HEADER SIGNALING PROTEIN 21-JUN-13 4BUO TITLE HIGH RESOLUTION STRUCTURE OF THERMOSTABLE AGONIST-BOUND TITLE 2 NEUROTENSIN RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUROTENSIN RECEPTOR TYPE 1; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 50-272 AND 291-390; COMPND 5 SYNONYM: NT-R-1, NTR1, HIGH-AFFINITY LEVOCABASTINE-INSENSITIVE COMPND 6 NEUROTENSIN RECEPTOR, NTRH; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 OTHER_DETAILS: THERMOSTABLE MUTANT WITH INTRACELLULAR LOOP 3 COMPND 10 DELETION B (E273-T290); COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: NEUROTENSIN/NEUROMEDIN N; COMPND 13 CHAIN: C, D; COMPND 14 FRAGMENT: C-TERMINUS, RESIDUES 8-13; COMPND 15 SYNONYM: NEUROTENSIN, NT; COMPND 16 ENGINEERED: YES; COMPND 17 OTHER_DETAILS: RESIDUES 8-13 CORRESPOND TO NEUROTENSIN C- TERMINUS. COMPND 18 RESIDUES 4-7 ARE PART OF AN ARTIFICIAL LINKER AND DO NOT COMPND 19 CORRESPOND TO NEUROTENSIN SEQUENCE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VARIANT: TUNER; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEP-TM86VDIC3III; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_COMMON: NORWAY RAT; SOURCE 14 ORGANISM_TAXID: 10116; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS SIGNALING PROTEIN, G PROTEIN COUPLED RECEPTOR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.EGLOFF,M.HILLENBRAND,K.M.SCHLINKMANN,A.BATYUK,P.MITTL,A.PLUECKTHUN REVDAT 3 26-FEB-14 4BUO 1 JRNL REVDAT 2 05-FEB-14 4BUO 1 JRNL REVDAT 1 29-JAN-14 4BUO 0 JRNL AUTH P.EGLOFF,M.HILLENBRAND,C.KLENK,A.BATYUK,P.HEINE,S.BALADA, JRNL AUTH 2 K.M.SCHLINKMANN,D.J.SCOTT,M.SCHUETZ,A.PLUECKTHUN JRNL TITL STRUCTURE OF SIGNALING-COMPETENT NEUROTENSIN RECEPTOR 1 JRNL TITL 2 OBTAINED BY DIRECTED EVOLUTION IN ESCHERICHIA COLI JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 E655 2014 JRNL REFN ISSN 0027-8424 JRNL PMID 24453215 JRNL DOI 10.1073/PNAS.1317903111 REMARK 2 REMARK 2 RESOLUTION. 2.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.750 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.821 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.35 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.75 REMARK 3 NUMBER OF REFLECTIONS : 31649 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.2490 REMARK 3 R VALUE (WORKING SET) : 0.2478 REMARK 3 FREE R VALUE : 0.2728 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0 REMARK 3 FREE R VALUE TEST SET COUNT : 1581 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 19.8216 - 6.0625 1.00 2950 155 0.2321 0.2527 REMARK 3 2 6.0625 - 4.8350 1.00 2805 148 0.2401 0.2657 REMARK 3 3 4.8350 - 4.2306 1.00 2784 146 0.2048 0.2228 REMARK 3 4 4.2306 - 3.8469 1.00 2788 147 0.2286 0.2591 REMARK 3 5 3.8469 - 3.5729 1.00 2748 144 0.2561 0.2899 REMARK 3 6 3.5729 - 3.3633 1.00 2754 145 0.2758 0.3257 REMARK 3 7 3.3633 - 3.1956 1.00 2718 143 0.3071 0.3682 REMARK 3 8 3.1956 - 3.0570 1.00 2730 144 0.3354 0.3521 REMARK 3 9 3.0570 - 2.9397 1.00 2740 144 0.3969 0.4093 REMARK 3 10 2.9397 - 2.8386 0.99 2677 143 0.4339 0.4554 REMARK 3 11 2.8386 - 2.7500 0.88 2374 122 0.4691 0.4789 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.55 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.94 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 109.97 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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 : 0.003 5160 REMARK 3 ANGLE : 0.653 7020 REMARK 3 CHIRALITY : 0.047 845 REMARK 3 PLANARITY : 0.003 854 REMARK 3 DIHEDRAL : 10.140 1774 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESSEQ 52:93 OR REMARK 3 RESSEQ 97:270 OR RESSEQ 297:384)) REMARK 3 SELECTION : (CHAIN B AND (RESSEQ 49:91 OR REMARK 3 RESSEQ 98:272 OR RESSEQ 291:386)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 NCS GROUP : 2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: CHAIN C REMARK 3 SELECTION : CHAIN D REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: PHENIX AND REFMAC WERE USED. REMARK 4 REMARK 4 4BUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-13. REMARK 100 THE PDBE ID CODE IS EBI-57351. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-AUG-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06DA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PILATUS REMARK 200 DETECTOR MANUFACTURER : DECTRIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32141 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.75 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.1 REMARK 200 R MERGE (I) : 0.08 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.85 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7 REMARK 200 DATA REDUNDANCY IN SHELL : 13.9 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.45 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: PDB ENTRY 3ZEV REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 21.5% (V/V) PEG600, 2 M NACL, 50 REMARK 280 MM GLYCINE PH 9.4 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.65500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.06500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.70000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.06500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.65500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.70000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.3 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15400 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.9 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A 47 REMARK 465 GLY A 48 REMARK 465 SER A 49 REMARK 465 GLY A 50 REMARK 465 PRO A 51 REMARK 465 SER A 94 REMARK 465 LEU A 95 REMARK 465 GLN A 96 REMARK 465 ALA A 271 REMARK 465 ALA A 272 REMARK 465 PHE A 291 REMARK 465 ASN A 292 REMARK 465 MET A 293 REMARK 465 THR A 294 REMARK 465 ILE A 295 REMARK 465 GLU A 296 REMARK 465 ALA A 385 REMARK 465 CYS A 386 REMARK 465 LEU A 387 REMARK 465 CYS A 388 REMARK 465 PRO A 389 REMARK 465 GLY A 390 REMARK 465 THR A 391 REMARK 465 ARG A 392 REMARK 465 GLU A 393 REMARK 465 LEU A 394 REMARK 465 GLU A 395 REMARK 465 VAL A 396 REMARK 465 LEU A 397 REMARK 465 PHE A 398 REMARK 465 GLN A 399 REMARK 465 PRO B 47 REMARK 465 GLY B 48 REMARK 465 LYS B 92 REMARK 465 LYS B 93 REMARK 465 SER B 94 REMARK 465 LEU B 95 REMARK 465 GLN B 96 REMARK 465 SER B 97 REMARK 465 LEU B 387 REMARK 465 CYS B 388 REMARK 465 PRO B 389 REMARK 465 GLY B 390 REMARK 465 THR B 391 REMARK 465 ARG B 392 REMARK 465 GLU B 393 REMARK 465 LEU B 394 REMARK 465 GLU B 395 REMARK 465 VAL B 396 REMARK 465 LEU B 397 REMARK 465 PHE B 398 REMARK 465 GLN B 399 REMARK 465 GLY C 4 REMARK 465 PRO C 5 REMARK 465 GLY C 6 REMARK 465 GLY C 7 REMARK 465 GLY D 4 REMARK 465 PRO D 5 REMARK 465 GLY D 6 REMARK 465 GLY D 7 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 GLN A 270 CG CD OE1 NE2 REMARK 470 ARG B 91 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LEU A 98 OG1 THR A 101 2.20 REMARK 500 REMARK 500 REMARK: NULL 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 PHE A 246 -76.07 -129.97 REMARK 500 ASN B 52 44.42 -75.88 REMARK 500 SER B 53 67.84 -115.36 REMARK 500 ASP B 54 63.94 -69.89 REMARK 500 TRP B 130 -81.75 -96.39 REMARK 500 PHE B 175 -61.29 -95.55 REMARK 500 LYS B 176 47.52 -107.17 REMARK 500 LYS B 178 -105.79 47.36 REMARK 500 LEU B 213 34.61 -86.50 REMARK 500 PHE B 246 -76.28 -127.81 REMARK 500 THR B 294 -155.89 -159.