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.


***  HORMONE 14-JAN-23 8I2H  ***

elNémo ID: 2602241749261548099

Job options:

ID        	=	 2602241749261548099
JOBID     	=	 HORMONE 14-JAN-23 8I2H
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    HORMONE                                 14-JAN-23   8I2H              
TITLE     FOLLICLE STIMULATING HORMONE RECEPTOR                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FOLLICLE-STIMULATING HORMONE RECEPTOR;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FSH-R,FOLLITROPIN RECEPTOR;                                 
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FSHR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    FSH, FSHR, GPCR, HORMONE                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.DUAN,P.XU,J.YANG,Y.JI,H.ZHANG,C.MAO,X.LUAN,Y.JIANG,Y.ZHANG,S.ZHANG, 
AUTHOR   2 H.E.XU                                                               
REVDAT   2   03-JUL-24 8I2H    1       REMARK                                   
REVDAT   1   22-MAR-23 8I2H    0                                                
REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 6.000                          
REMARK   3   NUMBER OF PARTICLES               : 356211                         
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 8I2H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300034808.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : FOLLICLE STIMULATING HORMONE      
REMARK 245                                    RECEPTOR                          
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON IV (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : 1200.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2200.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : OTHER                          
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 7000.00                        
REMARK 245   ILLUMINATION MODE                 : OTHER                          
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     HIS A    19                                                      
REMARK 465     LEU A   288                                                      
REMARK 465     HIS A   289                                                      
REMARK 465     PRO A   290                                                      
REMARK 465     ILE A   291                                                      
REMARK 465     CYS A   292                                                      
REMARK 465     ASN A   293                                                      
REMARK 465     LYS A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     ILE A   296                                                      
REMARK 465     LEU A   297                                                      
REMARK 465     ARG A   298                                                      
REMARK 465     GLN A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     VAL A   301                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     TYR A   303                                                      
REMARK 465     MET A   304                                                      
REMARK 465     THR A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     ARG A   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     GLN A   310                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     ALA A   315                                                      
REMARK 465     GLU A   316                                                      
REMARK 465     ASP A   317                                                      
REMARK 465     ASN A   318                                                      
REMARK 465     GLU A   319                                                      
REMARK 465     SER A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     TYR A   322                                                      
REMARK 465     SER A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     PHE A   326                                                      
REMARK 465     ASP A   327                                                      
REMARK 465     MET A   328                                                      
REMARK 465     THR A   329                                                      
REMARK 465     TYR A   330                                                      
REMARK 465     THR A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     PHE A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     TYR A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     LEU A   337                                                      
REMARK 465     CYS A   338                                                      
REMARK 465     ASN A   339                                                      
REMARK 465     GLU A   340                                                      
REMARK 465     VAL A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     ASP A   343                                                      
REMARK 465     CYS A   644                                                      
REMARK 465     GLY A   645                                                      
REMARK 465     CYS A   646                                                      
REMARK 465     TYR A   647                                                      
REMARK 465     GLU A   648                                                      
REMARK 465     MET A   649                                                      
REMARK 465     GLN A   650                                                      
REMARK 465     ALA A   651                                                      
REMARK 465     GLN A   652                                                      
REMARK 465     ILE A   653                                                      
REMARK 465     TYR A   654                                                      
REMARK 465     ARG A   655                                                      
REMARK 465     THR A   656                                                      
REMARK 465     GLU A   657                                                      
REMARK 465     THR A   658                                                      
REMARK 465     SER A   659                                                      
REMARK 465     SER A   660                                                      
REMARK 465     THR A   661                                                      
REMARK 465     VAL A   662                                                      
REMARK 465     HIS A   663                                                      
REMARK 465     ASN A   664                                                      
REMARK 465     THR A   665                                                      
REMARK 465     HIS A   666                                                      
REMARK 465     PRO A   667                                                      
REMARK 465     ARG A   668                                                      
REMARK 465     ASN A   669                                                      
REMARK 465     GLY A   670                                                      
REMARK 465     HIS A   671                                                      
REMARK 465     CYS A   672                                                      
REMARK 465     SER A   673                                                      
REMARK 465     SER A   674                                                      
REMARK 465     ALA A   675                                                      
REMARK 465     PRO A   676                                                      
REMARK 465     ARG A   677                                                      
REMARK 465     VAL A   678                                                      
REMARK 465     THR A   679                                                      
REMARK 465     ASN A   680                                                      
REMARK 465     GLY A   681                                                      
REMARK 465     SER A   682                                                      
REMARK 465     THR A   683                                                      
REMARK 465     TYR A   684                                                      
REMARK 465     ILE A   685                                                      
REMARK 465     LEU A   686                                                      
REMARK 465     VAL A   687                                                      
REMARK 465     PRO A   688                                                      
REMARK 465     LEU A   689                                                      
REMARK 465     SER A   690                                                      
REMARK 465     HIS A   691                                                      
REMARK 465     LEU A   692                                                      
REMARK 465     ALA A   693                                                      
REMARK 465     GLN A   694                                                      
REMARK 465     ASN A   695                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  20    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A  21    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  22    CG1  CG2  CD1                                       
REMARK 470     CYS A  23    SG                                                  
REMARK 470     HIS A  24    CG   ND1  CD2  CE1  NE2                             
REMARK 470     CYS A  25    SG                                                  
REMARK 470     SER A  26    OG                                                  
REMARK 470     ASN A  27    CG   OD1  ND2                                       
REMARK 470     ARG A  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A  29    CG1  CG2                                            
REMARK 470     PHE A  30    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A  31    CG   CD1  CD2                                       
REMARK 470     CYS A  32    SG                                                  
REMARK 470     GLN A  33    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     SER A  35    OG                                                  
REMARK 470     LYS A  36    CG   CD   CE   NZ                                   
REMARK 470     VAL A  37    CG1  CG2                                            
REMARK 470     THR A  38    OG1  CG2                                            
REMARK 470     GLU A  39    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  40    CG1  CG2  CD1                                       
REMARK 470     SER A  42    OG                                                  
REMARK 470     ASP A  43    CG   OD1  OD2                                       
REMARK 470     LEU A  44    CG   CD1  CD2                                       
REMARK 470     ARG A  46    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A  47    CG   OD1  ND2                                       
REMARK 470     ILE A  49    CG1  CG2  CD1                                       
REMARK 470     GLU A  50    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  51    CG   CD1  CD2                                       
REMARK 470     ARG A  52    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A  53    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A  54    CG1  CG2                                            
REMARK 470     LEU A  55    CG   CD1  CD2                                       
REMARK 470     THR A  56    OG1  CG2                                            
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     LEU A  58    CG   CD1  CD2                                       
REMARK 470     ARG A  59    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A  60    CG1  CG2                                            
REMARK 470     ILE A  61    CG1  CG2  CD1                                       
REMARK 470     GLN A  62    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  63    CG   CD   CE   NZ                                   
REMARK 470     PHE A  66    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A  67    OG                                                  
REMARK 470     PHE A  69    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A  71    CG   OD1  OD2                                       
REMARK 470     LEU A  72    CG   CD1  CD2                                       
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     ILE A  75    CG1  CG2  CD1                                       
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  77    CG1  CG2  CD1                                       
REMARK 470     SER A  78    OG                                                  
REMARK 470     GLN A  79    CG   CD   OE1  NE2                                  
REMARK 470     ASN A  80    CG   OD1  ND2                                       
REMARK 470     ASP A  81    CG   OD1  OD2                                       
REMARK 470     VAL A  82    CG1  CG2                                            
REMARK 470     LEU A  83    CG   CD1  CD2                                       
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     VAL A  85    CG1  CG2                                            
REMARK 470     ILE A  86    CG1  CG2  CD1                                       
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     VAL A  90    CG1  CG2                                            
REMARK 470     PHE A  91    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A  92    OG                                                  
REMARK 470     ASN A  93    CG   OD1  ND2                                       
REMARK 470     LEU A  94    CG   CD1  CD2                                       
REMARK 470     LYS A  96    CG   CD   CE   NZ                                   
REMARK 470     LEU A  97    CG   CD1  CD2                                       
REMARK 470     HIS A  98    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A  99    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 100    CG1  CG2  CD1                                       
REMARK 470     ARG A 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 102    CG1  CG2  CD1                                       
REMARK 470     GLU A 103    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 104    CG   CD   CE   NZ                                   
REMARK 470     ASN A 106    CG   OD1  ND2                                       
REMARK 470     ASN A 107    CG   OD1  ND2                                       
REMARK 470     LEU A 108    CG   CD1  CD2                                       
REMARK 470     LEU A 109    CG   CD1  CD2                                       
REMARK 470     TYR A 110    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 111    CG1  CG2  CD1                                       
REMARK 470     ASN A 112    CG   OD1  ND2                                       
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 116    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 117    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 118    CG   OD1  ND2                                       
REMARK 470     LEU A 119    CG   CD1  CD2                                       
REMARK 470     ASN A 121    CG   OD1  ND2                                       
REMARK 470     LEU A 122    CG   CD1  CD2                                       
REMARK 470     GLN A 123    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 124    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 125    CG   CD1  CD2                                       
REMARK 470     LEU A 126    CG   CD1  CD2                                       
REMARK 470     ILE A 127    CG1  CG2  CD1                                       
REMARK 470     SER A 128    OG                                                  
REMARK 470     ASN A 129    CG   OD1  ND2                                       
REMARK 470     THR A 130    OG1  CG2                                            
REMARK 470     ILE A 132    CG1  CG2  CD1                                       
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     HIS A 134    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 135    CG   CD1  CD2                                       
REMARK 470     ASP A 137    CG   OD1  OD2                                       
REMARK 470     VAL A 138    CG1  CG2                                            
REMARK 470     HIS A 139    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     ILE A 141    CG1  CG2  CD1                                       
REMARK 470     HIS A 142    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 143    OG                                                  
REMARK 470     LEU A 144    CG   CD1  CD2                                       
REMARK 470     GLN A 145    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     VAL A 147    CG1  CG2                                            
REMARK 470     LEU A 148    CG   CD1  CD2                                       
REMARK 470     LEU A 149    CG   CD1  CD2                                       
REMARK 470     ASP A 150    CG   OD1  OD2                                       
REMARK 470     ILE A 151    CG1  CG2  CD1                                       
REMARK 470     GLN A 152    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 153    CG   OD1  OD2                                       
REMARK 470     ASN A 154    CG   OD1  ND2                                       
REMARK 470     ILE A 155    CG1  CG2  CD1                                       
REMARK 470     ASN A 156    CG   OD1  ND2                                       
REMARK 470     ILE A 157    CG1  CG2  CD1                                       
REMARK 470     HIS A 158    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A 159    OG1  CG2                                            
REMARK 470     ILE A 160    CG1  CG2  CD1                                       
REMARK 470     GLU A 161    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 163    CG   OD1  ND2                                       
REMARK 470     SER A 164    OG                                                  
REMARK 470     PHE A 165    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 166    CG1  CG2                                            
REMARK 470     LEU A 168    CG   CD1  CD2                                       
REMARK 470     SER A 169    OG                                                  
REMARK 470     PHE A 170    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 171    CG   CD   OE1  OE2                                  
REMARK 470     SER A 172    OG                                                  
REMARK 470     VAL A 173    CG1  CG2                                            
REMARK 470     ILE A 174    CG1  CG2  CD1                                       
REMARK 470     LEU A 175    CG   CD1  CD2                                       
REMARK 470     TRP A 176    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 176    CZ3  CH2                                            
REMARK 470     LEU A 177    CG   CD1  CD2                                       
REMARK 470     ASN A 178    CG   OD1  ND2                                       
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     ASN A 180    CG   OD1  ND2                                       
REMARK 470     ILE A 182    CG1  CG2  CD1                                       
REMARK 470     GLN A 183    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 185    CG1  CG2  CD1                                       
REMARK 470     HIS A 186    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 187    CG   OD1  ND2                                       
REMARK 470     CYS A 188    SG                                                  
REMARK 470     PHE A 190    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 191    CG   OD1  ND2                                       
REMARK 470     THR A 193    OG1  CG2                                            
REMARK 470     GLN A 194    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 195    CG   CD1  CD2                                       
REMARK 470     ASP A 196    CG   OD1  OD2                                       
REMARK 470     GLU A 197    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 198    CG   CD1  CD2                                       
REMARK 470     ASN A 199    CG   OD1  ND2                                       
REMARK 470     LEU A 200    CG   CD1  CD2                                       
REMARK 470     SER A 201    OG                                                  
REMARK 470     ASP A 202    CG   OD1  OD2                                       
REMARK 470     ASN A 203    CG   OD1  ND2                                       
REMARK 470     ASN A 204    CG   OD1  ND2                                       
REMARK 470     ASN A 205    CG   OD1  ND2                                       
REMARK 470     LEU A 206    CG   CD1  CD2                                       
REMARK 470     GLU A 207    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 208    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 209    CG   CD1  CD2                                       
REMARK 470     ASN A 211    CG   OD1  ND2                                       
REMARK 470     ASP A 212    CG   OD1  OD2                                       
REMARK 470     VAL A 213    CG1  CG2                                            
REMARK 470     PHE A 214    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS A 215    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 218    OG                                                  
REMARK 470     VAL A 221    CG1  CG2                                            
REMARK 470     ILE A 222    CG1  CG2  CD1                                       
REMARK 470     LEU A 223    CG   CD1  CD2                                       
REMARK 470     ASP A 224    CG   OD1  OD2                                       
REMARK 470     ILE A 225    CG1  CG2  CD1                                       
REMARK 470     SER A 226    OG                                                  
REMARK 470     ARG A 227    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 228    OG1  CG2                                            
REMARK 470     ARG A 229    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 230    CG1  CG2  CD1                                       
REMARK 470     HIS A 231    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 232    OG                                                  
REMARK 470     LEU A 233    CG   CD1  CD2                                       
REMARK 470     SER A 235    OG                                                  
REMARK 470     TYR A 236    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 238    CG   CD1  CD2                                       
REMARK 470     GLU A 239    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 240    CG   OD1  ND2                                       
REMARK 470     LEU A 241    CG   CD1  CD2                                       
REMARK 470     LYS A 242    CG   CD   CE   NZ                                   
REMARK 470     LYS A 243    CG   CD   CE   NZ                                   
REMARK 470     LEU A 244    CG   CD1  CD2                                       
REMARK 470     ARG A 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 248    OG                                                  
REMARK 470     THR A 249    OG1  CG2                                            
REMARK 470     TYR A 250    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 251    CG   OD1  ND2                                       
REMARK 470     LEU A 252    CG   CD1  CD2                                       
REMARK 470     LYS A 253    CG   CD   CE   NZ                                   
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     LEU A 255    CG   CD1  CD2                                       
REMARK 470     THR A 257    OG1  CG2                                            
REMARK 470     LEU A 258    CG   CD1  CD2                                       
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     LEU A 261    CG   CD1  CD2                                       
REMARK 470     VAL A 262    CG1  CG2                                            
REMARK 470     LEU A 264    CG   CD1  CD2                                       
REMARK 470     MET A 265    CG   SD   CE                                        
REMARK 470     GLU A 266    CG   CD   OE1  OE2                                  
REMARK 470     SER A 268    OG                                                  
REMARK 470     LEU A 269    CG   CD1  CD2                                       
REMARK 470     THR A 270    OG1  CG2                                            
REMARK 470     TYR A 271    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A 273    OG                                                  
REMARK 470     HIS A 274    CG   ND1  CD2  CE1  NE2                             
REMARK 470     CYS A 275    SG                                                  
REMARK 470     CYS A 276    SG                                                  
REMARK 470     PHE A 278    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 280    CG   OD1  ND2                                       
REMARK 470     TRP A 281    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 281    CZ3  CH2                                            
REMARK 470     ARG A 282    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 283    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 284    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 285    CG1  CG2  CD1                                       
REMARK 470     SER A 286    OG                                                  
REMARK 470     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 344    CG1  CG2                                            
REMARK 470     THR A 345    OG1  CG2                                            
REMARK 470     CYS A 346    SG                                                  
REMARK 470     SER A 347    OG                                                  
REMARK 470     LYS A 349    CG   CD   CE   NZ                                   
REMARK 470     ASP A 351    CG   OD1  OD2                                       
REMARK 470     PHE A 353    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 354    CG   OD1  ND2                                       
REMARK 470     CYS A 356    SG                                                  
REMARK 470     GLU A 357    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 358    CG   OD1  OD2                                       
REMARK 470     ILE A 359    CG1  CG2  CD1                                       
REMARK 470     MET A 360    CG   SD   CE                                        
REMARK 470     TYR A 362    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 363    CG   OD1  ND2                                       
REMARK 470     ILE A 364    CG1  CG2  CD1                                       
REMARK 470     LEU A 365    CG   CD1  CD2                                       
REMARK 470     ARG A 366    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 367    CG1  CG2                                            
REMARK 470     LEU A 368    CG   CD1  CD2                                       
REMARK 470     ILE A 369    CG1  CG2  CD1                                       
REMARK 470     TRP A 370    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 370    CZ3  CH2                                            
REMARK 470     PHE A 371    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 372    CG1  CG2  CD1                                       
