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*** CELL CYCLE 20-JAN-12 3VO9 ***elNémo ID: 260913204707142289Job options:ID = 260913204707142289 JOBID = CELL CYCLE 20-JAN-12 3VO9 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 CELL CYCLE 20-JAN-12 3VO9 TITLE STAPHYLOCOCCUS AUREUS FTSZ APO-FORM (SEMET) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CELL DIVISION PROTEIN FTSZ; COMPND 3 CHAIN: A, B, C, D; COMPND 4 FRAGMENT: UNP RESIDUES 12-316; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 158878; SOURCE 4 STRAIN: MU50; SOURCE 5 GENE: FTSZ; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET KEYWDS FTSZ, GTP-BINDING, TUBULIN HOMOLOG, POLYMERIZATION, GTPASE, CELL KEYWDS 2 DIVISION, CELL CYCLE EXPDTA X-RAY DIFFRACTION AUTHOR T.MATSUI,J.YAMANE,N.MOGI,M.YAO,I.TANAKA REVDAT 3 06-NOV-24 3VO9 1 SEQADV LINK REVDAT 2 14-AUG-13 3VO9 1 JRNL REVDAT 1 29-AUG-12 3VO9 0 JRNL AUTH T.MATSUI,J.YAMANE,N.MOGI,H.YAMAGUCHI,H.TAKEMOTO,M.YAO, JRNL AUTH 2 I.TANAKA JRNL TITL STRUCTURAL REORGANIZATION OF THE BACTERIAL CELL-DIVISION JRNL TITL 2 PROTEIN FTSZ FROM STAPHYLOCOCCUS AUREUS JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 68 1175 2012 JRNL REFN ISSN 0907-4449 JRNL PMID 22948918 JRNL DOI 10.1107/S0907444912022640 REMARK 2 REMARK 2 RESOLUTION. 2.71 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.7.2_869 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 35582 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.229 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.560 REMARK 3 FREE R VALUE TEST SET COUNT : 1621 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 31.7667 - 6.1808 0.96 3012 146 0.1952 0.2298 REMARK 3 2 6.1808 - 4.9117 1.00 2966 143 0.2243 0.2997 REMARK 3 3 4.9117 - 4.2925 1.00 2959 144 0.1762 0.2009 REMARK 3 4 4.2925 - 3.9008 1.00 2917 137 0.2011 0.2508 REMARK 3 5 3.9008 - 3.6217 1.00 2903 141 0.2085 0.2688 REMARK 3 6 3.6217 - 3.4084 1.00 2921 141 0.2199 0.2614 REMARK 3 7 3.4084 - 3.2379 1.00 2892 139 0.2461 0.2884 REMARK 3 8 3.2379 - 3.0971 1.00 2885 140 0.2585 0.3118 REMARK 3 9 3.0971 - 2.9779 0.99 2847 137 0.2705 0.3363 REMARK 3 10 2.9779 - 2.8752 0.93 2691 129 0.3260 0.3358 REMARK 3 11 2.8752 - 2.7854 0.88 2519 116 0.3389 0.3916 REMARK 3 12 2.7854 - 2.7058 0.85 2449 108 0.3608 0.3739 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.20 REMARK 3 SHRINKAGE RADIUS : 0.98 REMARK 3 K_SOL : 0.32 REMARK 3 B_SOL : 21.14 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.870 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.150 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 47.33 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.38930 REMARK 3 B22 (A**2) : 9.49030 REMARK 3 B33 (A**2) : -9.10100 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.012 8503 REMARK 3 ANGLE : 1.246 11480 REMARK 3 CHIRALITY : 0.075 1403 REMARK 3 PLANARITY : 0.005 1523 REMARK 3 DIHEDRAL : 17.881 3104 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3VO9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-12. REMARK 100 THE DEPOSITION ID IS D_1000095293. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36669 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.706 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 14.30 REMARK 200 R MERGE (I) : 0.12300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.48500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELX, RESOLVE 2.15, PHENIX 1.7.2_869 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM CHLORIDE, 0.1M SODIUM REMARK 280 ACETATE, 30% PEG 6000, 0.34M SODIUM MALONATE, PH 7.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.34600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.85900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.99350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.85900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.34600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.99350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D 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 GLY A 9 REMARK 465 HIS A 10 REMARK 465 MSE A 11 REMARK 465 HIS A 33 REMARK 465 GLY A 34 REMARK 465 MSE A 35 REMARK 465 ASN A 36 REMARK 465 GLY A 140 REMARK 465 ARG A 141 REMARK 465 LYS A 142 REMARK 465 ARG A 143 REMARK 465 GLN A 144 REMARK 465 ASP A 316 REMARK 465 GLY B 9 REMARK 465 HIS B 10 REMARK 465 MSE B 11 REMARK 465 HIS B 33 REMARK 465 GLY B 34 REMARK 465 MSE B 35 REMARK 465 ASN B 36 REMARK 465 SER B 137 REMARK 465 PHE B 138 REMARK 465 GLU B 139 REMARK 465 GLY B 140 REMARK 465 ARG B 141 REMARK 465 LYS B 142 REMARK 465 ARG B 143 REMARK 465 GLN B 144 REMARK 465 ASP B 316 REMARK 465 GLY C 9 REMARK 465 HIS C 10 REMARK 465 MSE C 11 REMARK 465 HIS C 33 REMARK 465 GLY C 34 REMARK 465 MSE C 35 REMARK 465 ASP C 316 REMARK 465 GLY D 9 REMARK 465 HIS D 10 REMARK 465 MSE D 11 REMARK 465 ALA D 12 REMARK 465 GLY D 34 REMARK 465 MSE D 35 REMARK 465 ASN D 36 REMARK 465 ASN D 37 REMARK 465 LEU D 69 REMARK 465 GLY D 70 REMARK 465 ALA D 71 REMARK 465 GLY D 72 REMARK 465 SER D 137 REMARK 465 PHE D 138 REMARK 465 GLU D 139 REMARK 465 GLY D 140 REMARK 465 ARG D 141 REMARK 465 LYS D 142 REMARK 465 ARG D 143 REMARK 465 GLN D 144 REMARK 465 ASP D 316 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 GLN A 195 19.79 56.97 REMARK 500 GLU A 301 0.12 -62.57 REMARK 500 GLN A 303 -113.33 61.02 REMARK 500 GLN B 146 -46.48 69.10 REMARK 500 LEU B 169 -37.41 -37.72 REMARK 500 LYS B 175 44.46 -104.61 REMARK 500 GLU B 206 70.89 -100.06 REMARK 500 ASN B 208 58.34 -94.80 REMARK 500 GLN B 221 97.70 -169.72 REMARK 500 ASN B 291 94.89 -61.50 REMARK 500 GLN B 303 -115.46 53.89 REMARK 500 ARG C 67 125.16 -37.63 REMARK 500 GLN C 94 105.53 -43.35 REMARK 500 SER C 137 145.55 -176.12 REMARK 500 ASP C 159 -71.19 -67.54 REMARK 500 MSE C 218 32.74 -92.72 REMARK 500 GLN C 303 -117.52 55.94 REMARK 500 SER D 85 35.26 -84.43 REMARK 500 GLU D 90 -72.01 -45.44 REMARK 500 ARG D 168 1.71 -66.23 REMARK 500 LYS D 175 49.04 -85.72 REMARK 500 GLU D 206 43.39 -67.48 REMARK 500 ASN D 220 -80.47 -68.60 REMARK 500 GLN D 303 -121.69 59.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3VO8 RELATED DB: PDB REMARK 900 RELATED ID: 3VOA RELATED DB: PDB REMARK 900 RELATED ID: 3VOB RELATED DB: PDB DBREF 3VO9 A 12 316 UNP P0A029 FTSZ_STAAM 12 316 DBREF 3VO9 B 12 316 UNP P0A029 FTSZ_STAAM 12 316 DBREF 3VO9 C 12 316 UNP P0A029 FTSZ_STAAM 12 316 DBREF 3VO9 D 12 316 UNP P0A029 FTSZ_STAAM 12 316 SEQADV 3VO9 GLY A 9 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 HIS A 10 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 MSE A 11 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 GLY B 9 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 HIS B 10 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 MSE B 11 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 GLY C 9 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 HIS C 10 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 MSE C 11 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 GLY D 9 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 HIS D 10 UNP P0A029 EXPRESSION TAG SEQADV 3VO9 MSE D 11 UNP P0A029 EXPRESSION TAG SEQRES 1 A 308 GLY HIS MSE ALA THR LEU LYS VAL ILE GLY VAL GLY GLY SEQRES 2 A 308 GLY GLY ASN ASN ALA VAL ASN ARG MSE ILE ASP HIS GLY SEQRES 3 A 308 MSE ASN ASN VAL GLU PHE ILE ALA ILE ASN THR ASP GLY SEQRES 4 A 308 GLN ALA LEU ASN LEU SER LYS ALA GLU SER LYS ILE GLN SEQRES 5 A 308 ILE GLY GLU LYS LEU THR ARG GLY LEU GLY ALA GLY ALA SEQRES 6 A 308 ASN PRO GLU ILE GLY LYS LYS ALA ALA GLU GLU SER ARG SEQRES 7 A 308 GLU GLN ILE GLU ASP ALA ILE GLN GLY ALA ASP MSE VAL SEQRES 8 A 308 PHE VAL THR SER GLY MSE GLY GLY GLY THR GLY THR GLY SEQRES 9 A 308 ALA ALA PRO VAL VAL ALA LYS ILE ALA LYS GLU MSE GLY SEQRES 10 A 308 ALA LEU THR VAL GLY VAL VAL THR ARG PRO PHE SER PHE SEQRES 11 A 308 GLU GLY ARG LYS ARG GLN THR GLN ALA ALA ALA GLY VAL SEQRES 12 A 308 GLU ALA MSE LYS ALA ALA VAL ASP THR LEU ILE VAL ILE SEQRES 13 A 308 PRO ASN ASP ARG LEU LEU ASP ILE VAL ASP LYS SER THR SEQRES 14 A 308 PRO MSE MSE GLU ALA PHE LYS GLU ALA ASP ASN VAL LEU SEQRES 15 A 308 ARG GLN GLY VAL GLN GLY ILE SER ASP LEU ILE ALA VAL SEQRES 16 A 308 SER GLY GLU VAL ASN LEU ASP PHE ALA ASP VAL LYS THR SEQRES 17 A 308 ILE MSE SER ASN GLN GLY SER ALA LEU MSE GLY ILE GLY SEQRES 18 A 308 VAL SER SER GLY GLU ASN ARG ALA VAL GLU ALA ALA LYS SEQRES 19 A 308 LYS ALA ILE SER SER PRO LEU LEU GLU THR SER ILE VAL SEQRES 20 A 308 GLY ALA GLN GLY VAL LEU MSE ASN ILE THR GLY GLY GLU SEQRES 21 A 308 SER LEU SER LEU PHE GLU ALA GLN GLU ALA ALA ASP ILE SEQRES 22 A 308 VAL GLN ASP ALA ALA ASP GLU ASP VAL ASN MSE ILE PHE SEQRES 23 A 308 GLY THR VAL ILE ASN PRO GLU LEU GLN ASP GLU ILE VAL SEQRES 24 A 308 VAL THR VAL ILE ALA THR GLY PHE ASP SEQRES 1 B 308 GLY HIS MSE ALA THR LEU LYS VAL ILE GLY VAL GLY GLY SEQRES 2 B 308 GLY GLY ASN ASN ALA VAL ASN ARG MSE ILE ASP HIS GLY SEQRES 3 B 308 MSE ASN ASN VAL GLU PHE ILE ALA ILE ASN THR ASP GLY SEQRES 4 B 308 GLN ALA LEU ASN LEU SER LYS ALA GLU SER LYS ILE GLN SEQRES 5 B 308 ILE GLY GLU LYS LEU THR ARG GLY LEU GLY ALA GLY ALA SEQRES 6 B 308 ASN PRO GLU ILE GLY LYS LYS ALA ALA GLU GLU SER ARG SEQRES 7 B 308 GLU GLN ILE GLU ASP ALA ILE GLN GLY ALA ASP MSE VAL SEQRES 8 B 308 PHE VAL THR SER GLY MSE GLY GLY GLY THR GLY THR GLY SEQRES 9 B 308 ALA ALA PRO VAL VAL ALA LYS ILE ALA LYS GLU MSE GLY SEQRES 10 B 308 ALA LEU THR VAL GLY VAL VAL THR ARG PRO PHE SER PHE SEQRES 11 B 308 GLU GLY ARG LYS ARG GLN THR GLN ALA ALA ALA GLY VAL SEQRES 12 B 308 GLU ALA MSE LYS ALA ALA VAL ASP THR LEU ILE VAL ILE SEQRES 13 B 308 PRO ASN ASP ARG LEU LEU ASP ILE VAL ASP LYS SER THR SEQRES 14 B 308 PRO MSE MSE GLU ALA PHE LYS GLU ALA ASP ASN VAL LEU SEQRES 15 B 308 ARG GLN GLY VAL GLN GLY ILE SER ASP LEU ILE ALA VAL SEQRES 16 B 308 SER GLY GLU VAL ASN LEU ASP PHE ALA ASP VAL LYS THR SEQRES 17 B 308 ILE MSE SER ASN GLN GLY SER ALA LEU MSE GLY ILE GLY SEQRES 18 B 308 VAL SER SER GLY GLU ASN ARG ALA VAL GLU ALA ALA LYS SEQRES 19 B 308 LYS ALA ILE SER SER PRO LEU LEU GLU THR SER ILE VAL SEQRES 20 B 308 GLY ALA GLN GLY VAL LEU MSE ASN ILE THR GLY GLY GLU SEQRES 21 B 308 SER LEU SER LEU PHE GLU ALA GLN GLU ALA ALA ASP ILE SEQRES 22 B 308 VAL GLN ASP ALA ALA ASP GLU ASP VAL ASN MSE ILE PHE SEQRES 23 B 308 GLY THR VAL ILE ASN PRO GLU LEU GLN ASP GLU ILE VAL SEQRES 24 B 308 VAL THR VAL ILE ALA THR GLY PHE ASP SEQRES 1 C 308 GLY HIS MSE ALA THR LEU LYS VAL ILE GLY VAL GLY GLY SEQRES 2 C 308 GLY GLY ASN ASN ALA VAL ASN ARG MSE ILE ASP HIS GLY SEQRES 3 C 308 MSE ASN ASN VAL GLU PHE ILE ALA ILE ASN THR ASP GLY SEQRES 4 C 308 GLN ALA LEU ASN LEU SER LYS ALA GLU SER LYS ILE GLN SEQRES 5 C 308 ILE GLY GLU LYS LEU THR ARG GLY LEU GLY ALA GLY ALA SEQRES 6 C 308 ASN PRO GLU ILE GLY LYS LYS ALA ALA GLU GLU SER ARG SEQRES 7 C 308 GLU GLN ILE GLU ASP ALA ILE GLN GLY ALA ASP MSE VAL SEQRES 8 C 308 PHE VAL THR SER GLY MSE GLY GLY GLY THR GLY THR GLY SEQRES 9 C 308 ALA ALA PRO VAL VAL ALA LYS ILE ALA LYS GLU MSE GLY SEQRES 10 C 308 ALA LEU THR VAL GLY VAL VAL THR ARG PRO PHE SER PHE SEQRES 11 C 308 GLU GLY ARG LYS ARG GLN THR GLN ALA ALA ALA GLY VAL SEQRES 12 C 308 GLU ALA MSE LYS ALA ALA VAL ASP THR LEU ILE VAL ILE SEQRES 13 C 308 PRO ASN ASP ARG LEU LEU ASP ILE VAL ASP LYS SER THR SEQRES 14 C 308 PRO MSE MSE GLU ALA PHE LYS GLU ALA ASP ASN VAL LEU SEQRES 15 C 308 ARG GLN GLY VAL GLN GLY ILE SER ASP LEU ILE ALA VAL SEQRES 16 C 308 SER GLY GLU VAL ASN LEU ASP PHE ALA ASP VAL LYS THR SEQRES 17 C 308 ILE MSE SER ASN GLN GLY SER ALA LEU MSE GLY ILE GLY SEQRES 18 C 308 VAL SER SER GLY GLU ASN ARG ALA VAL GLU ALA ALA LYS SEQRES 19 C 308 LYS ALA ILE SER SER PRO LEU LEU GLU THR SER ILE VAL SEQRES 20 C 308 GLY ALA GLN GLY VAL LEU MSE ASN ILE THR GLY GLY GLU SEQRES 21 C 308 SER LEU SER LEU PHE GLU ALA GLN GLU ALA ALA ASP ILE SEQRES 22 C 308 VAL GLN ASP ALA ALA ASP GLU ASP VAL ASN MSE ILE PHE SEQRES 23 C 308 GLY THR VAL ILE ASN PRO GLU LEU GLN ASP GLU ILE VAL SEQRES 24 C 308 VAL THR VAL ILE ALA THR GLY PHE ASP SEQRES 1 D 308 GLY HIS MSE ALA THR LEU LYS VAL ILE GLY VAL GLY GLY SEQRES 2 D 308 GLY GLY ASN ASN ALA VAL ASN ARG MSE ILE ASP HIS GLY SEQRES 3 D 308 MSE ASN ASN VAL GLU PHE ILE ALA ILE ASN THR ASP GLY SEQRES 4 D 308 GLN ALA LEU ASN LEU SER LYS ALA GLU SER LYS ILE GLN SEQRES 5 D 308 ILE GLY GLU LYS LEU THR ARG GLY LEU GLY ALA GLY ALA SEQRES 6 D 308 ASN PRO GLU ILE GLY LYS LYS ALA ALA GLU GLU SER ARG SEQRES 7 D 308 GLU GLN ILE GLU ASP ALA ILE GLN GLY ALA ASP MSE VAL SEQRES 8 D 308 PHE VAL THR SER GLY MSE GLY GLY GLY THR GLY THR GLY SEQRES 9 D 308 ALA ALA PRO VAL VAL ALA LYS ILE ALA LYS GLU MSE GLY SEQRES 10 D 308 ALA LEU THR VAL GLY VAL VAL THR ARG PRO PHE SER PHE SEQRES 11 D 308 GLU GLY ARG LYS ARG GLN THR GLN ALA ALA ALA GLY VAL SEQRES 12 D 308 GLU ALA MSE LYS ALA ALA VAL ASP THR LEU ILE VAL ILE SEQRES 13 D 308 PRO ASN ASP ARG LEU LEU ASP ILE VAL ASP LYS SER THR SEQRES 14 D 308 PRO MSE MSE GLU ALA PHE LYS GLU ALA ASP ASN VAL LEU SEQRES 15 D 308 ARG GLN GLY VAL GLN GLY ILE SER ASP LEU ILE ALA VAL SEQRES 16 D 308 SER GLY GLU VAL ASN LEU ASP PHE ALA ASP VAL LYS THR SEQRES 17 D 308 ILE MSE SER ASN GLN GLY SER ALA LEU MSE GLY ILE GLY SEQRES 18 D 308 VAL SER SER GLY GLU ASN ARG ALA VAL GLU ALA ALA LYS SEQRES 19 D 308 LYS ALA ILE SER SER PRO LEU LEU GLU THR SER ILE VAL SEQRES 20 D 308 GLY ALA GLN GLY VAL LEU MSE ASN ILE THR GLY GLY GLU SEQRES 21 D 308 SER LEU SER LEU PHE GLU ALA GLN GLU ALA ALA ASP ILE SEQRES 22 D 308 VAL GLN ASP ALA ALA ASP GLU ASP VAL ASN MSE ILE PHE SEQRES 23 D 308 GLY THR VAL ILE ASN PRO GLU LEU GLN ASP GLU ILE VAL SEQRES 24 D 308 VAL THR VAL ILE ALA THR GLY PHE ASP MODRES 3VO9 MSE A 30 MET SELENOMETHIONINE MODRES 3VO9 MSE A 98 MET SELENOMETHIONINE MODRES 3VO9 MSE A 105 MET SELENOMETHIONINE MODRES 3VO9 MSE A 124 MET SELENOMETHIONINE MODRES 3VO9 MSE A 154 MET SELENOMETHIONINE MODRES 3VO9 MSE A 179 MET SELENOMETHIONINE MODRES 3VO9 MSE A 180 MET SELENOMETHIONINE MODRES 3VO9 MSE A 218 MET SELENOMETHIONINE MODRES 3VO9 MSE A 226 MET SELENOMETHIONINE MODRES 3VO9 MSE A 262 MET SELENOMETHIONINE MODRES 3VO9 MSE A 292 MET SELENOMETHIONINE MODRES 3VO9 MSE B 30 MET SELENOMETHIONINE MODRES 3VO9 MSE B 98 MET SELENOMETHIONINE MODRES 3VO9 MSE B 105 MET SELENOMETHIONINE MODRES 3VO9 MSE B 124 MET SELENOMETHIONINE MODRES 3VO9 MSE B 154 MET SELENOMETHIONINE MODRES 3VO9 MSE B 179 MET SELENOMETHIONINE MODRES 3VO9 MSE B 180 MET SELENOMETHIONINE MODRES 3VO9 MSE B 218 MET SELENOMETHIONINE MODRES 3VO9 MSE B 226 MET SELENOMETHIONINE MODRES 3VO9 MSE B 262 MET SELENOMETHIONINE MODRES 3VO9 MSE B 292 MET SELENOMETHIONINE MODRES 3VO9 MSE C 30 MET SELENOMETHIONINE MODRES 3VO9 MSE C 98 MET SELENOMETHIONINE MODRES 3VO9 MSE C 105 MET SELENOMETHIONINE MODRES 3VO9 MSE C 124 MET SELENOMETHIONINE MODRES 3VO9 MSE C 154 MET SELENOMETHIONINE MODRES 3VO9 MSE C 179 MET SELENOMETHIONINE MODRES 3VO9 MSE C 180 MET SELENOMETHIONINE MODRES 3VO9 MSE C 218 MET SELENOMETHIONINE MODRES 3VO9 MSE C 226 MET SELENOMETHIONINE MODRES 3VO9 MSE C 262 MET SELENOMETHIONINE MODRES 3VO9 MSE C 292 MET SELENOMETHIONINE MODRES 3VO9 MSE D 30 MET SELENOMETHIONINE MODRES 3VO9 MSE D 98 MET SELENOMETHIONINE MODRES 3VO9 MSE D 105 MET SELENOMETHIONINE MODRES 3VO9 MSE D 124 MET SELENOMETHIONINE MODRES 3VO9 MSE D 154 MET SELENOMETHIONINE MODRES 3VO9 MSE D 179 MET SELENOMETHIONINE MODRES 3VO9 MSE D 180 MET SELENOMETHIONINE MODRES 3VO9 MSE D 218 MET SELENOMETHIONINE MODRES 3VO9 MSE D 226 MET SELENOMETHIONINE MODRES 3VO9 MSE D 262 MET SELENOMETHIONINE MODRES 3VO9 MSE D 292 MET SELENOMETHIONINE HET MSE A 30 8 HET MSE A 98 8 HET MSE A 105 8 HET MSE A 124 8 HET MSE A 154 8 HET MSE A 179 8 HET MSE A 180 8 HET MSE A 218 8 HET MSE A 226 8 HET MSE A 262 8 HET MSE A 292 8 HET MSE B 30 8 HET MSE B 98 8 HET MSE B 105 8 HET MSE B 124 8 HET MSE B 154 8 HET MSE B 179 8 HET MSE B 180 8 HET MSE B 218 8 HET MSE B 226 8 HET MSE B 262 8 HET MSE B 292 8 HET MSE C 30 8 HET MSE C 98 8 HET MSE C 105 8 HET MSE C 124 8 HET MSE C 154 8 HET MSE C 179 8 HET MSE C 180 8 HET MSE C 218 8 HET MSE C 226 8 HET MSE C 262 8 HET MSE C 292 8 HET MSE D 30 8 HET MSE D 98 8 HET MSE D 105 8 HET MSE D 124 8 HET MSE D 154 8 HET MSE D 179 8 HET MSE D 180 8 HET MSE D 218 8 HET MSE D 226 8 HET MSE D 262 8 HET MSE D 292 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE 44(C5 H11 N O2 SE) FORMUL 5 HOH *77(H2 O) HELIX 1 1 GLY A 20 ASP A 32 1 13 HELIX 2 2 GLN A 48 LEU A 52 1 5 HELIX 3 3 GLY A 62 ARG A 67 1 6 HELIX 4 4 ASN A 74 GLN A 94 1 21 HELIX 5 5 THR A 109 GLY A 125 1 17 HELIX 6 6 GLN A 146 VAL A 158 1 13 HELIX 7 7 PRO A 165 ILE A 197 1 33 HELIX 8 8 PHE A 211 THR A 216 1 6 HELIX 9 9 ASN A 235 ILE A 245 1 11 HELIX 10 10 SER A 247 ALA A 257 1 11 HELIX 11 11 SER A 271 ALA A 286 1 16 HELIX 12 12 PRO A 300 GLN A 303 1 4 SHEET 1 1 1 LEU A 14 VAL A 19 0 SHEET 2 2 1 GLU A 39 ASN A 44 0 SHEET 3 3 1 SER A 57 GLN A 60 0 SHEET 4 4 1 MSE A 98 THR A 102 0 SHEET 5 5 1 LEU A 127 VAL A 132 0 SHEET 6 6 1 THR A 160 VAL A 163 0 SHEET 7 7 1 ASP A 199 VAL A 203 0 SHEET 8 8 1 SER A 223 SER A 232 0 SHEET 9 9 1 GLY A 259 GLY A 266 0 SHEET 10 10 1 ASN A 291 ILE A 298 0 SHEET 11 11 1 GLU A 305 THR A 313 0 LINK C ARG A 29 N MSE A 30 1555 1555 1.33 LINK C MSE A 30 N ILE A 31 1555 1555 1.33 LINK C ASP A 97 N MSE A 98 1555 1555 1.32 LINK C MSE A 98 N VAL A 99 1555 1555 1.32 LINK C GLY A 104 N MSE A 105 1555 1555 1.33 LINK C MSE A 105 N GLY A 106 1555 1555 1.33 LINK C GLU A 123 N MSE A 124 1555 1555 1.33 LINK C MSE A 124 N GLY A 125 1555 1555 1.33 LINK C ALA A 153 N MSE A 154 1555 1555 1.33 LINK C MSE A 154 N LYS A 155 1555 1555 1.33 LINK C PRO A 178 N MSE A 179 1555 1555 1.32 LINK C MSE A 179 N MSE A 180 1555 1555 1.33 LINK C MSE A 180 N GLU A 181 1555 1555 1.34 LINK C ILE A 217 N MSE A 218 1555 1555 1.33 LINK C MSE A 218 N SER A 219 1555 1555 1.32 LINK C