? 269  PHE E CZ  1 
ATOM   4543 N  N   . MET E  1 21  ? -0.070  -1.496  82.536  1.00 30.78  ? 270  MET E N   1 
ATOM   4544 C  CA  . MET E  1 21  ? 1.186   -0.755  82.471  1.00 33.73  ? 270  MET E CA  1 
ATOM   4545 C  C   . MET E  1 21  ? 1.161   0.163   83.677  1.00 32.74  ? 270  MET E C   1 
ATOM   4546 O  O   . MET E  1 21  ? 0.254   1.013   83.788  1.00 27.02  ? 270  MET E O   1 
ATOM   4547 C  CB  . MET E  1 21  ? 1.305   0.128   81.229  1.00 37.28  ? 270  MET E CB  1 
ATOM   4548 C  CG  . MET E  1 21  ? 0.540   -0.313  80.003  1.00 41.86  ? 270  MET E CG  1 
ATOM   4549 S  SD  . MET E  1 21  ? 1.007   -1.941  79.433  1.00 47.11  ? 270  MET E SD  1 
ATOM   4550 C  CE  . MET E  1 21  ? 0.608   -1.811  77.701  1.00 52.34  ? 270  MET E CE  1 
ATOM   4551 N  N   . SER E  1 22  ? 2.143   -0.015  84.558  1.00 30.02  ? 271  SER E N   1 
ATOM   4552 C  CA  . SER E  1 22  ? 2.206   0.739   85.782  1.00 31.67  ? 271  SER E CA  1 
ATOM   4553 C  C   . SER E  1 22  ? 2.515   2.172   85.448  1.00 32.05  ? 271  SER E C   1 
ATOM   4554 O  O   . SER E  1 22  ? 3.150   2.461   84.427  1.00 30.42  ? 271  SER E O   1 
ATOM   4555 C  CB  . SER E  1 22  ? 3.276   0.167   86.740  1.00 32.31  ? 271  SER E CB  1 
ATOM   4556 O  OG  . SER E  1 22  ? 4.598   0.482   86.332  1.00 30.57  ? 271  SER E OG  1 
ATOM   4557 N  N   . ASN E  1 23  ? 2.100   3.079   86.312  1.00 33.83  ? 272  ASN E N   1 
ATOM   4558 C  CA  . ASN E  1 23  ? 2.585   4.459   86.175  1.00 40.45  ? 272  ASN E CA  1 
ATOM   4559 C  C   . ASN E  1 23  ? 3.614   4.869   87.228  1.00 36.39  ? 272  ASN E C   1 
ATOM   4560 O  O   . ASN E  1 23  ? 4.041   6.020   87.291  1.00 40.13  ? 272  ASN E O   1 
ATOM   4561 C  CB  . ASN E  1 23  ? 1.404   5.431   86.074  1.00 47.38  ? 272  ASN E CB  1 
ATOM   4562 C  CG  . ASN E  1 23  ? 0.823   5.452   84.664  1.00 56.57  ? 272  ASN E CG  1 
ATOM   4563 O  OD1 . ASN E  1 23  ? 1.555   5.688   83.678  1.00 53.81  ? 272  ASN E OD1 1 
ATOM   4564 N  ND2 . ASN E  1 23  ? -0.481  5.139   84.546  1.00 58.96  ? 272  ASN E ND2 1 
ATOM   4565 N  N   . SER E  1 24  ? 4.025   3.922   88.049  1.00 31.51  ? 273  SER E N   1 
ATOM   4566 C  CA  . SER E  1 24  ? 5.070   4.163   88.998  1.00 29.83  ? 273  SER E CA  1 
ATOM   4567 C  C   . SER E  1 24  ? 6.085   3.031   88.919  1.00 27.70  ? 273  SER E C   1 
ATOM   4568 O  O   . SER E  1 24  ? 5.935   2.106   88.120  1.00 29.42  ? 273  SER E O   1 
ATOM   4569 C  CB  . SER E  1 24  ? 4.490   4.328   90.409  1.00 29.27  ? 273  SER E CB  1 
ATOM   4570 O  OG  . SER E  1 24  ? 3.843   3.168   90.812  1.00 29.30  ? 273  SER E OG  1 
ATOM   4571 N  N   . GLN E  1 25  ? 7.135   3.149   89.722  1.00 27.86  ? 274  GLN E N   1 
ATOM   4572 C  CA  . GLN E  1 25  ? 8.274   2.262   89.654  1.00 29.87  ? 274  GLN E CA  1 
ATOM   4573 C  C   . GLN E  1 25  ? 8.423   1.403   90.894  1.00 30.08  ? 274  GLN E C   1 
ATOM   4574 O  O   . GLN E  1 25  ? 8.189   1.903   91.977  1.00 27.06  ? 274  GLN E O   1 
ATOM   4575 C  CB  . GLN E  1 25  ? 9.520   3.106   89.482  1.00 27.89  ? 274  GLN E CB  1 
ATOM   4576 C  CG  . GLN E  1 25  ? 9.498   3.840   88.147  1.00 27.47  ? 274  GLN E CG  1 
ATOM   4577 C  CD  . GLN E  1 25  ? 10.256  5.149   88.180  1.00 27.41  ? 274  GLN E CD  1 
ATOM   4578 O  OE1 . GLN E  1 25  ? 11.323  5.287   87.568  1.00 29.09  ? 274  GLN E OE1 1 
ATOM   4579 N  NE2 . GLN E  1 25  ? 9.736   6.087   88.912  1.00 23.53  ? 274  GLN E NE2 1 
ATOM   4580 N  N   . ARG E  1 26  ? 8.844   0.141   90.718  1.00 27.71  ? 275  ARG E N   1 
ATOM   4581 C  CA  . ARG E  1 26  ? 9.153   -0.709  91.834  1.00 28.12  ? 275  ARG E CA  1 
ATOM   4582 C  C   . ARG E  1 26  ? 10.356  -1.544  91.504  1.00 28.08  ? 275  ARG E C   1 
ATOM   4583 O  O   . ARG E  1 26  ? 10.673  -1.685  90.316  1.00 23.09  ? 275  ARG E O   1 
ATOM   4584 C  CB  . ARG E  1 26  ? 7.957   -1.612  92.144  1.00 30.66  ? 275  ARG E CB  1 
ATOM   4585 C  CG  . ARG E  1 26  ? 6.829   -0.906  92.879  1.00 33.48  ? 275  ARG E CG  1 
ATOM   4586 C  CD  . ARG E  1 26  ? 5.598   -1.813  92.977  1.00 35.02  ? 275  ARG E CD  1 
ATOM   4587 N  NE  . ARG E  1 26  ? 4.598   -1.330  93.954  1.00 40.33  ? 275  ARG E NE  1 
ATOM   4588 C  CZ  . ARG E  1 26  ? 4.051   -2.092  94.920  1.00 42.06  ? 275  ARG E CZ  1 
ATOM   4589 N  NH1 . ARG E  1 26  ? 4.364   -3.404  95.074  1.00 39.41  ? 275  ARG E NH1 1 
ATOM   4590 N  NH2 . ARG E  1 26  ? 3.202   -1.552  95.755  1.00 43.10  ? 275  ARG E NH2 1 
ATOM   4591 N  N   . ASN E  1 27  ? 11.048  -2.077  92.535  1.00 25.21  ? 276  ASN E N   1 
ATOM   4592 C  CA  . ASN E  1 27  ? 12.051  -3.132  92.277  1.00 26.54  ? 276  ASN E CA  1 
ATOM   4593 C  C   . ASN E  1 27  ? 11.375  -4.394  91.708  1.00 25.84  ? 276  ASN E C   1 
ATOM   4594 O  O   . ASN E  1 27  ? 10.136  -4.481  91.674  1.00 23.39  ? 276  ASN E O   1 
ATOM   4595 C  CB  . ASN E  1 27  ? 12.987  -3.402  93.471  1.00 29.49  ? 276  ASN E CB  1 
ATOM   4596 C  CG  . ASN E  1 27  ? 12.286  -4.025  94.698  1.00 31.84  ? 276  ASN E CG  1 
ATOM   4597 O  OD1 . ASN E  1 27  ? 11.309  -4.763  94.592  1.00 31.16  ? 276  ASN E OD1 1 
ATOM   4598 N  ND2 . ASN E  1 27  ? 12.805  -3.719  95.865  1.00 30.34  ? 276  ASN E ND2 1 
ATOM   4599 N  N   . TRP E  1 28  ? 12.166  -5.320  91.183  1.00 25.94  ? 277  TRP E N   1 
ATOM   4600 C  CA  . TRP E  1 28  ? 11.615  -6.474  90.478  1.00 27.51  ? 277  TRP E CA  1 
ATOM   4601 C  C   . TRP E  1 28  ? 10.737  -7.348  91.398  1.00 28.12  ? 277  TRP E C   1 
ATOM   4602 O  O   . TRP E  1 28  ? 9.631   -7.722  91.034  1.00 26.18  ? 277  TRP E O   1 
ATOM   4603 C  CB  . TRP E  1 28  ? 12.725  -7.304  89.834  1.00 26.47  ? 277  TRP E CB  1 
ATOM   4604 C  CG  . TRP E  1 28  ? 12.296  -8.380  88.866  1.00 27.45  ? 277  TRP E CG  1 
ATOM   4605 C  CD1 . TRP E  1 28  ? 12.049  -8.235  87.556  1.00 31.45  ? 277  TRP E CD1 1 
ATOM   4606 C  CD2 . TRP E  1 28  ? 12.200  -9.792  89.131  1.00 28.97  ? 277  TRP E CD2 1 
ATOM   4607 N  NE1 . TRP E  1 28  ? 11.776  -9.461  86.970  1.00 29.38  ? 277  TRP E NE1 1 
ATOM   4608 C  CE2 . TRP E  1 28  ? 11.848  -10.426 87.927  1.00 28.92  ? 277  TRP E CE2 1 
ATOM   4609 C  CE3 . TRP E  1 28  ? 12.349  -10.572 90.285  1.00 29.26  ? 277  TRP E CE3 1 
ATOM   4610 C  CZ2 . TRP E  1 28  ? 11.626  -11.811 87.829  1.00 28.96  ? 277  TRP E CZ2 1 
ATOM   4611 C  CZ3 . TRP E  1 28  ? 12.139  -11.952 90.194  1.00 31.14  ? 277  TRP E CZ3 1 
ATOM   4612 C  CH2 . TRP E  1 28  ? 11.776  -12.557 88.960  1.00 28.86  ? 277  TRP E CH2 1 
ATOM   4613 N  N   . HIS E  1 29  ? 11.208  -7.663  92.584  1.00 31.23  ? 278  HIS E N   1 
ATOM   4614 C  CA  . HIS E  1 29  ? 10.401  -8.524  93.462  1.00 34.72  ? 278  HIS E CA  1 
ATOM   4615 C  C   . HIS E  1 29  ? 9.122   -7.812  93.871  1.00 32.22  ? 278  HIS E C   1 
ATOM   4616 O  O   . HIS E  1 29  ? 8.092   -8.443  93.991  1.00 31.45  ? 278  HIS E O   1 
ATOM   4617 C  CB  . HIS E  1 29  ? 11.198  -8.996  94.672  1.00 35.28  ? 278  HIS E CB  1 
ATOM   4618 C  CG  . HIS E  1 29  ? 12.209  -10.044 94.342  1.00 39.01  ? 278  HIS E CG  1 
ATOM   4619 N  ND1 . HIS E  1 29  ? 13.512  -9.744  93.992  1.00 47.57  ? 278  HIS E ND1 1 
ATOM   4620 C  CD2 . HIS E  1 29  ? 12.114  -11.394 94.304  1.00 41.97  ? 278  HIS E CD2 1 
ATOM   4621 C  CE1 . HIS E  1 29  ? 14.175  -10.862 93.756  1.00 41.60  ? 278  HIS E CE1 1 
ATOM   4622 N  NE2 . HIS E  1 29  ? 13.353  -11.877 93.956  1.00 42.96  ? 278  HIS E NE2 1 
ATOM   4623 N  N   . ASP E  1 30  ? 9.168   -6.507  94.084  1.00 31.39  ? 279  ASP E N   1 
ATOM   4624 C  CA  . ASP E  1 30  ? 7.939   -5.796  94.452  1.00 31.37  ? 279  ASP E CA  1 
ATOM   4625 C  C   . ASP E  1 30  ? 6.991   -5.622  93.291  1.00 31.05  ? 279  ASP E C   1 
ATOM   4626 O  O   . ASP E  1 30  ? 5.809   -5.389  93.521  1.00 31.88  ? 279  ASP E O   1 
ATOM   4627 C  CB  . ASP E  1 30  ? 8.229   -4.433  95.068  1.00 34.44  ? 279  ASP E CB  1 
ATOM   4628 C  CG  . ASP E  1 30  ? 8.929   -4.534  96.400  1.00 38.14  ? 279  ASP E CG  1 
ATOM   4629 O  OD1 . ASP E  1 30  ? 8.945   -5.642  96.989  1.00 43.25  ? 279  ASP E OD1 1 
ATOM   4630 O  OD2 . ASP E  1 30  ? 9.481   -3.508  96.851  1.00 36.17  ? 279  ASP E OD2 1 
ATOM   4631 N  N   . SER E  1 31  ? 7.522   -5.688  92.052  1.00 28.46  ? 280  SER E N   1 
ATOM   4632 C  CA  . SER E  1 31  ? 6.734   -5.695  90.861  1.00 26.09  ? 280  SER E CA  1 
ATOM   4633 C  C   . SER E  1 31  ? 5.947   -7.015  90.749  1.00 25.63  ? 280  SER E C   1 
ATOM   4634 O  O   . SER E  1 31  ? 4.790   -7.008  90.442  1.00 24.35  ? 280  SER E O   1 
ATOM   4635 C  CB  . SER E  1 31  ? 7.587   -5.436  89.617  1.00 23.87  ? 280  SER E CB  1 
ATOM   4636 O  OG  . SER E  1 31  ? 8.011   -4.079  89.617  1.00 22.87  ? 280  SER E OG  1 
ATOM   4637 N  N   . ILE E  1 32  ? 6.596   -8.122  91.009  1.00 26.48  ? 281  ILE E N   1 
ATOM   4638 C  CA  . ILE E  1 32  ? 5.935   -9.428  91.139  1.00 28.62  ? 281  ILE E CA  1 
ATOM   4639 C  C   . ILE E  1 32  ? 4.800   -9.419  92.129  1.00 28.32  ? 281  ILE E C   1 
ATOM   4640 O  O   . ILE E  1 32  ? 3.674   -9.816  91.814  1.00 30.81  ? 281  ILE E O   1 
ATOM   4641 C  CB  . ILE E  1 32  ? 6.946   -10.490 91.538  1.00 27.96  ? 281  ILE E CB  1 
ATOM   4642 C  CG1 . ILE E  1 32  ? 7.781   -10.820 90.304  1.00 31.73  ? 281  ILE E CG1 1 
ATOM   4643 C  CG2 . ILE E  1 32  ? 6.221   -11.719 92.064  1.00 30.13  ? 281  ILE E CG2 1 
ATOM   4644 C  CD1 . ILE E  1 32  ? 8.890   -11.798 90.544  1.00 37.03  ? 281  ILE E CD1 1 
ATOM   4645 N  N   . THR E  1 33  ? 5.065   -8.882  93.296  1.00 28.68  ? 282  THR E N   1 
ATOM   4646 C  CA  . THR E  1 33  ? 4.010   -8.715  94.300  1.00 30.08  ? 282  THR E CA  1 
ATOM   4647 C  C   . THR E  1 33  ? 2.861   -7.839  93.778  1.00 28.92  ? 282  THR E C   1 
ATOM   4648 O  O   . THR E  1 33  ? 1.692   -8.189  93.948  1.00 26.51  ? 282  THR E O   1 
ATOM   4649 C  CB  . THR E  1 33  ? 4.634   -8.175  95.589  1.00 28.96  ? 282  THR E CB  1 
ATOM   4650 O  OG1 . THR E  1 33  ? 5.582   -9.147  96.015  1.00 29.55  ? 282  THR E OG1 1 
ATOM   4651 C  CG2 . THR E  1 33  ? 3.635   -7.910  96.677  1.00 31.46  ? 282  THR E CG2 1 
ATOM   4652 N  N   . ALA E  1 34  ? 3.178   -6.748  93.095  1.00 27.48  ? 283  ALA E N   1 
ATOM   4653 C  CA  . ALA E  1 34  ? 2.112   -5.842  92.647  1.00 26.73  ? 283  ALA E CA  1 
ATOM   4654 C  C   . ALA E  1 34  ? 1.181   -6.498  91.587  1.00 26.74  ? 283  ALA E C   1 
ATOM   4655 O  O   . ALA E  1 34  ? 0.001   -6.317  91.612  1.00 23.88  ? 283  ALA E O   1 
ATOM   4656 C  CB  . ALA E  1 34  ? 2.685   -4.528  92.162  1.00 26.95  ? 283  ALA E CB  1 
ATOM   4657 N  N   . CYS E  1 35  ? 1.739   -7.298  90.682  1.00 26.75  ? 284  CYS E N   1 
ATOM   4658 C  CA  . CYS E  1 35  ? 0.969   -8.044  89.778  1.00 26.89  ? 284  CYS E CA  1 
ATOM   4659 C  C   . CYS E  1 35  ? 0.078   -9.085  90.506  1.00 29.65  ? 284  CYS E C   1 
ATOM   4660 O  O   . CYS E  1 35  ? -1.116  -9.141  90.227  1.00 28.25  ? 284  CYS E O   1 
ATOM   4661 C  CB  . CYS E  1 35  ? 1.885   -8.675  88.740  1.00 27.97  ? 284  CYS E CB  1 
ATOM   4662 S  SG  . CYS E  1 35  ? 2.636   -7.388  87.700  1.00 26.68  ? 284  CYS E SG  1 
ATOM   4663 N  N   . LYS E  1 36  ? 0.638   -9.874  91.425  1.00 32.44  ? 285  LYS E N   1 
ATOM   4664 C  CA  . LYS E  1 36  ? -0.148  -10.859 92.213  1.00 34.09  ? 285  LYS E CA  1 
ATOM   4665 C  C   . LYS E  1 36  ? -1.309  -10.199 92.947  1.00 34.19  ? 285  LYS E C   1 
ATOM   4666 O  O   . LYS E  1 36  ? -2.395  -10.769 93.089  1.00 33.21  ? 285  LYS E O   1 
ATOM   4667 C  CB  . LYS E  1 36  ? 0.724   -11.563 93.216  1.00 35.01  ? 285  LYS E CB  1 
ATOM   4668 C  CG  . LYS E  1 36  ? 1.572   -12.643 92.600  1.00 41.49  ? 285  LYS E CG  1 
ATOM   4669 C  CD  . LYS E  1 36  ? 2.476   -13.297 93.630  1.00 47.14  ? 285  LYS E CD  1 
ATOM   4670 C  CE  . LYS E  1 36  ? 3.467   -14.187 92.895  1.00 54.22  ? 285  LYS E CE  1 
ATOM   4671 N  NZ  . LYS E  1 36  ? 4.291   -15.046 93.790  1.00 58.67  ? 285  LYS E NZ  1 
ATOM   4672 N  N   . GLU E  1 37  ? -1.089  -8.976  93.376  1.00 29.75  ? 286  GLU E N   1 
ATOM   4673 C  CA  . GLU E  1 37  ? -2.096  -8.299  94.147  1.00 32.96  ? 286  GLU E CA  1 
ATOM   4674 C  C   . GLU E  1 37  ? -3.256  -7.707  93.302  1.00 30.56  ? 286  GLU E C   1 
ATOM   4675 O  O   . GLU E  1 37  ? -4.246  -7.261  93.869  1.00 25.88  ? 286  GLU E O   1 
ATOM   4676 C  CB  . GLU E  1 37  ? -1.442  -7.258  95.076  1.00 37.96  ? 286  GLU E CB  1 
ATOM   4677 C  CG  . GLU E  1 37  ? -0.576  -7.914  96.162  1.00 39.78  ? 286  GLU E CG  1 
ATOM   4678 C  CD  . GLU E  1 37  ? -0.135  -6.971  97.251  1.00 43.35  ? 286  GLU E CD  1 
ATOM   4679 O  OE1 . GLU E  1 37  ? -0.386  -5.752  97.133  1.00 42.34  ? 286  GLU E OE1 1 
ATOM   4680 O  OE2 . GLU E  1 37  ? 0.493   -7.456  98.223  1.00 52.90  ? 286  GLU E OE2 1 
ATOM   4681 N  N   . VAL E  1 38  ? -3.127  -7.725  91.975  1.00 29.48  ? 287  VAL E N   1 
ATOM   4682 C  CA  . VAL E  1 38  ? -4.256  -7.512  91.076  1.00 28.87  ? 287  VAL E CA  1 
ATOM   4683 C  C   . VAL E  1 38  ? -4.650  -8.754  90.228  1.00 29.31  ? 287  VAL E C   1 
ATOM   4684 O  O   . VAL E  1 38  ? -5.237  -8.599  89.138  1.00 31.20  ? 287  VAL E O   1 
ATOM   4685 C  CB  . VAL E  1 38  ? -4.051  -6.258  90.165  1.00 28.85  ? 287  VAL E CB  1 
ATOM   4686 C  CG1 . VAL E  1 38  ? -4.102  -5.024  91.025  1.00 29.99  ? 287  VAL E CG1 1 
ATOM   4687 C  CG2 . VAL E  1 38  ? -2.763  -6.309  89.350  1.00 26.26  ? 287  VAL E CG2 1 
ATOM   4688 N  N   . GLY E  1 39  ? -4.332  -9.947  90.728  1.00 28.25  ? 288  GLY E N   1 
ATOM   4689 C  CA  . GLY E  1 39  ? -4.683  -11.244 90.085  1.00 29.94  ? 288  GLY E CA  1 
ATOM   4690 C  C   . GLY E  1 39  ? -3.966  -11.497 88.778  1.00 29.43  ? 288  GLY E C   1 
ATOM   4691 O  O   . GLY E  1 39  ? -4.507  -12.075 87.843  1.00 29.76  ? 288  GLY E O   1 
ATOM   4692 N  N   . ALA E  1 40  ? -2.746  -11.009 88.680  1.00 29.39  ? 289  ALA E N   1 
ATOM   4693 C  CA  . ALA E  1 40  ? -2.015  -11.061 87.408  1.00 30.05  ? 289  ALA E CA  1 
ATOM   4694 C  C   . ALA E  1 40  ? -0.605  -11.563 87.643  1.00 30.10  ? 289  ALA E C   1 
ATOM   4695 O  O   . ALA E  1 40  ? -0.269  -12.014 88.730  1.00 28.80  ? 289  ALA E O   1 
ATOM   4696 C  CB  . ALA E  1 40  ? -1.991  -9.666  86.740  1.00 28.04  ? 289  ALA E CB  1 
ATOM   4697 N  N   . GLN E  1 41  ? 0.229   -11.412 86.618  1.00 28.73  ? 290  GLN E N   1 
ATOM   4698 C  CA  . GLN E  1 41  ? 1.571   -11.903 86.651  1.00 28.74  ? 290  GLN E CA  1 
ATOM   4699 C  C   . GLN E  1 41  ? 2.470   -10.916 85.913  1.00 28.10  ? 290  GLN E C   1 
ATOM   4700 O  O   . GLN E  1 41  ? 2.152   -10.473 84.793  1.00 27.54  ? 290  GLN E O   1 
ATOM   4701 C  CB  . GLN E  1 41  ? 1.626   -13.242 85.969  1.00 28.42  ? 290  GLN E CB  1 
ATOM   4702 C  CG  . GLN E  1 41  ? 2.987   -13.871 85.977  1.00 29.48  ? 290  GLN E CG  1 
ATOM   4703 C  CD  . GLN E  1 41  ? 2.948   -15.326 85.532  1.00 32.18  ? 290  GLN E CD  1 
ATOM   4704 O  OE1 . GLN E  1 41  ? 2.982   -15.621 84.347  1.00 36.02  ? 290  GLN E OE1 1 
ATOM   4705 N  NE2 . GLN E  1 41  ? 2.925   -16.235 86.495  1.00 30.98  ? 290  GLN E NE2 1 
ATOM   4706 N  N   . LEU E  1 42  ? 3.616   -10.614 86.531  1.00 29.36  ? 291  LEU E N   1 
ATOM   4707 C  CA  . LEU E  1 42  ? 4.636   -9.816  85.885  1.00 29.32  ? 291  LEU E CA  1 
ATOM   4708 C  C   . LEU E  1 42  ? 4.899   -10.497 84.510  1.00 27.51  ? 291  LEU E C   1 
ATOM   4709 O  O   . LEU E  1 42  ? 5.110   -11.698 84.444  1.00 29.67  ? 291  LEU E O   1 
ATOM   4710 C  CB  . LEU E  1 42  ? 5.882   -9.772  86.787  1.00 29.36  ? 291  LEU E CB  1 
ATOM   4711 C  CG  . LEU E  1 42  ? 6.970   -8.824  86.279  1.00 30.68  ? 291  LEU E CG  1 
ATOM   4712 C  CD1 . LEU E  1 42  ? 6.490   -7.374  86.262  1.00 29.29  ? 291  LEU E CD1 1 
ATOM   4713 C  CD2 . LEU E  1 42  ? 8.227   -8.976  87.126  1.00 30.82  ? 291  LEU E CD2 1 
ATOM   4714 N  N   . VAL E  1 43  ? 4.866   -9.725  83.434  1.00 28.45  ? 292  VAL E N   1 
ATOM   4715 C  CA  . VAL E  1 43  ? 4.497   -10.248 82.118  1.00 28.28  ? 292  VAL E CA  1 
ATOM   4716 C  C   . VAL E  1 43  ? 5.459   -11.365 81.657  1.00 29.42  ? 292  VAL E C   1 
ATOM   4717 O  O   . VAL E  1 43  ? 6.658   -11.210 81.727  1.00 26.51  ? 292  VAL E O   1 
ATOM   4718 C  CB  . VAL E  1 43  ? 4.309   -9.137  81.049  1.00 30.01  ? 292  VAL E CB  1 
ATOM   4719 C  CG1 . VAL E  1 43  ? 5.538   -8.210  80.925  1.00 30.49  ? 292  VAL E CG1 1 
ATOM   4720 C  CG2 . VAL E  1 43  ? 3.943   -9.720  79.668  1.00 29.99  ? 292  VAL E CG2 1 
ATOM   4721 N  N   . VAL E  1 44  ? 4.880   -12.491 81.210  1.00 30.18  ? 293  VAL E N   1 
ATOM   4722 C  CA  . VAL E  1 44  ? 5.605   -13.548 80.576  1.00 28.49  ? 293  VAL E CA  1 
ATOM   4723 C  C   . VAL E  1 44  ? 5.281   -13.520 79.097  1.00 30.46  ? 293  VAL E C   1 
ATOM   4724 O  O   . VAL E  1 44  ? 4.120   -13.605 78.687  1.00 27.13  ? 293  VAL E O   1 
ATOM   4725 C  CB  . VAL E  1 44  ? 5.229   -14.901 81.160  1.00 30.54  ? 293  VAL E CB  1 
ATOM   4726 C  CG1 . VAL E  1 44  ? 5.913   -16.032 80.387  1.00 29.91  ? 293  VAL E CG1 1 
ATOM   4727 C  CG2 . VAL E  1 44  ? 5.599   -14.924 82.625  1.00 30.12  ? 293  VAL E CG2 1 
ATOM   4728 N  N   . ILE E  1 45  ? 6.316   -13.418 78.289  1.00 28.58  ? 294  ILE E N   1 
ATOM   4729 C  CA  . ILE E  1 45  ? 6.103   -13.241 76.867  1.00 31.58  ? 294  ILE E CA  1 
ATOM   4730 C  C   . ILE E  1 45  ? 6.057   -14.578 76.174  1.00 34.59  ? 294  ILE E C   1 
ATOM   4731 O  O   . ILE E  1 45  ? 6.986   -15.376 76.300  1.00 37.21  ? 294  ILE E O   1 
ATOM   4732 C  CB  . ILE E  1 45  ? 7.215   -12.390 76.257  1.00 29.28  ? 294  ILE E CB  1 
ATOM   4733 C  CG1 . ILE E  1 45  ? 7.294   -11.053 77.015  1.00 29.15  ? 294  ILE E CG1 1 
ATOM   4734 C  CG2 . ILE E  1 45  ? 6.917   -12.176 74.796  1.00 29.10  ? 294  ILE E CG2 1 
ATOM   4735 C  CD1 . ILE E  1 45  ? 8.527   -10.223 76.721  1.00 30.73  ? 294  ILE E CD1 1 
ATOM   4736 N  N   . LYS E  1 46  ? 4.998   -14.811 75.404  1.00 37.21  ? 295  LYS E N   1 
ATOM   4737 C  CA  . LYS E  1 46  ? 4.807   -16.106 74.730  1.00 36.29  ? 295  LYS E CA  1 
ATOM   4738 C  C   . LYS E  1 46  ? 4.858   -16.084 73.181  1.00 36.19  ? 295  LYS E C   1 
ATOM   4739 O  O   . LYS E  1 46  ? 4.710   -17.117 72.556  1.00 34.38  ? 295  LYS E O   1 
ATOM   4740 C  CB  . LYS E  1 46  ? 3.485   -16.702 75.175  1.00 36.14  ? 295  LYS E CB  1 
ATOM   4741 C  CG  . LYS E  1 46  ? 3.347   -16.884 76.672  1.00 35.10  ? 295  LYS E CG  1 
ATOM   4742 C  CD  . LYS E  1 46  ? 4.092   -18.134 77.079  1.00 36.45  ? 295  LYS E CD  1 
ATOM   4743 C  CE  . LYS E  1 46  ? 3.691   -18.567 78.473  1.00 36.97  ? 295  LYS E CE  1 
ATOM   4744 N  NZ  . LYS E  1 46  ? 4.870   -19.171 79.158  1.00 35.98  ? 295  LYS E NZ  1 
ATOM   4745 N  N   . SER E  1 47  ? 5.057   -14.929 72.562  1.00 34.48  ? 296  SER E N   1 
ATOM   4746 C  CA  . SER E  1 47  ? 5.108   -14.887 71.114  1.00 35.06  ? 296  SER E CA  1 
ATOM   4747 C  C   . SER E  1 47  ? 5.806   -13.633 70.628  1.00 34.52  ? 296  SER E C   1 
ATOM   4748 O  O   . SER E  1 47  ? 5.934   -12.668 71.363  1.00 36.00  ? 296  SER E O   1 
ATOM   4749 C  CB  . SER E  1 47  ? 3.683   -14.949 70.529  1.00 35.87  ? 296  SER E CB  1 
ATOM   4750 O  OG  . SER E  1 47  ? 3.018   -13.694 70.590  1.00 33.23  ? 296  SER E OG  1 
ATOM   4751 N  N   . ALA E  1 48  ? 6.228   -13.638 69.374  1.00 33.72  ? 297  ALA E N   1 
ATOM   4752 C  CA  . ALA E  1 48  ? 6.869   -12.481 68.750  1.00 32.41  ? 297  ALA E CA  1 
ATOM   4753 C  C   . ALA E  1 48  ? 5.984   -11.237 68.667  1.00 31.97  ? 297  ALA E C   1 
ATOM   4754 O  O   . ALA E  1 48  ? 6.442   -10.120 68.856  1.00 36.97  ? 297  ALA E O   1 
ATOM   4755 C  CB  . ALA E  1 48  ? 7.362   -12.861 67.351  1.00 32.63  ? 297  ALA E CB  1 
ATOM   4756 N  N   . GLU E  1 49  ? 4.719   -11.420 68.343  1.00 32.97  ? 298  GLU E N   1 
ATOM   4757 C  CA  A GLU E  1 49  ? 3.727   -10.366 68.218  0.70 34.01  ? 298  GLU E CA  1 
ATOM   4758 C  CA  B GLU E  1 49  ? 3.863   -10.239 68.199  0.30 32.27  ? 298  GLU E CA  1 
ATOM   4759 C  C   . GLU E  1 49  ? 3.593   -9.642  69.582  1.00 31.93  ? 298  GLU E C   1 
ATOM   4760 O  O   . GLU E  1 49  ? 3.468   -8.421  69.687  1.00 32.62  ? 298  GLU E O   1 
ATOM   4761 C  CB  A GLU E  1 49  ? 2.362   -11.015 67.840  0.70 35.64  ? 298  GLU E CB  1 
ATOM   4762 C  CB  B GLU E  1 49  ? 2.571   -10.482 67.390  0.30 32.45  ? 298  GLU E CB  1 
ATOM   4763 C  CG  A GLU E  1 49  ? 2.209   -11.647 66.442  0.70 39.75  ? 298  GLU E CG  1 
ATOM   4764 C  CG  B GLU E  1 49  ? 2.684   -10.130 65.895  0.30 33.46  ? 298  GLU E CG  1 
ATOM   4765 C  CD  A GLU E  1 49  ? 3.028   -12.928 66.141  0.70 44.83  ? 298  GLU E CD  1 
ATOM   4766 C  CD  B GLU E  1 49  ? 2.775   -8.628  65.590  0.30 33.37  ? 298  GLU E CD  1 
ATOM   4767 O  OE1 A GLU E  1 49  ? 3.397   -13.735 67.048  0.70 37.09  ? 298  GLU E OE1 1 
ATOM   4768 O  OE1 B GLU E  1 49  ? 3.739   -7.960  66.030  0.30 33.68  ? 298  GLU E OE1 1 
ATOM   4769 O  OE2 A GLU E  1 49  ? 3.307   -13.133 64.924  0.70 50.63  ? 298  GLU E OE2 1 
ATOM   4770 O  OE2 B GLU E  1 49  ? 1.889   -8.104  64.883  0.30 31.71  ? 298  GLU E OE2 1 
ATOM   4771 N  N   . GLU E  1 50  ? 3.570   -10.460 70.627  1.00 28.84  ? 299  GLU E N   1 
ATOM   4772 C  CA  . GLU E  1 50  ? 3.414   -9.965  71.973  1.00 30.42  ? 299  GLU E CA  1 
ATOM   4773 C  C   . GLU E  1 50  ? 4.685   -9.164  72.381  1.00 33.50  ? 299  GLU E C   1 
ATOM   4774 O  O   . GLU E  1 50  ? 4.577   -8.084  72.974  1.00 26.73  ? 299  GLU E O   1 
ATOM   4775 C  CB  . GLU E  1 50  ? 3.143   -11.114 72.929  1.00 30.38  ? 299  GLU E CB  1 
ATOM   4776 C  CG  . GLU E  1 50  ? 2.888   -10.688 74.348  1.00 31.44  ? 299  GLU E CG  1 
ATOM   4777 C  CD  . GLU E  1 50  ? 2.619   -11.843 75.292  1.00 34.58  ? 299  GLU E CD  1 
ATOM   4778 O  OE1 . GLU E  1 50  ? 2.777   -13.022 74.891  1.00 36.03  ? 299  GLU E OE1 1 
ATOM   4779 O  OE2 . GLU E  1 50  ? 2.245   -11.547 76.460  1.00 33.63  ? 299  GLU E OE2 1 
ATOM   4780 N  N   . GLN E  1 51  ? 5.864   -9.687  72.021  1.00 31.08  ? 300  GLN E N   1 
ATOM   4781 C  CA  . GLN E  1 51  ? 7.107   -8.992  72.260  1.00 31.28  ? 300  GLN E CA  1 
ATOM   4782 C  C   . GLN E  1 51  ? 7.010   -7.631  71.619  1.00 33.00  ? 300  GLN E C   1 
ATOM   4783 O  O   . GLN E  1 51  ? 7.368   -6.624  72.249  1.00 33.14  ? 300  GLN E O   1 
ATOM   4784 C  CB  . GLN E  1 51  ? 8.293   -9.781  71.703  1.00 32.56  ? 300  GLN E CB  1 
ATOM   4785 C  CG  . GLN E  1 51  ? 9.566   -9.012  71.376  1.00 32.69  ? 300  GLN E CG  1 
ATOM   4786 C  CD  . GLN E  1 51  ? 10.191  -8.297  72.555  1.00 30.98  ? 300  GLN E CD  1 
ATOM   4787 O  OE1 . GLN E  1 51  ? 9.823   -8.511  73.730  1.00 30.44  ? 300  GLN E OE1 1 
ATOM   4788 N  NE2 . GLN E  1 51  ? 11.120  -7.409  72.248  1.00 27.58  ? 300  GLN E NE2 1 
ATOM   4789 N  N   . ASN E  1 52  ? 6.519   -7.586  70.380  1.00 32.86  ? 301  ASN E N   1 
ATOM   4790 C  CA  . ASN E  1 52  ? 6.526   -6.316  69.638  1.00 33.48  ? 301  ASN E CA  1 
ATOM   4791 C  C   . ASN E  1 52  ? 5.623   -5.326  70.320  1.00 30.58  ? 301  ASN E C   1 
ATOM   4792 O  O   . ASN E  1 52  ? 5.960   -4.172  70.425  1.00 28.45  ? 301  ASN E O   1 
ATOM   4793 C  CB  . ASN E  1 52  ? 6.051   -6.486  68.207  1.00 34.07  ? 301  ASN E CB  1 
ATOM   4794 C  CG  . ASN E  1 52  ? 6.950   -7.389  67.405  1.00 38.71  ? 301  ASN E CG  1 
ATOM   4795 O  OD1 . ASN E  1 52  ? 8.105   -7.633  67.793  1.00 39.71  ? 301  ASN E OD1 1 
ATOM   4796 N  ND2 . ASN E  1 52  ? 6.418   -7.937  66.306  1.00 35.62  ? 301  ASN E ND2 1 
ATOM   4797 N  N   . PHE E  1 53  ? 4.463   -5.811  70.747  1.00 29.17  ? 302  PHE E N   1 
ATOM   4798 C  CA  . PHE E  1 53  ? 3.515   -5.000  71.454  1.00 31.30  ? 302  PHE E CA  1 
ATOM   4799 C  C   . PHE E  1 53  ? 4.116   -4.420  72.751  1.00 30.62  ? 302  PHE E C   1 
ATOM   4800 O  O   . PHE E  1 53  ? 4.030   -3.226  73.006  1.00 32.33  ? 302  PHE E O   1 
ATOM   4801 C  CB  . PHE E  1 53  ? 2.248   -5.794  71.705  1.00 30.73  ? 302  PHE E CB  1 
ATOM   4802 C  CG  . PHE E  1 53  ? 1.334   -5.173  72.695  1.00 30.10  ? 302  PHE E CG  1 
ATOM   4803 C  CD1 . PHE E  1 53  ? 0.680   -3.979  72.414  1.00 33.64  ? 302  PHE E CD1 1 
ATOM   4804 C  CD2 . PHE E  1 53  ? 1.126   -5.787  73.917  1.00 30.33  ? 302  PHE E CD2 1 
ATOM   4805 C  CE1 . PHE E  1 53  ? -0.162  -3.393  73.359  1.00 33.07  ? 302  PHE E CE1 1 
ATOM   4806 C  CE2 . PHE E  1 53  ? 0.277   -5.222  74.855  1.00 32.06  ? 302  PHE E CE2 1 
ATOM   4807 C  CZ  . PHE E  1 53  ? -0.361  -4.020  74.573  1.00 33.29  ? 302  PHE E CZ  1 
ATOM   4808 N  N   . LEU E  1 54  ? 4.750   -5.263  73.528  1.00 30.81  ? 303  LEU E N   1 
ATOM   4809 C  CA  . LEU E  1 54  ? 5.292   -4.862  74.794  1.00 32.60  ? 303  LEU E CA  1 
ATOM   4810 C  C   . LEU E  1 54  ? 6.522   -3.954  74.608  1.00 33.08  ? 303  LEU E C   1 
ATOM   4811 O  O   . LEU E  1 54  ? 6.590   -2.884  75.215  1.00 27.96  ? 303  LEU E O   1 
ATOM   4812 C  CB  . LEU E  1 54  ? 5.625   -6.094  75.623  1.00 31.34  ? 303  LEU E CB  1 
ATOM   4813 C  CG  . LEU E  1 54  ? 4.432   -6.918  76.046  1.00 29.63  ? 303  LEU E CG  1 
ATOM   4814 C  CD1 . LEU E  1 54  ? 4.891   -8.255  76.588  1.00 29.14  ? 303  LEU E CD1 1 
ATOM   4815 C  CD2 . LEU E  1 54  ? 3.620   -6.188  77.092  1.00 34.01  ? 303  LEU E CD2 1 
ATOM   4816 N  N   . GLN E  1 55  ? 7.441   -4.343  73.715  1.00 32.23  ? 304  GLN E N   1 
ATOM   4817 C  CA  . GLN E  1 55  ? 8.674   -3.586  73.521  1.00 32.17  ? 304  GLN E CA  1 
ATOM   4818 C  C   . GLN E  1 55  ? 8.323   -2.135  73.250  1.00 31.83  ? 304  GLN E C   1 
ATOM   4819 O  O   . GLN E  1 55  ? 8.970   -1.197  73.759  1.00 30.80  ? 304  GLN E O   1 
ATOM   4820 C  CB  . GLN E  1 55  ? 9.517   -4.107  72.340  1.00 31.71  ? 304  GLN E CB  1 
ATOM   4821 C  CG  . GLN E  1 55  ? 10.911  -3.501  72.340  1.00 30.77  ? 304  GLN E CG  1 
ATOM   4822 C  CD  . GLN E  1 55  ? 11.759  -3.980  73.536  1.00 31.16  ? 304  GLN E CD  1 
ATOM   4823 O  OE1 . GLN E  1 55  ? 11.958  -5.168  73.708  1.00 31.20  ? 304  GLN E OE1 1 
ATOM   4824 N  NE2 . GLN E  1 55  ? 12.264  -3.040  74.361  1.00 30.11  ? 304  GLN E NE2 1 
ATOM   4825 N  N   . LEU E  1 56  ? 7.310   -1.978  72.410  1.00 33.99  ? 305  LEU E N   1 
ATOM   4826 C  CA  . LEU E  1 56  ? 6.860   -0.696  71.913  1.00 34.31  ? 305  LEU E CA  1 
ATOM   4827 C  C   . LEU E  1 56  ? 6.431   0.247   73.024  1.00 31.68  ? 305  LEU E C   1 
ATOM   4828 O  O   . LEU E  1 56  ? 6.656   1.461   72.939  1.00 31.91  ? 305  LEU E O   1 
ATOM   4829 C  CB  . LEU E  1 56  ? 5.722   -0.947  70.943  1.00 42.42  ? 305  LEU E CB  1 
ATOM   4830 C  CG  . LEU E  1 56  ? 5.154   0.288   70.266  1.00 48.19  ? 305  LEU E CG  1 
ATOM   4831 C  CD1 . LEU E  1 56  ? 6.000   0.679   69.072  1.00 46.90  ? 305  LEU E CD1 1 
ATOM   4832 C  CD2 . LEU E  1 56  ? 3.694   0.024   69.926  1.00 53.21  ? 305  LEU E CD2 1 
ATOM   4833 N  N   . GLN E  1 57  ? 5.840   -0.311  74.078  1.00 34.02  ? 306  GLN E N   1 
ATOM   4834 C  CA  . GLN E  1 57  ? 5.408   0.474   75.239  1.00 32.34  ? 306  GLN E CA  1 
ATOM   4835 C  C   . GLN E  1 57  ? 6.596   1.193   75.790  1.00 31.78  ? 306  GLN E C   1 
ATOM   4836 O  O   . GLN E  1 57  ? 6.493   2.373   76.061  1.00 33.96  ? 306  GLN E O   1 
ATOM   4837 C  CB  . GLN E  1 57  ? 4.791   -0.386  76.360  1.00 35.84  ? 306  GLN E CB  1 
ATOM   4838 C  CG  . GLN E  1 57  ? 3.577   -1.211  75.957  1.00 40.70  ? 306  GLN E CG  1 
ATOM   4839 C  CD  . GLN E  1 57  ? 2.519   -0.441  75.150  1.00 37.88  ? 306  GLN E CD  1 
ATOM   4840 O  OE1 . GLN E  1 57  ? 2.039   0.582   75.583  1.00 41.07  ? 306  GLN E OE1 1 
ATOM   4841 N  NE2 . GLN E  1 57  ? 2.162   -0.948  73.995  1.00 42.91  ? 306  GLN E NE2 1 
ATOM   4842 N  N   . SER E  1 58  ? 7.728   0.495   75.924  1.00 28.94  ? 307  SER E N   1 
ATOM   4843 C  CA  . SER E  1 58  ? 8.961   1.111   76.465  1.00 29.59  ? 307  SER E CA  1 
ATOM   4844 C  C   . SER E  1 58  ? 9.757   1.927   75.467  1.00 30.58  ? 307  SER E C   1 
ATOM   4845 O  O   . SER E  1 58  ? 10.250  2.998   75.785  1.00 31.48  ? 307  SER E O   1 
ATOM   4846 C  CB  . SER E  1 58  ? 9.869   0.031   77.078  1.00 30.55  ? 307  SER E CB  1 
ATOM   4847 O  OG  . SER E  1 58  ? 9.450   -0.249  78.425  1.00 32.66  ? 307  SER E OG  1 
ATOM   4848 N  N   . SER E  1 59  ? 9.908   1.429   74.247  1.00 29.16  ? 308  SER E N   1 
ATOM   4849 C  CA  . SER E  1 59  ? 10.719  2.146   73.269  1.00 32.18  ? 308  SER E CA  1 
ATOM   4850 C  C   . SER E  1 59  ? 10.105  3.549   72.963  1.00 35.07  ? 308  SER E C   1 
ATOM   4851 O  O   . SER E  1 59  ? 10.790  4.572   72.940  1.00 40.52  ? 308  SER E O   1 
ATOM   4852 C  CB  . SER E  1 59  ? 10.856  1.296   71.998  1.00 30.45  ? 308  SER E CB  1 
ATOM   4853 O  OG  . SER E  1 59  ? 9.646   1.256   71.270  1.00 31.01  ? 308  SER E OG  1 
ATOM   4854 N  N   . ARG E  1 60  ? 8.797   3.564   72.766  1.00 35.68  ? 309  ARG E N   1 
ATOM   4855 C  CA  . ARG E  1 60  ? 8.022   4.778   72.496  1.00 38.12  ? 309  ARG E CA  1 
ATOM   4856 C  C   . ARG E  1 60  ? 8.028   5.743   73.688  1.00 36.92  ? 309  ARG E C   1 
ATOM   4857 O  O   . ARG E  1 60  ? 8.154   6.951   73.521  1.00 36.28  ? 309  ARG E O   1 
ATOM   4858 C  CB  . ARG E  1 60  ? 6.598   4.331   72.132  1.00 42.59  ? 309  ARG E CB  1 
ATOM   4859 C  CG  . ARG E  1 60  ? 5.563   5.397   71.859  1.00 51.46  ? 309  ARG E CG  1 
ATOM   4860 C  CD  . ARG E  1 60  ? 4.218   4.771   71.419  1.00 58.09  ? 309  ARG E CD  1 
ATOM   4861 N  NE  . ARG E  1 60  ? 3.503   4.053   72.493  1.00 58.48  ? 309  ARG E NE  1 
ATOM   4862 C  CZ  . ARG E  1 60  ? 2.411   3.317   72.311  1.00 58.11  ? 309  ARG E CZ  1 
ATOM   4863 N  NH1 . ARG E  1 60  ? 1.835   2.700   73.332  1.00 54.96  ? 309  ARG E NH1 1 
ATOM   4864 N  NH2 . ARG E  1 60  ? 1.896   3.185   71.098  1.00 66.15  ? 309  ARG E NH2 1 
ATOM   4865 N  N   . SER E  1 61  ? 7.895   5.199   74.898  1.00 36.07  ? 310  SER E N   1 
ATOM   4866 C  CA  . SER E  1 61  ? 7.862   6.004   76.105  1.00 35.37  ? 310  SER E CA  1 
ATOM   4867 C  C   . SER E  1 61  ? 9.232   6.417   76.628  1.00 34.57  ? 310  SER E C   1 
ATOM   4868 O  O   . SER E  1 61  ? 9.299   7.286   77.478  1.00 31.73  ? 310  SER E O   1 
ATOM   4869 C  CB  . SER E  1 61  ? 7.115   5.267   77.209  1.00 36.71  ? 310  SER E CB  1 
ATOM   4870 O  OG  . SER E  1 61  ? 7.739   4.047   77.538  1.00 39.77  ? 310  SER E OG  1 
ATOM   4871 N  N   . ASN E  1 62  ? 10.307  5.813   76.121  1.00 32.76  ? 311  ASN E N   1 
ATOM   4872 C  CA  . ASN E  1 62  ? 11.638  5.960   76.684  1.00 33.55  ? 311  ASN E CA  1 
ATOM   4873 C  C   . ASN E  1 62  ? 11.757  5.586   78.168  1.00 34.06  ? 311  ASN E C   1 
ATOM   4874 O  O   . ASN E  1 62  ? 12.613  6.091   78.899  1.00 42.49  ? 311  ASN E O   1 
ATOM   4875 C  CB  . ASN E  1 62  ? 12.099  7.377   76.489  1.00 36.62  ? 311  ASN E CB  1 
ATOM   4876 C  CG  . ASN E  1 62  ? 12.063  7.795   75.047  1.00 39.18  ? 311  ASN E CG  1 
ATOM   4877 O  OD1 . ASN E  1 62  ? 12.861  7.315   74.248  1.00 45.83  ? 311  ASN E OD1 1 
ATOM   4878 N  ND2 . ASN E  1 62  ? 11.124  8.697   74.698  1.00 36.51  ? 311  ASN E ND2 1 
ATOM   4879 N  N   . ARG E  1 63  ? 10.916  4.680   78.606  1.00 32.18  ? 312  ARG E N   1 
ATOM   4880 C  CA  . ARG E  1 63  ? 10.960  4.207   79.963  1.00 32.48  ? 312  ARG E CA  1 
ATOM   4881 C  C   . ARG E  1 63  ? 11.501  2.781   80.044  1.00 33.72  ? 312  ARG E C   1 
ATOM   4882 O  O   . ARG E  1 63  ? 11.612  2.076   79.031  1.00 37.92  ? 312  ARG E O   1 
ATOM   4883 C  CB  . ARG E  1 63  ? 9.604   4.397   80.561  1.00 32.98  ? 312  ARG E CB  1 
ATOM   4884 C  CG  . ARG E  1 63  ? 9.291   5.906   80.503  1.00 35.61  ? 312  ARG E CG  1 
ATOM   4885 C  CD  . ARG E  1 63  ? 8.298   6.360   81.538  1.00 36.52  ? 312  ARG E CD  1 
ATOM   4886 N  NE  . ARG E  1 63  ? 7.861   7.762   81.417  1.00 38.01  ? 312  ARG E NE  1 
ATOM   4887 C  CZ  . ARG E  1 63  ? 8.475   8.835   81.929  1.00 36.93  ? 312  ARG E CZ  1 
ATOM   4888 N  NH1 . ARG E  1 63  ? 7.885   10.034  81.769  1.00 35.50  ? 312  ARG E NH1 1 
ATOM   4889 N  NH2 . ARG E  1 63  ? 9.670   8.744   82.572  1.00 33.65  ? 312  ARG E NH2 1 
ATOM   4890 N  N   . PHE E  1 64  ? 11.965  2.419   81.232  1.00 29.58  ? 313  PHE E N   1 
ATOM   4891 C  CA  . PHE E  1 64  ? 12.594  1.146   81.468  1.00 28.00  ? 313  PHE E CA  1 
ATOM   4892 C  C   . PHE E  1 64  ? 11.592  0.341   82.282  1.00 28.85  ? 313  PHE E C   1 
ATOM   4893 O  O   . PHE E  1 64  ? 11.001  0.877   83.248  1.00 26.46  ? 313  PHE E O   1 
ATOM   4894 C  CB  . PHE E  1 64  ? 13.863  1.330   82.308  1.00 28.17  ? 313  PHE E CB  1 
ATOM   4895 C  CG  . PHE E  1 64  ? 14.955  2.100   81.638  1.00 28.48  ? 313  PHE E CG  1 
ATOM   4896 C  CD1 . PHE E  1 64  ? 15.221  1.944   80.274  1.00 29.43  ? 313  PHE E CD1 1 
ATOM   4897 C  CD2 . PHE E  1 64  ? 15.769  2.942   82.390  1.00 29.38  ? 313  PHE E CD2 1 
ATOM   4898 C  CE1 . PHE E  1 64  ? 16.223  2.669   79.664  1.00 29.22  ? 313  PHE E CE1 1 
ATOM   4899 C  CE2 . PHE E  1 64  ? 16.785  3.643   81.788  1.00 28.99  ? 313  PHE E CE2 1 
ATOM   4900 C  CZ  . PHE E  1 64  ? 17.007  3.513   80.420  1.00 29.86  ? 313  PHE E CZ  1 
ATOM   4901 N  N   . THR E  1 65  ? 11.379  -0.923  81.910  1.00 26.09  ? 314  THR E N   1 
ATOM   4902 C  CA  . THR E  1 65  ? 10.178  -1.652  82.401  1.00 23.72  ? 314  THR E CA  1 
ATOM   4903 C  C   . THR E  1 65  ? 10.474  -3.086  82.625  1.00 21.71  ? 314  THR E C   1 
ATOM   4904 O  O   . THR E  1 65  ? 11.023  -3.744  81.749  1.00 20.88  ? 314  THR E O   1 
ATOM   4905 C  CB  . THR E  1 65  ? 9.041   -1.597  81.368  1.00 24.15  ? 314  THR E CB  1 
ATOM   4906 O  OG1 . THR E  1 65  ? 8.788   -0.239  80.970  1.00 23.55  ? 314  THR E OG1 1 
ATOM   4907 C  CG2 . THR E  1 65  ? 7.765   -2.182  81.931  1.00 24.14  ? 314  THR E CG2 1 
ATOM   4908 N  N   . TRP E  1 66  ? 10.156  -3.578  83.807  1.00 22.59  ? 315  TRP E N   1 
ATOM   4909 C  CA  . TRP E  1 66  ? 10.436  -4.983  84.141  1.00 23.20  ? 315  TRP E CA  1 
ATOM   4910 C  C   . TRP E  1 66  ? 9.517   -5.955  83.365  1.00 26.12  ? 315  TRP E C   1 
ATOM   4911 O  O   . TRP E  1 66  ? 8.346   -5.632  82.991  1.00 25.19  ? 315  TRP E O   1 
ATOM   4912 C  CB  . TRP E  1 66  ? 10.208  -5.212  85.622  1.00 22.42  ? 315  TRP E CB  1 
ATOM   4913 C  CG  . TRP E  1 66  ? 11.198  -4.592  86.609  1.00 23.57  ? 315  TRP E CG  1 
ATOM   4914 C  CD1 . TRP E  1 66  ? 10.893  -3.844  87.714  1.00 24.07  ? 315  TRP E CD1 1 
ATOM   4915 C  CD2 . TRP E  1 66  ? 12.609  -4.787  86.647  1.00 24.50  ? 315  TRP E CD2 1 
ATOM   4916 N  NE1 . TRP E  1 66  ? 12.024  -3.547  88.406  1.00 26.09  ? 315  TRP E NE1 1 
ATOM   4917 C  CE2 . TRP E  1 66  ? 13.094  -4.084  87.756  1.00 24.69  ? 315  TRP E CE2 1 
ATOM   4918 C  CE3 . TRP E  1 66  ? 13.512  -5.474  85.829  1.00 24.78  ? 315  TRP E CE3 1 
ATOM   4919 C  CZ2 . TRP E  1 66  ? 14.444  -4.028  88.066  1.00 27.51  ? 315  TRP E CZ2 1 
ATOM   4920 C  CZ3 . TRP E  1 66  ? 14.859  -5.414  86.130  1.00 25.85  ? 315  TRP E CZ3 1 