REMARK 470     SER A 373    OG                                                  
REMARK 470     ILE A 374    CG1  CG2  CD1                                       
REMARK 470     LEU A 375    CG   CD1  CD2                                       
REMARK 470     ILE A 377    CG1  CG2  CD1                                       
REMARK 470     THR A 378    OG1  CG2                                            
REMARK 470     ASN A 380    CG   OD1  ND2                                       
REMARK 470     ILE A 381    CG1  CG2  CD1                                       
REMARK 470     ILE A 382    CG1  CG2  CD1                                       
REMARK 470     VAL A 383    CG1  CG2                                            
REMARK 470     LEU A 384    CG   CD1  CD2                                       
REMARK 470     VAL A 385    CG1  CG2                                            
REMARK 470     ILE A 386    CG1  CG2  CD1                                       
REMARK 470     LEU A 387    CG   CD1  CD2                                       
REMARK 470     THR A 388    OG1  CG2                                            
REMARK 470     THR A 389    OG1  CG2                                            
REMARK 470     SER A 390    OG                                                  
REMARK 470     GLN A 391    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 392    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 393    CG   CD   CE   NZ                                   
REMARK 470     LEU A 394    CG   CD1  CD2                                       
REMARK 470     THR A 395    OG1  CG2                                            
REMARK 470     VAL A 396    CG1  CG2                                            
REMARK 470     ARG A 398    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 399    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 400    CG   CD1  CD2                                       
REMARK 470     MET A 401    CG   SD   CE                                        
REMARK 470     CYS A 402    SG                                                  
REMARK 470     ASN A 403    CG   OD1  ND2                                       
REMARK 470     LEU A 404    CG   CD1  CD2                                       
REMARK 470     PHE A 406    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 408    CG   OD1  OD2                                       
REMARK 470     LEU A 409    CG   CD1  CD2                                       
REMARK 470     CYS A 410    SG                                                  
REMARK 470     ILE A 411    CG1  CG2  CD1                                       
REMARK 470     ILE A 413    CG1  CG2  CD1                                       
REMARK 470     TYR A 414    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 415    CG   CD1  CD2                                       
REMARK 470     LEU A 416    CG   CD1  CD2                                       
REMARK 470     LEU A 417    CG   CD1  CD2                                       
REMARK 470     ILE A 418    CG1  CG2  CD1                                       
REMARK 470     SER A 420    OG                                                  
REMARK 470     VAL A 421    CG1  CG2                                            
REMARK 470     ASP A 422    CG   OD1  OD2                                       
REMARK 470     ILE A 423    CG1  CG2  CD1                                       
REMARK 470     HIS A 424    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A 425    OG1  CG2                                            
REMARK 470     LYS A 426    CG   CD   CE   NZ                                   
REMARK 470     SER A 427    OG                                                  
REMARK 470     GLN A 428    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 429    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS A 430    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 431    CG   OD1  ND2                                       
REMARK 470     TYR A 432    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 434    CG1  CG2  CD1                                       
REMARK 470     ASP A 435    CG   OD1  OD2                                       
REMARK 470     TRP A 436    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 436    CZ3  CH2                                            
REMARK 470     GLN A 437    CG   CD   OE1  NE2                                  
REMARK 470     THR A 438    OG1  CG2                                            
REMARK 470     CYS A 442    SG                                                  
REMARK 470     ASP A 443    CG   OD1  OD2                                       
REMARK 470     PHE A 447    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 448    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 449    OG1  CG2                                            
REMARK 470     VAL A 450    CG1  CG2                                            
REMARK 470     PHE A 451    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER A 453    OG                                                  
REMARK 470     GLU A 454    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 455    CG   CD1  CD2                                       
REMARK 470     SER A 456    OG                                                  
REMARK 470     VAL A 457    CG1  CG2                                            
REMARK 470     TYR A 458    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR A 459    OG1  CG2                                            
REMARK 470     LEU A 460    CG   CD1  CD2                                       
REMARK 470     THR A 461    OG1  CG2                                            
REMARK 470     ILE A 463    CG1  CG2  CD1                                       
REMARK 470     THR A 464    OG1  CG2                                            
REMARK 470     LEU A 465    CG   CD1  CD2                                       
REMARK 470     GLU A 466    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 467    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A 468    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 468    CZ3  CH2                                            
REMARK 470     HIS A 469    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A 470    OG1  CG2                                            
REMARK 470     ILE A 471    CG1  CG2  CD1                                       
REMARK 470     THR A 472    OG1  CG2                                            
REMARK 470     HIS A 473    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET A 475    CG   SD   CE                                        
REMARK 470     GLN A 476    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 477    CG   CD1  CD2                                       
REMARK 470     ASP A 478    CG   OD1  OD2                                       
REMARK 470     CYS A 479    SG                                                  
REMARK 470     LYS A 480    CG   CD   CE   NZ                                   
REMARK 470     VAL A 481    CG1  CG2                                            
REMARK 470     GLN A 482    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 483    CG   CD1  CD2                                       
REMARK 470     ARG A 484    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A 485    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 488    OG                                                  
REMARK 470     VAL A 489    CG1  CG2                                            
REMARK 470     MET A 490    CG   SD   CE                                        
REMARK 470     VAL A 491    CG1  CG2                                            
REMARK 470     MET A 492    CG   SD   CE                                        
REMARK 470     TRP A 494    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 494    CZ3  CH2                                            
REMARK 470     ILE A 495    CG1  CG2  CD1                                       
REMARK 470     PHE A 496    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 498    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 502    CG   CD1  CD2                                       
REMARK 470     PHE A 503    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 505    CG1  CG2  CD1                                       
REMARK 470     PHE A 506    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 508    CG1  CG2  CD1                                       
REMARK 470     SER A 509    OG                                                  
REMARK 470     SER A 510    OG                                                  
REMARK 470     TYR A 511    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A 512    CG   SD   CE                                        
REMARK 470     LYS A 513    CG   CD   CE   NZ                                   
REMARK 470     VAL A 514    CG1  CG2                                            
REMARK 470     SER A 515    OG                                                  
REMARK 470     ILE A 516    CG1  CG2  CD1                                       
REMARK 470     CYS A 517    SG                                                  
REMARK 470     LEU A 518    CG   CD1  CD2                                       
REMARK 470     MET A 520    CG   SD   CE                                        
REMARK 470     ASP A 521    CG   OD1  OD2                                       
REMARK 470     ILE A 522    CG1  CG2  CD1                                       
REMARK 470     ASP A 523    CG   OD1  OD2                                       
REMARK 470     SER A 524    OG                                                  
REMARK 470     LEU A 526    CG   CD1  CD2                                       
REMARK 470     SER A 527    OG                                                  
REMARK 470     GLN A 528    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 529    CG   CD1  CD2                                       
REMARK 470     TYR A 530    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 531    CG1  CG2                                            
REMARK 470     MET A 532    CG   SD   CE                                        
REMARK 470     SER A 533    OG                                                  
REMARK 470     LEU A 534    CG   CD1  CD2                                       
REMARK 470     LEU A 535    CG   CD1  CD2                                       
REMARK 470     VAL A 536    CG1  CG2                                            
REMARK 470     LEU A 537    CG   CD1  CD2                                       
REMARK 470     ASN A 538    CG   OD1  ND2                                       
REMARK 470     VAL A 539    CG1  CG2                                            
REMARK 470     LEU A 540    CG   CD1  CD2                                       
REMARK 470     PHE A 542    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 543    CG1  CG2                                            
REMARK 470     VAL A 544    CG1  CG2                                            
REMARK 470     ILE A 545    CG1  CG2  CD1                                       
REMARK 470     CYS A 546    SG                                                  
REMARK 470     CYS A 548    SG                                                  
REMARK 470     TYR A 549    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 550    CG1  CG2  CD1                                       
REMARK 470     HIS A 551    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 552    CG1  CG2  CD1                                       
REMARK 470     TYR A 553    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 554    CG   CD1  CD2                                       
REMARK 470     THR A 555    OG1  CG2                                            
REMARK 470     VAL A 556    CG1  CG2                                            
REMARK 470     ARG A 557    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 558    CG   OD1  ND2                                       
REMARK 470     ASN A 560    CG   OD1  ND2                                       
REMARK 470     ILE A 561    CG1  CG2  CD1                                       
REMARK 470     VAL A 562    CG1  CG2                                            
REMARK 470     SER A 563    OG                                                  
REMARK 470     SER A 564    OG                                                  
REMARK 470     SER A 565    OG                                                  
REMARK 470     SER A 566    OG                                                  
REMARK 470     ASP A 567    CG   OD1  OD2                                       
REMARK 470     THR A 568    OG1  CG2                                            
REMARK 470     ARG A 569    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 570    CG1  CG2  CD1                                       
REMARK 470     LYS A 572    CG   CD   CE   NZ                                   
REMARK 470     ARG A 573    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 574    CG   SD   CE                                        
REMARK 470     MET A 576    CG   SD   CE                                        
REMARK 470     LEU A 577    CG   CD1  CD2                                       
REMARK 470     ILE A 578    CG1  CG2  CD1                                       
REMARK 470     PHE A 579    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 580    OG1  CG2                                            
REMARK 470     ASP A 581    CG   OD1  OD2                                       
REMARK 470     PHE A 582    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 583    CG   CD1  CD2                                       
REMARK 470     CYS A 584    SG                                                  
REMARK 470     MET A 585    CG   SD   CE                                        
REMARK 470     ILE A 588    CG1  CG2  CD1                                       
REMARK 470     SER A 589    OG                                                  
REMARK 470     PHE A 590    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 591    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 593    CG1  CG2  CD1                                       
REMARK 470     SER A 594    OG                                                  
REMARK 470     SER A 596    OG                                                  
REMARK 470     LEU A 597    CG   CD1  CD2                                       
REMARK 470     LYS A 598    CG   CD   CE   NZ                                   
REMARK 470     VAL A 599    CG1  CG2                                            
REMARK 470     LEU A 601    CG   CD1  CD2                                       
REMARK 470     ILE A 602    CG1  CG2  CD1                                       
REMARK 470     THR A 603    OG1  CG2                                            
REMARK 470     VAL A 604    CG1  CG2                                            
REMARK 470     SER A 605    OG                                                  
REMARK 470     LYS A 606    CG   CD   CE   NZ                                   
REMARK 470     LYS A 608    CG   CD   CE   NZ                                   
REMARK 470     ILE A 609    CG1  CG2  CD1                                       
REMARK 470     LEU A 610    CG   CD1  CD2                                       
REMARK 470     LEU A 611    CG   CD1  CD2                                       
REMARK 470     VAL A 612    CG1  CG2                                            
REMARK 470     LEU A 613    CG   CD1  CD2                                       
REMARK 470     PHE A 614    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS A 615    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A 617    CG1  CG2  CD1                                       
REMARK 470     ASN A 618    CG   OD1  ND2                                       
REMARK 470     SER A 619    OG                                                  
REMARK 470     CYS A 620    SG                                                  
REMARK 470     ASN A 622    CG   OD1  ND2                                       
REMARK 470     PHE A 624    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 625    CG   CD1  CD2                                       
REMARK 470     TYR A 626    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 628    CG1  CG2  CD1                                       
REMARK 470     PHE A 629    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 630    OG1  CG2                                            
REMARK 470     LYS A 631    CG   CD   CE   NZ                                   
REMARK 470     ASN A 632    CG   OD1  ND2                                       
REMARK 470     PHE A 633    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 634    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 635    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 636    CG   OD1  OD2                                       
REMARK 470     PHE A 637    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 638    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 639    CG1  CG2  CD1                                       
REMARK 470     LEU A 640    CG   CD1  CD2                                       
REMARK 470     LEU A 641    CG   CD1  CD2                                       
REMARK 470     SER A 642    OG                                                  
REMARK 470     LYS A 643    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  34      174.36     71.71                                   
REMARK 500    THR A 425       34.44    -99.84                                   
REMARK 500    SER A 509      179.14     66.81                                   
REMARK 500    LEU A 613      -60.43    -90.77                                   
REMARK 500    TYR A 626      -60.90    -91.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-35136   RELATED DB: EMDB                             
REMARK 900 FOLLICLE STIMULATING HORMONE RECEPTOR                                
DBREF  8I2H A   14   695  UNP    P23945   FSHR_HUMAN      14    695             
HELIX    1   1 ASN A  363  THR A  389  1                                  27
HELIX    2   2 VAL A  396  HIS A  424  1                                  29
HELIX    3   3 TYR A  429  THR A  438  1                                  10
HELIX    4   4 ALA A  440  THR A  472  1                                  33
HELIX    5   5 LEU A  483  LEU A  502  1                                  20
HELIX    6   6 PRO A  504  PHE A  506  1                                   3
HELIX    7   7 TYR A  511  LYS A  513  1                                   3
HELIX    8   8 PRO A  525  ARG A  557  1                                  33
HELIX    9   9 SER A  565  SER A  596  1                                  32
HELIX   10  10 VAL A  604  ILE A  628  1                                  25
HELIX   11  11 LYS A  631  SER A  642  1                                  12
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1               
MODEL        1
ATOM      1  N   TYR A 362      95.933 117.691 111.719  1.00 87.33           N
ATOM      2  CA  TYR A 362      95.177 117.878 112.949  1.00 87.33           C
ATOM      3  C   TYR A 362      95.997 118.665 113.964  1.00 87.33           C
ATOM      4  O   TYR A 362      97.174 118.376 114.197  1.00 87.33           O
ATOM      5  CB  TYR A 362      94.758 116.527 113.531  1.00 87.33           C
ATOM      6  CG  TYR A 362      93.904 116.634 114.775  1.00 99.99           C
ATOM      7  CD1 TYR A 362      92.545 116.903 114.684  1.00 99.99           C
ATOM      8  CD2 TYR A 362      94.460 116.463 116.036  1.00 99.99           C
ATOM      9  CE1 TYR A 362      91.759 117.004 115.815  1.00 99.99           C
ATOM     10  CE2 TYR A 362      93.690 116.559 117.178  1.00 99.99           C
ATOM     11  CZ  TYR A 362      92.338 116.829 117.066  1.00 99.99           C
ATOM     12  OH  TYR A 362      91.562 116.926 118.197  1.00 99.99           O
ATOM     13  N   ASN A 363      95.362 119.670 114.572  1.00 89.36           N
ATOM     14  CA  ASN A 363      96.043 120.461 115.591  1.00 89.36           C
ATOM     15  C   ASN A 363      96.380 119.614 116.812  1.00 89.36           C
ATOM     16  O   ASN A 363      97.459 119.762 117.398  1.00 89.36           O
ATOM     17  CB  ASN A 363      95.185 121.659 116.002  1.00 89.36           C
ATOM     18  CG  ASN A 363      95.922 122.619 116.914  1.00 99.99           C
ATOM     19  OD1 ASN A 363      96.345 122.249 118.009  1.00 99.99           O
ATOM     20  ND2 ASN A 363      96.081 123.856 116.463  1.00 99.99           N
ATOM     21  N   ILE A 364      95.469 118.725 117.210  1.00 90.13           N
ATOM     22  CA  ILE A 364      95.721 117.870 118.366  1.00 90.13           C
ATOM     23  C   ILE A 364      96.920 116.966 118.105  1.00 90.13           C
ATOM     24  O   ILE A 364      97.779 116.781 118.975  1.00 90.13           O
ATOM     25  CB  ILE A 364      94.492 117.009 118.710  1.00 90.13           C
ATOM     26  CG1 ILE A 364      93.327 117.897 119.154  1.00 99.99           C
ATOM     27  CG2 ILE A 364      94.817 116.040 119.836  1.00 99.99           C
ATOM     28  CD1 ILE A 364      92.012 117.161 119.281  1.00 99.99           C
ATOM     29  N   LEU A 365      96.991 116.386 116.905  1.00 88.48           N
ATOM     30  CA  LEU A 365      98.122 115.526 116.570  1.00 88.48           C
ATOM     31  C   LEU A 365      99.429 116.307 116.588  1.00 88.48           C
ATOM     32  O   LEU A 365     100.441 115.826 117.109  1.00 88.48           O
ATOM     33  CB  LEU A 365      97.915 114.877 115.200  1.00 88.48           C
ATOM     34  CG  LEU A 365      96.742 113.900 115.083  1.00 99.99           C
ATOM     35  CD1 LEU A 365      96.564 113.446 113.643  1.00 99.99           C
ATOM     36  CD2 LEU A 365      96.981 112.669 115.943  1.00 99.99           C
ATOM     37  N   ARG A 366      99.427 117.519 116.026  1.00 91.21           N
ATOM     38  CA  ARG A 366     100.637 118.333 116.029  1.00 91.21           C
ATOM     39  C   ARG A 366     101.069 118.682 117.447  1.00 91.21           C
ATOM     40  O   ARG A 366     102.264 118.646 117.759  1.00 91.21           O
ATOM     41  CB  ARG A 366     100.425 119.612 115.217  1.00 91.21           C
ATOM     42  CG  ARG A 366     100.117 119.371 113.749  1.00 99.99           C
ATOM     43  CD  ARG A 366     101.321 118.800 113.020  1.00 99.99           C
ATOM     44  NE  ARG A 366     102.435 119.742 112.977  1.00 99.99           N
ATOM     45  CZ  ARG A 366     103.636 119.459 112.485  1.00 99.99           C
ATOM     46  NH1 ARG A 366     103.882 118.254 111.989  1.00 99.99           N
ATOM     47  NH2 ARG A 366     104.588 120.382 112.488  1.00 99.99           N
ATOM     48  N   VAL A 367     100.116 119.024 118.314  1.00 92.44           N
ATOM     49  CA  VAL A 367     100.449 119.338 119.699  1.00 92.44           C
ATOM     50  C   VAL A 367     101.015 118.114 120.409  1.00 92.44           C
ATOM     51  O   VAL A 367     101.994 118.214 121.156  1.00 92.44           O
ATOM     52  CB  VAL A 367      99.221 119.853 120.471  1.00 92.44           C
ATOM     53  CG1 VAL A 367      99.561 120.056 121.940  1.00 99.99           C
ATOM     54  CG2 VAL A 367      98.750 121.182 119.899  1.00 99.99           C
ATOM     55  N   LEU A 368     100.411 116.944 120.191  1.00 91.22           N
ATOM     56  CA  LEU A 368     100.851 115.741 120.890  1.00 91.22           C
ATOM     57  C   LEU A 368     102.203 115.262 120.372  1.00 91.22           C
ATOM     58  O   LEU A 368     102.955 114.597 121.093  1.00 91.22           O
ATOM     59  CB  LEU A 368      99.811 114.628 120.748  1.00 91.22           C
ATOM     60  CG  LEU A 368      98.451 114.883 121.403  1.00 99.99           C
ATOM     61  CD1 LEU A 368      97.474 113.769 121.062  1.00 99.99           C
ATOM     62  CD2 LEU A 368      98.589 114.947 122.916  1.00 99.99           C
ATOM     63  N   ILE A 369     102.522 115.578 119.114  1.00 91.38           N
ATOM     64  CA  ILE A 369     103.765 115.094 118.521  1.00 91.38           C
ATOM     65  C   ILE A 369     104.977 115.645 119.258  1.00 91.38           C
ATOM     66  O   ILE A 369     105.928 114.906 119.542  1.00 91.38           O
ATOM     67  CB  ILE A 369     103.865 115.474 117.032  1.00 91.38           C
ATOM     68  CG1 ILE A 369     102.772 114.767 116.227  1.00 99.99           C
ATOM     69  CG2 ILE A 369     105.218 115.068 116.468  1.00 99.99           C
ATOM     70  CD1 ILE A 369     102.645 115.263 114.804  1.00 99.99           C
ATOM     71  N   TRP A 370     104.979 116.944 119.563  1.00 93.07           N
ATOM     72  CA  TRP A 370     106.122 117.538 120.248  1.00 93.07           C
ATOM     73  C   TRP A 370     106.312 116.920 121.628  1.00 93.07           C
ATOM     74  O   TRP A 370     107.436 116.598 122.030  1.00 93.07           O
ATOM     75  CB  TRP A 370     105.948 119.053 120.366  1.00 93.07           C
ATOM     76  CG  TRP A 370     105.945 119.762 119.047  1.00 99.99           C
ATOM     77  CD1 TRP A 370     104.853 120.113 118.308  1.00 99.99           C
ATOM     78  CD2 TRP A 370     107.092 120.204 118.310  1.00 99.99           C
ATOM     79  NE1 TRP A 370     105.245 120.748 117.153  1.00 99.99           N
ATOM     80  CE2 TRP A 370     106.618 120.816 117.133  1.00 99.99           C
ATOM     81  CE3 TRP A 370     108.470 120.143 118.533  1.00 99.99           C
ATOM     82  CZ2 TRP A 370     107.474 121.364 116.178  1.00 99.99           C
ATOM     83  CZ3 TRP A 370     109.318 120.686 117.586  1.00 99.99           C
ATOM     84  CH2 TRP A 370     108.821 121.291 116.420  1.00 99.99           C
ATOM     85  N   PHE A 371     105.215 116.743 122.367  1.00 92.36           N
ATOM     86  CA  PHE A 371     105.304 116.141 123.693  1.00 92.36           C
ATOM     87  C   PHE A 371     105.821 114.712 123.607  1.00 92.36           C
ATOM     88  O   PHE A 371     106.664 114.294 124.410  1.00 92.36           O
ATOM     89  CB  PHE A 371     103.941 116.171 124.388  1.00 92.36           C
ATOM     90  CG  PHE A 371     103.963 115.632 125.789  1.00 99.99           C
ATOM     91  CD1 PHE A 371     104.408 116.415 126.841  1.00 99.99           C
ATOM     92  CD2 PHE A 371     103.540 114.343 126.058  1.00 99.99           C
ATOM     93  CE1 PHE A 371     104.429 115.920 128.131  1.00 99.99           C
ATOM     94  CE2 PHE A 371     103.561 113.844 127.347  1.00 99.99           C
ATOM     95  CZ  PHE A 371     104.004 114.634 128.384  1.00 99.99           C
ATOM     96  N   ILE A 372     105.327 113.944 122.634  1.00 90.82           N
ATOM     97  CA  ILE A 372     105.762 112.558 122.487  1.00 90.82           C
ATOM     98  C   ILE A 372     107.250 112.504 122.165  1.00 90.82           C
ATOM     99  O   ILE A 372     107.998 111.699 122.732  1.00 90.82           O
ATOM    100  CB  ILE A 372     104.968 111.831 121.386  1.00 90.82           C
ATOM    101  CG1 ILE A 372     103.494 111.716 121.779  1.00 99.99           C
ATOM    102  CG2 ILE A 372     105.520 110.431 121.166  1.00 99.99           C
ATOM    103  CD1 ILE A 372     102.599 111.232 120.660  1.00 99.99           C
ATOM    104  N   SER A 373     107.700 113.360 121.245  1.00 92.49           N
ATOM    105  CA  SER A 373     109.113 113.373 120.883  1.00 92.49           C
ATOM    106  C   SER A 373     109.983 113.763 122.071  1.00 92.49           C
ATOM    107  O   SER A 373     111.027 113.144 122.312  1.00 92.49           O
ATOM    108  CB  SER A 373     109.358 114.330 119.715  1.00 92.49           C
ATOM    109  OG  SER A 373     109.020 115.660 120.067  1.00 99.99           O
ATOM    110  N   ILE A 374     109.569 114.782 122.827  1.00 92.61           N
ATOM    111  CA  ILE A 374     110.353 115.215 123.981  1.00 92.61           C
ATOM    112  C   ILE A 374     110.431 114.098 125.014  1.00 92.61           C
ATOM    113  O   ILE A 374     111.499 113.815 125.571  1.00 92.61           O
ATOM    114  CB  ILE A 374     109.754 116.477 124.628  1.00 92.61           C