LEU A 225 N MSE A 226 1555 1555 1.33 LINK C MSE A 226 N GLY A 227 1555 1555 1.33 LINK C LEU A 261 N MSE A 262 1555 1555 1.32 LINK C MSE A 262 N ASN A 263 1555 1555 1.32 LINK C ASN A 291 N MSE A 292 1555 1555 1.33 LINK C MSE A 292 N ILE A 293 1555 1555 1.33 LINK C ARG B 29 N MSE B 30 1555 1555 1.34 LINK C MSE B 30 N ILE B 31 1555 1555 1.33 LINK C ASP B 97 N MSE B 98 1555 1555 1.32 LINK C MSE B 98 N VAL B 99 1555 1555 1.32 LINK C GLY B 104 N MSE B 105 1555 1555 1.33 LINK C MSE B 105 N GLY B 106 1555 1555 1.32 LINK C GLU B 123 N MSE B 124 1555 1555 1.34 LINK C MSE B 124 N GLY B 125 1555 1555 1.33 LINK C ALA B 153 N MSE B 154 1555 1555 1.33 LINK C MSE B 154 N LYS B 155 1555 1555 1.33 LINK C PRO B 178 N MSE B 179 1555 1555 1.33 LINK C MSE B 179 N MSE B 180 1555 1555 1.33 LINK C MSE B 180 N GLU B 181 1555 1555 1.33 LINK C ILE B 217 N MSE B 218 1555 1555 1.32 LINK C MSE B 218 N SER B 219 1555 1555 1.33 LINK C LEU B 225 N MSE B 226 1555 1555 1.33 LINK C MSE B 226 N GLY B 227 1555 1555 1.33 LINK C LEU B 261 N MSE B 262 1555 1555 1.33 LINK C MSE B 262 N ASN B 263 1555 1555 1.32 LINK C ASN B 291 N MSE B 292 1555 1555 1.33 LINK C MSE B 292 N ILE B 293 1555 1555 1.33 LINK C ARG C 29 N MSE C 30 1555 1555 1.33 LINK C MSE C 30 N ILE C 31 1555 1555 1.33 LINK C ASP C 97 N MSE C 98 1555 1555 1.33 LINK C MSE C 98 N VAL C 99 1555 1555 1.33 LINK C GLY C 104 N MSE C 105 1555 1555 1.33 LINK C MSE C 105 N GLY C 106 1555 1555 1.33 LINK C GLU C 123 N MSE C 124 1555 1555 1.33 LINK C MSE C 124 N GLY C 125 1555 1555 1.33 LINK C ALA C 153 N MSE C 154 1555 1555 1.33 LINK C MSE C 154 N LYS C 155 1555 1555 1.33 LINK C PRO C 178 N MSE C 179 1555 1555 1.32 LINK C MSE C 179 N MSE C 180 1555 1555 1.32 LINK C MSE C 180 N GLU C 181 1555 1555 1.33 LINK C ILE C 217 N MSE C 218 1555 1555 1.34 LINK C MSE C 218 N SER C 219 1555 1555 1.34 LINK C LEU C 225 N MSE C 226 1555 1555 1.33 LINK C MSE C 226 N GLY C 227 1555 1555 1.33 LINK C LEU C 261 N MSE C 262 1555 1555 1.32 LINK C MSE C 262 N ASN C 263 1555 1555 1.32 LINK C ASN C 291 N MSE C 292 1555 1555 1.33 LINK C MSE C 292 N ILE C 293 1555 1555 1.33 LINK C ARG D 29 N MSE D 30 1555 1555 1.34 LINK C MSE D 30 N ILE D 31 1555 1555 1.34 LINK C ASP D 97 N MSE D 98 1555 1555 1.33 LINK C MSE D 98 N VAL D 99 1555 1555 1.34 LINK C GLY D 104 N MSE D 105 1555 1555 1.33 LINK C MSE D 105 N GLY D 106 1555 1555 1.33 LINK C GLU D 123 N MSE D 124 1555 1555 1.34 LINK C MSE D 124 N GLY D 125 1555 1555 1.33 LINK C ALA D 153 N MSE D 154 1555 1555 1.34 LINK C MSE D 154 N LYS D 155 1555 1555 1.34 LINK C PRO D 178 N MSE D 179 1555 1555 1.33 LINK C MSE D 179 N MSE D 180 1555 1555 1.33 LINK C MSE D 180 N GLU D 181 1555 1555 1.34 LINK C ILE D 217 N MSE D 218 1555 1555 1.32 LINK C MSE D 218 N SER D 219 1555 1555 1.34 LINK C LEU D 225 N MSE D 226 1555 1555 1.33 LINK C MSE D 226 N GLY D 227 1555 1555 1.33 LINK C LEU D 261 N MSE D 262 1555 1555 1.32 LINK C MSE D 262 N ASN D 263 1555 1555 1.32 LINK C ASN D 291 N MSE D 292 1555 1555 1.33 LINK C MSE D 292 N ILE D 293 1555 1555 1.33 CRYST1 72.692 79.987 225.718 90.00 90.00 90.00 P 21 21 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013757 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012502 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004430 0.00000 ATOM 1 N ALA A 12 46.543 64.817 94.623 1.00 44.82 N ATOM 2 CA ALA A 12 46.394 65.993 95.487 1.00 50.46 C ATOM 3 C ALA A 12 44.946 66.220 95.959 1.00 53.70 C ATOM 4 O ALA A 12 44.011 66.165 95.153 1.00 53.08 O ATOM 5 CB ALA A 12 46.924 67.251 94.788 1.00 48.62 C ATOM 6 N THR A 13 44.776 66.501 97.256 1.00 47.69 N ATOM 7 CA THR A 13 43.453 66.660 97.858 1.00 46.73 C ATOM 8 C THR A 13 43.048 68.123 97.908 1.00 45.57 C ATOM 9 O THR A 13 43.756 68.948 98.472 1.00 47.84 O ATOM 10 CB THR A 13 43.410 66.104 99.308 1.00 49.36 C ATOM 11 OG1 THR A 13 43.885 64.754 99.339 1.00 51.94 O ATOM 12 CG2 THR A 13 41.992 66.126 99.856 1.00 49.07 C ATOM 13 N LEU A 14 41.907 68.455 97.321 1.00 46.18 N ATOM 14 CA LEU A 14 41.397 69.821 97.404 1.00 44.39 C ATOM 15 C LEU A 14 40.193 69.887 98.349 1.00 43.50 C ATOM 16 O LEU A 14 39.370 68.980 98.375 1.00 45.80 O ATOM 17 CB LEU A 14 41.029 70.349 96.006 1.00 40.04 C ATOM 18 CG LEU A 14 40.344 71.719 95.934 1.00 42.83 C ATOM 19 CD1 LEU A 14 41.116 72.767 96.714 1.00 45.61 C ATOM 20 CD2 LEU A 14 40.191 72.174 94.502 1.00 47.49 C ATOM 21 N LYS A 15 40.104 70.955 99.133 1.00 39.11 N ATOM 22 CA LYS A 15 38.964 71.168 100.019 1.00 36.76 C ATOM 23 C LYS A 15 38.396 72.564 99.888 1.00 37.29 C ATOM 24 O LYS A 15 39.110 73.545 100.025 1.00 37.01 O ATOM 25 CB LYS A 15 39.331 70.869 101.469 1.00 33.88 C ATOM 26 CG LYS A 15 39.531 69.401 101.692 1.00 39.33 C ATOM 27 CD LYS A 15 39.669 69.051 103.141 1.00 40.07 C ATOM 28 CE LYS A 15 39.612 67.543 103.308 1.00 43.69 C ATOM 29 NZ LYS A 15 40.569 67.066 104.343 1.00 46.68 N ATOM 30 N VAL A 16 37.101 72.630 99.600 1.00 33.83 N ATOM 31 CA VAL A 16 36.366 73.876 99.500 1.00 27.82 C ATOM 32 C VAL A 16 35.597 74.080 100.792 1.00 32.06 C ATOM 33 O VAL A 16 34.719 73.292 101.121 1.00 33.70 O ATOM 34 CB VAL A 16 35.373 73.828 98.321 1.00 31.44 C ATOM 35 CG1 VAL A 16 34.359 74.951 98.395 1.00 31.72 C ATOM 36 CG2 VAL A 16 36.108 73.891 97.012 1.00 36.85 C ATOM 37 N ILE A 17 35.937 75.133 101.528 1.00 31.85 N ATOM 38 CA ILE A 17 35.313 75.408 102.814 1.00 27.59 C ATOM 39 C ILE A 17 34.381 76.609 102.782 1.00 28.90 C ATOM 40 O ILE A 17 34.805 77.728 102.503 1.00 29.61 O ATOM 41 CB ILE A 17 36.372 75.621 103.898 1.00 27.28 C ATOM 42 CG1 ILE A 17 37.394 74.488 103.849 1.00 30.83 C ATOM 43 CG2 ILE A 17 35.724 75.714 105.269 1.00 27.23 C ATOM 44 CD1 ILE A 17 38.292 74.414 105.057 1.00 29.10 C ATOM 45 N GLY A 18 33.109 76.364 103.083 1.00 26.29 N ATOM 46 CA GLY A 18 32.114 77.419 103.143 1.00 27.07 C ATOM 47 C GLY A 18 31.817 77.901 104.550 1.00 31.49 C ATOM 48 O GLY A 18 31.394 77.132 105.396 1.00 33.42 O ATOM 49 N VAL A 19 32.024 79.183 104.804 1.00 27.34 N ATOM 50 CA VAL A 19 31.900 79.700 106.150 1.00 26.48 C ATOM 51 C VAL A 19 30.757 80.695 106.314 1.00 28.80 C ATOM 52 O VAL A 19 30.762 81.745 105.715 1.00 32.46 O ATOM 53 CB VAL A 19 33.224 80.342 106.622 1.00 27.58 C ATOM 54 CG1 VAL A 19 33.150 80.674 108.100 1.00 28.10 C ATOM 55 CG2 VAL A 19 34.369 79.405 106.388 1.00 25.62 C ATOM 56 N GLY A 20 29.781 80.359 107.145 1.00 31.35 N ATOM 57 CA GLY A 20 28.732 81.295 107.485 1.00 27.89 C ATOM 58 C GLY A 20 27.500 81.115 106.636 1.00 34.12 C ATOM 59 O GLY A 20 27.367 80.114 105.945 1.00 34.50 O ATOM 60 N GLY A 21 26.591 82.080 106.690 1.00 34.53 N ATOM 61 CA GLY A 21 25.389 82.013 105.896 1.00 30.21 C ATOM 62 C GLY A 21 25.759 81.968 104.432 1.00 36.08 C ATOM 63 O GLY A 21 25.416 81.030 103.724 1.00 37.31 O ATOM 64 N GLY A 22 26.484 82.983 103.984 1.00 37.08 N ATOM 65 CA GLY A 22 26.867 83.087 102.591 1.00 34.58 C ATOM 66 C GLY A 22 27.702 81.920 102.120 1.00 36.14 C ATOM 67 O GLY A 22 27.550 81.456 101.003 1.00 34.91 O ATOM 68 N GLY A 23 28.579 81.430 102.980 1.00 35.80 N ATOM 69 CA GLY A 23 29.474 80.360 102.594 1.00 33.60 C ATOM 70 C GLY A 23 28.789 79.024 102.436 1.00 35.08 C ATOM 71 O GLY A 23 29.151 78.255 101.557 1.00 36.73 O ATOM 72 N ASN A 24 27.809 78.746 103.293 1.00 35.06 N ATOM 73 CA ASN A 24 27.029 77.514 103.198 1.00 34.98 C ATOM 74 C ASN A 24 26.175 77.525 101.933 1.00 35.56 C ATOM 75 O ASN A 24 25.970 76.496 101.297 1.00 37.94 O ATOM 76 CB ASN A 24 26.138 77.292 104.440 1.00 33.70 C ATOM 77 CG ASN A 24 26.937 77.179 105.766 1.00 39.57 C ATOM 78 OD1 ASN A 24 26.342 77.044 106.830 1.00 40.25 O ATOM 79 ND2 ASN A 24 28.267 77.255 105.698 1.00 35.81 N ATOM 80 N ASN A 25 25.682 78.702 101.575 1.00 32.42 N ATOM 81 CA ASN A 25 24.958 78.860 100.331 1.00 35.08 C ATOM 82 C ASN A 25 25.902 78.729 99.142 1.00 37.70 C ATOM 83 O ASN A 25 25.492 78.323 98.064 1.00 36.76 O ATOM 84 CB ASN A 25 24.222 80.202 100.286 1.00 35.28 C ATOM 85 CG ASN A 25 23.145 80.324 101.360 1.00 40.09 C ATOM 86 OD1 ASN A 25 22.579 79.325 101.821 1.00 41.61 O ATOM 87 ND2 ASN A 25 22.853 81.558 101.759 1.00 41.84 N ATOM 88 N ALA A 26 27.169 79.075 99.345 1.00 38.51 N ATOM 89 CA ALA A 26 28.158 78.966 98.288 1.00 33.63 C ATOM 90 C ALA A 26 28.464 77.509 98.041 1.00 33.78 C ATOM 91 O ALA A 26 28.473 77.054 96.912 1.00 34.27 O ATOM 92 CB ALA A 26 29.413 79.717 98.648 1.00 33.80 C ATOM 93 N VAL A 27 28.699 76.780 99.120 1.00 34.81 N ATOM 94 CA VAL A 27 28.976 75.353 99.058 1.00 34.73 C ATOM 95 C VAL A 27 27.862 74.523 98.412 1.00 35.99 C ATOM 96 O VAL A 27 28.123 73.584 97.658 1.00 37.50 O ATOM 97 CB VAL A 27 29.280 74.823 100.461 1.00 30.76 C ATOM 98 CG1 VAL A 27 28.966 73.362 100.577 1.00 33.15 C ATOM 99 CG2 VAL A 27 30.711 75.042 100.766 1.00 30.26 C ATOM 100 N ASN A 28 26.622 74.877 98.705 1.00 34.29 N ATOM 101 CA ASN A 28 25.496 74.106 98.226 1.00 34.49 C ATOM 102 C ASN A 28 25.307 74.205 96.713 1.00 38.80 C ATOM 103 O ASN A 28 25.039 73.199 96.047 1.00 42.28 O ATOM 104 CB ASN A 28 24.222 74.489 98.973 1.00 35.35 C ATOM 105 CG ASN A 28 24.063 73.732 100.273 1.00 37.58 C ATOM 106 OD1 ASN A 28 24.658 72.678 100.472 1.00 39.66 O ATOM 107 ND2 ASN A 28 23.241 74.258 101.158 1.00 38.97 N ATOM 108 N ARG A 29 25.458 75.412 96.179 1.00 36.90 N ATOM 109 CA ARG A 29 25.405 75.620 94.742 1.00 35.78 C ATOM 110 C ARG A 29 26.519 74.844 94.057 1.00 37.78 C ATOM 111 O ARG A 29 26.312 74.251 93.008 1.00 41.34 O ATOM 112 CB ARG A 29 25.529 77.098 94.412 1.00 31.79 C ATOM 113 CG ARG A 29 24.462 77.962 95.035 1.00 33.22 C ATOM 114 CD ARG A 29 24.740 79.410 94.734 1.00 36.69 C ATOM 115 NE ARG A 29 25.572 79.535 93.533 1.00 43.93 N ATOM 116 CZ ARG A 29 26.348 80.583 93.259 1.00 44.14 C ATOM 117 NH1 ARG A 29 26.408 81.617 94.095 1.00 41.13 N ATOM 118 NH2 ARG A 29 27.070 80.595 92.148 1.00 43.26 N HETATM 119 N MSE A 30 27.701 74.842 94.663 1.00 38.00 N HETATM 120 CA MSE A 30 28.835 74.096 94.129 1.00 38.47 C HETATM 121 C MSE A 30 28.629 72.588 94.223 1.00 41.52 C HETATM 122 O MSE A 30 29.120 71.839 93.388 1.00 41.98 O HETATM 123 CB MSE A 30 30.142 74.504 94.813 1.00 38.10 C HETATM 124 CG MSE A 30 30.627 75.882 94.447 1.00 36.17 C HETATM 125 SE MSE A 30 32.093 76.453 95.558 0.60 25.36 Se HETATM 126 CE MSE A 30 33.519 75.411 94.879 1.00 44.88 C ATOM 127 N ILE A 31 27.915 72.126 95.241 1.00 41.89 N ATOM 128 CA ILE A 31 27.710 70.686 95.353 1.00 43.08 C ATOM 129 C ILE A 31 26.751 70.151 94.274 1.00 50.42 C ATOM 130 O ILE A 31 27.001 69.081 93.691 1.00 51.14 O ATOM 131 CB ILE A 31 27.276 70.285 96.753 1.00 37.77 C ATOM 132 CG1 ILE A 31 28.481 70.396 97.692 1.00 38.57 C ATOM 133 CG2 ILE A 31 26.734 68.879 96.751 1.00 37.62 C ATOM 134 CD1 ILE A 31 28.281 69.761 99.049 1.00 38.03 C ATOM 135 N ASP A 32 25.680 70.903 93.999 1.00 44.72 N ATOM 136 CA ASP A 32 24.727 70.547 92.948 1.00 47.21 C ATOM 137 C ASP A 32 25.358 70.501 91.555 1.00 51.73 C ATOM 138 O ASP A 32 25.701 71.529 90.974 1.00 51.65 O ATOM 139 CB ASP A 32 23.542 71.506 92.979 1.00 46.82 C ATOM 140 CG ASP A 32 22.807 71.470 94.318 1.00 56.48 C ATOM 141 OD1 ASP A 32 22.657 70.349 94.885 1.00 53.41 O ATOM 142 OD2 ASP A 32 22.392 72.556 94.815 1.00 53.71 O ATOM 143 N ASN A 37 36.054 66.427 91.660 1.00 58.11 N ATOM 144 CA ASN A 37 36.812 65.774 92.736 1.00 67.83 C ATOM 145 C ASN A 37 37.314 66.734 93.849 1.00 69.23 C ATOM 146 O ASN A 37 38.461 67.217 93.833 1.00 64.77 O ATOM 147 CB ASN A 37 37.966 64.940 92.162 1.00 71.49 C ATOM 148 CG ASN A 37 38.172 63.639 92.923 1.00 71.87 C ATOM 149 OD1 ASN A 37 37.786 63.532 94.091 1.00 70.00 O ATOM 150 ND2 ASN A 37 38.771 62.642 92.264 1.00 66.03 N ATOM 151 N VAL A 38 36.431 66.988 94.817 1.00 65.78 N ATOM 152 CA VAL A 38 36.612 68.029 95.826 1.00 52.30 C ATOM 153 C VAL A 38 35.778 67.680 97.045 1.00 50.36 C ATOM 154 O VAL A 38 34.596 67.417 96.906 1.00 54.99 O ATOM 155 CB VAL A 38 36.112 69.396 95.295 1.00 51.67 C ATOM 156 CG1 VAL A 38 37.266 70.268 94.900 1.00 50.60 C ATOM 157 CG2 VAL A 38 35.162 69.206 94.112 1.00 54.29 C ATOM 158 N GLU A 39 36.379 67.650 98.229 1.00 47.96 N ATOM 159 CA GLU A 39 35.609 67.492 99.456 1.00 47.69 C ATOM 160 C GLU A 39 35.091 68.846 99.898 1.00 43.71 C ATOM 161 O GLU A 39 35.835 69.810 99.910 1.00 43.03 O ATOM 162 CB GLU A 39 36.487 66.939 100.570 1.00 51.47 C ATOM 163 CG GLU A 39 37.069 65.560 100.316 1.00 60.15 C ATOM 164 CD GLU A 39 37.548 64.892 101.622 1.00 72.12 C ATOM 165 OE1 GLU A 39 37.130 65.362 102.728 1.00 66.93 O ATOM 166 OE2 GLU A 39 38.343 63.910 101.540 1.00 68.77 O ATOM 167 N PHE A 40 33.825 68.935 100.269 1.00 39.99 N ATOM 168 CA PHE A 40 33.314 70.190 100.805 1.00 38.01 C ATOM 169 C PHE A 40 33.187 70.144 102.339 1.00 38.93 C ATOM 170 O PHE A 40 32.952 69.091 102.928 1.00 42.14 O ATOM 171 CB PHE A 40 31.995 70.560 100.140 1.00 35.10 C ATOM 172 CG PHE A 40 32.106 70.773 98.663 1.00 36.99 C ATOM 173 CD1 PHE A 40 32.352 72.033 98.151 1.00 36.70 C ATOM 174 CD2 PHE A 40 31.952 69.715 97.775 1.00 38.07 C ATOM 175 CE1 PHE A 40 32.447 72.230 96.788 1.00 39.37 C ATOM 176 CE2 PHE A 40 32.048 69.908 96.423 1.00 34.30 C ATOM 177 CZ PHE A 40 32.297 71.159 95.926 1.00 38.22 C ATOM 178 N ILE A 41 33.387 71.287 102.982 1.00 34.05 N ATOM 179 CA ILE A 41 33.266 71.383 104.428 1.00 34.45 C ATOM 180 C ILE A 41 32.438 72.605 104.738 1.00 32.77 C ATOM 181 O ILE A 41 32.738 73.679 104.255 1.00 33.70 O ATOM 182 CB ILE A 41 34.633 71.548 105.107 1.00 32.24 C ATOM 183 CG1 ILE A 41 35.549 70.377 104.774 1.00 33.92 C ATOM 184 CG2 ILE A 41 34.473 71.653 106.610 1.00 31.42 C ATOM 185 CD1 ILE A 41 36.950 70.565 105.289 1.00 31.10 C ATOM 186 N ALA A 42 31.395 72.451 105.540 1.00 33.65 N ATOM 187 CA ALA A 42 30.577 73.599 105.895 1.00 30.91 C ATOM 188 C ALA A 42 30.754 73.983 107.348 1.00 32.44 C ATOM 189 O ALA A 42 30.544 73.169 108.243 1.00 35.48 O ATOM 190 CB ALA A 42 29.129 73.328 105.593 1.00 35.43 C ATOM 191 N ILE A 43 31.139 75.236 107.566 1.00 31.44 N ATOM 192 CA ILE A 43 31.370 75.769 108.905 1.00 28.50 C ATOM 193 C ILE A 43 30.360 76.873 109.214 1.00 30.46 C ATOM 194 O ILE A 43 30.093 77.719 108.372 1.00 30.21 O ATOM 195 CB ILE A 43 32.805 76.318 109.040 1.00 26.26 C ATOM 196 CG1 ILE A 43 33.831 75.200 108.877 1.00 27.55 C ATOM 197 CG2 ILE A 43 33.011 76.976 110.380 1.00 28.50 C ATOM 198 CD1 ILE A 43 35.231 75.627 109.196 1.00 29.24 C ATOM 199 N ASN A 44 29.793 76.855 110.419 1.00 28.80 N ATOM 200 CA ASN A 44 28.848 77.886 110.836 1.00 30.98 C ATOM 201 C ASN A 44 28.702 78.011 112.356 1.00 32.64 C ATOM 202 O ASN A 44 28.834 77.035 113.076 1.00 34.22 O ATOM 203 CB ASN A 44 27.491 77.603 110.212 1.00 32.79 C ATOM 204 CG ASN A 44 26.781 78.858 109.765 1.00 34.81 C ATOM 205 OD1 ASN A 44 26.938 79.926 110.350 1.00 35.17 O ATOM 206 ND2 ASN A 44 25.980 78.730 108.722 1.00 33.97 N ATOM 207 N THR A 45 28.432 79.213 112.843 1.00 34.53 N ATOM 208 CA THR A 45 28.156 79.403 114.253 1.00 34.22 C ATOM 209 C THR A 45 26.679 79.137 114.470 1.00 38.05 C ATOM 210 O THR A 45 26.230 78.925 115.593 1.00 43.34 O ATOM 211 CB THR A 45 28.424 80.837 114.686 1.00 33.42 C ATOM 212 OG1 THR A 45 27.580 81.716 113.937 1.00 34.51 O ATOM 213 CG2 THR A 45 29.857 81.207 114.442 1.00 29.00 C ATOM 214 N ASP A 46 25.926 79.169 113.379 1.00 38.30 N ATOM 215 CA ASP A 46 24.491 78.991 113.429 1.00 40.29 C ATOM 216 C ASP A 46 24.115 77.587 112.988 1.00 43.08 C ATOM 217 O ASP A 46 23.986 77.313 111.792 1.00 46.79 O ATOM 218 CB ASP A 46 23.830 80.043 112.543 1.00 43.94 C ATOM 219 CG ASP A 46 22.349 79.788 112.300 1.00 49.71 C ATOM 220 OD1 ASP A 46 21.725 78.930 112.964 1.00 47.63 O ATOM 221 OD2 ASP A 46 21.803 80.490 111.427 1.00 53.31 O ATOM 222 N GLY A 47 23.902 76.710 113.962 1.00 38.45 N ATOM 223 CA GLY A 47 23.596 75.324 113.685 1.00 38.63 C ATOM 224 C GLY A 47 22.297 75.099 112.946 1.00 43.36 C ATOM 225 O GLY A 47 22.041 73.992 112.478 1.00 47.11 O ATOM 226 N GLN A 48 21.463 76.128 112.835 1.00 41.66 N ATOM 227 CA GLN A 48 20.220 75.973 112.078 1.00 44.07 C ATOM 228 C GLN A 48 20.570 75.868 110.611 1.00 46.65 C ATOM 229 O GLN A 48 20.097 74.985 109.905 1.00 45.99 O ATOM 230 CB GLN A 48 19.248 77.140 112.304 1.00 46.10 C ATOM 231 CG GLN A 48 17.853 76.901 111.710 1.00 48.99 C ATOM 232 CD GLN A 48 16.962 78.145 111.730 1.00 50.32 C ATOM 233 OE1 GLN A 48 17.343 79.202 111.210 1.00 51.26 O ATOM 234 NE2 GLN A 48 15.766 78.021 112.321 1.00 43.56 N ATOM 235 N ALA A 49 21.429 76.776 110.176 1.00 46.79 N ATOM 236 CA ALA A 49 21.889 76.818 108.809 1.00 43.32 C ATOM 237 C ALA A 49 22.677 75.564 108.440 1.00 41.80 C ATOM 238 O ALA A 49 22.722 75.178 107.280 1.00 39.91 O ATOM 239 CB ALA A 49 22.724 78.064 108.599 1.00 45.99 C ATOM 240 N LEU A 50 23.290 74.926 109.430 1.00 40.04 N ATOM 241 CA LEU A 50 24.097 73.746 109.175 1.00 38.75 C ATOM 242 C LEU A 50 23.283 72.551 108.743 1.00 42.18 C ATOM 243 O LEU A 50 23.827 71.595 108.216 1.00 46.11 O ATOM 244 CB LEU A 50 24.946 73.383 110.381 1.00 37.49 C ATOM 245 CG LEU A 50 26.319 74.039 110.436 1.00 36.82 C ATOM 246 CD1 LEU A 50 27.156 73.387 111.511 1.00 35.41 C ATOM 247 CD2 LEU A 50 27.007 73.915 109.112 1.00 33.48 C ATOM 248 N ASN A 51 21.978 72.588 108.961 1.00 45.05 N ATOM 249 CA ASN A 51 21.145 71.460 108.558 1.00 43.31 C ATOM 250 C ASN A 51 20.699 71.550 107.115 1.00 41.99 C ATOM 251 O ASN A 51 20.301 70.553 106.530 1.00 43.56 O ATOM 252 CB ASN A 51 19.944 71.304 109.477 1.00 43.78 C ATOM 253 CG ASN A 51 20.316 70.681 110.798 1.00 53.21 C ATOM 254 OD1 ASN A 51 21.084 69.707 110.842 1.00 54.89 O ATOM 255 ND2 ASN A 51 19.788 71.239 111.890 1.00 49.28 N ATOM 256 N LEU A 52 20.782 72.745 106.548 1.00 39.41 N ATOM 257 CA LEU A 52 20.471 72.970 105.153 1.00 39.19 C ATOM 258 C LEU A 52 21.620 72.598 104.258 1.00 39.42 C ATOM 259 O LEU A 52 21.509 72.683 103.049 1.00 42.16 O ATOM 260 CB LEU A 52 20.197 74.440 104.937 1.00 41.81 C ATOM 261 CG LEU A 52 19.051 74.977 105.767 1.00 42.46 C ATOM 262 CD1 LEU A 52 19.202 76.468 