ATOM   4921 C  CH2 . TRP E  1 66  ? 15.311  -4.713  87.235  1.00 26.84  ? 315  TRP E CH2 1 
ATOM   4922 N  N   . MET E  1 67  ? 10.075  -7.125  83.086  1.00 26.95  ? 316  MET E N   1 
ATOM   4923 C  CA  . MET E  1 67  ? 9.331   -8.276  82.687  1.00 25.65  ? 316  MET E CA  1 
ATOM   4924 C  C   . MET E  1 67  ? 9.591   -9.390  83.673  1.00 26.87  ? 316  MET E C   1 
ATOM   4925 O  O   . MET E  1 67  ? 10.546  -9.361  84.442  1.00 24.48  ? 316  MET E O   1 
ATOM   4926 C  CB  . MET E  1 67  ? 9.709   -8.732  81.275  1.00 26.67  ? 316  MET E CB  1 
ATOM   4927 C  CG  . MET E  1 67  ? 11.044  -9.437  81.117  1.00 27.79  ? 316  MET E CG  1 
ATOM   4928 S  SD  . MET E  1 67  ? 11.485  -9.556  79.368  1.00 27.76  ? 316  MET E SD  1 
ATOM   4929 C  CE  . MET E  1 67  ? 12.004  -7.881  79.013  1.00 26.93  ? 316  MET E CE  1 
ATOM   4930 N  N   . GLY E  1 68  ? 8.780   -10.437 83.563  1.00 26.79  ? 317  GLY E N   1 
ATOM   4931 C  CA  . GLY E  1 68  ? 8.829   -11.555 84.496  1.00 24.32  ? 317  GLY E CA  1 
ATOM   4932 C  C   . GLY E  1 68  ? 9.882   -12.576 84.089  1.00 27.02  ? 317  GLY E C   1 
ATOM   4933 O  O   . GLY E  1 68  ? 9.570   -13.741 83.790  1.00 27.83  ? 317  GLY E O   1 
ATOM   4934 N  N   . LEU E  1 69  ? 11.134  -12.143 84.046  1.00 25.81  ? 318  LEU E N   1 
ATOM   4935 C  CA  . LEU E  1 69  ? 12.201  -13.005 83.570  1.00 26.14  ? 318  LEU E CA  1 
ATOM   4936 C  C   . LEU E  1 69  ? 13.442  -12.693 84.406  1.00 29.28  ? 318  LEU E C   1 
ATOM   4937 O  O   . LEU E  1 69  ? 13.777  -11.488 84.654  1.00 26.33  ? 318  LEU E O   1 
ATOM   4938 C  CB  . LEU E  1 69  ? 12.440  -12.762 82.078  1.00 25.47  ? 318  LEU E CB  1 
ATOM   4939 C  CG  . LEU E  1 69  ? 13.577  -13.602 81.478  1.00 27.10  ? 318  LEU E CG  1 
ATOM   4940 C  CD1 . LEU E  1 69  ? 13.097  -15.018 81.197  1.00 27.60  ? 318  LEU E CD1 1 
ATOM   4941 C  CD2 . LEU E  1 69  ? 14.126  -12.994 80.217  1.00 27.33  ? 318  LEU E CD2 1 
ATOM   4942 N  N   . SER E  1 70  ? 14.101  -13.759 84.867  1.00 29.01  ? 319  SER E N   1 
ATOM   4943 C  CA  . SER E  1 70  ? 15.317  -13.639 85.690  1.00 29.67  ? 319  SER E CA  1 
ATOM   4944 C  C   . SER E  1 70  ? 16.248  -14.836 85.521  1.00 32.22  ? 319  SER E C   1 
ATOM   4945 O  O   . SER E  1 70  ? 15.816  -15.886 85.069  1.00 29.24  ? 319  SER E O   1 
ATOM   4946 C  CB  . SER E  1 70  ? 14.964  -13.542 87.149  1.00 28.74  ? 319  SER E CB  1 
ATOM   4947 O  OG  . SER E  1 70  ? 14.693  -14.824 87.657  1.00 31.64  ? 319  SER E OG  1 
ATOM   4948 N  N   . ASP E  1 71  ? 17.527  -14.626 85.873  1.00 34.94  ? 320  ASP E N   1 
ATOM   4949 C  CA  . ASP E  1 71  ? 18.500  -15.712 86.103  1.00 31.29  ? 320  ASP E CA  1 
ATOM   4950 C  C   . ASP E  1 71  ? 18.944  -15.704 87.549  1.00 31.21  ? 320  ASP E C   1 
ATOM   4951 O  O   . ASP E  1 71  ? 20.067  -16.056 87.861  1.00 31.46  ? 320  ASP E O   1 
ATOM   4952 C  CB  . ASP E  1 71  ? 19.699  -15.715 85.094  1.00 30.28  ? 320  ASP E CB  1 
ATOM   4953 C  CG  . ASP E  1 71  ? 20.731  -14.599 85.331  1.00 31.60  ? 320  ASP E CG  1 
ATOM   4954 O  OD1 . ASP E  1 71  ? 20.475  -13.724 86.179  1.00 32.90  ? 320  ASP E OD1 1 
ATOM   4955 O  OD2 . ASP E  1 71  ? 21.793  -14.565 84.617  1.00 29.40  ? 320  ASP E OD2 1 
ATOM   4956 N  N   . LEU E  1 72  ? 18.031  -15.324 88.436  1.00 31.66  ? 321  LEU E N   1 
ATOM   4957 C  CA  . LEU E  1 72  ? 18.257  -15.402 89.857  1.00 34.02  ? 321  LEU E CA  1 
ATOM   4958 C  C   . LEU E  1 72  ? 18.642  -16.799 90.367  1.00 35.05  ? 321  LEU E C   1 
ATOM   4959 O  O   . LEU E  1 72  ? 19.630  -16.930 91.058  1.00 36.86  ? 321  LEU E O   1 
ATOM   4960 C  CB  . LEU E  1 72  ? 17.043  -14.899 90.633  1.00 34.59  ? 321  LEU E CB  1 
ATOM   4961 C  CG  . LEU E  1 72  ? 16.795  -13.391 90.635  1.00 36.40  ? 321  LEU E CG  1 
ATOM   4962 C  CD1 . LEU E  1 72  ? 15.354  -13.137 91.041  1.00 37.54  ? 321  LEU E CD1 1 
ATOM   4963 C  CD2 . LEU E  1 72  ? 17.754  -12.603 91.533  1.00 34.23  ? 321  LEU E CD2 1 
ATOM   4964 N  N   . ASN E  1 73  ? 17.873  -17.826 90.021  1.00 37.81  ? 322  ASN E N   1 
ATOM   4965 C  CA  . ASN E  1 73  ? 18.101  -19.201 90.519  1.00 36.84  ? 322  ASN E CA  1 
ATOM   4966 C  C   . ASN E  1 73  ? 19.469  -19.755 90.145  1.00 39.08  ? 322  ASN E C   1 
ATOM   4967 O  O   . ASN E  1 73  ? 20.149  -20.346 90.990  1.00 39.50  ? 322  ASN E O   1 
ATOM   4968 C  CB  . ASN E  1 73  ? 17.038  -20.166 89.997  1.00 41.30  ? 322  ASN E CB  1 
ATOM   4969 C  CG  . ASN E  1 73  ? 17.289  -21.620 90.448  1.00 44.71  ? 322  ASN E CG  1 
ATOM   4970 O  OD1 . ASN E  1 73  ? 17.513  -22.524 89.633  1.00 46.85  ? 322  ASN E OD1 1 
ATOM   4971 N  ND2 . ASN E  1 73  ? 17.290  -21.827 91.744  1.00 43.42  ? 322  ASN E ND2 1 
ATOM   4972 N  N   . GLN E  1 74  ? 19.825  -19.609 88.865  1.00 37.79  ? 323  GLN E N   1 
ATOM   4973 C  CA  . GLN E  1 74  ? 21.170  -19.873 88.415  1.00 36.70  ? 323  GLN E CA  1 
ATOM   4974 C  C   . GLN E  1 74  ? 21.640  -18.948 87.294  1.00 33.38  ? 323  GLN E C   1 
ATOM   4975 O  O   . GLN E  1 74  ? 21.075  -18.895 86.185  1.00 31.79  ? 323  GLN E O   1 
ATOM   4976 C  CB  . GLN E  1 74  ? 21.344  -21.327 87.948  1.00 37.89  ? 323  GLN E CB  1 
ATOM   4977 C  CG  . GLN E  1 74  ? 22.827  -21.670 87.664  1.00 40.36  ? 323  GLN E CG  1 
ATOM   4978 C  CD  . GLN E  1 74  ? 23.049  -23.154 87.518  1.00 40.59  ? 323  GLN E CD  1 
ATOM   4979 O  OE1 . GLN E  1 74  ? 23.316  -23.650 86.418  1.00 41.77  ? 323  GLN E OE1 1 
ATOM   4980 N  NE2 . GLN E  1 74  ? 22.834  -23.887 88.615  1.00 41.25  ? 323  GLN E NE2 1 
ATOM   4981 N  N   . GLU E  1 75  ? 22.750  -18.289 87.579  1.00 34.50  ? 324  GLU E N   1 
ATOM   4982 C  CA  . GLU E  1 75  ? 23.374  -17.362 86.657  1.00 34.75  ? 324  GLU E CA  1 
ATOM   4983 C  C   . GLU E  1 75  ? 23.501  -17.894 85.239  1.00 35.05  ? 324  GLU E C   1 
ATOM   4984 O  O   . GLU E  1 75  ? 23.957  -19.003 85.027  1.00 39.90  ? 324  GLU E O   1 
ATOM   4985 C  CB  . GLU E  1 75  ? 24.773  -16.977 87.170  1.00 35.42  ? 324  GLU E CB  1 
ATOM   4986 C  CG  . GLU E  1 75  ? 25.429  -15.921 86.303  1.00 35.21  ? 324  GLU E CG  1 
ATOM   4987 C  CD  . GLU E  1 75  ? 24.580  -14.649 86.229  1.00 34.99  ? 324  GLU E CD  1 
ATOM   4988 O  OE1 . GLU E  1 75  ? 23.911  -14.265 87.246  1.00 27.97  ? 324  GLU E OE1 1 
ATOM   4989 O  OE2 . GLU E  1 75  ? 24.587  -14.078 85.116  1.00 34.09  ? 324  GLU E OE2 1 
ATOM   4990 N  N   . GLY E  1 76  ? 23.117  -17.088 84.263  1.00 32.94  ? 325  GLY E N   1 
ATOM   4991 C  CA  . GLY E  1 76  ? 23.162  -17.505 82.863  1.00 32.39  ? 325  GLY E CA  1 
ATOM   4992 C  C   . GLY E  1 76  ? 21.964  -18.330 82.387  1.00 32.60  ? 325  GLY E C   1 
ATOM   4993 O  O   . GLY E  1 76  ? 21.824  -18.572 81.188  1.00 32.50  ? 325  GLY E O   1 
ATOM   4994 N  N   . THR E  1 77  ? 21.122  -18.813 83.300  1.00 31.71  ? 326  THR E N   1 
ATOM   4995 C  CA  . THR E  1 77  ? 19.906  -19.522 82.859  1.00 31.94  ? 326  THR E CA  1 
ATOM   4996 C  C   . THR E  1 77  ? 18.695  -18.665 83.166  1.00 33.08  ? 326  THR E C   1 
ATOM   4997 O  O   . THR E  1 77  ? 18.318  -18.479 84.356  1.00 32.50  ? 326  THR E O   1 
ATOM   4998 C  CB  . THR E  1 77  ? 19.728  -20.919 83.506  1.00 33.33  ? 326  THR E CB  1 
ATOM   4999 O  OG1 . THR E  1 77  ? 20.796  -21.753 83.079  1.00 34.83  ? 326  THR E OG1 1 
ATOM   5000 C  CG2 . THR E  1 77  ? 18.424  -21.595 83.030  1.00 32.60  ? 326  THR E CG2 1 
ATOM   5001 N  N   . TRP E  1 78  ? 18.110  -18.139 82.089  1.00 33.92  ? 327  TRP E N   1 
ATOM   5002 C  CA  . TRP E  1 78  ? 17.003  -17.187 82.173  1.00 35.44  ? 327  TRP E CA  1 
ATOM   5003 C  C   . TRP E  1 78  ? 15.689  -17.934 82.093  1.00 35.65  ? 327  TRP E C   1 
ATOM   5004 O  O   . TRP E  1 78  ? 15.454  -18.673 81.155  1.00 33.65  ? 327  TRP E O   1 
ATOM   5005 C  CB  . TRP E  1 78  ? 17.105  -16.136 81.060  1.00 34.90  ? 327  TRP E CB  1 
ATOM   5006 C  CG  . TRP E  1 78  ? 18.212  -15.210 81.336  1.00 34.31  ? 327  TRP E CG  1 
ATOM   5007 C  CD1 . TRP E  1 78  ? 19.504  -15.375 80.972  1.00 33.22  ? 327  TRP E CD1 1 
ATOM   5008 C  CD2 . TRP E  1 78  ? 18.151  -14.010 82.096  1.00 33.23  ? 327  TRP E CD2 1 
ATOM   5009 N  NE1 . TRP E  1 78  ? 20.251  -14.348 81.444  1.00 34.59  ? 327  TRP E NE1 1 
ATOM   5010 C  CE2 . TRP E  1 78  ? 19.456  -13.504 82.165  1.00 32.84  ? 327  TRP E CE2 1 
ATOM   5011 C  CE3 . TRP E  1 78  ? 17.114  -13.307 82.737  1.00 33.76  ? 327  TRP E CE3 1 
ATOM   5012 C  CZ2 . TRP E  1 78  ? 19.762  -12.319 82.827  1.00 31.41  ? 327  TRP E CZ2 1 
ATOM   5013 C  CZ3 . TRP E  1 78  ? 17.415  -12.144 83.407  1.00 33.02  ? 327  TRP E CZ3 1 
ATOM   5014 C  CH2 . TRP E  1 78  ? 18.725  -11.656 83.445  1.00 32.89  ? 327  TRP E CH2 1 
ATOM   5015 N  N   . GLN E  1 79  ? 14.837  -17.675 83.077  1.00 38.21  ? 328  GLN E N   1 
ATOM   5016 C  CA  . GLN E  1 79  ? 13.610  -18.404 83.302  1.00 40.53  ? 328  GLN E CA  1 
ATOM   5017 C  C   . GLN E  1 79  ? 12.456  -17.428 83.562  1.00 33.06  ? 328  GLN E C   1 
ATOM   5018 O  O   . GLN E  1 79  ? 12.580  -16.576 84.435  1.00 35.83  ? 328  GLN E O   1 
ATOM   5019 C  CB  . GLN E  1 79  ? 13.859  -19.305 84.523  1.00 47.41  ? 328  GLN E CB  1 
ATOM   5020 C  CG  . GLN E  1 79  ? 12.652  -20.019 85.114  1.00 54.63  ? 328  GLN E CG  1 
ATOM   5021 C  CD  . GLN E  1 79  ? 12.994  -21.420 85.596  1.00 61.10  ? 328  GLN E CD  1 
ATOM   5022 O  OE1 . GLN E  1 79  ? 14.176  -21.799 85.702  1.00 69.91  ? 328  GLN E OE1 1 
ATOM   5023 N  NE2 . GLN E  1 79  ? 11.964  -22.211 85.860  1.00 64.92  ? 328  GLN E NE2 1 
ATOM   5024 N  N   . TRP E  1 80  ? 11.357  -17.555 82.810  1.00 27.53  ? 329  TRP E N   1 
ATOM   5025 C  CA  . TRP E  1 80  ? 10.116  -16.774 83.030  1.00 28.14  ? 329  TRP E CA  1 
ATOM   5026 C  C   . TRP E  1 80  ? 9.605   -17.092 84.412  1.00 29.62  ? 329  TRP E C   1 
ATOM   5027 O  O   . TRP E  1 80  ? 9.922   -18.155 84.930  1.00 30.64  ? 329  TRP E O   1 
ATOM   5028 C  CB  . TRP E  1 80  ? 9.043   -17.101 81.973  1.00 26.83  ? 329  TRP E CB  1 
ATOM   5029 C  CG  . TRP E  1 80  ? 9.480   -16.735 80.620  1.00 26.23  ? 329  TRP E CG  1 
ATOM   5030 C  CD1 . TRP E  1 80  ? 9.947   -17.577 79.643  1.00 26.57  ? 329  TRP E CD1 1 
ATOM   5031 C  CD2 . TRP E  1 80  ? 9.582   -15.410 80.093  1.00 27.33  ? 329  TRP E CD2 1 
ATOM   5032 N  NE1 . TRP E  1 80  ? 10.316  -16.855 78.534  1.00 27.08  ? 329  TRP E NE1 1 
ATOM   5033 C  CE2 . TRP E  1 80  ? 10.110  -15.521 78.787  1.00 26.97  ? 329  TRP E CE2 1 
ATOM   5034 C  CE3 . TRP E  1 80  ? 9.299   -14.131 80.609  1.00 27.10  ? 329  TRP E CE3 1 
ATOM   5035 C  CZ2 . TRP E  1 80  ? 10.340  -14.420 77.996  1.00 27.72  ? 329  TRP E CZ2 1 
ATOM   5036 C  CZ3 . TRP E  1 80  ? 9.531   -13.038 79.819  1.00 25.72  ? 329  TRP E CZ3 1 
ATOM   5037 C  CH2 . TRP E  1 80  ? 10.034  -13.177 78.538  1.00 27.73  ? 329  TRP E CH2 1 
ATOM   5038 N  N   . VAL E  1 81  ? 8.875   -16.180 85.043  1.00 29.91  ? 330  VAL E N   1 
ATOM   5039 C  CA  . VAL E  1 81  ? 8.301   -16.453 86.379  1.00 30.46  ? 330  VAL E CA  1 
ATOM   5040 C  C   . VAL E  1 81  ? 7.178   -17.528 86.419  1.00 34.31  ? 330  VAL E C   1 
ATOM   5041 O  O   . VAL E  1 81  ? 6.806   -17.959 87.471  1.00 33.71  ? 330  VAL E O   1 
ATOM   5042 C  CB  . VAL E  1 81  ? 7.728   -15.190 87.064  1.00 33.15  ? 330  VAL E CB  1 
ATOM   5043 C  CG1 . VAL E  1 81  ? 8.842   -14.260 87.577  1.00 33.76  ? 330  VAL E CG1 1 
ATOM   5044 C  CG2 . VAL E  1 81  ? 6.769   -14.462 86.144  1.00 32.08  ? 330  VAL E CG2 1 
ATOM   5045 N  N   . ASP E  1 82  ? 6.629   -17.941 85.285  1.00 35.77  ? 331  ASP E N   1 
ATOM   5046 C  CA  . ASP E  1 82  ? 5.677   -19.064 85.268  1.00 37.71  ? 331  ASP E CA  1 
ATOM   5047 C  C   . ASP E  1 82  ? 6.438   -20.377 85.112  1.00 40.50  ? 331  ASP E C   1 
ATOM   5048 O  O   . ASP E  1 82  ? 5.838   -21.427 84.875  1.00 39.73  ? 331  ASP E O   1 
ATOM   5049 C  CB  . ASP E  1 82  ? 4.646   -18.927 84.124  1.00 33.91  ? 331  ASP E CB  1 
ATOM   5050 C  CG  . ASP E  1 82  ? 5.267   -19.144 82.756  1.00 37.08  ? 331  ASP E CG  1 
ATOM   5051 O  OD1 . ASP E  1 82  ? 6.516   -19.211 82.658  1.00 36.77  ? 331  ASP E OD1 1 
ATOM   5052 O  OD2 . ASP E  1 82  ? 4.526   -19.191 81.753  1.00 39.30  ? 331  ASP E OD2 1 
ATOM   5053 N  N   . GLY E  1 83  ? 7.760   -20.296 85.174  1.00 39.54  ? 332  GLY E N   1 
ATOM   5054 C  CA  . GLY E  1 83  ? 8.617   -21.470 85.220  1.00 36.26  ? 332  GLY E CA  1 
ATOM   5055 C  C   . GLY E  1 83  ? 9.090   -21.874 83.850  1.00 35.52  ? 332  GLY E C   1 
ATOM   5056 O  O   . GLY E  1 83  ? 9.919   -22.755 83.723  1.00 45.73  ? 332  GLY E O   1 
ATOM   5057 N  N   . SER E  1 84  ? 8.571   -21.242 82.818  1.00 37.11  ? 333  SER E N   1 
ATOM   5058 C  CA  . SER E  1 84  ? 8.876   -21.652 81.454  1.00 37.99  ? 333  SER E CA  1 
ATOM   5059 C  C   . SER E  1 84  ? 10.256  -21.143 81.037  1.00 40.01  ? 333  SER E C   1 
ATOM   5060 O  O   . SER E  1 84  ? 10.712  -20.118 81.523  1.00 41.32  ? 333  SER E O   1 
ATOM   5061 C  CB  . SER E  1 84  ? 7.771   -21.213 80.477  1.00 38.54  ? 333  SER E CB  1 
ATOM   5062 O  OG  . SER E  1 84  ? 7.499   -19.814 80.496  1.00 41.79  ? 333  SER E OG  1 
ATOM   5063 N  N   . PRO E  1 85  ? 10.927  -21.864 80.128  1.00 42.69  ? 334  PRO E N   1 
ATOM   5064 C  CA  . PRO E  1 85  ? 12.276  -21.491 79.774  1.00 40.20  ? 334  PRO E CA  1 
ATOM   5065 C  C   . PRO E  1 85  ? 12.308  -20.370 78.763  1.00 41.96  ? 334  PRO E C   1 
ATOM   5066 O  O   . PRO E  1 85  ? 11.340  -20.140 78.023  1.00 46.17  ? 334  PRO E O   1 
ATOM   5067 C  CB  . PRO E  1 85  ? 12.831  -22.774 79.131  1.00 41.68  ? 334  PRO E CB  1 
ATOM   5068 C  CG  . PRO E  1 85  ? 11.618  -23.364 78.452  1.00 41.92  ? 334  PRO E CG  1 
ATOM   5069 C  CD  . PRO E  1 85  ? 10.466  -23.058 79.382  1.00 41.33  ? 334  PRO E CD  1 
ATOM   5070 N  N   . LEU E  1 86  ? 13.438  -19.683 78.716  1.00 37.95  ? 335  LEU E N   1 
ATOM   5071 C  CA  . LEU E  1 86  ? 13.654  -18.720 77.693  1.00 38.14  ? 335  LEU E CA  1 
ATOM   5072 C  C   . LEU E  1 86  ? 14.035  -19.494 76.432  1.00 42.83  ? 335  LEU E C   1 
ATOM   5073 O  O   . LEU E  1 86  ? 15.073  -20.140 76.386  1.00 43.51  ? 335  LEU E O   1 
ATOM   5074 C  CB  . LEU E  1 86  ? 14.759  -17.735 78.090  1.00 34.96  ? 335  LEU E CB  1 
ATOM   5075 C  CG  . LEU E  1 86  ? 15.017  -16.695 77.006  1.00 32.57  ? 335  LEU E CG  1 
ATOM   5076 C  CD1 . LEU E  1 86  ? 13.793  -15.807 76.772  1.00 31.20  ? 335  LEU E CD1 1 
ATOM   5077 C  CD2 . LEU E  1 86  ? 16.240  -15.866 77.334  1.00 36.14  ? 335  LEU E CD2 1 
ATOM   5078 N  N   . LEU E  1 87  ? 13.197  -19.409 75.410  1.00 42.73  ? 336  LEU E N   1 
ATOM   5079 C  CA  . LEU E  1 87  ? 13.418  -20.139 74.174  1.00 44.47  ? 336  LEU E CA  1 
ATOM   5080 C  C   . LEU E  1 87  ? 14.518  -19.510 73.316  1.00 44.56  ? 336  LEU E C   1 
ATOM   5081 O  O   . LEU E  1 87  ? 14.620  -18.282 73.242  1.00 43.78  ? 336  LEU E O   1 
ATOM   5082 C  CB  . LEU E  1 87  ? 12.106  -20.227 73.369  1.00 45.57  ? 336  LEU E CB  1 
ATOM   5083 C  CG  . LEU E  1 87  ? 10.923  -20.932 74.055  1.00 47.28  ? 336  LEU E CG  1 
ATOM   5084 C  CD1 . LEU E  1 87  ? 9.628   -20.794 73.258  1.00 45.38  ? 336  LEU E CD1 1 
ATOM   5085 C  CD2 . LEU E  1 87  ? 11.258  -22.407 74.294  1.00 46.38  ? 336  LEU E CD2 1 
ATOM   5086 N  N   . PRO E  1 88  ? 15.337  -20.354 72.637  1.00 43.38  ? 337  PRO E N   1 
ATOM   5087 C  CA  . PRO E  1 88  ? 16.372  -19.843 71.732  1.00 39.84  ? 337  PRO E CA  1 
ATOM   5088 C  C   . PRO E  1 88  ? 15.864  -18.748 70.824  1.00 37.08  ? 337  PRO E C   1 
ATOM   5089 O  O   . PRO E  1 88  ? 16.551  -17.773 70.591  1.00 38.09  ? 337  PRO E O   1 
ATOM   5090 C  CB  . PRO E  1 88  ? 16.786  -21.081 70.903  1.00 39.96  ? 337  PRO E CB  1 
ATOM   5091 C  CG  . PRO E  1 88  ? 16.418  -22.247 71.754  1.00 40.45  ? 337  PRO E CG  1 
ATOM   5092 C  CD  . PRO E  1 88  ? 15.408  -21.819 72.792  1.00 41.77  ? 337  PRO E CD  1 
ATOM   5093 N  N   . SER E  1 89  ? 14.648  -18.889 70.322  1.00 36.66  ? 338  SER E N   1 
ATOM   5094 C  CA  . SER E  1 89  ? 14.146  -17.928 69.348  1.00 40.79  ? 338  SER E CA  1 
ATOM   5095 C  C   . SER E  1 89  ? 13.896  -16.531 69.945  1.00 42.86  ? 338  SER E C   1 
ATOM   5096 O  O   . SER E  1 89  ? 13.699  -15.571 69.199  1.00 47.26  ? 338  SER E O   1 
ATOM   5097 C  CB  . SER E  1 89  ? 12.850  -18.444 68.734  1.00 41.78  ? 338  SER E CB  1 
ATOM   5098 O  OG  . SER E  1 89  ? 11.827  -18.471 69.717  1.00 42.53  ? 338  SER E OG  1 
ATOM   5099 N  N   . PHE E  1 90  ? 13.887  -16.439 71.274  1.00 39.67  ? 339  PHE E N   1 
ATOM   5100 C  CA  . PHE E  1 90  ? 13.685  -15.173 71.972  1.00 41.91  ? 339  PHE E CA  1 
ATOM   5101 C  C   . PHE E  1 90  ? 14.969  -14.417 72.268  1.00 41.84  ? 339  PHE E C   1 
ATOM   5102 O  O   . PHE E  1 90  ? 14.913  -13.204 72.498  1.00 40.32  ? 339  PHE E O   1 
ATOM   5103 C  CB  . PHE E  1 90  ? 12.922  -15.403 73.265  1.00 43.57  ? 339  PHE E CB  1 
ATOM   5104 C  CG  . PHE E  1 90  ? 11.457  -15.552 73.055  1.00 48.47  ? 339  PHE E CG  1 
ATOM   5105 C  CD1 . PHE E  1 90  ? 10.966  -16.576 72.263  1.00 51.42  ? 339  PHE E CD1 1 
ATOM   5106 C  CD2 . PHE E  1 90  ? 10.567  -14.663 73.622  1.00 52.41  ? 339  PHE E CD2 1 
ATOM   5107 C  CE1 . PHE E  1 90  ? 9.621   -16.718 72.036  1.00 49.86  ? 339  PHE E CE1 1 
ATOM   5108 C  CE2 . PHE E  1 90  ? 9.215   -14.801 73.407  1.00 55.51  ? 339  PHE E CE2 1 
ATOM   5109 C  CZ  . PHE E  1 90  ? 8.743   -15.826 72.604  1.00 56.14  ? 339  PHE E CZ  1 
ATOM   5110 N  N   . LYS E  1 91  ? 16.111  -15.116 72.207  1.00 40.63  ? 340  LYS E N   1 
ATOM   5111 C  CA  . LYS E  1 91  ? 17.404  -14.568 72.583  1.00 40.72  ? 340  LYS E CA  1 
ATOM   5112 C  C   . LYS E  1 91  ? 17.815  -13.417 71.680  1.00 40.43  ? 340  LYS E C   1 
ATOM   5113 O  O   . LYS E  1 91  ? 18.572  -12.552 72.104  1.00 46.16  ? 340  LYS E O   1 
ATOM   5114 C  CB  . LYS E  1 91  ? 18.471  -15.663 72.612  1.00 48.65  ? 340  LYS E CB  1 
ATOM   5115 C  CG  . LYS E  1 91  ? 18.255  -16.703 73.713  1.00 53.89  ? 340  LYS E CG  1 
ATOM   5116 C  CD  . LYS E  1 91  ? 19.085  -17.954 73.452  1.00 63.34  ? 340  LYS E CD  1 
ATOM   5117 C  CE  . LYS E  1 91  ? 19.402  -18.726 74.730  1.00 70.44  ? 340  LYS E CE  1 
ATOM   5118 N  NZ  . LYS E  1 91  ? 18.193  -19.127 75.503  1.00 74.30  ? 340  LYS E NZ  1 
ATOM   5119 N  N   . GLN E  1 92  ? 17.261  -13.374 70.466  1.00 36.58  ? 341  GLN E N   1 
ATOM   5120 C  CA  . GLN E  1 92  ? 17.384  -12.234 69.580  1.00 35.05  ? 341  GLN E CA  1 
ATOM   5121 C  C   . GLN E  1 92  ? 16.852  -10.925 70.118  1.00 33.30  ? 341  GLN E C   1 
ATOM   5122 O  O   . GLN E  1 92  ? 17.183  -9.896  69.586  1.00 31.11  ? 341  GLN E O   1 
ATOM   5123 C  CB  . GLN E  1 92  ? 16.656  -12.482 68.282  1.00 39.03  ? 341  GLN E CB  1 
ATOM   5124 C  CG  . GLN E  1 92  ? 15.174  -12.706 68.454  1.00 43.11  ? 341  GLN E CG  1 
ATOM   5125 C  CD  . GLN E  1 92  ? 14.458  -12.837 67.136  1.00 44.61  ? 341  GLN E CD  1 
ATOM   5126 O  OE1 . GLN E  1 92  ? 14.485  -11.926 66.321  1.00 46.35  ? 341  GLN E OE1 1 
ATOM   5127 N  NE2 . GLN E  1 92  ? 13.795  -13.972 66.930  1.00 42.94  ? 341  GLN E NE2 1 
ATOM   5128 N  N   . TYR E  1 93  ? 16.025  -10.953 71.153  1.00 35.37  ? 342  TYR E N   1 
ATOM   5129 C  CA  . TYR E  1 93  ? 15.497  -9.705  71.766  1.00 31.87  ? 342  TYR E CA  1 
ATOM   5130 C  C   . TYR E  1 93  ? 16.443  -8.948  72.693  1.00 33.55  ? 342  TYR E C   1 
ATOM   5131 O  O   . TYR E  1 93  ? 16.333  -7.693  72.833  1.00 34.68  ? 342  TYR E O   1 
ATOM   5132 C  CB  . TYR E  1 93  ? 14.171  -10.028 72.444  1.00 33.62  ? 342  TYR E CB  1 
ATOM   5133 C  CG  . TYR E  1 93  ? 13.156  -10.512 71.397  1.00 33.49  ? 342  TYR E CG  1 
ATOM   5134 C  CD1 . TYR E  1 93  ? 12.968  -9.808  70.206  1.00 32.47  ? 342  TYR E CD1 1 
ATOM   5135 C  CD2 . TYR E  1 93  ? 12.446  -11.690 71.582  1.00 33.14  ? 342  TYR E CD2 1 
ATOM   5136 C  CE1 . TYR E  1 93  ? 12.063  -10.236 69.268  1.00 32.58  ? 342  TYR E CE1 1 
ATOM   5137 C  CE2 . TYR E  1 93  ? 11.537  -12.140 70.646  1.00 34.21  ? 342  TYR E CE2 1 
ATOM   5138 C  CZ  . TYR E  1 93  ? 11.369  -11.436 69.483  1.00 34.12  ? 342  TYR E CZ  1 
ATOM   5139 O  OH  . TYR E  1 93  ? 10.462  -11.916 68.571  1.00 34.06  ? 342  TYR E OH  1 
ATOM   5140 N  N   . TRP E  1 94  ? 17.397  -9.667  73.283  1.00 30.44  ? 343  TRP E N   1 
ATOM   5141 C  CA  . TRP E  1 94  ? 18.473  -9.024  74.038  1.00 32.49  ? 343  TRP E CA  1 
ATOM   5142 C  C   . TRP E  1 94  ? 19.137  -7.896  73.241  1.00 31.37  ? 343  TRP E C   1 
ATOM   5143 O  O   . TRP E  1 94  ? 19.430  -8.073  72.079  1.00 31.51  ? 343  TRP E O   1 
ATOM   5144 C  CB  . TRP E  1 94  ? 19.564  -10.036 74.425  1.00 31.40  ? 343  TRP E CB  1 
ATOM   5145 C  CG  . TRP E  1 94  ? 19.165  -11.022 75.465  1.00 29.60  ? 343  TRP E CG  1 
ATOM   5146 C  CD1 . TRP E  1 94  ? 19.109  -12.363 75.301  1.00 28.35  ? 343  TRP E CD1 1 
ATOM   5147 C  CD2 . TRP E  1 94  ? 18.791  -10.757 76.835  1.00 28.22  ? 343  TRP E CD2 1 
ATOM   5148 N  NE1 . TRP E  1 94  ? 18.700  -12.967 76.473  1.00 31.29  ? 343  TRP E NE1 1 
ATOM   5149 C  CE2 . TRP E  1 94  ? 18.497  -12.007 77.431  1.00 30.44  ? 343  TRP E CE2 1 
ATOM   5150 C  CE3 . TRP E  1 94  ? 18.668  -9.591  77.608  1.00 26.91  ? 343  TRP E CE3 1 
ATOM   5151 C  CZ2 . TRP E  1 94  ? 18.109  -12.134 78.773  1.00 28.68  ? 343  TRP E CZ2 1 
ATOM   5152 C  CZ3 . TRP E  1 94  ? 18.256  -9.695  78.918  1.00 25.84  ? 343  TRP E CZ3 1 
ATOM   5153 C  CH2 . TRP E  1 94  ? 17.979  -10.968 79.498  1.00 30.36  ? 343  TRP E CH2 1 
ATOM   5154 N  N   . ASN E  1 95  ? 19.378  -6.751  73.870  1.00 31.72  ? 344  ASN E N   1 
ATOM   5155 C  CA  . ASN E  1 95  ? 20.142  -5.701  73.221  1.00 34.29  ? 344  ASN E CA  1 
ATOM   5156 C  C   . ASN E  1 95  ? 21.520  -6.251  72.943  1.00 37.13  ? 344  ASN E C   1 
ATOM   5157 O  O   . ASN E  1 95  ? 21.972  -7.166  73.619  1.00 33.33  ? 344  ASN E O   1 
ATOM   5158 C  CB  . ASN E  1 95  ? 20.276  -4.448  74.087  1.00 33.72  ? 344  ASN E CB  1 
ATOM   5159 C  CG  . ASN E  1 95  ? 18.983  -3.700  74.244  1.00 34.79  ? 344  ASN E CG  1 
ATOM   5160 O  OD1 . ASN E  1 95  ? 18.120  -3.753  73.376  1.00 34.53  ? 344  ASN E OD1 1 
ATOM   5161 N  ND2 . ASN E  1 95  ? 18.831  -2.994  75.373  1.00 34.50  ? 344  ASN E ND2 1 
ATOM   5162 N  N   . ARG E  1 96  ? 22.181  -5.688  71.931  1.00 43.89  ? 345  ARG E N   1 
ATOM   5163 C  CA  . ARG E  1 96  ? 23.540  -6.066  71.603  1.00 43.78  ? 345  ARG E CA  1 
ATOM   5164 C  C   . ARG E  1 96  ? 24.386  -5.974  72.857  1.00 39.17  ? 345  ARG E C   1 
ATOM   5165 O  O   . ARG E  1 96  ? 24.336  -4.990  73.574  1.00 44.05  ? 345  ARG E O   1 
ATOM   5166 C  CB  . ARG E  1 96  ? 24.110  -5.157  70.504  1.00 53.76  ? 345  ARG E CB  1 
ATOM   5167 C  CG  . ARG E  1 96  ? 25.618  -5.319  70.260  1.00 64.08  ? 345  ARG E CG  1 
ATOM   5168 C  CD  . ARG E  1 96  ? 26.132  -4.604  69.009  1.00 72.94  ? 345  ARG E CD  1 
ATOM   5169 N  NE  . ARG E  1 96  ? 25.427  -5.042  67.799  1.00 84.26  ? 345  ARG E NE  1 
ATOM   5170 C  CZ  . ARG E  1 96  ? 24.414  -4.395  67.217  1.00 90.65  ? 345  ARG E CZ  1 
ATOM   5171 N  NH1 . ARG E  1 96  ? 23.854  -4.903  66.122  1.00 91.81  ? 345  ARG E NH1 1 
ATOM   5172 N  NH2 . ARG E  1 96  ? 23.950  -3.246  67.710  1.00 93.48  ? 345  ARG E NH2 1 
ATOM   5173 N  N   . GLY E  1 97  ? 25.142  -7.034  73.106  1.00 35.97  ? 346  GLY E N   1 
ATOM   5174 C  CA  . GLY E  1 97  ? 26.002  -7.174  74.253  1.00 34.62  ? 346  GLY E CA  1 
ATOM   5175 C  C   . GLY E  1 97  ? 25.300  -7.697  75.503  1.00 36.48  ? 346  GLY E C   1 
ATOM   5176 O  O   . GLY E  1 97  ? 25.947  -7.870  76.515  1.00 36.47  ? 346  GLY E O   1 
ATOM   5177 N  N   . GLU E  1 98  ? 23.981  -7.901  75.467  1.00 34.56  ? 347  GLU E N   1 
ATOM   5178 C  CA  . GLU E  1 98  ? 23.279  -8.348  76.669  1.00 34.90  ? 347  GLU E CA  1 
ATOM   5179 C  C   . GLU E  1 98  ? 22.855  -9.787  76.460  1.00 33.46  ? 347  GLU E C   1 
ATOM   5180 O  O   . GLU E  1 98  ? 22.841  -10.238 75.315  1.00 33.99  ? 347  GLU E O   1 
ATOM   5181 C  CB  . GLU E  1 98  ? 22.104  -7.439  76.952  1.00 34.64  ? 347  GLU E CB  1 
ATOM   5182 C  CG  . GLU E  1 98  ? 22.475  -5.946  76.971  1.00 33.28  ? 347  GLU E CG  1 
ATOM   5183 C  CD  . GLU E  1 98  ? 23.357  -5.498  78.149  1.00 32.36  ? 347  GLU E CD  1 
ATOM   5184 O  OE1 . GLU E  1 98  ? 23.638  -6.270  79.096  1.00 33.04  ? 347  GLU E OE1 1 
ATOM   5185 O  OE2 . GLU E  1 98  ? 23.763  -4.314  78.147  1.00 34.79  ? 347  GLU E OE2 1 
ATOM   5186 N  N   . PRO E  1 99  ? 22.573  -10.533 77.525  1.00 30.57  ? 348  PRO E N   1 
ATOM   5187 C  CA  . PRO E  1 99  ? 22.780  -10.111 78.907  1.00 33.52  ? 348  PRO E CA  1 
ATOM   5188 C  C   . PRO E  1 99  ? 24.259  -10.275 79.347  1.00 36.27  ? 348  PRO E C   1 
ATOM   5189 O  O   . PRO E  1 99  ? 24.865  -11.301 79.040  1.00 37.81  ? 348  PRO E O   1 
ATOM   5190 C  CB  . PRO E  1 99  ? 21.874  -11.068 79.678  1.00 30.56  ? 348  PRO E CB  1 
ATOM   5191 C  CG  . PRO E  1 99  ? 21.974  -12.348 78.901  1.00 33.06  ? 348  PRO E CG  1 
ATOM   5192 C  CD  . PRO E  1 99  ? 22.210  -11.956 77.446  1.00 30.98  ? 348  PRO E CD  1 
ATOM   5193 N  N   . ASN E  1 100 ? 24.808  -9.301  80.076  1.00 35.41  ? 349  ASN E N   1 
ATOM   5194 C  CA  . ASN E  1 100 ? 26.258  -9.282  80.460  1.00 33.81  ? 349  ASN E CA  1 
ATOM   5195 C  C   . ASN E  1 100 ? 26.540  -9.468  81.959  1.00 32.21  ? 349  ASN E C   1 
ATOM   5196 O  O   . ASN E  1 100 ? 27.676  -9.590  82.366  1.00 32.95  ? 349  ASN E O   1 
ATOM   5197 C  CB  . ASN E  1 100 ? 26.894  -7.972  79.966  1.00 36.07  ? 349  ASN E CB  1 
ATOM   5198 C  CG  . ASN E  1 100 ? 26.181  -6.716  80.506  1.00 38.08  ? 349  ASN E CG  1 
ATOM   5199 O  OD1 . ASN E  1 100 ? 25.286  -6.802  81.355  1.00 31.55  ? 349  ASN E OD1 1 
ATOM   5200 N  ND2 . ASN E  1 100 ? 26.598  -5.539  80.022  1.00 37.52  ? 349  ASN E ND2 1 
ATOM   5201 N  N   . ASN E  1 101 ? 25.509  -9.455  82.790  1.00 30.40  ? 350  ASN E N   1 
ATOM   5202 C  CA  . ASN E  1 101 ? 25.674  -9.644  84.232  1.00 30.39  ? 350  ASN E CA  1 
ATOM   5203 C  C   . ASN E  1 101 ? 26.584  -8.617  84.904  1.00 32.09  ? 350  ASN E C   1 
ATOM   5204 O  O   . ASN E  1 101 ? 27.047  -8.851  86.025  1.00 30.02  ? 350  ASN E O   1 
ATOM   5205 C  CB  . ASN E  1 101 ? 26.185  -11.075 84.569  1.00 29.36  ? 350  ASN E CB  1 
ATOM   5206 C  CG  . ASN E  1 101 ? 25.840  -11.487 85.989  1.00 29.34  ? 350  ASN E CG  1 
ATOM   5207 O  OD1 . ASN E  1 101 ? 24.776  -11.164 86.497  1.00 31.27  ? 350  ASN E OD1 1 
ATOM   5208 N  ND2 . ASN E  1 101 ? 26.742  -12.187 86.646  1.00 34.32  ? 350  ASN E ND2 1 
ATOM   5209 N  N   . VAL E  1 102 ? 26.770  -7.447  84.276  1.00 35.51  ? 351  VAL E N   1 
ATOM   5210 C  CA  . VAL E  1 102 ? 27.759  -6.496  84.755  1.00 33.35  ? 351  VAL E CA  1 
ATOM   5211 C  C   . VAL E  1 102 ? 27.339  -5.894  86.095  1.00 34.91  ? 351  VAL E C   1 
ATOM   5212 O  O   . VAL E  1 102 ? 26.349  -5.188  86.216  1.00 33.78  ? 351  VAL E O   1 
ATOM   5213 C  CB  . VAL E  1 102 ? 28.105  -5.414  83.704  1.00 35.49  ? 351  VAL E CB  1 
ATOM   5214 C  CG1 . VAL E  1 102 ? 26.977  -4.390  83.514  1.00 35.42  ? 351  VAL E CG1 1 
ATOM   5215 C  CG2 . VAL E  1 102 ? 29.379  -4.690  84.106  1.00 35.17  ? 351  VAL E CG2 1 
ATOM   5216 N  N   . GLY E  1 103 ? 28.124  -6.178  87.112  1.00 37.37  ? 352  GLY E N   1 
ATOM   5217 C  CA  . GLY E  1 103 ? 27.758  -5.794  88.483  1.00 40.86  ? 352  GLY E CA  1 
ATOM   5218 C  C   . GLY E  1 103 ? 26.651  -6.661  89.072  1.00 37.44  ? 352  GLY E C   1 
ATOM   5219 O  O   . GLY E  1 103 ? 25.995  -6.244  90.026  1.00 39.27  ? 352  GLY E O   1 
ATOM   5220 N  N   . GLU E  1 104 ? 26.472  -7.865  88.515  1.00 38.36  ? 353  GLU E N   1 
ATOM   5221 C  CA  . GLU E  1 104 ? 25.384  -8.783  88.912  1.00 38.82  ? 353  GLU E CA  1 
ATOM   5222 C  C   . GLU E  1 104 ? 23.989  -8.232  88.629  1.00 34.93  ? 353  GLU E C   1 
ATOM   5223 O  O   . GLU E  1 104 ? 23.430  -7.401  89.369  1.00 34.87  ? 353  GLU E O   1 
ATOM   5224 C  CB  . GLU E  1 104 ? 25.532  -9.250  90.355  1.00 42.55  ? 353  GLU E CB  1 
ATOM   5225 C  CG  . GLU E  1 104 ? 26.931  -9.844  90.534  1.00 53.41  ? 353  GLU E CG  1 
ATOM   5226 C  CD  . GLU E  1 104 ? 26.962  -11.164 91.276  1.00 60.26  ? 353  GLU E CD  1 
ATOM   5227 O  OE1 . GLU E  1 104 ? 27.073  -11.132 92.526  1.00 66.08  ? 353  GLU E OE1 1 
ATOM   5228 O  OE2 . GLU E  1 104 ? 26.910  -12.218 90.597  1.00 60.39  ? 353  GLU E OE2 1 
ATOM   5229 N  N   . GLU E  1 105 ? 23.456  -8.749  87.532  1.00 31.66  ? 354  GLU E N   1 
ATOM   5230 C  CA  . GLU E  1 105 ? 22.215  -8.305  86.956  1.00 29.02  ? 354  GLU E CA  1 
ATOM   5231 C  C   . GLU E  1 105 ? 21.410  -9.546  86.690  1.00 26.39  ? 354  GLU E C   1 
ATOM   5232 O  O   . GLU E  1 105 ? 21.696  -10.277 85.783  1.00 24.32  ? 354  GLU E O   1 
ATOM   5233 C  CB  . GLU E  1 105 ? 22.515  -7.558  85.643  1.00 26.59  ? 354  GLU E CB  1 
ATOM   5234 C  CG  . GLU E  1 105 ? 23.186  -6.212  85.888  1.00 27.97  ? 354  GLU E CG  1 
ATOM   5235 C  CD  . GLU E  1 105 ? 23.488  -5.419  84.635  1.00 28.83  ? 354  GLU E CD  1 
ATOM   5236 O  OE1 . GLU E  1 105 ? 23.857  -6.045  83.587  1.00 28.61  ? 354  GLU E OE1 1 
ATOM   5237 O  OE2 . GLU E  1 105 ? 23.347  -4.160  84.712  1.00 31.20  ? 354  GLU E OE2 1 
ATOM   5238 N  N   . ASP E  1 106 ? 20.392  -9.791  87.506  1.00 28.61  ? 355  ASP E N   1 
ATOM   5239 C  CA  . ASP E  1 106 ? 19.612  -11.003 87.351  1.00 27.41  ? 355  ASP E CA  1 
ATOM   5240 C  C   . ASP E  1 106 ? 18.157  -10.804 86.904  1.00 29.18  ? 355  ASP E C   1 
ATOM   5241 O  O   . ASP E  1 106 ? 17.431  -11.771 86.817  1.00 31.29  ? 355  ASP E O   1 
ATOM   5242 C  CB  . ASP E  1 106 ? 19.673  -11.789 88.636  1.00 28.12  ? 355  ASP E CB  1 
ATOM   5243 C  CG  . ASP E  1 106 ? 21.086  -12.161 89.011  1.00 28.38  ? 355  ASP E CG  1 
ATOM   5244 O  OD1 . ASP E  1 106 ? 21.966  -12.308 88.109  1.00 24.13  ? 355  ASP E OD1 1 
ATOM   5245 O  OD2 . ASP E  1 106 ? 21.292  -12.285 90.234  1.00 28.99  ? 355  ASP E OD2 1 
ATOM   5246 N  N   . CYS E  1 107 ? 17.750  -9.572  86.597  1.00 27.72  ? 356  CYS E N   1 
ATOM   5247 C  CA  . CYS E  1 107 ? 16.365  -9.317  86.214  1.00 28.13  ? 356  CYS E CA  1 
ATOM   5248 C  C   . CYS E  1 107 ? 16.312  -8.682  84.842  1.00 28.41  ? 356  CYS E C   1 
ATOM   5249 O  O   . CYS E  1 107 ? 17.175  -7.893  84.522  1.00 27.61  ? 356  CYS E O   1 
ATOM   5250 C  CB  . CYS E  1 107 ? 15.720  -8.446  87.270  1.00 30.55  ? 356  CYS E CB  1 
ATOM   5251 S  SG  . CYS E  1 107 ? 15.478  -9.336  88.838  1.00 30.74  ? 356  CYS E SG  1 
ATOM   5252 N  N   . ALA E  1 108 ? 15.335  -9.080  84.023  1.00 26.85  ? 357  ALA E N   1 
ATOM   5253 C  CA  . ALA E  1 108 ? 15.195  -8.594  82.637  1.00 28.28  ? 357  ALA E CA  1 
ATOM   5254 C  C   . ALA E  1 108 ? 14.266  -7.367  82.516  1.00 29.55  ? 357  ALA E C   1 
ATOM   5255 O  O   . ALA E  1 108 ? 13.215  -7.274  83.172  1.00 29.15  ? 357  ALA E O   1 
ATOM   5256 C  CB  . ALA E  1 108 ? 14.682  -9.698  81.726  1.00 29.03  ? 357  ALA E CB  1 
ATOM   5257 N  N   . GLU E  1 109 ? 14.669  -6.425  81.677  1.00 28.81  ? 358  GLU E N   1 
ATOM   5258 C  CA  . GLU E  1 109 ? 13.920  -5.175  81.505  1.00 27.82  ? 358  GLU E CA  1 
ATOM   5259 C  C   . GLU E  1 109 ? 13.848  -4.927  80.029  1.00 27.32  ? 358  GLU E C   1 
ATOM   5260 O  O   . GLU E  1 109 ? 14.745  -5.368  79.271  1.00 25.21  ? 358  GLU E O   1 
ATOM   5261 C  CB  . GLU E  1 109 ? 14.592  -3.985  82.206  1.00 30.46  ? 358  GLU E CB  1 
ATOM   5262 C  CG  . GLU E  1 109 ? 16.030  -3.695  81.748  1.00 34.43  ? 358  GLU E CG  1 
ATOM   5263 C  CD  . GLU E  1 109 ? 16.512  -2.274  81.981  1.00 36.87  ? 358  GLU E CD  1 
ATOM   5264 O  OE1 . GLU E  1 109 ? 15.714  -1.405  82.368  1.00 36.60  ? 358  GLU E OE1 1 
ATOM   5265 O  OE2 . GLU E  1 109 ? 17.720  -2.014  81.752  1.00 38.93  ? 358  GLU E OE2 1 
ATOM   5266 N  N   . PHE E  1 110 ? 12.779  -4.258  79.617  1.00 25.50  ? 359  PHE E N   1 
ATOM   5267 C  CA  . PHE E  1 110 ? 12.719  -3.725  78.290  1.00 26.49  ? 359  PHE E CA  1 
ATOM   5268 C  C   . PHE E  1 110 ? 13.493  -2.414  78.414  1.00 28.97  ? 359  PHE E C   1 
ATOM   5269 O  O   . PHE E  1 110 ? 13.304  -1.644  79.376  1.00 27.47  ? 359  PHE E O   1 
ATOM   5270 C  CB  . PHE E  1 110 ? 11.292  -3.392  77.825  1.00 25.92  ? 359  PHE E CB  1 
ATOM   5271 C  CG  . PHE E  1 110 ? 10.345  -4.551  77.801  1.00 26.03  ? 359  PHE E CG  1 
ATOM   5272 C  CD1 . PHE E  1 110 ? 10.213  -5.325  76.661  1.00 26.32  ? 359  PHE E CD1 1 
ATOM   5273 C  CD2 . PHE E  1 110 ? 9.531   -4.825  78.868  1.00 27.10  ? 359  PHE E CD2 1 
ATOM   5274 C  CE1 . PHE E  1 110 ? 9.318   -6.358  76.599  1.00 25.62  ? 359  PHE E CE1 1 
ATOM   5275 C  CE2 . PHE E  1 110 ? 8.646   -5.884  78.821  1.00 27.67  ? 359  PHE E CE2 1 
ATOM   5276 C  CZ  . PHE E  1 110 ? 8.531   -6.640  77.679  1.00 26.35  ? 359  PHE E CZ  1 
ATOM   5277 N  N   . SER E  1 111 ? 14.321  -2.130  77.426  1.00 29.63  ? 360  SER E N   1 
ATOM   5278 C  CA  . SER E  1 111 ? 15.196  -0.982  77.487  1.00 32.43  ? 360  SER E CA  1 
ATOM   5279 C  C   . SER E  1 111 ? 15.557  -0.614  76.079  1.00 32.09  ? 360  SER E C   1 
ATOM   5280 O  O   . SER E  1 111 ? 16.326  -1.318  75.414  1.00 32.17  ? 360  SER E O   1 
ATOM   5281 C  CB  . SER E  1 111 ? 16.447  -1.359  78.289  1.00 33.79  ? 360  SER E CB  1 
ATOM   5282 O  OG  . SER E  1 111 ? 17.344  -0.270  78.381  1.00 37.71  ? 360  SER E OG  1 
ATOM   5283 N  N   . GLY E  1 112 ? 14.993  0.482   75.610  1.00 35.78  ? 361  GLY E N   1 
ATOM   5284 C  CA  . GLY E  1 112 ? 15.207  0.896   74.219  1.00 35.99  ? 361  GLY E CA  1 
ATOM   5285 C  C   . GLY E  1 112 ? 14.450  -0.033  73.287  1.00 37.55  ? 361  GLY E C   1 
ATOM   5286 O  O   . GLY E  1 112 ? 13.271  -0.253  73.468  1.00 34.99  ? 361  GLY E O   1 
ATOM   5287 N  N   . ASN E  1 113 ? 15.150  -0.613  72.317  1.00 37.72  ? 362  ASN E N   1 
ATOM   5288 C  CA  . ASN E  1 113 ? 14.536  -1.477  71.363  1.00 38.15  ? 362  ASN E CA  1 
ATOM   5289 C  C   . ASN E  1 113 ? 14.604  -2.939  71.743  1.00 36.28  ? 362  ASN E C   1 
ATOM   5290 O  O   . ASN E  1 113 ? 14.072  -3.806  71.020  1.00 33.51  ? 362  ASN E O   1 
ATOM   5291 C  CB  . ASN E  1 113 ? 15.231  -1.292  70.031  1.00 42.29  ? 362  ASN E CB  1 
ATOM   5292 C  CG  . ASN E  1 113 ? 15.105  0.113   69.525  1.00 46.65  ? 362  ASN E CG  1 
ATOM   5293 O  OD1 . ASN E  1 113 ? 16.101  0.746   69.164  1.00 52.26  ? 362  ASN E OD1 1 
ATOM   5294 N  ND2 . ASN E  1 113 ? 13.877  0.634   69.527  1.00 48.51  ? 362  ASN E ND2 1 
ATOM   5295 N  N   . GLY E  1 114 ? 15.251  -3.247  72.857  1.00 31.25  ? 363  GLY E N   1 
ATOM   5296 C  CA  . GLY E  1 114 ? 15.278  -4.641  73.255  1.00 30.94  ? 363  GLY E CA  1 
ATOM   5297 C  C   . GLY E  1 114 ? 15.261  -4.848  74.727  1.00 30.15  ? 363  GLY E C   1 
ATOM   5298 O  O   . GLY E  1 114 ? 14.745  -4.019  75.463  1.00 27.10  ? 363  GLY E O   1 
ATOM   5299 N  N   . TRP E  1 115 ? 15.931  -5.925  75.141  1.00 29.70  ? 364  TRP E N   1 