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1385 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1387 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1389 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1390 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1391 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1387 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1388 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1389 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ZEV RELATED DB: PDB REMARK 900 STRUCTURE OF THERMOSTABLE AGONIST-BOUND NEUROTENSIN REMARK 900 RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION REMARK 900 RELATED ID: 4BV0 RELATED DB: PDB REMARK 900 HIGH RESOLUTION STRUCTURE OF EVOLVED AGONIST-BOUND REMARK 900 NEUROTENSIN RECEPTOR 1 MUTANT WITHOUT LYSOZYME FUSION REMARK 900 RELATED ID: 4BWB RELATED DB: PDB REMARK 900 STRUCTURE OF EVOLVED AGONIST-BOUND NEUROTENSIN RECEPTOR REMARK 900 1 MUTANT WITHOUT LYSOZYME FUSION REMARK 999 REMARK 999 SEQUENCE REMARK 999 CHAINS C AND D - THE SEQUENCE RRPYIL REPRESENTS NEUROTENSIN REMARK 999 RESIDUES 8-13 AND THE REST IS LINKER. DBREF 4BUO A 50 272 UNP P20789 NTR1_RAT 50 272 DBREF 4BUO A 291 390 UNP P20789 NTR1_RAT 291 390 DBREF 4BUO B 50 272 UNP P20789 NTR1_RAT 50 272 DBREF 4BUO B 291 390 UNP P20789 NTR1_RAT 291 390 DBREF 4BUO C 8 13 UNP P20068 NEUT_RAT 157 162 DBREF 4BUO D 8 13 UNP P20068 NEUT_RAT 157 162 SEQADV 4BUO PRO A 47 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLY A 48 UNP P20789 EXPRESSION TAG SEQADV 4BUO SER A 49 UNP P20789 EXPRESSION TAG SEQADV 4BUO THR A 391 UNP P20789 EXPRESSION TAG SEQADV 4BUO ARG A 392 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLU A 393 UNP P20789 EXPRESSION TAG SEQADV 4BUO LEU A 394 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLU A 395 UNP P20789 EXPRESSION TAG SEQADV 4BUO VAL A 396 UNP P20789 EXPRESSION TAG SEQADV 4BUO LEU A 397 UNP P20789 EXPRESSION TAG SEQADV 4BUO PHE A 398 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLN A 399 UNP P20789 EXPRESSION TAG SEQADV 4BUO LEU A 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 4BUO ASP A 103 UNP P20789 HIS 103 ENGINEERED MUTATION SEQADV 4BUO TYR A 105 UNP P20789 HIS 105 ENGINEERED MUTATION SEQADV 4BUO VAL A 161 UNP P20789 ALA 161 ENGINEERED MUTATION SEQADV 4BUO LEU A 167 UNP P20789 ARG 167 ENGINEERED MUTATION SEQADV 4BUO LEU A 213 UNP P20789 ARG 213 ENGINEERED MUTATION SEQADV 4BUO LEU A 234 UNP P20789 VAL 234 ENGINEERED MUTATION SEQADV 4BUO ALA A 253 UNP P20789 ILE 253 ENGINEERED MUTATION SEQADV 4BUO ARG A 305 UNP P20789 HIS 305 ENGINEERED MUTATION SEQADV 4BUO VAL A 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 4BUO ALA A 362 UNP P20789 SER 362 ENGINEERED MUTATION SEQADV 4BUO PRO B 47 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLY B 48 UNP P20789 EXPRESSION TAG SEQADV 4BUO SER B 49 UNP P20789 EXPRESSION TAG SEQADV 4BUO THR B 391 UNP P20789 EXPRESSION TAG SEQADV 4BUO ARG B 392 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLU B 393 UNP P20789 EXPRESSION TAG SEQADV 4BUO LEU B 394 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLU B 395 UNP P20789 EXPRESSION TAG SEQADV 4BUO VAL B 396 UNP P20789 EXPRESSION TAG SEQADV 4BUO LEU B 397 UNP P20789 EXPRESSION TAG SEQADV 4BUO PHE B 398 UNP P20789 EXPRESSION TAG SEQADV 4BUO GLN B 399 UNP P20789 EXPRESSION TAG SEQADV 4BUO LEU B 86 UNP P20789 ALA 86 ENGINEERED MUTATION SEQADV 4BUO ASP B 103 UNP P20789 HIS 103 ENGINEERED MUTATION SEQADV 4BUO TYR B 105 UNP P20789 HIS 105 ENGINEERED MUTATION SEQADV 4BUO VAL B 161 UNP P20789 ALA 161 ENGINEERED MUTATION SEQADV 4BUO LEU B 167 UNP P20789 ARG 167 ENGINEERED MUTATION SEQADV 4BUO LEU B 213 UNP P20789 ARG 213 ENGINEERED MUTATION SEQADV 4BUO LEU B 234 UNP P20789 VAL 234 ENGINEERED MUTATION SEQADV 4BUO ALA B 253 UNP P20789 ILE 253 ENGINEERED MUTATION SEQADV 4BUO ARG B 305 UNP P20789 HIS 305 ENGINEERED MUTATION SEQADV 4BUO VAL B 358 UNP P20789 PHE 358 ENGINEERED MUTATION SEQADV 4BUO ALA B 362 UNP P20789 SER 362 ENGINEERED MUTATION SEQADV 4BUO GLY C 4 UNP P20068 SEE REMARK 999 SEQADV 4BUO PRO C 5 UNP P20068 SEE REMARK 999 SEQADV 4BUO GLY C 6 UNP P20068 SEE REMARK 999 SEQADV 4BUO GLY C 7 UNP P20068 SEE REMARK 999 SEQADV 4BUO GLY D 4 UNP P20068 SEE REMARK 999 SEQADV 4BUO PRO D 5 UNP P20068 SEE REMARK 999 SEQADV 4BUO GLY D 6 UNP P20068 SEE REMARK 999 SEQADV 4BUO GLY D 7 UNP P20068 SEE REMARK 999 SEQRES 1 A 335 PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN THR SEQRES 2 A 335 ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR LEU SEQRES 3 A 335 ALA LEU PHE VAL VAL GLY THR VAL GLY ASN SER VAL THR SEQRES 4 A 335 LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER LEU SEQRES 5 A 335 GLN SER THR VAL ASP TYR TYR LEU GLY SER LEU ALA LEU SEQRES 6 A 335 SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL GLU SEQRES 7 A 335 LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA PHE SEQRES 8 A 335 GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG ASP SEQRES 9 A 335 ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER LEU SEQRES 10 A 335 SER VAL GLU LEU TYR LEU ALA ILE CYS HIS PRO PHE LYS SEQRES 11 A 335 ALA LYS THR LEU MET SER ARG SER ARG THR LYS LYS PHE SEQRES 12 A 335 ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA ILE SEQRES 13 A 335 PRO MET LEU PHE THR MET GLY LEU GLN ASN LEU SER GLY SEQRES 14 A 335 ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO ILE SEQRES 15 A 335 VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN VAL ASN SEQRES 16 A 335 THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA SER SEQRES 17 A 335 ILE LEU ASN THR VAL ILE ALA ASN LYS LEU THR VAL MET SEQRES 18 A 335 VAL HIS GLN ALA ALA PHE ASN MET THR ILE GLU PRO GLY SEQRES 19 A 335 ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU VAL LEU ARG SEQRES 20 A 335 ALA VAL VAL ILE ALA PHE VAL VAL CYS TRP LEU PRO TYR SEQRES 21 A 335 HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SER ASP GLU SEQRES 22 A 335 GLN TRP THR THR PHE LEU PHE ASP PHE TYR HIS TYR PHE SEQRES 23 A 335 TYR MET LEU THR ASN ALA LEU VAL TYR VAL SER ALA ALA SEQRES 24 A 335 ILE ASN PRO ILE LEU TYR ASN LEU VAL SER ALA ASN PHE SEQRES 25 A 335 ARG GLN VAL PHE LEU SER THR LEU ALA CYS LEU CYS PRO SEQRES 26 A 335 GLY THR ARG GLU LEU GLU VAL LEU PHE GLN SEQRES 1 B 335 PRO GLY SER GLY PRO ASN SER ASP LEU ASP VAL ASN THR SEQRES 2 B 335 ASP ILE TYR SER LYS VAL LEU VAL THR ALA ILE TYR LEU SEQRES 3 B 335 ALA LEU PHE VAL VAL GLY THR VAL GLY ASN SER VAL THR SEQRES 4 B 335 LEU PHE THR LEU ALA ARG LYS LYS SER LEU GLN SER LEU SEQRES 5 B 335 GLN SER THR VAL ASP TYR TYR LEU GLY SER LEU ALA LEU SEQRES 6 B 335 SER ASP LEU LEU ILE LEU LEU LEU ALA MET PRO VAL GLU SEQRES 7 B 335 LEU TYR ASN PHE ILE TRP VAL HIS HIS PRO TRP ALA PHE SEQRES 8 B 335 GLY ASP ALA GLY CYS ARG GLY TYR TYR PHE LEU ARG ASP SEQRES 9 B 335 ALA CYS THR TYR ALA THR ALA LEU ASN VAL VAL SER LEU SEQRES 10 B 335 SER VAL GLU LEU TYR LEU ALA ILE CYS HIS PRO PHE LYS SEQRES 11 B 335 ALA LYS THR LEU MET SER ARG SER ARG THR LYS LYS PHE SEQRES 12 B 335 ILE SER ALA ILE TRP LEU ALA SER ALA LEU LEU ALA ILE SEQRES 13 B 335 PRO MET LEU PHE THR MET GLY LEU GLN ASN LEU SER GLY SEQRES 14 B 335 ASP GLY THR HIS PRO GLY GLY LEU VAL CYS THR PRO ILE SEQRES 15 B 335 VAL ASP THR ALA THR LEU LYS VAL VAL ILE GLN VAL ASN SEQRES 16 B 335 THR PHE MET SER PHE LEU PHE PRO MET LEU VAL ALA SER SEQRES 17 B 335 ILE LEU ASN THR VAL ILE ALA ASN LYS LEU THR VAL MET SEQRES 18 B 335 VAL HIS GLN ALA ALA PHE ASN MET THR ILE GLU PRO GLY SEQRES 19 B 335 ARG VAL GLN ALA LEU ARG ARG GLY VAL LEU VAL LEU ARG SEQRES 20 B 335 ALA VAL VAL ILE ALA PHE VAL VAL CYS TRP LEU PRO TYR SEQRES 21 B 335 HIS VAL ARG ARG LEU MET PHE CYS TYR ILE SER ASP GLU SEQRES 22 B 335 GLN TRP THR THR PHE LEU PHE ASP PHE TYR HIS TYR PHE SEQRES 23 B 335 TYR MET LEU THR ASN ALA LEU VAL TYR VAL SER ALA ALA SEQRES 24 B 335 ILE ASN PRO ILE LEU TYR ASN LEU VAL SER ALA ASN PHE SEQRES 25 B 335 ARG GLN VAL PHE LEU SER THR LEU ALA CYS LEU CYS PRO SEQRES 26 B 335 GLY THR ARG GLU LEU GLU VAL LEU PHE GLN SEQRES 1 C 10 GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU SEQRES 1 D 10 GLY PRO GLY GLY ARG ARG PRO TYR ILE LEU HET GLY A1385 5 HET GLY A1386 5 HET GLY A1387 5 HET GLY A1388 5 HET GLY A1389 5 HET GLY A1390 5 HET GLY A1391 5 HET GLY A1392 5 HET GLY B1387 5 HET GLY B1388 5 HET GLY B1389 5 HETNAM GLY GLYCINE FORMUL 3 GLY 11(C2 H5 N O2) HELIX 1 1 ASP A 60 ARG A 91 1 32 HELIX 2 2 LEU A 98 LEU A 119 1 22 HELIX 3 3 LEU A 119 TRP A 130 1 12 HELIX 4 4 PHE A 137 HIS A 173 1 37 HELIX 5 5 HIS A 173 THR A 179 1 7 HELIX 6 6 SER A 182 ILE A 202 1 21 HELIX 7 7 PRO A 203 THR A 207 1 5 HELIX 8 8 HIS A 219 GLY A 221 5 3 HELIX 9 9 ASP A 230 PHE A 246 1 17 HELIX 10 10 PHE A 246 GLN A 270 1 25 HELIX 11 11 PRO A 297 ILE A 334 1 38 HELIX 12 12 THR A 340 SER A 373 1 34 HELIX 13 13 SER A 373 LEU A 384 1 12 HELIX 14 14 ASP B 60 ALA B 90 1 31 HELIX 15 15 GLN B 99 PHE B 128 1 30 HELIX 16 16 PHE B 137 HIS B 173 1 37 HELIX 17 17 SER B 182 ILE B 202 1 21 HELIX 18 18 PRO B 203 THR B 207 1 5 HELIX 19 19 HIS B 219 GLY B 221 5 3 HELIX 20 20 ASP B 230 PHE B 246 1 17 HELIX 21 21 PHE B 246 ALA B 272 1 27 HELIX 22 22 GLU B 296 ILE B 334 1 39 HELIX 23 23 THR B 340 ALA B 385 1 46 SHEET 1 AA 2 MET A 208 ASN A 212 0 SHEET 2 AA 2 LEU A 223 PRO A 227 -1 O VAL A 224 N GLN A 211 SHEET 1 BA 2 MET B 208 ASN B 212 0 SHEET 2 BA 2 LEU B 223 PRO B 227 -1 O VAL B 224 N GLN B 211 SSBOND 1 CYS A 142 CYS A 225 1555 1555 2.03 SSBOND 2 CYS B 142 CYS B 225 1555 1555 2.03 CISPEP 1 HIS A 133 PRO A 134 0 0.43 CISPEP 2 GLY B 50 PRO B 51 0 -1.22 CISPEP 3 HIS B 133 PRO B 134 0 -0.33 SITE 1 AC1 1 PHE A 206 