HEADER SIGNALING PROTEIN, ELECTRON TRANSPORT 07-DEC-12 4IB4 TITLE CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF 5-HT2B-BRIL IN COMPLEX TITLE 2 WITH ERGOTAMINE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF HUMAN 5-HYDROXYTRYPTAMINE RECEPTOR 2B COMPND 3 AND E. COLI SOLUBLE CYTOCHROME B562; COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: HTR2B, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS ERGOTAMINE, NOVEL PROTEIN ENGINEERING, GPCR NETWORK, MEMBRANE KEYWDS 2 PROTEIN, PSI-BIOLOGY, STRUCTURAL GENOMICS, GPCR, SIGNALING PROTEIN, KEYWDS 3 ELECTRON TRANSPORT, GPCR DOCK EXPDTA X-RAY DIFFRACTION AUTHOR D.WACKER,C.WANG,V.KATRITCH,G.W.HAN,X.HUANG,E.VARDY,J.D.MCCORVY, AUTHOR 2 Y.JIANG,M.CHU,F.Y.SIU,W.LIU,H.E.XU,V.CHEREZOV,B.L.ROTH,R.C.STEVENS, AUTHOR 3 GPCR NETWORK (GPCR) REVDAT 6 15-NOV-17 4IB4 1 REMARK REVDAT 5 07-JUN-17 4IB4 1 COMPND SOURCE REMARK REVDAT 4 15-MAY-13 4IB4 1 JRNL REVDAT 3 10-APR-13 4IB4 1 JRNL REVDAT 2 03-APR-13 4IB4 1 JRNL REVDAT 1 13-MAR-13 4IB4 0 JRNL AUTH D.WACKER,C.WANG,V.KATRITCH,G.W.HAN,X.P.HUANG,E.VARDY, JRNL AUTH 2 J.D.MCCORVY,Y.JIANG,M.CHU,F.Y.SIU,W.LIU,H.E.XU,V.CHEREZOV, JRNL AUTH 3 B.L.ROTH,R.C.STEVENS JRNL TITL STRUCTURAL FEATURES FOR FUNCTIONAL SELECTIVITY AT SEROTONIN JRNL TITL 2 RECEPTORS. JRNL REF SCIENCE V. 340 615 2013 JRNL REFN ISSN 0036-8075 JRNL PMID 23519215 JRNL DOI 10.1126/SCIENCE.1232808 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.84 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.7 REMARK 3 NUMBER OF REFLECTIONS : 15818 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.227 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 823 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 2.8900 - 2.7000 0.91 2735 162 0.2596 0.2540 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 72.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.04 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.01210 REMARK 3 B22 (A**2) : -1.23750 REMARK 3 B33 (A**2) : 3.24970 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 : 0.009 3121 REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL 1432 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|48 - A|400 } REMARK 3 ORIGIN FOR THE GROUP (A): 22.3909 17.7334 -2.6841 REMARK 3 T TENSOR REMARK 3 T11: -0.0480 T22: -0.2239 REMARK 3 T33: -0.1946 T12: 0.0189 REMARK 3 T13: -0.0017 T23: -0.0207 REMARK 3 L TENSOR REMARK 3 L11: 1.7189 L22: 1.5218 REMARK 3 L33: 2.7370 L12: 0.0732 REMARK 3 L13: -0.4784 L23: 0.6197 REMARK 3 S TENSOR REMARK 3 S11: 0.0917 S12: 0.0111 S13: 0.1175 REMARK 3 S21: -0.0336 S22: -0.0676 S23: 0.0689 REMARK 3 S31: -0.0945 S32: -0.0891 S33: -0.0240 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1001- A|1106 } REMARK 3 ORIGIN FOR THE GROUP (A): 47.5778 5.8100 -45.2388 REMARK 3 T TENSOR REMARK 3 T11: -0.1673 T22: 0.2320 REMARK 3 T33: -0.2113 T12: -0.0730 REMARK 3 T13: -0.0564 T23: -0.1484 REMARK 3 L TENSOR REMARK 3 L11: 2.8264 L22: 0.1612 REMARK 3 L33: 3.2782 L12: -0.0790 REMARK 3 L13: 0.1103 L23: -1.3957 REMARK 3 S TENSOR REMARK 3 S11: 0.0176 S12: -0.1509 S13: 0.0292 REMARK 3 S21: 0.0616 S22: -0.0076 S23: 0.0432 REMARK 3 S31: 0.0267 S32: 0.0473 S33: -0.0100 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { A|2002 - A|2002 } REMARK 3 ORIGIN FOR THE GROUP (A): 5.3036 33.5433 -9.5529 REMARK 3 T TENSOR REMARK 3 T11: -0.0176 T22: 0.0061 REMARK 3 T33: -0.0015 T12: 0.0658 REMARK 3 T13: 0.0103 T23: -0.0175 REMARK 3 L TENSOR REMARK 3 L11: 0.0574 L22: 0.0037 REMARK 3 L33: 0.0000 L12: -0.5008 REMARK 3 L13: 0.1414 L23: 0.0997 REMARK 3 S TENSOR REMARK 3 S11: 0.0014 S12: 0.0138 S13: 0.0053 REMARK 3 S21: -0.0019 S22: -0.0026 S23: -0.0032 REMARK 3 S31: 0.0004 S32: -0.0014 S33: 0.0012 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 4IB4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-13. REMARK 100 THE DEPOSITION ID IS D_1000076531. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : AUG-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 17 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16041 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 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 (%) : 90.5 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.7000 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 (%) : 92.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.91000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3PBL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS/HCL PH 8.0, 100 MM REMARK 280 MAGNESIUM SULFATE AND 30% (V/V) PEG400, LIPID CUBIC PHASE (LCP) , REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.30350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.30350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.28550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.87500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.28550 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.87500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 85.30350 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.28550 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.87500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 85.30350 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.28550 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.87500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 26 REMARK 465 TYR A 27 REMARK 465 LYS A 28 REMARK 465 ASP A 29 REMARK 465 ASP A 30 REMARK 465 ASP A 31 REMARK 465 ASP A 32 REMARK 465 GLY A 33 REMARK 465 ALA A 34 REMARK 465 PRO A 35 REMARK 465 THR A 36 REMARK 465 GLU A 37 REMARK 465 SER A 38 REMARK 465 ILE A 39 REMARK 465 PRO A 40 REMARK 465 GLU A 41 REMARK 465 GLU A 42 REMARK 465 MET A 43 REMARK 465 LYS A 44 REMARK 465 GLN A 45 REMARK 465 ILE A 46 REMARK 465 VAL A 47 REMARK 465 ASP A 198 REMARK 465 VAL A 199 REMARK 465 ASP A 200 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 ALA A 401 REMARK 465 THR A 402 REMARK 465 LYS A 403 REMARK 465 SER A 404 REMARK 465 VAL A 405 REMARK 465 GLY A 406 REMARK 465 ARG A 407 REMARK 465 PRO A 408 REMARK 465 LEU A 409 REMARK 465 GLU A 410 REMARK 465 VAL A 411 REMARK 465 LEU A 412 REMARK 465 PHE A 413 REMARK 465 GLN A 414 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 53 CG CD CE NZ REMARK 470 LYS A 84 CE NZ REMARK 470 GLU A 118 CG CD OE1 OE2 REMARK 470 MET A 120 CG SD CE REMARK 470 VAL A 126 CG1 CG2 REMARK 470 LEU A 127 CG CD1 CD2 REMARK 470 ILE A 161 CG1 CG2 CD1 REMARK 470 GLN A 162 CG CD OE1 NE2 REMARK 470 ASN A 164 CG OD1 ND2 REMARK 470 GLN A 165 CG CD OE1 NE2 REMARK 470 TYR A 166 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 169 CZ NH1 NH2 REMARK 470 ILE A 195 CG1 CG2 CD1 REMARK 470 GLU A 196 CD OE1 OE2 REMARK 470 THR A 197 OG1 CG2 REMARK 470 ASN A 203 CG OD1 ND2 REMARK 470 ILE A 205 CG1 CG2 CD1 REMARK 470 GLU A 212 CG CD OE1 OE2 REMARK 470 LEU A1003 CG CD1 CD2 REMARK 470 ASP A1039 CG OD1 OD2 REMARK 470 GLN A1041 CG CD OE1 NE2 REMARK 470 LYS A1042 CD CE NZ REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A1073 CG OD1 OD2 REMARK 470 ASP A1074 CG OD1 OD2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 GLU A1092 CD OE1 OE2 REMARK 470 ILE A1102 CG1 CG2 CD1 REMARK 470 ARG A 321 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 324 CD CE NZ REMARK 470 ASP A 351 CG OD1 OD2 REMARK 470 THR A 357 OG1 CG2 REMARK 470 LYS A 385 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 64 -60.32 -125.48 REMARK 500 PHE A 117 -157.28 -108.20 REMARK 500 LYS A 159 78.00 -118.54 REMARK 500 ILE A 161 -156.61 -90.72 REMARK 500 PHE A 226 -53.18 -121.82 REMARK 500 ASN A 398 -64.92 -92.06 REMARK 500 TYR A 399 18.85 57.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 2004 REMARK 610 OLB A 2005 REMARK 610 OLB A 2006 REMARK 610 OLB A 2007 REMARK 610 OLA A 2009 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ERM A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLB A 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLB A 2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLB A 2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2008 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2009 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2010 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2011 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-4 RELATED DB: TARGETTRACK DBREF 4IB4 A 36 248 UNP P41595 5HT2B_HUMAN 36 248 DBREF 4IB4 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4IB4 A 314 405 UNP P41595 5HT2B_HUMAN 314 405 SEQADV 4IB4 ASP A 26 UNP P41595 EXPRESSION TAG SEQADV 4IB4 TYR A 27 UNP P41595 EXPRESSION TAG SEQADV 4IB4 LYS A 28 UNP P41595 EXPRESSION TAG SEQADV 4IB4 ASP A 29 UNP P41595 EXPRESSION TAG SEQADV 4IB4 ASP A 30 UNP P41595 EXPRESSION TAG SEQADV 4IB4 ASP A 31 UNP P41595 EXPRESSION TAG SEQADV 4IB4 ASP A 32 UNP P41595 EXPRESSION TAG SEQADV 4IB4 GLY A 33 UNP P41595 EXPRESSION TAG SEQADV 4IB4 ALA A 34 UNP P41595 EXPRESSION TAG SEQADV 4IB4 PRO A 35 UNP P41595 EXPRESSION TAG SEQADV 4IB4 TRP A 144 UNP P41595 MET 144 ENGINEERED MUTATION SEQADV 4IB4 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4IB4 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4IB4 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 4IB4 GLY A 406 UNP P41595 EXPRESSION TAG SEQADV 4IB4 ARG A 407 UNP P41595 EXPRESSION TAG SEQADV 4IB4 PRO A 408 UNP P41595 EXPRESSION TAG SEQADV 4IB4 LEU A 409 UNP P41595 EXPRESSION TAG SEQADV 4IB4 GLU A 410 UNP P41595 EXPRESSION TAG SEQADV 4IB4 VAL A 411 UNP P41595 EXPRESSION TAG SEQADV 4IB4 LEU A 412 UNP P41595 EXPRESSION TAG SEQADV 4IB4 PHE A 413 UNP P41595 EXPRESSION TAG SEQADV 4IB4 GLN A 414 UNP P41595 EXPRESSION TAG SEQRES 1 A 430 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO THR GLU SER SEQRES 2 A 430 ILE PRO GLU GLU MET LYS GLN ILE VAL GLU GLU GLN GLY SEQRES 3 A 430 ASN LYS LEU HIS TRP ALA ALA LEU LEU ILE LEU MET VAL SEQRES 4 A 430 ILE ILE PRO THR ILE GLY GLY ASN THR LEU VAL ILE LEU SEQRES 5 A 430 ALA VAL SER LEU GLU LYS LYS LEU GLN TYR ALA THR ASN SEQRES 6 A 430 TYR PHE LEU MET SER LEU ALA VAL ALA ASP LEU LEU VAL SEQRES 7 A 430 GLY LEU PHE VAL MET PRO ILE ALA LEU LEU THR ILE MET SEQRES 8 A 430 PHE GLU ALA MET TRP PRO LEU PRO LEU VAL LEU CYS PRO SEQRES 9 A 430 ALA TRP LEU PHE LEU ASP VAL LEU PHE SER THR ALA SER SEQRES 10 A 430 ILE TRP HIS LEU CYS ALA ILE SER VAL ASP ARG TYR ILE SEQRES 11 A 430 ALA ILE LYS LYS PRO ILE GLN ALA ASN GLN TYR ASN SER SEQRES 12 A 430 ARG ALA THR ALA PHE ILE LYS ILE THR VAL VAL TRP LEU SEQRES 13 A 430 ILE SER ILE GLY ILE ALA ILE PRO VAL PRO ILE LYS GLY SEQRES 14 A 430 ILE GLU THR ASP VAL ASP ASN PRO ASN ASN ILE THR CYS SEQRES 15 A 430 VAL LEU THR LYS GLU ARG PHE GLY ASP PHE MET LEU PHE SEQRES 16 A 430 GLY SER LEU ALA ALA PHE PHE THR PRO LEU ALA ILE MET SEQRES 17 A 430 ILE VAL THR TYR PHE LEU THR ILE HIS ALA LEU GLN LYS SEQRES 18 A 430 LYS ALA ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN SEQRES 19 A 430 ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA SEQRES 20 A 430 GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA SEQRES 21 A 430 LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP SEQRES 22 A 430 LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS SEQRES 23 A 430 GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU SEQRES 24 A 430 LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA SEQRES 25 A 430 ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE SEQRES 26 A 430 GLN LYS TYR LEU GLN THR ILE SER ASN GLU GLN ARG ALA SEQRES 27 A 430 SER LYS VAL LEU GLY ILE VAL PHE PHE LEU PHE LEU LEU SEQRES 28 A 430 MET TRP CYS PRO PHE PHE ILE THR ASN ILE THR LEU VAL SEQRES 29 A 430 LEU CYS ASP SER CYS ASN GLN THR THR LEU GLN MET LEU SEQRES 30 A 430 LEU GLU ILE PHE VAL TRP ILE GLY TYR VAL SER SER GLY SEQRES 31 A 430 VAL ASN PRO LEU VAL TYR THR LEU PHE ASN LYS THR PHE SEQRES 32 A 430 ARG ASP ALA PHE GLY ARG TYR ILE THR CYS ASN TYR ARG SEQRES 33 A 430 ALA THR LYS SER VAL GLY ARG PRO LEU GLU VAL LEU PHE SEQRES 34 A 430 GLN HET ERM A2001 43 HET PLM A2002 17 HET CLR A2003 28 HET OLC A2004 19 HET OLB A2005 15 HET OLB A2006 16 HET OLB A2007 16 HET OLA A2008 20 HET OLA A2009 17 HET PEG A2010 7 HET PEG A2011 7 HETNAM ERM ERGOTAMINE HETNAM PLM PALMITIC ACID HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 ERM C33 H35 N5 O5 FORMUL 3 PLM C16 H32 O2 FORMUL 4 CLR C27 H46 O FORMUL 5 OLC C21 H40 O4 FORMUL 6 OLB 3(C21 H40 O4) FORMUL 9 OLA 2(C18 H34 O2) FORMUL 11 PEG 2(C4 H10 O3) FORMUL 13 HOH *9(H2 O) HELIX 1 1 LYS A 53 VAL A 64 1 12 HELIX 2 2 VAL A 64 GLU A 82 1 19 HELIX 3 3 LYS A 83 GLN A 86 5 4 HELIX 4 4 TYR A 87 VAL A 107 1 21 HELIX 5 5 VAL A 107 LEU A 112 1 6 HELIX 6 6 LEU A 112 PHE A 117 1 6 HELIX 7 7 VAL A 126 LYS A 159 1 34 HELIX 8 8 ASN A 164 ILE A 188 1 25 HELIX 9 9 ILE A 188 GLY A 194 1 7 HELIX 10 10 THR A 210 PHE A 226 1 17 HELIX 11 11 PHE A 226 ALA A 1020 1 43 HELIX 12 12 ASN A 1022 ALA A 1037 1 16 HELIX 13 13 ALA A 1037 LYS A 1042 1 6 HELIX 14 14 ASP A 1060 GLY A 1082 1 23 HELIX 15 15 LYS A 1083 GLN A 1093 1 11 HELIX 16 16 LEU A 1094 CYS A 350 1 50 HELIX 17 17 ASN A 354 LEU A 382 1 29 HELIX 18 18 ASN A 384 ILE A 395 1 12 SSBOND 1 CYS A 128 CYS A 207 1555 1555 2.04 SSBOND 2 CYS A 350 CYS A 353 1555 1555 2.04 LINK SG CYS A 397 C1 PLM A2002 1555 1555 1.66 SITE 1 AC1 16 ASP A 135 VAL A 136 SER A 139 THR A 140 SITE 2 AC1 16 VAL A 208 LEU A 209 THR A 210 LYS A 211 SITE 3 AC1 16 MET A 218 ALA A 225 TRP A 337 PHE A 340 SITE 4 AC1 16 ASN A 344 LEU A 347 GLN A 359 HOH A2020 SITE 1 AC2 5 ILE A 66 THR A 343 ILE A 395 THR A 396 SITE 2 AC2 5 CYS A 397 SITE 1 AC3 4 GLY A 70 THR A 73 TYR A 394 TYR A 399 SITE 1 AC4 5 SER A 150 MET A 233 THR A 240 LEU A 326 SITE 2 AC4 5 HOH A2017 SITE 1 AC5 2 PRO A 191 ILE A 192 SITE 1 AC6 3 MET A 360 TYR A 399 OLB A2007 SITE 1 AC7 3 LEU A 81 TYR A 399 OLB A2006 SITE 1 AC8 1 TRP A 56 SITE 1 AC9 4 GLY A 185 LYS A 193 ASP A 216 PHE A 217 SITE 1 BC1 2 TYR A 380 ASN A 384 SITE 1 BC2 1 ILE A 182 CRYST1 60.571 119.750 170.607 90.00 90.00 90.00 C 2 2 21 8 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 0.016510 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008351 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005861 0.00000 ATOM 1 N GLU A 48 18.652 38.221 29.331 1.00118.89 N ANISOU 1 N GLU A 48 17397 14692 13084 -1091 1928 -4228 N ATOM 2 CA GLU A 48 18.815 38.640 27.940 1.00117.19 C ANISOU 2 CA GLU A 48 17184 14207 13137 -1002 1902 -4117 C ATOM 3 C GLU A 48 17.736 38.042 27.032 1.00118.59 C ANISOU 3 C GLU A 48 17253 14346 13460 -792 1924 -3909 C ATOM 4 O GLU A 48 17.244 36.939 27.287 1.00117.10 O ANISOU 4 O GLU A 48 16962 14371 13160 -766 1896 -3778 O ATOM 5 CB GLU A 48 20.213 38.268 27.406 1.00117.09 C ANISOU 5 CB GLU A 48 17149 14215 13124 -1144 1723 -4001 C ATOM 6 CG GLU A 48 21.325 39.201 27.857 1.00128.37 C ANISOU 6 CG GLU A 48 18683 15583 14509 -1341 1710 -4219 C ATOM 7 CD GLU A 48 21.224 40.622 27.337 1.00146.95 C ANISOU 7 CD GLU A 48 21169 17589 17078 -1314 1833 -4362 C ATOM 8 OE1 GLU A 48 21.583 40.851 26.160 1.00142.01 O ANISOU 8 OE1 GLU A 48 20547 16767 16642 -1282 1795 -4232 O ATOM 9 OE2 GLU A 48 20.777 41.506 28.104 1.00137.88 O ANISOU 9 OE2 GLU A 48 20130 16355 15903 -1322 1973 -4604 O ATOM 10 N GLU A 49 17.379 38.784 25.968 1.00114.26 N ANISOU 10 N GLU A 49 16734 13523 13155 -649 1973 -3879 N ATOM 11 CA GLU A 49 16.389 38.389 24.967 1.00112.16 C ANISOU 11 CA GLU A 49 16367 13203 13048 -440 1985 -3698 C ATOM 12 C GLU A 49 16.995 38.506 23.562 1.00112.59 C ANISOU 12 C GLU A 49 16430 13068 13281 -409 1882 -3524 C ATOM 13 O GLU A 49 17.603 39.527 23.233 1.00113.31 O ANISOU 13 O GLU A 49 16646 12933 13474 -452 1900 -3605 O ATOM 14 CB GLU A 49 15.109 39.245 25.103 1.00115.50 C ANISOU 14 CB GLU A 49 16812 13492 13579 -245 2161 -3840 C ATOM 15 CG GLU A 49 14.021 38.973 24.068 1.00124.94 C ANISOU 15 CG GLU A 49 17888 14641 14942 -12 2173 -3679 C ATOM 16 CD GLU A 49 13.420 37.578 24.036 1.00141.94 C ANISOU 16 CD GLU A 49 19864 17057 17007 3 2123 -3512 C ATOM 17 OE1 GLU A 49 13.399 36.971 22.940 1.00129.88 O ANISOU 17 OE1 GLU A 49 18253 15517 15580 69 2022 -3302 O ATOM 18 OE2 GLU A 49 12.959 37.098 25.096 1.00137.41 O ANISOU 18 OE2 GLU A 49 19246 16701 16264 -58 2191 -3595 O ATOM 19 N GLN A 50 16.826 37.450 22.747 1.00105.14 N ANISOU 19 N GLN A 50 15361 12217 12369 -344 1784 -3289 N ATOM 20 CA GLN A 50 17.318 37.381 21.367 1.00102.41 C ANISOU 20 CA GLN A 50 15006 11731 12173 -305 1685 -3104 C ATOM 21 C GLN A 50 16.567 38.375 20.454 1.00104.35 C ANISOU 21 C GLN A 50 15308 11709 12634 -102 1768 -3101 C ATOM 22 O GLN A 50 17.210 39.110 19.702 1.00104.19 O ANISOU 22 O GLN A 50 15387 11469 12731 -115 1748 -3070 O ATOM 23 CB GLN A 50 17.248 35.941 20.799 1.00101.45 C ANISOU 23 CB GLN A 50 14741 11792 12013 -289 1566 -2872 C ATOM 24 CG GLN A 50 15.941 35.171 21.052 1.00117.61 C ANISOU 24 CG GLN A 50 16665 13997 14024 -171 1618 -2826 C ATOM 25 CD GLN A 50 15.934 34.446 22.377 1.00137.98 C ANISOU 25 CD GLN A 50 19218 16826 16382 -294 1635 -2887 C ATOM 26 OE1 GLN A 50 16.748 33.551 22.636 1.00133.18 O ANISOU 26 OE1 GLN A 50 18597 16364 15642 -425 1526 -2798 O ATOM 27 NE2 GLN A 50 15.000 34.804 23.242 1.00131.09 N ANISOU 27 NE2 GLN A 50 18337 16011 15459 -241 1774 -3036 N ATOM 28 N GLY A 51 15.236 38.412 20.567 1.00 99.08 N ANISOU 28 N GLY A 51 14574 11064 12006 82 1862 -3136 N ATOM 29 CA GLY A 51 14.377 39.296 19.787 1.00 98.47 C ANISOU 29 CA GLY A 51 14531 10763 12119 316 1936 -3133 C ATOM 30 C GLY A 51 13.493 38.556 18.804 1.00 97.31 C ANISOU 30 C GLY A 51 14228 10692 12052 492 1877 -2938 C ATOM 31 O GLY A 51 12.897 37.531 19.156 1.00 96.44 O ANISOU 31 O GLY A 51 13964 10827 11851 485 1862 -2892 O ATOM 32 N ASN A 52 13.404 39.079 17.561 1.00 89.85 N ANISOU 32 N ASN A 52 13331 9538 11272 644 1847 -2825 N ATOM 33 CA ASN A 52 12.599 38.513 16.474 1.00 86.42 C ANISOU 33 CA ASN A 52 12760 9156 10922 823 1779 -2644 C ATOM 34 C ASN A 52 13.469 38.250 15.250 1.00 84.37 C ANISOU 34 C ASN A 52 12543 8803 10713 774 1652 -2448 C ATOM 35 O ASN A 52 14.307 39.085 14.894 1.00 84.37 O ANISOU 35 O ASN A 52 12711 8576 10770 722 1660 -2457 O ATOM 36 CB ASN A 52 11.439 39.447 16.120 1.00 87.81 C ANISOU 36 CB ASN A 52 12940 9186 11239 1107 1867 -2697 C ATOM 37 CG ASN A 52 10.348 38.851 15.256 1.00106.72 C ANISOU 37 CG ASN A 52 15150 11700 13699 1309 1810 -2559 C ATOM 38 OD1 ASN A 52 10.422 37.713 14.771 1.00101.44 O ANISOU 38 OD1 ASN A 52 14349 11215 12978 1236 1705 -2415 O ATOM 39 ND2 ASN A 52 9.296 39.624 15.043 1.00 98.99 N ANISOU 39 ND2 ASN A 52 14156 10620 12835 1574 1877 -2609 N ATOM 40 N LYS A 53 13.255 37.089 14.601 1.00 75.68 N ANISOU 40 N LYS A 53 11292 7875 9587 782 1546 -2280 N ATOM 41 CA LYS A 53 14.031 36.656 13.442 1.00 71.97 C ANISOU 41 CA LYS A 53 10840 7359 9147 734 1426 -2094 C ATOM 42 C LYS A 53 13.128 36.276 12.248 1.00 71.15 C ANISOU 42 C LYS A 53 10622 7287 9123 931 1361 -1939 C ATOM 43 O LYS A 53 13.413 35.311 11.537 1.00 68.36 O ANISOU 43 O LYS A 53 10192 7041 8742 877 1256 -1792 O ATOM 44 CB LYS A 53 14.947 35.483 13.842 1.00 72.43 C ANISOU 44 CB LYS A 53 10843 7607 9071 507 1342 -2044 C ATOM 45 N LEU A 54 12.068 37.066 12.003 1.00 67.18 N ANISOU 45 N LEU A 54 10114 6690 8720 1165 1422 -1978 N ATOM 46 CA LEU A 54 11.158 36.839 10.876 1.00 65.88 C ANISOU 46 CA LEU A 54 9838 6564 8630 1376 1356 -1848 C ATOM 47 C LEU A 54 11.813 37.270 9.551 1.00 68.67 C ANISOU 47 C LEU A 54 10324 6715 9051 1425 1282 -1691 C ATOM 48 O LEU A 54 11.562 36.645 8.520 1.00 66.93 O ANISOU 48 O LEU A 54 10015 6575 8841 1499 1181 -1542 O ATOM 49 CB LEU A 54 9.816 37.571 11.086 1.00 67.79 C ANISOU 49 CB LEU A 54 10017 6790 8951 1630 1441 -1951 C ATOM 50 CG LEU A 54 8.669 37.206 10.129 1.00 71.60 C ANISOU 50 CG LEU A 54 10325 7388 9493 1857 1370 -1850 C ATOM 51 CD1 LEU A 54 8.114 35.817 10.416 1.00 70.23 C ANISOU 51 CD1 LEU A 54 9911 7534 9239 1767 1336 -1847 C ATOM 52 CD2 LEU A 54 7.570 38.228 10.198 1.00 75.78 C ANISOU 52 CD2 LEU A 54 10849 7819 10124 2146 1448 -1940 C ATOM 53 N HIS A 55 12.667 38.315 9.586 1.00 66.24 N ANISOU 53 N HIS A 55 10234 6153 8781 1368 1337 -1728 N ATOM 54 CA HIS A 55 13.386 38.826 8.413 1.00 66.37 C ANISOU 54 CA HIS A 55 10409 5956 8854 1383 1295 -1587 C ATOM 55 C HIS A 55 14.306 37.760 7.789 1.00 69.16 C ANISOU 55 C HIS A 55 10710 6432 9136 1204 1185 -1449 C ATOM 56 O HIS A 55 14.505 37.789 6.576 1.00 68.49 O ANISOU 56 O HIS A 55 10675 6268 9082 1266 1122 -1294 O ATOM 57 CB HIS A 55 14.187 40.090 8.754 1.00 68.73 C ANISOU 57 CB HIS A 55 10950 5966 9199 1304 1399 -1683 C ATOM 58 CG HIS A 55 15.083 39.951 9.943 1.00 71.63 C ANISOU 58 CG HIS A 55 11337 6394 9484 1038 1444 -1834 C ATOM 59 ND1 HIS A 55 14.582 39.994 11.231 1.00 74.18 N ANISOU 59 ND1 HIS A 55 11606 6815 9766 1025 1521 -2018 N ATOM 60 CD2 HIS A 55 16.425 39.796 9.999 1.00 72.38 C ANISOU 60 CD2 HIS A 55 11497 6478 9528 788 1419 -1827 C ATOM 61 CE1 HIS A 55 15.628 39.852 12.027 1.00 73.10 C ANISOU 61 CE1 HIS A 55 11508 6724 9543 770 1530 -2112 C ATOM 62 NE2 HIS A 55 16.759 39.732 11.331 1.00 72.39 N ANISOU 62 NE2 HIS A 55 11481 6575 9449 624 1467 -2005 N ATOM 63 N TRP A 56 14.832 36.809 8.598 1.00 65.32 N ANISOU 63 N TRP A 56 10126 6142 8551 997 1160 -1501 N ATOM 64 CA TRP A 56 15.671 35.723 8.081 1.00 63.57 C ANISOU 64 CA TRP A 56 9844 6048 8263 844 1058 -1382 C ATOM 65 C TRP A 56 14.795 34.709 7.350 1.00 67.10 C ANISOU 65 C TRP A 56 10122 6674 8698 958 969 -1265 C ATOM 66 O TRP A 56 15.164 34.259 6.262 1.00 65.68 O ANISOU 66 O TRP A 56 9938 6502 8516 953 886 -1125 O ATOM 67 CB TRP A 56 16.506 35.041 9.186 1.00 61.53 C ANISOU 67 CB TRP A 56 9546 5934 7899 612 1055 -1470 C ATOM 68 CG TRP A 56 17.427 35.960 9.942 1.00 64.01 C ANISOU 68 CG TRP A 56 10005 6108 8207 470 1130 -1602 C ATOM 69 CD1 TRP A 56 17.402 36.220 11.281 1.00 67.90 C ANISOU 69 CD1 TRP A 56 10512 6643 8645 392 1202 -1776 C ATOM 70 CD2 TRP A 56 18.490 36.762 9.397 1.00 64.38 C ANISOU 70 CD2 TRP A 56 10206 5955 8299 376 1148 -1582 C ATOM 71 NE1 TRP A 56 18.376 37.139 11.605 1.00 68.61 N ANISOU 71 NE1 TRP A 56 10749 6573 8745 255 1255 -1875 N ATOM 72 CE2 TRP A 56 19.058 37.489 10.469 1.00 69.69 C ANISOU 72 CE2 TRP A 56 10973 6557 8949 235 1227 -1759 C ATOM 73 CE3 TRP A 56 19.009 36.949 8.104 1.00 65.32 C ANISOU 73 CE3 TRP A 56 10396 5953 8471 386 1112 -1437 C ATOM 74 CZ2 TRP A 56 20.120 38.382 10.288 1.00 69.95 C ANISOU 74 CZ2 TRP A 56 11159 6400 9018 94 1273 -1800 C ATOM 75 CZ3 TRP A 56 20.056 37.839 7.926 1.00 67.81 C ANISOU 75 CZ3 TRP A 56 10868 6078 8819 250 1165 -1467 C ATOM 76 CH2 TRP A 56 20.603 38.541 9.009 1.00 69.79 C ANISOU 76 CH2 TRP A 56 11202 6260 9057 100 1245 -1650 C ATOM 77 N ALA A 57 13.615 34.392 7.927 1.00 64.21 N ANISOU 77 N ALA A 57 9617 6455 8326 1055 993 -1335 N ATOM 78 CA ALA A 57 12.631 33.462 7.365 1.00 63.24 C ANISOU 78 CA ALA A 57 9313 6520 8195 1152 923 -1260 C ATOM 79 C ALA A 57 12.131 33.923 5.991 1.00 67.18 C ANISOU 79 C ALA A 57 9826 6930 8768 1360 865 -1141 C ATOM 80 O ALA A 57 12.026 33.103 5.084 1.00 65.94 O ANISOU 80 O ALA A 57 9583 6882 8588 1369 768 -1027 O ATOM 81 CB ALA A 57 11.459 33.311 8.318 1.00 64.94 C ANISOU 81 CB ALA A 57 9389 6886 8400 1214 991 -1384 C ATOM 82 N ALA A 58 11.860 35.229 5.831 1.00 64.93 N ANISOU 82 N ALA A 58 9663 6443 8565 1528 923 -1167 N ATOM 83 CA ALA A 58 11.393 35.801 4.570 1.00 65.70 C ANISOU 83 CA ALA A 58 9806 6434 8723 1751 870 -1047 C ATOM 84 C ALA A 58 12.501 35.789 3.509 1.00 68.48 C ANISOU 84 C ALA A 58 10299 6665 9055 1663 811 -898 C ATOM 85 O ALA A 58 12.226 35.516 2.337 1.00 67.79 O ANISOU 85 O ALA A 58 10183 6612 8961 1774 721 -763 O ATOM 86 CB ALA A 58 10.894 37.217 4.795 1.00 68.94 C ANISOU 86 CB ALA A 58 10340 6631 9223 1950 961 -1118 C ATOM 87 N LEU A 59 13.751 36.062 3.931 1.00 64.49 N ANISOU 87 N LEU A 59 9935 6036 8533 1457 864 -930 N ATOM 88 CA LEU A 59 14.936 36.078 3.074 1.00 63.65 C ANISOU 88 CA LEU A 59 9956 5823 8405 1335 833 -814 C ATOM 89 C LEU A 59 15.234 34.685 2.502 1.00 64.77 C ANISOU 89 C LEU A 59 9961 6178 8472 1234 727 -723 C ATOM 90 O LEU A 59 15.628 34.582 1.341 1.00 64.40 O ANISOU 90 O LEU A 59 9966 6094 8409 1249 671 -588 O ATOM 91 CB LEU A 59 16.147 36.585 3.876 1.00 64.08 C ANISOU 91 CB LEU A 59 10145 5747 8457 1118 919 -911 C ATOM 92 CG LEU A 59 17.304 37.160 3.060 1.00 69.54 C ANISOU 92 CG LEU A 59 11017 6245 9159 1015 939 -823 C ATOM 93 CD1 LEU A 59 17.735 38.505 3.618 1.00 71.97 C ANISOU 93 CD1 LEU A 59 11524 6294 9528 962 1063 -927 C ATOM 94 CD2 LEU A 59 18.480 36.188 2.996 1.00 69.63 C ANISOU 94 CD2 LEU A 59 10960 6397 9097 784 887 -794 C ATOM 95 N LEU A 60 15.049 33.624 3.319 1.00 59.27 N ANISOU 95 N LEU A 60 9104 5693 7723 1131 706 -795 N ATOM 96 CA LEU A 60 15.315 32.236 2.931 1.00 56.72 C ANISOU 96 CA LEU A 60 8660 5560 7332 1028 616 -727 C ATOM 97 C LEU A 60 14.259 31.687 1.966 1.00 61.58 C ANISOU 97 C LEU A 60 9153 6299 7946 1184 532 -644 C ATOM 98 O LEU A 60 14.591 30.818 1.167 1.00 60.43 O ANISOU 98 O LEU A 60 8963 6243 7754 1128 455 -557 O ATOM 99 CB LEU A 60 15.455 31.323 4.161 1.00 55.26 C ANISOU 99 CB LEU A 60 8372 5536 7087 872 630 -823 C ATOM 100 CG LEU A 60 16.694 31.579 5.037 1.00 58.85 C ANISOU 100 CG LEU A 60 8921 5928 7512 688 681 -899 C ATOM 101 CD1 LEU A 60 16.549 30.938 6.401 1.00 58.34 C ANISOU 101 CD1 LEU A 60 8771 6011 7382 589 707 -1006 C ATOM 102 CD2 LEU A 60 17.986 31.163 4.342 1.00 58.74 C ANISOU 102 CD2 LEU A 60 8952 5899 7466 557 629 -813 C ATOM 103 N ILE A 61 13.011 32.192 2.013 1.00 60.17 N ANISOU 103 N ILE A 61 8914 6132 7816 1380 544 -678 N ATOM 104 CA ILE A 61 11.941 31.783 1.092 1.00 60.73 C ANISOU 104 CA ILE A 61 8852 6338 7885 1542 456 -614 C ATOM 105 C ILE A 61 12.266 32.303 -0.324 1.00 67.23 C ANISOU 105 C ILE A 61 9801 7038 8707 1650 395 -466 C ATOM 106 O ILE A 61 12.224 31.533 -1.283 1.00 65.90 O ANISOU 106 O ILE A 61 9569 6983 8487 1646 302 -380 O ATOM 107 CB ILE A 61 10.545 32.271 1.587 1.00 65.29 C ANISOU 107 CB ILE A 61 9311 6980 8517 1733 489 -706 C ATOM 108 CG1 ILE A 61 10.089 31.478 2.825 1.00 65.09 C ANISOU 108 CG1 ILE A 61 9129 7136 8467 1610 541 -836 C ATOM 109 CG2 ILE A 61 9.487 32.196 0.474 1.00 66.79 C ANISOU 109 CG2 ILE A 61 9383 7280 8713 1944 389 -632 C ATOM 110 CD1 ILE A 61 9.022 32.178 3.718 1.00 74.14 C ANISOU 110 CD1 ILE A 61 10194 8310 9667 1752 628 -969 C ATOM 111 N LEU A 62 12.619 33.596 -0.437 1.00 67.16 N ANISOU 111 N LEU A 62 9982 6789 8745 1733 457 -441 N ATOM 112 CA LEU A 62 12.917 34.264 -1.702 1.00 68.82 C ANISOU 112 CA LEU A 62 10351 6848 8950 1840 423 -294 C ATOM 113 C LEU A 62 14.239 33.839 -2.365 1.00 72.68 C ANISOU 113 C LEU A 62 10938 7298 9379 1647 409 -205 C ATOM 114 O LEU A 62 14.280 33.694 -3.589 1.00 72.22 O ANISOU 114 O LEU A 62 10917 7252 9272 1711 340 -76 O ATOM 115 CB LEU A 62 12.946 35.782 -1.484 1.00 71.10 C ANISOU 115 CB LEU A 62 10839 6861 9313 1963 517 -303 C ATOM 116 CG LEU A 62 11.644 36.520 -1.762 1.00 78.56 C ANISOU 116 CG LEU A 62 11759 7783 10308 2275 493 -288 C ATOM 117 CD1 LEU A 62 11.531 37.760 -0.895 1.00 80.71 C ANISOU 117 CD1 LEU A 62 12165 7832 10670 2358 616 -387 C ATOM 118 CD2 LEU A 62 11.521 36.890 -3.241 1.00 82.79 C ANISOU 118 CD2 LEU A 62 12403 8247 10807 2450 411 -104 C ATOM 119 N MET A 63 15.317 33.693 -1.582 1.00 69.06 N ANISOU 119 N MET A 63 10520 6801 8918 1423 476 -277 N ATOM 120 CA MET A 63 16.643 33.416 -2.130 1.00 67.96 C ANISOU 120 CA MET A 63 10466 6621 8733 1244 478 -210 C ATOM 121 C MET A 63 17.069 31.953 -2.066 1.00 66.64 C ANISOU 121 C MET A 63 10149 6667 8502 1093 415 -222 C ATOM 122 O MET A 63 18.100 31.623 -2.661 1.00 65.37 O ANISOU 122 O MET A 63 10035 6502 8299 976 405 -159 O ATOM 123 CB MET A 63 17.693 34.285 -1.420 1.00 71.46 C ANISOU 123 CB MET A 63 11059 6878 9215 1092 590 -278 C ATOM 124 CG MET A 63 17.720 35.721 -1.915 1.00 78.24 C ANISOU 124 CG MET A 63 12139 7467 10121 1186 661 -214 C ATOM 125 SD MET A 63 18.605 36.863 -0.810 1.00 84.95 S ANISOU 125 SD MET A 63 13155 8086 11036 1024 807 -346 S ATOM 126 CE MET A 63 20.310 36.217 -0.946 1.00 80.20 C ANISOU 126 CE MET A 63 12538 7557 10377 719 814 -345 C ATOM 127 N VAL A 64 16.316 31.074 -1.367 1.00 60.28 N ANISOU 127 N VAL A 64 9173 6040 7689 1090 382 -302 N ATOM 128 CA VAL A 64 16.708 29.658 -1.272 1.00 57.11 C ANISOU 128 CA VAL A 64 8654 5813 7230 951 329 -310 C ATOM 129 C VAL A 64 15.568 28.725 -1.730 1.00 58.34 C ANISOU 129 C VAL A 64 8654 6151 7360 1041 245 -292 C ATOM 130 O VAL A 64 15.774 27.973 -2.676 1.00 56.89 O ANISOU 130 O VAL A 64 8446 6042 7128 1019 177 -222 O ATOM 131 CB VAL A 64 17.234 29.249 0.141 1.00 59.85 C ANISOU 131 CB VAL A 64 8962 6209 7571 791 376 -421 C ATOM 132 CG1 VAL A 64 17.714 27.800 0.166 1.00 58.04 C ANISOU 132 CG1 VAL A 64 8646 6127 7281 662 321 -407 C ATOM 133 CG2 VAL A 64 18.342 30.178 0.622 1.00 60.10 C ANISOU 133 CG2 VAL A 64 9130 6081 7626 692 455 -463 C ATOM 134 N ILE A 65 14.395 28.767 -1.067 1.00 54.46 N ANISOU 134 N ILE A 65 8054 5738 6900 1131 254 -368 N ATOM 135 CA ILE A 65 13.265 27.865 -1.321 1.00 54.19 C ANISOU 135 CA ILE A 65 7846 5898 6847 1186 187 -382 C ATOM 136 C ILE A 65 12.653 28.077 -2.722 1.00 60.25 C ANISOU 136 C ILE A 65 8599 6695 7598 1352 98 -289 C ATOM 137 O ILE A 65 12.504 27.088 -3.448 1.00 59.62 O ANISOU 137 O ILE A 65 8437 6749 7467 1314 21 -258 O ATOM 138 CB ILE A 65 12.209 27.932 -0.181 1.00 57.84 C ANISOU 138 CB ILE A 65 8186 6444 7346 1228 239 -499 C ATOM 139 CG1 ILE A 65 12.875 27.525 1.167 1.00 56.93 C ANISOU 139 CG1 ILE A 65 8087 6333 7213 1043 313 -580 C ATOM 140 CG2 ILE A 65 10.998 27.027 -0.479 1.00 58.48 C ANISOU 140 CG2 ILE A 65 8069 6737 7413 1274 177 -523 C ATOM 141 CD1 ILE A 65 12.167 27.892 2.407 1.00 61.37 C ANISOU 141 CD1 ILE A 65 8600 6914 7803 1068 399 -697 C ATOM 142 N ILE A 66 12.322 29.333 -3.109 1.00 58.56 N ANISOU 142 N ILE A 66 8475 6356 7421 1536 108 -245 N ATOM 143 CA ILE A 66 11.764 29.641 -4.432 1.00 59.24 C ANISOU 143 CA ILE A 66 8566 6466 7476 1717 17 -143 C ATOM 144 C ILE A 66 12.779 29.217 -5.530 1.00 61.24 C ANISOU 144 C ILE A 66 8923 6692 7652 1623 -27 -34 C ATOM 145 O ILE A 66 12.374 28.421 -6.381 1.00 60.57 O ANISOU 145 O ILE A 66 8745 6765 7506 1642 -121 -3 O ATOM 146 CB ILE A 66 11.291 31.119 -4.566 1.00 64.92 C ANISOU 146 CB ILE A 66 9393 7025 8249 1947 43 -105 C ATOM 147 CG1 ILE A 66 10.002 31.341 -3.744 1.00 66.67 C ANISOU 147 CG1 ILE A 66 9453 7345 8535 2084 60 -218 C ATOM 148 CG2 ILE A 66 11.072 31.525 -6.046 1.00 67.22 C ANISOU 148 CG2 ILE A 66 9757 7300 8482 2124 -52 40 C ATOM 149 CD1 ILE A 66 9.758 32.751 -3.296 1.00 74.77 C ANISOU 149 CD1 ILE A 66 10598 8172 9639 2257 138 -237 C ATOM 150 N PRO A 67 14.084 29.627 -5.507 1.00 57.21 N ANISOU 150 N PRO A 67 8585 6012 7141 1504 43 7 N ATOM 151 CA PRO A 67 15.016 29.169 -6.562 1.00 56.37 C ANISOU 151 CA PRO A 67 8555 5907 6958 1415 12 99 C ATOM 152 C PRO A 67 15.186 27.649 -6.628 1.00 58.99 C ANISOU 152 C PRO A 67 8754 6418 7240 1274 -39 57 C ATOM 153 O PRO A 67 15.311 27.120 -7.734 1.00 59.06 O ANISOU 153 O PRO A 67 8767 6497 7174 1273 -102 121 O ATOM 154 CB PRO A 67 16.337 29.845 -6.191 1.00 57.90 C ANISOU 154 CB PRO A 67 8915 5907 7177 1287 116 111 C ATOM 155 CG PRO A 67 15.934 31.037 -5.401 1.00 63.63 C ANISOU 155 CG PRO A 67 9710 6482 7984 1378 187 67 C ATOM 156 CD PRO A 67 14.763 30.572 -4.596 1.00 58.98 C ANISOU 156 CD PRO A 67 8940 6043 7429 1444 156 -35 C ATOM 157 N THR A 68 15.154 26.949 -5.469 1.00 54.44 N ANISOU 157 N THR A 68 8073 5912 6699 1161 -10 -49 N ATOM 158 CA THR A 68 15.265 25.487 -5.389 1.00 52.89 C ANISOU 158 CA THR A 68 7768 5861 6466 1029 -46 -92 C ATOM 159 C THR A 68 14.106 24.823 -6.148 1.00 57.63 C ANISOU 159 C THR A 68 8238 6630 7028 1109 -141 -94 C ATOM 160 O THR A 68 14.364 24.023 -7.048 1.00 57.35 O ANISOU 160 O THR A 68 8195 6666 6930 1062 -196 -64 O ATOM 161 CB THR A 68 15.323 25.020 -3.920 1.00 59.92 C ANISOU 161 CB THR A 68 8597 6776 7395 913 11 -191 C ATOM 162 OG1 THR A 68 16.507 25.543 -3.317 1.00 60.24 O ANISOU 162 OG1 THR A 68 8750 6685 7452 824 82 -195 O ATOM 163 CG2 THR A 68 15.307 23.494 -3.776 1.00 55.98 C ANISOU 163 CG2 THR A 68 8002 6408 6860 790 -21 -228 C ATOM 164 N ILE A 69 12.848 25.168 -5.801 1.00 54.65 N ANISOU 164 N ILE A 69 7751 6326 6688 1229 -158 -142 N ATOM 165 CA ILE A 69 11.651 24.596 -6.423 1.00 55.35 C ANISOU 165 CA ILE A 69 7682 6603 6747 1303 -250 -166 C ATOM 166 C ILE A 69 11.594 24.991 -7.914 1.00 60.96 C ANISOU 166 C ILE A 69 8452 7323 7386 1436 -339 -63 C ATOM 167 O ILE A 69 11.292 24.140 -8.753 1.00 60.97 O ANISOU 167 O ILE A 69 8379 7466 7319 1410 -422 -65 O ATOM 168 CB ILE A 69 10.357 24.985 -5.643 1.00 59.69 C ANISOU 168 CB ILE A 69 8085 7237 7359 1410 -236 -249 C ATOM 169 CG1 ILE A 69 10.432 24.490 -4.169 1.00 59.16 C ANISOU 169 CG1 ILE A 69 7965 7177 7337 1258 -140 -351 C ATOM 170 CG2 ILE A 69 9.084 24.450 -6.345 1.00 61.47 C ANISOU 170 CG2 ILE A 69 8120 7683 7551 1491 -339 -283 C ATOM 171 CD1 ILE A 69 9.349 25.036 -3.207 1.00 66.22 C ANISOU 171 CD1 ILE A 69 8744 8123 8295 1352 -87 -441 C ATOM 172 N GLY A 70 11.930 26.243 -8.218 1.00 58.49 N ANISOU 172 N GLY A 70 8287 6853 7082 1565 -316 25 N ATOM 173 CA GLY A 70 11.932 26.766 -9.580 1.00 59.68 C ANISOU 173 CA GLY A 70 8533 6989 7155 1702 -388 145 C ATOM 174 C GLY A 70 12.924 26.100 -10.511 1.00 63.00 C ANISOU 174 C GLY A 70 9043 7411 7484 1579 -404 204 C ATOM 175 O GLY A 70 12.534 25.572 -11.554 1.00 63.41 O ANISOU 175 O GLY A 70 9050 7600 7443 1619 -500 231 O ATOM 176 N GLY A 71 14.194 26.114 -10.119 1.00 58.31 N ANISOU 176 N GLY A 71 8563 6678 6912 1430 -309 211 N ATOM 177 CA GLY A 71 15.291 25.544 -10.893 1.00 57.12 C ANISOU 177 CA GLY A 71 8499 6518 6689 1308 -298 256 C ATOM 178 C GLY A 71 15.214 24.050 -11.140 1.00 59.04 C ANISOU 178 C GLY A 71 8623 6925 6885 1196 -352 186 C ATOM 179 O GLY A 71 15.572 23.588 -12.226 1.00 58.37 O ANISOU 179 O GLY A 71 8579 6893 6706 1175 -391 226 O ATOM 180 N ASN A 72 14.747 23.287 -10.137 1.00 54.60 N ANISOU 180 N ASN A 72 7926 6435 6383 1118 -347 79 N ATOM 181 CA ASN A 72 14.652 21.827 -10.226 1.00 53.52 C ANISOU 181 CA ASN A 72 7694 6426 6217 996 -382 5 C ATOM 182 C ASN A 72 13.470 21.370 -11.073 1.00 58.29 C ANISOU 182 C ASN A 72 8181 7209 6758 1066 -492 -21 C ATOM 183 O ASN A 72 13.611 20.372 -11.780 1.00 57.53 O ANISOU 183 O ASN A 72 8068 7195 6597 987 -532 -49 O ATOM 184 CB ASN A 72 14.607 21.189 -8.842 1.00 52.01 C ANISOU 184 CB ASN A 72 7425 6233 6101 879 -327 -86 C ATOM 185 CG ASN A 72 15.946 21.256 -8.148 1.00 63.65 C ANISOU 185 CG ASN A 72 9002 7576 7608 778 -242 -74 C ATOM 186 OD1 ASN A 72 16.940 20.668 -8.592 1.00 55.07 O ANISOU 186 OD1 ASN A 72 7973 6467 6483 699 -232 -57 O ATOM 187 ND2 ASN A 72 16.019 22.014 -7.071 1.00 52.97 N ANISOU 187 ND2 ASN A 72 7666 6140 6321 782 -179 -91 N ATOM 188 N THR A 73 12.329 22.097 -11.040 1.00 56.18 N ANISOU 188 N THR A 73 7829 7008 6509 1216 -541 -21 N ATOM 189 CA THR A 73 11.167 21.755 -11.867 1.00 57.49 C ANISOU 189 CA THR A 73 7861 7372 6610 1296 -660 -52 C ATOM 190 C THR A 73 11.505 21.985 -13.343 1.00 62.26 C ANISOU 190 C THR A 73 8570 7998 7089 1375 -732 44 C ATOM 191 O THR A 73 11.083 21.187 -14.180 1.00 63.30 O ANISOU 191 O THR A 73 8625 8291 7133 1350 -821 2 O ATOM 192 CB THR A 73 9.896 22.505 -11.445 1.00 69.09 C ANISOU 192 CB THR A 73 9198 8920 8131 1458 -696 -77 C ATOM 193 OG1 THR A 73 10.204 23.865 -11.155 1.00 76.23 O ANISOU 193 OG1 THR A 73 10230 9654 9080 1597 -644 10 O ATOM 194 CG2 THR A 73 9.214 21.871 -10.257 1.00 64.44 C ANISOU 194 CG2 THR A 73 8445 8411 7629 1356 -650 -205 C ATOM 195 N LEU A 74 12.307 23.033 -13.650 1.00 58.14 N ANISOU 195 N LEU A 74 8229 7312 6549 1453 -687 167 N ATOM 196 CA LEU A 74 12.762 23.362 -15.008 1.00 58.56 C ANISOU 196 CA LEU A 74 8418 7361 6473 1521 -730 277 C ATOM 197 C LEU A 74 13.622 22.238 -15.588 1.00 61.64 C ANISOU 197 C LEU A 74 8842 7790 6789 1353 -716 242 C ATOM 198 O LEU A 74 13.484 21.921 -16.773 1.00 62.28 O ANISOU 198 O LEU A 74 8938 7986 6739 1383 -795 265 O ATOM 199 CB LEU A 74 13.555 24.682 -15.023 1.00 58.82 C ANISOU 199 CB LEU A 74 8652 7177 6518 1594 -647 408 C ATOM 200 CG LEU A 74 12.751 25.984 -15.055 1.00 65.01 C ANISOU 200 CG LEU A 74 9472 7907 7321 1822 -682 490 C ATOM 201 CD1 LEU A 74 13.541 27.115 -14.436 1.00 64.87 C ANISOU 201 CD1 LEU A 74 9630 7633 7384 1825 -555 559 C ATOM 202 CD2 LEU A 74 12.367 26.364 -16.479 1.00 69.55 C ANISOU 202 CD2 LEU A 74 10115 8566 7745 1987 -791 605 C ATOM 203 N VAL A 75 14.498 21.634 -14.753 1.00 56.67 N ANISOU 203 N VAL A 75 8224 7070 6238 1188 -619 183 N ATOM 204 CA VAL A 75 15.387 20.525 -15.141 1.00 55.52 C ANISOU 204 CA VAL A 75 8108 6940 6047 1038 -590 138 C ATOM 205 C VAL A 75 14.529 19.262 -15.388 1.00 60.15 C ANISOU 205 C VAL A 75 8553 7702 6601 976 -672 21 C ATOM 206 O VAL A 75 14.751 18.563 -16.387 1.00 60.00 O ANISOU 206 O VAL A 75 8558 7760 6479 933 -709 -1 O ATOM 207 CB VAL A 75 16.523 20.283 -14.097 1.00 57.32 C ANISOU 207 CB VAL A 75 8380 7028 6372 907 -474 111 C ATOM 208 CG1 VAL A 75 17.354 19.045 -14.437 1.00 56.08 C ANISOU 208 CG1 VAL A 75 8236 6894 6179 778 -450 54 C ATOM 209 CG2 VAL A 75 17.428 21.507 -13.965 1.00 57.03 C ANISOU 209 CG2 VAL A 75 8481 6831 6359 939 -390 210 C ATOM 210 N ILE A 76 13.536 19.001 -14.497 1.00 56.67 N ANISOU 210 N ILE A 76 7966 7323 6243 966 -694 -60 N ATOM 211 CA ILE A 76 12.614 17.859 -14.587 1.00 56.76 C ANISOU 211 CA ILE A 76 7830 7495 6241 884 -758 -182 C ATOM 212 C ILE A 76 11.749 18.007 -15.850 1.00 62.06 C ANISOU 212 C ILE A 76 8444 8349 6788 989 -889 -178 C ATOM 213 O ILE A 76 11.580 17.027 -16.578 1.00 62.36 O ANISOU 213 O ILE A 76 8447 8499 6747 903 -941 -256 O ATOM 214 CB ILE A 76 11.765 17.692 -13.285 1.00 59.67 C ANISOU 214 CB ILE A 76 8058 7889 6726 844 -730 -261 C ATOM 215 CG1 ILE A 76 12.635 17.149 -12.132 1.00 58.20 C ANISOU 215 CG1 ILE A 76 7930 7557 6628 703 -616 -285 C ATOM 216 CG2 ILE A 76 10.538 16.777 -13.495 1.00 61.72 C ANISOU 216 CG2 ILE A 76 8139 8346 6965 782 -807 -383 C ATOM 217 CD1 ILE A 76 12.140 17.497 -10.723 1.00 64.39 C ANISOU 217 CD1 ILE A 76 8642 8305 7517 698 -556 -312 C ATOM 218 N LEU A 77 11.248 19.224 -16.131 1.00 59.53 N ANISOU 218 N LEU A 77 8124 8052 6443 1179 -944 -87 N ATOM 219 CA LEU A 77 10.418 19.476 -17.314 1.00 61.50 C ANISOU 219 CA LEU A 77 8322 8485 6561 1313 -1084 -65 C ATOM 220 C LEU A 77 11.194 19.256 -18.619 1.00 65.51 C ANISOU 220 C LEU A 77 8975 9002 6914 1299 -1108 -8 C ATOM 221 O LEU A 77 10.646 18.652 -19.541 1.00 66.30 O ANISOU 221 O LEU A 77 9008 9288 6893 1294 -1215 -65 O ATOM 222 CB LEU A 77 9.803 20.888 -17.299 1.00 62.91 C ANISOU 222 CB LEU A 77 8499 8653 6749 1548 -1129 41 C ATOM 223 CG LEU A 77 8.624 21.117 -16.342 1.00 68.14 C ANISOU 223 CG LEU A 77 8966 9402 7524 1615 -1151 -35 C ATOM 224 CD1 LEU A 77 8.305 22.587 -16.227 1.00 69.48 C ANISOU 224 CD1 LEU A 77 9191 9480 7728 1849 -1154 80 C ATOM 225 CD2 LEU A 77 7.379 20.332 -16.763 1.00 71.37 C ANISOU 225 CD2 LEU A 77 9148 10094 7875 1612 -1284 -155 C ATOM 226 N ALA A 78 12.465 19.713 -18.680 1.00 60.79 N ANISOU 226 N ALA A 78 8566 8216 6314 1280 -1004 92 N ATOM 227 CA ALA A 78 13.339 19.592 -19.851 1.00 60.54 C ANISOU 227 CA ALA A 78 8685 8179 6139 1260 -994 151 C ATOM 228 C ALA A 78 13.582 18.127 -20.242 1.00 63.84 C ANISOU 228 C ALA A 78 9064 8683 6509 1091 -997 17 C ATOM 229 O ALA A 78 13.431 17.788 -21.416 1.00 64.75 O ANISOU 229 O ALA A 78 9203 8931 6468 1102 -1070 3 O ATOM 230 CB ALA A 78 14.663 20.298 -19.596 1.00 60.08 C ANISOU 230 CB ALA A 78 8804 7903 6121 1240 -859 259 C ATOM 231 N VAL A 79 13.903 17.257 -19.263 1.00 58.36 N ANISOU 231 N VAL A 79 8317 7914 5943 942 -919 -84 N ATOM 232 CA VAL A 79 14.160 15.827 -19.492 1.00 57.47 C ANISOU 232 CA VAL A 79 8184 7840 5810 783 -905 -216 C ATOM 233 C VAL A 79 12.845 15.100 -19.881 1.00 63.29 C ANISOU 233 C VAL A 79 8767 8785 6495 752 -1026 -341 C ATOM 234 O VAL A 79 12.895 14.158 -20.669 1.00 64.43 O ANISOU 234 O VAL A 79 8922 9014 6547 665 -1056 -434 O ATOM 235 CB VAL A 79 14.858 15.177 -18.260 1.00 59.11 C ANISOU 235 CB VAL A 79 8396 7891 6170 656 -789 -267 C ATOM 236 CG1 VAL A 79 15.070 13.674 -18.442 1.00 58.63 C ANISOU 236 CG1 VAL A 79 8330 7846 6100 506 -771 -401 C ATOM 237 CG2 VAL A 79 16.188 15.863 -17.958 1.00 57.66 C ANISOU 237 CG2 VAL A 79 8345 7538 6026 676 -680 -162 C ATOM 238 N SER A 80 11.685 15.558 -19.368 1.00 60.35 N ANISOU 238 N SER A 80 8248 8503 6178 824 -1093 -351 N ATOM 239 CA SER A 80 10.374 14.956 -19.635 1.00 61.73 C ANISOU 239 CA SER A 80 8240 8896 6317 789 -1207 -478 C ATOM 240 C SER A 80 9.745 15.386 -20.969 1.00 68.32 C ANISOU 240 C SER A 80 9047 9939 6973 921 -1357 -451 C ATOM 241 O SER A 80 9.129 14.551 -21.629 1.00 69.21 O ANISOU 241 O SER A 80 9068 10232 6998 839 -1443 -578 O ATOM 242 CB SER A 80 9.396 15.291 -18.513 1.00 65.35 C ANISOU 242 CB SER A 80 8533 9388 6908 817 -1209 -507 C ATOM 243 OG SER A 80 9.826 14.767 -17.269 1.00 73.77 O ANISOU 243 OG SER A 80 9613 10298 8119 678 -1083 -549 O ATOM 244 N LEU A 81 9.855 16.679 -21.340 1.00 66.06 N ANISOU 244 N LEU A 81 8842 9628 6628 1123 -1390 -289 N ATOM 245 CA LEU A 81 9.216 17.237 -22.538 1.00 68.33 C ANISOU 245 CA LEU A 81 9115 10110 6738 1286 -1541 -233 C ATOM 246 C LEU A 81 10.104 17.259 -23.794 1.00 73.32 C ANISOU 246 C LEU A 81 9940 10732 7185 1294 -1541 -160 C ATOM 247 O LEU A 81 9.566 17.066 -24.887 1.00 75.61 O ANISOU 247 O LEU A 81 10194 11234 7300 1326 -1669 -199 O ATOM 248 CB LEU A 81 8.695 18.658 -22.269 1.00 69.30 C ANISOU 248 CB LEU A 81 9226 10215 6889 1526 -1587 -90 C ATOM 249 CG LEU A 81 7.585 18.804 -21.220 1.00 74.23 C ANISOU 249 CG LEU A 81 9634 10908 7663 1567 -1612 -164 C ATOM 250 CD1 LEU A 81 7.532 20.215 -20.677 1.00 74.67 C ANISOU 250 CD1 LEU A 81 9749 10829 7795 1779 -1584 -15 C ATOM 251 CD2 LEU A 81 6.230 18.407 -21.781 1.00 78.85 C ANISOU 251 CD2 LEU A 81 9987 11808 8164 1605 -1783 -280 C ATOM 252 N GLU A 82 11.422 17.532 -23.668 1.00 67.87 N ANISOU 252 N GLU A 82 9444 9822 6523 1265 -1400 -59 N ATOM 253 CA GLU A 82 12.325 17.582 -24.827 1.00 68.11 C ANISOU 253 CA GLU A 82 9658 9842 6380 1263 -1374 10 C ATOM 254 C GLU A 82 12.896 16.179 -25.123 1.00 71.67 C ANISOU 254 C GLU A 82 10113 10314 6804 1061 -1323 -150 C ATOM 255 O GLU A 82 13.642 15.623 -24.310 1.00 69.10 O ANISOU 255 O GLU A 82 9800 9832 6624 933 -1200 -207 O ATOM 256 CB GLU A 82 13.444 18.633 -24.619 1.00 68.52 C ANISOU 256 CB GLU A 82 9902 9663 6468 1317 -1241 184 C ATOM 257 CG GLU A 82 14.498 18.705 -25.718 1.00 80.01 C ANISOU 257 CG GLU A 82 11549 11097 7754 1296 -1181 260 C ATOM 258 CD GLU A 82 14.029 19.187 -27.077 1.00103.87 C ANISOU 258 CD GLU A 82 14644 14287 10535 1436 -1303 352 C ATOM 259 OE1 GLU A 82 14.013 20.420 -27.297 1.00101.62 O ANISOU 259 OE1 GLU A 82 14470 13935 10204 1597 -1313 533 O ATOM 260 OE2 GLU A 82 13.703 18.331 -27.931 1.00 99.34 O ANISOU 260 OE2 GLU A 82 14028 13905 9811 1384 -1387 245 O ATOM 261 N LYS A 83 12.539 15.621 -26.301 1.00 70.52 N ANISOU 261 N LYS A 83 9965 10363 6466 1045 -1421 -222 N ATOM 262 CA LYS A 83 12.975 14.290 -26.738 1.00 70.38 C ANISOU 262 CA LYS A 83 9963 10378 6401 868 -1382 -388 C ATOM 263 C LYS A 83 14.478 14.244 -27.047 1.00 73.76 C ANISOU 263 C LYS A 83 10580 10649 6795 820 -1231 -334 C ATOM 264 O LYS A 83 15.083 13.177 -26.931 1.00 72.98 O ANISOU 264 O LYS A 83 10500 10490 6737 678 -1148 -463 O ATOM 265 CB LYS A 83 12.163 13.803 -27.945 1.00 75.35 C ANISOU 265 CB LYS A 83 10533 11276 6821 865 -1536 -491 C ATOM 266 CG LYS A 83 10.790 13.278 -27.548 1.00 92.83 C ANISOU 266 CG LYS A 83 12518 13656 9096 820 -1659 -635 C ATOM 267 CD LYS A 83 10.197 12.349 -28.594 1.00104.65 C ANISOU 267 CD LYS A 83 13951 15395 10418 727 -1777 -811 C ATOM 268 CE LYS A 83 8.853 11.799 -28.179 1.00116.92 C ANISOU 268 CE LYS A 83 15261 17122 12040 649 -1886 -973 C ATOM 269 NZ LYS A 83 7.761 12.796 -28.348 1.00127.57 N ANISOU 269 NZ LYS A 83 16467 18673 13331 846 -2050 -887 N ATOM 270 N LYS A 84 15.083 15.403 -27.389 1.00 70.23 N ANISOU 270 N LYS A 84 10272 10129 6283 938 -1185 -146 N ATOM 271 CA LYS A 84 16.516 15.548 -27.674 1.00 69.16 C ANISOU 271 CA LYS A 84 10304 9858 6116 897 -1031 -80 C ATOM 272 C LYS A 84 17.373 15.363 -26.401 1.00 70.22 C ANISOU 272 C LYS A 84 10428 9774 6480 812 -886 -95 C ATOM 273 O LYS A 84 18.599 15.302 -26.499 1.00 68.99 O ANISOU 273 O LYS A 84 10371 9513 6328 758 -752 -75 O ATOM 274 CB LYS A 84 16.806 16.926 -28.302 1.00 72.94 C ANISOU 274 CB LYS A 84 10933 10316 6466 1036 -1022 132 C ATOM 275 CG LYS A 84 16.334 17.078 -29.742 1.00 92.00 C ANISOU 275 CG LYS A 84 13413 12939 8605 1115 -1137 166 C ATOM 276 CD LYS A 84 16.627 18.472 -30.281 1.00103.22 C ANISOU 276 CD LYS A 84 15007 14309 9903 1256 -1118 398 C ATOM 277 N LEU A 85 16.735 15.293 -25.218 1.00 65.92 N ANISOU 277 N LEU A 85 9756 9174 6115 803 -912 -131 N ATOM 278 CA LEU A 85 17.427 15.116 -23.934 1.00 63.72 