ATOM    115  CG1 ILE A 374     109.834 117.661 123.662  1.00 99.99           C
ATOM    116  CG2 ILE A 374     110.513 116.837 125.897  1.00 99.99           C
ATOM    117  CD1 ILE A 374     109.059 118.877 124.119  1.00 99.99           C
ATOM    118  N   LEU A 375     109.296 113.448 125.288  1.00 90.79           N
ATOM    119  CA  LEU A 375     109.285 112.366 126.265  1.00 90.79           C
ATOM    120  C   LEU A 375     110.170 111.212 125.817  1.00 90.79           C
ATOM    121  O   LEU A 375     110.923 110.651 126.620  1.00 90.79           O
ATOM    122  CB  LEU A 375     107.857 111.873 126.502  1.00 90.79           C
ATOM    123  CG  LEU A 375     106.891 112.872 127.142  1.00 99.99           C
ATOM    124  CD1 LEU A 375     105.480 112.305 127.185  1.00 99.99           C
ATOM    125  CD2 LEU A 375     107.317 113.193 128.566  1.00 99.99           C
ATOM    126  N   ALA A 376     110.097 110.843 124.536  1.00 91.01           N
ATOM    127  CA  ALA A 376     110.920 109.750 124.033  1.00 91.01           C
ATOM    128  C   ALA A 376     112.401 110.088 124.141  1.00 91.01           C
ATOM    129  O   ALA A 376     113.212 109.256 124.565  1.00 91.01           O
ATOM    130  CB  ALA A 376     110.555 109.425 122.577  1.00 91.01           C
ATOM    131  N   ILE A 377     112.774 111.313 123.762  1.00 93.66           N
ATOM    132  CA  ILE A 377     114.177 111.712 123.824  1.00 93.66           C
ATOM    133  C   ILE A 377     114.669 111.688 125.265  1.00 93.66           C
ATOM    134  O   ILE A 377     115.754 111.173 125.563  1.00 93.66           O
ATOM    135  CB  ILE A 377     114.391 113.115 123.228  1.00 93.66           C
ATOM    136  CG1 ILE A 377     114.074 113.114 121.731  1.00 99.99           C
ATOM    137  CG2 ILE A 377     115.834 113.560 123.415  1.00 99.99           C
ATOM    138  CD1 ILE A 377     114.026 114.494 121.115  1.00 99.99           C
ATOM    139  N   THR A 378     113.877 112.248 126.183  1.00 92.02           N
ATOM    140  CA  THR A 378     114.280 112.280 127.585  1.00 92.02           C
ATOM    141  C   THR A 378     114.416 110.871 128.146  1.00 92.02           C
ATOM    142  O   THR A 378     115.379 110.563 128.858  1.00 92.02           O
ATOM    143  CB  THR A 378     113.276 113.072 128.443  1.00 92.02           C
ATOM    144  OG1 THR A 378     111.994 112.433 128.395  1.00 99.99           O
ATOM    145  CG2 THR A 378     113.136 114.494 127.923  1.00 99.99           C
ATOM    146  N   GLY A 379     113.458 109.996 127.832  1.00 89.72           N
ATOM    147  CA  GLY A 379     113.530 108.631 128.326  1.00 89.72           C
ATOM    148  C   GLY A 379     114.739 107.889 127.795  1.00 89.72           C
ATOM    149  O   GLY A 379     115.433 107.193 128.540  1.00 89.72           O
ATOM    150  N   ASN A 380     115.010 108.028 126.495  1.00 93.01           N
ATOM    151  CA  ASN A 380     116.174 107.368 125.915  1.00 93.01           C
ATOM    152  C   ASN A 380     117.465 107.883 126.538  1.00 93.01           C
ATOM    153  O   ASN A 380     118.360 107.094 126.868  1.00 93.01           O
ATOM    154  CB  ASN A 380     116.204 107.569 124.399  1.00 93.01           C
ATOM    155  CG  ASN A 380     115.108 106.801 123.687  1.00 99.99           C
ATOM    156  OD1 ASN A 380     114.254 107.390 123.025  1.00 99.99           O
ATOM    157  ND2 ASN A 380     115.131 105.481 123.819  1.00 99.99           N
ATOM    158  N   ILE A 381     117.579 109.202 126.714  1.00 93.87           N
ATOM    159  CA  ILE A 381     118.790 109.770 127.300  1.00 93.87           C
ATOM    160  C   ILE A 381     118.972 109.267 128.726  1.00 93.87           C
ATOM    161  O   ILE A 381     120.076 108.882 129.132  1.00 93.87           O
ATOM    162  CB  ILE A 381     118.750 111.309 127.296  1.00 93.87           C
ATOM    163  CG1 ILE A 381     118.751 111.839 125.861  1.00 99.99           C
ATOM    164  CG2 ILE A 381     119.962 111.876 128.020  1.00 99.99           C
ATOM    165  CD1 ILE A 381     118.474 113.322 125.757  1.00 99.99           C
ATOM    166  N   ILE A 382     117.891 109.265 129.510  1.00 90.85           N
ATOM    167  CA  ILE A 382     117.980 108.822 130.898  1.00 90.85           C
ATOM    168  C   ILE A 382     118.371 107.352 130.964  1.00 90.85           C
ATOM    169  O   ILE A 382     119.213 106.955 131.778  1.00 90.85           O
ATOM    170  CB  ILE A 382     116.650 109.034 131.644  1.00 90.85           C
ATOM    171  CG1 ILE A 382     116.331 110.526 131.753  1.00 99.99           C
ATOM    172  CG2 ILE A 382     116.728 108.454 133.048  1.00 99.99           C
ATOM    173  CD1 ILE A 382     114.935 110.818 132.256  1.00 99.99           C
ATOM    174  N   VAL A 383     117.763 106.520 130.115  1.00 89.77           N
ATOM    175  CA  VAL A 383     118.074 105.094 130.124  1.00 89.77           C
ATOM    176  C   VAL A 383     119.532 104.866 129.751  1.00 89.77           C
ATOM    177  O   VAL A 383     120.233 104.069 130.388  1.00 89.77           O
ATOM    178  CB  VAL A 383     117.167 104.313 129.156  1.00 89.77           C
ATOM    179  CG1 VAL A 383     117.589 102.853 129.090  1.00 99.99           C
ATOM    180  CG2 VAL A 383     115.718 104.373 129.617  1.00 99.99           C
ATOM    181  N   LEU A 384     120.013 105.556 128.714  1.00 92.15           N
ATOM    182  CA  LEU A 384     121.404 105.395 128.307  1.00 92.15           C
ATOM    183  C   LEU A 384     122.354 105.837 129.411  1.00 92.15           C
ATOM    184  O   LEU A 384     123.353 105.162 129.689  1.00 92.15           O
ATOM    185  CB  LEU A 384     121.682 106.183 127.026  1.00 92.15           C
ATOM    186  CG  LEU A 384     120.940 105.721 125.770  1.00 99.99           C
ATOM    187  CD1 LEU A 384     121.195 106.675 124.613  1.00 99.99           C
ATOM    188  CD2 LEU A 384     121.405 104.335 125.353  1.00 99.99           C
ATOM    189  N   VAL A 385     122.060 106.969 130.056  1.00 91.11           N
ATOM    190  CA  VAL A 385     122.926 107.466 131.121  1.00 91.11           C
ATOM    191  C   VAL A 385     122.956 106.478 132.281  1.00 91.11           C
ATOM    192  O   VAL A 385     124.019 106.174 132.834  1.00 91.11           O
ATOM    193  CB  VAL A 385     122.463 108.844 131.628  1.00 91.11           C
ATOM    194  CG1 VAL A 385     123.303 109.285 132.817  1.00 99.99           C
ATOM    195  CG2 VAL A 385     122.598 109.888 130.530  1.00 99.99           C
ATOM    196  N   ILE A 386     121.787 105.963 132.667  1.00 88.31           N
ATOM    197  CA  ILE A 386     121.723 105.017 133.776  1.00 88.31           C
ATOM    198  C   ILE A 386     122.499 103.751 133.440  1.00 88.31           C
ATOM    199  O   ILE A 386     123.255 103.230 134.269  1.00 88.31           O
ATOM    200  CB  ILE A 386     120.268 104.652 134.123  1.00 88.31           C
ATOM    201  CG1 ILE A 386     119.519 105.881 134.642  1.00 99.99           C
ATOM    202  CG2 ILE A 386     120.230 103.574 135.196  1.00 99.99           C
ATOM    203  CD1 ILE A 386     118.027 105.674 134.781  1.00 99.99           C
ATOM    204  N   LEU A 387     122.327 103.235 132.221  1.00 87.66           N
ATOM    205  CA  LEU A 387     123.029 102.017 131.833  1.00 87.66           C
ATOM    206  C   LEU A 387     124.538 102.229 131.815  1.00 87.66           C
ATOM    207  O   LEU A 387     125.296 101.368 132.277  1.00 87.66           O
ATOM    208  CB  LEU A 387     122.551 101.536 130.462  1.00 87.66           C
ATOM    209  CG  LEU A 387     121.090 101.090 130.371  1.00 99.99           C
ATOM    210  CD1 LEU A 387     120.711 100.779 128.931  1.00 99.99           C
ATOM    211  CD2 LEU A 387     120.859  99.838 131.203  1.00 99.99           C
ATOM    212  N   THR A 388     124.994 103.367 131.285  1.00 87.57           N
ATOM    213  CA  THR A 388     126.430 103.609 131.191  1.00 87.57           C
ATOM    214  C   THR A 388     127.056 103.855 132.558  1.00 87.57           C
ATOM    215  O   THR A 388     128.165 103.378 132.823  1.00 87.57           O
ATOM    216  CB  THR A 388     126.741 104.812 130.282  1.00 87.57           C
ATOM    217  OG1 THR A 388     126.157 105.998 130.837  1.00 99.99           O
ATOM    218  CG2 THR A 388     126.172 104.589 128.889  1.00 99.99           C
ATOM    219  N   THR A 389     126.370 104.590 133.434  1.00 86.90           N
ATOM    220  CA  THR A 389     126.933 104.954 134.728  1.00 86.90           C
ATOM    221  C   THR A 389     126.724 103.887 135.795  1.00 86.90           C
ATOM    222  O   THR A 389     127.250 104.037 136.904  1.00 86.90           O
ATOM    223  CB  THR A 389     126.336 106.273 135.252  1.00 86.90           C
ATOM    224  OG1 THR A 389     124.924 106.120 135.443  1.00 99.99           O
ATOM    225  CG2 THR A 389     126.579 107.399 134.258  1.00 99.99           C
ATOM    226  N   SER A 390     125.977 102.826 135.499  1.00 82.56           N
ATOM    227  CA  SER A 390     125.733 101.792 136.494  1.00 82.56           C
ATOM    228  C   SER A 390     127.045 101.159 136.940  1.00 82.56           C
ATOM    229  O   SER A 390     127.893 100.796 136.118  1.00 82.56           O
ATOM    230  CB  SER A 390     124.787 100.726 135.938  1.00 82.56           C
ATOM    231  OG  SER A 390     125.354 100.078 134.814  1.00 99.99           O
ATOM    232  N   GLN A 391     127.210 101.027 138.258  1.00 80.19           N
ATOM    233  CA  GLN A 391     128.425 100.421 138.793  1.00 80.19           C
ATOM    234  C   GLN A 391     128.459  98.918 138.547  1.00 80.19           C
ATOM    235  O   GLN A 391     129.542  98.326 138.487  1.00 80.19           O
ATOM    236  CB  GLN A 391     128.551 100.705 140.291  1.00 80.19           C
ATOM    237  CG  GLN A 391     128.737 102.175 140.630  1.00 99.99           C
ATOM    238  CD  GLN A 391     127.420 102.922 140.727  1.00 99.99           C
ATOM    239  OE1 GLN A 391     126.352 102.341 140.541  1.00 99.99           O
ATOM    240  NE2 GLN A 391     127.496 104.214 141.024  1.00 99.99           N
ATOM    241  N   TYR A 392     127.295  98.289 138.404  1.00 77.94           N
ATOM    242  CA  TYR A 392     127.246  96.852 138.176  1.00 77.94           C
ATOM    243  C   TYR A 392     127.775  96.513 136.787  1.00 77.94           C
ATOM    244  O   TYR A 392     127.834  97.361 135.893  1.00 77.94           O
ATOM    245  CB  TYR A 392     125.818  96.331 138.347  1.00 77.94           C
ATOM    246  CG  TYR A 392     124.829  96.918 137.364  1.00 99.99           C
ATOM    247  CD1 TYR A 392     124.596  96.309 136.139  1.00 99.99           C
ATOM    248  CD2 TYR A 392     124.132  98.081 137.667  1.00 99.99           C
ATOM    249  CE1 TYR A 392     123.696  96.839 135.236  1.00 99.99           C
ATOM    250  CE2 TYR A 392     123.228  98.626 136.777  1.00 99.99           C
ATOM    251  CZ  TYR A 392     123.010  98.003 135.561  1.00 99.99           C
ATOM    252  OH  TYR A 392     122.112  98.538 134.668  1.00 99.99           O
ATOM    253  N   LYS A 393     128.166  95.253 136.614  1.00 81.43           N
ATOM    254  CA  LYS A 393     128.690  94.804 135.332  1.00 81.43           C
ATOM    255  C   LYS A 393     127.629  94.936 134.246  1.00 81.43           C
ATOM    256  O   LYS A 393     126.434  94.738 134.483  1.00 81.43           O
ATOM    257  CB  LYS A 393     129.179  93.358 135.430  1.00 81.43           C
ATOM    258  CG  LYS A 393     129.810  92.828 134.153  1.00 99.99           C
ATOM    259  CD  LYS A 393     130.272  91.390 134.321  1.00 99.99           C
ATOM    260  CE  LYS A 393     130.903  90.861 133.042  1.00 99.99           C
ATOM    261  NZ  LYS A 393     129.918  90.777 131.929  1.00 99.99           N
ATOM    262  N   LEU A 394     128.079  95.276 133.041  1.00 85.63           N
ATOM    263  CA  LEU A 394     127.186  95.468 131.900  1.00 85.63           C
ATOM    264  C   LEU A 394     126.955  94.120 131.230  1.00 85.63           C
ATOM    265  O   LEU A 394     127.842  93.582 130.563  1.00 85.63           O
ATOM    266  CB  LEU A 394     127.777  96.485 130.922  1.00 85.63           C
ATOM    267  CG  LEU A 394     127.924  97.918 131.440  1.00 99.99           C
ATOM    268  CD1 LEU A 394     128.654  98.784 130.425  1.00 99.99           C
ATOM    269  CD2 LEU A 394     126.559  98.537 131.699  1.00 99.99           C
ATOM    270  N   THR A 395     125.758  93.569 131.408  1.00 88.23           N
ATOM    271  CA  THR A 395     125.416  92.284 130.823  1.00 88.23           C
ATOM    272  C   THR A 395     124.904  92.461 129.395  1.00 88.23           C
ATOM    273  O   THR A 395     124.591  93.568 128.949  1.00 88.23           O
ATOM    274  CB  THR A 395     124.353  91.548 131.660  1.00 88.23           C
ATOM    275  OG1 THR A 395     123.147  92.322 131.693  1.00 99.99           O
ATOM    276  CG2 THR A 395     124.845  91.342 133.084  1.00 99.99           C
ATOM    277  N   VAL A 396     124.828  91.344 128.677  1.00 89.68           N
ATOM    278  CA  VAL A 396     124.348  91.328 127.296  1.00 89.68           C
ATOM    279  C   VAL A 396     122.962  91.961 127.234  1.00 89.68           C
ATOM    280  O   VAL A 396     122.700  92.787 126.345  1.00 89.68           O
ATOM    281  CB  VAL A 396     124.301  89.896 126.732  1.00 89.68           C
ATOM    282  CG1 VAL A 396     123.684  89.891 125.341  1.00 99.99           C
ATOM    283  CG2 VAL A 396     125.703  89.314 126.638  1.00 99.99           C
ATOM    284  N   PRO A 397     122.040  91.598 128.132  1.00 85.50           N
ATOM    285  CA  PRO A 397     120.747  92.302 128.146  1.00 85.50           C
ATOM    286  C   PRO A 397     120.896  93.798 128.343  1.00 85.50           C
ATOM    287  O   PRO A 397     120.110  94.572 127.784  1.00 85.50           O
ATOM    288  CB  PRO A 397     119.992  91.612 129.283  1.00 85.50           C
ATOM    289  CG  PRO A 397     120.575  90.217 129.322  1.00 85.50           C
ATOM    290  CD  PRO A 397     122.052  90.460 129.061  1.00 85.50           C
ATOM    291  N   ARG A 398     121.889  94.232 129.123  1.00 87.95           N
ATOM    292  CA  ARG A 398     122.133  95.663 129.271  1.00 87.95           C
ATOM    293  C   ARG A 398     122.515  96.294 127.937  1.00 87.95           C
ATOM    294  O   ARG A 398     122.039  97.383 127.598  1.00 87.95           O
ATOM    295  CB  ARG A 398     123.229  95.915 130.308  1.00 87.95           C
ATOM    296  CG  ARG A 398     122.840  95.539 131.727  1.00 99.99           C
ATOM    297  CD  ARG A 398     123.972  95.815 132.704  1.00 99.99           C
ATOM    298  NE  ARG A 398     124.272  97.240 132.804  1.00 99.99           N
ATOM    299  CZ  ARG A 398     125.277  97.744 133.513  1.00 99.99           C
ATOM    300  NH1 ARG A 398     126.086  96.935 134.183  1.00 99.99           N
ATOM    301  NH2 ARG A 398     125.472  99.056 133.546  1.00 99.99           N
ATOM    302  N   PHE A 399     123.373  95.623 127.165  1.00 92.78           N
ATOM    303  CA  PHE A 399     123.754  96.142 125.855  1.00 92.78           C
ATOM    304  C   PHE A 399     122.553  96.191 124.917  1.00 92.78           C
ATOM    305  O   PHE A 399     122.386  97.146 124.149  1.00 92.78           O
ATOM    306  CB  PHE A 399     124.868  95.290 125.244  1.00 92.78           C
ATOM    307  CG  PHE A 399     125.367  95.800 123.923  1.00 99.99           C
ATOM    308  CD1 PHE A 399     126.270  96.848 123.866  1.00 99.99           C
ATOM    309  CD2 PHE A 399     124.935  95.235 122.737  1.00 99.99           C
ATOM    310  CE1 PHE A 399     126.729  97.320 122.651  1.00 99.99           C
ATOM    311  CE2 PHE A 399     125.392  95.704 121.520  1.00 99.99           C
ATOM    312  CZ  PHE A 399     126.291  96.746 121.477  1.00 99.99           C
ATOM    313  N   LEU A 400     121.709  95.157 124.958  1.00 91.73           N
ATOM    314  CA  LEU A 400     120.511  95.155 124.124  1.00 91.73           C
ATOM    315  C   LEU A 400     119.583  96.303 124.499  1.00 91.73           C
ATOM    316  O   LEU A 400     119.026  96.977 123.624  1.00 91.73           O
ATOM    317  CB  LEU A 400     119.775  93.819 124.246  1.00 91.73           C
ATOM    318  CG  LEU A 400     120.516  92.587 123.721  1.00 99.99           C
ATOM    319  CD1 LEU A 400     119.738  91.318 124.036  1.00 99.99           C
ATOM    320  CD2 LEU A 400     120.696  92.671 122.214  1.00 99.99           C
ATOM    321  N   MET A 401     119.407  96.541 125.800  1.00 89.27           N
ATOM    322  CA  MET A 401     118.579  97.656 126.246  1.00 89.27           C
ATOM    323  C   MET A 401     119.174  98.986 125.808  1.00 89.27           C
ATOM    324  O   MET A 401     118.443  99.903 125.420  1.00 89.27           O
ATOM    325  CB  MET A 401     118.413  97.626 127.766  1.00 89.27           C
ATOM    326  CG  MET A 401     117.504  98.714 128.313  1.00 99.99           C
ATOM    327  SD  MET A 401     115.796  98.535 127.765  1.00 99.99           S
ATOM    328  CE  MET A 401     115.032  99.939 128.572  1.00 99.99           C
ATOM    329  N   CYS A 402     120.501  99.116 125.871  1.00 93.01           N
ATOM    330  CA  CYS A 402     121.142 100.347 125.422  1.00 93.01           C
ATOM    331  C   CYS A 402     120.921 100.571 123.930  1.00 93.01           C
ATOM    332  O   CYS A 402     120.654 101.697 123.496  1.00 93.01           O
ATOM    333  CB  CYS A 402     122.639 100.316 125.733  1.00 93.01           C
ATOM    334  SG  CYS A 402     123.555  98.982 124.896  1.00 99.99           S
ATOM    335  N   ASN A 403     121.033  99.510 123.129  1.00 94.87           N
ATOM    336  CA  ASN A 403     120.788  99.636 121.695  1.00 94.87           C
ATOM    337  C   ASN A 403     119.340 100.029 121.421  1.00 94.87           C
ATOM    338  O   ASN A 403     119.062 100.877 120.563  1.00 94.87           O
ATOM    339  CB  ASN A 403     121.126  98.329 120.977  1.00 94.87           C
ATOM    340  CG  ASN A 403     122.615  98.048 120.946  1.00 99.99           C
ATOM    341  OD1 ASN A 403     123.078  97.039 121.476  1.00 99.99           O
ATOM    342  ND2 ASN A 403     123.372  98.943 120.322  1.00 99.99           N
ATOM    343  N   LEU A 404     118.401  99.413 122.143  1.00 92.46           N
ATOM    344  CA  LEU A 404     116.995  99.770 121.979  1.00 92.46           C
ATOM    345  C   LEU A 404     116.754 101.224 122.363  1.00 92.46           C
ATOM    346  O   LEU A 404     115.992 101.934 121.696  1.00 92.46           O
ATOM    347  CB  LEU A 404     116.107  98.847 122.815  1.00 92.46           C
ATOM    348  CG  LEU A 404     116.096  97.370 122.416  1.00 99.99           C
ATOM    349  CD1 LEU A 404     115.294  96.549 123.413  1.00 99.99           C
ATOM    350  CD2 LEU A 404     115.470  97.191 121.041  1.00 99.99           C
ATOM    351  N   ALA A 405     117.392 101.684 123.441  1.00 93.36           N
ATOM    352  CA  ALA A 405     117.248 103.075 123.854  1.00 93.36           C
ATOM    353  C   ALA A 405     117.823 104.019 122.807  1.00 93.36           C
ATOM    354  O   ALA A 405     117.261 105.088 122.551  1.00 93.36           O
ATOM    355  CB  ALA A 405     117.931 103.309 125.210  1.00 93.36           C
ATOM    356  N   PHE A 406     118.953 103.650 122.201  1.00 95.71           N
ATOM    357  CA  PHE A 406     119.521 104.475 121.139  1.00 95.71           C
ATOM    358  C   PHE A 406     118.582 104.552 119.941  1.00 95.71           C
ATOM    359  O   PHE A 406     118.390 105.628 119.359  1.00 95.71           O
ATOM    360  CB  PHE A 406     120.883 103.929 120.706  1.00 95.71           C
ATOM    361  CG  PHE A 406     121.567 104.764 119.664  1.00 99.99           C
ATOM    362  CD1 PHE A 406     122.250 105.916 120.016  1.00 99.99           C
ATOM    363  CD2 PHE A 406     121.531 104.401 118.330  1.00 99.99           C
ATOM    364  CE1 PHE A 406     122.880 106.686 119.057  1.00 99.99           C
ATOM    365  CE2 PHE A 406     122.159 105.169 117.368  1.00 99.99           C
ATOM    366  CZ  PHE A 406     122.835 106.311 117.732  1.00 99.99           C
ATOM    367  N   ALA A 407     117.990 103.420 119.555  1.00 95.31           N
ATOM    368  CA  ALA A 407     117.035 103.426 118.451  1.00 95.31           C
ATOM    369  C   ALA A 407     115.828 104.297 118.782  1.00 95.31           C
ATOM    370  O   ALA A 407     115.343 105.061 117.937  1.00 95.31           O
ATOM    371  CB  ALA A 407     116.584 101.996 118.119  1.00 95.31           C
ATOM    372  N   ASP A 408     115.326 104.190 120.014  1.00 93.03           N
ATOM    373  CA  ASP A 408     114.200 105.019 120.430  1.00 93.03           C
ATOM    374  C   ASP A 408     114.565 106.496 120.421  1.00 93.03           C
ATOM    375  O   ASP A 408     113.743 107.335 120.040  1.00 93.03           O
ATOM    376  CB  ASP A 408     113.717 104.608 121.822  1.00 93.03           C
ATOM    377  CG  ASP A 408     112.406 105.267 122.202  1.00 99.99           C
ATOM    378  OD1 ASP A 408     112.150 106.396 121.733  1.00 99.99           O
ATOM    379  OD2 ASP A 408     111.634 104.655 122.969  1.00 99.99           O
ATOM    380  N   LEU A 409     115.784 106.835 120.846  1.00 94.64           N
ATOM    381  CA  LEU A 409     116.223 108.225 120.812  1.00 94.64           C
ATOM    382  C   LEU A 409     116.302 108.739 119.382  1.00 94.64           C
ATOM    383  O   LEU A 409     115.924 109.882 119.104  1.00 94.64           O
ATOM    384  CB  LEU A 409     117.580 108.376 121.503  1.00 94.64           C
ATOM    385  CG  LEU A 409     117.613 108.081 123.004  1.00 99.99           C
ATOM    386  CD1 LEU A 409     119.040 108.126 123.528  1.00 99.99           C
ATOM    387  CD2 LEU A 409     116.793 109.106 123.770  1.00 99.99           C
ATOM    388  N   CYS A 410     116.799 107.913 118.459  1.00 95.83           N
ATOM    389  CA  CYS A 410     116.833 108.317 117.056  1.00 95.83           C
ATOM    390  C   CYS A 410     115.425 108.540 116.514  1.00 95.83           C
ATOM    391  O   CYS A 410     115.171 109.519 115.798  1.00 95.83           O
ATOM    392  CB  CYS A 410     117.562 107.268 116.214  1.00 95.83           C
ATOM    393  SG  CYS A 410     116.772 105.627 116.207  1.00 99.99           S
ATOM    394  N   ILE A 411     114.494 107.643 116.849  1.00 92.90           N
ATOM    395  CA  ILE A 411     113.114 107.803 116.400  1.00 92.90           C
ATOM    396  C   ILE A 411     112.515 109.082 116.972  1.00 92.90           C
ATOM    397  O   ILE A 411     111.810 109.824 116.276  1.00 92.90           O
ATOM    398  CB  ILE A 411     112.245 106.600 116.808  1.00 92.90           C
ATOM    399  CG1 ILE A 411     112.720 105.332 116.095  1.00 99.99           C
ATOM    400  CG2 ILE A 411     110.789 106.843 116.440  1.00 99.99           C
ATOM    401  CD1 ILE A 411     112.082 104.063 116.614  1.00 99.99           C
ATOM    402  N   GLY A 412     112.778 109.356 118.251  1.00 94.00           N
ATOM    403  CA  GLY A 412     112.270 110.574 118.859  1.00 94.00           C
ATOM    404  C   GLY A 412     112.861 111.824 118.237  1.00 94.00           C
ATOM    405  O   GLY A 412     112.174 112.835 118.084  1.00 94.00           O
ATOM    406  N   ILE A 413     114.145 111.776 117.879  1.00 94.76           N
ATOM    407  CA  ILE A 413     114.770 112.909 117.206  1.00 94.76           C
ATOM    408  C   ILE A 413     114.118 113.145 115.850  1.00 94.76           C
ATOM    409  O   ILE A 413     113.844 114.289 115.466  1.00 94.76           O
ATOM    410  CB  ILE A 413     116.283 112.690 117.020  1.00 94.76           C
ATOM    411  CG1 ILE A 413     116.985 112.634 118.378  1.00 99.99           C
ATOM    412  CG2 ILE A 413     116.890 113.825 116.209  1.00 99.99           C
ATOM    413  CD1 ILE A 413     118.427 112.186 118.302  1.00 99.99           C
ATOM    414  N   TYR A 414     113.864 112.069 115.102  1.00 94.56           N
ATOM    415  CA  TYR A 414     113.179 112.213 113.820  1.00 94.56           C
ATOM    416  C   TYR A 414     111.786 112.805 114.008  1.00 94.56           C
ATOM    417  O   TYR A 414     111.365 113.685 113.246  1.00 94.56           O
ATOM    418  CB  TYR A 414     113.088 110.863 113.106  1.00 94.56           C
ATOM    419  CG  TYR A 414     112.454 110.936 111.735  1.00 99.99           C
ATOM    420  CD1 TYR A 414     113.188 111.355 110.633  1.00 99.99           C
ATOM    421  CD2 TYR A 414     111.124 110.584 111.546  1.00 99.99           C
ATOM    422  CE1 TYR A 414     112.617 111.426 109.379  1.00 99.99           C
ATOM    423  CE2 TYR A 414     110.536 110.648 110.299  1.00 99.99           C
ATOM    424  CZ  TYR A 414     111.284 111.068 109.214  1.00 99.99           C
ATOM    425  OH  TYR A 414     110.709 111.135 107.967  1.00 99.99           O
ATOM    426  N   LEU A 415     111.056 112.332 115.021  1.00 93.80           N
ATOM    427  CA  LEU A 415     109.720 112.860 115.283  1.00 93.80           C
ATOM    428  C   LEU A 415     109.773 114.336 115.659  1.00 93.80           C
ATOM    429  O   LEU A 415     108.925 115.124 115.225  1.00 93.80           O
ATOM    430  CB  LEU A 415     109.035 112.060 116.393  1.00 93.80           C
ATOM    431  CG  LEU A 415     108.729 110.593 116.081  1.00 99.99           C
ATOM    432  CD1 LEU A 415     108.188 109.884 117.313  1.00 99.99           C
ATOM    433  CD2 LEU A 415     107.690 110.485 114.976  1.00 99.99           C
ATOM    434  N   LEU A 416     110.752 114.726 116.478  1.00 94.35           N
ATOM    435  CA  LEU A 416     110.895 116.128 116.851  1.00 94.35           C
ATOM    436  C   LEU A 416     111.215 116.988 115.637  1.00 94.35           C
ATOM    437  O   LEU A 416     110.690 118.099 115.497  1.00 94.35           O
ATOM    438  CB  LEU A 416     111.982 116.291 117.914  1.00 94.35           C
ATOM    439  CG  LEU A 416     111.707 115.640 119.272  1.00 99.99           C
ATOM    440  CD1 LEU A 416     112.923 115.753 120.178  1.00 99.99           C
ATOM    441  CD2 LEU A 416     110.535 116.317 119.964  1.00 99.99           C
ATOM    442  N   LEU A 417     112.080 116.495 114.749  1.00 95.01           N
ATOM    443  CA  LEU A 417     112.383 117.230 113.526  1.00 95.01           C
ATOM    444  C   LEU A 417     111.133 117.397 112.672  1.00 95.01           C
ATOM    445  O   LEU A 417     110.879 118.476 112.121  1.00 95.01           O
ATOM    446  CB  LEU A 417     113.479 116.518 112.731  1.00 95.01           C
ATOM    447  CG  LEU A 417     114.857 116.443 113.392  1.00 99.99           C
ATOM    448  CD1 LEU A 417     115.804 115.589 112.564  1.00 99.99           C
ATOM    449  CD2 LEU A 417     115.464 117.831 113.526  1.00 99.99           C
ATOM    450  N   ILE A 418     110.335 116.334 112.554  1.00 93.83           N
ATOM    451  CA  ILE A 418     109.104 116.414 111.770  1.00 93.83           C
ATOM    452  C   ILE A 418     108.147 117.427 112.385  1.00 93.83           C
ATOM    453  O   ILE A 418     107.520 118.224 111.676  1.00 93.83           O
ATOM    454  CB  ILE A 418     108.409 115.044 111.670  1.00 93.83           C
ATOM    455  CG1 ILE A 418     109.281 114.059 110.889  1.00 99.99           C
ATOM    456  CG2 ILE A 418     107.071 115.175 110.958  1.00 99.99           C
ATOM    457  CD1 ILE A 418     108.789 112.629 110.946  1.00 99.99           C
ATOM    458  N   ALA A 419     108.011 117.406 113.713  1.00 94.19           N
ATOM    459  CA  ALA A 419     107.125 118.353 114.383  1.00 94.19           C
ATOM    460  C   ALA A 419     107.597 119.786 114.180  1.00 94.19           C
ATOM    461  O   ALA A 419     106.785 120.689 113.945  1.00 94.19           O
ATOM    462  CB  ALA A 419     107.031 118.036 115.883  1.00 94.19           C
ATOM    463  N   SER A 420     108.908 120.018 114.276  1.00 95.27           N
ATOM    464  CA  SER A 420     109.442 121.358 114.056  1.00 95.27           C
ATOM    465  C   SER A 420     109.180 121.819 112.629  1.00 95.27           C
ATOM    466  O   SER A 420     108.809 122.975 112.393  1.00 95.27           O
ATOM    467  CB  SER A 420     110.941 121.394 114.358  1.00 95.27           C
ATOM    468  OG  SER A 420     111.656 120.528 113.493  1.00 99.99           O
ATOM    469  N   VAL A 421     109.369 120.923 111.657  1.00 95.13           N
ATOM    470  CA  VAL A 421     109.105 121.274 110.265  1.00 95.13           C
ATOM    471  C   VAL A 421     107.637 121.633 110.079  1.00 95.13           C