106.025 1.00 46.27 C ATOM 263 CD2 LEU A 52 17.858 74.728 104.950 1.00 42.16 C ATOM 264 N SER A 53 22.741 72.209 104.835 1.00 40.89 N ATOM 265 CA SER A 53 23.911 71.952 104.018 1.00 41.41 C ATOM 266 C SER A 53 23.910 70.544 103.480 1.00 41.15 C ATOM 267 O SER A 53 23.568 69.594 104.188 1.00 42.44 O ATOM 268 CB SER A 53 25.196 72.152 104.805 1.00 40.74 C ATOM 269 OG SER A 53 26.299 71.994 103.928 1.00 43.32 O ATOM 270 N LYS A 54 24.318 70.414 102.226 1.00 41.08 N ATOM 271 CA LYS A 54 24.474 69.115 101.626 1.00 38.39 C ATOM 272 C LYS A 54 25.903 68.654 101.801 1.00 40.63 C ATOM 273 O LYS A 54 26.255 67.563 101.398 1.00 41.24 O ATOM 274 CB LYS A 54 24.095 69.192 100.161 1.00 35.89 C ATOM 275 CG LYS A 54 22.695 69.719 99.939 1.00 38.43 C ATOM 276 CD LYS A 54 22.496 70.099 98.494 1.00 42.91 C ATOM 277 CE LYS A 54 21.092 70.622 98.254 1.00 48.26 C ATOM 278 NZ LYS A 54 21.113 71.908 97.484 1.00 50.29 N ATOM 279 N ALA A 55 26.724 69.487 102.420 1.00 40.11 N ATOM 280 CA ALA A 55 28.089 69.094 102.669 1.00 35.60 C ATOM 281 C ALA A 55 28.062 67.815 103.478 1.00 38.59 C ATOM 282 O ALA A 55 27.152 67.575 104.259 1.00 44.90 O ATOM 283 CB ALA A 55 28.852 70.177 103.386 1.00 34.89 C ATOM 284 N GLU A 56 29.056 66.981 103.237 1.00 41.68 N ATOM 285 CA GLU A 56 29.211 65.692 103.874 1.00 41.72 C ATOM 286 C GLU A 56 29.818 65.881 105.248 1.00 41.54 C ATOM 287 O GLU A 56 29.719 65.015 106.103 1.00 43.33 O ATOM 288 CB GLU A 56 30.158 64.860 103.016 1.00 47.21 C ATOM 289 CG GLU A 56 31.375 65.687 102.455 1.00 53.16 C ATOM 290 CD GLU A 56 31.178 66.288 101.002 1.00 49.36 C ATOM 291 OE1 GLU A 56 30.052 66.710 100.656 1.00 41.74 O ATOM 292 OE2 GLU A 56 32.166 66.334 100.218 1.00 44.37 O ATOM 293 N SER A 57 30.467 67.017 105.449 1.00 38.71 N ATOM 294 CA SER A 57 31.171 67.290 106.690 1.00 34.36 C ATOM 295 C SER A 57 30.829 68.690 107.193 1.00 36.81 C ATOM 296 O SER A 57 31.113 69.691 106.519 1.00 37.76 O ATOM 297 CB SER A 57 32.673 67.139 106.469 1.00 34.93 C ATOM 298 OG SER A 57 33.394 68.072 107.237 1.00 38.15 O ATOM 299 N LYS A 58 30.193 68.762 108.360 1.00 35.35 N ATOM 300 CA LYS A 58 29.713 70.037 108.873 1.00 33.02 C ATOM 301 C LYS A 58 30.255 70.300 110.243 1.00 33.60 C ATOM 302 O LYS A 58 30.406 69.387 111.046 1.00 36.28 O ATOM 303 CB LYS A 58 28.202 70.050 108.962 1.00 32.86 C ATOM 304 CG LYS A 58 27.521 69.397 107.815 1.00 32.83 C ATOM 305 CD LYS A 58 26.042 69.473 108.032 1.00 38.79 C ATOM 306 CE LYS A 58 25.326 68.262 107.455 1.00 44.91 C ATOM 307 NZ LYS A 58 25.640 67.003 108.205 1.00 47.06 N ATOM 308 N ILE A 59 30.550 71.554 110.525 1.00 32.85 N ATOM 309 CA ILE A 59 31.136 71.883 111.801 1.00 32.43 C ATOM 310 C ILE A 59 30.492 73.111 112.381 1.00 33.15 C ATOM 311 O ILE A 59 30.548 74.191 111.797 1.00 34.92 O ATOM 312 CB ILE A 59 32.609 72.189 111.670 1.00 34.49 C ATOM 313 CG1 ILE A 59 33.350 71.055 110.991 1.00 33.29 C ATOM 314 CG2 ILE A 59 33.216 72.443 113.031 1.00 35.15 C ATOM 315 CD1 ILE A 59 34.739 71.428 110.744 1.00 35.43 C ATOM 316 N GLN A 60 29.878 72.936 113.542 1.00 34.56 N ATOM 317 CA GLN A 60 29.385 74.061 114.299 1.00 35.89 C ATOM 318 C GLN A 60 30.522 74.618 115.136 1.00 39.65 C ATOM 319 O GLN A 60 31.196 73.884 115.856 1.00 38.61 O ATOM 320 CB GLN A 60 28.224 73.647 115.189 1.00 37.88 C ATOM 321 CG GLN A 60 27.350 74.816 115.573 1.00 41.94 C ATOM 322 CD GLN A 60 26.245 74.433 116.517 1.00 48.15 C ATOM 323 OE1 GLN A 60 26.221 73.319 117.048 1.00 54.46 O ATOM 324 NE2 GLN A 60 25.320 75.361 116.746 1.00 45.57 N ATOM 325 N ILE A 61 30.748 75.919 115.016 1.00 35.62 N ATOM 326 CA ILE A 61 31.809 76.559 115.761 1.00 32.89 C ATOM 327 C ILE A 61 31.272 77.428 116.881 1.00 32.25 C ATOM 328 O ILE A 61 30.204 78.021 116.765 1.00 32.27 O ATOM 329 CB ILE A 61 32.768 77.362 114.852 1.00 31.02 C ATOM 330 CG1 ILE A 61 32.007 78.376 113.999 1.00 29.65 C ATOM 331 CG2 ILE A 61 33.549 76.426 113.999 1.00 29.64 C ATOM 332 CD1 ILE A 61 32.887 79.415 113.341 1.00 26.59 C ATOM 333 N GLY A 62 32.019 77.457 117.980 1.00 35.29 N ATOM 334 CA GLY A 62 31.744 78.350 119.098 1.00 38.73 C ATOM 335 C GLY A 62 30.477 78.072 119.875 1.00 39.64 C ATOM 336 O GLY A 62 29.728 78.984 120.198 1.00 38.90 O ATOM 337 N GLU A 63 30.248 76.801 120.167 1.00 41.95 N ATOM 338 CA GLU A 63 29.029 76.372 120.818 1.00 44.98 C ATOM 339 C GLU A 63 28.838 77.077 122.147 1.00 43.89 C ATOM 340 O GLU A 63 27.754 77.576 122.433 1.00 45.13 O ATOM 341 CB GLU A 63 29.051 74.862 121.016 1.00 52.39 C ATOM 342 CG GLU A 63 27.923 74.134 120.298 1.00 58.56 C ATOM 343 CD GLU A 63 27.845 72.648 120.661 1.00 68.21 C ATOM 344 OE1 GLU A 63 28.504 72.245 121.662 1.00 67.90 O ATOM 345 OE2 GLU A 63 27.118 71.894 119.946 1.00 67.20 O ATOM 346 N LYS A 64 29.905 77.128 122.939 1.00 41.55 N ATOM 347 CA LYS A 64 29.901 77.807 124.222 1.00 43.22 C ATOM 348 C LYS A 64 29.722 79.312 124.072 1.00 42.16 C ATOM 349 O LYS A 64 28.898 79.905 124.747 1.00 43.37 O ATOM 350 CB LYS A 64 31.208 77.519 124.971 1.00 45.40 C ATOM 351 CG LYS A 64 31.422 76.071 125.408 1.00 47.13 C ATOM 352 CD LYS A 64 32.787 75.848 126.082 1.00 46.49 C ATOM 353 CE LYS A 64 33.930 76.511 125.306 1.00 52.58 C ATOM 354 NZ LYS A 64 35.092 75.609 125.030 1.00 49.73 N ATOM 355 N LEU A 65 30.493 79.930 123.190 1.00 40.71 N ATOM 356 CA LEU A 65 30.477 81.378 123.045 1.00 37.04 C ATOM 357 C LEU A 65 29.140 81.906 122.569 1.00 34.90 C ATOM 358 O LEU A 65 28.830 83.068 122.734 1.00 36.05 O ATOM 359 CB LEU A 65 31.574 81.813 122.080 1.00 34.81 C ATOM 360 CG LEU A 65 31.795 83.318 121.939 1.00 35.73 C ATOM 361 CD1 LEU A 65 32.279 83.891 123.256 1.00 34.64 C ATOM 362 CD2 LEU A 65 32.772 83.609 120.856 1.00 30.86 C ATOM 363 N THR A 66 28.325 81.045 121.998 1.00 41.24 N ATOM 364 CA THR A 66 27.176 81.524 121.252 1.00 45.64 C ATOM 365 C THR A 66 25.848 81.189 121.934 1.00 45.75 C ATOM 366 O THR A 66 24.781 81.622 121.502 1.00 46.97 O ATOM 367 CB THR A 66 27.242 80.994 119.802 1.00 40.35 C ATOM 368 OG1 THR A 66 26.723 81.977 118.911 1.00 47.24 O ATOM 369 CG2 THR A 66 26.475 79.689 119.648 1.00 42.12 C ATOM 370 N ARG A 67 25.937 80.426 123.015 1.00 47.67 N ATOM 371 CA ARG A 67 24.767 80.062 123.809 1.00 52.33 C ATOM 372 C ARG A 67 23.940 81.281 124.238 1.00 51.04 C ATOM 373 O ARG A 67 24.483 82.288 124.692 1.00 47.79 O ATOM 374 CB ARG A 67 25.195 79.252 125.030 1.00 49.38 C ATOM 375 CG ARG A 67 24.057 78.818 125.929 1.00 57.21 C ATOM 376 CD ARG A 67 24.524 77.718 126.886 1.00 66.95 C ATOM 377 NE ARG A 67 25.420 76.783 126.189 1.00 69.86 N ATOM 378 CZ ARG A 67 26.703 76.582 126.507 1.00 64.92 C ATOM 379 NH1 ARG A 67 27.252 77.247 127.534 1.00 60.62 N ATOM 380 NH2 ARG A 67 27.436 75.711 125.798 1.00 61.64 N ATOM 381 N GLY A 68 22.628 81.188 124.066 1.00 55.72 N ATOM 382 CA GLY A 68 21.743 82.294 124.375 1.00 56.92 C ATOM 383 C GLY A 68 22.016 83.595 123.629 1.00 56.44 C ATOM 384 O GLY A 68 21.567 84.671 124.054 1.00 57.19 O ATOM 385 N LEU A 69 22.741 83.518 122.520 1.00 54.04 N ATOM 386 CA LEU A 69 22.960 84.708 121.716 1.00 58.57 C ATOM 387 C LEU A 69 21.786 84.879 120.765 1.00 65.26 C ATOM 388 O LEU A 69 21.134 83.893 120.384 1.00 63.34 O ATOM 389 CB LEU A 69 24.256 84.576 120.921 1.00 57.79 C ATOM 390 CG LEU A 69 24.700 85.749 120.045 1.00 59.75 C ATOM 391 CD1 LEU A 69 25.979 86.331 120.615 1.00 55.06 C ATOM 392 CD2 LEU A 69 24.896 85.314 118.587 1.00 53.24 C ATOM 393 N GLY A 70 21.517 86.125 120.377 1.00 68.75 N ATOM 394 CA GLY A 70 20.398 86.418 119.490 1.00 66.77 C ATOM 395 C GLY A 70 20.791 87.056 118.170 1.00 63.79 C ATOM 396 O GLY A 70 21.687 86.573 117.462 1.00 63.72 O ATOM 397 N ALA A 71 20.112 88.141 117.815 1.00 61.44 N ATOM 398 CA ALA A 71 20.520 88.881 116.624 1.00 65.16 C ATOM 399 C ALA A 71 21.776 89.703 116.941 1.00 67.72 C ATOM 400 O ALA A 71 22.332 89.626 118.063 1.00 68.16 O ATOM 401 CB ALA A 71 19.391 89.780 116.122 1.00 64.23 C ATOM 402 N GLY A 72 22.221 90.480 115.955 1.00 64.08 N ATOM 403 CA GLY A 72 23.352 91.375 116.134 1.00 67.85 C ATOM 404 C GLY A 72 24.729 90.715 116.152 1.00 65.76 C ATOM 405 O GLY A 72 25.740 91.414 116.345 1.00 59.33 O ATOM 406 N ALA A 73 24.770 89.386 115.990 1.00 59.02 N ATOM 407 CA ALA A 73 26.028 88.643 115.881 1.00 47.79 C ATOM 408 C ALA A 73 26.981 89.323 114.894 1.00 44.77 C ATOM 409 O ALA A 73 26.642 89.518 113.730 1.00 50.84 O ATOM 410 CB ALA A 73 25.750 87.223 115.450 1.00 46.80 C ATOM 411 N ASN A 74 28.167 89.685 115.366 1.00 39.35 N ATOM 412 CA ASN A 74 29.119 90.469 114.583 1.00 35.79 C ATOM 413 C ASN A 74 30.299 89.615 114.077 1.00 33.92 C ATOM 414 O ASN A 74 30.360 88.431 114.383 1.00 35.53 O ATOM 415 CB ASN A 74 29.600 91.646 115.436 1.00 32.08 C ATOM 416 CG ASN A 74 30.302 91.201 116.707 1.00 38.05 C ATOM 417 OD1 ASN A 74 31.202 90.368 116.676 1.00 36.77 O ATOM 418 ND2 ASN A 74 29.877 91.746 117.835 1.00 37.49 N ATOM 419 N PRO A 75 31.233 90.203 113.298 1.00 32.55 N ATOM 420 CA PRO A 75 32.446 89.464 112.914 1.00 32.24 C ATOM 421 C PRO A 75 33.265 88.881 114.085 1.00 35.20 C ATOM 422 O PRO A 75 33.844 87.795 113.966 1.00 32.19 O ATOM 423 CB PRO A 75 33.283 90.530 112.208 1.00 30.28 C ATOM 424 CG PRO A 75 32.305 91.458 111.644 1.00 31.15 C ATOM 425 CD PRO A 75 31.118 91.472 112.552 1.00 31.53 C ATOM 426 N GLU A 76 33.323 89.597 115.203 1.00 33.75 N ATOM 427 CA GLU A 76 34.204 89.214 116.284 1.00 31.47 C ATOM 428 C GLU A 76 33.710 87.934 116.926 1.00 29.71 C ATOM 429 O GLU A 76 34.490 87.064 117.233 1.00 25.62 O ATOM 430 CB GLU A 76 34.330 90.371 117.278 1.00 33.34 C ATOM 431 CG GLU A 76 35.422 90.258 118.297 1.00 39.53 C ATOM 432 CD GLU A 76 36.787 90.251 117.684 1.00 47.65 C ATOM 433 OE1 GLU A 76 36.967 90.721 116.505 1.00 45.53 O ATOM 434 OE2 GLU A 76 37.767 89.776 118.362 1.00 47.89 O ATOM 435 N ILE A 77 32.405 87.806 117.078 1.00 31.31 N ATOM 436 CA ILE A 77 31.839 86.584 117.608 1.00 31.34 C ATOM 437 C ILE A 77 32.338 85.392 116.809 1.00 31.62 C ATOM 438 O ILE A 77 32.781 84.403 117.378 1.00 29.33 O ATOM 439 CB ILE A 77 30.307 86.621 117.571 1.00 30.90 C ATOM 440 CG1 ILE A 77 29.810 87.720 118.481 1.00 34.98 C ATOM 441 CG2 ILE A 77 29.727 85.342 118.083 1.00 30.74 C ATOM 442 CD1 ILE A 77 30.125 87.459 119.917 1.00 35.29 C ATOM 443 N GLY A 78 32.293 85.507 115.484 1.00 31.08 N ATOM 444 CA GLY A 78 32.634 84.410 114.601 1.00 28.52 C ATOM 445 C GLY A 78 34.104 84.101 114.604 1.00 29.86 C ATOM 446 O GLY A 78 34.509 82.951 114.529 1.00 29.08 O ATOM 447 N LYS A 79 34.903 85.152 114.685 1.00 28.42 N ATOM 448 CA LYS A 79 36.337 85.015 114.862 1.00 27.21 C ATOM 449 C LYS A 79 36.665 84.201 116.114 1.00 30.04 C ATOM 450 O LYS A 79 37.412 83.236 116.041 1.00 30.07 O ATOM 451 CB LYS A 79 36.980 86.394 114.914 1.00 25.33 C ATOM 452 CG LYS A 79 38.473 86.412 115.096 1.00 30.27 C ATOM 453 CD LYS A 79 38.931 87.834 115.282 1.00 33.88 C ATOM 454 CE LYS A 79 40.363 87.904 115.745 1.00 41.47 C ATOM 455 NZ LYS A 79 41.308 87.395 114.736 1.00 41.86 N ATOM 456 N LYS A 80 36.077 84.558 117.257 1.00 31.26 N ATOM 457 CA LYS A 80 36.391 83.862 118.511 1.00 29.34 C ATOM 458 C LYS A 80 35.808 82.484 118.494 1.00 29.62 C ATOM 459 O LYS A 80 36.417 81.546 118.973 1.00 30.02 O ATOM 460 CB LYS A 80 35.901 84.623 119.752 1.00 28.52 C ATOM 461 CG LYS A 80 36.629 85.913 120.043 1.00 30.92 C ATOM 462 CD LYS A 80 38.115 85.726 119.979 1.00 34.61 C ATOM 463 CE LYS A 80 38.821 87.058 119.956 1.00 43.21 C ATOM 464 NZ LYS A 80 40.307 86.883 119.947 1.00 50.27 N ATOM 465 N ALA A 81 34.620 82.372 117.934 1.00 27.28 N ATOM 466 CA ALA A 81 33.967 81.086 117.787 1.00 28.68 C ATOM 467 C ALA A 81 34.819 80.075 117.034 1.00 31.94 C ATOM 468 O ALA A 81 34.821 78.897 117.370 1.00 34.65 O ATOM 469 CB ALA A 81 32.643 81.256 117.091 1.00 30.27 C ATOM 470 N ALA A 82 35.532 80.540 116.013 1.00 29.13 N ATOM 471 CA ALA A 82 36.384 79.677 115.228 1.00 29.79 C ATOM 472 C ALA A 82 37.626 79.303 116.013 1.00 30.86 C ATOM 473 O ALA A 82 38.112 78.186 115.916 1.00 33.69 O ATOM 474 CB ALA A 82 36.752 80.348 113.931 1.00 28.54 C ATOM 475 N GLU A 83 38.148 80.237 116.790 1.00 32.22 N ATOM 476 CA GLU A 83 39.264 79.926 117.673 1.00 31.26 C ATOM 477 C GLU A 83 38.896 78.873 118.726 1.00 32.20 C ATOM 478 O GLU A 83 39.702 78.007 119.025 1.00 36.34 O ATOM 479 CB GLU A 83 39.828 81.199 118.309 1.00 31.12 C ATOM 480 CG GLU A 83 40.501 82.120 117.308 1.00 39.03 C ATOM 481 CD GLU A 83 40.820 83.498 117.881 1.00 48.15 C ATOM 482 OE1 GLU A 83 40.810 83.658 119.127 1.00 50.94 O ATOM 483 OE2 GLU A 83 41.084 84.433 117.084 1.00 47.26 O ATOM 484 N GLU A 84 37.668 78.928 119.224 1.00 32.08 N ATOM 485 CA GLU A 84 37.190 77.948 120.187 1.00 30.95 C ATOM 486 C GLU A 84 37.094 76.538 119.603 1.00 33.09 C ATOM 487 O GLU A 84 37.408 75.564 120.280 1.00 36.85 O ATOM 488 CB GLU A 84 35.832 78.371 120.746 1.00 34.05 C ATOM 489 CG GLU A 84 35.142 77.295 121.565 1.00 38.66 C ATOM 490 CD GLU A 84 33.697 77.631 121.869 1.00 49.01 C ATOM 491 OE1 GLU A 84 33.402 78.817 122.121 1.00 46.41 O ATOM 492 OE2 GLU A 84 32.858 76.707 121.858 1.00 46.63 O ATOM 493 N SER A 85 36.656 76.430 118.353 1.00 32.45 N ATOM 494 CA SER A 85 36.460 75.130 117.729 1.00 32.73 C ATOM 495 C SER A 85 37.624 74.780 116.816 1.00 34.25 C ATOM 496 O SER A 85 37.460 74.009 115.872 1.00 36.45 O ATOM 497 CB SER A 85 35.132 75.082 116.972 1.00 32.33 C ATOM 498 OG SER A 85 34.037 75.385 117.817 1.00 35.30 O ATOM 499 N ARG A 86 38.793 75.350 117.125 1.00 34.68 N ATOM 500 CA ARG A 86 40.027 75.159 116.362 1.00 34.20 C ATOM 501 C ARG A 86 40.390 73.695 116.080 1.00 39.49 C ATOM 502 O ARG A 86 40.683 73.332 114.944 1.00 41.59 O ATOM 503 CB ARG A 86 41.191 75.882 117.030 1.00 33.58 C ATOM 504 CG ARG A 86 42.532 75.413 116.529 1.00 39.49 C ATOM 505 CD ARG A 86 43.657 76.381 116.856 1.00 45.33 C ATOM 506 NE ARG A 86 44.634 76.399 115.762 1.00 48.88 N ATOM 507 CZ ARG A 86 45.313 77.468 115.368 1.00 49.90 C ATOM 508 NH1 ARG A 86 45.146 78.630 115.984 1.00 53.14 N ATOM 509 NH2 ARG A 86 46.150 77.370 114.341 1.00 50.25 N ATOM 510 N GLU A 87 40.346 72.854 117.102 1.00 41.76 N ATOM 511 CA GLU A 87 40.705 71.459 116.935 1.00 43.14 C ATOM 512 C GLU A 87 39.793 70.738 115.970 1.00 40.53 C ATOM 513 O GLU A 87 40.242 69.891 115.204 1.00 42.36 O ATOM 514 CB GLU A 87 40.686 70.740 118.276 1.00 46.35 C ATOM 515 CG GLU A 87 41.897 71.008 119.130 1.00 48.28 C ATOM 516 CD GLU A 87 41.783 70.346 120.485 1.00 54.26 C ATOM 517 OE1 GLU A 87 40.835 69.543 120.681 1.00 51.87 O ATOM 518 OE2 GLU A 87 42.642 70.635 121.353 1.00 54.91 O ATOM 519 N GLN A 88 38.508 71.057 116.038 1.00 38.98 N ATOM 520 CA GLN A 88 37.506 70.462 115.151 1.00 40.56 C ATOM 521 C GLN A 88 37.679 70.922 113.712 1.00 40.01 C ATOM 522 O GLN A 88 37.473 70.142 112.794 1.00 39.11 O ATOM 523 CB GLN A 88 36.091 70.769 115.638 1.00 41.85 C ATOM 524 CG GLN A 88 35.638 69.933 116.814 1.00 48.57 C ATOM 525 CD GLN A 88 34.126 70.007 117.021 1.00 70.38 C ATOM 526 OE1 GLN A 88 33.493 71.048 116.760 1.00 66.92 O ATOM 527 NE2 GLN A 88 33.531 68.895 117.491 1.00 80.30 N ATOM 528 N ILE A 89 38.055 72.184 113.523 1.00 37.96 N ATOM 529 CA ILE A 89 38.386 72.663 112.193 1.00 36.87 C ATOM 530 C ILE A 89 39.636 71.951 111.684 1.00 38.06 C ATOM 531 O ILE A 89 39.662 71.506 110.549 1.00 43.12 O ATOM 532 CB ILE A 89 38.539 74.191 112.133 1.00 35.06 C ATOM 533 CG1 ILE A 89 37.214 74.847 112.485 1.00 31.08 C ATOM 534 CG2 ILE A 89 38.946 74.627 110.754 1.00 31.45 C ATOM 535 CD1 ILE A 89 37.308 76.315 112.741 1.00 28.44 C ATOM 536 N GLU A 90 40.651 71.791 112.527 1.00 38.11 N ATOM 537 CA GLU A 90 41.865 71.072 112.127 1.00 40.62 C ATOM 538 C GLU A 90 41.617 69.636 111.688 1.00 41.96 C ATOM 539 O GLU A 90 42.303 69.132 110.807 1.00 45.41 O ATOM 540 CB GLU A 90 42.875 71.055 113.263 1.00 41.14 C ATOM 541 CG GLU A 90 43.592 72.358 113.476 1.00 42.65 C ATOM 542 CD GLU A 90 44.336 72.421 114.812 1.00 49.39 C ATOM 543 OE1 GLU A 90 44.215 71.464 115.613 1.00 48.84 O ATOM 544 OE2 GLU A 90 45.037 73.438 115.052 1.00 49.17 O ATOM 545 N ASP A 91 40.649 68.976 112.317 1.00 39.66 N ATOM 546 CA ASP A 91 40.374 67.574 112.037 1.00 41.10 C ATOM 547 C ASP A 91 39.560 67.436 110.756 1.00 42.88 C ATOM 548 O ASP A 91 39.498 66.364 110.155 1.00 46.73 O ATOM 549 CB ASP A 91 39.632 66.889 113.201 1.00 46.92 C ATOM 550 CG ASP A 91 40.538 66.613 114.445 1.00 55.14 C ATOM 551 OD1 ASP A 91 41.796 66.601 114.328 1.00 58.25 O ATOM 552 OD2 ASP A 91 39.963 66.381 115.549 1.00 51.15 O ATOM 553 N ALA A 92 38.930 68.515 110.322 1.00 42.37 N ATOM 554 CA ALA A 92 38.189 68.444 109.078 1.00 37.34 C ATOM 555 C ALA A 92 39.070 68.807 107.887 1.00 40.94 C ATOM 556 O ALA A 92 38.738 68.497 106.756 1.00 42.14 O ATOM 557 CB ALA A 92 36.977 69.320 109.132 1.00 34.31 C ATOM 558 N ILE A 93 40.195 69.454 108.151 1.00 40.24 N ATOM 559 CA ILE A 93 41.095 69.894 107.093 1.00 43.59 C ATOM 560 C ILE A 93 42.272 68.926 106.912 1.00 46.28 C ATOM 561 O ILE A 93 42.940 68.949 105.891 1.00 45.09 O ATOM 562 CB ILE A 93 41.619 71.320 107.384 1.00 43.84 C ATOM 563 CG1 ILE A 93 40.470 72.303 107.490 1.00 36.70 C ATOM 564 CG2 ILE A 93 42.569 71.814 106.305 1.00 43.65 C ATOM 565 CD1 ILE A 93 40.949 73.708 107.679 1.00 39.33 C ATOM 566 N GLN A 94 42.496 68.071 107.911 1.00 49.13 N ATOM 567 CA GLN A 94 43.581 67.090 107.904 1.00 49.78 C ATOM 568 C GLN A 94 43.728 66.420 106.555 1.00 48.96 C ATOM 569 O GLN A 94 42.762 65.878 106.014 1.00 45.28 O ATOM 570 CB GLN A 94 43.382 66.028 108.993 1.00 49.40 C ATOM 571 CG GLN A 94 44.615 65.159 109.269 1.00 53.35 C ATOM 572 CD GLN A 94 45.616 65.814 110.251 1.00 69.55 C ATOM 573 OE1 GLN A 94 45.232 66.634 111.100 1.00 70.78 O ATOM 574 NE2 GLN A 94 46.900 65.442 110.139 1.00 62.38 N ATOM 575 N GLY A 95 44.936 66.501 106.006 1.00 49.04 N ATOM 576 CA GLY A 95 45.287 65.806 104.782 1.00 48.23 C ATOM 577 C GLY A 95 45.049 66.572 103.500 1.00 47.41 C ATOM 578 O GLY A 95 45.195 66.021 102.413 1.00 55.86 O ATOM 579 N ALA