C ANISOU 278 CA LEU A 85 9460 8709 6043 731 -795 -145 C ATOM 279 C LEU A 85 17.066 13.775 -23.269 1.00 66.08 C ANISOU 279 C LEU A 85 9647 9008 6451 607 -803 -317 C ATOM 280 O LEU A 85 17.579 13.472 -22.192 1.00 63.89 O ANISOU 280 O LEU A 85 9353 8590 6333 547 -718 -337 O ATOM 281 CB LEU A 85 17.120 16.286 -22.971 1.00 63.08 C ANISOU 281 CB LEU A 85 9355 8530 6083 823 -792 -25 C ATOM 282 CG LEU A 85 17.666 17.668 -23.351 1.00 68.06 C ANISOU 282 CG LEU A 85 10126 9079 6654 923 -742 155 C ATOM 283 CD1 LEU A 85 17.035 18.746 -22.492 1.00 68.32 C ANISOU 283 CD1 LEU A 85 10127 9041 6790 1033 -771 248 C ATOM 284 CD2 LEU A 85 19.184 17.724 -23.230 1.00 68.49 C ANISOU 284 CD2 LEU A 85 10282 8989 6752 838 -583 182 C ATOM 285 N GLN A 86 16.224 12.957 -23.923 1.00 63.46 N ANISOU 285 N GLN A 86 9249 8834 6027 562 -900 -442 N ATOM 286 CA GLN A 86 15.805 11.672 -23.368 1.00 63.02 C ANISOU 286 CA GLN A 86 9105 8772 6065 427 -902 -609 C ATOM 287 C GLN A 86 16.876 10.589 -23.647 1.00 66.95 C ANISOU 287 C GLN A 86 9701 9178 6560 327 -799 -704 C ATOM 288 O GLN A 86 16.664 9.647 -24.415 1.00 67.26 O ANISOU 288 O GLN A 86 9748 9300 6509 249 -829 -841 O ATOM 289 CB GLN A 86 14.402 11.281 -23.867 1.00 66.09 C ANISOU 289 CB GLN A 86 9370 9370 6371 402 -1046 -718 C ATOM 290 CG GLN A 86 13.338 12.325 -23.495 1.00 78.94 C ANISOU 290 CG GLN A 86 10874 11091 8026 517 -1144 -637 C ATOM 291 CD GLN A 86 11.910 11.892 -23.712 1.00 96.87 C ANISOU 291 CD GLN A 86 12976 13578 10254 477 -1279 -765 C ATOM 292 OE1 GLN A 86 11.530 11.355 -24.761 1.00 93.05 O ANISOU 292 OE1 GLN A 86 12481 13260 9615 439 -1364 -862 O ATOM 293 NE2 GLN A 86 11.067 12.187 -22.736 1.00 89.26 N ANISOU 293 NE2 GLN A 86 11865 12633 9417 486 -1304 -774 N ATOM 294 N TYR A 87 18.040 10.765 -22.990 1.00 62.77 N ANISOU 294 N TYR A 87 9239 8479 6132 335 -677 -635 N ATOM 295 CA TYR A 87 19.222 9.898 -23.010 1.00 62.02 C ANISOU 295 CA TYR A 87 9225 8273 6067 276 -565 -701 C ATOM 296 C TYR A 87 19.559 9.462 -21.585 1.00 63.16 C ANISOU 296 C TYR A 87 9340 8253 6405 231 -498 -712 C ATOM 297 O TYR A 87 19.384 10.253 -20.655 1.00 61.63 O ANISOU 297 O TYR A 87 9098 8011 6308 267 -501 -620 O ATOM 298 CB TYR A 87 20.429 10.634 -23.616 1.00 63.49 C ANISOU 298 CB TYR A 87 9509 8436 6177 342 -481 -599 C ATOM 299 CG TYR A 87 20.347 10.897 -25.100 1.00 67.57 C ANISOU 299 CG TYR A 87 10092 9104 6478 375 -519 -594 C ATOM 300 CD1 TYR A 87 20.898 10.004 -26.017 1.00 70.72 C ANISOU 300 CD1 TYR A 87 10557 9542 6772 329 -473 -709 C ATOM 301 CD2 TYR A 87 19.808 12.082 -25.590 1.00 69.28 C ANISOU 301 CD2 TYR A 87 10321 9415 6588 466 -594 -465 C ATOM 302 CE1 TYR A 87 20.870 10.263 -27.387 1.00 73.28 C ANISOU 302 CE1 TYR A 87 10951 10015 6877 356 -501 -703 C ATOM 303 CE2 TYR A 87 19.770 12.351 -26.958 1.00 71.91 C ANISOU 303 CE2 TYR A 87 10731 9890 6700 504 -630 -443 C ATOM 304 CZ TYR A 87 20.309 11.442 -27.854 1.00 80.28 C ANISOU 304 CZ TYR A 87 11852 11003 7646 443 -583 -563 C ATOM 305 OH TYR A 87 20.281 11.707 -29.203 1.00 82.76 O ANISOU 305 OH TYR A 87 12251 11469 7726 477 -615 -543 O ATOM 306 N ALA A 88 20.094 8.235 -21.431 1.00 59.18 N ANISOU 306 N ALA A 88 8879 7658 5948 164 -434 -821 N ATOM 307 CA ALA A 88 20.492 7.584 -20.172 1.00 57.69 C ANISOU 307 CA ALA A 88 8689 7309 5921 125 -371 -839 C ATOM 308 C ALA A 88 21.237 8.505 -19.188 1.00 60.51 C ANISOU 308 C ALA A 88 9035 7580 6375 189 -317 -707 C ATOM 309 O ALA A 88 20.923 8.491 -17.999 1.00 59.18 O ANISOU 309 O ALA A 88 8825 7337 6323 167 -316 -683 O ATOM 310 CB ALA A 88 21.354 6.374 -20.472 1.00 58.80 C ANISOU 310 CB ALA A 88 8913 7363 6064 96 -297 -946 C ATOM 311 N THR A 89 22.204 9.302 -19.687 1.00 57.62 N ANISOU 311 N THR A 89 8707 7231 5955 254 -269 -627 N ATOM 312 CA THR A 89 23.037 10.223 -18.901 1.00 56.49 C ANISOU 312 CA THR A 89 8556 7018 5891 298 -210 -517 C ATOM 313 C THR A 89 22.204 11.350 -18.237 1.00 60.02 C ANISOU 313 C THR A 89 8950 7475 6379 323 -263 -422 C ATOM 314 O THR A 89 22.596 11.833 -17.171 1.00 58.82 O ANISOU 314 O THR A 89 8777 7243 6329 331 -227 -365 O ATOM 315 CB THR A 89 24.195 10.790 -19.764 1.00 65.25 C ANISOU 315 CB THR A 89 9718 8157 6918 335 -135 -472 C ATOM 316 OG1 THR A 89 24.988 11.683 -18.980 1.00 63.06 O ANISOU 316 OG1 THR A 89 9424 7815 6721 354 -77 -380 O ATOM 317 CG2 THR A 89 23.722 11.489 -21.050 1.00 66.14 C ANISOU 317 CG2 THR A 89 9874 8389 6868 362 -174 -428 C ATOM 318 N ASN A 90 21.070 11.752 -18.851 1.00 56.80 N ANISOU 318 N ASN A 90 8518 7171 5890 343 -350 -413 N ATOM 319 CA ASN A 90 20.213 12.810 -18.313 1.00 56.02 C ANISOU 319 CA ASN A 90 8368 7089 5827 392 -402 -331 C ATOM 320 C ASN A 90 19.241 12.284 -17.256 1.00 59.01 C ANISOU 320 C ASN A 90 8656 7456 6308 343 -440 -391 C ATOM 321 O ASN A 90 18.682 13.091 -16.512 1.00 57.93 O ANISOU 321 O ASN A 90 8469 7310 6233 381 -458 -335 O ATOM 322 CB ASN A 90 19.459 13.532 -19.430 1.00 56.56 C ANISOU 322 CB ASN A 90 8446 7286 5760 464 -482 -284 C ATOM 323 CG ASN A 90 20.349 14.395 -20.293 1.00 74.54 C ANISOU 323 CG ASN A 90 10828 9557 7938 517 -431 -184 C ATOM 324 OD1 ASN A 90 21.354 14.956 -19.843 1.00 67.05 O ANISOU 324 OD1 ASN A 90 9923 8505 7049 515 -339 -118 O ATOM 325 ND2 ASN A 90 19.989 14.542 -21.555 1.00 68.93 N ANISOU 325 ND2 ASN A 90 10160 8966 7066 559 -488 -170 N ATOM 326 N TYR A 91 19.066 10.942 -17.149 1.00 56.00 N ANISOU 326 N TYR A 91 8264 7064 5949 255 -439 -505 N ATOM 327 CA TYR A 91 18.197 10.350 -16.122 1.00 55.46 C ANISOU 327 CA TYR A 91 8123 6974 5974 182 -454 -562 C ATOM 328 C TYR A 91 18.870 10.473 -14.753 1.00 56.31 C ANISOU 328 C TYR A 91 8246 6948 6200 178 -382 -510 C ATOM 329 O TYR A 91 18.178 10.510 -13.735 1.00 54.56 O ANISOU 329 O TYR A 91 7965 6713 6053 145 -385 -512 O ATOM 330 CB TYR A 91 17.788 8.908 -16.461 1.00 57.92 C ANISOU 330 CB TYR A 91 8442 7297 6269 74 -465 -697 C ATOM 331 CG TYR A 91 16.886 8.858 -17.675 1.00 62.27 C ANISOU 331 CG TYR A 91 8948 8012 6700 64 -556 -765 C ATOM 332 CD1 TYR A 91 15.622 9.443 -17.654 1.00 65.46 C ANISOU 332 CD1 TYR A 91 9232 8550 7087 81 -641 -764 C ATOM 333 CD2 TYR A 91 17.316 8.280 -18.863 1.00 64.17 C ANISOU 333 CD2 TYR A 91 9261 8289 6834 48 -558 -836 C ATOM 334 CE1 TYR A 91 14.810 9.456 -18.787 1.00 68.50 C ANISOU 334 CE1 TYR A 91 9564 9113 7349 87 -741 -824 C ATOM 335 CE2 TYR A 91 16.513 8.284 -20.004 1.00 66.88 C ANISOU 335 CE2 TYR A 91 9564 8802 7045 40 -651 -900 C ATOM 336 CZ TYR A 91 15.259 8.874 -19.961 1.00 77.66 C ANISOU 336 CZ TYR A 91 10805 10312 8393 61 -749 -891 C ATOM 337 OH TYR A 91 14.454 8.872 -21.076 1.00 84.00 O ANISOU 337 OH TYR A 91 11555 11307 9056 63 -857 -957 O ATOM 338 N PHE A 92 20.215 10.639 -14.751 1.00 52.73 N ANISOU 338 N PHE A 92 7861 6418 5754 215 -319 -462 N ATOM 339 CA PHE A 92 21.028 10.915 -13.565 1.00 51.79 C ANISOU 339 CA PHE A 92 7753 6199 5727 225 -261 -409 C ATOM 340 C PHE A 92 20.670 12.289 -13.041 1.00 54.74 C ANISOU 340 C PHE A 92 8086 6585 6128 271 -270 -328 C ATOM 341 O PHE A 92 20.511 12.462 -11.834 1.00 54.26 O ANISOU 341 O PHE A 92 7997 6476 6144 255 -253 -312 O ATOM 342 CB PHE A 92 22.529 10.859 -13.892 1.00 53.75 C ANISOU 342 CB PHE A 92 8058 6403 5963 257 -198 -392 C ATOM 343 CG PHE A 92 23.184 9.503 -13.838 1.00 56.00 C ANISOU 343 CG PHE A 92 8386 6623 6268 234 -165 -463 C ATOM 344 CD1 PHE A 92 23.561 8.943 -12.622 1.00 58.85 C ANISOU 344 CD1 PHE A 92 8752 6893 6714 225 -140 -458 C ATOM 345 CD2 PHE A 92 23.498 8.819 -15.005 1.00 59.69 C ANISOU 345 CD2 PHE A 92 8899 7118 6664 235 -156 -532 C ATOM 346 CE1 PHE A 92 24.191 7.697 -12.573 1.00 60.54 C ANISOU 346 CE1 PHE A 92 9023 7032 6949 229 -111 -513 C ATOM 347 CE2 PHE A 92 24.136 7.576 -14.956 1.00 63.15 C ANISOU 347 CE2 PHE A 92 9388 7477 7129 232 -118 -602 C ATOM 348 CZ PHE A 92 24.484 7.027 -13.740 1.00 60.84 C ANISOU 348 CZ PHE A 92 9106 7081 6929 237 -97 -587 C ATOM 349 N LEU A 93 20.522 13.260 -13.974 1.00 50.94 N ANISOU 349 N LEU A 93 7614 6165 5575 333 -296 -276 N ATOM 350 CA LEU A 93 20.163 14.651 -13.710 1.00 50.48 C ANISOU 350 CA LEU A 93 7543 6104 5533 397 -304 -195 C ATOM 351 C LEU A 93 18.735 14.776 -13.207 1.00 54.48 C ANISOU 351 C LEU A 93 7961 6666 6072 409 -363 -219 C ATOM 352 O LEU A 93 18.502 15.567 -12.293 1.00 54.06 O ANISOU 352 O LEU A 93 7884 6572 6085 437 -345 -184 O ATOM 353 CB LEU A 93 20.345 15.522 -14.965 1.00 51.30 C ANISOU 353 CB LEU A 93 7707 6249 5536 467 -316 -125 C ATOM 354 CG LEU A 93 21.779 15.787 -15.410 1.00 55.93 C ANISOU 354 CG LEU A 93 8375 6784 6092 456 -236 -84 C ATOM 355 CD1 LEU A 93 21.811 16.378 -16.805 1.00 57.06 C ANISOU 355 CD1 LEU A 93 8589 6986 6105 507 -248 -24 C ATOM 356 CD2 LEU A 93 22.496 16.702 -14.431 1.00 58.46 C ANISOU 356 CD2 LEU A 93 8709 7004 6497 449 -168 -30 C ATOM 357 N MET A 94 17.784 14.007 -13.792 1.00 51.70 N ANISOU 357 N MET A 94 7555 6416 5674 382 -428 -291 N ATOM 358 CA MET A 94 16.373 14.027 -13.397 1.00 52.32 C ANISOU 358 CA MET A 94 7520 6582 5779 381 -484 -334 C ATOM 359 C MET A 94 16.197 13.536 -11.949 1.00 53.34 C ANISOU 359 C MET A 94 7608 6648 6011 299 -432 -374 C ATOM 360 O MET A 94 15.515 14.205 -11.171 1.00 52.26 O ANISOU 360 O MET A 94 7402 6528 5925 331 -431 -362 O ATOM 361 CB MET A 94 15.502 13.206 -14.359 1.00 56.44 C ANISOU 361 CB MET A 94 7984 7238 6221 342 -561 -422 C ATOM 362 CG MET A 94 14.027 13.500 -14.201 1.00 62.34 C ANISOU 362 CG MET A 94 8589 8119 6978 367 -633 -460 C ATOM 363 SD MET A 94 12.961 12.537 -15.289 1.00 69.83 S ANISOU 363 SD MET A 94 9448 9257 7829 302 -734 -584 S ATOM 364 CE MET A 94 11.364 13.094 -14.722 1.00 67.81 C ANISOU 364 CE MET A 94 8991 9153 7621 339 -796 -623 C ATOM 365 N SER A 95 16.834 12.399 -11.587 1.00 48.54 N ANISOU 365 N SER A 95 7051 5964 5427 204 -386 -417 N ATOM 366 CA SER A 95 16.792 11.832 -10.236 1.00 47.86 C ANISOU 366 CA SER A 95 6958 5809 5420 125 -333 -438 C ATOM 367 C SER A 95 17.368 12.839 -9.214 1.00 51.51 C ANISOU 367 C SER A 95 7439 6199 5934 177 -287 -365 C ATOM 368 O SER A 95 16.754 13.075 -8.167 1.00 51.29 O ANISOU 368 O SER A 95 7361 6172 5954 153 -264 -373 O ATOM 369 CB SER A 95 17.552 10.512 -10.193 1.00 50.89 C ANISOU 369 CB SER A 95 7424 6105 5806 48 -297 -477 C ATOM 370 OG SER A 95 17.414 9.850 -8.946 1.00 56.95 O ANISOU 370 OG SER A 95 8205 6800 6633 -25 -248 -485 O ATOM 371 N LEU A 96 18.508 13.475 -9.560 1.00 47.33 N ANISOU 371 N LEU A 96 6977 5619 5389 237 -269 -304 N ATOM 372 CA LEU A 96 19.163 14.513 -8.760 1.00 46.79 C ANISOU 372 CA LEU A 96 6931 5486 5361 274 -226 -247 C ATOM 373 C LEU A 96 18.218 15.703 -8.551 1.00 51.21 C ANISOU 373 C LEU A 96 7439 6079 5938 340 -242 -225 C ATOM 374 O LEU A 96 18.083 16.171 -7.420 1.00 51.03 O ANISOU 374 O LEU A 96 7400 6022 5968 334 -207 -224 O ATOM 375 CB LEU A 96 20.471 14.970 -9.451 1.00 46.73 C ANISOU 375 CB LEU A 96 6994 5437 5322 308 -201 -199 C ATOM 376 CG LEU A 96 21.227 16.173 -8.853 1.00 50.78 C ANISOU 376 CG LEU A 96 7536 5889 5869 332 -155 -146 C ATOM 377 CD1 LEU A 96 21.746 15.883 -7.451 1.00 49.90 C ANISOU 377 CD1 LEU A 96 7417 5731 5812 283 -120 -165 C ATOM 378 CD2 LEU A 96 22.374 16.567 -9.738 1.00 52.93 C ANISOU 378 CD2 LEU A 96 7866 6143 6100 346 -124 -108 C ATOM 379 N ALA A 97 17.553 16.165 -9.641 1.00 47.89 N ANISOU 379 N ALA A 97 6998 5731 5469 411 -296 -209 N ATOM 380 CA ALA A 97 16.593 17.268 -9.643 1.00 47.78 C ANISOU 380 CA ALA A 97 6935 5755 5466 509 -324 -185 C ATOM 381 C ALA A 97 15.359 16.943 -8.788 1.00 51.99 C ANISOU 381 C ALA A 97 7348 6361 6044 482 -335 -254 C ATOM 382 O ALA A 97 14.854 17.834 -8.110 1.00 51.76 O ANISOU 382 O ALA A 97 7281 6324 6060 544 -316 -248 O ATOM 383 CB ALA A 97 16.176 17.596 -11.066 1.00 49.30 C ANISOU 383 CB ALA A 97 7133 6023 5574 598 -395 -150 C ATOM 384 N VAL A 98 14.899 15.669 -8.795 1.00 49.56 N ANISOU 384 N VAL A 98 6986 6118 5727 381 -351 -327 N ATOM 385 CA VAL A 98 13.747 15.192 -8.005 1.00 50.33 C ANISOU 385 CA VAL A 98 6967 6293 5862 318 -344 -403 C ATOM 386 C VAL A 98 14.104 15.270 -6.506 1.00 53.74 C ANISOU 386 C VAL A 98 7425 6639 6354 266 -260 -399 C ATOM 387 O VAL A 98 13.326 15.826 -5.730 1.00 53.12 O ANISOU 387 O VAL A 98 7269 6600 6313 291 -236 -423 O ATOM 388 CB VAL A 98 13.275 13.763 -8.440 1.00 54.62 C ANISOU 388 CB VAL A 98 7472 6904 6377 195 -368 -484 C ATOM 389 CG1 VAL A 98 12.383 13.101 -7.385 1.00 54.65 C ANISOU 389 CG1 VAL A 98 7391 6946 6427 77 -321 -556 C ATOM 390 CG2 VAL A 98 12.557 13.807 -9.787 1.00 55.46 C ANISOU 390 CG2 VAL A 98 7507 7148 6417 247 -463 -513 C ATOM 391 N ALA A 99 15.290 14.739 -6.123 1.00 50.26 N ANISOU 391 N ALA A 99 7091 6092 5914 206 -219 -372 N ATOM 392 CA ALA A 99 15.812 14.741 -4.752 1.00 49.55 C ANISOU 392 CA ALA A 99 7043 5928 5857 159 -153 -362 C ATOM 393 C ALA A 99 15.891 16.168 -4.216 1.00 54.27 C ANISOU 393 C ALA A 99 7640 6498 6484 243 -128 -334 C ATOM 394 O ALA A 99 15.366 16.446 -3.136 1.00 54.10 O ANISOU 394 O ALA A 99 7579 6489 6488 225 -84 -363 O ATOM 395 CB ALA A 99 17.191 14.084 -4.709 1.00 49.26 C ANISOU 395 CB ALA A 99 7112 5799 5804 123 -138 -329 C ATOM 396 N ASP A 100 16.480 17.081 -5.012 1.00 51.09 N ANISOU 396 N ASP A 100 7286 6054 6071 331 -148 -283 N ATOM 397 CA ASP A 100 16.639 18.486 -4.652 1.00 51.11 C ANISOU 397 CA ASP A 100 7317 6000 6104 408 -119 -256 C ATOM 398 C ASP A 100 15.295 19.218 -4.605 1.00 54.64 C ANISOU 398 C ASP A 100 7676 6508 6575 498 -131 -281 C ATOM 399 O ASP A 100 15.126 20.084 -3.750 1.00 54.47 O ANISOU 399 O ASP A 100 7658 6445 6593 535 -85 -296 O ATOM 400 CB ASP A 100 17.624 19.174 -5.599 1.00 53.18 C ANISOU 400 CB ASP A 100 7670 6193 6344 459 -126 -189 C ATOM 401 CG ASP A 100 19.055 18.694 -5.407 1.00 64.97 C ANISOU 401 CG ASP A 100 9230 7630 7826 381 -98 -175 C ATOM 402 OD1 ASP A 100 19.449 18.442 -4.245 1.00 66.02 O ANISOU 402 OD1 ASP A 100 9366 7740 7981 320 -64 -202 O ATOM 403 OD2 ASP A 100 19.796 18.622 -6.408 1.00 70.85 O ANISOU 403 OD2 ASP A 100 10021 8363 8535 390 -110 -139 O ATOM 404 N LEU A 101 14.327 18.832 -5.460 1.00 51.45 N ANISOU 404 N LEU A 101 7188 6213 6148 535 -194 -299 N ATOM 405 CA LEU A 101 12.979 19.408 -5.444 1.00 52.62 C ANISOU 405 CA LEU A 101 7220 6455 6319 633 -217 -334 C ATOM 406 C LEU A 101 12.238 19.000 -4.160 1.00 57.06 C ANISOU 406 C LEU A 101 7685 7075 6920 555 -159 -415 C ATOM 407 O LEU A 101 11.511 19.821 -3.592 1.00 57.32 O ANISOU 407 O LEU A 101 7651 7136 6992 638 -133 -447 O ATOM 408 CB LEU A 101 12.169 18.983 -6.687 1.00 53.59 C ANISOU 408 CB LEU A 101 7258 6710 6393 677 -311 -343 C ATOM 409 CG LEU A 101 10.695 19.430 -6.754 1.00 59.92 C ANISOU 409 CG LEU A 101 7900 7654 7211 785 -356 -391 C ATOM 410 CD1 LEU A 101 10.571 20.941 -6.902 1.00 60.67 C ANISOU 410 CD1 LEU A 101 8035 7688 7328 979 -363 -330 C ATOM 411 CD2 LEU A 101 9.947 18.710 -7.863 1.00 63.73 C ANISOU 411 CD2 LEU A 101 8281 8299 7635 779 -454 -426 C ATOM 412 N LEU A 102 12.435 17.735 -3.709 1.00 53.08 N ANISOU 412 N LEU A 102 7186 6582 6402 401 -133 -447 N ATOM 413 CA LEU A 102 11.820 17.173 -2.506 1.00 52.88 C ANISOU 413 CA LEU A 102 7094 6604 6393 297 -66 -512 C ATOM 414 C LEU A 102 12.343 17.856 -1.232 1.00 56.24 C ANISOU 414 C LEU A 102 7586 6944 6837 298 11 -506 C ATOM 415 O LEU A 102 11.580 17.984 -0.270 1.00 56.21 O ANISOU 415 O LEU A 102 7511 6996 6849 272 73 -564 O ATOM 416 CB LEU A 102 12.013 15.654 -2.444 1.00 52.68 C ANISOU 416 CB LEU A 102 7096 6581 6340 138 -57 -527 C ATOM 417 CG LEU A 102 11.109 14.843 -3.393 1.00 58.60 C ANISOU 417 CG LEU A 102 7746 7446 7073 91 -111 -580 C ATOM 418 CD1 LEU A 102 11.668 13.464 -3.641 1.00 58.22 C ANISOU 418 CD1 LEU A 102 7787 7339 6996 -36 -113 -576 C ATOM 419 CD2 LEU A 102 9.690 14.730 -2.860 1.00 63.21 C ANISOU 419 CD2 LEU A 102 8166 8171 7680 37 -76 -668 C ATOM 420 N VAL A 103 13.617 18.335 -1.241 1.00 52.04 N ANISOU 420 N VAL A 103 7181 6291 6300 324 12 -447 N ATOM 421 CA VAL A 103 14.216 19.105 -0.137 1.00 51.34 C ANISOU 421 CA VAL A 103 7160 6125 6223 324 73 -452 C ATOM 422 C VAL A 103 13.459 20.446 -0.022 1.00 56.11 C ANISOU 422 C VAL A 103 7718 6731 6871 451 96 -483 C ATOM 423 O VAL A 103 13.037 20.821 1.072 1.00 56.13 O ANISOU 423 O VAL A 103 7693 6749 6887 442 162 -542 O ATOM 424 CB VAL A 103 15.748 19.344 -0.298 1.00 54.04 C ANISOU 424 CB VAL A 103 7627 6356 6551 311 64 -395 C ATOM 425 CG1 VAL A 103 16.324 20.083 0.904 1.00 54.01 C ANISOU 425 CG1 VAL A 103 7678 6295 6549 286 123 -421 C ATOM 426 CG2 VAL A 103 16.498 18.046 -0.505 1.00 53.04 C ANISOU 426 CG2 VAL A 103 7540 6227 6387 223 36 -364 C ATOM 427 N GLY A 104 13.290 21.125 -1.161 1.00 52.83 N ANISOU 427 N GLY A 104 7303 6299 6472 575 43 -443 N ATOM 428 CA GLY A 104 12.608 22.410 -1.270 1.00 54.09 C ANISOU 428 CA GLY A 104 7438 6438 6674 730 52 -455 C ATOM 429 C GLY A 104 11.160 22.426 -0.821 1.00 59.65 C ANISOU 429 C GLY A 104 7983 7275 7405 784 67 -534 C ATOM 430 O GLY A 104 10.712 23.416 -0.240 1.00 60.09 O ANISOU 430 O GLY A 104 8024 7305 7504 888 115 -575 O ATOM 431 N LEU A 105 10.424 21.331 -1.077 1.00 57.41 N ANISOU 431 N LEU A 105 7579 7135 7100 709 36 -567 N ATOM 432 CA LEU A 105 9.007 21.199 -0.727 1.00 59.19 C ANISOU 432 CA LEU A 105 7620 7521 7347 733 52 -654 C ATOM 433 C LEU A 105 8.762 20.620 0.666 1.00 64.80 C ANISOU 433 C LEU A 105 8289 8279 8053 589 154 -729 C ATOM 434 O LEU A 105 7.831 21.064 1.332 1.00 66.03 O ANISOU 434 O LEU A 105 8329 8521 8238 638 211 -808 O ATOM 435 CB LEU A 105 8.264 20.303 -1.740 1.00 59.77 C ANISOU 435 CB LEU A 105 7571 7744 7396 707 -33 -666 C ATOM 436 CG LEU A 105 8.129 20.784 -3.188 1.00 65.29 C ANISOU 436 CG LEU A 105 8265 8463 8079 863 -146 -607 C ATOM 437 CD1 LEU A 105 7.852 19.612 -4.125 1.00 65.28 C ANISOU 437 CD1 LEU A 105 8193 8582 8028 771 -226 -620 C ATOM 438 CD2 LEU A 105 7.044 21.853 -3.330 1.00 68.90 C ANISOU 438 CD2 LEU A 105 8601 9002 8576 1072 -171 -636 C ATOM 439 N PHE A 106 9.541 19.603 1.085 1.00 61.24 N ANISOU 439 N PHE A 106 7929 7781 7558 419 179 -704 N ATOM 440 CA PHE A 106 9.282 18.887 2.337 1.00 61.77 C ANISOU 440 CA PHE A 106 7975 7897 7599 270 272 -757 C ATOM 441 C PHE A 106 10.300 19.092 3.468 1.00 65.17 C ANISOU 441 C PHE A 106 8552 8216 7995 212 334 -736 C ATOM 442 O PHE A 106 9.949 18.830 4.620 1.00 65.40 O ANISOU 442 O PHE A 106 8565 8291 7992 121 420 -783 O ATOM 443 CB PHE A 106 9.173 17.379 2.049 1.00 63.58 C ANISOU 443 CB PHE A 106 8185 8178 7793 109 257 -751 C ATOM 444 CG PHE A 106 8.012 17.029 1.152 1.00 66.64 C ANISOU 444 CG PHE A 106 8403 8714 8204 122 207 -803 C ATOM 445 CD1 PHE A 106 6.736 16.848 1.677 1.00 71.88 C ANISOU 445 CD1 PHE A 106 8893 9535 8883 75 270 -899 C ATOM 446 CD2 PHE A 106 8.185 16.904 -0.221 1.00 68.51 C ANISOU 446 CD2 PHE A 106 8642 8951 8437 177 100 -765 C ATOM 447 CE1 PHE A 106 5.656 16.540 0.843 1.00 74.05 C ANISOU 447 CE1 PHE A 106 8986 9973 9177 81 215 -961 C ATOM 448 CE2 PHE A 106 7.104 16.604 -1.054 1.00 72.59 C ANISOU 448 CE2 PHE A 106 8992 9626 8961 188 41 -823 C ATOM 449 CZ PHE A 106 5.849 16.419 -0.516 1.00 72.40 C ANISOU 449 CZ PHE A 106 8784 9765 8958 139 95 -924 C ATOM 450 N VAL A 107 11.535 19.520 3.172 1.00 60.86 N ANISOU 450 N VAL A 107 8139 7539 7445 252 292 -671 N ATOM 451 CA VAL A 107 12.556 19.675 4.216 1.00 60.10 C ANISOU 451 CA VAL A 107 8167 7360 7309 191 335 -660 C ATOM 452 C VAL A 107 12.745 21.164 4.596 1.00 63.65 C ANISOU 452 C VAL A 107 8655 7738 7791 294 369 -697 C ATOM 453 O VAL A 107 12.631 21.505 5.775 1.00 64.01 O ANISOU 453 O VAL A 107 8713 7796 7812 261 445 -759 O ATOM 454 CB VAL A 107 13.889 18.994 3.797 1.00 62.93 C ANISOU 454 CB VAL A 107 8638 7639 7635 134 275 -578 C ATOM 455 CG1 VAL A 107 15.036 19.373 4.728 1.00 62.35 C ANISOU 455 CG1 VAL A 107 8673 7496 7523 97 297 -571 C ATOM 456 CG2 VAL A 107 13.731 17.476 3.733 1.00 62.61 C ANISOU 456 CG2 VAL A 107 8588 7641 7558 23 263 -553 C ATOM 457 N MET A 108 13.032 22.029 3.609 1.00 59.44 N ANISOU 457 N MET A 108 8154 7125 7307 411 321 -661 N ATOM 458 CA MET A 108 13.280 23.462 3.802 1.00 59.45 C ANISOU 458 CA MET A 108 8221 7020 7349 509 354 -686 C ATOM 459 C MET A 108 12.090 24.229 4.449 1.00 64.79 C ANISOU 459 C MET A 108 8815 7740 8061 602 426 -781 C ATOM 460 O MET A 108 12.378 25.019 5.351 1.00 64.55 O ANISOU 460 O MET A 108 8851 7641 8032 601 493 -841 O ATOM 461 CB MET A 108 13.689 24.140 2.492 1.00 61.37 C ANISOU 461 CB MET A 108 8522 7166 7630 615 293 -612 C ATOM 462 CG MET A 108 15.078 23.776 2.028 1.00 63.32 C ANISOU 462 CG MET A 108 8871 7342 7846 532 253 -539 C ATOM 463 SD MET A 108 15.571 24.791 0.624 1.00 67.39 S ANISOU 463 SD MET A 108 9479 7731 8395 644 215 -456 S ATOM 464 CE MET A 108 16.578 23.651 -0.249 1.00 62.73 C ANISOU 464 CE MET A 108 8916 7166 7754 546 152 -381 C ATOM 465 N PRO A 109 10.787 24.040 4.072 1.00 62.24 N ANISOU 465 N PRO A 109 8343 7538 7768 681 417 -810 N ATOM 466 CA PRO A 109 9.715 24.806 4.746 1.00 63.44 C ANISOU 466 CA PRO A 109 8406 7740 7959 784 494 -911 C ATOM 467 C PRO A 109 9.563 24.453 6.233 1.00 66.94 C ANISOU 467 C PRO A 109 8832 8251 8350 657 598 -999 C ATOM 468 O PRO A 109 9.260 25.338 7.034 1.00 67.25 O ANISOU 468 O PRO A 109 8878 8266 8407 719 681 -1087 O ATOM 469 CB PRO A 109 8.457 24.431 3.951 1.00 66.07 C ANISOU 469 CB PRO A 109 8557 8224 8322 872 445 -920 C ATOM 470 CG PRO A 109 8.973 23.915 2.635 1.00 69.43 C ANISOU 470 CG PRO A 109 9018 8629 8733 862 332 -814 C ATOM 471 CD PRO A 109 10.215 23.180 3.015 1.00 63.49 C ANISOU 471 CD PRO A 109 8396 7804 7925 686 338 -768 C ATOM 472 N ILE A 110 9.818 23.177 6.604 1.00 62.60 N ANISOU 472 N ILE A 110 8279 7775 7731 483 598 -973 N ATOM 473 CA ILE A 110 9.758 22.690 7.990 1.00 62.64 C ANISOU 473 CA ILE A 110 8293 7848 7660 345 692 -1031 C ATOM 474 C ILE A 110 10.976 23.235 8.773 1.00 65.65 C ANISOU 474 C ILE A 110 8838 8113 7993 301 712 -1033 C ATOM 475 O ILE A 110 10.877 23.445 9.984 1.00 65.84 O ANISOU 475 O ILE A 110 8882 8173 7961 248 800 -1111 O ATOM 476 CB ILE A 110 9.668 21.127 8.045 1.00 65.39 C ANISOU 476 CB ILE A 110 8612 8286 7947 180 682 -982 C ATOM 477 CG1 ILE A 110 8.556 20.535 7.119 1.00 66.62 C ANISOU 477 CG1 ILE A 110 8604 8557 8151 200 648 -987 C ATOM 478 CG2 ILE A 110 9.569 20.583 9.480 1.00 66.47 C ANISOU 478 CG2 ILE A 110 8775 8491 7988 36 785 -1023 C ATOM 479 CD1 ILE A 110 7.046 20.795 7.497 1.00 76.36 C ANISOU 479 CD1 ILE A 110 9643 9952 9417 242 730 -1101 C ATOM 480 N ALA A 111 12.108 23.487 8.075 1.00 60.80 N ANISOU 480 N ALA A 111 8332 7375 7396 317 633 -958 N ATOM 481 CA ALA A 111 13.335 24.024 8.675 1.00 60.05 C ANISOU 481 CA ALA A 111 8373 7180 7261 266 638 -967 C ATOM 482 C ALA A 111 13.195 25.515 9.090 1.00 65.03 C ANISOU 482 C ALA A 111 9045 7723 7938 360 705 -1064 C ATOM 483 O ALA A 111 13.966 25.975 9.932 1.00 64.68 O ANISOU 483 O ALA A 111 9097 7631 7849 295 736 -1116 O ATOM 484 CB ALA A 111 14.505 23.853 7.718 1.00 59.42 C ANISOU 484 CB ALA A 111 8371 7011 7196 253 545 -869 C ATOM 485 N LEU A 112 12.222 26.256 8.517 1.00 63.10 N ANISOU 485 N LEU A 112 8732 7462 7781 515 724 -1095 N ATOM 486 CA LEU A 112 11.979 27.666 8.860 1.00 64.87 C ANISOU 486 CA LEU A 112 9003 7582 8061 631 795 -1188 C ATOM 487 C LEU A 112 11.321 27.821 10.238 1.00 71.27 C ANISOU 487 C LEU A 112 9770 8482 8826 602 909 -1322 C ATOM 488 O LEU A 112 11.464 28.873 10.860 1.00 71.78 O ANISOU 488 O LEU A 112 9913 8454 8906 642 980 -1420 O ATOM 489 CB LEU A 112 11.080 28.356 7.815 1.00 65.78 C ANISOU 489 CB LEU A 112 9055 7658 8279 837 772 -1167 C ATOM 490 CG LEU A 112 11.612 28.593 6.401 1.00 69.52 C ANISOU 490 CG LEU A 112 9595 8018 8800 909 676 -1043 C ATOM 491 CD1 LEU A 112 10.473 28.937 5.479 1.00 70.40 C ANISOU 491 CD1 LEU A 112 9604 8166 8979 1109 640 -1019 C ATOM 492 CD2 LEU A 112 12.642 29.717 6.363 1.00 72.14 C ANISOU 492 CD2 LEU A 112 10110 8138 9162 915 699 -1042 C ATOM 493 N LEU A 113 10.580 26.785 10.694 1.00 68.98 N ANISOU 493 N LEU A 113 9363 8370 8478 526 936 -1332 N ATOM 494 CA LEU A 113 9.825 26.760 11.952 1.00 70.58 C ANISOU 494 CA LEU A 113 9504 8691 8621 485 1056 -1452 C ATOM 495 C LEU A 113 10.678 27.092 13.180 1.00 76.52 C ANISOU 495 C LEU A 113 10391 9407 9274 372 1111 -1522 C ATOM 496 O LEU A 113 10.195 27.808 14.057 1.00 77.66 O ANISOU 496 O LEU A 113 10531 9576 9401 403 1220 -1654 O ATOM 497 CB LEU A 113 9.126 25.406 12.163 1.00 70.39 C ANISOU 497 CB LEU A 113 9357 8851 8537 374 1073 -1423 C ATOM 498 CG LEU A 113 8.085 24.976 11.113 1.00 75.11 C ANISOU 498 CG LEU A 113 9786 9535 9217 458 1030 -1388 C ATOM 499 CD1 LEU A 113 7.701 23.521 11.302 1.00 74.59 C ANISOU 499 CD1 LEU A 113 9645 9611 9084 295 1037 -1345 C ATOM 500 CD2 LEU A 113 6.843 25.873 11.133 1.00 79.22 C ANISOU 500 CD2 LEU A 113 10165 10117 9816 629 1103 -1503 C ATOM 501 N THR A 114 11.935 26.602 13.241 1.00 72.91 N ANISOU 501 N THR A 114 10047 8905 8752 252 1037 -1445 N ATOM 502 CA THR A 114 12.827 26.880 14.374 1.00 73.64 C ANISOU 502 CA THR A 114 10257 8985 8739 143 1066 -1512 C ATOM 503 C THR A 114 13.231 28.373 14.393 1.00 79.72 C ANISOU 503 C THR A 114 11121 9593 9576 218 1097 -1609 C ATOM 504 O THR A 114 13.419 28.935 15.475 1.00 80.55 O ANISOU 504 O THR A 114 11294 9700 9610 162 1166 -1731 O ATOM 505 CB THR A 114 14.052 25.935 14.388 1.00 81.93 C ANISOU 505 CB THR A 114 11378 10054 9699 11 967 -1403 C ATOM 506 OG1 THR A 114 14.751 26.092 15.624 1.00 84.31 O ANISOU 506 OG1 THR A 114 11770 10391 9875 -93 993 -1477 O ATOM 507 CG2 THR A 114 15.014 26.147 13.208 1.00 78.82 C ANISOU 507 CG2 THR A 114 11027 9534 9388 43 860 -1309 C ATOM 508 N ILE A 115 13.320 29.009 13.203 1.00 76.49 N ANISOU 508 N ILE A 115 10725 9040 9296 337 1050 -1558 N ATOM 509 CA ILE A 115 13.684 30.418 13.047 1.00 77.47 C ANISOU 509 CA ILE A 115 10960 8975 9501 411 1083 -1629 C ATOM 510 C ILE A 115 12.478 31.298 13.429 1.00 84.86 C ANISOU 510 C ILE A 115 11857 9889 10497 562 1196 -1756 C ATOM 511 O ILE A 115 12.642 32.234 14.211 1.00 86.13 O ANISOU 511 O ILE A 115 12112 9962 10653 559 1279 -1891 O ATOM 512 CB ILE A 115 14.211 30.717 11.606 1.00 79.49 C ANISOU 512 CB ILE A 115 11263 9083 9857 479 997 -1505 C ATOM 513 CG1 ILE A 115 15.365 29.767 11.216 1.00 77.97 C ANISOU 513 CG1 ILE A 115 11084 8935 9605 341 893 -1387 C ATOM 514 CG2 ILE A 115 14.639 32.185 11.448 1.00 81.11 C ANISOU 514 CG2 ILE A 115 11613 9065 10140 530 1044 -1570 C ATOM 515 CD1 ILE A 115 15.419 29.396 9.751 1.00 85.50 C ANISOU 515 CD1 ILE A 115 12007 9852 10626 412 805 -1242 C ATOM 516 N MET A 116 11.277 30.985 12.896 1.00 82.78 N ANISOU 516 N MET A 116 11449 9712 10291 693 1200 -1724 N ATOM 517 CA MET A 116 10.043 31.741 13.143 1.00 85.08 C ANISOU 517 CA MET A 116 11666 10011 10650 867 1299 -1838 C ATOM 518 C MET A 116 9.515 31.553 14.566 1.00 91.39 C ANISOU 518 C MET A 116 12414 10960 11351 791 1420 -1984 C ATOM 519 O MET A 116 9.046 32.521 15.168 1.00 93.05 O ANISOU 519 O MET A 116 12647 11116 11592 888 1528 -2130 O ATOM 520 CB MET A 116 8.943 31.352 12.143 1.00 87.57 C ANISOU 520 CB MET A 116 11810 10418 11043 1019 1251 -1763 C ATOM 521 CG MET A 116 9.246 31.744 10.717 1.00 90.92 C ANISOU 521 CG MET A 116 12288 10695 11562 1142 1146 -1634 C ATOM 522 SD MET A 116 7.867 31.461 9.577 1.00 96.17 S ANISOU 522 SD MET A 116 12747 11484 12309 1351 1084 -1571 S ATOM 523 CE MET A 116 7.927 29.675 9.418 1.00 90.98 C ANISOU 523 CE MET A 116 11964 11044 11561 1146 1011 -1482 C ATOM 524 N PHE A 117 9.569 30.316 15.091 1.00 87.87 N ANISOU 524 N PHE A 117 11907 10694 10784 623 1410 -1943 N ATOM 525 CA PHE A 117 9.065 29.987 16.427 1.00 89.31 C ANISOU 525 CA PHE A 117 12047 11039 10847 528 1527 -2059 C ATOM 526 C PHE A 117 10.236 29.716 17.395 1.00 94.53 C ANISOU 526 C PHE A 117 12852 11709 11356 331 1514 -2069 C ATOM 527 O PHE A 117 11.340 30.214 17.163 1.00 93.76 O ANISOU 527 O PHE A 117 12884 11468 11273 300 1445 -2046 O ATOM 528 CB PHE A 117 8.090 28.788 16.349 1.00 90.87 C ANISOU 528 CB PHE A 117 12067 11446 11014 487 1544 -2008 C ATOM 529 CG PHE A 117 6.921 28.993 15.409 1.00 93.08 C ANISOU 529 CG PHE A 117 12174 11761 11431 671 1539 -2004 C ATOM 530 CD1 PHE A 117 5.745 29.589 15.853 1.00 98.34 C ANISOU 530 CD1 PHE A 117 12711 12516 12137 796 1663 -2147 C ATOM 531 CD2 PHE A 117 6.998 28.594 14.078 1.00 93.66 C ANISOU 531 CD2 PHE A 117 12205 11796 11586 726 1409 -1864 C ATOM 532 CE1 PHE A 117 4.669 29.784 14.981 1.00100.05 C ANISOU 532 CE1 PHE A 117 12748 12791 12477 982 1645 -2147 C ATOM 533 CE2 PHE A 117 5.924 28.798 13.206 1.00 97.26 C ANISOU 533 CE2 PHE A 117 12494 12306 12153 902 1389 -1863 C ATOM 534 CZ PHE A 117 4.766 29.387 13.663 1.00 97.55 C ANISOU 534 CZ PHE A 117 12393 12440 12231 1033 1502 -2003 C ATOM 535 N GLU A 118 9.989 28.968 18.489 1.00 92.68 N ANISOU 535 N GLU A 118 12594 11650 10970 200 1583 -2106 N ATOM 536 CA GLU A 118 10.995 28.632 19.497 1.00 92.81 C ANISOU 536 CA GLU A 118 12737 11713 10815 26 1567 -2112 C ATOM 537 C GLU A 118 11.685 27.296 19.153 1.00 95.53 C ANISOU 537 C GLU A 118 13092 12113 11091 -91 1446 -1929 C ATOM 538 O GLU A 118 11.654 26.873 17.994 1.00 93.96 O ANISOU 538 O GLU A 118 12834 11869 10998 -38 1363 -1807 O ATOM 539 CB GLU A 118 10.346 28.585 20.892 1.00 96.11 C ANISOU 539 CB GLU A 118 13144 12288 11087 -43 1713 -2246 C ATOM 540 N ALA A 119 12.332 26.653 20.146 1.00 92.46 N ANISOU 540 N ALA A 119 12790 11820 10522 -239 1434 -1911 N ATOM 541 CA ALA A 119 13.029 25.377 19.966 1.00 90.99 C ANISOU 541 CA ALA A 119 12636 11681 10254 -338 1326 -1742 C ATOM 542 C ALA A 119 12.054 24.184 19.960 1.00 94.55 C ANISOU 542 C ALA A 119 13002 12250 10673 -382 1376 -1659 C ATOM 543 O ALA A 119 12.400 23.126 19.427 1.00 93.53 O ANISOU 543 O ALA A 119 12881 12117 10538 -427 1290 -1509 O ATOM 544 CB ALA A 119 14.074 25.192 21.055 1.00 92.21 C ANISOU 544 CB ALA A 119 12916 11902 10217 -458 1291 -1755 C ATOM 545 N MET A 120 10.840 24.359 20.538 1.00 91.44 N ANISOU 545 N MET A 120 12525 11957 10260 -375 1524 -1764 N ATOM 546 CA MET A 120 9.800 23.323 20.624 1.00 90.91 C ANISOU 546 CA MET A 120 12362 12016 10162 -441 1603 -1714 C ATOM 547 C MET A 120 9.223 22.976 19.243 1.00 91.37 C ANISOU 547 C MET A 120 12289 12035 10394 -365 1548 -1640 C ATOM 548 O MET A 120 9.215 23.822 18.345 1.00 90.32 O ANISOU 548 O MET A 120 12105 11801 10413 -222 1497 -1670 O ATOM 549 CB MET A 120 8.674 23.765 21.572 1.00 95.37 C ANISOU 549 CB MET A 120 12852 12711 10672 -446 1787 -1872 C ATOM 550 N TRP A 121 8.757 21.723 19.085 1.00 86.34 N ANISOU 550 N TRP A 121 11608 11475 9724 -468 1561 -1542 N ATOM 551 CA TRP A 121 8.177 21.180 17.850 1.00 84.77 C ANISOU 551 CA TRP A 121 11282 11267 9659 -434 1510 -1475 C ATOM 552 C TRP A 121 6.643 21.394 17.869 1.00 89.98 C ANISOU 552 C TRP A 121 11742 12063 10384 -400 1639 -1591 C ATOM 553 O TRP A 121 5.980 20.919 18.799 1.00 91.16 O ANISOU 553 O TRP A 121 11862 12346 10428 -522 1774 -1634 O ATOM 554 CB TRP A 121 8.566 19.691 17.715 1.00 82.27 C ANISOU 554 CB TRP A 121 11043 10950 9268 -579 1459 -1320 C ATOM 555 CG TRP A 121 8.021 18.949 16.532 1.00 82.27 C ANISOU 555 CG TRP A 121 10933 10945 9379 -584 1411 -1256 C ATOM 556 CD1 TRP A 121 7.072 17.973 16.553 1.00 85.98 C ANISOU 556 CD1 TRP A 121 11321 11513 9833 -708 1490 -1243 C ATOM 557 CD2 TRP A 121 8.509 19.003 15.184 1.00 80.57 C ANISOU 557 CD2 TRP A 121 10700 10623 9291 -484 1269 -1192 C ATOM 558 NE1 TRP A 121 6.880 17.470 15.288 1.00 84.44 N ANISOU 558 NE1 TRP A 121 11045 11284 9753 -687 1403 -1191 N ATOM 559 CE2 TRP A 121 7.753 18.082 14.428 1.00 84.47 C ANISOU 559 CE2 TRP A 121 11090 11166 9840 -544 1265 -1155 C ATOM 560 CE3 TRP A 121 9.473 19.787 14.525 1.00 80.47 C ANISOU 560 CE3 TRP A 121 10745 10483 9348 -357 1155 -1172 C ATOM 561 CZ2 TRP A 121 7.942 17.909 13.052 1.00 82.68 C ANISOU 561 CZ2 TRP A 121 10821 10872 9723 -473 1144 -1099 C ATOM 562 CZ3 TRP A 121 9.676 19.596 13.168 1.00 80.63 C ANISOU 562 CZ3 TRP A 121 10728 10432 9475 -289 1043 -1103 C ATOM 563 CH2 TRP A 121 8.914 18.669 12.446 1.00 81.33 C ANISOU 563 CH2 TRP A 121 10717 10579 9606 -341 1034 -1068 C ATOM 564 N PRO A 122 6.069 22.149 16.893 1.00 85.87 N ANISOU 564 N PRO A 122 11080 11519 10026 -231 1605 -1646 N ATOM 565 CA PRO A 122 4.614 22.410 16.929 1.00 87.14 C ANISOU 565 CA PRO A 122 11026 11832 10251 -175 1720 -1768 C ATOM 566 C PRO A 122 3.756 21.319 16.277 1.00 90.30 C ANISOU 566 C PRO A 122 11268 12349 10693 -262 1718 -1723 C ATOM 567 O PRO A 122 2.612 21.116 16.690 1.00 91.97 O ANISOU 567 O PRO A 122 11312 12732 10900 -308 1846 -1818 O ATOM 568 CB PRO A 122 4.473 23.734 16.176 1.00 89.07 C ANISOU 568 CB PRO A 122 11210 11989 10644 67 1668 -1837 C ATOM 569 CG PRO A 122 5.685 23.820 15.287 1.00 91.55 C ANISOU 569 CG PRO A 122 11668 12116 11000 109 1504 -1711 C ATOM 570 CD PRO A 122 6.713 22.819 15.742 1.00 85.89 C ANISOU 570 CD PRO A 122 11113 11366 10154 -78 1463 -1598 C ATOM 571 N LEU A 123 4.305 20.628 15.265 1.00 84.12 N ANISOU 571 N LEU A 123 10534 11479 9949 -292 1580 -1591 N ATOM 572 CA LEU A 123 3.669 19.559 14.493 1.00 83.56 C ANISOU 572 CA LEU A 123 10341 11489 9920 -385 1554 -1545 C ATOM 573 C LEU A 123 3.523 18.251 15.321 1.00 86.22 C ANISOU 573 C LEU A 123 10739 11894 10127 -638 1657 -1499 C ATOM 574 O LEU A 123 4.056 18.201 16.432 1.00 85.63 O ANISOU 574 O LEU A 123 10819 11796 9922 -718 1725 -1483 O ATOM 575 CB LEU A 123 4.535 19.312 13.238 1.00 81.86 C ANISOU 575 CB LEU A 123 10203 11131 9772 -328 1375 -1423 C ATOM 576 CG LEU A 123 4.109 20.037 11.960 1.00 86.92 C ANISOU 576 CG LEU A 123 10698 11774 10554 -130 1276 -1450 C ATOM 577 CD1 LEU A 123 4.592 21.481 11.949 1.00 87.08 C ANISOU 577 CD1 LEU A 123 10784 11678 10623 73 1245 -1483 C ATOM 578 CD2 LEU A 123 4.648 19.328 10.735 1.00 88.23 C ANISOU 578 CD2 LEU A 123 10903 11863 10757 -149 1133 -1336 C ATOM 579 N PRO A 124 2.828 17.180 14.829 1.00 82.25 N ANISOU 579 N PRO A 124 10133 11472 9647 -775 1673 -1478 N ATOM 580 CA PRO A 124 2.742 15.937 15.621 1.00 82.54 C ANISOU 580 CA PRO A 124 10266 11538 9558 -1024 1781 -1422 C ATOM 581 C PRO A 124 4.109 15.279 15.847 1.00 85.29 C ANISOU 581 C PRO A 124 10891 11708 9809 -1088 1701 -1263 C ATOM 582 O PRO A 124 5.029 15.444 15.037 1.00 83.57 O ANISOU 582 O PRO A 124 10752 11353 9646 -978 1547 -1188 O ATOM 583 CB PRO A 124 1.832 15.035 14.778 1.00 84.82 C ANISOU 583 CB PRO A 124 10390 11917 9922 -1139 1786 -1438 C ATOM 584 CG PRO A 124 1.113 15.954 13.861 1.00 89.52 C ANISOU 584 CG PRO A 124 10745 12608 10661 -945 1721 -1544 C ATOM 585 CD PRO A 124 2.093 17.034 13.555 1.00 83.60 C ANISOU 585 CD PRO A 124 10107 11710 9948 -722 1596 -1506 C ATOM 586 N LEU A 125 4.229 14.531 16.960 1.00 82.40 N ANISOU 586 N LEU A 125 10669 11352 9289 -1261 1812 -1211 N ATOM 587 CA LEU A 125 5.438 13.839 17.422 1.00 81.15 C ANISOU 587 CA LEU A 125 10775 11052 9006 -1324 1756 -1059 C ATOM 588 C LEU A 125 6.023 12.865 16.385 1.00 82.53 C ANISOU 588 C LEU A 125 11033 11086 9240 -1349 1630 -936 C ATOM 589 O LEU A 125 7.243 12.733 16.310 1.00 80.75 O ANISOU 589 O LEU A 125 10978 10725 8976 -1288 1515 -830 O ATOM 590 CB LEU A 125 5.158 13.068 18.737 1.00 83.13 C ANISOU 590 CB LEU A 125 11146 11363 9078 -1522 1919 -1022 C ATOM 591 CG LEU A 125 4.765 13.841 20.032 1.00 89.38 C ANISOU 591 CG LEU A 125 11926 12285 9748 -1527 2060 -1123 C ATOM 592 CD1 LEU A 125 5.641 15.074 20.279 1.00 88.32 C ANISOU 592 CD1 LEU A 125 11850 12104 9602 -1343 1964 -1161 C ATOM 593 CD2 LEU A 125 3.266 14.162 20.086 1.00 93.68 C ANISOU 593 CD2 LEU A 125 12219 13020 10356 -1569 2218 -1286 C ATOM 594 N VAL A 126 5.159 12.190 15.601 1.00 78.85 N ANISOU 594 N VAL A 126 10439 10659 8863 -1441 1652 -962 N ATOM 595 CA VAL A 126 5.548 11.206 14.584 1.00 77.37 C ANISOU 595 CA VAL A 126 10317 10346 8732 -1483 1552 -871 C ATOM 596 C VAL A 126 6.290 11.845 13.401 1.00 78.25 C ANISOU 596 C VAL A 126 10398 10377 8958 -1283 1371 -861 C ATOM 597 O VAL A 126 7.135 11.183 12.793 1.00 76.59 O ANISOU 597 O VAL A 126 10314 10027 8759 -1275 1269 -761 O ATOM 598 CB VAL A 126 4.321 10.418 14.079 1.00 82.59 C ANISOU 598 CB VAL A 126 10828 11098 9454 -1652 1635 -935 C ATOM 599 N LEU A 127 5.974 13.114 13.073 1.00 73.62 N ANISOU 599 N LEU A 127 9650 9870 8452 -1121 1341 -961 N ATOM 600 CA LEU A 127 6.575 13.835 11.948 1.00 71.39 C ANISOU 600 CA LEU A 127 9336 9517 8272 -933 1188 -953 C ATOM 601 C LEU A 127 7.994 14.359 12.247 1.00 72.63 C ANISOU 601 C LEU A 127 9671 9542 8383 -829 1104 -876 C ATOM 602 O LEU A 127 8.694 14.759 11.314 1.00 70.71 O ANISOU 602 O LEU A 127 9445 9214 8209 -707 980 -842 O ATOM 603 CB LEU A 127 5.669 14.999 11.530 1.00 72.17 C ANISOU 603 CB LEU A 127 9217 9737 8467 -791 1196 -1079 C ATOM 604 N CYS A 128 8.422 14.360 13.523 1.00 69.39 N ANISOU 604 N CYS A 128 9387 9128 7848 -881 1171 -855 N ATOM 605 CA CYS A 128 9.751 14.843 13.911 1.00 68.15 C ANISOU 605 CA CYS A 128 9381 8878 7634 -800 1093 -800 C ATOM 606 C CYS A 128 10.869 13.890 13.400 1.00 68.72 C ANISOU 606 C CYS A 128 9602 8821 7689 -815 982 -665 C ATOM 607 O CYS A 128 11.725 14.385 12.661 1.00 67.14 O ANISOU 607 O CYS A 128 9417 8545 7548 -699 869 -643 O ATOM 608 CB CYS A 128 9.848 15.088 15.416 1.00 70.07 C ANISOU 608 CB CYS A 128 9709 9180 7733 -855 1188 -826 C ATOM 609 SG CYS A 128 11.515 15.496 16.004 1.00 73.51 S ANISOU 609 SG CYS A 128 10323 9532 8073 -786 1085 -766 S ATOM 610 N PRO A 129 10.897 12.556 13.696 1.00 63.73 N ANISOU 610 N PRO A 129 9080 8152 6983 -947 1015 -576 N ATOM 611 CA PRO A 129 11.976 11.722 13.132 1.00 61.84 C ANISOU 611 CA PRO A 129 8975 7779 6741 -925 906 -458 C ATOM 612 C PRO A 129 11.856 11.551 11.608 1.00 62.85 C ANISOU 612 C PRO A 129 9015 7858 7007 -876 826 -468 C ATOM 613 O PRO A 129 12.872 11.323 10.946 1.00 60.68 O ANISOU 613 O PRO A 129 8812 7486 6758 -801 720 -403 O ATOM 614 CB PRO A 129 11.828 10.389 13.871 1.00 64.77 C ANISOU 614 CB PRO A 129 9491 8115 7003 -1076 984 -369 C ATOM 615 CG PRO A 129 10.417 10.340 14.292 1.00 70.87 C ANISOU 615 CG PRO A 129 10153 9000 7772 -1207 1132 -452 C ATOM 616 CD PRO A 129 9.997 11.752 14.554 1.00 66.62 C ANISOU 616 CD PRO A 129 9466 8583 7263 -1118 1158 -575 C ATOM 617 N ALA A 130 10.626 11.703 11.056 1.00 58.76 N ANISOU 617 N ALA A 130 8331 7426 6570 -912 876 -557 N ATOM 618 CA ALA A 130 10.328 11.607 9.622 1.00 57.30 C ANISOU 618 CA ALA A 130 8041 7232 6500 -871 803 -585 C ATOM 619 C ALA A 130 10.965 12.757 8.841 1.00 58.88 C ANISOU 619 C ALA A 130 8195 7408 6769 -690 696 -598 C ATOM 620 O ALA A 130 11.489 12.531 7.748 1.00 57.92 O ANISOU 620 O ALA A 130 8092 7218 6698 -636 602 -561 O ATOM 621 CB ALA A 130 8.823 11.600 9.396 1.00 59.13 C ANISOU 621 CB ALA A 130 8084 7600 6782 -946 882 -689 C ATOM 622 N TRP A 131 10.920 13.984 9.396 1.00 54.07 N ANISOU 622 N TRP A 131 7537 6847 6159 -603 720 -655 N ATOM 623 CA TRP A 131 11.506 15.163 8.760 1.00 52.43 C ANISOU 623 CA TRP A 131 7307 6600 6015 -445 639 -668 C ATOM 624 C TRP A 131 13.038 15.079 8.793 1.00 54.32 C ANISOU 624 C TRP A 131 7696 6728 6215 -412 561 -585 C ATOM 625 O TRP A 131 13.683 15.393 7.790 1.00 52.81 O ANISOU 625 O TRP A 131 7509 6475 6081 -326 475 -558 O ATOM 626 CB TRP A 131 11.003 16.463 9.425 1.00 51.51 C ANISOU 626 CB TRP A 131 7118 6546 5908 -372 702 -761 C ATOM 627 CG TRP A 131 11.801 17.679 9.055 1.00 51.40 C ANISOU 627 CG TRP A 131 7136 6454 5940 -233 639 -766 C ATOM 628 CD1 TRP A 131 11.868 18.275 7.830 1.00 53.79 C ANISOU 628 CD1 TRP A 131 7391 6714 6332 -116 564 -758 C ATOM 629 CD2 TRP A 131 12.695 18.407 9.906 1.00 50.95 C ANISOU 629 CD2 TRP A 131 7177 6349 5833 -214 648 -778 C ATOM 630 NE1 TRP A 131 12.730 19.348 7.871 1.00 52.82 N ANISOU 630 NE1 TRP A 131 7339 6505 6225 -31 538 -761 N ATOM 631 CE2 TRP A 131 13.252 19.453 9.134 1.00 54.37 C ANISOU 631 CE2 TRP A 131 7618 6700 6341 -94 587 -782 C ATOM 632 CE3 TRP A 131 13.068 18.292 11.259 1.00 52.48 C ANISOU 632 CE3 TRP A 131 7456 6568 5916 -292 703 -790 C ATOM 633 CZ2 TRP A 131 14.171 20.368 9.664 1.00 53.30 C ANISOU 633 CZ2 TRP A 131 7566 6500 6186 -68 585 -809 C ATOM 634 CZ3 TRP A 131 13.976 19.202 11.784 1.00 53.50 C ANISOU 634 CZ3 TRP A 131 7659 6652 6017 -254 687 -821 C ATOM 635 CH2 TRP A 131 14.516 20.225 10.991 1.00 53.49 C ANISOU 635 CH2 TRP A 131 7658 6564 6104 -151 632 -836 C ATOM 636 N LEU A 132 13.611 14.645 9.937 1.00 50.36 N ANISOU 636 N LEU A 132 7311 6215 5609 -480 591 -544 N ATOM 637 CA LEU A 132 15.059 14.500 10.104 1.00 49.24 C ANISOU 637 CA LEU A 132 7293 5999 5418 -448 515 -471 C ATOM 638 C LEU A 132 15.594 13.434 9.152 1.00 53.05 C ANISOU 638 C LEU A 132 7827 6402 5929 -448 443 -391 C ATOM 639 O LEU A 132 16.647 13.640 8.544 1.00 51.55 O ANISOU 639 O LEU A 132 7664 6155 5765 -372 360 -359 O ATOM 640 CB LEU A 132 15.432 14.169 11.560 1.00 49.84 C ANISOU 640 CB LEU A 132 7477 6104 5358 -515 557 -442 C ATOM 641 CG LEU A 132 15.233 15.279 12.605 1.00 54.45 C ANISOU 641 CG LEU A 132 8039 6761 5889 -509 618 -530 C ATOM 642 CD1 LEU A 132 15.100 14.690 14.002 1.00 55.73 C ANISOU 642 CD1 LEU A 132 8293 6982 5900 -608 692 -505 C ATOM 643 CD2 LEU A 132 16.367 16.287 12.571 1.00 54.17 C ANISOU 643 CD2 LEU A 132 8026 6695 5862 -427 544 -553 C ATOM 644 N PHE A 133 14.833 12.325 8.979 1.00 50.83 N ANISOU 644 N PHE A 133 7551 6115 5646 -541 484 -370 N ATOM 645 CA PHE A 133 15.165 11.228 8.070 1.00 50.23 C ANISOU 645 CA PHE A 133 7531 5954 5600 -555 433 -312 C ATOM 646 C PHE A 133 15.205 11.728 6.618 1.00 53.33 C ANISOU 646 C PHE A 133 7831 6340 6093 -468 362 -346 C ATOM 647 O PHE A 133 16.170 11.425 5.917 1.00 52.62 O ANISOU 647 O PHE A 133 7796 6179 6019 -410 290 -300 O ATOM 648 CB PHE A 133 14.175 10.047 8.220 1.00 53.19 C ANISOU 648 CB PHE A 133 7928 6325 5957 -698 512 -308 C ATOM 649 CG PHE A 133 14.297 8.977 7.156 1.00 54.90 C ANISOU 649 CG PHE A 133 8188 6452 6219 -726 473 -280 C ATOM 650 CD1 PHE A 133 15.356 8.075 7.171 1.00 58.26 C ANISOU 650 CD1 PHE A 133 8771 6755 6609 -702 431 -190 C ATOM 651 CD2 PHE A 133 13.367 8.889 6.125 1.00 57.38 C ANISOU 651 CD2 PHE A 133 8383 6811 6609 -766 474 -353 C ATOM 652 CE1 PHE A 133 15.486 7.106 6.170 1.00 59.34 C ANISOU 652 CE1 PHE A 133 8957 6798 6791 -720 402 -179 C ATOM 653 CE2 PHE A 133 13.500 7.925 5.121 1.00 60.37 C ANISOU 653 CE2 PHE A 133 8807 7109 7023 -798 438 -345 C ATOM 654 CZ PHE A 133 14.555 7.036 5.153 1.00 58.67 C ANISOU 654 CZ PHE A 133 8760 6755 6777 -777 409 -261 C ATOM 655 N LEU A 134 14.170 12.483 6.171 1.00 49.73 N ANISOU 655 N LEU A 134 7235 5965 5696 -451 384 -424 N ATOM 656 CA LEU A 134 14.101 13.009 4.801 1.00 49.04 C ANISOU 656 CA LEU A 134 7064 5883 5685 -362 316 -448 C ATOM 657 C LEU A 134 15.210 14.018 4.538 1.00 51.81 C ANISOU 657 C LEU A 134 7449 6186 6052 -245 258 -424 C ATOM 658 O LEU A 134 15.745 14.056 3.433 1.00 51.43 O ANISOU 658 O LEU A 134 7406 6098 6036 -186 193 -400 O ATOM 659 CB LEU A 134 12.734 13.644 4.487 1.00 49.84 C ANISOU 659 CB LEU A 134 7006 6095 5836 -346 344 -531 C ATOM 660 CG LEU A 134 11.513 12.711 4.440 1.00 55.50 C ANISOU 660 CG LEU A 134 7643 6889 6555 -472 396 -579 C ATOM 661 CD1 LEU A 134 10.248 13.505 4.197 1.00 56.23 C ANISOU 661 CD1 LEU A 134 7551 7119 6696 -428 419 -669 C ATOM 662 CD2 LEU A 134 11.660 11.614 3.380 1.00 57.31 C ANISOU 662 CD2 LEU A 134 7901 7074 6800 -521 341 -561 C ATOM 663 N ASP A 135 15.570 14.809 5.556 1.00 47.78 N ANISOU 663 N ASP A 135 6964 5681 5510 -226 288 -437 N ATOM 664 CA ASP A 135 16.636 15.801 5.480 1.00 46.72 C ANISOU 664 CA ASP A 135 6864 5501 5386 -147 250 -429 C ATOM 665 C ASP A 135 17.968 15.116 5.159 1.00 50.07 C ANISOU 665 C ASP A 135 7373 5864 5786 -143 187 -361 C ATOM 666 O ASP A 135 18.634 15.513 4.204 1.00 49.31 O ANISOU 666 O ASP A 135 7275 5732 5730 -81 139 -346 O ATOM 667 CB ASP A 135 16.721 16.593 6.799 1.00 48.84 C ANISOU 667 CB ASP A 135 7153 5797 5609 -160 302 -472 C ATOM 668 CG ASP A 135 17.638 17.796 6.763 1.00 56.56 C ANISOU 668 CG ASP A 135 8153 6731 6608 -97 280 -494 C ATOM 669 OD1 ASP A 135 18.819 17.632 6.422 1.00 55.93 O ANISOU 669 OD1 ASP A 135 8119 6608 6523 -86 223 -451 O ATOM 670 OD2 ASP A 135 17.194 18.883 7.152 1.00 65.14 O ANISOU 670 OD2 ASP A 135 9211 7826 7712 -68 329 -562 O ATOM 671 N VAL A 136 18.335 14.074 5.930 1.00 46.73 N ANISOU 671 N VAL A 136 7027 5433 5297 -201 192 -317 N ATOM 672 CA VAL A 136 19.579 13.325 5.730 1.00 45.80 C ANISOU 672 CA VAL A 136 6985 5263 5153 -177 132 -254 C ATOM 673 C VAL A 136 19.508 12.546 4.402 1.00 48.42 C ANISOU 673 C VAL A 136 7314 5548 5535 -162 100 -234 C ATOM 674 O VAL A 136 20.485 12.553 3.664 1.00 47.58 O ANISOU 674 O VAL A 136 7219 5411 5450 -102 50 -214 O ATOM 675 CB VAL A 136 19.909 12.397 6.937 1.00 50.07 C ANISOU 675 CB VAL A 136 7625 5801 5600 -222 143 -201 C ATOM 676 CG1 VAL A 136 21.241 11.674 6.736 1.00 49.72 C ANISOU 676 CG1 VAL A 136 7648 5709 5533 -165 72 -137 C ATOM 677 CG2 VAL A 136 19.928 13.179 8.250 1.00 50.06 C ANISOU 677 CG2 VAL A 136 7627 5865 5530 -243 173 -232 C ATOM 678 N LEU A 137 18.348 11.923 4.088 1.00 45.20 N ANISOU 678 N LEU A 137 6883 5147 5145 -223 135 -253 N ATOM 679 CA LEU A 137 18.117 11.126 2.878 