ATOM   5300 C  CA  . TRP E  1 115 ? 16.009  -6.324  76.535  1.00 31.24  ? 364  TRP E CA  1 
ATOM   5301 C  C   . TRP E  1 115 ? 17.416  -6.072  77.103  1.00 30.90  ? 364  TRP E C   1 
ATOM   5302 O  O   . TRP E  1 115 ? 18.427  -6.195  76.402  1.00 29.02  ? 364  TRP E O   1 
ATOM   5303 C  CB  . TRP E  1 115 ? 15.687  -7.811  76.713  1.00 29.64  ? 364  TRP E CB  1 
ATOM   5304 C  CG  . TRP E  1 115 ? 14.357  -8.304  76.138  1.00 30.10  ? 364  TRP E CG  1 
ATOM   5305 C  CD1 . TRP E  1 115 ? 13.377  -7.575  75.588  1.00 30.53  ? 364  TRP E CD1 1 
ATOM   5306 C  CD2 . TRP E  1 115 ? 13.906  -9.669  76.109  1.00 30.64  ? 364  TRP E CD2 1 
ATOM   5307 N  NE1 . TRP E  1 115 ? 12.337  -8.391  75.196  1.00 31.98  ? 364  TRP E NE1 1 
ATOM   5308 C  CE2 . TRP E  1 115 ? 12.649  -9.682  75.511  1.00 31.85  ? 364  TRP E CE2 1 
ATOM   5309 C  CE3 . TRP E  1 115 ? 14.483  -10.887 76.483  1.00 32.18  ? 364  TRP E CE3 1 
ATOM   5310 C  CZ2 . TRP E  1 115 ? 11.935  -10.867 75.299  1.00 34.52  ? 364  TRP E CZ2 1 
ATOM   5311 C  CZ3 . TRP E  1 115 ? 13.762  -12.057 76.298  1.00 31.42  ? 364  TRP E CZ3 1 
ATOM   5312 C  CH2 . TRP E  1 115 ? 12.517  -12.035 75.705  1.00 31.53  ? 364  TRP E CH2 1 
ATOM   5313 N  N   . ASN E  1 116 ? 17.445  -5.743  78.377  1.00 26.17  ? 365  ASN E N   1 
ATOM   5314 C  CA  . ASN E  1 116 ? 18.691  -5.647  79.106  1.00 29.00  ? 365  ASN E CA  1 
ATOM   5315 C  C   . ASN E  1 116 ? 18.492  -6.385  80.394  1.00 27.55  ? 365  ASN E C   1 
ATOM   5316 O  O   . ASN E  1 116 ? 17.380  -6.410  80.889  1.00 28.84  ? 365  ASN E O   1 
ATOM   5317 C  CB  . ASN E  1 116 ? 19.074  -4.187  79.406  1.00 26.04  ? 365  ASN E CB  1 
ATOM   5318 C  CG  . ASN E  1 116 ? 20.325  -4.105  80.223  1.00 29.64  ? 365  ASN E CG  1 
ATOM   5319 O  OD1 . ASN E  1 116 ? 21.278  -4.899  80.005  1.00 26.69  ? 365  ASN E OD1 1 
ATOM   5320 N  ND2 . ASN E  1 116 ? 20.318  -3.240  81.240  1.00 27.56  ? 365  ASN E ND2 1 
ATOM   5321 N  N   . ASP E  1 117 ? 19.555  -7.010  80.919  1.00 30.03  ? 366  ASP E N   1 
ATOM   5322 C  CA  . ASP E  1 117 ? 19.605  -7.409  82.321  1.00 29.88  ? 366  ASP E CA  1 
ATOM   5323 C  C   . ASP E  1 117 ? 20.156  -6.289  83.191  1.00 28.68  ? 366  ASP E C   1 
ATOM   5324 O  O   . ASP E  1 117 ? 21.129  -5.651  82.841  1.00 25.47  ? 366  ASP E O   1 
ATOM   5325 C  CB  . ASP E  1 117 ? 20.396  -8.745  82.567  1.00 33.92  ? 366  ASP E CB  1 
ATOM   5326 C  CG  . ASP E  1 117 ? 21.882  -8.704  82.096  1.00 35.37  ? 366  ASP E CG  1 
ATOM   5327 O  OD1 . ASP E  1 117 ? 22.247  -7.861  81.225  1.00 32.40  ? 366  ASP E OD1 1 
ATOM   5328 O  OD2 . ASP E  1 117 ? 22.659  -9.570  82.585  1.00 36.97  ? 366  ASP E OD2 1 
ATOM   5329 N  N   . ASP E  1 118 ? 19.512  -6.079  84.350  1.00 27.36  ? 367  ASP E N   1 
ATOM   5330 C  CA  . ASP E  1 118 ? 19.808  -4.980  85.229  1.00 26.80  ? 367  ASP E CA  1 
ATOM   5331 C  C   . ASP E  1 118 ? 19.646  -5.470  86.624  1.00 28.06  ? 367  ASP E C   1 
ATOM   5332 O  O   . ASP E  1 118 ? 19.157  -6.583  86.859  1.00 25.85  ? 367  ASP E O   1 
ATOM   5333 C  CB  . ASP E  1 118 ? 18.909  -3.737  84.953  1.00 27.66  ? 367  ASP E CB  1 
ATOM   5334 C  CG  . ASP E  1 118 ? 19.572  -2.397  85.425  1.00 28.63  ? 367  ASP E CG  1 
ATOM   5335 O  OD1 . ASP E  1 118 ? 20.645  -2.457  86.087  1.00 31.00  ? 367  ASP E OD1 1 
ATOM   5336 O  OD2 . ASP E  1 118 ? 19.019  -1.299  85.174  1.00 26.46  ? 367  ASP E OD2 1 
ATOM   5337 N  N   . LYS E  1 119 ? 20.026  -4.613  87.556  1.00 27.16  ? 368  LYS E N   1 
ATOM   5338 C  CA  . LYS E  1 119 ? 19.982  -4.918  88.958  1.00 27.45  ? 368  LYS E CA  1 
ATOM   5339 C  C   . LYS E  1 119 ? 18.571  -5.037  89.478  1.00 27.51  ? 368  LYS E C   1 
ATOM   5340 O  O   . LYS E  1 119 ? 17.800  -4.096  89.436  1.00 24.88  ? 368  LYS E O   1 
ATOM   5341 C  CB  . LYS E  1 119 ? 20.787  -3.891  89.764  1.00 30.09  ? 368  LYS E CB  1 
ATOM   5342 C  CG  . LYS E  1 119 ? 22.234  -3.809  89.266  1.00 36.49  ? 368  LYS E CG  1 
ATOM   5343 C  CD  . LYS E  1 119 ? 23.096  -2.955  90.181  1.00 47.62  ? 368  LYS E CD  1 
ATOM   5344 C  CE  . LYS E  1 119 ? 24.257  -2.314  89.437  1.00 55.32  ? 368  LYS E CE  1 
ATOM   5345 N  NZ  . LYS E  1 119 ? 24.820  -1.171  90.217  1.00 62.86  ? 368  LYS E NZ  1 
ATOM   5346 N  N   . CYS E  1 120 ? 18.273  -6.219  90.016  1.00 28.33  ? 369  CYS E N   1 
ATOM   5347 C  CA  . CYS E  1 120 ? 16.955  -6.543  90.524  1.00 29.55  ? 369  CYS E CA  1 
ATOM   5348 C  C   . CYS E  1 120 ? 16.436  -5.566  91.581  1.00 29.15  ? 369  CYS E C   1 
ATOM   5349 O  O   . CYS E  1 120 ? 15.244  -5.455  91.787  1.00 29.16  ? 369  CYS E O   1 
ATOM   5350 C  CB  . CYS E  1 120 ? 16.971  -7.970  91.110  1.00 29.31  ? 369  CYS E CB  1 
ATOM   5351 S  SG  . CYS E  1 120 ? 17.248  -9.227  89.846  1.00 32.17  ? 369  CYS E SG  1 
ATOM   5352 N  N   . ASN E  1 121 ? 17.328  -4.859  92.252  1.00 29.84  ? 370  ASN E N   1 
ATOM   5353 C  CA  . ASN E  1 121 ? 16.899  -3.986  93.342  1.00 31.43  ? 370  ASN E CA  1 
ATOM   5354 C  C   . ASN E  1 121 ? 16.615  -2.557  92.879  1.00 27.08  ? 370  ASN E C   1 
ATOM   5355 O  O   . ASN E  1 121 ? 16.171  -1.778  93.668  1.00 25.92  ? 370  ASN E O   1 
ATOM   5356 C  CB  . ASN E  1 121 ? 17.927  -3.984  94.472  1.00 34.86  ? 370  ASN E CB  1 
ATOM   5357 C  CG  . ASN E  1 121 ? 19.168  -3.213  94.091  1.00 40.98  ? 370  ASN E CG  1 
ATOM   5358 O  OD1 . ASN E  1 121 ? 19.738  -3.436  93.020  1.00 38.97  ? 370  ASN E OD1 1 
ATOM   5359 N  ND2 . ASN E  1 121 ? 19.550  -2.256  94.928  1.00 50.17  ? 370  ASN E ND2 1 
ATOM   5360 N  N   . LEU E  1 122 ? 16.894  -2.224  91.624  1.00 25.24  ? 371  LEU E N   1 
ATOM   5361 C  CA  . LEU E  1 122 ? 16.490  -0.941  91.087  1.00 28.73  ? 371  LEU E CA  1 
ATOM   5362 C  C   . LEU E  1 122 ? 14.979  -0.798  90.764  1.00 27.15  ? 371  LEU E C   1 
ATOM   5363 O  O   . LEU E  1 122 ? 14.294  -1.767  90.486  1.00 25.92  ? 371  LEU E O   1 
ATOM   5364 C  CB  . LEU E  1 122 ? 17.277  -0.642  89.834  1.00 29.70  ? 371  LEU E CB  1 
ATOM   5365 C  CG  . LEU E  1 122 ? 18.758  -0.361  90.090  1.00 31.24  ? 371  LEU E CG  1 
ATOM   5366 C  CD1 . LEU E  1 122 ? 19.467  -0.138  88.746  1.00 32.09  ? 371  LEU E CD1 1 
ATOM   5367 C  CD2 . LEU E  1 122 ? 18.984  0.834   90.993  1.00 31.64  ? 371  LEU E CD2 1 
ATOM   5368 N  N   . ALA E  1 123 ? 14.484  0.428   90.845  1.00 25.08  ? 372  ALA E N   1 
ATOM   5369 C  CA  . ALA E  1 123 ? 13.069  0.715   90.554  1.00 26.21  ? 372  ALA E CA  1 
ATOM   5370 C  C   . ALA E  1 123 ? 12.880  0.958   89.064  1.00 25.42  ? 372  ALA E C   1 
ATOM   5371 O  O   . ALA E  1 123 ? 13.638  1.682   88.450  1.00 26.32  ? 372  ALA E O   1 
ATOM   5372 C  CB  . ALA E  1 123 ? 12.556  1.913   91.372  1.00 24.57  ? 372  ALA E CB  1 
ATOM   5373 N  N   . LYS E  1 124 ? 11.889  0.278   88.481  1.00 25.30  ? 373  LYS E N   1 
ATOM   5374 C  CA  . LYS E  1 124 ? 11.476  0.488   87.118  1.00 24.33  ? 373  LYS E CA  1 
ATOM   5375 C  C   . LYS E  1 124 ? 9.960   0.387   87.051  1.00 23.16  ? 373  LYS E C   1 
ATOM   5376 O  O   . LYS E  1 124 ? 9.307   -0.080  87.963  1.00 23.00  ? 373  LYS E O   1 
ATOM   5377 C  CB  . LYS E  1 124 ? 12.054  -0.585  86.194  1.00 25.94  ? 373  LYS E CB  1 
ATOM   5378 C  CG  . LYS E  1 124 ? 13.569  -0.718  86.260  1.00 27.76  ? 373  LYS E CG  1 
ATOM   5379 C  CD  . LYS E  1 124 ? 14.087  -1.645  85.188  1.00 27.01  ? 373  LYS E CD  1 
ATOM   5380 C  CE  . LYS E  1 124 ? 15.582  -1.833  85.354  1.00 30.76  ? 373  LYS E CE  1 
ATOM   5381 N  NZ  . LYS E  1 124 ? 16.288  -0.656  84.765  1.00 35.48  ? 373  LYS E NZ  1 
ATOM   5382 N  N   . PHE E  1 125 ? 9.425   0.779   85.917  1.00 22.30  ? 374  PHE E N   1 
ATOM   5383 C  CA  . PHE E  1 125 ? 8.046   0.504   85.586  1.00 23.03  ? 374  PHE E CA  1 
ATOM   5384 C  C   . PHE E  1 125 ? 7.914   -1.023  85.400  1.00 23.59  ? 374  PHE E C   1 
ATOM   5385 O  O   . PHE E  1 125 ? 8.940   -1.779  85.328  1.00 20.41  ? 374  PHE E O   1 
ATOM   5386 C  CB  . PHE E  1 125 ? 7.626   1.300   84.339  1.00 23.76  ? 374  PHE E CB  1 
ATOM   5387 C  CG  . PHE E  1 125 ? 7.650   2.800   84.552  1.00 24.60  ? 374  PHE E CG  1 
ATOM   5388 C  CD1 . PHE E  1 125 ? 8.805   3.523   84.370  1.00 24.28  ? 374  PHE E CD1 1 
ATOM   5389 C  CD2 . PHE E  1 125 ? 6.517   3.472   84.997  1.00 27.90  ? 374  PHE E CD2 1 
ATOM   5390 C  CE1 . PHE E  1 125 ? 8.845   4.877   84.608  1.00 24.33  ? 374  PHE E CE1 1 
ATOM   5391 C  CE2 . PHE E  1 125 ? 6.547   4.849   85.224  1.00 26.77  ? 374  PHE E CE2 1 
ATOM   5392 C  CZ  . PHE E  1 125 ? 7.720   5.540   85.024  1.00 25.43  ? 374  PHE E CZ  1 
ATOM   5393 N  N   . TRP E  1 126 ? 6.665   -1.475  85.406  1.00 21.22  ? 375  TRP E N   1 
ATOM   5394 C  CA  . TRP E  1 126 ? 6.392   -2.882  85.233  1.00 25.03  ? 375  TRP E CA  1 
ATOM   5395 C  C   . TRP E  1 126 ? 5.082   -3.065  84.470  1.00 24.40  ? 375  TRP E C   1 
ATOM   5396 O  O   . TRP E  1 126 ? 4.254   -2.142  84.399  1.00 22.69  ? 375  TRP E O   1 
ATOM   5397 C  CB  . TRP E  1 126 ? 6.346   -3.623  86.571  1.00 22.87  ? 375  TRP E CB  1 
ATOM   5398 C  CG  . TRP E  1 126 ? 5.121   -3.370  87.401  1.00 25.03  ? 375  TRP E CG  1 
ATOM   5399 C  CD1 . TRP E  1 126 ? 3.928   -4.113  87.410  1.00 27.54  ? 375  TRP E CD1 1 
ATOM   5400 C  CD2 . TRP E  1 126 ? 4.939   -2.332  88.365  1.00 24.95  ? 375  TRP E CD2 1 
ATOM   5401 N  NE1 . TRP E  1 126 ? 3.040   -3.558  88.341  1.00 24.25  ? 375  TRP E NE1 1 
ATOM   5402 C  CE2 . TRP E  1 126 ? 3.637   -2.479  88.926  1.00 25.72  ? 375  TRP E CE2 1 
ATOM   5403 C  CE3 . TRP E  1 126 ? 5.750   -1.288  88.814  1.00 27.26  ? 375  TRP E CE3 1 
ATOM   5404 C  CZ2 . TRP E  1 126 ? 3.138   -1.613  89.909  1.00 26.06  ? 375  TRP E CZ2 1 
ATOM   5405 C  CZ3 . TRP E  1 126 ? 5.268   -0.436  89.773  1.00 27.65  ? 375  TRP E CZ3 1 
ATOM   5406 C  CH2 . TRP E  1 126 ? 3.961   -0.603  90.322  1.00 27.75  ? 375  TRP E CH2 1 
ATOM   5407 N  N   . ILE E  1 127 ? 4.898   -4.269  83.933  1.00 23.17  ? 376  ILE E N   1 
ATOM   5408 C  CA  . ILE E  1 127 ? 3.676   -4.612  83.224  1.00 24.63  ? 376  ILE E CA  1 
ATOM   5409 C  C   . ILE E  1 127 ? 3.167   -5.938  83.721  1.00 25.72  ? 376  ILE E C   1 
ATOM   5410 O  O   . ILE E  1 127 ? 3.901   -6.916  83.743  1.00 28.79  ? 376  ILE E O   1 
ATOM   5411 C  CB  . ILE E  1 127 ? 3.911   -4.706  81.710  1.00 26.15  ? 376  ILE E CB  1 
ATOM   5412 C  CG1 . ILE E  1 127 ? 4.317   -3.353  81.144  1.00 27.26  ? 376  ILE E CG1 1 
ATOM   5413 C  CG2 . ILE E  1 127 ? 2.641   -5.145  80.988  1.00 28.41  ? 376  ILE E CG2 1 
ATOM   5414 C  CD1 . ILE E  1 127 ? 4.920   -3.454  79.755  1.00 27.13  ? 376  ILE E CD1 1 
ATOM   5415 N  N   . CYS E  1 128 ? 1.913   -5.985  84.111  1.00 26.24  ? 377  CYS E N   1 
ATOM   5416 C  CA  . CYS E  1 128 ? 1.283   -7.265  84.429  1.00 28.24  ? 377  CYS E CA  1 
ATOM   5417 C  C   . CYS E  1 128 ? 0.418   -7.766  83.310  1.00 29.12  ? 377  CYS E C   1 
ATOM   5418 O  O   . CYS E  1 128 ? -0.147  -6.985  82.538  1.00 31.11  ? 377  CYS E O   1 
ATOM   5419 C  CB  . CYS E  1 128 ? 0.366   -7.155  85.636  1.00 29.30  ? 377  CYS E CB  1 
ATOM   5420 S  SG  . CYS E  1 128 ? 1.010   -6.256  87.033  1.00 29.03  ? 377  CYS E SG  1 
ATOM   5421 N  N   . LYS E  1 129 ? 0.249   -9.082  83.280  1.00 29.44  ? 378  LYS E N   1 
ATOM   5422 C  CA  . LYS E  1 129 ? -0.587  -9.710  82.317  1.00 28.73  ? 378  LYS E CA  1 
ATOM   5423 C  C   . LYS E  1 129 ? -1.553  -10.673 82.970  1.00 31.61  ? 378  LYS E C   1 
ATOM   5424 O  O   . LYS E  1 129 ? -1.205  -11.376 83.918  1.00 25.62  ? 378  LYS E O   1 
ATOM   5425 C  CB  . LYS E  1 129 ? 0.297   -10.425 81.313  1.00 28.01  ? 378  LYS E CB  1 
ATOM   5426 C  CG  . LYS E  1 129 ? -0.324  -11.543 80.531  1.00 29.93  ? 378  LYS E CG  1 
ATOM   5427 C  CD  . LYS E  1 129 ? 0.673   -11.977 79.464  1.00 28.71  ? 378  LYS E CD  1 
ATOM   5428 C  CE  . LYS E  1 129 ? 0.272   -13.240 78.767  1.00 31.67  ? 378  LYS E CE  1 
ATOM   5429 N  NZ  . LYS E  1 129 ? 1.397   -13.854 77.967  1.00 32.30  ? 378  LYS E NZ  1 
ATOM   5430 N  N   . LYS E  1 130 ? -2.771  -10.720 82.429  1.00 32.93  ? 379  LYS E N   1 
ATOM   5431 C  CA  . LYS E  1 130 ? -3.655  -11.826 82.722  1.00 35.19  ? 379  LYS E CA  1 
ATOM   5432 C  C   . LYS E  1 130 ? -4.614  -12.113 81.596  1.00 34.05  ? 379  LYS E C   1 
ATOM   5433 O  O   . LYS E  1 130 ? -4.762  -11.322 80.667  1.00 30.92  ? 379  LYS E O   1 
ATOM   5434 C  CB  . LYS E  1 130 ? -4.421  -11.596 84.007  1.00 36.16  ? 379  LYS E CB  1 
ATOM   5435 C  CG  . LYS E  1 130 ? -5.669  -10.745 83.905  1.00 37.48  ? 379  LYS E CG  1 
ATOM   5436 C  CD  . LYS E  1 130 ? -6.031  -10.350 85.331  1.00 38.39  ? 379  LYS E CD  1 
ATOM   5437 C  CE  . LYS E  1 130 ? -7.218  -9.445  85.385  1.00 40.62  ? 379  LYS E CE  1 
ATOM   5438 N  NZ  . LYS E  1 130 ? -7.579  -9.281  86.818  1.00 41.59  ? 379  LYS E NZ  1 
ATOM   5439 N  N   . SER E  1 131 ? -5.236  -13.288 81.693  1.00 37.88  ? 380  SER E N   1 
ATOM   5440 C  CA  . SER E  1 131 ? -6.238  -13.742 80.706  1.00 38.30  ? 380  SER E CA  1 
ATOM   5441 C  C   . SER E  1 131 ? -7.397  -12.774 80.638  1.00 34.32  ? 380  SER E C   1 
ATOM   5442 O  O   . SER E  1 131 ? -7.852  -12.298 81.656  1.00 31.46  ? 380  SER E O   1 
ATOM   5443 C  CB  . SER E  1 131 ? -6.794  -15.120 81.079  1.00 37.97  ? 380  SER E CB  1 
ATOM   5444 O  OG  . SER E  1 131 ? -5.939  -16.124 80.582  1.00 41.74  ? 380  SER E OG  1 
ATOM   5445 N  N   . ALA E  1 132 ? -7.843  -12.483 79.430  1.00 37.17  ? 381  ALA E N   1 
ATOM   5446 C  CA  . ALA E  1 132 ? -9.119  -11.775 79.221  1.00 39.73  ? 381  ALA E CA  1 
ATOM   5447 C  C   . ALA E  1 132 ? -10.270 -12.619 79.742  1.00 38.11  ? 381  ALA E C   1 
ATOM   5448 O  O   . ALA E  1 132 ? -10.253 -13.842 79.662  1.00 35.89  ? 381  ALA E O   1 
ATOM   5449 C  CB  . ALA E  1 132 ? -9.336  -11.484 77.755  1.00 37.19  ? 381  ALA E CB  1 
ATOM   5450 N  N   . ALA E  1 133 ? -11.258 -11.951 80.302  1.00 40.54  ? 382  ALA E N   1 
ATOM   5451 C  CA  . ALA E  1 133 ? -12.440 -12.622 80.786  1.00 43.54  ? 382  ALA E CA  1 
ATOM   5452 C  C   . ALA E  1 133 ? -13.300 -13.020 79.591  1.00 46.23  ? 382  ALA E C   1 
ATOM   5453 O  O   . ALA E  1 133 ? -13.189 -12.423 78.528  1.00 50.20  ? 382  ALA E O   1 
ATOM   5454 C  CB  . ALA E  1 133 ? -13.201 -11.720 81.737  1.00 40.48  ? 382  ALA E CB  1 
ATOM   5455 N  N   . SER E  1 134 ? -14.122 -14.052 79.767  1.00 51.44  ? 383  SER E N   1 
ATOM   5456 C  CA  . SER E  1 134 ? -15.034 -14.518 78.722  1.00 56.90  ? 383  SER E CA  1 
ATOM   5457 C  C   . SER E  1 134 ? -16.368 -13.844 78.889  1.00 52.37  ? 383  SER E C   1 
ATOM   5458 O  O   . SER E  1 134 ? -17.090 -14.160 79.824  1.00 47.21  ? 383  SER E O   1 
ATOM   5459 C  CB  . SER E  1 134 ? -15.231 -16.020 78.832  1.00 59.39  ? 383  SER E CB  1 
ATOM   5460 O  OG  . SER E  1 134 ? -13.979 -16.662 78.722  1.00 66.86  ? 383  SER E OG  1 
ATOM   5461 N  N   . CYS E  1 135 ? -16.687 -12.919 77.990  1.00 51.39  ? 384  CYS E N   1 
ATOM   5462 C  CA  . CYS E  1 135 ? -17.946 -12.179 78.071  1.00 58.20  ? 384  CYS E CA  1 
ATOM   5463 C  C   . CYS E  1 135 ? -19.030 -12.674 77.073  1.00 66.53  ? 384  CYS E C   1 
ATOM   5464 O  O   . CYS E  1 135 ? -18.982 -12.411 75.855  1.00 79.34  ? 384  CYS E O   1 
ATOM   5465 C  CB  . CYS E  1 135 ? -17.688 -10.676 77.901  1.00 57.09  ? 384  CYS E CB  1 
ATOM   5466 S  SG  . CYS E  1 135 ? -16.663 -9.867  79.172  1.00 56.41  ? 384  CYS E SG  1 
ATOM   5467 N  N   . CYS F  1 4   ? 44.250  15.922  105.186 1.00 65.17  ? 253  CYS F N   1 
ATOM   5468 C  CA  . CYS F  1 4   ? 43.253  16.848  104.577 1.00 65.29  ? 253  CYS F CA  1 
ATOM   5469 C  C   . CYS F  1 4   ? 42.757  16.333  103.211 1.00 63.96  ? 253  CYS F C   1 
ATOM   5470 O  O   . CYS F  1 4   ? 43.539  16.204  102.272 1.00 68.92  ? 253  CYS F O   1 
ATOM   5471 C  CB  . CYS F  1 4   ? 43.877  18.232  104.380 1.00 66.81  ? 253  CYS F CB  1 
ATOM   5472 S  SG  . CYS F  1 4   ? 42.701  19.526  103.901 1.00 78.65  ? 253  CYS F SG  1 
ATOM   5473 N  N   . HIS F  1 5   ? 41.461  16.079  103.083 1.00 55.44  ? 254  HIS F N   1 
ATOM   5474 C  CA  . HIS F  1 5   ? 40.898  15.720  101.775 1.00 51.53  ? 254  HIS F CA  1 
ATOM   5475 C  C   . HIS F  1 5   ? 40.005  16.815  101.214 1.00 47.66  ? 254  HIS F C   1 
ATOM   5476 O  O   . HIS F  1 5   ? 39.226  17.403  101.944 1.00 47.19  ? 254  HIS F O   1 
ATOM   5477 C  CB  . HIS F  1 5   ? 40.130  14.438  101.904 1.00 46.81  ? 254  HIS F CB  1 
ATOM   5478 C  CG  . HIS F  1 5   ? 40.932  13.333  102.497 1.00 44.07  ? 254  HIS F CG  1 
ATOM   5479 N  ND1 . HIS F  1 5   ? 41.889  12.649  101.783 1.00 42.14  ? 254  HIS F ND1 1 
ATOM   5480 C  CD2 . HIS F  1 5   ? 40.939  12.806  103.745 1.00 42.92  ? 254  HIS F CD2 1 
ATOM   5481 C  CE1 . HIS F  1 5   ? 42.430  11.724  102.557 1.00 43.87  ? 254  HIS F CE1 1 
ATOM   5482 N  NE2 . HIS F  1 5   ? 41.867  11.795  103.751 1.00 44.71  ? 254  HIS F NE2 1 
ATOM   5483 N  N   . PRO F  1 6   ? 40.135  17.113  99.914  1.00 45.40  ? 255  PRO F N   1 
ATOM   5484 C  CA  . PRO F  1 6   ? 39.215  18.116  99.382  1.00 45.42  ? 255  PRO F CA  1 
ATOM   5485 C  C   . PRO F  1 6   ? 37.733  17.669  99.484  1.00 46.41  ? 255  PRO F C   1 
ATOM   5486 O  O   . PRO F  1 6   ? 36.880  18.504  99.814  1.00 44.44  ? 255  PRO F O   1 
ATOM   5487 C  CB  . PRO F  1 6   ? 39.683  18.313  97.920  1.00 45.79  ? 255  PRO F CB  1 
ATOM   5488 C  CG  . PRO F  1 6   ? 40.491  17.107  97.588  1.00 46.47  ? 255  PRO F CG  1 
ATOM   5489 C  CD  . PRO F  1 6   ? 41.043  16.564  98.884  1.00 44.76  ? 255  PRO F CD  1 
ATOM   5490 N  N   . CYS F  1 7   ? 37.455  16.377  99.271  1.00 42.49  ? 256  CYS F N   1 
ATOM   5491 C  CA  . CYS F  1 7   ? 36.079  15.864  99.341  1.00 44.84  ? 256  CYS F CA  1 
ATOM   5492 C  C   . CYS F  1 7   ? 35.914  14.773  100.374 1.00 46.33  ? 256  CYS F C   1 
ATOM   5493 O  O   . CYS F  1 7   ? 36.892  14.122  100.769 1.00 48.61  ? 256  CYS F O   1 
ATOM   5494 C  CB  . CYS F  1 7   ? 35.612  15.323  97.983  1.00 40.75  ? 256  CYS F CB  1 
ATOM   5495 S  SG  . CYS F  1 7   ? 35.707  16.553  96.677  1.00 41.37  ? 256  CYS F SG  1 
ATOM   5496 N  N   . PRO F  1 8   ? 34.661  14.538  100.801 1.00 47.76  ? 257  PRO F N   1 
ATOM   5497 C  CA  . PRO F  1 8   ? 34.383  13.377  101.639 1.00 46.34  ? 257  PRO F CA  1 
ATOM   5498 C  C   . PRO F  1 8   ? 34.664  12.072  100.930 1.00 44.34  ? 257  PRO F C   1 
ATOM   5499 O  O   . PRO F  1 8   ? 34.724  12.013  99.710  1.00 37.97  ? 257  PRO F O   1 
ATOM   5500 C  CB  . PRO F  1 8   ? 32.888  13.488  101.924 1.00 45.31  ? 257  PRO F CB  1 
ATOM   5501 C  CG  . PRO F  1 8   ? 32.591  14.917  101.774 1.00 46.17  ? 257  PRO F CG  1 
ATOM   5502 C  CD  . PRO F  1 8   ? 33.457  15.357  100.623 1.00 48.14  ? 257  PRO F CD  1 
ATOM   5503 N  N   . TRP F  1 9   ? 34.827  11.021  101.713 1.00 44.48  ? 258  TRP F N   1 
ATOM   5504 C  CA  . TRP F  1 9   ? 35.168  9.739   101.143 1.00 48.68  ? 258  TRP F CA  1 
ATOM   5505 C  C   . TRP F  1 9   ? 34.053  9.291   100.181 1.00 47.97  ? 258  TRP F C   1 
ATOM   5506 O  O   . TRP F  1 9   ? 32.885  9.306   100.541 1.00 43.84  ? 258  TRP F O   1 
ATOM   5507 C  CB  . TRP F  1 9   ? 35.366  8.743   102.281 1.00 50.54  ? 258  TRP F CB  1 
ATOM   5508 C  CG  . TRP F  1 9   ? 36.175  7.547   101.962 1.00 50.21  ? 258  TRP F CG  1 
ATOM   5509 C  CD1 . TRP F  1 9   ? 36.399  6.989   100.739 1.00 47.30  ? 258  TRP F CD1 1 
ATOM   5510 C  CD2 . TRP F  1 9   ? 36.800  6.696   102.916 1.00 54.14  ? 258  TRP F CD2 1 
ATOM   5511 N  NE1 . TRP F  1 9   ? 37.151  5.850   100.870 1.00 47.46  ? 258  TRP F NE1 1 
ATOM   5512 C  CE2 . TRP F  1 9   ? 37.412  5.645   102.199 1.00 52.64  ? 258  TRP F CE2 1 
ATOM   5513 C  CE3 . TRP F  1 9   ? 36.904  6.720   104.316 1.00 53.90  ? 258  TRP F CE3 1 
ATOM   5514 C  CZ2 . TRP F  1 9   ? 38.136  4.636   102.830 1.00 53.41  ? 258  TRP F CZ2 1 
ATOM   5515 C  CZ3 . TRP F  1 9   ? 37.610  5.723   104.940 1.00 54.17  ? 258  TRP F CZ3 1 
ATOM   5516 C  CH2 . TRP F  1 9   ? 38.218  4.683   104.195 1.00 56.81  ? 258  TRP F CH2 1 
ATOM   5517 N  N   . GLU F  1 10  ? 34.424  8.905   98.962  1.00 49.38  ? 259  GLU F N   1 
ATOM   5518 C  CA  . GLU F  1 10  ? 33.373  8.379   98.001  1.00 38.66  ? 259  GLU F CA  1 
ATOM   5519 C  C   . GLU F  1 10  ? 32.750  9.437   97.143  1.00 37.90  ? 259  GLU F C   1 
ATOM   5520 O  O   . GLU F  1 10  ? 32.066  9.095   96.213  1.00 39.66  ? 259  GLU F O   1 
ATOM   5521 C  CB  . GLU F  1 10  ? 32.239  7.585   98.672  1.00 40.79  ? 259  GLU F CB  1 
ATOM   5522 C  CG  . GLU F  1 10  ? 32.725  6.441   99.539  1.00 41.75  ? 259  GLU F CG  1 
ATOM   5523 C  CD  . GLU F  1 10  ? 31.713  5.334   99.645  1.00 43.29  ? 259  GLU F CD  1 
ATOM   5524 O  OE1 . GLU F  1 10  ? 30.956  5.133   98.676  1.00 43.21  ? 259  GLU F OE1 1 
ATOM   5525 O  OE2 . GLU F  1 10  ? 31.699  4.645   100.687 1.00 47.40  ? 259  GLU F OE2 1 
ATOM   5526 N  N   . TRP F  1 11  ? 32.899  10.743  97.460  1.00 42.89  ? 260  TRP F N   1 
ATOM   5527 C  CA  . TRP F  1 11  ? 32.526  11.842  96.579  1.00 36.97  ? 260  TRP F CA  1 
ATOM   5528 C  C   . TRP F  1 11  ? 33.614  12.008  95.510  1.00 37.08  ? 260  TRP F C   1 
ATOM   5529 O  O   . TRP F  1 11  ? 34.753  11.689  95.740  1.00 39.31  ? 260  TRP F O   1 
ATOM   5530 C  CB  . TRP F  1 11  ? 32.343  13.134  97.348  1.00 36.08  ? 260  TRP F CB  1 
ATOM   5531 C  CG  . TRP F  1 11  ? 31.203  13.105  98.329  1.00 37.25  ? 260  TRP F CG  1 
ATOM   5532 C  CD1 . TRP F  1 11  ? 31.019  12.215  99.338  1.00 39.25  ? 260  TRP F CD1 1 
ATOM   5533 C  CD2 . TRP F  1 11  ? 30.105  14.032  98.407  1.00 33.69  ? 260  TRP F CD2 1 
ATOM   5534 N  NE1 . TRP F  1 11  ? 29.869  12.518  100.036 1.00 38.39  ? 260  TRP F NE1 1 
ATOM   5535 C  CE2 . TRP F  1 11  ? 29.291  13.624  99.481  1.00 35.98  ? 260  TRP F CE2 1 
ATOM   5536 C  CE3 . TRP F  1 11  ? 29.726  15.140  97.664  1.00 33.52  ? 260  TRP F CE3 1 
ATOM   5537 C  CZ2 . TRP F  1 11  ? 28.136  14.279  99.829  1.00 33.66  ? 260  TRP F CZ2 1 
ATOM   5538 C  CZ3 . TRP F  1 11  ? 28.588  15.801  98.029  1.00 35.25  ? 260  TRP F CZ3 1 
ATOM   5539 C  CH2 . TRP F  1 11  ? 27.802  15.367  99.107  1.00 33.94  ? 260  TRP F CH2 1 
ATOM   5540 N  N   . THR F  1 12  ? 33.256  12.474  94.336  1.00 35.90  ? 261  THR F N   1 
ATOM   5541 C  CA  . THR F  1 12  ? 34.214  12.656  93.262  1.00 37.24  ? 261  THR F CA  1 
ATOM   5542 C  C   . THR F  1 12  ? 34.587  14.126  93.221  1.00 39.61  ? 261  THR F C   1 
ATOM   5543 O  O   . THR F  1 12  ? 33.713  14.996  93.193  1.00 38.40  ? 261  THR F O   1 
ATOM   5544 C  CB  . THR F  1 12  ? 33.586  12.288  91.927  1.00 36.13  ? 261  THR F CB  1 
ATOM   5545 O  OG1 . THR F  1 12  ? 33.139  10.941  91.991  1.00 38.00  ? 261  THR F OG1 1 
ATOM   5546 C  CG2 . THR F  1 12  ? 34.561  12.433  90.770  1.00 39.15  ? 261  THR F CG2 1 
ATOM   5547 N  N   . PHE F  1 13  ? 35.885  14.403  93.227  1.00 42.25  ? 262  PHE F N   1 
ATOM   5548 C  CA  . PHE F  1 13  ? 36.383  15.758  93.042  1.00 41.99  ? 262  PHE F CA  1 
ATOM   5549 C  C   . PHE F  1 13  ? 36.276  16.077  91.553  1.00 43.31  ? 262  PHE F C   1 
ATOM   5550 O  O   . PHE F  1 13  ? 36.720  15.315  90.708  1.00 45.24  ? 262  PHE F O   1 
ATOM   5551 C  CB  . PHE F  1 13  ? 37.829  15.890  93.551  1.00 41.25  ? 262  PHE F CB  1 
ATOM   5552 C  CG  . PHE F  1 13  ? 38.434  17.264  93.329  1.00 43.04  ? 262  PHE F CG  1 
ATOM   5553 C  CD1 . PHE F  1 13  ? 38.314  18.256  94.298  1.00 41.52  ? 262  PHE F CD1 1 
ATOM   5554 C  CD2 . PHE F  1 13  ? 39.128  17.560  92.145  1.00 40.31  ? 262  PHE F CD2 1 
ATOM   5555 C  CE1 . PHE F  1 13  ? 38.860  19.509  94.090  1.00 42.24  ? 262  PHE F CE1 1 
ATOM   5556 C  CE2 . PHE F  1 13  ? 39.666  18.810  91.933  1.00 39.75  ? 262  PHE F CE2 1 
ATOM   5557 C  CZ  . PHE F  1 13  ? 39.532  19.789  92.907  1.00 41.50  ? 262  PHE F CZ  1 
ATOM   5558 N  N   . PHE F  1 14  ? 35.657  17.190  91.218  1.00 41.82  ? 263  PHE F N   1 
ATOM   5559 C  CA  . PHE F  1 14  ? 35.730  17.682  89.847  1.00 39.14  ? 263  PHE F CA  1 
ATOM   5560 C  C   . PHE F  1 14  ? 35.812  19.192  89.903  1.00 44.85  ? 263  PHE F C   1 
ATOM   5561 O  O   . PHE F  1 14  ? 34.925  19.894  90.456  1.00 44.71  ? 263  PHE F O   1 
ATOM   5562 C  CB  . PHE F  1 14  ? 34.563  17.229  88.969  1.00 38.56  ? 263  PHE F CB  1 
ATOM   5563 C  CG  . PHE F  1 14  ? 34.574  17.837  87.583  1.00 37.77  ? 263  PHE F CG  1 
ATOM   5564 C  CD1 . PHE F  1 14  ? 35.317  17.271  86.565  1.00 36.39  ? 263  PHE F CD1 1 
ATOM   5565 C  CD2 . PHE F  1 14  ? 33.834  18.983  87.310  1.00 36.61  ? 263  PHE F CD2 1 
ATOM   5566 C  CE1 . PHE F  1 14  ? 35.317  17.831  85.299  1.00 38.74  ? 263  PHE F CE1 1 
ATOM   5567 C  CE2 . PHE F  1 14  ? 33.860  19.577  86.064  1.00 38.54  ? 263  PHE F CE2 1 
ATOM   5568 C  CZ  . PHE F  1 14  ? 34.593  18.998  85.046  1.00 39.60  ? 263  PHE F CZ  1 
ATOM   5569 N  N   . GLN F  1 15  ? 36.922  19.671  89.352  1.00 45.66  ? 264  GLN F N   1 
ATOM   5570 C  CA  . GLN F  1 15  ? 37.155  21.083  89.116  1.00 41.37  ? 264  GLN F CA  1 
ATOM   5571 C  C   . GLN F  1 15  ? 36.749  21.986  90.247  1.00 36.50  ? 264  GLN F C   1 
ATOM   5572 O  O   . GLN F  1 15  ? 36.098  22.962  90.022  1.00 35.32  ? 264  GLN F O   1 
ATOM   5573 C  CB  . GLN F  1 15  ? 36.441  21.480  87.837  1.00 41.73  ? 264  GLN F CB  1 
ATOM   5574 C  CG  . GLN F  1 15  ? 37.059  20.806  86.618  1.00 43.15  ? 264  GLN F CG  1 
ATOM   5575 C  CD  . GLN F  1 15  ? 36.742  21.533  85.343  1.00 42.93  ? 264  GLN F CD  1 
ATOM   5576 O  OE1 . GLN F  1 15  ? 36.084  22.573  85.358  1.00 47.78  ? 264  GLN F OE1 1 
ATOM   5577 N  NE2 . GLN F  1 15  ? 37.197  20.995  84.228  1.00 47.77  ? 264  GLN F NE2 1 
ATOM   5578 N  N   . GLY F  1 16  ? 37.124  21.628  91.468  1.00 39.51  ? 265  GLY F N   1 
ATOM   5579 C  CA  . GLY F  1 16  ? 36.989  22.505  92.623  1.00 37.98  ? 265  GLY F CA  1 
ATOM   5580 C  C   . GLY F  1 16  ? 35.782  22.224  93.493  1.00 41.84  ? 265  GLY F C   1 
ATOM   5581 O  O   . GLY F  1 16  ? 35.570  22.916  94.514  1.00 39.07  ? 265  GLY F O   1 
ATOM   5582 N  N   . ASN F  1 17  ? 34.975  21.233  93.095  1.00 40.55  ? 266  ASN F N   1 
ATOM   5583 C  CA  . ASN F  1 17  ? 33.812  20.831  93.898  1.00 37.26  ? 266  ASN F CA  1 
ATOM   5584 C  C   . ASN F  1 17  ? 33.751  19.319  94.067  1.00 37.96  ? 266  ASN F C   1 
ATOM   5585 O  O   . ASN F  1 17  ? 34.371  18.555  93.308  1.00 36.92  ? 266  ASN F O   1 
ATOM   5586 C  CB  . ASN F  1 17  ? 32.519  21.318  93.244  1.00 40.52  ? 266  ASN F CB  1 
ATOM   5587 C  CG  . ASN F  1 17  ? 32.470  22.825  93.061  1.00 37.38  ? 266  ASN F CG  1 
ATOM   5588 O  OD1 . ASN F  1 17  ? 32.236  23.547  94.011  1.00 37.69  ? 266  ASN F OD1 1 
ATOM   5589 N  ND2 . ASN F  1 17  ? 32.646  23.291  91.833  1.00 32.32  ? 266  ASN F ND2 1 
ATOM   5590 N  N   . CYS F  1 18  ? 32.957  18.915  95.050  1.00 33.36  ? 267  CYS F N   1 
ATOM   5591 C  CA  . CYS F  1 18  ? 32.718  17.538  95.363  1.00 34.64  ? 267  CYS F CA  1 
ATOM   5592 C  C   . CYS F  1 18  ? 31.315  17.092  94.908  1.00 35.03  ? 267  CYS F C   1 
ATOM   5593 O  O   . CYS F  1 18  ? 30.335  17.789  95.138  1.00 37.79  ? 267  CYS F O   1 
ATOM   5594 C  CB  . CYS F  1 18  ? 32.866  17.427  96.868  1.00 40.28  ? 267  CYS F CB  1 
ATOM   5595 S  SG  . CYS F  1 18  ? 34.494  18.068  97.360  1.00 42.76  ? 267  CYS F SG  1 
ATOM   5596 N  N   . TYR F  1 19  ? 31.237  15.942  94.246  1.00 34.44  ? 268  TYR F N   1 
ATOM   5597 C  CA  . TYR F  1 19  ? 29.998  15.417  93.657  1.00 32.93  ? 268  TYR F CA  1 
ATOM   5598 C  C   . TYR F  1 19  ? 29.717  14.056  94.257  1.00 33.97  ? 268  TYR F C   1 
ATOM   5599 O  O   . TYR F  1 19  ? 30.620  13.246  94.396  1.00 36.54  ? 268  TYR F O   1 
ATOM   5600 C  CB  . TYR F  1 19  ? 30.115  15.272  92.154  1.00 32.43  ? 268  TYR F CB  1 
ATOM   5601 C  CG  . TYR F  1 19  ? 30.302  16.583  91.499  1.00 34.25  ? 268  TYR F CG  1 
ATOM   5602 C  CD1 . TYR F  1 19  ? 31.544  17.187  91.474  1.00 37.49  ? 268  TYR F CD1 1 
ATOM   5603 C  CD2 . TYR F  1 19  ? 29.230  17.271  90.969  1.00 36.05  ? 268  TYR F CD2 1 
ATOM   5604 C  CE1 . TYR F  1 19  ? 31.718  18.441  90.914  1.00 38.62  ? 268  TYR F CE1 1 
ATOM   5605 C  CE2 . TYR F  1 19  ? 29.393  18.515  90.384  1.00 33.94  ? 268  TYR F CE2 1 
ATOM   5606 C  CZ  . TYR F  1 19  ? 30.637  19.105  90.369  1.00 36.35  ? 268  TYR F CZ  1 
ATOM   5607 O  OH  . TYR F  1 19  ? 30.798  20.358  89.827  1.00 31.55  ? 268  TYR F OH  1 
ATOM   5608 N  N   . PHE F  1 20  ? 28.483  13.834  94.665  1.00 32.67  ? 269  PHE F N   1 
ATOM   5609 C  CA  . PHE F  1 20  ? 28.038  12.527  95.137  1.00 32.76  ? 269  PHE F CA  1 
ATOM   5610 C  C   . PHE F  1 20  ? 27.062  11.931  94.116  1.00 30.90  ? 269  PHE F C   1 
ATOM   5611 O  O   . PHE F  1 20  ? 26.019  12.533  93.842  1.00 32.79  ? 269  PHE F O   1 
ATOM   5612 C  CB  . PHE F  1 20  ? 27.361  12.699  96.493  1.00 35.93  ? 269  PHE F CB  1 
ATOM   5613 C  CG  . PHE F  1 20  ? 26.694  11.464  96.987  1.00 38.30  ? 269  PHE F CG  1 
ATOM   5614 C  CD1 . PHE F  1 20  ? 27.423  10.478  97.612  1.00 42.77  ? 269  PHE F CD1 1 
ATOM   5615 C  CD2 . PHE F  1 20  ? 25.343  11.264  96.772  1.00 42.79  ? 269  PHE F CD2 1 
ATOM   5616 C  CE1 . PHE F  1 20  ? 26.810  9.315   98.061  1.00 43.17  ? 269  PHE F CE1 1 
ATOM   5617 C  CE2 . PHE F  1 20  ? 24.723  10.109  97.213  1.00 41.96  ? 269  PHE F CE2 1 
ATOM   5618 C  CZ  . PHE F  1 20  ? 25.461  9.142   97.862  1.00 44.00  ? 269  PHE F CZ  1 
ATOM   5619 N  N   . MET F  1 21  ? 27.421  10.811  93.504  1.00 29.74  ? 270  MET F N   1 
ATOM   5620 C  CA  . MET F  1 21  ? 26.530  10.123  92.570  1.00 33.30  ? 270  MET F CA  1 
ATOM   5621 C  C   . MET F  1 21  ? 25.735  9.104   93.403  1.00 31.98  ? 270  MET F C   1 
ATOM   5622 O  O   . MET F  1 21  ? 26.324  8.280   94.054  1.00 29.87  ? 270  MET F O   1 
ATOM   5623 C  CB  . MET F  1 21  ? 27.282  9.352   91.474  1.00 36.42  ? 270  MET F CB  1 
ATOM   5624 C  CG  . MET F  1 21  ? 28.470  10.013  90.787  1.00 43.13  ? 270  MET F CG  1 
ATOM   5625 S  SD  . MET F  1 21  ? 28.410  11.791  90.725  1.00 52.62  ? 270  MET F SD  1 
ATOM   5626 C  CE  . MET F  1 21  ? 29.887  12.171  89.766  1.00 52.62  ? 270  MET F CE  1 
ATOM   5627 N  N   . SER F  1 22  ? 24.412  9.150   93.385  1.00 29.85  ? 271  SER F N   1 
ATOM   5628 C  CA  . SER F  1 22  ? 23.634  8.205   94.199  1.00 28.42  ? 271  SER F CA  1 
ATOM   5629 C  C   . SER F  1 22  ? 23.711  6.857   93.551  1.00 27.67  ? 271  SER F C   1 
ATOM   5630 O  O   . SER F  1 22  ? 23.941  6.740   92.375  1.00 30.24  ? 271  SER F O   1 
ATOM   5631 C  CB  . SER F  1 22  ? 22.156  8.620   94.309  1.00 27.85  ? 271  SER F CB  1 
ATOM   5632 O  OG  . SER F  1 22  ? 21.483  8.398   93.086  1.00 25.35  ? 271  SER F OG  1 
ATOM   5633 N  N   . ASN F  1 23  ? 23.527  5.839   94.346  1.00 31.78  ? 272  ASN F N   1 
ATOM   5634 C  CA  A ASN F  1 23  ? 23.360  4.505   93.776  0.50 32.03  ? 272  ASN F CA  1 
ATOM   5635 C  CA  B ASN F  1 23  ? 23.396  4.457   93.895  0.50 32.82  ? 272  ASN F CA  1 
ATOM   5636 C  C   . ASN F  1 23  ? 21.956  3.999   94.015  1.00 30.55  ? 272  ASN F C   1 
ATOM   5637 O  O   . ASN F  1 23  ? 21.665  2.852   93.754  1.00 30.40  ? 272  ASN F O   1 
ATOM   5638 C  CB  A ASN F  1 23  ? 24.448  3.541   94.252  0.50 33.12  ? 272  ASN F CB  1 
ATOM   5639 C  CB  B ASN F  1 23  ? 24.288  3.540   94.735  0.50 35.14  ? 272  ASN F CB  1 
ATOM   5640 C  CG  A ASN F  1 23  ? 25.777  3.801   93.557  0.50 34.83  ? 272  ASN F CG  1 
ATOM   5641 C  CG  B ASN F  1 23  ? 24.090  3.746   96.221  0.50 38.17  ? 272  ASN F CG  1 
ATOM   5642 O  OD1 A ASN F  1 23  ? 25.850  3.899   92.320  0.50 32.81  ? 272  ASN F OD1 1 
ATOM   5643 O  OD1 B ASN F  1 23  ? 23.019  3.455   96.759  0.50 39.71  ? 272  ASN F OD1 1 
ATOM   5644 N  ND2 A ASN F  1 23  ? 26.833  3.945   94.352  0.50 37.23  ? 272  ASN F ND2 1 
ATOM   5645 N  ND2 B ASN F  1 23  ? 25.114  4.294   96.887  0.50 40.90  ? 272  ASN F ND2 1 
ATOM   5646 N  N   . SER F  1 24  ? 21.063  4.895   94.431  1.00 29.74  ? 273  SER F N   1 
ATOM   5647 C  CA  . SER F  1 24  ? 19.634  4.569   94.455  1.00 29.90  ? 273  SER F CA  1 
ATOM   5648 C  C   . SER F  1 24  ? 18.802  5.713   93.826  1.00 29.05  ? 273  SER F C   1 
ATOM   5649 O  O   . SER F  1 24  ? 19.343  6.727   93.373  1.00 29.07  ? 273  SER F O   1 
ATOM   5650 C  CB  . SER F  1 24  ? 19.175  4.216   95.887  1.00 29.56  ? 273  SER F CB  1 
ATOM   5651 O  OG  . SER F  1 24  ? 19.166  5.376   96.683  1.00 30.77  ? 273  SER F OG  1 
ATOM   5652 N  N   . GLN F  1 25  ? 17.493  5.516   93.751  1.00 27.59  ? 274  GLN F N   1 
ATOM   5653 C  CA  . GLN F  1 25  ? 16.589  6.417   93.002  1.00 25.62  ? 274  GLN F CA  1 
ATOM   5654 C  C   . GLN F  1 25  ? 15.604  7.103   93.941  1.00 25.24  ? 274  GLN F C   1 
ATOM   5655 O  O   . GLN F  1 25  ? 15.094  6.506   94.843  1.00 25.22  ? 274  GLN F O   1 
ATOM   5656 C  CB  . GLN F  1 25  ? 15.836  5.620   91.961  1.00 24.61  ? 274  GLN F CB  1 
ATOM   5657 C  CG  . GLN F  1 25  ? 16.693  5.044   90.833  1.00 24.84  ? 274  GLN F CG  1 
ATOM   5658 C  CD  . GLN F  1 25  ? 16.136  3.724   90.325  1.00 27.28  ? 274  GLN F CD  1 
ATOM   5659 O  OE1 . GLN F  1 25  ? 16.130  2.722   91.055  1.00 29.02  ? 274  GLN F OE1 1 
ATOM   5660 N  NE2 . GLN F  1 25  ? 15.616  3.727   89.095  1.00 27.04  ? 274  GLN F NE2 1 
ATOM   5661 N  N   . ARG F  1 26  ? 15.332  8.361   93.720  1.00 25.39  ? 275  ARG F N   1 
ATOM   5662 C  CA  . ARG F  1 26  ? 14.348  9.069   94.510  1.00 27.43  ? 275  ARG F CA  1 
ATOM   5663 C  C   . ARG F  1 26  ? 13.615  10.054  93.614  1.00 27.37  ? 275  ARG F C   1 
ATOM   5664 O  O   . ARG F  1 26  ? 14.075  10.364  92.490  1.00 27.11  ? 275  ARG F O   1 
ATOM   5665 C  CB  . ARG F  1 26  ? 15.041  9.823   95.676  1.00 32.82  ? 275  ARG F CB  1 
ATOM   5666 C  CG  . ARG F  1 26  ? 15.561  8.928   96.802  1.00 35.04  ? 275  ARG F CG  1 
ATOM   5667 C  CD  . ARG F  1 26  ? 16.453  9.714   97.737  1.00 41.00  ? 275  ARG F CD  1 
ATOM   5668 N  NE  . ARG F  1 26  ? 16.618  9.053   99.034  1.00 45.28  ? 275  ARG F NE  1 
ATOM   5669 C  CZ  . ARG F  1 26  ? 16.336  9.631   100.203 1.00 45.52  ? 275  ARG F CZ  1 
ATOM   5670 N  NH1 . ARG F  1 26  ? 15.887  10.896  100.272 1.00 45.00  ? 275  ARG F NH1 1 
ATOM   5671 N  NH2 . ARG F  1 26  ? 16.483  8.943   101.315 1.00 48.00  ? 275  ARG F NH2 1 
ATOM   5672 N  N   . ASN F  1 27  ? 12.492  10.586  94.094  1.00 24.71  ? 276  ASN F N   1 
ATOM   5673 C  CA  . ASN F  1 27  ? 11.805  11.614  93.323  1.00 24.56  ? 276  ASN F CA  1 
ATOM   5674 C  C   . ASN F  1 27  ? 12.603  12.894  93.461  1.00 23.57  ? 276  ASN F C   1 
ATOM   5675 O  O   . ASN F  1 27  ? 13.608  12.949  94.183  1.00 25.96  ? 276  ASN F O   1 
ATOM   5676 C  CB  . ASN F  1 27  ? 10.301  11.739  93.670  1.00 23.01  ? 276  ASN F CB  1 
ATOM   5677 C  CG  . ASN F  1 27  ? 10.050  12.198  95.101  1.00 23.79  ? 276  ASN F CG  1 