A 96 44.685 67.843 103.609 1.00 46.59 N ATOM 580 CA ALA A 96 44.420 68.648 102.415 1.00 44.75 C ATOM 581 C ALA A 96 45.686 69.315 101.905 1.00 46.18 C ATOM 582 O ALA A 96 46.490 69.816 102.685 1.00 45.53 O ATOM 583 CB ALA A 96 43.355 69.686 102.686 1.00 41.49 C ATOM 584 N ASP A 97 45.849 69.324 100.587 1.00 44.47 N ATOM 585 CA ASP A 97 46.995 69.962 99.964 1.00 44.33 C ATOM 586 C ASP A 97 46.674 71.394 99.630 1.00 41.77 C ATOM 587 O ASP A 97 47.499 72.275 99.832 1.00 42.15 O ATOM 588 CB ASP A 97 47.417 69.224 98.694 1.00 48.45 C ATOM 589 CG ASP A 97 47.894 67.814 98.969 1.00 55.55 C ATOM 590 OD1 ASP A 97 48.762 67.624 99.855 1.00 56.02 O ATOM 591 OD2 ASP A 97 47.384 66.892 98.300 1.00 57.55 O HETATM 592 N MSE A 98 45.483 71.627 99.107 1.00 37.83 N HETATM 593 CA MSE A 98 45.053 72.987 98.838 1.00 37.92 C HETATM 594 C MSE A 98 43.734 73.223 99.551 1.00 38.54 C HETATM 595 O MSE A 98 42.976 72.292 99.767 1.00 41.67 O HETATM 596 CB MSE A 98 44.918 73.243 97.320 1.00 40.24 C HETATM 597 CG MSE A 98 44.556 74.703 96.959 1.00 42.66 C HETATM 598 SE MSE A 98 44.931 75.282 95.139 0.60 38.89 Se HETATM 599 CE MSE A 98 46.707 74.507 95.051 1.00 50.58 C ATOM 600 N VAL A 99 43.461 74.465 99.920 1.00 35.43 N ATOM 601 CA VAL A 99 42.187 74.812 100.532 1.00 31.45 C ATOM 602 C VAL A 99 41.597 76.106 99.961 1.00 33.27 C ATOM 603 O VAL A 99 42.300 77.082 99.740 1.00 35.55 O ATOM 604 CB VAL A 99 42.295 74.856 102.061 1.00 31.04 C ATOM 605 CG1 VAL A 99 41.354 75.858 102.628 1.00 31.55 C ATOM 606 CG2 VAL A 99 42.040 73.488 102.628 1.00 32.33 C ATOM 607 N PHE A 100 40.296 76.070 99.693 1.00 32.69 N ATOM 608 CA PHE A 100 39.529 77.205 99.213 1.00 30.50 C ATOM 609 C PHE A 100 38.547 77.606 100.303 1.00 29.13 C ATOM 610 O PHE A 100 37.699 76.809 100.661 1.00 33.63 O ATOM 611 CB PHE A 100 38.703 76.759 98.014 1.00 35.72 C ATOM 612 CG PHE A 100 39.372 76.938 96.701 1.00 38.50 C ATOM 613 CD1 PHE A 100 39.346 78.154 96.075 1.00 44.48 C ATOM 614 CD2 PHE A 100 39.988 75.879 96.062 1.00 46.78 C ATOM 615 CE1 PHE A 100 39.962 78.333 94.815 1.00 53.36 C ATOM 616 CE2 PHE A 100 40.608 76.038 94.806 1.00 51.34 C ATOM 617 CZ PHE A 100 40.593 77.264 94.183 1.00 52.69 C ATOM 618 N VAL A 101 38.646 78.826 100.820 1.00 28.06 N ATOM 619 CA VAL A 101 37.758 79.286 101.884 1.00 29.19 C ATOM 620 C VAL A 101 36.976 80.479 101.395 1.00 30.09 C ATOM 621 O VAL A 101 37.556 81.403 100.857 1.00 28.10 O ATOM 622 CB VAL A 101 38.539 79.744 103.135 1.00 28.55 C ATOM 623 CG1 VAL A 101 37.601 80.275 104.173 1.00 26.21 C ATOM 624 CG2 VAL A 101 39.335 78.620 103.703 1.00 29.64 C ATOM 625 N THR A 102 35.662 80.463 101.590 1.00 29.01 N ATOM 626 CA THR A 102 34.825 81.585 101.195 1.00 28.05 C ATOM 627 C THR A 102 33.780 81.862 102.261 1.00 27.63 C ATOM 628 O THR A 102 33.368 80.967 102.967 1.00 30.26 O ATOM 629 CB THR A 102 34.115 81.321 99.841 1.00 29.13 C ATOM 630 OG1 THR A 102 33.476 82.517 99.373 1.00 32.43 O ATOM 631 CG2 THR A 102 33.085 80.223 99.983 1.00 28.17 C ATOM 632 N SER A 103 33.357 83.109 102.385 1.00 30.33 N ATOM 633 CA SER A 103 32.216 83.403 103.220 1.00 29.92 C ATOM 634 C SER A 103 31.092 83.947 102.356 1.00 33.82 C ATOM 635 O SER A 103 30.183 84.585 102.844 1.00 33.07 O ATOM 636 CB SER A 103 32.581 84.349 104.373 1.00 27.46 C ATOM 637 OG SER A 103 33.006 85.616 103.924 1.00 32.08 O ATOM 638 N GLY A 104 31.174 83.679 101.058 1.00 34.37 N ATOM 639 CA GLY A 104 30.144 84.054 100.103 1.00 34.34 C ATOM 640 C GLY A 104 29.592 85.469 100.204 1.00 38.66 C ATOM 641 O GLY A 104 30.319 86.423 100.475 1.00 38.69 O HETATM 642 N MSE A 105 28.289 85.601 99.986 1.00 38.29 N HETATM 643 CA MSE A 105 27.630 86.892 100.078 1.00 37.54 C HETATM 644 C MSE A 105 27.163 87.112 101.495 1.00 42.75 C HETATM 645 O MSE A 105 27.272 86.228 102.336 1.00 44.79 O HETATM 646 CB MSE A 105 26.417 86.935 99.163 1.00 35.77 C HETATM 647 CG MSE A 105 26.680 86.461 97.758 1.00 38.71 C HETATM 648 SE MSE A 105 27.848 87.652 96.829 0.60 38.93 Se HETATM 649 CE MSE A 105 26.585 89.031 96.278 1.00 38.85 C ATOM 650 N GLY A 106 26.624 88.295 101.758 1.00 43.20 N ATOM 651 CA GLY A 106 26.041 88.593 103.055 1.00 46.15 C ATOM 652 C GLY A 106 27.050 88.778 104.173 1.00 49.64 C ATOM 653 O GLY A 106 28.252 88.543 104.001 1.00 49.12 O ATOM 654 N GLY A 107 26.546 89.209 105.327 1.00 50.23 N ATOM 655 CA GLY A 107 27.374 89.464 106.496 1.00 50.16 C ATOM 656 C GLY A 107 27.337 88.316 107.486 1.00 48.26 C ATOM 657 O GLY A 107 27.526 87.157 107.116 1.00 51.96 O ATOM 658 N GLY A 108 27.082 88.630 108.749 1.00 42.67 N ATOM 659 CA GLY A 108 27.009 87.610 109.781 1.00 40.40 C ATOM 660 C GLY A 108 28.360 87.246 110.356 1.00 36.02 C ATOM 661 O GLY A 108 29.323 87.995 110.250 1.00 32.97 O ATOM 662 N THR A 109 28.429 86.068 110.954 1.00 32.98 N ATOM 663 CA THR A 109 29.617 85.655 111.686 1.00 28.78 C ATOM 664 C THR A 109 30.747 85.119 110.807 1.00 29.71 C ATOM 665 O THR A 109 31.887 85.080 111.243 1.00 29.48 O ATOM 666 CB THR A 109 29.277 84.620 112.754 1.00 28.66 C ATOM 667 OG1 THR A 109 28.688 83.480 112.130 1.00 33.22 O ATOM 668 CG2 THR A 109 28.324 85.194 113.729 1.00 32.77 C ATOM 669 N GLY A 110 30.432 84.718 109.579 1.00 29.06 N ATOM 670 CA GLY A 110 31.409 84.098 108.705 1.00 27.95 C ATOM 671 C GLY A 110 32.535 85.019 108.312 1.00 28.13 C ATOM 672 O GLY A 110 33.668 84.603 108.165 1.00 29.12 O ATOM 673 N THR A 111 32.202 86.285 108.154 1.00 27.92 N ATOM 674 CA THR A 111 33.159 87.323 107.839 1.00 29.46 C ATOM 675 C THR A 111 34.358 87.331 108.780 1.00 32.27 C ATOM 676 O THR A 111 35.492 87.634 108.372 1.00 34.29 O ATOM 677 CB THR A 111 32.469 88.675 107.945 1.00 33.81 C ATOM 678 OG1 THR A 111 31.321 88.682 107.093 1.00 40.63 O ATOM 679 CG2 THR A 111 33.399 89.796 107.541 1.00 37.77 C ATOM 680 N GLY A 112 34.098 87.017 110.047 1.00 29.24 N ATOM 681 CA GLY A 112 35.126 86.974 111.055 1.00 26.94 C ATOM 682 C GLY A 112 35.753 85.608 111.131 1.00 26.75 C ATOM 683 O GLY A 112 36.946 85.486 111.333 1.00 28.82 O ATOM 684 N ALA A 113 34.955 84.572 110.957 1.00 27.40 N ATOM 685 CA ALA A 113 35.460 83.218 111.109 1.00 25.04 C ATOM 686 C ALA A 113 36.328 82.762 109.949 1.00 27.08 C ATOM 687 O ALA A 113 37.310 82.062 110.149 1.00 28.82 O ATOM 688 CB ALA A 113 34.318 82.258 111.309 1.00 26.52 C ATOM 689 N ALA A 114 35.951 83.154 108.736 1.00 27.83 N ATOM 690 CA ALA A 114 36.632 82.693 107.525 1.00 25.61 C ATOM 691 C ALA A 114 38.133 82.962 107.493 1.00 27.58 C ATOM 692 O ALA A 114 38.891 82.114 107.051 1.00 28.27 O ATOM 693 CB ALA A 114 35.959 83.235 106.282 1.00 26.51 C ATOM 694 N PRO A 115 38.565 84.147 107.954 1.00 27.77 N ATOM 695 CA PRO A 115 40.008 84.346 108.115 1.00 28.95 C ATOM 696 C PRO A 115 40.648 83.350 109.085 1.00 31.41 C ATOM 697 O PRO A 115 41.762 82.876 108.845 1.00 30.32 O ATOM 698 CB PRO A 115 40.095 85.756 108.693 1.00 27.78 C ATOM 699 CG PRO A 115 38.918 86.431 108.153 1.00 31.49 C ATOM 700 CD PRO A 115 37.832 85.415 108.114 1.00 26.69 C ATOM 701 N VAL A 116 39.957 83.027 110.167 1.00 27.03 N ATOM 702 CA VAL A 116 40.563 82.159 111.148 1.00 27.22 C ATOM 703 C VAL A 116 40.670 80.771 110.568 1.00 30.21 C ATOM 704 O VAL A 116 41.680 80.110 110.726 1.00 30.77 O ATOM 705 CB VAL A 116 39.817 82.155 112.506 1.00 28.46 C ATOM 706 CG1 VAL A 116 40.428 81.126 113.425 1.00 31.42 C ATOM 707 CG2 VAL A 116 39.862 83.523 113.139 1.00 29.01 C ATOM 708 N VAL A 117 39.630 80.339 109.873 1.00 25.54 N ATOM 709 CA VAL A 117 39.684 79.069 109.157 1.00 28.26 C ATOM 710 C VAL A 117 40.863 79.021 108.172 1.00 30.22 C ATOM 711 O VAL A 117 41.616 78.068 108.141 1.00 28.98 O ATOM 712 CB VAL A 117 38.374 78.797 108.409 1.00 28.82 C ATOM 713 CG1 VAL A 117 38.436 77.464 107.711 1.00 30.62 C ATOM 714 CG2 VAL A 117 37.208 78.843 109.364 1.00 25.97 C ATOM 715 N ALA A 118 41.030 80.069 107.385 1.00 28.79 N ATOM 716 CA ALA A 118 42.158 80.175 106.478 1.00 31.16 C ATOM 717 C ALA A 118 43.494 80.063 107.196 1.00 33.46 C ATOM 718 O ALA A 118 44.376 79.325 106.760 1.00 35.24 O ATOM 719 CB ALA A 118 42.089 81.487 105.712 1.00 30.34 C ATOM 720 N LYS A 119 43.639 80.810 108.286 1.00 33.72 N ATOM 721 CA LYS A 119 44.859 80.811 109.085 1.00 31.43 C ATOM 722 C LYS A 119 45.157 79.438 109.659 1.00 33.72 C ATOM 723 O LYS A 119 46.303 79.038 109.756 1.00 36.73 O ATOM 724 CB LYS A 119 44.723 81.829 110.210 1.00 33.85 C ATOM 725 CG LYS A 119 45.939 82.008 111.080 1.00 39.81 C ATOM 726 CD LYS A 119 45.528 82.475 112.471 1.00 41.72 C ATOM 727 CE LYS A 119 44.813 81.350 113.236 1.00 47.57 C ATOM 728 NZ LYS A 119 44.375 81.705 114.640 1.00 52.53 N ATOM 729 N ILE A 120 44.121 78.710 110.033 1.00 34.72 N ATOM 730 CA ILE A 120 44.317 77.365 110.533 1.00 34.11 C ATOM 731 C ILE A 120 44.875 76.455 109.458 1.00 34.63 C ATOM 732 O ILE A 120 45.802 75.699 109.714 1.00 41.60 O ATOM 733 CB ILE A 120 43.018 76.747 111.046 1.00 32.06 C ATOM 734 CG1 ILE A 120 42.631 77.345 112.386 1.00 32.78 C ATOM 735 CG2 ILE A 120 43.169 75.265 111.195 1.00 31.57 C ATOM 736 CD1 ILE A 120 41.295 76.892 112.847 1.00 33.00 C ATOM 737 N ALA A 121 44.317 76.519 108.254 1.00 36.04 N ATOM 738 CA ALA A 121 44.734 75.622 107.190 1.00 35.23 C ATOM 739 C ALA A 121 46.154 75.935 106.745 1.00 40.17 C ATOM 740 O ALA A 121 46.920 75.032 106.414 1.00 42.16 O ATOM 741 CB ALA A 121 43.780 75.687 106.040 1.00 34.64 C ATOM 742 N LYS A 122 46.524 77.205 106.757 1.00 38.77 N ATOM 743 CA LYS A 122 47.902 77.553 106.456 1.00 41.14 C ATOM 744 C LYS A 122 48.889 76.910 107.434 1.00 45.41 C ATOM 745 O LYS A 122 49.926 76.403 107.028 1.00 46.91 O ATOM 746 CB LYS A 122 48.070 79.064 106.453 1.00 38.45 C ATOM 747 CG LYS A 122 48.846 79.604 105.268 1.00 39.44 C ATOM 748 CD LYS A 122 48.465 81.064 105.028 1.00 40.89 C ATOM 749 CE LYS A 122 49.631 82.009 105.295 1.00 45.17 C ATOM 750 NZ LYS A 122 49.202 83.420 105.589 1.00 46.45 N ATOM 751 N GLU A 123 48.569 76.924 108.722 1.00 44.33 N ATOM 752 CA GLU A 123 49.468 76.337 109.707 1.00 46.93 C ATOM 753 C GLU A 123 49.469 74.810 109.615 1.00 50.14 C ATOM 754 O GLU A 123 50.367 74.143 110.144 1.00 52.31 O ATOM 755 CB GLU A 123 49.154 76.843 111.113 1.00 46.20 C ATOM 756 CG GLU A 123 49.613 78.280 111.315 1.00 52.77 C ATOM 757 CD GLU A 123 49.036 78.921 112.567 1.00 60.90 C ATOM 758 OE1 GLU A 123 48.388 78.198 113.369 1.00 60.14 O ATOM 759 OE2 GLU A 123 49.227 80.152 112.738 1.00 65.05 O HETATM 760 N MSE A 124 48.520 74.278 108.854 1.00 45.65 N HETATM 761 CA MSE A 124 48.536 72.881 108.485 1.00 48.67 C HETATM 762 C MSE A 124 49.423 72.719 107.282 1.00 49.03 C HETATM 763 O MSE A 124 49.886 71.592 107.012 1.00 50.96 O HETATM 764 CB MSE A 124 47.129 72.424 108.133 1.00 48.92 C HETATM 765 CG MSE A 124 46.147 72.840 109.218 1.00 52.21 C HETATM 766 SE MSE A 124 45.543 71.240 110.189 0.60 65.23 Se HETATM 767 CE MSE A 124 46.723 71.403 111.756 1.00 51.34 C ATOM 768 N GLY A 125 49.673 73.803 106.551 1.00 45.74 N ATOM 769 CA GLY A 125 50.563 73.746 105.397 1.00 48.86 C ATOM 770 C GLY A 125 49.888 73.550 104.046 1.00 47.60 C ATOM 771 O GLY A 125 50.550 73.396 103.014 1.00 43.22 O ATOM 772 N ALA A 126 48.561 73.544 104.067 1.00 43.87 N ATOM 773 CA ALA A 126 47.779 73.572 102.858 1.00 38.46 C ATOM 774 C ALA A 126 47.937 74.938 102.222 1.00 40.57 C ATOM 775 O ALA A 126 47.950 75.942 102.911 1.00 41.79 O ATOM 776 CB ALA A 126 46.351 73.331 103.184 1.00 37.73 C ATOM 777 N LEU A 127 48.083 74.971 100.908 1.00 38.26 N ATOM 778 CA LEU A 127 47.984 76.209 100.158 1.00 37.03 C ATOM 779 C LEU A 127 46.577 76.764 100.312 1.00 37.22 C ATOM 780 O LEU A 127 45.606 76.107 99.977 1.00 36.62 O ATOM 781 CB LEU A 127 48.271 75.949 98.682 1.00 38.25 C ATOM 782 CG LEU A 127 48.565 77.225 97.915 1.00 39.18 C ATOM 783 CD1 LEU A 127 49.740 77.905 98.571 1.00 41.34 C ATOM 784 CD2 LEU A 127 48.870 76.929 96.478 1.00 39.36 C ATOM 785 N THR A 128 46.468 77.988 100.797 1.00 33.91 N ATOM 786 CA THR A 128 45.182 78.529 101.196 1.00 33.31 C ATOM 787 C THR A 128 44.753 79.672 100.302 1.00 31.20 C ATOM 788 O THR A 128 45.468 80.639 100.130 1.00 33.98 O ATOM 789 CB THR A 128 45.232 79.035 102.652 1.00 34.96 C ATOM 790 OG1 THR A 128 45.474 77.933 103.530 1.00 39.26 O ATOM 791 CG2 THR A 128 43.932 79.695 103.036 1.00 33.37 C ATOM 792 N VAL A 129 43.566 79.565 99.743 1.00 28.78 N ATOM 793 CA VAL A 129 43.111 80.567 98.820 1.00 30.35 C ATOM 794 C VAL A 129 41.823 81.159 99.339 1.00 30.91 C ATOM 795 O VAL A 129 40.892 80.432 99.636 1.00 32.07 O ATOM 796 CB VAL A 129 42.871 79.950 97.398 1.00 36.12 C ATOM 797 CG1 VAL A 129 42.452 81.025 96.394 1.00 32.52 C ATOM 798 CG2 VAL A 129 44.112 79.216 96.900 1.00 30.49 C ATOM 799 N GLY A 130 41.761 82.477 99.441 1.00 30.72 N ATOM 800 CA GLY A 130 40.519 83.123 99.798 1.00 29.39 C ATOM 801 C GLY A 130 39.699 83.516 98.579 1.00 32.64 C ATOM 802 O GLY A 130 40.179 84.239 97.721 1.00 34.24 O ATOM 803 N VAL A 131 38.459 83.036 98.512 1.00 31.30 N ATOM 804 CA VAL A 131 37.522 83.408 97.462 1.00 29.68 C ATOM 805 C VAL A 131 36.529 84.441 97.969 1.00 29.54 C ATOM 806 O VAL A 131 35.744 84.165 98.866 1.00 31.57 O ATOM 807 CB VAL A 131 36.736 82.183 97.003 1.00 30.53 C ATOM 808 CG1 VAL A 131 35.888 82.494 95.774 1.00 28.95 C ATOM 809 CG2 VAL A 131 37.695 81.029 96.755 1.00 31.02 C ATOM 810 N VAL A 132 36.564 85.635 97.394 1.00 29.29 N ATOM 811 CA VAL A 132 35.621 86.667 97.776 1.00 31.81 C ATOM 812 C VAL A 132 34.676 86.918 96.638 1.00 33.76 C ATOM 813 O VAL A 132 35.112 87.277 95.563 1.00 37.34 O ATOM 814 CB VAL A 132 36.311 88.006 98.099 1.00 32.83 C ATOM 815 CG1 VAL A 132 35.289 89.024 98.550 1.00 39.76 C ATOM 816 CG2 VAL A 132 37.347 87.819 99.161 1.00 35.44 C ATOM 817 N THR A 133 33.384 86.736 96.875 1.00 35.85 N ATOM 818 CA THR A 133 32.376 87.094 95.884 1.00 36.73 C ATOM 819 C THR A 133 31.542 88.288 96.361 1.00 38.00 C ATOM 820 O THR A 133 30.759 88.857 95.618 1.00 39.35 O ATOM 821 CB THR A 133 31.455 85.908 95.527 1.00 37.77 C ATOM 822 OG1 THR A 133 30.891 85.368 96.724 1.00 38.34 O ATOM 823 CG2 THR A 133 32.221 84.812 94.823 1.00 35.34 C ATOM 824 N ARG A 134 31.734 88.692 97.603 1.00 40.25 N ATOM 825 CA ARG A 134 30.919 89.765 98.142 1.00 41.48 C ATOM 826 C ARG A 134 31.426 91.126 97.697 1.00 47.57 C ATOM 827 O ARG A 134 32.598 91.451 97.876 1.00 50.88 O ATOM 828 CB ARG A 134 30.902 89.691 99.650 1.00 40.37 C ATOM 829 CG ARG A 134 30.068 90.737 100.288 1.00 45.30 C ATOM 830 CD ARG A 134 30.298 90.671 101.767 1.00 47.71 C ATOM 831 NE ARG A 134 29.308 91.406 102.539 1.00 50.58 N ATOM 832 CZ ARG A 134 29.463 91.673 103.830 1.00 54.97 C ATOM 833 NH1 ARG A 134 30.566 91.263 104.450 1.00 54.63 N ATOM 834 NH2 ARG A 134 28.537 92.352 104.498 1.00 52.44 N ATOM 835 N PRO A 135 30.542 91.935 97.106 1.00 51.85 N ATOM 836 CA PRO A 135 30.959 93.248 96.603 1.00 50.35 C ATOM 837 C PRO A 135 31.503 94.119 97.722 1.00 50.30 C ATOM 838 O PRO A 135 30.962 94.115 98.827 1.00 50.44 O ATOM 839 CB PRO A 135 29.661 93.846 96.064 1.00 47.33 C ATOM 840 CG PRO A 135 28.788 92.672 95.803 1.00 53.42 C ATOM 841 CD PRO A 135 29.115 91.675 96.861 1.00 52.97 C ATOM 842 N PHE A 136 32.570 94.849 97.432 1.00 50.34 N ATOM 843 CA PHE A 136 33.153 95.749 98.411 1.00 53.08 C ATOM 844 C PHE A 136 33.827 96.896 97.699 1.00 55.39 C ATOM 845 O PHE A 136 34.000 96.859 96.485 1.00 56.82 O ATOM 846 CB PHE A 136 34.176 95.021 99.274 1.00 54.01 C ATOM 847 CG PHE A 136 35.364 94.530 98.511 1.00 53.80 C ATOM 848 CD1 PHE A 136 35.274 93.397 97.708 1.00 52.88 C ATOM 849 CD2 PHE A 136 36.575 95.195 98.588 1.00 54.22 C ATOM 850 CE1 PHE A 136 36.363 92.939 97.001 1.00 48.83 C ATOM 851 CE2 PHE A 136 37.674 94.730 97.876 1.00 56.42 C ATOM 852 CZ PHE A 136 37.562 93.601 97.091 1.00 51.57 C ATOM 853 N SER A 137 34.182 97.920 98.465 1.00 61.32 N ATOM 854 CA SER A 137 34.901 99.088 97.959 1.00 64.30 C ATOM 855 C SER A 137 35.601 99.804 99.124 1.00 67.05 C ATOM 856 O SER A 137 35.109 99.799 100.263 1.00 67.09 O ATOM 857 CB SER A 137 33.957 100.044 97.225 1.00 66.31 C ATOM 858 OG SER A 137 34.634 101.233 96.849 1.00 68.63 O ATOM 859 N PHE A 138 36.752 100.408 98.840 1.00 66.82 N ATOM 860 CA PHE A 138 37.604 100.942 99.900 1.00 68.14 C ATOM 861 C PHE A 138 37.849 102.476 99.867 1.00 70.74 C ATOM 862 O PHE A 138 38.333 103.051 100.864 1.00 73.10 O ATOM 863 CB PHE A 138 38.920 100.159 99.963 1.00 68.46 C ATOM 864 CG PHE A 138 38.992 99.206 101.120 1.00 70.17 C ATOM 865 CD1 PHE A 138 39.068 99.689 102.431 1.00 70.30 C ATOM 866 CD2 PHE A 138 38.976 97.833 100.914 1.00 63.87 C ATOM 867 CE1 PHE A 138 39.136 98.816 103.527 1.00 64.33 C ATOM 868 CE2 PHE A 138 39.041 96.950 102.001 1.00 64.84 C ATOM 869 CZ PHE A 138 39.123 97.449 103.312 1.00 65.18 C ATOM 870 N GLU A 139 37.523 103.123 98.737 1.00 70.20 N ATOM 871 CA GLU A 139 37.599 104.590 98.628 1.00 72.37 C ATOM 872 C GLU A 139 36.690 105.329 99.643 1.00 73.32 C ATOM 873 O GLU A 139 35.500 105.002 99.814 1.00 76.41 O ATOM 874 CB GLU A 139 37.310 105.060 97.183 1.00 70.31 C ATOM 875 CG GLU A 139 35.996 104.530 96.541 1.00 73.81 C ATOM 876 CD GLU A 139 36.112 104.303 94.999 1.00 78.77 C ATOM 877 OE1 GLU A 139 36.983 104.954 94.360 1.00 76.14 O ATOM 878 OE2 GLU A 139 35.333 103.461 94.441 1.00 75.86 O ATOM 879 N THR A 145 32.050 99.449 104.169 1.00 63.95 N ATOM 880 CA THR A 145 33.202 99.335 105.080 1.00 68.97 C ATOM 881 C THR A 145 33.179 98.065 105.962 1.00 67.49 C ATOM 882 O THR A 145 34.242 97.545 106.321 1.00 67.16 O ATOM 883 CB THR A 145 33.420 100.632 105.960 1.00 65.99 C ATOM 884 OG1 THR A 145 34.789 100.717 106.390 1.00 59.20 O ATOM 885 CG2 THR A 145 32.490 100.656 107.179 1.00 60.24 C ATOM 886 N GLN A 146 31.987 97.565 106.303 1.00 66.93 N ATOM 887 CA GLN A 146 31.879 96.308 107.062 1.00 66.52 C ATOM 888 C GLN A 146 32.282 95.104 106.182 1.00 62.52 C ATOM 889 O GLN A 146 33.034 94.224 106.616 1.00 60.15 O ATOM 890 CB GLN A 146 30.472 96.106 107.672 1.00 65.26 C ATOM 891 CG GLN A 146 29.689 97.389 