1.00 44.94 C ANISOU 679 CA LEU A 137 6847 5079 5149 -231 110 -254 C ATOM 680 C LEU A 137 18.345 11.918 1.583 1.00 49.60 C ANISOU 680 C LEU A 137 7373 5684 5789 -150 61 -275 C ATOM 681 O LEU A 137 19.145 11.497 0.745 1.00 49.58 O ANISOU 681 O LEU A 137 7409 5638 5793 -111 21 -253 O ATOM 682 CB LEU A 137 16.688 10.534 2.869 1.00 45.60 C ANISOU 682 CB LEU A 137 6886 5198 5241 -334 161 -297 C ATOM 683 CG LEU A 137 16.261 9.725 1.624 1.00 50.25 C ANISOU 683 CG LEU A 137 7458 5771 5863 -366 138 -326 C ATOM 684 CD1 LEU A 137 17.019 8.425 1.520 1.00 50.77 C ANISOU 684 CD1 LEU A 137 7657 5722 5909 -394 132 -281 C ATOM 685 CD2 LEU A 137 14.776 9.432 1.644 1.00 53.00 C ANISOU 685 CD2 LEU A 137 7715 6197 6226 -472 186 -392 C ATOM 686 N PHE A 138 17.626 13.032 1.408 1.00 45.88 N ANISOU 686 N PHE A 138 6813 5272 5346 -118 69 -315 N ATOM 687 CA PHE A 138 17.697 13.821 0.189 1.00 45.07 C ANISOU 687 CA PHE A 138 6665 5181 5278 -38 27 -321 C ATOM 688 C PHE A 138 19.008 14.591 0.065 1.00 48.12 C ANISOU 688 C PHE A 138 7094 5522 5666 25 8 -289 C ATOM 689 O PHE A 138 19.503 14.736 -1.055 1.00 47.72 O ANISOU 689 O PHE A 138 7050 5457 5625 71 -25 -272 O ATOM 690 CB PHE A 138 16.489 14.758 0.083 1.00 47.30 C ANISOU 690 CB PHE A 138 6848 5532 5590 -4 40 -365 C ATOM 691 CG PHE A 138 15.150 14.059 0.018 1.00 49.85 C ANISOU 691 CG PHE A 138 7091 5931 5917 -70 57 -414 C ATOM 692 CD1 PHE A 138 14.954 12.967 -0.826 1.00 53.47 C ANISOU 692 CD1 PHE A 138 7555 6395 6368 -126 28 -423 C ATOM 693 CD2 PHE A 138 14.073 14.514 0.768 1.00 52.88 C ANISOU 693 CD2 PHE A 138 7389 6390 6315 -83 106 -464 C ATOM 694 CE1 PHE A 138 13.721 12.313 -0.875 1.00 55.35 C ANISOU 694 CE1 PHE A 138 7709 6709 6610 -213 48 -483 C ATOM 695 CE2 PHE A 138 12.834 13.867 0.706 1.00 56.78 C ANISOU 695 CE2 PHE A 138 7786 6975 6814 -160 128 -521 C ATOM 696 CZ PHE A 138 12.666 12.775 -0.117 1.00 55.17 C ANISOU 696 CZ PHE A 138 7586 6775 6603 -233 97 -530 C ATOM 697 N SER A 139 19.592 15.050 1.191 1.00 44.11 N ANISOU 697 N SER A 139 6615 5004 5141 15 31 -286 N ATOM 698 CA SER A 139 20.867 15.779 1.149 1.00 43.06 C ANISOU 698 CA SER A 139 6509 4843 5010 49 17 -271 C ATOM 699 C SER A 139 22.038 14.850 0.801 1.00 45.64 C ANISOU 699 C SER A 139 6877 5148 5317 55 -18 -236 C ATOM 700 O SER A 139 22.950 15.295 0.100 1.00 45.61 O ANISOU 700 O SER A 139 6870 5132 5326 87 -32 -227 O ATOM 701 CB SER A 139 21.140 16.492 2.463 1.00 46.08 C ANISOU 701 CB SER A 139 6902 5236 5372 26 46 -297 C ATOM 702 OG SER A 139 20.032 17.283 2.855 1.00 53.29 O ANISOU 702 OG SER A 139 7778 6166 6306 33 88 -341 O ATOM 703 N THR A 140 22.005 13.571 1.276 1.00 40.28 N ANISOU 703 N THR A 140 6239 4459 4606 25 -24 -216 N ATOM 704 CA THR A 140 23.018 12.540 0.991 1.00 39.86 C ANISOU 704 CA THR A 140 6232 4375 4537 52 -56 -183 C ATOM 705 C THR A 140 22.904 12.095 -0.483 1.00 44.34 C ANISOU 705 C THR A 140 6795 4920 5132 75 -69 -190 C ATOM 706 O THR A 140 23.928 11.862 -1.132 1.00 44.16 O ANISOU 706 O THR A 140 6780 4887 5111 122 -88 -182 O ATOM 707 CB THR A 140 22.863 11.347 1.962 1.00 44.76 C ANISOU 707 CB THR A 140 6925 4967 5115 21 -50 -151 C ATOM 708 OG1 THR A 140 23.066 11.805 3.294 1.00 42.69 O ANISOU 708 OG1 THR A 140 6670 4742 4806 4 -44 -144 O ATOM 709 CG2 THR A 140 23.826 10.198 1.669 1.00 42.32 C ANISOU 709 CG2 THR A 140 6679 4607 4795 73 -82 -115 C ATOM 710 N ALA A 141 21.658 11.975 -0.997 1.00 40.92 N ANISOU 710 N ALA A 141 6340 4496 4712 41 -57 -215 N ATOM 711 CA ALA A 141 21.372 11.588 -2.376 1.00 41.00 C ANISOU 711 CA ALA A 141 6341 4505 4731 52 -75 -234 C ATOM 712 C ALA A 141 21.977 12.580 -3.375 1.00 45.30 C ANISOU 712 C ALA A 141 6858 5072 5281 112 -89 -228 C ATOM 713 O ALA A 141 22.564 12.148 -4.372 1.00 44.47 O ANISOU 713 O ALA A 141 6773 4958 5165 139 -102 -230 O ATOM 714 CB ALA A 141 19.871 11.469 -2.593 1.00 41.97 C ANISOU 714 CB ALA A 141 6418 4667 4861 -1 -69 -272 C ATOM 715 N SER A 142 21.886 13.898 -3.077 1.00 42.33 N ANISOU 715 N SER A 142 6449 4715 4920 131 -77 -221 N ATOM 716 CA SER A 142 22.412 14.949 -3.948 1.00 42.36 C ANISOU 716 CA SER A 142 6448 4720 4927 176 -76 -205 C ATOM 717 C SER A 142 23.944 14.903 -4.048 1.00 46.20 C ANISOU 717 C SER A 142 6954 5193 5406 184 -67 -192 C ATOM 718 O SER A 142 24.477 15.194 -5.116 1.00 46.32 O ANISOU 718 O SER A 142 6977 5213 5411 207 -61 -180 O ATOM 719 CB SER A 142 21.938 16.330 -3.502 1.00 45.95 C ANISOU 719 CB SER A 142 6884 5170 5404 191 -55 -204 C ATOM 720 OG SER A 142 22.570 16.781 -2.316 1.00 57.12 O ANISOU 720 OG SER A 142 8306 6569 6828 162 -30 -214 O ATOM 721 N ILE A 143 24.640 14.495 -2.965 1.00 42.35 N ANISOU 721 N ILE A 143 6470 4702 4918 168 -68 -194 N ATOM 722 CA ILE A 143 26.103 14.390 -2.954 1.00 42.16 C ANISOU 722 CA ILE A 143 6436 4693 4889 184 -68 -193 C ATOM 723 C ILE A 143 26.538 13.129 -3.735 1.00 46.27 C ANISOU 723 C ILE A 143 6976 5206 5397 222 -82 -194 C ATOM 724 O ILE A 143 27.440 13.218 -4.575 1.00 45.89 O ANISOU 724 O ILE A 143 6911 5179 5347 247 -68 -200 O ATOM 725 CB ILE A 143 26.700 14.431 -1.514 1.00 45.11 C ANISOU 725 CB ILE A 143 6798 5089 5254 168 -79 -198 C ATOM 726 CG1 ILE A 143 26.251 15.719 -0.758 1.00 45.77 C ANISOU 726 CG1 ILE A 143 6870 5172 5346 124 -56 -216 C ATOM 727 CG2 ILE A 143 28.236 14.345 -1.561 1.00 44.77 C ANISOU 727 CG2 ILE A 143 6714 5089 5206 191 -89 -207 C ATOM 728 CD1 ILE A 143 26.298 15.637 0.785 1.00 53.18 C ANISOU 728 CD1 ILE A 143 7812 6139 6254 98 -68 -228 C ATOM 729 N TRP A 144 25.882 11.976 -3.484 1.00 42.67 N ANISOU 729 N TRP A 144 6563 4715 4935 220 -98 -194 N ATOM 730 CA TRP A 144 26.205 10.715 -4.155 1.00 42.69 C ANISOU 730 CA TRP A 144 6606 4684 4931 255 -104 -205 C ATOM 731 C TRP A 144 25.809 10.703 -5.646 1.00 46.13 C ANISOU 731 C TRP A 144 7045 5128 5356 254 -96 -232 C ATOM 732 O TRP A 144 26.406 9.941 -6.410 1.00 45.44 O ANISOU 732 O TRP A 144 6981 5026 5257 292 -91 -255 O ATOM 733 CB TRP A 144 25.579 9.535 -3.422 1.00 41.85 C ANISOU 733 CB TRP A 144 6566 4515 4820 234 -112 -196 C ATOM 734 CG TRP A 144 26.399 9.109 -2.249 1.00 43.29 C ANISOU 734 CG TRP A 144 6773 4684 4991 275 -128 -162 C ATOM 735 CD1 TRP A 144 26.267 9.530 -0.959 1.00 46.29 C ANISOU 735 CD1 TRP A 144 7149 5087 5352 249 -136 -135 C ATOM 736 CD2 TRP A 144 27.538 8.241 -2.275 1.00 43.92 C ANISOU 736 CD2 TRP A 144 6880 4738 5068 363 -145 -153 C ATOM 737 NE1 TRP A 144 27.226 8.938 -0.167 1.00 46.44 N ANISOU 737 NE1 TRP A 144 7196 5102 5346 314 -166 -102 N ATOM 738 CE2 TRP A 144 28.021 8.143 -0.950 1.00 48.23 C ANISOU 738 CE2 TRP A 144 7440 5298 5589 393 -174 -110 C ATOM 739 CE3 TRP A 144 28.187 7.512 -3.289 1.00 45.59 C ANISOU 739 CE3 TRP A 144 7109 4922 5293 429 -138 -181 C ATOM 740 CZ2 TRP A 144 29.119 7.345 -0.610 1.00 48.39 C ANISOU 740 CZ2 TRP A 144 7482 5307 5598 501 -206 -86 C ATOM 741 CZ3 TRP A 144 29.281 6.732 -2.952 1.00 48.04 C ANISOU 741 CZ3 TRP A 144 7440 5213 5603 536 -159 -166 C ATOM 742 CH2 TRP A 144 29.733 6.649 -1.627 1.00 49.14 C ANISOU 742 CH2 TRP A 144 7584 5367 5718 577 -197 -115 C ATOM 743 N HIS A 145 24.837 11.545 -6.066 1.00 43.09 N ANISOU 743 N HIS A 145 6636 4772 4965 224 -98 -231 N ATOM 744 CA HIS A 145 24.454 11.636 -7.479 1.00 43.75 C ANISOU 744 CA HIS A 145 6722 4884 5016 231 -103 -250 C ATOM 745 C HIS A 145 25.593 12.252 -8.286 1.00 48.63 C ANISOU 745 C HIS A 145 7334 5530 5614 267 -76 -237 C ATOM 746 O HIS A 145 25.943 11.714 -9.334 1.00 49.02 O ANISOU 746 O HIS A 145 7404 5592 5628 287 -68 -263 O ATOM 747 CB HIS A 145 23.165 12.438 -7.681 1.00 44.55 C ANISOU 747 CB HIS A 145 6794 5022 5112 215 -123 -244 C ATOM 748 CG HIS A 145 21.931 11.598 -7.710 1.00 48.35 C ANISOU 748 CG HIS A 145 7268 5514 5589 170 -148 -285 C ATOM 749 ND1 HIS A 145 21.182 11.375 -6.569 1.00 50.05 N ANISOU 749 ND1 HIS A 145 7465 5718 5835 122 -142 -292 N ATOM 750 CD2 HIS A 145 21.344 10.964 -8.749 1.00 50.72 C ANISOU 750 CD2 HIS A 145 7574 5844 5852 153 -172 -330 C ATOM 751 CE1 HIS A 145 20.172 10.611 -6.947 1.00 50.03 C ANISOU 751 CE1 HIS A 145 7451 5737 5822 70 -159 -340 C ATOM 752 NE2 HIS A 145 20.234 10.328 -8.246 1.00 50.81 N ANISOU 752 NE2 HIS A 145 7563 5862 5881 86 -182 -369 N ATOM 753 N LEU A 146 26.207 13.335 -7.765 1.00 45.31 N ANISOU 753 N LEU A 146 6886 5117 5212 264 -53 -207 N ATOM 754 CA LEU A 146 27.338 14.031 -8.391 1.00 45.90 C ANISOU 754 CA LEU A 146 6948 5219 5273 271 -11 -196 C ATOM 755 C LEU A 146 28.548 13.109 -8.494 1.00 51.56 C ANISOU 755 C LEU A 146 7644 5955 5990 301 5 -229 C ATOM 756 O LEU A 146 29.264 13.145 -9.496 1.00 51.53 O ANISOU 756 O LEU A 146 7635 5987 5956 313 44 -242 O ATOM 757 CB LEU A 146 27.701 15.315 -7.621 1.00 45.72 C ANISOU 757 CB LEU A 146 6902 5189 5280 237 15 -173 C ATOM 758 CG LEU A 146 26.628 16.418 -7.546 1.00 49.88 C ANISOU 758 CG LEU A 146 7455 5684 5814 227 13 -141 C ATOM 759 CD1 LEU A 146 27.245 17.713 -7.154 1.00 50.14 C ANISOU 759 CD1 LEU A 146 7489 5693 5870 187 61 -128 C ATOM 760 CD2 LEU A 146 25.938 16.638 -8.882 1.00 52.17 C ANISOU 760 CD2 LEU A 146 7784 5981 6055 258 5 -113 C ATOM 761 N CYS A 147 28.735 12.252 -7.474 1.00 48.98 N ANISOU 761 N CYS A 147 7311 5607 5693 322 -23 -241 N ATOM 762 CA CYS A 147 29.779 11.234 -7.401 1.00 49.58 C ANISOU 762 CA CYS A 147 7373 5691 5777 383 -22 -268 C ATOM 763 C CYS A 147 29.557 10.196 -8.517 1.00 52.69 C ANISOU 763 C CYS A 147 7818 6057 6145 416 -13 -305 C ATOM 764 O CYS A 147 30.516 9.798 -9.174 1.00 53.37 O ANISOU 764 O CYS A 147 7884 6173 6221 466 18 -340 O ATOM 765 CB CYS A 147 29.783 10.586 -6.019 1.00 50.44 C ANISOU 765 CB CYS A 147 7491 5765 5907 405 -64 -253 C ATOM 766 SG CYS A 147 31.044 9.307 -5.801 1.00 55.73 S ANISOU 766 SG CYS A 147 8153 6435 6587 518 -77 -272 S ATOM 767 N ALA A 148 28.286 9.785 -8.738 1.00 47.64 N ANISOU 767 N ALA A 148 7238 5371 5493 382 -36 -311 N ATOM 768 CA ALA A 148 27.881 8.833 -9.774 1.00 47.15 C ANISOU 768 CA ALA A 148 7232 5284 5400 388 -32 -362 C ATOM 769 C ALA A 148 27.963 9.466 -11.179 1.00 49.76 C ANISOU 769 C ALA A 148 7553 5685 5670 382 -6 -377 C ATOM 770 O ALA A 148 28.355 8.777 -12.113 1.00 50.11 O ANISOU 770 O ALA A 148 7623 5736 5680 411 20 -430 O ATOM 771 CB ALA A 148 26.470 8.328 -9.506 1.00 47.66 C ANISOU 771 CB ALA A 148 7341 5301 5468 328 -65 -372 C ATOM 772 N ILE A 149 27.610 10.763 -11.326 1.00 44.79 N ANISOU 772 N ILE A 149 6896 5099 5022 349 -6 -328 N ATOM 773 CA ILE A 149 27.688 11.494 -12.604 1.00 45.08 C ANISOU 773 CA ILE A 149 6944 5197 4988 345 21 -317 C ATOM 774 C ILE A 149 29.168 11.597 -13.029 1.00 51.03 C ANISOU 774 C ILE A 149 7669 5990 5731 368 90 -330 C ATOM 775 O ILE A 149 29.480 11.398 -14.206 1.00 51.80 O ANISOU 775 O ILE A 149 7790 6132 5760 379 127 -360 O ATOM 776 CB ILE A 149 26.990 12.899 -12.527 1.00 47.37 C ANISOU 776 CB ILE A 149 7232 5500 5269 321 7 -247 C ATOM 777 CG1 ILE A 149 25.449 12.764 -12.419 1.00 47.49 C ANISOU 777 CG1 ILE A 149 7255 5512 5279 311 -60 -251 C ATOM 778 CG2 ILE A 149 27.360 13.791 -13.719 1.00 47.64 C ANISOU 778 CG2 ILE A 149 7296 5580 5226 322 49 -210 C ATOM 779 CD1 ILE A 149 24.728 13.902 -11.671 1.00 53.08 C ANISOU 779 CD1 ILE A 149 7941 6206 6021 307 -80 -196 C ATOM 780 N SER A 150 30.067 11.883 -12.054 1.00 47.21 N ANISOU 780 N SER A 150 7125 5504 5308 372 108 -317 N ATOM 781 CA SER A 150 31.514 12.020 -12.244 1.00 47.27 C ANISOU 781 CA SER A 150 7070 5572 5320 385 172 -339 C ATOM 782 C SER A 150 32.145 10.719 -12.732 1.00 52.68 C ANISOU 782 C SER A 150 7751 6268 5997 459 191 -411 C ATOM 783 O SER A 150 32.919 10.753 -13.688 1.00 54.04 O ANISOU 783 O SER A 150 7898 6506 6127 469 259 -445 O ATOM 784 CB SER A 150 32.187 12.457 -10.945 1.00 50.12 C ANISOU 784 CB SER A 150 7355 5941 5746 374 163 -325 C ATOM 785 OG SER A 150 31.697 13.707 -10.490 1.00 57.53 O ANISOU 785 OG SER A 150 8304 6859 6696 305 159 -273 O ATOM 786 N VAL A 151 31.831 9.581 -12.072 1.00 49.17 N ANISOU 786 N VAL A 151 7338 5754 5591 511 141 -435 N ATOM 787 CA VAL A 151 32.368 8.257 -12.418 1.00 50.28 C ANISOU 787 CA VAL A 151 7498 5869 5736 597 156 -505 C ATOM 788 C VAL A 151 31.866 7.867 -13.831 1.00 55.94 C ANISOU 788 C VAL A 151 8287 6590 6378 581 185 -558 C ATOM 789 O VAL A 151 32.667 7.415 -14.647 1.00 56.64 O ANISOU 789 O VAL A 151 8366 6716 6437 633 243 -623 O ATOM 790 CB VAL A 151 32.038 7.191 -11.327 1.00 53.80 C ANISOU 790 CB VAL A 151 7993 6210 6239 648 100 -500 C ATOM 791 CG1 VAL A 151 32.328 5.766 -11.802 1.00 54.55 C ANISOU 791 CG1 VAL A 151 8153 6235 6338 735 119 -572 C ATOM 792 CG2 VAL A 151 32.802 7.477 -10.040 1.00 53.23 C ANISOU 792 CG2 VAL A 151 7843 6164 6217 687 73 -458 C ATOM 793 N ASP A 152 30.574 8.125 -14.129 1.00 52.72 N ANISOU 793 N ASP A 152 7938 6161 5931 512 144 -537 N ATOM 794 CA ASP A 152 29.934 7.867 -15.422 1.00 53.28 C ANISOU 794 CA ASP A 152 8072 6258 5914 485 149 -586 C ATOM 795 C ASP A 152 30.629 8.652 -16.551 1.00 57.41 C ANISOU 795 C ASP A 152 8575 6886 6351 478 217 -580 C ATOM 796 O ASP A 152 30.917 8.083 -17.612 1.00 58.09 O ANISOU 796 O ASP A 152 8698 7009 6365 496 258 -652 O ATOM 797 CB ASP A 152 28.445 8.241 -15.356 1.00 54.94 C ANISOU 797 CB ASP A 152 8314 6459 6104 417 79 -553 C ATOM 798 CG ASP A 152 27.580 7.538 -16.379 1.00 71.70 C ANISOU 798 CG ASP A 152 10499 8596 8148 388 56 -629 C ATOM 799 OD1 ASP A 152 27.340 6.314 -16.217 1.00 73.92 O ANISOU 799 OD1 ASP A 152 10828 8799 8459 385 47 -704 O ATOM 800 OD2 ASP A 152 27.100 8.216 -17.317 1.00 78.25 O ANISOU 800 OD2 ASP A 152 11337 9513 8883 364 42 -612 O ATOM 801 N ARG A 153 30.925 9.945 -16.295 1.00 52.36 N ANISOU 801 N ARG A 153 7889 6289 5718 445 237 -499 N ATOM 802 CA ARG A 153 31.580 10.857 -17.229 1.00 52.40 C ANISOU 802 CA ARG A 153 7887 6378 5643 416 314 -473 C ATOM 803 C ARG A 153 33.018 10.429 -17.516 1.00 57.57 C ANISOU 803 C ARG A 153 8478 7090 6305 455 405 -538 C ATOM 804 O ARG A 153 33.468 10.561 -18.655 1.00 58.17 O ANISOU 804 O ARG A 153 8571 7242 6288 442 481 -562 O ATOM 805 CB ARG A 153 31.532 12.291 -16.693 1.00 51.45 C ANISOU 805 CB ARG A 153 7748 6254 5547 361 317 -373 C ATOM 806 CG ARG A 153 30.676 13.259 -17.524 1.00 62.69 C ANISOU 806 CG ARG A 153 9251 7698 6871 326 311 -300 C ATOM 807 CD ARG A 153 29.202 12.888 -17.648 1.00 68.85 C ANISOU 807 CD ARG A 153 10082 8456 7621 344 209 -297 C ATOM 808 NE ARG A 153 28.882 12.476 -19.017 1.00 78.53 N ANISOU 808 NE ARG A 153 11369 9751 8717 354 207 -336 N ATOM 809 CZ ARG A 153 28.557 11.238 -19.381 1.00 91.68 C ANISOU 809 CZ ARG A 153 13048 11422 10363 370 174 -434 C ATOM 810 NH1 ARG A 153 28.460 10.275 -18.472 1.00 80.58 N ANISOU 810 NH1 ARG A 153 11611 9944 9062 380 143 -490 N ATOM 811 NH2 ARG A 153 28.299 10.960 -20.650 1.00 74.95 N ANISOU 811 NH2 ARG A 153 10987 9379 8113 370 174 -478 N ATOM 812 N TYR A 154 33.726 9.889 -16.500 1.00 54.19 N ANISOU 812 N TYR A 154 7974 6637 5978 509 396 -568 N ATOM 813 CA TYR A 154 35.092 9.378 -16.653 1.00 54.93 C ANISOU 813 CA TYR A 154 7983 6797 6093 573 471 -640 C ATOM 814 C TYR A 154 35.079 8.136 -17.554 1.00 59.78 C ANISOU 814 C TYR A 154 8655 7396 6662 646 495 -740 C ATOM 815 O TYR A 154 35.934 8.021 -18.437 1.00 60.56 O ANISOU 815 O TYR A 154 8717 7580 6712 672 588 -804 O ATOM 816 CB TYR A 154 35.735 9.070 -15.281 1.00 55.64 C ANISOU 816 CB TYR A 154 7978 6869 6294 634 430 -639 C ATOM 817 CG TYR A 154 36.954 8.170 -15.343 1.00 58.18 C ANISOU 817 CG TYR A 154 8214 7243 6650 750 476 -725 C ATOM 818 CD1 TYR A 154 36.938 6.904 -14.767 1.00 60.31 C ANISOU 818 CD1 TYR A 154 8515 7425 6975 872 423 -763 C ATOM 819 CD2 TYR A 154 38.120 8.580 -15.984 1.00 60.02 C ANISOU 819 CD2 TYR A 154 8337 7611 6858 742 578 -771 C ATOM 820 CE1 TYR A 154 38.053 6.069 -14.822 1.00 62.14 C ANISOU 820 CE1 TYR A 154 8671 7697 7240 1008 461 -841 C ATOM 821 CE2 TYR A 154 39.236 7.749 -16.060 1.00 62.31 C ANISOU 821 CE2 TYR A 154 8528 7965 7181 866 621 -861 C ATOM 822 CZ TYR A 154 39.200 6.495 -15.471 1.00 70.72 C ANISOU 822 CZ TYR A 154 9626 8938 8306 1012 557 -895 C ATOM 823 OH TYR A 154 40.294 5.663 -15.540 1.00 74.73 O ANISOU 823 OH TYR A 154 10042 9502 8851 1163 595 -982 O ATOM 824 N ILE A 155 34.092 7.230 -17.335 1.00 55.59 N ANISOU 824 N ILE A 155 8218 6756 6146 668 420 -761 N ATOM 825 CA ILE A 155 33.878 5.998 -18.099 1.00 55.99 C ANISOU 825 CA ILE A 155 8352 6762 6161 719 435 -865 C ATOM 826 C ILE A 155 33.565 6.366 -19.567 1.00 60.88 C ANISOU 826 C ILE A 155 9025 7469 6639 657 482 -896 C ATOM 827 O ILE A 155 34.101 5.728 -20.470 1.00 61.25 O ANISOU 827 O ILE A 155 9091 7552 6629 702 552 -996 O ATOM 828 CB ILE A 155 32.784 5.114 -17.429 1.00 58.21 C ANISOU 828 CB ILE A 155 8725 6900 6493 715 348 -871 C ATOM 829 CG1 ILE A 155 33.336 4.470 -16.129 1.00 58.00 C ANISOU 829 CG1 ILE A 155 8670 6784 6585 807 321 -855 C ATOM 830 CG2 ILE A 155 32.246 4.034 -18.387 1.00 59.93 C ANISOU 830 CG2 ILE A 155 9053 7068 6651 715 359 -985 C ATOM 831 CD1 ILE A 155 32.288 3.948 -15.149 1.00 61.14 C ANISOU 831 CD1 ILE A 155 9145 7048 7036 774 241 -814 C ATOM 832 N ALA A 156 32.781 7.440 -19.798 1.00 57.62 N ANISOU 832 N ALA A 156 8635 7097 6162 568 446 -807 N ATOM 833 CA ALA A 156 32.456 7.933 -21.143 1.00 58.69 C ANISOU 833 CA ALA A 156 8830 7325 6146 516 477 -807 C ATOM 834 C ALA A 156 33.724 8.358 -21.925 1.00 65.76 C ANISOU 834 C ALA A 156 9680 8332 6974 520 607 -825 C ATOM 835 O ALA A 156 33.747 8.233 -23.149 1.00 66.76 O ANISOU 835 O ALA A 156 9865 8536 6964 504 659 -871 O ATOM 836 CB ALA A 156 31.489 9.100 -21.052 1.00 58.54 C ANISOU 836 CB ALA A 156 8836 7316 6089 449 411 -688 C ATOM 837 N ILE A 157 34.770 8.835 -21.214 1.00 63.22 N ANISOU 837 N ILE A 157 9249 8030 6741 532 661 -796 N ATOM 838 CA ILE A 157 36.051 9.257 -21.785 1.00 64.76 C ANISOU 838 CA ILE A 157 9370 8341 6895 520 794 -819 C ATOM 839 C ILE A 157 36.981 8.026 -21.963 1.00 73.29 C ANISOU 839 C ILE A 157 10389 9445 8011 629 857 -959 C ATOM 840 O ILE A 157 37.517 7.834 -23.055 1.00 74.11 O ANISOU 840 O ILE A 157 10501 9642 8015 634 961 -1034 O ATOM 841 CB ILE A 157 36.689 10.382 -20.908 1.00 66.92 C ANISOU 841 CB ILE A 157 9543 8637 7248 461 818 -732 C ATOM 842 CG1 ILE A 157 35.976 11.731 -21.154 1.00 66.56 C ANISOU 842 CG1 ILE A 157 9580 8574 7136 356 800 -602 C ATOM 843 CG2 ILE A 157 38.211 10.526 -21.129 1.00 68.67 C ANISOU 843 CG2 ILE A 157 9636 8983 7472 453 956 -787 C ATOM 844 CD1 ILE A 157 35.889 12.661 -19.934 1.00 68.66 C ANISOU 844 CD1 ILE A 157 9797 8784 7509 306 759 -515 C ATOM 845 N LYS A 158 37.165 7.211 -20.896 1.00 72.21 N ANISOU 845 N LYS A 158 10202 9226 8010 724 797 -991 N ATOM 846 CA LYS A 158 38.047 6.037 -20.880 1.00 74.40 C ANISOU 846 CA LYS A 158 10425 9501 8342 861 842 -1111 C ATOM 847 C LYS A 158 37.550 4.920 -21.809 1.00 83.32 C ANISOU 847 C LYS A 158 11681 10574 9401 907 855 -1223 C ATOM 848 O LYS A 158 38.370 4.233 -22.418 1.00 84.56 O ANISOU 848 O LYS A 158 11811 10778 9541 995 947 -1340 O ATOM 849 CB LYS A 158 38.207 5.502 -19.445 1.00 75.94 C ANISOU 849 CB LYS A 158 10568 9601 8685 956 755 -1089 C ATOM 850 CG LYS A 158 39.479 4.685 -19.209 1.00 89.74 C ANISOU 850 CG LYS A 158 12205 11386 10505 1116 805 -1182 C ATOM 851 CD LYS A 158 40.711 5.559 -18.945 1.00 99.91 C ANISOU 851 CD LYS A 158 13296 12843 11823 1104 869 -1171 C ATOM 852 CE LYS A 158 41.853 5.267 -19.895 1.00110.73 C ANISOU 852 CE LYS A 158 14565 14352 13155 1171 1006 -1292 C ATOM 853 NZ LYS A 158 42.517 3.968 -19.598 1.00121.06 N ANISOU 853 NZ LYS A 158 15830 15622 14546 1385 999 -1390 N ATOM 854 N LYS A 159 36.222 4.746 -21.912 1.00 82.39 N ANISOU 854 N LYS A 159 11695 10366 9244 844 767 -1198 N ATOM 855 CA LYS A 159 35.560 3.750 -22.765 1.00 84.47 C ANISOU 855 CA LYS A 159 12088 10574 9432 851 764 -1310 C ATOM 856 C LYS A 159 34.681 4.510 -23.788 1.00 91.91 C ANISOU 856 C LYS A 159 13105 11603 10213 728 748 -1273 C ATOM 857 O LYS A 159 33.469 4.637 -23.573 1.00 90.27 O ANISOU 857 O LYS A 159 12961 11341 9995 661 643 -1223 O ATOM 858 CB LYS A 159 34.741 2.774 -21.889 1.00 86.39 C ANISOU 858 CB LYS A 159 12411 10635 9777 880 665 -1324 C ATOM 859 CG LYS A 159 34.195 1.538 -22.603 1.00102.67 C ANISOU 859 CG LYS A 159 14606 12608 11795 893 672 -1467 C ATOM 860 CD LYS A 159 33.155 0.798 -21.750 1.00111.87 C ANISOU 860 CD LYS A 159 15864 13595 13049 867 576 -1458 C ATOM 861 CE LYS A 159 33.760 -0.168 -20.754 1.00121.78 C ANISOU 861 CE LYS A 159 17129 14695 14446 1000 583 -1473 C ATOM 862 NZ LYS A 159 32.728 -0.767 -19.869 1.00128.79 N ANISOU 862 NZ LYS A 159 18117 15409 15408 950 501 -1443 N ATOM 863 N PRO A 160 35.278 5.089 -24.869 1.00 92.86 N ANISOU 863 N PRO A 160 13212 11869 10201 697 850 -1286 N ATOM 864 CA PRO A 160 34.463 5.865 -25.829 1.00 94.23 C ANISOU 864 CA PRO A 160 13468 12129 10205 597 827 -1229 C ATOM 865 C PRO A 160 33.447 5.004 -26.592 1.00102.89 C ANISOU 865 C PRO A 160 14686 13206 11201 578 767 -1335 C ATOM 866 O PRO A 160 32.333 5.467 -26.855 1.00102.01 O ANISOU 866 O PRO A 160 14633 13119 11005 508 673 -1274 O ATOM 867 CB PRO A 160 35.502 6.487 -26.769 1.00 97.05 C ANISOU 867 CB PRO A 160 13793 12638 10446 577 973 -1232 C ATOM 868 CG PRO A 160 36.699 5.624 -26.654 1.00101.94 C ANISOU 868 CG PRO A 160 14328 13261 11144 677 1075 -1360 C ATOM 869 CD PRO A 160 36.705 5.075 -25.262 1.00 96.00 C ANISOU 869 CD PRO A 160 13516 12369 10590 755 994 -1350 C ATOM 870 N ILE A 161 33.820 3.747 -26.912 1.00103.66 N ANISOU 870 N ILE A 161 14817 13257 11312 643 819 -1499 N ATOM 871 CA ILE A 161 32.961 2.784 -27.602 1.00105.80 C ANISOU 871 CA ILE A 161 15205 13495 11499 615 776 -1634 C ATOM 872 C ILE A 161 32.175 1.960 -26.554 1.00111.72 C ANISOU 872 C ILE A 161 15985 14062 12400 617 674 -1653 C ATOM 873 O ILE A 161 31.959 2.451 -25.440 1.00109.84 O ANISOU 873 O ILE A 161 15690 13764 12281 611 608 -1526 O ATOM 874 CB ILE A 161 33.808 1.896 -28.550 1.00111.00 C ANISOU 874 CB ILE A 161 15899 14189 12086 680 906 -1813 C ATOM 875 N GLN A 162 31.714 0.734 -26.927 1.00111.31 N ANISOU 875 N GLN A 162 16035 13922 12335 610 667 -1813 N ATOM 876 CA GLN A 162 30.950 -0.214 -26.093 1.00111.52 C ANISOU 876 CA GLN A 162 16122 13762 12489 590 594 -1856 C ATOM 877 C GLN A 162 29.650 0.414 -25.506 1.00114.96 C ANISOU 877 C GLN A 162 16540 14205 12935 477 459 -1746 C ATOM 878 O GLN A 162 29.092 -0.106 -24.531 1.00114.34 O ANISOU 878 O GLN A 162 16490 13980 12972 446 403 -1746 O ATOM 879 CB GLN A 162 31.836 -0.789 -24.968 1.00112.57 C ANISOU 879 CB GLN A 162 16225 13737 12811 715 633 -1831 C ATOM 880 N ALA A 163 29.163 1.509 -26.129 1.00111.19 N ANISOU 880 N ALA A 163 16022 13897 12329 421 414 -1654 N ATOM 881 CA ALA A 163 27.957 2.224 -25.714 1.00109.85 C ANISOU 881 CA ALA A 163 15819 13765 12155 338 290 -1552 C ATOM 882 C ALA A 163 26.746 1.785 -26.548 1.00114.08 C ANISOU 882 C ALA A 163 16414 14366 12566 238 211 -1668 C ATOM 883 O ALA A 163 26.784 1.843 -27.781 1.00115.33 O ANISOU 883 O ALA A 163 16618 14652 12551 224 232 -1747 O ATOM 884 CB ALA A 163 28.173 3.727 -25.833 1.00109.82 C ANISOU 884 CB ALA A 163 15751 13893 12084 350 282 -1387 C ATOM 885 N ASN A 164 25.692 1.308 -25.863 1.00108.94 N ANISOU 885 N ASN A 164 15759 13636 11998 160 125 -1686 N ATOM 886 CA ASN A 164 24.435 0.857 -26.467 1.00109.23 C ANISOU 886 CA ASN A 164 15822 13739 11941 42 37 -1804 C ATOM 887 C ASN A 164 23.277 1.562 -25.773 1.00110.20 C ANISOU 887 C ASN A 164 15854 13915 12104 -14 -81 -1696 C ATOM 888 O ASN A 164 23.263 1.623 -24.546 1.00108.48 O ANISOU 888 O ASN A 164 15598 13576 12045 -5 -80 -1611 O ATOM 889 CB ASN A 164 24.298 -0.664 -26.373 1.00111.09 C ANISOU 889 CB ASN A 164 16153 13807 12249 -18 76 -1985 C ATOM 890 N GLN A 165 22.324 2.112 -26.554 1.00105.96 N ANISOU 890 N GLN A 165 15279 13568 11415 -61 -183 -1700 N ATOM 891 CA GLN A 165 21.168 2.880 -26.068 1.00104.27 C ANISOU 891 CA GLN A 165 14961 13442 11215 -93 -302 -1605 C ATOM 892 C GLN A 165 20.315 2.113 -25.033 1.00105.03 C ANISOU 892 C GLN A 165 15020 13426 11461 -197 -334 -1666 C ATOM 893 O GLN A 165 20.083 2.636 -23.939 1.00102.85 O ANISOU 893 O GLN A 165 14674 13099 11305 -180 -351 -1546 O ATOM 894 CB GLN A 165 20.286 3.328 -27.245 1.00107.13 C ANISOU 894 CB GLN A 165 15297 14039 11369 -117 -412 -1638 C ATOM 895 N TYR A 166 19.869 0.882 -25.376 1.00100.95 N ANISOU 895 N TYR A 166 14559 12866 10931 -315 -330 -1855 N ATOM 896 CA TYR A 166 19.032 0.027 -24.523 1.00 99.78 C ANISOU 896 CA TYR A 166 14397 12606 10910 -447 -343 -1933 C ATOM 897 C TYR A 166 19.768 -0.411 -23.246 1.00 99.34 C ANISOU 897 C TYR A 166 14400 12302 11043 -409 -245 -1864 C ATOM 898 O TYR A 166 19.183 -0.373 -22.158 1.00 98.23 O ANISOU 898 O TYR A 166 14208 12097 11018 -463 -262 -1806 O ATOM 899 CB TYR A 166 18.554 -1.207 -25.303 1.00103.06 C ANISOU 899 CB TYR A 166 14884 13019 11256 -591 -345 -2164 C ATOM 900 N ASN A 167 21.047 -0.807 -23.386 1.00 92.90 N ANISOU 900 N ASN A 167 13686 11363 10250 -310 -145 -1872 N ATOM 901 CA ASN A 167 21.894 -1.261 -22.284 1.00 90.42 C ANISOU 901 CA ASN A 167 13433 10828 10096 -243 -59 -1809 C ATOM 902 C ASN A 167 22.278 -0.107 -21.346 1.00 87.83 C ANISOU 902 C ASN A 167 13013 10520 9840 -144 -70 -1607 C ATOM 903 O ASN A 167 22.303 -0.315 -20.132 1.00 86.84 O ANISOU 903 O ASN A 167 12896 10256 9845 -142 -50 -1539 O ATOM 904 CB ASN A 167 23.138 -1.963 -22.818 1.00 93.60 C ANISOU 904 CB ASN A 167 13947 11128 10489 -145 42 -1889 C ATOM 905 CG ASN A 167 22.807 -3.191 -23.629 1.00124.98 C ANISOU 905 CG ASN A 167 18038 15035 14414 -243 71 -2102 C ATOM 906 OD1 ASN A 167 22.500 -3.112 -24.824 1.00122.80 O ANISOU 906 OD1 ASN A 167 17761 14914 13985 -291 41 -2211 O ATOM 907 ND2 ASN A 167 22.813 -4.349 -22.985 1.00118.51 N ANISOU 907 ND2 ASN A 167 17332 13980 13716 -282 128 -2166 N ATOM 908 N SER A 168 22.547 1.102 -21.892 1.00 80.13 N ANISOU 908 N SER A 168 11962 9711 8772 -70 -100 -1514 N ATOM 909 CA SER A 168 22.895 2.288 -21.094 1.00 76.52 C ANISOU 909 CA SER A 168 11425 9276 8375 10 -107 -1336 C ATOM 910 C SER A 168 21.731 2.743 -20.211 1.00 74.66 C ANISOU 910 C SER A 168 11106 9062 8199 -57 -182 -1270 C ATOM 911 O SER A 168 21.983 3.239 -19.113 1.00 72.27 O ANISOU 911 O SER A 168 10766 8696 7996 -16 -169 -1155 O ATOM 912 CB SER A 168 23.348 3.444 -21.980 1.00 80.09 C ANISOU 912 CB SER A 168 11841 9884 8706 84 -111 -1260 C ATOM 913 OG SER A 168 24.747 3.387 -22.211 1.00 89.79 O ANISOU 913 OG SER A 168 13114 11079 9925 169 -14 -1268 O ATOM 914 N ARG A 169 20.470 2.567 -20.678 1.00 69.29 N ANISOU 914 N ARG A 169 10387 8485 7455 -161 -259 -1351 N ATOM 915 CA ARG A 169 19.277 2.929 -19.908 1.00 67.64 C ANISOU 915 CA ARG A 169 10079 8324 7298 -230 -327 -1314 C ATOM 916 C ARG A 169 19.196 2.065 -18.645 1.00 69.47 C ANISOU 916 C ARG A 169 10350 8372 7675 -301 -274 -1324 C ATOM 917 O ARG A 169 18.987 2.604 -17.555 1.00 68.16 O ANISOU 917 O ARG A 169 10123 8185 7590 -293 -280 -1224 O ATOM 918 CB ARG A 169 17.994 2.795 -20.748 1.00 68.38 C ANISOU 918 CB ARG A 169 10109 8586 7286 -329 -421 -1425 C ATOM 919 CG ARG A 169 16.818 3.583 -20.165 1.00 75.13 C ANISOU 919 CG ARG A 169 10820 9558 8169 -353 -502 -1366 C ATOM 920 CD ARG A 169 15.469 2.999 -20.544 1.00 80.30 C ANISOU 920 CD ARG A 169 11398 10333 8780 -500 -575 -1514 C ATOM 921 NE ARG A 169 14.360 3.764 -19.975 1.00 81.71 N ANISOU 921 NE ARG A 169 11417 10636 8991 -510 -647 -1465 N ATOM 922 N ALA A 170 19.406 0.737 -18.794 1.00 65.34 N ANISOU 922 N ALA A 170 9942 7708 7176 -364 -216 -1443 N ATOM 923 CA ALA A 170 19.406 -0.231 -17.697 1.00 64.36 C ANISOU 923 CA ALA A 170 9898 7381 7176 -427 -155 -1450 C ATOM 924 C ALA A 170 20.515 0.099 -16.701 1.00 65.37 C ANISOU 924 C ALA A 170 10055 7394 7389 -293 -104 -1309 C ATOM 925 O ALA A 170 20.238 0.214 -15.506 1.00 64.21 O ANISOU 925 O ALA A 170 9890 7182 7324 -316 -96 -1226 O ATOM 926 CB ALA A 170 19.586 -1.641 -18.241 1.00 66.70 C ANISOU 926 CB ALA A 170 10338 7537 7470 -498 -99 -1606 C ATOM 927 N THR A 171 21.749 0.320 -17.214 1.00 60.35 N ANISOU 927 N THR A 171 9449 6759 6723 -157 -71 -1285 N ATOM 928 CA THR A 171 22.959 0.670 -16.465 1.00 58.53 C ANISOU 928 CA THR A 171 9224 6459 6557 -20 -29 -1171 C ATOM 929 C THR A 171 22.740 1.949 -15.640 1.00 60.18 C ANISOU 929 C THR A 171 9320 6755 6792 2 -70 -1031 C ATOM 930 O THR A 171 23.134 1.977 -14.472 1.00 59.38 O ANISOU 930 O THR A 171 9224 6566 6772 42 -51 -947 O ATOM 931 CB THR A 171 24.142 0.823 -17.441 1.00 66.62 C ANISOU 931 CB THR A 171 10262 7532 7520 96 11 -1197 C ATOM 932 OG1 THR A 171 24.254 -0.365 -18.229 1.00 67.81 O ANISOU 932 OG1 THR A 171 10519 7608 7638 71 51 -1345 O ATOM 933 CG2 THR A 171 25.471 1.109 -16.733 1.00 63.81 C ANISOU 933 CG2 THR A 171 9895 7119 7233 233 57 -1105 C ATOM 934 N ALA A 172 22.108 2.993 -16.238 1.00 55.73 N ANISOU 934 N ALA A 172 8662 6358 6154 -18 -128 -1010 N ATOM 935 CA ALA A 172 21.820 4.269 -15.562 1.00 53.94 C ANISOU 935 CA ALA A 172 8338 6207 5949 8 -164 -890 C ATOM 936 C ALA A 172 20.825 4.069 -14.410 1.00 55.53 C ANISOU 936 C ALA A 172 8510 6363 6225 -79 -180 -875 C ATOM 937 O ALA A 172 21.121 4.503 -13.301 1.00 53.42 O ANISOU 937 O ALA A 172 8224 6050 6023 -45 -164 -784 O ATOM 938 CB ALA A 172 21.297 5.306 -16.553 1.00 54.75 C ANISOU 938 CB ALA A 172 8372 6482 5950 21 -222 -875 C ATOM 939 N PHE A 173 19.696 3.359 -14.655 1.00 52.88 N ANISOU 939 N PHE A 173 8172 6043 5876 -201 -203 -973 N ATOM 940 CA PHE A 173 18.677 3.040 -13.645 1.00 53.27 C ANISOU 940 CA PHE A 173 8191 6059 5988 -313 -202 -979 C ATOM 941 C PHE A 173 19.256 2.222 -12.467 1.00 55.73 C ANISOU 941 C PHE A 173 8611 6178 6387 -319 -132 -938 C ATOM 942 O PHE A 173 18.858 2.454 -11.323 1.00 55.08 O ANISOU 942 O PHE A 173 8499 6073 6355 -354 -120 -875 O ATOM 943 CB PHE A 173 17.496 2.285 -14.277 1.00 57.23 C ANISOU 943 CB PHE A 173 8674 6617 6455 -462 -229 -1117 C ATOM 944 CG PHE A 173 16.507 3.109 -15.077 1.00 60.24 C ANISOU 944 CG PHE A 173 8914 7218 6757 -473 -319 -1148 C ATOM 945 CD1 PHE A 173 15.501 2.493 -15.814 1.00 65.95 C ANISOU 945 CD1 PHE A 173 9598 8035 7426 -599 -362 -1288 C ATOM 946 CD2 PHE A 173 16.568 4.500 -15.078 1.00 62.10 C ANISOU 946 CD2 PHE A 173 9059 7564 6970 -354 -364 -1039 C ATOM 947 CE1 PHE A 173 14.580 3.252 -16.547 1.00 67.72 C ANISOU 947 CE1 PHE A 173 9681 8483 7568 -589 -461 -1314 C ATOM 948 CE2 PHE A 173 15.651 5.259 -15.815 1.00 65.83 C ANISOU 948 CE2 PHE A 173 9414 8232 7367 -337 -453 -1056 C ATOM 949 CZ PHE A 173 14.661 4.630 -16.542 1.00 65.63 C ANISOU 949 CZ PHE A 173 9336 8319 7281 -446 -508 -1190 C ATOM 950 N ILE A 174 20.204 1.293 -12.746 1.00 51.21 N ANISOU 950 N ILE A 174 8164 5471 5823 -272 -86 -972 N ATOM 951 CA ILE A 174 20.887 0.473 -11.737 1.00 50.59 C ANISOU 951 CA ILE A 174 8205 5204 5815 -240 -28 -924 C ATOM 952 C ILE A 174 21.699 1.396 -10.804 1.00 53.12 C ANISOU 952 C ILE A 174 8474 5545 6163 -120 -34 -788 C ATOM 953 O ILE A 174 21.524 1.313 -9.587 1.00 52.95 O ANISOU 953 O ILE A 174 8474 5460 6183 -145 -19 -719 O ATOM 954 CB ILE A 174 21.769 -0.640 -12.396 1.00 54.19 C ANISOU 954 CB ILE A 174 8798 5523 6271 -181 17 -999 C ATOM 955 CG1 ILE A 174 20.894 -1.790 -12.944 1.00 55.75 C ANISOU 955 CG1 ILE A 174 9083 5639 6459 -335 41 -1139 C ATOM 956 CG2 ILE A 174 22.859 -1.176 -11.435 1.00 53.73 C ANISOU 956 CG2 ILE A 174 8842 5299 6275 -63 60 -916 C ATOM 957 CD1 ILE A 174 21.502 -2.575 -14.138 1.00 60.31 C ANISOU 957 CD1 ILE A 174 9757 6159 7000 -294 70 -1263 C ATOM 958 N LYS A 175 22.551 2.282 -11.376 1.00 48.32 N ANISOU 958 N LYS A 175 7801 5035 5523 -7 -53 -757 N ATOM 959 CA LYS A 175 23.400 3.229 -10.639 1.00 47.04 C ANISOU 959 CA LYS A 175 7581 4910 5383 92 -57 -650 C ATOM 960 C LYS A 175 22.570 4.222 -9.820 1.00 50.51 C ANISOU 960 C LYS A 175 7932 5426 5833 39 -86 -587 C ATOM 961 O LYS A 175 22.975 4.564 -8.708 1.00 49.73 O ANISOU 961 O LYS A 175 7824 5304 5767 76 -80 -509 O ATOM 962 CB LYS A 175 24.339 3.985 -11.588 1.00 49.90 C ANISOU 962 CB LYS A 175 7891 5367 5702 185 -57 -648 C ATOM 963 CG LYS A 175 25.414 3.096 -12.214 1.00 70.24 C ANISOU 963 CG LYS A 175 10538 7876 8275 269 -16 -704 C ATOM 964 CD LYS A 175 26.502 3.898 -12.927 1.00 80.62 C ANISOU 964 CD LYS A 175 11788 9295 9550 354 3 -694 C ATOM 965 CE LYS A 175 27.575 2.997 -13.495 1.00 89.89 C ANISOU 965 CE LYS A 175 13015 10413 10726 449 53 -759 C ATOM 966 NZ LYS A 175 28.706 3.769 -14.070 1.00 97.99 N ANISOU 966 NZ LYS A 175 13964 11552 11716 521 87 -750 N ATOM 967 N ILE A 176 21.400 4.658 -10.352 1.00 47.59 N ANISOU 967 N ILE A 176 7495 5154 5432 -39 -118 -627 N ATOM 968 CA ILE A 176 20.460 5.560 -9.672 1.00 47.07 C ANISOU 968 CA ILE A 176 7336 5168 5379 -82 -141 -587 C ATOM 969 C ILE A 176 19.945 4.865 -8.405 1.00 50.57 C ANISOU 969 C ILE A 176 7820 5524 5869 -165 -107 -574 C ATOM 970 O ILE A 176 20.037 5.437 -7.320 1.00 49.51 O ANISOU 970 O ILE A 176 7659 5393 5759 -147 -98 -504 O ATOM 971 CB ILE A 176 19.290 6.011 -10.620 1.00 51.06 C ANISOU 971 CB ILE A 176 7754 5809 5836 -129 -191 -645 C ATOM 972 CG1 ILE A 176 19.754 7.026 -11.704 1.00 51.33 C ANISOU 972 CG1 ILE A 176 7752 5941 5809 -33 -225 -617 C ATOM 973 CG2 ILE A 176 18.057 6.542 -9.848 1.00 52.08 C ANISOU 973 CG2 ILE A 176 7787 6011 5991 -194 -207 -639 C ATOM 974 CD1 ILE A 176 20.364 8.328 -11.177 1.00 62.04 C ANISOU 974 CD1 ILE A 176 9075 7312 7187 53 -217 -516 C ATOM 975 N THR A 177 19.441 3.620 -8.551 1.00 47.91 N ANISOU 975 N THR A 177 7561 5104 5539 -263 -82 -643 N ATOM 976 CA THR A 177 18.903 2.796 -7.467 1.00 48.21 C ANISOU 976 CA THR A 177 7666 5039 5611 -367 -33 -633 C ATOM 977 C THR A 177 19.946 2.615 -6.352 1.00 51.49 C ANISOU 977 C THR A 177 8173 5343 6049 -280 -6 -532 C ATOM 978 O THR A 177 19.602 2.818 -5.193 1.00 50.99 O ANISOU 978 O THR A 177 8105 5275 5994 -318 15 -474 O ATOM 979 CB THR A 177 18.398 1.455 -8.022 1.00 56.20 C ANISOU 979 CB THR A 177 8770 5957 6625 -488 -2 -734 C ATOM 980 OG1 THR A 177 17.478 1.723 -9.083 1.00 52.91 O ANISOU 980 OG1 THR A 177 8249 5682 6174 -558 -45 -834 O ATOM 981 CG2 THR A 177 17.709 0.594 -6.956 1.00 55.65 C ANISOU 981 CG2 THR A 177 8779 5779 6586 -629 63 -725 C ATOM 982 N VAL A 178 21.212 2.290 -6.707 1.00 48.22 N ANISOU 982 N VAL A 178 7826 4861 5635 -157 -10 -516 N ATOM 983 CA VAL A 178 22.332 2.097 -5.770 1.00 47.92 C ANISOU 983 CA VAL A 178 7858 4740 5610 -47 -2 -428 C ATOM 984 C VAL A 178 22.560 3.377 -4.943 1.00 51.58 C ANISOU 984 C VAL A 178 8218 5314 6066 -3 -28 -353 C ATOM 985 O VAL A 178 22.707 3.285 -3.724 1.00 52.07 O ANISOU 985 O VAL A 178 8321 5336 6125 3 -19 -283 O ATOM 986 CB VAL A 178 23.630 1.638 -6.493 1.00 51.76 C ANISOU 986 CB VAL A 178 8391 5175 6099 89 -5 -446 C ATOM 987 CG1 VAL A 178 24.834 1.634 -5.551 1.00 51.43 C ANISOU 987 CG1 VAL A 178 8376 5097 6066 225 -16 -358 C ATOM 988 CG2 VAL A 178 23.450 0.261 -7.125 1.00 52.80 C ANISOU 988 CG2 VAL A 178 8656 5164 6241 52 32 -525 C ATOM 989 N VAL A 179 22.545 4.557 -5.595 1.00 47.30 N ANISOU 989 N VAL A 179 7556 4903 5513 22 -57 -369 N ATOM 990 CA VAL A 179 22.719 5.866 -4.935 1.00 46.11 C ANISOU 990 CA VAL A 179 7313 4845 5360 53 -74 -316 C ATOM 991 C VAL A 179 21.596 6.084 -3.897 1.00 49.81 C ANISOU 991 C VAL A 179 7763 5333 5832 -41 -57 -299 C ATOM 992 O VAL A 179 21.880 6.523 -2.778 1.00 49.76 O ANISOU 992 O VAL A 179 7752 5334 5819 -22 -53 -244 O ATOM 993 CB VAL A 179 22.801 7.026 -5.970 1.00 48.83 C ANISOU 993 CB VAL A 179 7563 5299 5692 88 -97 -336 C ATOM 994 CG1 VAL A 179 22.479 8.378 -5.342 1.00 47.71 C ANISOU 994 CG1 VAL A 179 7339 5233 5554 85 -105 -299 C ATOM 995 CG2 VAL A 179 24.171 7.060 -6.641 1.00 48.48 C ANISOU 995 CG2 VAL A 179 7525 5256 5640 184 -97 -335 C ATOM 996 N TRP A 180 20.345 5.744 -4.259 1.00 46.29 N ANISOU 996 N TRP A 180 7297 4904 5388 -145 -45 -355 N ATOM 997 CA TRP A 180 19.200 5.890 -3.362 1.00 46.30 C ANISOU 997 CA TRP A 180 7261 4939 5392 -245 -16 -356 C ATOM 998 C TRP A 180 19.265 4.900 -2.202 1.00 49.99 C ANISOU 998 C TRP A 180 7848 5295 5852 -300 33 -310 C ATOM 999 O TRP A 180 18.906 5.278 -1.091 1.00 49.73 O ANISOU 999 O TRP A 180 7800 5292 5805 -334 59 -273 O ATOM 1000 CB TRP A 180 17.877 5.759 -4.112 1.00 45.70 C ANISOU 1000 CB TRP A 180 7111 4934 5320 -346 -17 -440 C ATOM 1001 CG TRP A 180 17.483 7.025 -4.810 1.00 46.31 C ANISOU 1001 CG TRP A 180 7055 5148 5393 -290 -64 -460 C ATOM 1002 CD1 TRP A 180 17.589 7.292 -6.142 1.00 49.24 C ANISOU 1002 CD1 TRP A 180 7392 5573 5743 -240 -113 -495 C ATOM 1003 CD2 TRP A 180 16.983 8.221 -4.198 1.00 45.94 C ANISOU 1003 CD2 TRP A 180 6910 5190 5355 -263 -65 -439 C ATOM 1004 NE1 TRP A 180 17.145 8.567 -6.407 1.00 48.46 N ANISOU 1004 NE1 TRP A 180 7187 5586 5639 -180 -147 -484 N ATOM 1005 CE2 TRP A 180 16.766 9.161 -5.232 1.00 49.76 C ANISOU 1005 CE2 TRP A 180 7310 5767 5830 -189 -117 -455 C ATOM 1006 CE3 TRP A 180 16.670 8.586 -2.875 1.00 47.14 C ANISOU 1006 CE3 TRP A 180 7046 5350 5517 -290 -21 -411 C ATOM 1007 CZ2 TRP A 180 16.249 10.441 -4.986 1.00 48.75 C ANISOU 1007 CZ2 TRP A 180 7088 5721 5713 -131 -128 -442 C ATOM 1008 CZ3 TRP A 180 16.169 9.856 -2.633 1.00 48.29 C ANISOU 1008 CZ3 TRP A 180 7089 5587 5674 -241 -27 -413 C ATOM 1009 CH2 TRP A 180 15.955 10.764 -3.680 1.00 48.80 C ANISOU 1009 CH2 TRP A 180 7076 5725 5740 -158 -80 -428 C ATOM 1010 N LEU A 181 19.768 3.670 -2.438 1.00 46.10 N ANISOU 1010 N LEU A 181 7486 4669 5362 -296 47 -307 N ATOM 1011 CA LEU A 181 19.912 2.661 -1.383 1.00 46.31 C ANISOU 1011 CA LEU A 181 7661 4562 5374 -330 92 -245 C ATOM 1012 C LEU A 181 21.050 3.052 -0.416 1.00 49.24 C ANISOU 1012 C LEU A 181 8061 4932 5717 -203 64 -150 C ATOM 1013 O LEU A 181 20.922 2.828 0.795 1.00 48.61 O ANISOU 1013 O LEU A 181 8053 4817 5600 -235 93 -83 O ATOM 1014 CB LEU A 181 20.131 1.255 -1.966 1.00 47.20 C ANISOU 1014 CB LEU A 181 7920 4511 5502 -347 117 -273 C ATOM 1015 CG LEU A 181 18.976 0.668 -2.794 1.00 52.17 C ANISOU 1015 CG LEU A 181 8541 5129 6151 -507 151 -380 C ATOM 1016 CD1 LEU A 181 19.407 -0.583 -3.496 1.00 53.59 C ANISOU 1016 CD1 LEU A 181 8863 5150 6349 -496 168 -425 C ATOM 1017 CD2 LEU A 181 17.727 0.405 -1.951 1.00 53.92 C ANISOU 1017 CD2 LEU A 181 8778 5344 6366 -687 221 -380 C ATOM 1018 N ILE A 182 22.133 3.677 -0.950 1.00 44.82 N ANISOU 1018 N ILE A 182 7438 4427 5165 -70 10 -149 N ATOM 1019 CA ILE A 182 23.258 4.204 -0.164 1.00 44.58 C ANISOU 1019 CA ILE A 182 7394 4435 5109 44 -28 -83 C ATOM 1020 C ILE A 182 22.713 5.297 0.785 1.00 48.17 C ANISOU 1020 C ILE A 182 7768 4996 5539 -10 -22 -67 C ATOM 1021 O ILE A 182 23.053 5.306 1.974 1.00 48.70 O ANISOU 1021 O ILE A 182 7877 5067 5558 11 -26 -6 O ATOM 1022 CB ILE A 182 24.403 4.737 -1.089 1.00 47.04 C ANISOU 1022 CB ILE A 182 7629 4803 5442 164 -71 -108 C ATOM 1023 CG1 ILE A 182 25.284 3.578 -1.604 1.00 48.15 C ANISOU 1023 CG1 ILE A 182 7864 4834 5595 260 -75 -108 C ATOM 1024 CG2 ILE A 182 25.263 5.821 -0.390 1.00 46.76 C ANISOU 1024 CG2 ILE A 182 7509 4871 5387 231 -108 -74 C ATOM 1025 CD1 ILE A 182 26.187 3.923 -2.825 1.00 52.57 C ANISOU 1025 CD1 ILE A 182 8347 5451 6177 350 -93 -161 C ATOM 1026 N SER A 183 21.837 6.185 0.249 1.00 42.82 N ANISOU 1026 N SER A 183 6980 4404 4885 -72 -12 -126 N ATOM 1027 CA SER A 183 21.212 7.299 0.969 1.00 41.55 C ANISOU 1027 CA SER A 183 6733 4340 4712 -113 3 -133 C ATOM 1028 C SER A 183 20.274 6.832 2.083 1.00 44.54 C ANISOU 1028 C SER A 183 7163 4702 5057 -219 60 -114 C ATOM 1029 O SER A 183 20.272 7.456 3.144 1.00 44.34 O ANISOU 1029 O SER A 183 7121 4731 4994 -224 72 -93 O ATOM 1030 CB SER A 183 20.461 8.204 0.003 1.00 44.40 C ANISOU 1030 CB SER A 183 6978 4781 5111 -130 -3 -196 C ATOM 1031 OG SER A 183 21.385 8.745 -0.926 1.00 53.72 O ANISOU 1031 OG SER A 183 8125 5978 6307 -40 -44 -202 O ATOM 1032 N ILE A 184 19.502 5.741 1.863 1.00 41.03 N ANISOU 1032 N ILE A 184 6786 4185 4620 -314 102 -129 N ATOM 1033 CA ILE A 184 18.596 5.184 2.879 1.00 41.78 C ANISOU 1033 CA ILE A 184 6939 4256 4678 -440 176 -110 C ATOM 1034 C ILE A 184 19.448 4.650 4.058 1.00 47.58 C ANISOU 1034 C ILE A 184 7817 4916 5344 -393 177 -8 C ATOM 1035 O ILE A 184 19.162 4.993 5.204 1.00 47.49 O ANISOU 1035 O ILE A 184 7813 4956 5274 -433 212 23 O ATOM 1036 CB ILE A 184 17.613 4.105 2.315 1.00 45.33 C ANISOU 1036 CB ILE A 184 7430 4638 5156 -577 229 -159 C ATOM 1037 CG1 ILE A 184 16.715 4.677 1.186 1.00 44.93 C ANISOU 1037 CG1 ILE A 184 7217 4698 5155 -617 212 -264 C ATOM 1038 CG2 ILE A 184 16.748 3.494 3.433 1.00 46.47 C ANISOU 1038 CG2 ILE A 184 7650 4750 5256 -725 323 -131 C ATOM 1039 CD1 ILE A 184 16.213 3.618 0.139 1.00 49.51 C ANISOU 1039 CD1 ILE A 184 7830 5216 5767 -709 222 -334 C ATOM 1040 N GLY A 185 20.510 3.896 3.745 1.00 44.90 N ANISOU 1040 N GLY A 185 7581 4473 5006 -294 135 39 N ATOM 1041 CA GLY A 185 21.437 3.310 4.712 1.00 45.41 C ANISOU 1041 CA GLY A 185 7781 4468 5004 -210 114 142 C ATOM 1042 C GLY A 185 22.135 4.297 5.623 1.00 49.01 C ANISOU 1042 C GLY A 185 8177 5043 5402 -132 65 174 C ATOM 1043 O GLY A 185 22.428 3.972 6.773 1.00 50.10 O ANISOU 1043 O GLY A 185 8414 5167 5452 -116 64 256 O ATOM 1044 N ILE A 186 22.408 5.505 5.121 1.00 44.28 N ANISOU 1044 N ILE A 186 7425 4558 4843 -90 25 111 N ATOM 1045 CA ILE A 186 23.069 6.561 5.889 1.00 43.46 C ANISOU 1045 CA ILE A 186 7251 4569 4693 -36 -17 114 C ATOM 1046 C ILE A 186 22.011 7.309 6.737 1.00 48.24 C ANISOU 1046 C ILE A 186 7813 5252 5263 -144 44 84 C ATOM 1047 O ILE A 186 22.325 7.728 7.848 1.00 47.86 O ANISOU 1047 O ILE A 186 7778 5271 5137 -135 33 106 O ATOM 1048 CB ILE A 186 23.887 7.504 4.935 1.00 44.81 C ANISOU 1048 CB ILE A 186 7294 4804 4926 45 -71 58 C ATOM 1049 CG1 ILE A 186 25.118 6.757 4.362 1.00 45.24 C ANISOU 1049 CG1 ILE A 186 7385 4806 4996 167 -126 88 C ATOM 1050 CG2 ILE A 186 24.305 8.830 5.616 1.00 43.96 C ANISOU 1050 CG2 ILE A 186 7097 4815 4790 55 -94 29 C ATOM 1051 CD1 ILE A 186 25.861 7.439 3.186 1.00 51.04 C ANISOU 1051 CD1 ILE A 186 8010 5587 5797 226 -154 31 C ATOM 1052 N ALA A 187 20.771 7.458 6.222 1.00 45.28 N ANISOU 1052 N ALA A 187 7383 4883 4940 -242 105 25 N ATOM 1053 CA ALA A 187 19.699 8.185 6.909 1.00 45.60 C ANISOU 1053 CA ALA A 187 7358 5007 4960 -332 171 -20 C ATOM 1054 C ALA A 187 18.886 7.330 7.912 1.00 50.94 C ANISOU 1054 C ALA A 187 8136 5655 5565 -449 254 21 C ATOM 1055 O ALA A 187 18.324 7.891 8.854 1.00 50.50 O ANISOU 1055 O ALA A 187 8052 5681 5457 -506 309 -1 O ATOM 1056 CB ALA A 187 18.760 8.798 5.886 1.00 45.75 C ANISOU 1056 CB ALA A 187 7246 5070 5066 -362 189 -106 C ATOM 1057 N ILE A 188 18.860 5.990 7.737 1.00 48.64 N ANISOU 1057 N ILE A 188 7972 5241 5266 -486 273 78 N ATOM 1058 CA ILE A 188 18.090 5.055 8.567 1.00 50.13 C ANISOU 1058 CA ILE A 188 8283 5375 5390 -616 367 126 C ATOM 1059 C ILE A 188 18.494 5.039 10.095 1.00 55.52 C ANISOU 1059 C ILE A 188 9078 6082 5934 -606 380 214 C ATOM 1060 O ILE A 188 17.595 4.739 10.890 1.00 56.08 O ANISOU 1060 O ILE A 188 9201 6164 5942 -737 482 228 O ATOM 1061 CB ILE A 188 18.060 3.625 7.947 1.00 53.86 C ANISOU 1061 CB ILE A 188 8890 5680 5895 -658 386 164 C ATOM 1062 CG1 ILE A 188 16.743 2.880 8.259 1.00 55.90 C ANISOU 1062 CG1 ILE A 188 9199 5901 6141 -860 512 149 C ATOM 1063 CG2 ILE A 188 19.316 2.788 8.229 1.00 54.12 C ANISOU 1063 CG2 ILE A 188 9099 5588 5878 -533 327 277 C ATOM 1064 CD1 ILE A 188 15.463 3.433 7.570 1.00 63.01 C ANISOU 1064 CD1 ILE A 188 9905 6913 7122 -973 556 16 C ATOM 1065 N PRO A 189 19.731 5.391 10.569 1.00 51.59 N ANISOU 1065 N PRO A 189 8609 5615 5378 -468 288 264 N ATOM 1066 CA PRO A 189 19.975 5.389 12.025 1.00 52.39 C ANISOU 1066 CA PRO A 189 8812 5765 5330 -470 298 338 C ATOM 1067 C PRO A 189 19.146 6.423 12.795 1.00 57.05 C ANISOU 1067 C PRO A 189 9308 6496 5872 -563 371 263 C ATOM 1068 O PRO A 189 18.957 6.244 13.991 1.00 58.01 O ANISOU 1068 O PRO A 189 9529 6653 5860 -616 421 316 O ATOM 1069 CB PRO A 189 21.465 5.724 12.137 1.00 53.59 C ANISOU 1069 CB PRO A 189 8953 5959 5451 -301 168 369 C ATOM 1070 CG PRO A 189 22.036 5.400 10.818 1.00 57.21 C ANISOU 1070 CG PRO A 189 9374 6333 6030 -215 109 354 C ATOM 1071 CD PRO A 189 20.965 5.761 9.852 1.00 51.88 C ANISOU 1071 CD PRO A 189 8585 5658 5468 -314 174 255 C ATOM 1072 N VAL A 190 18.648 7.490 12.124 1.00 52.49 N ANISOU 1072 N VAL A 190 8551 5997 5397 -573 381 142 N ATOM 1073 CA VAL A 190 17.836 8.540 12.753 1.00 52.07 C ANISOU 1073 CA VAL A 190 8396 6069 5318 -637 454 53 C ATOM 1074 C VAL A 190 16.473 7.948 13.234 1.00 57.20 C ANISOU 1074 C VAL A 190 9074 6726 5932 -800 594 48 C ATOM 1075 O VAL A 190 16.279 7.940 14.450 1.00 57.61 O ANISOU 1075 O VAL A 190 9198 6835 5856 -858 657 74 O ATOM 1076 CB VAL A 190 17.669 9.802 11.858 1.00 54.22 C ANISOU 1076 CB VAL A 190 8487 6401 5714 -583 426 -63 C ATOM 1077 CG1 VAL A 190 16.635 10.762 12.437 1.00 54.49 C ANISOU 1077 CG1 VAL A 190 8423 6545 5735 -641 517 -161 C ATOM 1078 CG2 VAL A 190 19.005 10.511 11.658 1.00 52.98 C ANISOU 1078 CG2 VAL A 190 8309 6253 5570 -457 314 -65 C ATOM 1079 N PRO A 191 15.549 7.415 12.375 1.00 54.45 N ANISOU 1079 N PRO A 191 8673 6334 5681 -886 648 12 N ATOM 1080 CA PRO A 191 14.282 