SITE 1 AC2 2 ASP A 103 TYR A 104 SITE 1 AC3 3 GLU A 166 MET A 181 PHE B 243 SITE 1 AC4 2 LEU A 322 VAL A 326 SITE 1 AC5 1 ALA A 140 SITE 1 AC6 1 PHE A 206 SITE 1 AC7 1 TRP B 194 SITE 1 AC8 4 GLN B 99 ARG B 305 SER B 373 ASN B 375 SITE 1 AC9 5 LEU A 247 PHE A 248 LEU B 180 MET B 181 SITE 2 AC9 5 PHE B 189 CRYST1 63.310 89.400 212.130 90.00 90.00 90.00 P 21 21 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 0.015795 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011186 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004714 0.00000 MTRIX1 1 -0.897400 -0.096480 0.430500 26.98000 1 MTRIX2 1 -0.055670 -0.943200 -0.327400 -22.54000 1 MTRIX3 1 0.437700 -0.317800 0.841100 -10.70000 1 ATOM 1 N ASN A 52 5.307 -37.589 -56.582 1.00152.42 N ANISOU 1 N ASN A 52 25901 15492 16518 1039 117 -3869 N ATOM 2 CA ASN A 52 6.520 -37.217 -55.862 1.00150.08 C ANISOU 2 CA ASN A 52 25091 15374 16557 1090 200 -3519 C ATOM 3 C ASN A 52 6.576 -37.809 -54.456 1.00150.52 C ANISOU 3 C ASN A 52 25137 15051 17001 1133 132 -3445 C ATOM 4 O ASN A 52 5.789 -37.445 -53.584 1.00148.44 O ANISOU 4 O ASN A 52 24597 14797 17005 910 -49 -3189 O ATOM 5 CB ASN A 52 6.672 -35.693 -55.811 1.00 94.83 C ANISOU 5 CB ASN A 52 17755 8695 9583 743 -18 -3255 C ATOM 6 CG ASN A 52 5.351 -34.979 -55.586 1.00 96.19 C ANISOU 6 CG ASN A 52 18110 8676 9761 335 -418 -3304 C ATOM 7 OD1 ASN A 52 4.425 -35.528 -54.991 1.00 99.86 O ANISOU 7 OD1 ASN A 52 18852 8737 10355 262 -566 -3437 O ATOM 8 ND2 ASN A 52 5.256 -33.750 -56.075 1.00 93.61 N ANISOU 8 ND2 ASN A 52 17624 8637 9306 64 -602 -3186 N ATOM 9 N SER A 53 7.514 -38.725 -54.242 1.00137.26 N ANISOU 9 N SER A 53 23769 13037 15346 1432 285 -3669 N ATOM 10 CA SER A 53 7.649 -39.380 -52.947 1.00137.72 C ANISOU 10 CA SER A 53 23838 12719 15768 1533 251 -3593 C ATOM 11 C SER A 53 8.830 -38.829 -52.154 1.00136.48 C ANISOU 11 C SER A 53 23229 12775 15851 1814 496 -3321 C ATOM 12 O SER A 53 9.338 -39.485 -51.244 1.00136.38 O ANISOU 12 O SER A 53 23127 12530 16160 1887 463 -3174 O ATOM 13 CB SER A 53 7.784 -40.894 -53.120 1.00107.32 C ANISOU 13 CB SER A 53 20510 8403 11864 1771 316 -3938 C ATOM 14 OG SER A 53 8.929 -41.221 -53.887 1.00110.41 O ANISOU 14 OG SER A 53 20958 8935 12058 2199 684 -4110 O ATOM 15 N ASP A 54 9.261 -37.621 -52.503 1.00 99.45 N ANISOU 15 N ASP A 54 18263 8527 10997 1957 728 -3245 N ATOM 16 CA ASP A 54 10.371 -36.976 -51.811 1.00 98.48 C ANISOU 16 CA ASP A 54 17705 8645 11069 2220 964 -2999 C ATOM 17 C ASP A 54 9.890 -36.168 -50.609 1.00 95.29 C ANISOU 17 C ASP A 54 16877 8450 10880 1952 795 -2644 C ATOM 18 O ASP A 54 10.642 -35.949 -49.659 1.00 94.43 O ANISOU 18 O ASP A 54 16457 8397 11026 2097 878 -2416 O ATOM 19 CB ASP A 54 11.159 -36.082 -52.770 1.00145.79 C ANISOU 19 CB ASP A 54 23562 15028 16803 2458 1283 -3049 C ATOM 20 CG ASP A 54 11.912 -36.874 -53.819 1.00149.19 C ANISOU 20 CG ASP A 54 24388 15286 17011 2776 1508 -3398 C ATOM 21 OD1 ASP A 54 12.312 -38.020 -53.525 1.00151.11 O ANISOU 21 OD1 ASP A 54 24936 15092 17384 2931 1480 -3568 O ATOM 22 OD2 ASP A 54 12.105 -36.352 -54.937 1.00150.02 O ANISOU 22 OD2 ASP A 54 24509 15687 16804 2875 1720 -3502 O ATOM 23 N LEU A 55 8.636 -35.730 -50.655 1.00 88.63 N ANISOU 23 N LEU A 55 16025 7726 9926 1570 554 -2601 N ATOM 24 CA LEU A 55 8.056 -34.956 -49.563 1.00 84.47 C ANISOU 24 CA LEU A 55 15125 7389 9580 1307 390 -2290 C ATOM 25 C LEU A 55 7.325 -35.860 -48.577 1.00 84.03 C ANISOU 25 C LEU A 55 15145 6999 9782 1085 134 -2208 C ATOM 26 O LEU A 55 6.609 -35.381 -47.697 1.00 82.38 O ANISOU 26 O LEU A 55 14813 6869 9619 746 -93 -2073 O ATOM 27 CB LEU A 55 7.097 -33.885 -50.097 1.00 67.54 C ANISOU 27 CB LEU A 55 12902 5555 7206 1023 263 -2264 C ATOM 28 CG LEU A 55 7.658 -32.771 -50.987 1.00 64.21 C ANISOU 28 CG LEU A 55 12199 5575 6622 1129 465 -2157 C ATOM 29 CD1 LEU A 55 9.035 -32.339 -50.506 1.00 68.77 C ANISOU 29 CD1 LEU A 55 12945 6204 6980 1456 762 -2361 C ATOM 30 CD2 LEU A 55 7.709 -33.202 -52.446 1.00 61.77 C ANISOU 30 CD2 LEU A 55 11840 5506 6125 819 278 -2111 C ATOM 31 N ASP A 56 7.507 -37.168 -48.728 1.00 68.95 N ANISOU 31 N ASP A 56 13434 4719 8046 1281 177 -2280 N ATOM 32 CA ASP A 56 6.854 -38.135 -47.854 1.00 70.49 C ANISOU 32 CA ASP A 56 13747 4554 8482 1074 -57 -2203 C ATOM 33 C ASP A 56 7.593 -38.293 -46.529 1.00 69.08 C ANISOU 33 C ASP A 56 13347 4295 8604 1271 31 -1967 C ATOM 34 O ASP A 56 8.816 -38.425 -46.501 1.00 69.15 O ANISOU 34 O ASP A 56 13224 4411 8639 1631 275 -1947 O ATOM 35 CB ASP A 56 6.728 -39.494 -48.548 1.00 96.84 C ANISOU 35 CB ASP A 56 17607 7429 11759 1070 -156 -2508 C ATOM 36 CG ASP A 56 5.773 -39.461 -49.724 1.00 97.09 C ANISOU 36 CG ASP A 56 17870 7492 11528 760 -351 -2703 C ATOM 37 OD1 ASP A 56 5.827 -38.491 -50.506 1.00 99.59 O ANISOU 37 OD1 ASP A 56 18597 7606 11639 859 -326 -3020 O ATOM 38 OD2 ASP A 56 4.964 -40.401 -49.862 1.00 94.79 O ANISOU 38 OD2 ASP A 56 17354 7431 11232 426 -534 -2541 O ATOM 39 N VAL A 57 6.837 -38.281 -45.436 1.00 68.39 N ANISOU 39 N VAL A 57 13215 4028 8740 1033 -170 -1779 N ATOM 40 CA VAL A 57 7.397 -38.472 -44.104 1.00 67.71 C ANISOU 40 CA VAL A 57 12953 3846 8928 1190 -120 -1539 C ATOM 41 C VAL A 57 7.139 -39.893 -43.614 1.00 73.27 C ANISOU 41 C VAL A 57 13987 4034 9819 1094 -292 -1567 C ATOM 42 O VAL A 57 5.990 -40.325 -43.515 1.00 75.10 O ANISOU 42 O VAL A 57 14412 4094 10028 748 -514 -1631 O ATOM 43 CB VAL A 57 6.803 -37.473 -43.098 1.00 61.08 C ANISOU 43 CB VAL A 57 11681 3345 8182 988 -179 -1211 C ATOM 44 CG1 VAL A 57 7.222 -37.833 -41.687 1.00 60.97 C ANISOU 44 CG1 VAL A 57 11501 3244 8420 1159 -134 -963 C ATOM 45 CG2 VAL A 57 7.230 -36.055 -43.446 1.00 55.86 C ANISOU 45 CG2 VAL A 57 10724 3165 7336 1042 -38 -1187 C ATOM 46 N ASN A 58 8.213 -40.614 -43.308 1.00136.64 N ANISOU 46 N ASN A 58 22069 11808 18039 1394 -201 -1505 N ATOM 47 CA ASN A 58 8.109 -42.016 -42.917 1.00138.40 C ANISOU 47 CA ASN A 58 22641 11495 18450 1347 -350 -1531 C ATOM 48 C ASN A 58 7.821 -42.227 -41.434 1.00136.41 C ANISOU 48 C ASN A 58 22202 11181 18447 1161 -485 -1178 C ATOM 49 O ASN A 58 8.714 -42.573 -40.661 1.00137.58 O ANISOU 49 O ASN A 58 22437 11036 18803 1361 -474 -1067 O ATOM 50 CB ASN A 58 9.377 -42.775 -43.313 1.00144.13 C ANISOU 50 CB ASN A 58 23619 11911 19233 1816 -177 -1711 C ATOM 51 CG ASN A 58 9.660 -42.699 -44.799 1.00146.55 C ANISOU 51 CG ASN A 58 24162 12249 19270 2000 -30 -2081 C ATOM 52 OD1 ASN A 58 8.743 -42.596 -45.614 1.00147.28 O ANISOU 52 OD1 ASN A 58 24521 12255 19184 1737 -165 -2294 O ATOM 53 ND2 ASN A 58 10.937 -42.750 -45.161 1.00147.77 N ANISOU 53 ND2 ASN A 58 24215 12543 19388 2450 249 -2152 N ATOM 54 N THR A 59 6.568 -42.022 -41.044 1.00 76.11 N ANISOU 54 N THR A 59 14317 3820 10782 785 -612 -1001 N ATOM 55 CA THR A 59 6.129 -42.308 -39.684 1.00 75.27 C ANISOU 55 CA THR A 59 14062 3661 10875 556 -743 -679 C ATOM 56 C THR A 59 4.969 -43.296 -39.717 1.00 80.40 C ANISOU 56 C THR A 59 15035 3900 11614 206 -980 -715 C ATOM 57 O THR A 59 3.974 -43.073 -40.407 1.00 80.59 O ANISOU 57 O THR A 59 15137 3968 11517 -102 -1111 -850 O ATOM 58 CB THR A 59 5.699 -41.030 -38.940 1.00 69.74 C ANISOU 58 CB THR A 59 12926 3460 10112 334 -747 -457 C ATOM 59 OG1 THR A 59 4.691 -40.348 -39.697 1.00 68.21 O ANISOU 59 OG1 THR A 59 12736 3438 9744 48 -840 -603 O ATOM 60 CG2 THR A 59 6.890 -40.104 -38.737 1.00 65.25 C ANISOU 60 CG2 THR A 59 12039 3269 9482 652 -536 -387 C ATOM 61 N ASP A 60 5.103 -44.388 -38.970 1.00 84.95 N ANISOU 61 N ASP A 60 15796 4074 12409 249 -1045 -584 N ATOM 62 CA ASP A 60 4.110 -45.460 -38.983 1.00 90.88 C ANISOU 62 CA ASP A 60 16889 4369 13272 -71 -1270 -608 C ATOM 63 C ASP A 60 2.728 -45.005 -38.518 1.00 88.73 C ANISOU 63 C ASP A 60 16423 4301 12990 -584 -1441 -443 C ATOM 64 O ASP A 60 2.587 -43.967 -37.871 1.00 83.08 O ANISOU 64 O ASP A 60 15302 4019 12245 -667 -1384 -224 O ATOM 65 CB ASP A 60 4.592 -46.655 -38.153 1.00139.29 C ANISOU 65 CB ASP A 60 23201 10070 19654 62 -1305 -422 C ATOM 66 CG ASP A 60 5.129 -46.247 -36.792 1.00136.37 C ANISOU 66 CG ASP A 60 22468 9948 19398 17 -1279 -21 C ATOM 67 OD1 ASP A 60 4.597 -45.286 -36.199 1.00134.98 O ANISOU 67 OD1 ASP A 60 22243 9736 19308 -374 -1428 204 O ATOM 68 OD2 ASP A 60 6.084 -46.895 -36.313 1.00135.53 O ANISOU 68 OD2 ASP A 60 22123 10081 19289 365 -1111 73 O ATOM 69 N ILE A 61 1.714 -45.796 -38.855 1.00102.24 N ANISOU 69 N ILE A 61 18426 5691 14728 -923 -1652 -556 N ATOM 70 CA ILE A 61 0.329 -45.462 -38.541 1.00101.11 C ANISOU 70 CA ILE A 61 18109 5722 14584 -1423 -1829 -427 C ATOM 