ATOM    472  O   VAL A 421     107.302 122.621 109.413  1.00 95.13           O
ATOM    473  CB  VAL A 421     109.479 120.124 109.313  1.00 95.13           C
ATOM    474  CG1 VAL A 421     109.082 120.463 107.884  1.00 99.99           C
ATOM    475  CG2 VAL A 421     110.979 119.870 109.347  1.00 99.99           C
ATOM    476  N   ASP A 422     106.737 120.838 110.663  1.00 93.87           N
ATOM    477  CA  ASP A 422     105.311 121.119 110.534  1.00 93.87           C
ATOM    478  C   ASP A 422     104.951 122.454 111.176  1.00 93.87           C
ATOM    479  O   ASP A 422     104.160 123.226 110.621  1.00 93.87           O
ATOM    480  CB  ASP A 422     104.484 119.995 111.161  1.00 93.87           C
ATOM    481  CG  ASP A 422     102.993 120.203 110.989  1.00 99.99           C
ATOM    482  OD1 ASP A 422     102.532 120.275 109.831  1.00 99.99           O
ATOM    483  OD2 ASP A 422     102.283 120.293 112.014  1.00 99.99           O
ATOM    484  N   ILE A 423     105.520 122.743 112.348  1.00 93.85           N
ATOM    485  CA  ILE A 423     105.194 123.981 113.047  1.00 93.85           C
ATOM    486  C   ILE A 423     105.723 125.186 112.280  1.00 93.85           C
ATOM    487  O   ILE A 423     105.068 126.234 112.215  1.00 93.85           O
ATOM    488  CB  ILE A 423     105.769 123.991 114.475  1.00 93.85           C
ATOM    489  CG1 ILE A 423     105.109 122.903 115.324  1.00 99.99           C
ATOM    490  CG2 ILE A 423     105.524 125.337 115.140  1.00 99.99           C
ATOM    491  CD1 ILE A 423     105.777 122.682 116.663  1.00 99.99           C
ATOM    492  N   HIS A 424     106.915 125.063 111.691  1.00 94.64           N
ATOM    493  CA  HIS A 424     107.502 126.191 110.975  1.00 94.64           C
ATOM    494  C   HIS A 424     106.633 126.611 109.796  1.00 94.64           C
ATOM    495  O   HIS A 424     106.439 127.808 109.553  1.00 94.64           O
ATOM    496  CB  HIS A 424     108.911 125.844 110.491  1.00 94.64           C
ATOM    497  CG  HIS A 424     109.891 125.609 111.598  1.00 99.99           C
ATOM    498  ND1 HIS A 424     110.001 124.401 112.250  1.00 99.99           N
ATOM    499  CD2 HIS A 424     110.803 126.430 112.170  1.00 99.99           C
ATOM    500  CE1 HIS A 424     110.942 124.488 113.175  1.00 99.99           C
ATOM    501  NE2 HIS A 424     111.444 125.707 113.147  1.00 99.99           N
ATOM    502  N   THR A 425     106.099 125.641 109.052  1.00 91.87           N
ATOM    503  CA  THR A 425     105.287 125.908 107.873  1.00 91.87           C
ATOM    504  C   THR A 425     103.793 125.800 108.157  1.00 91.87           C
ATOM    505  O   THR A 425     103.033 125.367 107.284  1.00 91.87           O
ATOM    506  CB  THR A 425     105.633 124.947 106.721  1.00 91.87           C
ATOM    507  OG1 THR A 425     104.897 125.318 105.547  1.00 99.99           O
ATOM    508  CG2 THR A 425     105.275 123.517 107.094  1.00 99.99           C
ATOM    509  N   LYS A 426     103.357 126.181 109.356  1.00 89.53           N
ATOM    510  CA  LYS A 426     101.943 126.106 109.698  1.00 89.53           C
ATOM    511  C   LYS A 426     101.134 127.073 108.844  1.00 89.53           C
ATOM    512  O   LYS A 426     101.434 128.269 108.782  1.00 89.53           O
ATOM    513  CB  LYS A 426     101.735 126.402 111.184  1.00 89.53           C
ATOM    514  CG  LYS A 426     102.417 125.414 112.116  1.00 99.99           C
ATOM    515  CD  LYS A 426     101.770 124.042 112.033  1.00 99.99           C
ATOM    516  CE  LYS A 426     102.453 123.052 112.964  1.00 99.99           C
ATOM    517  NZ  LYS A 426     103.863 122.793 112.562  1.00 99.99           N
ATOM    518  N   SER A 427     100.106 126.544 108.179  1.00 85.41           N
ATOM    519  CA  SER A 427      99.222 127.348 107.343  1.00 85.41           C
ATOM    520  C   SER A 427      99.910 127.789 106.056  1.00 85.41           C
ATOM    521  O   SER A 427      99.311 128.501 105.243  1.00 85.41           O
ATOM    522  CB  SER A 427      98.725 128.573 108.112  1.00 85.41           C
ATOM    523  OG  SER A 427      99.804 129.414 108.483  1.00 99.99           O
ATOM    524  N   GLN A 428     101.164 127.378 105.859  1.00 85.40           N
ATOM    525  CA  GLN A 428     101.935 127.733 104.676  1.00 85.40           C
ATOM    526  C   GLN A 428     102.750 126.562 104.139  1.00 85.40           C
ATOM    527  O   GLN A 428     103.746 126.776 103.440  1.00 85.40           O
ATOM    528  CB  GLN A 428     102.869 128.907 104.977  1.00 85.40           C
ATOM    529  CG  GLN A 428     104.022 128.560 105.905  1.00 99.99           C
ATOM    530  CD  GLN A 428     103.585 128.418 107.350  1.00 99.99           C
ATOM    531  OE1 GLN A 428     102.407 128.579 107.671  1.00 99.99           O
ATOM    532  NE2 GLN A 428     104.534 128.113 108.226  1.00 99.99           N
ATOM    533  N   TYR A 429     102.347 125.327 104.452  1.00 87.45           N
ATOM    534  CA  TYR A 429     103.108 124.167 104.001  1.00 87.45           C
ATOM    535  C   TYR A 429     103.161 124.083 102.482  1.00 87.45           C
ATOM    536  O   TYR A 429     104.149 123.594 101.923  1.00 87.45           O
ATOM    537  CB  TYR A 429     102.510 122.879 104.571  1.00 87.45           C
ATOM    538  CG  TYR A 429     102.603 122.774 106.077  1.00 99.99           C
ATOM    539  CD1 TYR A 429     103.751 122.281 106.686  1.00 99.99           C
ATOM    540  CD2 TYR A 429     101.545 123.167 106.884  1.00 99.99           C
ATOM    541  CE1 TYR A 429     103.844 122.182 108.059  1.00 99.99           C
ATOM    542  CE2 TYR A 429     101.620 123.075 108.261  1.00 99.99           C
ATOM    543  CZ  TYR A 429     102.771 122.583 108.846  1.00 99.99           C
ATOM    544  OH  TYR A 429     102.857 122.487 110.216  1.00 99.99           O
ATOM    545  N   HIS A 430     102.117 124.557 101.798  1.00 84.25           N
ATOM    546  CA  HIS A 430     102.078 124.452 100.342  1.00 84.25           C
ATOM    547  C   HIS A 430     103.240 125.199  99.702  1.00 84.25           C
ATOM    548  O   HIS A 430     103.867 124.701  98.760  1.00 84.25           O
ATOM    549  CB  HIS A 430     100.750 124.986  99.801  1.00 84.25           C
ATOM    550  CG  HIS A 430      99.559 124.183 100.223  1.00 99.99           C
ATOM    551  ND1 HIS A 430      98.938 124.356 101.440  1.00 99.99           N
ATOM    552  CD2 HIS A 430      98.876 123.200  99.589  1.00 99.99           C
ATOM    553  CE1 HIS A 430      97.923 123.514 101.536  1.00 99.99           C
ATOM    554  NE2 HIS A 430      97.863 122.803 100.427  1.00 99.99           N
ATOM    555  N   ASN A 431     103.542 126.401 100.199  1.00 84.75           N
ATOM    556  CA  ASN A 431     104.652 127.168  99.643  1.00 84.75           C
ATOM    557  C   ASN A 431     105.978 126.441  99.838  1.00 84.75           C
ATOM    558  O   ASN A 431     106.813 126.408  98.926  1.00 84.75           O
ATOM    559  CB  ASN A 431     104.716 128.557 100.280  1.00 84.75           C
ATOM    560  CG  ASN A 431     104.962 128.502 101.774  1.00 99.99           C
ATOM    561  OD1 ASN A 431     104.890 127.437 102.387  1.00 99.99           O
ATOM    562  ND2 ASN A 431     105.256 129.652 102.368  1.00 99.99           N
ATOM    563  N   TYR A 432     106.188 125.853 101.016  1.00 90.15           N
ATOM    564  CA  TYR A 432     107.431 125.155 101.318  1.00 90.15           C
ATOM    565  C   TYR A 432     107.344 123.651 101.099  1.00 90.15           C
ATOM    566  O   TYR A 432     108.307 122.940 101.409  1.00 90.15           O
ATOM    567  CB  TYR A 432     107.860 125.424 102.762  1.00 90.15           C
ATOM    568  CG  TYR A 432     106.871 124.932 103.796  1.00 99.99           C
ATOM    569  CD1 TYR A 432     106.963 123.647 104.314  1.00 99.99           C
ATOM    570  CD2 TYR A 432     105.850 125.756 104.251  1.00 99.99           C
ATOM    571  CE1 TYR A 432     106.066 123.190 105.257  1.00 99.99           C
ATOM    572  CE2 TYR A 432     104.942 125.317 105.195  1.00 99.99           C
ATOM    573  CZ  TYR A 432     105.052 124.032 105.698  1.00 99.99           C
ATOM    574  OH  TYR A 432     104.153 123.586 106.637  1.00 99.99           O
ATOM    575  N   ALA A 433     106.221 123.150 100.580  1.00 90.47           N
ATOM    576  CA  ALA A 433     106.080 121.712 100.375  1.00 90.47           C
ATOM    577  C   ALA A 433     107.116 121.195  99.385  1.00 90.47           C
ATOM    578  O   ALA A 433     107.736 120.148  99.605  1.00 90.47           O
ATOM    579  CB  ALA A 433     104.665 121.373  99.885  1.00 90.47           C
ATOM    580  N   ILE A 434     107.315 121.918  98.280  1.00 90.95           N
ATOM    581  CA  ILE A 434     108.276 121.479  97.272  1.00 90.95           C
ATOM    582  C   ILE A 434     109.683 121.457  97.853  1.00 90.95           C
ATOM    583  O   ILE A 434     110.439 120.498  97.653  1.00 90.95           O
ATOM    584  CB  ILE A 434     108.246 122.389  96.030  1.00 90.95           C
ATOM    585  CG1 ILE A 434     106.894 122.282  95.322  1.00 99.99           C
ATOM    586  CG2 ILE A 434     109.338 121.988  95.049  1.00 99.99           C
ATOM    587  CD1 ILE A 434     106.689 123.314  94.236  1.00 99.99           C
ATOM    588  N   ASP A 435     110.059 122.511  98.581  1.00 91.98           N
ATOM    589  CA  ASP A 435     111.395 122.564  99.165  1.00 91.98           C
ATOM    590  C   ASP A 435     111.597 121.448 100.182  1.00 91.98           C
ATOM    591  O   ASP A 435     112.656 120.809 100.211  1.00 91.98           O
ATOM    592  CB  ASP A 435     111.639 123.924  99.822  1.00 91.98           C
ATOM    593  CG  ASP A 435     113.042 124.057 100.381  1.00 99.99           C
ATOM    594  OD1 ASP A 435     114.008 123.949  99.598  1.00 99.99           O
ATOM    595  OD2 ASP A 435     113.175 124.271 101.606  1.00 99.99           O
ATOM    596  N   TRP A 436     110.595 121.198 101.025  1.00 93.61           N
ATOM    597  CA  TRP A 436     110.728 120.173 102.055  1.00 93.61           C
ATOM    598  C   TRP A 436     110.827 118.784 101.437  1.00 93.61           C
ATOM    599  O   TRP A 436     111.719 117.999 101.780  1.00 93.61           O
ATOM    600  CB  TRP A 436     109.549 120.234 103.028  1.00 93.61           C
ATOM    601  CG  TRP A 436     109.493 121.502 103.824  1.00 99.99           C
ATOM    602  CD1 TRP A 436     108.771 122.622 103.531  1.00 99.99           C
ATOM    603  CD2 TRP A 436     110.190 121.776 105.046  1.00 99.99           C
ATOM    604  NE1 TRP A 436     108.974 123.582 104.494  1.00 99.99           N
ATOM    605  CE2 TRP A 436     109.842 123.085 105.437  1.00 99.99           C
ATOM    606  CE3 TRP A 436     111.071 121.043 105.845  1.00 99.99           C
ATOM    607  CZ2 TRP A 436     110.345 123.678 106.593  1.00 99.99           C
ATOM    608  CZ3 TRP A 436     111.571 121.633 106.992  1.00 99.99           C
ATOM    609  CH2 TRP A 436     111.208 122.939 107.359  1.00 99.99           C
ATOM    610  N   GLN A 437     109.913 118.459 100.519  1.00 92.36           N
ATOM    611  CA  GLN A 437     109.929 117.136  99.904  1.00 92.36           C
ATOM    612  C   GLN A 437     111.195 116.920  99.085  1.00 92.36           C
ATOM    613  O   GLN A 437     111.825 115.859  99.175  1.00 92.36           O
ATOM    614  CB  GLN A 437     108.695 116.940  99.022  1.00 92.36           C
ATOM    615  CG  GLN A 437     107.381 116.934  99.785  1.00 99.99           C
ATOM    616  CD  GLN A 437     107.263 115.758 100.733  1.00 99.99           C
ATOM    617  OE1 GLN A 437     107.661 114.641 100.404  1.00 99.99           O
ATOM    618  NE2 GLN A 437     106.716 116.007 101.918  1.00 99.99           N
ATOM    619  N   THR A 438     111.585 117.911  98.282  1.00 91.38           N
ATOM    620  CA  THR A 438     112.786 117.793  97.464  1.00 91.38           C
ATOM    621  C   THR A 438     114.057 118.124  98.234  1.00 91.38           C
ATOM    622  O   THR A 438     115.153 117.809  97.757  1.00 91.38           O
ATOM    623  CB  THR A 438     112.719 118.709  96.228  1.00 91.38           C
ATOM    624  OG1 THR A 438     112.636 120.077  96.647  1.00 99.99           O
ATOM    625  CG2 THR A 438     111.497 118.377  95.385  1.00 99.99           C
ATOM    626  N   GLY A 439     113.939 118.746  99.402  1.00 92.63           N
ATOM    627  CA  GLY A 439     115.107 119.105 100.176  1.00 92.63           C
ATOM    628  C   GLY A 439     115.754 117.903 100.837  1.00 92.63           C
ATOM    629  O   GLY A 439     115.179 116.820 100.957  1.00 92.63           O
ATOM    630  N   ALA A 440     116.997 118.111 101.278  1.00 93.92           N
ATOM    631  CA  ALA A 440     117.726 117.045 101.955  1.00 93.92           C
ATOM    632  C   ALA A 440     117.105 116.708 103.304  1.00 93.92           C
ATOM    633  O   ALA A 440     117.344 115.621 103.842  1.00 93.92           O
ATOM    634  CB  ALA A 440     119.200 117.434 102.143  1.00 93.92           C
ATOM    635  N   GLY A 441     116.312 117.623 103.867  1.00 94.55           N
ATOM    636  CA  GLY A 441     115.721 117.369 105.171  1.00 94.55           C
ATOM    637  C   GLY A 441     114.781 116.179 105.168  1.00 94.55           C
ATOM    638  O   GLY A 441     114.815 115.347 106.078  1.00 94.55           O
ATOM    639  N   CYS A 442     113.923 116.085 104.149  1.00 95.55           N
ATOM    640  CA  CYS A 442     113.002 114.957 104.066  1.00 95.55           C
ATOM    641  C   CYS A 442     113.744 113.636 103.907  1.00 95.55           C
ATOM    642  O   CYS A 442     113.389 112.644 104.554  1.00 95.55           O
ATOM    643  CB  CYS A 442     112.025 115.147 102.905  1.00 95.55           C
ATOM    644  SG  CYS A 442     110.767 113.837 102.755  1.00 99.99           S
ATOM    645  N   ASP A 443     114.770 113.602 103.053  1.00 95.99           N
ATOM    646  CA  ASP A 443     115.546 112.379 102.885  1.00 95.99           C
ATOM    647  C   ASP A 443     116.242 111.991 104.182  1.00 95.99           C
ATOM    648  O   ASP A 443     116.270 110.812 104.552  1.00 95.99           O
ATOM    649  CB  ASP A 443     116.573 112.546 101.764  1.00 95.99           C
ATOM    650  CG  ASP A 443     117.359 111.277 101.499  1.00 99.99           C
ATOM    651  OD1 ASP A 443     116.734 110.252 101.154  1.00 99.99           O
ATOM    652  OD2 ASP A 443     118.601 111.307 101.636  1.00 99.99           O
ATOM    653  N   ALA A 444     116.810 112.972 104.886  1.00 96.21           N
ATOM    654  CA  ALA A 444     117.472 112.684 106.154  1.00 96.21           C
ATOM    655  C   ALA A 444     116.481 112.137 107.173  1.00 96.21           C
ATOM    656  O   ALA A 444     116.778 111.174 107.888  1.00 96.21           O
ATOM    657  CB  ALA A 444     118.158 113.944 106.703  1.00 96.21           C
ATOM    658  N   ALA A 445     115.293 112.740 107.251  1.00 95.97           N
ATOM    659  CA  ALA A 445     114.286 112.269 108.195  1.00 95.97           C
ATOM    660  C   ALA A 445     113.852 110.847 107.866  1.00 95.97           C
ATOM    661  O   ALA A 445     113.721 110.001 108.760  1.00 95.97           O
ATOM    662  CB  ALA A 445     113.070 113.207 108.200  1.00 95.97           C
ATOM    663  N   GLY A 446     113.621 110.564 106.583  1.00 95.64           N
ATOM    664  CA  GLY A 446     113.232 109.218 106.196  1.00 95.64           C
ATOM    665  C   GLY A 446     114.309 108.196 106.502  1.00 95.64           C
ATOM    666  O   GLY A 446     114.021 107.109 107.013  1.00 95.64           O
ATOM    667  N   PHE A 447     115.565 108.530 106.199  1.00 97.31           N
ATOM    668  CA  PHE A 447     116.665 107.618 106.489  1.00 97.31           C
ATOM    669  C   PHE A 447     116.785 107.374 107.986  1.00 97.31           C
ATOM    670  O   PHE A 447     116.994 106.238 108.427  1.00 97.31           O
ATOM    671  CB  PHE A 447     117.979 108.170 105.934  1.00 97.31           C
ATOM    672  CG  PHE A 447     119.152 107.254 106.130  1.00 99.99           C
ATOM    673  CD1 PHE A 447     119.359 106.178 105.282  1.00 99.99           C
ATOM    674  CD2 PHE A 447     120.051 107.464 107.160  1.00 99.99           C
ATOM    675  CE1 PHE A 447     120.438 105.334 105.462  1.00 99.99           C
ATOM    676  CE2 PHE A 447     121.131 106.622 107.343  1.00 99.99           C
ATOM    677  CZ  PHE A 447     121.325 105.556 106.493  1.00 99.99           C
ATOM    678  N   PHE A 448     116.657 108.433 108.789  1.00 95.61           N
ATOM    679  CA  PHE A 448     116.741 108.277 110.236  1.00 95.61           C
ATOM    680  C   PHE A 448     115.616 107.394 110.760  1.00 95.61           C
ATOM    681  O   PHE A 448     115.849 106.521 111.603  1.00 95.61           O
ATOM    682  CB  PHE A 448     116.703 109.642 110.925  1.00 95.61           C
ATOM    683  CG  PHE A 448     116.857 109.572 112.417  1.00 99.99           C
ATOM    684  CD1 PHE A 448     118.107 109.424 112.994  1.00 99.99           C
ATOM    685  CD2 PHE A 448     115.753 109.655 113.247  1.00 99.99           C
ATOM    686  CE1 PHE A 448     118.249 109.359 114.367  1.00 99.99           C
ATOM    687  CE2 PHE A 448     115.891 109.589 114.620  1.00 99.99           C
ATOM    688  CZ  PHE A 448     117.140 109.443 115.180  1.00 99.99           C
ATOM    689  N   THR A 449     114.391 107.605 110.274  1.00 92.97           N
ATOM    690  CA  THR A 449     113.269 106.787 110.724  1.00 92.97           C
ATOM    691  C   THR A 449     113.473 105.325 110.344  1.00 92.97           C
ATOM    692  O   THR A 449     113.241 104.420 111.156  1.00 92.97           O
ATOM    693  CB  THR A 449     111.937 107.283 110.133  1.00 92.97           C
ATOM    694  OG1 THR A 449     111.977 107.181 108.704  1.00 99.99           O
ATOM    695  CG2 THR A 449     111.691 108.735 110.516  1.00 99.99           C
ATOM    696  N   VAL A 450     113.912 105.076 109.109  1.00 94.70           N
ATOM    697  CA  VAL A 450     114.129 103.704 108.662  1.00 94.70           C
ATOM    698  C   VAL A 450     115.219 103.041 109.495  1.00 94.70           C
ATOM    699  O   VAL A 450     115.085 101.887 109.919  1.00 94.70           O
ATOM    700  CB  VAL A 450     114.515 103.650 107.172  1.00 94.70           C
ATOM    701  CG1 VAL A 450     114.855 102.226 106.760  1.00 99.99           C
ATOM    702  CG2 VAL A 450     113.363 104.139 106.306  1.00 99.99           C
ATOM    703  N   PHE A 451     116.319 103.759 109.735  1.00 97.08           N
ATOM    704  CA  PHE A 451     117.413 103.200 110.520  1.00 97.08           C
ATOM    705  C   PHE A 451     116.964 102.900 111.944  1.00 97.08           C
ATOM    706  O   PHE A 451     117.299 101.851 112.504  1.00 97.08           O
ATOM    707  CB  PHE A 451     118.607 104.156 110.532  1.00 97.08           C
ATOM    708  CG  PHE A 451     119.804 103.621 111.263  1.00 99.99           C
ATOM    709  CD1 PHE A 451     120.659 102.717 110.654  1.00 99.99           C
ATOM    710  CD2 PHE A 451     120.080 104.020 112.558  1.00 99.99           C
ATOM    711  CE1 PHE A 451     121.761 102.224 111.326  1.00 99.99           C
ATOM    712  CE2 PHE A 451     121.180 103.528 113.234  1.00 99.99           C
ATOM    713  CZ  PHE A 451     122.022 102.630 112.617  1.00 99.99           C
ATOM    714  N   ALA A 452     116.203 103.815 112.550  1.00 95.20           N
ATOM    715  CA  ALA A 452     115.724 103.589 113.909  1.00 95.20           C
ATOM    716  C   ALA A 452     114.809 102.374 113.974  1.00 95.20           C
ATOM    717  O   ALA A 452     114.941 101.539 114.877  1.00 95.20           O
ATOM    718  CB  ALA A 452     114.991 104.831 114.437  1.00 95.20           C
ATOM    719  N   SER A 453     113.878 102.252 113.023  1.00 91.33           N
ATOM    720  CA  SER A 453     112.984 101.100 113.019  1.00 91.33           C
ATOM    721  C   SER A 453     113.751  99.798 112.826  1.00 91.33           C
ATOM    722  O   SER A 453     113.490  98.815 113.532  1.00 91.33           O
ATOM    723  CB  SER A 453     111.924 101.248 111.926  1.00 91.33           C
ATOM    724  OG  SER A 453     112.520 101.300 110.642  1.00 99.99           O
ATOM    725  N   GLU A 454     114.700  99.772 111.886  1.00 93.81           N
ATOM    726  CA  GLU A 454     115.476  98.559 111.657  1.00 93.81           C
ATOM    727  C   GLU A 454     116.300  98.191 112.884  1.00 93.81           C
ATOM    728  O   GLU A 454     116.369  97.016 113.262  1.00 93.81           O
ATOM    729  CB  GLU A 454     116.390  98.729 110.442  1.00 93.81           C
ATOM    730  CG  GLU A 454     117.424  99.834 110.592  1.00 99.99           C
ATOM    731  CD  GLU A 454     118.310  99.972 109.371  1.00 99.99           C
ATOM    732  OE1 GLU A 454     119.000  98.991 109.023  1.00 99.99           O
ATOM    733  OE2 GLU A 454     118.314 101.061 108.759  1.00 99.99           O
ATOM    734  N   LEU A 455     116.934  99.180 113.518  1.00 95.41           N
ATOM    735  CA  LEU A 455     117.735  98.908 114.706  1.00 95.41           C
ATOM    736  C   LEU A 455     116.866  98.377 115.837  1.00 95.41           C
ATOM    737  O   LEU A 455     117.246  97.429 116.532  1.00 95.41           O
ATOM    738  CB  LEU A 455     118.475 100.170 115.154  1.00 95.41           C
ATOM    739  CG  LEU A 455     119.532 100.714 114.190  1.00 99.99           C
ATOM    740  CD1 LEU A 455     120.080 102.042 114.689  1.00 99.99           C
ATOM    741  CD2 LEU A 455     120.692  99.740 114.060  1.00 99.99           C
ATOM    742  N   SER A 456     115.691  98.979 116.040  1.00 92.01           N
ATOM    743  CA  SER A 456     114.799  98.507 117.092  1.00 92.01           C
ATOM    744  C   SER A 456     114.347  97.077 116.826  1.00 92.01           C
ATOM    745  O   SER A 456     114.337  96.240 117.737  1.00 92.01           O
ATOM    746  CB  SER A 456     113.585  99.429 117.219  1.00 92.01           C
ATOM    747  OG  SER A 456     113.970 100.723 117.649  1.00 99.99           O
ATOM    748  N   VAL A 457     113.975  96.775 115.580  1.00 90.95           N
ATOM    749  CA  VAL A 457     113.531  95.425 115.251  1.00 90.95           C
ATOM    750  C   VAL A 457     114.659  94.425 115.469  1.00 90.95           C
ATOM    751  O   VAL A 457     114.452  93.350 116.047  1.00 90.95           O
ATOM    752  CB  VAL A 457     113.037  95.333 113.796  1.00 90.95           C
ATOM    753  CG1 VAL A 457     112.696  93.894 113.438  1.00 99.99           C
ATOM    754  CG2 VAL A 457     111.791  96.184 113.601  1.00 99.99           C
ATOM    755  N   TYR A 458     115.869  94.758 115.012  1.00 94.10           N
ATOM    756  CA  TYR A 458     116.998  93.848 115.172  1.00 94.10           C
ATOM    757  C   TYR A 458     117.317  93.625 116.645  1.00 94.10           C
ATOM    758  O   TYR A 458     117.582  92.495 117.069  1.00 94.10           O
ATOM    759  CB  TYR A 458     118.229  94.387 114.441  1.00 94.10           C
ATOM    760  CG  TYR A 458     119.427  93.466 114.497  1.00 99.99           C
ATOM    761  CD1 TYR A 458     119.525  92.373 113.646  1.00 99.99           C
ATOM    762  CD2 TYR A 458     120.458  93.693 115.400  1.00 99.99           C
ATOM    763  CE1 TYR A 458     120.615  91.527 113.691  1.00 99.99           C
ATOM    764  CE2 TYR A 458     121.556  92.859 115.459  1.00 99.99           C
ATOM    765  CZ  TYR A 458     121.634  91.775 114.603  1.00 99.99           C
ATOM    766  OH  TYR A 458     122.723  90.938 114.653  1.00 99.99           O
ATOM    767  N   THR A 459     117.301  94.696 117.442  1.00 93.04           N
ATOM    768  CA  THR A 459     117.592  94.559 118.865  1.00 93.04           C
ATOM    769  C   THR A 459     116.543  93.700 119.558  1.00 93.04           C
ATOM    770  O   THR A 459     116.880  92.837 120.378  1.00 93.04           O
ATOM    771  CB  THR A 459     117.662  95.931 119.561  1.00 93.04           C
ATOM    772  OG1 THR A 459     116.392  96.587 119.459  1.00 99.99           O
ATOM    773  CG2 THR A 459     118.722  96.805 118.909  1.00 99.99           C
ATOM    774  N   LEU A 460     115.264  93.919 119.242  1.00 88.94           N
ATOM    775  CA  LEU A 460     114.213  93.109 119.848  1.00 88.94           C
ATOM    776  C   LEU A 460     114.360  91.643 119.461  1.00 88.94           C
ATOM    777  O   LEU A 460     114.226  90.752 120.308  1.00 88.94           O
ATOM    778  CB  LEU A 460     112.833  93.627 119.438  1.00 88.94           C
ATOM    779  CG  LEU A 460     112.462  95.028 119.929  1.00 99.99           C
ATOM    780  CD1 LEU A 460     111.136  95.473 119.332  1.00 99.99           C
ATOM    781  CD2 LEU A 460     112.330  95.048 121.444  1.00 99.99           C
ATOM    782  N   THR A 461     114.644  91.373 118.184  1.00 91.25           N
ATOM    783  CA  THR A 461     114.814  89.993 117.744  1.00 91.25           C
ATOM    784  C   THR A 461     116.000  89.337 118.438  1.00 91.25           C
ATOM    785  O   THR A 461     115.915  88.182 118.872  1.00 91.25           O
ATOM    786  CB  THR A 461     115.011  89.907 116.219  1.00 91.25           C
ATOM    787  OG1 THR A 461     116.204  90.610 115.849  1.00 99.99           O
ATOM    788  CG2 THR A 461     113.828  90.529 115.493  1.00 99.99           C
ATOM    789  N   ALA A 462     117.118  90.058 118.552  1.00 92.90           N
ATOM    790  CA  ALA A 462     118.296  89.501 119.207  1.00 92.90           C
ATOM    791  C   ALA A 462     118.019  89.218 120.678  1.00 92.90           C
ATOM    792  O   ALA A 462     118.418  88.175 121.208  1.00 92.90           O
ATOM    793  CB  ALA A 462     119.493  90.453 119.066  1.00 92.90           C
ATOM    794  N   ILE A 463     117.333  90.142 121.356  1.00 86.96           N
ATOM    795  CA  ILE A 463     117.018  89.943 122.769  1.00 86.96           C
ATOM    796  C   ILE A 463     116.113  88.730 122.940  1.00 86.96           C
ATOM    797  O   ILE A 463     116.310  87.905 123.840  1.00 86.96           O
ATOM    798  CB  ILE A 463     116.340  91.185 123.376  1.00 86.96           C
ATOM    799  CG1 ILE A 463     117.304  92.373 123.377  1.00 99.99           C
ATOM    800  CG2 ILE A 463     115.911  90.911 124.810  1.00 99.99           C
ATOM    801  CD1 ILE A 463     116.651  93.690 123.732  1.00 99.99           C
ATOM    802  N   THR A 464     115.103  88.607 122.076  1.00 85.36           N
ATOM    803  CA  THR A 464     114.193  87.470 122.162  1.00 85.36           C
ATOM    804  C   THR A 464     114.933  86.160 121.924  1.00 85.36           C
ATOM    805  O   THR A 464     114.714  85.171 122.633  1.00 85.36           O
ATOM    806  CB  THR A 464     113.040  87.592 121.149  1.00 85.36           C
ATOM    807  OG1 THR A 464     113.570  87.599 119.817  1.00 99.99           O
ATOM    808  CG2 THR A 464     112.265  88.881 121.376  1.00 99.99           C
ATOM    809  N   LEU A 465     115.816  86.134 120.923  1.00 90.27           N
ATOM    810  CA  LEU A 465     116.575  84.920 120.640  1.00 90.27           C
ATOM    811  C   LEU A 465     117.478  84.553 121.810  1.00 90.27           C
ATOM    812  O   LEU A 465     117.576  83.377 122.183  1.00 90.27           O
ATOM    813  CB  LEU A 465     117.405  85.092 119.367  1.00 90.27           C
ATOM    814  CG  LEU A 465     116.621  85.273 118.065  1.00 99.99           C
ATOM    815  CD1 LEU A 465     117.562  85.577 116.909  1.00 99.99           C
ATOM    816  CD2 LEU A 465     115.846  84.010 117.726  1.00 99.99           C
ATOM    817  N   GLU A 466     118.148  85.544 122.400  1.00 87.96           N
ATOM    818  CA  GLU A 466     119.020  85.272 123.538  1.00 87.96           C
ATOM    819  C   GLU A 466     118.221  84.737 124.720  1.00 87.96           C
ATOM    820  O   GLU A 466     118.642  83.787 125.390  1.00 87.96           O
ATOM    821  CB  GLU A 466     119.783  86.535 123.942  1.00 87.96           C
ATOM    822  CG  GLU A 466     118.892  87.681 124.395  1.00 99.99           C
ATOM    823  CD  GLU A 466     119.682  88.912 124.788  1.00 99.99           C
ATOM    824  OE1 GLU A 466     120.508  88.817 125.720  1.00 99.99           O
ATOM    825  OE2 GLU A 466     119.477  89.975 124.163  1.00 99.99           O
ATOM    826  N   ARG A 467     117.061  85.339 124.993  1.00 83.58           N
ATOM    827  CA  ARG A 467     116.229  84.872 126.097  1.00 83.58           C
ATOM    828  C   ARG A 467     115.753  83.445 125.855  1.00 83.58           C