6.880 12.918 1.00 55.68 C ANISOU 1080 CA PRO A 191 8841 6517 5798 -1061 791 -4 C ATOM 1081 C PRO A 191 14.435 5.629 13.801 1.00 61.32 C ANISOU 1081 C PRO A 191 9782 7132 6386 -1148 850 127 C ATOM 1082 O PRO A 191 13.614 5.447 14.700 1.00 62.32 O ANISOU 1082 O PRO A 191 9943 7312 6424 -1283 976 128 O ATOM 1083 CB PRO A 191 13.455 6.565 11.669 1.00 57.02 C ANISOU 1083 CB PRO A 191 8896 6666 6103 -1124 807 -77 C ATOM 1084 CG PRO A 191 14.433 6.417 10.583 1.00 60.33 C ANISOU 1084 CG PRO A 191 9339 6987 6596 -997 681 -47 C ATOM 1085 CD PRO A 191 15.559 7.345 10.897 1.00 54.90 C ANISOU 1085 CD PRO A 191 8645 6338 5877 -841 587 -29 C ATOM 1086 N ILE A 192 15.467 4.784 13.562 1.00 57.86 N ANISOU 1086 N ILE A 192 9501 6549 5934 -1064 766 237 N ATOM 1087 CA ILE A 192 15.726 3.561 14.346 1.00 59.31 C ANISOU 1087 CA ILE A 192 9931 6607 5998 -1110 806 382 C ATOM 1088 C ILE A 192 16.124 3.939 15.792 1.00 65.18 C ANISOU 1088 C ILE A 192 10759 7444 6562 -1082 812 446 C ATOM 1089 O ILE A 192 15.657 3.296 16.734 1.00 66.47 O ANISOU 1089 O ILE A 192 11069 7586 6600 -1202 920 522 O ATOM 1090 CB ILE A 192 16.782 2.639 13.655 1.00 61.81 C ANISOU 1090 CB ILE A 192 10383 6748 6354 -985 702 475 C ATOM 1091 CG1 ILE A 192 16.198 2.003 12.365 1.00 61.75 C ANISOU 1091 CG1 ILE A 192 10339 6631 6492 -1062 732 413 C ATOM 1092 CG2 ILE A 192 17.316 1.552 14.608 1.00 64.13 C ANISOU 1092 CG2 ILE A 192 10948 6916 6504 -967 715 646 C ATOM 1093 CD1 ILE A 192 17.204 1.256 11.461 1.00 66.68 C ANISOU 1093 CD1 ILE A 192 11057 7096 7183 -924 631 463 C ATOM 1094 N LYS A 193 16.970 4.974 15.958 1.00 61.81 N ANISOU 1094 N LYS A 193 10245 7124 6117 -937 702 411 N ATOM 1095 CA LYS A 193 17.413 5.454 17.271 1.00 62.97 C ANISOU 1095 CA LYS A 193 10452 7384 6091 -907 690 446 C ATOM 1096 C LYS A 193 16.328 6.294 17.936 1.00 68.20 C ANISOU 1096 C LYS A 193 11008 8193 6712 -1033 818 337 C ATOM 1097 O LYS A 193 16.088 6.133 19.130 1.00 69.45 O ANISOU 1097 O LYS A 193 11280 8407 6703 -1111 899 387 O ATOM 1098 CB LYS A 193 18.716 6.264 17.166 1.00 64.61 C ANISOU 1098 CB LYS A 193 10589 7661 6301 -730 531 423 C ATOM 1099 CG LYS A 193 19.967 5.408 17.036 1.00 80.31 C ANISOU 1099 CG LYS A 193 12712 9553 8248 -586 405 554 C ATOM 1100 CD LYS A 193 20.784 5.422 18.314 1.00 92.37 C ANISOU 1100 CD LYS A 193 14351 11173 9572 -520 342 635 C ATOM 1101 CE LYS A 193 22.030 6.251 18.162 1.00101.21 C ANISOU 1101 CE LYS A 193 15367 12383 10704 -360 181 596 C ATOM 1102 NZ LYS A 193 22.847 6.224 19.400 1.00112.38 N ANISOU 1102 NZ LYS A 193 16881 13907 11911 -289 101 671 N ATOM 1103 N GLY A 194 15.705 7.186 17.163 1.00 64.37 N ANISOU 1103 N GLY A 194 10312 7772 6372 -1040 836 192 N ATOM 1104 CA GLY A 194 14.643 8.073 17.627 1.00 65.26 C ANISOU 1104 CA GLY A 194 10292 8025 6478 -1129 953 67 C ATOM 1105 C GLY A 194 15.111 9.254 18.455 1.00 71.13 C ANISOU 1105 C GLY A 194 10998 8897 7132 -1058 922 1 C ATOM 1106 O GLY A 194 16.278 9.324 18.855 1.00 70.54 O ANISOU 1106 O GLY A 194 11015 8821 6966 -963 813 64 O ATOM 1107 N ILE A 195 14.190 10.200 18.713 1.00 69.52 N ANISOU 1107 N ILE A 195 10649 8809 6956 -1101 1018 -138 N ATOM 1108 CA ILE A 195 14.442 11.398 19.517 1.00 69.86 C ANISOU 1108 CA ILE A 195 10653 8969 6923 -1053 1015 -232 C ATOM 1109 C ILE A 195 13.605 11.322 20.792 1.00 76.76 C ANISOU 1109 C ILE A 195 11579 9953 7634 -1179 1172 -255 C ATOM 1110 O ILE A 195 12.404 11.047 20.722 1.00 76.90 O ANISOU 1110 O ILE A 195 11526 10002 7689 -1291 1310 -297 O ATOM 1111 CB ILE A 195 14.158 12.691 18.714 1.00 71.56 C ANISOU 1111 CB ILE A 195 10673 9212 7304 -970 996 -382 C ATOM 1112 N GLU A 196 14.247 11.526 21.957 1.00 75.66 N ANISOU 1112 N GLU A 196 11557 9885 7305 -1169 1152 -230 N ATOM 1113 CA GLU A 196 13.580 11.482 23.263 1.00 78.18 C ANISOU 1113 CA GLU A 196 11949 10322 7433 -1286 1298 -248 C ATOM 1114 C GLU A 196 12.709 12.727 23.485 1.00 84.11 C ANISOU 1114 C GLU A 196 12532 11195 8231 -1298 1410 -446 C ATOM 1115 O GLU A 196 12.997 13.790 22.925 1.00 82.67 O ANISOU 1115 O GLU A 196 12226 11008 8178 -1189 1339 -558 O ATOM 1116 CB GLU A 196 14.609 11.341 24.396 1.00 80.56 C ANISOU 1116 CB GLU A 196 12431 10675 7502 -1255 1221 -162 C ATOM 1117 CG GLU A 196 14.817 9.908 24.851 1.00 91.91 C ANISOU 1117 CG GLU A 196 14089 12051 8782 -1322 1241 37 C ATOM 1118 N THR A 197 11.643 12.582 24.304 1.00 83.26 N ANISOU 1118 N THR A 197 12428 11191 8016 -1430 1593 -487 N ATOM 1119 CA THR A 197 10.691 13.647 24.648 1.00114.50 C ANISOU 1119 CA THR A 197 16231 15277 11996 -1445 1729 -678 C ATOM 1120 C THR A 197 11.358 14.760 25.464 1.00141.94 C ANISOU 1120 C THR A 197 19740 18831 15360 -1370 1687 -779 C ATOM 1121 O THR A 197 12.312 14.513 26.198 1.00103.21 O ANISOU 1121 O THR A 197 14998 13936 10282 -1362 1599 -693 O ATOM 1122 CB THR A 197 9.507 13.062 25.420 1.00124.49 C ANISOU 1122 CB THR A 197 17511 16645 13146 -1620 1942 -683 C ATOM 1123 N ASN A 201 8.793 13.844 31.415 1.00127.98 N ANISOU 1123 N ASN A 201 18391 17711 12525 -1976 2474 -851 N ATOM 1124 CA ASN A 201 7.517 14.391 31.866 1.00129.31 C ANISOU 1124 CA ASN A 201 18409 18029 12694 -2058 2708 -1034 C ATOM 1125 C ASN A 201 6.816 15.224 30.756 1.00131.11 C ANISOU 1125 C ASN A 201 18353 18228 13234 -1952 2714 -1208 C ATOM 1126 O ASN A 201 5.649 14.920 30.494 1.00131.54 O ANISOU 1126 O ASN A 201 18258 18338 13382 -2041 2873 -1259 O ATOM 1127 CB ASN A 201 7.675 15.216 33.154 1.00132.42 C ANISOU 1127 CB ASN A 201 18877 18587 12849 -2065 2783 -1164 C ATOM 1128 CG ASN A 201 8.263 14.451 34.316 1.00156.82 C ANISOU 1128 CG ASN A 201 22247 21733 15606 -2155 2770 -1000 C ATOM 1129 OD1 ASN A 201 9.413 14.670 34.712 1.00151.22 O ANISOU 1129 OD1 ASN A 201 21663 21026 14767 -2068 2601 -970 O ATOM 1130 ND2 ASN A 201 7.486 13.550 34.904 1.00150.24 N ANISOU 1130 ND2 ASN A 201 21515 20953 14616 -2332 2948 -891 N ATOM 1131 N PRO A 202 7.445 16.234 30.074 1.00125.18 N ANISOU 1131 N PRO A 202 17519 17399 12644 -1771 2553 -1299 N ATOM 1132 CA PRO A 202 6.700 16.971 29.031 1.00123.55 C ANISOU 1132 CA PRO A 202 17062 17163 12718 -1663 2568 -1445 C ATOM 1133 C PRO A 202 6.370 16.107 27.804 1.00124.58 C ANISOU 1133 C PRO A 202 17097 17195 13043 -1684 2523 -1335 C ATOM 1134 O PRO A 202 7.189 15.290 27.373 1.00122.89 O ANISOU 1134 O PRO A 202 17007 16853 12834 -1690 2380 -1159 O ATOM 1135 CB PRO A 202 7.638 18.128 28.666 1.00123.81 C ANISOU 1135 CB PRO A 202 17095 17103 12842 -1487 2395 -1520 C ATOM 1136 CG PRO A 202 8.992 17.654 29.028 1.00127.89 C ANISOU 1136 CG PRO A 202 17829 17565 13198 -1503 2236 -1362 C ATOM 1137 CD PRO A 202 8.815 16.774 30.229 1.00125.71 C ANISOU 1137 CD PRO A 202 17712 17409 12644 -1663 2360 -1280 C ATOM 1138 N ASN A 203 5.149 16.292 27.256 1.00120.24 N ANISOU 1138 N ASN A 203 16320 16716 12650 -1693 2647 -1451 N ATOM 1139 CA ASN A 203 4.620 15.570 26.089 1.00118.36 C ANISOU 1139 CA ASN A 203 15950 16423 12597 -1725 2624 -1391 C ATOM 1140 C ASN A 203 5.111 16.176 24.759 1.00117.21 C ANISOU 1140 C ASN A 203 15712 16141 12683 -1536 2427 -1396 C ATOM 1141 O ASN A 203 4.739 15.689 23.688 1.00115.85 O ANISOU 1141 O ASN A 203 15435 15919 12664 -1543 2380 -1350 O ATOM 1142 CB ASN A 203 3.089 15.558 26.127 1.00121.49 C ANISOU 1142 CB ASN A 203 16116 16987 13057 -1805 2829 -1532 C ATOM 1143 N ASN A 204 5.945 17.230 24.835 1.00110.88 N ANISOU 1143 N ASN A 204 14952 15281 11895 -1380 2320 -1455 N ATOM 1144 CA ASN A 204 6.521 17.922 23.683 1.00107.60 C ANISOU 1144 CA ASN A 204 14478 14731 11674 -1205 2145 -1459 C ATOM 1145 C ASN A 204 8.024 17.663 23.590 1.00106.40 C ANISOU 1145 C ASN A 204 14521 14447 11459 -1178 1965 -1321 C ATOM 1146 O ASN A 204 8.701 17.588 24.620 1.00106.96 O ANISOU 1146 O ASN A 204 14757 14549 11334 -1233 1966 -1287 O ATOM 1147 CB ASN A 204 6.243 19.426 23.769 1.00109.99 C ANISOU 1147 CB ASN A 204 14667 15057 12067 -1048 2177 -1649 C ATOM 1148 CG ASN A 204 4.934 19.861 23.151 1.00136.68 C ANISOU 1148 CG ASN A 204 17799 18519 15613 -978 2273 -1774 C ATOM 1149 OD1 ASN A 204 3.923 19.144 23.166 1.00132.36 O ANISOU 1149 OD1 ASN A 204 17139 18080 15070 -1090 2378 -1767 O ATOM 1150 ND2 ASN A 204 4.919 21.070 22.611 1.00129.09 N ANISOU 1150 ND2 ASN A 204 16747 17510 14790 -790 2241 -1896 N ATOM 1151 N ILE A 205 8.542 17.540 22.353 1.00 97.55 N ANISOU 1151 N ILE A 205 13373 13194 10498 -1088 1809 -1247 N ATOM 1152 CA ILE A 205 9.959 17.291 22.090 1.00 94.32 C ANISOU 1152 CA ILE A 205 13113 12666 10060 -1047 1634 -1125 C ATOM 1153 C ILE A 205 10.584 18.436 21.283 1.00 92.67 C ANISOU 1153 C ILE A 205 12845 12361 10004 -886 1516 -1191 C ATOM 1154 O ILE A 205 9.867 19.206 20.641 1.00 92.12 O ANISOU 1154 O ILE A 205 12626 12288 10088 -797 1551 -1294 O ATOM 1155 CB ILE A 205 10.134 15.940 21.356 1.00 96.63 C ANISOU 1155 CB ILE A 205 13459 12877 10379 -1110 1566 -953 C ATOM 1156 N THR A 206 11.923 18.552 21.337 1.00 84.98 N ANISOU 1156 N THR A 206 11990 11315 8984 -850 1379 -1133 N ATOM 1157 CA THR A 206 12.701 19.535 20.577 1.00 81.90 C ANISOU 1157 CA THR A 206 11572 10821 8724 -727 1267 -1177 C ATOM 1158 C THR A 206 13.360 18.748 19.425 1.00 79.71 C ANISOU 1158 C THR A 206 11308 10439 8538 -699 1129 -1031 C ATOM 1159 O THR A 206 14.205 17.885 19.674 1.00 78.92 O ANISOU 1159 O THR A 206 11323 10327 8337 -741 1050 -914 O ATOM 1160 CB THR A 206 13.667 20.345 21.487 1.00 90.64 C ANISOU 1160 CB THR A 206 12777 11946 9718 -722 1233 -1255 C ATOM 1161 OG1 THR A 206 14.681 20.962 20.690 1.00 90.03 O ANISOU 1161 OG1 THR A 206 12703 11757 9748 -642 1103 -1251 O ATOM 1162 CG2 THR A 206 14.312 19.506 22.593 1.00 90.28 C ANISOU 1162 CG2 THR A 206 12875 11987 9441 -821 1211 -1174 C ATOM 1163 N CYS A 207 12.902 18.992 18.178 1.00 72.02 N ANISOU 1163 N CYS A 207 10218 9400 7747 -621 1106 -1039 N ATOM 1164 CA CYS A 207 13.346 18.273 16.977 1.00 68.78 C ANISOU 1164 CA CYS A 207 9805 8898 7431 -593 993 -921 C ATOM 1165 C CYS A 207 14.762 18.687 16.538 1.00 67.40 C ANISOU 1165 C CYS A 207 9695 8635 7279 -528 859 -886 C ATOM 1166 O CYS A 207 14.957 19.570 15.692 1.00 66.13 O ANISOU 1166 O CYS A 207 9482 8402 7244 -437 816 -928 O ATOM 1167 CB CYS A 207 12.342 18.432 15.843 1.00 68.71 C ANISOU 1167 CB CYS A 207 9648 8874 7585 -533 1011 -952 C ATOM 1168 SG CYS A 207 12.202 16.977 14.777 1.00 72.01 S ANISOU 1168 SG CYS A 207 10054 9253 8054 -586 954 -823 S ATOM 1169 N VAL A 208 15.744 18.006 17.131 1.00 60.66 N ANISOU 1169 N VAL A 208 8958 7794 6297 -576 797 -804 N ATOM 1170 CA VAL A 208 17.176 18.191 16.924 1.00 58.12 C ANISOU 1170 CA VAL A 208 8691 7427 5964 -534 671 -768 C ATOM 1171 C VAL A 208 17.886 16.917 17.404 1.00 59.56 C ANISOU 1171 C VAL A 208 8985 7633 6013 -576 608 -636 C ATOM 1172 O VAL A 208 17.427 16.274 18.352 1.00 60.00 O ANISOU 1172 O VAL A 208 9109 7754 5933 -649 674 -604 O ATOM 1173 CB VAL A 208 17.708 19.486 17.627 1.00 61.81 C ANISOU 1173 CB VAL A 208 9170 7922 6392 -525 675 -896 C ATOM 1174 CG1 VAL A 208 17.509 19.450 19.144 1.00 63.15 C ANISOU 1174 CG1 VAL A 208 9411 8210 6373 -602 743 -945 C ATOM 1175 CG2 VAL A 208 19.163 19.776 17.272 1.00 60.67 C ANISOU 1175 CG2 VAL A 208 9049 7738 6266 -494 550 -879 C ATOM 1176 N LEU A 209 18.975 16.542 16.724 1.00 53.55 N ANISOU 1176 N LEU A 209 8242 6814 5289 -523 487 -557 N ATOM 1177 CA LEU A 209 19.794 15.397 17.105 1.00 53.18 C ANISOU 1177 CA LEU A 209 8299 6777 5128 -524 409 -430 C ATOM 1178 C LEU A 209 20.800 15.893 18.146 1.00 59.05 C ANISOU 1178 C LEU A 209 9088 7615 5731 -521 344 -466 C ATOM 1179 O LEU A 209 21.437 16.920 17.915 1.00 58.83 O ANISOU 1179 O LEU A 209 8999 7594 5760 -495 300 -558 O ATOM 1180 CB LEU A 209 20.480 14.765 15.871 1.00 51.55 C ANISOU 1180 CB LEU A 209 8079 6476 5032 -455 315 -343 C ATOM 1181 CG LEU A 209 19.560 14.298 14.727 1.00 54.33 C ANISOU 1181 CG LEU A 209 8377 6742 5522 -460 363 -324 C ATOM 1182 CD1 LEU A 209 20.353 13.912 13.504 1.00 52.75 C ANISOU 1182 CD1 LEU A 209 8151 6461 5430 -385 271 -275 C ATOM 1183 CD2 LEU A 209 18.687 13.135 15.145 1.00 57.11 C ANISOU 1183 CD2 LEU A 209 8806 7082 5811 -537 436 -247 C ATOM 1184 N THR A 210 20.864 15.245 19.325 1.00 57.39 N ANISOU 1184 N THR A 210 8988 7485 5332 -561 349 -406 N ATOM 1185 CA THR A 210 21.762 15.667 20.413 1.00 58.52 C ANISOU 1185 CA THR A 210 9174 7750 5310 -563 281 -445 C ATOM 1186 C THR A 210 23.149 15.036 20.248 1.00 63.69 C ANISOU 1186 C THR A 210 9855 8418 5926 -480 121 -346 C ATOM 1187 O THR A 210 23.271 13.971 19.640 1.00 63.19 O ANISOU 1187 O THR A 210 9830 8271 5910 -428 85 -218 O ATOM 1188 CB THR A 210 21.174 15.348 21.805 1.00 64.83 C ANISOU 1188 CB THR A 210 10083 8650 5899 -638 362 -432 C ATOM 1189 OG1 THR A 210 21.030 13.936 21.966 1.00 66.31 O ANISOU 1189 OG1 THR A 210 10387 8798 6008 -642 368 -261 O ATOM 1190 CG2 THR A 210 19.853 16.060 22.072 1.00 60.38 C ANISOU 1190 CG2 THR A 210 9473 8106 5364 -713 524 -559 C ATOM 1191 N LYS A 211 24.190 15.704 20.790 1.00 61.14 N ANISOU 1191 N LYS A 211 9504 8206 5519 -469 28 -419 N ATOM 1192 CA LYS A 211 25.583 15.253 20.742 1.00 61.39 C ANISOU 1192 CA LYS A 211 9527 8297 5502 -385 -132 -355 C ATOM 1193 C LYS A 211 25.778 13.969 21.582 1.00 67.41 C ANISOU 1193 C LYS A 211 10432 9108 6074 -337 -186 -192 C ATOM 1194 O LYS A 211 26.628 13.140 21.244 1.00 67.59 O ANISOU 1194 O LYS A 211 10468 9117 6097 -231 -299 -82 O ATOM 1195 CB LYS A 211 26.517 16.375 21.235 1.00 64.34 C ANISOU 1195 CB LYS A 211 9822 8802 5820 -414 -204 -501 C ATOM 1196 CG LYS A 211 28.008 16.116 21.023 1.00 77.61 C ANISOU 1196 CG LYS A 211 11434 10561 7494 -333 -368 -474 C ATOM 1197 CD LYS A 211 28.862 17.142 21.748 1.00 87.93 C ANISOU 1197 CD LYS A 211 12672 12033 8703 -390 -438 -625 C ATOM 1198 CE LYS A 211 30.213 16.586 22.119 1.00 98.15 C ANISOU 1198 CE LYS A 211 13927 13482 9885 -303 -615 -570 C ATOM 1199 NZ LYS A 211 31.071 17.612 22.766 1.00107.98 N ANISOU 1199 NZ LYS A 211 15083 14905 11040 -378 -688 -739 N ATOM 1200 N GLU A 212 24.987 13.807 22.664 1.00 64.67 N ANISOU 1200 N GLU A 212 10196 8813 5561 -408 -100 -175 N ATOM 1201 CA GLU A 212 25.069 12.645 23.549 1.00 65.71 C ANISOU 1201 CA GLU A 212 10494 8982 5490 -375 -133 -12 C ATOM 1202 C GLU A 212 24.489 11.379 22.885 1.00 68.58 C ANISOU 1202 C GLU A 212 10951 9171 5935 -352 -76 147 C ATOM 1203 O GLU A 212 25.071 10.302 23.020 1.00 69.32 O ANISOU 1203 O GLU A 212 11158 9234 5946 -260 -159 305 O ATOM 1204 CB GLU A 212 24.351 12.933 24.874 1.00 68.57 C ANISOU 1204 CB GLU A 212 10951 9460 5643 -478 -39 -52 C ATOM 1205 N ARG A 213 23.365 11.519 22.157 1.00 62.91 N ANISOU 1205 N ARG A 213 10185 8340 5376 -432 61 100 N ATOM 1206 CA ARG A 213 22.665 10.415 21.501 1.00 61.91 C ANISOU 1206 CA ARG A 213 10134 8053 5336 -446 133 217 C ATOM 1207 C ARG A 213 23.106 10.162 20.052 1.00 63.56 C ANISOU 1207 C ARG A 213 10257 8137 5755 -362 68 230 C ATOM 1208 O ARG A 213 23.113 9.007 19.632 1.00 63.76 O ANISOU 1208 O ARG A 213 10380 8041 5806 -323 59 357 O ATOM 1209 CB ARG A 213 21.154 10.686 21.510 1.00 62.16 C ANISOU 1209 CB ARG A 213 10142 8060 5416 -585 315 146 C ATOM 1210 CG ARG A 213 20.339 9.646 22.256 1.00 74.95 C ANISOU 1210 CG ARG A 213 11934 9647 6898 -676 426 268 C ATOM 1211 CD ARG A 213 19.645 8.700 21.296 1.00 83.07 C ANISOU 1211 CD ARG A 213 12982 10509 8072 -718 497 334 C ATOM 1212 NE ARG A 213 18.194 8.890 21.279 1.00 88.13 N ANISOU 1212 NE ARG A 213 13564 11161 8760 -866 673 253 N ATOM 1213 CZ ARG A 213 17.342 8.254 22.076 1.00103.26 C ANISOU 1213 CZ ARG A 213 15600 13081 10551 -995 810 314 C ATOM 1214 NH1 ARG A 213 17.786 7.390 22.983 1.00 92.25 N ANISOU 1214 NH1 ARG A 213 14419 11666 8965 -991 792 472 N ATOM 1215 NH2 ARG A 213 16.041 8.480 21.980 1.00 91.30 N ANISOU 1215 NH2 ARG A 213 13994 11599 9098 -1127 969 220 N ATOM 1216 N PHE A 214 23.429 11.222 19.279 1.00 57.62 N ANISOU 1216 N PHE A 214 9339 7405 5149 -342 36 100 N ATOM 1217 CA PHE A 214 23.765 11.094 17.858 1.00 55.29 C ANISOU 1217 CA PHE A 214 8957 7003 5046 -276 -8 100 C ATOM 1218 C PHE A 214 25.199 11.538 17.498 1.00 57.79 C ANISOU 1218 C PHE A 214 9182 7380 5395 -173 -149 67 C ATOM 1219 O PHE A 214 25.509 11.662 16.310 1.00 55.64 O ANISOU 1219 O PHE A 214 8819 7040 5280 -130 -173 40 O ATOM 1220 CB PHE A 214 22.738 11.882 17.018 1.00 55.68 C ANISOU 1220 CB PHE A 214 8893 7002 5259 -346 94 -11 C ATOM 1221 CG PHE A 214 21.388 11.206 16.975 1.00 57.59 C ANISOU 1221 CG PHE A 214 9190 7174 5518 -435 221 26 C ATOM 1222 CD1 PHE A 214 20.423 11.479 17.940 1.00 61.66 C ANISOU 1222 CD1 PHE A 214 9734 7759 5936 -537 335 -15 C ATOM 1223 CD2 PHE A 214 21.097 10.259 16.000 1.00 59.16 C ANISOU 1223 CD2 PHE A 214 9409 7246 5823 -428 233 91 C ATOM 1224 CE1 PHE A 214 19.193 10.820 17.929 1.00 63.07 C ANISOU 1224 CE1 PHE A 214 9947 7889 6126 -637 460 12 C ATOM 1225 CE2 PHE A 214 19.859 9.613 15.979 1.00 62.73 C ANISOU 1225 CE2 PHE A 214 9901 7644 6288 -534 352 112 C ATOM 1226 CZ PHE A 214 18.916 9.897 16.944 1.00 61.93 C ANISOU 1226 CZ PHE A 214 9815 7622 6094 -641 466 73 C ATOM 1227 N GLY A 215 26.057 11.709 18.505 1.00 55.80 N ANISOU 1227 N GLY A 215 8951 7263 4987 -138 -239 69 N ATOM 1228 CA GLY A 215 27.450 12.114 18.330 1.00 56.08 C ANISOU 1228 CA GLY A 215 8883 7393 5031 -55 -374 27 C ATOM 1229 C GLY A 215 28.218 11.272 17.331 1.00 60.75 C ANISOU 1229 C GLY A 215 9453 7907 5722 69 -452 110 C ATOM 1230 O GLY A 215 28.813 11.813 16.393 1.00 58.95 O ANISOU 1230 O GLY A 215 9092 7678 5627 93 -484 37 O ATOM 1231 N ASP A 216 28.174 9.936 17.507 1.00 59.62 N ANISOU 1231 N ASP A 216 9450 7686 5515 146 -470 263 N ATOM 1232 CA ASP A 216 28.835 8.981 16.615 1.00 59.79 C ANISOU 1232 CA ASP A 216 9479 7613 5623 279 -533 347 C ATOM 1233 C ASP A 216 28.169 8.967 15.240 1.00 61.65 C ANISOU 1233 C ASP A 216 9668 7699 6057 236 -445 310 C ATOM 1234 O ASP A 216 28.873 8.832 14.237 1.00 60.26 O ANISOU 1234 O ASP A 216 9409 7493 5992 319 -494 295 O ATOM 1235 CB ASP A 216 28.847 7.567 17.220 1.00 63.56 C ANISOU 1235 CB ASP A 216 10155 8016 5980 367 -558 522 C ATOM 1236 CG ASP A 216 29.889 7.351 18.304 1.00 77.31 C ANISOU 1236 CG ASP A 216 11929 9908 7536 488 -698 586 C ATOM 1237 OD1 ASP A 216 31.016 7.889 18.168 1.00 77.81 O ANISOU 1237 OD1 ASP A 216 11837 10111 7616 568 -814 515 O ATOM 1238 OD2 ASP A 216 29.599 6.600 19.261 1.00 85.45 O ANISOU 1238 OD2 ASP A 216 13143 10923 8402 504 -694 712 O ATOM 1239 N PHE A 217 26.823 9.132 15.190 1.00 57.41 N ANISOU 1239 N PHE A 217 9171 7087 5556 108 -317 286 N ATOM 1240 CA PHE A 217 26.097 9.179 13.921 1.00 55.92 C ANISOU 1240 CA PHE A 217 8930 6782 5538 62 -240 242 C ATOM 1241 C PHE A 217 26.556 10.390 13.106 1.00 59.68 C ANISOU 1241 C PHE A 217 9235 7314 6129 61 -262 120 C ATOM 1242 O PHE A 217 26.765 10.275 11.904 1.00 57.75 O ANISOU 1242 O PHE A 217 8933 7001 6008 98 -267 106 O ATOM 1243 CB PHE A 217 24.565 9.203 14.117 1.00 57.21 C ANISOU 1243 CB PHE A 217 9141 6893 5705 -74 -107 227 C ATOM 1244 CG PHE A 217 23.836 9.529 12.831 1.00 56.95 C ANISOU 1244 CG PHE A 217 9015 6787 5838 -120 -45 156 C ATOM 1245 CD1 PHE A 217 23.763 8.597 11.799 1.00 59.14 C ANISOU 1245 CD1 PHE A 217 9323 6941 6206 -90 -43 200 C ATOM 1246 CD2 PHE A 217 23.304 10.796 12.615 1.00 58.00 C ANISOU 1246 CD2 PHE A 217 9030 6975 6031 -179 4 41 C ATOM 1247 CE1 PHE A 217 23.141 8.918 10.590 1.00 58.68 C ANISOU 1247 CE1 PHE A 217 9175 6839 6283 -126 -1 132 C ATOM 1248 CE2 PHE A 217 22.690 11.119 11.401 1.00 59.54 C ANISOU 1248 CE2 PHE A 217 9141 7115 6368 -198 43 -14 C ATOM 1249 CZ PHE A 217 22.608 10.176 10.398 1.00 57.17 C ANISOU 1249 CZ PHE A 217 8867 6715 6142 -174 37 32 C ATOM 1250 N MET A 218 26.708 11.536 13.773 1.00 58.22 N ANISOU 1250 N MET A 218 8983 7245 5892 11 -268 31 N ATOM 1251 CA MET A 218 27.154 12.795 13.196 1.00 58.15 C ANISOU 1251 CA MET A 218 8837 7282 5974 -11 -276 -88 C ATOM 1252 C MET A 218 28.569 12.666 12.635 1.00 63.58 C ANISOU 1252 C MET A 218 9445 8015 6698 82 -378 -85 C ATOM 1253 O MET A 218 28.864 13.226 11.584 1.00 62.53 O ANISOU 1253 O MET A 218 9218 7859 6683 77 -368 -145 O ATOM 1254 CB MET A 218 27.092 13.886 14.275 1.00 61.40 C ANISOU 1254 CB MET A 218 9229 7804 6297 -88 -260 -182 C ATOM 1255 CG MET A 218 26.298 15.127 13.882 1.00 64.70 C ANISOU 1255 CG MET A 218 9587 8184 6813 -169 -166 -296 C ATOM 1256 SD MET A 218 24.763 14.956 12.914 1.00 67.96 S ANISOU 1256 SD MET A 218 10007 8461 7353 -194 -53 -280 S ATOM 1257 CE MET A 218 23.761 14.137 14.087 1.00 65.87 C ANISOU 1257 CE MET A 218 9855 8217 6955 -247 10 -221 C ATOM 1258 N LEU A 219 29.425 11.889 13.310 1.00 62.81 N ANISOU 1258 N LEU A 219 9386 7986 6494 173 -473 -12 N ATOM 1259 CA LEU A 219 30.810 11.670 12.910 1.00 63.49 C ANISOU 1259 CA LEU A 219 9379 8143 6601 279 -576 -12 C ATOM 1260 C LEU A 219 30.916 10.712 11.707 1.00 67.70 C ANISOU 1260 C LEU A 219 9928 8551 7243 370 -569 53 C ATOM 1261 O LEU A 219 31.444 11.112 10.666 1.00 66.93 O ANISOU 1261 O LEU A 219 9721 8453 7255 380 -566 -5 O ATOM 1262 CB LEU A 219 31.604 11.128 14.101 1.00 65.36 C ANISOU 1262 CB LEU A 219 9652 8510 6673 366 -689 46 C ATOM 1263 CG LEU A 219 33.082 11.441 14.103 1.00 71.28 C ANISOU 1263 CG LEU A 219 10249 9423 7410 438 -806 -11 C ATOM 1264 CD1 LEU A 219 33.516 11.922 15.461 1.00 73.25 C ANISOU 1264 CD1 LEU A 219 10482 9859 7491 413 -887 -50 C ATOM 1265 CD2 LEU A 219 33.895 10.227 13.696 1.00 74.96 C ANISOU 1265 CD2 LEU A 219 10720 9871 7890 621 -887 87 C ATOM 1266 N PHE A 220 30.414 9.468 11.842 1.00 64.71 N ANISOU 1266 N PHE A 220 9696 8062 6829 426 -557 168 N ATOM 1267 CA PHE A 220 30.508 8.458 10.787 1.00 64.62 C ANISOU 1267 CA PHE A 220 9725 7919 6909 513 -548 223 C ATOM 1268 C PHE A 220 29.530 8.708 9.620 1.00 65.59 C ANISOU 1268 C PHE A 220 9834 7926 7161 421 -446 175 C ATOM 1269 O PHE A 220 29.830 8.316 8.490 1.00 64.42 O ANISOU 1269 O PHE A 220 9660 7711 7106 477 -442 170 O ATOM 1270 CB PHE A 220 30.350 7.045 11.365 1.00 68.24 C ANISOU 1270 CB PHE A 220 10365 8280 7283 596 -564 359 C ATOM 1271 CG PHE A 220 31.436 6.735 12.373 1.00 72.26 C ANISOU 1271 CG PHE A 220 10887 8908 7661 728 -685 421 C ATOM 1272 CD1 PHE A 220 32.762 6.595 11.973 1.00 76.54 C ANISOU 1272 CD1 PHE A 220 11318 9531 8231 880 -784 407 C ATOM 1273 CD2 PHE A 220 31.143 6.633 13.727 1.00 76.12 C ANISOU 1273 CD2 PHE A 220 11487 9447 7987 704 -702 487 C ATOM 1274 CE1 PHE A 220 33.770 6.345 12.909 1.00 79.43 C ANISOU 1274 CE1 PHE A 220 11674 10034 8470 1016 -911 458 C ATOM 1275 CE2 PHE A 220 32.151 6.377 14.660 1.00 80.91 C ANISOU 1275 CE2 PHE A 220 12103 10183 8455 836 -829 547 C ATOM 1276 CZ PHE A 220 33.457 6.234 14.245 1.00 79.65 C ANISOU 1276 CZ PHE A 220 11822 10111 8331 997 -940 532 C ATOM 1277 N GLY A 221 28.420 9.394 9.889 1.00 60.47 N ANISOU 1277 N GLY A 221 9196 7270 6512 291 -368 135 N ATOM 1278 CA GLY A 221 27.445 9.779 8.872 1.00 58.26 C ANISOU 1278 CA GLY A 221 8884 6911 6341 211 -285 84 C ATOM 1279 C GLY A 221 28.037 10.788 7.912 1.00 59.72 C ANISOU 1279 C GLY A 221 8933 7139 6617 215 -294 0 C ATOM 1280 O GLY A 221 27.840 10.671 6.703 1.00 58.41 O ANISOU 1280 O GLY A 221 8745 6906 6542 220 -265 -14 O ATOM 1281 N SER A 222 28.806 11.761 8.449 1.00 55.94 N ANISOU 1281 N SER A 222 8372 6776 6107 204 -332 -56 N ATOM 1282 CA SER A 222 29.513 12.794 7.681 1.00 55.09 C ANISOU 1282 CA SER A 222 8144 6713 6073 189 -334 -135 C ATOM 1283 C SER A 222 30.616 12.179 6.808 1.00 58.59 C ANISOU 1283 C SER A 222 8535 7166 6560 287 -381 -118 C ATOM 1284 O SER A 222 30.830 12.630 5.675 1.00 57.62 O ANISOU 1284 O SER A 222 8349 7022 6521 276 -349 -157 O ATOM 1285 CB SER A 222 30.126 13.834 8.614 1.00 59.14 C ANISOU 1285 CB SER A 222 8593 7347 6528 138 -364 -207 C ATOM 1286 OG SER A 222 29.129 14.591 9.280 1.00 67.51 O ANISOU 1286 OG SER A 222 9693 8396 7563 48 -304 -247 O ATOM 1287 N LEU A 223 31.314 11.153 7.341 1.00 55.04 N ANISOU 1287 N LEU A 223 8115 6750 6047 392 -453 -58 N ATOM 1288 CA LEU A 223 32.387 10.455 6.636 1.00 54.84 C ANISOU 1288 CA LEU A 223 8039 6742 6057 513 -500 -43 C ATOM 1289 C LEU A 223 31.821 9.679 5.463 1.00 56.18 C ANISOU 1289 C LEU A 223 8275 6769 6303 541 -446 -15 C ATOM 1290 O LEU A 223 32.410 9.700 4.386 1.00 55.75 O ANISOU 1290 O LEU A 223 8148 6720 6315 580 -435 -50 O ATOM 1291 CB LEU A 223 33.165 9.510 7.582 1.00 56.55 C ANISOU 1291 CB LEU A 223 8290 7018 6179 644 -596 25 C ATOM 1292 CG LEU A 223 34.029 10.184 8.665 1.00 62.50 C ANISOU 1292 CG LEU A 223 8946 7958 6845 642 -679 -16 C ATOM 1293 CD1 LEU A 223 34.176 9.293 9.882 1.00 64.47 C ANISOU 1293 CD1 LEU A 223 9295 8238 6961 741 -761 79 C ATOM 1294 CD2 LEU A 223 35.401 10.592 8.128 1.00 64.47 C ANISOU 1294 CD2 LEU A 223 9013 8343 7140 693 -725 -91 C ATOM 1295 N ALA A 224 30.653 9.043 5.660 1.00 51.21 N ANISOU 1295 N ALA A 224 7777 6022 5659 505 -405 39 N ATOM 1296 CA ALA A 224 29.979 8.223 4.657 1.00 50.09 C ANISOU 1296 CA ALA A 224 7710 5744 5577 510 -355 56 C ATOM 1297 C ALA A 224 29.213 9.046 3.610 1.00 51.05 C ANISOU 1297 C ALA A 224 7780 5845 5772 414 -290 -6 C ATOM 1298 O ALA A 224 29.200 8.659 2.435 1.00 50.14 O ANISOU 1298 O ALA A 224 7666 5672 5711 437 -267 -23 O ATOM 1299 CB ALA A 224 29.026 7.253 5.339 1.00 51.30 C ANISOU 1299 CB ALA A 224 8019 5789 5682 485 -331 129 C ATOM 1300 N ALA A 225 28.569 10.153 4.029 1.00 45.41 N ANISOU 1300 N ALA A 225 7027 5175 5050 317 -262 -41 N ATOM 1301 CA ALA A 225 27.748 10.968 3.140 1.00 44.02 C ANISOU 1301 CA ALA A 225 6814 4977 4935 246 -208 -87 C ATOM 1302 C ALA A 225 28.522 12.034 2.375 1.00 47.64 C ANISOU 1302 C ALA A 225 7173 5491 5436 245 -204 -137 C ATOM 1303 O ALA A 225 28.093 12.399 1.278 1.00 46.63 O ANISOU 1303 O ALA A 225 7031 5331 5356 225 -169 -157 O ATOM 1304 CB ALA A 225 26.627 11.631 3.923 1.00 44.49 C ANISOU 1304 CB ALA A 225 6887 5043 4972 159 -169 -100 C ATOM 1305 N PHE A 226 29.619 12.564 2.947 1.00 44.69 N ANISOU 1305 N PHE A 226 6734 5206 5039 258 -238 -160 N ATOM 1306 CA PHE A 226 30.361 13.650 2.309 1.00 43.88 C ANISOU 1306 CA PHE A 226 6543 5154 4977 226 -218 -214 C ATOM 1307 C PHE A 226 31.829 13.322 2.037 1.00 48.93 C ANISOU 1307 C PHE A 226 7099 5875 5617 290 -255 -229 C ATOM 1308 O PHE A 226 32.265 13.521 0.908 1.00 48.34 O ANISOU 1308 O PHE A 226 6981 5802 5586 293 -220 -251 O ATOM 1309 CB PHE A 226 30.264 14.934 3.158 1.00 45.24 C ANISOU 1309 CB PHE A 226 6690 5368 5133 141 -204 -261 C ATOM 1310 CG PHE A 226 30.987 16.141 2.600 1.00 46.08 C ANISOU 1310 CG PHE A 226 6724 5505 5280 82 -170 -318 C ATOM 1311 CD1 PHE A 226 30.452 16.865 1.539 1.00 48.00 C ANISOU 1311 CD1 PHE A 226 6988 5674 5577 49 -108 -320 C ATOM 1312 CD2 PHE A 226 32.184 16.573 3.156 1.00 47.88 C ANISOU 1312 CD2 PHE A 226 6868 5839 5486 53 -200 -370 C ATOM 1313 CE1 PHE A 226 31.120 17.976 1.025 1.00 48.65 C ANISOU 1313 CE1 PHE A 226 7029 5764 5691 -16 -63 -362 C ATOM 1314 CE2 PHE A 226 32.851 17.684 2.641 1.00 50.57 C ANISOU 1314 CE2 PHE A 226 7147 6201 5866 -28 -154 -429 C ATOM 1315 CZ PHE A 226 32.312 18.381 1.583 1.00 48.16 C ANISOU 1315 CZ PHE A 226 6886 5797 5615 -65 -79 -419 C ATOM 1316 N PHE A 227 32.597 12.881 3.048 1.00 47.28 N ANISOU 1316 N PHE A 227 6862 5748 5355 343 -322 -222 N ATOM 1317 CA PHE A 227 34.036 12.645 2.878 1.00 48.42 C ANISOU 1317 CA PHE A 227 6896 6001 5500 414 -365 -249 C ATOM 1318 C PHE A 227 34.376 11.411 2.018 1.00 53.81 C ANISOU 1318 C PHE A 227 7597 6640 6209 539 -370 -217 C ATOM 1319 O PHE A 227 35.452 11.403 1.414 1.00 55.13 O ANISOU 1319 O PHE A 227 7656 6889 6402 586 -370 -258 O ATOM 1320 CB PHE A 227 34.763 12.600 4.229 1.00 51.06 C ANISOU 1320 CB PHE A 227 7182 6459 5759 446 -450 -255 C ATOM 1321 CG PHE A 227 34.694 13.936 4.937 1.00 52.40 C ANISOU 1321 CG PHE A 227 7310 6692 5906 312 -438 -321 C ATOM 1322 CD1 PHE A 227 35.492 15.001 4.530 1.00 55.59 C ANISOU 1322 CD1 PHE A 227 7595 7179 6349 227 -410 -407 C ATOM 1323 CD2 PHE A 227 33.796 14.144 5.979 1.00 54.12 C ANISOU 1323 CD2 PHE A 227 7619 6879 6067 261 -440 -305 C ATOM 1324 CE1 PHE A 227 35.397 16.248 5.157 1.00 56.64 C ANISOU 1324 CE1 PHE A 227 7709 7343 6467 93 -388 -479 C ATOM 1325 CE2 PHE A 227 33.706 15.388 6.609 1.00 56.94 C ANISOU 1325 CE2 PHE A 227 7948 7281 6406 141 -420 -380 C ATOM 1326 CZ PHE A 227 34.507 16.431 6.194 1.00 55.47 C ANISOU 1326 CZ PHE A 227 7654 7158 6263 58 -395 -468 C ATOM 1327 N THR A 228 33.474 10.412 1.912 1.00 49.57 N ANISOU 1327 N THR A 228 7191 5977 5669 583 -363 -158 N ATOM 1328 CA THR A 228 33.720 9.244 1.056 1.00 49.49 C ANISOU 1328 CA THR A 228 7219 5899 5687 693 -357 -141 C ATOM 1329 C THR A 228 33.462 9.650 -0.421 1.00 52.02 C ANISOU 1329 C THR A 228 7519 6185 6062 638 -282 -185 C ATOM 1330 O THR A 228 34.402 9.502 -1.205 1.00 51.40 O ANISOU 1330 O THR A 228 7363 6159 6007 698 -267 -223 O ATOM 1331 CB THR A 228 32.933 8.007 1.520 1.00 55.38 C ANISOU 1331 CB THR A 228 8123 6514 6407 743 -372 -68 C ATOM 1332 OG1 THR A 228 33.325 7.715 2.861 1.00 52.04 O ANISOU 1332 OG1 THR A 228 7719 6140 5915 802 -443 -19 O ATOM 1333 CG2 THR A 228 33.173 6.775 0.627 1.00 52.99 C ANISOU 1333 CG2 THR A 228 7881 6116 6138 853 -357 -64 C ATOM 1334 N PRO A 229 32.287 10.225 -0.830 1.00 48.05 N ANISOU 1334 N PRO A 229 7069 5616 5572 532 -234 -184 N ATOM 1335 CA PRO A 229 32.133 10.634 -2.243 1.00 47.54 C ANISOU 1335 CA PRO A 229 6988 5537 5539 495 -175 -217 C ATOM 1336 C PRO A 229 33.101 11.742 -2.667 1.00 52.42 C ANISOU 1336 C PRO A 229 7492 6256 6170 455 -144 -260 C ATOM 1337 O PRO A 229 33.388 11.838 -3.854 1.00 53.10 O ANISOU 1337 O PRO A 229 7557 6351 6268 457 -96 -284 O ATOM 1338 CB PRO A 229 30.683 11.115 -2.331 1.00 48.23 C ANISOU 1338 CB PRO A 229 7143 5556 5627 406 -151 -201 C ATOM 1339 CG PRO A 229 30.299 11.428 -0.957 1.00 52.35 C ANISOU 1339 CG PRO A 229 7678 6087 6127 369 -179 -180 C ATOM 1340 CD PRO A 229 31.047 10.496 -0.072 1.00 48.91 C ANISOU 1340 CD PRO A 229 7251 5671 5661 453 -232 -155 C ATOM 1341 N LEU A 230 33.629 12.545 -1.711 1.00 49.16 N ANISOU 1341 N LEU A 230 7010 5920 5748 408 -165 -276 N ATOM 1342 CA LEU A 230 34.612 13.604 -1.984 1.00 49.11 C ANISOU 1342 CA LEU A 230 6893 6011 5757 343 -129 -328 C ATOM 1343 C LEU A 230 35.937 12.959 -2.408 1.00 53.78 C ANISOU 1343 C LEU A 230 7378 6702 6354 430 -136 -364 C ATOM 1344 O LEU A 230 36.492 13.345 -3.437 1.00 54.47 O ANISOU 1344 O LEU A 230 7405 6831 6459 396 -70 -399 O ATOM 1345 CB LEU A 230 34.796 14.539 -0.763 1.00 49.24 C ANISOU 1345 CB LEU A 230 6867 6084 5758 262 -154 -353 C ATOM 1346 CG LEU A 230 35.883 15.632 -0.831 1.00 54.56 C ANISOU 1346 CG LEU A 230 7420 6863 6446 170 -120 -423 C ATOM 1347 CD1 LEU A 230 35.652 16.605 -1.981 1.00 54.28 C ANISOU 1347 CD1 LEU A 230 7414 6766 6443 74 -21 -428 C ATOM 1348 CD2 LEU A 230 35.974 16.389 0.480 1.00 56.89 C ANISOU 1348 CD2 LEU A 230 7686 7212 6716 94 -157 -461 C ATOM 1349 N ALA A 231 36.404 11.941 -1.647 1.00 49.93 N ANISOU 1349 N ALA A 231 6872 6251 5849 550 -211 -350 N ATOM 1350 CA ALA A 231 37.617 11.167 -1.938 1.00 50.07 C ANISOU 1350 CA ALA A 231 6786 6364 5875 674 -230 -383 C ATOM 1351 C ALA A 231 37.536 10.518 -3.339 1.00 52.86 C ANISOU 1351 C ALA A 231 7182 6652 6252 731 -165 -393 C ATOM 1352 O ALA A 231 38.490 10.634 -4.105 1.00 53.36 O ANISOU 1352 O ALA A 231 7133 6811 6332 754 -120 -449 O ATOM 1353 CB ALA A 231 37.825 10.101 -0.870 1.00 51.30 C ANISOU 1353 CB ALA A 231 6964 6529 5998 815 -329 -342 C ATOM 1354 N ILE A 232 36.379 9.896 -3.685 1.00 47.72 N ANISOU 1354 N ILE A 232 6684 5850 5598 737 -155 -349 N ATOM 1355 CA ILE A 232 36.109 9.255 -4.982 1.00 47.14 C ANISOU 1355 CA ILE A 232 6674 5705 5534 774 -100 -367 C ATOM 1356 C ILE A 232 36.193 10.304 -6.111 1.00 52.40 C ANISOU 1356 C ILE A 232 7294 6418 6196 667 -15 -400 C ATOM 1357 O ILE A 232 36.858 10.053 -7.122 1.00 52.70 O ANISOU 1357 O ILE A 232 7288 6502 6233 706 41 -447 O ATOM 1358 CB ILE A 232 34.732 8.516 -4.985 1.00 48.88 C ANISOU 1358 CB ILE A 232 7060 5766 5745 769 -113 -323 C ATOM 1359 CG1 ILE A 232 34.719 7.340 -3.968 1.00 49.54 C ANISOU 1359 CG1 ILE A 232 7215 5782 5825 877 -180 -280 C ATOM 1360 CG2 ILE A 232 34.355 8.026 -6.401 1.00 48.89 C ANISOU 1360 CG2 ILE A 232 7125 5707 5745 777 -56 -358 C ATOM 1361 CD1 ILE A 232 33.318 6.860 -3.524 1.00 52.10 C ANISOU 1361 CD1 ILE A 232 7690 5969 6138 822 -192 -229 C ATOM 1362 N MET A 233 35.541 11.475 -5.920 1.00 48.61 N ANISOU 1362 N MET A 233 6835 5923 5710 538 -1 -375 N ATOM 1363 CA MET A 233 35.524 12.573 -6.890 1.00 48.55 C ANISOU 1363 CA MET A 233 6818 5937 5693 434 78 -384 C ATOM 1364 C MET A 233 36.920 13.188 -7.098 1.00 52.66 C ANISOU 1364 C MET A 233 7196 6591 6223 397 132 -437 C ATOM 1365 O MET A 233 37.206 13.627 -8.215 1.00 52.67 O ANISOU 1365 O MET A 233 7189 6618 6206 346 217 -452 O ATOM 1366 CB MET A 233 34.514 13.650 -6.488 1.00 50.40 C ANISOU 1366 CB MET A 233 7117 6106 5926 331 75 -342 C ATOM 1367 CG MET A 233 33.105 13.292 -6.875 1.00 54.05 C ANISOU 1367 CG MET A 233 7700 6465 6373 341 58 -303 C ATOM 1368 SD MET A 233 31.865 14.240 -5.975 1.00 58.69 S ANISOU 1368 SD MET A 233 8343 6986 6970 269 31 -263 S ATOM 1369 CE MET A 233 31.510 15.466 -7.160 1.00 55.59 C ANISOU 1369 CE MET A 233 7990 6571 6560 203 97 -240 C ATOM 1370 N ILE A 234 37.790 13.196 -6.054 1.00 49.07 N ANISOU 1370 N ILE A 234 6627 6232 5787 418 85 -468 N ATOM 1371 CA ILE A 234 39.168 13.696 -6.170 1.00 50.19 C ANISOU 1371 CA ILE A 234 6601 6529 5941 377 130 -536 C ATOM 1372 C ILE A 234 39.953 12.727 -7.066 1.00 54.96 C ANISOU 1372 C ILE A 234 7137 7199 6545 496 165 -580 C ATOM 1373 O ILE A 234 40.607 13.173 -8.009 1.00 55.63 O ANISOU 1373 O ILE A 234 7151 7362 6625 436 262 -624 O ATOM 1374 CB ILE A 234 39.859 13.923 -4.783 1.00 54.04 C ANISOU 1374 CB ILE A 234 6970 7125 6438 371 52 -568 C ATOM 1375 CG1 ILE A 234 39.276 15.163 -4.066 1.00 53.66 C ANISOU 1375 CG1 ILE A 234 6975 7027 6388 219 52 -553 C ATOM 1376 CG2 ILE A 234 41.397 14.056 -4.923 1.00 56.37 C ANISOU 1376 CG2 ILE A 234 7054 7616 6747 366 81 -656 C ATOM 1377 CD1 ILE A 234 39.539 15.235 -2.554 1.00 60.17 C ANISOU 1377 CD1 ILE A 234 7749 7915 7198 228 -48 -568 C ATOM 1378 N VAL A 235 39.855 11.405 -6.783 1.00 50.82 N ANISOU 1378 N VAL A 235 6650 6633 6025 662 96 -569 N ATOM 1379 CA VAL A 235 40.515 10.325 -7.529 1.00 51.13 C ANISOU 1379 CA VAL A 235 6648 6707 6070 807 122 -616 C ATOM 1380 C VAL A 235 40.107 10.395 -9.015 1.00 55.41 C ANISOU 1380 C VAL A 235 7273 7195 6584 757 225 -628 C ATOM 1381 O VAL A 235 40.986 10.424 -9.885 1.00 56.06 O ANISOU 1381 O VAL A 235 7259 7381 6659 766 310 -693 O ATOM 1382 CB VAL A 235 40.215 8.925 -6.899 1.00 54.35 C ANISOU 1382 CB VAL A 235 7140 7021 6487 986 31 -584 C ATOM 1383 CG1 VAL A 235 40.566 7.777 -7.847 1.00 54.73 C ANISOU 1383 CG1 VAL A 235 7211 7039 6544 1131 73 -631 C ATOM 1384 CG2 VAL A 235 40.939 8.753 -5.567 1.00 54.80 C ANISOU 1384 CG2 VAL A 235 7089 7177 6554 1073 -68 -579 C ATOM 1385 N THR A 236 38.786 10.467 -9.295 1.00 51.06 N ANISOU 1385 N THR A 236 6891 6502 6009 700 217 -570 N ATOM 1386 CA THR A 236 38.263 10.507 -10.664 1.00 50.99 C ANISOU 1386 CA THR A 236 6973 6447 5953 658 293 -576 C ATOM 1387 C THR A 236 38.709 11.781 -11.380 1.00 54.05 C ANISOU 1387 C THR A 236 7308 6919 6311 521 391 -580 C ATOM 1388 O THR A 236 38.899 11.741 -12.599 1.00 54.93 O ANISOU 1388 O THR A 236 7438 7059 6372 510 476 -608 O ATOM 1389 CB THR A 236 36.739 10.324 -10.719 1.00 62.31 C ANISOU 1389 CB THR A 236 8573 7735 7366 631 247 -519 C ATOM 1390 OG1 THR A 236 36.105 11.351 -9.970 1.00 66.59 O ANISOU 1390 OG1 THR A 236 9135 8248 7917 530 214 -459 O ATOM 1391 CG2 THR A 236 36.292 8.956 -10.219 1.00 61.71 C ANISOU 1391 CG2 THR A 236 8574 7560 7313 746 178 -521 C ATOM 1392 N TYR A 237 38.924 12.886 -10.629 1.00 47.81 N ANISOU 1392 N TYR A 237 6457 6165 5544 414 388 -558 N ATOM 1393 CA TYR A 237 39.414 14.140 -11.199 1.00 46.84 C ANISOU 1393 CA TYR A 237 6295 6101 5399 267 491 -560 C ATOM 1394 C TYR A 237 40.793 13.909 -11.822 1.00 50.66 C ANISOU 1394 C TYR A 237 6626 6742 5879 281 581 -644 C ATOM 1395 O TYR A 237 40.982 14.257 -12.978 1.00 51.10 O ANISOU 1395 O TYR A 237 6707 6826 5882 215 691 -649 O ATOM 1396 CB TYR A 237 39.452 15.286 -10.150 1.00 47.18 C ANISOU 1396 CB TYR A 237 6305 6143 5479 148 469 -541 C ATOM 1397 CG TYR A 237 40.185 16.519 -10.637 1.00 48.51 C ANISOU 1397 CG TYR A 237 6422 6372 5638 -16 587 -558 C ATOM 1398 CD1 TYR A 237 39.530 17.494 -11.383 1.00 50.02 C ANISOU 1398 CD1 TYR A 237 6754 6464 5788 -121 658 -490 C ATOM 1399 CD2 TYR A 237 41.550 16.677 -10.412 1.00 50.10 C ANISOU 1399 CD2 TYR A 237 6435 6734 5867 -64 632 -642 C ATOM 1400 CE1 TYR A 237 40.214 18.599 -11.887 1.00 51.73 C ANISOU 1400 CE1 TYR A 237 6950 6714 5991 -279 782 -496 C ATOM 1401 CE2 TYR A 237 42.247 17.765 -10.930 1.00 51.96 C ANISOU 1401 CE2 TYR A 237 6625 7024 6092 -238 760 -665 C ATOM 1402 CZ TYR A 237 41.573 18.729 -11.658 1.00 58.38 C ANISOU 1402 CZ TYR A 237 7606 7710 6864 -351 840 -587 C ATOM 1403 OH TYR A 237 42.249 19.821 -12.139 1.00 60.36 O ANISOU 1403 OH TYR A 237 7839 7991 7104 -534 976 -598 O ATOM 1404 N PHE A 238 41.737 13.311 -11.072 1.00 47.77 N ANISOU 1404 N PHE A 238 6101 6487 5562 373 535 -709 N ATOM 1405 CA PHE A 238 43.093 13.033 -11.560 1.00 49.21 C ANISOU 1405 CA PHE A 238 6102 6845 5751 408 614 -804 C ATOM 1406 C PHE A 238 43.106 11.904 -12.602 1.00 54.66 C ANISOU 1406 C PHE A 238 6835 7524 6411 547 655 -841 C ATOM 1407 O PHE A 238 43.972 11.918 -13.478 1.00 56.00 O ANISOU 1407 O PHE A 238 6900 7819 6559 539 767 -913 O ATOM 1408 CB PHE A 238 44.060 12.724 -10.408 1.00 51.59 C ANISOU 1408 CB PHE A 238 6210 7282 6109 489 533 -862 C ATOM 1409 CG PHE A 238 44.339 13.920 -9.526 1.00 53.00 C ANISOU 1409 CG PHE A 238 6308 7521 6310 325 517 -864 C ATOM 1410 CD1 PHE A 238 45.165 14.952 -9.962 1.00 56.60 C ANISOU 1410 CD1 PHE A 238 6647 8095 6764 147 636 -918 C ATOM 1411 CD2 PHE A 238 43.767 14.021 -8.261 1.00 54.21 C ANISOU 1411 CD2 PHE A 238 6508 7609 6479 338 392 -820 C ATOM 1412 CE1 PHE A 238 45.405 16.066 -9.152 1.00 57.73 C ANISOU 1412 CE1 PHE A 238 6728 8277 6928 -21 628 -935 C ATOM 1413 CE2 PHE A 238 44.010 15.135 -7.450 1.00 56.95 C ANISOU 1413 CE2 PHE A 238 6789 8009 6840 181 381 -838 C ATOM 1414 CZ PHE A 238 44.831 16.147 -7.900 1.00 56.14 C ANISOU 1414 CZ PHE A 238 6575 8012 6743 1 497 -900 C ATOM 1415 N LEU A 239 42.139 10.958 -12.535 1.00 50.40 N ANISOU 1415 N LEU A 239 6450 6836 5866 660 577 -802 N ATOM 1416 CA LEU A 239 42.020 9.880 -13.524 1.00 50.59 C ANISOU 1416 CA LEU A 239 6545 6821 5857 777 615 -847 C ATOM 1417 C LEU A 239 41.561 10.441 -14.871 1.00 54.30 C ANISOU 1417 C LEU A 239 7120 7274 6239 660 720 -833 C ATOM 1418 O LEU A 239 42.018 9.965 -15.913 1.00 54.63 O ANISOU 1418 O LEU A 239 7146 7377 6234 704 811 -903 O ATOM 1419 CB LEU A 239 41.037 8.789 -13.058 1.00 49.75 C ANISOU 1419 CB LEU A 239 6587 6547 5770 897 508 -813 C ATOM 1420 CG LEU A 239 41.515 7.752 -12.030 1.00 54.56 C ANISOU 1420 CG LEU A 239 7136 7150 6444 1079 419 -833 C ATOM 1421 CD1 LEU A 239 40.347 6.905 -11.546 1.00 53.32 C ANISOU 1421 CD1 LEU A 239 7160 6801 6297 1136 327 -774 C ATOM 1422 CD2 LEU A 239 42.598 6.842 -12.600 1.00 57.41 C ANISOU 1422 CD2 LEU A 239 7403 7592 6818 1240 479 -935 C ATOM 1423 N THR A 240 40.657 11.458 -14.842 1.00 49.96 N ANISOU 1423 N THR A 240 6680 6645 5657 522 705 -743 N ATOM 1424 CA THR A 240 40.102 12.109 -16.039 1.00 49.89 C ANISOU 1424 CA THR A 240 6792 6613 5553 417 784 -703 C ATOM 1425 C THR A 240 41.169 12.975 -16.700 1.00 57.41 C ANISOU 1425 C THR A 240 7645 7701 6468 304 928 -730 C ATOM 1426 O THR A 240 41.268 12.976 -17.932 1.00 58.43 O ANISOU 1426 O THR A 240 7826 7873 6504 278 1029 -747 O ATOM 1427 CB THR A 240 38.842 12.910 -15.701 1.00 50.10 C ANISOU 1427 CB THR A 240 6953 6515 5567 334 717 -596 C ATOM 1428 OG1 THR A 240 37.957 12.085 -14.940 1.00 46.45 O ANISOU 1428 OG1 THR A 240 6553 5947 5149 425 594 -583 O ATOM 1429 CG2 THR A 240 38.124 13.421 -16.940 1.00 46.16 C ANISOU 1429 CG2 THR A 240 6595 5987 4958 265 770 -543 C ATOM 1430 N ILE A 241 41.984 13.676 -15.880 1.00 55.06 N ANISOU 1430 N ILE A 241 7204 7481 6236 229 943 -742 N ATOM 1431 CA ILE A 241 43.091 14.523 -16.327 1.00 56.91 C ANISOU 1431 CA ILE A 241 7319 7853 6452 94 1086 -780 C ATOM 1432 C ILE A 241 44.112 13.637 -17.082 1.00 63.10 C ANISOU 1432 C ILE A 241 7971 8789 7216 189 1175 -895 C ATOM 1433 O ILE A 241 44.571 14.032 -18.156 1.00 63.99 O ANISOU 1433 O ILE A 241 8077 8984 7253 97 1323 -916 O ATOM 1434 CB ILE A 241 43.688 15.311 -15.105 1.00 60.38 C ANISOU 1434 CB ILE A 241 7620 8344 6976 -4 1058 -791 C ATOM 1435 CG1 ILE A 241 43.109 16.745 -15.009 1.00 60.36 C ANISOU 1435 CG1 ILE A 241 7744 8235 6954 -192 1094 -698 C ATOM 1436 CG2 ILE A 241 45.224 15.385 -15.116 1.00 63.56 C ANISOU 1436 CG2 ILE A 241 7778 8961 7412 -43 1150 -904 C ATOM 1437 CD1 ILE A 241 41.584 16.891 -14.843 1.00 68.53 C ANISOU 1437 CD1 ILE A 241 8982 9078 7977 -160 990 -592 C ATOM 1438 N HIS A 242 44.390 12.418 -16.558 1.00 59.99 N ANISOU 1438 N HIS A 242 7493 8417 6884 380 1090 -963 N ATOM 1439 CA HIS A 242 45.305 11.443 -17.157 1.00 61.43 C ANISOU 1439 CA HIS A 242 7552 8725 7062 514 1160 -1081 C ATOM 1440 C HIS A 242 44.725 10.853 -18.458 1.00 64.84 C ANISOU 1440 C HIS A 242 8147 9094 7395 558 1222 -1093 C ATOM 1441 O HIS A 242 45.452 10.765 -19.451 1.00 65.88 O ANISOU 1441 O HIS A 242 8214 9350 7467 548 1362 -1171 O ATOM 1442 CB HIS A 242 45.631 10.314 -16.160 1.00 62.48 C ANISOU 1442 CB HIS A 242 7587 8863 7291 726 1037 -1130 C ATOM 1443 CG HIS A 242 46.809 9.477 -16.559 1.00 68.33 C ANISOU 1443 CG HIS A 242 8149 9761 8053 877 1107 -1260 C ATOM 1444 ND1 HIS A 242 46.693 8.464 -17.501 1.00 70.91 N ANISOU 1444 ND1 HIS A 242 8558 10046 8337 1009 1159 -1324 N ATOM 1445 CD2 HIS A 242 48.094 9.532 -16.136 1.00 71.98 C ANISOU 1445 CD2 HIS A 242 8351 10425 8572 916 1133 -1346 C ATOM 1446 CE1 HIS A 242 47.905 7.945 -17.623 1.00 72.27 C ANISOU 1446 CE1 HIS A 242 8525 10387 8548 1136 1220 -1442 C ATOM 1447 NE2 HIS A 242 48.781 8.552 -16.821 1.00 73.33 N ANISOU 1447 NE2 HIS A 242 8438 10682 8743 1089 1204 -1459 N ATOM 1448 N ALA A 243 43.431 10.442 -18.444 1.00 59.35 N ANISOU 1448 N ALA A 243 7653 8222 6676 598 1122 -1026 N ATOM 1449 CA ALA A 243 42.742 9.837 -19.595 1.00 58.81 C ANISOU 1449 CA ALA A 243 7748 8090 6507 634 1153 -1045 C ATOM 1450 C ALA A 243 42.646 10.793 -20.802 1.00 62.35 C ANISOU 1450 C ALA A 243 8275 8593 6821 475 1278 -1005 C ATOM 1451 O ALA A 243 42.828 10.345 -21.938 1.00 62.77 O ANISOU 1451 O ALA A 243 8368 8704 6776 500 1372 -1072 O ATOM 1452 CB ALA A 243 41.352 9.367 -19.192 1.00 57.80 C ANISOU 1452 CB ALA A 243 7794 7779 6390 676 1012 -981 C ATOM 1453 N LEU A 244 42.388 12.100 -20.555 1.00 57.86 N ANISOU 1453 N LEU A 244 7740 8003 6242 317 1284 -897 N ATOM 1454 CA LEU A 244 42.275 13.116 -21.605 1.00 58.02 C ANISOU 1454 CA LEU A 244 7860 8052 6133 165 1400 -831 C ATOM 1455 C LEU A 244 43.633 13.416 -22.250 1.00 64.89 C ANISOU 1455 C LEU A 244 8588 9102 6967 89 1584 -906 C ATOM 1456 O LEU A 244 43.683 13.578 -23.468 1.00 66.24 O ANISOU 1456 O LEU A 244 8841 9327 6999 31 1704 -905 O ATOM 1457 CB LEU A 244 41.624 14.404 -21.080 1.00 56.75 C ANISOU 1457 CB LEU A 244 7787 7789 5987 35 1356 -695 C ATOM 1458 CG LEU A 244 40.102 14.346 -20.847 1.00 59.47 C ANISOU 1458 CG LEU A 244 8303 7974 6321 81 1206 -606 C ATOM 1459 CD1 LEU A 244 39.629 15.537 -20.052 1.00 58.17 C ANISOU 1459 CD1 LEU A 244 8174 7712 6214 -12 1156 -500 C ATOM 1460 CD2 LEU A 244 39.319 14.258 -22.166 1.00 62.42 C ANISOU 1460 CD2 LEU A 244 8851 8332 6534 79 1227 -564 C ATOM 1461 N GLN A 245 44.728 13.450 -21.458 1.00 62.58 N ANISOU 1461 N GLN A 245 8075 8915 6788 90 1608 -979 N ATOM 1462 CA GLN A 245 46.091 13.672 -21.968 1.00 64.63 C ANISOU 1462 CA GLN A 245 8152 9373 7031 18 1783 -1073 C ATOM 1463 C GLN A 245 46.551 12.469 -22.804 1.00 70.57 C ANISOU 1463 C GLN A 245 8854 10225 7734 169 1853 -1202 C ATOM 1464 O GLN A 245 47.116 12.664 -23.881 1.00 72.18 O ANISOU 1464 O GLN A 245 9038 10554 7835 91 2026 -1247 O ATOM 1465 CB GLN A 245 47.086 13.939 -20.828 1.00 66.32 C ANISOU 1465 CB GLN A 245 8122 9693 7384 -1 1762 -1131 C ATOM 1466 CG GLN A 245 46.968 15.330 -20.208 1.00 85.50 C ANISOU 1466 CG GLN A 245 10567 12076 9843 -210 1769 -1041 C ATOM 1467 CD GLN A 245 47.735 15.493 -18.906 1.00110.34 C ANISOU 1467 CD GLN A 245 13487 15314 13123 -218 1703 -1104 C ATOM 1468 OE1 GLN A 245 48.259 14.534 -18.317 1.00106.73 O ANISOU 1468 OE1 GLN A 245 12859 14953 12742 -45 1628 -1198 O ATOM 1469 NE2 GLN A 245 47.799 16.723 -18.412 1.00103.34 N ANISOU 1469 NE2 GLN A 245 12604 14397 12264 -416 1724 -1052 N ATOM 1470 N LYS A 246 46.276 11.232 -22.323 1.00 66.67 N ANISOU 1470 N LYS A 246 8356 9666 7310 380 1728 -1261 N ATOM 1471 CA LYS A 246 46.619 9.983 -23.010 1.00 67.88 C ANISOU 1471 CA LYS A 246 8485 9873 7434 549 1778 -1392 C ATOM 1472 C LYS A 246 45.907 9.902 -24.371 1.00 72.63 C ANISOU 1472 C LYS A 246 9297 10435 7865 503 1849 -1379 C ATOM 1473 O LYS A 246 46.537 9.522 -25.359 1.00 74.15 O ANISOU 1473 O LYS A 246 9450 10749 7973 529 1992 -1485 O ATOM 1474 CB LYS A 246 46.274 8.758 -22.141 1.00 69.36 C ANISOU 1474 CB LYS A 246 8678 9942 7733 769 1617 -1429 C ATOM 1475 CG LYS A 246 46.925 7.467 -22.634 1.00 86.41 C ANISOU 1475 CG LYS A 246 10774 12157 9900 969 1676 -1584 C ATOM 1476 CD LYS A 246 46.453 6.232 -21.874 1.00 97.26 C ANISOU 1476 CD LYS A 246 12219 13364 11370 1178 1523 -1602 C ATOM 1477 CE LYS A 246 46.518 4.970 -22.712 1.00111.72 C ANISOU 1477 CE LYS A 246 14121 15161 13165 1343 1581 -1735 C ATOM 1478 NZ LYS A 246 47.915 4.559 -23.037 1.00122.27 N ANISOU 1478 NZ LYS A 246 15238 16681 14538 1476 1703 -1881 N ATOM 1479 N LYS A 247 44.611 10.282 -24.417 1.00 67.80 N ANISOU 1479 N LYS A 247 8897 9668 7195 436 1749 -1254 N ATOM 1480 CA LYS A 247 43.779 10.295 -25.626 1.00 67.90 C ANISOU 1480 CA LYS A 247 9118 9647 7034 390 1779 -1223 C ATOM 1481 C LYS A 247 44.382 11.225 -26.679 1.00 73.79 C ANISOU 1481 C LYS A 247 9871 10531 7635 230 1967 -1198 C ATOM 1482 O LYS A 247 44.512 10.831 -27.838 1.00 74.13 O ANISOU 1482 O LYS A 247 9981 10652 7532 238 2071 -1264 O ATOM 1483 CB LYS A 247 42.344 10.736 -25.280 1.00 68.43 C ANISOU 1483 CB LYS A 247 9367 9545 7089 348 1622 -1083 C ATOM 1484 CG LYS A 247 41.248 9.916 -25.946 1.00 78.56 C ANISOU 1484 CG LYS A 247 10826 10748 8274 418 1544 -1109 C ATOM 1485 CD LYS A 247 39.862 10.419 -25.540 1.00 85.28 C ANISOU 1485 CD LYS A 247 11817 11460 9126 377 1389 -977 C ATOM 1486 CE LYS A 247 38.758 9.411 -25.779 1.00 96.79 C ANISOU 1486 CE LYS A 247 13400 12831 10545 457 1276 -1027 C ATOM 1487 NZ LYS A 247 38.424 9.249 -27.222 1.00107.62 N ANISOU 1487 NZ LYS A 247 14900 14278 11713 426 1334 -1061 N ATOM 1488 N ALA A 248 44.783 12.441 -26.258 1.00 71.94 N ANISOU 1488 N ALA A 248 9571 10325 7437 76 2020 -1108 N ATOM 1489 CA ALA A 248 45.400 13.460 -27.109 1.00 74.29 C ANISOU 1489 CA ALA A 248 9881 10735 7612 -107 2211 -1066 C ATOM 1490 C ALA A 248 46.780 13.010 -27.608 1.00 82.80 C ANISOU 1490 C ALA A 248 10757 12022 8680 -97 2394 -1224 C ATOM 1491 O ALA A 248 47.099 13.213 -28.780 1.00 83.97 O ANISOU 1491 O ALA A 248 10960 12278 8667 -185 2564 -1239 O ATOM 1492 CB ALA A 248 45.518 14.771 -26.347 1.00 74.43 C ANISOU 1492 CB ALA A 248 9877 10701 7703 -273 2212 -948 C ATOM 1493 N ALA A1001 47.577 12.377 -26.722 1.00 78.46 N ANISOU 1493 N ALA A1001 8613 14559 6641 -744 -437 -2800 N ATOM 1494 CA ALA A1001 48.921 11.875 -27.017 1.00 78.26 C ANISOU 1494 CA ALA A1001 8532 14555 6649 -924 -498 -2686 C ATOM 1495 C ALA A1001 48.893 10.745 -28.046 1.00 81.53 C ANISOU 1495 C ALA A1001 8861 14887 7231 -902 -493 -2431 C ATOM 1496 O ALA A1001 49.803 10.666 -28.868 1.00 80.70 O ANISOU 1496 O ALA A1001 8789 14647 7226 -1002 -532 -2368 O ATOM 1497 CB ALA A1001 49.598 11.399 -25.742 1.00 80.17 C ANISOU 1497 CB ALA A1001 8616 15157 6687 -1007 -517 -2659 C ATOM 1498 N ASP A1002 47.862 9.880 -28.004 1.00 78.59 N ANISOU 1498 N ASP A1002 8381 14600 6880 -776 -448 -2285 N ATOM 1499 CA ASP A1002 47.701 8.768 -28.946 1.00 77.07 C ANISOU 1499 CA ASP A1002 8128 14315 6841 -756 -445 -2062 C ATOM 1500 C ASP A1002 47.229 9.272 -30.310 1.00 81.56 C ANISOU 1500 C ASP A1002 8835 14574 7579 -719 -440 -2097 C ATOM 1501 O ASP A1002 47.586 8.674 -31.326 1.00 79.94 O ANISOU 1501 O ASP A1002 8632 14236 7504 -753 -457 -1975 O ATOM 1502 CB ASP A1002 46.733 7.709 -28.393 1.00 78.68 C ANISOU 1502 CB ASP A1002 8177 14712 7005 -666 -413 -1893 C ATOM 1503 CG ASP A1002 47.241 6.940 -27.180 1.00 89.07 C ANISOU 1503 CG ASP A1002 9318 16343 8183 -704 -420 -1778 C ATOM 1504 OD1 ASP A1002 48.341 7.275 -26.674 1.00 89.68 O ANISOU 1504 OD1 ASP A1002 9385 16526 8163 -798 -444 -1850 O ATOM 1505 OD2 ASP A1002 46.535 6.012 -26.729 1.00 95.85 O ANISOU 1505 OD2 ASP A1002 10037 17358 9024 -650 -403 -1602 O ATOM 1506 N LEU A1003 46.447 10.373 -30.332 1.00 80.58 N ANISOU 1506 N LEU A1003 8824 14346 7448 -638 -411 -2261 N ATOM 1507 CA LEU A1003 45.939 11.002 -31.555 1.00 80.88 C ANISOU 1507 CA LEU A1003 8983 14112 7635 -590 -397 -2292 C ATOM 1508 C LEU A1003 47.097 11.546 -32.399 1.00 87.57 C ANISOU 1508 C LEU A1003 9933 14761 8579 -717 -448 -2336 C ATOM 1509 O LEU A1003 47.137 11.295 -33.604 1.00 86.03 O ANISOU 1509 O LEU A1003 9753 14413 8522 -727 -458 -2239 O ATOM 1510 CB LEU A1003 44.944 12.123 -31.223 1.00 82.33 C ANISOU 1510 CB LEU A1003 9263 14246 7772 -455 -345 -2455 C ATOM 1511 N GLU A1004 48.051 12.250 -31.752 1.00 87.54 N ANISOU 1511 N GLU A1004 9985 14789 8488 -825 -488 -2472 N ATOM 1512 CA GLU A1004 49.254 12.820 -32.369 1.00 88.33 C ANISOU 1512 CA GLU A1004 10162 14752 8648 -976 -550 -2501 C ATOM 1513 C GLU A1004 50.200 11.698 -32.816 1.00 91.91 C ANISOU 1513 C GLU A1004 10491 15305 9126 -1051 -581 -2306 C ATOM 1514 O GLU A1004 50.819 11.821 -33.868 1.00 90.50 O ANISOU 1514 O GLU A1004 10343 14995 9048 -1111 -614 -2247 O ATOM 1515 CB GLU A1004 49.958 13.773 -31.379 1.00 92.11 C ANISOU 1515 CB GLU A1004 10720 15284 8995 -1094 -593 -2692 C ATOM 1516 CG GLU A1004 51.086 14.610 -31.969 1.00106.05 C ANISOU 1516 CG GLU A1004 12588 16888 10819 -1270 -668 -2737 C ATOM 1517 CD GLU A1004 50.656 15.761 -32.858 1.00132.34 C ANISOU 1517 CD GLU A1004 16095 19892 14295 -1241 -668 -2833 C ATOM 1518 OE1 GLU A1004 50.875 15.674 -34.088 1.00128.64 O ANISOU 1518 OE1 GLU A1004 15623 19284 13970 -1265 -686 -2708 O ATOM 1519 OE2 GLU A1004 50.115 16.758 -32.325 1.00128.14 O ANISOU 1519 OE2 GLU A1004 15705 19250 13731 -1185 -646 -3028 O ATOM 1520 N ASP A1005 50.287 10.604 -32.023 1.00 89.92 N ANISOU 1520 N ASP A1005 10094 15291 8778 -1030 -565 -2197 N ATOM 1521 CA ASP A1005 51.106 9.410 -32.282 1.00 89.59 C ANISOU 1521 CA ASP A1005 9934 15357 8749 -1061 -578 -2001 C ATOM 1522 C ASP A1005 50.705 8.740 -33.609 1.00 92.78 C ANISOU 1522 C ASP A1005 10352 15584 9315 -990 -563 -1879 C ATOM 1523 O ASP A1005 51.578 8.265 -34.336 1.00 91.38 O ANISOU 1523 O ASP A1005 10152 15382 9184 -1024 -584 -1776 O ATOM 1524 CB ASP A1005 50.954 8.407 -31.117 1.00 92.22 C ANISOU 1524 CB ASP A1005 10117 15954 8967 -1022 -551 -1900 C ATOM 1525 CG ASP A1005 52.090 7.414 -30.935 1.00104.99 C ANISOU 1525 CG ASP A1005 11609 17741 10541 -1070 -564 -1725 C ATOM 1526 OD1 ASP A1005 52.436 6.713 -31.917 1.00104.81 O ANISOU 1526 OD1 ASP A1005 11584 17611 10628 -1042 -564 -1594 O ATOM 1527 OD2 ASP A1005 52.577 7.274 -29.792 1.00112.90 O ANISOU 1527 OD2 ASP A1005 12507 18999 11390 -1120 -569 -1711 O ATOM 1528 N ASN A1006 49.389 8.705 -33.914 1.00 89.88 N ANISOU 1528 N ASN A1006 10016 15118 9015 -891 -527 -1889 N ATOM 1529 CA ASN A1006 48.847 8.126 -35.144 1.00 88.88 C ANISOU 1529 CA ASN A1006 9907 14839 9023 -838 -517 -1792 C ATOM 1530 C ASN A1006 48.902 9.137 -36.294 1.00 93.70 C ANISOU 1530 C ASN A1006 10624 15245 9733 -855 -531 -1867 C ATOM 1531 O ASN A1006 49.172 8.739 -37.426 1.00 92.32 O ANISOU 1531 O ASN A1006 10454 14977 9647 -858 -543 -1789 O ATOM 1532 CB ASN A1006 47.412 7.628 -34.933 1.00 89.45 C ANISOU 1532 CB ASN A1006 9942 14939 9105 -748 -480 -1743 C ATOM 1533 CG ASN A1006 47.241 6.578 -33.854 1.00111.52 C ANISOU 1533 CG ASN A1006 12618 17939 11816 -734 -470 -1635 C ATOM 1534 OD1 ASN A1006 46.237 6.560 -33.137 1.00107.16 O ANISOU 1534 OD1 ASN A1006 12015 17502 11200 -678 -445 -1633 O ATOM 1535 ND2 ASN A1006 48.193 5.661 -33.723 1.00102.27 N ANISOU 1535 ND2 ASN A1006 11387 16832 10640 -773 -487 -1522 N ATOM 1536 N TRP A1007 48.654 10.435 -36.003 1.00 92.55 N ANISOU 1536 N TRP A1007 10565 15030 9570 -861 -528 -2016 N ATOM 1537 CA TRP A1007 48.689 11.541 -36.969 1.00 93.39 C ANISOU 1537 CA TRP A1007 10777 14932 9775 -880 -541 -2081 C ATOM 1538 C TRP A1007 50.112 11.725 -37.519 1.00 97.34 C ANISOU 1538 C TRP A1007 11279 15410 10295 -1005 -601 -2046 C ATOM 1539 O TRP A1007 50.263 11.981 -38.714 1.00 96.22 O ANISOU 1539 O TRP A1007 11161 15143 10255 -1015 -616 -1997 O ATOM 1540 CB TRP A1007 48.164 12.831 -36.313 1.00 94.40 C ANISOU 1540 CB TRP A1007 11012 14985 9870 -850 -522 -2254 C ATOM 1541 CG TRP A1007 48.387 14.102 -37.080 1.00 96.70 C ANISOU 1541 CG TRP A1007 11429 15051 10263 -889 -544 -2324 C ATOM 1542 CD1 TRP A1007 49.295 15.079 -36.793 1.00101.09 C ANISOU 1542 CD1 TRP A1007 12079 15529 10803 -1016 -598 -2430 C ATOM 1543 CD2 TRP A1007 47.645 14.565 -38.218 1.00 96.34 C ANISOU 1543 CD2 TRP A1007 11423 14834 10349 -809 -514 -2280 C ATOM 1544 NE1 TRP A1007 49.180 16.113 -37.693 1.00101.31 N ANISOU 1544 NE1 TRP A1007 12209 15323 10960 -1020 -607 -2448 N ATOM 1545 CE2 TRP A1007 48.172 15.826 -38.577 1.00101.65 C ANISOU 1545 CE2 TRP A1007 12214 15315 11094 -884 -550 -2353 C ATOM 1546 CE3 TRP A1007 46.595 14.028 -38.984 1.00 96.78 C ANISOU 1546 CE3 TRP A1007 11417 14890 10463 -696 -465 -2174 C ATOM 1547 CZ2 TRP A1007 47.689 16.556 -39.672 1.00101.07 C ANISOU 1547 CZ2 TRP A1007 12191 15055 11158 -830 -531 -2310 C ATOM 1548 CZ3 TRP A1007 46.110 14.759 -40.060 1.00 98.34 C ANISOU 1548 CZ3 TRP A1007 11658 14927 10778 -647 -445 -2140 C ATOM 1549 CH2 TRP A1007 46.659 16.003 -40.399 1.00100.03 C ANISOU 1549 CH2 TRP A1007 11982 14956 11071 -704 -473 -2201 C ATOM 1550 N GLU A1008 51.144 11.558 -36.658 1.00 94.94 N ANISOU 1550 N GLU A1008 10930 15263 9879 -1100 -636 -2051 N ATOM 1551 CA GLU A1008 52.556 11.645 -37.044 1.00 94.95 C ANISOU 1551 CA GLU A1008 10902 15310 9865 -1223 -695 -1987 C ATOM 1552 C GLU A1008 52.955 10.438 -37.898 1.00 97.46 C ANISOU 1552 C GLU A1008 11128 15682 10221 -1168 -685 -1815 C ATOM 1553 O GLU A1008 53.594 10.627 -38.930 1.00 96.89 O ANISOU 1553 O GLU A1008 11052 15559 10202 -1201 -716 -1752 O ATOM 1554 CB GLU A1008 53.478 11.749 -35.816 1.00 97.65 C ANISOU 1554 CB GLU A1008 11201 15848 10053 -1339 -730 -2025 C ATOM 1555 CG GLU A1008 53.596 13.150 -35.242 1.00110.49 C ANISOU 1555 CG GLU A1008 12947 17395 11638 -1454 -771 -2207 C ATOM 1556 CD GLU A1008 54.686 13.310 -34.201 1.00134.83 C ANISOU 1556 CD GLU A1008 15985 20687 14556 -1615 -825 -2240 C ATOM 1557 OE1 GLU A1008 54.576 12.695 -33.115 1.00130.02 O ANISOU 1557 OE1 GLU A1008 15290 20290 13821 -1584 -797 -2241 O ATOM 1558 OE2 GLU A1008 55.649 14.064 -34.468 1.00132.29 O ANISOU 1558 OE2 GLU A1008 15704 20335 14224 -1785 -900 -2254 O ATOM 1559 N THR A1009 52.562 9.206 -37.476 1.00 93.19 N ANISOU 1559 N THR A1009 10516 15239 9652 -1079 -644 -1739 N ATOM 1560 CA THR A1009 52.838 7.941 -38.176 1.00 91.98 C ANISOU 1560 CA THR A1009 10304 15108 9535 -1007 -629 -1595 C ATOM 1561 C THR A1009 52.213 7.974 -39.584 1.00 94.99 C ANISOU 1561 C THR A1009 10739 15312 10040 -951 -621 -1588 C ATOM 1562 O THR A1009 52.865 7.547 -40.537 1.00 94.28 O ANISOU 1562 O THR A1009 10629 15215 9976 -930 -632 -1510 O ATOM 1563 CB THR A1009 52.342 6.736 -37.342 1.00 99.29 C ANISOU 1563 CB THR A1009 11169 16132 10425 -936 -591 -1524 C ATOM 1564 OG1 THR A1009 52.941 6.785 -36.045 1.00 99.96 O ANISOU 1564 OG1 THR A1009 11184 16414 10382 -991 -597 -1525 O ATOM 1565 CG2 THR A1009 52.670 5.387 -37.985 1.00 97.01 C ANISOU 1565 CG2 THR A1009 10846 15835 10177 -859 -575 -1383 C ATOM 1566 N LEU A1010 50.980 8.512 -39.713 1.00 91.53 N ANISOU 1566 N LEU A1010 10360 14758 9661 -920 -601 -1665 N ATOM 1567 CA LEU A1010 50.273 8.637 -40.989 1.00 90.86 C ANISOU 1567 CA LEU A1010 10309 14536 9678 -876 -591 -1653 C ATOM 1568 C LEU A1010 50.976 9.628 -41.928 1.00 94.98 C ANISOU 1568 C LEU A1010 10855 14987 10247 -931 -626 -1660 C ATOM 1569 O LEU A1010 51.230 9.281 -43.081 1.00 93.68 O ANISOU 1569 O LEU A1010 10667 14803 10124 -907 -634 -1593 O ATOM 1570 CB LEU A1010 48.808 9.068 -40.773 1.00 91.09 C ANISOU 1570 CB LEU A1010 10373 14500 9737 -825 -555 -1712 C ATOM 1571 CG LEU A1010 47.783 7.955 -40.537 1.00 95.49 C ANISOU 1571 CG LEU A1010 10891 15104 10285 -768 -527 -1652 C ATOM 1572 CD1 LEU A1010 46.619 8.457 -39.707 1.00 96.26 C ANISOU 1572 CD1 LEU A1010 10993 15234 10348 -721 -492 -1706 C ATOM 1573 CD2 LEU A1010 47.263 7.389 -41.851 1.00 97.01 C ANISOU 1573 CD2 LEU A1010 11085 15223 10552 -745 -527 -1588 C ATOM 1574 N ASN A1011 51.303 10.839 -41.428 1.00 92.79 N ANISOU 1574 N ASN A1011 10624 14676 9956 -1008 -651 -1740 N ATOM 1575 CA ASN A1011 51.949 11.910 -42.193 1.00 93.36 C ANISOU 1575 CA ASN A1011 10724 14670 10080 -1088 -696 -1734 C ATOM 1576 C ASN A1011 53.403 11.606 -42.578 1.00 98.29 C ANISOU 1576 C ASN A1011 11272 15420 10653 -1159 -745 -1633 C ATOM 1577 O ASN A1011 53.832 12.029 -43.654 1.00 97.99 O ANISOU 1577 O ASN A1011 11212 15355 10666 -1183 -775 -1564 O ATOM 1578 CB ASN A1011 51.906 13.223 -41.416 1.00 95.23 C ANISOU 1578 CB ASN A1011 11055 14815 10314 -1167 -717 -1857 C ATOM 1579 CG ASN A1011 50.559 13.904 -41.377 1.00117.46 C ANISOU 1579 CG ASN A1011 13955 17476 13198 -1077 -667 -1944 C ATOM 1580 OD1 ASN A1011 49.561 13.440 -41.945 1.00111.40 O ANISOU 1580 OD1 ASN A1011 13160 16691 12476 -966 -617 -1901 O ATOM 1581 ND2 ASN A1011 50.509 15.047 -40.715 1.00110.42 N ANISOU 1581 ND2 ASN A1011 13172 16474 12308 -1124 -679 -2067 N ATOM 1582 N ASP A1012 54.165 10.913 -41.705 1.00 95.43 N ANISOU 1582 N ASP A1012 10856 15223 10182 -1185 -752 -1605 N ATOM 1583 CA ASP A1012 55.571 10.583 -41.961 1.00 95.64 C ANISOU 1583 CA ASP A1012 10792 15414 10133 -1233 -790 -1487 C ATOM 1584 C ASP A1012 55.707 9.497 -43.029 1.00 99.16 C ANISOU 1584 C ASP A1012 11181 15898 10598 -1106 -761 -1379 C ATOM 1585 O ASP A1012 56.597 9.599 -43.876 1.00 99.14 O ANISOU 1585 O ASP A1012 11118 15975 10577 -1119 -791 -1284 O ATOM 1586 CB ASP A1012 56.297 10.170 -40.669 1.00 98.02 C ANISOU 1586 CB ASP A1012 11038 15904 10302 -1284 -795 -1472 C ATOM 1587 CG ASP A1012 56.656 11.325 -39.743 1.00106.81 C ANISOU 1587 CG ASP A1012 12192 17037 11353 -1453 -849 -1567 C ATOM 1588 OD1 ASP A1012 55.928 12.345 -39.747 1.00106.31 O ANISOU 1588 OD1 ASP A1012 12241 16789 11363 -1491 -859 -1694 O ATOM 1589 OD2 ASP A1012 57.648 11.197 -38.996 1.00114.92 O ANISOU 1589 OD2 ASP A1012 13143 18267 12253 -1544 -879 -1515 O ATOM 1590 N ASN A1013 54.823 8.480 -43.007 1.00 95.11 N ANISOU 1590 N ASN A1013 10690 15332 10116 -989 -707 -1395 N ATOM 1591 CA ASN A1013 54.827 7.400 -43.995 1.00 94.50 C ANISOU 1591 CA ASN A1013 10594 15252 10058 -869 -680 -1327 C ATOM 1592 C ASN A1013 54.309 7.899 -45.354 1.00 98.61 C ANISOU 1592 C ASN A1013 11135 15669 10661 -854 -689 -1341 C ATOM 1593 O ASN A1013 54.713 7.357 -46.384 1.00 98.09 O ANISOU 1593 O ASN A1013 11038 15647 10586 -781 -686 -1284 O ATOM 1594 CB ASN A1013 54.020 6.193 -43.512 1.00 94.44 C ANISOU 1594 CB ASN A1013 10618 15202 10065 -783 -635 -1337 C ATOM 1595 CG ASN A1013 54.783 5.286 -42.574 1.00118.45 C ANISOU 1595 CG ASN A1013 13608 18374 13023 -748 -618 -1260 C ATOM 1596 OD1 ASN A1013 54.448 5.151 -41.393 1.00113.26 O ANISOU 1596 OD1 ASN A1013 12940 17756 12335 -775 -606 -1275 O ATOM 1597 ND2 ASN A1013 55.821 4.629 -43.076 1.00111.11 N ANISOU 1597 ND2 ASN A1013 12635 17534 12047 -670 -609 -1164 N ATOM 1598 N LEU A1014 53.445 8.944 -45.357 1.00 95.40 N ANISOU 1598 N LEU A1014 10777 15144 10328 -910 -695 -1412 N ATOM 1599 CA LEU A1014 52.902 9.562 -46.571 1.00 95.09 C ANISOU 1599 CA LEU A1014 10741 15022 10368 -901 -699 -1406 C ATOM 1600 C LEU A1014 53.981 10.354 -47.312 1.00100.27 C ANISOU 1600 C LEU A1014 11338 15744 11018 -966 -749 -1327 C ATOM 1601 O LEU A1014 53.946 10.428 -48.542 1.00 99.44 O ANISOU 1601 O LEU A1014 11188 15654 10942 -931 -754 -1272 O ATOM 1602 CB LEU A1014 51.708 10.477 -46.249 1.00 95.19 C ANISOU 1602 CB LEU A1014 10816 14895 10454 -922 -680 -1483 C ATOM 1603 CG LEU A1014 50.321 9.819 -46.222 1.00 99.30 C ANISOU 1603 CG LEU A1014 11362 15366 11001 -846 -632 -1515 C ATOM 1604 CD1 LEU A1014 49.323 10.692 -45.490 1.00 99.72 C ANISOU 1604 CD1 LEU A1014 11469 15334 11087 -845 -606 -1585 C ATOM 1605 CD2 LEU A1014 49.809 9.519 -47.629 1.00101.48 C ANISOU 1605 CD2 LEU A1014 11605 15633 11318 -803 -625 -1468 C ATOM 1606 N LYS A1015 54.941 10.936 -46.557 1.00 98.48 N ANISOU 1606 N LYS A1015 11097 15579 10740 -1071 -792 -1311 N ATOM 1607 CA LYS A1015 56.069 11.706 -47.090 1.00 99.41 C ANISOU 1607 CA LYS A1015 11148 15787 10837 -1168 -856 -1212 C ATOM 1608 C LYS A1015 57.091 10.779 -47.764 1.00104.25 C ANISOU 1608 C LYS A1015 11651 16605 11355 -1089 -857 -1091 C ATOM 1609 O LYS A1015 57.820 11.222 -48.653 1.00104.34 O ANISOU 1609 O LYS A1015 11576 16718 11349 -1123 -899 -980 O ATOM 1610 CB LYS A1015 56.738 12.545 -45.990 1.00102.91 C ANISOU 1610 CB LYS A1015 11619 16244 11239 -1329 -910 -1239 C ATOM 1611 CG LYS A1015 55.969 13.814 -45.641 1.00115.06 C ANISOU 1611 CG LYS A1015 13275 17565 12878 -1413 -924 -1347 C ATOM 1612 CD LYS A1015 56.639 14.600 -44.519 1.00123.87 C ANISOU 1612 CD LYS A1015 14442 18685 13937 -1584 -982 -1406 C ATOM 1613 CE LYS A1015 55.762 15.705 -43.973 1.00131.69 C ANISOU 1613 CE LYS A1015 15585 19437 15014 -1624 -979 -1556 C ATOM 1614 NZ LYS A1015 55.646 16.852 -44.915 1.00139.04 N ANISOU 1614 NZ LYS A1015 16556 20196 16076 -1681 -1015 -1510 N ATOM 1615 N VAL A1016 57.136 9.496 -47.340 1.00101.19 N ANISOU 1615 N VAL A1016 11264 16279 10904 -975 -808 -1102 N ATOM 1616 CA VAL A1016 58.007 8.457 -47.903 1.00101.51 C ANISOU 1616 CA VAL A1016 11227 16490 10852 -850 -789 -1004 C ATOM 1617 C VAL A1016 57.502 8.131 -49.319 1.00106.55 C ANISOU 1617 C VAL A1016 11862 17090 11530 -742 -768 -1010 C ATOM 1618 O VAL A1016 58.312 7.990 -50.236 1.00106.92 O ANISOU 1618 O VAL A1016 11821 17294 11511 -678 -779 -915 O ATOM 1619 CB VAL A1016 58.074 7.190 -46.991 1.00105.03 C ANISOU 1619 CB VAL A1016 11697 16967 11242 -752 -737 -1015 C ATOM 1620 CG1 VAL A1016 58.897 6.069 -47.627 1.00105.08 C ANISOU 1620 CG1 VAL A1016 11648 17115 11161 -583 -703 -922 C ATOM 1621 CG2 VAL A1016 58.624 7.531 -45.609 1.00105.41 C ANISOU 1621 CG2 VAL A1016 11721 17103 11227 -865 -758 -1000 C ATOM 1622 N ILE A1017 56.163 8.061 -49.488 1.00103.24 N ANISOU 1622 N ILE A1017 11529 16493 11206 -727 -742 -1113 N ATOM 1623 CA ILE A1017 55.474 7.757 -50.746 1.00103.12 C ANISOU 1623 CA ILE A1017 11517 16441 11224 -650 -724 -1137 C ATOM 1624 C ILE A1017 55.675 8.902 -51.763 1.00108.89 C ANISOU 1624 C ILE A1017 12162 17230 11983 -711 -765 -1061 C ATOM 1625 O ILE A1017 56.008 8.614 -52.914 1.00108.82 O ANISOU 1625 O ILE A1017 12083 17340 11925 -633 -765 -1011 O ATOM 1626 CB ILE A1017 53.962 7.452 -50.502 1.00105.50 C ANISOU 1626 CB ILE A1017 11914 16567 11605 -649 -692 -1243 C ATOM 1627 CG1 ILE A1017 53.776 6.321 -49.464 1.00105.72 C ANISOU 1627 CG1 ILE A1017 12014 16546 11611 -604 -661 -1289 C ATOM 1628 CG2 ILE A1017 53.230 7.105 -51.811 1.00106.05 C ANISOU 1628 CG2 ILE A1017 11979 16624 11689 -593 -680 -1266 C ATOM 1629 CD1 ILE A1017 52.469 6.385 -48.678 1.00112.04 C ANISOU 1629 CD1 ILE A1017 12880 17214 12475 -651 -643 -1360 C ATOM 1630 N GLU A1018 55.502 10.182 -51.345 1.00106.93 N ANISOU 1630 N GLU A1018 11920 16899 11808 -843 -799 -1049 N ATOM 1631 CA GLU A1018 55.655 11.344 -52.239 1.00107.98 C ANISOU 1631 CA GLU A1018 11978 17057 11992 -915 -842 -955 C ATOM 1632 C GLU A1018 57.119 11.527 -52.710 1.00114.40 C ANISOU 1632 C GLU A1018 12663 18090 12713 -943 -894 -807 C ATOM 1633 O GLU A1018 57.348 12.182 -53.728 1.00114.77 O ANISOU 1633 O GLU A1018 12612 18218 12778 -973 -930 -696 O ATOM 1634 CB GLU A1018 55.109 12.640 -51.597 1.00109.78 C ANISOU 1634 CB GLU A1018 12278 17100 12334 -1039 -862 -987 C ATOM 1635 CG GLU A1018 55.986 13.285 -50.531 1.00122.38 C ANISOU 1635 CG GLU A1018 13904 18689 13907 -1174 -914 -983 C ATOM 1636 CD GLU A1018 55.528 14.621 -49.971 1.00145.73 C ANISOU 1636 CD GLU A1018 16958 21441 16971 -1293 -939 -1035 C ATOM 1637 OE1 GLU A1018 54.709 15.307 -50.627 1.00139.03 O ANISOU 1637 OE1 GLU A1018 16128 20465 16232 -1276 -923 -1023 O ATOM 1638 OE2 GLU A1018 56.019 14.998 -48.882 1.00141.43 O ANISOU 1638 OE2 GLU A1018 16473 20869 16394 -1402 -974 -1085 O ATOM 1639 N LYS A1019 58.087 10.932 -51.982 1.00112.12 N ANISOU 1639 N LYS A1019 12359 17923 12320 -929 -898 -785 N ATOM 1640 CA LYS A1019 59.520 10.970 -52.291 1.00113.32 C ANISOU 1640 CA LYS A1019 12375 18330 12353 -942 -942 -626 C ATOM 1641 C LYS A1019 60.027 9.645 -52.914 1.00118.61 C ANISOU 1641 C LYS A1019 12988 19182 12896 -733 -891 -599 C ATOM 1642 O LYS A1019 61.136 9.620 -53.454 1.00119.17 O ANISOU 1642 O LYS A1019 12924 19506 12850 -696 -914 -452 O ATOM 1643 CB LYS A1019 60.327 11.279 -51.017 1.00116.52 C ANISOU 1643 CB LYS A1019 12785 18779 12707 -1076 -981 -598 C ATOM 1644 CG LYS A1019 60.267 12.739 -50.570 1.00131.52 C ANISOU 1644 CG LYS A1019 14721 20553 14697 -1301 -1057 -591 C ATOM 1645 CD LYS A1019 60.936 12.968 -49.205 1.00141.65 C ANISOU 1645 CD LYS A1019 16033 21871 15916 -1447 -1096 -607 C ATOM 1646 CE LYS A1019 62.438 13.159 -49.269 1.00153.01 C ANISOU 1646 CE LYS A1019 17321 23600 17217 -1546 -1166 -416 C ATOM 1647 NZ LYS A1019 62.816 14.463 -49.879 1.00162.72 N ANISOU 1647 NZ LYS A1019 18498 24829 18501 -1736 -1264 -295 N ATOM 1648 N AALA A1020 59.223 8.565 -52.836 0.49114.90 N ANISOU 1648 N AALA A1020 12625 18587 12447 -600 -823 -733 N ATOM 1649 N BALA A1020 59.223 8.565 -52.836 0.51114.90 N ANISOU 1649 N BALA A1020 12624 18586 12446 -600 -823 -733 N ATOM 1650 CA ALA A1020 59.565 7.237 -53.354 1.00115.25 C ANISOU 1650 CA ALA A1020 12666 18733 12389 -393 -770 -745 C ATOM 1651 C ALA A1020 59.868 7.243 -54.859 1.00121.44 C ANISOU 1651 C ALA A1020 13345 19693 13105 -295 -776 -682 C ATOM 1652 O ALA A1020 59.209 7.944 -55.631 1.00120.67 O ANISOU 1652 O ALA A1020 13217 19557 13075 -362 -800 -686 O ATOM 1653 CB ALA A1020 58.436 6.260 -53.072 1.00115.24 C ANISOU 1653 CB ALA A1020 12819 18514 12452 -320 -716 -907 C ATOM 1654 N ASP A1021 60.879 6.438 -55.258 1.00120.49 N ANISOU 1654 N ASP A1021 13159 19784 12838 -119 -747 -617 N ATOM 1655 CA ASP A1021 61.371 6.249 -56.630 1.00121.86 C ANISOU 1655 CA ASP A1021 13220 20185 12897 23 -742 -555 C ATOM 1656 C ASP A1021 61.092 4.823 -57.115 1.00127.43 C ANISOU 1656 C ASP A1021 14038 20840 13539 253 -670 -696 C ATOM 1657 O ASP A1021 60.813 4.625 -58.300 1.00127.43 O ANISOU 1657 O ASP A1021 14015 20916 13488 346 -661 -745 O ATOM 1658 CB ASP A1021 62.880 6.542 -56.709 1.00124.97 C ANISOU 1658 CB ASP A1021 13428 20911 13144 51 -771 -340 C ATOM 1659 CG ASP A1021 63.265 7.950 -56.304 1.00135.06 C ANISOU 1659 CG ASP A1021 14602 22238 14475 -202 -858 -194 C ATOM 1660 OD1 ASP A1021 63.548 8.166 -55.107 1.00135.24 O ANISOU 1660 OD1 ASP A1021 14668 22190 14526 -320 -874 -182 O ATOM 1661 OD2 ASP A1021 63.299 8.832 -57.188 1.00141.83 O ANISOU 1661 OD2 ASP A1021 15338 23208 15345 -286 -913 -88 O ATOM 1662 N ASN A1022 61.176 3.838 -56.196 1.00125.04 N ANISOU 1662 N ASN A1022 13860 20409 13239 338 -620 -758 N ATOM 1663 CA ASN A1022 60.960 2.412 -56.459 1.00125.99 C ANISOU 1663 CA ASN A1022 14127 20423 13321 548 -554 -892 C ATOM 1664 C ASN A1022 59.713 1.878 -55.732 1.00130.23 C ANISOU 1664 C ASN A1022 14856 20623 14002 466 -541 -1049 C ATOM 1665 O ASN A1022 59.192 2.538 -54.831 1.00128.60 O ANISOU 1665 O ASN A1022 14657 20301 13903 282 -571 -1038 O ATOM 1666 CB ASN A1022 62.197 1.604 -56.057 1.00127.97 C ANISOU 1666 CB ASN A1022 14350 20829 13444 754 -500 -792 C ATOM 1667 CG ASN A1022 62.668 1.881 -54.655 1.00151.25 C ANISOU 1667 CG ASN A1022 17257 23793 16417 649 -507 -674 C ATOM 1668 OD1 ASN A1022 63.394 2.845 -54.397 1.00146.22 O ANISOU 1668 OD1 ASN A1022 16459 23363 15734 527 -556 -516 O ATOM 1669 ND2 ASN A1022 62.250 1.053 -53.718 1.00143.00 N ANISOU 1669 ND2 ASN A1022 16354 22538 15442 678 -467 -743 N ATOM 1670 N ALA A1023 59.249 0.678 -56.132 1.00128.69 N ANISOU 1670 N ALA A1023 14818 20277 13801 603 -501 -1192 N ATOM 1671 CA ALA A1023 58.068 0.009 -55.583 1.00128.72 C ANISOU 1671 CA ALA A1023 15003 19978 13927 529 -496 -1328 C ATOM 1672 C ALA A1023 58.267 -0.473 -54.138 1.00134.02 C ANISOU 1672 C ALA A1023 15732 20536 14653 525 -470 -1274 C ATOM 1673 O ALA A1023 57.296 -0.488 -53.378 1.00132.91 O ANISOU 1673 O ALA A1023 15668 20206 14627 384 -486 -1322 O ATOM 1674 CB ALA A1023 57.681 -1.167 -56.464 1.00130.71 C ANISOU 1674 CB ALA A1023 15411 20110 14142 668 -470 -1486 C ATOM 1675 N ALA A1024 59.505 -0.867 -53.762 1.00132.50 N ANISOU 1675 N ALA A1024 15486 20489 14368 684 -428 -1158 N ATOM 1676 CA ALA A1024 59.838 -1.364 -52.420 1.00132.94 C ANISOU 1676 CA ALA A1024 15567 20492 14452 702 -396 -1077 C ATOM 1677 C ALA A1024 59.679 -0.285 -51.334 1.00136.23 C ANISOU 1677 C ALA A1024 15884 20955 14924 477 -440 -1001 C ATOM 1678 O ALA A1024 59.356 -0.620 -50.192 1.00135.43 O ANISOU 1678 O ALA A1024 15829 20745 14884 423 -429 -988 O ATOM 1679 CB ALA A1024 61.253 -1.918 -52.399 1.00135.24 C ANISOU 1679 CB ALA A1024 15790 20988 14608 934 -337 -944 C ATOM 1680 N GLN A1025 59.895 0.999 -51.695 1.00132.87 N ANISOU 1680 N GLN A1025 15326 20684 14473 348 -492 -953 N ATOM 1681 CA GLN A1025 59.763 2.151 -50.798 1.00132.12 C ANISOU 1681 CA GLN A1025 15158 20616 14426 131 -541 -907 C ATOM 1682 C GLN A1025 58.304 2.376 -50.382 1.00135.81 C ANISOU 1682 C GLN A1025 15730 20841 15031 -13 -559 -1034 C ATOM 1683 O GLN A1025 58.052 2.810 -49.257 1.00134.84 O ANISOU 1683 O GLN A1025 15604 20680 14950 -138 -573 -1027 O ATOM 1684 CB GLN A1025 60.313 3.423 -51.462 1.00133.46 C ANISOU 1684 CB GLN A1025 15184 20976 14549 35 -596 -824 C ATOM 1685 CG GLN A1025 61.823 3.589 -51.347 1.00149.95 C ANISOU 1685 CG GLN A1025 17120 23360 16495 85 -600 -644 C ATOM 1686 CD GLN A1025 62.266 4.982 -51.729 1.00167.95 C ANISOU 1686 CD GLN A1025 19262 25798 18755 -83 -676 -544 C ATOM 1687 OE1 GLN A1025 62.043 5.956 -51.002 1.00162.82 O ANISOU 1687 OE1 GLN A1025 18609 25088 18170 -294 -729 -546 O ATOM 1688 NE2 GLN A1025 62.924 5.106 -52.870 1.00160.10 N ANISOU 1688 NE2 GLN A1025 18155 25011 17666 8 -686 -453 N ATOM 1689 N VAL A1026 57.354 2.085 -51.295 1.00132.98 N ANISOU 1689 N VAL A1026 15455 20346 14724 7 -558 -1145 N ATOM 1690 CA VAL A1026 55.909 2.233 -51.081 1.00132.30 C ANISOU 1690 CA VAL A1026 15453 20065 14749 -114 -573 -1247 C ATOM 1691 C VAL A1026 55.381 1.021 -50.291 1.00137.29 C ANISOU 1691 C VAL A1026 16206 20532 15425 -76 -544 -1288 C ATOM 1692 O VAL A1026 54.614 1.207 -49.345 1.00136.13 O ANISOU 1692 O VAL A1026 16081 20299 15344 -184 -553 -1301 O ATOM 1693 CB VAL A1026 55.133 2.429 -52.419 1.00136.03 C ANISOU 1693 CB VAL A1026 15940 20506 15240 -125 -590 -1324 C ATOM 1694 CG1 VAL A1026 53.654 2.725 -52.172 1.00135.06 C ANISOU 1694 CG1 VAL A1026 15872 20229 15216 -257 -604 -1395 C ATOM 1695 CG2 VAL A1026 55.756 3.533 -53.270 1.00135.85 C ANISOU 1695 CG2 VAL A1026 15780 20665 15172 -147 -618 -1251 C ATOM 1696 N LYS A1027 55.803 -0.205 -50.679 1.00135.88 N ANISOU 1696 N LYS A1027 16106 20313 15208 85 -510 -1302 N ATOM 1697 CA LYS A1027 55.408 -1.486 -50.080 1.00136.86 C ANISOU 1697 CA LYS A1027 16362 20258 15382 138 -485 -1325 C ATOM 1698 C LYS A1027 55.607 -1.528 -48.557 1.00141.79 C ANISOU 1698 C LYS A1027 16945 20902 16028 97 -471 -1227 C ATOM 1699 O LYS A1027 54.702 -1.963 -47.844 1.00141.22 O ANISOU 1699 O LYS A1027 16938 20688 16032 23 -478 -1242 O ATOM 1700 CB LYS A1027 56.188 -2.644 -50.726 1.00140.93 C ANISOU 1700 CB LYS A1027 16961 20750 15837 355 -441 -1336 C ATOM 1701 CG LYS A1027 55.627 -3.102 -52.064 1.00156.73 C ANISOU 1701 CG LYS A1027 19072 22648 17830 392 -455 -1479 C ATOM 1702 CD LYS A1027 56.476 -4.210 -52.668 1.00169.06 C ANISOU 1702 CD LYS A1027 20731 24189 19317 636 -404 -1506 C ATOM 1703 CE LYS A1027 55.924 -4.693 -53.985 1.00181.83 C ANISOU 1703 CE LYS A1027 22470 25710 20908 670 -421 -1674 C ATOM 1704 NZ LYS A1027 56.768 -5.763 -54.578 1.00193.31 N ANISOU 1704 NZ LYS A1027 24038 27134 22277 935 -366 -1723 N ATOM 1705 N ASP A1028 56.776 -1.076 -48.066 1.00139.45 N ANISOU 1705 N ASP A1028 16527 20806 15651 134 -456 -1116 N ATOM 1706 CA ASP A1028 57.109 -1.086 -46.640 1.00139.74 C ANISOU 1706 CA ASP A1028 16501 20917 15677 96 -442 -1015 C ATOM 1707 C ASP A1028 56.414 0.045 -45.864 1.00143.11 C ANISOU 1707 C ASP A1028 16874 21364 16138 -104 -484 -1047 C ATOM 1708 O ASP A1028 55.965 -0.190 -44.742 1.00142.76 O ANISOU 1708 O ASP A1028 16831 21290 16123 -158 -479 -1024 O ATOM 1709 CB ASP A1028 58.631 -1.001 -46.438 1.00142.43 C ANISOU 1709 CB ASP A1028 16721 21501 15896 197 -415 -877 C ATOM 1710 CG ASP A1028 59.144 -1.881 -45.316 1.00153.68 C ANISOU 1710 CG ASP A1028 18125 22970 17296 287 -366 -752 C ATOM 1711 OD1 ASP A1028 58.891 -1.549 -44.136 1.00153.84 O ANISOU 1711 OD1 ASP A1028 18094 23031 17329 164 -379 -718 O ATOM 1712 OD2 ASP A1028 59.812 -2.894 -45.616 1.00160.86 O ANISOU 1712 OD2 ASP A1028 19065 23888 18166 492 -310 -683 O ATOM 1713 N ALA A1029 56.331 1.258 -46.453 1.00139.23 N ANISOU 1713 N ALA A1029 16334 20925 15641 -200 -523 -1093 N ATOM 1714 CA ALA A1029 55.723 2.443 -45.834 1.00138.40 C ANISOU 1714 CA ALA A1029 16198 20820 15569 -365 -557 -1137 C ATOM 1715 C ALA A1029 54.196 2.335 -45.695 1.00142.06 C ANISOU 1715 C ALA A1029 16742 21111 16125 -425 -561 -1226 C ATOM 1716 O ALA A1029 53.618 3.003 -44.833 1.00141.27 O ANISOU 1716 O ALA A1029 16627 21007 16041 -521 -571 -1254 O ATOM 1717 CB ALA A1029 56.074 3.686 -46.636 1.00138.86 C ANISOU 1717 CB ALA A1029 16198 20949 15613 -434 -596 -1144 C ATOM 1718 N LEU A1030 53.552 1.510 -46.539 1.00139.05 N ANISOU 1718 N LEU A1030 16442 20602 15788 -369 -554 -1269 N ATOM 1719 CA LEU A1030 52.100 1.318 -46.547 1.00138.70 C ANISOU 1719 CA LEU A1030 16461 20422 15816 -436 -563 -1330 C ATOM 1720 C LEU A1030 51.651 0.229 -45.564 1.00143.59 C ANISOU 1720 C LEU A1030 17126 20970 16462 -430 -551 -1290 C ATOM 1721 O LEU A1030 50.544 0.321 -45.028 1.00142.80 O ANISOU 1721 O LEU A1030 17030 20827 16399 -512 -562 -1301 O ATOM 1722 CB LEU A1030 51.635 0.973 -47.969 1.00138.78 C ANISOU 1722 CB LEU A1030 16531 20354 15847 -411 -574 -1392 C ATOM 1723 CG LEU A1030 50.364 1.655 -48.478 1.00142.94 C ANISOU 1723 CG LEU A1030 17054 20838 16418 -509 -594 -1443 C ATOM 1724 CD1 LEU A1030 50.553 3.155 -48.647 1.00142.53 C ANISOU 1724 CD1 LEU A1030 16919 20870 16366 -555 -600 -1439 C ATOM 1725 CD2 LEU A1030 49.970 1.091 -49.809 1.00145.82 C ANISOU 1725 CD2 LEU A1030 17475 21149 16780 -492 -606 -1499 C ATOM 1726 N THR A1031 52.509 -0.789 -45.321 1.00141.49 N ANISOU 1726 N THR A1031 16883 20702 16174 -326 -526 -1224 N ATOM 1727 CA THR A1031 52.236 -1.903 -44.399 1.00142.24 C ANISOU 1727 CA THR A1031 17015 20724 16304 -309 -513 -1153 C ATOM 1728 C THR A1031 52.212 -1.431 -42.934 1.00146.38 C ANISOU 1728 C THR A1031 17437 21383 16798 -373 -508 -1086 C ATOM 1729 O THR A1031 51.531 -2.046 -42.110 1.00146.26 O ANISOU 1729 O THR A1031 17424 21331 16816 -407 -509 -1030 O ATOM 1730 CB THR A1031 53.247 -3.048 -44.588 1.00151.12 C ANISOU 1730 CB THR A1031 18196 21806 17416 -151 -477 -1090 C ATOM 1731 OG1 THR A1031 54.562 -2.520 -44.770 1.00150.55 O ANISOU 1731 OG1 THR A1031 18039 21909 17255 -65 -453 -1050 O ATOM 1732 CG2 THR A1031 52.885 -3.962 -45.748 1.00150.24 C ANISOU 1732 CG2 THR A1031 18236 21498 17351 -95 -485 -1169 C ATOM 1733 N LYS A1032 52.947 -0.344 -42.621 1.00143.02 N ANISOU 1733 N LYS A1032 16919 21121 16302 -400 -507 -1091 N ATOM 1734 CA LYS A1032 53.021 0.255 -41.283 1.00143.09 C ANISOU 1734 CA LYS A1032 16834 21279 16255 -469 -507 -1060 C ATOM 1735 C LYS A1032 51.686 0.917 -40.920 1.00147.11 C ANISOU 1735 C LYS A1032 17348 21753 16795 -567 -525 -1135 C ATOM 1736 O LYS A1032 51.269 0.862 -39.762 1.00146.98 O ANISOU 1736 O LYS A1032 17279 21819 16749 -601 -520 -1102 O ATOM 1737 CB LYS A1032 54.169 1.285 -41.200 1.00145.48 C ANISOU 1737 CB LYS A1032 17058 21747 16470 -497 -515 -1062 C ATOM 1738 CG LYS A1032 55.565 0.724 -41.490 1.00158.38 C ANISOU 1738 CG LYS A1032 18652 23483 18043 -391 -492 -958 C ATOM 1739 CD LYS A1032 56.251 0.150 -40.250 1.00167.87 C ANISOU 1739 CD LYS A1032 19764 24848 19172 -360 -463 -827 C ATOM 1740 CE LYS A1032 57.496 -0.637 -40.591 1.00178.53 C ANISOU 1740 CE LYS A1032 21081 26284 20469 -209 -424 -698 C ATOM 1741 NZ LYS A1032 58.609 0.235 -41.053 1.00187.50 N ANISOU 1741 NZ LYS A1032 22136 27598 21507 -230 -443 -676 N ATOM 1742 N MET A1033 51.017 1.522 -41.922 1.00143.58 N ANISOU 1742 N MET A1033 16952 21206 16394 -597 -542 -1224 N ATOM 1743 CA MET A1033 49.727 2.206 -41.791 1.00143.30 C ANISOU 1743 CA MET A1033 16921 21143 16385 -661 -550 -1284 C ATOM 1744 C MET A1033 48.561 1.210 -41.678 1.00148.51 C ANISOU 1744 C MET A1033 17608 21729 17090 -675 -555 -1237 C ATOM 1745 O MET A1033 47.491 1.583 -41.193 1.00148.01 O ANISOU 1745 O MET A1033 17516 21702 17021 -717 -556 -1243 O ATOM 1746 CB MET A1033 49.492 3.142 -42.992 1.00144.97 C ANISOU 1746 CB MET A1033 17161 21292 16630 -678 -562 -1361 C ATOM 1747 CG MET A1033 50.446 4.318 -43.048 1.00148.41 C ANISOU 1747 CG MET A1033 17567 21790 17031 -699 -570 -1397 C ATOM 1748 SD MET A1033 50.655 4.964 -44.726 1.00152.00 S ANISOU 1748 SD MET A1033 18038 22187 17528 -691 -587 -1422 S ATOM 1749 CE MET A1033 49.347 6.156 -44.782 1.00148.41 C ANISOU 1749 CE MET A1033 17596 21668 17125 -735 -581 -1484 C ATOM 1750 N ARG A1034 48.768 -0.045 -42.131 1.00146.45 N ANISOU 1750 N ARG A1034 17408 21368 16869 -640 -561 -1186 N ATOM 1751 CA ARG A1034 47.767 -1.116 -42.129 1.00147.32 C ANISOU 1751 CA ARG A1034 17566 21377 17033 -680 -582 -1133 C ATOM 1752 C ARG A1034 47.425 -1.602 -40.706 1.00153.12 C ANISOU 1752 C ARG A1034 18231 22197 17752 -704 -579 -1022 C ATOM 1753 O ARG A1034 46.248 -1.833 -40.415 1.00153.00 O ANISOU 1753 O ARG A1034 18197 22184 17751 -776 -602 -977 O ATOM 1754 CB ARG A1034 48.257 -2.295 -42.986 1.00148.14 C ANISOU 1754 CB ARG A1034 17779 21323 17182 -625 -588 -1126 C ATOM 1755 CG ARG A1034 47.143 -3.198 -43.498 1.00158.51 C ANISOU 1755 CG ARG A1034 19182 22487 18557 -704 -629 -1117 C ATOM 1756 CD ARG A1034 47.690 -4.333 -44.343 1.00167.51 C ANISOU 1756 CD ARG A1034 20462 23448 19737 -638 -634 -1145 C ATOM 1757 NE ARG A1034 46.627 -5.206 -44.843 1.00175.20 N ANISOU 1757 NE ARG A1034 21542 24261 20766 -744 -687 -1151 N ATOM 1758 CZ ARG A1034 46.001 -5.040 -46.004 1.00188.16 C ANISOU 1758 CZ ARG A1034 23235 25856 22400 -816 -720 -1248 C ATOM 1759 NH1 ARG A1034 46.321 -4.028 -46.801 1.00173.49 N ANISOU 1759 NH1 ARG A1034 21329 24099 20492 -777 -701 -1336 N ATOM 1760 NH2 ARG A1034 45.048 -5.884 -46.377 1.00175.90 N ANISOU 1760 NH2 ARG A1034 21779 24169 20887 -939 -778 -1245 N ATOM 1761 N ALA A1035 48.443 -1.768 -39.836 1.00151.01 N ANISOU 1761 N ALA A1035 17908 22028 17443 -649 -553 -959 N ATOM 1762 CA ALA A1035 48.273 -2.245 -38.458 1.00152.01 C ANISOU 1762 CA ALA A1035 17944 22273 17541 -662 -547 -836 C ATOM 1763 C ALA A1035 48.101 -1.093 -37.441 1.00156.44 C ANISOU 1763 C ALA A1035 18391 23047 18003 -689 -534 -878 C ATOM 1764 O ALA A1035 47.759 -1.353 -36.284 1.00156.56 O ANISOU 1764 O ALA A1035 18311 23203 17972 -705 -530 -786 O ATOM 1765 CB ALA A1035 49.458 -3.115 -38.062 1.00153.57 C ANISOU 1765 CB ALA A1035 18130 22481 17738 -579 -521 -727 C ATOM 1766 N ALA A1036 48.327 0.166 -37.875 1.00152.97 N ANISOU 1766 N ALA A1036 17966 22627 17529 -694 -529 -1014 N ATOM 1767 CA ALA A1036 48.213 1.361 -37.030 1.00153.09 C ANISOU 1767 CA ALA A1036 17916 22798 17454 -716 -519 -1092 C ATOM 1768 C ALA A1036 46.880 2.116 -37.238 1.00157.20 C ANISOU 1768 C ALA A1036 18452 23298 17981 -734 -520 -1166 C ATOM 1769 O ALA A1036 46.584 3.048 -36.482 1.00156.98 O ANISOU 1769 O ALA A1036 18383 23386 17877 -730 -505 -1236 O ATOM 1770 CB ALA A1036 49.385 2.296 -37.295 1.00153.58 C ANISOU 1770 CB ALA A1036 17995 22884 17477 -718 -518 -1181 C ATOM 1771 N ALA A1037 46.079 1.709 -38.247 1.00153.83 N ANISOU 1771 N ALA A1037 18080 22735 17633 -748 -535 -1150 N ATOM 1772 CA ALA A1037 44.783 2.314 -38.576 1.00153.64 C ANISOU 1772 CA ALA A1037 18055 22710 17613 -758 -531 -1184 C ATOM 1773 C ALA A1037 43.712 2.004 -37.515 1.00158.50 C ANISOU 1773 C ALA A1037 18577 23477 18169 -765 -528 -1094 C ATOM 1774 O ALA A1037 42.777 2.792 -37.345 1.00158.22 O ANISOU 1774 O ALA A1037 18508 23520 18088 -736 -507 -1129 O ATOM 1775 CB ALA A1037 44.314 1.831 -39.939 1.00154.00 C ANISOU 1775 CB ALA A1037 18166 22607 17739 -791 -554 -1171 C ATOM 1776 N LEU A1038 43.853 0.861 -36.811 1.00155.81 N ANISOU 1776 N LEU A1038 18187 23186 17827 -790 -545 -964 N ATOM 1777 CA LEU A1038 42.928 0.402 -35.768 1.00156.53 C ANISOU 1777 CA LEU A1038 18165 23449 17860 -807 -551 -837 C ATOM 1778 C LEU A1038 43.218 1.042 -34.388 1.00160.80 C ANISOU 1778 C LEU A1038 18606 24217 18275 -753 -518 -868 C ATOM 1779 O LEU A1038 42.423 0.865 -33.463 1.00161.30 O ANISOU 1779 O LEU A1038 18554 24472 18260 -746 -516 -775 O ATOM 1780 CB LEU A1038 42.939 -1.140 -35.655 1.00157.24 C ANISOU 1780 CB LEU A1038 18248 23480 18017 -869 -591 -661 C ATOM 1781 CG LEU A1038 44.299 -1.834 -35.522 1.00161.99 C ANISOU 1781 CG LEU A1038 18883 24006 18658 -843 -585 -629 C ATOM 1782 CD1 LEU A1038 44.316 -2.772 -34.333 1.00163.27 C ANISOU 1782 CD1 LEU A1038 18935 24300 18799 -855 -593 -441 C ATOM 1783 CD2 LEU A1038 44.654 -2.578 -36.795 1.00164.06 C ANISOU 1783 CD2 LEU A1038 19289 24009 19036 -859 -608 -644 C ATOM 1784 N ASP A1039 44.333 1.791 -34.257 1.00156.79 N ANISOU 1784 N ASP A1039 18135 23706 17733 -724 -498 -997 N ATOM 1785 CA ASP A1039 44.723 2.453 -33.007 1.00157.21 C ANISOU 1785 CA ASP A1039 18111 23968 17653 -693 -474 -1059 C ATOM 1786 C ASP A1039 43.867 3.696 -32.714 1.00161.23 C ANISOU 1786 C ASP A1039 18625 24554 18082 -635 -445 -1191 C ATOM 1787 O ASP A1039 43.608 3.986 -31.545 1.00161.81 O ANISOU 1787 O ASP A1039 18607 24848 18026 -595 -426 -1203 O ATOM 1788 CB ASP A1039 46.206 2.840 -33.041 1.00158.76 C ANISOU 1788 CB ASP A1039 18352 24135 17836 -710 -475 -1146 C ATOM 1789 N ALA A1040 43.446 4.429 -33.766 1.00156.93 N ANISOU 1789 N ALA A1040 18181 23839 17607 -615 -437 -1285 N ATOM 1790 CA ALA A1040 42.636 5.645 -33.648 1.00157.15 C ANISOU 1790 CA ALA A1040 18236 23897 17579 -533 -398 -1405 C ATOM 1791 C ALA A1040 41.127 5.353 -33.677 1.00161.32 C ANISOU 1791 C ALA A1040 18686 24521 18087 -487 -384 -1288 C ATOM 1792 O ALA A1040 40.350 6.143 -33.134 1.00161.70 O ANISOU 1792 O ALA A1040 18708 24687 18042 -385 -340 -1345 O ATOM 1793 CB ALA A1040 42.992 6.617 -34.762 1.00157.20 C ANISOU 1793 CB ALA A1040 18374 23681 17674 -531 -394 -1533 C ATOM 1794 N GLN A1041 40.717 4.231 -34.308 1.00157.47 N ANISOU 1794 N GLN A1041 18166 23990 17677 -563 -422 -1123 N ATOM 1795 CA GLN A1041 39.315 3.820 -34.436 1.00157.76 C ANISOU 1795 CA GLN A1041 18118 24130 17695 -564 -426 -978 C ATOM 1796 C GLN A1041 38.842 2.966 -33.247 1.00162.55 C ANISOU 1796 C GLN A1041 18571 24981 18209 -580 -443 -812 C ATOM 1797 O GLN A1041 37.744 3.202 -32.739 1.00163.01 O ANISOU 1797 O GLN A1041 18522 25251 18162 -516 -420 -744 O ATOM 1798 CB GLN A1041 39.095 3.056 -35.748 1.00158.37 C ANISOU 1798 CB GLN A1041 18250 24026 17896 -668 -472 -896 C ATOM 1799 N LYS A1042 39.655 1.976 -32.819 1.00159.02 N ANISOU 1799 N LYS A1042 18101 24521 17796 -655 -479 -729 N ATOM 1800 CA LYS A1042 39.334 1.081 -31.702 1.00188.46 C ANISOU 1800 CA LYS A1042 21676 28476 21455 -683 -500 -541 C ATOM 1801 C LYS A1042 40.567 0.838 -30.825 1.00207.78 C ANISOU 1801 C LYS A1042 24094 30985 23869 -678 -494 -558 C ATOM 1802 O LYS A1042 40.435 0.527 -29.644 1.00166.74 O ANISOU 1802 O LYS A1042 18746 26043 18562 -660 -491 -455 O ATOM 1803 CB LYS A1042 38.740 -0.255 -32.202 1.00191.31 C ANISOU 1803 CB LYS A1042 22016 28756 21915 -811 -566 -325 C ATOM 1804 CG LYS A1042 39.642 -1.072 -33.131 1.00205.39 C ANISOU 1804 CG LYS A1042 23944 30236 23859 -894 -603 -332 C ATOM 1805 N LYS A1059 29.978 0.479 -35.332 1.00138.50 N ANISOU 1805 N LYS A1059 14804 22950 14871 -997 -635 460 N ATOM 1806 CA LYS A1059 29.406 0.768 -36.643 1.00138.07 C ANISOU 1806 CA LYS A1059 14791 22824 14845 -1057 -639 458 C ATOM 1807 C LYS A1059 30.100 1.970 -37.293 1.00140.89 C ANISOU 1807 C LYS A1059 15293 22980 15261 -887 -549 201 C ATOM 1808 O LYS A1059 30.534 1.863 -38.438 1.00139.34 O ANISOU 1808 O LYS A1059 15228 22534 15180 -981 -576 104 O ATOM 1809 CB LYS A1059 27.892 1.005 -36.539 1.00142.09 C ANISOU 1809 CB LYS A1059 15091 23708 15189 -1034 -626 687 C ATOM 1810 N ASP A1060 30.207 3.105 -36.568 1.00138.06 N ANISOU 1810 N ASP A1060 14912 22727 14818 -642 -446 90 N ATOM 1811 CA ASP A1060 30.852 4.332 -37.050 1.00137.09 C ANISOU 1811 CA ASP A1060 14927 22409 14751 -479 -364 -142 C ATOM 1812 C ASP A1060 32.379 4.182 -37.040 1.00139.42 C ANISOU 1812 C ASP A1060 15391 22409 15175 -525 -387 -339 C ATOM 1813 O ASP A1060 33.046 4.663 -37.959 1.00137.83 O ANISOU 1813 O ASP A1060 15322 21969 15077 -524 -375 -481 O ATOM 1814 CB ASP A1060 30.421 5.540 -36.204 1.00140.10 C ANISOU 1814 CB ASP A1060 15251 22982 14998 -211 -254 -201 C ATOM 1815 CG ASP A1060 30.644 6.870 -36.891 1.00149.97 C ANISOU 1815 CG ASP A1060 16623 24060 16299 -46 -168 -375 C ATOM 1816 OD1 ASP A1060 31.712 7.480 -36.670 1.00150.04 O ANISOU 1816 OD1 ASP A1060 16776 23863 16369 21 -142 -593 O ATOM 1817 OD2 ASP A1060 29.748 7.303 -37.648 1.00155.69 O ANISOU 1817 OD2 ASP A1060 17291 24863 16999 8 -129 -278 O ATOM 1818 N PHE A1061 32.924 3.514 -36.002 1.00136.19 N ANISOU 1818 N PHE A1061 14957 22042 14747 -564 -420 -322 N ATOM 1819 CA PHE A1061 34.355 3.242 -35.850 1.00135.01 C ANISOU 1819 CA PHE A1061 14932 21672 14694 -607 -442 -464 C ATOM 1820 C PHE A1061 34.751 1.998 -36.650 1.00138.54 C ANISOU 1820 C PHE A1061 15448 21921 15269 -806 -530 -396 C ATOM 1821 O PHE A1061 35.890 1.907 -37.110 1.00137.10 O ANISOU 1821 O PHE A1061 15398 21506 15188 -831 -540 -525 O ATOM 1822 CB PHE A1061 34.720 3.065 -34.371 1.00137.46 C ANISOU 1822 CB PHE A1061 15162 22153 14913 -552 -433 -452 C ATOM 1823 N ARG A1062 33.803 1.048 -36.815 1.00136.14 N ANISOU 1823 N ARG A1062 15060 21715 14953 -948 -595 -192 N ATOM 1824 CA ARG A1062 33.963 -0.206 -37.561 1.00135.94 C ANISOU 1824 CA ARG A1062 15112 21500 15040 -1151 -686 -120 C ATOM 1825 C ARG A1062 34.096 0.061 -39.071 1.00138.79 C ANISOU 1825 C ARG A1062 15597 21656 15479 -1194 -691 -236 C ATOM 1826 O ARG A1062 34.769 -0.698 -39.773 1.00137.93 O ANISOU 1826 O ARG A1062 15618 21314 15476 -1295 -741 -290 O ATOM 1827 CB ARG A1062 32.769 -1.137 -37.293 1.00137.95 C ANISOU 1827 CB ARG A1062 15234 21940 15240 -1306 -761 135 C ATOM 1828 CG ARG A1062 33.162 -2.571 -36.945 1.00149.06 C ANISOU 1828 CG ARG A1062 16675 23230 16733 -1469 -849 256 C ATOM 1829 CD ARG A1062 33.049 -2.866 -35.457 1.00159.54 C ANISOU 1829 CD ARG A1062 17845 24793 17980 -1426 -846 408 C ATOM 1830 NE ARG A1062 31.657 -2.975 -35.010 1.00169.38 N ANISOU 1830 NE ARG A1062 18893 26365 19100 -1482 -875 642 N ATOM 1831 CZ ARG A1062 30.982 -4.117 -34.915 1.00184.33 C ANISOU 1831 CZ ARG A1062 20719 28308 21011 -1693 -979 885 C ATOM 1832 NH1 ARG A1062 31.560 -5.268 -35.232 1.00172.16 N ANISOU 1832 NH1 ARG A1062 19316 26474 19622 -1859 -1059 909 N ATOM 1833 NH2 ARG A1062 29.722 -4.116 -34.498 1.00171.44 N ANISOU 1833 NH2 ARG A1062 18881 27017 19241 -1737 -1004 1113 N ATOM 1834 N HIS A1063 33.440 1.135 -39.558 1.00135.06 N ANISOU 1834 N HIS A1063 15080 21287 14949 -1102 -635 -267 N ATOM 1835 CA HIS A1063 33.450 1.583 -40.953 1.00134.05 C ANISOU 1835 CA HIS A1063 15027 21034 14872 -1120 -626 -352 C ATOM 1836 C HIS A1063 34.526 2.660 -41.166 1.00136.26 C ANISOU 1836 C HIS A1063 15407 21161 15205 -967 -557 -557 C ATOM 1837 O HIS A1063 35.098 2.743 -42.256 1.00134.84 O ANISOU 1837 O HIS A1063 15322 20810 15102 -999 -567 -652 O ATOM 1838 CB HIS A1063 32.056 2.104 -41.348 1.00135.65 C ANISOU 1838 CB HIS A1063 15094 21470 14975 -1108 -603 -218 C ATOM 1839 CG HIS A1063 32.002 2.860 -42.639 1.00138.48 C ANISOU 1839 CG HIS A1063 15487 21767 15360 -1070 -565 -291 C ATOM 1840 ND1 HIS A1063 31.783 4.224 -42.661 1.00140.14 N ANISOU 1840 ND1 HIS A1063 15664 22045 15537 -867 -465 -340 N ATOM 1841 CD2 HIS A1063 32.137 2.419 -43.912 1.00139.90 C ANISOU 1841 CD2 HIS A1063 15727 21835 15592 -1208 -615 -313 C ATOM 1842 CE1 HIS A1063 31.777 4.568 -43.939 1.00139.13 C ANISOU 1842 CE1 HIS A1063 15561 21852 15450 -890 -457 -367 C ATOM 1843 NE2 HIS A1063 31.997 3.517 -44.728 1.00139.29 N ANISOU 1843 NE2 HIS A1063 15632 21781 15513 -1093 -546 -357 N ATOM 1844 N GLY A1064 34.783 3.457 -40.123 1.00132.73 N ANISOU 1844 N GLY A1064 14935 20787 14708 -813 -495 -619 N ATOM 1845 CA GLY A1064 35.780 4.524 -40.118 1.00131.74 C ANISOU 1845 CA GLY A1064 14904 20529 14623 -688 -439 -805 C ATOM 1846 C GLY A1064 37.167 4.052 -40.510 1.00134.30 C ANISOU 1846 C GLY A1064 15348 20633 15046 -755 -478 -909 C ATOM 1847 O GLY A1064 37.812 4.660 -41.368 1.00133.12 O ANISOU 1847 O GLY A1064 15278 20341 14959 -729 -463 -1017 O ATOM 1848 N PHE A1065 37.613 2.937 -39.904 1.00130.66 N ANISOU 1848 N PHE A1065 14889 20158 14596 -836 -526 -856 N ATOM 1849 CA PHE A1065 38.902 2.309 -40.190 1.00129.52 C ANISOU 1849 CA PHE A1065 14847 19832 14534 -881 -558 -923 C ATOM 1850 C PHE A1065 38.848 1.551 -41.518 1.00132.40 C ANISOU 1850 C PHE A1065 15283 20054 14969 -988 -608 -907 C ATOM 1851 O PHE A1065 39.816 1.597 -42.278 1.00131.30 O ANISOU 1851 O PHE A1065 15235 19767 14888 -976 -610 -1005 O ATOM 1852 CB PHE A1065 39.303 1.358 -39.053 1.00131.81 C ANISOU 1852 CB PHE A1065 15105 20169 14808 -909 -582 -846 C ATOM 1853 N ASP A1066 37.703 0.877 -41.797 1.00128.99 N ANISOU 1853 N ASP A1066 14804 19688 14519 -1096 -651 -782 N ATOM 1854 CA ASP A1066 37.431 0.064 -42.991 1.00128.64 C ANISOU 1854 CA ASP A1066 14825 19532 14518 -1230 -711 -765 C ATOM 1855 C ASP A1066 37.691 0.815 -44.310 1.00130.43 C ANISOU 1855 C ASP A1066 15098 19693 14767 -1196 -688 -877 C ATOM 1856 O ASP A1066 38.140 0.185 -45.270 1.00129.82 O ANISOU 1856 O ASP A1066 15116 19476 14733 -1262 -728 -934 O ATOM 1857 CB ASP A1066 35.986 -0.452 -42.970 1.00131.71 C ANISOU 1857 CB ASP A1066 15123 20069 14852 -1361 -759 -600 C ATOM 1858 CG ASP A1066 35.812 -1.812 -43.613 1.00143.32 C ANISOU 1858 CG ASP A1066 16681 21403 16370 -1549 -852 -555 C ATOM 1859 OD1 ASP A1066 35.719 -1.874 -44.858 1.00143.62 O ANISOU 1859 OD1 ASP A1066 16786 21361 16422 -1615 -876 -626 O ATOM 1860 OD2 ASP A1066 35.752 -2.814 -42.870 1.00150.92 O ANISOU 1860 OD2 ASP A1066 17648 22341 17355 -1635 -903 -446 O ATOM 1861 N ILE A1067 37.422 2.145 -44.355 1.00125.76 N ANISOU 1861 N ILE A1067 14442 19198 14142 -1086 -624 -906 N ATOM 1862 CA ILE A1067 37.661 2.985 -45.538 1.00124.59 C ANISOU 1862 CA ILE A1067 14315 19004 14020 -1044 -597 -984 C ATOM 1863 C ILE A1067 39.175 3.074 -45.788 1.00126.94 C ANISOU 1863 C ILE A1067 14711 19141 14379 -994 -595 -1111 C ATOM 1864 O ILE A1067 39.631 2.723 -46.877 1.00126.15 O ANISOU 1864 O ILE A1067 14668 18955 14308 -1034 -622 -1160 O ATOM 1865 CB ILE A1067 37.010 4.402 -45.419 1.00127.68 C ANISOU 1865 CB ILE A1067 14622 19515 14375 -923 -524 -965 C ATOM 1866 CG1 ILE A1067 35.466 4.319 -45.410 1.00129.02 C ANISOU 1866 CG1 ILE A1067 14671 19886 14463 -959 -520 -812 C ATOM 1867 CG2 ILE A1067 37.512 5.352 -46.533 1.00127.83 C ANISOU 1867 CG2 ILE A1067 14667 19460 14444 -870 -495 -1037 C ATOM 1868 CD1 ILE A1067 34.738 5.668 -45.242 1.00135.96 C ANISOU 1868 CD1 ILE A1067 15467 20892 15300 -802 -432 -775 C ATOM 1869 N LEU A1068 39.937 3.524 -44.770 1.00122.87 N ANISOU 1869 N LEU A1068 14207 18613 13866 -909 -564 -1158 N ATOM 1870 CA LEU A1068 41.388 3.704 -44.827 1.00121.93 C ANISOU 1870 CA LEU A1068 14155 18390 13785 -863 -560 -1252 C ATOM 1871 C LEU A1068 42.130 2.372 -45.007 1.00125.05 C ANISOU 1871 C LEU A1068 14620 18686 14205 -910 -603 -1253 C ATOM 1872 O LEU A1068 43.086 2.336 -45.780 1.00124.33 O ANISOU 1872 O LEU A1068 14582 18519 14139 -886 -609 -1314 O ATOM 1873 CB LEU A1068 41.898 4.444 -43.579 1.00122.07 C ANISOU 1873 CB LEU A1068 14157 18450 13775 -790 -526 -1291 C ATOM 1874 CG LEU A1068 41.764 5.975 -43.609 1.00126.74 C ANISOU 1874 CG LEU A1068 14737 19053 14366 -715 -480 -1350 C ATOM 1875 CD1 LEU A1068 40.438 6.433 -43.011 1.00127.58 C ANISOU 1875 CD1 LEU A1068 14779 19278 14418 -664 -441 -1302 C ATOM 1876 CD2 LEU A1068 42.912 6.637 -42.870 1.00128.92 C ANISOU 1876 CD2 LEU A1068 15052 19297 14636 -682 -472 -1438 C ATOM 1877 N VAL A1069 41.676 1.283 -44.337 1.00121.52 N ANISOU 1877 N VAL A1069 14175 18245 13753 -969 -632 -1174 N ATOM 1878 CA VAL A1069 42.269 -0.065 -44.443 1.00121.47 C ANISOU 1878 CA VAL A1069 14255 18115 13784 -1004 -670 -1161 C ATOM 1879 C VAL A1069 42.089 -0.585 -45.892 1.00124.97 C ANISOU 1879 C VAL A1069 14776 18458 14248 -1063 -706 -1208 C ATOM 1880 O VAL A1069 43.027 -1.152 -46.459 1.00124.60 O ANISOU 1880 O VAL A1069 14820 18298 14226 -1024 -713 -1270 O ATOM 1881 CB VAL A1069 41.699 -1.040 -43.367 1.00126.20 C ANISOU 1881 CB VAL A1069 14829 18739 14382 -1067 -698 -1038 C ATOM 1882 CG1 VAL A1069 41.983 -2.505 -43.702 1.00126.89 C ANISOU 1882 CG1 VAL A1069 15030 18654 14528 -1123 -746 -1012 C ATOM 1883 CG2 VAL A1069 42.248 -0.702 -41.984 1.00125.90 C ANISOU 1883 CG2 VAL A1069 14719 18805 14310 -992 -662 -1008 C ATOM 1884 N GLY A1070 40.912 -0.338 -46.472 1.00121.24 N ANISOU 1884 N GLY A1070 14258 18056 13750 -1146 -724 -1177 N ATOM 1885 CA GLY A1070 40.595 -0.702 -47.849 1.00121.14 C ANISOU 1885 CA GLY A1070 14297 17999 13732 -1223 -761 -1223 C ATOM 1886 C GLY A1070 41.366 0.128 -48.861 1.00123.18 C ANISOU 1886 C GLY A1070 14556 18262 13987 -1136 -730 -1319 C ATOM 1887 O GLY A1070 41.786 -0.397 -49.898 1.00122.91 O ANISOU 1887 O GLY A1070 14597 18156 13948 -1147 -754 -1394 O ATOM 1888 N GLN A1071 41.570 1.435 -48.552 1.00118.03 N ANISOU 1888 N GLN A1071 13821 17693 13333 -1048 -677 -1316 N ATOM 1889 CA GLN A1071 42.312 2.391 -49.382 1.00116.72 C ANISOU 1889 CA GLN A1071 13634 17543 13172 -973 -651 -1374 C ATOM 1890 C GLN A1071 43.800 2.054 -49.414 1.00120.34 C ANISOU 1890 C GLN A1071 14159 17922 13644 -899 -651 -1436 C ATOM 1891 O GLN A1071 44.436 2.249 -50.450 1.00119.88 O ANISOU 1891 O GLN A1071 14106 17871 13574 -863 -653 -1482 O ATOM 1892 CB GLN A1071 42.110 3.831 -48.895 1.00117.32 C ANISOU 1892 CB GLN A1071 13628 17691 13256 -911 -602 -1348 C ATOM 1893 CG GLN A1071 40.867 4.498 -49.470 1.00129.96 C ANISOU 1893 CG GLN A1071 15145 19396 14839 -935 -584 -1285 C ATOM 1894 CD GLN A1071 40.754 5.957 -49.096 1.00147.12 C ANISOU 1894 CD GLN A1071 17265 21601 17033 -845 -528 -1268 C ATOM 1895 OE1 GLN A1071 40.820 6.337 -47.921 1.00143.45 O ANISOU 1895 OE1 GLN A1071 16812 21125 16569 -796 -504 -1281 O ATOM 1896 NE2 GLN A1071 40.532 6.807 -50.087 1.00137.67 N ANISOU 1896 NE2 GLN A1071 16012 20446 15851 -821 -505 -1238 N ATOM 1897 N ILE A1072 44.350 1.547 -48.289 1.00116.83 N ANISOU 1897 N ILE A1072 13747 17433 13209 -870 -646 -1420 N ATOM 1898 CA ILE A1072 45.751 1.127 -48.170 1.00116.62 C ANISOU 1898 CA ILE A1072 13769 17360 13182 -789 -639 -1447 C ATOM 1899 C ILE A1072 45.934 -0.183 -48.970 1.00121.43 C ANISOU 1899 C ILE A1072 14483 17864 13791 -786 -666 -1486 C ATOM 1900 O ILE A1072 46.913 -0.310 -49.706 1.00120.86 O ANISOU 1900 O ILE A1072 14441 17785 13696 -703 -659 -1533 O ATOM 1901 CB ILE A1072 46.182 1.009 -46.669 1.00119.72 C ANISOU 1901 CB ILE A1072 14144 17769 13575 -764 -622 -1398 C ATOM 1902 CG1 ILE A1072 46.292 2.400 -45.970 1.00119.55 C ANISOU 1902 CG1 ILE A1072 14044 17843 13538 -753 -596 -1402 C ATOM 1903 CG2 ILE A1072 47.450 0.158 -46.453 1.00120.77 C ANISOU 1903 CG2 ILE A1072 14327 17860 13701 -685 -615 -1388 C ATOM 1904 CD1 ILE A1072 47.282 3.467 -46.577 1.00126.60 C ANISOU 1904 CD1 ILE A1072 14910 18769 14423 -714 -588 -1441 C ATOM 1905 N ASP A1073 44.969 -1.121 -48.856 1.00119.17 N ANISOU 1905 N ASP A1073 14255 17502 13523 -879 -701 -1465 N ATOM 1906 CA ASP A1073 44.962 -2.402 -49.572 1.00120.26 C ANISOU 1906 CA ASP A1073 14525 17501 13666 -903 -737 -1518 C ATOM 1907 C ASP A1073 44.866 -2.184 -51.093 1.00124.12 C ANISOU 1907 C ASP A1073 15027 18024 14109 -912 -751 -1611 C ATOM 1908 O ASP A1073 45.538 -2.888 -51.850 1.00124.40 O ANISOU 1908 O ASP A1073 15165 17979 14123 -846 -756 -1696 O ATOM 1909 CB ASP A1073 43.805 -3.287 -49.084 1.00123.08 C ANISOU 1909 CB ASP A1073 14927 17782 14054 -1047 -786 -1456 C ATOM 1910 N ASP A1074 44.050 -1.196 -51.526 1.00119.97 N ANISOU 1910 N ASP A1074 14392 17633 13560 -977 -750 -1589 N ATOM 1911 CA ASP A1074 43.870 -0.836 -52.936 1.00119.87 C ANISOU 1911 CA ASP A1074 14347 17703 13494 -994 -760 -1649 C ATOM 1912 C ASP A1074 45.145 -0.192 -53.491 1.00122.83 C ANISOU 1912 C ASP A1074 14682 18142 13846 -853 -725 -1684 C ATOM 1913 O ASP A1074 45.514 -0.464 -54.635 1.00122.88 O ANISOU 1913 O ASP A1074 14712 18179 13796 -818 -735 -1758 O ATOM 1914 CB ASP A1074 42.669 0.104 -53.114 1.00121.28 C ANISOU 1914 CB ASP A1074 14398 18025 13659 -1084 -758 -1575 C ATOM 1915 N ALA A1075 45.821 0.644 -52.673 1.00118.34 N ANISOU 1915 N ALA A1075 14046 17609 13308 -782 -689 -1627 N ATOM 1916 CA ALA A1075 47.072 1.313 -53.039 1.00117.78 C ANISOU 1916 CA ALA A1075 13922 17616 13215 -673 -666 -1627 C ATOM 1917 C ALA A1075 48.260 0.339 -52.986 1.00122.31 C ANISOU 1917 C ALA A1075 14582 18131 13758 -559 -658 -1665 C ATOM 1918 O ALA A1075 49.254 0.567 -53.679 1.00122.18 O ANISOU 1918 O ALA A1075 14532 18202 13689 -462 -648 -1677 O ATOM 1919 CB ALA A1075 47.323 2.505 -52.131 1.00117.66 C ANISOU 1919 CB ALA A1075 13822 17645 13237 -669 -643 -1558 C ATOM 1920 N LEU A1076 48.152 -0.746 -52.180 1.00119.14 N ANISOU 1920 N LEU A1076 14285 17595 13388 -559 -661 -1666 N ATOM 1921 CA LEU A1076 49.183 -1.788 -52.082 1.00119.71 C ANISOU 1921 CA LEU A1076 14454 17587 13441 -431 -644 -1687 C ATOM 1922 C LEU A1076 49.088 -2.717 -53.294 1.00123.61 C ANISOU 1922 C LEU A1076 15068 18005 13892 -398 -662 -1802 C ATOM 1923 O LEU A1076 50.110 -3.236 -53.742 1.00124.13 O ANISOU 1923 O LEU A1076 15190 18067 13908 -243 -637 -1841 O ATOM 1924 CB LEU A1076 49.066 -2.584 -50.769 1.00120.28 C ANISOU 1924 CB LEU A1076 14591 17539 13573 -446 -640 -1627 C ATOM 1925 CG LEU A1076 50.311 -3.375 -50.339 1.00125.99 C ANISOU 1925 CG LEU A1076 15368 18219 14283 -287 -602 -1593 C ATOM 1926 CD1 LEU A1076 51.241 -2.525 -49.483 1.00125.33 C ANISOU 1926 CD1 LEU A1076 15150 18299 14169 -234 -570 -1500 C ATOM 1927 CD2 LEU A1076 49.923 -4.627 -49.584 1.00129.68 C ANISOU 1927 CD2 LEU A1076 15947 18506 14818 -309 -610 -1554 C ATOM 1928 N LYS A1077 47.862 -2.900 -53.834 1.00119.46 N ANISOU 1928 N LYS A1077 14577 17439 13372 -541 -706 -1854 N ATOM 1929 CA LYS A1077 47.571 -3.694 -55.033 1.00120.21 C ANISOU 1929 CA LYS A1077 14787 17476 13413 -556 -737 -1983 C ATOM 1930 C LYS A1077 48.323 -3.089 -56.233 1.00123.02 C ANISOU 1930 C LYS A1077 15061 18012 13671 -443 -716 -2033 C ATOM 1931 O LYS A1077 48.884 -3.830 -57.043 1.00123.95 O ANISOU 1931 O LYS A1077 15279 18099 13717 -332 -712 -2143 O ATOM 1932 CB LYS A1077 46.045 -3.741 -55.282 1.00122.86 C ANISOU 1932 CB LYS A1077 15123 17802 13758 -771 -793 -1992 C ATOM 1933 CG LYS A1077 45.598 -4.458 -56.561 1.00138.77 C ANISOU 1933 CG LYS A1077 17242 19788 15697 -836 -838 -2134 C ATOM 1934 CD LYS A1077 45.310 -5.941 -56.354 1.00150.06 C ANISOU 1934 CD LYS A1077 18898 20956 17161 -895 -883 -2214 C ATOM 1935 CE LYS A1077 44.809 -6.583 -57.625 1.00161.30 C ANISOU 1935 CE LYS A1077 20437 22353 18497 -986 -938 -2376 C ATOM 1936 NZ LYS A1077 44.525 -8.030 -57.441 1.00171.76 N ANISOU 1936 NZ LYS A1077 22011 23383 19866 -1061 -992 -2463 N ATOM 1937 N LEU A1078 48.363 -1.741 -56.308 1.00117.47 N ANISOU 1937 N LEU A1078 14175 17494 12963 -462 -702 -1945 N ATOM 1938 CA LEU A1078 49.064 -0.983 -57.348 1.00116.88 C ANISOU 1938 CA LEU A1078 13980 17622 12807 -373 -688 -1942 C ATOM 1939 C LEU A1078 50.578 -1.105 -57.166 1.00120.70 C ANISOU 1939 C LEU A1078 14456 18153 13250 -185 -650 -1913 C ATOM 1940 O LEU A1078 51.304 -1.169 -58.159 1.00120.87 O ANISOU 1940 O LEU A1078 14447 18308 13171 -63 -639 -1950 O ATOM 1941 CB LEU A1078 48.636 0.498 -57.337 1.00115.54 C ANISOU 1941 CB LEU A1078 13631 17597 12672 -460 -687 -1831 C ATOM 1942 CG LEU A1078 47.170 0.807 -57.686 1.00119.93 C ANISOU 1942 CG LEU A1078 14147 18176 13244 -619 -712 -1825 C ATOM 1943 CD1 LEU A1078 46.777 2.186 -57.203 1.00118.76 C ANISOU 1943 CD1 LEU A1078 13863 18097 13166 -672 -695 -1700 C ATOM 1944 CD2 LEU A1078 46.906 0.681 -59.180 1.00123.42 C ANISOU 1944 CD2 LEU A1078 14552 18758 13584 -634 -732 -1892 C ATOM 1945 N ALA A1079 51.043 -1.152 -55.896 1.00116.79 N ANISOU 1945 N ALA A1079 13977 17580 12818 -159 -629 -1835 N ATOM 1946 CA ALA A1079 52.454 -1.306 -55.527 1.00116.86 C ANISOU 1946 CA ALA A1079 13965 17652 12784 7 -591 -1776 C ATOM 1947 C ALA A1079 52.951 -2.721 -55.853 1.00122.49 C ANISOU 1947 C ALA A1079 14841 18254 13447 170 -566 -1867 C ATOM 1948 O ALA A1079 54.106 -2.878 -56.256 1.00122.92 O ANISOU 1948 O ALA A1079 14864 18430 13409 354 -531 -1847 O ATOM 1949 CB ALA A1079 52.652 -1.003 -54.050 1.00116.73 C ANISOU 1949 CB ALA A1079 13917 17597 12840 -37 -579 -1671 C ATOM 1950 N ASN A1080 52.069 -3.743 -55.694 1.00119.70 N ANISOU 1950 N ASN A1080 14661 17670 13151 104 -586 -1959 N ATOM 1951 CA ASN A1080 52.351 -5.149 -56.017 1.00121.31 C ANISOU 1951 CA ASN A1080 15065 17697 13329 239 -571 -2068 C ATOM 1952 C ASN A1080 52.473 -5.319 -57.536 1.00125.87 C ANISOU 1952 C ASN A1080 15676 18364 13785 321 -577 -2212 C ATOM 1953 O ASN A1080 53.319 -6.083 -58.004 1.00127.22 O ANISOU 1953 O ASN A1080 15948 18511 13877 534 -538 -2283 O ATOM 1954 CB ASN A1080 51.258 -6.079 -55.461 1.00122.63 C ANISOU 1954 CB ASN A1080 15404 17588 13601 94 -610 -2115 C ATOM 1955 CG ASN A1080 51.224 -6.230 -53.954 1.00144.79 C ANISOU 1955 CG ASN A1080 18201 20298 16514 53 -598 -1978 C ATOM 1956 OD1 ASN A1080 50.159 -6.168 -53.330 1.00137.52 O ANISOU 1956 OD1 ASN A1080 17276 19303 15673 -136 -640 -1939 O ATOM 1957 ND2 ASN A1080 52.370 -6.490 -53.332 1.00137.75 N ANISOU 1957 ND2 ASN A1080 17298 19427 15613 235 -541 -1891 N ATOM 1958 N GLU A1081 51.626 -4.584 -58.293 1.00121.09 N ANISOU 1958 N GLU A1081 14975 17879 13153 165 -620 -2246 N ATOM 1959 CA GLU A1081 51.575 -4.543 -59.759 1.00121.51 C ANISOU 1959 CA GLU A1081 15012 18078 13078 201 -634 -2366 C ATOM 1960 C GLU A1081 52.869 -3.933 -60.328 1.00124.29 C ANISOU 1960 C GLU A1081 15207 18704 13315 402 -590 -2299 C ATOM 1961 O GLU A1081 53.349 -4.371 -61.378 1.00125.31 O ANISOU 1961 O GLU A1081 15372 18931 13309 556 -575 -2409 O ATOM 1962 CB GLU A1081 50.348 -3.720 -60.205 1.00121.91 C ANISOU 1962 CB GLU A1081 14947 18231 13143 -29 -685 -2353 C ATOM 1963 CG GLU A1081 50.072 -3.715 -61.701 1.00133.52 C ANISOU 1963 CG GLU A1081 16391 19862 14477 -37 -708 -2475 C ATOM 1964 CD GLU A1081 49.156 -2.596 -62.156 1.00151.13 C ANISOU 1964 CD GLU A1081 18428 22288 16707 -213 -737 -2392 C ATOM 1965 OE1 GLU A1081 49.671 -1.590 -62.694 1.00140.48 O ANISOU 1965 OE1 GLU A1081 16883 21189 15302 -149 -720 -2299 O ATOM 1966 OE2 GLU A1081 47.923 -2.722 -61.973 1.00145.43 O ANISOU 1966 OE2 GLU A1081 17742 21476 16039 -413 -778 -2400 O ATOM 1967 N GLY A1082 53.406 -2.937 -59.621 1.00118.46 N ANISOU 1967 N GLY A1082 14296 18093 12619 393 -575 -2120 N ATOM 1968 CA GLY A1082 54.620 -2.221 -59.996 1.00117.72 C ANISOU 1968 CA GLY A1082 14025 18276 12428 536 -548 -2006 C ATOM 1969 C GLY A1082 54.380 -0.771 -60.370 1.00119.03 C ANISOU 1969 C GLY A1082 13972 18651 12605 399 -580 -1889 C ATOM 1970 O GLY A1082 55.339 -0.026 -60.590 1.00118.40 O ANISOU 1970 O GLY A1082 13723 18802 12462 471 -573 -1759 O ATOM 1971 N LYS A1083 53.094 -0.361 -60.448 1.00113.86 N ANISOU 1971 N LYS A1083 13313 17921 12028 200 -617 -1917 N ATOM 1972 CA LYS A1083 52.677 0.999 -60.797 1.00112.11 C ANISOU 1972 CA LYS A1083 12903 17857 11838 70 -642 -1804 C ATOM 1973 C LYS A1083 52.963 1.955 -59.632 1.00113.40 C ANISOU 1973 C LYS A1083 12991 17986 12111 -2 -641 -1655 C ATOM 1974 O LYS A1083 52.171 2.054 -58.690 1.00112.25 O ANISOU 1974 O LYS A1083 12911 17663 12074 -117 -645 -1658 O ATOM 1975 CB LYS A1083 51.193 1.025 -61.194 1.00114.47 C ANISOU 1975 CB LYS A1083 13227 18093 12173 -96 -670 -1872 C ATOM 1976 N VAL A1084 54.122 2.635 -59.694 1.00108.75 N ANISOU 1976 N VAL A1084 12263 17579 11477 65 -638 -1527 N ATOM 1977 CA VAL A1084 54.584 3.570 -58.666 1.00106.97 C ANISOU 1977 CA VAL A1084 11968 17345 11332 -10 -647 -1393 C ATOM 1978 C VAL A1084 53.759 4.866 -58.676 1.00108.07 C ANISOU 1978 C VAL A1084 12018 17469 11573 -176 -674 -1323 C ATOM 1979 O VAL A1084 53.324 5.296 -57.609 1.00106.90 O ANISOU 1979 O VAL A1084 11915 17173 11530 -274 -676 -1309 O ATOM 1980 CB VAL A1084 56.108 3.872 -58.727 1.00111.56 C ANISOU 1980 CB VAL A1084 12428 18139 11822 92 -647 -1262 C ATOM 1981 CG1 VAL A1084 56.911 2.779 -58.031 1.00112.01 C ANISOU 1981 CG1 VAL A1084 12583 18154 11824 237 -609 -1289 C ATOM 1982 CG2 VAL A1084 56.602 4.090 -60.159 1.00112.35 C ANISOU 1982 CG2 VAL A1084 12385 18505 11797 181 -657 -1214 C ATOM 1983 N LYS A1085 53.533 5.471 -59.866 1.00103.41 N ANISOU 1983 N LYS A1085 11304 17039 10950 -192 -690 -1276 N ATOM 1984 CA LYS A1085 52.780 6.721 -60.035 1.00101.89 C ANISOU 1984 CA LYS A1085 11016 16844 10854 -320 -706 -1185 C ATOM 1985 C LYS A1085 51.319 6.567 -59.579 1.00103.16 C ANISOU 1985 C LYS A1085 11275 16821 11100 -410 -692 -1267 C ATOM 1986 O LYS A1085 50.792 7.476 -58.935 1.00101.71 O ANISOU 1986 O LYS A1085 11080 16539 11024 -497 -690 -1207 O ATOM 1987 CB LYS A1085 52.842 7.199 -61.497 1.00104.99 C ANISOU 1987 CB LYS A1085 11240 17477 11174 -298 -721 -1104 C ATOM 1988 CG LYS A1085 52.539 8.687 -61.674 1.00118.01 C ANISOU 1988 CG LYS A1085 12756 19156 12928 -405 -740 -941 C ATOM 1989 CD LYS A1085 52.941 9.211 -63.052 1.00128.53 C ANISOU 1989 CD LYS A1085 13887 20768 14182 -375 -760 -812 C ATOM 1990 CE LYS A1085 54.294 9.890 -63.041 1.00140.01 C ANISOU 1990 CE LYS A1085 15220 22361 15615 -367 -797 -648 C ATOM 1991 NZ LYS A1085 54.654 10.436 -64.376 1.00149.13 N ANISOU 1991 NZ LYS A1085 16156 23815 16693 -343 -821 -494 N ATOM 1992 N GLU A1086 50.686 5.416 -59.897 1.00 99.15 N ANISOU 1992 N GLU A1086 10868 16269 10535 -387 -684 -1400 N ATOM 1993 CA GLU A1086 49.298 5.089 -59.542 1.00 98.23 C ANISOU 1993 CA GLU A1086 10835 16016 10472 -482 -679 -1465 C ATOM 1994 C GLU A1086 49.117 4.941 -58.020 1.00 99.99 C ANISOU 1994 C GLU A1086 11167 16039 10785 -518 -669 -1479 C ATOM 1995 O GLU A1086 48.084 5.354 -57.494 1.00 99.08 O ANISOU 1995 O GLU A1086 11057 15847 10741 -602 -662 -1456 O ATOM 1996 CB GLU A1086 48.841 3.805 -60.249 1.00100.63 C ANISOU 1996 CB GLU A1086 11234 16319 10682 -469 -689 -1606 C ATOM 1997 CG GLU A1086 48.759 3.907 -61.766 1.00114.30 C ANISOU 1997 CG GLU A1086 12854 18269 12304 -454 -700 -1614 C ATOM 1998 CD GLU A1086 47.478 4.484 -62.341 1.00141.35 C ANISOU 1998 CD GLU A1086 16178 21783 15743 -575 -706 -1557 C ATOM 1999 OE1 GLU A1086 46.387 4.177 -61.807 1.00139.77 O ANISOU 1999 OE1 GLU A1086 16052 21463 15590 -678 -709 -1585 O ATOM 2000 OE2 GLU A1086 47.564 5.192 -63.371 1.00137.77 O ANISOU 2000 OE2 GLU A1086 15560 21546 15242 -564 -706 -1471 O ATOM 2001 N ALA A1087 50.117 4.352 -57.323 1.00 95.38 N ANISOU 2001 N ALA A1087 10656 15401 10184 -443 -664 -1504 N ATOM 2002 CA ALA A1087 50.110 4.164 -55.867 1.00 94.07 C ANISOU 2002 CA ALA A1087 10573 15087 10083 -466 -654 -1506 C ATOM 2003 C ALA A1087 50.294 5.504 -55.145 1.00 95.76 C ANISOU 2003 C ALA A1087 10714 15304 10368 -522 -654 -1415 C ATOM 2004 O ALA A1087 49.615 5.756 -54.148 1.00 94.69 O ANISOU 2004 O ALA A1087 10619 15062 10295 -581 -644 -1421 O ATOM 2005 CB ALA A1087 51.201 3.186 -55.454 1.00 95.29 C ANISOU 2005 CB ALA A1087 10800 15221 10186 -357 -643 -1533 C ATOM 2006 N GLN A1088 51.191 6.368 -55.671 1.00 91.59 N ANISOU 2006 N GLN A1088 10078 14900 9822 -507 -668 -1332 N ATOM 2007 CA GLN A1088 51.471 7.713 -55.154 1.00 90.80 C ANISOU 2007 CA GLN A1088 9921 14789 9791 -576 -681 -1246 C ATOM 2008 C GLN A1088 50.246 8.622 -55.302 1.00 93.95 C ANISOU 2008 C GLN A1088 10298 15121 10277 -642 -670 -1225 C ATOM 2009 O GLN A1088 50.026 9.491 -54.455 1.00 93.56 O ANISOU 2009 O GLN A1088 10276 14972 10302 -693 -665 -1211 O ATOM 2010 CB GLN A1088 52.672 8.340 -55.882 1.00 92.53 C ANISOU 2010 CB GLN A1088 10020 15171 9966 -560 -711 -1138 C ATOM 2011 CG GLN A1088 54.025 7.739 -55.516 1.00104.30 C ANISOU 2011 CG GLN A1088 11506 16754 11368 -495 -719 -1117 C ATOM 2012 CD GLN A1088 55.149 8.304 -56.353 1.00120.40 C ANISOU 2012 CD GLN A1088 13402 19004 13339 -476 -752 -987 C ATOM 2013 OE1 GLN A1088 55.070 8.391 -57.586 1.00114.65 O ANISOU 2013 OE1 GLN A1088 12584 18408 12570 -434 -757 -951 O ATOM 2014 NE2 GLN A1088 56.240 8.671 -55.700 1.00112.40 N ANISOU 2014 NE2 GLN A1088 12349 18061 12297 -511 -779 -903 N ATOM 2015 N ALA A1089 49.461 8.423 -56.386 1.00 89.84 N ANISOU 2015 N ALA A1089 9729 14671 9735 -634 -662 -1223 N ATOM 2016 CA ALA A1089 48.241 9.177 -56.672 1.00 89.42 C ANISOU 2016 CA ALA A1089 9632 14597 9745 -676 -642 -1178 C ATOM 2017 C ALA A1089 47.139 8.804 -55.686 1.00 93.18 C ANISOU 2017 C ALA A1089 10201 14952 10251 -701 -616 -1240 C ATOM 2018 O ALA A1089 46.438 9.693 -55.203 1.00 92.60 O ANISOU 2018 O ALA A1089 10121 14815 10248 -717 -590 -1200 O ATOM 2019 CB ALA A1089 47.783 8.916 -58.099 1.00 90.49 C ANISOU 2019 CB ALA A1089 9673 14889 9818 -667 -643 -1152 C ATOM 2020 N ALA A1090 47.011 7.493 -55.370 1.00 90.15 N ANISOU 2020 N ALA A1090 9904 14536 9814 -697 -622 -1330 N ATOM 2021 CA ALA A1090 46.025 6.942 -54.433 1.00 90.01 C ANISOU 2021 CA ALA A1090 9961 14428 9810 -731 -609 -1371 C ATOM 2022 C ALA A1090 46.279 7.426 -53.002 1.00 94.54 C ANISOU 2022 C ALA A1090 10583 14906 10433 -726 -595 -1375 C ATOM 2023 O ALA A1090 45.323 7.628 -52.253 1.00 94.07 O ANISOU 2023 O ALA A1090 10539 14805 10397 -743 -573 -1371 O ATOM 2024 CB ALA A1090 46.047 5.422 -54.481 1.00 90.88 C ANISOU 2024 CB ALA A1090 10159 14510 9862 -736 -630 -1450 C ATOM 2025 N ALA A1091 47.563 7.626 -52.638 1.00 91.75 N ANISOU 2025 N ALA A1091 10238 14545 10077 -703 -609 -1378 N ATOM 2026 CA ALA A1091 47.983 8.101 -51.321 1.00 91.89 C ANISOU 2026 CA ALA A1091 10296 14500 10119 -714 -605 -1391 C ATOM 2027 C ALA A1091 47.724 9.606 -51.151 1.00 97.69 C ANISOU 2027 C ALA A1091 11008 15188 10922 -736 -594 -1360 C ATOM 2028 O ALA A1091 47.404 10.034 -50.043 1.00 97.75 O ANISOU 2028 O ALA A1091 11065 15127 10949 -742 -577 -1396 O ATOM 2029 CB ALA A1091 49.454 7.794 -51.097 1.00 92.60 C ANISOU 2029 CB ALA A1091 10386 14634 10165 -698 -629 -1386 C ATOM 2030 N GLU A1092 47.867 10.406 -52.232 1.00 95.65 N ANISOU 2030 N GLU A1092 10680 14965 10698 -740 -603 -1291 N ATOM 2031 CA GLU A1092 47.639 11.858 -52.197 1.00 96.65 C ANISOU 2031 CA GLU A1092 10798 15017 10909 -754 -592 -1245 C ATOM 2032 C GLU A1092 46.142 12.183 -52.144 1.00102.11 C ANISOU 2032 C GLU A1092 11490 15673 11636 -713 -540 -1235 C ATOM 2033 O GLU A1092 45.760 13.232 -51.619 1.00102.25 O ANISOU 2033 O GLU A1092 11547 15588 11717 -692 -513 -1233 O ATOM 2034 CB GLU A1092 48.300 12.553 -53.390 1.00 98.47 C ANISOU 2034 CB GLU A1092 10937 15309 11168 -773 -621 -1142 C ATOM 2035 CG GLU A1092 49.732 12.961 -53.102 1.00110.13 C ANISOU 2035 CG GLU A1092 12415 16793 12638 -831 -674 -1120 C ATOM 2036 N GLN A1093 45.304 11.274 -52.674 1.00 99.39 N ANISOU 2036 N GLN A1093 11106 15418 11240 -701 -526 -1226 N ATOM 2037 CA GLN A1093 43.843 11.377 -52.661 1.00 99.85 C ANISOU 2037 CA GLN A1093 11138 15500 11300 -672 -480 -1191 C ATOM 2038 C GLN A1093 43.304 10.877 -51.306 1.00104.82 C ANISOU 2038 C GLN A1093 11840 16088 11900 -661 -462 -1257 C ATOM 2039 O GLN A1093 42.169 11.184 -50.938 1.00104.95 O ANISOU 2039 O GLN A1093 11840 16122 11915 -618 -418 -1224 O ATOM 2040 CB GLN A1093 43.235 10.590 -53.835 1.00101.05 C ANISOU 2040 CB GLN A1093 11210 15791 11392 -700 -489 -1149 C ATOM 2041 CG GLN A1093 43.474 11.252 -55.195 1.00113.58 C ANISOU 2041 CG GLN A1093 12688 17466 12999 -695 -490 -1054 C ATOM 2042 CD GLN A1093 43.329 10.312 -56.373 1.00126.82 C ANISOU 2042 CD GLN A1093 14300 19298 14589 -735 -517 -1054 C ATOM 2043 OE1 GLN A1093 42.513 9.379 -56.377 1.00121.53 O ANISOU 2043 OE1 GLN A1093 13642 18680 13853 -777 -522 -1086 O ATOM 2044 NE2 GLN A1093 44.093 10.569 -57.425 1.00115.62 N ANISOU 2044 NE2 GLN A1093 12807 17967 13158 -730 -540 -1014 N ATOM 2045 N LEU A1094 44.145 10.127 -50.563 1.00101.71 N ANISOU 2045 N LEU A1094 11509 15664 11474 -689 -494 -1331 N ATOM 2046 CA LEU A1094 43.889 9.585 -49.227 1.00101.95 C ANISOU 2046 CA LEU A1094 11593 15676 11469 -685 -486 -1383 C ATOM 2047 C LEU A1094 44.094 10.694 -48.164 1.00107.06 C ANISOU 2047 C LEU A1094 12290 16246 12143 -649 -462 -1430 C ATOM 2048 O LEU A1094 43.584 10.570 -47.047 1.00107.13 O ANISOU 2048 O LEU A1094 12322 16266 12115 -621 -439 -1464 O ATOM 2049 CB LEU A1094 44.840 8.386 -48.997 1.00101.68 C ANISOU 2049 CB LEU A1094 11594 15647 11393 -720 -526 -1422 C ATOM 2050 CG LEU A1094 44.800 7.630 -47.671 1.00106.57 C ANISOU 2050 CG LEU A1094 12252 16266 11973 -725 -525 -1451 C ATOM 2051 CD1 LEU A1094 44.875 6.142 -47.904 1.00106.70 C ANISOU 2051 CD1 LEU A1094 12289 16291 11962 -754 -553 -1441 C ATOM 2052 CD2 LEU A1094 45.948 8.058 -46.764 1.00109.14 C ANISOU 2052 CD2 LEU A1094 12609 16571 12290 -723 -533 -1496 C ATOM 2053 N LYS A1095 44.826 11.779 -48.523 1.00103.96 N ANISOU 2053 N LYS A1095 11912 15780 11809 -656 -473 -1431 N ATOM 2054 CA LYS A1095 45.108 12.924 -47.648 1.00104.53 C ANISOU 2054 CA LYS A1095 12058 15745 11914 -644 -463 -1493 C ATOM 2055 C LYS A1095 43.829 13.691 -47.274 1.00109.89 C ANISOU 2055 C LYS A1095 12758 16382 12613 -545 -397 -1494 C ATOM 2056 O LYS A1095 43.775 14.274 -46.192 1.00110.23 O ANISOU 2056 O LYS A1095 12879 16359 12644 -510 -377 -1582 O ATOM 2057 CB LYS A1095 46.129 13.878 -48.287 1.00107.10 C ANISOU 2057 CB LYS A1095 12392 15993 12307 -698 -501 -1465 C ATOM 2058 CG LYS A1095 47.574 13.400 -48.156 1.00117.43 C ANISOU 2058 CG LYS A1095 13696 17350 13572 -785 -564 -1479 C ATOM 2059 CD LYS A1095 48.583 14.540 -48.294 1.00126.06 C ANISOU 2059 CD LYS A1095 14814 18365 14720 -865 -611 -1460 C ATOM 2060 CE LYS A1095 49.164 14.660 -49.682 1.00133.15 C ANISOU 2060 CE LYS A1095 15617 19325 15650 -893 -644 -1337 C ATOM 2061 NZ LYS A1095 50.224 15.700 -49.740 1.00140.84 N ANISOU 2061 NZ LYS A1095 16603 20241 16670 -997 -705 -1293 N ATOM 2062 N THR A1096 42.805 13.686 -48.153 1.00107.08 N ANISOU 2062 N THR A1096 12327 16086 12273 -494 -360 -1397 N ATOM 2063 CA THR A1096 41.523 14.349 -47.878 1.00108.10 C ANISOU 2063 CA THR A1096 12451 16216 12406 -375 -285 -1365 C ATOM 2064 C THR A1096 40.655 13.467 -46.959 1.00111.62 C ANISOU 2064 C THR A1096 12872 16789 12750 -343 -263 -1379 C ATOM 2065 O THR A1096 39.801 13.991 -46.239 1.00112.14 O ANISOU 2065 O THR A1096 12953 16869 12786 -230 -203 -1389 O ATOM 2066 CB THR A1096 40.782 14.719 -49.175 1.00117.61 C ANISOU 2066 CB THR A1096 13558 17476 13653 -336 -252 -1225 C ATOM 2067 OG1 THR A1096 40.696 13.575 -50.026 1.00118.14 O ANISOU 2067 OG1 THR A1096 13533 17688 13668 -419 -290 -1168 O ATOM 2068 CG2 THR A1096 41.430 15.887 -49.910 1.00116.25 C ANISOU 2068 CG2 THR A1096 13405 17172 13594 -337 -259 -1184 C ATOM 2069 N THR A1097 40.891 12.136 -46.977 1.00106.81 N ANISOU 2069 N THR A1097 12227 16270 12086 -436 -312 -1372 N ATOM 2070 CA THR A1097 40.165 11.158 -46.160 1.00106.31 C ANISOU 2070 CA THR A1097 12130 16328 11935 -439 -309 -1357 C ATOM 2071 C THR A1097 40.690 11.164 -44.714 1.00109.05 C ANISOU 2071 C THR A1097 12542 16654 12240 -424 -313 -1460 C ATOM 2072 O THR A1097 39.884 11.034 -43.792 1.00109.23 O ANISOU 2072 O THR A1097 12537 16775 12190 -364 -281 -1451 O ATOM 2073 CB THR A1097 40.245 9.749 -46.777 1.00115.67 C ANISOU 2073 CB THR A1097 13275 17579 13096 -551 -365 -1310 C ATOM 2074 OG1 THR A1097 40.176 9.835 -48.202 1.00116.16 O ANISOU 2074 OG1 THR A1097 13291 17651 13192 -582 -374 -1252 O ATOM 2075 CG2 THR A1097 39.145 8.823 -46.267 1.00114.98 C ANISOU 2075 CG2 THR A1097 13131 17625 12933 -575 -367 -1239 C ATOM 2076 N ARG A1098 42.025 11.304 -44.514 1.00104.28 N ANISOU 2076 N ARG A1098 12004 15956 11663 -481 -352 -1544 N ATOM 2077 CA ARG A1098 42.634 11.332 -43.176 1.00104.11 C ANISOU 2077 CA ARG A1098 12031 15940 11586 -486 -361 -1641 C ATOM 2078 C ARG A1098 42.302 12.643 -42.443 1.00107.86 C ANISOU 2078 C ARG A1098 12576 16355 12053 -391 -313 -1732 C ATOM 2079 O ARG A1098 42.182 12.631 -41.218 1.00107.78 O ANISOU 2079 O ARG A1098 12581 16413 11959 -356 -298 -1803 O ATOM 2080 CB ARG A1098 44.160 11.084 -43.212 1.00104.23 C ANISOU 2080 CB ARG A1098 12078 15909 11613 -584 -419 -1681 C ATOM 2081 CG ARG A1098 45.009 12.146 -43.913 1.00114.70 C ANISOU 2081 CG ARG A1098 13455 17111 13015 -619 -440 -1708 C ATOM 2082 CD ARG A1098 46.113 12.666 -43.011 1.00122.52 C ANISOU 2082 CD ARG A1098 14506 18072 13974 -686 -476 -1799 C ATOM 2083 NE ARG A1098 47.206 13.278 -43.772 1.00130.77 N ANISOU 2083 NE ARG A1098 15567 19040 15079 -767 -524 -1779 N ATOM 2084 CZ ARG A1098 47.281 14.567 -44.088 1.00146.06 C ANISOU 2084 CZ ARG A1098 17569 20836 17090 -780 -529 -1805 C ATOM 2085 NH1 ARG A1098 46.323 15.406 -43.715 1.00134.88 N ANISOU 2085 NH1 ARG A1098 16226 19325 15699 -693 -478 -1870 N ATOM 2086 NH2 ARG A1098 48.312 15.027 -44.783 1.00133.27 N ANISOU 2086 NH2 ARG A1098 15943 19174 15519 -873 -584 -1756 N ATOM 2087 N ASN A1099 42.137 13.756 -43.194 1.00104.24 N ANISOU 2087 N ASN A1099 12160 15770 11678 -342 -287 -1729 N ATOM 2088 CA ASN A1099 41.775 15.071 -42.660 1.00105.25 C ANISOU 2088 CA ASN A1099 12382 15790 11819 -231 -235 -1817 C ATOM 2089 C ASN A1099 40.362 15.050 -42.078 1.00109.54 C ANISOU 2089 C ASN A1099 12879 16460 12283 -75 -158 -1786 C ATOM 2090 O ASN A1099 40.120 15.678 -41.049 1.00110.59 O ANISOU 2090 O ASN A1099 13083 16579 12356 28 -116 -1896 O ATOM 2091 CB ASN A1099 41.874 16.147 -43.750 1.00105.52 C ANISOU 2091 CB ASN A1099 12459 15652 11980 -213 -225 -1777 C ATOM 2092 CG ASN A1099 43.272 16.628 -44.050 1.00125.60 C ANISOU 2092 CG ASN A1099 15071 18057 14595 -351 -298 -1821 C ATOM 2093 OD1 ASN A1099 44.107 16.824 -43.158 1.00120.21 O ANISOU 2093 OD1 ASN A1099 14467 17334 13874 -425 -339 -1940 O ATOM 2094 ND2 ASN A1099 43.536 16.899 -45.317 1.00116.66 N ANISOU 2094 ND2 ASN A1099 13897 16868 13559 -390 -317 -1714 N ATOM 2095 N ALA A1100 39.442 14.309 -42.734 1.00104.92 N ANISOU 2095 N ALA A1100 12170 16016 11680 -62 -142 -1636 N ATOM 2096 CA ALA A1100 38.042 14.158 -42.339 1.00105.20 C ANISOU 2096 CA ALA A1100 12120 16227 11626 67 -77 -1553 C ATOM 2097 C ALA A1100 37.886 13.401 -41.013 1.00108.58 C ANISOU 2097 C ALA A1100 12510 16819 11925 68 -86 -1589 C ATOM 2098 O ALA A1100 36.937 13.673 -40.277 1.00109.40 O ANISOU 2098 O ALA A1100 12574 17057 11934 212 -23 -1572 O ATOM 2099 CB ALA A1100 37.269 13.441 -43.435 1.00105.18 C ANISOU 2099 CB ALA A1100 11988 16347 11630 20 -83 -1376 C ATOM 2100 N TYR A1101 38.804 12.459 -40.711 1.00103.48 N ANISOU 2100 N TYR A1101 11865 16183 11271 -77 -158 -1621 N ATOM 2101 CA TYR A1101 38.758 11.663 -39.484 1.00103.29 C ANISOU 2101 CA TYR A1101 11788 16323 11134 -93 -173 -1629 C ATOM 2102 C TYR A1101 39.603 12.269 -38.358 1.00107.31 C ANISOU 2102 C TYR A1101 12389 16789 11594 -75 -174 -1804 C ATOM 2103 O TYR A1101 39.269 12.070 -37.187 1.00107.57 O ANISOU 2103 O TYR A1101 12379 16986 11506 -18 -155 -1830 O ATOM 2104 CB TYR A1101 39.185 10.210 -39.749 1.00103.30 C ANISOU 2104 CB TYR A1101 11726 16373 11149 -249 -244 -1536 C ATOM 2105 CG TYR A1101 38.099 9.381 -40.403 1.00105.03 C ANISOU 2105 CG TYR A1101 11840 16705 11360 -280 -251 -1368 C ATOM 2106 CD1 TYR A1101 37.042 8.865 -39.656 1.00107.87 C ANISOU 2106 CD1 TYR A1101 12092 17277 11616 -242 -235 -1262 C ATOM 2107 CD2 TYR A1101 38.128 9.108 -41.768 1.00104.93 C ANISOU 2107 CD2 TYR A1101 11829 16610 11431 -357 -278 -1308 C ATOM 2108 CE1 TYR A1101 36.031 8.116 -40.255 1.00108.79 C ANISOU 2108 CE1 TYR A1101 12109 17510 11716 -302 -254 -1094 C ATOM 2109 CE2 TYR A1101 37.128 8.350 -42.376 1.00105.84 C ANISOU 2109 CE2 TYR A1101 11853 16837 11524 -413 -294 -1163 C ATOM 2110 CZ TYR A1101 36.083 7.852 -41.614 1.00114.40 C ANISOU 2110 CZ TYR A1101 12836 18121 12508 -396 -285 -1053 C ATOM 2111 OH TYR A1101 35.093 7.103 -42.203 1.00115.63 O ANISOU 2111 OH TYR A1101 12899 18401 12635 -483 -314 -897 O ATOM 2112 N ILE A1102 40.683 13.003 -38.700 1.00103.49 N ANISOU 2112 N ILE A1102 12021 16108 11191 -136 -202 -1914 N ATOM 2113 CA ILE A1102 41.555 13.644 -37.711 1.00104.06 C ANISOU 2113 CA ILE A1102 12192 16133 11214 -158 -217 -2086 C ATOM 2114 C ILE A1102 40.849 14.855 -37.101 1.00109.22 C ANISOU 2114 C ILE A1102 12937 16743 11820 10 -146 -2211 C ATOM 2115 O ILE A1102 40.865 15.006 -35.880 1.00109.63 O ANISOU 2115 O ILE A1102 13007 16899 11747 55 -133 -2327 O ATOM 2116 CB ILE A1102 42.928 14.031 -38.305 1.00106.67 C ANISOU 2116 CB ILE A1102 12607 16284 11639 -299 -280 -2139 C ATOM 2117 N GLN A1103 40.204 15.691 -37.949 1.00106.13 N ANISOU 2117 N GLN A1103 12596 16209 11519 116 -96 -2182 N ATOM 2118 CA GLN A1103 39.464 16.885 -37.537 1.00108.01 C ANISOU 2118 CA GLN A1103 12938 16371 11732 314 -15 -2287 C ATOM 2119 C GLN A1103 38.222 16.510 -36.715 1.00112.63 C ANISOU 2119 C GLN A1103 13413 17217 12162 489 57 -2236 C ATOM 2120 O GLN A1103 37.866 17.246 -35.790 1.00114.14 O ANISOU 2120 O GLN A1103 13684 17427 12258 647 114 -2377 O ATOM 2121 CB GLN A1103 39.070 17.733 -38.760 1.00109.66 C ANISOU 2121 CB GLN A1103 13199 16381 12087 388 25 -2214 C ATOM 2122 CG GLN A1103 38.738 19.194 -38.449 1.00130.25 C ANISOU 2122 CG GLN A1103 15978 18795 14716 572 99 -2351 C ATOM 2123 CD GLN A1103 39.895 19.951 -37.840 1.00153.80 C ANISOU 2123 CD GLN A1103 19153 21565 17717 470 43 -2575 C ATOM 2124 OE1 GLN A1103 39.963 20.149 -36.623 1.00151.67 O ANISOU 2124 OE1 GLN A1103 18957 21352 17318 521 54 -2751 O ATOM 2125 NE2 GLN A1103 40.833 20.384 -38.671 1.00146.43 N ANISOU 2125 NE2 GLN A1103 18298 20407 16932 313 -23 -2567 N ATOM 2126 N LYS A1104 37.580 15.364 -37.042 1.00107.61 N ANISOU 2126 N LYS A1104 12599 16792 11497 454 48 -2037 N ATOM 2127 CA LYS A1104 36.408 14.850 -36.330 1.00107.91 C ANISOU 2127 CA LYS A1104 12494 17121 11384 583 98 -1936 C ATOM 2128 C LYS A1104 36.799 14.354 -34.934 1.00111.81 C ANISOU 2128 C LYS A1104 12955 17793 11734 555 72 -2025 C ATOM 2129 O LYS A1104 36.118 14.688 -33.962 1.00113.20 O ANISOU 2129 O LYS A1104 13107 18140 11764 729 134 -2076 O ATOM 2130 CB LYS A1104 35.719 13.727 -37.124 1.00108.98 C ANISOU 2130 CB LYS A1104 12458 17411 11537 496 71 -1694 C ATOM 2131 CG LYS A1104 34.517 14.201 -37.943 1.00123.46 C ANISOU 2131 CG LYS A1104 14230 19298 13382 640 145 -1551 C ATOM 2132 CD LYS A1104 33.513 13.070 -38.224 1.00131.87 C ANISOU 2132 CD LYS A1104 15095 20633 14376 578 125 -1313 C ATOM 2133 CE LYS A1104 33.809 12.264 -39.473 1.00138.16 C ANISOU 2133 CE LYS A1104 15856 21354 15285 369 50 -1203 C ATOM 2134 NZ LYS A1104 33.433 12.993 -40.713 1.00145.09 N ANISOU 2134 NZ LYS A1104 16741 22140 16249 425 93 -1135 N ATOM 2135 N TYR A1105 37.905 13.584 -34.832 1.00106.52 N ANISOU 2135 N TYR A1105 12277 17103 11095 351 -13 -2037 N ATOM 2136 CA TYR A1105 38.393 13.051 -33.558 1.00106.45 C ANISOU 2136 CA TYR A1105 12216 17276 10954 303 -43 -2096 C ATOM 2137 C TYR A1105 39.013 14.158 -32.690 1.00109.34 C ANISOU 2137 C TYR A1105 12734 17558 11252 356 -27 -2352 C ATOM 2138 O TYR A1105 38.999 14.038 -31.463 1.00110.21 O ANISOU 2138 O TYR A1105 12798 17877 11200 402 -17 -2427 O ATOM 2139 CB TYR A1105 39.389 11.899 -33.770 1.00106.73 C ANISOU 2139 CB TYR A1105 12194 17310 11048 88 -130 -2010 C ATOM 2140 CG TYR A1105 39.281 10.834 -32.700 1.00110.19 C ANISOU 2140 CG TYR A1105 12481 18028 11359 56 -150 -1915 C ATOM 2141 CD1 TYR A1105 38.371 9.786 -32.820 1.00112.12 C ANISOU 2141 CD1 TYR A1105 12572 18441 11588 46 -158 -1697 C ATOM 2142 CD2 TYR A1105 40.058 10.895 -31.546 1.00112.22 C ANISOU 2142 CD2 TYR A1105 12739 18394 11506 25 -167 -2032 C ATOM 2143 CE1 TYR A1105 38.245 8.818 -31.823 1.00113.91 C ANISOU 2143 CE1 TYR A1105 12650 18922 11707 12 -181 -1583 C ATOM 2144 CE2 TYR A1105 39.941 9.934 -30.541 1.00113.75 C ANISOU 2144 CE2 TYR A1105 12772 18867 11580 1 -182 -1922 C ATOM 2145 CZ TYR A1105 39.035 8.894 -30.686 1.00122.34 C ANISOU 2145 CZ TYR A1105 13710 20104 12671 -2 -189 -1690 C ATOM 2146 OH TYR A1105 38.917 7.938 -29.702 1.00124.98 O ANISOU 2146 OH TYR A1105 13879 20708 12900 -33 -210 -1554 O ATOM 2147 N LEU A1106 39.523 15.240 -33.321 1.00103.70 N ANISOU 2147 N LEU A1106 12200 16546 10656 344 -28 -2483 N ATOM 2148 CA LEU A1106 40.098 16.399 -32.629 1.00104.01 C ANISOU 2148 CA LEU A1106 12422 16445 10652 370 -24 -2739 C ATOM 2149 C LEU A1106 38.985 17.258 -32.004 1.00106.61 C ANISOU 2149 C LEU A1106 12810 16823 10873 639 78 -2845 C ATOM 2150 O LEU A1106 39.217 17.930 -30.999 1.00108.07 O ANISOU 2150 O LEU A1106 13107 17015 10941 696 91 -3065 O ATOM 2151 CB LEU A1106 40.949 17.240 -33.597 1.00103.83 C ANISOU 2151 CB LEU A1106 12566 16077 10807 258 -65 -2807 C ATOM 2152 CG LEU A1106 42.058 18.086 -32.977 1.00110.02 C ANISOU 2152 CG LEU A1106 13526 16710 11565 146 -117 -3042 C ATOM 2153 CD1 LEU A1106 43.314 17.260 -32.733 1.00108.93 C ANISOU 2153 CD1 LEU A1106 13310 16684 11395 -95 -212 -3012 C ATOM 2154 CD2 LEU A1106 42.398 19.259 -33.869 1.00113.35 C ANISOU 2154 CD2 LEU A1106 14136 16773 12157 121 -128 -3108 C ATOM 2155 N GLN A 314 37.784 17.236 -32.609 1.00 99.99 N ANISOU 2155 N GLN A 314 14803 13570 9617 -266 1825 -93 N ATOM 2156 CA GLN A 314 36.618 17.970 -32.124 1.00 97.40 C ANISOU 2156 CA GLN A 314 14582 13101 9324 -223 1660 61 C ATOM 2157 C GLN A 314 35.977 17.228 -30.950 1.00 95.71 C ANISOU 2157 C GLN A 314 14239 12805 9322 -121 1481 -26 C ATOM 2158 O GLN A 314 35.439 17.871 -30.052 1.00 93.71 O ANISOU 2158 O GLN A 314 13991 12421 9193 -110 1386 68 O ATOM 2159 CB GLN A 314 35.600 18.174 -33.253 1.00 99.97 C ANISOU 2159 CB GLN A 314 15113 13473 9399 -169 1578 165 C ATOM 2160 CG GLN A 314 34.703 19.387 -33.048 1.00116.59 C ANISOU 2160 CG GLN A 314 17365 15444 11487 -150 1484 377 C ATOM 2161 CD GLN A 314 33.332 19.188 -33.642 1.00138.45 C ANISOU 2161 CD GLN A 314 20253 18256 14096 -28 1297 430 C ATOM 2162 OE1 GLN A 314 33.158 19.075 -34.861 1.00136.25 O ANISOU 2162 OE1 GLN A 314 20102 18103 13565 -17 1316 454 O ATOM 2163 NE2 GLN A 314 32.319 19.166 -32.788 1.00129.49 N ANISOU 2163 NE2 GLN A 314 19073 17031 13097 65 1111 446 N ATOM 2164 N THR A 315 36.040 15.879 -30.960 1.00 89.91 N ANISOU 2164 N THR A 315 13401 12138 8622 -50 1445 -205 N ATOM 2165 CA THR A 315 35.486 15.006 -29.917 1.00 86.80 C ANISOU 2165 CA THR A 315 12899 11668 8414 40 1293 -299 C ATOM 2166 C THR A 315 36.266 15.188 -28.603 1.00 87.37 C ANISOU 2166 C THR A 315 12814 11665 8720 12 1327 -317 C ATOM 2167 O THR A 315 35.636 15.300 -27.551 1.00 84.91 O ANISOU 2167 O THR A 315 12468 11242 8552 48 1201 -282 O ATOM 2168 CB THR A 315 35.476 13.535 -30.387 1.00 93.76 C ANISOU 2168 CB THR A 315 13742 12627 9255 112 1275 -486 C ATOM 2169 OG1 THR A 315 34.901 13.456 -31.693 1.00 95.19 O ANISOU 2169 OG1 THR A 315 14066 12908 9192 115 1265 -479 O ATOM 2170 CG2 THR A 315 34.702 12.621 -29.449 1.00 89.66 C ANISOU 2170 CG2 THR A 315 13161 12015 8892 195 1111 -564 C ATOM 2171 N ILE A 316 37.622 15.241 -28.668 1.00 83.82 N ANISOU 2171 N ILE A 316 12260 11289 8298 -53 1497 -376 N ATOM 2172 CA ILE A 316 38.493 15.417 -27.494 1.00 82.26 C ANISOU 2172 CA ILE A 316 11894 11058 8303 -86 1534 -407 C ATOM 2173 C ILE A 316 38.303 16.838 -26.902 1.00 84.24 C ANISOU 2173 C ILE A 316 12200 11203 8606 -184 1532 -249 C ATOM 2174 O ILE A 316 38.254 16.970 -25.677 1.00 82.42 O ANISOU 2174 O ILE A 316 11880 10889 8547 -176 1458 -248 O ATOM 2175 CB ILE A 316 40.000 15.059 -27.768 1.00 86.76 C ANISOU 2175 CB ILE A 316 12311 11769 8886 -123 1714 -532 C ATOM 2176 CG1 ILE A 316 40.916 15.294 -26.545 1.00 86.74 C ANISOU 2176 CG1 ILE A 316 12112 11759 9084 -157 1739 -570 C ATOM 2177 CG2 ILE A 316 40.575 15.749 -28.992 1.00 89.96 C ANISOU 2177 CG2 ILE A 316 12797 12278 9104 -242 1900 -486 C ATOM 2178 CD1 ILE A 316 41.005 14.169 -25.587 1.00 94.95 C ANISOU 2178 CD1 ILE A 316 13015 12778 10284 -19 1627 -684 C ATOM 2179 N SER A 317 38.145 17.872 -27.758 1.00 80.95 N ANISOU 2179 N SER A 317 11946 10779 8034 -269 1609 -116 N ATOM 2180 CA SER A 317 37.941 19.254 -27.306 1.00 80.10 C ANISOU 2180 CA SER A 317 11927 10545 7962 -358 1622 38 C ATOM 2181 C SER A 317 36.611 19.399 -26.546 1.00 80.27 C ANISOU 2181 C SER A 317 12009 10430 8060 -262 1425 111 C ATOM 2182 O SER A 317 36.571 20.082 -25.520 1.00 78.98 O ANISOU 2182 O SER A 317 11819 10155 8036 -300 1399 157 O ATOM 2183 CB SER A 317 38.003 20.230 -28.478 1.00 85.73 C ANISOU 2183 CB SER A 317 12832 11268 8473 -450 1749 175 C ATOM 2184 OG SER A 317 36.950 20.021 -29.404 1.00 95.70 O ANISOU 2184 OG SER A 317 14258 12545 9558 -351 1648 242 O ATOM 2185 N ASN A 318 35.546 18.725 -27.029 1.00 74.88 N ANISOU 2185 N ASN A 318 11394 9768 7289 -144 1291 103 N ATOM 2186 CA ASN A 318 34.221 18.732 -26.407 1.00 72.63 C ANISOU 2186 CA ASN A 318 11145 9387 7066 -49 1106 152 C ATOM 2187 C ASN A 318 34.250 18.002 -25.061 1.00 73.06 C ANISOU 2187 C ASN A 318 11034 9397 7328 -10 1023 46 C ATOM 2188 O ASN A 318 33.649 18.491 -24.103 1.00 71.91 O ANISOU 2188 O ASN A 318 10885 9145 7295 8 935 99 O ATOM 2189 CB ASN A 318 33.169 18.115 -27.339 1.00 74.68 C ANISOU 2189 CB ASN A 318 11495 9715 7166 46 993 147 C ATOM 2190 CG ASN A 318 32.844 18.919 -28.586 1.00102.46 C ANISOU 2190 CG ASN A 318 15201 13270 10460 38 1027 283 C ATOM 2191 OD1 ASN A 318 32.366 18.370 -29.585 1.00100.09 O ANISOU 2191 OD1 ASN A 318 14965 13075 9989 91 976 257 O ATOM 2192 ND2 ASN A 318 33.083 20.230 -28.572 1.00 93.84 N ANISOU 2192 ND2 ASN A 318 14213 12089 9353 -28 1112 432 N ATOM 2193 N GLU A 319 34.969 16.857 -24.983 1.00 68.02 N ANISOU 2193 N GLU A 319 10269 8839 6737 11 1056 -102 N ATOM 2194 CA GLU A 319 35.147 16.061 -23.762 1.00 65.85 C ANISOU 2194 CA GLU A 319 9847 8530 6642 58 990 -201 C ATOM 2195 C GLU A 319 35.881 16.881 -22.691 1.00 67.85 C ANISOU 2195 C GLU A 319 10012 8734 7036 -18 1039 -172 C ATOM 2196 O GLU A 319 35.477 16.874 -21.529 1.00 66.10 O ANISOU 2196 O GLU A 319 9739 8432 6943 9 943 -170 O ATOM 2197 CB GLU A 319 35.934 14.772 -24.063 1.00 67.77 C ANISOU 2197 CB GLU A 319 9994 8869 6888 107 1040 -354 C ATOM 2198 CG GLU A 319 35.118 13.646 -24.677 1.00 78.41 C ANISOU 2198 CG GLU A 319 11400 10231 8162 194 951 -429 C ATOM 2199 CD GLU A 319 35.902 12.420 -25.116 1.00104.68 C ANISOU 2199 CD GLU A 319 14663 13634 11477 249 1017 -585 C ATOM 2200 OE1 GLU A 319 35.332 11.597 -25.868 1.00105.76 O ANISOU 2200 OE1 GLU A 319 14873 13792 11520 296 975 -655 O ATOM 2201 OE2 GLU A 319 37.081 12.279 -24.717 1.00 99.60 O ANISOU 2201 OE2 GLU A 319 13893 13034 10916 249 1111 -646 O ATOM 2202 N GLN A 320 36.939 17.607 -23.104 1.00 64.74 N ANISOU 2202 N GLN A 320 9603 8392 6604 -128 1195 -153 N ATOM 2203 CA GLN A 320 37.766 18.460 -22.251 1.00 64.19 C ANISOU 2203 CA GLN A 320 9447 8295 6646 -235 1266 -141 C ATOM 2204 C GLN A 320 36.974 19.669 -21.740 1.00 66.62 C ANISOU 2204 C GLN A 320 9874 8454 6984 -279 1218 -10 C ATOM 2205 O GLN A 320 37.121 20.032 -20.570 1.00 65.15 O ANISOU 2205 O GLN A 320 9613 8208 6932 -314 1187 -23 O ATOM 2206 CB GLN A 320 39.009 18.921 -23.019 1.00 67.44 C ANISOU 2206 CB GLN A 320 9823 8811 6989 -361 1460 -159 C ATOM 2207 CG GLN A 320 40.179 19.298 -22.118 1.00 86.91 C ANISOU 2207 CG GLN A 320 12112 11321 9589 -462 1535 -227 C ATOM 2208 CD GLN A 320 41.520 18.910 -22.698 1.00111.07 C ANISOU 2208 CD GLN A 320 15033 14554 12614 -519 1694 -332 C ATOM 2209 OE1 GLN A 320 41.699 18.772 -23.918 1.00108.65 O ANISOU 2209 OE1 GLN A 320 14799 14320 12162 -536 1798 -326 O ATOM 2210 NE2 GLN A 320 42.500 18.731 -21.826 1.00104.13 N ANISOU 2210 NE2 GLN A 320 13941 13761 11862 -546 1715 -436 N ATOM 2211 N ARG A 321 36.135 20.280 -22.612 1.00 63.09 N ANISOU 2211 N ARG A 321 9612 7951 6406 -267 1210 110 N ATOM 2212 CA ARG A 321 35.301 21.436 -22.273 1.00 62.43 C ANISOU 2212 CA ARG A 321 9664 7718 6338 -277 1165 242 C ATOM 2213 C ARG A 321 34.234 21.047 -21.259 1.00 64.19 C ANISOU 2213 C ARG A 321 9848 7873 6668 -168 993 224 C ATOM 2214 O ARG A 321 34.045 21.767 -20.278 1.00 63.89 O ANISOU 2214 O ARG A 321 9811 7728 6738 -196 969 255 O ATOM 2215 CB ARG A 321 34.656 22.047 -23.524 1.00 63.91 C ANISOU 2215 CB ARG A 321 10057 7884 6344 -255 1183 377 C ATOM 2216 N ALA A 322 33.563 19.895 -21.472 1.00 58.78 N ANISOU 2216 N ALA A 322 9128 7251 5955 -57 884 163 N ATOM 2217 CA ALA A 322 32.532 19.382 -20.568 1.00 56.16 C ANISOU 2217 CA ALA A 322 8753 6871 5715 34 731 136 C ATOM 2218 C ALA A 322 33.128 18.986 -19.211 1.00 58.65 C ANISOU 2218 C ALA A 322 8921 7173 6192 12 719 48 C ATOM 2219 O ALA A 322 32.491 19.239 -18.187 1.00 58.60 O ANISOU 2219 O ALA A 322 8900 7086 6278 35 639 64 O ATOM 2220 CB ALA A 322 31.819 18.197 -21.198 1.00 56.39 C ANISOU 2220 CB ALA A 322 8783 6975 5667 125 642 77 C ATOM 2221 N SER A 323 34.348 18.396 -19.196 1.00 54.00 N ANISOU 2221 N SER A 323 8218 6671 5630 -23 797 -44 N ATOM 2222 CA SER A 323 35.024 17.987 -17.959 1.00 52.63 C ANISOU 2222 CA SER A 323 7896 6509 5593 -28 778 -125 C ATOM 2223 C SER A 323 35.447 19.209 -17.109 1.00 55.67 C ANISOU 2223 C SER A 323 8262 6834 6056 -135 825 -89 C ATOM 2224 O SER A 323 35.402 19.134 -15.880 1.00 53.81 O ANISOU 2224 O SER A 323 7951 6570 5925 -127 760 -123 O ATOM 2225 CB SER A 323 36.226 17.094 -18.256 1.00 56.31 C ANISOU 2225 CB SER A 323 8240 7097 6059 -17 848 -232 C ATOM 2226 OG SER A 323 37.328 17.825 -18.767 1.00 68.56 O ANISOU 2226 OG SER A 323 9767 8715 7566 -126 995 -230 O ATOM 2227 N LYS A 324 35.843 20.321 -17.764 1.00 53.36 N ANISOU 2227 N LYS A 324 8050 6519 5705 -241 941 -23 N ATOM 2228 CA LYS A 324 36.232 21.558 -17.091 1.00 54.04 C ANISOU 2228 CA LYS A 324 8148 6529 5858 -364 1003 7 C ATOM 2229 C LYS A 324 35.008 22.204 -16.443 1.00 59.38 C ANISOU 2229 C LYS A 324 8930 7057 6575 -320 911 81 C