ATOM   5678 O  OD1 . ASN F  1 27  ? 10.629  13.156  95.548  1.00 23.86  ? 276  ASN F OD1 1 
ATOM   5679 N  ND2 . ASN F  1 27  ? 9.156   11.514  95.803  1.00 23.76  ? 276  ASN F ND2 1 
ATOM   5680 N  N   . TRP F  1 28  ? 12.222  13.924  92.738  1.00 23.88  ? 277  TRP F N   1 
ATOM   5681 C  CA  . TRP F  1 28  ? 13.056  15.124  92.718  1.00 25.94  ? 277  TRP F CA  1 
ATOM   5682 C  C   . TRP F  1 28  ? 13.132  15.852  94.072  1.00 26.61  ? 277  TRP F C   1 
ATOM   5683 O  O   . TRP F  1 28  ? 14.200  16.299  94.489  1.00 25.45  ? 277  TRP F O   1 
ATOM   5684 C  CB  . TRP F  1 28  ? 12.520  16.065  91.676  1.00 26.22  ? 277  TRP F CB  1 
ATOM   5685 C  CG  . TRP F  1 28  ? 13.359  17.246  91.353  1.00 24.44  ? 277  TRP F CG  1 
ATOM   5686 C  CD1 . TRP F  1 28  ? 14.391  17.278  90.487  1.00 24.83  ? 277  TRP F CD1 1 
ATOM   5687 C  CD2 . TRP F  1 28  ? 13.202  18.582  91.862  1.00 22.45  ? 277  TRP F CD2 1 
ATOM   5688 N  NE1 . TRP F  1 28  ? 14.867  18.553  90.382  1.00 26.54  ? 277  TRP F NE1 1 
ATOM   5689 C  CE2 . TRP F  1 28  ? 14.160  19.372  91.230  1.00 24.87  ? 277  TRP F CE2 1 
ATOM   5690 C  CE3 . TRP F  1 28  ? 12.297  19.183  92.719  1.00 22.58  ? 277  TRP F CE3 1 
ATOM   5691 C  CZ2 . TRP F  1 28  ? 14.284  20.745  91.458  1.00 24.89  ? 277  TRP F CZ2 1 
ATOM   5692 C  CZ3 . TRP F  1 28  ? 12.412  20.549  92.963  1.00 25.76  ? 277  TRP F CZ3 1 
ATOM   5693 C  CH2 . TRP F  1 28  ? 13.397  21.323  92.317  1.00 24.91  ? 277  TRP F CH2 1 
ATOM   5694 N  N   . HIS F  1 29  ? 12.010  15.958  94.762  1.00 26.45  ? 278  HIS F N   1 
ATOM   5695 C  CA  A HIS F  1 29  ? 12.015  16.610  96.071  0.50 28.06  ? 278  HIS F CA  1 
ATOM   5696 C  CA  B HIS F  1 29  ? 11.965  16.605  96.076  0.50 26.71  ? 278  HIS F CA  1 
ATOM   5697 C  C   . HIS F  1 29  ? 12.756  15.803  97.131  1.00 27.84  ? 278  HIS F C   1 
ATOM   5698 O  O   . HIS F  1 29  ? 13.531  16.359  97.909  1.00 28.59  ? 278  HIS F O   1 
ATOM   5699 C  CB  A HIS F  1 29  ? 10.608  16.953  96.517  0.50 28.38  ? 278  HIS F CB  1 
ATOM   5700 C  CB  B HIS F  1 29  ? 10.509  16.802  96.509  0.50 25.43  ? 278  HIS F CB  1 
ATOM   5701 C  CG  A HIS F  1 29  ? 10.055  18.146  95.812  0.50 29.98  ? 278  HIS F CG  1 
ATOM   5702 C  CG  B HIS F  1 29  ? 9.618   17.306  95.412  0.50 24.42  ? 278  HIS F CG  1 
ATOM   5703 N  ND1 A HIS F  1 29  ? 10.485  19.433  96.078  0.50 30.29  ? 278  HIS F ND1 1 
ATOM   5704 N  ND1 B HIS F  1 29  ? 8.797   16.476  94.686  0.50 24.95  ? 278  HIS F ND1 1 
ATOM   5705 C  CD2 A HIS F  1 29  ? 9.130   18.248  94.828  0.50 29.66  ? 278  HIS F CD2 1 
ATOM   5706 C  CD2 B HIS F  1 29  ? 9.453   18.546  94.889  0.50 25.26  ? 278  HIS F CD2 1 
ATOM   5707 C  CE1 A HIS F  1 29  ? 9.846   20.273  95.284  0.50 29.71  ? 278  HIS F CE1 1 
ATOM   5708 C  CE1 B HIS F  1 29  ? 8.156   17.181  93.769  0.50 24.81  ? 278  HIS F CE1 1 
ATOM   5709 N  NE2 A HIS F  1 29  ? 9.019   19.581  94.518  0.50 29.05  ? 278  HIS F NE2 1 
ATOM   5710 N  NE2 B HIS F  1 29  ? 8.539   18.440  93.869  0.50 24.96  ? 278  HIS F NE2 1 
ATOM   5711 N  N   . ASP F  1 30  ? 12.573  14.486  97.157  1.00 29.01  ? 279  ASP F N   1 
ATOM   5712 C  CA  . ASP F  1 30  ? 13.342  13.672  98.092  1.00 29.55  ? 279  ASP F CA  1 
ATOM   5713 C  C   . ASP F  1 30  ? 14.866  13.766  97.827  1.00 28.88  ? 279  ASP F C   1 
ATOM   5714 O  O   . ASP F  1 30  ? 15.663  13.570  98.744  1.00 31.80  ? 279  ASP F O   1 
ATOM   5715 C  CB  . ASP F  1 30  ? 12.891  12.205  98.021  1.00 31.97  ? 279  ASP F CB  1 
ATOM   5716 C  CG  . ASP F  1 30  ? 11.531  11.980  98.686  1.00 36.47  ? 279  ASP F CG  1 
ATOM   5717 O  OD1 . ASP F  1 30  ? 11.061  12.897  99.385  1.00 36.07  ? 279  ASP F OD1 1 
ATOM   5718 O  OD2 . ASP F  1 30  ? 10.933  10.890  98.505  1.00 38.63  ? 279  ASP F OD2 1 
ATOM   5719 N  N   . SER F  1 31  ? 15.253  13.990  96.565  1.00 27.32  ? 280  SER F N   1 
ATOM   5720 C  CA  . SER F  1 31  ? 16.658  14.086  96.169  1.00 27.71  ? 280  SER F CA  1 
ATOM   5721 C  C   . SER F  1 31  ? 17.249  15.339  96.750  1.00 28.94  ? 280  SER F C   1 
ATOM   5722 O  O   . SER F  1 31  ? 18.327  15.304  97.336  1.00 28.53  ? 280  SER F O   1 
ATOM   5723 C  CB  . SER F  1 31  ? 16.828  14.073  94.642  1.00 25.44  ? 280  SER F CB  1 
ATOM   5724 O  OG  . SER F  1 31  ? 16.487  12.794  94.163  1.00 24.66  ? 280  SER F OG  1 
ATOM   5725 N  N   . ILE F  1 32  ? 16.522  16.444  96.604  1.00 27.53  ? 281  ILE F N   1 
ATOM   5726 C  CA  . ILE F  1 32  ? 16.868  17.669  97.277  1.00 27.87  ? 281  ILE F CA  1 
ATOM   5727 C  C   . ILE F  1 32  ? 17.127  17.391  98.758  1.00 28.06  ? 281  ILE F C   1 
ATOM   5728 O  O   . ILE F  1 32  ? 18.137  17.813  99.311  1.00 27.01  ? 281  ILE F O   1 
ATOM   5729 C  CB  . ILE F  1 32  ? 15.774  18.742  97.087  1.00 28.66  ? 281  ILE F CB  1 
ATOM   5730 C  CG1 . ILE F  1 32  ? 15.778  19.185  95.630  1.00 29.09  ? 281  ILE F CG1 1 
ATOM   5731 C  CG2 . ILE F  1 32  ? 16.011  19.947  97.985  1.00 27.31  ? 281  ILE F CG2 1 
ATOM   5732 C  CD1 . ILE F  1 32  ? 14.737  20.215  95.320  1.00 28.93  ? 281  ILE F CD1 1 
ATOM   5733 N  N   . THR F  1 33  ? 16.245  16.628  99.385  1.00 27.98  ? 282  THR F N   1 
ATOM   5734 C  CA  . THR F  1 33  ? 16.372  16.382  100.819 1.00 29.16  ? 282  THR F CA  1 
ATOM   5735 C  C   . THR F  1 33  ? 17.616  15.542  101.112 1.00 30.61  ? 282  THR F C   1 
ATOM   5736 O  O   . THR F  1 33  ? 18.376  15.851  102.027 1.00 27.57  ? 282  THR F O   1 
ATOM   5737 C  CB  . THR F  1 33  ? 15.112  15.714  101.373 1.00 30.23  ? 282  THR F CB  1 
ATOM   5738 O  OG1 . THR F  1 33  ? 14.023  16.605  101.178 1.00 33.77  ? 282  THR F OG1 1 
ATOM   5739 C  CG2 . THR F  1 33  ? 15.235  15.422  102.868 1.00 31.02  ? 282  THR F CG2 1 
ATOM   5740 N  N   . ALA F  1 34  ? 17.827  14.501  100.316 1.00 30.98  ? 283  ALA F N   1 
ATOM   5741 C  CA  . ALA F  1 34  ? 18.981  13.626  100.537 1.00 31.45  ? 283  ALA F CA  1 
ATOM   5742 C  C   . ALA F  1 34  ? 20.245  14.475  100.466 1.00 28.75  ? 283  ALA F C   1 
ATOM   5743 O  O   . ALA F  1 34  ? 21.134  14.322  101.274 1.00 29.96  ? 283  ALA F O   1 
ATOM   5744 C  CB  . ALA F  1 34  ? 19.024  12.480  99.507  1.00 29.70  ? 283  ALA F CB  1 
ATOM   5745 N  N   . CYS F  1 35  ? 20.311  15.359  99.486  1.00 31.38  ? 284  CYS F N   1 
ATOM   5746 C  CA  . CYS F  1 35  ? 21.480  16.200  99.301  1.00 32.73  ? 284  CYS F CA  1 
ATOM   5747 C  C   . CYS F  1 35  ? 21.691  17.150  100.501 1.00 35.75  ? 284  CYS F C   1 
ATOM   5748 O  O   . CYS F  1 35  ? 22.809  17.304  100.999 1.00 32.04  ? 284  CYS F O   1 
ATOM   5749 C  CB  . CYS F  1 35  ? 21.345  16.965  97.995  1.00 31.37  ? 284  CYS F CB  1 
ATOM   5750 S  SG  . CYS F  1 35  ? 21.642  15.971  96.530  1.00 29.65  ? 284  CYS F SG  1 
ATOM   5751 N  N   . LYS F  1 36  ? 20.613  17.758  100.990 1.00 35.44  ? 285  LYS F N   1 
ATOM   5752 C  CA  . LYS F  1 36  ? 20.725  18.621  102.156 1.00 36.59  ? 285  LYS F CA  1 
ATOM   5753 C  C   . LYS F  1 36  ? 21.307  17.904  103.357 1.00 36.38  ? 285  LYS F C   1 
ATOM   5754 O  O   . LYS F  1 36  ? 22.054  18.481  104.118 1.00 37.63  ? 285  LYS F O   1 
ATOM   5755 C  CB  . LYS F  1 36  ? 19.378  19.138  102.589 1.00 40.21  ? 285  LYS F CB  1 
ATOM   5756 C  CG  . LYS F  1 36  ? 18.886  20.342  101.841 1.00 45.15  ? 285  LYS F CG  1 
ATOM   5757 C  CD  . LYS F  1 36  ? 17.522  20.786  102.393 1.00 51.39  ? 285  LYS F CD  1 
ATOM   5758 C  CE  . LYS F  1 36  ? 17.374  20.684  103.923 1.00 52.08  ? 285  LYS F CE  1 
ATOM   5759 N  NZ  . LYS F  1 36  ? 16.104  21.307  104.445 1.00 57.52  ? 285  LYS F NZ  1 
ATOM   5760 N  N   . GLU F  1 37  ? 20.944  16.644  103.534 1.00 40.40  ? 286  GLU F N   1 
ATOM   5761 C  CA  . GLU F  1 37  ? 21.357  15.877  104.701 1.00 41.16  ? 286  GLU F CA  1 
ATOM   5762 C  C   . GLU F  1 37  ? 22.840  15.477  104.723 1.00 40.07  ? 286  GLU F C   1 
ATOM   5763 O  O   . GLU F  1 37  ? 23.313  14.992  105.727 1.00 39.96  ? 286  GLU F O   1 
ATOM   5764 C  CB  . GLU F  1 37  ? 20.481  14.629  104.827 1.00 41.90  ? 286  GLU F CB  1 
ATOM   5765 C  CG  . GLU F  1 37  ? 19.038  14.946  105.188 1.00 45.33  ? 286  GLU F CG  1 
ATOM   5766 C  CD  . GLU F  1 37  ? 18.120  13.738  105.155 1.00 47.21  ? 286  GLU F CD  1 
ATOM   5767 O  OE1 . GLU F  1 37  ? 18.442  12.759  104.427 1.00 49.31  ? 286  GLU F OE1 1 
ATOM   5768 O  OE2 . GLU F  1 37  ? 17.062  13.787  105.845 1.00 45.52  ? 286  GLU F OE2 1 
ATOM   5769 N  N   . VAL F  1 38  ? 23.551  15.645  103.612 1.00 36.19  ? 287  VAL F N   1 
ATOM   5770 C  CA  . VAL F  1 38  ? 25.010  15.505  103.588 1.00 35.22  ? 287  VAL F CA  1 
ATOM   5771 C  C   . VAL F  1 38  ? 25.621  16.871  103.267 1.00 36.12  ? 287  VAL F C   1 
ATOM   5772 O  O   . VAL F  1 38  ? 26.669  16.977  102.651 1.00 41.18  ? 287  VAL F O   1 
ATOM   5773 C  CB  . VAL F  1 38  ? 25.469  14.426  102.589 1.00 33.96  ? 287  VAL F CB  1 
ATOM   5774 C  CG1 . VAL F  1 38  ? 24.920  13.078  103.008 1.00 36.56  ? 287  VAL F CG1 1 
ATOM   5775 C  CG2 . VAL F  1 38  ? 24.994  14.715  101.193 1.00 34.16  ? 287  VAL F CG2 1 
ATOM   5776 N  N   . GLY F  1 39  ? 24.921  17.922  103.655 1.00 37.50  ? 288  GLY F N   1 
ATOM   5777 C  CA  . GLY F  1 39  ? 25.399  19.288  103.476 1.00 38.91  ? 288  GLY F CA  1 
ATOM   5778 C  C   . GLY F  1 39  ? 25.663  19.726  102.057 1.00 40.87  ? 288  GLY F C   1 
ATOM   5779 O  O   . GLY F  1 39  ? 26.532  20.558  101.824 1.00 42.65  ? 288  GLY F O   1 
ATOM   5780 N  N   . ALA F  1 40  ? 24.885  19.203  101.108 1.00 39.52  ? 289  ALA F N   1 
ATOM   5781 C  CA  . ALA F  1 40  ? 25.067  19.545  99.713  1.00 35.52  ? 289  ALA F CA  1 
ATOM   5782 C  C   . ALA F  1 40  ? 23.753  20.036  99.114  1.00 35.08  ? 289  ALA F C   1 
ATOM   5783 O  O   . ALA F  1 40  ? 22.748  20.130  99.781  1.00 35.07  ? 289  ALA F O   1 
ATOM   5784 C  CB  . ALA F  1 40  ? 25.618  18.346  98.962  1.00 34.34  ? 289  ALA F CB  1 
ATOM   5785 N  N   . GLN F  1 41  ? 23.815  20.360  97.847  1.00 35.41  ? 290  GLN F N   1 
ATOM   5786 C  CA  . GLN F  1 41  ? 22.706  20.799  97.047  1.00 34.96  ? 290  GLN F CA  1 
ATOM   5787 C  C   . GLN F  1 41  ? 22.525  19.868  95.849  1.00 34.00  ? 290  GLN F C   1 
ATOM   5788 O  O   . GLN F  1 41  ? 23.507  19.453  95.259  1.00 32.00  ? 290  GLN F O   1 
ATOM   5789 C  CB  . GLN F  1 41  ? 23.099  22.130  96.497  1.00 37.83  ? 290  GLN F CB  1 
ATOM   5790 C  CG  . GLN F  1 41  ? 22.002  22.891  95.843  1.00 39.17  ? 290  GLN F CG  1 
ATOM   5791 C  CD  . GLN F  1 41  ? 22.350  24.370  95.759  1.00 41.31  ? 290  GLN F CD  1 
ATOM   5792 O  OE1 . GLN F  1 41  ? 23.357  24.765  95.110  1.00 38.84  ? 290  GLN F OE1 1 
ATOM   5793 N  NE2 . GLN F  1 41  ? 21.509  25.201  96.404  1.00 36.16  ? 290  GLN F NE2 1 
ATOM   5794 N  N   . LEU F  1 42  ? 21.282  19.601  95.442  1.00 27.75  ? 291  LEU F N   1 
ATOM   5795 C  CA  . LEU F  1 42  ? 21.058  18.836  94.242  1.00 27.26  ? 291  LEU F CA  1 
ATOM   5796 C  C   . LEU F  1 42  ? 21.718  19.597  93.108  1.00 27.36  ? 291  LEU F C   1 
ATOM   5797 O  O   . LEU F  1 42  ? 21.593  20.835  93.010  1.00 31.13  ? 291  LEU F O   1 
ATOM   5798 C  CB  . LEU F  1 42  ? 19.553  18.635  94.031  1.00 25.98  ? 291  LEU F CB  1 
ATOM   5799 C  CG  . LEU F  1 42  ? 19.085  17.894  92.787  1.00 26.95  ? 291  LEU F CG  1 
ATOM   5800 C  CD1 . LEU F  1 42  ? 19.526  16.442  92.746  1.00 28.22  ? 291  LEU F CD1 1 
ATOM   5801 C  CD2 . LEU F  1 42  ? 17.566  17.947  92.797  1.00 28.53  ? 291  LEU F CD2 1 
ATOM   5802 N  N   . VAL F  1 43  ? 22.392  18.883  92.225  1.00 26.65  ? 292  VAL F N   1 
ATOM   5803 C  CA  . VAL F  1 43  ? 23.427  19.527  91.401  1.00 27.23  ? 292  VAL F CA  1 
ATOM   5804 C  C   . VAL F  1 43  ? 22.997  20.742  90.570  1.00 28.16  ? 292  VAL F C   1 
ATOM   5805 O  O   . VAL F  1 43  ? 22.078  20.681  89.727  1.00 27.63  ? 292  VAL F O   1 
ATOM   5806 C  CB  . VAL F  1 43  ? 24.203  18.519  90.537  1.00 26.34  ? 292  VAL F CB  1 
ATOM   5807 C  CG1 . VAL F  1 43  ? 23.358  17.925  89.439  1.00 25.53  ? 292  VAL F CG1 1 
ATOM   5808 C  CG2 . VAL F  1 43  ? 25.417  19.215  89.944  1.00 28.09  ? 292  VAL F CG2 1 
ATOM   5809 N  N   . VAL F  1 44  ? 23.677  21.859  90.799  1.00 30.03  ? 293  VAL F N   1 
ATOM   5810 C  CA  . VAL F  1 44  ? 23.470  23.037  89.961  1.00 30.22  ? 293  VAL F CA  1 
ATOM   5811 C  C   . VAL F  1 44  ? 24.663  23.283  89.035  1.00 32.75  ? 293  VAL F C   1 
ATOM   5812 O  O   . VAL F  1 44  ? 25.810  23.384  89.492  1.00 35.51  ? 293  VAL F O   1 
ATOM   5813 C  CB  . VAL F  1 44  ? 23.242  24.272  90.798  1.00 33.24  ? 293  VAL F CB  1 
ATOM   5814 C  CG1 . VAL F  1 44  ? 23.175  25.506  89.887  1.00 33.30  ? 293  VAL F CG1 1 
ATOM   5815 C  CG2 . VAL F  1 44  ? 21.972  24.103  91.637  1.00 35.34  ? 293  VAL F CG2 1 
ATOM   5816 N  N   . ILE F  1 45  ? 24.403  23.371  87.743  1.00 29.99  ? 294  ILE F N   1 
ATOM   5817 C  CA  . ILE F  1 45  ? 25.486  23.438  86.764  1.00 35.35  ? 294  ILE F CA  1 
ATOM   5818 C  C   . ILE F  1 45  ? 25.877  24.901  86.480  1.00 39.68  ? 294  ILE F C   1 
ATOM   5819 O  O   . ILE F  1 45  ? 25.019  25.719  86.166  1.00 42.87  ? 294  ILE F O   1 
ATOM   5820 C  CB  . ILE F  1 45  ? 25.067  22.715  85.478  1.00 34.01  ? 294  ILE F CB  1 
ATOM   5821 C  CG1 . ILE F  1 45  ? 24.744  21.251  85.791  1.00 33.35  ? 294  ILE F CG1 1 
ATOM   5822 C  CG2 . ILE F  1 45  ? 26.175  22.751  84.440  1.00 37.43  ? 294  ILE F CG2 1 
ATOM   5823 C  CD1 . ILE F  1 45  ? 24.196  20.485  84.604  1.00 34.25  ? 294  ILE F CD1 1 
ATOM   5824 N  N   . LYS F  1 46  ? 27.165  25.213  86.608  1.00 41.27  ? 295  LYS F N   1 
ATOM   5825 C  CA  . LYS F  1 46  ? 27.674  26.569  86.411  1.00 41.32  ? 295  LYS F CA  1 
ATOM   5826 C  C   . LYS F  1 46  ? 28.605  26.732  85.194  1.00 43.88  ? 295  LYS F C   1 
ATOM   5827 O  O   . LYS F  1 46  ? 29.067  27.820  84.951  1.00 46.68  ? 295  LYS F O   1 
ATOM   5828 C  CB  . LYS F  1 46  ? 28.446  27.010  87.647  1.00 43.03  ? 295  LYS F CB  1 
ATOM   5829 C  CG  . LYS F  1 46  ? 27.634  27.160  88.909  1.00 40.40  ? 295  LYS F CG  1 
ATOM   5830 C  CD  . LYS F  1 46  ? 26.589  28.259  88.801  1.00 36.72  ? 295  LYS F CD  1 
ATOM   5831 C  CE  . LYS F  1 46  ? 25.967  28.489  90.171  1.00 37.50  ? 295  LYS F CE  1 
ATOM   5832 N  NZ  . LYS F  1 46  ? 24.547  28.907  90.045  1.00 38.73  ? 295  LYS F NZ  1 
ATOM   5833 N  N   . SER F  1 47  ? 28.869  25.680  84.430  1.00 41.31  ? 296  SER F N   1 
ATOM   5834 C  CA  . SER F  1 47  ? 29.755  25.789  83.264  1.00 40.68  ? 296  SER F CA  1 
ATOM   5835 C  C   . SER F  1 47  ? 29.592  24.624  82.291  1.00 41.14  ? 296  SER F C   1 
ATOM   5836 O  O   . SER F  1 47  ? 29.183  23.517  82.685  1.00 38.54  ? 296  SER F O   1 
ATOM   5837 C  CB  . SER F  1 47  ? 31.239  25.848  83.695  1.00 41.65  ? 296  SER F CB  1 
ATOM   5838 O  OG  . SER F  1 47  ? 31.777  24.565  83.967  1.00 41.31  ? 296  SER F OG  1 
ATOM   5839 N  N   . ALA F  1 48  ? 29.939  24.892  81.031  1.00 37.25  ? 297  ALA F N   1 
ATOM   5840 C  CA  . ALA F  1 48  ? 29.931  23.912  79.973  1.00 39.38  ? 297  ALA F CA  1 
ATOM   5841 C  C   . ALA F  1 48  ? 30.724  22.658  80.331  1.00 41.83  ? 297  ALA F C   1 
ATOM   5842 O  O   . ALA F  1 48  ? 30.281  21.537  80.069  1.00 42.70  ? 297  ALA F O   1 
ATOM   5843 C  CB  . ALA F  1 48  ? 30.506  24.536  78.718  1.00 40.94  ? 297  ALA F CB  1 
ATOM   5844 N  N   . GLU F  1 49  ? 31.887  22.873  80.948  1.00 44.81  ? 298  GLU F N   1 
ATOM   5845 C  CA  A GLU F  1 49  ? 32.824  21.808  81.340  0.70 44.94  ? 298  GLU F CA  1 
ATOM   5846 C  CA  B GLU F  1 49  ? 32.795  21.782  81.288  0.30 44.10  ? 298  GLU F CA  1 
ATOM   5847 C  C   . GLU F  1 49  ? 32.136  20.875  82.354  1.00 42.35  ? 298  GLU F C   1 
ATOM   5848 O  O   . GLU F  1 49  ? 32.142  19.649  82.226  1.00 44.45  ? 298  GLU F O   1 
ATOM   5849 C  CB  A GLU F  1 49  ? 34.087  22.382  82.032  0.70 48.83  ? 298  GLU F CB  1 
ATOM   5850 C  CB  B GLU F  1 49  ? 34.161  22.306  81.782  0.30 46.77  ? 298  GLU F CB  1 
ATOM   5851 C  CG  A GLU F  1 49  ? 34.954  23.355  81.237  0.70 51.67  ? 298  GLU F CG  1 
ATOM   5852 C  CG  B GLU F  1 49  ? 34.743  23.531  81.063  0.30 48.89  ? 298  GLU F CG  1 
ATOM   5853 C  CD  A GLU F  1 49  ? 34.212  24.618  80.844  0.70 52.73  ? 298  GLU F CD  1 
ATOM   5854 C  CD  B GLU F  1 49  ? 34.727  23.430  79.540  0.30 50.50  ? 298  GLU F CD  1 
ATOM   5855 O  OE1 A GLU F  1 49  ? 33.900  25.428  81.745  0.70 52.61  ? 298  GLU F OE1 1 
ATOM   5856 O  OE1 B GLU F  1 49  ? 34.034  22.534  79.008  0.30 53.95  ? 298  GLU F OE1 1 
ATOM   5857 O  OE2 A GLU F  1 49  ? 33.923  24.784  79.633  0.70 56.05  ? 298  GLU F OE2 1 
ATOM   5858 O  OE2 B GLU F  1 49  ? 35.405  24.254  78.874  0.30 48.50  ? 298  GLU F OE2 1 
ATOM   5859 N  N   . GLU F  1 50  ? 31.586  21.474  83.396  1.00 36.01  ? 299  GLU F N   1 
ATOM   5860 C  CA  . GLU F  1 50  ? 30.832  20.742  84.394  1.00 36.94  ? 299  GLU F CA  1 
ATOM   5861 C  C   . GLU F  1 50  ? 29.623  19.983  83.772  1.00 35.63  ? 299  GLU F C   1 
ATOM   5862 O  O   . GLU F  1 50  ? 29.338  18.847  84.165  1.00 36.43  ? 299  GLU F O   1 
ATOM   5863 C  CB  . GLU F  1 50  ? 30.382  21.698  85.495  1.00 35.98  ? 299  GLU F CB  1 
ATOM   5864 C  CG  . GLU F  1 50  ? 29.573  21.029  86.579  1.00 37.62  ? 299  GLU F CG  1 
ATOM   5865 C  CD  . GLU F  1 50  ? 29.198  21.985  87.673  1.00 38.13  ? 299  GLU F CD  1 
ATOM   5866 O  OE1 . GLU F  1 50  ? 28.974  21.536  88.813  1.00 38.89  ? 299  GLU F OE1 1 
ATOM   5867 O  OE2 . GLU F  1 50  ? 29.127  23.184  87.398  1.00 38.87  ? 299  GLU F OE2 1 
ATOM   5868 N  N   . GLN F  1 51  ? 28.975  20.560  82.762  1.00 33.14  ? 300  GLN F N   1 
ATOM   5869 C  CA  . GLN F  1 51  ? 27.883  19.867  82.095  1.00 34.66  ? 300  GLN F CA  1 
ATOM   5870 C  C   . GLN F  1 51  ? 28.384  18.621  81.385  1.00 36.58  ? 300  GLN F C   1 
ATOM   5871 O  O   . GLN F  1 51  ? 27.734  17.585  81.426  1.00 30.27  ? 300  GLN F O   1 
ATOM   5872 C  CB  . GLN F  1 51  ? 27.132  20.766  81.110  1.00 33.32  ? 300  GLN F CB  1 
ATOM   5873 C  CG  . GLN F  1 51  ? 26.563  20.015  79.890  1.00 34.82  ? 300  GLN F CG  1 
ATOM   5874 C  CD  . GLN F  1 51  ? 25.354  19.158  80.215  1.00 35.02  ? 300  GLN F CD  1 
ATOM   5875 O  OE1 . GLN F  1 51  ? 24.781  19.255  81.312  1.00 32.33  ? 300  GLN F OE1 1 
ATOM   5876 N  NE2 . GLN F  1 51  ? 24.948  18.329  79.263  1.00 29.01  ? 300  GLN F NE2 1 
ATOM   5877 N  N   . ASN F  1 52  ? 29.521  18.739  80.706  1.00 37.87  ? 301  ASN F N   1 
ATOM   5878 C  CA  . ASN F  1 52  ? 30.101  17.609  79.997  1.00 39.68  ? 301  ASN F CA  1 
ATOM   5879 C  C   . ASN F  1 52  ? 30.424  16.467  80.954  1.00 34.93  ? 301  ASN F C   1 
ATOM   5880 O  O   . ASN F  1 52  ? 30.113  15.316  80.691  1.00 37.04  ? 301  ASN F O   1 
ATOM   5881 C  CB  . ASN F  1 52  ? 31.355  18.039  79.246  1.00 45.98  ? 301  ASN F CB  1 
ATOM   5882 C  CG  . ASN F  1 52  ? 31.042  18.975  78.086  1.00 51.79  ? 301  ASN F CG  1 
ATOM   5883 O  OD1 . ASN F  1 52  ? 29.909  19.027  77.601  1.00 53.58  ? 301  ASN F OD1 1 
ATOM   5884 N  ND2 . ASN F  1 52  ? 32.052  19.718  77.633  1.00 52.99  ? 301  ASN F ND2 1 
ATOM   5885 N  N   . PHE F  1 53  ? 31.048  16.808  82.054  1.00 34.33  ? 302  PHE F N   1 
ATOM   5886 C  CA  . PHE F  1 53  ? 31.312  15.877  83.128  1.00 35.62  ? 302  PHE F CA  1 
ATOM   5887 C  C   . PHE F  1 53  ? 30.038  15.152  83.632  1.00 36.33  ? 302  PHE F C   1 
ATOM   5888 O  O   . PHE F  1 53  ? 29.965  13.928  83.612  1.00 37.06  ? 302  PHE F O   1 
ATOM   5889 C  CB  . PHE F  1 53  ? 31.983  16.647  84.256  1.00 34.70  ? 302  PHE F CB  1 
ATOM   5890 C  CG  . PHE F  1 53  ? 32.079  15.884  85.525  1.00 37.06  ? 302  PHE F CG  1 
ATOM   5891 C  CD1 . PHE F  1 53  ? 32.797  14.690  85.580  1.00 36.57  ? 302  PHE F CD1 1 
ATOM   5892 C  CD2 . PHE F  1 53  ? 31.438  16.347  86.681  1.00 38.44  ? 302  PHE F CD2 1 
ATOM   5893 C  CE1 . PHE F  1 53  ? 32.892  13.967  86.762  1.00 35.72  ? 302  PHE F CE1 1 
ATOM   5894 C  CE2 . PHE F  1 53  ? 31.524  15.628  87.873  1.00 38.64  ? 302  PHE F CE2 1 
ATOM   5895 C  CZ  . PHE F  1 53  ? 32.264  14.442  87.915  1.00 37.52  ? 302  PHE F CZ  1 
ATOM   5896 N  N   . LEU F  1 54  ? 29.040  15.905  84.069  1.00 35.76  ? 303  LEU F N   1 
ATOM   5897 C  CA  . LEU F  1 54  ? 27.801  15.309  84.589  1.00 35.21  ? 303  LEU F CA  1 
ATOM   5898 C  C   . LEU F  1 54  ? 27.024  14.524  83.531  1.00 34.90  ? 303  LEU F C   1 
ATOM   5899 O  O   . LEU F  1 54  ? 26.516  13.425  83.802  1.00 30.84  ? 303  LEU F O   1 
ATOM   5900 C  CB  . LEU F  1 54  ? 26.913  16.377  85.221  1.00 34.05  ? 303  LEU F CB  1 
ATOM   5901 C  CG  . LEU F  1 54  ? 27.567  17.099  86.389  1.00 33.48  ? 303  LEU F CG  1 
ATOM   5902 C  CD1 . LEU F  1 54  ? 26.853  18.402  86.761  1.00 33.61  ? 303  LEU F CD1 1 
ATOM   5903 C  CD2 . LEU F  1 54  ? 27.682  16.178  87.584  1.00 34.73  ? 303  LEU F CD2 1 
ATOM   5904 N  N   . GLN F  1 55  ? 26.961  15.045  82.303  1.00 35.05  ? 304  GLN F N   1 
ATOM   5905 C  CA  . GLN F  1 55  ? 26.245  14.337  81.259  1.00 35.68  ? 304  GLN F CA  1 
ATOM   5906 C  C   . GLN F  1 55  ? 26.909  12.973  81.003  1.00 39.41  ? 304  GLN F C   1 
ATOM   5907 O  O   . GLN F  1 55  ? 26.240  11.991  80.633  1.00 37.04  ? 304  GLN F O   1 
ATOM   5908 C  CB  . GLN F  1 55  ? 26.203  15.136  79.949  1.00 33.42  ? 304  GLN F CB  1 
ATOM   5909 C  CG  . GLN F  1 55  ? 25.251  14.565  78.917  1.00 31.33  ? 304  GLN F CG  1 
ATOM   5910 C  CD  . GLN F  1 55  ? 23.817  14.843  79.282  1.00 31.49  ? 304  GLN F CD  1 
ATOM   5911 O  OE1 . GLN F  1 55  ? 23.471  15.980  79.577  1.00 28.16  ? 304  GLN F OE1 1 
ATOM   5912 N  NE2 . GLN F  1 55  ? 22.967  13.803  79.273  1.00 29.98  ? 304  GLN F NE2 1 
ATOM   5913 N  N   . LEU F  1 56  ? 28.228  12.929  81.176  1.00 37.84  ? 305  LEU F N   1 
ATOM   5914 C  CA  . LEU F  1 56  ? 28.987  11.709  80.896  1.00 37.88  ? 305  LEU F CA  1 
ATOM   5915 C  C   . LEU F  1 56  ? 28.562  10.615  81.883  1.00 36.80  ? 305  LEU F C   1 
ATOM   5916 O  O   . LEU F  1 56  ? 28.344  9.492   81.459  1.00 38.87  ? 305  LEU F O   1 
ATOM   5917 C  CB  . LEU F  1 56  ? 30.497  11.981  80.959  1.00 39.73  ? 305  LEU F CB  1 
ATOM   5918 C  CG  . LEU F  1 56  ? 31.490  10.845  80.740  1.00 44.84  ? 305  LEU F CG  1 
ATOM   5919 C  CD1 . LEU F  1 56  ? 31.446  10.408  79.275  1.00 46.37  ? 305  LEU F CD1 1 
ATOM   5920 C  CD2 . LEU F  1 56  ? 32.893  11.282  81.165  1.00 45.29  ? 305  LEU F CD2 1 
ATOM   5921 N  N   . GLN F  1 57  ? 28.380  10.953  83.166  1.00 34.62  ? 306  GLN F N   1 
ATOM   5922 C  CA  . GLN F  1 57  ? 27.943  9.962   84.153  1.00 36.80  ? 306  GLN F CA  1 
ATOM   5923 C  C   . GLN F  1 57  ? 26.672  9.225   83.680  1.00 34.44  ? 306  GLN F C   1 
ATOM   5924 O  O   . GLN F  1 57  ? 26.544  8.012   83.848  1.00 35.75  ? 306  GLN F O   1 
ATOM   5925 C  CB  . GLN F  1 57  ? 27.679  10.571  85.549  1.00 37.59  ? 306  GLN F CB  1 
ATOM   5926 C  CG  . GLN F  1 57  ? 28.770  11.469  86.126  1.00 43.81  ? 306  GLN F CG  1 
ATOM   5927 C  CD  . GLN F  1 57  ? 30.201  10.901  86.057  1.00 47.51  ? 306  GLN F CD  1 
ATOM   5928 O  OE1 . GLN F  1 57  ? 30.454  9.788   86.485  1.00 47.59  ? 306  GLN F OE1 1 
ATOM   5929 N  NE2 . GLN F  1 57  ? 31.147  11.701  85.553  1.00 45.25  ? 306  GLN F NE2 1 
ATOM   5930 N  N   . SER F  1 58  ? 25.722  9.969   83.128  1.00 33.93  ? 307  SER F N   1 
ATOM   5931 C  CA  . SER F  1 58  ? 24.448  9.394   82.726  1.00 33.97  ? 307  SER F CA  1 
ATOM   5932 C  C   . SER F  1 58  ? 24.530  8.735   81.377  1.00 34.07  ? 307  SER F C   1 
ATOM   5933 O  O   . SER F  1 58  ? 24.002  7.651   81.184  1.00 36.67  ? 307  SER F O   1 
ATOM   5934 C  CB  . SER F  1 58  ? 23.353  10.458  82.746  1.00 34.66  ? 307  SER F CB  1 
ATOM   5935 O  OG  . SER F  1 58  ? 22.894  10.571  84.092  1.00 38.73  ? 307  SER F OG  1 
ATOM   5936 N  N   . SER F  1 59  ? 25.181  9.368   80.423  1.00 32.52  ? 308  SER F N   1 
ATOM   5937 C  CA  . SER F  1 59  ? 25.167  8.801   79.076  1.00 36.07  ? 308  SER F CA  1 
ATOM   5938 C  C   . SER F  1 59  ? 25.824  7.443   79.043  1.00 37.41  ? 308  SER F C   1 
ATOM   5939 O  O   . SER F  1 59  ? 25.327  6.552   78.382  1.00 44.01  ? 308  SER F O   1 
ATOM   5940 C  CB  . SER F  1 59  ? 25.844  9.724   78.075  1.00 37.27  ? 308  SER F CB  1 
ATOM   5941 O  OG  . SER F  1 59  ? 27.093  10.149  78.552  1.00 40.98  ? 308  SER F OG  1 
ATOM   5942 N  N   . ARG F  1 60  ? 26.919  7.277   79.776  1.00 35.40  ? 309  ARG F N   1 
ATOM   5943 C  CA  . ARG F  1 60  ? 27.674  6.020   79.741  1.00 37.69  ? 309  ARG F CA  1 
ATOM   5944 C  C   . ARG F  1 60  ? 27.049  4.962   80.666  1.00 35.37  ? 309  ARG F C   1 
ATOM   5945 O  O   . ARG F  1 60  ? 27.203  3.795   80.427  1.00 34.84  ? 309  ARG F O   1 
ATOM   5946 C  CB  . ARG F  1 60  ? 29.185  6.237   80.044  1.00 41.10  ? 309  ARG F CB  1 
ATOM   5947 C  CG  . ARG F  1 60  ? 29.540  6.343   81.529  1.00 46.36  ? 309  ARG F CG  1 
ATOM   5948 C  CD  . ARG F  1 60  ? 31.050  6.493   81.776  1.00 52.21  ? 309  ARG F CD  1 
ATOM   5949 N  NE  . ARG F  1 60  ? 31.289  7.287   82.987  1.00 55.99  ? 309  ARG F NE  1 
ATOM   5950 C  CZ  . ARG F  1 60  ? 32.481  7.624   83.481  1.00 65.01  ? 309  ARG F CZ  1 
ATOM   5951 N  NH1 . ARG F  1 60  ? 32.542  8.361   84.585  1.00 70.85  ? 309  ARG F NH1 1 
ATOM   5952 N  NH2 . ARG F  1 60  ? 33.612  7.230   82.904  1.00 68.56  ? 309  ARG F NH2 1 
ATOM   5953 N  N   . SER F  1 61  ? 26.360  5.367   81.726  1.00 35.64  ? 310  SER F N   1 
ATOM   5954 C  CA  . SER F  1 61  ? 25.683  4.408   82.603  1.00 35.38  ? 310  SER F CA  1 
ATOM   5955 C  C   . SER F  1 61  ? 24.276  3.998   82.096  1.00 36.34  ? 310  SER F C   1 
ATOM   5956 O  O   . SER F  1 61  ? 23.695  3.035   82.575  1.00 34.55  ? 310  SER F O   1 
ATOM   5957 C  CB  . SER F  1 61  ? 25.559  5.010   83.983  1.00 38.34  ? 310  SER F CB  1 
ATOM   5958 O  OG  . SER F  1 61  ? 24.649  6.094   83.959  1.00 38.49  ? 310  SER F OG  1 
ATOM   5959 N  N   . ASN F  1 62  ? 23.761  4.733   81.104  1.00 37.73  ? 311  ASN F N   1 
ATOM   5960 C  CA  . ASN F  1 62  ? 22.386  4.637   80.634  1.00 36.39  ? 311  ASN F CA  1 
ATOM   5961 C  C   . ASN F  1 62  ? 21.394  4.834   81.780  1.00 37.83  ? 311  ASN F C   1 
ATOM   5962 O  O   . ASN F  1 62  ? 20.325  4.228   81.786  1.00 42.38  ? 311  ASN F O   1 
ATOM   5963 C  CB  . ASN F  1 62  ? 22.132  3.315   79.912  1.00 40.41  ? 311  ASN F CB  1 
ATOM   5964 C  CG  . ASN F  1 62  ? 23.149  3.041   78.815  1.00 43.99  ? 311  ASN F CG  1 
ATOM   5965 O  OD1 . ASN F  1 62  ? 23.272  3.805   77.855  1.00 48.53  ? 311  ASN F OD1 1 
ATOM   5966 N  ND2 . ASN F  1 62  ? 23.894  1.946   78.954  1.00 45.46  ? 311  ASN F ND2 1 
ATOM   5967 N  N   . ARG F  1 63  ? 21.747  5.696   82.732  1.00 38.25  ? 312  ARG F N   1 
ATOM   5968 C  CA  . ARG F  1 63  ? 20.896  6.009   83.890  1.00 39.50  ? 312  ARG F CA  1 
ATOM   5969 C  C   . ARG F  1 63  ? 20.279  7.406   83.764  1.00 38.99  ? 312  ARG F C   1 
ATOM   5970 O  O   . ARG F  1 63  ? 20.903  8.333   83.271  1.00 42.55  ? 312  ARG F O   1 
ATOM   5971 C  CB  . ARG F  1 63  ? 21.700  5.988   85.193  1.00 45.60  ? 312  ARG F CB  1 
ATOM   5972 C  CG  . ARG F  1 63  ? 22.499  4.710   85.443  1.00 50.43  ? 312  ARG F CG  1 
ATOM   5973 C  CD  . ARG F  1 63  ? 21.621  3.591   85.931  1.00 47.15  ? 312  ARG F CD  1 
ATOM   5974 N  NE  . ARG F  1 63  ? 22.326  2.316   86.089  1.00 45.63  ? 312  ARG F NE  1 
ATOM   5975 C  CZ  . ARG F  1 63  ? 21.714  1.132   86.052  1.00 45.45  ? 312  ARG F CZ  1 
ATOM   5976 N  NH1 . ARG F  1 63  ? 20.386  1.086   85.852  1.00 41.70  ? 312  ARG F NH1 1 
ATOM   5977 N  NH2 . ARG F  1 63  ? 22.410  -0.011  86.196  1.00 40.94  ? 312  ARG F NH2 1 
ATOM   5978 N  N   . PHE F  1 64  ? 19.057  7.551   84.250  1.00 33.45  ? 313  PHE F N   1 
ATOM   5979 C  CA  . PHE F  1 64  ? 18.409  8.837   84.286  1.00 28.41  ? 313  PHE F CA  1 
ATOM   5980 C  C   . PHE F  1 64  ? 18.655  9.462   85.625  1.00 25.73  ? 313  PHE F C   1 
ATOM   5981 O  O   . PHE F  1 64  ? 18.419  8.838   86.661  1.00 22.42  ? 313  PHE F O   1 
ATOM   5982 C  CB  . PHE F  1 64  ? 16.922  8.718   84.067  1.00 28.54  ? 313  PHE F CB  1 
ATOM   5983 C  CG  . PHE F  1 64  ? 16.573  8.080   82.809  1.00 28.89  ? 313  PHE F CG  1 
ATOM   5984 C  CD1 . PHE F  1 64  ? 17.261  8.395   81.642  1.00 31.87  ? 313  PHE F CD1 1 
ATOM   5985 C  CD2 . PHE F  1 64  ? 15.553  7.156   82.761  1.00 29.43  ? 313  PHE F CD2 1 
ATOM   5986 C  CE1 . PHE F  1 64  ? 16.953  7.767   80.445  1.00 31.79  ? 313  PHE F CE1 1 
ATOM   5987 C  CE2 . PHE F  1 64  ? 15.212  6.555   81.567  1.00 30.47  ? 313  PHE F CE2 1 
ATOM   5988 C  CZ  . PHE F  1 64  ? 15.930  6.834   80.405  1.00 32.15  ? 313  PHE F CZ  1 
ATOM   5989 N  N   . THR F  1 65  ? 19.107  10.713  85.597  1.00 24.61  ? 314  THR F N   1 
ATOM   5990 C  CA  . THR F  1 65  ? 19.600  11.388  86.776  1.00 25.05  ? 314  THR F CA  1 
ATOM   5991 C  C   . THR F  1 65  ? 19.069  12.824  86.906  1.00 24.53  ? 314  THR F C   1 
ATOM   5992 O  O   . THR F  1 65  ? 19.234  13.633  85.998  1.00 27.90  ? 314  THR F O   1 
ATOM   5993 C  CB  . THR F  1 65  ? 21.139  11.407  86.716  1.00 25.72  ? 314  THR F CB  1 
ATOM   5994 O  OG1 . THR F  1 65  ? 21.600  10.090  86.450  1.00 27.16  ? 314  THR F OG1 1 
ATOM   5995 C  CG2 . THR F  1 65  ? 21.767  11.867  88.021  1.00 27.06  ? 314  THR F CG2 1 
ATOM   5996 N  N   . TRP F  1 66  ? 18.454  13.129  88.032  1.00 22.11  ? 315  TRP F N   1 
ATOM   5997 C  CA  . TRP F  1 66  ? 18.020  14.491  88.336  1.00 23.87  ? 315  TRP F CA  1 
ATOM   5998 C  C   . TRP F  1 66  ? 19.188  15.492  88.513  1.00 24.58  ? 315  TRP F C   1 
ATOM   5999 O  O   . TRP F  1 66  ? 20.267  15.160  89.036  1.00 24.13  ? 315  TRP F O   1 
ATOM   6000 C  CB  . TRP F  1 66  ? 17.312  14.494  89.696  1.00 23.85  ? 315  TRP F CB  1 
ATOM   6001 C  CG  . TRP F  1 66  ? 15.991  13.785  89.799  1.00 23.69  ? 315  TRP F CG  1 
ATOM   6002 C  CD1 . TRP F  1 66  ? 15.613  12.923  90.776  1.00 24.31  ? 315  TRP F CD1 1 
ATOM   6003 C  CD2 . TRP F  1 66  ? 14.836  13.978  88.978  1.00 23.19  ? 315  TRP F CD2 1 
ATOM   6004 N  NE1 . TRP F  1 66  ? 14.327  12.537  90.599  1.00 23.84  ? 315  TRP F NE1 1 
ATOM   6005 C  CE2 . TRP F  1 66  ? 13.820  13.166  89.499  1.00 24.83  ? 315  TRP F CE2 1 
ATOM   6006 C  CE3 . TRP F  1 66  ? 14.577  14.720  87.836  1.00 23.94  ? 315  TRP F CE3 1 
ATOM   6007 C  CZ2 . TRP F  1 66  ? 12.562  13.097  88.928  1.00 24.25  ? 315  TRP F CZ2 1 
ATOM   6008 C  CZ3 . TRP F  1 66  ? 13.323  14.657  87.274  1.00 24.21  ? 315  TRP F CZ3 1 
ATOM   6009 C  CH2 . TRP F  1 66  ? 12.335  13.850  87.822  1.00 24.44  ? 315  TRP F CH2 1 
ATOM   6010 N  N   . MET F  1 67  ? 18.922  16.719  88.115  1.00 25.34  ? 316  MET F N   1 
ATOM   6011 C  CA  . MET F  1 67  ? 19.718  17.870  88.437  1.00 26.68  ? 316  MET F CA  1 
ATOM   6012 C  C   . MET F  1 67  ? 18.786  18.833  89.122  1.00 25.76  ? 316  MET F C   1 
ATOM   6013 O  O   . MET F  1 67  ? 17.591  18.679  89.044  1.00 25.79  ? 316  MET F O   1 
ATOM   6014 C  CB  . MET F  1 67  ? 20.286  18.502  87.158  1.00 27.01  ? 316  MET F CB  1 
ATOM   6015 C  CG  . MET F  1 67  ? 19.311  19.339  86.342  1.00 29.01  ? 316  MET F CG  1 
ATOM   6016 S  SD  . MET F  1 67  ? 19.929  19.787  84.680  1.00 30.10  ? 316  MET F SD  1 
ATOM   6017 C  CE  . MET F  1 67  ? 20.023  18.215  83.832  1.00 29.56  ? 316  MET F CE  1 
ATOM   6018 N  N   . GLY F  1 68  ? 19.341  19.868  89.732  1.00 26.96  ? 317  GLY F N   1 
ATOM   6019 C  CA  . GLY F  1 68  ? 18.566  20.811  90.516  1.00 27.89  ? 317  GLY F CA  1 
ATOM   6020 C  C   . GLY F  1 68  ? 18.055  21.948  89.681  1.00 28.62  ? 317  GLY F C   1 
ATOM   6021 O  O   . GLY F  1 68  ? 18.427  23.080  89.911  1.00 33.84  ? 317  GLY F O   1 
ATOM   6022 N  N   . LEU F  1 69  ? 17.157  21.616  88.748  1.00 26.91  ? 318  LEU F N   1 
ATOM   6023 C  CA  . LEU F  1 69  ? 16.601  22.520  87.761  1.00 25.79  ? 318  LEU F CA  1 
ATOM   6024 C  C   . LEU F  1 69  ? 15.152  22.143  87.557  1.00 27.31  ? 318  LEU F C   1 
ATOM   6025 O  O   . LEU F  1 69  ? 14.851  20.965  87.282  1.00 24.90  ? 318  LEU F O   1 
ATOM   6026 C  CB  . LEU F  1 69  ? 17.343  22.352  86.443  1.00 26.81  ? 318  LEU F CB  1 
ATOM   6027 C  CG  . LEU F  1 69  ? 17.036  23.272  85.280  1.00 28.81  ? 318  LEU F CG  1 
ATOM   6028 C  CD1 . LEU F  1 69  ? 17.216  24.738  85.659  1.00 30.39  ? 318  LEU F CD1 1 
ATOM   6029 C  CD2 . LEU F  1 69  ? 17.945  22.910  84.117  1.00 30.37  ? 318  LEU F CD2 1 
ATOM   6030 N  N   . SER F  1 70  ? 14.265  23.138  87.706  1.00 26.11  ? 319  SER F N   1 
ATOM   6031 C  CA  . SER F  1 70  ? 12.834  22.935  87.646  1.00 25.83  ? 319  SER F CA  1 
ATOM   6032 C  C   . SER F  1 70  ? 12.127  24.177  87.085  1.00 28.01  ? 319  SER F C   1 
ATOM   6033 O  O   . SER F  1 70  ? 12.663  25.307  87.192  1.00 28.61  ? 319  SER F O   1 
ATOM   6034 C  CB  . SER F  1 70  ? 12.295  22.622  89.055  1.00 26.25  ? 319  SER F CB  1 
ATOM   6035 O  OG  . SER F  1 70  ? 11.923  23.783  89.759  1.00 27.13  ? 319  SER F OG  1 
ATOM   6036 N  N   . ASP F  1 71  ? 10.975  23.963  86.435  1.00 25.26  ? 320  ASP F N   1 
ATOM   6037 C  CA  . ASP F  1 71  ? 10.025  25.037  86.230  1.00 25.05  ? 320  ASP F CA  1 
ATOM   6038 C  C   . ASP F  1 71  ? 8.718   24.845  87.003  1.00 26.82  ? 320  ASP F C   1 
ATOM   6039 O  O   . ASP F  1 71  ? 7.619   25.200  86.498  1.00 26.81  ? 320  ASP F O   1 
ATOM   6040 C  CB  . ASP F  1 71  ? 9.783   25.305  84.722  1.00 26.01  ? 320  ASP F CB  1 
ATOM   6041 C  CG  . ASP F  1 71  ? 8.866   24.275  84.040  1.00 26.98  ? 320  ASP F CG  1 
ATOM   6042 O  OD1 . ASP F  1 71  ? 8.619   23.176  84.553  1.00 26.60  ? 320  ASP F OD1 1 
ATOM   6043 O  OD2 . ASP F  1 71  ? 8.424   24.555  82.920  1.00 30.45  ? 320  ASP F OD2 1 
ATOM   6044 N  N   . LEU F  1 72  ? 8.836   24.280  88.216  1.00 25.67  ? 321  LEU F N   1 
ATOM   6045 C  CA  . LEU F  1 72  ? 7.707   24.154  89.091  1.00 29.65  ? 321  LEU F CA  1 
ATOM   6046 C  C   . LEU F  1 72  ? 7.047   25.510  89.442  1.00 35.26  ? 321  LEU F C   1 
ATOM   6047 O  O   . LEU F  1 72  ? 5.824   25.626  89.465  1.00 40.16  ? 321  LEU F O   1 
ATOM   6048 C  CB  . LEU F  1 72  ? 8.124   23.485  90.400  1.00 29.24  ? 321  LEU F CB  1 
ATOM   6049 C  CG  . LEU F  1 72  ? 8.422   21.994  90.267  1.00 27.09  ? 321  LEU F CG  1 
ATOM   6050 C  CD1 . LEU F  1 72  ? 9.278   21.550  91.417  1.00 27.10  ? 321  LEU F CD1 1 
ATOM   6051 C  CD2 . LEU F  1 72  ? 7.089   21.247  90.225  1.00 27.01  ? 321  LEU F CD2 1 
ATOM   6052 N  N   . ASN F  1 73  ? 7.846   26.512  89.753  1.00 36.11  ? 322  ASN F N   1 
ATOM   6053 C  CA  . ASN F  1 73  ? 7.282   27.749  90.274  1.00 38.83  ? 322  ASN F CA  1 
ATOM   6054 C  C   . ASN F  1 73  ? 6.552   28.477  89.146  1.00 35.66  ? 322  ASN F C   1 
ATOM   6055 O  O   . ASN F  1 73  ? 5.443   28.929  89.311  1.00 33.50  ? 322  ASN F O   1 
ATOM   6056 C  CB  . ASN F  1 73  ? 8.361   28.625  90.911  1.00 41.22  ? 322  ASN F CB  1 