ATOM    829  O   ARG A 467     115.762  82.609 126.767  1.00 83.58           O
ATOM    830  CB  ARG A 467     115.031  85.803 126.297  1.00 83.58           C
ATOM    831  CG  ARG A 467     114.147  85.432 127.475  1.00 99.99           C
ATOM    832  CD  ARG A 467     112.980  86.396 127.614  1.00 99.99           C
ATOM    833  NE  ARG A 467     112.119  86.053 128.743  1.00 99.99           N
ATOM    834  CZ  ARG A 467     112.339  86.441 129.995  1.00 99.99           C
ATOM    835  NH1 ARG A 467     113.396  87.187 130.281  1.00 99.99           N
ATOM    836  NH2 ARG A 467     111.501  86.081 130.957  1.00 99.99           N
ATOM    837  N   TRP A 468     115.329  83.147 124.624  1.00 84.17           N
ATOM    838  CA  TRP A 468     114.874  81.798 124.306  1.00 84.17           C
ATOM    839  C   TRP A 468     116.003  80.789 124.463  1.00 84.17           C
ATOM    840  O   TRP A 468     115.799  79.695 125.002  1.00 84.17           O
ATOM    841  CB  TRP A 468     114.311  81.743 122.885  1.00 84.17           C
ATOM    842  CG  TRP A 468     115.318  82.079 121.828  1.00 99.99           C
ATOM    843  CD1 TRP A 468     115.593  83.315 121.319  1.00 99.99           C
ATOM    844  CD2 TRP A 468     116.187  81.161 121.150  1.00 99.99           C
ATOM    845  NE1 TRP A 468     116.577  83.228 120.366  1.00 99.99           N
ATOM    846  CE2 TRP A 468     116.960  81.914 120.244  1.00 99.99           C
ATOM    847  CE3 TRP A 468     116.384  79.780 121.224  1.00 99.99           C
ATOM    848  CZ2 TRP A 468     117.917  81.331 119.415  1.00 99.99           C
ATOM    849  CZ3 TRP A 468     117.333  79.203 120.402  1.00 99.99           C
ATOM    850  CH2 TRP A 468     118.091  79.976 119.506  1.00 99.99           C
ATOM    851  N   HIS A 469     117.204  81.136 123.994  1.00 85.52           N
ATOM    852  CA  HIS A 469     118.340  80.234 124.145  1.00 85.52           C
ATOM    853  C   HIS A 469     118.675  80.013 125.615  1.00 85.52           C
ATOM    854  O   HIS A 469     118.968  78.885 126.028  1.00 85.52           O
ATOM    855  CB  HIS A 469     119.561  80.781 123.403  1.00 85.52           C
ATOM    856  CG  HIS A 469     120.753  79.876 123.450  1.00 99.99           C
ATOM    857  ND1 HIS A 469     122.026  80.306 123.154  1.00 99.99           N
ATOM    858  CD2 HIS A 469     120.862  78.562 123.757  1.00 99.99           C
ATOM    859  CE1 HIS A 469     122.870  79.296 123.279  1.00 99.99           C
ATOM    860  NE2 HIS A 469     122.190  78.227 123.644  1.00 99.99           N
ATOM    861  N   THR A 470     118.637  81.077 126.419  1.00 80.54           N
ATOM    862  CA  THR A 470     118.946  80.941 127.838  1.00 80.54           C
ATOM    863  C   THR A 470     117.913  80.076 128.550  1.00 80.54           C
ATOM    864  O   THR A 470     118.264  79.276 129.426  1.00 80.54           O
ATOM    865  CB  THR A 470     119.017  82.313 128.534  1.00 80.54           C
ATOM    866  OG1 THR A 470     117.742  82.962 128.448  1.00 99.99           O
ATOM    867  CG2 THR A 470     120.064  83.194 127.869  1.00 99.99           C
ATOM    868  N   ILE A 471     116.636  80.220 128.191  1.00 76.02           N
ATOM    869  CA  ILE A 471     115.589  79.501 128.909  1.00 76.02           C
ATOM    870  C   ILE A 471     115.489  78.050 128.450  1.00 76.02           C
ATOM    871  O   ILE A 471     115.563  77.131 129.274  1.00 76.02           O
ATOM    872  CB  ILE A 471     114.217  80.176 128.730  1.00 76.02           C
ATOM    873  CG1 ILE A 471     114.218  81.565 129.372  1.00 99.99           C
ATOM    874  CG2 ILE A 471     113.124  79.343 129.383  1.00 99.99           C
ATOM    875  CD1 ILE A 471     112.996  82.393 129.040  1.00 99.99           C
ATOM    876  N   THR A 472     115.324  77.812 127.147  1.00 77.81           N
ATOM    877  CA  THR A 472     115.162  76.448 126.655  1.00 77.81           C
ATOM    878  C   THR A 472     116.456  75.650 126.740  1.00 77.81           C
ATOM    879  O   THR A 472     116.420  74.415 126.704  1.00 77.81           O
ATOM    880  CB  THR A 472     114.669  76.429 125.197  1.00 77.81           C
ATOM    881  OG1 THR A 472     115.640  77.061 124.353  1.00 99.99           O
ATOM    882  CG2 THR A 472     113.349  77.174 125.071  1.00 99.99           C
ATOM    883  N   HIS A 473     117.597  76.329 126.855  1.00 77.17           N
ATOM    884  CA  HIS A 473     118.892  75.665 126.934  1.00 77.17           C
ATOM    885  C   HIS A 473     119.549  75.949 128.278  1.00 77.17           C
ATOM    886  O   HIS A 473     120.738  76.279 128.336  1.00 77.17           O
ATOM    887  CB  HIS A 473     119.797  76.116 125.786  1.00 77.17           C
ATOM    888  CG  HIS A 473     120.108  77.581 125.802  1.00 99.99           C
ATOM    889  ND1 HIS A 473     121.041  78.135 126.649  1.00 99.99           N
ATOM    890  CD2 HIS A 473     119.608  78.607 125.073  1.00 99.99           C
ATOM    891  CE1 HIS A 473     121.101  79.438 126.441  1.00 99.99           C
ATOM    892  NE2 HIS A 473     120.243  79.750 125.490  1.00 99.99           N
ATOM    893  N   ALA A 474     118.781  75.827 129.362  1.00 70.16           N
ATOM    894  CA  ALA A 474     119.263  76.146 130.701  1.00 70.16           C
ATOM    895  C   ALA A 474     120.613  75.516 131.023  1.00 70.16           C
ATOM    896  O   ALA A 474     121.289  75.996 131.940  1.00 70.16           O
ATOM    897  CB  ALA A 474     118.243  75.706 131.761  1.00 70.16           C
ATOM    898  N   MET A 475     121.022  74.464 130.312  1.00 60.87           N
ATOM    899  CA  MET A 475     122.356  73.906 130.481  1.00 60.87           C
ATOM    900  C   MET A 475     123.453  74.892 130.108  1.00 60.87           C
ATOM    901  O   MET A 475     124.471  74.960 130.806  1.00 60.87           O
ATOM    902  CB  MET A 475     122.514  72.633 129.648  1.00 60.87           C
ATOM    903  CG  MET A 475     121.618  71.487 130.089  1.00 99.99           C
ATOM    904  SD  MET A 475     122.017  70.886 131.740  1.00 99.99           S
ATOM    905  CE  MET A 475     123.596  70.097 131.439  1.00 99.99           C
ATOM    906  N   GLN A 476     123.270  75.651 129.029  1.00 62.26           N
ATOM    907  CA  GLN A 476     124.197  76.708 128.637  1.00 62.26           C
ATOM    908  C   GLN A 476     123.572  78.044 129.024  1.00 62.26           C
ATOM    909  O   GLN A 476     122.362  78.237 128.867  1.00 62.26           O
ATOM    910  CB  GLN A 476     124.496  76.630 127.139  1.00 62.26           C
ATOM    911  CG  GLN A 476     123.277  76.827 126.251  1.00 99.99           C
ATOM    912  CD  GLN A 476     123.612  76.745 124.776  1.00 99.99           C
ATOM    913  OE1 GLN A 476     124.642  76.193 124.392  1.00 99.99           O
ATOM    914  NE2 GLN A 476     122.737  77.294 123.941  1.00 99.99           N
ATOM    915  N   LEU A 477     124.393  78.964 129.536  1.00 60.34           N
ATOM    916  CA  LEU A 477     123.860  80.228 130.036  1.00 60.34           C
ATOM    917  C   LEU A 477     123.028  80.949 128.983  1.00 60.34           C
ATOM    918  O   LEU A 477     121.887  81.338 129.255  1.00 60.34           O
ATOM    919  CB  LEU A 477     124.995  81.138 130.510  1.00 60.34           C
ATOM    920  CG  LEU A 477     125.799  80.647 131.716  1.00 99.99           C
ATOM    921  CD1 LEU A 477     126.978  81.568 131.987  1.00 99.99           C
ATOM    922  CD2 LEU A 477     124.929  80.610 132.962  1.00 99.99           C
ATOM    923  N   ASP A 478     123.573  81.134 127.784  1.00 58.44           N
ATOM    924  CA  ASP A 478     122.847  81.755 126.679  1.00 58.44           C
ATOM    925  C   ASP A 478     123.081  80.959 125.401  1.00 58.44           C
ATOM    926  O   ASP A 478     123.291  81.513 124.321  1.00 58.44           O
ATOM    927  CB  ASP A 478     123.281  83.211 126.504  1.00 58.44           C
ATOM    928  CG  ASP A 478     124.750  83.343 126.156  1.00 99.99           C
ATOM    929  OD1 ASP A 478     125.585  82.735 126.858  1.00 99.99           O
ATOM    930  OD2 ASP A 478     125.069  84.055 125.180  1.00 99.99           O
ATOM    931  N   CYS A 479     123.036  79.632 125.515  1.00 63.83           N
ATOM    932  CA  CYS A 479     123.322  78.747 124.388  1.00 63.83           C
ATOM    933  C   CYS A 479     124.703  79.043 123.808  1.00 63.83           C
ATOM    934  O   CYS A 479     124.870  79.207 122.598  1.00 63.83           O
ATOM    935  CB  CYS A 479     122.248  78.890 123.308  1.00 63.83           C
ATOM    936  SG  CYS A 479     120.586  78.348 123.822  1.00 99.99           S
ATOM    937  N   LYS A 480     125.702  79.115 124.687  1.00 72.50           N
ATOM    938  CA  LYS A 480     127.060  79.456 124.284  1.00 72.50           C
ATOM    939  C   LYS A 480     127.096  80.854 123.681  1.00 72.50           C
ATOM    940  O   LYS A 480     127.512  81.035 122.532  1.00 72.50           O
ATOM    941  CB  LYS A 480     127.598  78.426 123.289  1.00 72.50           C
ATOM    942  CG  LYS A 480     127.810  77.043 123.881  1.00 99.99           C
ATOM    943  CD  LYS A 480     128.345  76.072 122.840  1.00 99.99           C
ATOM    944  CE  LYS A 480     127.302  75.779 121.773  1.00 99.99           C
ATOM    945  NZ  LYS A 480     126.121  75.066 122.332  1.00 99.99           N
ATOM    946  N   VAL A 481     126.657  81.846 124.452  1.00 78.79           N
ATOM    947  CA  VAL A 481     126.634  83.240 124.028  1.00 78.79           C
ATOM    948  C   VAL A 481     127.443  84.060 125.021  1.00 78.79           C
ATOM    949  O   VAL A 481     127.275  83.921 126.238  1.00 78.79           O
ATOM    950  CB  VAL A 481     125.194  83.776 123.930  1.00 78.79           C
ATOM    951  CG1 VAL A 481     125.199  85.263 123.607  1.00 99.99           C
ATOM    952  CG2 VAL A 481     124.428  83.049 122.835  1.00 99.99           C
ATOM    953  N   GLN A 482     128.321  84.914 124.500  1.00 86.72           N
ATOM    954  CA  GLN A 482     129.179  85.756 125.318  1.00 86.72           C
ATOM    955  C   GLN A 482     128.985  87.214 124.928  1.00 86.72           C
ATOM    956  O   GLN A 482     128.273  87.530 123.970  1.00 86.72           O
ATOM    957  CB  GLN A 482     130.643  85.338 125.165  1.00 86.72           C
ATOM    958  CG  GLN A 482     130.949  83.946 125.690  1.00 99.99           C
ATOM    959  CD  GLN A 482     130.664  82.862 124.667  1.00 99.99           C
ATOM    960  OE1 GLN A 482     130.233  83.148 123.550  1.00 99.99           O
ATOM    961  NE2 GLN A 482     130.908  81.614 125.046  1.00 99.99           N
ATOM    962  N   LEU A 483     129.628  88.104 125.688  1.00 90.35           N
ATOM    963  CA  LEU A 483     129.511  89.532 125.411  1.00 90.35           C
ATOM    964  C   LEU A 483     130.048  89.880 124.030  1.00 90.35           C
ATOM    965  O   LEU A 483     129.468  90.721 123.333  1.00 90.35           O
ATOM    966  CB  LEU A 483     130.247  90.347 126.476  1.00 90.35           C
ATOM    967  CG  LEU A 483     129.689  90.264 127.899  1.00 99.99           C
ATOM    968  CD1 LEU A 483     130.595  90.998 128.875  1.00 99.99           C
ATOM    969  CD2 LEU A 483     128.306  90.893 127.970  1.00 99.99           C
ATOM    970  N   ARG A 484     131.155  89.256 123.620  1.00 92.34           N
ATOM    971  CA  ARG A 484     131.721  89.539 122.305  1.00 92.34           C
ATOM    972  C   ARG A 484     130.747  89.155 121.196  1.00 92.34           C
ATOM    973  O   ARG A 484     130.588  89.887 120.212  1.00 92.34           O
ATOM    974  CB  ARG A 484     133.048  88.800 122.122  1.00 92.34           C
ATOM    975  CG  ARG A 484     132.928  87.286 122.181  1.00 99.99           C
ATOM    976  CD  ARG A 484     134.280  86.618 121.992  1.00 99.99           C
ATOM    977  NE  ARG A 484     134.183  85.161 122.045  1.00 99.99           N
ATOM    978  CZ  ARG A 484     134.203  84.451 123.168  1.00 99.99           C
ATOM    979  NH1 ARG A 484     134.319  85.065 124.338  1.00 99.99           N
ATOM    980  NH2 ARG A 484     134.109  83.130 123.119  1.00 99.99           N
ATOM    981  N   HIS A 485     130.092  88.001 121.336  1.00 92.50           N
ATOM    982  CA  HIS A 485     129.120  87.581 120.332  1.00 92.50           C
ATOM    983  C   HIS A 485     127.954  88.559 120.256  1.00 92.50           C
ATOM    984  O   HIS A 485     127.490  88.902 119.162  1.00 92.50           O
ATOM    985  CB  HIS A 485     128.608  86.172 120.638  1.00 92.50           C
ATOM    986  CG  HIS A 485     129.661  85.112 120.543  1.00 99.99           C
ATOM    987  ND1 HIS A 485     130.533  84.835 121.572  1.00 99.99           N
ATOM    988  CD2 HIS A 485     129.983  84.263 119.538  1.00 99.99           C
ATOM    989  CE1 HIS A 485     131.346  83.859 121.205  1.00 99.99           C
ATOM    990  NE2 HIS A 485     131.033  83.494 119.977  1.00 99.99           N
ATOM    991  N   ALA A 486     127.465  89.017 121.411  1.00 93.56           N
ATOM    992  CA  ALA A 486     126.376  89.988 121.415  1.00 93.56           C
ATOM    993  C   ALA A 486     126.804  91.294 120.758  1.00 93.56           C
ATOM    994  O   ALA A 486     126.035  91.898 120.002  1.00 93.56           O
ATOM    995  CB  ALA A 486     125.892  90.251 122.849  1.00 93.56           C
ATOM    996  N   ALA A 487     128.027  91.748 121.038  1.00 96.53           N
ATOM    997  CA  ALA A 487     128.521  92.974 120.419  1.00 96.53           C
ATOM    998  C   ALA A 487     128.624  92.818 118.907  1.00 96.53           C
ATOM    999  O   ALA A 487     128.264  93.726 118.150  1.00 96.53           O
ATOM   1000  CB  ALA A 487     129.886  93.364 121.006  1.00 96.53           C
ATOM   1001  N   SER A 488     129.121  91.667 118.448  1.00 96.98           N
ATOM   1002  CA  SER A 488     129.222  91.425 117.012  1.00 96.98           C
ATOM   1003  C   SER A 488     127.843  91.406 116.365  1.00 96.98           C
ATOM   1004  O   SER A 488     127.644  91.961 115.277  1.00 96.98           O
ATOM   1005  CB  SER A 488     129.953  90.109 116.740  1.00 96.98           C
ATOM   1006  OG  SER A 488     129.243  89.010 117.285  1.00 99.99           O
ATOM   1007  N   VAL A 489     126.875  90.763 117.021  1.00 96.52           N
ATOM   1008  CA  VAL A 489     125.518  90.717 116.484  1.00 96.52           C
ATOM   1009  C   VAL A 489     124.931  92.120 116.406  1.00 96.52           C
ATOM   1010  O   VAL A 489     124.278  92.483 115.420  1.00 96.52           O
ATOM   1011  CB  VAL A 489     124.603  89.822 117.340  1.00 96.52           C
ATOM   1012  CG1 VAL A 489     123.169  89.887 116.835  1.00 99.99           C
ATOM   1013  CG2 VAL A 489     125.068  88.375 117.282  1.00 99.99           C
ATOM   1014  N   MET A 490     125.143  92.927 117.448  1.00 97.66           N
ATOM   1015  CA  MET A 490     124.642  94.297 117.437  1.00 97.66           C
ATOM   1016  C   MET A 490     125.289  95.112 116.324  1.00 97.66           C
ATOM   1017  O   MET A 490     124.616  95.902 115.654  1.00 97.66           O
ATOM   1018  CB  MET A 490     124.886  94.968 118.790  1.00 97.66           C
ATOM   1019  CG  MET A 490     124.079  94.373 119.932  1.00 99.99           C
ATOM   1020  SD  MET A 490     124.396  95.191 121.508  1.00 99.99           S
ATOM   1021  CE  MET A 490     126.007  94.526 121.918  1.00 99.99           C
ATOM   1022  N   VAL A 491     126.596  94.938 116.117  1.00 98.21           N
ATOM   1023  CA  VAL A 491     127.282  95.663 115.051  1.00 98.21           C
ATOM   1024  C   VAL A 491     126.726  95.260 113.692  1.00 98.21           C
ATOM   1025  O   VAL A 491     126.493  96.109 112.822  1.00 98.21           O
ATOM   1026  CB  VAL A 491     128.800  95.408 115.082  1.00 98.21           C
ATOM   1027  CG1 VAL A 491     129.477  96.072 113.892  1.00 99.99           C
ATOM   1028  CG2 VAL A 491     129.409  95.972 116.357  1.00 99.99           C
ATOM   1029  N   MET A 492     126.510  93.959 113.485  1.00 97.81           N
ATOM   1030  CA  MET A 492     125.949  93.498 112.219  1.00 97.81           C
ATOM   1031  C   MET A 492     124.548  94.059 112.005  1.00 97.81           C
ATOM   1032  O   MET A 492     124.201  94.482 110.895  1.00 97.81           O
ATOM   1033  CB  MET A 492     125.919  91.969 112.171  1.00 97.81           C
ATOM   1034  CG  MET A 492     125.048  91.331 113.242  1.00 99.99           C
ATOM   1035  SD  MET A 492     125.039  89.532 113.153  1.00 99.99           S
ATOM   1036  CE  MET A 492     123.984  89.269 111.729  1.00 99.99           C
ATOM   1037  N   GLY A 493     123.727  94.065 113.056  1.00 97.91           N
ATOM   1038  CA  GLY A 493     122.391  94.625 112.932  1.00 97.91           C
ATOM   1039  C   GLY A 493     122.416  96.106 112.609  1.00 97.91           C
ATOM   1040  O   GLY A 493     121.630  96.591 111.792  1.00 97.91           O
ATOM   1041  N   TRP A 494     123.322  96.846 113.251  1.00 98.38           N
ATOM   1042  CA  TRP A 494     123.452  98.271 112.967  1.00 98.38           C
ATOM   1043  C   TRP A 494     123.888  98.500 111.525  1.00 98.38           C
ATOM   1044  O   TRP A 494     123.392  99.409 110.850  1.00 98.38           O
ATOM   1045  CB  TRP A 494     124.446  98.921 113.931  1.00 98.38           C
ATOM   1046  CG  TRP A 494     123.995  98.906 115.359  1.00 99.99           C
ATOM   1047  CD1 TRP A 494     124.316  97.981 116.310  1.00 99.99           C
ATOM   1048  CD2 TRP A 494     123.138  99.862 115.996  1.00 99.99           C
ATOM   1049  NE1 TRP A 494     123.713  98.299 117.504  1.00 99.99           N
ATOM   1050  CE2 TRP A 494     122.983  99.452 117.335  1.00 99.99           C
ATOM   1051  CE3 TRP A 494     122.489 101.021 115.565  1.00 99.99           C
ATOM   1052  CZ2 TRP A 494     122.205 100.160 118.250  1.00 99.99           C
ATOM   1053  CZ3 TRP A 494     121.717 101.724 116.471  1.00 99.99           C
ATOM   1054  CH2 TRP A 494     121.579 101.294 117.801  1.00 99.99           C
ATOM   1055  N   ILE A 495     124.824  97.683 111.038  1.00 98.53           N
ATOM   1056  CA  ILE A 495     125.274  97.814 109.654  1.00 98.53           C
ATOM   1057  C   ILE A 495     124.122  97.540 108.696  1.00 98.53           C
ATOM   1058  O   ILE A 495     123.934  98.257 107.705  1.00 98.53           O
ATOM   1059  CB  ILE A 495     126.440  96.856 109.347  1.00 98.53           C
ATOM   1060  CG1 ILE A 495     127.672  97.234 110.173  1.00 99.99           C
ATOM   1061  CG2 ILE A 495     126.809  96.921 107.873  1.00 99.99           C
ATOM   1062  CD1 ILE A 495     128.783  96.210 110.115  1.00 99.99           C
ATOM   1063  N   PHE A 496     123.338  96.496 108.971  1.00 97.80           N
ATOM   1064  CA  PHE A 496     122.198  96.180 108.116  1.00 97.80           C
ATOM   1065  C   PHE A 496     121.177  97.311 108.128  1.00 97.80           C
ATOM   1066  O   PHE A 496     120.623  97.678 107.084  1.00 97.80           O
ATOM   1067  CB  PHE A 496     121.542  94.871 108.559  1.00 97.80           C
ATOM   1068  CG  PHE A 496     120.402  94.438 107.684  1.00 99.99           C
ATOM   1069  CD1 PHE A 496     120.638  93.798 106.479  1.00 99.99           C
ATOM   1070  CD2 PHE A 496     119.092  94.668 108.064  1.00 99.99           C
ATOM   1071  CE1 PHE A 496     119.588  93.400 105.673  1.00 99.99           C
ATOM   1072  CE2 PHE A 496     118.040  94.272 107.260  1.00 99.99           C
ATOM   1073  CZ  PHE A 496     118.289  93.636 106.064  1.00 99.99           C
ATOM   1074  N   ALA A 497     120.909  97.874 109.308  1.00 98.11           N
ATOM   1075  CA  ALA A 497     119.962  98.979 109.403  1.00 98.11           C
ATOM   1076  C   ALA A 497     120.454 100.193 108.629  1.00 98.11           C
ATOM   1077  O   ALA A 497     119.673 100.858 107.938  1.00 98.11           O
ATOM   1078  CB  ALA A 497     119.716  99.354 110.872  1.00 98.11           C
ATOM   1079  N   PHE A 498     121.748 100.505 108.738  1.00 98.07           N
ATOM   1080  CA  PHE A 498     122.302 101.626 107.987  1.00 98.07           C
ATOM   1081  C   PHE A 498     122.199 101.385 106.487  1.00 98.07           C
ATOM   1082  O   PHE A 498     121.852 102.297 105.727  1.00 98.07           O
ATOM   1083  CB  PHE A 498     123.759 101.869 108.383  1.00 98.07           C
ATOM   1084  CG  PHE A 498     124.383 103.054 107.705  1.00 99.99           C
ATOM   1085  CD1 PHE A 498     124.146 104.338 108.165  1.00 99.99           C
ATOM   1086  CD2 PHE A 498     125.207 102.888 106.607  1.00 99.99           C
ATOM   1087  CE1 PHE A 498     124.719 105.429 107.540  1.00 99.99           C
ATOM   1088  CE2 PHE A 498     125.781 103.977 105.979  1.00 99.99           C
ATOM   1089  CZ  PHE A 498     125.538 105.249 106.447  1.00 99.99           C
ATOM   1090  N   ALA A 499     122.495 100.162 106.041  1.00 97.60           N
ATOM   1091  CA  ALA A 499     122.380  99.850 104.621  1.00 97.60           C
ATOM   1092  C   ALA A 499     120.943 100.004 104.142  1.00 97.60           C
ATOM   1093  O   ALA A 499     120.696 100.551 103.061  1.00 97.60           O
ATOM   1094  CB  ALA A 499     122.883  98.426 104.338  1.00 97.60           C
ATOM   1095  N   ALA A 500     119.981  99.526 104.933  1.00 97.26           N
ATOM   1096  CA  ALA A 500     118.577  99.665 104.557  1.00 97.26           C
ATOM   1097  C   ALA A 500     118.173 101.133 104.490  1.00 97.26           C
ATOM   1098  O   ALA A 500     117.478 101.558 103.559  1.00 97.26           O
ATOM   1099  CB  ALA A 500     117.676  98.912 105.546  1.00 97.26           C
ATOM   1100  N   ALA A 501     118.605 101.928 105.472  1.00 97.54           N
ATOM   1101  CA  ALA A 501     118.260 103.345 105.485  1.00 97.54           C
ATOM   1102  C   ALA A 501     118.925 104.094 104.339  1.00 97.54           C
ATOM   1103  O   ALA A 501     118.421 105.136 103.905  1.00 97.54           O
ATOM   1104  CB  ALA A 501     118.654 103.984 106.825  1.00 97.54           C
ATOM   1105  N   LEU A 502     120.059 103.593 103.847  1.00 96.94           N
ATOM   1106  CA  LEU A 502     120.740 104.249 102.737  1.00 96.94           C
ATOM   1107  C   LEU A 502     120.119 103.896 101.391  1.00 96.94           C
ATOM   1108  O   LEU A 502     120.401 104.565 100.391  1.00 96.94           O
ATOM   1109  CB  LEU A 502     122.225 103.883 102.728  1.00 96.94           C
ATOM   1110  CG  LEU A 502     123.051 104.367 103.922  1.00 99.99           C
ATOM   1111  CD1 LEU A 502     124.465 103.812 103.858  1.00 99.99           C
ATOM   1112  CD2 LEU A 502     123.136 105.885 103.935  1.00 99.99           C
ATOM   1113  N   PHE A 503     119.280 102.860 101.343  1.00 96.78           N
ATOM   1114  CA  PHE A 503     118.689 102.448 100.071  1.00 96.78           C
ATOM   1115  C   PHE A 503     117.880 103.559  99.419  1.00 96.78           C
ATOM   1116  O   PHE A 503     118.079 103.817  98.219  1.00 96.78           O
ATOM   1117  CB  PHE A 503     117.800 101.219 100.266  1.00 96.78           C
ATOM   1118  CG  PHE A 503     118.549  99.991 100.697  1.00 99.99           C
ATOM   1119  CD1 PHE A 503     119.154  99.167  99.762  1.00 99.99           C
ATOM   1120  CD2 PHE A 503     118.652  99.657 102.036  1.00 99.99           C
ATOM   1121  CE1 PHE A 503     119.844  98.038 100.158  1.00 99.99           C
ATOM   1122  CE2 PHE A 503     119.340  98.528 102.435  1.00 99.99           C
ATOM   1123  CZ  PHE A 503     119.937  97.717 101.494  1.00 99.99           C
ATOM   1124  N   PRO A 504     116.970 104.244 100.117  1.00 96.34           N
ATOM   1125  CA  PRO A 504     116.235 105.341  99.466  1.00 96.34           C
ATOM   1126  C   PRO A 504     117.139 106.432  98.923  1.00 96.34           C
ATOM   1127  O   PRO A 504     116.832 107.012  97.873  1.00 96.34           O
ATOM   1128  CB  PRO A 504     115.299 105.832 100.572  1.00 96.34           C
ATOM   1129  CG  PRO A 504     115.073 104.610 101.435  1.00 96.34           C
ATOM   1130  CD  PRO A 504     116.442 103.953 101.458  1.00 96.34           C
ATOM   1131  N   ILE A 505     118.247 106.731  99.604  1.00 94.78           N
ATOM   1132  CA  ILE A 505     119.164 107.752  99.109  1.00 94.78           C
ATOM   1133  C   ILE A 505     119.810 107.312  97.801  1.00 94.78           C
ATOM   1134  O   ILE A 505     120.176 108.152  96.969  1.00 94.78           O
ATOM   1135  CB  ILE A 505     120.264 108.069 100.138  1.00 94.78           C
ATOM   1136  CG1 ILE A 505     119.655 108.697 101.394  1.00 99.99           C
ATOM   1137  CG2 ILE A 505     121.277 109.043  99.554  1.00 99.99           C
ATOM   1138  CD1 ILE A 505     120.625 108.821 102.548  1.00 99.99           C
ATOM   1139  N   PHE A 506     119.961 106.002  97.592  1.00 94.38           N
ATOM   1140  CA  PHE A 506     120.616 105.465  96.405  1.00 94.38           C
ATOM   1141  C   PHE A 506     119.650 105.248  95.246  1.00 94.38           C
ATOM   1142  O   PHE A 506     119.969 104.499  94.311  1.00 94.38           O
ATOM   1143  CB  PHE A 506     121.318 104.145  96.731  1.00 94.38           C
ATOM   1144  CG  PHE A 506     122.455 104.287  97.701  1.00 99.99           C
ATOM   1145  CD1 PHE A 506     123.722 104.632  97.261  1.00 99.99           C
ATOM   1146  CD2 PHE A 506     122.260 104.078  99.055  1.00 99.99           C
ATOM   1147  CE1 PHE A 506     124.768 104.763  98.154  1.00 99.99           C
ATOM   1148  CE2 PHE A 506     123.305 104.207  99.950  1.00 99.99           C
ATOM   1149  CZ  PHE A 506     124.560 104.550  99.499  1.00 99.99           C
ATOM   1150  N   GLY A 507     118.478 105.879  95.278  1.00 91.17           N
ATOM   1151  CA  GLY A 507     117.521 105.769  94.199  1.00 91.17           C
ATOM   1152  C   GLY A 507     116.546 104.618  94.313  1.00 91.17           C
ATOM   1153  O   GLY A 507     115.633 104.522  93.483  1.00 91.17           O
ATOM   1154  N   ILE A 508     116.702 103.744  95.304  1.00 92.96           N
ATOM   1155  CA  ILE A 508     115.774 102.640  95.525  1.00 92.96           C
ATOM   1156  C   ILE A 508     114.566 103.222  96.250  1.00 92.96           C
ATOM   1157  O   ILE A 508     114.567 103.363  97.474  1.00 92.96           O
ATOM   1158  CB  ILE A 508     116.428 101.507  96.337  1.00 92.96           C
ATOM   1159  CG1 ILE A 508     117.573 100.874  95.542  1.00 99.99           C
ATOM   1160  CG2 ILE A 508     115.409 100.425  96.660  1.00 99.99           C
ATOM   1161  CD1 ILE A 508     118.422  99.918  96.350  1.00 99.99           C
ATOM   1162  N   SER A 509     113.524 103.557  95.488  1.00 93.32           N
ATOM   1163  CA  SER A 509     112.373 104.269  96.030  1.00 93.32           C
ATOM   1164  C   SER A 509     112.790 105.674  96.446  1.00 93.32           C
ATOM   1165  O   SER A 509     113.961 106.044  96.309  1.00 93.32           O
ATOM   1166  CB  SER A 509     111.777 103.503  97.212  1.00 93.32           C
ATOM   1167  OG  SER A 509     110.616 104.149  97.706  1.00 99.99           O
ATOM   1168  N   SER A 510     111.846 106.467  96.948  1.00 93.72           N
ATOM   1169  CA  SER A 510     112.137 107.838  97.339  1.00 93.72           C
ATOM   1170  C   SER A 510     111.255 108.226  98.515  1.00 93.72           C
ATOM   1171  O   SER A 510     110.087 107.833  98.581  1.00 93.72           O
ATOM   1172  CB  SER A 510     111.929 108.788  96.158  1.00 93.72           C
ATOM   1173  OG  SER A 510     110.581 108.771  95.722  1.00 99.99           O
ATOM   1174  N   TYR A 511     111.825 109.000  99.438  1.00 94.82           N
ATOM   1175  CA  TYR A 511     111.083 109.489 100.592  1.00 94.82           C
ATOM   1176  C   TYR A 511     110.264 110.735 100.284  1.00 94.82           C
ATOM   1177  O   TYR A 511     109.393 111.095 101.083  1.00 94.82           O
ATOM   1178  CB  TYR A 511     112.033 109.786 101.754  1.00 94.82           C
ATOM   1179  CG  TYR A 511     113.049 110.865 101.454  1.00 99.99           C
ATOM   1180  CD1 TYR A 511     112.771 112.199 101.720  1.00 99.99           C
ATOM   1181  CD2 TYR A 511     114.285 110.546 100.904  1.00 99.99           C
ATOM   1182  CE1 TYR A 511     113.692 113.190 101.450  1.00 99.99           C
ATOM   1183  CE2 TYR A 511     115.219 111.524 100.626  1.00 99.99           C
ATOM   1184  CZ  TYR A 511     114.922 112.847 100.900  1.00 99.99           C
ATOM   1185  OH  TYR A 511     115.845 113.828 100.627  1.00 99.99           O