ATOM 2230 O LYS A 324 35.106 22.711 -15.322 1.00 59.78 O ANISOU 2230 O LYS A 324 8939 7050 6723 -370 896 56 O ATOM 2231 CB LYS A 324 36.910 22.534 -18.064 1.00 58.20 C ANISOU 2231 CB LYS A 324 8762 7051 6302 -497 1166 66 C ATOM 2232 CG LYS A 324 38.381 22.221 -18.323 1.00 74.07 C ANISOU 2232 CG LYS A 324 10619 9210 8315 -595 1290 -32 C ATOM 2233 N VAL A 325 33.849 22.151 -17.137 1.00 55.68 N ANISOU 2233 N VAL A 325 8586 6543 6025 -219 845 162 N ATOM 2234 CA VAL A 325 32.571 22.681 -16.658 1.00 54.69 C ANISOU 2234 CA VAL A 325 8551 6300 5929 -147 752 230 C ATOM 2235 C VAL A 325 32.136 21.866 -15.439 1.00 56.84 C ANISOU 2235 C VAL A 325 8705 6588 6302 -84 638 149 C ATOM 2236 O VAL A 325 31.930 22.452 -14.381 1.00 57.13 O ANISOU 2236 O VAL A 325 8734 6547 6426 -106 618 144 O ATOM 2237 CB VAL A 325 31.486 22.706 -17.770 1.00 59.06 C ANISOU 2237 CB VAL A 325 9236 6844 6358 -44 700 324 C ATOM 2238 CG1 VAL A 325 30.101 22.987 -17.193 1.00 58.18 C ANISOU 2238 CG1 VAL A 325 9162 6654 6287 62 580 363 C ATOM 2239 CG2 VAL A 325 31.830 23.725 -18.850 1.00 60.52 C ANISOU 2239 CG2 VAL A 325 9577 6981 6438 -104 814 434 C ATOM 2240 N LEU A 326 32.043 20.526 -15.574 1.00 51.85 N ANISOU 2240 N LEU A 326 7993 6051 5654 -15 575 83 N ATOM 2241 CA LEU A 326 31.661 19.603 -14.498 1.00 50.25 C ANISOU 2241 CA LEU A 326 7697 5862 5532 42 476 14 C ATOM 2242 C LEU A 326 32.555 19.796 -13.252 1.00 54.17 C ANISOU 2242 C LEU A 326 8091 6363 6129 -24 498 -44 C ATOM 2243 O LEU A 326 32.048 19.767 -12.132 1.00 53.28 O ANISOU 2243 O LEU A 326 7949 6211 6082 -3 430 -62 O ATOM 2244 CB LEU A 326 31.733 18.147 -15.001 1.00 49.86 C ANISOU 2244 CB LEU A 326 7601 5901 5444 107 440 -50 C ATOM 2245 CG LEU A 326 31.218 17.041 -14.064 1.00 53.10 C ANISOU 2245 CG LEU A 326 7952 6306 5917 171 341 -106 C ATOM 2246 CD1 LEU A 326 30.469 15.978 -14.833 1.00 52.87 C ANISOU 2246 CD1 LEU A 326 7958 6307 5824 235 288 -132 C ATOM 2247 CD2 LEU A 326 32.359 16.373 -13.312 1.00 55.10 C ANISOU 2247 CD2 LEU A 326 8094 6604 6237 167 355 -180 C ATOM 2248 N GLY A 327 33.853 20.004 -13.470 1.00 51.12 N ANISOU 2248 N GLY A 327 7644 6037 5742 -107 593 -79 N ATOM 2249 CA GLY A 327 34.838 20.210 -12.417 1.00 50.98 C ANISOU 2249 CA GLY A 327 7509 6058 5804 -180 614 -146 C ATOM 2250 C GLY A 327 34.557 21.401 -11.522 1.00 55.18 C ANISOU 2250 C GLY A 327 8083 6490 6392 -255 618 -125 C ATOM 2251 O GLY A 327 34.439 21.231 -10.310 1.00 54.10 O ANISOU 2251 O GLY A 327 7885 6355 6316 -244 551 -170 O ATOM 2252 N ILE A 328 34.437 22.611 -12.110 1.00 53.02 N ANISOU 2252 N ILE A 328 7932 6122 6092 -329 701 -56 N ATOM 2253 CA ILE A 328 34.186 23.861 -11.380 1.00 53.30 C ANISOU 2253 CA ILE A 328 8038 6034 6181 -404 726 -39 C ATOM 2254 C ILE A 328 32.827 23.802 -10.646 1.00 56.79 C ANISOU 2254 C ILE A 328 8529 6396 6654 -296 619 -16 C ATOM 2255 O ILE A 328 32.785 24.092 -9.446 1.00 56.52 O ANISOU 2255 O ILE A 328 8457 6335 6685 -327 591 -68 O ATOM 2256 CB ILE A 328 34.291 25.122 -12.296 1.00 57.72 C ANISOU 2256 CB ILE A 328 8751 6483 6699 -492 847 45 C ATOM 2257 CG1 ILE A 328 35.677 25.213 -12.966 1.00 59.54 C ANISOU 2257 CG1 ILE A 328 8923 6805 6897 -625 973 14 C ATOM 2258 CG2 ILE A 328 33.999 26.412 -11.505 1.00 58.98 C ANISOU 2258 CG2 ILE A 328 9003 6485 6924 -565 880 54 C ATOM 2259 CD1 ILE A 328 35.734 26.046 -14.280 1.00 68.49 C ANISOU 2259 CD1 ILE A 328 10222 7859 7940 -682 1094 121 C ATOM 2260 N VAL A 329 31.740 23.417 -11.358 1.00 52.44 N ANISOU 2260 N VAL A 329 8050 5824 6049 -177 562 51 N ATOM 2261 CA VAL A 329 30.362 23.336 -10.836 1.00 50.84 C ANISOU 2261 CA VAL A 329 7881 5568 5868 -73 467 72 C ATOM 2262 C VAL A 329 30.283 22.340 -9.648 1.00 52.72 C ANISOU 2262 C VAL A 329 7998 5874 6158 -47 387 -9 C ATOM 2263 O VAL A 329 29.705 22.684 -8.615 1.00 51.46 O ANISOU 2263 O VAL A 329 7840 5664 6049 -40 355 -29 O ATOM 2264 CB VAL A 329 29.324 23.005 -11.956 1.00 54.08 C ANISOU 2264 CB VAL A 329 8362 5986 6199 40 417 145 C ATOM 2265 CG1 VAL A 329 27.909 22.876 -11.398 1.00 52.91 C ANISOU 2265 CG1 VAL A 329 8212 5812 6077 141 320 149 C ATOM 2266 CG2 VAL A 329 29.353 24.062 -13.064 1.00 55.18 C ANISOU 2266 CG2 VAL A 329 8644 6049 6271 29 490 244 C ATOM 2267 N PHE A 330 30.883 21.143 -9.783 1.00 49.01 N ANISOU 2267 N PHE A 330 7439 5511 5672 -32 362 -54 N ATOM 2268 CA PHE A 330 30.861 20.135 -8.717 1.00 48.24 C ANISOU 2268 CA PHE A 330 7252 5467 5611 2 289 -114 C ATOM 2269 C PHE A 330 31.770 20.535 -7.542 1.00 53.78 C ANISOU 2269 C PHE A 330 7878 6193 6363 -77 305 -173 C ATOM 2270 O PHE A 330 31.443 20.213 -6.400 1.00 52.73 O ANISOU 2270 O PHE A 330 7712 6067 6257 -58 246 -204 O ATOM 2271 CB PHE A 330 31.233 18.738 -9.252 1.00 49.47 C ANISOU 2271 CB PHE A 330 7355 5707 5736 58 262 -141 C ATOM 2272 CG PHE A 330 30.198 18.027 -10.109 1.00 50.16 C ANISOU 2272 CG PHE A 330 7497 5787 5774 134 218 -113 C ATOM 2273 CD1 PHE A 330 30.256 16.653 -10.298 1.00 52.53 C ANISOU 2273 CD1 PHE A 330 7766 6132 6061 188 179 -153 C ATOM 2274 CD2 PHE A 330 29.173 18.735 -10.731 1.00 52.10 C ANISOU 2274 CD2 PHE A 330 7828 5984 5985 154 213 -53 C ATOM 2275 CE1 PHE A 330 29.308 15.998 -11.088 1.00 53.31 C ANISOU 2275 CE1 PHE A 330 7913 6230 6113 235 141 -146 C ATOM 2276 CE2 PHE A 330 28.226 18.079 -11.524 1.00 54.60 C ANISOU 2276 CE2 PHE A 330 8177 6322 6248 217 162 -41 C ATOM 2277 CZ PHE A 330 28.303 16.717 -11.701 1.00 52.47 C ANISOU 2277 CZ PHE A 330 7871 6100 5965 245 128 -95 C ATOM 2278 N PHE A 331 32.877 21.264 -7.813 1.00 52.62 N ANISOU 2278 N PHE A 331 7707 6066 6221 -176 387 -194 N ATOM 2279 CA PHE A 331 33.788 21.751 -6.773 1.00 53.78 C ANISOU 2279 CA PHE A 331 7772 6254 6408 -272 404 -265 C ATOM 2280 C PHE A 331 33.115 22.850 -5.929 1.00 58.65 C ANISOU 2280 C PHE A 331 8465 6761 7060 -319 409 -267 C ATOM 2281 O PHE A 331 33.284 22.855 -4.710 1.00 58.07 O ANISOU 2281 O PHE A 331 8333 6720 7009 -347 369 -329 O ATOM 2282 CB PHE A 331 35.123 22.262 -7.362 1.00 57.07 C ANISOU 2282 CB PHE A 331 8132 6730 6822 -387 502 -298 C ATOM 2283 CG PHE A 331 36.034 22.911 -6.343 1.00 59.83 C ANISOU 2283 CG PHE A 331 8391 7130 7212 -511 523 -385 C ATOM 2284 CD1 PHE A 331 36.677 22.148 -5.373 1.00 63.15 C ANISOU 2284 CD1 PHE A 331 8665 7686 7641 -485 447 -458 C ATOM 2285 CD2 PHE A 331 36.218 24.290 -6.329 1.00 63.31 C ANISOU 2285 CD2 PHE A 331 8901 7478 7676 -655 614 -394 C ATOM 2286 CE1 PHE A 331 37.489 22.753 -4.407 1.00 65.24 C ANISOU 2286 CE1 PHE A 331 8837 8022 7931 -602 451 -549 C ATOM 2287 CE2 PHE A 331 37.034 24.894 -5.365 1.00 67.25 C ANISOU 2287 CE2 PHE A 331 9314 8029 8208 -789 632 -494 C ATOM 2288 CZ PHE A 331 37.664 24.121 -4.411 1.00 65.35 C ANISOU 2288 CZ PHE A 331 8910 7951 7969 -763 545 -575 C ATOM 2289 N LEU A 332 32.363 23.770 -6.574 1.00 56.18 N ANISOU 2289 N LEU A 332 8284 6318 6744 -317 458 -201 N ATOM 2290 CA LEU A 332 31.652 24.849 -5.884 1.00 56.81 C ANISOU 2290 CA LEU A 332 8453 6272 6861 -337 473 -202 C ATOM 2291 C LEU A 332 30.511 24.295 -5.025 1.00 59.55 C ANISOU 2291 C LEU A 332 8788 6621 7216 -235 383 -209 C ATOM 2292 O LEU A 332 30.207 24.875 -3.984 1.00 59.24 O ANISOU 2292 O LEU A 332 8768 6531 7209 -261 383 -254 O ATOM 2293 CB LEU A 332 31.129 25.910 -6.865 1.00 58.17 C ANISOU 2293 CB LEU A 332 8779 6300 7023 -329 543 -115 C ATOM 2294 CG LEU A 332 32.198 26.825 -7.499 1.00 65.31 C ANISOU 2294 CG LEU A 332 9735 7153 7926 -471 664 -109 C ATOM 2295 CD1 LEU A 332 31.616 27.637 -8.641 1.00 66.61 C ANISOU 2295 CD1 LEU A 332 10070 7184 8054 -430 722 8 C ATOM 2296 CD2 LEU A 332 32.849 27.750 -6.466 1.00 68.98 C ANISOU 2296 CD2 LEU A 332 10201 7558 8450 -612 719 -197 C ATOM 2297 N PHE A 333 29.918 23.155 -5.437 1.00 55.65 N ANISOU 2297 N PHE A 333 8263 6189 6691 -134 315 -177 N ATOM 2298 CA PHE A 333 28.875 22.444 -4.698 1.00 55.01 C ANISOU 2298 CA PHE A 333 8161 6126 6613 -55 240 -185 C ATOM 2299 C PHE A 333 29.452 21.861 -3.406 1.00 58.01 C ANISOU 2299 C PHE A 333 8456 6586 6998 -92 201 -254 C ATOM 2300 O PHE A 333 28.853 22.013 -2.340 1.00 57.65 O ANISOU 2300 O PHE A 333 8416 6527 6963 -89 180 -284 O ATOM 2301 CB PHE A 333 28.264 21.319 -5.561 1.00 56.83 C ANISOU 2301 CB PHE A 333 8385 6401 6808 34 189 -143 C ATOM 2302 CG PHE A 333 27.378 20.342 -4.813 1.00 58.61 C ANISOU 2302 CG PHE A 333 8575 6661 7033 85 121 -161 C ATOM 2303 CD1 PHE A 333 26.002 20.525 -4.762 1.00 62.12 C ANISOU 2303 CD1 PHE A 333 9046 7070 7485 137 100 -146 C ATOM 2304 CD2 PHE A 333 27.921 19.233 -4.168 1.00 61.28 C ANISOU 2304 CD2 PHE A 333 8853 7068 7361 82 83 -191 C ATOM 2305 CE1 PHE A 333 25.183 19.620 -4.080 1.00 62.77 C ANISOU 2305 CE1 PHE A 333 9093 7191 7566 159 54 -167 C ATOM 2306 CE2 PHE A 333 27.103 18.334 -3.476 1.00 64.10 C ANISOU 2306 CE2 PHE A 333 9201 7442 7713 114 35 -198 C ATOM 2307 CZ PHE A 333 25.738 18.532 -3.442 1.00 62.18 C ANISOU 2307 CZ PHE A 333 8981 7167 7477 139 27 -188 C ATOM 2308 N LEU A 334 30.592 21.151 -3.523 1.00 53.89 N ANISOU 2308 N LEU A 334 7857 6159 6462 -113 190 -276 N ATOM 2309 CA LEU A 334 31.265 20.489 -2.410 1.00 53.78 C ANISOU 2309 CA LEU A 334 7757 6239 6438 -123 139 -329 C ATOM 2310 C LEU A 334 31.804 21.502 -1.405 1.00 59.85 C ANISOU 2310 C LEU A 334 8504 7015 7220 -225 162 -397 C ATOM 2311 O LEU A 334 31.770 21.244 -0.200 1.00 59.59 O ANISOU 2311 O LEU A 334 8441 7032 7168 -227 113 -436 O ATOM 2312 CB LEU A 334 32.400 19.586 -2.931 1.00 53.96 C ANISOU 2312 CB LEU A 334 7695 6362 6445 -99 126 -338 C ATOM 2313 CG LEU A 334 31.974 18.289 -3.641 1.00 57.56 C ANISOU 2313 CG LEU A 334 8168 6820 6881 5 91 -294 C ATOM 2314 CD1 LEU A 334 33.068 17.788 -4.566 1.00 58.07 C ANISOU 2314 CD1 LEU A 334 8171 6955 6938 21 119 -307 C ATOM 2315 CD2 LEU A 334 31.578 17.208 -2.646 1.00 58.74 C ANISOU 2315 CD2 LEU A 334 8314 6991 7016 70 16 -291 C ATOM 2316 N LEU A 335 32.262 22.665 -1.907 1.00 58.04 N ANISOU 2316 N LEU A 335 8305 6731 7018 -317 243 -413 N ATOM 2317 CA LEU A 335 32.809 23.781 -1.134 1.00 58.95 C ANISOU 2317 CA LEU A 335 8415 6831 7153 -442 285 -491 C ATOM 2318 C LEU A 335 31.747 24.414 -0.232 1.00 62.36 C ANISOU 2318 C LEU A 335 8930 7169 7596 -435 284 -511 C ATOM 2319 O LEU A 335 32.059 24.813 0.888 1.00 62.21 O ANISOU 2319 O LEU A 335 8885 7182 7569 -508 276 -595 O ATOM 2320 CB LEU A 335 33.362 24.831 -2.110 1.00 60.16 C ANISOU 2320 CB LEU A 335 8617 6908 7334 -542 390 -483 C ATOM 2321 CG LEU A 335 34.348 25.858 -1.573 1.00 66.34 C ANISOU 2321 CG LEU A 335 9371 7696 8140 -713 452 -580 C ATOM 2322 CD1 LEU A 335 35.738 25.244 -1.386 1.00 67.48 C ANISOU 2322 CD1 LEU A 335 9341 8031 8266 -773 426 -648 C ATOM 2323 CD2 LEU A 335 34.437 27.041 -2.515 1.00 68.85 C ANISOU 2323 CD2 LEU A 335 9809 7862 8488 -803 573 -546 C ATOM 2324 N MET A 336 30.499 24.503 -0.723 1.00 58.55 N ANISOU 2324 N MET A 336 8537 6584 7125 -343 291 -443 N ATOM 2325 CA MET A 336 29.381 25.083 0.015 1.00 58.53 C ANISOU 2325 CA MET A 336 8604 6497 7138 -311 298 -462 C ATOM 2326 C MET A 336 28.826 24.114 1.080 1.00 60.21 C ANISOU 2326 C MET A 336 8765 6801 7313 -258 225 -482 C ATOM 2327 O MET A 336 28.134 24.562 1.996 1.00 60.11 O ANISOU 2327 O MET A 336 8782 6757 7299 -260 236 -529 O ATOM 2328 CB MET A 336 28.281 25.531 -0.945 1.00 61.31 C ANISOU 2328 CB MET A 336 9050 6730 7515 -220 327 -384 C ATOM 2329 CG MET A 336 28.641 26.787 -1.723 1.00 66.77 C ANISOU 2329 CG MET A 336 9842 7288 8240 -273 415 -363 C ATOM 2330 SD MET A 336 27.369 27.265 -2.915 1.00 71.82 S ANISOU 2330 SD MET A 336 10595 7804 8888 -131 428 -251 S ATOM 2331 CE MET A 336 26.234 28.155 -1.834 1.00 69.24 C ANISOU 2331 CE MET A 336 10329 7372 8608 -75 447 -306 C ATOM 2332 N TRP A 337 29.150 22.807 0.981 1.00 54.69 N ANISOU 2332 N TRP A 337 7998 6206 6578 -214 161 -449 N ATOM 2333 CA TRP A 337 28.751 21.792 1.961 1.00 53.47 C ANISOU 2333 CA TRP A 337 7812 6127 6376 -173 98 -452 C ATOM 2334 C TRP A 337 29.847 21.589 3.029 1.00 58.09 C ANISOU 2334 C TRP A 337 8331 6824 6915 -231 57 -512 C ATOM 2335 O TRP A 337 29.564 21.048 4.102 1.00 56.71 O ANISOU 2335 O TRP A 337 8153 6706 6687 -216 15 -524 O ATOM 2336 CB TRP A 337 28.422 20.460 1.275 1.00 51.13 C ANISOU 2336 CB TRP A 337 7503 5858 6067 -89 55 -380 C ATOM 2337 CG TRP A 337 26.971 20.284 0.946 1.00 51.41 C ANISOU 2337 CG TRP A 337 7582 5837 6115 -30 62 -342 C ATOM 2338 CD1 TRP A 337 26.414 20.236 -0.297 1.00 53.96 C ANISOU 2338 CD1 TRP A 337 7927 6115 6459 20 71 -294 C ATOM 2339 CD2 TRP A 337 25.888 20.141 1.878 1.00 51.14 C ANISOU 2339 CD2 TRP A 337 7561 5803 6064 -18 60 -358 C ATOM 2340 NE1 TRP A 337 25.051 20.068 -0.200 1.00 53.02 N ANISOU 2340 NE1 TRP A 337 7820 5980 6345 64 65 -284 N ATOM 2341 CE2 TRP A 337 24.700 20.014 1.123 1.00 54.39 C ANISOU 2341 CE2 TRP A 337 7986 6179 6500 38 67 -323 C ATOM 2342 CE3 TRP A 337 25.800 20.152 3.283 1.00 52.63 C ANISOU 2342 CE3 TRP A 337 7749 6034 6213 -54 57 -403 C ATOM 2343 CZ2 TRP A 337 23.446 19.862 1.722 1.00 53.70 C ANISOU 2343 CZ2 TRP A 337 7895 6100 6409 55 76 -337 C ATOM 2344 CZ3 TRP A 337 24.558 19.989 3.875 1.00 54.16 C ANISOU 2344 CZ3 TRP A 337 7957 6227 6395 -38 74 -410 C ATOM 2345 CH2 TRP A 337 23.399 19.841 3.098 1.00 54.53 C ANISOU 2345 CH2 TRP A 337 8001 6242 6478 14 86 -380 C ATOM 2346 N CYS A 338 31.090 22.040 2.729 1.00 56.48 N ANISOU 2346 N CYS A 338 8072 6662 6725 -301 71 -551 N ATOM 2347 CA CYS A 338 32.260 21.965 3.612 1.00 57.49 C ANISOU 2347 CA CYS A 338 8110 6922 6811 -361 26 -622 C ATOM 2348 C CYS A 338 32.013 22.630 4.977 1.00 60.28 C ANISOU 2348 C CYS A 338 8488 7292 7125 -428 22 -704 C ATOM 2349 O CYS A 338 32.351 21.994 5.981 1.00 60.56 O ANISOU 2349 O CYS A 338 8475 7450 7087 -413 -53 -725 O ATOM 2350 CB CYS A 338 33.495 22.556 2.942 1.00 59.11 C ANISOU 2350 CB CYS A 338 8247 7162 7051 -449 66 -665 C ATOM 2351 SG CYS A 338 34.327 21.427 1.807 1.00 63.30 S ANISOU 2351 SG CYS A 338 8683 7785 7584 -369 36 -611 S ATOM 2352 N PRO A 339 31.458 23.874 5.080 1.00 55.30 N ANISOU 2352 N PRO A 339 7935 6544 6532 -493 98 -754 N ATOM 2353 CA PRO A 339 31.271 24.471 6.411 1.00 55.15 C ANISOU 2353 CA PRO A 339 7938 6549 6467 -559 99 -851 C ATOM 2354 C PRO A 339 30.416 23.606 7.339 1.00 57.00 C ANISOU 2354 C PRO A 339 8194 6835 6628 -481 50 -821 C ATOM 2355 O PRO A 339 30.801 23.432 8.495 1.00 57.19 O ANISOU 2355 O PRO A 339 8192 6971 6568 -519 3 -882 O ATOM 2356 CB PRO A 339 30.600 25.811 6.104 1.00 57.16 C ANISOU 2356 CB PRO A 339 8296 6630 6794 -605 202 -889 C ATOM 2357 CG PRO A 339 31.005 26.133 4.726 1.00 61.69 C ANISOU 2357 CG PRO A 339 8880 7120 7437 -612 250 -832 C ATOM 2358 CD PRO A 339 30.994 24.809 4.030 1.00 56.43 C ANISOU 2358 CD PRO A 339 8161 6525 6754 -503 187 -727 C ATOM 2359 N PHE A 340 29.313 23.008 6.825 1.00 51.20 N ANISOU 2359 N PHE A 340 7502 6035 5915 -381 59 -730 N ATOM 2360 CA PHE A 340 28.425 22.169 7.629 1.00 49.88 C ANISOU 2360 CA PHE A 340 7361 5907 5683 -325 33 -699 C ATOM 2361 C PHE A 340 29.123 20.916 8.151 1.00 52.41 C ANISOU 2361 C PHE A 340 7638 6358 5917 -292 -58 -655 C ATOM 2362 O PHE A 340 29.054 20.669 9.351 1.00 52.64 O ANISOU 2362 O PHE A 340 7682 6467 5853 -307 -88 -679 O ATOM 2363 CB PHE A 340 27.135 21.775 6.877 1.00 50.69 C ANISOU 2363 CB PHE A 340 7502 5922 5834 -244 66 -623 C ATOM 2364 CG PHE A 340 26.293 20.781 7.651 1.00 52.03 C ANISOU 2364 CG PHE A 340 7691 6142 5937 -208 47 -586 C ATOM 2365 CD1 PHE A 340 25.551 21.185 8.758 1.00 55.70 C ANISOU 2365 CD1 PHE A 340 8187 6624 6353 -237 87 -644 C ATOM 2366 CD2 PHE A 340 26.281 19.436 7.305 1.00 53.47 C ANISOU 2366 CD2 PHE A 340 7867 6348 6100 -155 1 -497 C ATOM 2367 CE1 PHE A 340 24.825 20.260 9.512 1.00 56.54 C ANISOU 2367 CE1 PHE A 340 8315 6782 6386 -223 84 -607 C ATOM 2368 CE2 PHE A 340 25.559 18.511 8.061 1.00 56.57 C ANISOU 2368 CE2 PHE A 340 8294 6773 6427 -143 -4 -459 C ATOM 2369 CZ PHE A 340 24.833 18.930 9.158 1.00 55.45 C ANISOU 2369 CZ PHE A 340 8180 6658 6232 -182 40 -510 C ATOM 2370 N PHE A 341 29.766 20.125 7.271 1.00 47.59 N ANISOU 2370 N PHE A 341 6984 5766 5333 -238 -100 -588 N ATOM 2371 CA PHE A 341 30.398 18.864 7.664 1.00 46.97 C ANISOU 2371 CA PHE A 341 6876 5788 5184 -174 -186 -534 C ATOM 2372 C PHE A 341 31.687 19.042 8.498 1.00 52.40 C ANISOU 2372 C PHE A 341 7484 6624 5801 -209 -256 -598 C ATOM 2373 O PHE A 341 32.013 18.135 9.268 1.00 52.39 O ANISOU 2373 O PHE A 341 7480 6717 5710 -149 -335 -559 O ATOM 2374 CB PHE A 341 30.637 17.961 6.443 1.00 47.42 C ANISOU 2374 CB PHE A 341 6914 5809 5294 -93 -200 -457 C ATOM 2375 CG PHE A 341 29.340 17.389 5.908 1.00 47.27 C ANISOU 2375 CG PHE A 341 6969 5684 5307 -50 -162 -391 C ATOM 2376 CD1 PHE A 341 28.639 16.419 6.622 1.00 49.70 C ANISOU 2376 CD1 PHE A 341 7340 5989 5556 -16 -180 -338 C ATOM 2377 CD2 PHE A 341 28.791 17.856 4.723 1.00 47.87 C ANISOU 2377 CD2 PHE A 341 7055 5670 5464 -52 -106 -384 C ATOM 2378 CE1 PHE A 341 27.423 15.913 6.147 1.00 49.35 C ANISOU 2378 CE1 PHE A 341 7347 5860 5542 -1 -140 -294 C ATOM 2379 CE2 PHE A 341 27.585 17.333 4.239 1.00 49.66 C ANISOU 2379 CE2 PHE A 341 7330 5826 5713 -17 -82 -337 C ATOM 2380 CZ PHE A 341 26.905 16.371 4.959 1.00 47.46 C ANISOU 2380 CZ PHE A 341 7095 5552 5385 0 -97 -300 C ATOM 2381 N ILE A 342 32.381 20.199 8.401 1.00 49.82 N ANISOU 2381 N ILE A 342 7099 6320 5509 -309 -228 -697 N ATOM 2382 CA ILE A 342 33.589 20.441 9.201 1.00 51.16 C ANISOU 2382 CA ILE A 342 7173 6653 5612 -364 -297 -781 C ATOM 2383 C ILE A 342 33.170 20.852 10.638 1.00 57.07 C ANISOU 2383 C ILE A 342 7972 7454 6257 -420 -311 -847 C ATOM 2384 O ILE A 342 33.660 20.254 11.599 1.00 57.23 O ANISOU 2384 O ILE A 342 7963 7621 6161 -384 -406 -843 O ATOM 2385 CB ILE A 342 34.560 21.459 8.526 1.00 54.67 C ANISOU 2385 CB ILE A 342 7530 7110 6132 -476 -253 -872 C ATOM 2386 CG1 ILE A 342 35.237 20.821 7.286 1.00 54.54 C ANISOU 2386 CG1 ILE A 342 7437 7105 6179 -410 -258 -812 C ATOM 2387 CG2 ILE A 342 35.623 21.980 9.514 1.00 56.79 C ANISOU 2387 CG2 ILE A 342 7698 7549 6328 -577 -311 -998 C ATOM 2388 CD1 ILE A 342 35.850 21.802 6.271 1.00 60.18 C ANISOU 2388 CD1 ILE A 342 8109 7770 6986 -520 -169 -866 C ATOM 2389 N THR A 343 32.246 21.839 10.772 1.00 54.85 N ANISOU 2389 N THR A 343 7773 7057 6011 -492 -218 -903 N ATOM 2390 CA THR A 343 31.727 22.357 12.057 1.00 55.99 C ANISOU 2390 CA THR A 343 7977 7233 6065 -551 -204 -984 C ATOM 2391 C THR A 343 31.014 21.239 12.829 1.00 61.06 C ANISOU 2391 C THR A 343 8681 7920 6601 -462 -243 -893 C ATOM 2392 O THR A 343 31.123 21.164 14.055 1.00 61.60 O ANISOU 2392 O THR A 343 8767 8104 6536 -487 -286 -934 O ATOM 2393 CB THR A 343 30.794 23.558 11.817 1.00 61.82 C ANISOU 2393 CB THR A 343 8793 7806 6888 -612 -82 -1051 C ATOM 2394 OG1 THR A 343 31.437 24.471 10.929 1.00 61.14 O ANISOU 2394 OG1 THR A 343 8675 7650 6906 -689 -36 -1104 O ATOM 2395 CG2 THR A 343 30.419 24.282 13.104 1.00 61.81 C ANISOU 2395 CG2 THR A 343 8845 7837 6802 -686 -52 -1169 C ATOM 2396 N ASN A 344 30.306 20.369 12.092 1.00 57.45 N ANISOU 2396 N ASN A 344 8262 7372 6195 -370 -225 -772 N ATOM 2397 CA ASN A 344 29.591 19.203 12.594 1.00 57.54 C ANISOU 2397 CA ASN A 344 8343 7392 6125 -297 -244 -669 C ATOM 2398 C ASN A 344 30.535 18.315 13.401 1.00 62.92 C ANISOU 2398 C ASN A 344 9006 8224 6676 -246 -360 -625 C ATOM 2399 O ASN A 344 30.272 18.054 14.574 1.00 63.33 O ANISOU 2399 O ASN A 344 9120 8351 6593 -252 -381 -617 O ATOM 2400 CB ASN A 344 29.025 18.431 11.409 1.00 58.15 C ANISOU 2400 CB ASN A 344 8440 7354 6301 -222 -216 -565 C ATOM 2401 CG ASN A 344 27.974 17.439 11.761 1.00 85.15 C ANISOU 2401 CG ASN A 344 11944 10737 9671 -184 -194 -478 C ATOM 2402 OD1 ASN A 344 26.906 17.791 12.274 1.00 82.21 O ANISOU 2402 OD1 ASN A 344 11617 10333 9284 -226 -119 -507 O ATOM 2403 ND2 ASN A 344 28.229 16.188 11.416 1.00 77.15 N ANISOU 2403 ND2 ASN A 344 10952 9718 8643 -106 -246 -374 N ATOM 2404 N ILE A 345 31.663 17.915 12.779 1.00 59.73 N ANISOU 2404 N ILE A 345 8515 7874 6307 -192 -435 -601 N ATOM 2405 CA ILE A 345 32.714 17.078 13.358 1.00 60.88 C ANISOU 2405 CA ILE A 345 8618 8168 6346 -110 -560 -558 C ATOM 2406 C ILE A 345 33.439 17.834 14.497 1.00 66.42 C ANISOU 2406 C ILE A 345 9261 9044 6931 -189 -622 -674 C ATOM 2407 O ILE A 345 33.797 17.204 15.497 1.00 67.37 O ANISOU 2407 O ILE A 345 9402 9296 6901 -132 -716 -635 O ATOM 2408 CB ILE A 345 33.659 16.606 12.214 1.00 63.76 C ANISOU 2408 CB ILE A 345 8883 8536 6807 -30 -600 -524 C ATOM 2409 CG1 ILE A 345 33.116 15.305 11.595 1.00 63.35 C ANISOU 2409 CG1 ILE A 345 8917 8365 6787 90 -591 -386 C ATOM 2410 CG2 ILE A 345 35.136 16.453 12.647 1.00 65.88 C ANISOU 2410 CG2 ILE A 345 9020 9006 7004 14 -724 -563 C ATOM 2411 CD1 ILE A 345 33.323 15.175 10.153 1.00 69.69 C ANISOU 2411 CD1 ILE A 345 9669 9085 7726 125 -555 -372 C ATOM 2412 N THR A 346 33.614 19.171 14.358 1.00 62.97 N ANISOU 2412 N THR A 346 8765 8603 6556 -321 -566 -815 N ATOM 2413 CA THR A 346 34.257 20.034 15.359 1.00 64.42 C ANISOU 2413 CA THR A 346 8894 8939 6645 -429 -608 -958 C ATOM 2414 C THR A 346 33.424 20.053 16.659 1.00 69.48 C ANISOU 2414 C THR A 346 9651 9610 7137 -455 -596 -971 C ATOM 2415 O THR A 346 33.991 19.904 17.737 1.00 70.15 O ANISOU 2415 O THR A 346 9715 9875 7061 -460 -692 -1007 O ATOM 2416 CB THR A 346 34.479 21.449 14.791 1.00 71.67 C ANISOU 2416 CB THR A 346 9761 9787 7684 -577 -520 -1100 C ATOM 2417 OG1 THR A 346 35.142 21.345 13.534 1.00 70.70 O ANISOU 2417 OG1 THR A 346 9547 9628 7689 -553 -514 -1070 O ATOM 2418 CG2 THR A 346 35.304 22.340 15.719 1.00 71.54 C ANISOU 2418 CG2 THR A 346 9672 9930 7581 -711 -565 -1270 C ATOM 2419 N LEU A 347 32.088 20.194 16.546 1.00 66.20 N ANISOU 2419 N LEU A 347 9350 9036 6767 -465 -479 -940 N ATOM 2420 CA LEU A 347 31.158 20.207 17.681 1.00 67.11 C ANISOU 2420 CA LEU A 347 9575 9171 6752 -492 -438 -954 C ATOM 2421 C LEU A 347 31.166 18.858 18.435 1.00 73.28 C ANISOU 2421 C LEU A 347 10423 10047 7373 -391 -521 -813 C ATOM 2422 O LEU A 347 31.018 18.844 19.658 1.00 74.96 O ANISOU 2422 O LEU A 347 10700 10369 7413 -421 -540 -838 O ATOM 2423 CB LEU A 347 29.735 20.551 17.186 1.00 65.85 C ANISOU 2423 CB LEU A 347 9493 8827 6702 -509 -291 -948 C ATOM 2424 CG LEU A 347 28.630 20.813 18.231 1.00 71.41 C ANISOU 2424 CG LEU A 347 10294 9539 7301 -555 -208 -996 C ATOM 2425 CD1 LEU A 347 29.004 21.933 19.203 1.00 72.95 C ANISOU 2425 CD1 LEU A 347 10481 9829 7406 -665 -204 -1174 C ATOM 2426 CD2 LEU A 347 27.325 21.174 17.552 1.00 73.28 C ANISOU 2426 CD2 LEU A 347 10566 9607 7670 -549 -73 -994 C ATOM 2427 N VAL A 348 31.374 17.744 17.709 1.00 69.59 N ANISOU 2427 N VAL A 348 9952 9534 6955 -273 -570 -669 N ATOM 2428 CA VAL A 348 31.405 16.387 18.253 1.00 70.40 C ANISOU 2428 CA VAL A 348 10141 9683 6927 -162 -643 -517 C ATOM 2429 C VAL A 348 32.762 16.115 18.930 1.00 77.34 C ANISOU 2429 C VAL A 348 10947 10768 7670 -97 -806 -519 C ATOM 2430 O VAL A 348 32.782 15.770 20.109 1.00 78.41 O ANISOU 2430 O VAL A 348 11158 11024 7610 -77 -866 -484 O ATOM 2431 CB VAL A 348 31.078 15.317 17.159 1.00 72.94 C ANISOU 2431 CB VAL A 348 10502 9846 7366 -61 -618 -374 C ATOM 2432 CG1 VAL A 348 31.258 13.896 17.689 1.00 73.77 C ANISOU 2432 CG1 VAL A 348 10711 9975 7344 62 -696 -213 C ATOM 2433 CG2 VAL A 348 29.667 15.499 16.604 1.00 71.21 C ANISOU 2433 CG2 VAL A 348 10348 9457 7254 -123 -471 -370 C ATOM 2434 N LEU A 349 33.879 16.257 18.187 1.00 75.15 N ANISOU 2434 N LEU A 349 10520 10546 7486 -61 -877 -560 N ATOM 2435 CA LEU A 349 35.229 15.950 18.672 1.00 77.26 C ANISOU 2435 CA LEU A 349 10680 11029 7647 19 -1041 -568 C ATOM 2436 C LEU A 349 35.781 16.952 19.704 1.00 85.04 C ANISOU 2436 C LEU A 349 11591 12217 8502 -99 -1098 -731 C ATOM 2437 O LEU A 349 36.369 16.513 20.695 1.00 87.05 O ANISOU 2437 O LEU A 349 11847 12661 8567 -33 -1228 -704 O ATOM 2438 CB LEU A 349 36.218 15.827 17.499 1.00 76.73 C ANISOU 2438 CB LEU A 349 10455 10968 7730 82 -1080 -579 C ATOM 2439 CG LEU A 349 36.096 14.586 16.598 1.00 80.17 C ANISOU 2439 CG LEU A 349 10942 11268 8251 245 -1079 -419 C ATOM 2440 CD1 LEU A 349 36.992 14.712 15.392 1.00 79.53 C ANISOU 2440 CD1 LEU A 349 10699 11194 8326 274 -1084 -466 C ATOM 2441 CD2 LEU A 349 36.461 13.310 17.346 1.00 84.51 C ANISOU 2441 CD2 LEU A 349 11563 11902 8646 425 -1206 -278 C ATOM 2442 N CYS A 350 35.634 18.272 19.470 1.00 82.08 N ANISOU 2442 N CYS A 350 11160 11805 8221 -269 -1008 -899 N ATOM 2443 CA CYS A 350 36.155 19.297 20.380 1.00 83.90 C ANISOU 2443 CA CYS A 350 11325 12211 8344 -406 -1048 -1080 C ATOM 2444 C CYS A 350 35.185 19.524 21.546 1.00 87.91 C ANISOU 2444 C CYS A 350 11987 12719 8695 -468 -993 -1104 C ATOM 2445 O CYS A 350 34.036 19.922 21.336 1.00 85.92 O ANISOU 2445 O CYS A 350 11840 12284 8523 -525 -845 -1111 O ATOM 2446 CB CYS A 350 36.455 20.594 19.631 1.00 84.19 C ANISOU 2446 CB CYS A 350 11259 12183 8547 -566 -963 -1250 C ATOM 2447 SG CYS A 350 37.177 21.908 20.653 1.00 90.66 S ANISOU 2447 SG CYS A 350 11993 13201 9254 -766 -1003 -1502 S ATOM 2448 N ASP A 351 35.664 19.253 22.774 1.00 86.79 N ANISOU 2448 N ASP A 351 11854 12800 8323 -447 -1117 -1116 N ATOM 2449 CA ASP A 351 34.910 19.409 24.023 1.00 87.56 C ANISOU 2449 CA ASP A 351 12093 12949 8225 -504 -1082 -1144 C ATOM 2450 C ASP A 351 35.185 20.772 24.667 1.00 92.33 C ANISOU 2450 C ASP A 351 12641 13668 8772 -688 -1067 -1389 C ATOM 2451 O ASP A 351 34.324 21.299 25.374 1.00 92.07 O ANISOU 2451 O ASP A 351 12723 13604 8657 -777 -969 -1466 O ATOM 2452 CB ASP A 351 35.255 18.280 25.005 1.00 91.05 C ANISOU 2452 CB ASP A 351 12605 13565 8425 -365 -1225 -998 C ATOM 2453 N SER A 352 36.384 21.336 24.415 1.00 89.65 N ANISOU 2453 N SER A 352 12124 13461 8479 -750 -1157 -1520 N ATOM 2454 CA SER A 352 36.834 22.636 24.928 1.00 90.81 C ANISOU 2454 CA SER A 352 12200 13717 8588 -945 -1151 -1771 C ATOM 2455 C SER A 352 36.202 23.814 24.168 1.00 92.93 C ANISOU 2455 C SER A 352 12500 13737 9074 -1091 -962 -1897 C ATOM 2456 O SER A 352 36.131 24.915 24.712 1.00 93.45 O ANISOU 2456 O SER A 352 12585 13816 9106 -1255 -903 -2100 O ATOM 2457 CB SER A 352 38.355 22.734 24.852 1.00 96.04 C ANISOU 2457 CB SER A 352 12646 14617 9228 -966 -1313 -1861 C ATOM 2458 OG SER A 352 38.831 22.416 23.554 1.00104.23 O ANISOU 2458 OG SER A 352 13568 15557 10476 -905 -1304 -1788 O ATOM 2459 N CYS A 353 35.756 23.583 22.917 1.00 87.46 N ANISOU 2459 N CYS A 353 11819 12816 8595 -1023 -869 -1780 N ATOM 2460 CA CYS A 353 35.132 24.580 22.040 1.00 86.05 C ANISOU 2460 CA CYS A 353 11680 12384 8629 -1119 -697 -1856 C ATOM 2461 C CYS A 353 33.791 25.058 22.604 1.00 87.37 C ANISOU 2461 C CYS A 353 12012 12418 8764 -1153 -559 -1898 C ATOM 2462 O CYS A 353 33.103 24.292 23.284 1.00 87.21 O ANISOU 2462 O CYS A 353 12087 12441 8609 -1066 -567 -1794 O ATOM 2463 CB CYS A 353 34.959 24.017 20.633 1.00 84.88 C ANISOU 2463 CB CYS A 353 11510 12062 8677 -1010 -656 -1695 C ATOM 2464 SG CYS A 353 36.511 23.625 19.783 1.00 89.43 S ANISOU 2464 SG CYS A 353 11881 12771 9328 -978 -780 -1671 S ATOM 2465 N ASN A 354 33.414 26.317 22.298 1.00 81.76 N ANISOU 2465 N ASN A 354 11341 11541 8182 -1276 -423 -2049 N ATOM 2466 CA ASN A 354 32.149 26.914 22.733 1.00 80.53 C ANISOU 2466 CA ASN A 354 11327 11247 8025 -1299 -276 -2114 C ATOM 2467 C ASN A 354 30.991 26.316 21.916 1.00 81.02 C ANISOU 2467 C ASN A 354 11453 11121 8209 -1161 -187 -1935 C ATOM 2468 O ASN A 354 30.851 26.598 20.721 1.00 79.23 O ANISOU 2468 O ASN A 354 11206 10717 8180 -1136 -129 -1886 O ATOM 2469 CB ASN A 354 32.194 28.439 22.622 1.00 79.80 C ANISOU 2469 CB ASN A 354 11260 11016 8044 -1453 -163 -2327 C ATOM 2470 CG ASN A 354 31.002 29.124 23.234 1.00 99.02 C ANISOU 2470 CG ASN A 354 13831 13341 10452 -1475 -21 -2432 C ATOM 2471 OD1 ASN A 354 29.937 29.226 22.625 1.00 92.44 O ANISOU 2471 OD1 ASN A 354 13067 12309 9747 -1392 99 -2365 O ATOM 2472 ND2 ASN A 354 31.155 29.612 24.453 1.00 92.68 N ANISOU 2472 ND2 ASN A 354 13060 12675 9478 -1583 -33 -2609 N ATOM 2473 N GLN A 355 30.186 25.464 22.576 1.00 76.17 N ANISOU 2473 N GLN A 355 10915 10561 7464 -1081 -179 -1836 N ATOM 2474 CA GLN A 355 29.050 24.735 22.001 1.00 73.57 C ANISOU 2474 CA GLN A 355 10640 10097 7215 -966 -103 -1673 C ATOM 2475 C GLN A 355 27.951 25.671 21.485 1.00 74.36 C ANISOU 2475 C GLN A 355 10790 9987 7478 -977 62 -1746 C ATOM 2476 O GLN A 355 27.341 25.367 20.462 1.00 71.73 O ANISOU 2476 O GLN A 355 10451 9510 7294 -894 110 -1633 O ATOM 2477 CB GLN A 355 28.453 23.758 23.033 1.00 75.70 C ANISOU 2477 CB GLN A 355 10990 10487 7284 -917 -116 -1579 C ATOM 2478 CG GLN A 355 29.459 22.788 23.662 1.00 94.97 C ANISOU 2478 CG GLN A 355 13409 13136 9539 -878 -285 -1488 C ATOM 2479 CD GLN A 355 29.951 21.743 22.695 1.00117.74 C ANISOU 2479 CD GLN A 355 16240 15982 12514 -761 -370 -1304 C ATOM 2480 OE1 GLN A 355 29.257 20.767 22.394 1.00114.12 O ANISOU 2480 OE1 GLN A 355 15842 15445 12073 -675 -338 -1143 O ATOM 2481 NE2 GLN A 355 31.165 21.919 22.195 1.00111.26 N ANISOU 2481 NE2 GLN A 355 15301 15218 11754 -764 -474 -1334 N ATOM 2482 N THR A 356 27.714 26.802 22.181 1.00 71.16 N ANISOU 2482 N THR A 356 10433 9565 7039 -1070 144 -1937 N ATOM 2483 CA THR A 356 26.698 27.805 21.831 1.00 70.31 C ANISOU 2483 CA THR A 356 10381 9259 7075 -1064 302 -2028 C ATOM 2484 C THR A 356 27.016 28.487 20.488 1.00 71.44 C ANISOU 2484 C THR A 356 10493 9209 7441 -1061 327 -2023 C ATOM 2485 O THR A 356 26.122 28.629 19.650 1.00 69.91 O ANISOU 2485 O THR A 356 10319 8848 7394 -973 411 -1960 O ATOM 2486 CB THR A 356 26.572 28.858 22.947 1.00 81.92 C ANISOU 2486 CB THR A 356 11918 10761 8445 -1168 376 -2252 C ATOM 2487 OG1 THR A 356 26.741 28.246 24.230 1.00 83.82 O ANISOU 2487 OG1 THR A 356 12181 11228 8440 -1199 317 -2263 O ATOM 2488 CG2 THR A 356 25.258 29.626 22.881 1.00 80.65 C ANISOU 2488 CG2 THR A 356 11826 10427 8390 -1119 547 -2330 C ATOM 2489 N THR A 357 28.281 28.918 20.301 1.00 67.09 N ANISOU 2489 N THR A 357 9892 8694 6906 -1160 254 -2090 N ATOM 2490 CA THR A 357 28.753 29.597 19.094 1.00 65.46 C ANISOU 2490 CA THR A 357 9663 8320 6887 -1188 282 -2091 C ATOM 2491 C THR A 357 28.784 28.631 17.905 1.00 65.34 C ANISOU 2491 C THR A 357 9588 8271 6969 -1074 232 -1884 C ATOM 2492 O THR A 357 28.416 29.035 16.802 1.00 63.87 O ANISOU 2492 O THR A 357 9424 7898 6945 -1029 300 -1836 O ATOM 2493 CB THR A 357 30.124 30.238 19.337 1.00 73.11 C ANISOU 2493 CB THR A 357 10579 9374 7825 -1351 223 -2232 C ATOM 2494 N LEU A 358 29.190 27.359 18.128 1.00 60.05 N ANISOU 2494 N LEU A 358 8853 7771 6192 -1019 114 -1763 N ATOM 2495 CA LEU A 358 29.251 26.350 17.064 1.00 57.85 C ANISOU 2495 CA LEU A 358 8523 7465 5991 -911 65 -1578 C ATOM 2496 C LEU A 358 27.852 25.944 16.571 1.00 60.61 C ANISOU 2496 C LEU A 358 8928 7691 6411 -797 143 -1471 C ATOM 2497 O LEU A 358 27.697 25.647 15.388 1.00 59.09 O ANISOU 2497 O LEU A 358 8714 7398 6340 -727 150 -1363 O ATOM 2498 CB LEU A 358 30.037 25.107 17.501 1.00 57.78 C ANISOU 2498 CB LEU A 358 8449 7657 5849 -869 -77 -1485 C ATOM 2499 CG LEU A 358 31.559 25.241 17.634 1.00 63.17 C ANISOU 2499 CG LEU A 358 9026 8490 6486 -947 -184 -1556 C ATOM 2500 CD1 LEU A 358 32.150 23.984 18.235 1.00 63.63 C ANISOU 2500 CD1 LEU A 358 9038 8753 6387 -870 -326 -1462 C ATOM 2501 CD2 LEU A 358 32.223 25.510 16.290 1.00 64.48 C ANISOU 2501 CD2 LEU A 358 9117 8568 6816 -959 -176 -1530 C ATOM 2502 N GLN A 359 26.841 25.947 17.463 1.00 57.93 N ANISOU 2502 N GLN A 359 8650 7372 5988 -784 206 -1508 N ATOM 2503 CA GLN A 359 25.452 25.634 17.116 1.00 57.28 C ANISOU 2503 CA GLN A 359 8598 7199 5965 -692 290 -1435 C ATOM 2504 C GLN A 359 24.857 26.755 16.250 1.00 63.09 C ANISOU 2504 C GLN A 359 9356 7740 6873 -665 390 -1489 C ATOM 2505 O GLN A 359 24.182 26.475 15.262 1.00 61.20 O ANISOU 2505 O GLN A 359 9102 7409 6742 -574 414 -1390 O ATOM 2506 CB GLN A 359 24.615 25.407 18.379 1.00 59.42 C ANISOU 2506 CB GLN A 359 8919 7566 6092 -704 342 -1481 C ATOM 2507 CG GLN A 359 24.725 23.980 18.922 1.00 72.01 C ANISOU 2507 CG GLN A 359 10517 9305 7540 -681 265 -1351 C ATOM 2508 CD GLN A 359 24.261 23.833 20.352 1.00 92.76 C ANISOU 2508 CD GLN A 359 13205 12060 9979 -726 305 -1408 C ATOM 2509 OE1 GLN A 359 24.930 23.202 21.175 1.00 89.59 O ANISOU 2509 OE1 GLN A 359 12825 11809 9404 -754 217 -1380 O ATOM 2510 NE2 GLN A 359 23.103 24.393 20.685 1.00 85.58 N ANISOU 2510 NE2 GLN A 359 12324 11103 9089 -724 437 -1487 N ATOM 2511 N MET A 360 25.169 28.021 16.593 1.00 63.32 N ANISOU 2511 N MET A 360 9428 7705 6924 -743 443 -1646 N ATOM 2512 CA MET A 360 24.757 29.233 15.874 1.00 64.28 C ANISOU 2512 CA MET A 360 9602 7621 7201 -720 540 -1707 C ATOM 2513 C MET A 360 25.305 29.203 14.431 1.00 66.91 C ANISOU 2513 C MET A 360 9908 7852 7663 -693 505 -1597 C ATOM 2514 O MET A 360 24.572 29.535 13.497 1.00 66.31 O ANISOU 2514 O MET A 360 9857 7630 7708 -598 559 -1539 O ATOM 2515 CB MET A 360 25.249 30.476 16.647 1.00 68.97 C ANISOU 2515 CB MET A 360 10261 8175 7771 -841 593 -1905 C ATOM 2516 CG MET A 360 24.972 31.813 15.962 1.00 74.12 C ANISOU 2516 CG MET A 360 10998 8583 8580 -826 700 -1974 C ATOM 2517 SD MET A 360 26.391 32.454 15.024 1.00 79.08 S ANISOU 2517 SD MET A 360 11634 9106 9306 -945 675 -1975 S ATOM 2518 CE MET A 360 27.415 33.067 16.355 1.00 77.69 C ANISOU 2518 CE MET A 360 11470 9041 9009 -1152 662 -2195 C ATOM 2519 N LEU A 361 26.580 28.782 14.258 1.00 62.63 N ANISOU 2519 N LEU A 361 9309 7403 7087 -769 412 -1568 N ATOM 2520 CA LEU A 361 27.239 28.674 12.951 1.00 61.10 C ANISOU 2520 CA LEU A 361 9079 7144 6994 -759 382 -1471 C ATOM 2521 C LEU A 361 26.618 27.550 12.125 1.00 63.16 C ANISOU 2521 C LEU A 361 9302 7413 7284 -629 345 -1302 C ATOM 2522 O LEU A 361 26.384 27.736 10.932 1.00 61.89 O ANISOU 2522 O LEU A 361 9153 7131 7232 -572 371 -1227 O ATOM 2523 CB LEU A 361 28.763 28.453 13.100 1.00 61.35 C ANISOU 2523 CB LEU A 361 9032 7308 6969 -871 294 -1503 C ATOM 2524 CG LEU A 361 29.567 29.573 13.785 1.00 67.29 C ANISOU 2524 CG LEU A 361 9805 8061 7702 -1034 324 -1684 C ATOM 2525 CD1 LEU A 361 30.884 29.057 14.304 1.00 67.94 C ANISOU 2525 CD1 LEU A 361 9775 8360 7678 -1124 210 -1723 C ATOM 2526 CD2 LEU A 361 29.777 30.775 12.869 1.00 69.73 C ANISOU 2526 CD2 LEU A 361 10177 8163 8154 -1097 419 -1719 C ATOM 2527 N LEU A 362 26.323 26.400 12.768 1.00 59.94 N ANISOU 2527 N LEU A 362 8860 7141 6773 -588 290 -1244 N ATOM 2528 CA LEU A 362 25.706 25.232 12.131 1.00 58.84 C ANISOU 2528 CA LEU A 362 8692 7013 6650 -485 259 -1099 C ATOM 2529 C LEU A 362 24.365 25.582 11.498 1.00 63.05 C ANISOU 2529 C LEU A 362 9253 7424 7279 -398 339 -1074 C ATOM 2530 O LEU A 362 24.092 25.115 10.398 1.00 62.13 O ANISOU 2530 O LEU A 362 9114 7261 7232 -329 322 -972 O ATOM 2531 CB LEU A 362 25.510 24.080 13.132 1.00 58.99 C ANISOU 2531 CB LEU A 362 8703 7178 6533 -476 210 -1056 C ATOM 2532 CG LEU A 362 26.556 22.962 13.178 1.00 63.55 C ANISOU 2532 CG LEU A 362 9238 7875 7034 -476 97 -980 C ATOM 2533 CD1 LEU A 362 26.061 21.819 14.035 1.00 64.35 C ANISOU 2533 CD1 LEU A 362 9368 8077 7004 -451 68 -916 C ATOM 2534 CD2 LEU A 362 26.865 22.406 11.796 1.00 64.10 C ANISOU 2534 CD2 LEU A 362 9268 7889 7199 -414 62 -871 C ATOM 2535 N GLU A 363 23.548 26.419 12.184 1.00 60.63 N ANISOU 2535 N GLU A 363 8989 7074 6973 -395 423 -1176 N ATOM 2536 CA GLU A 363 22.235 26.897 11.733 1.00 60.58 C ANISOU 2536 CA GLU A 363 8996 6967 7055 -296 501 -1176 C ATOM 2537 C GLU A 363 22.363 27.644 10.387 1.00 63.79 C ANISOU 2537 C GLU A 363 9430 7216 7592 -243 514 -1133 C ATOM 2538 O GLU A 363 21.519 27.459 9.507 1.00 63.12 O ANISOU 2538 O GLU A 363 9323 7087 7575 -137 519 -1056 O ATOM 2539 CB GLU A 363 21.601 27.797 12.815 1.00 63.51 C ANISOU 2539 CB GLU A 363 9411 7321 7398 -307 593 -1320 C ATOM 2540 CG GLU A 363 20.201 28.307 12.504 1.00 77.36 C ANISOU 2540 CG GLU A 363 11160 8998 9236 -185 676 -1336 C ATOM 2541 CD GLU A 363 19.075 27.318 12.724 1.00105.56 C ANISOU 2541 CD GLU A 363 14656 12687 12765 -135 684 -1285 C ATOM 2542 OE1 GLU A 363 18.494 26.852 11.718 1.00105.66 O ANISOU 2542 OE1 GLU A 363 14614 12686 12847 -53 659 -1188 O ATOM 2543 OE2 GLU A 363 18.755 27.029 13.900 1.00103.08 O ANISOU 2543 OE2 GLU A 363 14339 12483 12343 -187 721 -1349 O ATOM 2544 N ILE A 364 23.432 28.450 10.221 1.00 60.00 N ANISOU 2544 N ILE A 364 8997 6663 7139 -324 519 -1181 N ATOM 2545 CA ILE A 364 23.695 29.195 8.984 1.00 59.27 C ANISOU 2545 CA ILE A 364 8953 6413 7153 -299 542 -1136 C ATOM 2546 C ILE A 364 24.218 28.222 7.905 1.00 59.94 C ANISOU 2546 C ILE A 364 8979 6551 7243 -282 465 -1001 C ATOM 2547 O ILE A 364 23.759 28.277 6.760 1.00 59.43 O ANISOU 2547 O ILE A 364 8929 6406 7246 -194 470 -913 O ATOM 2548 CB ILE A 364 24.674 30.393 9.221 1.00 63.53 C ANISOU 2548 CB ILE A 364 9568 6854 7715 -424 591 -1245 C ATOM 2549 CG1 ILE A 364 24.132 31.373 10.278 1.00 64.62 C ANISOU 2549 CG1 ILE A 364 9778 6929 7846 -440 675 -1396 C ATOM 2550 CG2 ILE A 364 24.990 31.138 7.907 1.00 65.26 C ANISOU 2550 CG2 ILE A 364 9861 6899 8037 -411 630 -1182 C ATOM 2551 CD1 ILE A 364 25.201 31.988 11.160 1.00 71.05 C ANISOU 2551 CD1 ILE A 364 10620 7768 8607 -614 687 -1541 C ATOM 2552 N PHE A 365 25.146 27.321 8.289 1.00 54.21 N ANISOU 2552 N PHE A 365 8189 5968 6441 -355 392 -990 N ATOM 2553 CA PHE A 365 25.796 26.360 7.387 1.00 52.10 C ANISOU 2553 CA PHE A 365 7864 5759 6172 -343 323 -883 C ATOM 2554 C PHE A 365 24.829 25.330 6.807 1.00 54.58 C ANISOU 2554 C PHE A 365 8148 6101 6491 -233 292 -779 C ATOM 2555 O PHE A 365 25.062 24.858 5.688 1.00 53.95 O ANISOU 2555 O PHE A 365 8048 6011 6440 -197 261 -693 O ATOM 2556 CB PHE A 365 26.971 25.667 8.081 1.00 53.45 C ANISOU 2556 CB PHE A 365 7972 6079 6257 -424 251 -908 C ATOM 2557 CG PHE A 365 28.104 26.589 8.476 1.00 55.67 C ANISOU 2557 CG PHE A 365 8253 6364 6533 -553 266 -1016 C ATOM 2558 CD1 PHE A 365 28.269 27.826 7.859 1.00 59.37 C ANISOU 2558 CD1 PHE A 365 8787 6684 7089 -604 345 -1055 C ATOM 2559 CD2 PHE A 365 29.033 26.202 9.429 1.00 58.11 C ANISOU 2559 CD2 PHE A 365 8502 6830 6749 -627 200 -1077 C ATOM 2560 CE1 PHE A 365 29.322 28.667 8.213 1.00 61.36 C ANISOU 2560 CE1 PHE A 365 9039 6936 7341 -750 369 -1167 C ATOM 2561 CE2 PHE A 365 30.090 27.043 9.778 1.00 62.17 C ANISOU 2561 CE2 PHE A 365 8996 7369 7256 -763 210 -1193 C ATOM 2562 CZ PHE A 365 30.226 28.270 9.170 1.00 61.01 C ANISOU 2562 CZ PHE A 365 8911 7066 7203 -835 300 -1243 C ATOM 2563 N VAL A 366 23.741 25.005 7.541 1.00 50.03 N ANISOU 2563 N VAL A 366 7565 5562 5881 -191 309 -796 N ATOM 2564 CA VAL A 366 22.672 24.106 7.085 1.00 48.66 C ANISOU 2564 CA VAL A 366 7355 5418 5715 -110 293 -720 C ATOM 2565 C VAL A 366 22.016 24.770 5.855 1.00 51.87 C ANISOU 2565 C VAL A 366 7777 5717 6214 -20 319 -681 C ATOM 2566 O VAL A 366 21.791 24.106 4.837 1.00 50.67 O ANISOU 2566 O VAL A 366 7597 5575 6081 29 280 -598 O ATOM 2567 CB VAL A 366 21.645 23.801 8.228 1.00 52.81 C ANISOU 2567 CB VAL A 366 7867 6014 6184 -108 328 -766 C ATOM 2568 CG1 VAL A 366 20.335 23.235 7.687 1.00 52.12 C ANISOU 2568 CG1 VAL A 366 7733 5940 6130 -33 339 -717 C ATOM 2569 CG2 VAL A 366 22.231 22.850 9.264 1.00 52.65 C ANISOU 2569 CG2 VAL A 366 7843 6109 6051 -178 286 -760 C ATOM 2570 N TRP A 367 21.787 26.101 5.938 1.00 48.81 N ANISOU 2570 N TRP A 367 7445 5223 5879 2 383 -742 N ATOM 2571 CA TRP A 367 21.161 26.880 4.876 1.00 48.70 C ANISOU 2571 CA TRP A 367 7466 5093 5943 107 409 -702 C ATOM 2572 C TRP A 367 22.086 27.080 3.669 1.00 53.81 C ANISOU 2572 C TRP A 367 8158 5669 6619 90 390 -627 C ATOM 2573 O TRP A 367 21.582 27.043 2.545 1.00 53.25 O ANISOU 2573 O TRP A 367 8092 5562 6578 183 372 -548 O ATOM 2574 CB TRP A 367 20.606 28.206 5.406 1.00 48.03 C ANISOU 2574 CB TRP A 367 7446 4899 5905 150 490 -790 C ATOM 2575 CG TRP A 367 19.335 27.971 6.162 1.00 49.03 C ANISOU 2575 CG TRP A 367 7510 5100 6018 216 516 -843 C ATOM 2576 CD1 TRP A 367 19.203 27.831 7.513 1.00 52.21 C ANISOU 2576 CD1 TRP A 367 7896 5579 6362 152 552 -939 C ATOM 2577 CD2 TRP A 367 18.059 27.627 5.597 1.00 48.77 C ANISOU 2577 CD2 TRP A 367 7403 5111 6015 342 503 -801 C ATOM 2578 NE1 TRP A 367 17.906 27.494 7.831 1.00 51.86 N ANISOU 2578 NE1 TRP A 367 7777 5611 6315 227 579 -961 N ATOM 2579 CE2 TRP A 367 17.181 27.363 6.673 1.00 53.00 C ANISOU 2579 CE2 TRP A 367 7875 5742 6520 343 547 -882 C ATOM 2580 CE3 TRP A 367 17.557 27.560 4.283 1.00 49.76 C ANISOU 2580 CE3 TRP A 367 7506 5215 6184 453 459 -709 C ATOM 2581 CZ2 TRP A 367 15.828 27.057 6.477 1.00 52.60 C ANISOU 2581 CZ2 TRP A 367 7724 5769 6493 445 554 -882 C ATOM 2582 CZ3 TRP A 367 16.220 27.243 4.091 1.00 51.39 C ANISOU 2582 CZ3 TRP A 367 7613 5506 6409 560 450 -709 C ATOM 2583 CH2 TRP A 367 15.374 26.985 5.178 1.00 52.47 C ANISOU 2583 CH2 TRP A 367 7671 5740 6525 552 499 -798 C ATOM 2584 N ILE A 368 23.423 27.209 3.878 1.00 50.96 N ANISOU 2584 N ILE A 368 7816 5308 6237 -29 390 -654 N ATOM 2585 CA ILE A 368 24.391 27.331 2.773 1.00 51.07 C ANISOU 2585 CA ILE A 368 7858 5278 6270 -67 386 -593 C ATOM 2586 C ILE A 368 24.389 25.990 1.976 1.00 54.74 C ANISOU 2586 C ILE A 368 8251 5845 6703 -26 313 -503 C ATOM 2587 O ILE A 368 24.466 26.003 0.742 1.00 53.48 O ANISOU 2587 O ILE A 368 8115 5646 6558 14 309 -426 O ATOM 2588 CB ILE A 368 25.811 27.763 3.271 1.00 54.74 C ANISOU 2588 CB ILE A 368 8331 5747 6722 -218 408 -665 C ATOM 2589 CG1 ILE A 368 25.776 29.201 3.837 1.00 56.70 C ANISOU 2589 CG1 ILE A 368 8675 5859 7010 -267 492 -760 C ATOM 2590 CG2 ILE A 368 26.868 27.669 2.154 1.00 55.06 C ANISOU 2590 CG2 ILE A 368 8369 5780 6771 -270 408 -605 C ATOM 2591 CD1 ILE A 368 26.899 29.543 4.820 1.00 65.82 C ANISOU 2591 CD1 ILE A 368 9815 7058 8134 -430 505 -878 C ATOM 2592 N GLY A 369 24.236 24.874 2.699 1.00 51.95 N ANISOU 2592 N GLY A 369 7827 5613 6300 -34 264 -514 N ATOM 2593 CA GLY A 369 24.142 23.532 2.132 1.00 51.52 C ANISOU 2593 CA GLY A 369 7718 5641 6217 1 203 -446 C ATOM 2594 C GLY A 369 22.881 23.352 1.309 1.00 56.63 C ANISOU 2594 C GLY A 369 8359 6270 6886 101 195 -396 C ATOM 2595 O GLY A 369 22.934 22.771 0.223 1.00 55.93 O ANISOU 2595 O GLY A 369 8259 6200 6793 134 160 -334 O ATOM 2596 N TYR A 370 21.739 23.883 1.809 1.00 54.61 N ANISOU 2596 N TYR A 370 8105 5992 6653 153 226 -433 N ATOM 2597 CA TYR A 370 20.441 23.861 1.125 1.00 55.07 C ANISOU 2597 CA TYR A 370 8134 6054 6736 259 214 -403 C ATOM 2598 C TYR A 370 20.499 24.631 -0.204 1.00 62.45 C ANISOU 2598 C TYR A 370 9125 6901 7700 332 213 -338 C ATOM 2599 O TYR A 370 19.874 24.197 -1.174 1.00 62.87 O ANISOU 2599 O TYR A 370 9147 6994 7745 404 168 -286 O ATOM 2600 CB TYR A 370 19.343 24.455 2.016 1.00 56.48 C ANISOU 2600 CB TYR A 370 8293 6231 6937 305 260 -471 C ATOM 2601 CG TYR A 370 18.862 23.584 3.160 1.00 57.13 C ANISOU 2601 CG TYR A 370 8311 6420 6977 252 266 -520 C ATOM 2602 CD1 TYR A 370 19.097 22.210 3.169 1.00 57.73 C ANISOU 2602 CD1 TYR A 370 8352 6578 7005 192 221 -484 C ATOM 2603 CD2 TYR A 370 18.119 24.124 4.204 1.00 58.59 C ANISOU 2603 CD2 TYR A 370 8480 6617 7165 265 325 -601 C ATOM 2604 CE1 TYR A 370 18.649 21.408 4.216 1.00 57.60 C ANISOU 2604 CE1 TYR A 370 8301 6644 6941 136 237 -514 C ATOM 2605 CE2 TYR A 370 17.652 23.330 5.247 1.00 59.42 C ANISOU 2605 CE2 TYR A 370 8535 6824 7217 207 343 -639 C ATOM 2606 CZ TYR A 370 17.922 21.973 5.251 1.00 65.91 C ANISOU 2606 CZ TYR A 370 9336 7718 7988 138 300 -589 C ATOM 2607 OH TYR A 370 17.465 21.206 6.291 1.00 67.99 O ANISOU 2607 OH TYR A 370 9576 8067 8192 72 328 -614 O ATOM 2608 N VAL A 371 21.249 25.767 -0.244 1.00 60.43 N ANISOU 2608 N VAL A 371 8960 6530 7471 306 263 -342 N ATOM 2609 CA VAL A 371 21.485 26.582 -1.448 1.00 61.42 C ANISOU 2609 CA VAL A 371 9173 6551 7612 357 278 -269 C ATOM 2610 C VAL A 371 22.269 25.731 -2.457 1.00 65.55 C ANISOU 2610 C VAL A 371 9680 7134 8092 315 239 -205 C ATOM 2611 O VAL A 371 21.878 25.627 -3.619 1.00 65.01 O ANISOU 2611 O VAL A 371 9627 7073 8003 392 208 -132 O ATOM 2612 CB VAL A 371 22.255 27.907 -1.139 1.00 66.70 C ANISOU 2612 CB VAL A 371 9956 7069 8319 298 360 -298 C ATOM 2613 CG1 VAL A 371 22.402 28.775 -2.387 1.00 67.40 C ANISOU 2613 CG1 VAL A 371 10159 7033 8417 348 387 -205 C ATOM 2614 CG2 VAL A 371 21.602 28.700 -0.020 1.00 67.64 C ANISOU 2614 CG2 VAL A 371 10098 7123 8480 333 407 -383 C ATOM 2615 N SER A 372 23.380 25.121 -1.974 1.00 62.31 N ANISOU 2615 N SER A 372 9235 6780 7661 200 238 -239 N ATOM 2616 CA SER A 372 24.324 24.280 -2.707 1.00 61.69 C ANISOU 2616 CA SER A 372 9128 6765 7546 154 213 -203 C ATOM 2617 C SER A 372 23.623 23.162 -3.462 1.00 65.56 C ANISOU 2617 C SER A 372 9571 7335 8003 224 150 -161 C ATOM 2618 O SER A 372 23.831 23.034 -4.661 1.00 65.39 O ANISOU 2618 O SER A 372 9574 7316 7954 249 141 -105 O ATOM 2619 CB SER A 372 25.353 23.690 -1.751 1.00 64.89 C ANISOU 2619 CB SER A 372 9476 7242 7937 57 206 -262 C ATOM 2620 OG SER A 372 26.439 23.125 -2.462 1.00 74.36 O ANISOU 2620 OG SER A 372 10651 8491 9113 19 198 -238 O ATOM 2621 N SER A 373 22.786 22.375 -2.775 1.00 62.30 N ANISOU 2621 N SER A 373 9095 6988 7587 243 114 -194 N ATOM 2622 