ATOM   6057 C  CG  . ASN F  1 73  ? 7.774   29.835  91.623  1.00 43.75  ? 322  ASN F CG  1 
ATOM   6058 O  OD1 . ASN F  1 73  ? 8.081   30.963  91.274  1.00 46.99  ? 322  ASN F OD1 1 
ATOM   6059 N  ND2 . ASN F  1 73  ? 6.920   29.600  92.593  1.00 43.38  ? 322  ASN F ND2 1 
ATOM   6060 N  N   . GLN F  1 74  ? 7.171   28.525  87.977  1.00 36.52  ? 323  GLN F N   1 
ATOM   6061 C  CA  . GLN F  1 74  ? 6.557   29.129  86.832  1.00 35.78  ? 323  GLN F CA  1 
ATOM   6062 C  C   . GLN F  1 74  ? 6.883   28.420  85.516  1.00 33.64  ? 323  GLN F C   1 
ATOM   6063 O  O   . GLN F  1 74  ? 8.011   28.540  85.029  1.00 32.41  ? 323  GLN F O   1 
ATOM   6064 C  CB  . GLN F  1 74  ? 6.978   30.595  86.694  1.00 37.13  ? 323  GLN F CB  1 
ATOM   6065 C  CG  . GLN F  1 74  ? 6.283   31.190  85.486  1.00 38.98  ? 323  GLN F CG  1 
ATOM   6066 C  CD  . GLN F  1 74  ? 6.587   32.629  85.300  1.00 43.46  ? 323  GLN F CD  1 
ATOM   6067 O  OE1 . GLN F  1 74  ? 5.786   33.467  85.683  1.00 40.16  ? 323  GLN F OE1 1 
ATOM   6068 N  NE2 . GLN F  1 74  ? 7.763   32.934  84.724  1.00 43.65  ? 323  GLN F NE2 1 
ATOM   6069 N  N   . GLU F  1 75  ? 5.852   27.817  84.904  1.00 30.54  ? 324  GLU F N   1 
ATOM   6070 C  CA  . GLU F  1 75  ? 5.995   27.022  83.691  1.00 34.01  ? 324  GLU F CA  1 
ATOM   6071 C  C   . GLU F  1 75  ? 6.773   27.728  82.605  1.00 34.09  ? 324  GLU F C   1 
ATOM   6072 O  O   . GLU F  1 75  ? 6.527   28.875  82.328  1.00 38.09  ? 324  GLU F O   1 
ATOM   6073 C  CB  . GLU F  1 75  ? 4.620   26.612  83.131  1.00 34.82  ? 324  GLU F CB  1 
ATOM   6074 C  CG  . GLU F  1 75  ? 4.700   25.745  81.860  1.00 35.12  ? 324  GLU F CG  1 
ATOM   6075 C  CD  . GLU F  1 75  ? 5.451   24.437  82.092  1.00 34.54  ? 324  GLU F CD  1 
ATOM   6076 O  OE1 . GLU F  1 75  ? 5.325   23.863  83.220  1.00 33.74  ? 324  GLU F OE1 1 
ATOM   6077 O  OE2 . GLU F  1 75  ? 6.176   23.998  81.155  1.00 33.15  ? 324  GLU F OE2 1 
ATOM   6078 N  N   . GLY F  1 76  ? 7.708   27.030  81.970  1.00 35.06  ? 325  GLY F N   1 
ATOM   6079 C  CA  . GLY F  1 76  ? 8.574   27.654  80.966  1.00 34.61  ? 325  GLY F CA  1 
ATOM   6080 C  C   . GLY F  1 76  ? 9.737   28.466  81.547  1.00 38.81  ? 325  GLY F C   1 
ATOM   6081 O  O   . GLY F  1 76  ? 10.705  28.734  80.836  1.00 35.72  ? 325  GLY F O   1 
ATOM   6082 N  N   . THR F  1 77  ? 9.663   28.846  82.831  1.00 36.30  ? 326  THR F N   1 
ATOM   6083 C  CA  . THR F  1 77  ? 10.777  29.557  83.474  1.00 39.28  ? 326  THR F CA  1 
ATOM   6084 C  C   . THR F  1 77  ? 11.656  28.597  84.315  1.00 35.56  ? 326  THR F C   1 
ATOM   6085 O  O   . THR F  1 77  ? 11.347  28.275  85.475  1.00 29.86  ? 326  THR F O   1 
ATOM   6086 C  CB  . THR F  1 77  ? 10.291  30.714  84.377  1.00 41.64  ? 326  THR F CB  1 
ATOM   6087 O  OG1 . THR F  1 77  ? 9.495   31.640  83.610  1.00 42.21  ? 326  THR F OG1 1 
ATOM   6088 C  CG2 . THR F  1 77  ? 11.516  31.439  84.998  1.00 41.40  ? 326  THR F CG2 1 
ATOM   6089 N  N   . TRP F  1 78  ? 12.737  28.150  83.702  1.00 31.95  ? 327  TRP F N   1 
ATOM   6090 C  CA  . TRP F  1 78  ? 13.616  27.200  84.313  1.00 33.23  ? 327  TRP F CA  1 
ATOM   6091 C  C   . TRP F  1 78  ? 14.604  27.865  85.280  1.00 33.97  ? 327  TRP F C   1 
ATOM   6092 O  O   . TRP F  1 78  ? 15.332  28.771  84.953  1.00 34.84  ? 327  TRP F O   1 
ATOM   6093 C  CB  . TRP F  1 78  ? 14.299  26.351  83.234  1.00 31.82  ? 327  TRP F CB  1 
ATOM   6094 C  CG  . TRP F  1 78  ? 13.307  25.410  82.605  1.00 30.97  ? 327  TRP F CG  1 
ATOM   6095 C  CD1 . TRP F  1 78  ? 12.532  25.653  81.518  1.00 33.30  ? 327  TRP F CD1 1 
ATOM   6096 C  CD2 . TRP F  1 78  ? 12.982  24.081  83.041  1.00 32.52  ? 327  TRP F CD2 1 
ATOM   6097 N  NE1 . TRP F  1 78  ? 11.719  24.556  81.244  1.00 33.27  ? 327  TRP F NE1 1 
ATOM   6098 C  CE2 . TRP F  1 78  ? 11.985  23.580  82.171  1.00 34.95  ? 327  TRP F CE2 1 
ATOM   6099 C  CE3 . TRP F  1 78  ? 13.439  23.263  84.074  1.00 33.26  ? 327  TRP F CE3 1 
ATOM   6100 C  CZ2 . TRP F  1 78  ? 11.433  22.302  82.320  1.00 31.81  ? 327  TRP F CZ2 1 
ATOM   6101 C  CZ3 . TRP F  1 78  ? 12.916  22.000  84.205  1.00 32.65  ? 327  TRP F CZ3 1 
ATOM   6102 C  CH2 . TRP F  1 78  ? 11.915  21.526  83.327  1.00 33.86  ? 327  TRP F CH2 1 
ATOM   6103 N  N   . GLN F  1 79  ? 14.624  27.360  86.489  1.00 36.45  ? 328  GLN F N   1 
ATOM   6104 C  CA  . GLN F  1 79  ? 15.307  27.998  87.559  1.00 37.16  ? 328  GLN F CA  1 
ATOM   6105 C  C   . GLN F  1 79  ? 16.067  26.912  88.324  1.00 35.69  ? 328  GLN F C   1 
ATOM   6106 O  O   . GLN F  1 79  ? 15.495  25.873  88.667  1.00 32.50  ? 328  GLN F O   1 
ATOM   6107 C  CB  . GLN F  1 79  ? 14.253  28.666  88.418  1.00 41.09  ? 328  GLN F CB  1 
ATOM   6108 C  CG  . GLN F  1 79  ? 14.789  29.571  89.504  1.00 50.81  ? 328  GLN F CG  1 
ATOM   6109 C  CD  . GLN F  1 79  ? 13.678  30.344  90.209  1.00 55.86  ? 328  GLN F CD  1 
ATOM   6110 O  OE1 . GLN F  1 79  ? 12.564  30.504  89.673  1.00 58.78  ? 328  GLN F OE1 1 
ATOM   6111 N  NE2 . GLN F  1 79  ? 13.969  30.816  91.416  1.00 54.88  ? 328  GLN F NE2 1 
ATOM   6112 N  N   . TRP F  1 80  ? 17.354  27.154  88.596  1.00 34.25  ? 329  TRP F N   1 
ATOM   6113 C  CA  . TRP F  1 80  ? 18.174  26.224  89.362  1.00 29.84  ? 329  TRP F CA  1 
ATOM   6114 C  C   . TRP F  1 80  ? 17.743  26.298  90.830  1.00 30.02  ? 329  TRP F C   1 
ATOM   6115 O  O   . TRP F  1 80  ? 17.022  27.215  91.224  1.00 32.37  ? 329  TRP F O   1 
ATOM   6116 C  CB  . TRP F  1 80  ? 19.637  26.551  89.222  1.00 27.65  ? 329  TRP F CB  1 
ATOM   6117 C  CG  . TRP F  1 80  ? 20.169  26.375  87.880  1.00 27.24  ? 329  TRP F CG  1 
ATOM   6118 C  CD1 . TRP F  1 80  ? 20.418  27.354  86.964  1.00 29.11  ? 329  TRP F CD1 1 
ATOM   6119 C  CD2 . TRP F  1 80  ? 20.575  25.148  87.275  1.00 28.03  ? 329  TRP F CD2 1 
ATOM   6120 N  NE1 . TRP F  1 80  ? 20.934  26.815  85.826  1.00 29.54  ? 329  TRP F NE1 1 
ATOM   6121 C  CE2 . TRP F  1 80  ? 21.066  25.461  86.001  1.00 28.57  ? 329  TRP F CE2 1 
ATOM   6122 C  CE3 . TRP F  1 80  ? 20.594  23.807  87.704  1.00 27.50  ? 329  TRP F CE3 1 
ATOM   6123 C  CZ2 . TRP F  1 80  ? 21.534  24.495  85.137  1.00 28.63  ? 329  TRP F CZ2 1 
ATOM   6124 C  CZ3 . TRP F  1 80  ? 21.047  22.879  86.879  1.00 27.25  ? 329  TRP F CZ3 1 
ATOM   6125 C  CH2 . TRP F  1 80  ? 21.526  23.212  85.586  1.00 30.29  ? 329  TRP F CH2 1 
ATOM   6126 N  N   . VAL F  1 81  ? 18.126  25.311  91.629  1.00 30.07  ? 330  VAL F N   1 
ATOM   6127 C  CA  . VAL F  1 81  ? 17.699  25.298  93.033  1.00 30.33  ? 330  VAL F CA  1 
ATOM   6128 C  C   . VAL F  1 81  ? 18.387  26.350  93.903  1.00 30.83  ? 330  VAL F C   1 
ATOM   6129 O  O   . VAL F  1 81  ? 17.913  26.628  94.975  1.00 31.38  ? 330  VAL F O   1 
ATOM   6130 C  CB  . VAL F  1 81  ? 17.790  23.907  93.702  1.00 29.44  ? 330  VAL F CB  1 
ATOM   6131 C  CG1 . VAL F  1 81  ? 16.843  22.942  93.046  1.00 27.95  ? 330  VAL F CG1 1 
ATOM   6132 C  CG2 . VAL F  1 81  ? 19.215  23.360  93.706  1.00 32.54  ? 330  VAL F CG2 1 
ATOM   6133 N  N   . ASP F  1 82  ? 19.461  26.959  93.427  1.00 33.04  ? 331  ASP F N   1 
ATOM   6134 C  CA  . ASP F  1 82  ? 20.059  28.117  94.134  1.00 36.26  ? 331  ASP F CA  1 
ATOM   6135 C  C   . ASP F  1 82  ? 19.451  29.467  93.752  1.00 36.98  ? 331  ASP F C   1 
ATOM   6136 O  O   . ASP F  1 82  ? 19.970  30.484  94.170  1.00 40.25  ? 331  ASP F O   1 
ATOM   6137 C  CB  . ASP F  1 82  ? 21.576  28.192  93.910  1.00 33.90  ? 331  ASP F CB  1 
ATOM   6138 C  CG  . ASP F  1 82  ? 21.948  28.408  92.458  1.00 37.72  ? 331  ASP F CG  1 
ATOM   6139 O  OD1 . ASP F  1 82  ? 21.036  28.486  91.565  1.00 38.50  ? 331  ASP F OD1 1 
ATOM   6140 O  OD2 . ASP F  1 82  ? 23.182  28.478  92.210  1.00 37.36  ? 331  ASP F OD2 1 
ATOM   6141 N  N   . GLY F  1 83  ? 18.406  29.466  92.926  1.00 34.95  ? 332  GLY F N   1 
ATOM   6142 C  CA  . GLY F  1 83  ? 17.690  30.684  92.549  1.00 35.41  ? 332  GLY F CA  1 
ATOM   6143 C  C   . GLY F  1 83  ? 18.139  31.235  91.209  1.00 37.76  ? 332  GLY F C   1 
ATOM   6144 O  O   . GLY F  1 83  ? 17.536  32.167  90.663  1.00 40.97  ? 332  GLY F O   1 
ATOM   6145 N  N   . SER F  1 84  ? 19.222  30.691  90.674  1.00 39.32  ? 333  SER F N   1 
ATOM   6146 C  CA  . SER F  1 84  ? 19.788  31.262  89.471  1.00 37.43  ? 333  SER F CA  1 
ATOM   6147 C  C   . SER F  1 84  ? 18.996  30.825  88.212  1.00 40.22  ? 333  SER F C   1 
ATOM   6148 O  O   . SER F  1 84  ? 18.440  29.732  88.153  1.00 38.60  ? 333  SER F O   1 
ATOM   6149 C  CB  . SER F  1 84  ? 21.267  30.914  89.392  1.00 37.62  ? 333  SER F CB  1 
ATOM   6150 O  OG  . SER F  1 84  ? 21.489  29.527  89.265  1.00 40.30  ? 333  SER F OG  1 
ATOM   6151 N  N   . PRO F  1 85  ? 18.929  31.694  87.200  1.00 40.05  ? 334  PRO F N   1 
ATOM   6152 C  CA  . PRO F  1 85  ? 18.179  31.408  86.000  1.00 38.47  ? 334  PRO F CA  1 
ATOM   6153 C  C   . PRO F  1 85  ? 18.917  30.425  85.116  1.00 38.21  ? 334  PRO F C   1 
ATOM   6154 O  O   . PRO F  1 85  ? 20.121  30.313  85.198  1.00 35.15  ? 334  PRO F O   1 
ATOM   6155 C  CB  . PRO F  1 85  ? 18.158  32.770  85.297  1.00 37.92  ? 334  PRO F CB  1 
ATOM   6156 C  CG  . PRO F  1 85  ? 19.522  33.311  85.635  1.00 38.54  ? 334  PRO F CG  1 
ATOM   6157 C  CD  . PRO F  1 85  ? 19.616  32.996  87.096  1.00 39.04  ? 334  PRO F CD  1 
ATOM   6158 N  N   . LEU F  1 86  ? 18.202  29.738  84.240  1.00 37.27  ? 335  LEU F N   1 
ATOM   6159 C  CA  . LEU F  1 86  ? 18.876  29.003  83.179  1.00 37.12  ? 335  LEU F CA  1 
ATOM   6160 C  C   . LEU F  1 86  ? 19.341  29.902  81.998  1.00 40.63  ? 335  LEU F C   1 
ATOM   6161 O  O   . LEU F  1 86  ? 18.536  30.410  81.227  1.00 40.40  ? 335  LEU F O   1 
ATOM   6162 C  CB  . LEU F  1 86  ? 17.969  27.940  82.663  1.00 35.02  ? 335  LEU F CB  1 
ATOM   6163 C  CG  . LEU F  1 86  ? 18.549  27.071  81.544  1.00 37.79  ? 335  LEU F CG  1 
ATOM   6164 C  CD1 . LEU F  1 86  ? 19.743  26.256  82.027  1.00 34.06  ? 335  LEU F CD1 1 
ATOM   6165 C  CD2 . LEU F  1 86  ? 17.418  26.183  81.001  1.00 37.27  ? 335  LEU F CD2 1 
ATOM   6166 N  N   . LEU F  1 87  ? 20.645  30.020  81.821  1.00 40.86  ? 336  LEU F N   1 
ATOM   6167 C  CA  . LEU F  1 87  ? 21.199  30.886  80.780  1.00 43.30  ? 336  LEU F CA  1 
ATOM   6168 C  C   . LEU F  1 87  ? 20.972  30.331  79.396  1.00 44.89  ? 336  LEU F C   1 
ATOM   6169 O  O   . LEU F  1 87  ? 21.081  29.132  79.210  1.00 47.72  ? 336  LEU F O   1 
ATOM   6170 C  CB  . LEU F  1 87  ? 22.695  31.081  80.991  1.00 40.40  ? 336  LEU F CB  1 
ATOM   6171 C  CG  . LEU F  1 87  ? 23.071  31.542  82.399  1.00 43.50  ? 336  LEU F CG  1 
ATOM   6172 C  CD1 . LEU F  1 87  ? 24.593  31.565  82.584  1.00 44.04  ? 336  LEU F CD1 1 
ATOM   6173 C  CD2 . LEU F  1 87  ? 22.430  32.908  82.684  1.00 42.41  ? 336  LEU F CD2 1 
ATOM   6174 N  N   . PRO F  1 88  ? 20.669  31.205  78.409  1.00 48.92  ? 337  PRO F N   1 
ATOM   6175 C  CA  . PRO F  1 88  ? 20.586  30.831  76.981  1.00 46.34  ? 337  PRO F CA  1 
ATOM   6176 C  C   . PRO F  1 88  ? 21.709  29.957  76.435  1.00 43.75  ? 337  PRO F C   1 
ATOM   6177 O  O   . PRO F  1 88  ? 21.440  29.080  75.602  1.00 49.10  ? 337  PRO F O   1 
ATOM   6178 C  CB  . PRO F  1 88  ? 20.570  32.191  76.244  1.00 49.22  ? 337  PRO F CB  1 
ATOM   6179 C  CG  . PRO F  1 88  ? 20.621  33.241  77.319  1.00 50.07  ? 337  PRO F CG  1 
ATOM   6180 C  CD  . PRO F  1 88  ? 20.203  32.589  78.606  1.00 48.11  ? 337  PRO F CD  1 
ATOM   6181 N  N   . SER F  1 89  ? 22.946  30.168  76.866  1.00 41.76  ? 338  SER F N   1 
ATOM   6182 C  CA  . SER F  1 89  ? 24.054  29.277  76.411  1.00 44.70  ? 338  SER F CA  1 
ATOM   6183 C  C   . SER F  1 89  ? 23.857  27.796  76.809  1.00 46.15  ? 338  SER F C   1 
ATOM   6184 O  O   . SER F  1 89  ? 24.500  26.912  76.225  1.00 50.69  ? 338  SER F O   1 
ATOM   6185 C  CB  . SER F  1 89  ? 25.424  29.741  76.933  1.00 41.21  ? 338  SER F CB  1 
ATOM   6186 O  OG  . SER F  1 89  ? 25.369  30.075  78.308  1.00 41.88  ? 338  SER F OG  1 
ATOM   6187 N  N   . PHE F  1 90  ? 22.983  27.544  77.795  1.00 42.25  ? 339  PHE F N   1 
ATOM   6188 C  CA  . PHE F  1 90  ? 22.658  26.187  78.243  1.00 43.38  ? 339  PHE F CA  1 
ATOM   6189 C  C   . PHE F  1 90  ? 21.467  25.521  77.525  1.00 44.04  ? 339  PHE F C   1 
ATOM   6190 O  O   . PHE F  1 90  ? 21.346  24.304  77.584  1.00 42.35  ? 339  PHE F O   1 
ATOM   6191 C  CB  . PHE F  1 90  ? 22.456  26.177  79.763  1.00 43.82  ? 339  PHE F CB  1 
ATOM   6192 C  CG  . PHE F  1 90  ? 23.735  26.337  80.548  1.00 47.59  ? 339  PHE F CG  1 
ATOM   6193 C  CD1 . PHE F  1 90  ? 24.553  27.458  80.373  1.00 47.15  ? 339  PHE F CD1 1 
ATOM   6194 C  CD2 . PHE F  1 90  ? 24.135  25.368  81.468  1.00 52.83  ? 339  PHE F CD2 1 
ATOM   6195 C  CE1 . PHE F  1 90  ? 25.725  27.610  81.086  1.00 45.64  ? 339  PHE F CE1 1 
ATOM   6196 C  CE2 . PHE F  1 90  ? 25.313  25.521  82.196  1.00 53.35  ? 339  PHE F CE2 1 
ATOM   6197 C  CZ  . PHE F  1 90  ? 26.115  26.639  81.998  1.00 51.02  ? 339  PHE F CZ  1 
ATOM   6198 N  N   . LYS F  1 91  ? 20.617  26.269  76.812  1.00 46.44  ? 340  LYS F N   1 
ATOM   6199 C  CA  . LYS F  1 91  ? 19.474  25.652  76.078  1.00 47.45  ? 340  LYS F CA  1 
ATOM   6200 C  C   . LYS F  1 91  ? 19.878  24.584  75.055  1.00 47.09  ? 340  LYS F C   1 
ATOM   6201 O  O   . LYS F  1 91  ? 19.101  23.646  74.750  1.00 42.87  ? 340  LYS F O   1 
ATOM   6202 C  CB  . LYS F  1 91  ? 18.644  26.719  75.374  1.00 57.87  ? 340  LYS F CB  1 
ATOM   6203 C  CG  . LYS F  1 91  ? 17.906  27.622  76.338  1.00 66.26  ? 340  LYS F CG  1 
ATOM   6204 C  CD  . LYS F  1 91  ? 17.363  28.858  75.631  1.00 74.05  ? 340  LYS F CD  1 
ATOM   6205 C  CE  . LYS F  1 91  ? 16.384  29.610  76.522  1.00 74.76  ? 340  LYS F CE  1 
ATOM   6206 N  NZ  . LYS F  1 91  ? 16.900  29.774  77.910  1.00 75.66  ? 340  LYS F NZ  1 
ATOM   6207 N  N   . GLN F  1 92  ? 21.092  24.717  74.519  1.00 44.19  ? 341  GLN F N   1 
ATOM   6208 C  CA  . GLN F  1 92  ? 21.639  23.678  73.644  1.00 42.88  ? 341  GLN F CA  1 
ATOM   6209 C  C   . GLN F  1 92  ? 21.664  22.274  74.275  1.00 39.92  ? 341  GLN F C   1 
ATOM   6210 O  O   . GLN F  1 92  ? 21.622  21.256  73.562  1.00 37.61  ? 341  GLN F O   1 
ATOM   6211 C  CB  . GLN F  1 92  ? 23.047  24.047  73.186  1.00 42.40  ? 341  GLN F CB  1 
ATOM   6212 C  CG  . GLN F  1 92  ? 24.035  24.159  74.326  1.00 46.50  ? 341  GLN F CG  1 
ATOM   6213 C  CD  . GLN F  1 92  ? 25.421  24.522  73.841  1.00 46.30  ? 341  GLN F CD  1 
ATOM   6214 O  OE1 . GLN F  1 92  ? 25.899  23.967  72.867  1.00 52.16  ? 341  GLN F OE1 1 
ATOM   6215 N  NE2 . GLN F  1 92  ? 26.077  25.434  74.531  1.00 45.46  ? 341  GLN F NE2 1 
ATOM   6216 N  N   . TYR F  1 93  ? 21.741  22.200  75.600  1.00 41.83  ? 342  TYR F N   1 
ATOM   6217 C  CA  . TYR F  1 93  ? 21.846  20.881  76.268  1.00 41.44  ? 342  TYR F CA  1 
ATOM   6218 C  C   . TYR F  1 93  ? 20.540  20.055  76.249  1.00 35.93  ? 342  TYR F C   1 
ATOM   6219 O  O   . TYR F  1 93  ? 20.591  18.828  76.345  1.00 35.89  ? 342  TYR F O   1 
ATOM   6220 C  CB  . TYR F  1 93  ? 22.487  21.008  77.671  1.00 42.58  ? 342  TYR F CB  1 
ATOM   6221 C  CG  . TYR F  1 93  ? 23.873  21.657  77.587  1.00 44.24  ? 342  TYR F CG  1 
ATOM   6222 C  CD1 . TYR F  1 93  ? 24.825  21.213  76.647  1.00 41.96  ? 342  TYR F CD1 1 
ATOM   6223 C  CD2 . TYR F  1 93  ? 24.230  22.720  78.428  1.00 45.53  ? 342  TYR F CD2 1 
ATOM   6224 C  CE1 . TYR F  1 93  ? 26.060  21.817  76.545  1.00 40.55  ? 342  TYR F CE1 1 
ATOM   6225 C  CE2 . TYR F  1 93  ? 25.477  23.317  78.335  1.00 42.28  ? 342  TYR F CE2 1 
ATOM   6226 C  CZ  . TYR F  1 93  ? 26.374  22.865  77.379  1.00 42.98  ? 342  TYR F CZ  1 
ATOM   6227 O  OH  . TYR F  1 93  ? 27.621  23.428  77.279  1.00 49.19  ? 342  TYR F OH  1 
ATOM   6228 N  N   . TRP F  1 94  ? 19.396  20.690  76.021  1.00 33.22  ? 343  TRP F N   1 
ATOM   6229 C  CA  . TRP F  1 94  ? 18.146  19.937  76.028  1.00 34.94  ? 343  TRP F CA  1 
ATOM   6230 C  C   . TRP F  1 94  ? 18.202  19.029  74.835  1.00 40.32  ? 343  TRP F C   1 
ATOM   6231 O  O   . TRP F  1 94  ? 18.681  19.436  73.768  1.00 38.98  ? 343  TRP F O   1 
ATOM   6232 C  CB  . TRP F  1 94  ? 16.903  20.817  75.871  1.00 34.49  ? 343  TRP F CB  1 
ATOM   6233 C  CG  . TRP F  1 94  ? 16.534  21.766  76.989  1.00 31.72  ? 343  TRP F CG  1 
ATOM   6234 C  CD1 . TRP F  1 94  ? 16.635  23.127  76.957  1.00 31.92  ? 343  TRP F CD1 1 
ATOM   6235 C  CD2 . TRP F  1 94  ? 15.930  21.441  78.253  1.00 29.18  ? 343  TRP F CD2 1 
ATOM   6236 N  NE1 . TRP F  1 94  ? 16.160  23.667  78.136  1.00 29.72  ? 343  TRP F NE1 1 
ATOM   6237 C  CE2 . TRP F  1 94  ? 15.729  22.651  78.946  1.00 28.69  ? 343  TRP F CE2 1 
ATOM   6238 C  CE3 . TRP F  1 94  ? 15.579  20.239  78.884  1.00 32.18  ? 343  TRP F CE3 1 
ATOM   6239 C  CZ2 . TRP F  1 94  ? 15.182  22.704  80.213  1.00 28.11  ? 343  TRP F CZ2 1 
ATOM   6240 C  CZ3 . TRP F  1 94  ? 15.037  20.299  80.173  1.00 31.24  ? 343  TRP F CZ3 1 
ATOM   6241 C  CH2 . TRP F  1 94  ? 14.827  21.521  80.802  1.00 30.96  ? 343  TRP F CH2 1 
ATOM   6242 N  N   . ASN F  1 95  ? 17.719  17.808  75.001  1.00 39.01  ? 344  ASN F N   1 
ATOM   6243 C  CA  . ASN F  1 95  ? 17.492  16.940  73.860  1.00 38.63  ? 344  ASN F CA  1 
ATOM   6244 C  C   . ASN F  1 95  ? 16.511  17.612  72.924  1.00 41.12  ? 344  ASN F C   1 
ATOM   6245 O  O   . ASN F  1 95  ? 15.732  18.495  73.340  1.00 35.18  ? 344  ASN F O   1 
ATOM   6246 C  CB  . ASN F  1 95  ? 16.894  15.585  74.296  1.00 37.34  ? 344  ASN F CB  1 
ATOM   6247 C  CG  . ASN F  1 95  ? 17.797  14.821  75.253  1.00 37.24  ? 344  ASN F CG  1 
ATOM   6248 O  OD1 . ASN F  1 95  ? 19.011  15.006  75.247  1.00 37.84  ? 344  ASN F OD1 1 
ATOM   6249 N  ND2 . ASN F  1 95  ? 17.200  13.966  76.101  1.00 37.09  ? 344  ASN F ND2 1 
ATOM   6250 N  N   . ARG F  1 96  ? 16.546  17.166  71.665  1.00 44.43  ? 345  ARG F N   1 
ATOM   6251 C  CA  . ARG F  1 96  ? 15.700  17.714  70.592  1.00 49.20  ? 345  ARG F CA  1 
ATOM   6252 C  C   . ARG F  1 96  ? 14.214  17.560  70.944  1.00 43.59  ? 345  ARG F C   1 
ATOM   6253 O  O   . ARG F  1 96  ? 13.789  16.538  71.442  1.00 41.93  ? 345  ARG F O   1 
ATOM   6254 C  CB  . ARG F  1 96  ? 16.060  17.035  69.267  1.00 57.36  ? 345  ARG F CB  1 
ATOM   6255 C  CG  . ARG F  1 96  ? 15.135  17.275  68.073  1.00 70.18  ? 345  ARG F CG  1 
ATOM   6256 C  CD  . ARG F  1 96  ? 15.566  16.458  66.843  1.00 76.15  ? 345  ARG F CD  1 
ATOM   6257 N  NE  . ARG F  1 96  ? 16.632  17.116  66.070  1.00 91.82  ? 345  ARG F NE  1 
ATOM   6258 C  CZ  . ARG F  1 96  ? 17.956  16.998  66.275  1.00 99.08  ? 345  ARG F CZ  1 
ATOM   6259 N  NH1 . ARG F  1 96  ? 18.461  16.227  67.243  1.00 93.92  ? 345  ARG F NH1 1 
ATOM   6260 N  NH2 . ARG F  1 96  ? 18.801  17.667  65.486  1.00 98.13  ? 345  ARG F NH2 1 
ATOM   6261 N  N   . GLY F  1 97  ? 13.436  18.606  70.736  1.00 40.31  ? 346  GLY F N   1 
ATOM   6262 C  CA  . GLY F  1 97  ? 12.038  18.572  71.131  1.00 41.37  ? 346  GLY F CA  1 
ATOM   6263 C  C   . GLY F  1 97  ? 11.773  18.823  72.617  1.00 41.06  ? 346  GLY F C   1 
ATOM   6264 O  O   . GLY F  1 97  ? 10.627  18.793  73.033  1.00 42.92  ? 346  GLY F O   1 
ATOM   6265 N  N   . GLU F  1 98  ? 12.821  19.081  73.413  1.00 39.86  ? 347  GLU F N   1 
ATOM   6266 C  CA  . GLU F  1 98  ? 12.683  19.371  74.860  1.00 37.62  ? 347  GLU F CA  1 
ATOM   6267 C  C   . GLU F  1 98  ? 13.076  20.838  75.149  1.00 36.85  ? 347  GLU F C   1 
ATOM   6268 O  O   . GLU F  1 98  ? 13.849  21.424  74.380  1.00 34.96  ? 347  GLU F O   1 
ATOM   6269 C  CB  . GLU F  1 98  ? 13.559  18.406  75.689  1.00 35.12  ? 347  GLU F CB  1 
ATOM   6270 C  CG  . GLU F  1 98  ? 13.402  16.918  75.316  1.00 34.36  ? 347  GLU F CG  1 
ATOM   6271 C  CD  . GLU F  1 98  ? 12.052  16.302  75.716  1.00 34.00  ? 347  GLU F CD  1 
ATOM   6272 O  OE1 . GLU F  1 98  ? 11.298  16.921  76.495  1.00 32.30  ? 347  GLU F OE1 1 
ATOM   6273 O  OE2 . GLU F  1 98  ? 11.744  15.178  75.275  1.00 35.84  ? 347  GLU F OE2 1 
ATOM   6274 N  N   . PRO F  1 99  ? 12.584  21.435  76.238  1.00 32.90  ? 348  PRO F N   1 
ATOM   6275 C  CA  . PRO F  1 99  ? 11.580  20.847  77.123  1.00 33.80  ? 348  PRO F CA  1 
ATOM   6276 C  C   . PRO F  1 99  ? 10.183  20.990  76.519  1.00 33.33  ? 348  PRO F C   1 
ATOM   6277 O  O   . PRO F  1 99  ? 9.864   22.061  76.038  1.00 35.49  ? 348  PRO F O   1 
ATOM   6278 C  CB  . PRO F  1 99  ? 11.682  21.703  78.381  1.00 32.47  ? 348  PRO F CB  1 
ATOM   6279 C  CG  . PRO F  1 99  ? 12.117  23.054  77.887  1.00 31.20  ? 348  PRO F CG  1 
ATOM   6280 C  CD  . PRO F  1 99  ? 12.947  22.809  76.636  1.00 32.36  ? 348  PRO F CD  1 
ATOM   6281 N  N   . ASN F  1 100 ? 9.389   19.913  76.548  1.00 29.55  ? 349  ASN F N   1 
ATOM   6282 C  CA  . ASN F  1 100 ? 8.044   19.876  75.994  1.00 30.85  ? 349  ASN F CA  1 
ATOM   6283 C  C   . ASN F  1 100 ? 6.891   19.836  77.024  1.00 30.50  ? 349  ASN F C   1 
ATOM   6284 O  O   . ASN F  1 100 ? 5.729   19.856  76.639  1.00 36.90  ? 349  ASN F O   1 
ATOM   6285 C  CB  . ASN F  1 100 ? 7.916   18.664  75.034  1.00 32.14  ? 349  ASN F CB  1 
ATOM   6286 C  CG  . ASN F  1 100 ? 8.158   17.318  75.722  1.00 33.77  ? 349  ASN F CG  1 
ATOM   6287 O  OD1 . ASN F  1 100 ? 8.474   17.252  76.930  1.00 33.06  ? 349  ASN F OD1 1 
ATOM   6288 N  ND2 . ASN F  1 100 ? 8.001   16.224  74.958  1.00 30.59  ? 349  ASN F ND2 1 
ATOM   6289 N  N   . ASN F  1 101 ? 7.191   19.739  78.312  1.00 28.43  ? 350  ASN F N   1 
ATOM   6290 C  CA  . ASN F  1 101 ? 6.146   19.797  79.346  1.00 30.35  ? 350  ASN F CA  1 
ATOM   6291 C  C   . ASN F  1 101 ? 5.018   18.795  79.087  1.00 30.07  ? 350  ASN F C   1 
ATOM   6292 O  O   . ASN F  1 101 ? 3.898   19.043  79.442  1.00 30.06  ? 350  ASN F O   1 
ATOM   6293 C  CB  . ASN F  1 101 ? 5.532   21.214  79.439  1.00 28.14  ? 350  ASN F CB  1 
ATOM   6294 C  CG  . ASN F  1 101 ? 4.811   21.422  80.735  1.00 29.24  ? 350  ASN F CG  1 
ATOM   6295 O  OD1 . ASN F  1 101 ? 5.365   21.141  81.785  1.00 33.64  ? 350  ASN F OD1 1 
ATOM   6296 N  ND2 . ASN F  1 101 ? 3.577   21.884  80.694  1.00 28.94  ? 350  ASN F ND2 1 
ATOM   6297 N  N   . VAL F  1 102 ? 5.323   17.652  78.497  1.00 30.70  ? 351  VAL F N   1 
ATOM   6298 C  CA  . VAL F  1 102 ? 4.277   16.729  78.081  1.00 30.21  ? 351  VAL F CA  1 
ATOM   6299 C  C   . VAL F  1 102 ? 3.657   15.990  79.298  1.00 31.90  ? 351  VAL F C   1 
ATOM   6300 O  O   . VAL F  1 102 ? 4.297   15.214  80.039  1.00 30.54  ? 351  VAL F O   1 
ATOM   6301 C  CB  . VAL F  1 102 ? 4.765   15.843  76.914  1.00 30.63  ? 351  VAL F CB  1 
ATOM   6302 C  CG1 . VAL F  1 102 ? 5.919   14.927  77.342  1.00 30.48  ? 351  VAL F CG1 1 
ATOM   6303 C  CG2 . VAL F  1 102 ? 3.624   15.086  76.241  1.00 27.85  ? 351  VAL F CG2 1 
ATOM   6304 N  N   . GLY F  1 103 ? 2.375   16.270  79.481  1.00 31.06  ? 352  GLY F N   1 
ATOM   6305 C  CA  . GLY F  1 103 ? 1.604   15.794  80.632  1.00 34.18  ? 352  GLY F CA  1 
ATOM   6306 C  C   . GLY F  1 103 ? 1.913   16.544  81.920  1.00 32.41  ? 352  GLY F C   1 
ATOM   6307 O  O   . GLY F  1 103 ? 1.477   16.125  83.019  1.00 34.94  ? 352  GLY F O   1 
ATOM   6308 N  N   . GLU F  1 104 ? 2.660   17.635  81.764  1.00 32.49  ? 353  GLU F N   1 
ATOM   6309 C  CA  . GLU F  1 104 ? 3.268   18.427  82.861  1.00 33.37  ? 353  GLU F CA  1 
ATOM   6310 C  C   . GLU F  1 104 ? 4.547   17.772  83.382  1.00 32.77  ? 353  GLU F C   1 
ATOM   6311 O  O   . GLU F  1 104 ? 4.518   16.794  84.103  1.00 34.67  ? 353  GLU F O   1 
ATOM   6312 C  CB  . GLU F  1 104 ? 2.305   18.715  84.014  1.00 34.41  ? 353  GLU F CB  1 
ATOM   6313 C  CG  . GLU F  1 104 ? 0.937   19.233  83.556  1.00 38.40  ? 353  GLU F CG  1 
ATOM   6314 C  CD  . GLU F  1 104 ? 0.233   20.093  84.622  1.00 47.50  ? 353  GLU F CD  1 
ATOM   6315 O  OE1 . GLU F  1 104 ? 0.309   19.766  85.845  1.00 41.53  ? 353  GLU F OE1 1 
ATOM   6316 O  OE2 . GLU F  1 104 ? -0.405  21.105  84.232  1.00 54.65  ? 353  GLU F OE2 1 
ATOM   6317 N  N   . GLU F  1 105 ? 5.675   18.355  83.007  1.00 30.38  ? 354  GLU F N   1 
ATOM   6318 C  CA  . GLU F  1 105 ? 6.973   17.854  83.374  1.00 27.90  ? 354  GLU F CA  1 
ATOM   6319 C  C   . GLU F  1 105 ? 7.688   19.086  83.822  1.00 28.05  ? 354  GLU F C   1 
ATOM   6320 O  O   . GLU F  1 105 ? 7.929   20.001  82.970  1.00 28.97  ? 354  GLU F O   1 
ATOM   6321 C  CB  . GLU F  1 105 ? 7.652   17.272  82.134  1.00 27.17  ? 354  GLU F CB  1 
ATOM   6322 C  CG  . GLU F  1 105 ? 6.924   16.069  81.587  1.00 28.62  ? 354  GLU F CG  1 
ATOM   6323 C  CD  . GLU F  1 105 ? 7.687   15.339  80.499  1.00 28.39  ? 354  GLU F CD  1 
ATOM   6324 O  OE1 . GLU F  1 105 ? 8.169   16.002  79.550  1.00 30.84  ? 354  GLU F OE1 1 
ATOM   6325 O  OE2 . GLU F  1 105 ? 7.831   14.097  80.613  1.00 29.27  ? 354  GLU F OE2 1 
ATOM   6326 N  N   . ASP F  1 106 ? 7.973   19.175  85.129  1.00 25.10  ? 355  ASP F N   1 
ATOM   6327 C  CA  . ASP F  1 106 ? 8.641   20.364  85.650  1.00 25.49  ? 355  ASP F CA  1 
ATOM   6328 C  C   . ASP F  1 106 ? 10.027  20.159  86.261  1.00 24.19  ? 355  ASP F C   1 
ATOM   6329 O  O   . ASP F  1 106 ? 10.542  21.074  86.887  1.00 22.97  ? 355  ASP F O   1 
ATOM   6330 C  CB  . ASP F  1 106 ? 7.760   21.064  86.684  1.00 24.92  ? 355  ASP F CB  1 
ATOM   6331 C  CG  . ASP F  1 106 ? 6.363   21.418  86.142  1.00 26.87  ? 355  ASP F CG  1 
ATOM   6332 O  OD1 . ASP F  1 106 ? 6.158   21.534  84.872  1.00 20.31  ? 355  ASP F OD1 1 
ATOM   6333 O  OD2 . ASP F  1 106 ? 5.494   21.649  87.047  1.00 22.38  ? 355  ASP F OD2 1 
ATOM   6334 N  N   . CYS F  1 107 ? 10.608  18.976  86.117  1.00 22.92  ? 356  CYS F N   1 
ATOM   6335 C  CA  . CYS F  1 107 ? 11.962  18.742  86.675  1.00 23.88  ? 356  CYS F CA  1 
ATOM   6336 C  C   . CYS F  1 107 ? 12.920  18.219  85.614  1.00 24.70  ? 356  CYS F C   1 
ATOM   6337 O  O   . CYS F  1 107 ? 12.556  17.370  84.763  1.00 23.10  ? 356  CYS F O   1 
ATOM   6338 C  CB  . CYS F  1 107 ? 11.878  17.786  87.838  1.00 22.51  ? 356  CYS F CB  1 
ATOM   6339 S  SG  . CYS F  1 107 ? 11.078  18.490  89.287  1.00 25.37  ? 356  CYS F SG  1 
ATOM   6340 N  N   . ALA F  1 108 ? 14.167  18.676  85.689  1.00 24.45  ? 357  ALA F N   1 
ATOM   6341 C  CA  . ALA F  1 108 ? 15.120  18.372  84.612  1.00 25.10  ? 357  ALA F CA  1 
ATOM   6342 C  C   . ALA F  1 108 ? 15.999  17.170  84.974  1.00 24.91  ? 357  ALA F C   1 
ATOM   6343 O  O   . ALA F  1 108 ? 16.402  16.998  86.122  1.00 23.88  ? 357  ALA F O   1 
ATOM   6344 C  CB  . ALA F  1 108 ? 15.974  19.601  84.295  1.00 25.20  ? 357  ALA F CB  1 
ATOM   6345 N  N   . GLU F  1 109 ? 16.304  16.356  83.969  1.00 25.59  ? 358  GLU F N   1 
ATOM   6346 C  CA  . GLU F  1 109 ? 17.060  15.119  84.136  1.00 27.52  ? 358  GLU F CA  1 
ATOM   6347 C  C   . GLU F  1 109 ? 18.093  15.022  83.043  1.00 26.93  ? 358  GLU F C   1 
ATOM   6348 O  O   . GLU F  1 109 ? 17.855  15.517  81.980  1.00 26.96  ? 358  GLU F O   1 
ATOM   6349 C  CB  . GLU F  1 109 ? 16.154  13.878  84.039  1.00 27.22  ? 358  GLU F CB  1 
ATOM   6350 C  CG  . GLU F  1 109 ? 15.234  13.817  82.819  1.00 28.68  ? 358  GLU F CG  1 
ATOM   6351 C  CD  . GLU F  1 109 ? 14.719  12.419  82.499  1.00 30.00  ? 358  GLU F CD  1 
ATOM   6352 O  OE1 . GLU F  1 109 ? 13.939  12.250  81.531  1.00 34.43  ? 358  GLU F OE1 1 
ATOM   6353 O  OE2 . GLU F  1 109 ? 15.096  11.462  83.207  1.00 33.06  ? 358  GLU F OE2 1 
ATOM   6354 N  N   . PHE F  1 110 ? 19.255  14.432  83.341  1.00 26.61  ? 359  PHE F N   1 
ATOM   6355 C  CA  . PHE F  1 110 ? 20.182  13.985  82.302  1.00 26.00  ? 359  PHE F CA  1 
ATOM   6356 C  C   . PHE F  1 110 ? 19.561  12.712  81.786  1.00 25.38  ? 359  PHE F C   1 
ATOM   6357 O  O   . PHE F  1 110 ? 19.157  11.836  82.543  1.00 26.35  ? 359  PHE F O   1 
ATOM   6358 C  CB  . PHE F  1 110 ? 21.570  13.676  82.835  1.00 26.25  ? 359  PHE F CB  1 
ATOM   6359 C  CG  . PHE F  1 110 ? 22.173  14.787  83.653  1.00 28.33  ? 359  PHE F CG  1 
ATOM   6360 C  CD1 . PHE F  1 110 ? 22.935  15.773  83.056  1.00 30.36  ? 359  PHE F CD1 1 
ATOM   6361 C  CD2 . PHE F  1 110 ? 21.974  14.848  85.003  1.00 27.62  ? 359  PHE F CD2 1 
ATOM   6362 C  CE1 . PHE F  1 110 ? 23.466  16.795  83.806  1.00 27.56  ? 359  PHE F CE1 1 
ATOM   6363 C  CE2 . PHE F  1 110 ? 22.522  15.844  85.752  1.00 27.38  ? 359  PHE F CE2 1 
ATOM   6364 C  CZ  . PHE F  1 110 ? 23.267  16.819  85.158  1.00 27.68  ? 359  PHE F CZ  1 
ATOM   6365 N  N   . SER F  1 111 ? 19.425  12.659  80.478  1.00 31.08  ? 360  SER F N   1 
ATOM   6366 C  CA  . SER F  1 111 ? 18.728  11.603  79.790  1.00 32.87  ? 360  SER F CA  1 
ATOM   6367 C  C   . SER F  1 111 ? 19.421  11.398  78.437  1.00 34.46  ? 360  SER F C   1 
ATOM   6368 O  O   . SER F  1 111 ? 19.201  12.154  77.496  1.00 32.78  ? 360  SER F O   1 
ATOM   6369 C  CB  . SER F  1 111 ? 17.249  11.982  79.621  1.00 33.63  ? 360  SER F CB  1 
ATOM   6370 O  OG  . SER F  1 111 ? 16.530  10.919  79.004  1.00 34.58  ? 360  SER F OG  1 
ATOM   6371 N  N   . GLY F  1 112 ? 20.266  10.365  78.376  1.00 36.62  ? 361  GLY F N   1 
ATOM   6372 C  CA  . GLY F  1 112 ? 21.076  10.061  77.208  1.00 34.72  ? 361  GLY F CA  1 
ATOM   6373 C  C   . GLY F  1 112 ? 22.184  11.073  77.036  1.00 35.90  ? 361  GLY F C   1 
ATOM   6374 O  O   . GLY F  1 112 ? 23.048  11.217  77.913  1.00 32.74  ? 361  GLY F O   1 
ATOM   6375 N  N   . ASN F  1 113 ? 22.157  11.790  75.916  1.00 36.47  ? 362  ASN F N   1 
ATOM   6376 C  CA  . ASN F  1 113 ? 23.208  12.795  75.637  1.00 37.67  ? 362  ASN F CA  1 
ATOM   6377 C  C   . ASN F  1 113 ? 22.860  14.236  76.032  1.00 34.11  ? 362  ASN F C   1 
ATOM   6378 O  O   . ASN F  1 113 ? 23.720  15.076  76.070  1.00 38.69  ? 362  ASN F O   1 
ATOM   6379 C  CB  . ASN F  1 113 ? 23.634  12.731  74.173  1.00 40.64  ? 362  ASN F CB  1 
ATOM   6380 C  CG  . ASN F  1 113 ? 24.274  11.401  73.832  1.00 41.19  ? 362  ASN F CG  1 
ATOM   6381 O  OD1 . ASN F  1 113 ? 23.852  10.729  72.915  1.00 39.06  ? 362  ASN F OD1 1 
ATOM   6382 N  ND2 . ASN F  1 113 ? 25.261  10.996  74.625  1.00 44.32  ? 362  ASN F ND2 1 
ATOM   6383 N  N   . GLY F  1 114 ? 21.618  14.518  76.376  1.00 33.74  ? 363  GLY F N   1 
ATOM   6384 C  CA  . GLY F  1 114 ? 21.289  15.838  76.858  1.00 32.95  ? 363  GLY F CA  1 
ATOM   6385 C  C   . GLY F  1 114 ? 20.341  15.786  78.017  1.00 34.49  ? 363  GLY F C   1 
ATOM   6386 O  O   . GLY F  1 114 ? 20.353  14.836  78.832  1.00 31.01  ? 363  GLY F O   1 
ATOM   6387 N  N   . TRP F  1 115 ? 19.518  16.831  78.071  1.00 34.54  ? 364  TRP F N   1 
ATOM   6388 C  CA  . TRP F  1 115 ? 18.582  17.030  79.136  1.00 31.39  ? 364  TRP F CA  1 
ATOM   6389 C  C   . TRP F  1 115 ? 17.181  16.771  78.614  1.00 30.88  ? 364  TRP F C   1 
ATOM   6390 O  O   . TRP F  1 115 ? 16.907  16.957  77.442  1.00 27.19  ? 364  TRP F O   1 
ATOM   6391 C  CB  . TRP F  1 115 ? 18.638  18.459  79.623  1.00 33.27  ? 364  TRP F CB  1 
ATOM   6392 C  CG  . TRP F  1 115 ? 19.952  18.930  80.143  1.00 32.97  ? 364  TRP F CG  1 
ATOM   6393 C  CD1 . TRP F  1 115 ? 21.126  18.204  80.328  1.00 30.39  ? 364  TRP F CD1 1 
ATOM   6394 C  CD2 . TRP F  1 115 ? 20.209  20.244  80.610  1.00 31.43  ? 364  TRP F CD2 1 
ATOM   6395 N  NE1 . TRP F  1 115 ? 22.089  19.033  80.874  1.00 30.96  ? 364  TRP F NE1 1 
ATOM   6396 C  CE2 . TRP F  1 115 ? 21.549  20.288  81.040  1.00 32.48  ? 364  TRP F CE2 1 
ATOM   6397 C  CE3 . TRP F  1 115 ? 19.432  21.406  80.688  1.00 34.19  ? 364  TRP F CE3 1 
ATOM   6398 C  CZ2 . TRP F  1 115 ? 22.127  21.457  81.525  1.00 34.86  ? 364  TRP F CZ2 1 
ATOM   6399 C  CZ3 . TRP F  1 115 ? 20.008  22.566  81.193  1.00 34.79  ? 364  TRP F CZ3 1 
ATOM   6400 C  CH2 . TRP F  1 115 ? 21.332  22.581  81.609  1.00 34.47  ? 364  TRP F CH2 1 
ATOM   6401 N  N   . ASN F  1 116 ? 16.315  16.336  79.530  1.00 28.64  ? 365  ASN F N   1 
ATOM   6402 C  CA  . ASN F  1 116 ? 14.916  16.198  79.284  1.00 28.14  ? 365  ASN F CA  1 
ATOM   6403 C  C   . ASN F  1 116 ? 14.180  16.724  80.514  1.00 29.69  ? 365  ASN F C   1 
ATOM   6404 O  O   . ASN F  1 116 ? 14.699  16.667  81.614  1.00 27.31  ? 365  ASN F O   1 
ATOM   6405 C  CB  . ASN F  1 116 ? 14.531  14.721  79.044  1.00 26.00  ? 365  ASN F CB  1 
ATOM   6406 C  CG  . ASN F  1 116 ? 13.036  14.534  78.954  1.00 27.03  ? 365  ASN F CG  1 
ATOM   6407 O  OD1 . ASN F  1 116 ? 12.360  15.373  78.394  1.00 26.27  ? 365  ASN F OD1 1 
ATOM   6408 N  ND2 . ASN F  1 116 ? 12.500  13.514  79.614  1.00 27.27  ? 365  ASN F ND2 1 
ATOM   6409 N  N   . ASP F  1 117 ? 12.971  17.234  80.301  1.00 28.75  ? 366  ASP F N   1 
ATOM   6410 C  CA  . ASP F  1 117 ? 12.042  17.447  81.391  1.00 30.97  ? 366  ASP F CA  1 
ATOM   6411 C  C   . ASP F  1 117 ? 11.151  16.229  81.555  1.00 28.00  ? 366  ASP F C   1 
ATOM   6412 O  O   . ASP F  1 117 ? 10.669  15.675  80.571  1.00 31.50  ? 366  ASP F O   1 
ATOM   6413 C  CB  . ASP F  1 117 ? 11.212  18.747  81.230  1.00 31.37  ? 366  ASP F CB  1 
ATOM   6414 C  CG  . ASP F  1 117 ? 10.375  18.808  79.956  1.00 29.13  ? 366  ASP F CG  1 
ATOM   6415 O  OD1 . ASP F  1 117 ? 10.659  18.116  78.986  1.00 27.91  ? 366  ASP F OD1 1 
ATOM   6416 O  OD2 . ASP F  1 117 ? 9.396   19.584  79.943  1.00 30.19  ? 366  ASP F OD2 1 
ATOM   6417 N  N   . ASP F  1 118 ? 10.923  15.873  82.809  1.00 27.55  ? 367  ASP F N   1 
ATOM   6418 C  CA  . ASP F  1 118 ? 10.144  14.726  83.197  1.00 26.27  ? 367  ASP F CA  1 
ATOM   6419 C  C   . ASP F  1 118 ? 9.377   15.048  84.478  1.00 27.02  ? 367  ASP F C   1 
ATOM   6420 O  O   . ASP F  1 118 ? 9.518   16.103  85.071  1.00 22.90  ? 367  ASP F O   1 
ATOM   6421 C  CB  . ASP F  1 118 ? 11.054  13.497  83.403  1.00 27.23  ? 367  ASP F CB  1 
ATOM   6422 C  CG  . ASP F  1 118 ? 10.342  12.155  83.120  1.00 27.26  ? 367  ASP F CG  1 
ATOM   6423 O  OD1 . ASP F  1 118 ? 9.115   12.137  82.939  1.00 25.09  ? 367  ASP F OD1 1 
ATOM   6424 O  OD2 . ASP F  1 118 ? 11.004  11.099  83.121  1.00 31.46  ? 367  ASP F OD2 1 
ATOM   6425 N  N   . LYS F  1 119 ? 8.507   14.123  84.835  1.00 27.78  ? 368  LYS F N   1 
ATOM   6426 C  CA  . LYS F  1 119 ? 7.634   14.237  85.981  1.00 30.95  ? 368  LYS F CA  1 
ATOM   6427 C  C   . LYS F  1 119 ? 8.418   14.190  87.266  1.00 28.94  ? 368  LYS F C   1 
ATOM   6428 O  O   . LYS F  1 119 ? 9.177   13.231  87.521  1.00 25.93  ? 368  LYS F O   1 
ATOM   6429 C  CB  . LYS F  1 119 ? 6.600   13.117  85.928  1.00 33.42  ? 368  LYS F CB  1 
ATOM   6430 C  CG  . LYS F  1 119 ? 5.541   13.394  84.891  1.00 37.56  ? 368  LYS F CG  1 
ATOM   6431 C  CD  . LYS F  1 119 ? 4.599   12.233  84.662  1.00 47.44  ? 368  LYS F CD  1 
ATOM   6432 C  CE  . LYS F  1 119 ? 4.108   12.244  83.218  1.00 56.97  ? 368  LYS F CE  1 
ATOM   6433 N  NZ  . LYS F  1 119 ? 3.769   13.612  82.674  1.00 58.19  ? 368  LYS F NZ  1 
ATOM   6434 N  N   . CYS F  1 120 ? 8.219   15.237  88.075  1.00 29.80  ? 369  CYS F N   1 