71 C ILE A 61 0.072 -45.462 -37.035 1.00 99.75 C ANISOU 71 C ILE A 61 17670 5644 14585 -1615 -1845 -24 C ATOM 72 O ILE A 61 -0.777 -44.717 -36.544 1.00 96.24 O ANISOU 72 O ILE A 61 16874 5587 14104 -1871 -1862 147 O ATOM 73 CB ILE A 61 -0.648 -46.435 -39.233 1.00100.25 C ANISOU 73 CB ILE A 61 18397 5194 14501 -1761 -2077 -616 C ATOM 74 CG1 ILE A 61 -0.231 -46.664 -40.687 1.00102.74 C ANISOU 74 CG1 ILE A 61 19059 5349 14627 -1542 -2059 -1035 C ATOM 75 CG2 ILE A 61 -2.076 -45.911 -39.160 1.00 99.38 C ANISOU 75 CG2 ILE A 61 18052 5338 14370 -2263 -2254 -507 C ATOM 76 CD1 ILE A 61 -1.158 -47.584 -41.450 1.00109.03 C ANISOU 76 CD1 ILE A 61 20323 5586 15517 -1243 -2030 -1206 C ATOM 77 N TYR A 62 0.812 -46.298 -36.311 1.00102.41 N ANISOU 77 N TYR A 62 18184 5626 15103 -1476 -1836 127 N ATOM 78 CA TYR A 62 0.673 -46.401 -34.859 1.00101.69 C ANISOU 78 CA TYR A 62 17902 5572 15164 -1657 -1858 518 C ATOM 79 C TYR A 62 0.879 -45.051 -34.179 1.00 96.22 C ANISOU 79 C TYR A 62 16741 5430 14388 -1527 -1687 724 C ATOM 80 O TYR A 62 0.028 -44.587 -33.415 1.00 94.26 O ANISOU 80 O TYR A 62 16217 5444 14155 -1813 -1708 976 O ATOM 81 CB TYR A 62 1.672 -47.414 -34.295 1.00160.56 C ANISOU 81 CB TYR A 62 25664 12527 22813 -1469 -1878 632 C ATOM 82 CG TYR A 62 1.457 -48.834 -34.762 1.00163.85 C ANISOU 82 CG TYR A 62 26576 12342 23336 -1625 -2065 454 C ATOM 83 CD1 TYR A 62 0.217 -49.257 -35.221 1.00164.43 C ANISOU 83 CD1 TYR A 62 26746 12353 23378 -2072 -2251 339 C ATOM 84 CD2 TYR A 62 2.497 -49.755 -34.741 1.00166.46 C ANISOU 84 CD2 TYR A 62 27283 12159 23804 -1325 -2067 401 C ATOM 85 CE1 TYR A 62 0.019 -50.557 -35.648 1.00167.50 C ANISOU 85 CE1 TYR A 62 27607 12176 23859 -2240 -2442 169 C ATOM 86 CE2 TYR A 62 2.309 -51.056 -35.164 1.00169.55 C ANISOU 86 CE2 TYR A 62 28162 11966 24292 -1467 -2244 225 C ATOM 87 CZ TYR A 62 1.068 -51.452 -35.617 1.00170.04 C ANISOU 87 CZ TYR A 62 28327 11971 24311 -1936 -2436 105 C ATOM 88 OH TYR A 62 0.876 -52.748 -36.041 1.00173.19 O ANISOU 88 OH TYR A 62 29229 11774 24802 -2101 -2633 -79 O ATOM 89 N SER A 63 2.016 -44.427 -34.469 1.00102.36 N ANISOU 89 N SER A 63 17432 6385 15076 -1099 -1514 612 N ATOM 90 CA SER A 63 2.354 -43.133 -33.890 1.00 99.34 C ANISOU 90 CA SER A 63 16631 6507 14605 -961 -1362 776 C ATOM 91 C SER A 63 1.346 -42.061 -34.293 1.00 97.10 C ANISOU 91 C SER A 63 16067 6660 14166 -1207 -1367 724 C ATOM 92 O SER A 63 1.016 -41.184 -33.499 1.00 94.19 O ANISOU 92 O SER A 63 15365 6658 13765 -1316 -1318 936 O ATOM 93 CB SER A 63 3.768 -42.714 -34.298 1.00 85.95 C ANISOU 93 CB SER A 63 14909 4894 12854 -469 -1188 648 C ATOM 94 OG SER A 63 3.905 -42.689 -35.708 1.00 87.58 O ANISOU 94 OG SER A 63 15237 5123 12917 -355 -1146 308 O ATOM 95 N LYS A 64 0.855 -42.141 -35.526 1.00 75.18 N ANISOU 95 N LYS A 64 13442 3835 11287 -1286 -1432 437 N ATOM 96 CA LYS A 64 -0.126 -41.178 -36.019 1.00 71.71 C ANISOU 96 CA LYS A 64 12770 3770 10708 -1519 -1468 375 C ATOM 97 C LYS A 64 -1.448 -41.276 -35.263 1.00 73.28 C ANISOU 97 C LYS A 64 12811 4035 10999 -1957 -1597 603 C ATOM 98 O LYS A 64 -2.012 -40.262 -34.851 1.00 69.41 O ANISOU 98 O LYS A 64 11970 3955 10450 -2072 -1552 738 O ATOM 99 CB LYS A 64 -0.362 -41.360 -37.521 1.00 81.90 C ANISOU 99 CB LYS A 64 14315 4931 11872 -1544 -1552 32 C ATOM 100 CG LYS A 64 0.818 -40.955 -38.389 1.00 81.14 C ANISOU 100 CG LYS A 64 14292 4912 11626 -1131 -1387 -202 C ATOM 101 CD LYS A 64 0.454 -41.004 -39.864 1.00 84.03 C ANISOU 101 CD LYS A 64 14975 5105 11849 -1166 -1475 -545 C ATOM 102 CE LYS A 64 1.599 -40.514 -40.735 1.00 81.86 C ANISOU 102 CE LYS A 64 14600 5158 11345 -910 -1320 -729 C ATOM 103 NZ LYS A 64 1.249 -40.542 -42.183 1.00 84.78 N ANISOU 103 NZ LYS A 64 15297 5378 11537 -945 -1403 -1063 N ATOM 104 N VAL A 65 -1.936 -42.499 -35.081 1.00 78.79 N ANISOU 104 N VAL A 65 13770 4323 11843 -2196 -1751 647 N ATOM 105 CA VAL A 65 -3.186 -42.724 -34.363 1.00 81.37 C ANISOU 105 CA VAL A 65 13959 4683 12275 -2636 -1871 878 C ATOM 106 C VAL A 65 -3.044 -42.351 -32.887 1.00 79.29 C ANISOU 106 C VAL A 65 13415 4647 12066 -2624 -1748 1223 C ATOM 107 O VAL A 65 -3.941 -41.742 -32.302 1.00 78.10 O ANISOU 107 O VAL A 65 12955 4813 11905 -2877 -1741 1400 O ATOM 108 CB VAL A 65 -3.659 -44.189 -34.491 1.00 88.94 C ANISOU 108 CB VAL A 65 15293 5107 13394 -2897 -2065 867 C ATOM 109 CG1 VAL A 65 -4.904 -44.429 -33.650 1.00 91.98 C ANISOU 109 CG1 VAL A 65 15503 5546 13902 -3363 -2169 1149 C ATOM 110 CG2 VAL A 65 -3.927 -44.532 -35.946 1.00 91.69 C ANISOU 110 CG2 VAL A 65 15931 5241 13664 -2957 -2211 514 C ATOM 111 N LEU A 66 -1.909 -42.714 -32.296 1.00 79.15 N ANISOU 111 N LEU A 66 13503 4475 12097 -2319 -1651 1314 N ATOM 112 CA LEU A 66 -1.628 -42.387 -30.901 1.00 77.65 C ANISOU 112 CA LEU A 66 13088 4484 11932 -2278 -1545 1635 C ATOM 113 C LEU A 66 -1.614 -40.877 -30.680 1.00 71.18 C ANISOU 113 C LEU A 66 11873 4217 10955 -2182 -1405 1661 C ATOM 114 O LEU A 66 -2.316 -40.354 -29.806 1.00 70.39 O ANISOU 114 O LEU A 66 11508 4400 10836 -2383 -1367 1879 O ATOM 115 CB LEU A 66 -0.288 -42.987 -30.474 1.00 79.03 C ANISOU 115 CB LEU A 66 13457 4391 12180 -1925 -1489 1701 C ATOM 116 CG LEU A 66 0.158 -42.711 -29.037 1.00 78.02 C ANISOU 116 CG LEU A 66 13136 4445 12060 -1850 -1399 2031 C ATOM 117 CD1 LEU A 66 -0.793 -43.363 -28.044 1.00 82.10 C ANISOU 117 CD1 LEU A 66 13635 4899 12662 -2250 -1474 2324 C ATOM 118 CD2 LEU A 66 1.586 -43.187 -28.813 1.00 79.62 C ANISOU 118 CD2 LEU A 66 13527 4381 12341 -1468 -1368 2072 C ATOM 119 N VAL A 67 -0.811 -40.186 -31.484 1.00 70.82 N ANISOU 119 N VAL A 67 11799 4316 10794 -1876 -1322 1437 N ATOM 120 CA VAL A 67 -0.697 -38.734 -31.413 1.00 66.24 C ANISOU 120 CA VAL A 67 10881 4221 10065 -1768 -1199 1436 C ATOM 121 C VAL A 67 -2.043 -38.062 -31.666 1.00 65.16 C ANISOU 121 C VAL A 67 10533 4351 9871 -2082 -1255 1417 C ATOM 122 O VAL A 67 -2.381 -37.086 -31.008 1.00 62.35 O ANISOU 122 O VAL A 67 9873 4369 9446 -2125 -1175 1542 O ATOM 123 CB VAL A 67 0.369 -38.199 -32.399 1.00 88.06 C ANISOU 123 CB VAL A 67 13680 7060 12721 -1408 -1108 1193 C ATOM 124 CG1 VAL A 67 0.235 -36.697 -32.588 1.00 85.83 C ANISOU 124 CG1 VAL A 67 13069 7254 12288 -1346 -1007 1182 C ATOM 125 CG2 VAL A 67 1.764 -38.549 -31.906 1.00 89.70 C ANISOU 125 CG2 VAL A 67 14012 7076 12995 -1069 -1034 1246 C ATOM 126 N THR A 68 -2.813 -38.597 -32.609 1.00 63.24 N ANISOU 126 N THR A 68 10457 3908 9661 -2297 -1401 1259 N ATOM 127 CA THR A 68 -4.146 -38.072 -32.888 1.00 63.36 C ANISOU 127 CA THR A 68 10272 4151 9650 -2611 -1486 1252 C ATOM 128 C THR A 68 -5.055 -38.207 -31.669 1.00 65.74 C ANISOU 128 C THR A 68 10367 4562 10047 -2905 -1485 1552 C ATOM 129 O THR A 68 -5.783 -37.276 -31.325 1.00 63.72 O ANISOU 129 O THR A 68 9789 4681 9741 -3013 -1434 1640 O ATOM 130 CB THR A 68 -4.796 -38.782 -34.091 1.00 67.27 C ANISOU 130 CB THR A 68 11016 4373 10170 -2813 -1679 1035 C ATOM 131 OG1 THR A 68 -3.999 -38.564 -35.261 1.00 65.16 O ANISOU 131 OG1 THR A 68 10930 4055 9774 -2540 -1659 747 O ATOM 132 CG2 THR A 68 -6.200 -38.248 -34.336 1.00 68.00 C ANISOU 132 CG2 THR A 68 10865 4717 10255 -3150 -1790 1058 C ATOM 133 N ALA A 69 -5.001 -39.365 -31.017 1.00 71.35 N ANISOU 133 N ALA A 69 11272 4944 10895 -3023 -1532 1713 N ATOM 134 CA ALA A 69 -5.807 -39.619 -29.826 1.00 74.30 C ANISOU 134 CA ALA A 69 11481 5398 11352 -3313 -1516 2021 C ATOM 135 C ALA A 69 -5.452 -38.657 -28.694 1.00 70.61 C ANISOU 135 C ALA A 69 10738 5301 10788 -3150 -1328 2211 C ATOM 136 O ALA A 69 -6.335 -38.033 -28.095 1.00 70.57 O ANISOU 136 O ALA A 69 10443 5614 10759 -3338 -1265 2368 O ATOM 137 CB ALA A 69 -5.643 -41.058 -29.373 1.00 79.16 C ANISOU 137 CB ALA A 69 12405 5552 12123 -3440 -1604 2163 C ATOM 138 N ILE A 70 -4.157 -38.541 -28.411 1.00 66.94 N ANISOU 138 N ILE A 70 10365 4800 10268 -2797 -1239 2191 N ATOM 139 CA ILE A 70 -3.671 -37.609 -27.395 1.00 63.59 C ANISOU 139 CA ILE A 70 9715 4712 9735 -2622 -1082 2342 C ATOM 140 C ILE A 70 -4.107 -36.186 -27.729 1.00 59.18 C ANISOU 140 C ILE A 70 8850 4588 9048 -2602 -1009 2237 C ATOM 141 O ILE A 70 -4.533 -35.428 -26.855 1.00 58.44 O ANISOU 141 O ILE A 70 8507 4810 8889 -2672 -909 2394 O ATOM 142 CB ILE A 70 -2.134 -37.660 -27.279 1.00 61.49 C ANISOU 142 CB ILE A 70 9587 4338 9438 -2235 -1027 2301 C ATOM 143 CG1 ILE A 70 -1.677 -39.063 -26.872 1.00 66.28 C ANISOU 143 CG1 ILE A 70 10476 4529 10178 -2228 -1093 2453 C ATOM 144 CG2 ILE A 70 -1.631 -36.622 -26.286 1.00 57.86 C ANISOU 144 CG2 ILE A 70 8884 4256 8844 -2064 -890 2414 C ATOM 145 CD1 ILE