CA SER A 373 22.038 21.285 -3.393 1.00 61.69 C ANISOU 2622 CA SER A 373 8970 6986 7484 285 59 -174 C ATOM 2623 C SER A 373 20.887 21.836 -4.233 1.00 67.22 C ANISOU 2623 C SER A 373 9674 7677 8187 387 40 -141 C ATOM 2624 O SER A 373 20.639 21.322 -5.323 1.00 68.02 O ANISOU 2624 O SER A 373 9766 7825 8252 422 -3 -107 O ATOM 2625 CB SER A 373 21.521 20.316 -2.332 1.00 63.15 C ANISOU 2625 CB SER A 373 9096 7234 7663 251 43 -220 C ATOM 2626 OG SER A 373 22.583 19.601 -1.723 1.00 64.67 O ANISOU 2626 OG SER A 373 9288 7448 7836 183 40 -232 O ATOM 2627 N GLY A 374 20.244 22.896 -3.740 1.00 63.67 N ANISOU 2627 N GLY A 374 9243 7173 7776 440 69 -156 N ATOM 2628 CA GLY A 374 19.104 23.555 -4.367 1.00 64.11 C ANISOU 2628 CA GLY A 374 9296 7221 7841 566 47 -127 C ATOM 2629 C GLY A 374 19.303 24.051 -5.783 1.00 68.36 C ANISOU 2629 C GLY A 374 9909 7721 8344 632 28 -40 C ATOM 2630 O GLY A 374 18.490 23.737 -6.655 1.00 68.85 O ANISOU 2630 O GLY A 374 9932 7860 8368 710 -36 -11 O ATOM 2631 N VAL A 375 20.378 24.826 -6.027 1.00 64.60 N ANISOU 2631 N VAL A 375 9541 7134 7870 592 84 -1 N ATOM 2632 CA VAL A 375 20.669 25.409 -7.351 1.00 64.83 C ANISOU 2632 CA VAL A 375 9670 7109 7854 643 87 94 C ATOM 2633 C VAL A 375 21.654 24.535 -8.177 1.00 66.31 C ANISOU 2633 C VAL A 375 9858 7359 7979 560 81 117 C ATOM 2634 O VAL A 375 21.870 24.818 -9.358 1.00 66.33 O ANISOU 2634 O VAL A 375 9939 7342 7923 591 85 195 O ATOM 2635 CB VAL A 375 21.165 26.890 -7.267 1.00 70.11 C ANISOU 2635 CB VAL A 375 10478 7603 8559 646 170 131 C ATOM 2636 CG1 VAL A 375 20.135 27.786 -6.581 1.00 70.99 C ANISOU 2636 CG1 VAL A 375 10602 7642 8730 760 177 107 C ATOM 2637 CG2 VAL A 375 22.536 27.014 -6.595 1.00 69.44 C ANISOU 2637 CG2 VAL A 375 10418 7464 8503 484 247 80 C ATOM 2638 N ASN A 376 22.224 23.482 -7.559 1.00 61.18 N ANISOU 2638 N ASN A 376 9127 6784 7335 467 73 53 N ATOM 2639 CA ASN A 376 23.206 22.570 -8.156 1.00 60.35 C ANISOU 2639 CA ASN A 376 9009 6739 7185 398 74 54 C ATOM 2640 C ASN A 376 22.810 22.043 -9.567 1.00 64.08 C ANISOU 2640 C ASN A 376 9491 7281 7577 458 23 99 C ATOM 2641 O ASN A 376 23.608 22.274 -10.482 1.00 64.51 O ANISOU 2641 O ASN A 376 9610 7321 7580 438 60 146 O ATOM 2642 CB ASN A 376 23.507 21.389 -7.219 1.00 60.02 C ANISOU 2642 CB ASN A 376 8878 6761 7164 332 55 -19 C ATOM 2643 CG ASN A 376 24.261 20.233 -7.839 1.00 83.89 C ANISOU 2643 CG ASN A 376 11873 9853 10148 296 41 -32 C ATOM 2644 OD1 ASN A 376 23.840 19.077 -7.736 1.00 75.48 O ANISOU 2644 OD1 ASN A 376 10755 8840 9084 286 3 -72 O ATOM 2645 ND2 ASN A 376 25.414 20.509 -8.452 1.00 78.13 N ANISOU 2645 ND2 ASN A 376 11185 9119 9383 273 81 -1 N ATOM 2646 N PRO A 377 21.675 21.307 -9.790 1.00 58.76 N ANISOU 2646 N PRO A 377 8752 6694 6881 516 -54 79 N ATOM 2647 CA PRO A 377 21.406 20.799 -11.149 1.00 58.41 C ANISOU 2647 CA PRO A 377 8719 6728 6746 558 -104 107 C ATOM 2648 C PRO A 377 21.171 21.916 -12.174 1.00 62.36 C ANISOU 2648 C PRO A 377 9316 7192 7187 647 -105 203 C ATOM 2649 O PRO A 377 21.640 21.787 -13.306 1.00 62.41 O ANISOU 2649 O PRO A 377 9380 7227 7104 644 -100 246 O ATOM 2650 CB PRO A 377 20.160 19.913 -10.977 1.00 59.84 C ANISOU 2650 CB PRO A 377 8799 7009 6929 584 -183 48 C ATOM 2651 CG PRO A 377 20.047 19.669 -9.529 1.00 63.50 C ANISOU 2651 CG PRO A 377 9204 7447 7478 529 -158 -11 C ATOM 2652 CD PRO A 377 20.616 20.876 -8.854 1.00 59.38 C ANISOU 2652 CD PRO A 377 8740 6816 7006 531 -93 19 C ATOM 2653 N LEU A 378 20.479 23.011 -11.772 1.00 58.29 N ANISOU 2653 N LEU A 378 8831 6603 6715 728 -102 241 N ATOM 2654 CA LEU A 378 20.175 24.148 -12.645 1.00 58.90 C ANISOU 2654 CA LEU A 378 9022 6618 6740 837 -104 347 C ATOM 2655 C LEU A 378 21.454 24.794 -13.206 1.00 61.64 C ANISOU 2655 C LEU A 378 9506 6863 7051 767 -8 417 C ATOM 2656 O LEU A 378 21.550 24.955 -14.425 1.00 61.75 O ANISOU 2656 O LEU A 378 9604 6897 6959 806 -17 498 O ATOM 2657 CB LEU A 378 19.316 25.207 -11.919 1.00 59.55 C ANISOU 2657 CB LEU A 378 9115 6614 6897 942 -103 359 C ATOM 2658 CG LEU A 378 18.923 26.442 -12.747 1.00 65.93 C ANISOU 2658 CG LEU A 378 10056 7335 7660 1090 -111 479 C ATOM 2659 CD1 LEU A 378 17.800 26.129 -13.721 1.00 67.12 C ANISOU 2659 CD1 LEU A 378 10152 7633 7719 1232 -234 514 C ATOM 2660 CD2 LEU A 378 18.542 27.600 -11.857 1.00 69.06 C ANISOU 2660 CD2 LEU A 378 10496 7589 8153 1166 -68 479 C ATOM 2661 N VAL A 379 22.427 25.133 -12.323 1.00 56.32 N ANISOU 2661 N VAL A 379 8849 6096 6456 654 83 380 N ATOM 2662 CA VAL A 379 23.705 25.770 -12.674 1.00 55.83 C ANISOU 2662 CA VAL A 379 8893 5942 6379 553 190 423 C ATOM 2663 C VAL A 379 24.450 24.925 -13.727 1.00 58.59 C ANISOU 2663 C VAL A 379 9232 6396 6633 496 199 430 C ATOM 2664 O VAL A 379 24.863 25.465 -14.750 1.00 59.06 O ANISOU 2664 O VAL A 379 9407 6422 6612 488 252 515 O ATOM 2665 CB VAL A 379 24.580 26.048 -11.412 1.00 58.27 C ANISOU 2665 CB VAL A 379 9171 6179 6789 427 266 345 C ATOM 2666 CG1 VAL A 379 26.027 26.382 -11.781 1.00 58.21 C ANISOU 2666 CG1 VAL A 379 9219 6133 6764 289 374 358 C ATOM 2667 CG2 VAL A 379 23.977 27.165 -10.562 1.00 58.43 C ANISOU 2667 CG2 VAL A 379 9248 6064 6888 476 288 346 C ATOM 2668 N TYR A 380 24.555 23.608 -13.493 1.00 53.45 N ANISOU 2668 N TYR A 380 8456 5865 5987 462 153 342 N ATOM 2669 CA TYR A 380 25.233 22.642 -14.359 1.00 52.98 C ANISOU 2669 CA TYR A 380 8372 5907 5850 418 161 321 C ATOM 2670 C TYR A 380 24.567 22.545 -15.760 1.00 57.01 C ANISOU 2670 C TYR A 380 8945 6488 6230 504 106 385 C ATOM 2671 O TYR A 380 25.264 22.647 -16.775 1.00 56.90 O ANISOU 2671 O TYR A 380 9001 6497 6121 472 162 427 O ATOM 2672 CB TYR A 380 25.269 21.264 -13.653 1.00 52.66 C ANISOU 2672 CB TYR A 380 8202 5949 5859 386 116 212 C ATOM 2673 CG TYR A 380 25.931 20.142 -14.428 1.00 54.32 C ANISOU 2673 CG TYR A 380 8384 6253 6004 356 123 169 C ATOM 2674 CD1 TYR A 380 27.278 20.207 -14.781 1.00 56.61 C ANISOU 2674 CD1 TYR A 380 8684 6548 6275 282 215 163 C ATOM 2675 CD2 TYR A 380 25.231 18.983 -14.745 1.00 54.82 C ANISOU 2675 CD2 TYR A 380 8401 6400 6029 394 44 118 C ATOM 2676 CE1 TYR A 380 27.894 19.169 -15.479 1.00 57.36 C ANISOU 2676 CE1 TYR A 380 8749 6731 6314 269 230 112 C ATOM 2677 CE2 TYR A 380 25.839 17.933 -15.432 1.00 55.85 C ANISOU 2677 CE2 TYR A 380 8517 6600 6103 371 57 65 C ATOM 2678 CZ TYR A 380 27.170 18.031 -15.800 1.00 63.54 C ANISOU 2678 CZ TYR A 380 9505 7578 7059 318 151 62 C ATOM 2679 OH TYR A 380 27.763 16.995 -16.479 1.00 65.15 O ANISOU 2679 OH TYR A 380 9692 7853 7210 310 171 0 O ATOM 2680 N THR A 381 23.228 22.384 -15.802 1.00 53.36 N ANISOU 2680 N THR A 381 8448 6073 5753 610 0 388 N ATOM 2681 CA THR A 381 22.433 22.250 -17.029 1.00 54.07 C ANISOU 2681 CA THR A 381 8573 6259 5713 703 -79 435 C ATOM 2682 C THR A 381 22.420 23.551 -17.862 1.00 60.17 C ANISOU 2682 C THR A 381 9505 6955 6400 775 -49 578 C ATOM 2683 O THR A 381 22.210 23.489 -19.075 1.00 60.90 O ANISOU 2683 O THR A 381 9662 7127 6350 826 -84 635 O ATOM 2684 CB THR A 381 20.998 21.793 -16.707 1.00 59.30 C ANISOU 2684 CB THR A 381 9128 7007 6396 789 -202 386 C ATOM 2685 OG1 THR A 381 20.432 22.646 -15.711 1.00 58.40 O ANISOU 2685 OG1 THR A 381 8999 6804 6386 844 -202 402 O ATOM 2686 CG2 THR A 381 20.931 20.342 -16.254 1.00 55.79 C ANISOU 2686 CG2 THR A 381 8559 6650 5989 713 -235 257 C ATOM 2687 N LEU A 382 22.678 24.712 -17.228 1.00 57.27 N ANISOU 2687 N LEU A 382 9216 6430 6113 775 21 635 N ATOM 2688 CA LEU A 382 22.718 26.013 -17.902 1.00 58.80 C ANISOU 2688 CA LEU A 382 9591 6507 6242 837 69 779 C ATOM 2689 C LEU A 382 23.886 26.115 -18.898 1.00 63.89 C ANISOU 2689 C LEU A 382 10350 7148 6779 737 173 838 C ATOM 2690 O LEU A 382 23.884 27.013 -19.738 1.00 64.77 O ANISOU 2690 O LEU A 382 10628 7190 6789 790 205 972 O ATOM 2691 CB LEU A 382 22.801 27.156 -16.876 1.00 59.00 C ANISOU 2691 CB LEU A 382 9677 6343 6396 831 139 799 C ATOM 2692 CG LEU A 382 21.477 27.634 -16.284 1.00 64.34 C ANISOU 2692 CG LEU A 382 10327 6984 7134 993 53 808 C ATOM 2693 CD1 LEU A 382 21.689 28.258 -14.920 1.00 64.40 C ANISOU 2693 CD1 LEU A 382 10328 6847 7293 942 124 750 C ATOM 2694 CD2 LEU A 382 20.769 28.611 -17.211 1.00 68.77 C ANISOU 2694 CD2 LEU A 382 11046 7483 7599 1163 17 960 C ATOM 2695 N PHE A 383 24.864 25.193 -18.820 1.00 60.52 N ANISOU 2695 N PHE A 383 9835 6794 6366 601 230 742 N ATOM 2696 CA PHE A 383 26.018 25.163 -19.718 1.00 61.58 C ANISOU 2696 CA PHE A 383 10042 6952 6402 497 340 771 C ATOM 2697 C PHE A 383 25.711 24.357 -20.993 1.00 66.95 C ANISOU 2697 C PHE A 383 10729 7795 6916 551 277 776 C ATOM 2698 O PHE A 383 26.397 24.528 -22.004 1.00 68.04 O ANISOU 2698 O PHE A 383 10966 7960 6928 500 360 832 O ATOM 2699 CB PHE A 383 27.260 24.640 -18.991 1.00 62.33 C ANISOU 2699 CB PHE A 383 10028 7059 6596 344 433 658 C ATOM 2700 CG PHE A 383 27.773 25.644 -17.985 1.00 64.19 C ANISOU 2700 CG PHE A 383 10290 7142 6956 260 520 663 C ATOM 2701 CD1 PHE A 383 27.343 25.612 -16.664 1.00 66.14 C ANISOU 2701 CD1 PHE A 383 10446 7345 7340 277 467 592 C ATOM 2702 CD2 PHE A 383 28.654 26.649 -18.367 1.00 68.26 C ANISOU 2702 CD2 PHE A 383 10932 7559 7445 154 661 734 C ATOM 2703 CE1 PHE A 383 27.790 26.560 -15.740 1.00 67.44 C ANISOU 2703 CE1 PHE A 383 10641 7372 7609 195 546 583 C ATOM 2704 CE2 PHE A 383 29.100 27.599 -17.443 1.00 71.69 C ANISOU 2704 CE2 PHE A 383 11397 7847 7994 60 743 723 C ATOM 2705 CZ PHE A 383 28.663 27.549 -16.134 1.00 68.52 C ANISOU 2705 CZ PHE A 383 10902 7408 7725 84 681 643 C ATOM 2706 N ASN A 384 24.648 23.528 -20.958 1.00 63.00 N ANISOU 2706 N ASN A 384 10128 7403 6406 645 135 715 N ATOM 2707 CA ASN A 384 24.152 22.774 -22.109 1.00 63.31 C ANISOU 2707 CA ASN A 384 10166 7603 6286 700 52 702 C ATOM 2708 C ASN A 384 23.168 23.686 -22.850 1.00 68.66 C ANISOU 2708 C ASN A 384 10963 8281 6844 847 -30 841 C ATOM 2709 O ASN A 384 22.190 24.140 -22.250 1.00 68.41 O ANISOU 2709 O ASN A 384 10899 8210 6884 954 -116 865 O ATOM 2710 CB ASN A 384 23.498 21.468 -21.654 1.00 62.44 C ANISOU 2710 CB ASN A 384 9889 7603 6234 706 -54 556 C ATOM 2711 CG ASN A 384 23.159 20.519 -22.773 1.00 83.11 C ANISOU 2711 CG ASN A 384 12494 10387 8698 724 -124 502 C ATOM 2712 OD1 ASN A 384 22.171 20.690 -23.486 1.00 77.74 O ANISOU 2712 OD1 ASN A 384 11836 9797 7905 826 -235 545 O ATOM 2713 ND2 ASN A 384 23.943 19.465 -22.916 1.00 74.89 N ANISOU 2713 ND2 ASN A 384 11408 9397 7651 631 -67 395 N ATOM 2714 N LYS A 385 23.458 24.002 -24.123 1.00 66.43 N ANISOU 2714 N LYS A 385 10823 8043 6375 859 4 939 N ATOM 2715 CA LYS A 385 22.653 24.919 -24.936 1.00 68.11 C ANISOU 2715 CA LYS A 385 11181 8254 6443 1010 -68 1097 C ATOM 2716 C LYS A 385 21.215 24.441 -25.147 1.00 71.40 C ANISOU 2716 C LYS A 385 11493 8826 6810 1159 -265 1059 C ATOM 2717 O LYS A 385 20.314 25.280 -25.134 1.00 72.35 O ANISOU 2717 O LYS A 385 11659 8905 6923 1316 -347 1161 O ATOM 2718 CB LYS A 385 23.310 25.172 -26.301 1.00 72.51 C ANISOU 2718 CB LYS A 385 11906 8860 6783 977 7 1195 C ATOM 2719 N THR A 386 20.994 23.118 -25.330 1.00 65.68 N ANISOU 2719 N THR A 386 10626 8275 6055 1111 -336 909 N ATOM 2720 CA THR A 386 19.651 22.566 -25.579 1.00 65.27 C ANISOU 2720 CA THR A 386 10455 8396 5949 1218 -518 847 C ATOM 2721 C THR A 386 18.791 22.663 -24.292 1.00 66.44 C ANISOU 2721 C THR A 386 10457 8492 6293 1269 -580 792 C ATOM 2722 O THR A 386 17.605 22.991 -24.397 1.00 66.71 O ANISOU 2722 O THR A 386 10439 8610 6299 1416 -715 820 O ATOM 2723 CB THR A 386 19.675 21.147 -26.229 1.00 70.22 C ANISOU 2723 CB THR A 386 10992 9207 6480 1130 -562 692 C ATOM 2724 OG1 THR A 386 18.993 20.188 -25.424 1.00 68.32 O ANISOU 2724 OG1 THR A 386 10563 9018 6377 1089 -631 533 O ATOM 2725 CG2 THR A 386 21.080 20.660 -26.617 1.00 66.44 C ANISOU 2725 CG2 THR A 386 10587 8702 5957 987 -410 655 C ATOM 2726 N PHE A 387 19.399 22.422 -23.097 1.00 60.01 N ANISOU 2726 N PHE A 387 9580 7552 5669 1156 -481 717 N ATOM 2727 CA PHE A 387 18.761 22.552 -21.774 1.00 57.97 C ANISOU 2727 CA PHE A 387 9202 7229 5596 1181 -507 665 C ATOM 2728 C PHE A 387 18.396 24.023 -21.504 1.00 61.90 C ANISOU 2728 C PHE A 387 9798 7590 6131 1318 -500 805 C ATOM 2729 O PHE A 387 17.280 24.312 -21.067 1.00 61.54 O ANISOU 2729 O PHE A 387 9666 7574 6141 1440 -592 797 O ATOM 2730 CB PHE A 387 19.700 22.045 -20.661 1.00 57.50 C ANISOU 2730 CB PHE A 387 9085 7067 5694 1026 -393 571 C ATOM 2731 CG PHE A 387 19.407 20.691 -20.060 1.00 57.56 C ANISOU 2731 CG PHE A 387 8930 7163 5778 944 -435 411 C ATOM 2732 CD1 PHE A 387 18.321 20.509 -19.210 1.00 60.37 C ANISOU 2732 CD1 PHE A 387 9155 7558 6227 987 -515 350 C ATOM 2733 CD2 PHE A 387 20.273 19.623 -20.259 1.00 58.80 C ANISOU 2733 CD2 PHE A 387 9072 7348 5922 822 -380 321 C ATOM 2734 CE1 PHE A 387 18.073 19.261 -18.621 1.00 60.15 C ANISOU 2734 CE1 PHE A 387 8996 7591 6266 893 -537 210 C ATOM 2735 CE2 PHE A 387 20.020 18.374 -19.678 1.00 60.45 C ANISOU 2735 CE2 PHE A 387 9159 7607 6204 750 -410 183 C ATOM 2736 CZ PHE A 387 18.923 18.203 -18.859 1.00 58.19 C ANISOU 2736 CZ PHE A 387 8758 7352 6002 776 -486 133 C ATOM 2737 N ARG A 388 19.353 24.944 -21.784 1.00 58.48 N ANISOU 2737 N ARG A 388 9549 7003 5666 1293 -381 927 N ATOM 2738 CA ARG A 388 19.244 26.401 -21.642 1.00 59.12 C ANISOU 2738 CA ARG A 388 9781 6906 5774 1402 -342 1071 C ATOM 2739 C ARG A 388 18.154 26.956 -22.579 1.00 65.66 C ANISOU 2739 C ARG A 388 10673 7815 6459 1620 -476 1190 C ATOM 2740 O ARG A 388 17.489 27.932 -22.223 1.00 66.35 O ANISOU 2740 O ARG A 388 10799 7804 6605 1776 -509 1264 O ATOM 2741 CB ARG A 388 20.609 27.053 -21.931 1.00 57.93 C ANISOU 2741 CB ARG A 388 9818 6597 5597 1282 -173 1161 C ATOM 2742 CG ARG A 388 20.729 28.514 -21.520 1.00 67.69 C ANISOU 2742 CG ARG A 388 11224 7596 6900 1338 -91 1285 C ATOM 2743 CD ARG A 388 22.157 29.041 -21.578 1.00 77.27 C ANISOU 2743 CD ARG A 388 12583 8654 8124 1161 96 1331 C ATOM 2744 NE ARG A 388 22.716 29.049 -22.933 1.00 86.48 N ANISOU 2744 NE ARG A 388 13892 9871 9095 1126 145 1433 N ATOM 2745 CZ ARG A 388 23.698 28.256 -23.351 1.00100.05 C ANISOU 2745 CZ ARG A 388 15566 11692 10756 966 220 1364 C ATOM 2746 NH1 ARG A 388 24.252 27.380 -22.522 1.00 86.07 N ANISOU 2746 NH1 ARG A 388 13615 9976 9111 837 247 1199 N ATOM 2747 NH2 ARG A 388 24.134 28.333 -24.599 1.00 90.05 N ANISOU 2747 NH2 ARG A 388 14439 10477 9301 942 270 1459 N ATOM 2748 N ASP A 389 17.964 26.332 -23.760 1.00 63.46 N ANISOU 2748 N ASP A 389 10402 7721 5991 1641 -556 1202 N ATOM 2749 CA ASP A 389 16.920 26.733 -24.705 1.00 66.02 C ANISOU 2749 CA ASP A 389 10767 8165 6151 1851 -706 1306 C ATOM 2750 C ASP A 389 15.562 26.254 -24.213 1.00 70.37 C ANISOU 2750 C ASP A 389 11089 8877 6770 1961 -867 1195 C ATOM 2751 O ASP A 389 14.571 26.955 -24.414 1.00 72.35 O ANISOU 2751 O ASP A 389 11344 9160 6985 2176 -978 1280 O ATOM 2752 CB ASP A 389 17.189 26.207 -26.128 1.00 69.11 C ANISOU 2752 CB ASP A 389 11233 8725 6302 1823 -743 1336 C ATOM 2753 CG ASP A 389 18.361 26.846 -26.856 1.00 78.83 C ANISOU 2753 CG ASP A 389 12711 9825 7417 1750 -593 1478 C ATOM 2754 OD1 ASP A 389 18.728 27.996 -26.511 1.00 78.65 O ANISOU 2754 OD1 ASP A 389 12852 9577 7454 1786 -495 1613 O ATOM 2755 OD2 ASP A 389 18.915 26.196 -27.769 1.00 86.77 O ANISOU 2755 OD2 ASP A 389 13749 10950 8269 1649 -565 1448 O ATOM 2756 N ALA A 390 15.516 25.071 -23.556 1.00 64.92 N ANISOU 2756 N ALA A 390 10200 8284 6181 1816 -873 1007 N ATOM 2757 CA ALA A 390 14.288 24.513 -22.986 1.00 64.64 C ANISOU 2757 CA ALA A 390 9933 8403 6225 1871 -999 879 C ATOM 2758 C ALA A 390 13.779 25.417 -21.858 1.00 69.62 C ANISOU 2758 C ALA A 390 10527 8895 7029 1979 -977 903 C ATOM 2759 O ALA A 390 12.606 25.794 -21.880 1.00 71.00 O ANISOU 2759 O ALA A 390 10604 9172 7200 2161 -1099 913 O ATOM 2760 CB ALA A 390 14.527 23.097 -22.478 1.00 63.24 C ANISOU 2760 CB ALA A 390 9600 8307 6122 1667 -974 690 C ATOM 2761 N PHE A 391 14.686 25.840 -20.935 1.00 65.06 N ANISOU 2761 N PHE A 391 10035 8092 6594 1878 -822 914 N ATOM 2762 CA PHE A 391 14.388 26.733 -19.805 1.00 64.75 C ANISOU 2762 CA PHE A 391 9989 7893 6720 1955 -773 924 C ATOM 2763 C PHE A 391 13.835 28.090 -20.274 1.00 72.45 C ANISOU 2763 C PHE A 391 11106 8778 7644 2199 -816 1089 C ATOM 2764 O PHE A 391 12.928 28.626 -19.634 1.00 73.59 O ANISOU 2764 O PHE A 391 11172 8904 7884 2351 -858 1075 O ATOM 2765 CB PHE A 391 15.633 26.968 -18.925 1.00 64.50 C ANISOU 2765 CB PHE A 391 10047 7645 6813 1782 -600 907 C ATOM 2766 CG PHE A 391 16.339 25.769 -18.325 1.00 63.33 C ANISOU 2766 CG PHE A 391 9788 7544 6729 1561 -542 765 C ATOM 2767 CD1 PHE A 391 15.654 24.581 -18.081 1.00 65.34 C ANISOU 2767 CD1 PHE A 391 9843 7980 7003 1516 -626 628 C ATOM 2768 CD2 PHE A 391 17.673 25.849 -17.944 1.00 63.76 C ANISOU 2768 CD2 PHE A 391 9937 7457 6832 1399 -402 766 C ATOM 2769 CE1 PHE A 391 16.306 23.480 -17.518 1.00 64.04 C ANISOU 2769 CE1 PHE A 391 9603 7834 6897 1328 -570 510 C ATOM 2770 CE2 PHE A 391 18.322 24.749 -17.376 1.00 64.57 C ANISOU 2770 CE2 PHE A 391 9938 7604 6992 1225 -359 642 C ATOM 2771 CZ PHE A 391 17.634 23.574 -17.164 1.00 61.82 C ANISOU 2771 CZ PHE A 391 9417 7413 6657 1198 -443 522 C ATOM 2772 N GLY A 392 14.376 28.614 -21.378 1.00 70.07 N ANISOU 2772 N GLY A 392 11015 8422 7188 2241 -801 1243 N ATOM 2773 CA GLY A 392 13.951 29.880 -21.969 1.00 72.40 C ANISOU 2773 CA GLY A 392 11489 8613 7406 2476 -838 1428 C ATOM 2774 C GLY A 392 12.528 29.841 -22.494 1.00 78.49 C ANISOU 2774 C GLY A 392 12128 9606 8088 2720 -1039 1440 C ATOM 2775 O GLY A 392 11.838 30.865 -22.503 1.00 80.23 O ANISOU 2775 O GLY A 392 12421 9748 8313 2964 -1090 1551 O ATOM 2776 N ARG A 393 12.083 28.646 -22.931 1.00 74.64 N ANISOU 2776 N ARG A 393 11443 9399 7519 2656 -1156 1318 N ATOM 2777 CA ARG A 393 10.734 28.394 -23.432 1.00 76.02 C ANISOU 2777 CA ARG A 393 11439 9843 7604 2845 -1359 1286 C ATOM 2778 C ARG A 393 9.744 28.224 -22.272 1.00 80.71 C ANISOU 2778 C ARG A 393 11777 10507 8381 2895 -1399 1141 C ATOM 2779 O ARG A 393 8.655 28.790 -22.328 1.00 82.10 O ANISOU 2779 O ARG A 393 11868 10773 8551 3142 -1519 1174 O ATOM 2780 CB ARG A 393 10.720 27.150 -24.329 1.00 74.09 C ANISOU 2780 CB ARG A 393 11090 9861 7199 2716 -1450 1191 C ATOM 2781 CG ARG A 393 11.011 27.438 -25.797 1.00 81.91 C ANISOU 2781 CG ARG A 393 12277 10911 7936 2794 -1506 1345 C ATOM 2782 CD ARG A 393 11.928 26.404 -26.429 1.00 84.83 C ANISOU 2782 CD ARG A 393 12685 11350 8197 2553 -1445 1273 C ATOM 2783 NE ARG A 393 11.429 25.031 -26.291 1.00 84.91 N ANISOU 2783 NE ARG A 393 12444 11598 8220 2421 -1529 1056 N ATOM 2784 CZ ARG A 393 12.190 23.945 -26.390 1.00 94.88 C ANISOU 2784 CZ ARG A 393 13690 12894 9465 2189 -1457 935 C ATOM 2785 NH1 ARG A 393 13.493 24.056 -26.623 1.00 80.67 N ANISOU 2785 NH1 ARG A 393 12085 10932 7635 2066 -1302 1002 N ATOM 2786 NH2 ARG A 393 11.655 22.741 -26.249 1.00 80.20 N ANISOU 2786 NH2 ARG A 393 11620 11229 7624 2076 -1532 741 N ATOM 2787 N TYR A 394 10.128 27.466 -21.217 1.00 76.13 N ANISOU 2787 N TYR A 394 11079 9888 7958 2671 -1296 983 N ATOM 2788 CA TYR A 394 9.266 27.191 -20.060 1.00 76.03 C ANISOU 2788 CA TYR A 394 10828 9947 8112 2675 -1309 834 C ATOM 2789 C TYR A 394 9.011 28.423 -19.178 1.00 80.89 C ANISOU 2789 C TYR A 394 11505 10361 8869 2842 -1243 893 C ATOM 2790 O TYR A 394 7.944 28.492 -18.572 1.00 81.00 O ANISOU 2790 O TYR A 394 11323 10484 8969 2963 -1302 809 O ATOM 2791 CB TYR A 394 9.816 26.044 -19.189 1.00 74.93 C ANISOU 2791 CB TYR A 394 10583 9806 8082 2389 -1210 669 C ATOM 2792 CG TYR A 394 10.187 24.776 -19.932 1.00 76.33 C ANISOU 2792 CG TYR A 394 10720 10137 8144 2206 -1246 594 C ATOM 2793 CD1 TYR A 394 9.384 24.279 -20.957 1.00 80.16 C ANISOU 2793 CD1 TYR A 394 11097 10881 8478 2273 -1407 565 C ATOM 2794 CD2 TYR A 394 11.303 24.030 -19.558 1.00 74.84 C ANISOU 2794 CD2 TYR A 394 10588 9845 8002 1967 -1123 534 C ATOM 2795 CE1 TYR A 394 9.724 23.113 -21.643 1.00 80.99 C ANISOU 2795 CE1 TYR A 394 11178 11117 8477 2101 -1433 479 C ATOM 2796 CE2 TYR A 394 11.647 22.858 -20.230 1.00 75.21 C ANISOU 2796 CE2 TYR A 394 10608 10016 7951 1813 -1147 456 C ATOM 2797 CZ TYR A 394 10.856 22.404 -21.273 1.00 84.55 C ANISOU 2797 CZ TYR A 394 11704 11439 8983 1874 -1297 425 C ATOM 2798 OH TYR A 394 11.190 21.248 -21.933 1.00 84.49 O ANISOU 2798 OH TYR A 394 11680 11545 8879 1717 -1315 332 O ATOM 2799 N ILE A 395 9.959 29.389 -19.105 1.00 78.28 N ANISOU 2799 N ILE A 395 11437 9742 8562 2844 -1116 1024 N ATOM 2800 CA ILE A 395 9.777 30.611 -18.295 1.00 79.49 C ANISOU 2800 CA ILE A 395 11683 9671 8848 2996 -1040 1076 C ATOM 2801 C ILE A 395 8.688 31.518 -18.920 1.00 87.03 C ANISOU 2801 C ILE A 395 12656 10676 9735 3344 -1173 1193 C ATOM 2802 O ILE A 395 8.075 32.309 -18.202 1.00 87.92 O ANISOU 2802 O ILE A 395 12749 10689 9966 3520 -1154 1187 O ATOM 2803 CB ILE A 395 11.090 31.400 -18.008 1.00 82.09 C ANISOU 2803 CB ILE A 395 12290 9671 9228 2880 -859 1167 C ATOM 2804 CG1 ILE A 395 11.822 31.839 -19.297 1.00 84.07 C ANISOU 2804 CG1 ILE A 395 12796 9838 9307 2895 -851 1352 C ATOM 2805 CG2 ILE A 395 12.013 30.627 -17.054 1.00 79.84 C ANISOU 2805 CG2 ILE A 395 11943 9340 9051 2581 -732 1028 C ATOM 2806 CD1 ILE A 395 12.470 33.234 -19.228 1.00 93.75 C ANISOU 2806 CD1 ILE A 395 14325 10726 10568 2947 -716 1503 C ATOM 2807 N THR A 396 8.438 31.377 -20.239 1.00 85.36 N ANISOU 2807 N THR A 396 12476 10631 9328 3448 -1311 1291 N ATOM 2808 CA THR A 396 7.402 32.110 -20.974 1.00 88.65 C ANISOU 2808 CA THR A 396 12895 11143 9644 3789 -1469 1409 C ATOM 2809 C THR A 396 6.190 31.178 -21.216 1.00 94.54 C ANISOU 2809 C THR A 396 13299 12279 10341 3850 -1657 1267 C ATOM 2810 O THR A 396 5.280 31.530 -21.973 1.00 96.83 O ANISOU 2810 O THR A 396 13531 12737 10524 4123 -1825 1338 O ATOM 2811 CB THR A 396 7.965 32.702 -22.282 1.00 96.29 C ANISOU 2811 CB THR A 396 14153 12025 10406 3876 -1495 1632 C ATOM 2812 OG1 THR A 396 8.361 31.650 -23.165 1.00 93.27 O ANISOU 2812 OG1 THR A 396 13733 11840 9864 3682 -1542 1594 O ATOM 2813 CG2 THR A 396 9.118 33.677 -22.045 1.00 94.54 C ANISOU 2813 CG2 THR A 396 14269 11414 10238 3818 -1302 1773 C ATOM 2814 N CYS A 397 6.188 29.997 -20.543 1.00 90.09 N ANISOU 2814 N CYS A 397 12514 11857 9859 3590 -1624 1065 N ATOM 2815 CA CYS A 397 5.176 28.929 -20.577 1.00 90.98 C ANISOU 2815 CA CYS A 397 12295 12320 9953 3550 -1759 889 C ATOM 2816 C CYS A 397 4.875 28.482 -22.023 1.00 97.48 C ANISOU 2816 C CYS A 397 13095 13401 10543 3612 -1939 935 C ATOM 2817 O CYS A 397 3.748 28.637 -22.502 1.00 99.43 O ANISOU 2817 O CYS A 397 13173 13889 10716 3836 -2115 930 O ATOM 2818 CB CYS A 397 3.906 29.342 -19.833 1.00 93.15 C ANISOU 2818 CB CYS A 397 12335 12702 10354 3757 -1815 806 C ATOM 2819 SG CYS A 397 4.114 29.494 -18.039 1.00 95.11 S ANISOU 2819 SG CYS A 397 12547 12727 10864 3630 -1609 688 S ATOM 2820 N ASN A 398 5.892 27.916 -22.705 1.00 93.84 N ANISOU 2820 N ASN A 398 12794 12900 9960 3411 -1894 970 N ATOM 2821 CA ASN A 398 5.766 27.448 -24.087 1.00 95.73 C ANISOU 2821 CA ASN A 398 13043 13368 9960 3434 -2043 1006 C ATOM 2822 C ASN A 398 5.367 25.966 -24.137 1.00100.48 C ANISOU 2822 C ASN A 398 13384 14252 10543 3212 -2110 782 C ATOM 2823 O ASN A 398 4.279 25.656 -24.630 1.00102.52 O ANISOU 2823 O ASN A 398 13426 14814 10713 3318 -2291 707 O ATOM 2824 CB ASN A 398 7.065 27.688 -24.868 1.00 94.17 C ANISOU 2824 CB ASN A 398 13170 12983 9628 3346 -1947 1162 C ATOM 2825 CG ASN A 398 6.916 27.780 -26.369 1.00105.67 C ANISOU 2825 CG ASN A 398 14728 14613 10808 3477 -2096 1282 C ATOM 2826 OD1 ASN A 398 6.332 26.911 -27.027 1.00 97.50 O ANISOU 2826 OD1 ASN A 398 13519 13885 9643 3440 -2243 1171 O ATOM 2827 ND2 ASN A 398 7.515 28.808 -26.952 1.00 94.96 N ANISOU 2827 ND2 ASN A 398 13673 13058 9348 3610 -2049 1509 N ATOM 2828 N TYR A 399 6.251 25.059 -23.648 1.00 95.07 N ANISOU 2828 N TYR A 399 12723 13463 9937 2907 -1967 675 N ATOM 2829 CA TYR A 399 6.095 23.590 -23.610 1.00 94.34 C ANISOU 2829 CA TYR A 399 12440 13560 9845 2655 -1987 465 C ATOM 2830 C TYR A 399 5.846 22.978 -25.022 1.00 99.55 C ANISOU 2830 C TYR A 399 13077 14485 10262 2651 -2144 440 C ATOM 2831 O TYR A 399 5.389 21.834 -25.124 1.00 99.05 O ANISOU 2831 O TYR A 399 12816 14638 10179 2493 -2209 253 O ATOM 2832 CB TYR A 399 4.979 23.145 -22.626 1.00 96.11 C ANISOU 2832 CB TYR A 399 12357 13933 10228 2625 -2018 287 C ATOM 2833 CG TYR A 399 4.864 23.961 -21.354 1.00 98.01 C ANISOU 2833 CG TYR A 399 12587 13982 10672 2717 -1911 317 C ATOM 2834 CD1 TYR A 399 3.760 24.778 -21.124 1.00102.27 C ANISOU 2834 CD1 TYR A 399 12984 14621 11251 2980 -2004 339 C ATOM 2835 CD2 TYR A 399 5.841 23.889 -20.362 1.00 96.34 C ANISOU 2835 CD2 TYR A 399 12494 13503 10606 2545 -1720 311 C ATOM 2836 CE1 TYR A 399 3.641 25.521 -19.951 1.00102.81 C ANISOU 2836 CE1 TYR A 399 13046 14514 11503 3065 -1897 350 C ATOM 2837 CE2 TYR A 399 5.739 24.638 -19.190 1.00 96.84 C ANISOU 2837 CE2 TYR A 399 12553 13398 10842 2620 -1621 325 C ATOM 2838 CZ TYR A 399 4.634 25.449 -18.987 1.00106.89 C ANISOU 2838 CZ TYR A 399 13697 14762 12155 2877 -1705 340 C ATOM 2839 OH TYR A 399 4.512 26.180 -17.831 1.00107.99 O ANISOU 2839 OH TYR A 399 13833 14738 12461 2954 -1600 338 O ATOM 2840 N ARG A 400 6.188 23.740 -26.092 1.00 97.48 N ANISOU 2840 N ARG A 400 13034 14193 9810 2809 -2193 627 N ATOM 2841 CA ARG A 400 6.056 23.417 -27.520 1.00120.85 C ANISOU 2841 CA ARG A 400 16033 17383 12503 2844 -2338 648 C ATOM 2842 C ARG A 400 4.612 23.048 -27.879 1.00154.64 C ANISOU 2842 C ARG A 400 20023 22028 16705 2958 -2563 529 C ATOM 2843 O ARG A 400 3.900 23.857 -28.470 1.00120.27 O ANISOU 2843 O ARG A 400 15657 17791 12250 3245 -2711 650 O ATOM 2844 CB ARG A 400 7.023 22.297 -27.943 1.00118.76 C ANISOU 2844 CB ARG A 400 15843 17110 12169 2555 -2250 541 C ATOM 2845 CG ARG A 400 7.405 22.355 -29.416 1.00129.09 C ANISOU 2845 CG ARG A 400 17331 18527 13191 2599 -2322 637 C ATOM 2846 CD ARG A 400 8.412 21.287 -29.787 1.00133.69 C ANISOU 2846 CD ARG A 400 18002 19074 13721 2326 -2208 530 C ATOM 2847 NE ARG A 400 8.882 21.445 -31.164 1.00140.97 N ANISOU 2847 NE ARG A 400 19125 20073 14364 2368 -2245 637 N ATOM 2848 CZ ARG A 400 9.959 22.141 -31.518 1.00153.42 C ANISOU 2848 CZ ARG A 400 20977 21440 15875 2387 -2112 819 C ATOM 2849 NH1 ARG A 400 10.693 22.756 -30.598 1.00137.71 N ANISOU 2849 NH1 ARG A 400 19091 19150 14082 2365 -1940 908 N ATOM 2850 NH2 ARG A 400 10.309 22.230 -32.794 1.00142.02 N ANISOU 2850 NH2 ARG A 400 19706 20094 14159 2417 -2146 907 N TER 2851 ARG A 400 HETATM 2852 C1 ERM A2001 23.443 14.527 4.822 1.00 54.30 C HETATM 2853 N1 ERM A2001 24.198 13.556 5.387 1.00 55.27 N HETATM 2854 O1 ERM A2001 21.825 18.775 11.405 1.00 55.79 O HETATM 2855 C10 ERM A2001 23.821 14.673 9.347 1.00 54.17 C HETATM 2856 C11 ERM A2001 24.633 13.531 9.134 1.00 54.11 C HETATM 2857 C12 ERM A2001 24.845 13.050 7.801 1.00 53.56 C HETATM 2858 C13 ERM A2001 24.248 13.712 6.779 1.00 55.14 C HETATM 2859 C14 ERM A2001 23.433 14.833 6.998 1.00 55.54 C HETATM 2860 C15 ERM A2001 21.480 19.656 6.214 1.00 54.58 C HETATM 2861 C16 ERM A2001 20.714 18.621 10.929 1.00 56.28 C HETATM 2862 C17 ERM A2001 19.482 19.617 12.891 1.00 58.30 C HETATM 2863 C18 ERM A2001 20.316 18.935 13.956 1.00 58.34 C HETATM 2864 C19 ERM A2001 22.346 19.519 15.212 1.00 60.25 C HETATM 2865 N2 ERM A2001 21.200 18.505 7.119 1.00 53.99 N HETATM 2866 C2 ERM A2001 22.941 15.353 5.782 1.00 54.63 C HETATM 2867 O2 ERM A2001 20.068 20.921 12.810 1.00 60.03 O HETATM 2868 C20 ERM A2001 22.747 20.825 15.923 1.00 61.60 C HETATM 2869 C21 ERM A2001 22.511 23.314 16.110 1.00 60.03 C HETATM 2870 C22 ERM A2001 21.807 24.351 15.264 1.00 59.55 C HETATM 2871 C23 ERM A2001 21.484 23.632 13.930 1.00 60.20 C HETATM 2872 C24 ERM A2001 21.254 22.226 14.501 1.00 61.08 C HETATM 2873 C25 ERM A2001 21.302 21.063 13.519 1.00 60.41 C HETATM 2874 C26 ERM A2001 17.997 19.623 13.245 1.00 56.32 C HETATM 2875 C27 ERM A2001 23.515 18.804 14.566 1.00 60.01 C HETATM 2876 C28 ERM A2001 24.425 18.071 15.538 1.00 60.75 C HETATM 2877 C29 ERM A2001 23.938 17.027 16.345 1.00 61.76 C HETATM 2878 C3 ERM A2001 22.027 16.545 5.777 1.00 53.77 C HETATM 2879 N3 ERM A2001 19.566 18.969 11.569 1.00 57.16 N HETATM 2880 O3 ERM A2001 20.125 17.834 14.423 1.00 58.48 O HETATM 2881 C30 ERM A2001 24.787 16.353 17.239 1.00 61.67 C HETATM 2882 C31 ERM A2001 26.147 16.703 17.305 1.00 61.35 C HETATM 2883 C32 ERM A2001 26.649 17.724 16.483 1.00 60.93 C HETATM 2884 C33 ERM A2001 25.791 18.400 15.595 1.00 60.95 C HETATM 2885 C4 ERM A2001 22.257 17.419 7.063 1.00 53.89 C HETATM 2886 N4 ERM A2001 21.310 19.790 14.237 1.00 59.56 N HETATM 2887 O4 ERM A2001 23.568 20.788 16.855 1.00 63.04 O HETATM 2888 C5 ERM A2001 20.910 19.087 8.477 1.00 54.03 C HETATM 2889 N5 ERM A2001 22.225 21.994 15.554 1.00 61.05 N HETATM 2890 O5 ERM A2001 22.378 21.154 12.635 1.00 60.18 O HETATM 2891 C6 ERM A2001 20.596 18.011 9.500 1.00 55.14 C HETATM 2892 C7 ERM A2001 21.432 16.761 9.339 1.00 55.10 C HETATM 2893 C8 ERM A2001 22.307 16.589 8.351 1.00 54.79 C HETATM 2894 C9 ERM A2001 23.206 15.363 8.294 1.00 54.83 C HETATM 2895 C1 PLM A2002 4.584 30.938 -17.373 1.00 75.83 C ANISOU 2895 C1 PLM A2002 9452 9739 9620 767 75 -185 C HETATM 2896 O2 PLM A2002 4.330 32.007 -18.214 1.00 75.75 O ANISOU 2896 O2 PLM A2002 9445 9731 9608 787 88 -186 O HETATM 2897 C2 PLM A2002 5.523 31.161 -16.247 1.00 75.53 C ANISOU 2897 C2 PLM A2002 9419 9701 9579 737 81 -174 C HETATM 2898 C3 PLM A2002 4.959 31.554 -14.929 1.00 74.91 C ANISOU 2898 C3 PLM A2002 9343 9612 9505 711 89 -179 C HETATM 2899 C4 PLM A2002 5.025 32.995 -14.533 1.00 74.43 C ANISOU 2899 C4 PLM A2002 9287 9549 9445 700 102 -174 C HETATM 2900 C5 PLM A2002 5.366 33.332 -13.123 1.00 74.68 C ANISOU 2900 C5 PLM A2002 9320 9575 9479 680 104 -172 C HETATM 2901 C6 PLM A2002 4.263 33.364 -12.095 1.00 74.80 C ANISOU 2901 C6 PLM A2002 9338 9585 9496 671 104 -178 C HETATM 2902 C7 PLM A2002 4.538 34.051 -10.784 1.00 75.21 C ANISOU 2902 C7 PLM A2002 9392 9634 9551 661 105 -175 C HETATM 2903 C8 PLM A2002 4.058 33.399 -9.514 1.00 75.07 C ANISOU 2903 C8 PLM A2002 9375 9613 9535 658 103 -176 C HETATM 2904 C9 PLM A2002 4.203 34.189 -8.227 1.00 74.40 C ANISOU 2904 C9 PLM A2002 9292 9526 9452 660 101 -174 C HETATM 2905 CA PLM A2002 4.317 33.432 -6.932 1.00 74.08 C ANISOU 2905 CA PLM A2002 9252 9481 9413 666 102 -174 C HETATM 2906 CB PLM A2002 5.417 33.844 -5.967 1.00 73.67 C ANISOU 2906 CB PLM A2002 9200 9425 9365 676 100 -178 C HETATM 2907 CC PLM A2002 5.110 33.871 -4.485 1.00 72.60 C ANISOU 2907 CC PLM A2002 9066 9288 9231 695 98 -177 C HETATM 2908 CD PLM A2002 6.237 34.153 -3.533 1.00 72.07 C ANISOU 2908 CD PLM A2002 8999 9214 9170 713 94 -187 C HETATM 2909 CE PLM A2002 6.661 35.582 -3.348 1.00 72.19 C ANISOU 2909 CE PLM A2002 9008 9226 9196 722 79 -189 C HETATM 2910 CF PLM A2002 7.924 35.874 -2.621 1.00 72.03 C ANISOU 2910 CF PLM A2002 8985 9195 9188 740 74 -203 C HETATM 2911 CG PLM A2002 7.854 36.222 -1.168 1.00 71.74 C ANISOU 2911 CG PLM A2002 8946 9154 9157 777 63 -210 C HETATM 2912 C1 CLR A2003 7.052 26.143 -13.210 1.00 70.31 C HETATM 2913 C2 CLR A2003 7.059 25.872 -14.718 1.00 69.96 C HETATM 2914 C3 CLR A2003 6.807 27.126 -15.549 1.00 70.48 C HETATM 2915 C4 CLR A2003 7.819 28.221 -15.212 1.00 69.70 C HETATM 2916 C5 CLR A2003 7.871 28.475 -13.713 1.00 70.24 C HETATM 2917 C6 CLR A2003 7.892 29.770 -13.320 1.00 70.37 C HETATM 2918 C7 CLR A2003 7.513 30.226 -11.922 1.00 70.85 C HETATM 2919 C8 CLR A2003 7.852 29.168 -10.861 1.00 71.74 C HETATM 2920 C9 CLR A2003 7.363 27.773 -11.333 1.00 71.02 C HETATM 2921 C10 CLR A2003 7.926 27.312 -12.706 1.00 70.39 C HETATM 2922 C11 CLR A2003 7.312 26.686 -10.231 1.00 71.59 C HETATM 2923 C12 CLR A2003 6.817 27.161 -8.855 1.00 72.64 C HETATM 2924 C13 CLR A2003 7.475 28.463 -8.362 1.00 74.37 C HETATM 2925 C14 CLR A2003 7.256 29.503 -9.474 1.00 73.56 C HETATM 2926 C15 CLR A2003 7.456 30.884 -8.855 1.00 74.02 C HETATM 2927 C16 CLR A2003 6.955 30.680 -7.425 1.00 74.88 C HETATM 2928 C17 CLR A2003 6.715 29.170 -7.218 1.00 75.64 C HETATM 2929 C18 CLR A2003 8.960 28.228 -7.992 1.00 75.07 C HETATM 2930 C19 CLR A2003 9.388 26.845 -12.593 1.00 69.64 C HETATM 2931 C20 CLR A2003 6.834 28.700 -5.745 1.00 78.34 C HETATM 2932 C21 CLR A2003 6.480 27.230 -5.493 1.00 78.53 C HETATM 2933 C22 CLR A2003 5.955 29.544 -4.821 1.00 81.29 C HETATM 2934 C23 CLR A2003 6.604 29.771 -3.465 1.00 83.66 C HETATM 2935 C24 CLR A2003 5.573 29.596 -2.360 1.00 86.11 C HETATM 2936 C25 CLR A2003 6.179 29.936 -1.006 1.00 88.43 C HETATM 2937 C26 CLR A2003 5.776 31.341 -0.575 1.00 88.61 C HETATM 2938 C27 CLR A2003 5.789 28.895 0.038 1.00 89.74 C HETATM 2939 O1 CLR A2003 6.923 26.772 -16.930 1.00 71.31 O HETATM 2940 C10 OLC A2004 41.401 18.821 -2.791 1.00 70.53 C HETATM 2941 C9 OLC A2004 42.250 18.634 -3.817 1.00 69.40 C HETATM 2942 C11 OLC A2004 40.055 19.510 -2.873 1.00 70.85 C HETATM 2943 C8 OLC A2004 42.026 19.078 -5.247 1.00 67.15 C HETATM 2944 C24 OLC A2004 34.969 13.631 -13.636 1.00 70.92 C HETATM 2945 C12 OLC A2004 39.302 19.713 -1.596 1.00 70.67 C HETATM 2946 C7 OLC A2004 41.507 18.076 -6.247 1.00 65.79 C HETATM 2947 C6 OLC A2004 40.355 18.513 -7.130 1.00 65.04 C HETATM 2948 C5 OLC A2004 38.975 17.979 -6.785 1.00 65.16 C HETATM 2949 C4 OLC A2004 37.789 18.495 -7.586 1.00 65.83 C HETATM 2950 C3 OLC A2004 36.571 17.583 -7.721 1.00 66.67 C HETATM 2951 C2 OLC A2004 35.758 17.702 -9.003 1.00 68.57 C HETATM 2952 C21 OLC A2004 35.472 14.868 -11.554 1.00 70.09 C HETATM 2953 C1 OLC A2004 35.239 16.434 -9.657 1.00 70.70 C HETATM 2954 C22 OLC A2004 35.818 14.711 -13.006 1.00 71.19 C HETATM 2955 O19 OLC A2004 34.208 15.965 -9.198 1.00 72.04 O HETATM 2956 O25 OLC A2004 34.702 13.671 -14.999 1.00 70.07 O HETATM 2957 O23 OLC A2004 35.676 15.918 -13.662 1.00 72.06 O HETATM 2958 O20 OLC A2004 35.617 16.146 -10.983 1.00 70.45 O HETATM 2959 C1 OLB A2005 11.059 2.716 13.970 1.00 94.59 C HETATM 2960 C2 OLB A2005 12.064 2.969 12.856 1.00 94.70 C HETATM 2961 C3 OLB A2005 11.776 2.408 11.466 1.00 94.33 C HETATM 2962 C4 OLB A2005 12.166 3.256 10.256 1.00 93.84 C HETATM 2963 C5 OLB A2005 11.122 3.496 9.176 1.00 93.18 C HETATM 2964 O19 OLB A2005 9.863 2.858 13.750 1.00 95.44 O HETATM 2965 O20 OLB A2005 11.499 2.342 15.248 1.00 93.41 O HETATM 2966 C21 OLB A2005 11.381 3.238 16.324 1.00 92.74 C HETATM 2967 C22 OLB A2005 11.917 2.821 17.661 1.00 92.72 C HETATM 2968 O23 OLB A2005 13.141 3.409 17.890 1.00 92.58 O HETATM 2969 C24 OLB A2005 10.954 3.233 18.739 1.00 93.27 C HETATM 2970 O25 OLB A2005 10.984 4.547 19.176 1.00 93.55 O HETATM 2971 C6 OLB A2005 11.482 4.452 8.049 1.00 92.52 C HETATM 2972 C7 OLB A2005 10.903 4.178 6.677 1.00 92.07 C HETATM 2973 C8 OLB A2005 11.866 3.951 5.539 1.00 91.72 C HETATM 2974 C1 OLB A2006 2.413 26.295 -14.523 1.00 98.18 C HETATM 2975 C2 OLB A2006 2.924 27.687 -14.180 1.00 95.31 C HETATM 2976 C3 OLB A2006 3.739 27.898 -12.907 1.00 92.36 C HETATM 2977 C4 OLB A2006 3.092 28.639 -11.741 1.00 89.20 C HETATM 2978 C5 OLB A2006 2.837 27.866 -10.456 1.00 85.81 C HETATM 2979 O19 OLB A2006 2.956 25.300 -14.058 1.00 98.72 O HETATM 2980 O20 OLB A2006 1.230 26.157 -15.260 1.00100.12 O HETATM 2981 C21 OLB A2006 1.251 25.679 -16.582 1.00101.15 C HETATM 2982 C22 OLB A2006 0.611 24.347 -16.862 1.00101.78 C HETATM 2983 O23 OLB A2006 -0.616 24.247 -16.241 1.00102.26 O HETATM 2984 C24 OLB A2006 0.454 24.152 -18.345 1.00101.58 C HETATM 2985 O25 OLB A2006 -0.620 24.752 -18.975 1.00101.45 O HETATM 2986 C6 OLB A2006 3.278 28.518 -9.158 1.00 83.16 C HETATM 2987 C7 OLB A2006 2.234 28.756 -8.090 1.00 81.21 C HETATM 2988 C8 OLB A2006 2.618 29.643 -6.934 1.00 80.22 C HETATM 2989 C9 OLB A2006 1.874 29.452 -5.638 1.00 79.71 C HETATM 2990 C1 OLB A2007 3.185 21.413 -17.953 1.00 98.44 C HETATM 2991 C2 OLB A2007 3.034 21.178 -16.458 1.00 96.60 C HETATM 2992 C3 OLB A2007 4.074 21.785 -15.521 1.00 95.16 C HETATM 2993 C4 OLB A2007 3.718 21.969 -14.048 1.00 93.72 C HETATM 2994 C5 OLB A2007 4.777 22.567 -13.130 1.00 92.32 C HETATM 2995 O19 OLB A2007 3.427 22.543 -18.359 1.00 99.43 O HETATM 2996 O20 OLB A2007 3.235 20.329 -18.843 1.00 99.05 O HETATM 2997 C21 OLB A2007 2.284 20.190 -19.873 1.00 99.95 C HETATM 2998 C22 OLB A2007 2.769 19.962 -21.279 1.00100.75 C HETATM 2999 O23 OLB A2007 2.717 18.621 -21.604 1.00100.82 O HETATM 3000 C24 OLB A2007 1.933 20.752 -22.250 1.00101.03 C HETATM 3001 O25 OLB A2007 2.088 20.496 -23.603 1.00100.87 O HETATM 3002 C6 OLB A2007 4.341 23.025 -11.746 1.00 91.22 C HETATM 3003 C7 OLB A2007 5.411 23.303 -10.708 1.00 90.29 C HETATM 3004 C8 OLB A2007 5.054 23.117 -9.253 1.00 89.53 C HETATM 3005 C9 OLB A2007 6.057 22.439 -8.352 1.00 88.66 C HETATM 3006 C1 OLA A2008 22.496 31.903 2.445 1.00 97.51 C HETATM 3007 O1 OLA A2008 21.652 32.358 1.640 1.00 97.44 O HETATM 3008 O2 OLA A2008 23.704 31.940 2.119 1.00 98.58 O HETATM 3009 C2 OLA A2008 22.060 31.305 3.768 1.00 95.91 C HETATM 3010 C3 OLA A2008 22.524 32.153 4.954 1.00 94.66 C HETATM 3011 C4 OLA A2008 21.347 32.618 5.811 1.00 93.61 C HETATM 3012 C5 OLA A2008 21.281 31.876 7.144 1.00 92.35 C HETATM 3013 C6 OLA A2008 20.537 32.690 8.199 1.00 91.10 C HETATM 3014 C7 OLA A2008 19.562 31.821 8.990 1.00 89.79 C HETATM 3015 C8 OLA A2008 20.002 31.689 10.444 1.00 89.10 C HETATM 3016 C9 OLA A2008 18.927 32.239 11.363 1.00 88.74 C HETATM 3017 C10 OLA A2008 19.160 32.922 12.494 1.00 88.25 C HETATM 3018 C11 OLA A2008 20.537 33.254 13.037 1.00 87.85 C HETATM 3019 C12 OLA A2008 20.802 34.753 12.925 1.00 86.95 C HETATM 3020 C13 OLA A2008 22.284 35.026 12.682 1.00 85.86 C HETATM 3021 C14 OLA A2008 22.501 35.873 11.432 1.00 84.88 C HETATM 3022 C15 OLA A2008 23.160 35.064 10.320 1.00 83.98 C HETATM 3023 C16 OLA A2008 22.865 35.629 8.934 1.00 82.52 C HETATM 3024 C17 OLA A2008 24.159 35.959 8.198 1.00 81.97 C HETATM 3025 C18 OLA A2008 24.314 35.126 6.930 1.00 81.48 C HETATM 3026 C1 OLA A2009 25.397 5.526 17.140 1.00 93.06 C HETATM 3027 O1 OLA A2009 25.386 6.742 17.453 1.00 93.82 O HETATM 3028 O2 OLA A2009 25.798 4.689 17.982 1.00 93.91 O HETATM 3029 C2 OLA A2009 24.915 5.068 15.779 1.00 90.42 C HETATM 3030 C3 OLA A2009 25.976 5.309 14.709 1.00 87.50 C HETATM 3031 C4 OLA A2009 25.530 4.733 13.370 1.00 84.98 C HETATM 3032 C5 OLA A2009 26.299 5.349 12.207 1.00 83.43 C HETATM 3033 C6 OLA A2009 26.026 4.591 10.911 1.00 81.86 C HETATM 3034 C7 OLA A2009 26.166 5.488 9.684 1.00 80.40 C HETATM 3035 C8 OLA A2009 25.723 4.758 8.418 1.00 78.98 C HETATM 3036 C9 OLA A2009 26.920 4.542 7.514 1.00 77.31 C HETATM 3037 C10 OLA A2009 26.943 3.772 6.416 1.00 75.46 C HETATM 3038 C11 OLA A2009 25.778 2.976 5.861 1.00 73.39 C HETATM 3039 C12 OLA A2009 26.159 2.437 4.485 1.00 71.17 C HETATM 3040 C13 OLA A2009 24.924 2.119 3.649 1.00 68.66 C HETATM 3041 C14 OLA A2009 25.295 1.368 2.374 1.00 66.27 C HETATM 3042 C15 OLA A2009 24.075 0.704 1.743 1.00 64.13 C HETATM 3043 C1 PEG A2010 28.342 20.926 -19.857 1.00 75.08 C HETATM 3044 O1 PEG A2010 28.648 21.408 -21.182 1.00 75.47 O HETATM 3045 C2 PEG A2010 26.845 20.916 -19.413 1.00 75.22 C HETATM 3046 O2 PEG A2010 26.411 19.875 -18.782 1.00 75.33 O HETATM 3047 C3 PEG A2010 24.997 19.530 -18.824 1.00 74.68 C HETATM 3048 C4 PEG A2010 24.614 18.056 -19.042 1.00 74.08 C HETATM 3049 O4 PEG A2010 24.111 17.706 -20.252 1.00 73.84 O HETATM 3050 C1 PEG A2011 29.859 1.899 -2.174 1.00 88.56 C HETATM 3051 O1 PEG A2011 29.679 0.991 -3.281 1.00 87.89 O HETATM 3052 C2 PEG A2011 28.920 1.746 -0.933 1.00 88.89 C HETATM 3053 O2 PEG A2011 28.627 2.811 -0.258 1.00 88.86 O HETATM 3054 C3 PEG A2011 28.701 2.799 1.198 1.00 87.89 C HETATM 3055 C4 PEG A2011 29.038 4.119 1.917 1.00 86.48 C HETATM 3056 O4 PEG A2011 30.280 4.260 2.448 1.00 85.33 O HETATM 3057 O HOH A2012 10.270 21.253 -24.337 1.00 68.86 O HETATM 3058 O HOH A2013 26.834 23.318 -7.960 1.00 80.25 O HETATM 3059 O HOH A2014 23.055 3.015 18.834 1.00 65.18 O HETATM 3060 O HOH A2015 18.174 26.960 16.997 1.00 82.22 O HETATM 3061 O HOH A2016 26.900 9.200 20.268 1.00 68.01 O HETATM 3062 O HOH A2017 37.598 17.695 -14.217 1.00 60.58 O HETATM 3063 O HOH A2018 27.490 24.375 4.712 1.00 40.16 O HETATM 3064 O HOH A2019 12.130 23.449 12.411 1.00 84.59 O HETATM 3065 O HOH A2020 17.202 18.753 9.846 1.00 42.23 O CONECT 609 1168 CONECT 1168 609 CONECT 2447 2464 CONECT 2464 2447 CONECT 2819 2895 CONECT 2852 2853 2866 CONECT 2853 2852 2858 CONECT 2854 2861 CONECT 2855 2856 2894 CONECT 2856 2855 2857 CONECT 2857 2856 2858 CONECT 2858 2853 2857 2859 CONECT 2859 2858 2866 2894 CONECT 2860 2865 CONECT 2861 2854 2879 2891 CONECT 2862 2863 2867 2874 2879 CONECT 2863 2862 2880 2886 CONECT 2864 2868 2875 2886 CONECT 2865 2860 2885 2888 CONECT 2866 2852 2859 2878 CONECT 2867 2862 2873 CONECT 2868 2864 2887 2889 CONECT 2869 2870 2889 CONECT 2870 2869 2871 CONECT 2871 2870 2872 CONECT 2872 2871 2873 2889 CONECT 2873 2867 2872 2886 2890 CONECT 2874 2862 CONECT 2875 2864 2876 CONECT 2876 2875 2877 2884 CONECT 2877 2876 2881 CONECT 2878 2866 2885 CONECT 2879 2861 2862 CONECT 2880 2863 CONECT 2881 2877 2882 CONECT 2882 2881 2883 CONECT 2883 2882 2884 CONECT 2884 2876 2883 CONECT 2885 2865 2878 2893 CONECT 2886 2863 2864 2873 CONECT 2887 2868 CONECT 2888 2865 2891 CONECT 2889 2868 2869 2872 CONECT 2890 2873 CONECT 2891 2861 2888 2892 CONECT 2892 2891 2893 CONECT 2893 2885 2892 2894 CONECT 2894 2855 2859 2893 CONECT 2895 2819 2896 2897 CONECT 2896 2895 CONECT 2897 2895 2898 CONECT 2898 2897 2899 CONECT 2899 2898 2900 CONECT 2900 2899 2901 CONECT 2901 2900 2902 CONECT 2902 2901 2903 CONECT 2903 2902 2904 CONECT 2904 2903 2905 CONECT 2905 2904 2906 CONECT 2906 2905 2907 CONECT 2907 2906 2908 CONECT 2908 2907 2909 CONECT 2909 2908 2910 CONECT 2910 2909 2911 CONECT 2911 2910 CONECT 2912 2913 2921 CONECT 2913 2912 2914 CONECT 2914 2913 2915 2939 CONECT 2915 2914 2916 CONECT 2916 2915 2917 2921 CONECT 2917 2916 2918 CONECT 2918 2917 2919 CONECT 2919 2918 2920 2925 CONECT 2920 2919 2921 2922 CONECT 2921 2912 2916 2920 2930 CONECT 2922 2920 2923 CONECT 2923 2922 2924 CONECT 2924 2923 2925 2928 2929 CONECT 2925 2919 2924 2926 CONECT 2926 2925 2927 CONECT 2927 2926 2928 CONECT 2928 2924 2927 2931 CONECT 2929 2924 CONECT 2930 2921 CONECT 2931 2928 2932 2933 CONECT 2932 2931 CONECT 2933 2931 2934 CONECT 2934 2933 2935 CONECT 2935 2934 2936 CONECT 2936 2935 2937 2938 CONECT 2937 2936 CONECT 2938 2936 CONECT 2939 2914 CONECT 2940 2941 2942 CONECT 2941 2940 2943 CONECT 2942 2940 2945 CONECT 2943 2941 2946 CONECT 2944 2954 2956 CONECT 2945 2942 CONECT 2946 2943 2947 CONECT 2947 2946 2948 CONECT 2948 2947 2949 CONECT 2949 2948 2950 CONECT 2950 2949 2951 CONECT 2951 2950 2953 CONECT 2952 2954 2958 CONECT 2953 2951 2955 2958 CONECT 2954 2944 2952 2957 CONECT 2955 2953 CONECT 2956 2944 CONECT 2957 2954 CONECT 2958 2952 2953 CONECT 2959 2960 2964 2965 CONECT 2960 2959 2961 CONECT 2961 2960 2962 CONECT 2962 2961 2963 CONECT 2963 2962 2971 CONECT 2964 2959 CONECT 2965 2959 2966 CONECT 2966 2965 2967 CONECT 2967 2966 2968 2969 CONECT 2968 2967 CONECT 2969 2967 2970 CONECT 2970 2969 CONECT 2971 2963 2972 CONECT 2972 2971 2973 CONECT 2973 2972 CONECT 2974 2975 2979 2980 CONECT 2975 2974 2976 CONECT 2976 2975 2977 CONECT 2977 2976 2978 CONECT 2978 2977 2986 CONECT 2979 2974 CONECT 2980 2974 2981 CONECT 2981 2980 2982 CONECT 2982 2981 2983 2984 CONECT 2983 2982 CONECT 2984 2982 2985 CONECT 2985 2984 CONECT 2986 2978 2987 CONECT 2987 2986 2988 CONECT 2988 2987 2989 CONECT 2989 2988 CONECT 2990 2991 2995 2996 CONECT 2991 2990 2992 CONECT 2992 2991 2993 CONECT 2993 2992 2994 CONECT 2994 2993 3002 CONECT 2995 2990 CONECT 2996 2990 2997 CONECT 2997 2996 2998 CONECT 2998 2997 2999 3000 CONECT 2999 2998 CONECT 3000 2998 3001 CONECT 3001 3000 CONECT 3002 2994 3003 CONECT 3003 3002 3004 CONECT 3004 3003 3005 CONECT 3005 3004 CONECT 3006 3007 3008 3009 CONECT 3007 3006 CONECT 3008 3006 CONECT 3009 3006 3010 CONECT 3010 3009 3011 CONECT 3011 3010 3012 CONECT 3012 3011 3013 CONECT 3013 3012 3014 CONECT 3014 3013 3015 CONECT 3015 3014 3016 CONECT 3016 3015 3017 CONECT 3017 3016 3018 CONECT 3018 3017 3019 CONECT 3019 3018 3020 CONECT 3020 3019 3021 CONECT 3021 3020 3022 CONECT 3022 3021 3023 CONECT 3023 3022 3024 CONECT 3024 3023 3025 CONECT 3025 3024 CONECT 3026 3027 3028 3029 CONECT 3027 3026 CONECT 3028 3026 CONECT 3029 3026 3030 CONECT 3030 3029 3031 CONECT 3031 3030 3032 CONECT 3032 3031 3033 CONECT 3033 3032 3034 CONECT 3034 3033 3035 CONECT 3035 3034 3036 CONECT 3036 3035 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3039 CONECT 3039 3038 3040 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3041 CONECT 3043 3044 3045 CONECT 3044 3043 CONECT 3045 3043 3046 CONECT 3046 3045 3047 CONECT 3047 3046 3048 CONECT 3048 3047 3049 CONECT 3049 3048 CONECT 3050 3051 3052 CONECT 3051 3050 CONECT 3052 3050 3053 CONECT 3053 3052 3054 CONECT 3054 3053 3055 CONECT 3055 3054 3056 CONECT 3056 3055 MASTER 438 0 11 18 0 0 16 6 3063 1 210 34 END