ATOM   6435 C  CA  . CYS F  1 120 ? 8.966   15.446  89.302  1.00 26.92  ? 369  CYS F CA  1 
ATOM   6436 C  C   . CYS F  1 120 ? 8.751   14.296  90.302  1.00 28.10  ? 369  CYS F C   1 
ATOM   6437 O  O   . CYS F  1 120 ? 9.593   14.041  91.193  1.00 26.76  ? 369  CYS F O   1 
ATOM   6438 C  CB  . CYS F  1 120 ? 8.587   16.802  89.915  1.00 26.70  ? 369  CYS F CB  1 
ATOM   6439 S  SG  . CYS F  1 120 ? 9.076   18.270  88.953  1.00 26.92  ? 369  CYS F SG  1 
ATOM   6440 N  N   . ASN F  1 121 ? 7.642   13.580  90.161  1.00 25.39  ? 370  ASN F N   1 
ATOM   6441 C  CA  . ASN F  1 121 ? 7.273   12.564  91.176  1.00 26.73  ? 370  ASN F CA  1 
ATOM   6442 C  C   . ASN F  1 121 ? 7.885   11.213  90.857  1.00 25.09  ? 370  ASN F C   1 
ATOM   6443 O  O   . ASN F  1 121 ? 7.735   10.275  91.631  1.00 24.63  ? 370  ASN F O   1 
ATOM   6444 C  CB  . ASN F  1 121 ? 5.750   12.425  91.314  1.00 29.21  ? 370  ASN F CB  1 
ATOM   6445 C  CG  . ASN F  1 121 ? 5.068   12.165  89.970  1.00 35.73  ? 370  ASN F CG  1 
ATOM   6446 O  OD1 . ASN F  1 121 ? 5.136   12.998  89.042  1.00 43.30  ? 370  ASN F OD1 1 
ATOM   6447 N  ND2 . ASN F  1 121 ? 4.430   11.013  89.844  1.00 41.54  ? 370  ASN F ND2 1 
ATOM   6448 N  N   . LEU F  1 122 ? 8.595   11.111  89.733  1.00 22.70  ? 371  LEU F N   1 
ATOM   6449 C  CA  . LEU F  1 122 ? 9.251   9.868   89.396  1.00 23.71  ? 371  LEU F CA  1 
ATOM   6450 C  C   . LEU F  1 122 ? 10.623  9.732   90.081  1.00 25.94  ? 371  LEU F C   1 
ATOM   6451 O  O   . LEU F  1 122 ? 11.267  10.713  90.463  1.00 26.21  ? 371  LEU F O   1 
ATOM   6452 C  CB  . LEU F  1 122 ? 9.378   9.705   87.875  1.00 23.03  ? 371  LEU F CB  1 
ATOM   6453 C  CG  . LEU F  1 122 ? 8.044   9.630   87.084  1.00 23.66  ? 371  LEU F CG  1 
ATOM   6454 C  CD1 . LEU F  1 122 ? 8.299   9.699   85.580  1.00 23.84  ? 371  LEU F CD1 1 
ATOM   6455 C  CD2 . LEU F  1 122 ? 7.214   8.401   87.458  1.00 24.69  ? 371  LEU F CD2 1 
ATOM   6456 N  N   . ALA F  1 123 ? 11.019  8.482   90.270  1.00 26.66  ? 372  ALA F N   1 
ATOM   6457 C  CA  . ALA F  1 123 ? 12.277  8.139   90.908  1.00 26.94  ? 372  ALA F CA  1 
ATOM   6458 C  C   . ALA F  1 123 ? 13.394  8.030   89.873  1.00 28.75  ? 372  ALA F C   1 
ATOM   6459 O  O   . ALA F  1 123 ? 13.274  7.318   88.862  1.00 29.37  ? 372  ALA F O   1 
ATOM   6460 C  CB  . ALA F  1 123 ? 12.131  6.850   91.651  1.00 25.57  ? 372  ALA F CB  1 
ATOM   6461 N  N   . LYS F  1 124 ? 14.456  8.780   90.124  1.00 26.88  ? 373  LYS F N   1 
ATOM   6462 C  CA  . LYS F  1 124 ? 15.630  8.737   89.291  1.00 27.21  ? 373  LYS F CA  1 
ATOM   6463 C  C   . LYS F  1 124 ? 16.861  8.796   90.230  1.00 28.57  ? 373  LYS F C   1 
ATOM   6464 O  O   . LYS F  1 124 ? 16.750  9.082   91.444  1.00 23.25  ? 373  LYS F O   1 
ATOM   6465 C  CB  . LYS F  1 124 ? 15.626  9.946   88.377  1.00 25.64  ? 373  LYS F CB  1 
ATOM   6466 C  CG  . LYS F  1 124 ? 14.410  10.071  87.487  1.00 26.87  ? 373  LYS F CG  1 
ATOM   6467 C  CD  . LYS F  1 124 ? 14.586  11.254  86.527  1.00 27.11  ? 373  LYS F CD  1 
ATOM   6468 C  CE  . LYS F  1 124 ? 13.399  11.476  85.668  1.00 28.09  ? 373  LYS F CE  1 
ATOM   6469 N  NZ  . LYS F  1 124 ? 13.275  10.405  84.646  1.00 32.90  ? 373  LYS F NZ  1 
ATOM   6470 N  N   . PHE F  1 125 ? 18.033  8.549   89.662  1.00 26.41  ? 374  PHE F N   1 
ATOM   6471 C  CA  . PHE F  1 125 ? 19.296  8.757   90.410  1.00 25.65  ? 374  PHE F CA  1 
ATOM   6472 C  C   . PHE F  1 125 ? 19.459  10.260  90.561  1.00 25.29  ? 374  PHE F C   1 
ATOM   6473 O  O   . PHE F  1 125 ? 18.752  11.029  89.913  1.00 23.69  ? 374  PHE F O   1 
ATOM   6474 C  CB  . PHE F  1 125 ? 20.480  8.128   89.665  1.00 25.36  ? 374  PHE F CB  1 
ATOM   6475 C  CG  . PHE F  1 125 ? 20.369  6.645   89.588  1.00 26.85  ? 374  PHE F CG  1 
ATOM   6476 C  CD1 . PHE F  1 125 ? 19.602  6.049   88.597  1.00 26.15  ? 374  PHE F CD1 1 
ATOM   6477 C  CD2 . PHE F  1 125 ? 20.975  5.836   90.576  1.00 29.23  ? 374  PHE F CD2 1 
ATOM   6478 C  CE1 . PHE F  1 125 ? 19.477  4.674   88.544  1.00 29.39  ? 374  PHE F CE1 1 
ATOM   6479 C  CE2 . PHE F  1 125 ? 20.840  4.466   90.533  1.00 30.52  ? 374  PHE F CE2 1 
ATOM   6480 C  CZ  . PHE F  1 125 ? 20.084  3.880   89.519  1.00 31.38  ? 374  PHE F CZ  1 
ATOM   6481 N  N   . TRP F  1 126 ? 20.338  10.665  91.467  1.00 24.88  ? 375  TRP F N   1 
ATOM   6482 C  CA  . TRP F  1 126 ? 20.569  12.059  91.689  1.00 27.65  ? 375  TRP F CA  1 
ATOM   6483 C  C   . TRP F  1 126 ? 22.047  12.291  92.006  1.00 26.92  ? 375  TRP F C   1 
ATOM   6484 O  O   . TRP F  1 126 ? 22.767  11.364  92.358  1.00 25.35  ? 375  TRP F O   1 
ATOM   6485 C  CB  . TRP F  1 126 ? 19.649  12.558  92.810  1.00 29.27  ? 375  TRP F CB  1 
ATOM   6486 C  CG  . TRP F  1 126 ? 20.058  12.139  94.116  1.00 30.79  ? 375  TRP F CG  1 
ATOM   6487 C  CD1 . TRP F  1 126 ? 20.934  12.796  94.945  1.00 33.09  ? 375  TRP F CD1 1 
ATOM   6488 C  CD2 . TRP F  1 126 ? 19.662  10.952  94.809  1.00 30.43  ? 375  TRP F CD2 1 
ATOM   6489 N  NE1 . TRP F  1 126 ? 21.098  12.082  96.109  1.00 32.31  ? 375  TRP F NE1 1 
ATOM   6490 C  CE2 . TRP F  1 126 ? 20.332  10.952  96.054  1.00 30.89  ? 375  TRP F CE2 1 
ATOM   6491 C  CE3 . TRP F  1 126 ? 18.828  9.903   94.503  1.00 30.61  ? 375  TRP F CE3 1 
ATOM   6492 C  CZ2 . TRP F  1 126 ? 20.172  9.937   96.996  1.00 34.26  ? 375  TRP F CZ2 1 
ATOM   6493 C  CZ3 . TRP F  1 126 ? 18.660  8.903   95.429  1.00 32.85  ? 375  TRP F CZ3 1 
ATOM   6494 C  CH2 . TRP F  1 126 ? 19.338  8.912   96.659  1.00 34.98  ? 375  TRP F CH2 1 
ATOM   6495 N  N   . ILE F  1 127 ? 22.472  13.542  91.869  1.00 25.86  ? 376  ILE F N   1 
ATOM   6496 C  CA  . ILE F  1 127 ? 23.843  13.932  92.092  1.00 25.49  ? 376  ILE F CA  1 
ATOM   6497 C  C   . ILE F  1 127 ? 23.789  15.152  92.964  1.00 26.95  ? 376  ILE F C   1 
ATOM   6498 O  O   . ILE F  1 127 ? 23.071  16.094  92.638  1.00 30.35  ? 376  ILE F O   1 
ATOM   6499 C  CB  . ILE F  1 127 ? 24.543  14.288  90.765  1.00 24.15  ? 376  ILE F CB  1 
ATOM   6500 C  CG1 . ILE F  1 127 ? 24.870  13.044  89.972  1.00 23.91  ? 376  ILE F CG1 1 
ATOM   6501 C  CG2 . ILE F  1 127 ? 25.850  15.012  91.033  1.00 25.51  ? 376  ILE F CG2 1 
ATOM   6502 C  CD1 . ILE F  1 127 ? 25.280  13.343  88.534  1.00 24.83  ? 376  ILE F CD1 1 
ATOM   6503 N  N   . CYS F  1 128 ? 24.551  15.136  94.043  1.00 27.69  ? 377  CYS F N   1 
ATOM   6504 C  CA  . CYS F  1 128 ? 24.738  16.301  94.906  1.00 31.98  ? 377  CYS F CA  1 
ATOM   6505 C  C   . CYS F  1 128 ? 26.105  16.952  94.629  1.00 31.86  ? 377  CYS F C   1 
ATOM   6506 O  O   . CYS F  1 128 ? 27.086  16.270  94.276  1.00 29.99  ? 377  CYS F O   1 
ATOM   6507 C  CB  . CYS F  1 128 ? 24.746  15.924  96.388  1.00 29.47  ? 377  CYS F CB  1 
ATOM   6508 S  SG  . CYS F  1 128 ? 23.383  14.936  96.981  1.00 32.68  ? 377  CYS F SG  1 
ATOM   6509 N  N   . LYS F  1 129 ? 26.151  18.251  94.860  1.00 31.69  ? 378  LYS F N   1 
ATOM   6510 C  CA  . LYS F  1 129 ? 27.376  19.041  94.761  1.00 34.20  ? 378  LYS F CA  1 
ATOM   6511 C  C   . LYS F  1 129 ? 27.505  19.872  96.000  1.00 36.05  ? 378  LYS F C   1 
ATOM   6512 O  O   . LYS F  1 129 ? 26.495  20.382  96.511  1.00 31.84  ? 378  LYS F O   1 
ATOM   6513 C  CB  . LYS F  1 129 ? 27.330  19.950  93.527  1.00 34.98  ? 378  LYS F CB  1 
ATOM   6514 C  CG  . LYS F  1 129 ? 28.316  21.124  93.436  1.00 34.60  ? 378  LYS F CG  1 
ATOM   6515 C  CD  . LYS F  1 129 ? 28.028  21.842  92.126  1.00 37.52  ? 378  LYS F CD  1 
ATOM   6516 C  CE  . LYS F  1 129 ? 28.874  23.079  91.814  1.00 39.42  ? 378  LYS F CE  1 
ATOM   6517 N  NZ  . LYS F  1 129 ? 28.399  23.662  90.514  1.00 40.29  ? 378  LYS F NZ  1 
ATOM   6518 N  N   . LYS F  1 130 ? 28.751  19.946  96.486  1.00 37.89  ? 379  LYS F N   1 
ATOM   6519 C  CA  . LYS F  1 130 ? 29.218  20.981  97.398  1.00 40.15  ? 379  LYS F CA  1 
ATOM   6520 C  C   . LYS F  1 130 ? 30.671  21.366  97.116  1.00 44.38  ? 379  LYS F C   1 
ATOM   6521 O  O   . LYS F  1 130 ? 31.387  20.684  96.357  1.00 38.91  ? 379  LYS F O   1 
ATOM   6522 C  CB  . LYS F  1 130 ? 29.051  20.559  98.847  1.00 42.89  ? 379  LYS F CB  1 
ATOM   6523 C  CG  . LYS F  1 130 ? 29.870  19.377  99.280  1.00 42.90  ? 379  LYS F CG  1 
ATOM   6524 C  CD  . LYS F  1 130 ? 29.323  18.894  100.610 1.00 44.88  ? 379  LYS F CD  1 
ATOM   6525 C  CE  . LYS F  1 130 ? 30.185  17.798  101.188 1.00 50.51  ? 379  LYS F CE  1 
ATOM   6526 N  NZ  . LYS F  1 130 ? 29.630  17.239  102.461 1.00 56.99  ? 379  LYS F NZ  1 
ATOM   6527 N  N   . SER F  1 131 ? 31.078  22.503  97.688  1.00 48.18  ? 380  SER F N   1 
ATOM   6528 C  CA  . SER F  1 131 ? 32.461  23.013  97.591  1.00 47.30  ? 380  SER F CA  1 
ATOM   6529 C  C   . SER F  1 131 ? 33.528  22.033  98.057  1.00 44.85  ? 380  SER F C   1 
ATOM   6530 O  O   . SER F  1 131 ? 33.337  21.346  99.064  1.00 42.94  ? 380  SER F O   1 
ATOM   6531 C  CB  . SER F  1 131 ? 32.609  24.248  98.477  1.00 49.70  ? 380  SER F CB  1 
ATOM   6532 O  OG  . SER F  1 131 ? 32.186  25.377  97.778  1.00 54.04  ? 380  SER F OG  1 
ATOM   6533 N  N   . ALA F  1 132 ? 34.669  22.001  97.367  1.00 44.80  ? 381  ALA F N   1 
ATOM   6534 C  CA  . ALA F  1 132 ? 35.865  21.344  97.935  1.00 48.44  ? 381  ALA F CA  1 
ATOM   6535 C  C   . ALA F  1 132 ? 36.337  22.094  99.186  1.00 49.55  ? 381  ALA F C   1 
ATOM   6536 O  O   . ALA F  1 132 ? 36.079  23.275  99.329  1.00 51.41  ? 381  ALA F O   1 
ATOM   6537 C  CB  . ALA F  1 132 ? 36.978  21.261  96.900  1.00 47.79  ? 381  ALA F CB  1 
ATOM   6538 N  N   . ALA F  1 133 ? 36.974  21.388  100.120 1.00 61.61  ? 382  ALA F N   1 
ATOM   6539 C  CA  . ALA F  1 133 ? 37.790  22.032  101.184 1.00 62.45  ? 382  ALA F CA  1 
ATOM   6540 C  C   . ALA F  1 133 ? 39.184  22.387  100.631 1.00 64.21  ? 382  ALA F C   1 
ATOM   6541 O  O   . ALA F  1 133 ? 39.650  21.764  99.678  1.00 61.27  ? 382  ALA F O   1 
ATOM   6542 C  CB  . ALA F  1 133 ? 37.914  21.112  102.388 1.00 61.95  ? 382  ALA F CB  1 
ATOM   6543 N  N   . SER F  1 134 ? 39.849  23.383  101.209 1.00 77.16  ? 383  SER F N   1 
ATOM   6544 C  CA  . SER F  1 134 ? 41.220  23.736  100.762 1.00 80.08  ? 383  SER F CA  1 
ATOM   6545 C  C   . SER F  1 134 ? 42.313  22.929  101.478 1.00 81.28  ? 383  SER F C   1 
ATOM   6546 O  O   . SER F  1 134 ? 42.257  22.750  102.698 1.00 74.20  ? 383  SER F O   1 
ATOM   6547 C  CB  . SER F  1 134 ? 41.485  25.238  100.880 1.00 79.11  ? 383  SER F CB  1 
ATOM   6548 O  OG  . SER F  1 134 ? 41.166  25.875  99.655  1.00 77.94  ? 383  SER F OG  1 
ATOM   6549 N  N   . CYS F  1 135 ? 43.268  22.417  100.688 1.00 86.43  ? 384  CYS F N   1 
ATOM   6550 C  CA  . CYS F  1 135 ? 44.489  21.747  101.189 1.00 89.40  ? 384  CYS F CA  1 
ATOM   6551 C  C   . CYS F  1 135 ? 45.672  22.071  100.258 1.00 80.96  ? 384  CYS F C   1 
ATOM   6552 O  O   . CYS F  1 135 ? 46.665  22.681  100.672 1.00 77.82  ? 384  CYS F O   1 
ATOM   6553 C  CB  . CYS F  1 135 ? 44.323  20.211  101.298 1.00 86.75  ? 384  CYS F CB  1 
ATOM   6554 S  SG  . CYS F  1 135 ? 42.725  19.541  101.851 1.00 85.51  ? 384  CYS F SG  1 
HETATM 6555 C  C4  . EZ8 G  2 .   ? 11.482  -6.710  15.963  1.00 30.75  ? 1001 EZ8 A C4  1 
HETATM 6556 C  C5  . EZ8 G  2 .   ? 12.563  -7.787  15.836  1.00 29.78  ? 1001 EZ8 A C5  1 
HETATM 6557 C  C6  . EZ8 G  2 .   ? 13.220  -7.891  17.157  1.00 31.49  ? 1001 EZ8 A C6  1 
HETATM 6558 N  N2  . EZ8 G  2 .   ? 9.219   -8.559  15.604  1.00 27.44  ? 1001 EZ8 A N2  1 
HETATM 6559 C  C3  . EZ8 G  2 .   ? 10.588  -6.752  14.722  1.00 29.48  ? 1001 EZ8 A C3  1 
HETATM 6560 C  CAP . EZ8 G  2 .   ? 8.674   -14.311 9.107   1.00 59.26  ? 1001 EZ8 A CAP 1 
HETATM 6561 C  CAL . EZ8 G  2 .   ? 8.310   -15.457 9.809   1.00 53.05  ? 1001 EZ8 A CAL 1 
HETATM 6562 C  CBM . EZ8 G  2 .   ? 9.235   -16.392 10.206  1.00 56.33  ? 1001 EZ8 A CBM 1 
HETATM 6563 C  CAV . EZ8 G  2 .   ? 8.780   -17.491 10.927  1.00 60.31  ? 1001 EZ8 A CAV 1 
HETATM 6564 O  OAE . EZ8 G  2 .   ? 9.327   -18.696 10.414  1.00 61.35  ? 1001 EZ8 A OAE 1 
HETATM 6565 C  CAM . EZ8 G  2 .   ? 10.577  -16.152 9.906   1.00 57.92  ? 1001 EZ8 A CAM 1 
HETATM 6566 C  CAQ . EZ8 G  2 .   ? 10.957  -15.000 9.195   1.00 58.75  ? 1001 EZ8 A CAQ 1 
HETATM 6567 C  CBO . EZ8 G  2 .   ? 10.009  -14.048 8.804   1.00 55.99  ? 1001 EZ8 A CBO 1 
HETATM 6568 C  CAZ . EZ8 G  2 .   ? 10.331  -12.890 8.114   1.00 50.64  ? 1001 EZ8 A CAZ 1 
HETATM 6569 N  NBF . EZ8 G  2 .   ? 11.014  -11.937 9.031   1.00 48.22  ? 1001 EZ8 A NBF 1 
HETATM 6570 C  CBK . EZ8 G  2 .   ? 10.430  -10.921 9.736   1.00 40.55  ? 1001 EZ8 A CBK 1 
HETATM 6571 O  OAC . EZ8 G  2 .   ? 9.213   -10.667 9.703   1.00 41.94  ? 1001 EZ8 A OAC 1 
HETATM 6572 C  CBW . EZ8 G  2 .   ? 11.398  -10.073 10.601  1.00 35.06  ? 1001 EZ8 A CBW 1 
HETATM 6573 C  CBB . EZ8 G  2 .   ? 11.825  -10.843 11.767  1.00 35.72  ? 1001 EZ8 A CBB 1 
HETATM 6574 C  CBV . EZ8 G  2 .   ? 12.647  -9.563  9.836   1.00 34.28  ? 1001 EZ8 A CBV 1 
HETATM 6575 C  CBJ . EZ8 G  2 .   ? 12.197  -8.689  8.666   1.00 34.17  ? 1001 EZ8 A CBJ 1 
HETATM 6576 O  OAB . EZ8 G  2 .   ? 11.454  -7.742  8.898   1.00 31.54  ? 1001 EZ8 A OAB 1 
HETATM 6577 N  NBE . EZ8 G  2 .   ? 12.707  -8.912  7.420   1.00 34.10  ? 1001 EZ8 A NBE 1 
HETATM 6578 C  CAY . EZ8 G  2 .   ? 12.237  -8.092  6.260   1.00 33.18  ? 1001 EZ8 A CAY 1 
HETATM 6579 C  CBN . EZ8 G  2 .   ? 13.079  -7.015  5.886   1.00 35.30  ? 1001 EZ8 A CBN 1 
HETATM 6580 C  CAN . EZ8 G  2 .   ? 13.905  -6.366  6.804   1.00 38.14  ? 1001 EZ8 A CAN 1 
HETATM 6581 C  CAJ . EZ8 G  2 .   ? 14.757  -5.324  6.419   1.00 34.68  ? 1001 EZ8 A CAJ 1 
HETATM 6582 C  CBL . EZ8 G  2 .   ? 14.797  -4.905  5.099   1.00 38.91  ? 1001 EZ8 A CBL 1 
HETATM 6583 C  CAU . EZ8 G  2 .   ? 15.685  -3.880  4.725   1.00 41.47  ? 1001 EZ8 A CAU 1 
HETATM 6584 O  OAD . EZ8 G  2 .   ? 14.949  -2.706  4.453   1.00 50.35  ? 1001 EZ8 A OAD 1 
HETATM 6585 C  CAK . EZ8 G  2 .   ? 13.974  -5.559  4.158   1.00 36.39  ? 1001 EZ8 A CAK 1 
HETATM 6586 C  CAO . EZ8 G  2 .   ? 13.127  -6.593  4.551   1.00 34.98  ? 1001 EZ8 A CAO 1 
HETATM 6587 C  CBA . EZ8 G  2 .   ? 13.427  -8.661  10.677  1.00 33.09  ? 1001 EZ8 A CBA 1 
HETATM 6588 C  CBT . EZ8 G  2 .   ? 13.875  -9.334  11.918  1.00 36.35  ? 1001 EZ8 A CBT 1 
HETATM 6589 O  OBG . EZ8 G  2 .   ? 14.917  -10.360 11.664  1.00 39.68  ? 1001 EZ8 A OBG 1 
HETATM 6590 C  CAX . EZ8 G  2 .   ? 15.801  -10.428 12.770  1.00 43.18  ? 1001 EZ8 A CAX 1 
HETATM 6591 C  CAT . EZ8 G  2 .   ? 16.498  -11.792 12.723  1.00 48.49  ? 1001 EZ8 A CAT 1 
HETATM 6592 CL CL1 . EZ8 G  2 .   ? 15.346  -13.117 12.262  1.00 57.77  ? 1001 EZ8 A CL1 1 
HETATM 6593 C  CBU . EZ8 G  2 .   ? 12.643  -9.942  12.679  1.00 35.33  ? 1001 EZ8 A CBU 1 
HETATM 6594 O  O1  . EZ8 G  2 .   ? 11.837  -8.873  13.152  1.00 33.49  ? 1001 EZ8 A O1  1 
HETATM 6595 C  C1  . EZ8 G  2 .   ? 11.133  -9.132  14.421  1.00 30.23  ? 1001 EZ8 A C1  1 
HETATM 6596 O  O5  . EZ8 G  2 .   ? 11.972  -9.064  15.583  1.00 26.40  ? 1001 EZ8 A O5  1 
HETATM 6597 O  O6  . EZ8 G  2 .   ? 14.442  -8.516  16.853  1.00 34.29  ? 1001 EZ8 A O6  1 
HETATM 6598 O  O4  . EZ8 G  2 .   ? 12.071  -5.425  16.084  1.00 30.09  ? 1001 EZ8 A O4  1 
HETATM 6599 O  O3  . EZ8 G  2 .   ? 9.595   -5.818  14.915  1.00 29.45  ? 1001 EZ8 A O3  1 
HETATM 6600 C  C2  . EZ8 G  2 .   ? 10.007  -8.157  14.524  1.00 28.12  ? 1001 EZ8 A C2  1 
HETATM 6601 C  CAR . EZ8 G  2 .   ? 8.001   -8.975  15.320  1.00 31.65  ? 1001 EZ8 A CAR 1 
HETATM 6602 N  NBD . EZ8 G  2 .   ? 9.381   -8.644  16.917  1.00 29.99  ? 1001 EZ8 A NBD 1 
HETATM 6603 N  NBC . EZ8 G  2 .   ? 8.272   -9.118  17.455  1.00 33.12  ? 1001 EZ8 A NBC 1 
HETATM 6604 C  CBP . EZ8 G  2 .   ? 7.411   -9.316  16.456  1.00 35.09  ? 1001 EZ8 A CBP 1 
HETATM 6605 C  CAS . EZ8 G  2 .   ? 5.986   -9.862  16.498  1.00 39.91  ? 1001 EZ8 A CAS 1 
HETATM 6606 N  NAA . EZ8 G  2 .   ? 5.306   -9.362  17.690  1.00 43.58  ? 1001 EZ8 A NAA 1 
HETATM 6607 CA CA  . CA  H  3 .   ? 10.340  -3.466  15.648  1.00 30.01  ? 1002 CA  A CA  1 
HETATM 6608 CA CA  . CA  I  3 .   ? 8.614   3.298   11.247  1.00 29.98  ? 1003 CA  A CA  1 
HETATM 6609 CA CA  . CA  J  3 .   ? 6.761   4.592   6.547   1.00 49.01  ? 1004 CA  A CA  1 
HETATM 6610 CL CL  . CL  K  4 .   ? -13.513 -9.680  17.781  1.00 64.34  ? 1005 CL  A CL  1 
HETATM 6611 CL CL  . CL  L  4 .   ? -7.495  -8.001  34.168  1.00 64.60  ? 1006 CL  A CL  1 
HETATM 6612 CL CL  . CL  M  4 .   ? -11.156 0.395   37.832  1.00 65.39  ? 1007 CL  A CL  1 
HETATM 6613 C  C4  . EZ8 N  2 .   ? -5.415  4.393   45.810  1.00 23.60  ? 1001 EZ8 B C4  1 
HETATM 6614 C  C5  . EZ8 N  2 .   ? -4.892  3.500   44.640  1.00 25.09  ? 1001 EZ8 B C5  1 
HETATM 6615 C  C6  . EZ8 N  2 .   ? -3.382  3.444   44.631  1.00 25.15  ? 1001 EZ8 B C6  1 
HETATM 6616 N  N2  . EZ8 N  2 .   ? -7.063  2.242   47.280  1.00 23.66  ? 1001 EZ8 B N2  1 
HETATM 6617 C  C3  . EZ8 N  2 .   ? -6.907  4.307   45.849  1.00 22.25  ? 1001 EZ8 B C3  1 
HETATM 6618 C  CAP . EZ8 N  2 .   ? -13.393 -2.641  43.667  1.00 39.77  ? 1001 EZ8 B CAP 1 
HETATM 6619 C  CAL . EZ8 N  2 .   ? -13.079 -3.833  44.364  1.00 42.46  ? 1001 EZ8 B CAL 1 
HETATM 6620 C  CBM . EZ8 N  2 .   ? -11.975 -4.622  44.003  1.00 42.86  ? 1001 EZ8 B CBM 1 
HETATM 6621 C  CAV . EZ8 N  2 .   ? -11.628 -5.747  44.724  1.00 47.81  ? 1001 EZ8 B CAV 1 
HETATM 6622 O  OAE . EZ8 N  2 .   ? -12.070 -6.975  44.133  1.00 54.00  ? 1001 EZ8 B OAE 1 
HETATM 6623 C  CAM . EZ8 N  2 .   ? -11.173 -4.180  42.948  1.00 43.86  ? 1001 EZ8 B CAM 1 
HETATM 6624 C  CAQ . EZ8 N  2 .   ? -11.471 -2.996  42.242  1.00 40.36  ? 1001 EZ8 B CAQ 1 
HETATM 6625 C  CBO . EZ8 N  2 .   ? -12.577 -2.207  42.592  1.00 37.59  ? 1001 EZ8 B CBO 1 
HETATM 6626 C  CAZ . EZ8 N  2 .   ? -12.877 -1.037  41.896  1.00 35.09  ? 1001 EZ8 B CAZ 1 
HETATM 6627 N  NBF . EZ8 N  2 .   ? -11.639 -0.184  41.740  1.00 34.40  ? 1001 EZ8 B NBF 1 
HETATM 6628 C  CBK . EZ8 N  2 .   ? -11.122 0.605   42.696  1.00 31.15  ? 1001 EZ8 B CBK 1 
HETATM 6629 O  OAC . EZ8 N  2 .   ? -11.546 0.620   43.856  1.00 32.27  ? 1001 EZ8 B OAC 1 
HETATM 6630 C  CBW . EZ8 N  2 .   ? -9.832  1.406   42.412  1.00 27.56  ? 1001 EZ8 B CBW 1 
HETATM 6631 C  CBB . EZ8 N  2 .   ? -8.717  0.487   42.648  1.00 25.63  ? 1001 EZ8 B CBB 1 
HETATM 6632 C  CBV . EZ8 N  2 .   ? -9.738  2.168   41.084  1.00 27.86  ? 1001 EZ8 B CBV 1 
HETATM 6633 C  CBJ . EZ8 N  2 .   ? -10.982 3.063   40.874  1.00 30.76  ? 1001 EZ8 B CBJ 1 
HETATM 6634 O  OAB . EZ8 N  2 .   ? -11.466 3.757   41.793  1.00 29.76  ? 1001 EZ8 B OAB 1 
HETATM 6635 N  NBE . EZ8 N  2 .   ? -11.554 3.007   39.679  1.00 29.85  ? 1001 EZ8 B NBE 1 
HETATM 6636 C  CAY . EZ8 N  2 .   ? -12.793 3.808   39.388  1.00 31.04  ? 1001 EZ8 B CAY 1 
HETATM 6637 C  CBN . EZ8 N  2 .   ? -12.510 4.933   38.575  1.00 31.05  ? 1001 EZ8 B CBN 1 
HETATM 6638 C  CAN . EZ8 N  2 .   ? -11.237 5.461   38.510  1.00 34.03  ? 1001 EZ8 B CAN 1 
HETATM 6639 C  CAJ . EZ8 N  2 .   ? -10.991 6.562   37.693  1.00 36.54  ? 1001 EZ8 B CAJ 1 
HETATM 6640 C  CBL . EZ8 N  2 .   ? -12.002 7.124   36.937  1.00 38.24  ? 1001 EZ8 B CBL 1 
HETATM 6641 C  CAU . EZ8 N  2 .   ? -11.738 8.191   36.139  1.00 42.39  ? 1001 EZ8 B CAU 1 
HETATM 6642 O  OAD . EZ8 N  2 .   ? -12.139 9.333   36.901  1.00 54.04  ? 1001 EZ8 B OAD 1 
HETATM 6643 C  CAK . EZ8 N  2 .   ? -13.286 6.596   37.003  1.00 35.19  ? 1001 EZ8 B CAK 1 
HETATM 6644 C  CAO . EZ8 N  2 .   ? -13.533 5.518   37.832  1.00 32.34  ? 1001 EZ8 B CAO 1 
HETATM 6645 C  CBA . EZ8 N  2 .   ? -8.548  3.084   41.160  1.00 28.69  ? 1001 EZ8 B CBA 1 
HETATM 6646 C  CBT . EZ8 N  2 .   ? -7.298  2.196   41.391  1.00 26.72  ? 1001 EZ8 B CBT 1 
HETATM 6647 O  OBG . EZ8 N  2 .   ? -7.129  1.328   40.265  1.00 29.02  ? 1001 EZ8 B OBG 1 
HETATM 6648 C  CAX . EZ8 N  2 .   ? -5.810  0.854   40.207  1.00 37.23  ? 1001 EZ8 B CAX 1 
HETATM 6649 C  CAT . EZ8 N  2 .   ? -5.783  -0.206  39.098  1.00 40.49  ? 1001 EZ8 B CAT 1 
HETATM 6650 CL CL1 . EZ8 N  2 .   ? -7.170  -1.384  39.333  1.00 53.02  ? 1001 EZ8 B CL1 1 
HETATM 6651 C  CBU . EZ8 N  2 .   ? -7.456  1.372   42.686  1.00 26.53  ? 1001 EZ8 B CBU 1 
HETATM 6652 O  O1  . EZ8 N  2 .   ? -7.472  2.323   43.745  1.00 24.33  ? 1001 EZ8 B O1  1 
HETATM 6653 C  C1  . EZ8 N  2 .   ? -6.759  2.007   44.877  1.00 24.50  ? 1001 EZ8 B C1  1 
HETATM 6654 O  O5  . EZ8 N  2 .   ? -5.327  2.170   44.847  1.00 24.14  ? 1001 EZ8 B O5  1 
HETATM 6655 O  O6  . EZ8 N  2 .   ? -3.084  2.639   43.481  1.00 29.70  ? 1001 EZ8 B O6  1 
HETATM 6656 O  O4  . EZ8 N  2 .   ? -5.049  5.742   45.562  1.00 22.66  ? 1001 EZ8 B O4  1 
HETATM 6657 O  O3  . EZ8 N  2 .   ? -7.392  5.041   46.943  1.00 22.03  ? 1001 EZ8 B O3  1 
HETATM 6658 C  C2  . EZ8 N  2 .   ? -7.377  2.849   46.001  1.00 23.78  ? 1001 EZ8 B C2  1 
HETATM 6659 C  CAR . EZ8 N  2 .   ? -7.964  1.767   48.172  1.00 25.75  ? 1001 EZ8 B CAR 1 
HETATM 6660 N  NBD . EZ8 N  2 .   ? -5.862  2.048   47.804  1.00 25.64  ? 1001 EZ8 B NBD 1 
HETATM 6661 N  NBC . EZ8 N  2 .   ? -5.970  1.495   48.994  1.00 27.10  ? 1001 EZ8 B NBC 1 
HETATM 6662 C  CBP . EZ8 N  2 .   ? -7.275  1.294   49.194  1.00 26.34  ? 1001 EZ8 B CBP 1 
HETATM 6663 C  CAS . EZ8 N  2 .   ? -7.865  0.661   50.398  1.00 28.84  ? 1001 EZ8 B CAS 1 
HETATM 6664 N  NAA . EZ8 N  2 .   ? -7.062  1.078   51.526  1.00 30.31  ? 1001 EZ8 B NAA 1 
HETATM 6665 CA CA  . CA  O  3 .   ? -6.395  7.402   46.882  1.00 22.15  ? 1002 CA  B CA  1 
HETATM 6666 CA CA  . CA  P  3 .   ? -11.063 14.169  46.818  1.00 25.55  ? 1003 CA  B CA  1 
HETATM 6667 CA CA  . CA  Q  3 .   ? -16.143 15.378  45.683  1.00 54.27  ? 1004 CA  B CA  1 
HETATM 6668 CL CL  . CL  R  4 .   ? -17.990 -1.103  67.093  1.00 66.53  ? 1005 CL  B CL  1 
HETATM 6669 CL CL  . CL  S  4 .   ? 0.183   8.635   77.233  1.00 63.88  ? 1006 CL  B CL  1 
HETATM 6670 C  C4  . EZ8 T  2 .   ? -3.556  -11.621 60.094  1.00 23.84  ? 1001 EZ8 C C4  1 
HETATM 6671 C  C5  . EZ8 T  2 .   ? -2.659  -10.777 61.001  1.00 26.26  ? 1001 EZ8 C C5  1 
HETATM 6672 C  C6  . EZ8 T  2 .   ? -1.247  -11.121 60.648  1.00 28.48  ? 1001 EZ8 C C6  1 
HETATM 6673 N  N2  . EZ8 T  2 .   ? -5.455  -9.410  59.222  1.00 24.47  ? 1001 EZ8 C N2  1 
HETATM 6674 C  C3  . EZ8 T  2 .   ? -4.919  -11.473 60.547  1.00 23.91  ? 1001 EZ8 C C3  1 
HETATM 6675 C  CAP . EZ8 T  2 .   ? -7.303  -3.775  65.435  1.00 46.41  ? 1001 EZ8 C CAP 1 
HETATM 6676 C  CAL . EZ8 T  2 .   ? -7.142  -2.584  64.691  1.00 45.35  ? 1001 EZ8 C CAL 1 
HETATM 6677 C  CBM . EZ8 T  2 .   ? -8.181  -2.082  63.906  1.00 47.00  ? 1001 EZ8 C CBM 1 
HETATM 6678 C  CAV . EZ8 T  2 .   ? -7.990  -0.925  63.148  1.00 50.46  ? 1001 EZ8 C CAV 1 
HETATM 6679 O  OAE . EZ8 T  2 .   ? -8.353  0.281   63.861  1.00 48.10  ? 1001 EZ8 C OAE 1 
HETATM 6680 C  CAM . EZ8 T  2 .   ? -9.392  -2.810  63.867  1.00 43.80  ? 1001 EZ8 C CAM 1 
HETATM 6681 C  CAQ . EZ8 T  2 .   ? -9.564  -3.999  64.599  1.00 44.89  ? 1001 EZ8 C CAQ 1 
HETATM 6682 C  CBO . EZ8 T  2 .   ? -8.500  -4.510  65.398  1.00 43.65  ? 1001 EZ8 C CBO 1 
HETATM 6683 C  CAZ . EZ8 T  2 .   ? -8.653  -5.687  66.168  1.00 41.22  ? 1001 EZ8 C CAZ 1 
HETATM 6684 N  NBF . EZ8 T  2 .   ? -7.565  -6.671  65.883  1.00 36.32  ? 1001 EZ8 C NBF 1 
HETATM 6685 C  CBK . EZ8 T  2 .   ? -7.539  -7.442  64.780  1.00 33.61  ? 1001 EZ8 C CBK 1 
HETATM 6686 O  OAC . EZ8 T  2 .   ? -8.374  -7.345  63.888  1.00 36.15  ? 1001 EZ8 C OAC 1 
HETATM 6687 C  CBW . EZ8 T  2 .   ? -6.333  -8.402  64.582  1.00 30.77  ? 1001 EZ8 C CBW 1 
HETATM 6688 C  CBB . EZ8 T  2 .   ? -5.285  -7.613  63.970  1.00 28.76  ? 1001 EZ8 C CBB 1 
HETATM 6689 C  CBV . EZ8 T  2 .   ? -5.875  -9.082  65.861  1.00 31.38  ? 1001 EZ8 C CBV 1 
HETATM 6690 C  CBJ . EZ8 T  2 .   ? -7.028  -9.899  66.472  1.00 33.02  ? 1001 EZ8 C CBJ 1 
HETATM 6691 O  OAB . EZ8 T  2 .   ? -7.731  -10.586 65.747  1.00 37.23  ? 1001 EZ8 C OAB 1 
HETATM 6692 N  NBE . EZ8 T  2 .   ? -7.165  -9.823  67.801  1.00 32.68  ? 1001 EZ8 C NBE 1 
HETATM 6693 C  CAY . EZ8 T  2 .   ? -8.227  -10.486 68.623  1.00 32.47  ? 1001 EZ8 C CAY 1 
HETATM 6694 C  CBN . EZ8 T  2 .   ? -7.751  -11.643 69.316  1.00 29.97  ? 1001 EZ8 C CBN 1 
HETATM 6695 C  CAN . EZ8 T  2 .   ? -8.479  -12.224 70.369  1.00 31.10  ? 1001 EZ8 C CAN 1 
HETATM 6696 C  CAJ . EZ8 T  2 .   ? -8.002  -13.377 71.002  1.00 28.33  ? 1001 EZ8 C CAJ 1 
HETATM 6697 C  CBL . EZ8 T  2 .   ? -6.807  -13.943 70.591  1.00 28.90  ? 1001 EZ8 C CBL 1 
HETATM 6698 C  CAU . EZ8 T  2 .   ? -6.267  -15.029 71.176  1.00 32.48  ? 1001 EZ8 C CAU 1 
HETATM 6699 O  OAD . EZ8 T  2 .   ? -7.276  -16.005 71.243  1.00 39.73  ? 1001 EZ8 C OAD 1 
HETATM 6700 C  CAK . EZ8 T  2 .   ? -6.091  -13.363 69.567  1.00 29.46  ? 1001 EZ8 C CAK 1 
HETATM 6701 C  CAO . EZ8 T  2 .   ? -6.555  -12.222 68.946  1.00 28.06  ? 1001 EZ8 C CAO 1 
HETATM 6702 C  CBA . EZ8 T  2 .   ? -4.831  -10.028 65.584  1.00 31.43  ? 1001 EZ8 C CBA 1 
HETATM 6703 C  CBT . EZ8 T  2 .   ? -3.669  -9.323  64.866  1.00 29.34  ? 1001 EZ8 C CBT 1 
HETATM 6704 O  OBG . EZ8 T  2 .   ? -2.974  -8.496  65.754  1.00 32.73  ? 1001 EZ8 C OBG 1 
HETATM 6705 C  CAX . EZ8 T  2 .   ? -1.621  -8.390  65.375  1.00 37.63  ? 1001 EZ8 C CAX 1 
HETATM 6706 C  CAT . EZ8 T  2 .   ? -1.070  -7.215  66.218  1.00 43.43  ? 1001 EZ8 C CAT 1 
HETATM 6707 CL CL1 . EZ8 T  2 .   ? -2.374  -5.979  66.637  1.00 53.34  ? 1001 EZ8 C CL1 1 
HETATM 6708 C  CBU . EZ8 T  2 .   ? -4.129  -8.547  63.660  1.00 29.95  ? 1001 EZ8 C CBU 1 
HETATM 6709 O  O1  . EZ8 T  2 .   ? -4.428  -9.517  62.669  1.00 25.08  ? 1001 EZ8 C O1  1 
HETATM 6710 C  C1  . EZ8 T  2 .   ? -4.232  -9.143  61.315  1.00 24.82  ? 1001 EZ8 C C1  1 
HETATM 6711 O  O5  . EZ8 T  2 .   ? -2.975  -9.368  60.800  1.00 25.11  ? 1001 EZ8 C O5  1 
HETATM 6712 O  O6  . EZ8 T  2 .   ? -0.406  -10.106 61.172  1.00 31.40  ? 1001 EZ8 C O6  1 
HETATM 6713 O  O4  . EZ8 T  2 .   ? -3.191  -12.987 60.093  1.00 24.38  ? 1001 EZ8 C O4  1 
HETATM 6714 O  O3  . EZ8 T  2 .   ? -5.835  -12.193 59.689  1.00 23.89  ? 1001 EZ8 C O3  1 
HETATM 6715 C  C2  . EZ8 T  2 .   ? -5.278  -9.972  60.518  1.00 23.87  ? 1001 EZ8 C C2  1 
HETATM 6716 C  CAR . EZ8 T  2 .   ? -6.592  -8.921  58.753  1.00 25.12  ? 1001 EZ8 C CAR 1 
HETATM 6717 N  NBD . EZ8 T  2 .   ? -4.512  -9.239  58.288  1.00 24.43  ? 1001 EZ8 C NBD 1 
HETATM 6718 N  NBC . EZ8 T  2 .   ? -4.963  -8.694  57.349  1.00 24.41  ? 1001 EZ8 C NBC 1 
HETATM 6719 C  CBP . EZ8 T  2 .   ? -6.255  -8.463  57.550  1.00 26.90  ? 1001 EZ8 C CBP 1 
HETATM 6720 C  CAS . EZ8 T  2 .   ? -7.197  -7.776  56.578  1.00 27.46  ? 1001 EZ8 C CAS 1 
HETATM 6721 N  NAA . EZ8 T  2 .   ? -6.713  -7.953  55.218  1.00 30.03  ? 1001 EZ8 C NAA 1 
HETATM 6722 CA CA  . CA  U  3 .   ? -5.057  -14.525 59.344  1.00 25.73  ? 1002 CA  C CA  1 
HETATM 6723 CA CA  . CA  V  3 .   ? -9.862  -20.970 61.350  1.00 27.95  ? 1003 CA  C CA  1 
HETATM 6724 CA CA  . CA  W  3 .   ? -14.113 -21.919 63.758  1.00 51.36  ? 1004 CA  C CA  1 
HETATM 6725 CL CL  . CL  X  4 .   ? -22.111 -4.897  44.537  1.00 60.06  ? 1005 CL  C CL  1 
HETATM 6726 CL CL  . CL  Y  4 .   ? -10.000 -15.788 28.746  1.00 58.86  ? 1006 CL  C CL  1 
HETATM 6727 CL CL  . CL  Z  4 .   ? 14.938  -10.685 6.085   1.00 59.28  ? 501  CL  D CL  1 
HETATM 6728 C  C4  . EZ8 AA 2 .   ? -1.431  -21.218 26.052  1.00 28.63  ? 502  EZ8 D C4  1 
HETATM 6729 C  C5  . EZ8 AA 2 .   ? -1.608  -20.269 27.221  1.00 30.07  ? 502  EZ8 D C5  1 
HETATM 6730 C  C6  . EZ8 AA 2 .   ? -0.318  -20.135 27.924  1.00 33.12  ? 502  EZ8 D C6  1 
HETATM 6731 N  N2  . EZ8 AA 2 .   ? -1.284  -19.041 23.803  1.00 26.84  ? 502  EZ8 D N2  1 
HETATM 6732 C  C3  . EZ8 AA 2 .   ? -2.484  -20.933 24.991  1.00 28.45  ? 502  EZ8 D C3  1 
HETATM 6733 C  CAP . EZ8 AA 2 .   ? -7.509  -13.022 22.912  1.00 53.84  ? 502  EZ8 D CAP 1 
HETATM 6734 C  CAL . EZ8 AA 2 .   ? -6.716  -11.905 22.618  1.00 57.43  ? 502  EZ8 D CAL 1 
HETATM 6735 C  CBM . EZ8 AA 2 .   ? -6.123  -11.147 23.646  1.00 64.66  ? 502  EZ8 D CBM 1 
HETATM 6736 C  CAV . EZ8 AA 2 .   ? -5.320  -10.042 23.370  1.00 68.43  ? 502  EZ8 D CAV 1 
HETATM 6737 O  OAE . EZ8 AA 2 .   ? -5.872  -8.870  24.034  1.00 64.79  ? 502  EZ8 D OAE 1 
HETATM 6738 C  CAM . EZ8 AA 2 .   ? -6.336  -11.532 24.973  1.00 61.32  ? 502  EZ8 D CAM 1 
HETATM 6739 C  CAQ . EZ8 AA 2 .   ? -7.126  -12.648 25.264  1.00 54.68  ? 502  EZ8 D CAQ 1 
HETATM 6740 C  CBO . EZ8 AA 2 .   ? -7.725  -13.410 24.258  1.00 53.19  ? 502  EZ8 D CBO 1 
HETATM 6741 C  CAZ . EZ8 AA 2 .   ? -8.546  -14.499 24.609  1.00 45.74  ? 502  EZ8 D CAZ 1 
HETATM 6742 N  NBF . EZ8 AA 2 .   ? -7.831  -15.491 25.455  1.00 40.64  ? 502  EZ8 D NBF 1 
HETATM 6743 C  CBK . EZ8 AA 2 .   ? -6.968  -16.381 24.903  1.00 34.06  ? 502  EZ8 D CBK 1 
HETATM 6744 O  OAC . EZ8 AA 2 .   ? -6.664  -16.366 23.713  1.00 34.37  ? 502  EZ8 D OAC 1 
HETATM 6745 C  CBW . EZ8 AA 2 .   ? -6.246  -17.377 25.819  1.00 30.86  ? 502  EZ8 D CBW 1 
HETATM 6746 C  CBB . EZ8 AA 2 .   ? -5.122  -16.712 26.444  1.00 27.91  ? 502  EZ8 D CBB 1 
HETATM 6747 C  CBV . EZ8 AA 2 .   ? -7.164  -17.986 26.861  1.00 30.09  ? 502  EZ8 D CBV 1 
HETATM 6748 C  CBJ . EZ8 AA 2 .   ? -8.328  -18.666 26.132  1.00 33.35  ? 502  EZ8 D CBJ 1 
HETATM 6749 O  OAB . EZ8 AA 2 .   ? -8.124  -19.543 25.279  1.00 33.92  ? 502  EZ8 D OAB 1 
HETATM 6750 N  NBE . EZ8 AA 2 .   ? -9.560  -18.320 26.545  1.00 31.60  ? 502  EZ8 D NBE 1 
HETATM 6751 C  CAY . EZ8 AA 2 .   ? -10.789 -18.828 25.918  1.00 28.89  ? 502  EZ8 D CAY 1 
HETATM 6752 C  CBN . EZ8 AA 2 .   ? -11.377 -19.892 26.607  1.00 30.06  ? 502  EZ8 D CBN 1 
HETATM 6753 C  CAN . EZ8 AA 2 .   ? -10.749 -20.732 27.505  1.00 31.29  ? 502  EZ8 D CAN 1 
HETATM 6754 C  CAJ . EZ8 AA 2 .   ? -11.451 -21.771 28.141  1.00 30.72  ? 502  EZ8 D CAJ 1 
HETATM 6755 C  CBL . EZ8 AA 2 .   ? -12.807 -21.950 27.852  1.00 32.64  ? 502  EZ8 D CBL 1 
HETATM 6756 C  CAU . EZ8 AA 2 .   ? -13.608 -22.926 28.374  1.00 36.84  ? 502  EZ8 D CAU 1 
HETATM 6757 O  OAD . EZ8 AA 2 .   ? -12.863 -23.715 29.284  1.00 37.62  ? 502  EZ8 D OAD 1 
HETATM 6758 C  CAK . EZ8 AA 2 .   ? -13.433 -21.132 26.953  1.00 31.44  ? 502  EZ8 D CAK 1 
HETATM 6759 C  CAO . EZ8 AA 2 .   ? -12.727 -20.123 26.319  1.00 33.08  ? 502  EZ8 D CAO 1 
HETATM 6760 C  CBA . EZ8 AA 2 .   ? -6.462  -19.028 27.594  1.00 31.30  ? 502  EZ8 D CBA 1 
HETATM 6761 C  CBT . EZ8 AA 2 .   ? -5.243  -18.434 28.257  1.00 31.20  ? 502  EZ8 D CBT 1 
HETATM 6762 O  OBG . EZ8 AA 2 .   ? -5.624  -17.450 29.299  1.00 32.73  ? 502  EZ8 D OBG 1 
HETATM 6763 C  CAX . EZ8 AA 2 .   ? -4.512  -17.130 30.121  1.00 37.27  ? 502  EZ8 D CAX 1 
HETATM 6764 C  CAT . EZ8 AA 2 .   ? -5.009  -16.009 31.038  1.00 44.28  ? 502  EZ8 D CAT 1 
HETATM 6765 CL CL1 . EZ8 AA 2 .   ? -5.622  -14.583 30.046  1.00 53.91  ? 502  EZ8 D CL1 1 
HETATM 6766 C  CBU . EZ8 AA 2 .   ? -4.359  -17.766 27.140  1.00 28.18  ? 502  EZ8 D CBU 1 
HETATM 6767 O  O1  . EZ8 AA 2 .   ? -4.024  -18.754 26.218  1.00 25.88  ? 502  EZ8 D O1  1 
HETATM 6768 C  C1  . EZ8 AA 2 .   ? -2.725  -18.597 25.721  1.00 26.41  ? 502  EZ8 D C1  1 
HETATM 6769 O  O5  . EZ8 AA 2 .   ? -1.781  -18.859 26.759  1.00 26.23  ? 502  EZ8 D O5  1 
HETATM 6770 O  O6  . EZ8 AA 2 .   ? -0.637  -20.034 29.283  1.00 38.17  ? 502  EZ8 D O6  1 
HETATM 6771 O  O4  . EZ8 AA 2 .   ? -1.551  -22.633 26.469  1.00 30.25  ? 502  EZ8 D O4  1 
HETATM 6772 O  O3  . EZ8 AA 2 .   ? -2.278  -21.785 23.873  1.00 27.12  ? 502  EZ8 D O3  1 
HETATM 6773 C  C2  . EZ8 AA 2 .   ? -2.517  -19.492 24.510  1.00 25.88  ? 502  EZ8 D C2  1 
HETATM 6774 C  CAR . EZ8 AA 2 .   ? -1.260  -18.518 22.580  1.00 24.83  ? 502  EZ8 D CAR 1 
HETATM 6775 N  NBD . EZ8 AA 2 .   ? -0.033  -19.023 24.292  1.00 26.66  ? 502  EZ8 D NBD 1 
HETATM 6776 N  NBC . EZ8 AA 2 .   ? 0.773   -18.529 23.312  1.00 30.10  ? 502  EZ8 D NBC 1 
HETATM 6777 C  CBP . EZ8 AA 2 .   ? -0.010  -18.204 22.291  1.00 26.53  ? 502  EZ8 D CBP 1 
HETATM 6778 C  CAS . EZ8 AA 2 .   ? 0.443   -17.608 20.972  1.00 27.96  ? 502  EZ8 D CAS 1 
HETATM 6779 N  NAA . EZ8 AA 2 .   ? 1.700   -18.286 20.617  1.00 30.54  ? 502  EZ8 D NAA 1 
HETATM 6780 CA CA  . CA  BA 3 .   ? -2.033  -24.170 24.547  1.00 26.64  ? 503  CA  D CA  1 
HETATM 6781 CA CA  . CA  CA 3 .   ? -6.500  -30.337 21.514  1.00 27.32  ? 504  CA  D CA  1 
HETATM 6782 CA CA  . CA  DA 3 .   ? -11.059 -31.096 18.842  1.00 62.64  ? 505  CA  D CA  1 
HETATM 6783 CL CL  . CL  EA 4 .   ? 4.097   -15.845 2.005   1.00 56.45  ? 506  CL  D CL  1 
HETATM 6784 CL CL  . CL  FA 4 .   ? -0.300  0.748   71.474  1.00 72.63  ? 501  CL  E CL  1 
HETATM 6785 CL CL  . CL  GA 4 .   ? -5.685  -7.412  69.798  1.00 54.91  ? 502  CL  E CL  1 
HETATM 6786 C  C4  . EZ8 HA 2 .   ? 24.244  -2.421  80.691  1.00 25.59  ? 503  EZ8 E C4  1 
HETATM 6787 C  C5  . EZ8 HA 2 .   ? 25.459  -1.584  80.576  1.00 27.99  ? 503  EZ8 E C5  1 
HETATM 6788 C  C6  . EZ8 HA 2 .   ? 26.231  -1.807  79.268  1.00 31.37  ? 503  EZ8 E C6  1 
HETATM 6789 N  N2  . EZ8 HA 2 .   ? 22.334  -0.500  82.133  1.00 28.84  ? 503  EZ8 E N2  1 
HETATM 6790 C  C3  . EZ8 HA 2 .   ? 23.926  -2.460  82.196  1.00 26.89  ? 503  EZ8 E C3  1 
HETATM 6791 C  CAP . EZ8 HA 2 .   ? 26.393  4.843   87.410  1.00 53.08  ? 503  EZ8 E CAP 1 
HETATM 6792 C  CAL . EZ8 HA 2 .   ? 25.767  6.058   87.071  1.00 52.79  ? 503  EZ8 E CAL 1 
HETATM 6793 C  CBM . EZ8 HA 2 .   ? 24.587  6.451   87.706  1.00 51.12  ? 503  EZ8 E CBM 1 
HETATM 6794 C  CAV . EZ8 HA 2 .   ? 23.990  7.643   87.363  1.00 57.10  ? 503  EZ8 E CAV 1 
HETATM 6795 O  OAE . EZ8 HA 2 .   ? 24.783  8.702   88.004  1.00 59.53  ? 503  EZ8 E OAE 1 
HETATM 6796 C  CAM . EZ8 HA 2 .   ? 24.048  5.633   88.690  1.00 45.94  ? 503  EZ8 E CAM 1 
HETATM 6797 C  CAQ . EZ8 HA 2 .   ? 24.664  4.428   89.044  1.00 48.09  ? 503  EZ8 E CAQ 1 
HETATM 6798 C  CBO . EZ8 HA 2 .   ? 25.856  3.995   88.403  1.00 47.57  ? 503  EZ8 E CBO 1 
HETATM 6799 C  CAZ . EZ8 HA 2 .   ? 26.479  2.797   88.788  1.00 40.90  ? 503  EZ8 E CAZ 1 
HETATM 6800 N  NBF . EZ8 HA 2 .   ? 26.880  2.017   87.590  1.00 36.98  ? 503  EZ8 E NBF 1 
HETATM 6801 C  CBK . EZ8 HA 2 .   ? 26.044  1.223   86.920  1.00 36.58  ? 503  EZ8 E CBK 1 
HETATM 6802 O  OAC . EZ8 HA 2 .   ? 24.861  1.141   87.213  1.00 40.04  ? 503  EZ8 E OAC 1 
HETATM 6803 C  CBW . EZ8 HA 2 .   ? 26.563  0.478   85.667  1.00 34.20  ? 503  EZ8 E CBW 1 
HETATM 6804 C  CBB . EZ8 HA 2 .   ? 26.521  1.391   84.539  1.00 32.03  ? 503  EZ8 E CBB 1 
HETATM 6805 C  CBV . EZ8 HA 2 .   ? 27.978  -0.151  85.810  1.00 35.72  ? 503  EZ8 E CBV 1 
HETATM 6806 C  CBJ . EZ8 HA 2 .   ? 28.011  -1.072  87.022  1.00 36.48  ? 503  EZ8 E CBJ 1 
HETATM 6807 O  OAB . EZ8 HA 2 .   ? 27.133  -1.905  87.173  1.00 34.82  ? 503  EZ8 E OAB 1 
HETATM 6808 N  NBE . EZ8 HA 2 .   ? 29.073  -0.967  87.821  1.00 36.01  ? 503  EZ8 E NBE 1 
HETATM 6809 C  CAY . EZ8 HA 2 .   ? 29.246  -1.756  89.055  1.00 36.79  ? 503  EZ8 E CAY 1 
HETATM 6810 C  CBN . EZ8 HA 2 .   ? 30.091  -2.883  88.956  1.00 36.21  ? 503  EZ8 E CBN 1 
HETATM 6811 C  CAN . EZ8 HA 2 .   ? 30.577  -3.393  90.145  1.00 36.74  ? 503  EZ8 E CAN 1 
HETATM 6812 C  CAJ . EZ8 HA 2 .   ? 31.415  -4.502  90.213  1.00 37.53  ? 503  EZ8 E CAJ 1 
HETATM 6813 C  CBL . EZ8 HA 2 .   ? 31.794  -5.127  89.041  1.00 38.22  ? 503  EZ8 E CBL 1 