ATOM   1186  N   MET A 512     110.516 111.396  99.152  1.00 91.22           N
ATOM   1187  CA  MET A 512     109.775 112.605  98.812  1.00 91.22           C
ATOM   1188  C   MET A 512     108.328 112.313  98.437  1.00 91.22           C
ATOM   1189  O   MET A 512     107.532 113.250  98.321  1.00 91.22           O
ATOM   1190  CB  MET A 512     110.459 113.348  97.663  1.00 91.22           C
ATOM   1191  CG  MET A 512     109.792 114.661  97.288  1.00 99.99           C
ATOM   1192  SD  MET A 512     109.879 115.887  98.607  1.00 99.99           S
ATOM   1193  CE  MET A 512     109.024 117.264  97.846  1.00 99.99           C
ATOM   1194  N   LYS A 513     107.971 111.043  98.245  1.00 87.66           N
ATOM   1195  CA  LYS A 513     106.611 110.683  97.868  1.00 87.66           C
ATOM   1196  C   LYS A 513     105.585 111.027  98.940  1.00 87.66           C
ATOM   1197  O   LYS A 513     104.393 111.112  98.625  1.00 87.66           O
ATOM   1198  CB  LYS A 513     106.521 109.190  97.549  1.00 87.66           C
ATOM   1199  CG  LYS A 513     107.287 108.773  96.304  1.00 99.99           C
ATOM   1200  CD  LYS A 513     107.154 107.281  96.047  1.00 99.99           C
ATOM   1201  CE  LYS A 513     107.921 106.865  94.802  1.00 99.99           C
ATOM   1202  NZ  LYS A 513     107.799 105.404  94.538  1.00 99.99           N
ATOM   1203  N   VAL A 514     106.009 111.223 100.188  1.00 88.75           N
ATOM   1204  CA  VAL A 514     105.105 111.559 101.280  1.00 88.75           C
ATOM   1205  C   VAL A 514     105.699 112.715 102.071  1.00 88.75           C
ATOM   1206  O   VAL A 514     106.917 112.910 102.107  1.00 88.75           O
ATOM   1207  CB  VAL A 514     104.859 110.350 102.201  1.00 88.75           C
ATOM   1208  CG1 VAL A 514     104.013 110.755 103.399  1.00 99.99           C
ATOM   1209  CG2 VAL A 514     104.128 109.248 101.448  1.00 99.99           C
ATOM   1210  N   SER A 515     104.819 113.488 102.712  1.00 89.55           N
ATOM   1211  CA  SER A 515     105.276 114.623 103.508  1.00 89.55           C
ATOM   1212  C   SER A 515     106.005 114.169 104.766  1.00 89.55           C
ATOM   1213  O   SER A 515     106.797 114.931 105.332  1.00 89.55           O
ATOM   1214  CB  SER A 515     104.097 115.522 103.886  1.00 89.55           C
ATOM   1215  OG  SER A 515     103.158 114.823 104.683  1.00 99.99           O
ATOM   1216  N   ILE A 516     105.754 112.941 105.217  1.00 90.75           N
ATOM   1217  CA  ILE A 516     106.380 112.418 106.428  1.00 90.75           C
ATOM   1218  C   ILE A 516     107.721 111.782 106.087  1.00 90.75           C
ATOM   1219  O   ILE A 516     108.363 111.166 106.946  1.00 90.75           O
ATOM   1220  CB  ILE A 516     105.477 111.386 107.129  1.00 90.75           C
ATOM   1221  CG1 ILE A 516     104.197 112.054 107.634  1.00 99.99           C
ATOM   1222  CG2 ILE A 516     106.199 110.766 108.316  1.00 99.99           C
ATOM   1223  CD1 ILE A 516     103.150 111.077 108.122  1.00 99.99           C
ATOM   1224  N   CYS A 517     108.156 111.924 104.835  1.00 93.51           N
ATOM   1225  CA  CYS A 517     109.423 111.394 104.341  1.00 93.51           C
ATOM   1226  C   CYS A 517     109.448 109.872 104.303  1.00 93.51           C
ATOM   1227  O   CYS A 517     110.530 109.282 104.183  1.00 93.51           O
ATOM   1228  CB  CYS A 517     110.585 111.897 105.199  1.00 93.51           C
ATOM   1229  SG  CYS A 517     110.855 113.698 105.120  1.00 99.99           S
ATOM   1230  N   LEU A 518     108.296 109.217 104.405  1.00 91.24           N
ATOM   1231  CA  LEU A 518     108.267 107.766 104.356  1.00 91.24           C
ATOM   1232  C   LEU A 518     108.618 107.277 102.950  1.00 91.24           C
ATOM   1233  O   LEU A 518     108.288 107.930 101.956  1.00 91.24           O
ATOM   1234  CB  LEU A 518     106.894 107.243 104.781  1.00 91.24           C
ATOM   1235  CG  LEU A 518     106.487 107.508 106.233  1.00 99.99           C
ATOM   1236  CD1 LEU A 518     105.051 107.068 106.477  1.00 99.99           C
ATOM   1237  CD2 LEU A 518     107.387 106.744 107.191  1.00 99.99           C
ATOM   1238  N   PRO A 519     109.290 106.126 102.838  1.00 91.73           N
ATOM   1239  CA  PRO A 519     109.630 105.605 101.507  1.00 91.73           C
ATOM   1240  C   PRO A 519     108.461 104.886 100.850  1.00 91.73           C
ATOM   1241  O   PRO A 519     108.559 103.704 100.507  1.00 91.73           O
ATOM   1242  CB  PRO A 519     110.827 104.695 101.789  1.00 91.73           C
ATOM   1243  CG  PRO A 519     111.469 105.298 103.018  1.00 91.73           C
ATOM   1244  CD  PRO A 519     110.273 105.719 103.854  1.00 91.73           C
ATOM   1245  N   MET A 520     107.345 105.595 100.672  1.00 85.44           N
ATOM   1246  CA  MET A 520     106.152 104.996 100.087  1.00 85.44           C
ATOM   1247  C   MET A 520     106.250 104.831  98.577  1.00 85.44           C
ATOM   1248  O   MET A 520     105.388 104.169  97.989  1.00 85.44           O
ATOM   1249  CB  MET A 520     104.914 105.830 100.421  1.00 85.44           C
ATOM   1250  CG  MET A 520     104.953 107.248  99.870  1.00 99.99           C
ATOM   1251  SD  MET A 520     103.480 108.197 100.285  1.00 99.99           S
ATOM   1252  CE  MET A 520     102.286 107.482  99.156  1.00 99.99           C
ATOM   1253  N   ASP A 521     107.264 105.410  97.937  1.00 86.92           N
ATOM   1254  CA  ASP A 521     107.394 105.306  96.490  1.00 86.92           C
ATOM   1255  C   ASP A 521     107.556 103.849  96.076  1.00 86.92           C
ATOM   1256  O   ASP A 521     108.555 103.205  96.411  1.00 86.92           O
ATOM   1257  CB  ASP A 521     108.578 106.140  95.997  1.00 86.92           C
ATOM   1258  CG  ASP A 521     108.714 106.124  94.487  1.00 99.99           C
ATOM   1259  OD1 ASP A 521     107.806 106.642  93.803  1.00 99.99           O
ATOM   1260  OD2 ASP A 521     109.728 105.595  93.987  1.00 99.99           O
ATOM   1261  N   ILE A 522     106.567 103.331  95.347  1.00 87.40           N
ATOM   1262  CA  ILE A 522     106.586 101.967  94.839  1.00 87.40           C
ATOM   1263  C   ILE A 522     106.271 101.907  93.350  1.00 87.40           C
ATOM   1264  O   ILE A 522     105.953 100.836  92.832  1.00 87.40           O
ATOM   1265  CB  ILE A 522     105.584 101.071  95.590  1.00 87.40           C
ATOM   1266  CG1 ILE A 522     105.995 100.925  97.057  1.00 99.99           C
ATOM   1267  CG2 ILE A 522     105.532  99.686  94.963  1.00 99.99           C
ATOM   1268  CD1 ILE A 522     104.946 100.262  97.922  1.00 99.99           C
ATOM   1269  N   ASP A 523     106.349 103.041  92.648  1.00 87.20           N
ATOM   1270  CA  ASP A 523     106.019 103.049  91.226  1.00 87.20           C
ATOM   1271  C   ASP A 523     106.942 102.127  90.439  1.00 87.20           C
ATOM   1272  O   ASP A 523     106.481 101.344  89.599  1.00 87.20           O
ATOM   1273  CB  ASP A 523     106.095 104.471  90.666  1.00 87.20           C
ATOM   1274  CG  ASP A 523     107.486 105.063  90.768  1.00 99.99           C
ATOM   1275  OD1 ASP A 523     108.076 105.009  91.868  1.00 99.99           O
ATOM   1276  OD2 ASP A 523     107.989 105.582  89.749  1.00 99.99           O
ATOM   1277  N   SER A 524     108.246 102.200  90.697  1.00 91.68           N
ATOM   1278  CA  SER A 524     109.183 101.331  89.999  1.00 91.68           C
ATOM   1279  C   SER A 524     109.149  99.929  90.606  1.00 91.68           C
ATOM   1280  O   SER A 524     108.899  99.779  91.805  1.00 91.68           O
ATOM   1281  CB  SER A 524     110.597 101.912  90.056  1.00 91.68           C
ATOM   1282  OG  SER A 524     111.055 102.007  91.394  1.00 99.99           O
ATOM   1283  N   PRO A 525     109.392  98.885  89.807  1.00 93.29           N
ATOM   1284  CA  PRO A 525     109.415  97.531  90.385  1.00 93.29           C
ATOM   1285  C   PRO A 525     110.440  97.371  91.494  1.00 93.29           C
ATOM   1286  O   PRO A 525     110.190  96.643  92.462  1.00 93.29           O
ATOM   1287  CB  PRO A 525     109.697  96.644  89.171  1.00 93.29           C
ATOM   1288  CG  PRO A 525     109.125  97.418  88.005  1.00 93.29           C
ATOM   1289  CD  PRO A 525     109.488  98.854  88.341  1.00 93.29           C
ATOM   1290  N   LEU A 526     111.593  98.035  91.380  1.00 94.40           N
ATOM   1291  CA  LEU A 526     112.635  97.882  92.390  1.00 94.40           C
ATOM   1292  C   LEU A 526     112.182  98.421  93.742  1.00 94.40           C
ATOM   1293  O   LEU A 526     112.392  97.776  94.777  1.00 94.40           O
ATOM   1294  CB  LEU A 526     113.918  98.589  91.948  1.00 94.40           C
ATOM   1295  CG  LEU A 526     114.610  98.023  90.706  1.00 99.99           C
ATOM   1296  CD1 LEU A 526     115.781  98.903  90.296  1.00 99.99           C
ATOM   1297  CD2 LEU A 526     115.140  96.624  90.977  1.00 99.99           C
ATOM   1298  N   SER A 527     111.564  99.604  93.757  1.00 93.94           N
ATOM   1299  CA  SER A 527     111.116 100.185  95.019  1.00 93.94           C
ATOM   1300  C   SER A 527     110.033  99.329  95.665  1.00 93.94           C
ATOM   1301  O   SER A 527     110.055  99.097  96.881  1.00 93.94           O
ATOM   1302  CB  SER A 527     110.601 101.609  94.801  1.00 93.94           C
ATOM   1303  OG  SER A 527     109.482 101.618  93.933  1.00 99.99           O
ATOM   1304  N   GLN A 528     109.075  98.854  94.867  1.00 93.28           N
ATOM   1305  CA  GLN A 528     108.020  98.002  95.406  1.00 93.28           C
ATOM   1306  C   GLN A 528     108.600  96.705  95.954  1.00 93.28           C
ATOM   1307  O   GLN A 528     108.190  96.228  97.018  1.00 93.28           O
ATOM   1308  CB  GLN A 528     106.971  97.704  94.333  1.00 93.28           C
ATOM   1309  CG  GLN A 528     106.168  98.918  93.896  1.00 99.99           C
ATOM   1310  CD  GLN A 528     105.141  98.584  92.832  1.00 99.99           C
ATOM   1311  OE1 GLN A 528     105.293  97.614  92.090  1.00 99.99           O
ATOM   1312  NE2 GLN A 528     104.087  99.389  92.756  1.00 99.99           N
ATOM   1313  N   LEU A 529     109.560  96.118  95.235  1.00 93.71           N
ATOM   1314  CA  LEU A 529     110.190  94.891  95.708  1.00 93.71           C
ATOM   1315  C   LEU A 529     110.931  95.125  97.018  1.00 93.71           C
ATOM   1316  O   LEU A 529     110.860  94.299  97.934  1.00 93.71           O
ATOM   1317  CB  LEU A 529     111.148  94.339  94.651  1.00 93.71           C
ATOM   1318  CG  LEU A 529     110.515  93.871  93.339  1.00 99.99           C
ATOM   1319  CD1 LEU A 529     111.588  93.487  92.332  1.00 99.99           C
ATOM   1320  CD2 LEU A 529     109.628  92.659  93.574  1.00 99.99           C
ATOM   1321  N   TYR A 530     111.651  96.243  97.125  1.00 95.47           N
ATOM   1322  CA  TYR A 530     112.367  96.546  98.360  1.00 95.47           C
ATOM   1323  C   TYR A 530     111.399  96.737  99.522  1.00 95.47           C
ATOM   1324  O   TYR A 530     111.637  96.242 100.631  1.00 95.47           O
ATOM   1325  CB  TYR A 530     113.234  97.794  98.185  1.00 95.47           C
ATOM   1326  CG  TYR A 530     112.447  99.047  97.869  1.00 99.99           C
ATOM   1327  CD1 TYR A 530     111.979  99.869  98.886  1.00 99.99           C
ATOM   1328  CD2 TYR A 530     112.176  99.404  96.554  1.00 99.99           C
ATOM   1329  CE1 TYR A 530     111.260 101.013  98.606  1.00 99.99           C
ATOM   1330  CE2 TYR A 530     111.458 100.545  96.255  1.00 99.99           C
ATOM   1331  CZ  TYR A 530     111.001 101.350  97.283  1.00 99.99           C
ATOM   1332  OH  TYR A 530     110.285 102.488  96.996  1.00 99.99           O
ATOM   1333  N   VAL A 531     110.300  97.457  99.286  1.00 93.16           N
ATOM   1334  CA  VAL A 531     109.317  97.675 100.344  1.00 93.16           C
ATOM   1335  C   VAL A 531     108.703  96.350 100.778  1.00 93.16           C
ATOM   1336  O   VAL A 531     108.529  96.090 101.976  1.00 93.16           O
ATOM   1337  CB  VAL A 531     108.203  98.635  99.889  1.00 93.16           C
ATOM   1338  CG1 VAL A 531     107.128  98.750 100.960  1.00 99.99           C
ATOM   1339  CG2 VAL A 531     108.769 100.022  99.626  1.00 99.99           C
ATOM   1340  N   MET A 532     108.359  95.495  99.812  1.00 91.94           N
ATOM   1341  CA  MET A 532     107.784  94.196 100.145  1.00 91.94           C
ATOM   1342  C   MET A 532     108.774  93.343 100.926  1.00 91.94           C
ATOM   1343  O   MET A 532     108.394  92.657 101.880  1.00 91.94           O
ATOM   1344  CB  MET A 532     107.343  93.464  98.876  1.00 91.94           C
ATOM   1345  CG  MET A 532     108.477  93.156  97.911  1.00 99.99           C
ATOM   1346  SD  MET A 532     107.917  92.295  96.430  1.00 99.99           S
ATOM   1347  CE  MET A 532     107.638  90.649  97.081  1.00 99.99           C
ATOM   1348  N   SER A 533     110.049  93.366 100.531  1.00 93.14           N
ATOM   1349  CA  SER A 533     111.060  92.601 101.253  1.00 93.14           C
ATOM   1350  C   SER A 533     111.210  93.102 102.683  1.00 93.14           C
ATOM   1351  O   SER A 533     111.319  92.303 103.620  1.00 93.14           O
ATOM   1352  CB  SER A 533     112.405  92.670 100.527  1.00 93.14           C
ATOM   1353  OG  SER A 533     112.879  94.003 100.460  1.00 99.99           O
ATOM   1354  N   LEU A 534     111.221  94.423 102.872  1.00 93.03           N
ATOM   1355  CA  LEU A 534     111.326  94.973 104.220  1.00 93.03           C
ATOM   1356  C   LEU A 534     110.124  94.570 105.067  1.00 93.03           C
ATOM   1357  O   LEU A 534     110.273  94.177 106.231  1.00 93.03           O
ATOM   1358  CB  LEU A 534     111.451  96.497 104.169  1.00 93.03           C
ATOM   1359  CG  LEU A 534     112.718  97.052 103.513  1.00 99.99           C
ATOM   1360  CD1 LEU A 534     112.644  98.566 103.398  1.00 99.99           C
ATOM   1361  CD2 LEU A 534     113.947  96.697 104.334  1.00 99.99           C
ATOM   1362  N   LEU A 535     108.921  94.658 104.495  1.00 90.77           N
ATOM   1363  CA  LEU A 535     107.723  94.273 105.234  1.00 90.77           C
ATOM   1364  C   LEU A 535     107.752  92.792 105.592  1.00 90.77           C
ATOM   1365  O   LEU A 535     107.382  92.407 106.708  1.00 90.77           O
ATOM   1366  CB  LEU A 535     106.466  94.595 104.423  1.00 90.77           C
ATOM   1367  CG  LEU A 535     106.196  96.077 104.152  1.00 99.99           C
ATOM   1368  CD1 LEU A 535     105.006  96.243 103.219  1.00 99.99           C
ATOM   1369  CD2 LEU A 535     105.890  96.812 105.447  1.00 99.99           C
ATOM   1370  N   VAL A 536     108.186  91.946 104.656  1.00 91.16           N
ATOM   1371  CA  VAL A 536     108.253  90.513 104.917  1.00 91.16           C
ATOM   1372  C   VAL A 536     109.269  90.217 106.011  1.00 91.16           C
ATOM   1373  O   VAL A 536     109.029  89.378 106.887  1.00 91.16           O
ATOM   1374  CB  VAL A 536     108.622  89.725 103.647  1.00 91.16           C
ATOM   1375  CG1 VAL A 536     108.807  88.250 103.969  1.00 99.99           C
ATOM   1376  CG2 VAL A 536     107.524  89.855 102.602  1.00 99.99           C
ATOM   1377  N   LEU A 537     110.423  90.886 105.974  1.00 92.07           N
ATOM   1378  CA  LEU A 537     111.428  90.683 107.012  1.00 92.07           C
ATOM   1379  C   LEU A 537     110.891  91.102 108.375  1.00 92.07           C
ATOM   1380  O   LEU A 537     111.093  90.406 109.376  1.00 92.07           O
ATOM   1381  CB  LEU A 537     112.704  91.460 106.682  1.00 92.07           C
ATOM   1382  CG  LEU A 537     113.463  91.017 105.430  1.00 99.99           C
ATOM   1383  CD1 LEU A 537     114.620  91.960 105.141  1.00 99.99           C
ATOM   1384  CD2 LEU A 537     114.027  89.616 105.612  1.00 99.99           C
ATOM   1385  N   ASN A 538     110.198  92.243 108.430  1.00 88.62           N
ATOM   1386  CA  ASN A 538     109.625  92.691 109.695  1.00 88.62           C
ATOM   1387  C   ASN A 538     108.589  91.699 110.211  1.00 88.62           C
ATOM   1388  O   ASN A 538     108.562  91.380 111.406  1.00 88.62           O
ATOM   1389  CB  ASN A 538     108.995  94.076 109.537  1.00 88.62           C
ATOM   1390  CG  ASN A 538     108.449  94.620 110.843  1.00 99.99           C
ATOM   1391  OD1 ASN A 538     109.184  94.779 111.816  1.00 99.99           O
ATOM   1392  ND2 ASN A 538     107.153  94.909 110.865  1.00 99.99           N
ATOM   1393  N   VAL A 539     107.730  91.195 109.322  1.00 88.72           N
ATOM   1394  CA  VAL A 539     106.705  90.241 109.735  1.00 88.72           C
ATOM   1395  C   VAL A 539     107.346  88.956 110.241  1.00 88.72           C
ATOM   1396  O   VAL A 539     106.920  88.388 111.254  1.00 88.72           O
ATOM   1397  CB  VAL A 539     105.741  89.914 108.580  1.00 88.72           C
ATOM   1398  CG1 VAL A 539     104.759  88.828 108.996  1.00 99.99           C
ATOM   1399  CG2 VAL A 539     104.949  91.150 108.181  1.00 99.99           C
ATOM   1400  N   LEU A 540     108.371  88.469 109.538  1.00 92.00           N
ATOM   1401  CA  LEU A 540     109.053  87.253 109.968  1.00 92.00           C
ATOM   1402  C   LEU A 540     109.719  87.448 111.323  1.00 92.00           C
ATOM   1403  O   LEU A 540     109.660  86.563 112.185  1.00 92.00           O
ATOM   1404  CB  LEU A 540     110.089  86.823 108.928  1.00 92.00           C
ATOM   1405  CG  LEU A 540     109.545  86.402 107.561  1.00 99.99           C
ATOM   1406  CD1 LEU A 540     110.683  86.143 106.586  1.00 99.99           C
ATOM   1407  CD2 LEU A 540     108.723  85.128 107.681  1.00 99.99           C
ATOM   1408  N   ALA A 541     110.362  88.599 111.530  1.00 90.92           N
ATOM   1409  CA  ALA A 541     110.991  88.872 112.818  1.00 90.92           C
ATOM   1410  C   ALA A 541     109.951  88.913 113.929  1.00 90.92           C
ATOM   1411  O   ALA A 541     110.162  88.360 115.015  1.00 90.92           O
ATOM   1412  CB  ALA A 541     111.771  90.194 112.769  1.00 90.92           C
ATOM   1413  N   PHE A 542     108.813  89.563 113.673  1.00 86.36           N
ATOM   1414  CA  PHE A 542     107.758  89.624 114.679  1.00 86.36           C
ATOM   1415  C   PHE A 542     107.224  88.234 115.000  1.00 86.36           C
ATOM   1416  O   PHE A 542     106.993  87.904 116.169  1.00 86.36           O
ATOM   1417  CB  PHE A 542     106.619  90.530 114.207  1.00 86.36           C
ATOM   1418  CG  PHE A 542     105.523  90.702 115.218  1.00 99.99           C
ATOM   1419  CD1 PHE A 542     105.664  91.592 116.270  1.00 99.99           C
ATOM   1420  CD2 PHE A 542     104.349  89.977 115.121  1.00 99.99           C
ATOM   1421  CE1 PHE A 542     104.656  91.751 117.202  1.00 99.99           C
ATOM   1422  CE2 PHE A 542     103.340  90.132 116.051  1.00 99.99           C
ATOM   1423  CZ  PHE A 542     103.493  91.021 117.091  1.00 99.99           C
ATOM   1424  N   VAL A 543     107.022  87.404 113.976  1.00 89.34           N
ATOM   1425  CA  VAL A 543     106.512  86.054 114.199  1.00 89.34           C
ATOM   1426  C   VAL A 543     107.511  85.236 115.008  1.00 89.34           C
ATOM   1427  O   VAL A 543     107.135  84.498 115.927  1.00 89.34           O
ATOM   1428  CB  VAL A 543     106.216  85.336 112.870  1.00 89.34           C
ATOM   1429  CG1 VAL A 543     105.804  83.894 113.122  1.00 99.99           C
ATOM   1430  CG2 VAL A 543     105.086  86.035 112.127  1.00 99.99           C
ATOM   1431  N   VAL A 544     108.798  85.345 114.672  1.00 91.02           N
ATOM   1432  CA  VAL A 544     109.824  84.602 115.400  1.00 91.02           C
ATOM   1433  C   VAL A 544     109.864  85.048 116.856  1.00 91.02           C
ATOM   1434  O   VAL A 544     109.976  84.227 117.774  1.00 91.02           O
ATOM   1435  CB  VAL A 544     111.214  84.788 114.764  1.00 91.02           C
ATOM   1436  CG1 VAL A 544     112.282  84.109 115.607  1.00 99.99           C
ATOM   1437  CG2 VAL A 544     111.246  84.183 113.368  1.00 99.99           C
ATOM   1438  N   ILE A 545     109.780  86.360 117.087  1.00 86.95           N
ATOM   1439  CA  ILE A 545     109.804  86.879 118.452  1.00 86.95           C
ATOM   1440  C   ILE A 545     108.597  86.372 119.230  1.00 86.95           C
ATOM   1441  O   ILE A 545     108.710  85.970 120.394  1.00 86.95           O
ATOM   1442  CB  ILE A 545     109.821  88.418 118.470  1.00 86.95           C
ATOM   1443  CG1 ILE A 545     111.118  88.945 117.852  1.00 99.99           C
ATOM   1444  CG2 ILE A 545     109.721  88.937 119.897  1.00 99.99           C
ATOM   1445  CD1 ILE A 545     111.119  90.438 117.611  1.00 99.99           C
ATOM   1446  N   CYS A 546     107.419  86.390 118.601  1.00 86.05           N
ATOM   1447  CA  CYS A 546     106.216  85.914 119.276  1.00 86.05           C
ATOM   1448  C   CYS A 546     106.328  84.434 119.619  1.00 86.05           C
ATOM   1449  O   CYS A 546     105.964  84.015 120.724  1.00 86.05           O
ATOM   1450  CB  CYS A 546     104.981  86.162 118.408  1.00 86.05           C
ATOM   1451  SG  CYS A 546     104.996  85.287 116.810  1.00 99.99           S
ATOM   1452  N   GLY A 547     106.831  83.626 118.684  1.00 89.14           N
ATOM   1453  CA  GLY A 547     106.999  82.209 118.962  1.00 89.14           C
ATOM   1454  C   GLY A 547     107.990  81.952 120.081  1.00 89.14           C
ATOM   1455  O   GLY A 547     107.750  81.115 120.957  1.00 89.14           O
ATOM   1456  N   CYS A 548     109.116  82.670 120.071  1.00 87.84           N
ATOM   1457  CA  CYS A 548     110.107  82.510 121.129  1.00 87.84           C
ATOM   1458  C   CYS A 548     109.529  82.907 122.481  1.00 87.84           C
ATOM   1459  O   CYS A 548     109.758  82.232 123.490  1.00 87.84           O
ATOM   1460  CB  CYS A 548     111.356  83.339 120.823  1.00 87.84           C
ATOM   1461  SG  CYS A 548     111.063  85.134 120.727  1.00 99.99           S
ATOM   1462  N   TYR A 549     108.775  84.008 122.520  1.00 81.91           N
ATOM   1463  CA  TYR A 549     108.155  84.441 123.767  1.00 81.91           C
ATOM   1464  C   TYR A 549     107.141  83.421 124.267  1.00 81.91           C
ATOM   1465  O   TYR A 549     107.083  83.138 125.468  1.00 81.91           O
ATOM   1466  CB  TYR A 549     107.482  85.803 123.586  1.00 81.91           C
ATOM   1467  CG  TYR A 549     108.445  86.928 123.285  1.00 99.99           C
ATOM   1468  CD1 TYR A 549     109.095  87.603 124.312  1.00 99.99           C
ATOM   1469  CD2 TYR A 549     108.704  87.313 121.976  1.00 99.99           C
ATOM   1470  CE1 TYR A 549     109.976  88.631 124.045  1.00 99.99           C
ATOM   1471  CE2 TYR A 549     109.583  88.340 121.691  1.00 99.99           C
ATOM   1472  CZ  TYR A 549     110.219  88.997 122.727  1.00 99.99           C
ATOM   1473  OH  TYR A 549     111.096  90.021 122.454  1.00 99.99           O
ATOM   1474  N   ILE A 550     106.335  82.860 123.363  1.00 84.07           N
ATOM   1475  CA  ILE A 550     105.358  81.852 123.764  1.00 84.07           C
ATOM   1476  C   ILE A 550     106.067  80.628 124.328  1.00 84.07           C
ATOM   1477  O   ILE A 550     105.665  80.072 125.358  1.00 84.07           O
ATOM   1478  CB  ILE A 550     104.463  81.433 122.584  1.00 84.07           C
ATOM   1479  CG1 ILE A 550     103.606  82.613 122.119  1.00 99.99           C
ATOM   1480  CG2 ILE A 550     103.537  80.297 122.993  1.00 99.99           C
ATOM   1481  CD1 ILE A 550     102.874  82.364 120.819  1.00 99.99           C
ATOM   1482  N   HIS A 551     107.133  80.186 123.656  1.00 85.34           N
ATOM   1483  CA  HIS A 551     107.881  79.030 124.139  1.00 85.34           C
ATOM   1484  C   HIS A 551     108.496  79.304 125.507  1.00 85.34           C
ATOM   1485  O   HIS A 551     108.461  78.444 126.395  1.00 85.34           O
ATOM   1486  CB  HIS A 551     108.972  78.642 123.140  1.00 85.34           C
ATOM   1487  CG  HIS A 551     108.445  78.168 121.821  1.00 99.99           C
ATOM   1488  ND1 HIS A 551     108.068  79.030 120.816  1.00 99.99           N
ATOM   1489  CD2 HIS A 551     108.228  76.918 121.345  1.00 99.99           C
ATOM   1490  CE1 HIS A 551     107.644  78.332 119.777  1.00 99.99           C
ATOM   1491  NE2 HIS A 551     107.731  77.049 120.071  1.00 99.99           N
ATOM   1492  N   ILE A 552     109.064  80.497 125.694  1.00 81.54           N
ATOM   1493  CA  ILE A 552     109.678  80.840 126.974  1.00 81.54           C
ATOM   1494  C   ILE A 552     108.626  80.861 128.075  1.00 81.54           C
ATOM   1495  O   ILE A 552     108.852  80.366 129.185  1.00 81.54           O
ATOM   1496  CB  ILE A 552     110.388  82.205 126.911  1.00 81.54           C
ATOM   1497  CG1 ILE A 552     111.568  82.148 125.939  1.00 99.99           C
ATOM   1498  CG2 ILE A 552     110.912  82.597 128.285  1.00 99.99           C
ATOM   1499  CD1 ILE A 552     112.174  83.500 125.634  1.00 99.99           C
ATOM   1500  N   TYR A 553     107.461  81.448 127.787  1.00 77.95           N
ATOM   1501  CA  TYR A 553     106.390  81.484 128.777  1.00 77.95           C
ATOM   1502  C   TYR A 553     105.908  80.084 129.131  1.00 77.95           C
ATOM   1503  O   TYR A 553     105.664  79.794 130.307  1.00 77.95           O
ATOM   1504  CB  TYR A 553     105.218  82.325 128.268  1.00 77.95           C
ATOM   1505  CG  TYR A 553     105.549  83.789 128.082  1.00 99.99           C
ATOM   1506  CD1 TYR A 553     105.471  84.677 129.148  1.00 99.99           C
ATOM   1507  CD2 TYR A 553     105.938  84.279 126.843  1.00 99.99           C
ATOM   1508  CE1 TYR A 553     105.772  86.015 128.987  1.00 99.99           C
ATOM   1509  CE2 TYR A 553     106.243  85.615 126.663  1.00 99.99           C
ATOM   1510  CZ  TYR A 553     106.160  86.481 127.736  1.00 99.99           C
ATOM   1511  OH  TYR A 553     106.461  87.812 127.569  1.00 99.99           O
ATOM   1512  N   LEU A 554     105.763  79.209 128.137  1.00 83.62           N
ATOM   1513  CA  LEU A 554     105.343  77.837 128.394  1.00 83.62           C
ATOM   1514  C   LEU A 554     106.371  77.117 129.258  1.00 83.62           C
ATOM   1515  O   LEU A 554     106.010  76.402 130.199  1.00 83.62           O
ATOM   1516  CB  LEU A 554     105.130  77.086 127.078  1.00 83.62           C
ATOM   1517  CG  LEU A 554     103.994  77.592 126.185  1.00 99.99           C
ATOM   1518  CD1 LEU A 554     103.989  76.855 124.855  1.00 99.99           C
ATOM   1519  CD2 LEU A 554     102.647  77.372 126.855  1.00 99.99           C
ATOM   1520  N   THR A 555     107.656  77.303 128.946  1.00 79.90           N
ATOM   1521  CA  THR A 555     108.709  76.649 129.716  1.00 79.90           C
ATOM   1522  C   THR A 555     108.739  77.150 131.155  1.00 79.90           C
ATOM   1523  O   THR A 555     108.923  76.365 132.092  1.00 79.90           O
ATOM   1524  CB  THR A 555     110.093  76.870 129.080  1.00 79.90           C
ATOM   1525  OG1 THR A 555     110.398  78.271 129.068  1.00 99.99           O
ATOM   1526  CG2 THR A 555     110.113  76.350 127.651  1.00 99.99           C
ATOM   1527  N   VAL A 556     108.560  78.459 131.349  1.00 75.46           N
ATOM   1528  CA  VAL A 556     108.649  79.030 132.690  1.00 75.46           C
ATOM   1529  C   VAL A 556     107.567  78.463 133.597  1.00 75.46           C
ATOM   1530  O   VAL A 556     107.832  78.131 134.759  1.00 75.46           O
ATOM   1531  CB  VAL A 556     108.531  80.565 132.659  1.00 75.46           C
ATOM   1532  CG1 VAL A 556     108.502  81.127 134.072  1.00 99.99           C
ATOM   1533  CG2 VAL A 556     109.714  81.175 131.923  1.00 99.99           C
ATOM   1534  N   ARG A 557     106.340  78.339 133.095  1.00 75.18           N
ATOM   1535  CA  ARG A 557     105.229  77.842 133.892  1.00 75.18           C
ATOM   1536  C   ARG A 557     105.224  76.325 134.032  1.00 75.18           C
ATOM   1537  O   ARG A 557     104.392  75.792 134.773  1.00 75.18           O
ATOM   1538  CB  ARG A 557     103.896  78.292 133.293  1.00 75.18           C
ATOM   1539  CG  ARG A 557     103.638  77.768 131.889  1.00 99.99           C
ATOM   1540  CD  ARG A 557     102.299  78.253 131.357  1.00 99.99           C
ATOM   1541  NE  ARG A 557     102.035  77.759 130.008  1.00 99.99           N
ATOM   1542  CZ  ARG A 557     102.472  78.344 128.898  1.00 99.99           C