108.019 1.00 66.88 C ATOM 892 CD GLN A 146 28.785 97.875 106.859 1.00 78.01 C ATOM 893 OE1 GLN A 146 29.214 97.923 105.685 1.00 72.48 O ATOM 894 NE2 GLN A 146 27.522 98.228 107.189 1.00 72.59 N ATOM 895 N ALA A 147 31.792 95.078 104.944 1.00 57.72 N ATOM 896 CA ALA A 147 32.243 94.075 103.979 1.00 60.03 C ATOM 897 C ALA A 147 33.726 94.242 103.726 1.00 57.36 C ATOM 898 O ALA A 147 34.487 93.279 103.785 1.00 53.57 O ATOM 899 CB ALA A 147 31.486 94.200 102.671 1.00 57.73 C ATOM 900 N ALA A 148 34.125 95.478 103.448 1.00 58.91 N ATOM 901 CA ALA A 148 35.523 95.795 103.175 1.00 60.45 C ATOM 902 C ALA A 148 36.466 95.346 104.298 1.00 57.18 C ATOM 903 O ALA A 148 37.564 94.844 104.041 1.00 54.22 O ATOM 904 CB ALA A 148 35.675 97.285 102.905 1.00 62.30 C ATOM 905 N ALA A 149 36.028 95.525 105.542 1.00 58.31 N ATOM 906 CA ALA A 149 36.796 95.064 106.697 1.00 59.73 C ATOM 907 C ALA A 149 37.070 93.560 106.576 1.00 54.88 C ATOM 908 O ALA A 149 38.192 93.092 106.789 1.00 49.93 O ATOM 909 CB ALA A 149 36.048 95.378 107.999 1.00 59.95 C ATOM 910 N GLY A 150 36.033 92.815 106.209 1.00 53.49 N ATOM 911 CA GLY A 150 36.150 91.377 106.048 1.00 51.52 C ATOM 912 C GLY A 150 37.147 90.956 104.985 1.00 50.36 C ATOM 913 O GLY A 150 37.903 89.997 105.193 1.00 46.27 O ATOM 914 N VAL A 151 37.149 91.674 103.861 1.00 49.59 N ATOM 915 CA VAL A 151 38.080 91.427 102.780 1.00 44.76 C ATOM 916 C VAL A 151 39.536 91.593 103.229 1.00 46.83 C ATOM 917 O VAL A 151 40.398 90.785 102.861 1.00 44.17 O ATOM 918 CB VAL A 151 37.798 92.355 101.588 1.00 49.40 C ATOM 919 CG1 VAL A 151 38.753 92.055 100.454 1.00 45.42 C ATOM 920 CG2 VAL A 151 36.392 92.168 101.095 1.00 46.96 C ATOM 921 N GLU A 152 39.813 92.624 104.030 1.00 48.21 N ATOM 922 CA GLU A 152 41.183 92.870 104.513 1.00 49.00 C ATOM 923 C GLU A 152 41.678 91.757 105.431 1.00 45.51 C ATOM 924 O GLU A 152 42.828 91.328 105.341 1.00 45.11 O ATOM 925 CB GLU A 152 41.303 94.243 105.197 1.00 53.16 C ATOM 926 CG GLU A 152 42.582 94.472 106.021 1.00 57.34 C ATOM 927 CD GLU A 152 43.908 94.406 105.212 1.00 67.98 C ATOM 928 OE1 GLU A 152 44.633 93.371 105.303 1.00 60.69 O ATOM 929 OE2 GLU A 152 44.252 95.401 104.514 1.00 68.26 O ATOM 930 N ALA A 153 40.800 91.278 106.303 1.00 46.00 N ATOM 931 CA ALA A 153 41.174 90.216 107.232 1.00 42.09 C ATOM 932 C ALA A 153 41.473 88.941 106.466 1.00 40.53 C ATOM 933 O ALA A 153 42.474 88.289 106.730 1.00 39.77 O ATOM 934 CB ALA A 153 40.080 89.986 108.280 1.00 40.65 C HETATM 935 N MSE A 154 40.618 88.600 105.506 1.00 37.38 N HETATM 936 CA MSE A 154 40.866 87.437 104.678 1.00 34.96 C HETATM 937 C MSE A 154 42.240 87.539 104.026 1.00 35.41 C HETATM 938 O MSE A 154 42.995 86.571 103.988 1.00 32.89 O HETATM 939 CB MSE A 154 39.795 87.293 103.597 1.00 34.04 C HETATM 940 CG MSE A 154 39.895 85.998 102.807 1.00 30.71 C HETATM 941 SE MSE A 154 39.627 84.404 103.843 0.60 22.79 Se HETATM 942 CE MSE A 154 37.850 83.999 103.305 1.00 27.95 C ATOM 943 N LYS A 155 42.570 88.727 103.536 1.00 36.31 N ATOM 944 CA LYS A 155 43.797 88.903 102.775 1.00 37.16 C ATOM 945 C LYS A 155 45.061 88.768 103.614 1.00 37.59 C ATOM 946 O LYS A 155 46.103 88.347 103.118 1.00 37.75 O ATOM 947 CB LYS A 155 43.793 90.231 102.035 1.00 39.74 C ATOM 948 CG LYS A 155 44.927 90.342 101.040 1.00 41.15 C ATOM 949 CD LYS A 155 44.831 91.611 100.259 1.00 43.84 C ATOM 950 CE LYS A 155 46.187 92.193 100.020 1.00 44.43 C ATOM 951 NZ LYS A 155 46.825 92.675 101.266 1.00 52.55 N ATOM 952 N ALA A 156 44.973 89.121 104.886 1.00 38.29 N ATOM 953 CA ALA A 156 46.106 88.944 105.775 1.00 33.26 C ATOM 954 C ALA A 156 46.320 87.467 106.087 1.00 34.13 C ATOM 955 O ALA A 156 47.439 87.038 106.341 1.00 38.91 O ATOM 956 CB ALA A 156 45.905 89.732 107.035 1.00 33.76 C ATOM 957 N ALA A 157 45.249 86.686 106.021 1.00 33.34 N ATOM 958 CA ALA A 157 45.267 85.299 106.477 1.00 30.65 C ATOM 959 C ALA A 157 45.552 84.240 105.414 1.00 34.42 C ATOM 960 O ALA A 157 45.882 83.106 105.732 1.00 37.28 O ATOM 961 CB ALA A 157 43.963 84.981 107.158 1.00 30.51 C ATOM 962 N VAL A 158 45.395 84.584 104.150 1.00 35.57 N ATOM 963 CA VAL A 158 45.519 83.572 103.108 1.00 33.03 C ATOM 964 C VAL A 158 46.837 83.689 102.368 1.00 36.05 C ATOM 965 O VAL A 158 47.509 84.707 102.451 1.00 38.58 O ATOM 966 CB VAL A 158 44.376 83.682 102.085 1.00 32.98 C ATOM 967 CG1 VAL A 158 43.047 83.326 102.718 1.00 29.96 C ATOM 968 CG2 VAL A 158 44.330 85.075 101.507 1.00 32.92 C ATOM 969 N ASP A 159 47.208 82.642 101.648 1.00 35.63 N ATOM 970 CA ASP A 159 48.344 82.729 100.739 1.00 39.10 C ATOM 971 C ASP A 159 48.007 83.629 99.547 1.00 37.49 C ATOM 972 O ASP A 159 48.773 84.511 99.184 1.00 42.57 O ATOM 973 CB ASP A 159 48.761 81.340 100.247 1.00 39.59 C ATOM 974 CG ASP A 159 49.417 80.504 101.328 1.00 41.40 C ATOM 975 OD1 ASP A 159 50.203 81.057 102.133 1.00 44.68 O ATOM 976 OD2 ASP A 159 49.148 79.284 101.371 1.00 42.90 O ATOM 977 N THR A 160 46.845 83.403 98.954 1.00 37.65 N ATOM 978 CA THR A 160 46.382 84.200 97.829 1.00 37.83 C ATOM 979 C THR A 160 44.887 84.529 97.927 1.00 35.29 C ATOM 980 O THR A 160 44.071 83.663 98.242 1.00 35.40 O ATOM 981 CB THR A 160 46.651 83.452 96.505 1.00 40.92 C ATOM 982 OG1 THR A 160 48.064 83.301 96.314 1.00 44.56 O ATOM 983 CG2 THR A 160 46.065 84.211 95.334 1.00 39.00 C ATOM 984 N LEU A 161 44.546 85.784 97.653 1.00 31.90 N ATOM 985 CA LEU A 161 43.163 86.209 97.570 1.00 30.69 C ATOM 986 C LEU A 161 42.737 86.314 96.127 1.00 32.06 C ATOM 987 O LEU A 161 43.409 86.951 95.337 1.00 32.82 O ATOM 988 CB LEU A 161 43.018 87.586 98.196 1.00 30.99 C ATOM 989 CG LEU A 161 41.584 88.046 98.426 1.00 32.88 C ATOM 990 CD1 LEU A 161 40.969 87.148 99.450 1.00 33.89 C ATOM 991 CD2 LEU A 161 41.507 89.478 98.875 1.00 33.25 C ATOM 992 N ILE A 162 41.613 85.704 95.782 1.00 30.45 N ATOM 993 CA ILE A 162 41.021 85.928 94.472 1.00 29.47 C ATOM 994 C ILE A 162 39.610 86.494 94.528 1.00 32.46 C ATOM 995 O ILE A 162 38.728 85.951 95.173 1.00 31.50 O ATOM 996 CB ILE A 162 41.016 84.669 93.607 1.00 31.18 C ATOM 997 CG1 ILE A 162 40.478 85.018 92.212 1.00 34.57 C ATOM 998 CG2 ILE A 162 40.212 83.559 94.273 1.00 30.58 C ATOM 999 CD1 ILE A 162 40.716 83.976 91.165 1.00 33.33 C ATOM 1000 N VAL A 163 39.402 87.606 93.852 1.00 31.11 N ATOM 1001 CA VAL A 163 38.066 88.156 93.746 1.00 33.63 C ATOM 1002 C VAL A 163 37.410 87.709 92.447 1.00 35.46 C ATOM 1003 O VAL A 163 38.031 87.745 91.393 1.00 37.86 O ATOM 1004 CB VAL A 163 38.094 89.675 93.820 1.00 35.21 C ATOM 1005 CG1 VAL A 163 36.742 90.239 93.452 1.00 38.86 C ATOM 1006 CG2 VAL A 163 38.495 90.112 95.220 1.00 35.10 C ATOM 1007 N ILE A 164 36.164 87.265 92.540 1.00 35.76 N ATOM 1008 CA ILE A 164 35.464 86.693 91.405 1.00 37.84 C ATOM 1009 C ILE A 164 34.005 87.028 91.568 1.00 37.04 C ATOM 1010 O ILE A 164 33.557 87.249 92.672 1.00 38.04 O ATOM 1011 CB ILE A 164 35.651 85.175 91.356 1.00 37.81 C ATOM 1012 CG1 ILE A 164 35.225 84.626 90.003 1.00 41.61 C ATOM 1013 CG2 ILE A 164 34.885 84.490 92.466 1.00 37.13 C ATOM 1014 CD1 ILE A 164 35.261 83.117 89.918 1.00 42.66 C ATOM 1015 N PRO A 165 33.264 87.146 90.468 1.00 42.17 N ATOM 1016 CA PRO A 165 31.843 87.425 90.693 1.00 39.22 C ATOM 1017 C PRO A 165 31.055 86.186 91.092 1.00 43.34 C ATOM 1018 O PRO A 165 31.436 85.061 90.774 1.00 44.87 O ATOM 1019 CB PRO A 165 31.361 87.970 89.349 1.00 41.11 C ATOM 1020 CG PRO A 165 32.408 87.627 88.373 1.00 44.40 C ATOM 1021 CD PRO A 165 33.692 87.491 89.101 1.00 45.07 C ATOM 1022 N ASN A 166 29.955 86.413 91.796 1.00 43.96 N ATOM 1023 CA ASN A 166 29.172 85.348 92.392 1.00 42.92 C ATOM 1024 C ASN A 166 28.592 84.368 91.369 1.00 42.74 C ATOM 1025 O ASN A 166 28.655 83.155 91.559 1.00 41.77 O ATOM 1026 CB ASN A 166 28.081 85.971 93.248 1.00 42.89 C ATOM 1027 CG ASN A 166 27.381 84.970 94.100 1.00 43.96 C ATOM 1028 OD1 ASN A 166 27.973 83.988 94.544 1.00 45.68 O ATOM 1029 ND2 ASN A 166 26.102 85.198 94.332 1.00 43.42 N ATOM 1030 N ASP A 167 28.046 84.905 90.278 1.00 47.05 N ATOM 1031 CA ASP A 167 27.575 84.094 89.136 1.00 48.39 C ATOM 1032 C ASP A 167 28.669 83.310 88.430 1.00 46.47 C ATOM 1033 O ASP A 167 28.385 82.425 87.639 1.00 50.93 O ATOM 1034 CB ASP A 167 26.869 84.969 88.095 1.00 56.39 C ATOM 1035 CG ASP A 167 27.619 86.259 87.819 1.00 60.37 C ATOM 1036 OD1 ASP A 167 28.120 86.868 88.815 1.00 60.28 O ATOM 1037 OD2 ASP A 167 27.699 86.657 86.623 1.00 59.88 O ATOM 1038 N ARG A 168 29.918 83.647 88.695 1.00 46.08 N ATOM 1039 CA ARG A 168 31.021 82.873 88.148 1.00 48.89 C ATOM 1040 C ARG A 168 31.625 81.892 89.150 1.00 45.95 C ATOM 1041 O ARG A 168 32.646 81.295 88.862 1.00 45.97 O ATOM 1042 CB ARG A 168 32.104 83.801 87.597 1.00 48.79 C ATOM 1043 CG ARG A 168 31.575 84.885 86.664 1.00 54.45 C ATOM 1044 CD ARG A 168 30.907 84.315 85.428 1.00 53.22 C ATOM 1045 NE ARG A 168 31.704 83.219 84.884 1.00 62.11 N ATOM 1046 CZ ARG A 168 31.185 82.081 84.416 1.00 67.32 C ATOM 1047 NH1 ARG A 168 29.860 81.903 84.423 1.00 61.81 N ATOM 1048 NH2 ARG A 168 31.987 81.124 83.940 1.00 65.77 N ATOM 1049 N LEU A 169 30.978 81.713 90.302 1.00 44.77 N ATOM 1050 CA LEU A 169 31.514 80.878 91.377 1.00 43.56 C ATOM 1051 C LEU A 169 31.884 79.469 90.952 1.00 43.54 C ATOM 1052 O LEU A 169 32.911 78.935 91.363 1.00 44.29 O ATOM 1053 CB LEU A 169 30.553 80.822 92.572 1.00 45.60 C ATOM 1054 CG LEU A 169 31.005 79.977 93.782 1.00 44.76 C ATOM 1055 CD1 LEU A 169 32.200 80.589 94.506 1.00 42.41 C ATOM 1056 CD2 LEU A 169 29.863 79.718 94.761 1.00 40.20 C ATOM 1057 N LEU A 170 31.053 78.869 90.120 1.00 46.66 N ATOM 1058 CA LEU A 170 31.258 77.470 89.759 1.00 48.09 C ATOM 1059 C LEU A 170 32.593 77.220 89.004 1.00 51.24 C ATOM 1060 O LEU A 170 33.127 76.101 89.005 1.00 53.36 O ATOM 1061 CB LEU A 170 30.011 76.920 89.048 1.00 44.02 C ATOM 1062 CG LEU A 170 28.795 76.977 89.995 1.00 44.03 C ATOM 1063 CD1 LEU A 170 27.446 76.982 89.310 1.00 41.51 C ATOM 1064 CD2 LEU A 170 28.873 75.797 90.893 1.00 45.54 C ATOM 1065 N ASP A 171 33.162 78.271 88.414 1.00 52.94 N ATOM 1066 CA ASP A 171 34.489 78.176 87.785 1.00 53.76 C ATOM 1067 C ASP A 171 35.610 77.688 88.704 1.00 51.60 C ATOM 1068 O ASP A 171 36.524 76.983 88.257 1.00 50.20 O ATOM 1069 CB ASP A 171 34.908 79.524 87.219 1.00 53.11 C ATOM 1070 CG ASP A 171 34.087 79.921 86.043 1.00 59.14 C ATOM 1071 OD1 ASP A 171 33.408 79.022 85.492 1.00 60.27 O ATOM 1072 OD2 ASP A 171 34.135 81.117 85.665 1.00 63.32 O ATOM 1073 N ILE A 172 35.566 78.079 89.975 1.00 51.09 N ATOM 1074 CA ILE A 172 36.657 77.693 90.856 1.00 53.38 C ATOM 1075 C ILE A 172 36.635 76.200 91.086 1.00 51.43 C ATOM 1076 O ILE A 172 37.669 75.613 91.376 1.00 54.55 O ATOM 1077 CB ILE A 172 36.704 78.465 92.202 1.00 54.75 C ATOM 1078 CG1 ILE A 172 35.772 77.812 93.233 1.00 53.25 C ATOM 1079 CG2 ILE A 172 36.461 79.980 91.969 1.00 49.49 C ATOM 1080 CD1 ILE A 172 35.758 78.504 94.591 1.00 48.40 C ATOM 1081 N VAL A 173 35.476 75.573 90.911 1.00 53.11 N ATOM 1082 CA VAL A 173 35.400 74.123 91.077 1.00 54.55 C ATOM 1083 C VAL A 173 35.396 73.414 89.718 1.00 51.51 C ATOM 1084 O VAL A 173 35.887 72.291 89.576 1.00 52.43 O ATOM 1085 CB VAL A 173 34.209 73.692 91.993 1.00 53.22 C ATOM 1086 CG1 VAL A 173 32.867 73.855 91.289 1.00 45.40 C ATOM 1087 CG2 VAL A 173 34.398 72.267 92.484 1.00 50.05 C ATOM 1088 N ASP A 174 34.877 74.095 88.709 1.00 50.59 N ATOM 1089 CA ASP A 174 34.812 73.508 87.384 1.00 51.24 C ATOM 1090 C ASP A 174 36.158 73.404 86.691 1.00 50.98 C ATOM 1091 O ASP A 174 36.365 72.541 85.836 1.00 50.82 O ATOM 1092 CB ASP A 174 33.873 74.315 86.518 1.00 55.02 C ATOM 1093 CG ASP A 174 32.576 73.618 86.326 1.00 62.36 C ATOM 1094 OD1 ASP A 174 32.621 72.374 86.147 1.00 65.03 O ATOM 1095 OD2 ASP A 174 31.522 74.289 86.394 1.00 62.55 O ATOM 1096 N LYS A 175 37.060 74.305 87.057 1.00 50.28 N ATOM 1097 CA LYS A 175 38.371 74.377 86.448 1.00 48.57 C ATOM 1098 C LYS A 175 39.413 74.387 87.560 1.00 45.44 C ATOM 1099 O LYS A 175 40.396 75.109 87.501 1.00 43.43 O ATOM 1100 CB LYS A 175 38.451 75.632 85.578 1.00 45.85 C ATOM 1101 CG LYS A 175 37.387 75.651 84.491 1.00 50.87 C ATOM 1102 CD LYS A 175 37.570 76.814 83.516 1.00 53.85 C ATOM 1103 CE LYS A 175 36.977 78.083 84.079 1.00 53.49 C ATOM 1104 NZ LYS A 175 35.575 77.795 84.494 1.00 59.30 N ATOM 1105 N SER A 176 39.177 73.562 88.574 1.00 46.22 N ATOM 1106 CA SER A 176 39.958 73.587 89.804 1.00 45.81 C ATOM 1107 C SER A 176 41.407 73.207 89.579 1.00 44.43 C ATOM 1108 O SER A 176 42.290 73.659 90.302 1.00 43.75 O ATOM 1109 CB SER A 176 39.348 72.653 90.836 1.00 45.70 C ATOM 1110 OG SER A 176 39.457 71.316 90.400 1.00 49.30 O ATOM 1111 N THR A 177 41.651 72.374 88.577 1.00 44.22 N ATOM 1112 CA THR A 177 43.009 71.922 88.304 1.00 46.49 C ATOM 1113 C THR A 177 43.830 72.960 87.555 1.00 44.26 C ATOM 1114 O THR A 177 44.980 73.196 87.892 1.00 46.12 O ATOM 1115 CB THR A 177 43.049 70.559 87.591 1.00 48.34 C ATOM 1116 OG1 THR A 177 42.265 69.613 88.337 1.00 56.47 O ATOM 1117 CG2 THR A 177 44.483 70.058 87.498 1.00 46.60 C ATOM 1118 N PRO A 178 43.255 73.590 86.533 1.00 43.38 N ATOM 1119 CA PRO A 178 43.991 74.730 85.990 1.00 41.62 C ATOM 1120 C PRO A 178 44.220 75.827 87.021 1.00 40.55 C ATOM 1121 O PRO A 178 45.275 76.435 87.036 1.00 42.88 O ATOM 1122 CB PRO A 178 43.030 75.278 84.948 1.00 40.32 C ATOM 1123 CG PRO A 178 42.272 74.145 84.526 1.00 43.49 C ATOM 1124 CD PRO A 178 42.099 73.247 85.696 1.00 44.49 C HETATM 1125 N MSE A 179 43.215 76.098 87.840 1.00 41.76 N HETATM 1126 CA MSE A 179 43.278 77.199 88.784 1.00 40.41 C HETATM 1127 C MSE A 179 44.202 76.851 89.949 1.00 41.08 C HETATM 1128 O MSE A 179 44.749 77.738 90.594 1.00 44.28 O HETATM 1129 CB MSE A 179 41.881 77.594 89.283 1.00 42.71 C HETATM 1130 CG MSE A 179 40.949 78.050 88.187 1.00 43.77 C HETATM 1131 SE MSE A 179 40.109 79.724 88.602 0.60 43.50 Se HETATM 1132 CE MSE A 179 39.147 79.979 86.904 1.00 50.34 C HETATM 1133 N MSE A 180 44.344 75.554 90.215 1.00 42.09 N HETATM 1134 CA MSE A 180 45.388 75.025 91.087 1.00 41.70 C HETATM 1135 C MSE A 180 46.769 75.546 90.614 1.00 41.64 C HETATM 1136 O MSE A 180 47.481 76.175 91.395 1.00 41.26 O HETATM 1137 CB MSE A 180 45.344 73.486 91.068 1.00 48.63 C HETATM 1138 CG MSE A 180 45.762 72.732 92.328 1.00 56.14 C HETATM 1139 SE MSE A 180 44.330 71.955 93.508 0.60 61.24 Se HETATM 1140 CE MSE A 180 43.064 71.309 92.177 1.00 46.47 C ATOM 1141 N GLU A 181 47.139 75.314 89.348 1.00 41.09 N ATOM 1142 CA GLU A 181 48.435 75.782 88.817 1.00 40.22 C ATOM 1143 C GLU A 181 48.605 77.298 88.893 1.00 37.77 C ATOM 1144 O GLU A 181 49.720 77.791 89.012 1.00 40.41 O ATOM 1145 CB GLU A 181 48.701 75.328 87.363 1.00 40.33 C ATOM 1146 CG GLU A 181 48.707 73.826 87.094 1.00 43.98 C ATOM 1147 CD GLU A 181 49.459 72.989 88.139 1.00 55.69 C ATOM 1148 OE1 GLU A 181 50.653 73.270 88.413 1.00 56.09 O ATOM 1149 OE2 GLU A 181 48.853 72.026 88.681 1.00 57.86 O ATOM 1150 N ALA A 182 47.508 78.038 88.808 1.00 36.84 N ATOM 1151 CA ALA A 182 47.574 79.495 88.894 1.00 36.67 C ATOM 1152 C ALA A 182 47.878 80.011 90.306 1.00 37.03 C ATOM 1153 O ALA A 182 48.567 81.011 90.462 1.00 39.90 O ATOM 1154 CB ALA A 182 46.302 80.126 88.350 1.00 30.49 C ATOM 1155 N PHE A 183 47.373 79.331 91.330 1.00 35.28 N ATOM 1156 CA PHE A 183 47.542 79.813 92.696 1.00 36.64 C ATOM 1157 C PHE A 183 48.897 79.414 93.238 1.00 35.26 C ATOM 1158 O PHE A 183 49.442 80.072 94.116 1.00 35.99 O ATOM 1159 CB PHE A 183 46.421 79.314 93.612 1.00 35.69 C ATOM 1160 CG PHE A 183 45.065 79.867 93.271 1.00 35.94 C ATOM 1161 CD1 PHE A 183 44.893 81.212 93.014 1.00 33.11 C ATOM 1162 CD2 PHE A 183 43.966 79.036 93.196 1.00 37.11 C ATOM 1163 CE1 PHE A 183 43.664 81.710 92.684 1.00 32.70 C ATOM 1164 CE2 PHE A 183 42.730 79.540 92.861 1.00 39.65 C ATOM 1165 CZ PHE A 183 42.584 80.876 92.609 1.00 35.76 C ATOM 1166 N LYS A 184 49.437 78.332 92.696 1.00 33.93 N ATOM 1167 CA LYS A 184 50.778 77.903 93.033 1.00 34.53 C ATOM 1168 C LYS A 184 51.747 78.924 92.478 1.00 35.49 C ATOM 1169 O LYS A 184 52.702 79.312 93.127 1.00 38.73 O ATOM 1170 CB LYS A 184 51.063 76.536 92.431 1.00 35.01 C ATOM 1171 CG LYS A 184 50.153 75.425 92.917 1.00 38.97 C ATOM 1172 CD LYS A 184 50.956 74.193 93.301 1.00 40.46 C ATOM 1173 CE LYS A 184 50.135 72.927 93.225 1.00 43.42 C ATOM 1174 NZ LYS A 184 49.933 72.499 91.804 1.00 50.42 N ATOM 1175 N GLU A 185 51.483 79.372 91.264 1.00 34.27 N ATOM 1176 CA GLU A 185 52.297 80.397 90.663 1.00 36.45 C ATOM 1177 C GLU A 185 52.233 81.669 91.492 1.00 35.26 C ATOM 1178 O GLU A 185 53.256 82.264 91.784 1.00 36.77 O ATOM 1179 CB GLU A 185 51.849 80.649 89.228 1.00 38.45 C ATOM 1180 CG GLU A 185 52.555 81.802 88.528 1.00 38.45 C ATOM 1181 CD GLU A 185 53.971 81.460 88.086 1.00 50.53 C ATOM 1182 OE1 GLU A 185 54.271 80.255 87.836 1.00 52.97 O ATOM 1183 OE2 GLU A 185 54.789 82.411 87.974 1.00 55.13 O ATOM 1184 N ALA A 186 51.034 82.083 91.880 1.00 34.98 N ATOM 1185 CA ALA A 186 50.881 83.248 92.751 1.00 33.15 C ATOM 1186 C ALA A 186 51.588 83.086 94.098 1.00 34.84 C ATOM 1187 O ALA A 186 52.147 84.026 94.616 1.00 34.37 O ATOM 1188 CB ALA A 186 49.418 83.574 92.964 1.00 30.74 C ATOM 1189 N ASP A 187 51.554 81.897 94.672 1.00 35.09 N ATOM 1190 CA ASP A 187 52.184 81.676 95.963 1.00 35.75 C ATOM 1191 C ASP A 187 53.709 81.695 95.774 1.00 38.30 C ATOM 1192 O ASP A 187 54.434 82.300 96.565 1.00 41.61 O ATOM 1193 CB ASP A 187 51.618 80.389 96.611 1.00 39.40 C ATOM 1194 CG ASP A 187 52.360 79.947 97.893 1.00 44.75 C ATOM 1195 OD1 ASP A 187 51.985 80.345 99.018 1.00 46.30 O ATOM 1196 OD2 ASP A 187 53.302 79.140 97.778 1.00 49.13 O ATOM 1197 N ASN A 188 54.200 81.090 94.701 1.00 36.36 N ATOM 1198 CA ASN A 188 55.628 81.174 94.392 1.00 36.61 C ATOM 1199 C ASN A 188 56.144 82.597 94.163 1.00 34.69 C ATOM 1200 O ASN A 188 57.232 82.929 94.597 1.00 39.01 O ATOM 1201 CB ASN A 188 55.996 80.294 93.195 1.00 36.07 C ATOM 