A 70 -0.174 -39.207 -26.749 1.00 65.04 C ANISOU 145 CD1 ILE A 70 10434 4261 10017 -1838 -1050 2438 C ATOM 146 N TYR A 71 -4.011 -35.843 -29.010 1.00 64.73 N ANISOU 146 N TYR A 71 9591 5295 9710 -2502 -1059 1971 N ATOM 147 CA TYR A 71 -4.408 -34.534 -29.511 1.00 62.93 C ANISOU 147 CA TYR A 71 9108 5433 9370 -2477 -1018 1858 C ATOM 148 C TYR A 71 -5.884 -34.247 -29.252 1.00 62.72 C ANISOU 148 C TYR A 71 8847 5603 9381 -2798 -1048 1963 C ATOM 149 O TYR A 71 -6.243 -33.145 -28.846 1.00 60.76 O ANISOU 149 O TYR A 71 8324 5708 9055 -2779 -953 2013 O ATOM 150 CB TYR A 71 -4.117 -34.429 -31.009 1.00 60.89 C ANISOU 150 CB TYR A 71 8979 5098 9061 -2356 -1092 1567 C ATOM 151 CG TYR A 71 -2.771 -33.826 -31.342 1.00 60.38 C ANISOU 151 CG TYR A 71 8985 5054 8903 -1991 -998 1449 C ATOM 152 CD1 TYR A 71 -1.639 -34.151 -30.604 1.00 59.83 C ANISOU 152 CD1 TYR A 71 8950 4937 8848 -1796 -906 1585 C ATOM 153 CD2 TYR A 71 -2.633 -32.939 -32.402 1.00 60.64 C ANISOU 153 CD2 TYR A 71 9040 5169 8832 -1852 -1005 1216 C ATOM 154 CE1 TYR A 71 -0.410 -33.605 -30.908 1.00 59.61 C ANISOU 154 CE1 TYR A 71 8951 4947 8751 -1474 -825 1490 C ATOM 155 CE2 TYR A 71 -1.409 -32.388 -32.716 1.00 60.48 C ANISOU 155 CE2 TYR A 71 9061 5188 8733 -1535 -906 1124 C ATOM 156 CZ TYR A 71 -0.300 -32.724 -31.966 1.00 59.99 C ANISOU 156 CZ TYR A 71 9007 5084 8705 -1349 -816 1261 C ATOM 157 OH TYR A 71 0.920 -32.175 -32.277 1.00 60.08 O ANISOU 157 OH TYR A 71 9024 5152 8652 -1045 -722 1182 O ATOM 158 N LEU A 72 -6.734 -35.241 -29.490 1.00 63.77 N ANISOU 158 N LEU A 72 9086 5504 9640 -3090 -1181 1993 N ATOM 159 CA LEU A 72 -8.170 -35.082 -29.278 1.00 65.54 C ANISOU 159 CA LEU A 72 9065 5911 9927 -3420 -1218 2111 C ATOM 160 C LEU A 72 -8.520 -34.997 -27.796 1.00 66.36 C ANISOU 160 C LEU A 72 8974 6208 10034 -3513 -1070 2401 C ATOM 161 O LEU A 72 -9.422 -34.251 -27.407 1.00 66.29 O ANISOU 161 O LEU A 72 8653 6532 10002 -3624 -996 2486 O ATOM 162 CB LEU A 72 -8.948 -36.218 -29.944 1.00 68.20 C ANISOU 162 CB LEU A 72 9576 5931 10406 -3738 -1416 2082 C ATOM 163 CG LEU A 72 -8.839 -36.297 -31.468 1.00 67.67 C ANISOU 163 CG LEU A 72 9691 5709 10312 -3704 -1581 1784 C ATOM 164 CD1 LEU A 72 -9.758 -37.376 -32.024 1.00 73.76 C ANISOU 164 CD1 LEU A 72 10639 6165 11221 -4059 -1795 1766 C ATOM 165 CD2 LEU A 72 -9.140 -34.947 -32.103 1.00 64.19 C ANISOU 165 CD2 LEU A 72 8980 5643 9766 -3639 -1575 1663 C ATOM 166 N ALA A 73 -7.807 -35.763 -26.973 1.00 65.65 N ANISOU 166 N ALA A 73 9070 5910 9963 -3456 -1024 2554 N ATOM 167 CA ALA A 73 -7.992 -35.701 -25.526 1.00 67.33 C ANISOU 167 CA ALA A 73 9142 6298 10143 -3531 -880 2836 C ATOM 168 C ALA A 73 -7.650 -34.308 -25.003 1.00 62.83 C ANISOU 168 C ALA A 73 8345 6122 9404 -3288 -714 2823 C ATOM 169 O ALA A 73 -8.434 -33.690 -24.275 1.00 63.60 O ANISOU 169 O ALA A 73 8184 6533 9448 -3390 -592 2958 O ATOM 170 CB ALA A 73 -7.142 -36.753 -24.836 1.00 71.12 C ANISOU 170 CB ALA A 73 9901 6457 10666 -3487 -890 2997 C ATOM 171 N LEU A 74 -6.476 -33.815 -25.389 1.00 66.95 N ANISOU 171 N LEU A 74 8968 6626 9843 -2967 -706 2655 N ATOM 172 CA LEU A 74 -6.043 -32.477 -25.004 1.00 64.55 C ANISOU 172 CA LEU A 74 8486 6656 9383 -2736 -576 2616 C ATOM 173 C LEU A 74 -6.959 -31.419 -25.608 1.00 63.88 C ANISOU 173 C LEU A 74 8142 6859 9270 -2789 -563 2495 C ATOM 174 O LEU A 74 -7.070 -30.309 -25.086 1.00 62.39 O ANISOU 174 O LEU A 74 7751 6981 8971 -2689 -442 2512 O ATOM 175 CB LEU A 74 -4.601 -32.231 -25.448 1.00 50.53 C ANISOU 175 CB LEU A 74 6868 4781 7550 -2411 -591 2461 C ATOM 176 CG LEU A 74 -3.525 -33.110 -24.809 1.00 51.92 C ANISOU 176 CG LEU A 74 7266 4713 7748 -2284 -597 2582 C ATOM 177 CD1 LEU A 74 -2.185 -32.880 -25.488 1.00 48.49 C ANISOU 177 CD1 LEU A 74 6947 4195 7283 -1968 -614 2405 C ATOM 178 CD2 LEU A 74 -3.428 -32.840 -23.317 1.00 53.00 C ANISOU 178 CD2 LEU A 74 7310 5043 7786 -2283 -486 2819 C ATOM 179 N PHE A 75 -7.615 -31.773 -26.708 1.00 53.79 N ANISOU 179 N PHE A 75 6882 5464 8090 -2942 -700 2371 N ATOM 180 CA PHE A 75 -8.545 -30.871 -27.375 1.00 52.91 C ANISOU 180 CA PHE A 75 6529 5603 7973 -3006 -724 2269 C ATOM 181 C PHE A 75 -9.810 -30.693 -26.553 1.00 56.27 C ANISOU 181 C PHE A 75 6671 6270 8440 -3234 -640 2461 C ATOM 182 O PHE A 75 -10.214 -29.569 -26.266 1.00 54.79 O ANISOU 182 O PHE A 75 6234 6404 8181 -3149 -532 2461 O ATOM 183 CB PHE A 75 -8.904 -31.391 -28.766 1.00 57.08 C ANISOU 183 CB PHE A 75 7172 5932 8582 -3124 -921 2091 C ATOM 184 CG PHE A 75 -9.889 -30.528 -29.501 1.00 56.58 C ANISOU 184 CG PHE A 75 6864 6118 8514 -3186 -979 1995 C ATOM 185 CD1 PHE A 75 -9.476 -29.372 -30.142 1.00 52.28 C ANISOU 185 CD1 PHE A 75 6280 5726 7857 -2945 -969 1824 C ATOM 186 CD2 PHE A 75 -11.229 -30.874 -29.556 1.00 60.80 C ANISOU 186 CD2 PHE A 75 7200 6735 9166 -3489 -1052 2091 C ATOM 187 CE1 PHE A 75 -10.381 -28.577 -30.821 1.00 52.19 C ANISOU 187 CE1 PHE A 75 6052 5931 7844 -2989 -1038 1751 C ATOM 188 CE2 PHE A 75 -12.138 -30.083 -30.232 1.00 60.78 C ANISOU 188 CE2 PHE A 75 6953 6967 9171 -3531 -1122 2016 C ATOM 189 CZ PHE A 75 -11.713 -28.933 -30.865 1.00 56.45 C ANISOU 189 CZ PHE A 75 6386 6556 8506 -3272 -1119 1846 C ATOM 190 N VAL A 76 -10.442 -31.802 -26.182 1.00 80.50 N ANISOU 190 N VAL A 76 9778 9182 11629 -3521 -683 2627 N ATOM 191 CA VAL A 76 -11.665 -31.725 -25.389 1.00 81.43 C ANISOU 191 CA VAL A 76 9607 9541 11791 -3758 -585 2832 C ATOM 192 C VAL A 76 -11.394 -31.167 -23.989 1.00 80.25 C ANISOU 192 C VAL A 76 9357 9634 11502 -3624 -356 2989 C ATOM 193 O VAL A 76 -12.073 -30.234 -23.548 1.00 79.93 O ANISOU 193 O VAL A 76 9029 9937 11404 -3597 -220 3022 O ATOM 194 CB VAL A 76 -12.423 -33.078 -25.324 1.00 76.58 C ANISOU 194 CB VAL A 76 9059 8696 11341 -4134 -685 2999 C ATOM 195 CG1 VAL A 76 -13.102 -33.368 -26.655 1.00 78.26 C ANISOU 195 CG1 VAL A 76 9267 8782 11683 -4324 -909 2849 C ATOM 196 CG2 VAL A 76 -11.491 -34.215 -24.939 1.00 77.68 C ANISOU 196 CG2 VAL A 76 9556 8465 11493 -4117 -718 3082 C ATOM 197 N VAL A 77 -10.388 -31.715 -23.311 1.00 63.90 N ANISOU 197 N VAL A 77 7530 7382 9367 -3523 -320 3076 N ATOM 198 CA VAL A 77 -10.036 -31.259 -21.968 1.00 63.72 C ANISOU 198 CA VAL A 77 7459 7566 9188 -3410 -129 3230 C ATOM 199 C VAL A 77 -9.640 -29.784 -21.976 1.00 59.06 C ANISOU 199 C VAL A 77 6745 7248 8447 -3117 -37 3070 C ATOM 200 O VAL A 77 -10.091 -29.000 -21.136 1.00 59.45 O ANISOU 200 O VAL A 77 6603 7601 8384 -3081 132 3142 O ATOM 201 CB VAL A 77 -8.893 -32.102 -21.361 1.00 64.29 C ANISOU 201 CB VAL A 77 7833 7372 9222 -3335 -150 3347 C ATOM 202 CG1 VAL A 77 -8.436 -31.512 -20.035 1.00 63.90 C ANISOU 202 CG1 VAL A 77 7749 7553 8976 -3198 22 3483 C ATOM 203 CG2 VAL A 77 -9.339 -33.545 -21.180 1.00 69.61 C ANISOU 203 CG2 VAL A 77 8641 7765 10041 -3636 -230 3540 C ATOM 204 N GLY A 78 -8.810 -29.410 -22.944 1.00 67.84 N ANISOU 204 N GLY A 78 7975 8245 9555 -2912 -145 2850 N ATOM 205 CA GLY A 78 -8.342 -28.043 -23.063 1.00 65.83 C ANISOU 205 CA GLY A 78 7639 8203 9172 -2646 -84 2697 C ATOM 206 C GLY A 78 -9.442 -27.050 -23.385 1.00 66.16 C ANISOU 206 C GLY A 78 7392 8523 9221 -2668 -37 2623 C ATOM 207 O GLY A 78 -9.584 -26.035 -22.705 1.00 65.57 O ANISOU 207 O GLY A 78 7176 8708 9028 -2539 102 2624 O ATOM 208 N THR A 79 -10.216 -27.337 -24.428 1.00 64.36 N ANISOU 208 N THR A 79 7086 8236 9133 -2825 -165 2555 N ATOM 209 CA THR A 79 -11.289 -26.443 -24.856 1.00 64.97 C ANISOU 209 CA THR A 79 6876 8568 9243 -2839 -153 2491 C ATOM 210 C THR A 79 -12.359 -26.287 -23.785 1.00 66.29 C ANISOU 210 C THR A 79 6775 9005 9409 -2963 24 2674 C ATOM 211 O THR A 79 -12.736 -25.165 -23.442 1.00 66.22 O ANISOU 211 O THR A 79 6567 9269 9326 -2816 150 2640 O ATOM 212 CB THR A 79 -11.948 -26.910 -26.170 1.00 66.38 C ANISOU 212 CB THR A 79 7026 8625 9570 -3012 -357 2399 C ATOM 213 OG1 THR A 79 -12.226 -28.314 -26.096 1.00 67.52 O ANISOU 213 OG1 THR A 79 7267 8553 9835 -3295 -433 2527 O ATOM 214 CG2 THR A 79 -11.030 -26.637 -27.353 1.00 66.43 C ANISOU 214 CG2 THR A 79 7251 8454 9536 -2838 -499 2179 C ATOM 215 N VAL A 80 -12.845 -27.409 -23.259 1.00 67.08 N ANISOU 215 N VAL A 80 6878 9023 9587 -3227 42 2870 N ATOM 216 CA VAL A 80 -13.842 -27.365 -22.194 1.00 69.68 C ANISOU 216 CA VAL A 80 6951 9619 9906 -3363 236 3067 C ATOM 217 C VAL A 80 -13.300 -26.600 -20.989 1.00 68.28 C ANISOU 217 C VAL A 80 6802 9625 9516 -3144 449 3105 C ATOM 218 O VAL A 80 -13.949 -25.683 -20.485 1.00 68.84 O ANISOU 218 O VAL A 80 6637 10002 9515 -3051 618 3106 O ATOM 219 CB VAL A 80 -14.297 -28.775 -21.764 1.00 74.11 C ANISOU 219 CB