ATOM   1543  NH1 ARG A 557     103.197  79.452 128.975  1.00 99.99           N
ATOM   1544  NH2 ARG A 557     102.182  77.822 127.715  1.00 99.99           N
ATOM   1545  N   ASN A 558     106.119  75.624 133.349  1.00 77.29           N
ATOM   1546  CA  ASN A 558     106.161  74.169 133.442  1.00 77.29           C
ATOM   1547  C   ASN A 558     106.608  73.754 134.839  1.00 77.29           C
ATOM   1548  O   ASN A 558     107.691  74.163 135.277  1.00 77.29           O
ATOM   1549  CB  ASN A 558     107.094  73.591 132.377  1.00 77.29           C
ATOM   1550  CG  ASN A 558     108.527  74.055 132.544  1.00 99.99           C
ATOM   1551  OD1 ASN A 558     108.793  75.251 132.661  1.00 99.99           O
ATOM   1552  ND2 ASN A 558     109.458  73.108 132.555  1.00 99.99           N
ATOM   1553  N   PRO A 559     105.825  72.955 135.572  1.00 70.50           N
ATOM   1554  CA  PRO A 559     106.256  72.556 136.921  1.00 70.50           C
ATOM   1555  C   PRO A 559     107.485  71.664 136.931  1.00 70.50           C
ATOM   1556  O   PRO A 559     108.146  71.566 137.972  1.00 70.50           O
ATOM   1557  CB  PRO A 559     105.014  71.867 137.489  1.00 70.50           C
ATOM   1558  CG  PRO A 559     103.861  72.528 136.767  1.00 70.50           C
ATOM   1559  CD  PRO A 559     104.395  72.692 135.355  1.00 70.50           C
ATOM   1560  N   ASN A 560     107.813  71.012 135.813  1.00 70.62           N
ATOM   1561  CA  ASN A 560     108.949  70.098 135.788  1.00 70.62           C
ATOM   1562  C   ASN A 560     110.286  70.827 135.831  1.00 70.62           C
ATOM   1563  O   ASN A 560     111.311  70.194 136.108  1.00 70.62           O
ATOM   1564  CB  ASN A 560     108.895  69.210 134.544  1.00 70.62           C
ATOM   1565  CG  ASN A 560     108.979  70.005 133.256  1.00 99.99           C
ATOM   1566  OD1 ASN A 560     108.236  70.966 133.059  1.00 99.99           O
ATOM   1567  ND2 ASN A 560     109.886  69.606 132.373  1.00 99.99           N
ATOM   1568  N   ILE A 561     110.301  72.130 135.565  1.00 65.94           N
ATOM   1569  CA  ILE A 561     111.526  72.923 135.543  1.00 65.94           C
ATOM   1570  C   ILE A 561     111.453  73.962 136.651  1.00 65.94           C
ATOM   1571  O   ILE A 561     110.438  74.654 136.800  1.00 65.94           O
ATOM   1572  CB  ILE A 561     111.732  73.605 134.178  1.00 65.94           C
ATOM   1573  CG1 ILE A 561     111.952  72.556 133.086  1.00 99.99           C
ATOM   1574  CG2 ILE A 561     112.945  74.522 134.217  1.00 99.99           C
ATOM   1575  CD1 ILE A 561     111.925  73.120 131.682  1.00 99.99           C
ATOM   1576  N   VAL A 562     112.530  74.077 137.428  1.00 63.21           N
ATOM   1577  CA  VAL A 562     112.598  75.043 138.518  1.00 63.21           C
ATOM   1578  C   VAL A 562     113.083  76.377 137.967  1.00 63.21           C
ATOM   1579  O   VAL A 562     114.289  76.647 137.932  1.00 63.21           O
ATOM   1580  CB  VAL A 562     113.530  74.559 139.644  1.00 63.21           C
ATOM   1581  CG1 VAL A 562     113.682  75.633 140.710  1.00 99.99           C
ATOM   1582  CG2 VAL A 562     112.967  73.307 140.300  1.00 99.99           C
ATOM   1583  N   SER A 563     112.148  77.217 137.528  1.00 56.35           N
ATOM   1584  CA  SER A 563     112.496  78.513 136.959  1.00 56.35           C
ATOM   1585  C   SER A 563     112.967  79.458 138.059  1.00 56.35           C
ATOM   1586  O   SER A 563     112.357  79.528 139.131  1.00 56.35           O
ATOM   1587  CB  SER A 563     111.302  79.107 136.209  1.00 56.35           C
ATOM   1588  OG  SER A 563     110.962  78.318 135.084  1.00 99.99           O
ATOM   1589  N   SER A 564     114.051  80.183 137.794  1.00 62.32           N
ATOM   1590  CA  SER A 564     114.574  81.135 138.762  1.00 62.32           C
ATOM   1591  C   SER A 564     113.749  82.419 138.758  1.00 62.32           C
ATOM   1592  O   SER A 564     113.055  82.738 137.788  1.00 62.32           O
ATOM   1593  CB  SER A 564     116.043  81.446 138.469  1.00 62.32           C
ATOM   1594  OG  SER A 564     116.192  82.044 137.193  1.00 99.99           O
ATOM   1595  N   SER A 565     113.830  83.160 139.866  1.00 62.73           N
ATOM   1596  CA  SER A 565     113.114  84.429 139.962  1.00 62.73           C
ATOM   1597  C   SER A 565     113.615  85.432 138.931  1.00 62.73           C
ATOM   1598  O   SER A 565     112.813  86.158 138.330  1.00 62.73           O
ATOM   1599  CB  SER A 565     113.248  85.015 141.369  1.00 62.73           C
ATOM   1600  OG  SER A 565     114.603  85.292 141.678  1.00 99.99           O
ATOM   1601  N   SER A 566     114.931  85.498 138.722  1.00 64.38           N
ATOM   1602  CA  SER A 566     115.468  86.380 137.691  1.00 64.38           C
ATOM   1603  C   SER A 566     114.941  85.990 136.318  1.00 64.38           C
ATOM   1604  O   SER A 566     114.648  86.857 135.485  1.00 64.38           O
ATOM   1605  CB  SER A 566     116.997  86.348 137.702  1.00 64.38           C
ATOM   1606  OG  SER A 566     117.482  85.049 137.413  1.00 99.99           O
ATOM   1607  N   ASP A 567     114.811  84.687 136.063  1.00 61.20           N
ATOM   1608  CA  ASP A 567     114.225  84.233 134.808  1.00 61.20           C
ATOM   1609  C   ASP A 567     112.790  84.724 134.673  1.00 61.20           C
ATOM   1610  O   ASP A 567     112.370  85.159 133.596  1.00 61.20           O
ATOM   1611  CB  ASP A 567     114.276  82.707 134.714  1.00 61.20           C
ATOM   1612  CG  ASP A 567     113.744  82.186 133.393  1.00 99.99           C
ATOM   1613  OD1 ASP A 567     114.308  82.549 132.340  1.00 99.99           O
ATOM   1614  OD2 ASP A 567     112.761  81.414 133.412  1.00 99.99           O
ATOM   1615  N   THR A 568     112.019  84.661 135.761  1.00 64.69           N
ATOM   1616  CA  THR A 568     110.641  85.140 135.718  1.00 64.69           C
ATOM   1617  C   THR A 568     110.585  86.636 135.433  1.00 64.69           C
ATOM   1618  O   THR A 568     109.753  87.095 134.641  1.00 64.69           O
ATOM   1619  CB  THR A 568     109.902  84.851 137.038  1.00 64.69           C
ATOM   1620  OG1 THR A 568     110.548  85.545 138.112  1.00 99.99           O
ATOM   1621  CG2 THR A 568     109.911  83.360 137.338  1.00 99.99           C
ATOM   1622  N   ARG A 569     111.456  87.416 136.077  1.00 66.49           N
ATOM   1623  CA  ARG A 569     111.474  88.856 135.833  1.00 66.49           C
ATOM   1624  C   ARG A 569     111.851  89.165 134.389  1.00 66.49           C
ATOM   1625  O   ARG A 569     111.245  90.037 133.750  1.00 66.49           O
ATOM   1626  CB  ARG A 569     112.445  89.550 136.790  1.00 66.49           C
ATOM   1627  CG  ARG A 569     112.016  89.508 138.247  1.00 99.99           C
ATOM   1628  CD  ARG A 569     113.023  90.214 139.141  1.00 99.99           C
ATOM   1629  NE  ARG A 569     114.315  89.533 139.152  1.00 99.99           N
ATOM   1630  CZ  ARG A 569     115.395  89.969 138.514  1.00 99.99           C
ATOM   1631  NH1 ARG A 569     115.341  91.090 137.808  1.00 99.99           N
ATOM   1632  NH2 ARG A 569     116.528  89.283 138.582  1.00 99.99           N
ATOM   1633  N   ILE A 570     112.853  88.461 133.859  1.00 66.45           N
ATOM   1634  CA  ILE A 570     113.261  88.671 132.472  1.00 66.45           C
ATOM   1635  C   ILE A 570     112.120  88.311 131.531  1.00 66.45           C
ATOM   1636  O   ILE A 570     111.866  89.005 130.540  1.00 66.45           O
ATOM   1637  CB  ILE A 570     114.507  87.839 132.119  1.00 66.45           C
ATOM   1638  CG1 ILE A 570     115.713  88.312 132.934  1.00 99.99           C
ATOM   1639  CG2 ILE A 570     114.840  87.978 130.641  1.00 99.99           C
ATOM   1640  CD1 ILE A 570     116.917  87.402 132.829  1.00 99.99           C
ATOM   1641  N   ALA A 571     111.420  87.213 131.824  1.00 63.94           N
ATOM   1642  CA  ALA A 571     110.291  86.813 130.994  1.00 63.94           C
ATOM   1643  C   ALA A 571     109.190  87.864 131.022  1.00 63.94           C
ATOM   1644  O   ALA A 571     108.603  88.182 129.984  1.00 63.94           O
ATOM   1645  CB  ALA A 571     109.738  85.456 131.453  1.00 63.94           C
ATOM   1646  N   LYS A 572     108.893  88.411 132.202  1.00 68.57           N
ATOM   1647  CA  LYS A 572     107.865  89.444 132.294  1.00 68.57           C
ATOM   1648  C   LYS A 572     108.259  90.685 131.502  1.00 68.57           C
ATOM   1649  O   LYS A 572     107.438  91.253 130.770  1.00 68.57           O
ATOM   1650  CB  LYS A 572     107.605  89.813 133.756  1.00 68.57           C
ATOM   1651  CG  LYS A 572     106.972  88.700 134.574  1.00 99.99           C
ATOM   1652  CD  LYS A 572     106.742  89.134 136.013  1.00 99.99           C
ATOM   1653  CE  LYS A 572     106.110  88.020 136.831  1.00 99.99           C
ATOM   1654  NZ  LYS A 572     107.017  86.846 136.968  1.00 99.99           N
ATOM   1655  N   ARG A 573     109.514  91.122 131.635  1.00 68.66           N
ATOM   1656  CA  ARG A 573     109.965  92.295 130.892  1.00 68.66           C
ATOM   1657  C   ARG A 573     109.907  92.049 129.389  1.00 68.66           C
ATOM   1658  O   ARG A 573     109.465  92.918 128.626  1.00 68.66           O
ATOM   1659  CB  ARG A 573     111.386  92.680 131.309  1.00 68.66           C
ATOM   1660  CG  ARG A 573     111.520  93.066 132.772  1.00 99.99           C
ATOM   1661  CD  ARG A 573     110.802  94.373 133.065  1.00 99.99           C
ATOM   1662  NE  ARG A 573     110.920  94.760 134.469  1.00 99.99           N
ATOM   1663  CZ  ARG A 573     110.385  95.860 134.988  1.00 99.99           C
ATOM   1664  NH1 ARG A 573     109.690  96.685 134.219  1.00 99.99           N
ATOM   1665  NH2 ARG A 573     110.546  96.129 136.276  1.00 99.99           N
ATOM   1666  N   MET A 574     110.345  90.868 128.948  1.00 65.76           N
ATOM   1667  CA  MET A 574     110.310  90.544 127.527  1.00 65.76           C
ATOM   1668  C   MET A 574     108.877  90.494 127.017  1.00 65.76           C
ATOM   1669  O   MET A 574     108.585  90.951 125.908  1.00 65.76           O
ATOM   1670  CB  MET A 574     111.013  89.211 127.264  1.00 65.76           C
ATOM   1671  CG  MET A 574     112.512  89.240 127.518  1.00 99.99           C
ATOM   1672  SD  MET A 574     113.302  87.651 127.197  1.00 99.99           S
ATOM   1673  CE  MET A 574     113.312  87.636 125.405  1.00 99.99           C
ATOM   1674  N   ALA A 575     107.966  89.932 127.814  1.00 65.94           N
ATOM   1675  CA  ALA A 575     106.565  89.876 127.415  1.00 65.94           C
ATOM   1676  C   ALA A 575     105.986  91.276 127.270  1.00 65.94           C
ATOM   1677  O   ALA A 575     105.275  91.569 126.303  1.00 65.94           O
ATOM   1678  CB  ALA A 575     105.746  89.065 128.430  1.00 65.94           C
ATOM   1679  N   MET A 576     106.281  92.159 128.227  1.00 69.37           N
ATOM   1680  CA  MET A 576     105.785  93.529 128.133  1.00 69.37           C
ATOM   1681  C   MET A 576     106.334  94.227 126.894  1.00 69.37           C
ATOM   1682  O   MET A 576     105.586  94.882 126.154  1.00 69.37           O
ATOM   1683  CB  MET A 576     106.152  94.319 129.390  1.00 69.37           C
ATOM   1684  CG  MET A 576     107.649  94.458 129.621  1.00 99.99           C
ATOM   1685  SD  MET A 576     108.040  95.394 131.110  1.00 99.99           S
ATOM   1686  CE  MET A 576     107.677  97.062 130.567  1.00 99.99           C
ATOM   1687  N   LEU A 577     107.640  94.091 126.648  1.00 68.91           N
ATOM   1688  CA  LEU A 577     108.244  94.735 125.485  1.00 68.91           C
ATOM   1689  C   LEU A 577     107.652  94.192 124.190  1.00 68.91           C
ATOM   1690  O   LEU A 577     107.363  94.951 123.258  1.00 68.91           O
ATOM   1691  CB  LEU A 577     109.762  94.542 125.494  1.00 68.91           C
ATOM   1692  CG  LEU A 577     110.523  95.208 126.642  1.00 99.99           C
ATOM   1693  CD1 LEU A 577     111.993  94.816 126.610  1.00 99.99           C
ATOM   1694  CD2 LEU A 577     110.434  96.722 126.539  1.00 99.99           C
ATOM   1695  N   ILE A 578     107.466  92.872 124.114  1.00 68.37           N
ATOM   1696  CA  ILE A 578     106.921  92.260 122.907  1.00 68.37           C
ATOM   1697  C   ILE A 578     105.487  92.714 122.683  1.00 68.37           C
ATOM   1698  O   ILE A 578     105.080  92.989 121.549  1.00 68.37           O
ATOM   1699  CB  ILE A 578     106.968  90.723 122.983  1.00 68.37           C
ATOM   1700  CG1 ILE A 578     108.418  90.235 123.022  1.00 99.99           C
ATOM   1701  CG2 ILE A 578     106.284  90.107 121.772  1.00 99.99           C
ATOM   1702  CD1 ILE A 578     108.559  88.762 123.337  1.00 99.99           C
ATOM   1703  N   PHE A 579     104.692  92.784 123.753  1.00 74.13           N
ATOM   1704  CA  PHE A 579     103.316  93.246 123.617  1.00 74.13           C
ATOM   1705  C   PHE A 579     103.275  94.682 123.113  1.00 74.13           C
ATOM   1706  O   PHE A 579     102.494  95.015 122.213  1.00 74.13           O
ATOM   1707  CB  PHE A 579     102.577  93.130 124.952  1.00 74.13           C
ATOM   1708  CG  PHE A 579     101.130  93.521 124.879  1.00 99.99           C
ATOM   1709  CD1 PHE A 579     100.182  92.638 124.389  1.00 99.99           C
ATOM   1710  CD2 PHE A 579     100.712  94.770 125.300  1.00 99.99           C
ATOM   1711  CE1 PHE A 579      98.850  92.997 124.321  1.00 99.99           C
ATOM   1712  CE2 PHE A 579      99.380  95.133 125.233  1.00 99.99           C
ATOM   1713  CZ  PHE A 579      98.448  94.245 124.745  1.00 99.99           C
ATOM   1714  N   THR A 580     104.117  95.550 123.680  1.00 78.19           N
ATOM   1715  CA  THR A 580     104.151  96.938 123.229  1.00 78.19           C
ATOM   1716  C   THR A 580     104.560  97.026 121.762  1.00 78.19           C
ATOM   1717  O   THR A 580     103.938  97.750 120.973  1.00 78.19           O
ATOM   1718  CB  THR A 580     105.120  97.783 124.077  1.00 78.19           C
ATOM   1719  OG1 THR A 580     106.451  97.270 123.939  1.00 99.99           O
ATOM   1720  CG2 THR A 580     104.723  97.736 125.544  1.00 99.99           C
ATOM   1721  N   ASP A 581     105.600  96.283 121.377  1.00 73.73           N
ATOM   1722  CA  ASP A 581     106.068  96.324 119.996  1.00 73.73           C
ATOM   1723  C   ASP A 581     104.999  95.819 119.037  1.00 73.73           C
ATOM   1724  O   ASP A 581     104.780  96.410 117.974  1.00 73.73           O
ATOM   1725  CB  ASP A 581     107.347  95.500 119.839  1.00 73.73           C
ATOM   1726  CG  ASP A 581     107.916  95.569 118.436  1.00 99.99           C
ATOM   1727  OD1 ASP A 581     108.246  96.684 117.982  1.00 99.99           O
ATOM   1728  OD2 ASP A 581     108.033  94.505 117.789  1.00 99.99           O
ATOM   1729  N   PHE A 582     104.325  94.724 119.392  1.00 76.24           N
ATOM   1730  CA  PHE A 582     103.273  94.192 118.535  1.00 76.24           C
ATOM   1731  C   PHE A 582     102.130  95.189 118.399  1.00 76.24           C
ATOM   1732  O   PHE A 582     101.643  95.444 117.292  1.00 76.24           O
ATOM   1733  CB  PHE A 582     102.755  92.862 119.085  1.00 76.24           C
ATOM   1734  CG  PHE A 582     101.715  92.212 118.219  1.00 99.99           C
ATOM   1735  CD1 PHE A 582     102.081  91.492 117.094  1.00 99.99           C
ATOM   1736  CD2 PHE A 582     100.371  92.316 118.527  1.00 99.99           C
ATOM   1737  CE1 PHE A 582     101.125  90.894 116.296  1.00 99.99           C
ATOM   1738  CE2 PHE A 582      99.412  91.720 117.731  1.00 99.99           C
ATOM   1739  CZ  PHE A 582      99.789  91.007 116.615  1.00 99.99           C
ATOM   1740  N   LEU A 583     101.703  95.782 119.516  1.00 78.24           N
ATOM   1741  CA  LEU A 583     100.620  96.757 119.457  1.00 78.24           C
ATOM   1742  C   LEU A 583     100.999  97.942 118.580  1.00 78.24           C
ATOM   1743  O   LEU A 583     100.159  98.475 117.846  1.00 78.24           O
ATOM   1744  CB  LEU A 583     100.253  97.236 120.863  1.00 78.24           C
ATOM   1745  CG  LEU A 583      99.666  96.184 121.807  1.00 99.99           C
ATOM   1746  CD1 LEU A 583      99.486  96.756 123.204  1.00 99.99           C
ATOM   1747  CD2 LEU A 583      98.309  95.713 121.308  1.00 99.99           C
ATOM   1748  N   CYS A 584     102.262  98.369 118.642  1.00 79.46           N
ATOM   1749  CA  CYS A 584     102.691  99.514 117.847  1.00 79.46           C
ATOM   1750  C   CYS A 584     102.885  99.167 116.375  1.00 79.46           C
ATOM   1751  O   CYS A 584     102.721 100.040 115.515  1.00 79.46           O
ATOM   1752  CB  CYS A 584     103.990 100.097 118.405  1.00 79.46           C
ATOM   1753  SG  CYS A 584     103.839 100.812 120.074  1.00 99.99           S
ATOM   1754  N   MET A 585     103.227  97.916 116.060  1.00 77.87           N
ATOM   1755  CA  MET A 585     103.655  97.574 114.708  1.00 77.87           C
ATOM   1756  C   MET A 585     102.581  96.891 113.870  1.00 77.87           C
ATOM   1757  O   MET A 585     102.488  97.167 112.668  1.00 77.87           O
ATOM   1758  CB  MET A 585     104.888  96.670 114.749  1.00 77.87           C
ATOM   1759  CG  MET A 585     104.656  95.333 115.437  1.00 99.99           C
ATOM   1760  SD  MET A 585     106.130  94.299 115.466  1.00 99.99           S
ATOM   1761  CE  MET A 585     106.184  93.740 113.764  1.00 99.99           C
ATOM   1762  N   ALA A 586     101.770  96.008 114.458  1.00 80.80           N
ATOM   1763  CA  ALA A 586     100.860  95.178 113.676  1.00 80.80           C
ATOM   1764  C   ALA A 586      99.942  96.019 112.793  1.00 80.80           C
ATOM   1765  O   ALA A 586      99.802  95.721 111.600  1.00 80.80           O
ATOM   1766  CB  ALA A 586     100.017  94.284 114.598  1.00 80.80           C
ATOM   1767  N   PRO A 587      99.299  97.070 113.322  1.00 83.27           N
ATOM   1768  CA  PRO A 587      98.415  97.877 112.467  1.00 83.27           C
ATOM   1769  C   PRO A 587      99.172  98.551 111.335  1.00 83.27           C
ATOM   1770  O   PRO A 587      98.732  98.536 110.180  1.00 83.27           O
ATOM   1771  CB  PRO A 587      97.785  98.860 113.455  1.00 83.27           C
ATOM   1772  CG  PRO A 587      97.795  98.118 114.773  1.00 83.27           C
ATOM   1773  CD  PRO A 587      99.130  97.396 114.746  1.00 83.27           C
ATOM   1774  N   ILE A 588     100.322  99.143 111.663  1.00 82.78           N
ATOM   1775  CA  ILE A 588     101.124  99.830 110.653  1.00 82.78           C
ATOM   1776  C   ILE A 588     101.614  98.839 109.606  1.00 82.78           C
ATOM   1777  O   ILE A 588     101.593  99.118 108.402  1.00 82.78           O
ATOM   1778  CB  ILE A 588     102.328 100.553 111.285  1.00 82.78           C
ATOM   1779  CG1 ILE A 588     101.852 101.678 112.206  1.00 99.99           C
ATOM   1780  CG2 ILE A 588     103.215 101.155 110.205  1.00 99.99           C
ATOM   1781  CD1 ILE A 588     102.951 102.284 113.049  1.00 99.99           C
ATOM   1782  N   SER A 589     102.077  97.668 110.051  1.00 82.91           N
ATOM   1783  CA  SER A 589     102.559  96.662 109.111  1.00 82.91           C
ATOM   1784  C   SER A 589     101.441  96.192 108.189  1.00 82.91           C
ATOM   1785  O   SER A 589     101.646  96.043 106.979  1.00 82.91           O
ATOM   1786  CB  SER A 589     103.159  95.471 109.861  1.00 82.91           C
ATOM   1787  OG  SER A 589     102.185  94.835 110.668  1.00 99.99           O
ATOM   1788  N   PHE A 590     100.251  95.951 108.743  1.00 86.15           N
ATOM   1789  CA  PHE A 590      99.126  95.519 107.919  1.00 86.15           C
ATOM   1790  C   PHE A 590      98.747  96.593 106.908  1.00 86.15           C
ATOM   1791  O   PHE A 590      98.483  96.295 105.736  1.00 86.15           O
ATOM   1792  CB  PHE A 590      97.922  95.170 108.796  1.00 86.15           C
ATOM   1793  CG  PHE A 590      96.743  94.647 108.027  1.00 99.99           C
ATOM   1794  CD1 PHE A 590      96.699  93.328 107.610  1.00 99.99           C
ATOM   1795  CD2 PHE A 590      95.677  95.473 107.720  1.00 99.99           C
ATOM   1796  CE1 PHE A 590      95.615  92.847 106.902  1.00 99.99           C
ATOM   1797  CE2 PHE A 590      94.591  94.996 107.011  1.00 99.99           C
ATOM   1798  CZ  PHE A 590      94.559  93.681 106.603  1.00 99.99           C
ATOM   1799  N   PHE A 591      98.714  97.854 107.345  1.00 86.92           N
ATOM   1800  CA  PHE A 591      98.381  98.940 106.429  1.00 86.92           C
ATOM   1801  C   PHE A 591      99.411  99.051 105.313  1.00 86.92           C
ATOM   1802  O   PHE A 591      99.055  99.239 104.144  1.00 86.92           O
ATOM   1803  CB  PHE A 591      98.277 100.266 107.185  1.00 86.92           C
ATOM   1804  CG  PHE A 591      97.868 101.425 106.323  1.00 99.99           C
ATOM   1805  CD1 PHE A 591      96.538 101.623 105.989  1.00 99.99           C
ATOM   1806  CD2 PHE A 591      98.808 102.318 105.844  1.00 99.99           C
ATOM   1807  CE1 PHE A 591      96.160 102.689 105.195  1.00 99.99           C
ATOM   1808  CE2 PHE A 591      98.434 103.385 105.049  1.00 99.99           C
ATOM   1809  CZ  PHE A 591      97.109 103.571 104.726  1.00 99.99           C
ATOM   1810  N   ALA A 592     100.697  98.938 105.655  1.00 85.10           N
ATOM   1811  CA  ALA A 592     101.740  99.014 104.638  1.00 85.10           C
ATOM   1812  C   ALA A 592     101.633  97.856 103.654  1.00 85.10           C
ATOM   1813  O   ALA A 592     101.798  98.043 102.443  1.00 85.10           O
ATOM   1814  CB  ALA A 592     103.130  99.026 105.290  1.00 85.10           C
ATOM   1815  N   ILE A 593     101.358  96.650 104.156  1.00 87.35           N
ATOM   1816  CA  ILE A 593     101.215  95.497 103.272  1.00 87.35           C
ATOM   1817  C   ILE A 593     100.035  95.696 102.330  1.00 87.35           C
ATOM   1818  O   ILE A 593     100.126  95.415 101.129  1.00 87.35           O
ATOM   1819  CB  ILE A 593     101.024  94.194 104.070  1.00 87.35           C
ATOM   1820  CG1 ILE A 593     102.279  93.880 104.887  1.00 99.99           C
ATOM   1821  CG2 ILE A 593     100.754  93.028 103.132  1.00 99.99           C
ATOM   1822  CD1 ILE A 593     102.096  92.755 105.880  1.00 99.99           C
ATOM   1823  N   SER A 594      98.910  96.183 102.857  1.00 88.29           N
ATOM   1824  CA  SER A 594      97.741  96.418 102.015  1.00 88.29           C
ATOM   1825  C   SER A 594      98.034  97.473 100.955  1.00 88.29           C
ATOM   1826  O   SER A 594      97.655  97.321  99.788  1.00 88.29           O
ATOM   1827  CB  SER A 594      96.544  96.843 102.867  1.00 88.29           C
ATOM   1828  OG  SER A 594      96.806  98.061 103.542  1.00 99.99           O
ATOM   1829  N   ALA A 595      98.710  98.556 101.345  1.00 84.68           N
ATOM   1830  CA  ALA A 595      99.021  99.619 100.395  1.00 84.68           C
ATOM   1831  C   ALA A 595      99.963  99.123  99.304  1.00 84.68           C
ATOM   1832  O   ALA A 595      99.799  99.459  98.126  1.00 84.68           O
ATOM   1833  CB  ALA A 595      99.638 100.825 101.118  1.00 84.68           C
ATOM   1834  N   SER A 596     100.961  98.321  99.681  1.00 85.29           N
ATOM   1835  CA  SER A 596     101.929  97.838  98.703  1.00 85.29           C
ATOM   1836  C   SER A 596     101.264  96.995  97.623  1.00 85.29           C
ATOM   1837  O   SER A 596     101.722  96.984  96.475  1.00 85.29           O
ATOM   1838  CB  SER A 596     103.028  97.027  99.392  1.00 85.29           C
ATOM   1839  OG  SER A 596     102.492  95.881 100.029  1.00 99.99           O
ATOM   1840  N   LEU A 597     100.189  96.288  97.965  1.00 86.78           N
ATOM   1841  CA  LEU A 597      99.478  95.441  97.017  1.00 86.78           C
ATOM   1842  C   LEU A 597      98.455  96.209  96.187  1.00 86.78           C
ATOM   1843  O   LEU A 597      97.565  95.585  95.599  1.00 86.78           O
ATOM   1844  CB  LEU A 597      98.775  94.294  97.745  1.00 86.78           C
ATOM   1845  CG  LEU A 597      99.682  93.278  98.444  1.00 99.99           C
ATOM   1846  CD1 LEU A 597      98.856  92.283  99.245  1.00 99.99           C
ATOM   1847  CD2 LEU A 597     100.502  92.502  97.426  1.00 99.99           C
ATOM   1848  N   LYS A 598      98.557  97.535  96.127  1.00 83.05           N
ATOM   1849  CA  LYS A 598      97.625  98.373  95.377  1.00 83.05           C
ATOM   1850  C   LYS A 598      96.208  98.294  95.935  1.00 83.05           C
ATOM   1851  O   LYS A 598      95.237  98.509  95.202  1.00 83.05           O
ATOM   1852  CB  LYS A 598      97.619  97.978  93.899  1.00 83.05           C
ATOM   1853  CG  LYS A 598      98.921  98.270  93.173  1.00 99.99           C
ATOM   1854  CD  LYS A 598      98.845  97.854  91.713  1.00 99.99           C
ATOM   1855  CE  LYS A 598     100.148  98.146  90.987  1.00 99.99           C
ATOM   1856  NZ  LYS A 598     100.087  97.743  89.554  1.00 99.99           N
ATOM   1857  N   VAL A 599      96.072  97.990  97.222  1.00 86.03           N
ATOM   1858  CA  VAL A 599      94.767  97.898  97.871  1.00 86.03           C
ATOM   1859  C   VAL A 599      94.809  98.703  99.164  1.00 86.03           C
ATOM   1860  O   VAL A 599      94.755  98.121 100.258  1.00 86.03           O
ATOM   1861  CB  VAL A 599      94.382  96.435  98.159  1.00 86.03           C
ATOM   1862  CG1 VAL A 599      93.080  96.371  98.943  1.00 99.99           C
ATOM   1863  CG2 VAL A 599      94.198  95.667  96.858  1.00 99.99           C
ATOM   1864  N   PRO A 600      94.903 100.030  99.095  1.00 78.96           N
ATOM   1865  CA  PRO A 600      94.947 100.834 100.325  1.00 78.96           C
ATOM   1866  C   PRO A 600      93.606 100.817 101.042  1.00 78.96           C
ATOM   1867  O   PRO A 600      92.602 101.322 100.535  1.00 78.96           O
ATOM   1868  CB  PRO A 600      95.366 102.215  99.818  1.00 78.96           C
ATOM   1869  CG  PRO A 600      96.170 101.924  98.571  1.00 78.96           C
ATOM   1870  CD  PRO A 600      95.403 100.779  97.933  1.00 78.96           C
ATOM   1871  N   LEU A 601      93.596 100.227 102.235  1.00 82.69           N
ATOM   1872  CA  LEU A 601      92.390 100.128 103.046  1.00 82.69           C
ATOM   1873  C   LEU A 601      92.195 101.322 103.971  1.00 82.69           C
ATOM   1874  O   LEU A 601      91.159 101.405 104.639  1.00 82.69           O
ATOM   1875  CB  LEU A 601      92.409  98.846 103.880  1.00 82.69           C
ATOM   1876  CG  LEU A 601      92.363  97.529 103.101  1.00 99.99           C
ATOM   1877  CD1 LEU A 601      92.535  96.344 104.039  1.00 99.99           C
ATOM   1878  CD2 LEU A 601      91.031  97.377 102.383  1.00 99.99           C
ATOM   1879  N   ILE A 602      93.156 102.243 104.028  1.00 82.80           N
ATOM   1880  CA  ILE A 602      93.067 103.418 104.884  1.00 82.80           C
ATOM   1881  C   ILE A 602      93.541 104.633 104.100  1.00 82.80           C
ATOM   1882  O   ILE A 602      94.357 104.525 103.180  1.00 82.80           O
ATOM   1883  CB  ILE A 602      93.903 103.247 106.166  1.00 82.80           C
ATOM   1884  CG1 ILE A 602      93.333 102.118 107.028  1.00 99.99           C
ATOM   1885  CG2 ILE A 602      93.894 104.530 106.983  1.00 99.99           C
ATOM   1886  CD1 ILE A 602      94.224 101.722 108.183  1.00 99.99           C
ATOM   1887  N   THR A 603      93.022 105.798 104.475  1.00 80.10           N
ATOM   1888  CA  THR A 603      93.385 107.049 103.829  1.00 80.10           C
ATOM   1889  C   THR A 603      94.759 107.509 104.299  1.00 80.10           C
ATOM   1890  O   THR A 603      95.272 107.056 105.326  1.00 80.10           O
ATOM   1891  CB  THR A 603      92.348 108.151 104.112  1.00 80.10           C
ATOM   1892  OG1 THR A 603      92.296 108.413 105.520  1.00 99.99           O
ATOM   1893  CG2 THR A 603      90.968 107.719 103.640  1.00 99.99           C
ATOM   1894  N   VAL A 604      95.357 108.420 103.528  1.00 79.00           N
ATOM   1895  CA  VAL A 604      96.680 108.928 103.874  1.00 79.00           C
ATOM   1896  C   VAL A 604      96.635 109.701 105.185  1.00 79.00           C
ATOM   1897  O   VAL A 604      97.576 109.637 105.984  1.00 79.00           O
ATOM   1898  CB  VAL A 604      97.243 109.836 102.766  1.00 79.00           C
ATOM   1899  CG1 VAL A 604      98.565 110.451 103.200  1.00 99.99           C