HETATM 6814 C  CAU . EZ8 HA 2 .   ? 32.618  -6.216  89.187  1.00 42.64  ? 503  EZ8 E CAU 1 
HETATM 6815 O  OAD . EZ8 HA 2 .   ? 32.767  -6.885  87.927  1.00 47.34  ? 503  EZ8 E OAD 1 
HETATM 6816 C  CAK . EZ8 HA 2 .   ? 31.310  -4.635  87.820  1.00 36.09  ? 503  EZ8 E CAK 1 
HETATM 6817 C  CAO . EZ8 HA 2 .   ? 30.453  -3.523  87.777  1.00 36.48  ? 503  EZ8 E CAO 1 
HETATM 6818 C  CBA . EZ8 HA 2 .   ? 28.347  -0.988  84.645  1.00 33.96  ? 503  EZ8 E CBA 1 
HETATM 6819 C  CBT . EZ8 HA 2 .   ? 28.202  -0.198  83.342  1.00 34.20  ? 503  EZ8 E CBT 1 
HETATM 6820 O  OBG . EZ8 HA 2 .   ? 29.246  0.760   83.298  1.00 37.41  ? 503  EZ8 E OBG 1 
HETATM 6821 C  CAX . EZ8 HA 2 .   ? 30.212  0.653   82.297  1.00 50.92  ? 503  EZ8 E CAX 1 
HETATM 6822 C  CAT . EZ8 HA 2 .   ? 30.282  2.047   81.728  1.00 56.94  ? 503  EZ8 E CAT 1 
HETATM 6823 CL CL1 . EZ8 HA 2 .   ? 30.060  3.189   83.139  1.00 77.48  ? 503  EZ8 E CL1 1 
HETATM 6824 C  CBU . EZ8 HA 2 .   ? 26.843  0.563   83.248  1.00 32.39  ? 503  EZ8 E CBU 1 
HETATM 6825 O  O1  . EZ8 HA 2 .   ? 25.815  -0.417  83.096  1.00 29.62  ? 503  EZ8 E O1  1 
HETATM 6826 C  C1  . EZ8 HA 2 .   ? 24.738  -0.092  82.274  1.00 26.65  ? 503  EZ8 E C1  1 
HETATM 6827 O  O5  . EZ8 HA 2 .   ? 25.034  -0.252  80.811  1.00 26.66  ? 503  EZ8 E O5  1 
HETATM 6828 O  O6  . EZ8 HA 2 .   ? 25.753  -0.881  78.412  1.00 34.40  ? 503  EZ8 E O6  1 
HETATM 6829 O  O4  . EZ8 HA 2 .   ? 24.471  -3.720  80.219  1.00 27.67  ? 503  EZ8 E O4  1 
HETATM 6830 O  O3  . EZ8 HA 2 .   ? 22.871  -3.315  82.455  1.00 23.35  ? 503  EZ8 E O3  1 
HETATM 6831 C  C2  . EZ8 HA 2 .   ? 23.612  -1.034  82.684  1.00 26.92  ? 503  EZ8 E C2  1 
HETATM 6832 C  CAR . EZ8 HA 2 .   ? 21.336  -0.102  82.935  1.00 28.61  ? 503  EZ8 E CAR 1 
HETATM 6833 N  NBD . EZ8 HA 2 .   ? 22.065  -0.286  80.988  1.00 27.76  ? 503  EZ8 E NBD 1 
HETATM 6834 N  NBC . EZ8 HA 2 .   ? 20.957  0.207   80.895  1.00 31.62  ? 503  EZ8 E NBC 1 
HETATM 6835 C  CBP . EZ8 HA 2 .   ? 20.467  0.359   82.125  1.00 30.98  ? 503  EZ8 E CBP 1 
HETATM 6836 C  CAS . EZ8 HA 2 .   ? 19.143  0.913   82.495  1.00 32.86  ? 503  EZ8 E CAS 1 
HETATM 6837 N  NAA . EZ8 HA 2 .   ? 18.224  0.519   81.404  1.00 32.60  ? 503  EZ8 E NAA 1 
HETATM 6838 CA CA  . CA  IA 3 .   ? 23.081  -5.604  81.330  1.00 29.03  ? 504  CA  E CA  1 
HETATM 6839 CA CA  . CA  JA 3 .   ? 22.700  -12.504 85.998  1.00 26.33  ? 505  CA  E CA  1 
HETATM 6840 CA CA  . CA  KA 3 .   ? 23.041  -13.728 90.504  1.00 53.96  ? 506  CA  E CA  1 
HETATM 6841 CL CL  . CL  LA 4 .   ? 0.857   1.989   89.225  1.00 59.35  ? 507  CL  E CL  1 
HETATM 6842 CL CL  . CL  MA 4 .   ? 31.729  0.789   87.934  1.00 51.98  ? 501  CL  F CL  1 
HETATM 6843 C  C4  . EZ8 NA 2 .   ? 9.713   13.067  76.547  1.00 32.52  ? 502  EZ8 F C4  1 
HETATM 6844 C  C5  . EZ8 NA 2 .   ? 8.837   12.275  75.582  1.00 33.11  ? 502  EZ8 F C5  1 
HETATM 6845 C  C6  . EZ8 NA 2 .   ? 8.973   12.665  74.132  1.00 39.11  ? 502  EZ8 F C6  1 
HETATM 6846 N  N2  . EZ8 NA 2 .   ? 10.478  10.825  78.615  1.00 30.29  ? 502  EZ8 F N2  1 
HETATM 6847 C  C3  . EZ8 NA 2 .   ? 9.075   12.859  77.913  1.00 30.66  ? 502  EZ8 F C3  1 
HETATM 6848 C  CAP . EZ8 NA 2 .   ? 4.142   4.892   79.397  1.00 42.44  ? 502  EZ8 F CAP 1 
HETATM 6849 C  CAL . EZ8 NA 2 .   ? 4.912   3.712   79.385  1.00 42.07  ? 502  EZ8 F CAL 1 
HETATM 6850 C  CBM . EZ8 NA 2 .   ? 5.527   3.244   80.558  1.00 48.71  ? 502  EZ8 F CBM 1 
HETATM 6851 C  CAV . EZ8 NA 2 .   ? 6.315   2.064   80.588  1.00 48.98  ? 502  EZ8 F CAV 1 
HETATM 6852 O  OAE . EZ8 NA 2 .   ? 5.481   0.912   80.245  1.00 45.29  ? 502  EZ8 F OAE 1 
HETATM 6853 C  CAM . EZ8 NA 2 .   ? 5.332   4.007   81.726  1.00 45.48  ? 502  EZ8 F CAM 1 
HETATM 6854 C  CAQ . EZ8 NA 2 .   ? 4.563   5.193   81.738  1.00 42.74  ? 502  EZ8 F CAQ 1 
HETATM 6855 C  CBO . EZ8 NA 2 .   ? 3.944   5.677   80.569  1.00 41.45  ? 502  EZ8 F CBO 1 
HETATM 6856 C  CAZ . EZ8 NA 2 .   ? 3.123   6.867   80.616  1.00 35.62  ? 502  EZ8 F CAZ 1 
HETATM 6857 N  NBF . EZ8 NA 2 .   ? 3.493   7.879   79.564  1.00 33.60  ? 502  EZ8 F NBF 1 
HETATM 6858 C  CBK . EZ8 NA 2 .   ? 4.589   8.604   79.708  1.00 31.82  ? 502  EZ8 F CBK 1 
HETATM 6859 O  OAC . EZ8 NA 2 .   ? 5.306   8.481   80.697  1.00 35.79  ? 502  EZ8 F OAC 1 
HETATM 6860 C  CBW . EZ8 NA 2 .   ? 5.012   9.585   78.611  1.00 30.34  ? 502  EZ8 F CBW 1 
HETATM 6861 C  CBB . EZ8 NA 2 .   ? 5.832   8.857   77.603  1.00 27.84  ? 502  EZ8 F CBB 1 
HETATM 6862 C  CBV . EZ8 NA 2 .   ? 3.829   10.316  78.004  1.00 30.47  ? 502  EZ8 F CBV 1 
HETATM 6863 C  CBJ . EZ8 NA 2 .   ? 3.031   11.069  79.084  1.00 30.21  ? 502  EZ8 F CBJ 1 
HETATM 6864 O  OAB . EZ8 NA 2 .   ? 3.562   11.762  79.954  1.00 29.29  ? 502  EZ8 F OAB 1 
HETATM 6865 N  NBE . EZ8 NA 2 .   ? 1.718   10.895  78.973  1.00 30.89  ? 502  EZ8 F NBE 1 
HETATM 6866 C  CAY . EZ8 NA 2 .   ? 0.750   11.533  79.871  1.00 31.87  ? 502  EZ8 F CAY 1 
HETATM 6867 C  CBN . EZ8 NA 2 .   ? 0.117   12.686  79.288  1.00 31.54  ? 502  EZ8 F CBN 1 
HETATM 6868 C  CAN . EZ8 NA 2 .   ? -1.032  13.136  79.942  1.00 32.94  ? 502  EZ8 F CAN 1 
HETATM 6869 C  CAJ . EZ8 NA 2 .   ? -1.755  14.220  79.499  1.00 29.47  ? 502  EZ8 F CAJ 1 
HETATM 6870 C  CBL . EZ8 NA 2 .   ? -1.336  14.920  78.395  1.00 31.27  ? 502  EZ8 F CBL 1 
HETATM 6871 C  CAU . EZ8 NA 2 .   ? -2.127  16.008  78.023  1.00 36.67  ? 502  EZ8 F CAU 1 
HETATM 6872 O  OAD . EZ8 NA 2 .   ? -1.301  17.044  77.491  1.00 45.70  ? 502  EZ8 F OAD 1 
HETATM 6873 C  CAK . EZ8 NA 2 .   ? -0.171  14.503  77.732  1.00 31.28  ? 502  EZ8 F CAK 1 
HETATM 6874 C  CAO . EZ8 NA 2 .   ? 0.574   13.388  78.178  1.00 27.98  ? 502  EZ8 F CAO 1 
HETATM 6875 C  CBA . EZ8 NA 2 .   ? 4.263   11.311  77.043  1.00 28.75  ? 502  EZ8 F CBA 1 
HETATM 6876 C  CBT . EZ8 NA 2 .   ? 5.107   10.637  75.922  1.00 28.46  ? 502  EZ8 F CBT 1 
HETATM 6877 O  OBG . EZ8 NA 2 .   ? 4.267   9.751   75.214  1.00 28.67  ? 502  EZ8 F OBG 1 
HETATM 6878 C  CAX . EZ8 NA 2 .   ? 4.511   9.671   73.828  1.00 35.36  ? 502  EZ8 F CAX 1 
HETATM 6879 C  CAT . EZ8 NA 2 .   ? 4.769   8.239   73.402  1.00 39.14  ? 502  EZ8 F CAT 1 
HETATM 6880 CL CL1 . EZ8 NA 2 .   ? 3.778   7.034   74.403  1.00 52.55  ? 502  EZ8 F CL1 1 
HETATM 6881 C  CBU . EZ8 NA 2 .   ? 6.285   9.872   76.523  1.00 28.31  ? 502  EZ8 F CBU 1 
HETATM 6882 O  O1  . EZ8 NA 2 .   ? 7.189   10.828  77.153  1.00 29.82  ? 502  EZ8 F O1  1 
HETATM 6883 C  C1  . EZ8 NA 2 .   ? 8.574   10.549  77.146  1.00 28.97  ? 502  EZ8 F C1  1 
HETATM 6884 O  O5  . EZ8 NA 2 .   ? 9.126   10.904  75.851  1.00 30.20  ? 502  EZ8 F O5  1 
HETATM 6885 O  O6  . EZ8 NA 2 .   ? 10.036  11.913  73.653  1.00 37.92  ? 502  EZ8 F O6  1 
HETATM 6886 O  O4  . EZ8 NA 2 .   ? 9.704   14.439  76.256  1.00 33.68  ? 502  EZ8 F O4  1 
HETATM 6887 O  O3  . EZ8 NA 2 .   ? 9.687   13.652  78.939  1.00 30.83  ? 502  EZ8 F O3  1 
HETATM 6888 C  C2  . EZ8 NA 2 .   ? 9.145   11.368  78.258  1.00 29.69  ? 502  EZ8 F C2  1 
HETATM 6889 C  CAR . EZ8 NA 2 .   ? 10.749  10.267  79.795  1.00 30.18  ? 502  EZ8 F CAR 1 
HETATM 6890 N  NBD . EZ8 NA 2 .   ? 11.505  10.710  77.891  1.00 29.39  ? 502  EZ8 F NBD 1 
HETATM 6891 N  NBC . EZ8 NA 2 .   ? 12.405  10.181  78.449  1.00 27.59  ? 502  EZ8 F NBC 1 
HETATM 6892 C  CBP . EZ8 NA 2 .   ? 11.994  9.862   79.680  1.00 30.94  ? 502  EZ8 F CBP 1 
HETATM 6893 C  CAS . EZ8 NA 2 .   ? 12.802  9.152   80.744  1.00 30.73  ? 502  EZ8 F CAS 1 
HETATM 6894 N  NAA . EZ8 NA 2 .   ? 14.129  9.765   80.796  1.00 31.92  ? 502  EZ8 F NAA 1 
HETATM 6895 CA CA  . CA  OA 3 .   ? 10.079  15.959  78.214  1.00 28.71  ? 503  CA  F CA  1 
HETATM 6896 CA CA  . CA  PA 3 .   ? 7.189   22.225  82.842  1.00 26.95  ? 504  CA  F CA  1 
HETATM 6897 CA CA  . CA  QA 3 .   ? 3.925   23.134  86.621  1.00 50.03  ? 505  CA  F CA  1 
HETATM 6898 CL CL  . CL  RA 4 .   ? 22.400  6.422   97.193  1.00 61.78  ? 506  CL  F CL  1 
HETATM 6899 O  O   . HOH SA 5 .   ? -4.860  3.588   8.030   1.00 44.58  ? 1101 HOH A O   1 
HETATM 6900 O  O   . HOH SA 5 .   ? 7.228   5.898   8.319   1.00 35.56  ? 1102 HOH A O   1 
HETATM 6901 O  O   . HOH SA 5 .   ? -5.142  -11.226 28.980  1.00 38.68  ? 1103 HOH A O   1 
HETATM 6902 O  O   . HOH SA 5 .   ? -12.199 -9.067  12.253  1.00 52.11  ? 1104 HOH A O   1 
HETATM 6903 O  O   . HOH SA 5 .   ? -1.698  1.095   40.354  1.00 49.11  ? 1105 HOH A O   1 
HETATM 6904 O  O   . HOH SA 5 .   ? -3.562  -6.995  5.338   1.00 42.01  ? 1106 HOH A O   1 
HETATM 6905 O  O   . HOH SA 5 .   ? -2.827  -5.664  24.875  1.00 44.63  ? 1107 HOH A O   1 
HETATM 6906 O  O   . HOH SA 5 .   ? 9.516   -6.808  10.586  1.00 45.69  ? 1108 HOH A O   1 
HETATM 6907 O  O   . HOH SA 5 .   ? -4.454  4.287   40.482  1.00 40.12  ? 1109 HOH A O   1 
HETATM 6908 O  O   . HOH SA 5 .   ? 3.482   15.233  8.028   1.00 38.14  ? 1110 HOH A O   1 
HETATM 6909 O  O   . HOH SA 5 .   ? 13.086  5.135   12.131  1.00 37.47  ? 1111 HOH A O   1 
HETATM 6910 O  O   . HOH SA 5 .   ? 14.435  -5.087  19.623  1.00 44.45  ? 1112 HOH A O   1 
HETATM 6911 O  O   . HOH SA 5 .   ? 7.461   -18.432 8.614   1.00 34.42  ? 1113 HOH A O   1 
HETATM 6912 O  O   . HOH SA 5 .   ? 4.065   10.143  12.159  1.00 33.95  ? 1114 HOH A O   1 
HETATM 6913 O  O   . HOH SA 5 .   ? -8.207  -14.162 13.643  1.00 36.26  ? 1115 HOH A O   1 
HETATM 6914 O  O   . HOH SA 5 .   ? -10.654 -0.511  6.812   1.00 44.98  ? 1116 HOH A O   1 
HETATM 6915 O  O   . HOH SA 5 .   ? -5.680  6.931   30.891  1.00 46.00  ? 1117 HOH A O   1 
HETATM 6916 O  O   . HOH SA 5 .   ? 8.376   3.298   7.319   1.00 23.92  ? 1118 HOH A O   1 
HETATM 6917 O  O   . HOH SA 5 .   ? -1.045  7.185   14.538  1.00 32.98  ? 1119 HOH A O   1 
HETATM 6918 O  O   . HOH SA 5 .   ? 10.332  7.296   29.139  1.00 38.22  ? 1120 HOH A O   1 
HETATM 6919 O  O   . HOH SA 5 .   ? -7.682  8.144   29.012  1.00 34.85  ? 1121 HOH A O   1 
HETATM 6920 O  O   . HOH SA 5 .   ? -13.634 -13.876 24.699  1.00 55.46  ? 1122 HOH A O   1 
HETATM 6921 O  O   . HOH SA 5 .   ? -20.184 -6.706  29.936  1.00 29.52  ? 1123 HOH A O   1 
HETATM 6922 O  O   . HOH SA 5 .   ? 8.917   -8.214  26.300  1.00 46.26  ? 1124 HOH A O   1 
HETATM 6923 O  O   . HOH SA 5 .   ? -0.824  11.394  28.657  1.00 33.94  ? 1125 HOH A O   1 
HETATM 6924 O  O   . HOH SA 5 .   ? 1.486   -4.821  33.198  1.00 34.55  ? 1126 HOH A O   1 
HETATM 6925 O  O   . HOH SA 5 .   ? -7.257  -6.694  8.142   1.00 31.39  ? 1127 HOH A O   1 
HETATM 6926 O  O   . HOH SA 5 .   ? 7.048   12.461  20.238  1.00 38.27  ? 1128 HOH A O   1 
HETATM 6927 O  O   . HOH SA 5 .   ? 9.617   2.743   12.981  1.00 30.03  ? 1129 HOH A O   1 
HETATM 6928 O  O   . HOH SA 5 .   ? -20.842 -1.545  31.916  1.00 36.52  ? 1130 HOH A O   1 
HETATM 6929 O  O   . HOH SA 5 .   ? -9.019  4.471   31.596  1.00 35.19  ? 1131 HOH A O   1 
HETATM 6930 O  O   . HOH SA 5 .   ? -17.566 -6.994  30.601  1.00 50.10  ? 1132 HOH A O   1 
HETATM 6931 O  O   . HOH SA 5 .   ? -9.540  4.081   15.735  1.00 36.17  ? 1133 HOH A O   1 
HETATM 6932 O  O   . HOH SA 5 .   ? -10.147 -11.933 11.601  1.00 46.58  ? 1134 HOH A O   1 
HETATM 6933 O  O   . HOH SA 5 .   ? 9.103   0.708   32.312  1.00 51.94  ? 1135 HOH A O   1 
HETATM 6934 O  O   . HOH SA 5 .   ? 2.065   9.730   24.858  1.00 31.32  ? 1136 HOH A O   1 
HETATM 6935 O  O   . HOH SA 5 .   ? 1.944   8.523   11.870  1.00 27.47  ? 1137 HOH A O   1 
HETATM 6936 O  O   . HOH SA 5 .   ? 0.581   8.402   34.287  1.00 45.07  ? 1138 HOH A O   1 
HETATM 6937 O  O   . HOH SA 5 .   ? 6.604   3.167   5.276   1.00 37.95  ? 1139 HOH A O   1 
HETATM 6938 O  O   . HOH SA 5 .   ? -3.104  -0.790  36.278  1.00 34.26  ? 1140 HOH A O   1 
HETATM 6939 O  O   . HOH SA 5 .   ? 4.764   -0.833  8.258   1.00 31.27  ? 1141 HOH A O   1 
HETATM 6940 O  O   . HOH SA 5 .   ? -3.826  -12.523 35.738  1.00 36.76  ? 1142 HOH A O   1 
HETATM 6941 O  O   . HOH SA 5 .   ? 12.730  -5.395  26.647  1.00 46.84  ? 1143 HOH A O   1 
HETATM 6942 O  O   . HOH SA 5 .   ? 11.392  4.060   6.677   1.00 32.02  ? 1144 HOH A O   1 
HETATM 6943 O  O   . HOH SA 5 .   ? 8.414   9.936   18.406  1.00 38.65  ? 1145 HOH A O   1 
HETATM 6944 O  O   . HOH SA 5 .   ? -19.813 -3.643  30.184  1.00 37.80  ? 1146 HOH A O   1 
HETATM 6945 O  O   . HOH SA 5 .   ? 10.762  4.998   14.370  1.00 40.96  ? 1147 HOH A O   1 
HETATM 6946 O  O   . HOH SA 5 .   ? -19.199 6.388   21.565  1.00 51.32  ? 1148 HOH A O   1 
HETATM 6947 O  O   . HOH SA 5 .   ? 9.971   6.782   20.342  1.00 34.33  ? 1149 HOH A O   1 
HETATM 6948 O  O   . HOH SA 5 .   ? -7.783  8.333   24.904  1.00 32.22  ? 1150 HOH A O   1 
HETATM 6949 O  O   . HOH SA 5 .   ? -23.827 0.024   36.531  1.00 47.02  ? 1151 HOH A O   1 
HETATM 6950 O  O   . HOH SA 5 .   ? -10.075 -10.814 24.515  1.00 47.88  ? 1152 HOH A O   1 
HETATM 6951 O  O   . HOH SA 5 .   ? 4.425   -1.505  31.793  1.00 40.62  ? 1153 HOH A O   1 
HETATM 6952 O  O   . HOH SA 5 .   ? 6.622   13.363  29.049  1.00 42.79  ? 1154 HOH A O   1 
HETATM 6953 O  O   . HOH SA 5 .   ? 2.330   -10.847 23.930  1.00 39.17  ? 1155 HOH A O   1 
HETATM 6954 O  O   A HOH SA 5 .   ? -20.853 -12.793 21.665  0.50 22.53  ? 1156 HOH A O   1 
HETATM 6955 O  O   B HOH SA 5 .   ? -18.973 -12.702 22.407  0.50 23.38  ? 1156 HOH A O   1 
HETATM 6956 O  O   . HOH SA 5 .   ? -1.739  16.849  15.520  1.00 53.69  ? 1157 HOH A O   1 
HETATM 6957 O  O   . HOH SA 5 .   ? 10.331  -6.337  20.391  1.00 38.96  ? 1158 HOH A O   1 
HETATM 6958 O  O   . HOH SA 5 .   ? -30.342 -0.786  33.033  1.00 58.79  ? 1159 HOH A O   1 
HETATM 6959 O  O   . HOH SA 5 .   ? -8.012  7.475   9.827   1.00 54.15  ? 1160 HOH A O   1 
HETATM 6960 O  O   . HOH SA 5 .   ? 14.526  -1.070  7.149   1.00 39.21  ? 1161 HOH A O   1 
HETATM 6961 O  O   . HOH SA 5 .   ? -1.183  -12.035 15.870  1.00 61.03  ? 1162 HOH A O   1 
HETATM 6962 O  O   . HOH SA 5 .   ? -24.275 -2.994  24.559  1.00 39.28  ? 1163 HOH A O   1 
HETATM 6963 O  O   . HOH SA 5 .   ? -23.009 1.611   27.765  1.00 54.27  ? 1164 HOH A O   1 
HETATM 6964 O  O   . HOH SA 5 .   ? -21.246 3.185   17.659  1.00 53.80  ? 1165 HOH A O   1 
HETATM 6965 O  O   . HOH SA 5 .   ? 7.007   15.100  11.904  1.00 38.99  ? 1166 HOH A O   1 
HETATM 6966 O  O   . HOH SA 5 .   ? -17.616 -12.068 26.843  1.00 52.16  ? 1167 HOH A O   1 
HETATM 6967 O  O   . HOH SA 5 .   ? 2.351   10.706  4.598   1.00 60.13  ? 1168 HOH A O   1 
HETATM 6968 O  O   . HOH SA 5 .   ? -0.014  -9.925  5.561   1.00 36.88  ? 1169 HOH A O   1 
HETATM 6969 O  O   . HOH SA 5 .   ? -12.912 7.328   21.544  1.00 49.46  ? 1170 HOH A O   1 
HETATM 6970 O  O   . HOH SA 5 .   ? 6.679   8.875   5.345   1.00 57.45  ? 1171 HOH A O   1 
HETATM 6971 O  O   A HOH SA 5 .   ? 13.887  1.021   24.550  0.50 24.31  ? 1172 HOH A O   1 
HETATM 6972 O  O   B HOH SA 5 .   ? 13.601  3.091   25.085  0.50 25.68  ? 1172 HOH A O   1 
HETATM 6973 O  O   . HOH SA 5 .   ? -14.406 11.027  24.633  1.00 57.83  ? 1173 HOH A O   1 
HETATM 6974 O  O   . HOH SA 5 .   ? -11.718 -15.383 24.838  1.00 55.35  ? 1174 HOH A O   1 
HETATM 6975 O  O   . HOH SA 5 .   ? -10.630 -4.008  35.313  1.00 47.88  ? 1175 HOH A O   1 
HETATM 6976 O  O   . HOH SA 5 .   ? -11.960 4.571   8.957   1.00 39.40  ? 1176 HOH A O   1 
HETATM 6977 O  O   . HOH SA 5 .   ? -25.068 11.170  37.776  1.00 55.31  ? 1177 HOH A O   1 
HETATM 6978 O  O   . HOH SA 5 .   ? 4.660   7.521   32.303  1.00 48.98  ? 1178 HOH A O   1 
HETATM 6979 O  O   . HOH SA 5 .   ? -1.239  -13.856 18.667  1.00 55.10  ? 1179 HOH A O   1 
HETATM 6980 O  O   . HOH SA 5 .   ? 4.093   -2.517  36.449  1.00 52.16  ? 1180 HOH A O   1 
HETATM 6981 O  O   . HOH SA 5 .   ? 2.035   -15.975 30.551  1.00 55.86  ? 1181 HOH A O   1 
HETATM 6982 O  O   . HOH SA 5 .   ? -0.759  -4.830  36.098  1.00 52.77  ? 1182 HOH A O   1 
HETATM 6983 O  O   . HOH SA 5 .   ? -20.839 -0.935  21.078  1.00 46.59  ? 1183 HOH A O   1 
HETATM 6984 O  O   . HOH SA 5 .   ? -21.139 3.241   26.511  1.00 50.36  ? 1184 HOH A O   1 
HETATM 6985 O  O   . HOH SA 5 .   ? -0.669  10.675  33.782  1.00 56.06  ? 1185 HOH A O   1 
HETATM 6986 O  O   . HOH SA 5 .   ? 11.205  -3.485  2.733   1.00 44.32  ? 1186 HOH A O   1 
HETATM 6987 O  O   . HOH SA 5 .   ? -26.616 1.285   28.477  1.00 40.30  ? 1187 HOH A O   1 
HETATM 6988 O  O   . HOH SA 5 .   ? -8.936  6.509   14.997  1.00 38.32  ? 1188 HOH A O   1 
HETATM 6989 O  O   . HOH SA 5 .   ? -21.990 0.576   18.242  1.00 60.04  ? 1189 HOH A O   1 
HETATM 6990 O  O   . HOH SA 5 .   ? -6.225  -13.211 9.139   1.00 51.50  ? 1190 HOH A O   1 
HETATM 6991 O  O   . HOH SA 5 .   ? -24.686 -0.363  25.152  1.00 56.87  ? 1191 HOH A O   1 
HETATM 6992 O  O   . HOH SA 5 .   ? -13.820 -16.900 24.153  1.00 52.05  ? 1192 HOH A O   1 
HETATM 6993 O  O   . HOH SA 5 .   ? 11.350  8.530   5.912   1.00 49.66  ? 1193 HOH A O   1 
HETATM 6994 O  O   . HOH SA 5 .   ? -29.032 -7.391  30.314  1.00 49.54  ? 1194 HOH A O   1 
HETATM 6995 O  O   . HOH SA 5 .   ? -28.187 0.672   26.501  1.00 39.72  ? 1195 HOH A O   1 
HETATM 6996 O  O   . HOH TA 5 .   ? 5.763   13.347  73.136  1.00 35.41  ? 1101 HOH B O   1 
HETATM 6997 O  O   . HOH TA 5 .   ? -20.460 8.528   53.644  1.00 44.81  ? 1102 HOH B O   1 
HETATM 6998 O  O   . HOH TA 5 .   ? -17.305 -5.480  76.171  1.00 54.35  ? 1103 HOH B O   1 
HETATM 6999 O  O   . HOH TA 5 .   ? -10.155 -2.560  67.966  1.00 38.38  ? 1104 HOH B O   1 
HETATM 7000 O  O   . HOH TA 5 .   ? -11.062 4.192   44.699  1.00 30.95  ? 1105 HOH B O   1 
HETATM 7001 O  O   . HOH TA 5 .   ? 3.243   5.741   53.564  1.00 37.21  ? 1106 HOH B O   1 
HETATM 7002 O  O   . HOH TA 5 .   ? -16.942 -7.080  63.971  1.00 43.76  ? 1107 HOH B O   1 
HETATM 7003 O  O   . HOH TA 5 .   ? -17.533 16.379  47.128  1.00 28.63  ? 1108 HOH B O   1 
HETATM 7004 O  O   . HOH TA 5 .   ? -5.527  22.488  61.698  1.00 35.77  ? 1109 HOH B O   1 
HETATM 7005 O  O   . HOH TA 5 .   ? -11.172 19.198  67.603  1.00 32.75  ? 1110 HOH B O   1 
HETATM 7006 O  O   . HOH TA 5 .   ? -3.585  2.370   50.456  1.00 41.29  ? 1111 HOH B O   1 
HETATM 7007 O  O   . HOH TA 5 .   ? -2.095  20.640  64.849  1.00 36.40  ? 1112 HOH B O   1 
HETATM 7008 O  O   . HOH TA 5 .   ? -12.924 20.244  51.807  1.00 29.37  ? 1113 HOH B O   1 
HETATM 7009 O  O   . HOH TA 5 .   ? -6.390  22.373  54.849  1.00 43.70  ? 1114 HOH B O   1 
HETATM 7010 O  O   . HOH TA 5 .   ? -8.511  22.840  46.709  1.00 34.12  ? 1115 HOH B O   1 
HETATM 7011 O  O   . HOH TA 5 .   ? -10.394 9.952   38.766  1.00 41.90  ? 1116 HOH B O   1 
HETATM 7012 O  O   . HOH TA 5 .   ? -24.290 6.883   55.468  1.00 49.48  ? 1117 HOH B O   1 
HETATM 7013 O  O   . HOH TA 5 .   ? -20.659 18.601  52.922  1.00 56.54  ? 1118 HOH B O   1 
HETATM 7014 O  O   . HOH TA 5 .   ? 4.416   17.668  55.813  1.00 36.69  ? 1119 HOH B O   1 
HETATM 7015 O  O   . HOH TA 5 .   ? -5.601  3.684   62.850  1.00 35.98  ? 1120 HOH B O   1 
HETATM 7016 O  O   . HOH TA 5 .   ? 3.376   4.691   63.993  1.00 36.94  ? 1121 HOH B O   1 
HETATM 7017 O  O   . HOH TA 5 .   ? -4.020  12.616  72.698  1.00 29.16  ? 1122 HOH B O   1 
HETATM 7018 O  O   . HOH TA 5 .   ? -5.022  17.844  48.411  1.00 43.96  ? 1123 HOH B O   1 
HETATM 7019 O  O   . HOH TA 5 .   ? 3.786   5.467   50.581  1.00 33.58  ? 1124 HOH B O   1 
HETATM 7020 O  O   . HOH TA 5 .   ? -13.252 6.107   43.294  1.00 54.71  ? 1125 HOH B O   1 
HETATM 7021 O  O   . HOH TA 5 .   ? -14.583 16.848  46.604  1.00 28.21  ? 1126 HOH B O   1 
HETATM 7022 O  O   . HOH TA 5 .   ? -3.442  -0.733  57.295  1.00 32.69  ? 1127 HOH B O   1 
HETATM 7023 O  O   . HOH TA 5 .   ? -5.835  24.436  49.758  1.00 48.03  ? 1128 HOH B O   1 
HETATM 7024 O  O   . HOH TA 5 .   ? 1.769   2.234   53.492  1.00 47.41  ? 1129 HOH B O   1 
HETATM 7025 O  O   . HOH TA 5 .   ? -22.101 2.889   52.514  1.00 38.09  ? 1130 HOH B O   1 
HETATM 7026 O  O   . HOH TA 5 .   ? -17.935 -4.781  60.081  1.00 20.90  ? 1131 HOH B O   1 
HETATM 7027 O  O   . HOH TA 5 .   ? -15.790 6.110   40.963  1.00 49.35  ? 1132 HOH B O   1 
HETATM 7028 O  O   . HOH TA 5 .   ? -8.706  13.628  47.004  1.00 18.48  ? 1133 HOH B O   1 
HETATM 7029 O  O   . HOH TA 5 .   ? -15.715 20.023  66.737  1.00 53.54  ? 1134 HOH B O   1 
HETATM 7030 O  O   . HOH TA 5 .   ? 0.550   14.548  49.227  1.00 31.99  ? 1135 HOH B O   1 
HETATM 7031 O  O   . HOH TA 5 .   ? -10.511 0.504   79.924  1.00 34.45  ? 1136 HOH B O   1 
HETATM 7032 O  O   . HOH TA 5 .   ? -10.006 24.564  57.577  1.00 37.80  ? 1137 HOH B O   1 
HETATM 7033 O  O   . HOH TA 5 .   ? -3.509  -2.464  66.561  1.00 34.45  ? 1138 HOH B O   1 
HETATM 7034 O  O   . HOH TA 5 .   ? 3.493   8.246   61.339  1.00 37.80  ? 1139 HOH B O   1 
HETATM 7035 O  O   . HOH TA 5 .   ? -1.419  14.025  71.588  1.00 40.79  ? 1140 HOH B O   1 
HETATM 7036 O  O   . HOH TA 5 .   ? -22.687 11.866  59.139  1.00 38.39  ? 1141 HOH B O   1 
HETATM 7037 O  O   . HOH TA 5 .   ? -21.939 2.315   57.160  1.00 24.25  ? 1142 HOH B O   1 
HETATM 7038 O  O   . HOH TA 5 .   ? 2.136   15.218  71.392  1.00 42.90  ? 1143 HOH B O   1 
HETATM 7039 O  O   . HOH TA 5 .   ? -9.446  5.279   81.871  1.00 37.69  ? 1144 HOH B O   1 
HETATM 7040 O  O   . HOH TA 5 .   ? -5.608  16.633  71.072  1.00 42.46  ? 1145 HOH B O   1 
HETATM 7041 O  O   . HOH TA 5 .   ? -9.351  15.153  40.531  1.00 41.74  ? 1146 HOH B O   1 
HETATM 7042 O  O   . HOH TA 5 .   ? -12.640 27.563  52.947  1.00 64.98  ? 1147 HOH B O   1 
HETATM 7043 O  O   . HOH TA 5 .   ? -17.598 14.043  44.999  1.00 29.91  ? 1148 HOH B O   1 
HETATM 7044 O  O   . HOH TA 5 .   ? -14.152 16.755  57.348  1.00 34.46  ? 1149 HOH B O   1 
HETATM 7045 O  O   . HOH TA 5 .   ? 5.652   11.719  62.746  1.00 52.75  ? 1150 HOH B O   1 
HETATM 7046 O  O   . HOH TA 5 .   ? -14.602 10.049  38.215  1.00 46.85  ? 1151 HOH B O   1 
HETATM 7047 O  O   . HOH TA 5 .   ? -17.174 3.498   81.014  1.00 44.41  ? 1152 HOH B O   1 
HETATM 7048 O  O   . HOH TA 5 .   ? -14.588 18.537  53.190  1.00 27.60  ? 1153 HOH B O   1 
HETATM 7049 O  O   . HOH TA 5 .   ? -12.522 -2.088  55.470  1.00 49.92  ? 1154 HOH B O   1 
HETATM 7050 O  O   . HOH TA 5 .   ? -14.597 14.432  44.370  1.00 23.33  ? 1155 HOH B O   1 
HETATM 7051 O  O   . HOH TA 5 .   ? -10.361 3.166   80.049  1.00 33.93  ? 1156 HOH B O   1 
HETATM 7052 O  O   . HOH TA 5 .   ? 3.032   7.864   69.840  1.00 42.72  ? 1157 HOH B O   1 
HETATM 7053 O  O   . HOH TA 5 .   ? -6.277  19.211  63.480  1.00 40.94  ? 1158 HOH B O   1 
HETATM 7054 O  O   . HOH TA 5 .   ? -18.082 14.550  75.470  1.00 45.95  ? 1159 HOH B O   1 
HETATM 7055 O  O   . HOH TA 5 .   ? -3.331  19.311  60.406  1.00 27.17  ? 1160 HOH B O   1 
HETATM 7056 O  O   . HOH TA 5 .   ? -0.702  5.873   45.112  1.00 37.56  ? 1161 HOH B O   1 
HETATM 7057 O  O   . HOH TA 5 .   ? 4.060   3.944   59.653  1.00 48.54  ? 1162 HOH B O   1 
HETATM 7058 O  O   . HOH TA 5 .   ? -25.292 12.232  62.708  1.00 47.40  ? 1163 HOH B O   1 
HETATM 7059 O  O   . HOH TA 5 .   ? -7.359  15.777  47.130  1.00 36.42  ? 1164 HOH B O   1 
HETATM 7060 O  O   . HOH TA 5 .   ? -2.324  4.604   49.096  1.00 30.82  ? 1165 HOH B O   1 
HETATM 7061 O  O   . HOH TA 5 .   ? -21.677 0.282   66.045  1.00 57.65  ? 1166 HOH B O   1 
HETATM 7062 O  O   . HOH TA 5 .   ? 2.920   2.922   62.014  1.00 38.29  ? 1167 HOH B O   1 
HETATM 7063 O  O   . HOH TA 5 .   ? -24.043 16.556  63.781  1.00 57.18  ? 1168 HOH B O   1 
HETATM 7064 O  O   . HOH TA 5 .   ? -12.439 -0.410  52.667  1.00 38.92  ? 1169 HOH B O   1 
HETATM 7065 O  O   . HOH TA 5 .   ? -15.568 9.878   47.833  1.00 21.39  ? 1170 HOH B O   1 
HETATM 7066 O  O   . HOH TA 5 .   ? -17.277 11.575  47.294  1.00 34.04  ? 1171 HOH B O   1 
HETATM 7067 O  O   . HOH TA 5 .   ? 3.643   17.648  66.300  1.00 44.21  ? 1172 HOH B O   1 
HETATM 7068 O  O   . HOH TA 5 .   ? -17.911 12.581  64.625  1.00 38.62  ? 1173 HOH B O   1 
HETATM 7069 O  O   . HOH TA 5 .   ? -20.365 0.706   49.621  1.00 31.83  ? 1174 HOH B O   1 
HETATM 7070 O  O   . HOH TA 5 .   ? -5.270  20.121  51.798  1.00 37.46  ? 1175 HOH B O   1 
HETATM 7071 O  O   . HOH TA 5 .   ? -18.663 6.815   76.502  1.00 41.21  ? 1176 HOH B O   1 
HETATM 7072 O  O   . HOH TA 5 .   ? 3.729   18.784  62.920  1.00 57.72  ? 1177 HOH B O   1 
HETATM 7073 O  O   . HOH TA 5 .   ? -14.212 16.056  74.080  1.00 37.24  ? 1178 HOH B O   1 
HETATM 7074 O  O   . HOH TA 5 .   ? -18.286 4.574   68.095  1.00 35.40  ? 1179 HOH B O   1 
HETATM 7075 O  O   . HOH TA 5 .   ? 5.576   8.756   68.653  1.00 55.83  ? 1180 HOH B O   1 
HETATM 7076 O  O   . HOH TA 5 .   ? -15.221 20.752  45.028  1.00 45.87  ? 1181 HOH B O   1 
HETATM 7077 O  O   . HOH TA 5 .   ? -17.638 21.134  63.169  1.00 48.62  ? 1182 HOH B O   1 
HETATM 7078 O  O   . HOH TA 5 .   ? -20.439 12.221  41.939  1.00 49.27  ? 1183 HOH B O   1 
HETATM 7079 O  O   . HOH TA 5 .   ? 2.508   23.224  59.476  1.00 38.46  ? 1184 HOH B O   1 
HETATM 7080 O  O   . HOH TA 5 .   ? -6.539  3.227   78.788  1.00 48.00  ? 1185 HOH B O   1 
HETATM 7081 O  O   . HOH TA 5 .   ? -9.080  16.725  68.330  1.00 39.97  ? 1186 HOH B O   1 
HETATM 7082 O  O   . HOH TA 5 .   ? -3.014  17.604  51.043  1.00 25.08  ? 1187 HOH B O   1 
HETATM 7083 O  O   . HOH TA 5 .   ? -21.496 14.086  70.596  1.00 37.25  ? 1188 HOH B O   1 
HETATM 7084 O  O   . HOH TA 5 .   ? -0.532  -2.612  57.052  1.00 49.83  ? 1189 HOH B O   1 
HETATM 7085 O  O   A HOH TA 5 .   ? -9.819  -5.070  57.307  0.50 27.30  ? 1190 HOH B O   1 
HETATM 7086 O  O   B HOH TA 5 .   ? -10.225 -3.283  56.746  0.50 37.98  ? 1190 HOH B O   1 
HETATM 7087 O  O   . HOH TA 5 .   ? -13.666 15.720  42.051  1.00 28.92  ? 1191 HOH B O   1 
HETATM 7088 O  O   . HOH TA 5 .   ? 2.927   13.792  50.293  1.00 47.25  ? 1192 HOH B O   1 
HETATM 7089 O  O   . HOH TA 5 .   ? 3.649   8.182   55.018  1.00 44.44  ? 1193 HOH B O   1 
HETATM 7090 O  O   . HOH TA 5 .   ? -3.624  24.928  55.414  1.00 39.08  ? 1194 HOH B O   1 
HETATM 7091 O  O   . HOH TA 5 .   ? 2.900   -3.738  68.349  1.00 48.26  ? 1195 HOH B O   1 
HETATM 7092 O  O   . HOH TA 5 .   ? -17.517 16.826  55.419  1.00 48.24  ? 1196 HOH B O   1 
HETATM 7093 O  O   . HOH TA 5 .   ? 5.269   16.821  52.665  1.00 57.75  ? 1197 HOH B O   1 
HETATM 7094 O  O   . HOH TA 5 .   ? 3.557   4.874   68.217  1.00 43.55  ? 1198 HOH B O   1 
HETATM 7095 O  O   . HOH TA 5 .   ? -1.211  6.532   42.606  1.00 43.38  ? 1199 HOH B O   1 
HETATM 7096 O  O   . HOH TA 5 .   ? -11.750 16.095  70.964  1.00 54.88  ? 1200 HOH B O   1 
HETATM 7097 O  O   . HOH TA 5 .   ? -17.446 14.938  64.251  1.00 51.79  ? 1201 HOH B O   1 
HETATM 7098 O  O   . HOH TA 5 .   ? 0.408   21.388  64.833  1.00 37.47  ? 1202 HOH B O   1 
HETATM 7099 O  O   . HOH TA 5 .   ? -4.214  20.287  62.853  1.00 37.34  ? 1203 HOH B O   1 
HETATM 7100 O  O   . HOH TA 5 .   ? 2.205   -6.881  61.329  1.00 56.70  ? 1204 HOH B O   1 
HETATM 7101 O  O   . HOH TA 5 .   ? -21.955 9.489   75.940  1.00 47.93  ? 1205 HOH B O   1 
HETATM 7102 O  O   A HOH TA 5 .   ? -14.640 0.576   39.374  0.50 23.05  ? 1206 HOH B O   1 
HETATM 7103 O  O   B HOH TA 5 .   ? -15.034 1.595   41.183  0.50 36.02  ? 1206 HOH B O   1 
HETATM 7104 O  O   . HOH TA 5 .   ? -4.422  7.714   39.641  1.00 48.27  ? 1207 HOH B O   1 
HETATM 7105 O  O   . HOH TA 5 .   ? -6.412  22.491  45.366  1.00 42.68  ? 1208 HOH B O   1 
HETATM 7106 O  O   . HOH TA 5 .   ? -1.584  2.830   76.749  1.00 40.29  ? 1209 HOH B O   1 
HETATM 7107 O  O   . HOH TA 5 .   ? -5.600  13.953  81.025  1.00 51.60  ? 1210 HOH B O   1 
HETATM 7108 O  O   . HOH TA 5 .   ? -23.394 3.436   48.645  1.00 43.38  ? 1211 HOH B O   1 
HETATM 7109 O  O   . HOH TA 5 .   ? -16.279 16.746  44.064  1.00 29.10  ? 1212 HOH B O   1 
HETATM 7110 O  O   . HOH TA 5 .   ? 3.803   -4.079  62.100  1.00 39.47  ? 1213 HOH B O   1 
HETATM 7111 O  O   . HOH TA 5 .   ? -16.252 18.251  57.697  1.00 36.27  ? 1214 HOH B O   1 
HETATM 7112 O  O   . HOH TA 5 .   ? 7.680   15.805  62.768  1.00 49.70  ? 1215 HOH B O   1 
HETATM 7113 O  O   . HOH TA 5 .   ? -3.434  22.493  66.317  1.00 39.87  ? 1216 HOH B O   1 
HETATM 7114 O  O   . HOH TA 5 .   ? -10.116 24.941  44.929  1.00 40.19  ? 1217 HOH B O   1 
HETATM 7115 O  O   . HOH TA 5 .   ? -17.953 22.058  60.174  1.00 54.80  ? 1218 HOH B O   1 
HETATM 7116 O  O   . HOH TA 5 .   ? -14.558 24.164  45.847  1.00 43.12  ? 1219 HOH B O   1 
HETATM 7117 O  O   . HOH TA 5 .   ? -21.200 6.785   76.180  1.00 46.60  ? 1220 HOH B O   1 
HETATM 7118 O  O   . HOH TA 5 .   ? -1.720  3.465   79.084  1.00 52.06  ? 1221 HOH B O   1 
HETATM 7119 O  O   . HOH TA 5 .   ? -0.877  26.747  57.407  1.00 54.32  ? 1222 HOH B O   1 
HETATM 7120 O  O   . HOH TA 5 .   ? -21.823 18.270  56.109  1.00 45.72  ? 1223 HOH B O   1 
HETATM 7121 O  O   . HOH TA 5 .   ? -13.950 -1.447  87.975  1.00 53.02  ? 1224 HOH B O   1 
HETATM 7122 O  O   . HOH TA 5 .   ? -2.279  25.426  64.583  1.00 38.42  ? 1225 HOH B O   1 
HETATM 7123 O  O   . HOH UA 5 .   ? -6.071  -23.422 63.013  1.00 38.74  ? 1101 HOH C O   1 
HETATM 7124 O  O   . HOH UA 5 .   ? -19.401 -1.470  51.134  1.00 28.21  ? 1102 HOH C O   1 
HETATM 7125 O  O   . HOH UA 5 .   ? -13.588 -27.224 57.235  1.00 25.45  ? 1103 HOH C O   1 
HETATM 7126 O  O   . HOH UA 5 .   ? -24.598 -5.755  48.877  1.00 53.62  ? 1104 HOH C O   1 
HETATM 7127 O  O   . HOH UA 5 .   ? -9.410  -16.537 70.090  1.00 45.76  ? 1105 HOH C O   1 
HETATM 7128 O  O   . HOH UA 5 .   ? -26.712 -13.529 36.235  1.00 48.45  ? 1106 HOH C O   1 
HETATM 7129 O  O   . HOH UA 5 .   ? -16.250 -23.490 52.698  1.00 33.61  ? 1107 HOH C O   1 
HETATM 7130 O  O   . HOH UA 5 .   ? -11.721 -7.517  63.860  1.00 49.58  ? 1108 HOH C O   1 
HETATM 7131 O  O   . HOH UA 5 .   ? -21.227 -8.899  59.509  1.00 34.03  ? 1109 HOH C O   1 
HETATM 7132 O  O   . HOH UA 5 .   ? -8.152  -27.783 40.904  1.00 33.14  ? 1110 HOH C O   1 
HETATM 7133 O  O   . HOH UA 5 .   ? -10.623 0.671   64.967  1.00 33.32  ? 1111 HOH C O   1 
HETATM 7134 O  O   . HOH UA 5 .   ? -13.047 -23.407 62.925  1.00 31.79  ? 1112 HOH C O   1 
HETATM 7135 O  O   . HOH UA 5 .   ? -1.883  -12.289 39.985  1.00 30.43  ? 1113 HOH C O   1 
HETATM 7136 O  O   . HOH UA 5 .   ? -6.586  -22.361 33.870  1.00 43.53  ? 1114 HOH C O   1 
HETATM 7137 O  O   . HOH UA 5 .   ? -22.978 -8.410  55.095  1.00 23.90  ? 1115 HOH C O   1 
HETATM 7138 O  O   . HOH UA 5 .   ? -9.668  -10.868 44.345  1.00 31.56  ? 1116 HOH C O   1 
HETATM 7139 O  O   . HOH UA 5 .   ? -12.338 -19.776 34.653  1.00 26.94  ? 1117 HOH C O   1 
HETATM 7140 O  O   . HOH UA 5 .   ? -23.997 -21.394 38.903  1.00 41.57  ? 1118 HOH C O   1 
HETATM 7141 O  O   . HOH UA 5 .   ? -10.746 -22.570 66.512  1.00 46.96  ? 1119 HOH C O   1 
HETATM 7142 O  O   . HOH UA 5 .   ? -16.039 -13.905 62.828  1.00 37.61  ? 1120 HOH C O   1 
HETATM 7143 O  O   . HOH UA 5 .   ? -7.943  -20.430 60.465  1.00 24.95  ? 1121 HOH C O   1 
HETATM 7144 O  O   . HOH UA 5 .   ? -25.230 -17.339 53.760  1.00 43.07  ? 1122 HOH C O   1 
HETATM 7145 O  O   . HOH UA 5 .   ? -14.530 1.018   45.230  1.00 55.04  ? 1123 HOH C O   1 
HETATM 7146 O  O   . HOH UA 5 .   ? -8.274  -11.125 63.067  1.00 28.39  ? 1124 HOH C O   1 
HETATM 7147 O  O   . HOH UA 5 .   ? -20.465 -14.387 57.842  1.00 35.13  ? 1125 HOH C O   1 
HETATM 7148 O  O   . HOH UA 5 .   ? -12.425 -21.049 64.373  1.00 31.90  ? 1126 HOH C O   1 
HETATM 7149 O  O   . HOH UA 5 .   ? -27.618 -13.981 53.868  1.00 39.44  ? 1127 HOH C O   1 
HETATM 7150 O  O   . HOH UA 5 .   ? -16.149 -22.756 63.159  1.00 34.62  ? 1128 HOH C O   1 
HETATM 7151 O  O   . HOH UA 5 .   ? -27.133 -10.791 44.547  1.00 42.64  ? 1129 HOH C O   1 
HETATM 7152 O  O   . HOH UA 5 .   ? -15.405 -20.675 64.728  1.00 37.80  ? 1130 HOH C O   1 
HETATM 7153 O  O   . HOH UA 5 .   ? 1.492   -25.480 47.679  1.00 42.57  ? 1131 HOH C O   1 
HETATM 7154 O  O   . HOH UA 5 .   ? -25.399 -14.575 29.170  1.00 51.50  ? 1132 HOH C O   1 
HETATM 7155 O  O   . HOH UA 5 .   ? -5.048  -6.457  48.648  1.00 36.61  ? 1133 HOH C O   1 
HETATM 7156 O  O   . HOH UA 5 .   ? 0.644   -9.826  50.355  1.00 46.15  ? 1134 HOH C O   1 
HETATM 7157 O  O   . HOH UA 5 .   ? 0.302   -12.521 43.732  1.00 42.34  ? 1135 HOH C O   1 
HETATM 7158 O  O   . HOH UA 5 .   ? -8.184  -29.874 60.695  1.00 29.49  ? 1136 HOH C O   1 
HETATM 7159 O  O   . HOH UA 5 .   ? -6.926  -27.439 54.424  1.00 39.54  ? 1137 HOH C O   1 
HETATM 7160 O  O   . HOH UA 5 .   ? -12.030 -23.030 32.914  1.00 43.13  ? 1138 HOH C O   1 
HETATM 7161 O  O   . HOH UA 5 .   ? -14.975 -7.169  43.917  1.00 31.87  ? 1139 HOH C O   1 
HETATM 7162 O  O   . HOH UA 5 .   ? -17.811 -7.609  37.641  1.00 46.86  ? 1140 HOH C O   1 
HETATM 7163 O  O   . HOH UA 5 .   ? -24.141 -20.012 34.236  1.00 40.11  ? 1141 HOH C O   1 
HETATM 7164 O  O   . HOH UA 5 .   ? -22.992 -4.267  50.149  1.00 44.56  ? 1142 HOH C O   1 
HETATM 7165 O  O   . HOH UA 5 .   ? -20.404 -9.508  29.818  1.00 28.59  ? 1143 HOH C O   1 
HETATM 7166 O  O   . HOH UA 5 .   ? -18.480 -22.255 37.030  1.00 44.55  ? 1144 HOH C O   1 
HETATM 7167 O  O   . HOH UA 5 .   ? -4.260  -15.258 34.857  1.00 43.79  ? 1145 HOH C O   1 
HETATM 7168 O  O   . HOH UA 5 .   ? 3.585   -13.489 52.010  1.00 38.01  ? 1146 HOH C O   1 
HETATM 7169 O  O   . HOH UA 5 .   ? -11.767 -6.266  56.080  1.00 39.36  ? 1147 HOH C O   1 
HETATM 7170 O  O   . HOH UA 5 .   ? 0.263   -22.215 55.092  1.00 34.72  ? 1148 HOH C O   1 
HETATM 7171 O  O   . HOH UA 5 .   ? -10.011 -21.084 34.488  1.00 39.15  ? 1149 HOH C O   1 
HETATM 7172 O  O   . HOH UA 5 .   ? -10.195 -29.736 44.999  1.00 43.16  ? 1150 HOH C O   1 
HETATM 7173 O  O   . HOH UA 5 .   ? -15.515 -23.542 40.339  1.00 31.92  ? 1151 HOH C O   1 
HETATM 7174 O  O   . HOH UA 5 .   ? -9.844  -22.721 36.578  1.00 32.23  ? 1152 HOH C O   1 
HETATM 7175 O  O   . HOH UA 5 .   ? -17.538 -20.953 42.186  1.00 42.19  ? 1153 HOH C O   1 
HETATM 7176 O  O   . HOH UA 5 .   ? -0.663  -5.882  41.781  1.00 37.98  ? 1154 HOH C O   1 
HETATM 7177 O  O   . HOH UA 5 .   ? -23.565 -16.545 31.658  1.00 41.92  ? 1155 HOH C O   1 
HETATM 7178 O  O   . HOH UA 5 .   ? -11.219 -3.795  51.018  1.00 41.10  ? 1156 HOH C O   1 
HETATM 7179 O  O   . HOH UA 5 .   ? -1.872  -11.930 55.846  1.00 42.38  ? 1157 HOH C O   1 
HETATM 7180 O  O   . HOH UA 5 .   ? -22.166 -18.676 46.928  1.00 30.65  ? 1158 HOH C O   1 
HETATM 7181 O  O   . HOH UA 5 .   ? -15.344 -9.813  29.854  1.00 37.10  ? 1159 HOH C O   1 
HETATM 7182 O  O   . HOH UA 5 .   ? -8.411  -4.423  40.296  1.00 40.70  ? 1160 HOH C O   1 
HETATM 7183 O  O   A HOH UA 5 .   ? -13.796 -26.664 64.188  0.50 22.41  ? 1161 HOH C O   1 
HETATM 7184 O  O   B HOH UA 5 .   ? -15.911 -26.495 63.751  0.50 23.87  ? 1161 HOH C O   1 
HETATM 7185 O  O   . HOH UA 5 .   ? -1.301  -10.372 41.732  1.00 40.84  ? 1162 HOH C O   1 
HETATM 7186 O  O   . HOH UA 5 .   ? -11.534 -26.074 44.246  1.00 36.65  ? 1163 HOH C O   1 
HETATM 7187 O  O   . HOH UA 5 .   ? -14.151 -16.285 61.474  1.00 22.60  ? 1164 HOH C O   1 
HETATM 7188 O  O   . HOH UA 5 .   ? -17.889 -10.319 29.607  1.00 47.89  ? 1165 HOH C O   1 
HETATM 7189 O  O   . HOH UA 5 .   ? -25.370 -21.282 43.314  1.00 49.89  ? 1166 HOH C O   1 
HETATM 7190 O  O   . HOH UA 5 .   ? -12.881 -23.476 36.688  1.00 45.26  ? 1167 HOH C O   1 
HETATM 7191 O  O   . HOH UA 5 .   ? -15.880 -18.060 62.467  1.00 42.05  ? 1168 HOH C O   1 