VAL A 80 7553 10032 10574 -3703 220 3298 C ATOM 220 CG1 VAL A 80 -15.119 -28.706 -20.485 1.00 76.35 C ANISOU 220 CG1 VAL A 80 7607 10608 10796 -3816 467 3524 C ATOM 221 CG2 VAL A 80 -15.094 -29.438 -22.878 1.00 75.49 C ANISOU 221 CG2 VAL A 80 7646 10076 10963 -3964 14 3268 C ATOM 222 N GLY A 81 -12.096 -26.964 -20.554 1.00 68.88 N ANISOU 222 N GLY A 81 7174 9508 9490 -3049 429 3124 N ATOM 223 CA GLY A 81 -11.466 -26.326 -19.412 1.00 67.75 C ANISOU 223 CA GLY A 81 7110 9502 9132 -2863 588 3164 C ATOM 224 C GLY A 81 -11.327 -24.819 -19.539 1.00 64.13 C ANISOU 224 C GLY A 81 6567 9245 8554 -2583 652 2974 C ATOM 225 O GLY A 81 -11.745 -24.074 -18.653 1.00 64.82 O ANISOU 225 O GLY A 81 6574 9571 8484 -2487 836 3010 O ATOM 226 N ASN A 82 -10.746 -24.369 -20.647 1.00 67.24 N ANISOU 226 N ASN A 82 7006 9532 9011 -2449 500 2771 N ATOM 227 CA ASN A 82 -10.507 -22.944 -20.861 1.00 66.47 C ANISOU 227 CA ASN A 82 6853 9588 8814 -2194 537 2596 C ATOM 228 C ASN A 82 -11.778 -22.133 -21.117 1.00 68.16 C ANISOU 228 C ASN A 82 6759 10054 9085 -2186 619 2556 C ATOM 229 O ASN A 82 -11.915 -21.013 -20.621 1.00 68.67 O ANISOU 229 O ASN A 82 6736 10323 9033 -2007 753 2495 O ATOM 230 CB ASN A 82 -9.499 -22.729 -21.994 1.00 55.47 C ANISOU 230 CB ASN A 82 5624 8000 7452 -2054 358 2413 C ATOM 231 CG ASN A 82 -8.103 -23.190 -21.626 1.00 53.81 C ANISOU 231 CG ASN A 82 5685 7598 7163 -1977 311 2434 C ATOM 232 OD1 ASN A 82 -7.364 -22.481 -20.942 1.00 52.84 O ANISOU 232 OD1 ASN A 82 5637 7551 6887 -1815 375 2414 O ATOM 233 ND2 ASN A 82 -7.734 -24.382 -22.079 1.00 53.79 N ANISOU 233 ND2 ASN A 82 5830 7339 7267 -2090 190 2474 N ATOM 234 N SER A 83 -12.702 -22.694 -21.892 1.00 88.65 N ANISOU 234 N SER A 83 9191 12630 11863 -2379 530 2591 N ATOM 235 CA SER A 83 -13.967 -22.016 -22.163 1.00 90.48 C ANISOU 235 CA SER A 83 9092 13106 12181 -2382 585 2574 C ATOM 236 C SER A 83 -14.773 -21.848 -20.877 1.00 92.34 C ANISOU 236 C SER A 83 9134 13616 12336 -2401 848 2719 C ATOM 237 O SER A 83 -15.264 -20.753 -20.573 1.00 93.51 O ANISOU 237 O SER A 83 9095 14000 12437 -2223 981 2655 O ATOM 238 CB SER A 83 -14.782 -22.783 -23.206 1.00100.54 C ANISOU 238 CB SER A 83 10227 14306 13668 -2629 416 2610 C ATOM 239 OG SER A 83 -15.043 -24.107 -22.775 1.00100.93 O ANISOU 239 OG SER A 83 10370 14200 13778 -2900 394 2778 O ATOM 240 N VAL A 84 -14.892 -22.940 -20.125 1.00 73.22 N ANISOU 240 N VAL A 84 6771 11159 9890 -2607 929 2916 N ATOM 241 CA VAL A 84 -15.573 -22.921 -18.834 1.00 76.73 C ANISOU 241 CA VAL A 84 7057 11870 10224 -2641 1199 3071 C ATOM 242 C VAL A 84 -14.871 -21.965 -17.874 1.00 74.70 C ANISOU 242 C VAL A 84 6934 11730 9719 -2361 1354 2980 C ATOM 243 O VAL A 84 -15.518 -21.291 -17.073 1.00 76.70 O ANISOU 243 O VAL A 84 7009 12258 9876 -2258 1575 2988 O ATOM 244 CB VAL A 84 -15.681 -24.341 -18.221 1.00 79.97 C ANISOU 244 CB VAL A 84 7542 12204 10640 -2933 1248 3325 C ATOM 245 CG1 VAL A 84 -16.039 -24.278 -16.749 1.00 79.24 C ANISOU 245 CG1 VAL A 84 7833 11847 10427 -2899 1161 3344 C ATOM 246 CG2 VAL A 84 -16.710 -25.165 -18.980 1.00 82.06 C ANISOU 246 CG2 VAL A 84 7615 12784 10782 -2976 1547 3490 C ATOM 247 N THR A 85 -13.548 -21.895 -17.972 1.00 63.21 N ANISOU 247 N THR A 85 5790 10067 8160 -2239 1235 2889 N ATOM 248 CA THR A 85 -12.776 -20.945 -17.180 1.00 61.13 C ANISOU 248 CA THR A 85 5674 9884 7667 -1992 1333 2787 C ATOM 249 C THR A 85 -13.206 -19.516 -17.500 1.00 61.59 C ANISOU 249 C THR A 85 5573 10095 7732 -1761 1374 2595 C ATOM 250 O THR A 85 -13.493 -18.728 -16.597 1.00 63.17 O ANISOU 250 O THR A 85 5725 10501 7775 -1608 1567 2556 O ATOM 251 CB THR A 85 -11.265 -21.095 -17.433 1.00 52.66 C ANISOU 251 CB THR A 85 4924 8558 6528 -1908 1159 2718 C ATOM 252 OG1 THR A 85 -10.841 -22.405 -17.036 1.00 54.67 O ANISOU 252 OG1 THR A 85 5334 8652 6787 -2097 1115 2904 O ATOM 253 CG2 THR A 85 -10.486 -20.055 -16.648 1.00 50.80 C ANISOU 253 CG2 THR A 85 4835 8413 6054 -1686 1241 2622 C ATOM 254 N LEU A 86 -13.260 -19.196 -18.791 1.00 75.57 N ANISOU 254 N LEU A 86 7275 11760 9681 -1736 1190 2477 N ATOM 255 CA LEU A 86 -13.694 -17.877 -19.243 1.00 76.43 C ANISOU 255 CA LEU A 86 7237 11982 9821 -1520 1195 2310 C ATOM 256 C LEU A 86 -15.092 -17.533 -18.740 1.00 79.12 C ANISOU 256 C LEU A 86 7247 12614 10202 -1505 1401 2368 C ATOM 257 O LEU A 86 -15.314 -16.446 -18.204 1.00 80.47 O ANISOU 257 O LEU A 86 7366 12942 10267 -1279 1549 2271 O ATOM 258 CB LEU A 86 -13.658 -17.787 -20.770 1.00 62.21 C ANISOU 258 CB LEU A 86 5414 10022 8201 -1535 949 2209 C ATOM 259 CG LEU A 86 -12.286 -17.627 -21.427 1.00 59.86 C ANISOU 259 CG LEU A 86 5404 9495 7847 -1425 778 2076 C ATOM 260 CD1 LEU A 86 -12.431 -17.503 -22.934 1.00 59.27 C ANISOU 260 CD1 LEU A 86 5297 9296 7928 -1450 559 1985 C ATOM 261 CD2 LEU A 86 -11.563 -16.417 -20.858 1.00 60.09 C ANISOU 261 CD2 LEU A 86 5532 9587 7712 -1169 857 1948 C ATOM 262 N PHE A 87 -16.030 -18.461 -18.910 1.00125.26 N ANISOU 262 N PHE A 87 12865 18526 16201 -1745 1413 2527 N ATOM 263 CA PHE A 87 -17.402 -18.236 -18.462 1.00127.85 C ANISOU 263 CA PHE A 87 12824 19154 16600 -1748 1610 2604 C ATOM 264 C PHE A 87 -17.486 -18.089 -16.944 1.00129.32 C ANISOU 264 C PHE A 87 13008 19560 16568 -1678 1924 2678 C ATOM 265 O PHE A 87 -18.363 -17.398 -16.426 1.00131.20 O ANISOU 265 O PHE A 87 13044 20039 16767 -1487 2122 2624 O ATOM 266 CB PHE A 87 -18.323 -19.359 -18.945 1.00158.71 C ANISOU 266 CB PHE A 87 16487 23084 20732 -2064 1535 2775 C ATOM 267 CG PHE A 87 -18.580 -19.337 -20.425 1.00158.72 C ANISOU 267 CG PHE A 87 16415 22948 20944 -2110 1249 2687 C ATOM 268 CD1 PHE A 87 -18.324 -18.197 -21.169 1.00158.31 C ANISOU 268 CD1 PHE A 87 16438 22827 20884 -1855 1122 2484 C ATOM 269 CD2 PHE A 87 -19.080 -20.455 -21.072 1.00159.31 C ANISOU 269 CD2 PHE A 87 16361 22956 21213 -2422 1100 2810 C ATOM 270 CE1 PHE A 87 -18.560 -18.173 -22.530 1.00158.38 C ANISOU 270 CE1 PHE A 87 16397 22721 21057 -1902 859 2411 C ATOM 271 CE2 PHE A 87 -19.318 -20.437 -22.433 1.00159.43 C ANISOU 271 CE2 PHE A 87 16332 22849 21393 -2472 826 2720 C ATOM 272 CZ PHE A 87 -19.057 -19.294 -23.163 1.00158.94 C ANISOU 272 CZ PHE A 87 16347 22737 21303 -2207 709 2523 C ATOM 273 N THR A 88 -16.569 -18.744 -16.239 1.00113.60 N ANISOU 273 N THR A 88 11253 17484 14427 -1820 1968 2801 N ATOM 274 CA THR A 88 -16.500 -18.655 -14.786 1.00115.02 C ANISOU 274 CA THR A 88 11477 17865 14360 -1778 2253 2885 C ATOM 275 C THR A 88 -16.032 -17.269 -14.365 1.00115.12 C ANISOU 275 C THR A 88 11677 17914 14151 -1456 2330 2679 C ATOM 276 O THR A 88 -16.593 -16.661 -13.453 1.00117.26 O ANISOU 276 O THR A 88 11865 18428 14263 -1315 2593 2659 O ATOM 277 CB THR A 88 -15.541 -19.710 -14.204 1.00 88.54 C ANISOU 277 CB THR A 88 8371 14386 10887 -2005 2243 3077 C ATOM 278 OG1 THR A 88 -16.060 -21.022 -14.455 1.00 86.25 O ANISOU 278 OG1 THR A 88 8395 13782 10596 -1981 1984 2992 O ATOM 279 CG2 THR A 88 -15.374 -19.516 -12.705 1.00 89.55 C ANISOU 279 CG2 THR A 88 8300 14526 11202 -2344 2240 3314 C ATOM 280 N LEU A 89 -15.003 -16.771 -15.043 1.00 91.78 N ANISOU 280 N LEU A 89 8977 14714 11179 -1343 2106 2525 N ATOM 281 CA LEU A 89 -14.463 -15.448 -14.749 1.00 92.01 C ANISOU 281 CA LEU A 89 9195 14747 11018 -1063 2143 2326 C ATOM 282 C LEU A 89 -15.414 -14.349 -15.214 1.00 93.81 C ANISOU 282 C LEU A 89 9200 15097 11347 -830 2201 2167 C ATOM 283 O LEU A 89 -15.313 -13.201 -14.777 1.00 95.23 O ANISOU 283 O LEU A 89 9456 15362 11364 -592 2333 2024 O ATOM 284 CB LEU A 89 -13.092 -15.278 -15.405 1.00117.23 C ANISOU 284 CB LEU A 89 12700 17659 14181 -1028 1888 2227 C ATOM 285 CG LEU A 89 -12.065 -16.348 -15.028 1.00115.45 C ANISOU 285 CG LEU A 89 12727 17310 13826 -1189 1832 2366 C ATOM 286 CD1 LEU A 89 -10.800 -16.203 -15.853 1.00113.07 C ANISOU 286 CD1 LEU A 89 12697 16772 13490 -1107 1606 2252 C ATOM 287 CD2 LEU A 89 -11.751 -16.295 -13.542 1.00116.90 C ANISOU 287 CD2 LEU A 89 12995 17687 13732 -1181 2069 2450 C ATOM 288 N ALA A 90 -16.336 -14.707 -16.102 1.00107.23 N ANISOU 288 N ALA A 90 10634 16795 13314 -899 2090 2193 N ATOM 289 CA ALA A 90 -17.322 -13.758 -16.605 1.00109.04 C ANISOU 289 CA ALA A 90 10609 17151 13671 -686 2131 2077 C ATOM 290 C ALA A 90 -18.392 -13.450 -15.561 1.00112.05 C ANISOU 290 C ALA A 90 10687 17858 14028 -642 2447 2162 C ATOM 291 O ALA A 90 -18.778 -12.300 -15.378 1.00114.03 O ANISOU 291 O ALA A 90 10763 18252 14309 -390 2567 2052 O ATOM 292 CB ALA A 90 -17.961 -14.284 -17.882 1.00121.02 C ANISOU 292 CB ALA A 90 11945 18568 15469 -786 1884 2089 C ATOM 293 N ARG