ATOM   1900  CG2 VAL A 604      97.480 109.038 101.492  1.00 99.99           C
ATOM   1901  N   SER A 605      95.554 110.445 105.427  1.00 79.95           N
ATOM   1902  CA  SER A 605      95.441 111.200 106.671  1.00 79.95           C
ATOM   1903  C   SER A 605      95.424 110.267 107.877  1.00 79.95           C
ATOM   1904  O   SER A 605      96.106 110.514 108.878  1.00 79.95           O
ATOM   1905  CB  SER A 605      94.183 112.070 106.658  1.00 79.95           C
ATOM   1906  OG  SER A 605      93.014 111.274 106.562  1.00 99.99           O
ATOM   1907  N   LYS A 606      94.647 109.185 107.797  1.00 84.54           N
ATOM   1908  CA  LYS A 606      94.607 108.224 108.895  1.00 84.54           C
ATOM   1909  C   LYS A 606      95.956 107.542 109.078  1.00 84.54           C
ATOM   1910  O   LYS A 606      96.399 107.323 110.212  1.00 84.54           O
ATOM   1911  CB  LYS A 606      93.517 107.178 108.653  1.00 84.54           C
ATOM   1912  CG  LYS A 606      92.103 107.733 108.701  1.00 99.99           C
ATOM   1913  CD  LYS A 606      91.073 106.643 108.453  1.00 99.99           C
ATOM   1914  CE  LYS A 606      91.141 106.135 107.021  1.00 99.99           C
ATOM   1915  NZ  LYS A 606      90.138 105.066 106.762  1.00 99.99           N
ATOM   1916  N   ALA A 607      96.617 107.189 107.973  1.00 83.93           N
ATOM   1917  CA  ALA A 607      97.920 106.540 108.068  1.00 83.93           C
ATOM   1918  C   ALA A 607      98.952 107.453 108.713  1.00 83.93           C
ATOM   1919  O   ALA A 607      99.778 106.988 109.507  1.00 83.93           O
ATOM   1920  CB  ALA A 607      98.406 106.099 106.679  1.00 83.93           C
ATOM   1921  N   LYS A 608      98.932 108.746 108.382  1.00 85.22           N
ATOM   1922  CA  LYS A 608      99.874 109.676 108.996  1.00 85.22           C
ATOM   1923  C   LYS A 608      99.667 109.751 110.503  1.00 85.22           C
ATOM   1924  O   LYS A 608     100.634 109.720 111.273  1.00 85.22           O
ATOM   1925  CB  LYS A 608      99.736 111.067 108.375  1.00 85.22           C
ATOM   1926  CG  LYS A 608     100.047 111.117 106.888  1.00 99.99           C
ATOM   1927  CD  LYS A 608     101.522 110.862 106.625  1.00 99.99           C
ATOM   1928  CE  LYS A 608     101.834 110.911 105.138  1.00 99.99           C
ATOM   1929  NZ  LYS A 608     103.278 110.662 104.864  1.00 99.99           N
ATOM   1930  N   ILE A 609      98.411 109.843 110.945  1.00 84.90           N
ATOM   1931  CA  ILE A 609      98.129 109.894 112.377  1.00 84.90           C
ATOM   1932  C   ILE A 609      98.565 108.600 113.050  1.00 84.90           C
ATOM   1933  O   ILE A 609      99.136 108.614 114.149  1.00 84.90           O
ATOM   1934  CB  ILE A 609      96.633 110.137 112.649  1.00 84.90           C
ATOM   1935  CG1 ILE A 609      96.216 111.519 112.141  1.00 99.99           C
ATOM   1936  CG2 ILE A 609      96.343 110.064 114.141  1.00 99.99           C
ATOM   1937  CD1 ILE A 609      94.722 111.748 112.150  1.00 99.99           C
ATOM   1938  N   LEU A 610      98.290 107.460 112.412  1.00 82.26           N
ATOM   1939  CA  LEU A 610      98.683 106.177 112.987  1.00 82.26           C
ATOM   1940  C   LEU A 610     100.197 106.086 113.132  1.00 82.26           C
ATOM   1941  O   LEU A 610     100.708 105.629 114.160  1.00 82.26           O
ATOM   1942  CB  LEU A 610      98.163 105.023 112.128  1.00 82.26           C
ATOM   1943  CG  LEU A 610      96.643 104.869 112.047  1.00 99.99           C
ATOM   1944  CD1 LEU A 610      96.265 103.783 111.051  1.00 99.99           C
ATOM   1945  CD2 LEU A 610      96.069 104.490 113.403  1.00 99.99           C
ATOM   1946  N   LEU A 611     100.934 106.525 112.111  1.00 78.97           N
ATOM   1947  CA  LEU A 611     102.390 106.472 112.173  1.00 78.97           C
ATOM   1948  C   LEU A 611     102.940 107.452 113.201  1.00 78.97           C
ATOM   1949  O   LEU A 611     103.967 107.180 113.833  1.00 78.97           O
ATOM   1950  CB  LEU A 611     102.996 106.762 110.799  1.00 78.97           C
ATOM   1951  CG  LEU A 611     102.699 105.741 109.697  1.00 99.99           C
ATOM   1952  CD1 LEU A 611     103.235 106.225 108.359  1.00 99.99           C
ATOM   1953  CD2 LEU A 611     103.351 104.405 110.015  1.00 99.99           C
ATOM   1954  N   VAL A 612     102.278 108.595 113.376  1.00 79.60           N
ATOM   1955  CA  VAL A 612     102.733 109.583 114.348  1.00 79.60           C
ATOM   1956  C   VAL A 612     102.497 109.096 115.772  1.00 79.60           C
ATOM   1957  O   VAL A 612     103.322 109.329 116.661  1.00 79.60           O
ATOM   1958  CB  VAL A 612     102.025 110.936 114.151  1.00 79.60           C
ATOM   1959  CG1 VAL A 612     102.422 111.911 115.249  1.00 99.99           C
ATOM   1960  CG2 VAL A 612     102.402 111.544 112.808  1.00 99.99           C
ATOM   1961  N   LEU A 613     101.370 108.428 116.018  1.00 79.48           N
ATOM   1962  CA  LEU A 613     101.002 108.045 117.379  1.00 79.48           C
ATOM   1963  C   LEU A 613     101.532 106.661 117.753  1.00 79.48           C
ATOM   1964  O   LEU A 613     102.313 106.525 118.700  1.00 79.48           O
ATOM   1965  CB  LEU A 613      99.482 108.075 117.552  1.00 79.48           C
ATOM   1966  CG  LEU A 613      98.813 109.446 117.428  1.00 99.99           C
ATOM   1967  CD1 LEU A 613      97.299 109.310 117.474  1.00 99.99           C
ATOM   1968  CD2 LEU A 613      99.243 110.358 118.566  1.00 99.99           C
ATOM   1969  N   PHE A 614     101.118 105.628 117.017  1.00 79.76           N
ATOM   1970  CA  PHE A 614     101.451 104.259 117.395  1.00 79.76           C
ATOM   1971  C   PHE A 614     102.950 103.994 117.309  1.00 79.76           C
ATOM   1972  O   PHE A 614     103.534 103.395 118.219  1.00 79.76           O
ATOM   1973  CB  PHE A 614     100.699 103.261 116.513  1.00 79.76           C
ATOM   1974  CG  PHE A 614     100.933 101.826 116.885  1.00 99.99           C
ATOM   1975  CD1 PHE A 614     100.255 101.251 117.946  1.00 99.99           C
ATOM   1976  CD2 PHE A 614     101.831 101.048 116.176  1.00 99.99           C
ATOM   1977  CE1 PHE A 614     100.470  99.930 118.290  1.00 99.99           C
ATOM   1978  CE2 PHE A 614     102.050  99.728 116.517  1.00 99.99           C
ATOM   1979  CZ  PHE A 614     101.368  99.167 117.574  1.00 99.99           C
ATOM   1980  N   HIS A 615     103.590 104.426 116.225  1.00 76.64           N
ATOM   1981  CA  HIS A 615     104.998 104.100 116.021  1.00 76.64           C
ATOM   1982  C   HIS A 615     105.903 104.635 117.122  1.00 76.64           C
ATOM   1983  O   HIS A 615     106.695 103.848 117.667  1.00 76.64           O
ATOM   1984  CB  HIS A 615     105.483 104.637 114.673  1.00 76.64           C
ATOM   1985  CG  HIS A 615     104.820 103.995 113.493  1.00 99.99           C
ATOM   1986  ND1 HIS A 615     103.591 104.398 113.020  1.00 99.99           N
ATOM   1987  CD2 HIS A 615     105.216 102.977 112.693  1.00 99.99           C
ATOM   1988  CE1 HIS A 615     103.260 103.656 111.977  1.00 99.99           C
ATOM   1989  NE2 HIS A 615     104.228 102.787 111.758  1.00 99.99           N
ATOM   1990  N   PRO A 616     105.850 105.917 117.500  1.00 77.59           N
ATOM   1991  CA  PRO A 616     106.667 106.391 118.623  1.00 77.59           C
ATOM   1992  C   PRO A 616     106.137 105.998 119.991  1.00 77.59           C
ATOM   1993  O   PRO A 616     106.868 106.146 120.980  1.00 77.59           O
ATOM   1994  CB  PRO A 616     106.694 107.906 118.413  1.00 77.59           C
ATOM   1995  CG  PRO A 616     106.531 108.076 116.919  1.00 77.59           C
ATOM   1996  CD  PRO A 616     105.517 107.003 116.564  1.00 77.59           C
ATOM   1997  N   ILE A 617     104.897 105.512 120.078  1.00 78.50           N
ATOM   1998  CA  ILE A 617     104.350 105.099 121.367  1.00 78.50           C
ATOM   1999  C   ILE A 617     105.153 103.936 121.935  1.00 78.50           C
ATOM   2000  O   ILE A 617     105.466 103.904 123.131  1.00 78.50           O
ATOM   2001  CB  ILE A 617     102.870 104.694 121.248  1.00 78.50           C
ATOM   2002  CG1 ILE A 617     102.016 105.901 120.854  1.00 99.99           C
ATOM   2003  CG2 ILE A 617     102.356 104.151 122.573  1.00 99.99           C
ATOM   2004  CD1 ILE A 617     100.593 105.549 120.483  1.00 99.99           C
ATOM   2005  N   ASN A 618     105.493 102.961 121.089  1.00 75.29           N
ATOM   2006  CA  ASN A 618     106.281 101.824 121.551  1.00 75.29           C
ATOM   2007  C   ASN A 618     107.652 102.274 122.040  1.00 75.29           C
ATOM   2008  O   ASN A 618     108.135 101.815 123.080  1.00 75.29           O
ATOM   2009  CB  ASN A 618     106.431 100.787 120.436  1.00 75.29           C
ATOM   2010  CG  ASN A 618     105.131 100.073 120.126  1.00 99.99           C
ATOM   2011  OD1 ASN A 618     104.745  99.136 120.823  1.00 99.99           O
ATOM   2012  ND2 ASN A 618     104.450 100.516 119.075  1.00 99.99           N
ATOM   2013  N   SER A 619     108.296 103.178 121.297  1.00 77.73           N
ATOM   2014  CA  SER A 619     109.599 103.680 121.719  1.00 77.73           C
ATOM   2015  C   SER A 619     109.506 104.430 123.041  1.00 77.73           C
ATOM   2016  O   SER A 619     110.376 104.274 123.905  1.00 77.73           O
ATOM   2017  CB  SER A 619     110.197 104.589 120.644  1.00 77.73           C
ATOM   2018  OG  SER A 619     109.379 105.725 120.425  1.00 99.99           O
ATOM   2019  N   CYS A 620     108.466 105.247 123.216  1.00 78.47           N
ATOM   2020  CA  CYS A 620     108.309 105.989 124.462  1.00 78.47           C
ATOM   2021  C   CYS A 620     108.039 105.054 125.634  1.00 78.47           C
ATOM   2022  O   CYS A 620     108.513 105.297 126.751  1.00 78.47           O
ATOM   2023  CB  CYS A 620     107.179 107.013 124.337  1.00 78.47           C
ATOM   2024  SG  CYS A 620     107.494 108.338 123.128  1.00 99.99           S
ATOM   2025  N   ALA A 621     107.269 103.988 125.406  1.00 77.68           N
ATOM   2026  CA  ALA A 621     106.950 103.058 126.484  1.00 77.68           C
ATOM   2027  C   ALA A 621     108.093 102.092 126.774  1.00 77.68           C
ATOM   2028  O   ALA A 621     108.133 101.500 127.859  1.00 77.68           O
ATOM   2029  CB  ALA A 621     105.679 102.262 126.152  1.00 77.68           C
ATOM   2030  N   ASN A 622     109.018 101.916 125.832  1.00 77.60           N
ATOM   2031  CA  ASN A 622     110.124 100.981 126.035  1.00 77.60           C
ATOM   2032  C   ASN A 622     110.931 101.276 127.290  1.00 77.60           C
ATOM   2033  O   ASN A 622     111.192 100.340 128.062  1.00 77.60           O
ATOM   2034  CB  ASN A 622     111.060 100.987 124.825  1.00 77.60           C
ATOM   2035  CG  ASN A 622     110.431 100.359 123.598  1.00 99.99           C
ATOM   2036  OD1 ASN A 622     110.267 101.013 122.569  1.00 99.99           O
ATOM   2037  ND2 ASN A 622     110.078  99.083 123.703  1.00 99.99           N
ATOM   2038  N   PRO A 623     111.364 102.512 127.553  1.00 73.43           N
ATOM   2039  CA  PRO A 623     112.085 102.774 128.811  1.00 73.43           C
ATOM   2040  C   PRO A 623     111.313 102.348 130.049  1.00 73.43           C
ATOM   2041  O   PRO A 623     111.823 101.562 130.858  1.00 73.43           O
ATOM   2042  CB  PRO A 623     112.342 104.281 128.753  1.00 73.43           C
ATOM   2043  CG  PRO A 623     112.402 104.589 127.273  1.00 73.43           C
ATOM   2044  CD  PRO A 623     111.309 103.706 126.698  1.00 73.43           C
ATOM   2045  N   PHE A 624     110.082 102.837 130.214  1.00 70.83           N
ATOM   2046  CA  PHE A 624     109.308 102.509 131.407  1.00 70.83           C
ATOM   2047  C   PHE A 624     109.064 101.009 131.507  1.00 70.83           C
ATOM   2048  O   PHE A 624     109.177 100.421 132.589  1.00 70.83           O
ATOM   2049  CB  PHE A 624     107.976 103.261 131.405  1.00 70.83           C
ATOM   2050  CG  PHE A 624     107.149 103.032 132.637  1.00 99.99           C
ATOM   2051  CD1 PHE A 624     107.422 103.716 133.809  1.00 99.99           C
ATOM   2052  CD2 PHE A 624     106.097 102.134 132.626  1.00 99.99           C
ATOM   2053  CE1 PHE A 624     106.661 103.505 134.944  1.00 99.99           C
ATOM   2054  CE2 PHE A 624     105.335 101.920 133.759  1.00 99.99           C
ATOM   2055  CZ  PHE A 624     105.616 102.607 134.918  1.00 99.99           C
ATOM   2056  N   LEU A 625     108.726 100.372 130.385  1.00 70.09           N
ATOM   2057  CA  LEU A 625     108.428  98.944 130.404  1.00 70.09           C
ATOM   2058  C   LEU A 625     109.657  98.125 130.784  1.00 70.09           C
ATOM   2059  O   LEU A 625     109.559  97.164 131.557  1.00 70.09           O
ATOM   2060  CB  LEU A 625     107.896  98.489 129.044  1.00 70.09           C
ATOM   2061  CG  LEU A 625     106.551  99.077 128.611  1.00 99.99           C
ATOM   2062  CD1 LEU A 625     106.215  98.658 127.188  1.00 99.99           C
ATOM   2063  CD2 LEU A 625     105.435  98.593 129.524  1.00 99.99           C
ATOM   2064  N   TYR A 626     110.825  98.491 130.254  1.00 66.96           N
ATOM   2065  CA  TYR A 626     112.004  97.641 130.394  1.00 66.96           C
ATOM   2066  C   TYR A 626     112.825  97.999 131.630  1.00 66.96           C
ATOM   2067  O   TYR A 626     113.005  97.170 132.528  1.00 66.96           O
ATOM   2068  CB  TYR A 626     112.884  97.736 129.147  1.00 66.96           C
ATOM   2069  CG  TYR A 626     113.429  99.123 128.885  1.00 99.99           C
ATOM   2070  CD1 TYR A 626     114.645  99.523 129.420  1.00 99.99           C
ATOM   2071  CD2 TYR A 626     112.722 100.027 128.102  1.00 99.99           C
ATOM   2072  CE1 TYR A 626     115.149 100.786 129.187  1.00 99.99           C
ATOM   2073  CE2 TYR A 626     113.210 101.296 127.857  1.00 99.99           C
ATOM   2074  CZ  TYR A 626     114.425 101.674 128.400  1.00 99.99           C
ATOM   2075  OH  TYR A 626     114.919 102.935 128.162  1.00 99.99           O
ATOM   2076  N   ALA A 627     113.330  99.232 131.695  1.00 67.63           N
ATOM   2077  CA  ALA A 627     114.305  99.596 132.719  1.00 67.63           C
ATOM   2078  C   ALA A 627     113.644 100.222 133.944  1.00 67.63           C
ATOM   2079  O   ALA A 627     113.884  99.787 135.075  1.00 67.63           O
ATOM   2080  CB  ALA A 627     115.352 100.563 132.148  1.00 67.63           C
ATOM   2081  N   ILE A 628     112.805 101.239 133.735  1.00 69.60           N
ATOM   2082  CA  ILE A 628     112.236 101.965 134.866  1.00 69.60           C
ATOM   2083  C   ILE A 628     111.472 101.023 135.788  1.00 69.60           C
ATOM   2084  O   ILE A 628     111.578 101.126 137.016  1.00 69.60           O
ATOM   2085  CB  ILE A 628     111.296 103.091 134.398  1.00 69.60           C
ATOM   2086  CG1 ILE A 628     112.081 104.158 133.632  1.00 99.99           C
ATOM   2087  CG2 ILE A 628     110.620 103.752 135.590  1.00 99.99           C
ATOM   2088  CD1 ILE A 628     111.207 105.175 132.933  1.00 99.99           C
ATOM   2089  N   PHE A 629     110.696 100.096 135.226  1.00 70.21           N
ATOM   2090  CA  PHE A 629     109.961  99.133 136.034  1.00 70.21           C
ATOM   2091  C   PHE A 629     110.871  98.160 136.772  1.00 70.21           C
ATOM   2092  O   PHE A 629     110.433  97.554 137.755  1.00 70.21           O
ATOM   2093  CB  PHE A 629     108.980  98.343 135.166  1.00 70.21           C
ATOM   2094  CG  PHE A 629     107.885  99.181 134.572  1.00 99.99           C
ATOM   2095  CD1 PHE A 629     106.733  99.453 135.291  1.00 99.99           C
ATOM   2096  CD2 PHE A 629     108.005  99.701 133.295  1.00 99.99           C
ATOM   2097  CE1 PHE A 629     105.726 100.225 134.745  1.00 99.99           C
ATOM   2098  CE2 PHE A 629     106.999 100.472 132.746  1.00 99.99           C
ATOM   2099  CZ  PHE A 629     105.858 100.735 133.472  1.00 99.99           C
ATOM   2100  N   THR A 630     112.114  97.994 136.327  1.00 71.33           N
ATOM   2101  CA  THR A 630     113.029  97.075 136.989  1.00 71.33           C
ATOM   2102  C   THR A 630     113.498  97.650 138.320  1.00 71.33           C
ATOM   2103  O   THR A 630     113.790  98.844 138.433  1.00 71.33           O
ATOM   2104  CB  THR A 630     114.252  96.764 136.107  1.00 71.33           C
ATOM   2105  OG1 THR A 630     114.985  97.970 135.858  1.00 99.99           O
ATOM   2106  CG2 THR A 630     113.813  96.171 134.777  1.00 99.99           C
ATOM   2107  N   LYS A 631     113.569  96.786 139.335  1.00 71.41           N
ATOM   2108  CA  LYS A 631     114.040  97.223 140.645  1.00 71.41           C
ATOM   2109  C   LYS A 631     115.502  97.651 140.590  1.00 71.41           C
ATOM   2110  O   LYS A 631     115.891  98.645 141.216  1.00 71.41           O
ATOM   2111  CB  LYS A 631     113.856  96.111 141.679  1.00 71.41           C
ATOM   2112  CG  LYS A 631     114.646  94.847 141.379  1.00 99.99           C
ATOM   2113  CD  LYS A 631     114.417  93.788 142.444  1.00 99.99           C
ATOM   2114  CE  LYS A 631     115.207  92.524 142.144  1.00 99.99           C
ATOM   2115  NZ  LYS A 631     116.677  92.761 142.206  1.00 99.99           N
ATOM   2116  N   ASN A 632     116.329  96.907 139.852  1.00 73.02           N
ATOM   2117  CA  ASN A 632     117.745  97.251 139.758  1.00 73.02           C
ATOM   2118  C   ASN A 632     117.938  98.616 139.111  1.00 73.02           C
ATOM   2119  O   ASN A 632     118.763  99.417 139.566  1.00 73.02           O
ATOM   2120  CB  ASN A 632     118.505  96.183 138.969  1.00 73.02           C
ATOM   2121  CG  ASN A 632     118.621  94.874 139.724  1.00 99.99           C
ATOM   2122  OD1 ASN A 632     118.495  94.838 140.947  1.00 99.99           O
ATOM   2123  ND2 ASN A 632     118.862  93.792 138.995  1.00 99.99           N
ATOM   2124  N   PHE A 633     117.187  98.900 138.044  1.00 74.89           N
ATOM   2125  CA  PHE A 633     117.297 100.201 137.394  1.00 74.89           C
ATOM   2126  C   PHE A 633     116.840 101.319 138.323  1.00 74.89           C
ATOM   2127  O   PHE A 633     117.443 102.398 138.348  1.00 74.89           O
ATOM   2128  CB  PHE A 633     116.481 100.224 136.100  1.00 74.89           C
ATOM   2129  CG  PHE A 633     116.599 101.509 135.332  1.00 99.99           C
ATOM   2130  CD1 PHE A 633     117.699 101.754 134.529  1.00 99.99           C
ATOM   2131  CD2 PHE A 633     115.611 102.474 135.411  1.00 99.99           C
ATOM   2132  CE1 PHE A 633     117.809 102.937 133.822  1.00 99.99           C
ATOM   2133  CE2 PHE A 633     115.718 103.658 134.707  1.00 99.99           C
ATOM   2134  CZ  PHE A 633     116.817 103.889 133.911  1.00 99.99           C
ATOM   2135  N   ARG A 634     115.772 101.084 139.089  1.00 79.74           N
ATOM   2136  CA  ARG A 634     115.319 102.089 140.046  1.00 79.74           C
ATOM   2137  C   ARG A 634     116.380 102.353 141.106  1.00 79.74           C
ATOM   2138  O   ARG A 634     116.630 103.508 141.472  1.00 79.74           O
ATOM   2139  CB  ARG A 634     114.011 101.649 140.706  1.00 79.74           C
ATOM   2140  CG  ARG A 634     112.825 101.595 139.759  1.00 99.99           C
ATOM   2141  CD  ARG A 634     111.515 101.466 140.519  1.00 99.99           C
ATOM   2142  NE  ARG A 634     111.425 100.200 141.242  1.00 99.99           N
ATOM   2143  CZ  ARG A 634     111.001  99.062 140.703  1.00 99.99           C
ATOM   2144  NH1 ARG A 634     110.627  99.028 139.431  1.00 99.99           N
ATOM   2145  NH2 ARG A 634     110.952  97.959 141.438  1.00 99.99           N
ATOM   2146  N   ARG A 635     117.014 101.294 141.613  1.00 79.14           N
ATOM   2147  CA  ARG A 635     118.072 101.467 142.604  1.00 79.14           C
ATOM   2148  C   ARG A 635     119.249 102.234 142.015  1.00 79.14           C
ATOM   2149  O   ARG A 635     119.830 103.107 142.671  1.00 79.14           O
ATOM   2150  CB  ARG A 635     118.537 100.110 143.135  1.00 79.14           C
ATOM   2151  CG  ARG A 635     117.490  99.372 143.953  1.00 99.99           C
ATOM   2152  CD  ARG A 635     118.102  98.202 144.707  1.00 99.99           C
ATOM   2153  NE  ARG A 635     118.607  97.173 143.802  1.00 99.99           N
ATOM   2154  CZ  ARG A 635     117.861  96.201 143.287  1.00 99.99           C
ATOM   2155  NH1 ARG A 635     116.572  96.124 143.585  1.00 99.99           N
ATOM   2156  NH2 ARG A 635     118.408  95.308 142.473  1.00 99.99           N
ATOM   2157  N   ASP A 636     119.619 101.916 140.772  1.00 78.69           N
ATOM   2158  CA  ASP A 636     120.715 102.629 140.123  1.00 78.69           C
ATOM   2159  C   ASP A 636     120.381 104.104 139.946  1.00 78.69           C
ATOM   2160  O   ASP A 636     121.231 104.973 140.174  1.00 78.69           O
ATOM   2161  CB  ASP A 636     121.039 101.996 138.769  1.00 78.69           C
ATOM   2162  CG  ASP A 636     122.220 102.655 138.085  1.00 99.99           C
ATOM   2163  OD1 ASP A 636     123.325 102.647 138.667  1.00 99.99           O
ATOM   2164  OD2 ASP A 636     122.041 103.179 136.964  1.00 99.99           O
ATOM   2165  N   PHE A 637     119.149 104.406 139.534  1.00 83.05           N
ATOM   2166  CA  PHE A 637     118.738 105.798 139.377  1.00 83.05           C
ATOM   2167  C   PHE A 637     118.762 106.527 140.714  1.00 83.05           C
ATOM   2168  O   PHE A 637     119.199 107.681 140.797  1.00 83.05           O
ATOM   2169  CB  PHE A 637     117.342 105.878 138.755  1.00 83.05           C
ATOM   2170  CG  PHE A 637     116.874 107.280 138.495  1.00 99.99           C
ATOM   2171  CD1 PHE A 637     117.306 107.974 137.377  1.00 99.99           C
ATOM   2172  CD2 PHE A 637     116.003 107.909 139.366  1.00 99.99           C
ATOM   2173  CE1 PHE A 637     116.876 109.265 137.137  1.00 99.99           C
ATOM   2174  CE2 PHE A 637     115.571 109.200 139.129  1.00 99.99           C
ATOM   2175  CZ  PHE A 637     116.007 109.878 138.013  1.00 99.99           C
ATOM   2176  N   PHE A 638     118.291 105.869 141.776  1.00 83.33           N
ATOM   2177  CA  PHE A 638     118.318 106.487 143.097  1.00 83.33           C
ATOM   2178  C   PHE A 638     119.748 106.762 143.544  1.00 83.33           C
ATOM   2179  O   PHE A 638     120.035 107.823 144.111  1.00 83.33           O
ATOM   2180  CB  PHE A 638     117.607 105.598 144.119  1.00 83.33           C
ATOM   2181  CG  PHE A 638     117.530 106.197 145.493  1.00 99.99           C
ATOM   2182  CD1 PHE A 638     116.569 107.148 145.797  1.00 99.99           C
ATOM   2183  CD2 PHE A 638     118.414 105.813 146.484  1.00 99.99           C
ATOM   2184  CE1 PHE A 638     116.497 107.700 147.062  1.00 99.99           C
ATOM   2185  CE2 PHE A 638     118.346 106.364 147.750  1.00 99.99           C
ATOM   2186  CZ  PHE A 638     117.386 107.307 148.039  1.00 99.99           C
ATOM   2187  N   ILE A 639     120.659 105.818 143.298  1.00 80.24           N
ATOM   2188  CA  ILE A 639     122.059 106.023 143.660  1.00 80.24           C
ATOM   2189  C   ILE A 639     122.640 107.193 142.876  1.00 80.24           C
ATOM   2190  O   ILE A 639     123.345 108.047 143.428  1.00 80.24           O
ATOM   2191  CB  ILE A 639     122.899 104.759 143.401  1.00 80.24           C
ATOM   2192  CG1 ILE A 639     122.445 103.620 144.316  1.00 99.99           C
ATOM   2193  CG2 ILE A 639     124.372 105.034 143.668  1.00 99.99           C
ATOM   2194  CD1 ILE A 639     123.049 102.278 143.968  1.00 99.99           C
ATOM   2195  N   LEU A 640     122.353 107.248 141.574  1.00 81.25           N
ATOM   2196  CA  LEU A 640     122.856 108.341 140.749  1.00 81.25           C
ATOM   2197  C   LEU A 640     122.295 109.679 141.214  1.00 81.25           C
ATOM   2198  O   LEU A 640     123.013 110.684 141.264  1.00 81.25           O
ATOM   2199  CB  LEU A 640     122.510 108.105 139.278  1.00 81.25           C
ATOM   2200  CG  LEU A 640     123.165 106.893 138.612  1.00 99.99           C
ATOM   2201  CD1 LEU A 640     122.623 106.694 137.205  1.00 99.99           C
ATOM   2202  CD2 LEU A 640     124.671 107.081 138.519  1.00 99.99           C
ATOM   2203  N   LEU A 641     121.006 109.709 141.561  1.00 81.17           N
ATOM   2204  CA  LEU A 641     120.397 110.953 142.021  1.00 81.17           C
ATOM   2205  C   LEU A 641     121.046 111.451 143.305  1.00 81.17           C
ATOM   2206  O   LEU A 641     121.129 112.665 143.527  1.00 81.17           O
ATOM   2207  CB  LEU A 641     118.894 110.767 142.235  1.00 81.17           C
ATOM   2208  CG  LEU A 641     118.063 110.463 140.985  1.00 99.99           C
ATOM   2209  CD1 LEU A 641     116.621 110.159 141.360  1.00 99.99           C
ATOM   2210  CD2 LEU A 641     118.067 111.652 140.037  1.00 99.99           C
ATOM   2211  N   SER A 642     121.511 110.537 144.160  1.00 83.06           N
ATOM   2212  CA  SER A 642     122.162 110.941 145.400  1.00 83.06           C
ATOM   2213  C   SER A 642     123.459 111.698 145.153  1.00 83.06           C
ATOM   2214  O   SER A 642     123.852 112.518 145.990  1.00 83.06           O
ATOM   2215  CB  SER A 642     122.443 109.722 146.280  1.00 83.06           C
ATOM   2216  OG  SER A 642     123.327 108.821 145.636  1.00 99.99           O
ATOM   2217  N   LYS A 643     124.129 111.445 144.033  1.00 79.41           N
ATOM   2218  CA  LYS A 643     125.378 112.127 143.716  1.00 79.41           C
ATOM   2219  C   LYS A 643     125.142 113.619 143.510  1.00 79.41           C
ATOM   2220  O   LYS A 643     124.410 114.022 142.607  1.00 79.41           O
ATOM   2221  CB  LYS A 643     126.023 111.514 142.472  1.00 79.41           C
ATOM   2222  CG  LYS A 643     126.512 110.088 142.664  1.00 99.99           C
ATOM   2223  CD  LYS A 643     127.140 109.542 141.392  1.00 99.99           C
ATOM   2224  CE  LYS A 643     126.097 109.351 140.301  1.00 99.99           C
ATOM   2225  NZ  LYS A 643     125.097 108.309 140.665  1.00 99.99           N
ATOM      1  C   UNL     1     117.668  90.555 111.380  1.00  0.00           C
ATOM      2  C   UNL     1     116.379  91.132 112.015  1.00  0.00           C
ATOM      3  C   UNL     1     115.578  89.918 112.561  1.00  0.00           C
ATOM      4  C   UNL     1     116.664  88.857 112.771  1.00  0.00           C
ATOM      5  C   UNL     1     116.185  87.416 112.787  1.00  0.00           C
ATOM      6  C   UNL     1     115.278  87.191 114.002  1.00  0.00           C
ATOM      7  C   UNL     1     114.949  85.732 114.110  1.00  0.00           C
ATOM      8  C   UNL     1     115.720  84.794 113.645  1.00  0.00           C
ATOM      9  C   UNL     1     117.016  85.053 112.936  1.00  0.00           C
ATOM     10  C   UNL     1     116.863  84.604 111.482  1.00  0.00           C
ATOM     11  C   UNL     1     118.121  84.202 113.569  1.00  0.00           C
ATOM     12  C   UNL     1     117.693  82.734 113.573  1.00  0.00           C
ATOM     13  C   UNL     1     116.444  82.565 114.440  1.00  0.00           C
ATOM     14  C   UNL     1     115.283  83.349 113.821  1.00  0.00           C
ATOM     15  C   UNL     1     117.420  86.518 112.939  1.00  0.00           C
ATOM     16  C   UNL     1     118.447  86.772 111.839  1.00  0.00           C
ATOM     17  C   UNL     1     118.830  88.257 111.749  1.00  0.00           C
ATOM     18  C   UNL     1     117.549  89.034 111.509  1.00  0.00           C
ATOM     19  C   UNL     1     116.823  88.478 110.281  1.00  0.00           C
ATOM     20  O   UNL     1     116.097  81.180 114.512  1.00  0.00           O
ATOM     21  H   UNL     1     115.318  81.012 113.959  1.00  0.00           H
ATOM     22  C   UNL     1     119.217  91.304 109.569  1.00  0.00           C
ATOM     23  C   UNL     1     117.764  90.966 109.910  1.00  0.00           C
ATOM     24  C   UNL     1     116.884  92.193 109.664  1.00  0.00           C
ATOM     25  C   UNL     1     115.614  91.769 108.923  1.00  0.00           C
ATOM     26  C   UNL     1     114.477  92.735 109.265  1.00  0.00           C
ATOM     27  C   UNL     1     114.979  94.175 109.139  1.00  0.00           C
ATOM     28  C   UNL     1     114.462  95.000 110.321  1.00  0.00           C
ATOM     29  C   UNL     1     114.465  94.782 107.832  1.00  0.00           C



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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.