HETATM 7192 O  O   . HOH UA 5 .   ? -13.031 -4.408  53.448  1.00 33.94  ? 1169 HOH C O   1 
HETATM 7193 O  O   . HOH UA 5 .   ? -27.141 -9.146  31.720  1.00 29.22  ? 1170 HOH C O   1 
HETATM 7194 O  O   . HOH UA 5 .   ? -26.201 -8.032  34.312  1.00 41.70  ? 1171 HOH C O   1 
HETATM 7195 O  O   . HOH UA 5 .   ? -7.360  -29.344 52.730  1.00 36.66  ? 1172 HOH C O   1 
HETATM 7196 O  O   . HOH UA 5 .   ? -7.738  -26.646 45.695  1.00 27.12  ? 1173 HOH C O   1 
HETATM 7197 O  O   . HOH UA 5 .   ? -2.117  -4.732  47.625  1.00 37.58  ? 1174 HOH C O   1 
HETATM 7198 O  O   . HOH UA 5 .   ? 1.605   -28.617 50.293  1.00 50.84  ? 1175 HOH C O   1 
HETATM 7199 O  O   . HOH UA 5 .   ? -11.046 -1.333  50.870  1.00 37.28  ? 1176 HOH C O   1 
HETATM 7200 O  O   . HOH UA 5 .   ? -0.925  -15.673 42.578  1.00 38.66  ? 1177 HOH C O   1 
HETATM 7201 O  O   . HOH UA 5 .   ? -20.353 -11.420 27.825  1.00 43.19  ? 1178 HOH C O   1 
HETATM 7202 O  O   . HOH UA 5 .   ? -3.261  -25.195 37.834  1.00 38.29  ? 1179 HOH C O   1 
HETATM 7203 O  O   . HOH UA 5 .   ? -4.129  -24.821 54.326  1.00 34.50  ? 1180 HOH C O   1 
HETATM 7204 O  O   . HOH UA 5 .   ? -14.205 -29.820 56.466  1.00 46.13  ? 1181 HOH C O   1 
HETATM 7205 O  O   . HOH UA 5 .   ? -23.400 -10.850 43.749  1.00 33.26  ? 1182 HOH C O   1 
HETATM 7206 O  O   . HOH UA 5 .   ? -6.497  -22.894 59.892  1.00 32.63  ? 1183 HOH C O   1 
HETATM 7207 O  O   . HOH UA 5 .   ? -22.807 -22.089 36.653  1.00 44.20  ? 1184 HOH C O   1 
HETATM 7208 O  O   . HOH UA 5 .   ? -15.588 -25.556 56.255  1.00 32.66  ? 1185 HOH C O   1 
HETATM 7209 O  O   . HOH UA 5 .   ? -1.068  -2.004  44.151  1.00 52.90  ? 1186 HOH C O   1 
HETATM 7210 O  O   . HOH UA 5 .   ? -5.943  -16.894 68.428  1.00 40.33  ? 1187 HOH C O   1 
HETATM 7211 O  O   . HOH UA 5 .   ? -21.344 -26.569 44.189  1.00 49.45  ? 1188 HOH C O   1 
HETATM 7212 O  O   . HOH UA 5 .   ? 2.184   -20.817 52.583  1.00 46.08  ? 1189 HOH C O   1 
HETATM 7213 O  O   . HOH UA 5 .   ? -18.387 -6.893  61.864  1.00 37.09  ? 1190 HOH C O   1 
HETATM 7214 O  O   . HOH UA 5 .   ? -30.920 -12.629 39.430  1.00 48.64  ? 1191 HOH C O   1 
HETATM 7215 O  O   . HOH UA 5 .   ? -19.570 -21.712 39.728  1.00 46.75  ? 1192 HOH C O   1 
HETATM 7216 O  O   . HOH UA 5 .   ? -23.136 -23.054 49.645  1.00 49.47  ? 1193 HOH C O   1 
HETATM 7217 O  O   . HOH UA 5 .   ? -1.850  -27.802 40.890  1.00 40.17  ? 1194 HOH C O   1 
HETATM 7218 O  O   . HOH UA 5 .   ? -25.131 -12.261 58.396  1.00 50.02  ? 1195 HOH C O   1 
HETATM 7219 O  O   . HOH UA 5 .   ? -21.985 -21.824 58.634  1.00 54.80  ? 1196 HOH C O   1 
HETATM 7220 O  O   . HOH UA 5 .   ? -31.396 -18.096 43.145  1.00 41.73  ? 1197 HOH C O   1 
HETATM 7221 O  O   . HOH UA 5 .   ? -2.975  -3.598  35.622  1.00 44.29  ? 1198 HOH C O   1 
HETATM 7222 O  O   A HOH UA 5 .   ? -5.839  -27.536 37.442  0.50 32.44  ? 1199 HOH C O   1 
HETATM 7223 O  O   B HOH UA 5 .   ? -7.486  -26.812 36.388  0.50 36.43  ? 1199 HOH C O   1 
HETATM 7224 O  O   . HOH UA 5 .   ? -26.519 -8.214  53.210  1.00 53.79  ? 1200 HOH C O   1 
HETATM 7225 O  O   . HOH UA 5 .   ? -2.232  -31.197 45.020  1.00 47.50  ? 1201 HOH C O   1 
HETATM 7226 O  O   . HOH UA 5 .   ? -0.909  -25.118 41.645  1.00 50.61  ? 1202 HOH C O   1 
HETATM 7227 O  O   . HOH UA 5 .   ? -27.589 -12.802 26.389  1.00 43.16  ? 1203 HOH C O   1 
HETATM 7228 O  O   . HOH UA 5 .   ? 1.240   -15.473 62.084  1.00 49.11  ? 1204 HOH C O   1 
HETATM 7229 O  O   . HOH UA 5 .   ? -4.056  -21.194 30.717  1.00 37.22  ? 1205 HOH C O   1 
HETATM 7230 O  O   . HOH UA 5 .   ? 1.612   -5.837  44.080  1.00 49.81  ? 1206 HOH C O   1 
HETATM 7231 O  O   . HOH UA 5 .   ? -5.681  -21.840 66.729  1.00 47.19  ? 1207 HOH C O   1 
HETATM 7232 O  O   . HOH UA 5 .   ? -3.570  -5.199  50.175  1.00 50.77  ? 1208 HOH C O   1 
HETATM 7233 O  O   . HOH UA 5 .   ? 1.905   -10.673 58.687  1.00 48.79  ? 1209 HOH C O   1 
HETATM 7234 O  O   . HOH UA 5 .   ? 1.817   -16.018 48.608  1.00 46.59  ? 1210 HOH C O   1 
HETATM 7235 O  O   . HOH UA 5 .   ? -9.279  -27.204 43.788  1.00 41.30  ? 1211 HOH C O   1 
HETATM 7236 O  O   . HOH UA 5 .   ? 1.211   -20.854 59.965  1.00 47.79  ? 1212 HOH C O   1 
HETATM 7237 O  O   . HOH UA 5 .   ? -32.561 -12.071 20.776  1.00 39.27  ? 1213 HOH C O   1 
HETATM 7238 O  O   . HOH UA 5 .   ? -23.769 -1.539  45.575  1.00 49.90  ? 1214 HOH C O   1 
HETATM 7239 O  O   . HOH UA 5 .   ? 3.758   -24.932 49.502  1.00 39.97  ? 1215 HOH C O   1 
HETATM 7240 O  O   . HOH UA 5 .   ? -22.555 -21.584 47.531  1.00 43.61  ? 1216 HOH C O   1 
HETATM 7241 O  O   . HOH UA 5 .   ? -7.247  -24.942 33.683  1.00 38.53  ? 1217 HOH C O   1 
HETATM 7242 O  O   . HOH UA 5 .   ? -18.773 -25.142 52.439  1.00 50.99  ? 1218 HOH C O   1 
HETATM 7243 O  O   . HOH UA 5 .   ? -0.301  -15.438 65.276  1.00 50.45  ? 1219 HOH C O   1 
HETATM 7244 O  O   . HOH UA 5 .   ? -5.152  -29.710 60.903  1.00 45.01  ? 1220 HOH C O   1 
HETATM 7245 O  O   . HOH UA 5 .   ? -14.449 -23.098 65.517  1.00 33.95  ? 1221 HOH C O   1 
HETATM 7246 O  O   . HOH UA 5 .   ? -1.124  -24.385 55.548  1.00 48.01  ? 1222 HOH C O   1 
HETATM 7247 O  O   . HOH UA 5 .   ? -30.259 -17.599 49.634  1.00 49.11  ? 1223 HOH C O   1 
HETATM 7248 O  O   . HOH UA 5 .   ? -9.990  -25.487 35.762  1.00 43.23  ? 1224 HOH C O   1 
HETATM 7249 O  O   . HOH UA 5 .   ? -19.092 -17.087 61.366  1.00 53.67  ? 1225 HOH C O   1 
HETATM 7250 O  O   . HOH UA 5 .   ? -17.086 -20.474 26.973  1.00 39.93  ? 1226 HOH C O   1 
HETATM 7251 O  O   . HOH UA 5 .   ? -10.169 -29.271 40.672  1.00 37.44  ? 1227 HOH C O   1 
HETATM 7252 O  O   . HOH UA 5 .   ? -29.659 -16.028 55.272  1.00 60.71  ? 1228 HOH C O   1 
HETATM 7253 O  O   . HOH UA 5 .   ? -15.533 -4.618  37.378  1.00 51.93  ? 1229 HOH C O   1 
HETATM 7254 O  O   . HOH UA 5 .   ? 1.772   -8.841  40.799  1.00 44.89  ? 1230 HOH C O   1 
HETATM 7255 O  O   . HOH UA 5 .   ? -17.240 1.706   37.600  1.00 55.38  ? 1231 HOH C O   1 
HETATM 7256 O  O   . HOH UA 5 .   ? -26.683 -4.632  24.425  1.00 44.76  ? 1232 HOH C O   1 
HETATM 7257 O  O   . HOH UA 5 .   ? -10.532 -25.322 67.138  1.00 61.18  ? 1233 HOH C O   1 
HETATM 7258 O  O   . HOH UA 5 .   ? -12.201 -10.414 26.962  1.00 49.22  ? 1234 HOH C O   1 
HETATM 7259 O  O   . HOH UA 5 .   ? -7.330  -25.567 67.189  1.00 57.65  ? 1235 HOH C O   1 
HETATM 7260 O  O   . HOH VA 5 .   ? -6.318  -20.285 23.303  1.00 38.65  ? 601  HOH D O   1 
HETATM 7261 O  O   . HOH VA 5 .   ? -6.272  -32.789 25.309  1.00 47.14  ? 602  HOH D O   1 
HETATM 7262 O  O   . HOH VA 5 .   ? -5.404  -36.655 16.589  1.00 34.51  ? 603  HOH D O   1 
HETATM 7263 O  O   . HOH VA 5 .   ? 21.159  -29.301 16.511  1.00 47.11  ? 604  HOH D O   1 
HETATM 7264 O  O   . HOH VA 5 .   ? 14.623  -34.199 9.754   1.00 44.79  ? 605  HOH D O   1 
HETATM 7265 O  O   . HOH VA 5 .   ? -7.835  -23.989 10.295  1.00 34.12  ? 606  HOH D O   1 
HETATM 7266 O  O   . HOH VA 5 .   ? -5.078  -23.162 -5.952  1.00 28.86  ? 607  HOH D O   1 
HETATM 7267 O  O   . HOH VA 5 .   ? -5.868  -39.211 22.891  1.00 39.15  ? 608  HOH D O   1 
HETATM 7268 O  O   . HOH VA 5 .   ? 3.707   -19.756 24.220  1.00 42.25  ? 609  HOH D O   1 
HETATM 7269 O  O   . HOH VA 5 .   ? -9.383  -32.532 19.361  1.00 34.77  ? 610  HOH D O   1 
HETATM 7270 O  O   . HOH VA 5 .   ? 11.424  -39.052 13.810  1.00 34.45  ? 611  HOH D O   1 
HETATM 7271 O  O   . HOH VA 5 .   ? -6.181  -18.222 6.694   1.00 26.33  ? 612  HOH D O   1 
HETATM 7272 O  O   . HOH VA 5 .   ? 2.816   -21.940 25.987  1.00 35.70  ? 613  HOH D O   1 
HETATM 7273 O  O   . HOH VA 5 .   ? -0.185  -37.434 21.311  1.00 39.57  ? 614  HOH D O   1 
HETATM 7274 O  O   . HOH VA 5 .   ? 10.883  -15.343 20.365  1.00 43.98  ? 615  HOH D O   1 
HETATM 7275 O  O   . HOH VA 5 .   ? 1.225   -23.464 29.633  1.00 37.88  ? 616  HOH D O   1 
HETATM 7276 O  O   . HOH VA 5 .   ? -11.190 -31.748 16.789  1.00 35.90  ? 617  HOH D O   1 
HETATM 7277 O  O   . HOH VA 5 .   ? -10.030 -22.605 16.217  1.00 42.14  ? 618  HOH D O   1 
HETATM 7278 O  O   A HOH VA 5 .   ? 1.737   -39.183 20.413  0.50 28.52  ? 619  HOH D O   1 
HETATM 7279 O  O   B HOH VA 5 .   ? 0.584   -39.572 18.802  0.50 34.51  ? 619  HOH D O   1 
HETATM 7280 O  O   . HOH VA 5 .   ? 16.263  -31.423 7.140   1.00 33.15  ? 620  HOH D O   1 
HETATM 7281 O  O   . HOH VA 5 .   ? 9.959   -23.923 25.989  1.00 40.63  ? 621  HOH D O   1 
HETATM 7282 O  O   . HOH VA 5 .   ? -10.439 -30.108 20.601  1.00 30.93  ? 622  HOH D O   1 
HETATM 7283 O  O   . HOH VA 5 .   ? -4.750  -30.003 22.733  1.00 22.84  ? 623  HOH D O   1 
HETATM 7284 O  O   . HOH VA 5 .   ? 6.676   -32.166 5.897   1.00 38.89  ? 624  HOH D O   1 
HETATM 7285 O  O   . HOH VA 5 .   ? 17.112  -22.564 -3.428  1.00 37.78  ? 625  HOH D O   1 
HETATM 7286 O  O   . HOH VA 5 .   ? 6.291   -9.867  7.366   1.00 47.83  ? 626  HOH D O   1 
HETATM 7287 O  O   . HOH VA 5 .   ? -9.799  -18.409 9.973   1.00 32.84  ? 627  HOH D O   1 
HETATM 7288 O  O   . HOH VA 5 .   ? -7.606  -8.190  22.010  1.00 35.41  ? 628  HOH D O   1 
HETATM 7289 O  O   . HOH VA 5 .   ? 10.404  -36.146 25.330  1.00 39.13  ? 629  HOH D O   1 
HETATM 7290 O  O   . HOH VA 5 .   ? -1.511  -16.179 16.727  1.00 37.34  ? 630  HOH D O   1 
HETATM 7291 O  O   . HOH VA 5 .   ? 1.537   -21.045 -1.489  1.00 52.57  ? 631  HOH D O   1 
HETATM 7292 O  O   . HOH VA 5 .   ? -0.393  -11.778 7.090   1.00 29.22  ? 632  HOH D O   1 
HETATM 7293 O  O   . HOH VA 5 .   ? 6.598   -32.100 -4.879  1.00 43.02  ? 633  HOH D O   1 
HETATM 7294 O  O   . HOH VA 5 .   ? -12.044 -20.930 23.071  1.00 50.32  ? 634  HOH D O   1 
HETATM 7295 O  O   . HOH VA 5 .   ? 20.046  -27.492 14.213  1.00 34.01  ? 635  HOH D O   1 
HETATM 7296 O  O   . HOH VA 5 .   ? -9.468  -16.216 13.847  1.00 40.02  ? 636  HOH D O   1 
HETATM 7297 O  O   . HOH VA 5 .   ? -2.263  -40.549 22.338  1.00 50.43  ? 637  HOH D O   1 
HETATM 7298 O  O   . HOH VA 5 .   ? 8.862   -34.708 6.356   1.00 34.62  ? 638  HOH D O   1 
HETATM 7299 O  O   . HOH VA 5 .   ? 0.561   -29.311 3.686   1.00 32.91  ? 639  HOH D O   1 
HETATM 7300 O  O   . HOH VA 5 .   ? 7.446   -37.247 16.298  1.00 23.54  ? 640  HOH D O   1 
HETATM 7301 O  O   . HOH VA 5 .   ? 0.255   -14.506 14.114  1.00 49.39  ? 641  HOH D O   1 
HETATM 7302 O  O   . HOH VA 5 .   ? 13.046  -35.406 7.183   1.00 31.71  ? 642  HOH D O   1 
HETATM 7303 O  O   . HOH VA 5 .   ? 6.746   -40.386 13.927  1.00 31.38  ? 643  HOH D O   1 
HETATM 7304 O  O   . HOH VA 5 .   ? -5.234  -35.047 14.010  1.00 33.72  ? 644  HOH D O   1 
HETATM 7305 O  O   . HOH VA 5 .   ? -8.281  -25.383 17.961  1.00 29.37  ? 645  HOH D O   1 
HETATM 7306 O  O   . HOH VA 5 .   ? -10.115 -27.199 16.841  1.00 40.45  ? 646  HOH D O   1 
HETATM 7307 O  O   . HOH VA 5 .   ? -5.757  -28.704 0.927   1.00 48.81  ? 647  HOH D O   1 
HETATM 7308 O  O   . HOH VA 5 .   ? 8.585   -23.676 28.451  1.00 39.01  ? 648  HOH D O   1 
HETATM 7309 O  O   . HOH VA 5 .   ? -12.240 -29.562 18.306  1.00 43.39  ? 649  HOH D O   1 
HETATM 7310 O  O   . HOH VA 5 .   ? -2.247  -33.433 11.506  1.00 39.41  ? 650  HOH D O   1 
HETATM 7311 O  O   . HOH VA 5 .   ? 11.346  -18.927 2.380   1.00 46.18  ? 651  HOH D O   1 
HETATM 7312 O  O   . HOH VA 5 .   ? 9.145   -33.756 -0.928  1.00 41.87  ? 652  HOH D O   1 
HETATM 7313 O  O   . HOH VA 5 .   ? 7.519   -36.939 12.239  1.00 57.26  ? 653  HOH D O   1 
HETATM 7314 O  O   . HOH VA 5 .   ? 6.438   -29.512 28.621  1.00 49.52  ? 654  HOH D O   1 
HETATM 7315 O  O   . HOH VA 5 .   ? 10.491  -21.299 -6.464  1.00 43.43  ? 655  HOH D O   1 
HETATM 7316 O  O   . HOH VA 5 .   ? -1.312  -27.191 31.953  1.00 52.06  ? 656  HOH D O   1 
HETATM 7317 O  O   . HOH VA 5 .   ? 3.576   -21.606 1.172   1.00 37.68  ? 657  HOH D O   1 
HETATM 7318 O  O   . HOH VA 5 .   ? 24.087  -31.354 13.226  1.00 43.66  ? 658  HOH D O   1 
HETATM 7319 O  O   . HOH VA 5 .   ? 19.093  -22.208 -0.286  1.00 52.85  ? 659  HOH D O   1 
HETATM 7320 O  O   . HOH VA 5 .   ? 14.812  -23.245 22.001  1.00 51.56  ? 660  HOH D O   1 
HETATM 7321 O  O   . HOH VA 5 .   ? -6.721  -41.320 11.564  1.00 57.22  ? 661  HOH D O   1 
HETATM 7322 O  O   . HOH VA 5 .   ? 6.813   -32.733 1.291   1.00 49.46  ? 662  HOH D O   1 
HETATM 7323 O  O   . HOH VA 5 .   ? -3.732  -32.419 23.892  1.00 34.34  ? 663  HOH D O   1 
HETATM 7324 O  O   . HOH VA 5 .   ? 10.807  -29.642 28.527  1.00 38.04  ? 664  HOH D O   1 
HETATM 7325 O  O   . HOH VA 5 .   ? -10.470 -25.361 28.199  1.00 39.61  ? 665  HOH D O   1 
HETATM 7326 O  O   . HOH VA 5 .   ? 3.414   -13.869 14.835  1.00 44.56  ? 666  HOH D O   1 
HETATM 7327 O  O   . HOH VA 5 .   ? 1.926   -34.732 23.561  1.00 48.10  ? 667  HOH D O   1 
HETATM 7328 O  O   . HOH VA 5 .   ? 11.445  -26.866 23.690  1.00 48.02  ? 668  HOH D O   1 
HETATM 7329 O  O   . HOH VA 5 .   ? 5.164   -40.194 26.605  1.00 49.43  ? 669  HOH D O   1 
HETATM 7330 O  O   . HOH VA 5 .   ? 10.157  -41.871 21.066  1.00 48.82  ? 670  HOH D O   1 
HETATM 7331 O  O   . HOH VA 5 .   ? -9.192  -31.026 27.435  1.00 47.11  ? 671  HOH D O   1 
HETATM 7332 O  O   . HOH VA 5 .   ? 17.208  -36.810 16.543  1.00 40.93  ? 672  HOH D O   1 
HETATM 7333 O  O   . HOH VA 5 .   ? -11.512 -30.179 22.746  1.00 49.58  ? 673  HOH D O   1 
HETATM 7334 O  O   . HOH VA 5 .   ? 14.439  -35.864 20.154  1.00 50.38  ? 674  HOH D O   1 
HETATM 7335 O  O   . HOH VA 5 .   ? 8.320   -25.368 -5.715  1.00 54.42  ? 675  HOH D O   1 
HETATM 7336 O  O   . HOH VA 5 .   ? 19.017  -24.422 -4.033  1.00 44.35  ? 676  HOH D O   1 
HETATM 7337 O  O   . HOH VA 5 .   ? 13.365  -28.911 24.872  1.00 38.44  ? 677  HOH D O   1 
HETATM 7338 O  O   . HOH VA 5 .   ? 14.701  -26.943 20.608  1.00 38.27  ? 678  HOH D O   1 
HETATM 7339 O  O   . HOH VA 5 .   ? 8.131   -16.942 18.803  1.00 50.53  ? 679  HOH D O   1 
HETATM 7340 O  O   . HOH VA 5 .   ? 12.967  -41.459 18.525  1.00 53.62  ? 680  HOH D O   1 
HETATM 7341 O  O   . HOH VA 5 .   ? 8.740   -41.093 10.033  1.00 48.96  ? 681  HOH D O   1 
HETATM 7342 O  O   A HOH VA 5 .   ? 2.953   -11.403 14.775  0.50 35.18  ? 682  HOH D O   1 
HETATM 7343 O  O   B HOH VA 5 .   ? 1.483   -10.706 14.110  0.50 29.51  ? 682  HOH D O   1 
HETATM 7344 O  O   . HOH VA 5 .   ? 13.994  -14.315 -1.426  1.00 55.45  ? 683  HOH D O   1 
HETATM 7345 O  O   . HOH VA 5 .   ? -1.791  -38.536 5.514   1.00 53.35  ? 684  HOH D O   1 
HETATM 7346 O  O   . HOH VA 5 .   ? 9.060   -13.018 -4.514  1.00 55.72  ? 685  HOH D O   1 
HETATM 7347 O  O   . HOH VA 5 .   ? -12.121 -35.202 19.282  1.00 49.67  ? 686  HOH D O   1 
HETATM 7348 O  O   . HOH VA 5 .   ? 20.656  -24.735 13.632  1.00 45.78  ? 687  HOH D O   1 
HETATM 7349 O  O   . HOH VA 5 .   ? 6.148   -16.853 23.595  1.00 42.79  ? 688  HOH D O   1 
HETATM 7350 O  O   . HOH VA 5 .   ? 12.811  -40.039 15.726  1.00 45.68  ? 689  HOH D O   1 
HETATM 7351 O  O   . HOH VA 5 .   ? -10.485 -26.586 12.859  1.00 55.42  ? 690  HOH D O   1 
HETATM 7352 O  O   . HOH VA 5 .   ? -5.007  -24.399 31.202  1.00 40.55  ? 691  HOH D O   1 
HETATM 7353 O  O   . HOH VA 5 .   ? -0.635  -31.827 3.941   1.00 37.61  ? 692  HOH D O   1 
HETATM 7354 O  O   . HOH VA 5 .   ? 2.597   -34.560 26.130  1.00 43.72  ? 693  HOH D O   1 
HETATM 7355 O  O   . HOH VA 5 .   ? 23.567  -34.630 12.839  1.00 47.31  ? 694  HOH D O   1 
HETATM 7356 O  O   . HOH VA 5 .   ? -8.098  -22.973 -5.407  1.00 29.45  ? 695  HOH D O   1 
HETATM 7357 O  O   . HOH VA 5 .   ? 20.532  -33.429 0.283   1.00 52.21  ? 696  HOH D O   1 
HETATM 7358 O  O   . HOH VA 5 .   ? -12.545 -32.256 20.093  1.00 38.89  ? 697  HOH D O   1 
HETATM 7359 O  O   . HOH VA 5 .   ? 11.008  -40.767 11.521  1.00 43.67  ? 698  HOH D O   1 
HETATM 7360 O  O   . HOH VA 5 .   ? 15.377  -37.081 9.090   1.00 47.64  ? 699  HOH D O   1 
HETATM 7361 O  O   . HOH WA 5 .   ? 17.710  -18.875 86.500  1.00 31.40  ? 601  HOH E O   1 
HETATM 7362 O  O   . HOH WA 5 .   ? 26.900  -13.850 89.009  1.00 47.59  ? 602  HOH E O   1 
HETATM 7363 O  O   . HOH WA 5 .   ? 14.442  -9.639  66.197  1.00 50.88  ? 603  HOH E O   1 
HETATM 7364 O  O   . HOH WA 5 .   ? 23.197  0.515   89.950  1.00 57.56  ? 604  HOH E O   1 
HETATM 7365 O  O   . HOH WA 5 .   ? 12.125  -15.472 86.524  1.00 40.80  ? 605  HOH E O   1 
HETATM 7366 O  O   . HOH WA 5 .   ? 1.617   -14.282 73.147  1.00 32.32  ? 606  HOH E O   1 
HETATM 7367 O  O   . HOH WA 5 .   ? 23.137  -21.342 83.800  1.00 31.44  ? 607  HOH E O   1 
HETATM 7368 O  O   . HOH WA 5 .   ? 22.493  -15.106 89.104  1.00 31.97  ? 608  HOH E O   1 
HETATM 7369 O  O   . HOH WA 5 .   ? 9.109   -21.065 77.292  1.00 40.75  ? 609  HOH E O   1 
HETATM 7370 O  O   . HOH WA 5 .   ? 1.662   -15.809 79.551  1.00 36.24  ? 610  HOH E O   1 
HETATM 7371 O  O   . HOH WA 5 .   ? 20.828  -10.423 91.942  1.00 42.57  ? 611  HOH E O   1 
HETATM 7372 O  O   . HOH WA 5 .   ? -7.390  -7.060  88.115  1.00 45.35  ? 612  HOH E O   1 
HETATM 7373 O  O   . HOH WA 5 .   ? 22.800  -12.668 92.291  1.00 31.31  ? 613  HOH E O   1 
HETATM 7374 O  O   . HOH WA 5 .   ? -1.217  -5.135  99.504  1.00 31.55  ? 614  HOH E O   1 
HETATM 7375 O  O   . HOH WA 5 .   ? 24.431  -2.830  86.669  1.00 38.04  ? 615  HOH E O   1 
HETATM 7376 O  O   . HOH WA 5 .   ? 0.032   -7.085  100.769 1.00 23.28  ? 616  HOH E O   1 
HETATM 7377 O  O   . HOH WA 5 .   ? 8.087   -10.964 94.749  1.00 42.25  ? 617  HOH E O   1 
HETATM 7378 O  O   . HOH WA 5 .   ? 20.321  -6.006  92.931  1.00 40.01  ? 618  HOH E O   1 
HETATM 7379 O  O   . HOH WA 5 .   ? -2.711  -14.840 72.689  1.00 39.48  ? 619  HOH E O   1 
HETATM 7380 O  O   . HOH WA 5 .   ? 24.246  8.684   90.599  1.00 45.09  ? 620  HOH E O   1 
HETATM 7381 O  O   . HOH WA 5 .   ? 13.896  -7.107  93.855  1.00 34.96  ? 621  HOH E O   1 
HETATM 7382 O  O   . HOH WA 5 .   ? 21.254  -14.844 91.448  1.00 36.39  ? 622  HOH E O   1 
HETATM 7383 O  O   . HOH WA 5 .   ? 23.049  -6.438  91.841  1.00 46.02  ? 623  HOH E O   1 
HETATM 7384 O  O   . HOH WA 5 .   ? -1.798  -11.440 74.403  1.00 40.04  ? 624  HOH E O   1 
HETATM 7385 O  O   . HOH WA 5 .   ? 7.234   -7.416  98.057  1.00 38.68  ? 625  HOH E O   1 
HETATM 7386 O  O   . HOH WA 5 .   ? 27.195  -0.027  90.736  1.00 52.58  ? 626  HOH E O   1 
HETATM 7387 O  O   . HOH WA 5 .   ? -4.082  -14.430 86.615  1.00 41.02  ? 627  HOH E O   1 
HETATM 7388 O  O   . HOH WA 5 .   ? 2.349   -6.518  67.832  1.00 36.44  ? 628  HOH E O   1 
HETATM 7389 O  O   . HOH WA 5 .   ? 24.349  -12.658 89.375  1.00 35.56  ? 629  HOH E O   1 
HETATM 7390 O  O   . HOH WA 5 .   ? 7.790   5.907   90.782  1.00 27.28  ? 630  HOH E O   1 
HETATM 7391 O  O   . HOH WA 5 .   ? 7.278   -18.313 78.207  1.00 52.52  ? 631  HOH E O   1 
HETATM 7392 O  O   . HOH WA 5 .   ? 7.990   -3.200  68.866  1.00 39.49  ? 632  HOH E O   1 
HETATM 7393 O  O   . HOH WA 5 .   ? -1.623  -3.829  95.625  1.00 45.65  ? 633  HOH E O   1 
HETATM 7394 O  O   . HOH WA 5 .   ? 7.743   -2.327  77.882  1.00 38.46  ? 634  HOH E O   1 
HETATM 7395 O  O   . HOH WA 5 .   ? -15.506 -12.281 75.595  1.00 53.67  ? 635  HOH E O   1 
HETATM 7396 O  O   . HOH WA 5 .   ? 5.758   2.622   93.064  1.00 51.49  ? 636  HOH E O   1 
HETATM 7397 O  O   . HOH WA 5 .   ? 14.619  -1.554  95.946  1.00 33.26  ? 637  HOH E O   1 
HETATM 7398 O  O   . HOH WA 5 .   ? 22.987  -12.095 84.028  1.00 25.65  ? 638  HOH E O   1 
HETATM 7399 O  O   . HOH WA 5 .   ? 13.246  2.454   76.823  1.00 42.14  ? 639  HOH E O   1 
HETATM 7400 O  O   . HOH WA 5 .   ? -10.381 -2.498  79.774  1.00 33.66  ? 640  HOH E O   1 
HETATM 7401 O  O   . HOH WA 5 .   ? 10.242  -1.427  95.131  1.00 28.14  ? 641  HOH E O   1 
HETATM 7402 O  O   . HOH WA 5 .   ? -2.573  -0.311  82.156  1.00 31.29  ? 642  HOH E O   1 
HETATM 7403 O  O   . HOH WA 5 .   ? 9.795   -9.643  66.793  1.00 50.04  ? 643  HOH E O   1 
HETATM 7404 O  O   . HOH WA 5 .   ? 26.537  -14.435 83.087  1.00 42.48  ? 644  HOH E O   1 
HETATM 7405 O  O   . HOH WA 5 .   ? 20.981  -3.484  70.599  1.00 37.92  ? 645  HOH E O   1 
HETATM 7406 O  O   . HOH WA 5 .   ? 16.115  1.707   86.333  1.00 41.90  ? 646  HOH E O   1 
HETATM 7407 O  O   . HOH WA 5 .   ? 3.811   -11.560 89.207  1.00 38.86  ? 647  HOH E O   1 
HETATM 7408 O  O   . HOH WA 5 .   ? 30.352  -7.933  86.626  1.00 37.57  ? 648  HOH E O   1 
HETATM 7409 O  O   . HOH WA 5 .   ? 21.674  -2.707  76.970  1.00 39.07  ? 649  HOH E O   1 
HETATM 7410 O  O   . HOH WA 5 .   ? 25.256  0.776   76.096  1.00 45.89  ? 650  HOH E O   1 
HETATM 7411 O  O   . HOH WA 5 .   ? 10.802  -17.783 75.533  1.00 40.58  ? 651  HOH E O   1 
HETATM 7412 O  O   A HOH WA 5 .   ? -4.334  -10.916 95.239  0.50 26.57  ? 652  HOH E O   1 
HETATM 7413 O  O   B HOH WA 5 .   ? -6.513  -13.544 94.284  0.50 22.94  ? 652  HOH E O   1 
HETATM 7414 O  O   . HOH WA 5 .   ? 12.990  3.486   85.996  1.00 41.65  ? 653  HOH E O   1 
HETATM 7415 O  O   . HOH WA 5 .   ? -9.301  -0.776  87.340  1.00 46.17  ? 654  HOH E O   1 
HETATM 7416 O  O   . HOH WA 5 .   ? 9.796   -1.281  69.838  1.00 51.62  ? 655  HOH E O   1 
HETATM 7417 O  O   . HOH WA 5 .   ? 15.752  -17.600 88.021  1.00 36.86  ? 656  HOH E O   1 
HETATM 7418 O  O   . HOH WA 5 .   ? -12.043 -2.962  86.605  1.00 45.17  ? 657  HOH E O   1 
HETATM 7419 O  O   . HOH WA 5 .   ? 18.203  -4.506  70.541  1.00 45.51  ? 658  HOH E O   1 
HETATM 7420 O  O   . HOH WA 5 .   ? 23.153  -14.356 82.022  1.00 35.32  ? 659  HOH E O   1 
HETATM 7421 O  O   . HOH WA 5 .   ? 2.313   -13.297 82.391  1.00 28.21  ? 660  HOH E O   1 
HETATM 7422 O  O   . HOH WA 5 .   ? 20.465  -8.412  90.111  1.00 29.96  ? 661  HOH E O   1 
HETATM 7423 O  O   . HOH WA 5 .   ? -12.122 -4.454  78.732  1.00 35.82  ? 662  HOH E O   1 
HETATM 7424 O  O   . HOH WA 5 .   ? -20.388 -6.732  85.285  1.00 53.39  ? 663  HOH E O   1 
HETATM 7425 O  O   . HOH WA 5 .   ? 12.382  -2.738  68.776  1.00 55.12  ? 664  HOH E O   1 
HETATM 7426 O  O   . HOH WA 5 .   ? 11.896  6.826   83.271  1.00 38.52  ? 665  HOH E O   1 
HETATM 7427 O  O   . HOH WA 5 .   ? 9.382   3.371   69.071  1.00 47.97  ? 666  HOH E O   1 
HETATM 7428 O  O   A HOH WA 5 .   ? 10.589  7.124   71.254  0.50 24.60  ? 667  HOH E O   1 
HETATM 7429 O  O   B HOH WA 5 .   ? 10.100  8.743   70.146  0.50 26.93  ? 667  HOH E O   1 
HETATM 7430 O  O   . HOH WA 5 .   ? 18.955  -18.772 79.183  1.00 46.92  ? 668  HOH E O   1 
HETATM 7431 O  O   . HOH WA 5 .   ? 0.185   -15.356 75.541  1.00 46.15  ? 669  HOH E O   1 
HETATM 7432 O  O   . HOH WA 5 .   ? 0.209   -3.983  89.577  1.00 38.30  ? 670  HOH E O   1 
HETATM 7433 O  O   . HOH WA 5 .   ? -1.672  2.978   82.332  1.00 60.99  ? 671  HOH E O   1 
HETATM 7434 O  O   . HOH WA 5 .   ? 19.728  -15.851 77.049  1.00 36.46  ? 672  HOH E O   1 
HETATM 7435 O  O   . HOH WA 5 .   ? -8.054  -2.017  75.494  1.00 42.74  ? 673  HOH E O   1 
HETATM 7436 O  O   . HOH WA 5 .   ? -5.007  -15.084 84.234  1.00 36.68  ? 674  HOH E O   1 
HETATM 7437 O  O   . HOH WA 5 .   ? -1.668  3.909   87.158  1.00 53.62  ? 675  HOH E O   1 
HETATM 7438 O  O   . HOH WA 5 .   ? 17.936  0.607   94.742  1.00 35.90  ? 676  HOH E O   1 
HETATM 7439 O  O   . HOH WA 5 .   ? 5.777   -16.369 67.845  1.00 36.87  ? 677  HOH E O   1 
HETATM 7440 O  O   . HOH WA 5 .   ? -0.691  -14.352 82.959  1.00 44.03  ? 678  HOH E O   1 
HETATM 7441 O  O   . HOH WA 5 .   ? -6.292  5.217   81.821  1.00 39.13  ? 679  HOH E O   1 
HETATM 7442 O  O   . HOH WA 5 .   ? 21.644  -10.154 71.113  1.00 43.61  ? 680  HOH E O   1 
HETATM 7443 O  O   . HOH WA 5 .   ? 13.885  -20.196 88.459  1.00 55.81  ? 681  HOH E O   1 
HETATM 7444 O  O   . HOH WA 5 .   ? -0.689  -12.648 72.306  1.00 43.96  ? 682  HOH E O   1 
HETATM 7445 O  O   . HOH WA 5 .   ? 20.290  -23.448 91.825  1.00 47.15  ? 683  HOH E O   1 
HETATM 7446 O  O   . HOH WA 5 .   ? 9.756   -16.587 68.097  1.00 53.20  ? 684  HOH E O   1 
HETATM 7447 O  O   . HOH WA 5 .   ? 12.334  4.540   83.648  1.00 49.19  ? 685  HOH E O   1 
HETATM 7448 O  O   . HOH WA 5 .   ? 18.317  -0.140  72.864  1.00 46.61  ? 686  HOH E O   1 
HETATM 7449 O  O   . HOH WA 5 .   ? -6.499  -4.896  93.821  1.00 52.43  ? 687  HOH E O   1 
HETATM 7450 O  O   . HOH WA 5 .   ? -0.884  -3.496  93.005  1.00 51.58  ? 688  HOH E O   1 
HETATM 7451 O  O   . HOH WA 5 .   ? 28.977  -13.304 84.511  1.00 51.23  ? 689  HOH E O   1 
HETATM 7452 O  O   . HOH WA 5 .   ? -0.669  -11.849 64.915  1.00 48.08  ? 690  HOH E O   1 
HETATM 7453 O  O   . HOH WA 5 .   ? 24.328  -18.774 90.460  1.00 45.10  ? 691  HOH E O   1 
HETATM 7454 O  O   . HOH WA 5 .   ? -9.093  -15.300 76.355  1.00 38.25  ? 692  HOH E O   1 
HETATM 7455 O  O   . HOH WA 5 .   ? -10.444 -9.385  83.513  1.00 41.86  ? 693  HOH E O   1 
HETATM 7456 O  O   . HOH WA 5 .   ? 22.338  -16.203 78.784  1.00 56.80  ? 694  HOH E O   1 
HETATM 7457 O  O   . HOH WA 5 .   ? 6.616   -15.708 91.351  1.00 40.63  ? 695  HOH E O   1 
HETATM 7458 O  O   . HOH WA 5 .   ? 15.035  7.739   76.964  1.00 49.22  ? 696  HOH E O   1 
HETATM 7459 O  O   . HOH WA 5 .   ? -2.277  -11.853 96.506  1.00 51.96  ? 697  HOH E O   1 
HETATM 7460 O  O   . HOH WA 5 .   ? -2.293  -15.356 81.018  1.00 50.43  ? 698  HOH E O   1 
HETATM 7461 O  O   . HOH WA 5 .   ? -17.386 -7.784  75.620  1.00 38.84  ? 699  HOH E O   1 
HETATM 7462 O  O   . HOH WA 5 .   ? 12.471  -0.058  95.611  1.00 46.67  ? 700  HOH E O   1 
HETATM 7463 O  O   . HOH WA 5 .   ? 4.010   -14.561 89.618  1.00 43.34  ? 701  HOH E O   1 
HETATM 7464 O  O   . HOH WA 5 .   ? 1.650   -15.267 89.899  1.00 49.95  ? 702  HOH E O   1 
HETATM 7465 O  O   . HOH WA 5 .   ? 14.604  -19.148 92.149  1.00 60.09  ? 703  HOH E O   1 
HETATM 7466 O  O   . HOH WA 5 .   ? -1.931  2.461   74.034  1.00 45.35  ? 704  HOH E O   1 
HETATM 7467 O  O   . HOH WA 5 .   ? -0.492  6.301   80.319  1.00 40.59  ? 705  HOH E O   1 
HETATM 7468 O  O   . HOH WA 5 .   ? -7.499  -4.805  88.961  1.00 45.81  ? 706  HOH E O   1 
HETATM 7469 O  O   . HOH WA 5 .   ? 24.271  -15.242 91.441  1.00 51.12  ? 707  HOH E O   1 
HETATM 7470 O  O   . HOH WA 5 .   ? 23.018  -9.618  93.063  1.00 49.64  ? 708  HOH E O   1 
HETATM 7471 O  O   . HOH WA 5 .   ? 29.679  2.102   90.815  1.00 57.78  ? 709  HOH E O   1 
HETATM 7472 O  O   . HOH WA 5 .   ? 20.377  -13.311 94.506  1.00 53.41  ? 710  HOH E O   1 
HETATM 7473 O  O   . HOH WA 5 .   ? -10.703 -12.638 73.980  1.00 36.66  ? 711  HOH E O   1 
HETATM 7474 O  O   . HOH WA 5 .   ? 4.600   -2.555  65.986  1.00 50.92  ? 712  HOH E O   1 
HETATM 7475 O  O   . HOH XA 5 .   ? 6.437   24.726  78.901  1.00 40.28  ? 601  HOH F O   1 
HETATM 7476 O  O   . HOH XA 5 .   ? 0.898   18.053  77.508  1.00 37.89  ? 602  HOH F O   1 
HETATM 7477 O  O   . HOH XA 5 .   ? 10.155  28.260  87.596  1.00 28.13  ? 603  HOH F O   1 
HETATM 7478 O  O   . HOH XA 5 .   ? 3.709   22.000  84.914  1.00 25.83  ? 604  HOH F O   1 
HETATM 7479 O  O   . HOH XA 5 .   ? 5.243   24.558  86.068  1.00 31.57  ? 605  HOH F O   1 
HETATM 7480 O  O   . HOH XA 5 .   ? 14.586  24.689  90.680  1.00 33.69  ? 606  HOH F O   1 
HETATM 7481 O  O   . HOH XA 5 .   ? 7.052   9.812   94.052  1.00 39.68  ? 607  HOH F O   1 
HETATM 7482 O  O   . HOH XA 5 .   ? 0.954   13.627  83.191  1.00 49.29  ? 608  HOH F O   1 
HETATM 7483 O  O   . HOH XA 5 .   ? 24.414  12.362  85.105  1.00 40.96  ? 609  HOH F O   1 
HETATM 7484 O  O   . HOH XA 5 .   ? 10.268  30.973  88.620  1.00 43.26  ? 610  HOH F O   1 
HETATM 7485 O  O   . HOH XA 5 .   ? 21.614  27.617  97.332  1.00 49.46  ? 611  HOH F O   1 
HETATM 7486 O  O   . HOH XA 5 .   ? 24.924  27.311  93.731  1.00 51.52  ? 612  HOH F O   1 
HETATM 7487 O  O   . HOH XA 5 .   ? 34.703  20.077  78.488  1.00 58.11  ? 613  HOH F O   1 
HETATM 7488 O  O   . HOH XA 5 .   ? 14.921  23.787  74.114  1.00 35.82  ? 614  HOH F O   1 
HETATM 7489 O  O   . HOH XA 5 .   ? 6.092   12.118  80.769  1.00 28.51  ? 615  HOH F O   1 
HETATM 7490 O  O   . HOH XA 5 .   ? 20.538  0.615   94.606  1.00 38.25  ? 616  HOH F O   1 
HETATM 7491 O  O   . HOH XA 5 .   ? 38.807  14.284  98.351  1.00 41.60  ? 617  HOH F O   1 
HETATM 7492 O  O   . HOH XA 5 .   ? 8.443   21.883  80.912  1.00 20.66  ? 618  HOH F O   1 
HETATM 7493 O  O   . HOH XA 5 .   ? 11.566  9.288   96.463  1.00 29.81  ? 619  HOH F O   1 
HETATM 7494 O  O   . HOH XA 5 .   ? 2.681   15.576  85.619  1.00 41.39  ? 620  HOH F O   1 
HETATM 7495 O  O   . HOH XA 5 .   ? 24.705  22.940  93.690  1.00 39.73  ? 621  HOH F O   1 
HETATM 7496 O  O   . HOH XA 5 .   ? 4.457   0.472   82.684  1.00 32.11  ? 622  HOH F O   1 
HETATM 7497 O  O   . HOH XA 5 .   ? 36.852  9.117   97.814  1.00 39.31  ? 623  HOH F O   1 
HETATM 7498 O  O   . HOH XA 5 .   ? 11.404  15.039  101.009 1.00 43.25  ? 624  HOH F O   1 
HETATM 7499 O  O   . HOH XA 5 .   ? 22.534  27.031  74.200  1.00 51.18  ? 625  HOH F O   1 
HETATM 7500 O  O   . HOH XA 5 .   ? 31.513  9.851   102.841 1.00 50.18  ? 626  HOH F O   1 
HETATM 7501 O  O   A HOH XA 5 .   ? 14.500  20.950  69.807  0.50 33.30  ? 627  HOH F O   1 
HETATM 7502 O  O   B HOH XA 5 .   ? 15.495  20.901  71.771  0.50 34.85  ? 627  HOH F O   1 
HETATM 7503 O  O   . HOH XA 5 .   ? 31.517  24.472  87.006  1.00 45.47  ? 628  HOH F O   1 
HETATM 7504 O  O   . HOH XA 5 .   ? 33.069  21.840  89.345  1.00 43.98  ? 629  HOH F O   1 
HETATM 7505 O  O   . HOH XA 5 .   ? 29.828  14.901  103.920 1.00 56.77  ? 630  HOH F O   1 
HETATM 7506 O  O   . HOH XA 5 .   ? 34.281  11.089  104.433 1.00 57.96  ? 631  HOH F O   1 
HETATM 7507 O  O   . HOH XA 5 .   ? 7.850   31.363  81.379  1.00 44.43  ? 632  HOH F O   1 
HETATM 7508 O  O   . HOH XA 5 .   ? 13.956  19.321  101.846 1.00 54.38  ? 633  HOH F O   1 
HETATM 7509 O  O   . HOH XA 5 .   ? 12.409  18.640  99.083  1.00 34.76  ? 634  HOH F O   1 
HETATM 7510 O  O   . HOH XA 5 .   ? 9.212   24.333  79.996  1.00 38.35  ? 635  HOH F O   1 
HETATM 7511 O  O   . HOH XA 5 .   ? 10.821  26.364  89.587  1.00 30.51  ? 636  HOH F O   1 
HETATM 7512 O  O   . HOH XA 5 .   ? 34.539  18.308  81.610  1.00 59.52  ? 637  HOH F O   1 
HETATM 7513 O  O   . HOH XA 5 .   ? 21.015  8.377   80.224  1.00 33.62  ? 638  HOH F O   1 
HETATM 7514 O  O   . HOH XA 5 .   ? 16.650  2.640   93.824  1.00 32.21  ? 639  HOH F O   1 
HETATM 7515 O  O   . HOH XA 5 .   ? 29.505  14.678  78.009  1.00 38.45  ? 640  HOH F O   1 
HETATM 7516 O  O   . HOH XA 5 .   ? 29.679  9.324   94.391  1.00 39.23  ? 641  HOH F O   1 
HETATM 7517 O  O   . HOH XA 5 .   ? 14.495  6.170   86.552  1.00 41.71  ? 642  HOH F O   1 
HETATM 7518 O  O   . HOH XA 5 .   ? 36.981  11.710  97.978  1.00 43.22  ? 643  HOH F O   1 
HETATM 7519 O  O   . HOH XA 5 .   ? 14.185  13.704  75.537  1.00 38.05  ? 644  HOH F O   1 
HETATM 7520 O  O   . HOH XA 5 .   ? 26.685  25.419  92.037  1.00 34.20  ? 645  HOH F O   1 
HETATM 7521 O  O   . HOH XA 5 .   ? 18.034  2.711   85.325  1.00 46.25  ? 646  HOH F O   1 
HETATM 7522 O  O   . HOH XA 5 .   ? 26.969  29.838  84.780  1.00 42.32  ? 647  HOH F O   1 
HETATM 7523 O  O   . HOH XA 5 .   ? 6.239   17.596  86.867  1.00 19.61  ? 648  HOH F O   1 
HETATM 7524 O  O   . HOH XA 5 .   ? 27.308  17.937  76.812  1.00 45.01  ? 649  HOH F O   1 
HETATM 7525 O  O   . HOH XA 5 .   ? 6.008   7.946   91.098  1.00 30.35  ? 650  HOH F O   1 
HETATM 7526 O  O   . HOH XA 5 .   ? 3.881   8.139   89.392  1.00 42.83  ? 651  HOH F O   1 
HETATM 7527 O  O   . HOH XA 5 .   ? 30.618  25.629  90.250  1.00 39.71  ? 652  HOH F O   1 
HETATM 7528 O  O   . HOH XA 5 .   ? 30.794  27.687  80.391  1.00 51.30  ? 653  HOH F O   1 
HETATM 7529 O  O   . HOH XA 5 .   ? 29.183  23.928  99.514  1.00 41.72  ? 654  HOH F O   1 
HETATM 7530 O  O   . HOH XA 5 .   ? 19.180  21.029  97.040  1.00 50.89  ? 655  HOH F O   1 
HETATM 7531 O  O   . HOH XA 5 .   ? 12.813  7.508   85.382  1.00 48.26  ? 656  HOH F O   1 
HETATM 7532 O  O   . HOH XA 5 .   ? 24.258  32.893  78.470  1.00 54.01  ? 657  HOH F O   1 
HETATM 7533 O  O   . HOH XA 5 .   ? 42.055  10.024  106.224 1.00 51.21  ? 658  HOH F O   1 
HETATM 7534 O  O   . HOH XA 5 .   ? 17.492  5.183   85.384  1.00 38.41  ? 659  HOH F O   1 
HETATM 7535 O  O   . HOH XA 5 .   ? 29.005  6.814   85.214  1.00 41.03  ? 660  HOH F O   1 
HETATM 7536 O  O   . HOH XA 5 .   ? 22.528  28.181  83.451  1.00 44.00  ? 661  HOH F O   1 
HETATM 7537 O  O   . HOH XA 5 .   ? 18.679  14.986  71.040  1.00 37.92  ? 662  HOH F O   1 
HETATM 7538 O  O   . HOH XA 5 .   ? 22.469  12.165  98.915  1.00 46.67  ? 663  HOH F O   1 
HETATM 7539 O  O   . HOH XA 5 .   ? 15.127  22.090  101.557 1.00 54.48  ? 664  HOH F O   1 
HETATM 7540 O  O   . HOH XA 5 .   ? 28.467  11.415  102.642 1.00 54.80  ? 665  HOH F O   1 
HETATM 7541 O  O   . HOH XA 5 .   ? 5.569   16.709  72.942  1.00 45.89  ? 666  HOH F O   1 
HETATM 7542 O  O   . HOH XA 5 .   ? 1.742   23.213  83.018  1.00 36.43  ? 667  HOH F O   1 
HETATM 7543 O  O   . HOH XA 5 .   ? 8.548   16.626  71.785  1.00 45.26  ? 668  HOH F O   1 
HETATM 7544 O  O   . HOH XA 5 .   ? 29.351  24.677  95.036  1.00 39.50  ? 669  HOH F O   1 
HETATM 7545 O  O   . HOH XA 5 .   ? 23.051  17.948  74.315  1.00 51.05  ? 670  HOH F O   1 
HETATM 7546 O  O   . HOH XA 5 .   ? 8.922   33.337  87.821  1.00 50.87  ? 671  HOH F O   1 
HETATM 7547 O  O   . HOH XA 5 .   ? 3.123   27.133  86.711  1.00 51.02  ? 672  HOH F O   1 
HETATM 7548 O  O   . HOH XA 5 .   ? 14.741  26.702  78.208  1.00 39.88  ? 673  HOH F O   1 
HETATM 7549 O  O   . HOH XA 5 .   ? 45.964  13.040  105.375 1.00 55.45  ? 674  HOH F O   1 
HETATM 7550 O  O   . HOH XA 5 .   ? 46.673  24.374  103.586 1.00 41.36  ? 675  HOH F O   1 
HETATM 7551 O  O   . HOH XA 5 .   ? 17.311  22.900  71.981  1.00 49.40  ? 676  HOH F O   1 
HETATM 7552 O  O   . HOH XA 5 .   ? -0.285  14.536  85.472  1.00 47.61  ? 677  HOH F O   1 
HETATM 7553 O  O   . HOH XA 5 .   ? 9.332   8.066   95.542  1.00 47.24  ? 678  HOH F O   1 
HETATM 7554 O  O   . HOH XA 5 .   ? 24.279  2.786   99.948  1.00 60.45  ? 679  HOH F O   1 
HETATM 7555 O  O   . HOH XA 5 .   ? 18.925  11.821  73.734  1.00 44.68  ? 680  HOH F O   1 
HETATM 7556 O  O   . HOH XA 5 .   ? 2.809   23.451  77.626  1.00 47.23  ? 681  HOH F O   1 
HETATM 7557 O  O   . HOH XA 5 .   ? -1.676  17.626  80.979  1.00 42.63  ? 682  HOH F O   1 
HETATM 7558 O  O   . HOH XA 5 .   ? 37.712  21.977  80.495  1.00 51.21  ? 683  HOH F O   1 
HETATM 7559 O  O   . HOH XA 5 .   ? 10.116  23.064  72.508  1.00 51.17  ? 684  HOH F O   1 
HETATM 7560 O  O   . HOH XA 5 .   ? 27.882  16.268  106.054 1.00 49.74  ? 685  HOH F O   1 
HETATM 7561 O  O   . HOH XA 5 .   ? 15.091  24.851  96.792  1.00 54.27  ? 686  HOH F O   1 
HETATM 7562 O  O   . HOH XA 5 .   ? 1.931   10.830  86.961  1.00 45.26  ? 687  HOH F O   1 
HETATM 7563 O  O   . HOH XA 5 .   ? 20.676  26.841  71.349  1.00 46.93  ? 688  HOH F O   1 
HETATM 7564 O  O   . HOH XA 5 .   ? 7.982   22.031  72.552  1.00 38.69  ? 689  HOH F O   1 
HETATM 7565 O  O   . HOH XA 5 .   ? 1.922   5.692   76.559  1.00 49.22  ? 690  HOH F O   1 
HETATM 7566 O  O   . HOH XA 5 .   ? 3.323   28.619  79.888  1.00 50.85  ? 691  HOH F O   1 
HETATM 7567 O  O   . HOH XA 5 .   ? 13.545  25.836  92.875  1.00 39.99  ? 692  HOH F O   1 
HETATM 7568 O  O   . HOH XA 5 .   ? 1.887   24.067  86.132  1.00 41.09  ? 693  HOH F O   1 
HETATM 7569 O  O   . HOH XA 5 .   ? 5.092   10.210  95.287  1.00 57.71  ? 694  HOH F O   1 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: december 26th, 2025.