1202 CG ASN A 188 56.064 78.832 93.540 1.00 36.66 C ATOM 1203 OD1 ASN A 188 56.094 78.465 94.703 1.00 39.44 O ATOM 1204 ND2 ASN A 188 56.101 77.987 92.529 1.00 35.08 N ATOM 1205 N VAL A 189 55.374 83.431 93.478 1.00 34.12 N ATOM 1206 CA VAL A 189 55.821 84.780 93.143 1.00 33.02 C ATOM 1207 C VAL A 189 55.896 85.620 94.396 1.00 34.44 C ATOM 1208 O VAL A 189 56.835 86.374 94.612 1.00 35.91 O ATOM 1209 CB VAL A 189 54.878 85.434 92.109 1.00 32.89 C ATOM 1210 CG1 VAL A 189 54.899 86.942 92.195 1.00 32.38 C ATOM 1211 CG2 VAL A 189 55.258 84.995 90.729 1.00 36.38 C ATOM 1212 N LEU A 190 54.896 85.442 95.241 1.00 38.40 N ATOM 1213 CA LEU A 190 54.718 86.254 96.433 1.00 36.06 C ATOM 1214 C LEU A 190 55.727 85.893 97.518 1.00 37.80 C ATOM 1215 O LEU A 190 56.000 86.687 98.400 1.00 42.62 O ATOM 1216 CB LEU A 190 53.291 86.105 96.941 1.00 34.04 C ATOM 1217 CG LEU A 190 52.715 87.244 97.763 1.00 37.03 C ATOM 1218 CD1 LEU A 190 53.010 88.519 97.052 1.00 36.18 C ATOM 1219 CD2 LEU A 190 51.200 87.063 97.896 1.00 41.79 C ATOM 1220 N ARG A 191 56.310 84.708 97.439 1.00 39.09 N ATOM 1221 CA ARG A 191 57.274 84.330 98.454 1.00 42.69 C ATOM 1222 C ARG A 191 58.677 84.580 97.964 1.00 40.32 C ATOM 1223 O ARG A 191 59.524 84.956 98.755 1.00 44.11 O ATOM 1224 CB ARG A 191 57.085 82.883 98.934 1.00 43.59 C ATOM 1225 CG ARG A 191 55.701 82.608 99.562 1.00 43.54 C ATOM 1226 CD ARG A 191 55.487 81.114 99.867 1.00 51.02 C ATOM 1227 NE ARG A 191 54.261 80.842 100.637 1.00 53.15 N ATOM 1228 CZ ARG A 191 54.194 80.843 101.974 1.00 55.59 C ATOM 1229 NH1 ARG A 191 55.281 81.099 102.707 1.00 52.77 N ATOM 1230 NH2 ARG A 191 53.035 80.595 102.579 1.00 48.64 N ATOM 1231 N GLN A 192 58.928 84.398 96.671 1.00 37.94 N ATOM 1232 CA GLN A 192 60.246 84.732 96.125 1.00 39.35 C ATOM 1233 C GLN A 192 60.427 86.236 96.106 1.00 41.11 C ATOM 1234 O GLN A 192 61.542 86.740 96.212 1.00 44.68 O ATOM 1235 CB GLN A 192 60.447 84.234 94.688 1.00 44.04 C ATOM 1236 CG GLN A 192 60.404 82.736 94.448 1.00 46.50 C ATOM 1237 CD GLN A 192 61.482 81.990 95.185 1.00 47.29 C ATOM 1238 OE1 GLN A 192 62.405 82.583 95.738 1.00 50.19 O ATOM 1239 NE2 GLN A 192 61.366 80.673 95.209 1.00 47.55 N ATOM 1240 N GLY A 193 59.326 86.955 95.944 1.00 38.20 N ATOM 1241 CA GLY A 193 59.398 88.393 95.836 1.00 33.78 C ATOM 1242 C GLY A 193 59.890 88.788 94.466 1.00 36.17 C ATOM 1243 O GLY A 193 60.587 89.780 94.315 1.00 38.68 O ATOM 1244 N VAL A 194 59.512 87.995 93.470 1.00 35.28 N ATOM 1245 CA VAL A 194 59.833 88.240 92.069 1.00 33.42 C ATOM 1246 C VAL A 194 59.468 89.657 91.611 1.00 36.23 C ATOM 1247 O VAL A 194 58.338 90.100 91.789 1.00 36.68 O ATOM 1248 CB VAL A 194 59.096 87.218 91.187 1.00 34.88 C ATOM 1249 CG1 VAL A 194 59.376 87.465 89.720 1.00 32.18 C ATOM 1250 CG2 VAL A 194 59.471 85.801 91.586 1.00 33.10 C ATOM 1251 N GLN A 195 60.438 90.366 91.040 1.00 33.94 N ATOM 1252 CA GLN A 195 60.245 91.727 90.560 1.00 31.82 C ATOM 1253 C GLN A 195 59.757 92.660 91.642 1.00 34.29 C ATOM 1254 O GLN A 195 59.179 93.703 91.354 1.00 38.99 O ATOM 1255 CB GLN A 195 59.271 91.756 89.400 1.00 30.53 C ATOM 1256 CG GLN A 195 59.903 91.623 88.050 1.00 36.48 C ATOM 1257 CD GLN A 195 58.878 91.820 86.954 1.00 38.96 C ATOM 1258 OE1 GLN A 195 57.712 92.096 87.246 1.00 35.95 O ATOM 1259 NE2 GLN A 195 59.298 91.671 85.686 1.00 34.00 N ATOM 1260 N GLY A 196 59.965 92.253 92.888 1.00 34.11 N ATOM 1261 CA GLY A 196 59.742 93.101 94.036 1.00 31.75 C ATOM 1262 C GLY A 196 58.348 93.013 94.589 1.00 34.62 C ATOM 1263 O GLY A 196 57.957 93.833 95.406 1.00 39.69 O ATOM 1264 N ILE A 197 57.593 92.015 94.158 1.00 34.99 N ATOM 1265 CA ILE A 197 56.198 91.892 94.573 1.00 35.48 C ATOM 1266 C ILE A 197 56.040 91.432 96.020 1.00 34.10 C ATOM 1267 O ILE A 197 56.600 90.420 96.415 1.00 35.74 O ATOM 1268 CB ILE A 197 55.432 90.939 93.648 1.00 32.35 C ATOM 1269 CG1 ILE A 197 55.479 91.467 92.216 1.00 32.57 C ATOM 1270 CG2 ILE A 197 54.003 90.763 94.147 1.00 30.40 C ATOM 1271 CD1 ILE A 197 54.920 90.534 91.198 1.00 29.44 C ATOM 1272 N SER A 198 55.271 92.171 96.808 1.00 36.59 N ATOM 1273 CA SER A 198 55.169 91.882 98.237 1.00 35.06 C ATOM 1274 C SER A 198 53.737 91.734 98.660 1.00 34.58 C ATOM 1275 O SER A 198 53.454 91.518 99.816 1.00 40.14 O ATOM 1276 CB SER A 198 55.746 93.034 99.030 1.00 38.00 C ATOM 1277 OG SER A 198 54.905 94.158 98.898 1.00 41.06 O ATOM 1278 N ASP A 199 52.833 91.876 97.708 1.00 37.05 N ATOM 1279 CA ASP A 199 51.411 91.912 97.971 1.00 36.37 C ATOM 1280 C ASP A 199 50.699 91.656 96.635 1.00 36.87 C ATOM 1281 O ASP A 199 51.040 92.269 95.639 1.00 38.04 O ATOM 1282 CB ASP A 199 51.054 93.283 98.553 1.00 39.54 C ATOM 1283 CG ASP A 199 49.671 93.320 99.147 1.00 49.33 C ATOM 1284 OD1 ASP A 199 48.856 92.470 98.757 1.00 53.42 O ATOM 1285 OD2 ASP A 199 49.395 94.187 99.999 1.00 54.47 O ATOM 1286 N LEU A 200 49.722 90.750 96.614 1.00 37.18 N ATOM 1287 CA LEU A 200 49.108 90.301 95.356 1.00 35.04 C ATOM 1288 C LEU A 200 47.620 89.977 95.485 1.00 34.66 C ATOM 1289 O LEU A 200 47.217 89.271 96.399 1.00 38.34 O ATOM 1290 CB LEU A 200 49.845 89.063 94.855 1.00 30.73 C ATOM 1291 CG LEU A 200 49.617 88.626 93.417 1.00 31.49 C ATOM 1292 CD1 LEU A 200 50.874 87.967 92.889 1.00 29.81 C ATOM 1293 CD2 LEU A 200 48.461 87.662 93.319 1.00 31.77 C ATOM 1294 N ILE A 201 46.806 90.476 94.564 1.00 30.07 N ATOM 1295 CA ILE A 201 45.399 90.086 94.498 1.00 30.17 C ATOM 1296 C ILE A 201 45.045 89.547 93.119 1.00 30.16 C ATOM 1297 O ILE A 201 45.344 90.168 92.113 1.00 32.51 O ATOM 1298 CB ILE A 201 44.464 91.258 94.859 1.00 31.23 C ATOM 1299 CG1 ILE A 201 44.373 91.407 96.370 1.00 36.69 C ATOM 1300 CG2 ILE A 201 43.060 91.040 94.329 1.00 34.36 C ATOM 1301 CD1 ILE A 201 43.631 92.640 96.794 1.00 41.20 C ATOM 1302 N ALA A 202 44.413 88.382 93.082 1.00 30.25 N ATOM 1303 CA ALA A 202 44.000 87.760 91.826 1.00 31.83 C ATOM 1304 C ALA A 202 42.575 88.118 91.417 1.00 32.08 C ATOM 1305 O ALA A 202 41.735 88.389 92.253 1.00 32.58 O ATOM 1306 CB ALA A 202 44.166 86.249 91.902 1.00 29.61 C ATOM 1307 N VAL A 203 42.317 88.141 90.115 1.00 33.04 N ATOM 1308 CA VAL A 203 40.966 88.395 89.605 1.00 37.09 C ATOM 1309 C VAL A 203 40.581 87.381 88.519 1.00 38.10 C ATOM 1310 O VAL A 203 41.417 86.982 87.710 1.00 36.81 O ATOM 1311 CB VAL A 203 40.827 89.826 89.058 1.00 36.29 C ATOM 1312 CG1 VAL A 203 39.407 90.105 88.679 1.00 40.63 C ATOM 1313 CG2 VAL A 203 41.263 90.821 90.088 1.00 33.72 C ATOM 1314 N SER A 204 39.323 86.944 88.527 1.00 39.27 N ATOM 1315 CA SER A 204 38.762 86.132 87.441 1.00 40.46 C ATOM 1316 C SER A 204 37.461 86.795 87.048 1.00 42.41 C ATOM 1317 O SER A 204 36.805 87.395 87.884 1.00 44.96 O ATOM 1318 CB SER A 204 38.500 84.690 87.888 1.00 40.60 C ATOM 1319 OG SER A 204 38.299 83.821 86.790 1.00 41.47 O ATOM 1320 N GLY A 205 37.100 86.716 85.775 1.00 45.64 N ATOM 1321 CA GLY A 205 35.831 87.251 85.302 1.00 48.02 C ATOM 1322 C GLY A 205 35.675 88.761 85.399 1.00 55.07 C ATOM 1323 O GLY A 205 36.562 89.471 85.865 1.00 54.00 O ATOM 1324 N GLU A 206 34.534 89.266 84.956 1.00 57.33 N ATOM 1325 CA GLU A 206 34.303 90.706 85.005 1.00 57.65 C ATOM 1326 C GLU A 206 33.938 91.137 86.417 1.00 56.24 C ATOM 1327 O GLU A 206 32.794 90.966 86.847 1.00 59.46 O ATOM 1328 CB GLU A 206 33.187 91.111 84.025 1.00 63.95 C ATOM 1329 CG GLU A 206 33.547 90.955 82.529 1.00 69.97 C ATOM 1330 CD GLU A 206 34.383 92.115 82.004 1.00 72.06 C ATOM 1331 OE1 GLU A 206 34.111 93.280 82.406 1.00 72.47 O ATOM 1332 OE2 GLU A 206 35.311 91.869 81.193 1.00 63.38 O ATOM 1333 N VAL A 207 34.897 91.692 87.147 1.00 53.15 N ATOM 1334 CA VAL A 207 34.621 92.131 88.515 1.00 55.78 C ATOM 1335 C VAL A 207 34.288 93.622 88.561 1.00 56.84 C ATOM 1336 O VAL A 207 34.937 94.420 87.881 1.00 53.75 O ATOM 1337 CB VAL A 207 35.816 91.823 89.445 1.00 52.61 C ATOM 1338 CG1 VAL A 207 35.655 92.499 90.779 1.00 48.16 C ATOM 1339 CG2 VAL A 207 35.940 90.341 89.627 1.00 48.94 C ATOM 1340 N ASN A 208 33.269 93.994 89.341 1.00 59.70 N ATOM 1341 CA ASN A 208 33.010 95.413 89.620 1.00 62.38 C ATOM 1342 C ASN A 208 34.031 95.971 90.631 1.00 59.87 C ATOM 1343 O ASN A 208 33.704 96.278 91.791 1.00 56.14 O ATOM 1344 CB ASN A 208 31.562 95.651 90.091 1.00 66.48 C ATOM 1345 CG ASN A 208 31.265 97.131 90.375 1.00 70.38 C ATOM 1346 OD1 ASN A 208 31.664 98.015 89.610 1.00 68.95 O ATOM 1347 ND2 ASN A 208 30.584 97.402 91.497 1.00 69.36 N ATOM 1348 N LEU A 209 35.278 96.079 90.183 1.00 56.28 N ATOM 1349 CA LEU A 209 36.318 96.659 91.010 1.00 56.23 C ATOM 1350 C LEU A 209 37.199 97.635 90.264 1.00 57.48 C ATOM 1351 O LEU A 209 37.456 97.507 89.070 1.00 52.97 O ATOM 1352 CB LEU A 209 37.168 95.585 91.666 1.00 54.38 C ATOM 1353 CG LEU A 209 36.657 95.144 93.031 1.00 56.20 C ATOM 1354 CD1 LEU A 209 37.676 94.249 93.708 1.00 54.67 C ATOM 1355 CD2 LEU A 209 36.321 96.352 93.896 1.00 55.21 C ATOM 1356 N ASP A 210 37.686 98.597 91.025 1.00 59.25 N ATOM 1357 CA ASP A 210 38.338 99.777 90.515 1.00 58.02 C ATOM 1358 C ASP A 210 39.684 99.886 91.251 1.00 61.00 C ATOM 1359 O ASP A 210 39.758 99.612 92.458 1.00 63.65 O ATOM 1360 CB ASP A 210 37.417 100.942 90.873 1.00 63.48 C ATOM 1361 CG ASP A 210 37.885 102.262 90.314 1.00 71.71 C ATOM 1362 OD1 ASP A 210 38.980 102.300 89.682 1.00 71.50 O ATOM 1363 OD2 ASP A 210 37.145 103.266 90.530 1.00 71.89 O ATOM 1364 N PHE A 211 40.754 100.258 90.556 1.00 59.92 N ATOM 1365 CA PHE A 211 42.053 100.263 91.223 1.00 61.28 C ATOM 1366 C PHE A 211 42.023 101.067 92.516 1.00 62.51 C ATOM 1367 O PHE A 211 42.552 100.642 93.545 1.00 62.01 O ATOM 1368 CB PHE A 211 43.181 100.807 90.349 1.00 61.75 C ATOM 1369 CG PHE A 211 44.491 100.888 91.088 1.00 66.03 C ATOM 1370 CD1 PHE A 211 45.220 99.731 91.348 1.00 65.58 C ATOM 1371 CD2 PHE A 211 44.965 102.103 91.585 1.00 68.91 C ATOM 1372 CE1 PHE A 211 46.423 99.780 92.067 1.00 67.04 C ATOM 1373 CE2 PHE A 211 46.173 102.168 92.304 1.00 67.21 C ATOM 1374 CZ PHE A 211 46.902 101.002 92.544 1.00 65.75 C ATOM 1375 N ALA A 212 41.389 102.231 92.442 1.00 63.17 N ATOM 1376 CA ALA A 212 41.324 103.141 93.567 1.00 63.29 C ATOM 1377 C ALA A 212 40.867 102.388 94.794 1.00 63.21 C ATOM 1378 O ALA A 212 41.453 102.516 95.869 1.00 63.37 O ATOM 1379 CB ALA A 212 40.365 104.273 93.258 1.00 66.15 C ATOM 1380 N ASP A 213 39.837 101.567 94.622 1.00 62.43 N ATOM 1381 CA ASP A 213 39.192 100.961 95.783 1.00 66.77 C ATOM 1382 C ASP A 213 39.803 99.618 96.192 1.00 66.20 C ATOM 1383 O ASP A 213 39.154 98.793 96.844 1.00 66.16 O ATOM 1384 CB ASP A 213 37.655 100.896 95.624 1.00 66.88 C ATOM 1385 CG ASP A 213 37.214 100.124 94.397 1.00 66.33 C ATOM 1386 OD1 ASP A 213 37.801 99.049 94.146 1.00 66.13 O ATOM 1387 OD2 ASP A 213 36.272 100.588 93.694 1.00 67.67 O ATOM 1388 N VAL A 214 41.064 99.417 95.831 1.00 62.88 N ATOM 1389 CA VAL A 214 41.734 98.160 96.124 1.00 60.81 C ATOM 1390 C VAL A 214 43.138 98.506 96.578 1.00 64.34 C ATOM 1391 O VAL A 214 43.770 97.742 97.332 1.00 65.32 O ATOM 1392 CB VAL A 214 41.752 97.226 94.874 1.00 60.91 C ATOM 1393 CG1 VAL A 214 42.996 97.448 94.024 1.00 59.67 C ATOM 1394 CG2 VAL A 214 41.610 95.764 95.279 1.00 58.97 C ATOM 1395 N LYS A 215 43.588 99.691 96.149 1.00 63.97 N ATOM 1396 CA LYS A 215 44.923 100.194 96.447 1.00 63.46 C ATOM 1397 C LYS A 215 45.113 100.441 97.941 1.00 65.33 C ATOM 1398 O LYS A 215 46.252 100.443 98.441 1.00 66.19 O ATOM 1399 CB LYS A 215 45.198 101.483 95.676 1.00 63.24 C ATOM 1400 CG LYS A 215 44.697 102.750 96.370 1.00 62.75 C ATOM 1401 CD LYS A 215 45.380 103.980 95.776 1.00 66.65 C ATOM 1402 CE LYS A 215 46.912 103.834 95.807 1.00 64.88 C ATOM 1403 NZ LYS A 215 47.604 104.729 94.806 1.00 62.20 N ATOM 1404 N THR A 216 43.996 100.646 98.641 1.00 64.52 N ATOM 1405 CA THR A 216 43.991 100.839 100.095 1.00 65.78 C ATOM 1406 C THR A 216 44.249 99.546 100.878 1.00 65.29 C ATOM 1407 O THR A 216 44.875 99.579 101.946 1.00 64.82 O ATOM 1408 CB THR A 216 42.642 101.429 100.565 1.00 69.23 C ATOM 1409 OG1 THR A 216 42.358 102.623 99.818 1.00 65.53 O ATOM 1410 CG2 THR A 216 42.670 101.726 102.076 1.00 66.28 C ATOM 1411 N ILE A 217 43.744 98.420 100.368 1.00 64.21 N ATOM 1412 CA ILE A 217 43.962 97.133 101.018 1.00 60.63 C ATOM 1413 C ILE A 217 45.408 96.771 100.862 1.00 61.25 C ATOM 1414 O ILE A 217 46.030 96.220 101.770 1.00 62.55 O ATOM 1415 CB ILE A 217 43.265 96.018 100.285 1.00 59.22 C ATOM 1416 CG1 ILE A 217 41.782 96.292 100.169 1.00 63.86 C ATOM 1417 CG2 ILE A 217 43.460 94.722 101.007 1.00 57.60 C ATOM 1418 CD1 ILE A 217 41.086 95.229 99.370 1.00 62.51 C HETATM 1419 N MSE A 218 45.926 97.067 99.678 1.00 58.72 N HETATM 1420 CA MSE A 218 47.243 96.621 99.284 1.00 57.58 C HETATM 1421 C MSE A 218 48.347 97.586 99.661 1.00 56.83 C HETATM 1422 O MSE A 218 48.114 98.760 99.932 1.00 56.34 O HETATM 1423 CB MSE A 218 47.265 96.372 97.786 1.00 54.64 C HETATM 1424 CG MSE A 218 46.459 95.163 97.391 1.00 52.54 C HETATM 1425 SE MSE A 218 46.940 94.597 95.624 0.60 38.06 Se HETATM 1426 CE MSE A 218 46.189 96.058 94.589 1.00 53.10 C ATOM 1427 N SER A 219 49.558 97.054 99.648 1.00 53.72 N ATOM 1428 CA SER A 219 50.746 97.777 100.054 1.00 53.84 C ATOM 1429 C SER A 219 50.933 99.139 99.397 1.00 57.75 C ATOM 1430 O SER A 219 50.357 99.445 98.347 1.00 56.81 O ATOM 1431 CB SER A 219 51.990 96.911 99.805 1.00 52.74 C ATOM 1432 OG SER A 219 52.028 95.788 100.682 1.00 48.61 O ATOM 1433 N ASN A 220 51.741 99.950 100.064 1.00 60.71 N ATOM 1434 CA ASN A 220 52.213 101.222 99.552 1.00 63.95 C ATOM 1435 C ASN A 220 53.084 100.968 98.318 1.00 58.16 C ATOM 1436 O ASN A 220 53.106 101.771 97.375 1.00 57.06 O ATOM 1437 CB ASN A 220 53.035 101.917 100.665 1.00 71.29 C ATOM 1438 CG ASN A 220 53.420 103.369 100.325 1.00 76.30 C ATOM 1439 OD1 ASN A 220 52.547 104.256 100.230 1.00 75.52 O ATOM 1440 ND2 ASN A 220 54.740 103.621 100.176 1.00 71.40 N ATOM 1441 N GLN A 221 53.802 99.846 98.325 1.00 55.81 N ATOM 1442 CA GLN A 221 54.675 99.498 97.204 1.00 53.81 C ATOM 1443 C GLN A 221 54.950 98.001 97.075 1.00 46.19 C ATOM 1444 O GLN A 221 55.049 97.279 98.063 1.00 41.82 O ATOM 1445 CB GLN A 221 55.988 100.296 97.257 1.00 56.12 C ATOM 1446 CG GLN A 221 56.618 100.415 98.644 1.00 60.61 C ATOM 1447 CD GLN A 221 57.449 101.693 98.786 1.00 70.94 C ATOM 1448 OE1 GLN A 221 56.963 102.800 98.503 1.00 73.62 O ATOM 1449 NE2 GLN A 221 58.705 101.548 99.216 1.00 68.62 N ATOM 1450 N GLY A 222 55.070 97.546 95.837 1.00 41.28 N ATOM 1451 CA GLY A 222 55.239 96.138 95.568 1.00 37.52 C ATOM 1452 C GLY A 222 53.921 95.403 95.432 1.00 36.08 C ATOM 1453 O GLY A 222 53.884 94.194 95.554 1.00 38.15 O ATOM 1454 N SER A 223 52.831 96.108 95.190 1.00 28.40 N ATOM 1455 CA SER A 223 51.579 95.402 95.012 1.00 31.14 C ATOM 1456 C SER A 223 51.387 94.943 93.560 1.00 33.79 C ATOM 1457 O SER A 223 51.871 95.573 92.635 1.00 33.73 O ATOM 1458 CB SER A 223 50.391 96.225 95.526 1.00 38.95 C ATOM 1459 OG SER A 223 50.140 97.368 94.737 1.00 40.12 O ATOM 1460 N ALA A 224 50.678 93.839 93.371 1.00 31.01 N ATOM 1461 CA ALA A 224 50.480 93.277 92.053 1.00 29.10 C ATOM 1462 C ALA A 224 49.044 92.845 91.828 1.00 33.18 C ATOM 1463 O ALA A 224 48.321 92.617 92.769 1.00 35.99 O ATOM 1464 CB ALA A 224 51.382 92.113 91.874 1.00 30.94 C ATOM 1465 N LEU A 225 48.645 92.729 90.567 1.00 32.79 N ATOM 1466 CA LEU A 225 47.332 92.217 90.187 1.00 28.95 C ATOM 1467 C LEU A 225 47.513 91.063 89.222 1.00 30.72 C ATOM 1468 O LEU A 225 48.264 91.176 88.266 1.00 30.67 O ATOM 1469 CB LEU A 225 46.508 93.308 89.517 1.00 29.86 C ATOM 1470 CG LEU A 225 46.004 94.385 90.473 1.00 37.72 C ATOM 1471 CD1 LEU A 225 45.315 95.502 89.736 1.00 36.67 C ATOM 1472 CD2 LEU A 225 45.062 93.772 91.482 1.00 36.15 C HETATM 1473 N MSE A 226 46.842 89.949 89.493 1.00 28.23 N HETATM 1474 CA MSE A 226 46.935 88.758 88.661 1.00 26.51 C HETATM 1475 C MSE A 226 45.594 88.413 88.037 1.00 28.69 C HETATM 1476 O MSE A 226 44.611 88.209 88.745 1.00 32.02 O HETATM 1477 CB MSE A 226 47.456 87.571 89.467 1.00 27.51 C HETATM 1478 CG MSE A 226 47.100 86.227 88.880 1.00 27.58 C HETATM 1479 SE MSE A 226 48.157 84.748 89.504 0.60 18.68 Se HETATM 1480 CE MSE A 226 46.778 83.738 90.324 1.00 35.22 C ATOM 1481 N GLY A 227 45.549 88.370 86.708 1.00 26.43 N ATOM 1482 CA GLY A 227 44.386 87.867 86.010 1.00 26.67 C ATOM 1483 C GLY A 227 44.568 86.417 85.622 1.00 28.66 C ATOM 1484 O GLY A 227 45.675 85.963 85.426 1.00 31.74 O ATOM 1485 N ILE A 228 43.476 85.678 85.523 1.00 29.49 N ATOM 1486 CA ILE A 228 43.548 84.290 85.092 1.00 28.64 C ATOM 1487 C ILE A 228 42.660 84.030 83.876 1.00 28.70 C ATOM 1488 O ILE A 228 41.587 84.600 83.736 1.00 29.91 O ATOM 1489 CB ILE A 228 43.163 83.311 86.213 1.00 28.30 C ATOM 1490 CG1 ILE A 228 44.037 83.552 87.443 1.00 29.01 C ATOM 1491 CG2 ILE A 228 43.303 81.870 85.749 1.00 28.87 C ATOM 1492 CD1 ILE A 228 43.443 83.011 88.755 1.00 28.87 C ATOM 1493 N GLY A 229 43.145 83.168 82.994 1.00 27.95 N ATOM 1494 CA GLY A 229 42.348 82.626 81.924 1.00 27.55 C ATOM 1495 C GLY A 229 42.590 81.149 81.729 1.00 31.26 C ATOM 1496 O GLY A 229 43.720 80.688 81.727 1.00 34.75 O ATOM 1497 N VAL A 230 41.511 80.401 81.579 1.00 33.17 N ATOM 1498 CA VAL A 230 41.580 78.980 81.303 1.00 35.69 C ATOM 1499 C VAL A 230 40.785 78.743 80.015 1.00 36.25 C ATOM 1500 O VAL A 230 39.750 79.370 79.797 1.00 35.44 O ATOM 1501 CB VAL A 230 40.915 78.221 82.441 1.00 32.41 C ATOM 1502 CG1 VAL A 230 41.054 76.759 82.253 1.00 37.54 C ATOM 1503 CG2 VAL A 230 41.509 78.639 83.756 1.00 30.56 C ATOM 1504 N SER A 231 41.273 77.873 79.144 1.00 37.45 N ATOM 1505 CA SER A 231 40.547 77.622 77.911 1.00 38.08 C ATOM 1506 C SER A 231 40.867 76.275 77.302 1.00 39.38 C ATOM 1507 O SER A 231 41.853 75.653 77.660 1.00 39.15 O ATOM 1508 CB SER A 231 40.830 78.726 76.904 1.00 35.08 C ATOM 1509 OG SER A 231 39.774 78.834 75.986 1.00 40.08 O ATOM 1510 N SER A 232 40.028 75.817 76.383 1.00 41.84 N ATOM 