A 91 -18.869 -14.483 -14.877 1.00223.80 N ANISOU 293 N ARG A 91 24780 32126 28128 -884 2588 2365 N ATOM 294 CA ARG A 91 -19.922 -14.321 -13.881 1.00226.74 C ANISOU 294 CA ARG A 91 24862 32831 28456 -880 2919 2479 C ATOM 295 C ARG A 91 -19.344 -14.193 -12.473 1.00228.15 C ANISOU 295 C ARG A 91 25232 33142 28314 -649 3187 2375 C ATOM 296 O ARG A 91 -19.987 -14.580 -11.496 1.00230.73 O ANISOU 296 O ARG A 91 25335 33733 28599 -466 3462 2342 O ATOM 297 CB ARG A 91 -20.875 -15.515 -13.935 1.00182.45 C ANISOU 297 CB ARG A 91 19151 27284 22887 -1249 2971 2752 C ATOM 298 CG ARG A 91 -20.165 -16.840 -13.674 1.00184.49 C ANISOU 298 CG ARG A 91 19183 27892 23024 -1281 3349 2901 C ATOM 299 CD ARG A 91 -21.111 -18.024 -13.593 1.00184.79 C ANISOU 299 CD ARG A 91 19238 27934 23041 -1660 3386 3181 C ATOM 300 NE ARG A 91 -20.362 -19.261 -13.384 1.00185.20 N ANISOU 300 NE ARG A 91 19038 27914 23414 -1946 3191 3324 N ATOM 301 CZ ARG A 91 -19.781 -19.955 -14.358 1.00185.37 C ANISOU 301 CZ ARG A 91 19067 27872 23492 -2310 3150 3567 C ATOM 302 NH1 ARG A 91 -19.862 -19.535 -15.611 1.00186.24 N ANISOU 302 NH1 ARG A 91 19417 27987 23358 -2425 3294 3709 N ATOM 303 NH2 ARG A 91 -19.120 -21.071 -14.083 1.00184.82 N ANISOU 303 NH2 ARG A 91 18781 27723 23718 -2566 2952 3669 N ATOM 304 N LYS A 92 -18.128 -13.662 -12.381 1.00176.89 N ANISOU 304 N LYS A 92 19153 26463 21594 -653 3100 2320 N ATOM 305 CA LYS A 92 -17.438 -13.510 -11.101 1.00178.14 C ANISOU 305 CA LYS A 92 19560 26721 21406 -491 3315 2235 C ATOM 306 C LYS A 92 -18.257 -12.699 -10.098 1.00180.54 C ANISOU 306 C LYS A 92 19798 27155 21644 -130 3492 2013 C ATOM 307 O LYS A 92 -18.649 -13.208 -9.048 1.00180.36 O ANISOU 307 O LYS A 92 19723 27011 21795 52 3336 1855 O ATOM 308 CB LYS A 92 -16.070 -12.856 -11.311 1.00144.02 C ATOM 309 CG LYS A 92 -15.194 -12.823 -10.068 1.00144.02 C ATOM 310 CD LYS A 92 -14.836 -14.227 -9.610 1.00144.02 C ATOM 311 CE LYS A 92 -13.916 -14.193 -8.404 1.00144.02 C ATOM 312 NZ LYS A 92 -13.519 -15.561 -7.978 1.00144.02 N ATOM 313 N LYS A 93 -18.508 -11.435 -10.426 1.00168.44 N ANISOU 313 N LYS A 93 18284 25863 19850 -22 3820 2006 N ATOM 314 CA LYS A 93 -19.306 -10.564 -9.570 1.00171.06 C ANISOU 314 CA LYS A 93 18576 26325 20091 340 4031 1789 C ATOM 315 C LYS A 93 -20.320 -9.767 -10.383 1.00170.51 C ANISOU 315 C LYS A 93 18919 26004 19863 548 3862 1532 C ATOM 316 O LYS A 93 -20.852 -10.255 -11.381 1.00171.17 O ANISOU 316 O LYS A 93 18973 25988 20076 799 3783 1342 O ATOM 317 CB LYS A 93 -18.406 -9.615 -8.775 1.00124.00 C ATOM 318 CG LYS A 93 -17.501 -10.312 -7.772 1.00124.00 C ATOM 319 CD LYS A 93 -16.641 -9.315 -7.015 1.00124.00 C ATOM 320 CE LYS A 93 -15.740 -10.018 -6.014 1.00124.00 C ATOM 321 NZ LYS A 93 -14.890 -9.057 -5.259 1.00124.00 N ATOM 322 N SER A 97 -8.970 -6.718 -4.116 1.00147.24 N ANISOU 322 N SER A 97 18928 22195 14824 449 3028 889 N ATOM 323 CA SER A 97 -9.643 -7.133 -5.340 1.00146.31 C ANISOU 323 CA SER A 97 18472 21990 15132 456 2957 938 C ATOM 324 C SER A 97 -8.635 -7.409 -6.451 1.00142.70 C ANISOU 324 C SER A 97 18070 21258 14891 333 2585 969 C ATOM 325 O SER A 97 -8.956 -7.300 -7.634 1.00141.58 O ANISOU 325 O SER A 97 17731 20995 15069 370 2475 947 O ATOM 326 CB SER A 97 -10.642 -6.067 -5.792 1.00117.06 C ANISOU 326 CB SER A 97 14636 18295 11544 743 3103 718 C ATOM 327 OG SER A 97 -9.985 -4.851 -6.105 1.00119.72 O ANISOU 327 OG SER A 97 15301 18571 11617 931 3123 462 O ATOM 328 N LEU A 98 -7.414 -7.763 -6.062 1.00269.85 N ANISOU 328 N LEU A 98 34438 37278 30814 192 2395 1026 N ATOM 329 CA LEU A 98 -6.368 -8.077 -7.029 1.00266.30 C ANISOU 329 CA LEU A 98 34021 36602 30561 66 2067 1087 C ATOM 330 C LEU A 98 -6.659 -9.384 -7.755 1.00264.20 C ANISOU 330 C LEU A 98 33518 36339 30528 -118 2033 1338 C ATOM 331 O LEU A 98 -6.194 -9.597 -8.874 1.00261.76 O ANISOU 331 O LEU A 98 33127 35855 30477 -180 1821 1374 O ATOM 332 CB LEU A 98 -4.996 -8.145 -6.354 1.00141.19 C ANISOU 332 CB LEU A 98 18500 20681 14464 -24 1866 1084 C ATOM 333 CG LEU A 98 -4.260 -6.821 -6.125 1.00138.98 C ANISOU 333 CG LEU A 98 18310 20158 14339 -29 1555 988 C ATOM 334 CD1 LEU A 98 -4.866 -6.037 -4.970 1.00140.39 C ANISOU 334 CD1 LEU A 98 18502 20235 14603 168 1568 738 C ATOM 335 CD2 LEU A 98 -2.777 -7.065 -5.896 1.00139.02 C ANISOU 335 CD2 LEU A 98 18598 20111 14110 -133 1343 1006 C ATOM 336 N GLN A 99 -7.427 -10.258 -7.111 1.00158.89 N ANISOU 336 N GLN A 99 20088 23196 17089 -212 2244 1511 N ATOM 337 CA GLN A 99 -7.826 -11.518 -7.725 1.00157.37 C ANISOU 337 CA GLN A 99 19673 23002 17121 -396 2235 1749 C ATOM 338 C GLN A 99 -8.635 -11.229 -8.985 1.00157.15 C ANISOU 338 C GLN A 99 19346 22921 17444 -340 2230 1698 C ATOM 339 O GLN A 99 -8.456 -11.875 -10.018 1.00155.38 O ANISOU 339 O GLN A 99 18980 22593 17467 -478 2106 1828 O ATOM 340 CB GLN A 99 -8.640 -12.359 -6.740 1.00141.75 C ANISOU 340 CB GLN A 99 17634 21259 14965 -506 2497 1941 C ATOM 341 CG GLN A 99 -8.886 -13.786 -7.197 1.00140.23 C ANISOU 341 CG GLN A 99 17294 21028 14958 -743 2448 2217 C ATOM 342 CD GLN A 99 -9.596 -14.617 -6.149 1.00142.10 C ANISOU 342 CD GLN A 99 17301 21502 15187 -833 2745 2378 C ATOM 343 OE1 GLN A 99 -8.960 -15.253 -5.309 1.00144.19 O ANISOU 343 OE1 GLN A 99 17479 21982 15326 -695 3007 2278 O ATOM 344 NE2 GLN A 99 -10.923 -14.619 -6.195 1.00141.52 N ANISOU 344 NE2 GLN A 99 17129 21389 15254 -1065 2709 2631 N ATOM 345 N SER A 100 -9.508 -10.229 -8.895 1.00126.59 N ANISOU 345 N SER A 100 15393 19116 13587 -131 2358 1506 N ATOM 346 CA SER A 100 -10.296 -9.789 -10.040 1.00126.65 C ANISOU 346 CA SER A 100 15132 19074 13915 -53 2326 1447 C ATOM 347 C SER A 100 -9.399 -9.372 -11.203 1.00124.43 C ANISOU 347 C SER A 100 14944 18529 13804 -45 2021 1359 C ATOM 348 O SER A 100 -9.802 -9.450 -12.362 1.00123.25 O ANISOU 348 O SER A 100 14607 18291 13929 -87 1906 1393 O ATOM 349 CB SER A 100 -11.218 -8.634 -9.646 1.00134.17 C ANISOU 349 CB SER A 100 15984 20162 14832 199 2542 1270 C ATOM 350 OG SER A 100 -12.114 -9.020 -8.617 1.00136.35 O ANISOU 350 OG SER A 100 16171 20707 14930 202 2855 1347 O ATOM 351 N THR A 101 -8.184 -8.932 -10.889 1.00131.76 N ANISOU 351 N THR A 101 16164 19342 14557 -2 1887 1251 N ATOM 352 CA THR A 101 -7.214 -8.593 -11.922 1.00129.75 C ANISOU 352 CA THR A 101 16003 18856 14442 -7 1612 1181 C ATOM 353 C THR A 101 -6.541 -9.853 -12.458 1.00126.65 C ANISOU 353 C THR A 101 15584 18368 14169 -210 1450 1367 C ATOM 354 O THR A 101 -6.332 -9.981 -13.663 1.00125.01 O ANISOU 354 O THR A 101 15284 18021 14194 -243 1294 1373 O ATOM 355 CB THR A 101 -6.143 -7.607 -11.414 1.00 79.62 C ANISOU 355 CB THR A 101 9959 12415 7876 68 1505 1027 C ATOM 356 OG1 THR A 101 -5.371 -8.226 -10.378 1.00 78.69 O ANISOU 356 OG1 THR A 101 10024 12328 7546 -69 1453 1141 O ATOM 357 CG2 THR A 101 -6.794 -6.340 -10.875 1.00 83.50 C ANISOU 357 CG2 THR A 101 10527 13000 8200 272 1693 840 C ATOM 358 N VAL A 102 -6.217 -10.791 -11.570 1.00112.45 N ANISOU 358 N VAL A 102 13880 16640 12203 -339 1490 1520 N ATOM 359 CA VAL A 102 -5.594 -12.040 -12.005 1.00109.80 C ANISOU 359 CA VAL A 102 13521 16208 11989 -516 1358 1709 C ATOM 360 C VAL A 102 -6.623 -12.915 -12.713 1.00109.52 C ANISOU 360 C VAL A 102 13218 16190 12204 -595 1424 1805 C ATOM 361 O VAL A 102 -6.274 -13.887 -13.380 1.00107.35 O ANISOU 361 O VAL A 102 12899 15777 12112 -706 1284 1898 O ATOM 362 CB VAL A 102 -4.913 -12.813 -10.847 1.00 86.17 C ANISOU 362 CB VAL A 102 10692 13281 8768 -636 1380 1879 C ATOM 363 CG1 VAL A 102 -4.157 -11.857 -9.936 1.00 87.22 C ANISOU 363 CG1 VAL A 102 11075 13470 8596 -550 1372 1764 C ATOM 364 CG2 VAL A 102 -5.920 -13.638 -10.062 1.00 87.83 C ANISOU 364 CG2 VAL A 102 10772 13661 8939 -739 1604 2047 C ATOM 365 N ASP A 103 -7.894 -12.555 -12.564 1.00 82.21 N ANISOU 365 N ASP A 103 9579 12904 8751 -539 1637 1781 N ATOM 366 CA ASP A 103 -8.957 -13.175 -13.341 1.00 82.17 C ANISOU 366 CA ASP A 103 9291 12926 9002 -609 1676 1852 C ATOM 367 C ASP A 103 -8.861 -12.720 -14.791 1.00 81.18 C ANISOU 367 C ASP A 103 9089 12652 9104 -526 1501 1719 C ATOM 368 O ASP A 103 -9.159 -13.482 -15.711 1.00 79.96 O ANISOU 368 O ASP A 103 8784 12426 9170 -632 1411 1785 O ATOM 369 CB ASP A 103 -10.331 -12.819 -12.769 1.00122.56 C ANISOU 369 CB ASP A 103 14196 18291 14080 -555 1951 1864 C ATOM 370 CG ASP A 103 -10.685 -13.642 -11.545 1.00123.61 C ANISOU 370 CG ASP A 103 14364 18590 14011 -684 2143 2042 C ATOM 371 OD1 ASP A 103 -9.770 -14.247 -10.949 1.00121.99 O ANISOU 371 OD1 ASP A 103 14305 18288 13758 -849 2040 2193 O ATOM 372 OD2 