1511 CA SER A 232 40.334 74.581 75.671 1.00 45.38 C ATOM 1512 C SER A 232 39.779 74.621 74.257 1.00 44.50 C ATOM 1513 O SER A 232 38.909 75.434 73.949 1.00 44.44 O ATOM 1514 CB SER A 232 39.828 73.350 76.434 1.00 45.82 C ATOM 1515 OG SER A 232 38.471 73.499 76.801 1.00 49.65 O ATOM 1516 N GLY A 233 40.305 73.758 73.398 1.00 42.53 N ATOM 1517 CA GLY A 233 39.826 73.662 72.038 1.00 44.71 C ATOM 1518 C GLY A 233 40.486 74.630 71.086 1.00 49.07 C ATOM 1519 O GLY A 233 41.637 75.019 71.270 1.00 45.73 O ATOM 1520 N GLU A 234 39.747 75.017 70.055 1.00 51.66 N ATOM 1521 CA GLU A 234 40.310 75.812 68.974 1.00 53.90 C ATOM 1522 C GLU A 234 40.648 77.205 69.495 1.00 50.40 C ATOM 1523 O GLU A 234 39.853 77.798 70.230 1.00 49.96 O ATOM 1524 CB GLU A 234 39.332 75.875 67.786 1.00 58.38 C ATOM 1525 CG GLU A 234 39.828 75.154 66.508 1.00 67.09 C ATOM 1526 CD GLU A 234 38.678 74.564 65.626 1.00 69.85 C ATOM 1527 OE1 GLU A 234 37.629 75.238 65.442 1.00 66.38 O ATOM 1528 OE2 GLU A 234 38.830 73.419 65.116 1.00 67.53 O ATOM 1529 N ASN A 235 41.833 77.699 69.128 1.00 47.65 N ATOM 1530 CA ASN A 235 42.248 79.043 69.469 1.00 45.39 C ATOM 1531 C ASN A 235 42.380 79.183 70.980 1.00 42.62 C ATOM 1532 O ASN A 235 42.246 80.273 71.516 1.00 41.80 O ATOM 1533 CB ASN A 235 41.225 80.048 68.929 1.00 47.31 C ATOM 1534 CG ASN A 235 41.823 81.410 68.644 1.00 50.65 C ATOM 1535 OD1 ASN A 235 42.951 81.526 68.171 1.00 51.72 O ATOM 1536 ND2 ASN A 235 41.056 82.455 68.923 1.00 46.12 N ATOM 1537 N ARG A 236 42.639 78.079 71.674 1.00 40.00 N ATOM 1538 CA ARG A 236 42.647 78.106 73.139 1.00 37.76 C ATOM 1539 C ARG A 236 43.703 79.023 73.766 1.00 38.57 C ATOM 1540 O ARG A 236 43.427 79.691 74.749 1.00 38.58 O ATOM 1541 CB ARG A 236 42.778 76.701 73.714 1.00 36.41 C ATOM 1542 CG ARG A 236 43.999 75.974 73.252 1.00 34.12 C ATOM 1543 CD ARG A 236 44.246 74.752 74.060 1.00 34.96 C ATOM 1544 NE ARG A 236 45.574 74.265 73.771 1.00 35.84 N ATOM 1545 CZ ARG A 236 46.054 73.110 74.206 1.00 39.14 C ATOM 1546 NH1 ARG A 236 45.293 72.329 74.955 1.00 42.08 N ATOM 1547 NH2 ARG A 236 47.292 72.738 73.896 1.00 39.21 N ATOM 1548 N ALA A 237 44.904 79.063 73.198 1.00 38.66 N ATOM 1549 CA ALA A 237 45.972 79.879 73.760 1.00 35.01 C ATOM 1550 C ALA A 237 45.598 81.346 73.796 1.00 34.90 C ATOM 1551 O ALA A 237 45.848 82.041 74.768 1.00 37.91 O ATOM 1552 CB ALA A 237 47.248 79.679 72.987 1.00 34.56 C ATOM 1553 N VAL A 238 44.973 81.799 72.727 1.00 34.80 N ATOM 1554 CA VAL A 238 44.667 83.197 72.543 1.00 32.26 C ATOM 1555 C VAL A 238 43.474 83.594 73.368 1.00 34.85 C ATOM 1556 O VAL A 238 43.422 84.684 73.895 1.00 33.91 O ATOM 1557 CB VAL A 238 44.383 83.467 71.065 1.00 36.51 C ATOM 1558 CG1 VAL A 238 43.913 84.895 70.836 1.00 34.45 C ATOM 1559 CG2 VAL A 238 45.627 83.145 70.252 1.00 34.18 C ATOM 1560 N GLU A 239 42.502 82.708 73.484 1.00 36.74 N ATOM 1561 CA GLU A 239 41.316 83.059 74.242 1.00 39.37 C ATOM 1562 C GLU A 239 41.641 83.107 75.743 1.00 37.18 C ATOM 1563 O GLU A 239 41.093 83.917 76.474 1.00 39.10 O ATOM 1564 CB GLU A 239 40.131 82.121 73.925 1.00 44.68 C ATOM 1565 CG GLU A 239 39.923 81.866 72.426 1.00 50.82 C ATOM 1566 CD GLU A 239 38.460 81.928 71.958 1.00 68.52 C ATOM 1567 OE1 GLU A 239 37.648 82.581 72.652 1.00 71.66 O ATOM 1568 OE2 GLU A 239 38.126 81.332 70.885 1.00 63.05 O ATOM 1569 N ALA A 240 42.561 82.260 76.188 1.00 36.11 N ATOM 1570 CA ALA A 240 42.963 82.256 77.588 1.00 33.60 C ATOM 1571 C ALA A 240 43.716 83.527 77.927 1.00 33.19 C ATOM 1572 O ALA A 240 43.500 84.133 78.976 1.00 32.97 O ATOM 1573 CB ALA A 240 43.819 81.044 77.890 1.00 33.18 C ATOM 1574 N ALA A 241 44.608 83.914 77.023 1.00 31.72 N ATOM 1575 CA ALA A 241 45.420 85.097 77.200 1.00 31.41 C ATOM 1576 C ALA A 241 44.509 86.296 77.202 1.00 35.04 C ATOM 1577 O ALA A 241 44.720 87.243 77.954 1.00 38.41 O ATOM 1578 CB ALA A 241 46.433 85.205 76.094 1.00 31.10 C ATOM 1579 N LYS A 242 43.483 86.248 76.362 1.00 35.10 N ATOM 1580 CA LYS A 242 42.500 87.322 76.309 1.00 33.54 C ATOM 1581 C LYS A 242 41.663 87.418 77.562 1.00 33.49 C ATOM 1582 O LYS A 242 41.421 88.501 78.085 1.00 35.88 O ATOM 1583 CB LYS A 242 41.587 87.210 75.071 1.00 34.76 C ATOM 1584 CG LYS A 242 42.207 87.598 73.714 1.00 37.02 C ATOM 1585 CD LYS A 242 41.370 88.708 73.055 1.00 44.78 C ATOM 1586 CE LYS A 242 40.826 88.349 71.681 1.00 39.75 C ATOM 1587 NZ LYS A 242 41.901 87.908 70.786 1.00 43.85 N ATOM 1588 N LYS A 243 41.209 86.273 78.057 1.00 33.87 N ATOM 1589 CA LYS A 243 40.396 86.246 79.265 1.00 34.75 C ATOM 1590 C LYS A 243 41.176 86.786 80.454 1.00 34.22 C ATOM 1591 O LYS A 243 40.622 87.450 81.327 1.00 34.70 O ATOM 1592 CB LYS A 243 39.918 84.825 79.556 1.00 33.15 C ATOM 1593 CG LYS A 243 38.498 84.547 79.099 1.00 38.05 C ATOM 1594 CD LYS A 243 38.093 83.115 79.397 1.00 41.80 C ATOM 1595 CE LYS A 243 38.587 82.168 78.318 1.00 42.78 C ATOM 1596 NZ LYS A 243 37.638 81.042 78.102 1.00 47.72 N ATOM 1597 N ALA A 244 42.470 86.495 80.474 1.00 31.41 N ATOM 1598 CA ALA A 244 43.336 86.890 81.555 1.00 29.17 C ATOM 1599 C ALA A 244 43.497 88.391 81.750 1.00 33.23 C ATOM 1600 O ALA A 244 43.705 88.836 82.881 1.00 34.53 O ATOM 1601 CB ALA A 244 44.685 86.224 81.408 1.00 30.92 C ATOM 1602 N ILE A 245 43.425 89.169 80.670 1.00 32.82 N ATOM 1603 CA ILE A 245 43.631 90.604 80.769 1.00 31.03 C ATOM 1604 C ILE A 245 42.337 91.351 80.499 1.00 35.31 C ATOM 1605 O ILE A 245 42.361 92.544 80.237 1.00 36.42 O ATOM 1606 CB ILE A 245 44.736 91.074 79.817 1.00 33.00 C ATOM 1607 CG1 ILE A 245 44.272 90.982 78.356 1.00 34.99 C ATOM 1608 CG2 ILE A 245 46.001 90.254 80.039 1.00 31.65 C ATOM 1609 CD1 ILE A 245 45.378 91.053 77.349 1.00 30.48 C ATOM 1610 N SER A 246 41.210 90.653 80.620 1.00 34.96 N ATOM 1611 CA SER A 246 39.908 91.201 80.259 1.00 37.78 C ATOM 1612 C SER A 246 39.171 91.880 81.398 1.00 42.00 C ATOM 1613 O SER A 246 38.324 92.736 81.159 1.00 47.41 O ATOM 1614 CB SER A 246 39.013 90.101 79.717 1.00 40.08 C ATOM 1615 OG SER A 246 38.665 89.217 80.761 1.00 43.78 O ATOM 1616 N SER A 247 39.459 91.510 82.636 1.00 39.66 N ATOM 1617 CA SER A 247 38.734 92.132 83.725 1.00 46.03 C ATOM 1618 C SER A 247 39.210 93.566 83.850 1.00 45.59 C ATOM 1619 O SER A 247 40.370 93.840 83.600 1.00 48.10 O ATOM 1620 CB SER A 247 38.947 91.376 85.029 1.00 45.64 C ATOM 1621 OG SER A 247 40.251 91.586 85.501 1.00 45.70 O ATOM 1622 N PRO A 248 38.306 94.485 84.223 1.00 48.27 N ATOM 1623 CA PRO A 248 38.560 95.917 84.389 1.00 46.97 C ATOM 1624 C PRO A 248 39.910 96.211 85.036 1.00 46.34 C ATOM 1625 O PRO A 248 40.725 96.918 84.438 1.00 46.93 O ATOM 1626 CB PRO A 248 37.455 96.345 85.351 1.00 49.49 C ATOM 1627 CG PRO A 248 36.339 95.449 85.045 1.00 49.94 C ATOM 1628 CD PRO A 248 36.922 94.142 84.585 1.00 50.26 C ATOM 1629 N LEU A 249 40.118 95.690 86.244 1.00 44.46 N ATOM 1630 CA LEU A 249 41.396 95.810 86.940 1.00 42.66 C ATOM 1631 C LEU A 249 42.606 95.559 86.047 1.00 43.06 C ATOM 1632 O LEU A 249 43.500 96.382 85.972 1.00 42.97 O ATOM 1633 CB LEU A 249 41.457 94.840 88.112 1.00 42.83 C ATOM 1634 CG LEU A 249 41.424 95.463 89.495 1.00 43.94 C ATOM 1635 CD1 LEU A 249 40.042 95.951 89.752 1.00 47.21 C ATOM 1636 CD2 LEU A 249 41.796 94.443 90.524 1.00 46.28 C ATOM 1637 N LEU A 250 42.650 94.423 85.375 1.00 41.29 N ATOM 1638 CA LEU A 250 43.832 94.113 84.609 1.00 38.77 C ATOM 1639 C LEU A 250 43.923 95.014 83.394 1.00 42.13 C ATOM 1640 O LEU A 250 44.976 95.561 83.099 1.00 46.32 O ATOM 1641 CB LEU A 250 43.845 92.651 84.203 1.00 37.61 C ATOM 1642 CG LEU A 250 44.667 91.766 85.143 1.00 37.40 C ATOM 1643 CD1 LEU A 250 46.139 92.053 84.981 1.00 34.98 C ATOM 1644 CD2 LEU A 250 44.254 91.956 86.594 1.00 35.94 C ATOM 1645 N GLU A 251 42.802 95.172 82.706 1.00 42.85 N ATOM 1646 CA GLU A 251 42.694 96.022 81.525 1.00 44.04 C ATOM 1647 C GLU A 251 43.260 97.426 81.774 1.00 46.57 C ATOM 1648 O GLU A 251 43.917 98.004 80.910 1.00 50.19 O ATOM 1649 CB GLU A 251 41.223 96.097 81.084 1.00 45.48 C ATOM 1650 CG GLU A 251 40.992 96.505 79.637 1.00 53.08 C ATOM 1651 CD GLU A 251 39.579 96.143 79.124 1.00 65.69 C ATOM 1652 OE1 GLU A 251 38.579 96.764 79.603 1.00 62.35 O ATOM 1653 OE2 GLU A 251 39.471 95.237 78.236 1.00 64.28 O ATOM 1654 N THR A 252 43.022 97.973 82.959 1.00 42.64 N ATOM 1655 CA THR A 252 43.499 99.309 83.241 1.00 42.35 C ATOM 1656 C THR A 252 44.945 99.254 83.662 1.00 43.58 C ATOM 1657 O THR A 252 45.768 100.031 83.201 1.00 49.00 O ATOM 1658 CB THR A 252 42.689 99.973 84.350 1.00 47.20 C ATOM 1659 OG1 THR A 252 41.294 99.884 84.037 1.00 48.51 O ATOM 1660 CG2 THR A 252 43.092 101.440 84.496 1.00 46.61 C ATOM 1661 N SER A 253 45.259 98.314 84.536 1.00 47.21 N ATOM 1662 CA SER A 253 46.562 98.300 85.183 1.00 45.22 C ATOM 1663 C SER A 253 47.712 97.877 84.262 1.00 42.26 C ATOM 1664 O SER A 253 48.770 98.500 84.271 1.00 43.86 O ATOM 1665 CB SER A 253 46.516 97.445 86.449 1.00 44.13 C ATOM 1666 OG SER A 253 46.198 96.106 86.137 1.00 43.79 O ATOM 1667 N ILE A 254 47.497 96.833 83.466 1.00 42.87 N ATOM 1668 CA ILE A 254 48.540 96.307 82.588 1.00 43.34 C ATOM 1669 C ILE A 254 49.112 97.352 81.638 1.00 47.09 C ATOM 1670 O ILE A 254 50.276 97.244 81.219 1.00 50.07 O ATOM 1671 CB ILE A 254 48.063 95.091 81.768 1.00 40.60 C ATOM 1672 CG1 ILE A 254 49.260 94.249 81.330 1.00 43.49 C ATOM 1673 CG2 ILE A 254 47.286 95.515 80.553 1.00 40.88 C ATOM 1674 CD1 ILE A 254 48.989 93.350 80.137 1.00 41.43 C ATOM 1675 N VAL A 255 48.306 98.366 81.325 1.00 46.24 N ATOM 1676 CA VAL A 255 48.729 99.465 80.464 1.00 49.42 C ATOM 1677 C VAL A 255 49.917 100.276 81.015 1.00 50.29 C ATOM 1678 O VAL A 255 50.920 100.468 80.332 1.00 52.16 O ATOM 1679 CB VAL A 255 47.523 100.389 80.124 1.00 51.71 C ATOM 1680 CG1 VAL A 255 47.949 101.846 79.994 1.00 51.95 C ATOM 1681 CG2 VAL A 255 46.828 99.903 78.848 1.00 53.46 C ATOM 1682 N GLY A 256 49.807 100.757 82.245 1.00 46.72 N ATOM 1683 CA GLY A 256 50.890 101.512 82.838 1.00 49.13 C ATOM 1684 C GLY A 256 51.920 100.644 83.536 1.00 48.70 C ATOM 1685 O GLY A 256 52.948 101.148 83.963 1.00 50.91 O ATOM 1686 N ALA A 257 51.650 99.347 83.653 1.00 44.76 N ATOM 1687 CA ALA A 257 52.511 98.439 84.415 1.00 42.12 C ATOM 1688 C ALA A 257 53.987 98.489 84.005 1.00 42.70 C ATOM 1689 O ALA A 257 54.301 98.456 82.821 1.00 43.59 O ATOM 1690 CB ALA A 257 51.987 97.016 84.302 1.00 39.50 C ATOM 1691 N GLN A 258 54.889 98.559 84.979 1.00 39.25 N ATOM 1692 CA GLN A 258 56.311 98.548 84.669 1.00 40.30 C ATOM 1693 C GLN A 258 56.881 97.145 84.577 1.00 38.46 C ATOM 1694 O GLN A 258 57.904 96.931 83.940 1.00 41.93 O ATOM 1695 CB GLN A 258 57.107 99.356 85.688 1.00 45.93 C ATOM 1696 CG GLN A 258 57.065 100.856 85.500 1.00 47.53 C ATOM 1697 CD GLN A 258 57.597 101.588 86.725 1.00 56.85 C ATOM 1698 OE1 GLN A 258 58.014 100.962 87.702 1.00 57.01 O ATOM 1699 NE2 GLN A 258 57.571 102.919 86.684 1.00 64.16 N ATOM 1700 N GLY A 259 56.237 96.187 85.218 1.00 37.53 N ATOM 1701 CA GLY A 259 56.691 94.819 85.104 1.00 36.30 C ATOM 1702 C GLY A 259 55.516 93.913 84.862 1.00 36.17 C ATOM 1703 O GLY A 259 54.425 94.195 85.321 1.00 35.45 O ATOM 1704 N VAL A 260 55.733 92.838 84.121 1.00 33.93 N ATOM 1705 CA VAL A 260 54.686 91.861 83.893 1.00 30.46 C ATOM 1706 C VAL A 260 55.241 90.437 83.960 1.00 33.84 C ATOM 1707 O VAL A 260 56.232 90.111 83.311 1.00 33.20 O ATOM 1708 CB VAL A 260 53.955 92.098 82.560 1.00 31.86 C ATOM 1709 CG1 VAL A 260 53.060 90.930 82.243 1.00 33.75 C ATOM 1710 CG2 VAL A 260 53.136 93.362 82.621 1.00 31.99 C ATOM 1711 N LEU A 261 54.612 89.605 84.782 1.00 31.29 N ATOM 1712 CA LEU A 261 54.955 88.199 84.862 1.00 31.23 C ATOM 1713 C LEU A 261 53.886 87.427 84.149 1.00 33.21 C ATOM 1714 O LEU A 261 52.719 87.489 84.517 1.00 34.67 O ATOM 1715 CB LEU A 261 55.004 87.751 86.310 1.00 31.56 C ATOM 1716 CG LEU A 261 55.983 88.592 87.102 1.00 32.77 C ATOM 1717 CD1 LEU A 261 55.879 88.253 88.559 1.00 34.60 C ATOM 1718 CD2 LEU A 261 57.379 88.338 86.587 1.00 34.69 C HETATM 1719 N MSE A 262 54.284 86.690 83.124 1.00 33.27 N HETATM 1720 CA MSE A 262 53.319 85.964 82.320 1.00 29.67 C HETATM 1721 C MSE A 262 53.613 84.490 82.343 1.00 30.95 C HETATM 1722 O MSE A 262 54.751 84.081 82.222 1.00 34.28 O HETATM 1723 CB MSE A 262 53.330 86.477 80.890 1.00 32.14 C HETATM 1724 CG MSE A 262 51.962 86.555 80.295 1.00 35.59 C HETATM 1725 SE MSE A 262 51.850 85.629 78.619 0.60 44.78 Se HETATM 1726 CE MSE A 262 52.207 83.804 79.182 1.00 36.73 C ATOM 1727 N ASN A 263 52.588 83.684 82.528 1.00 32.42 N ATOM 1728 CA ASN A 263 52.812 82.262 82.532 1.00 33.27 C ATOM 1729 C ASN A 263 51.694 81.521 81.837 1.00 33.67 C ATOM 1730 O ASN A 263 50.527 81.805 82.064 1.00 34.41 O ATOM 1731 CB ASN A 263 53.000 81.739 83.953 1.00 33.46 C ATOM 1732 CG ASN A 263 53.903 80.537 83.997 1.00 39.63 C ATOM 1733 OD1 ASN A 263 55.120 80.677 84.076 1.00 45.36 O ATOM 1734 ND2 ASN A 263 53.324 79.345 83.917 1.00 36.30 N ATOM 1735 N ILE A 264 52.063 80.579 80.980 1.00 28.96 N ATOM 1736 CA ILE A 264 51.100 79.681 80.372 1.00 26.97 C ATOM 1737 C ILE A 264 51.465 78.239 80.684 1.00 27.56 C ATOM 1738 O ILE A 264 52.604 77.825 80.520 1.00 28.33 O ATOM 1739 CB ILE A 264 50.955 79.927 78.858 1.00 27.76 C ATOM 1740 CG1 ILE A 264 49.850 79.038 78.281 1.00 29.04 C ATOM 1741 CG2 ILE A 264 52.293 79.725 78.138 1.00 29.22 C ATOM 1742 CD1 ILE A 264 49.574 79.268 76.815 1.00 29.09 C ATOM 1743 N THR A 265 50.497 77.489 81.190 1.00 27.03 N ATOM 1744 CA THR A 265 50.734 76.111 81.568 1.00 28.24 C ATOM 1745 C THR A 265 49.785 75.252 80.765 1.00 30.71 C ATOM 1746 O THR A 265 48.624 75.587 80.616 1.00 32.15 O ATOM 1747 CB THR A 265 50.536 75.879 83.105 1.00 29.73 C ATOM 1748 OG1 THR A 265 51.328 76.810 83.849 1.00 29.93 O ATOM 1749 CG2 THR A 265 50.954 74.487 83.503 1.00 32.04 C ATOM 1750 N GLY A 266 50.284 74.156 80.218 1.00 30.73 N ATOM 1751 CA GLY A 266 49.430 73.237 79.499 1.00 31.28 C ATOM 1752 C GLY A 266 50.012 71.845 79.527 1.00 36.54 C ATOM 1753 O GLY A 266 51.078 71.637 80.084 1.00 37.27 O ATOM 1754 N GLY A 267 49.311 70.890 78.928 1.00 34.66 N ATOM 1755 CA GLY A 267 49.784 69.522 78.877 1.00 37.87 C ATOM 1756 C GLY A 267 50.613 69.249 77.641 1.00 36.48 C ATOM 1757 O GLY A 267 50.981 70.180 76.943 1.00 35.90 O ATOM 1758 N GLU A 268 50.891 67.981 77.356 1.00 38.05 N ATOM 1759 CA GLU A 268 51.759 67.625 76.234 1.00 42.14 C ATOM 1760 C GLU A 268 51.394 68.235 74.851 1.00 41.75 C ATOM 1761 O GLU A 268 52.279 68.511 74.045 1.00 37.68 O ATOM 1762 CB GLU A 268 51.948 66.107 76.148 1.00 49.45 C ATOM 1763 CG GLU A 268 52.856 65.686 74.981 1.00 69.15 C ATOM 1764 CD GLU A 268 53.000 64.155 74.826 1.00 84.28 C ATOM 1765 OE1 GLU A 268 52.414 63.417 75.666 1.00 86.14 O ATOM 1766 OE2 GLU A 268 53.697 63.694 73.872 1.00 78.34 O ATOM 1767 N SER A 269 50.113 68.488 74.599 1.00 39.60 N ATOM 1768 CA SER A 269 49.708 69.111 73.338 1.00 36.84 C ATOM 1769 C SER A 269 50.136 70.567 73.191 1.00 36.97 C ATOM 1770 O SER A 269 50.031 71.137 72.120 1.00 36.43 O ATOM 1771 CB SER A 269 48.190 69.001 73.129 1.00 37.74 C ATOM 1772 OG SER A 269 47.458 69.886 73.965 1.00 40.25 O ATOM 1773 N LEU A 270 50.600 71.188 74.262 1.00 36.27 N ATOM 1774 CA LEU A 270 51.043 72.568 74.146 1.00 35.34 C ATOM 1775 C LEU A 270 52.447 72.606 73.565 1.00 35.57 C ATOM 1776 O LEU A 270 53.309 71.856 73.982 1.00 36.50 O ATOM 1777 CB LEU A 270 51.005 73.274 75.500 1.00 34.35 C ATOM 1778 CG LEU A 270 51.396 74.747 75.479 1.00 30.41 C ATOM 1779 CD1 LEU A 270 50.496 75.496 74.532 1.00 28.85 C ATOM 1780 CD2 LEU A 270 51.315 75.323 76.866 1.00 28.74 C ATOM 1781 N SER A 271 52.681 73.472 72.591 1.00 36.49 N ATOM 1782 CA SER A 271 54.019 73.611 72.040 1.00 34.27 C ATOM 1783 C SER A 271 54.476 75.008 72.311 1.00 32.66 C ATOM 1784 O SER A 271 53.667 75.863 72.613 1.00 35.37 O ATOM 1785 CB SER A 271 54.027 73.355 70.532 1.00 38.37 C ATOM 1786 OG SER A 271 53.275 74.338 69.834 1.00 39.27 O ATOM 1787 N LEU A 272 55.769 75.251 72.186 1.00 31.10 N ATOM 1788 CA LEU A 272 56.286 76.584 72.429 1.00 32.95 C ATOM 1789 C LEU A 272 55.676 77.608 71.456 1.00 34.92 C ATOM 1790 O LEU A 272 55.512 78.783 71.782 1.00 35.18 O ATOM 1791 CB LEU A 272 57.818 76.580 72.382 1.00 35.00 C ATOM 1792 CG LEU A 272 58.485 75.574 73.326 1.00 36.24 C ATOM 1793 CD1 LEU A 272 59.981 75.658 73.262 1.00 37.80 C ATOM 1794 CD2 LEU A 272 58.012 75.764 74.770 1.00 34.75 C ATOM 1795 N PHE A 273 55.310 77.149 70.265 1.00 35.28 N ATOM 1796 CA PHE A 273 54.767 78.043 69.258 1.00 33.43 C ATOM 1797 C PHE A 273 53.353 78.454 69.544 1.00 33.37 C ATOM 1798 O PHE A 273 52.950 79.554 69.178 1.00 34.10 O ATOM 1799 CB PHE A 273 54.894 77.436 67.874 1.00 34.32 C ATOM 1800 CG PHE A 273 56.243 77.616 67.293 1.00 35.46 C ATOM 1801 CD1 PHE A 273 56.591 78.815 66.715 1.00 35.84 C ATOM 1802 CD2 PHE A 273 57.185 76.609 67.372 1.00 39.47 C ATOM 1803 CE1 PHE A 273 57.847 79.002 66.206 1.00 42.61 C ATOM 1804 CE2 PHE A 273 58.444 76.786 66.857 1.00 41.32 C ATOM 1805 CZ PHE A 273 58.780 77.988 66.279 1.00 42.36 C ATOM 1806 N GLU A 274 52.607 77.570 70.200 1.00 32.35 N ATOM 1807 CA GLU A 274 51.261 77.892 70.646 1.00 33.29 C ATOM 1808 C GLU A 274 51.340 78.815 71.848 1.00 33.26 C ATOM 1809 O GLU A 274 50.602 79.788 71.956 1.00 33.85 O ATOM 1810 CB GLU A 274 50.483 76.618 70.995 1.00 34.08 C ATOM 1811 CG GLU A 274 49.024 76.861 71.412 1.00 32.14 C ATOM 1812 CD GLU A 274 48.182 75.594 71.501 1.00 36.45 C ATOM 1813 OE1 GLU A 274 48.735 74.480 71.604 1.00 37.48 O ATOM 1814 OE2 GLU A 274 46.944 75.715 71.456 1.00 41.91 O ATOM 1815 N ALA A 275 52.254 78.496 72.749 1.00 31.11 N ATOM 1816 CA ALA A 275 52.465 79.293 73.939 1.00 30.25 C ATOM 1817 C ALA A 275 52.751 80.721 73.528 1.00 33.75 C ATOM 1818 O ALA A 275 52.186 81.658 74.077 1.00 36.15 O ATOM 1819 CB ALA A 275 53.610 78.731 74.731 1.00 31.16 C ATOM 1820 N GLN A 276 53.606 80.876 72.528 1.00 32.92 N ATOM 1821 CA GLN A 276 54.009 82.186 72.055 1.00 34.27 C ATOM 1822 C GLN A 276 52.851 82.983 71.464 1.00 38.00 C ATOM 1823 O GLN A 276 52.888 84.212 71.433 1.00 39.96 O ATOM 1824 CB GLN A 276 55.146 82.050 71.036 1.00 39.49 C ATOM 1825 CG GLN A 276 55.677 83.367 70.473 1.00 41.86 C ATOM 1826 CD GLN A 276 56.720 84.001 71.359 1.00 48.90 C ATOM 1827 OE1 GLN A 276 57.704 83.362 71.727 1.00 49.93 O ATOM 1828 NE2 GLN A 276 56.512 85.265 71.712 1.00 48.79 N ATOM 1829 N GLU A 277 51.822 82.286 70.997 1.00 36.08 N ATOM 1830 CA GLU A 277 50.607 82.947 70.533 1.00 35.50 C ATOM 1831 C GLU A 277 49.965 83.755 71.654 1.00 37.11 C ATOM 1832 O GLU A 277 49.470 84.853 71.431 1.00 39.12 O ATOM 1833 CB GLU A 277 49.616 81.908 70.025 1.00 39.28 C ATOM 1834 CG GLU A 277 49.836 81.491 68.600 1.00 39.65 C ATOM 1835 CD GLU A 277 49.178 82.452 67.654 1.00 45.93 C ATOM 1836 OE1 GLU A 277 48.025 82.183 67.248 1.00 46.06 O ATOM 1837 OE2 GLU A 277 49.799 83.489 67.344 1.00 50.07 O ATOM 1838 N ALA A 278 49.978 83.201 72.864 1.00 34.94 N ATOM 1839 CA ALA A 278 49.400 83.862 74.026 1.00 33.89 C ATOM 1840 C ALA A 278 50.261 85.033 74.498 1.00 36.82 C ATOM 1841 O ALA A 278 49.765 86.127 74.766 1.00 35.28 O ATOM 1842 CB ALA A 278 49.210 82.854 75.151 1.00 33.77 C ATOM 1843 N ALA A 279 51.560 84.773 74.600 1.00 37.68 N ATOM 1844 CA ALA A 279 52.542 85.760 75.021 1.00 33.90 C ATOM 1845 C ALA A 279 52.502 87.006 74.150 1.00 37.08 C ATOM 1846 O ALA A 279 52.729 88.110 74.629 1.00 38.06 O ATOM 1847 CB ALA A 279 53.927 85.144 75.014 1.00 34.37 C ATOM 1848 N ASP A 280 52.200 86.832 72.869 1.00 39.09 N ATOM 1849 CA ASP A 280 52.073 87.980 71.974 1.00 38.74 C ATOM 1850 C ASP A 280 50.853 88.844 72.318 1.00 37.42 C ATOM 1851 O ASP A 280 50.939 90.065 72.324 1.00 37.75 O ATOM 1852 CB ASP A 280 52.073 87.556 70.500 1.00 39.30 C ATOM 1853 CG ASP A 280 53.472 87.134 69.993 1.00 51.05 C ATOM 1854 OD1 ASP A 280 54.487 87.325 70.718 1.00 51.22 O ATOM 1855 OD2 ASP A 280 53.563 86.617 68.852 1.00 48.70 O ATOM 1856 N ILE A 281 49.728 88.215 72.638 1.00 34.27 N ATOM 1857 CA ILE A 281 48.532 88.960 73.023 1.00 31.76 C ATOM 1858 C ILE A 281 48.786 89.893 74.201 1.00 35.09 C ATOM 1859 O ILE A 281 48.375 91.052 74.193 1.00 36.63 O ATOM 1860 CB ILE A 281 47.387 88.023 73.401 1.00 31.42 C ATOM 1861 CG1 ILE A 281 46.861 87.304 72.164 1.00 32.68 C ATOM 1862 CG2 ILE A 281 46.267 88.807 74.041 1.00 32.09 C ATOM 1863 CD1 ILE A 281 45.982 88.178 71.321 1.00 35.23 C ATOM 1864 N VAL A 282 49.468 89.366 75.211 1.00 34.60 N ATOM 1865 CA VAL A 282 49.777 90.094 76.431 1.00 33.69 C ATOM 1866 C VAL A 282 50.805 91.188 76.163 1.00 35.02 C ATOM 1867 O VAL A 282 50.649 92.324 76.585 1.00 34.77 O ATOM 1868 CB VAL A 282 50.309 89.120 77.507 1.00 36.92 C ATOM 1869 CG1 VAL A 282 50.823 89.860 78.730 1.00 35.41 C ATOM 1870 CG2 VAL A 282 49.235 88.118 77.880 1.00 32.82 C ATOM 1871 N GLN A 283 51.854 90.843 75.437 1.00 35.97 N ATOM 1872 CA GLN A 283 52.868 91.821 75.084 1.00 39.32 C ATOM 1873 C GLN A 283 52.331 93.006 74.255 1.00 38.89 C ATOM 1874 O GLN A 283 52.815 94.128 74.392 1.00 42.45 O ATOM 1875 CB GLN A 283 54.034 91.137 74.380 1.00 39.49 C ATOM 1876 CG GLN A 283 55.313 91.946 74.407 1.00 48.06 C ATOM 1877 CD GLN A 283 56.274 91.551 73.300 1.00 58.58 C ATOM 1878 OE1 GLN A 283 56.775 90.416 73.261 1.00 59.58 O ATOM 1879 NE2 GLN A 283 56.535 92.486 72.384 1.00 59.13 N ATOM 1880 N ASP A 284 51.328 92.770 73.416 1.00 35.15 N ATOM 1881 CA ASP A 284 50.704 93.866 72.691 1.00 37.89 C ATOM 1882 C ASP A 284 49.912 94.794 73.606 1.00 40.06 C ATOM 1883 O ASP A 284 49.782 95.979 73.335 1.00 43.42 O ATOM 1884 CB ASP A 284 49.796 93.337 71.587 1.00 46.26 C ATOM 1885 CG ASP A 284 49.857 94.189 70.315 1.00 65.88 C ATOM 1886 OD1 ASP A 284 50.622 93.807 69.382 1.00 71.89 O ATOM 1887 OD2 ASP A 284 49.137 95.231 70.247 1.00 65.06 O ATOM 1888 N ALA A 285 49.386 94.248 74.697 1.00 39.04 N ATOM 1889 CA ALA A 285 48.596 95.007 75.666 1.00 33.72 C ATOM 1890 C ALA A 285 49.431 95.787 76.702 1.00 38.79 C ATOM 1891 O ALA A 285 49.036 96.864 77.149 1.00 41.30 O ATOM 1892 CB ALA A 285 47.621 94.079 76.358 1.00 32.07 C ATOM 1893 N ALA A 286 50.573 95.233 77.097 1.00 38.67 N ATOM 1894 CA ALA A 286 51.499 95.956 77.953 1.00 41.46 C ATOM 1895 C ALA A 286 52.181 96.979 77.089 1.00 41.01 C ATOM 1896 O ALA A 286 52.278 96.796 75.886 1.00 46.41 O ATOM 1897 CB ALA A 286 52.529 95.018 78.557 1.00 38.93 C ATOM 1898 N ASP A 287 52.671 98.052 77.684 1.00 39.65 N ATOM 1899 CA ASP A 287 53.360 99.037 76.887 1.00 47.90 C ATOM 1900 C ASP A 287 54.722 98.556 76.445 1.00 51.29 C ATOM 1901 O ASP A 287 55.161 97.457 76.775 1.00 48.11 O ATOM 1902 CB ASP A 287 53.507 100.356 77.628 1.00 56.24 C ATOM 1903 CG ASP A 287 54.152 100.181 78.945 1.00 59.95 C ATOM 1904 OD1 ASP A 287 53.844 99.132 79.564 1.00 59.91 O ATOM 1905 OD2 ASP A 287 54.964 101.058 79.334 1.00 61.74 O ATOM 1906 N GLU A 288 55.384 99.417 75.689 1.00 54.13 N ATOM 1907 CA GLU A 288 56.594 99.050 74.982 1.00 55.75 C ATOM 1908 C GLU A 288 57.770 98.795 75.930 1.00 55.62 C ATOM 1909 O GLU A 288 58.516 97.827 75.751 1.00 53.06 O ATOM 1910 CB GLU A 288 56.928 100.119 73.923 1.00 59.79 C ATOM 1911 CG GLU A 288 55.881 100.266 72.787 1.00 63.03 C ATOM 1912 CD GLU A 288 55.957 99.154 71.693 1.00 69.75 C ATOM 1913 OE1 GLU A 288 56.865 98.264 71.767 1.00 65.70 O ATOM 1914 OE2 GLU A 288 55.100 99.175 70.759 1.00 59.42 O ATOM 1915 N ASP A 289 57.927 99.637 76.949 1.00 52.74 N ATOM 1916 CA ASP A 289 59.105 99.523 77.803 1.00 51.02 C ATOM 1917 C ASP A 289 58.953 98.572 78.978 1.00 50.66 C ATOM 1918 O ASP A 289 59.696 98.667 79.943 1.00 50.73 O ATOM 1919 CB ASP A 289 59.518 100.881 78.357 1.00 56.40 C ATOM 1920 CG ASP A 289 59.693 101.939 77.279 1.00 64.74 C ATOM 1921 OD1 ASP A 289 59.964 101.600 76.086 1.00 59.91 O ATOM 1922 OD2 ASP A 289 59.570 103.137 77.659 1.00 66.49 O ATOM 1923 N VAL A 290 58.004 97.658 78.921 1.00 48.86 N ATOM 1924 CA VAL A 290 57.764 96.823 80.075 1.00 41.76 C ATOM 1925 C VAL A 290 58.871 95.796 80.281 1.00 40.03 C ATOM 1926 O VAL A 290 59.500 95.352 79.329 1.00 42.37 O ATOM 1927 CB VAL A 290 56.380 96.149 80.004 1.00 42.84 C ATOM 1928 CG1 VAL A 290 56.390 95.016 79.003 1.00 42.93 C ATOM 1929 CG2 VAL A 290 55.933 95.651 81.410 1.00 39.90 C ATOM 1930 N ASN A 291 59.123 95.458 81.544 1.00 40.09 N ATOM 1931 CA ASN A 291 60.030 94.375 81.908 1.00 38.25 C ATOM 1932 C ASN A 291 59.192 93.121 82.086 1.00 36.78 C ATOM 1933 O ASN A 291 58.589 92.921 83.127 1.00 36.45 O ATOM 1934 CB ASN A 291 60.757 94.726 83.210 1.00 34.21 C ATOM 1935 CG ASN A 291 61.770 93.673 83.644 1.00 37.73 C ATOM 1936 OD1 ASN A 291 61.765 92.540 83.180 1.00 39.69 O ATOM 1937 ND2 ASN A 291 62.644 94.053 84.559 1.00 39.64 N HETATM 1938 N MSE A 292 59.143 92.276 81.066 1.00 36.06 N HETATM 1939 CA MSE A 292 58.210 91.161 81.092 1.00 34.82 C HETATM 1940 C MSE A 292 58.889 89.819 81.147 1.00 33.33 C HETATM 1941 O MSE A 292 59.675 89.484 80.276 1.00 36.60 O HETATM 1942 CB MSE A 292 57.255 91.191 79.894 1.00 34.64 C HETATM 1943 CG MSE A 292 56.176 90.116 79.983 1.00 34.54 C HETATM 1944 SE MSE A 292 55.070 89.919 78.414 0.60 34.50 Se HETATM 1945 CE MSE A 292 54.219 91.647 78.491 1.00 35.54 C ATOM 1946 N ILE A 293 58.567 89.045 82.175 1.00 32.89 N ATOM 1947 CA ILE A 293 59.034 87.678 82.268 1.00 31.25 C ATOM 1948 C ILE A 293 57.933 86.772 81.745 1.00 31.08 C ATOM 1949 O ILE A 293 56.805 86.837 82.208 1.00 35.08 O ATOM 1950 CB ILE A 293 59.402 87.309 83.703 1.00 27.89 C ATOM 1951 CG1 ILE A 293 60.398 88.321 84.257 1.00 35.35 C ATOM 1952 CG2 ILE A 293 59.991 85.928 83.760 1.00 28.63 C ATOM 1953 CD1 ILE A 293 60.745 88.121 85.730 1.00 36.11 C ATOM 1954 N PHE A 294 58.267 85.947 80.763 1.00 29.51 N ATOM 1955 CA PHE A 294 57.316 85.052 80.128 1.00 29.47 C ATOM 1956 C PHE A 294 57.731 83.620 80.383 1.00 31.64 C ATOM 1957 O PHE A 294 58.827 83.220 80.043 1.00 33.05 O ATOM 1958 CB PHE A 294 57.253 85.354 78.623 1.00 30.05 C ATOM 1959 CG PHE A 294 56.718 84.230 77.783 1.00 31.80 C ATOM 1960 CD1 PHE A 294 55.539 83.578 78.117 1.00 33.64 C ATOM 1961 CD2 PHE A 294 57.377 83.851 76.634 1.00 32.93 C ATOM 1962 CE1 PHE A 294 55.048 82.547 77.341 1.00 31.63 C ATOM 1963 CE2 PHE A 294 56.882 82.826 75.844 1.00 35.68 C ATOM 1964 CZ PHE A 294 55.715 82.169 76.206 1.00 31.40 C ATOM 1965 N GLY A 295 56.845 82.845 80.984 1.00 30.19 N ATOM 1966 CA GLY A 295 57.142 81.460 81.276 1.00 28.26 C ATOM 1967 C GLY A 295 56.176 80.517 80.606 1.00 27.72 C ATOM 1968 O GLY A 295 55.066 80.890 80.299 1.00 28.84 O ATOM 1969 N THR A 296 56.614 79.288 80.387 1.00 29.07 N ATOM 1970 CA THR A 296 55.853 78.290 79.654 1.00 27.54 C ATOM 1971 C THR A 296 56.101 76.936 80.280 1.00 29.30 C ATOM 1972 O THR A 296 57.221 76.444 80.272 1.00 30.43 O ATOM 1973 CB THR A 296 56.282 78.221 78.157 1.00 30.66 C ATOM 1974 OG1 THR A 296 55.951 79.445 77.502 1.00 31.96 O ATOM 1975 CG2 THR A 296 55.588 77.082 77.429 1.00 28.93 C ATOM 1976 N VAL A 297 55.055 76.331 80.825 1.00 28.37 N ATOM 1977 CA VAL A 297 55.215 75.021 81.431 1.00 29.92 C ATOM 1978 C VAL A 297 54.424 73.981 80.672 1.00 34.29 C ATOM 1979 O VAL A 297 53.281 74.196 80.317 1.00 36.61 O ATOM 1980 CB VAL A 297 54.821 75.020 82.932 1.00 30.03 C ATOM 1981 CG1 VAL A 297 54.948 73.641 83.520 1.00 28.28 C ATOM 1982 CG2 VAL A 297 55.689 75.980 83.700 1.00 28.53 C ATOM 1983 N ILE A 298 55.058 72.859 80.389 1.00 34.13 N ATOM 1984 CA ILE A 298 54.352 71.752 79.799 1.00 33.83 C ATOM 1985 C ILE A 298 54.199 70.742 80.901 1.00 36.73 C ATOM 1986 O ILE A 298 55.171 70.191 81.376 1.00 39.16 O ATOM 1987 CB ILE A 298 55.113 71.150 78.609 1.00 36.57 C ATOM 1988 CG1 ILE A 298 55.453 72.240 77.592 1.00 33.72 C ATOM 1989 CG2 ILE A 298 54.315 70.030 77.954 1.00 34.21 C ATOM 1990 CD1 ILE A 298 54.362 73.238 77.363 1.00 33.42 C ATOM 1991 N ASN A 299 52.964 70.530 81.328 1.00 40.17 N ATOM 1992 CA ASN A 299 52.682 69.656 82.452 1.00 42.55 C ATOM 1993 C ASN A 299 51.582 68.656 82.135 1.00 44.14 C ATOM 1994 O ASN A 299 50.413 69.018 82.094 1.00 44.28 O ATOM 1995 CB ASN A 299 52.281 70.507 83.647 1.00 44.71 C ATOM 1996 CG ASN A 299 52.053 69.692 84.899 1.00 49.91 C ATOM 1997 OD1 ASN A 299 52.363 68.500 84.953 1.00 53.22 O ATOM 1998 ND2 ASN A 299 51.520 70.340 85.925 1.00 51.34 N ATOM 1999 N PRO A 300 51.962 67.390 81.929 1.00 46.70 N ATOM 2000 CA PRO A 300 51.066 66.294 81.569 1.00 46.48 C ATOM 2001 C PRO A 300 49.748 66.248 82.337 1.00 51.75 C ATOM 2002 O PRO A 300 48.726 66.043 81.692 1.00 54.99 O ATOM 2003 CB PRO A 300 51.913 65.065 81.858 1.00 46.34 C ATOM 2004 CG PRO A 300 53.269 65.518 81.450 1.00 48.87 C ATOM 2005 CD PRO A 300 53.358 66.926 81.986 1.00 48.35 C ATOM 2006 N GLU A 301 49.725 66.465 83.644 1.00 52.79 N ATOM 2007 CA GLU A 301 48.454 66.344 84.356 1.00 52.75 C ATOM 2008 C GLU A 301 47.375 67.348 83.907 1.00 52.57 C ATOM 2009 O GLU A 301 46.257 67.332 84.425 1.00 54.36 O ATOM 2010 CB GLU A 301 48.656 66.377 85.884 1.00 60.30 C ATOM 2011 CG GLU A 301 48.679 67.760 86.562 1.00 62.00 C ATOM 2012 CD GLU A 301 49.237 67.696 88.004 1.00 74.14 C ATOM 2013 OE1 GLU A 301 49.283 66.573 88.573 1.00 71.77 O ATOM 2014 OE2 GLU A 301 49.648 68.758 88.559 1.00 73.73 O ATOM 2015 N LEU A 302 47.698 68.203 82.938 1.00 51.29 N ATOM 2016 CA LEU A 302 46.769 69.244 82.495 1.00 50.72 C ATOM 2017 C LEU A 302 45.876 68.791 81.339 1.00 53.05 C ATOM 2018 O LEU A 302 44.811 69.366 81.095 1.00 52.50 O ATOM 2019 CB LEU A 302 47.526 70.517 82.106 1.00 48.72 C ATOM 2020 CG LEU A 302 47.462 71.726 83.048 1.00 45.25 C ATOM 2021 CD1 LEU A 302 46.153 72.481 82.887 1.00 42.78 C ATOM 2022 CD2 LEU A 302 47.652 71.285 84.494 1.00 48.03 C ATOM 2023 N GLN A 303 46.311 67.768 80.623 1.00 51.98 N ATOM 2024 CA GLN A 303 45.509 67.231 79.526 1.00 55.19 C ATOM 2025 C GLN A 303 45.241 68.251 78.418 1.00 51.68 C ATOM 2026 O GLN A 303 46.166 68.679 77.719 1.00 49.66 O ATOM 2027 CB GLN A 303 44.199 66.627 80.051 1.00 52.70 C ATOM 2028 CG GLN A 303 44.439 65.468 81.036 1.00 63.45 C ATOM 2029 CD GLN A 303 43.381 65.388 82.148 1.00 66.49 C ATOM 2030 OE1 GLN A 303 42.826 64.309 82.426 1.00 67.60 O ATOM 2031 NE2 GLN A 303 43.108 66.530 82.797 1.00 60.96 N ATOM 2032 N ASP A 304 43.980 68.639 78.262 1.00 50.15 N ATOM 2033 CA ASP A 304 43.586 69.396 77.086 1.00 47.20 C ATOM 2034 C ASP A 304 43.226 70.845 77.323 1.00 46.52 C ATOM 2035 O ASP A 304 42.790 71.541 76.395 1.00 50.65 O ATOM 2036 CB ASP A 304 42.465 68.679 76.352 1.00 50.46 C ATOM 2037 CG ASP A 304 42.999 67.617 75.399 1.00 66.46 C ATOM 2038 OD1 ASP A 304 43.784 67.992 74.472 1.00 65.45 O ATOM 2039 OD2 ASP A 304 42.669 66.415 75.593 1.00 66.75 O ATOM 2040 N GLU A 305 43.437 71.300 78.552 1.00 46.83 N ATOM 2041 CA GLU A 305 43.159 72.674 78.929 1.00 44.70 C ATOM 2042 C GLU A 305 44.445 73.460 79.128 1.00 40.76 C ATOM 2043 O GLU A 305 45.491 72.894 79.401 1.00 43.22 O ATOM 2044 CB GLU A 305 42.371 72.693 80.225 1.00 47.63 C ATOM 2045 CG GLU A 305 41.433 73.851 80.314 1.00 51.39 C ATOM 2046 CD GLU A 305 39.998 73.410 80.577 1.00 64.13 C ATOM 2047 OE1 GLU A 305 39.098 73.805 79.768 1.00 61.13 O ATOM 2048 OE2 GLU A 305 39.781 72.681 81.595 1.00 64.17 O ATOM 2049 N ILE A 306 44.371 74.774 79.004 1.00 37.90 N ATOM 2050 CA ILE A 306 45.534 75.600 79.280 1.00 36.11 C ATOM 2051 C ILE A 306 45.189 76.721 80.271 1.00 37.12 C ATOM 2052 O ILE A 306 44.038 77.138 80.356 1.00 35.82 O ATOM 2053 CB ILE A 306 46.132 76.166 77.974 1.00 35.87 C ATOM 2054 CG1 ILE A 306 45.129 77.033 77.252 1.00 34.15 C ATOM 2055 CG2 ILE A 306 46.556 75.060 77.061 1.00 36.23 C ATOM 2056 CD1 ILE A 306 45.775 78.192 76.682 1.00 35.96 C ATOM 2057 N VAL A 307 46.172 77.188 81.039 1.00 33.54 N ATOM 2058 CA VAL A 307 45.937 78.272 81.991 1.00 28.05 C ATOM 2059 C VAL A 307 46.905 79.388 81.752 1.00 28.36 C ATOM 2060 O VAL A 307 48.099 79.166 81.716 1.00 32.11 O ATOM 2061 CB VAL A 307 46.229 77.862 83.422 1.00 29.50 C ATOM 2062 CG1 VAL A 307 45.372 78.673 84.380 1.00 31.48 C ATOM 2063 CG2 VAL A 307 46.044 76.394 83.602 1.00 35.68 C ATOM 2064 N VAL A 308 46.400 80.601 81.643 1.00 27.45 N ATOM 2065 CA VAL A 308 47.259 81.751 81.461 1.00 27.25 C ATOM 2066 C VAL A 308 47.125 82.671 82.656 1.00 28.95 C ATOM 2067 O VAL A 308 46.038 83.107 82.988 1.00 30.04 O ATOM 2068 CB VAL A 308 46.945 82.491 80.134 1.00 26.90 C ATOM 2069 CG1 VAL A 308 47.675 83.796 80.051 1.00 26.72 C ATOM 2070 CG2 VAL A 308 47.318 81.619 78.959 1.00 28.78 C ATOM 2071 N THR A 309 48.238 82.936 83.322 1.00 29.09 N ATOM 2072 CA THR A 309 48.259 83.989 84.318 1.00 29.16 C ATOM 2073 C THR A 309 49.093 85.178 83.874 1.00 30.33 C ATOM 2074 O THR A 309 50.196 85.020 83.372 1.00 31.88 O ATOM 2075 CB THR A 309 48.734 83.495 85.697 1.00 33.30 C ATOM 2076 OG1 THR A 309 49.856 82.615 85.548 1.00 38.37 O ATOM 2077 CG2 THR A 309 47.616 82.762 86.390 1.00 33.43 C ATOM 2078 N VAL A 310 48.539 86.367 84.067 1.00 28.83 N ATOM 2079 CA VAL A 310 49.238 87.602 83.795 1.00 26.14 C ATOM 2080 C VAL A 310 49.322 88.439 85.061 1.00 29.46 C ATOM 2081 O VAL A 310 48.320 88.913 85.552 1.00 31.74 O ATOM 2082 CB VAL A 310 48.519 88.396 82.701 1.00 27.45 C ATOM 2083 CG1 VAL A 310 49.063 89.797 82.611 1.00 29.55 C ATOM 2084 CG2 VAL A 310 48.666 87.692 81.387 1.00 30.40 C ATOM 2085 N ILE A 311 50.524 88.618 85.587 1.00 27.32 N ATOM 2086 CA ILE A 311 50.724 89.428 86.774 1.00 26.55 C ATOM 2087 C ILE A 311 51.286 90.801 86.432 1.00 29.80 C ATOM 2088 O ILE A 311 52.333 90.907 85.831 1.00 32.91 O ATOM 2089 CB ILE A 311 51.654 88.723 87.755 1.00 27.59 C ATOM 2090 CG1 ILE A 311 51.070 87.362 88.137 1.00 27.32 C ATOM 2091 CG2 ILE A 311 51.874 89.575 88.985 1.00 27.22 C ATOM 2092 CD1 ILE A 311 51.829 86.636 89.240 1.00 23.95 C ATOM 2093 N ALA A 312 50.572 91.851 86.818 1.00 31.43 N ATOM 2094 CA ALA A 312 51.008 93.227 86.606 1.00 29.53 C ATOM 2095 C ALA A 312 51.504 93.870 87.900 1.00 34.48 C ATOM 2096 O ALA A 312 50.963 93.646 88.969 1.00 33.80 O ATOM 2097 CB ALA A 312 49.882 94.045 86.027 1.00 29.64 C ATOM 2098 N THR A 313 52.540 94.681 87.791 1.00 36.79 N ATOM 2099 CA THR A 313 53.071 95.377 88.941 1.00 34.89 C ATOM 2100 C THR A 313 53.859 96.602 88.493 1.00 38.23 C ATOM 2101 O THR A 313 54.208 96.732 87.332 1.00 41.34 O ATOM 2102 CB THR A 313 53.985 94.476 89.761 1.00 34.45 C ATOM 2103 OG1 THR A 313 54.307 95.137 90.985 1.00 36.23 O ATOM 2104 CG2 THR A 313 55.272 94.179 89.004 1.00 34.62 C ATOM 2105 N GLY A 314 54.128 97.502 89.423 1.00 37.54 N ATOM 2106 CA GLY A 314 54.864 98.710 89.129 1.00 40.79 C ATOM 2107 C GLY A 314 53.965 99.803 88.608 1.00 45.23 C ATOM 2108 O GLY A 314 54.207 100.329 87.533 1.00 48.44 O ATOM 2109 N PHE A 315 52.926 100.154 89.360 1.00 46.97 N ATOM 2110 CA PHE A 315 52.000 101.203 88.917 1.00 51.31 C ATOM 2111 C PHE A 315 52.468 102.608 89.305 1.00 56.17 C ATOM 2112 O PHE A 315 52.987 102.834 90.409 1.00 53.35 O ATOM 2113 CB PHE A 315 50.591 100.959 89.461 1.00 50.38 C ATOM 2114 CG PHE A 315 50.195 99.511 89.481 1.00 47.92 C ATOM 2115 CD1 PHE A 315 50.064 98.802 88.308 1.00 43.31 C ATOM 2116 CD2 PHE A 315 49.960 98.864 90.676 1.00 47.64 C ATOM 2117 CE1 PHE A 315 49.711 97.487 88.329 1.00 42.13 C ATOM 2118 CE2 PHE A 315 49.603 97.543 90.702 1.00 42.23 C ATOM 2119 CZ PHE A 315 49.480 96.855 89.529 1.00 42.17 C CONECT 121 120 127 122 CONECT 119 120 110 CONECT 594 593 600 595 CONECT 592 593 586 CONECT 644 643 650 645 CONECT 642 643 640 CONECT 762 761 768 763 CONECT 760 753 761 CONECT 937 943 938 936 CONECT 935 932 936 CONECT 1127 1128 1126 1133 CONECT 1125 1120 1126 CONECT 1135 1134 1136 1141 CONECT 1133 1134 1127 CONECT 1421 1427 1422 1420 CONECT 1419 1413 1420 CONECT 1475 1481 1476 1474 CONECT 1473 1467 1474 CONECT 1721 1722 1727 1720 CONECT 1719 1713 1720 CONECT 1940 1941 1939 1946 CONECT 1938 1939 1932 END If you find results from this site helpful for your research, please cite one of our papers:
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