ASP A 103 -11.879 -13.682 -11.179 1.00126.20 O ANISOU 372 OD2 ASP A 103 14575 19149 14225 -611 2403 2035 O ATOM 373 N TYR A 104 -8.450 -11.471 -14.991 1.00 87.22 N ANISOU 373 N TYR A 104 9975 13362 9804 -348 1446 1535 N ATOM 374 CA TYR A 104 -8.234 -10.963 -16.338 1.00 86.46 C ANISOU 374 CA TYR A 104 9846 13112 9894 -277 1267 1425 C ATOM 375 C TYR A 104 -7.085 -11.731 -16.984 1.00 83.28 C ANISOU 375 C TYR A 104 9555 12520 9568 -400 1052 1483 C ATOM 376 O TYR A 104 -7.259 -12.338 -18.046 1.00 81.98 O ANISOU 376 O TYR A 104 9292 12259 9601 -449 934 1493 O ATOM 377 CB TYR A 104 -7.948 -9.459 -16.321 1.00 93.61 C ANISOU 377 CB TYR A 104 10882 13977 10708 -73 1249 1229 C ATOM 378 CG TYR A 104 -9.155 -8.603 -15.997 1.00 96.71 C ANISOU 378 CG TYR A 104 11142 14518 11087 105 1441 1134 C ATOM 379 CD1 TYR A 104 -10.430 -8.979 -16.404 1.00 97.43 C ANISOU 379 CD1 TYR A 104 10965 14657 11396 157 1461 1138 C ATOM 380 CD2 TYR A 104 -9.019 -7.420 -15.284 1.00 98.89 C ANISOU 380 CD2 TYR A 104 11563 14882 11128 235 1594 1034 C ATOM 381 CE1 TYR A 104 -11.532 -8.200 -16.111 1.00100.10 C ANISOU 381 CE1 TYR A 104 11156 15136 11741 347 1639 1058 C ATOM 382 CE2 TYR A 104 -10.115 -6.635 -14.986 1.00101.67 C ANISOU 382 CE2 TYR A 104 11795 15365 11470 430 1788 935 C ATOM 383 CZ TYR A 104 -11.368 -7.030 -15.402 1.00102.22 C ANISOU 383 CZ TYR A 104 11571 15487 11780 494 1813 953 C ATOM 384 OH TYR A 104 -12.465 -6.254 -15.109 1.00104.88 O ANISOU 384 OH TYR A 104 11762 15962 12127 714 2008 862 O ATOM 385 N TYR A 105 -5.927 -11.716 -16.324 1.00 68.88 N ANISOU 385 N TYR A 105 7937 10652 7582 -443 1002 1523 N ATOM 386 CA TYR A 105 -4.753 -12.460 -16.777 1.00 65.75 C ANISOU 386 CA TYR A 105 7635 10090 7256 -537 816 1587 C ATOM 387 C TYR A 105 -5.106 -13.904 -17.115 1.00 64.27 C ANISOU 387 C TYR A 105 7340 9863 7214 -694 809 1746 C ATOM 388 O TYR A 105 -4.912 -14.345 -18.251 1.00 62.28 O ANISOU 388 O TYR A 105 7064 9470 7128 -737 676 1747 O ATOM 389 CB TYR A 105 -3.645 -12.424 -15.721 1.00 59.65 C ANISOU 389 CB TYR A 105 7078 9302 6284 -549 760 1619 C ATOM 390 CG TYR A 105 -3.046 -11.055 -15.501 1.00 60.67 C ANISOU 390 CG TYR A 105 7348 9415 6291 -427 704 1458 C ATOM 391 CD1 TYR A 105 -2.205 -10.488 -16.447 1.00 59.08 C ANISOU 391 CD1 TYR A 105 7192 9073 6184 -396 532 1381 C ATOM 392 CD2 TYR A 105 -3.312 -10.335 -14.344 1.00 63.33 C ANISOU 392 CD2 TYR A 105 7785 9870 6408 -352 825 1383 C ATOM 393 CE1 TYR A 105 -1.653 -9.237 -16.254 1.00 60.17 C ANISOU 393 CE1 TYR A 105 7466 9178 6221 -313 468 1245 C ATOM 394 CE2 TYR A 105 -2.761 -9.082 -14.139 1.00 64.51 C ANISOU 394 CE2 TYR A 105 8091 9974 6447 -254 756 1226 C ATOM 395 CZ TYR A 105 -1.932 -8.538 -15.097 1.00 62.97 C ANISOU 395 CZ TYR A 105 7934 9627 6368 -246 570 1164 C ATOM 396 OH TYR A 105 -1.381 -7.292 -14.898 1.00 64.28 O ANISOU 396 OH TYR A 105 8261 9730 6433 -176 490 1019 O ATOM 397 N LEU A 106 -5.639 -14.623 -16.129 1.00 56.17 N ANISOU 397 N LEU A 106 6269 8958 6116 -786 954 1878 N ATOM 398 CA LEU A 106 -6.121 -15.987 -16.325 1.00 55.41 C ANISOU 398 CA LEU A 106 6082 8820 6151 -961 958 2044 C ATOM 399 C LEU A 106 -7.022 -16.048 -17.550 1.00 55.67 C ANISOU 399 C LEU A 106 5907 8832 6413 -994 931 2003 C ATOM 400 O LEU A 106 -6.807 -16.869 -18.448 1.00 54.39 O ANISOU 400 O LEU A 106 5724 8533 6408 -1117 826 2069 O ATOM 401 CB LEU A 106 -6.878 -16.475 -15.086 1.00 55.58 C ANISOU 401 CB LEU A 106 6074 9006 6036 -1057 1148 2199 C ATOM 402 CG LEU A 106 -6.110 -17.340 -14.084 1.00 54.99 C ANISOU 402 CG LEU A 106 6198 8905 5789 -1136 1133 2352 C ATOM 403 CD1 LEU A 106 -4.774 -16.709 -13.728 1.00 54.12 C ANISOU 403 CD1 LEU A 106 6295 8729 5536 -1017 1005 2259 C ATOM 404 CD2 LEU A 106 -6.946 -17.553 -12.837 1.00 57.35 C ANISOU 404 CD2 LEU A 106 6473 9421 5896 -1194 1359 2470 C ATOM 405 N GLY A 107 -8.003 -15.149 -17.594 1.00 51.20 N ANISOU 405 N GLY A 107 5197 8396 5862 -880 1017 1893 N ATOM 406 CA GLY A 107 -8.898 -15.050 -18.730 1.00 51.75 C ANISOU 406 CA GLY A 107 5059 8463 6140 -896 969 1854 C ATOM 407 C GLY A 107 -8.109 -14.971 -20.018 1.00 49.89 C ANISOU 407 C GLY A 107 4906 8038 6010 -856 759 1750 C ATOM 408 O GLY A 107 -8.309 -15.788 -20.923 1.00 49.18 O ANISOU 408 O GLY A 107 4734 7866 6087 -952 652 1766 O ATOM 409 N SER A 108 -7.186 -14.013 -20.078 1.00 60.64 N ANISOU 409 N SER A 108 6441 9335 7264 -727 699 1647 N ATOM 410 CA SER A 108 -6.318 -13.849 -21.238 1.00 58.74 C ANISOU 410 CA SER A 108 6291 8931 7097 -689 521 1561 C ATOM 411 C SER A 108 -5.677 -15.183 -21.596 1.00 56.10 C ANISOU 411 C SER A 108 6042 8444 6830 -820 421 1649 C ATOM 412 O SER A 108 -5.772 -15.639 -22.742 1.00 54.87 O ANISOU 412 O SER A 108 5881 8173 6795 -851 301 1611 O ATOM 413 CB SER A 108 -5.243 -12.792 -20.965 1.00 55.67 C ANISOU 413 CB SER A 108 6067 8513 6573 -555 487 1461 C ATOM 414 OG SER A 108 -4.347 -12.671 -22.056 1.00 53.59 O ANISOU 414 OG SER A 108 5889 8105 6370 -539 332 1406 O ATOM 415 N LEU A 109 -5.067 -15.821 -20.598 1.00 39.04 N ANISOU 415 N LEU A 109 3972 6280 4581 -888 470 1765 N ATOM 416 CA LEU A 109 -4.414 -17.109 -20.791 1.00 37.22 C ANISOU 416 CA LEU A 109 3833 5891 4416 -992 385 1863 C ATOM 417 C LEU A 109 -5.366 -18.089 -21.454 1.00 37.80 C ANISOU 417 C LEU A 109 3795 5916 4651 -1145 373 1926 C ATOM 418 O LEU A 109 -5.028 -18.702 -22.471 1.00 36.70 O ANISOU 418 O LEU A 109 3713 5606 4623 -1197 257 1915 O ATOM 419 CB LEU A 109 -3.918 -17.665 -19.454 1.00 33.38 C ANISOU 419 CB LEU A 109 3464 5425 3796 -1029 438 1998 C ATOM 420 CG LEU A 109 -2.697 -16.973 -18.847 1.00 32.31 C ANISOU 420 CG LEU A 109 3469 5306 3503 -914 400 1956 C ATOM 421 CD1 LEU A 109 -2.345 -17.592 -17.499 1.00 34.96 C ANISOU 421 CD1 LEU A 109 3905 5697 3683 -965 454 2105 C ATOM 422 CD2 LEU A 109 -1.522 -17.061 -19.804 1.00 30.20 C ANISOU 422 CD2 LEU A 109 3281 4879 3315 -860 249 1906 C ATOM 423 N ALA A 110 -6.572 -18.188 -20.901 1.00 34.10 N ANISOU 423 N ALA A 110 3167 5599 4190 -1219 494 1990 N ATOM 424 CA ALA A 110 -7.576 -19.102 -21.424 1.00 36.32 C ANISOU 424 CA ALA A 110 3315 5857 4631 -1396 479 2066 C ATOM 425 C ALA A 110 -7.787 -18.828 -22.905 1.00 34.55 C ANISOU 425 C ALA A 110 3015 5572 4543 -1378 346 1939 C ATOM 426 O ALA A 110 -7.749 -19.749 -23.728 1.00 35.23 O ANISOU 426 O ALA A 110 3105 5524 4757 -1515 238 1958 O ATOM 427 CB ALA A 110 -8.885 -18.952 -20.654 1.00 39.46 C ANISOU 427 CB ALA A 110 3515 6473 5006 -1465 654 2162 C ATOM 428 N LEU A 111 -7.972 -17.551 -23.236 1.00 39.40 N ANISOU 428 N LEU A 111 3580 6273 5118 -1213 344 1809 N ATOM 429 CA LEU A 111 -8.152 -17.142 -24.621 1.00 39.31 C ANISOU 429 CA LEU A 111 3520 6210 5206 -1179 207 1695 C ATOM 430 C LEU A 111 -6.982 -17.658 -25.449 1.00 36.93 C ANISOU 430 C LEU A 111 3420 5699 4912 -1174 69 1636 C ATOM 431 O LEU A 111 -7.178 -18.364 -26.447 1.00 36.75 O ANISOU 431 O LEU A 111 3406 5571 4987 -1256 -54 1600 O ATOM 432 CB LEU A 111 -8.253 -15.617 -24.724 1.00 65.46 C ANISOU 432 CB LEU A 111 6770 9638 8465 -989 234 1585 C ATOM 433 CG LEU A 111 -8.555 -15.043 -26.110 1.00 65.42 C ANISOU 433 CG LEU A 111 6728 9589 8540 -936 87 1480 C ATOM 434 CD1 LEU A 111 -9.884 -15.570 -26.630 1.00 66.92 C ANISOU 434 CD1 LEU A 111 6719 9828 8879 -1073 24 1524 C ATOM 435 CD2 LEU A 111 -8.553 -13.524 -26.079 1.00 66.70 C ANISOU 435 CD2 LEU A 111 6866 9834 8644 -736 115 1388 C ATOM 436 N SER A 112 -5.769 -17.354 -24.988 1.00 54.85 N ANISOU 436 N SER A 112 5849 7918 7072 -1077 89 1627 N ATOM 437 CA SER A 112 -4.551 -17.711 -25.707 1.00 52.76 C ANISOU 437 CA SER A 112 5755 7481 6810 -1043 -12 1579 C ATOM 438 C SER A 112 -4.464 -19.217 -25.918 1.00 52.72 C ANISOU 438 C SER A 112 5826 7310 6896 -1179 -64 1647 C ATOM 439 O SER A 112 -3.834 -19.683 -26.867 1.00 52.01 O ANISOU 439 O SER A 112 5841 7069 6849 -1171 -159 1578 O ATOM 440 CB SER A 112 -3.313 -17.216 -24.957 1.00 88.56 C ANISOU 440 CB SER A 112 10406 12019 11221 -930 23 1588 C ATOM 441 OG SER A 112 -3.139 -17.929 -23.746 1.00 86.86 O ANISOU 441 OG SER A 112 10322 11658 11022 -889 -57 1558 O ATOM 442 N ASP A 113 -5.099 -19.975 -25.029 1.00 58.87 N ANISOU 442 N ASP A 113 6564 8108 7696 -1304 4 1782 N ATOM 443 CA ASP A 113 -5.163 -21.417 -25.194 1.00 59.34 C ANISOU 443 CA ASP A 113 6709 7986 7854 -1452 -49 1862 C ATOM 444 C ASP A 113 -6.231 -21.776 -26.221 1.00 60.76 C ANISOU 444 C ASP A 113 6795 8129 8161 -1603 -133 1826 C ATOM 445 O ASP A 113 -5.943 -22.464 -27.205 1.00 61.04 O ANISOU 445 O ASP A 113 6951 7968 8274 -1670 -244 1782 O ATOM 446 CB ASP A 113 -5.434 -22.102 -23.853 1.00102.14 C ANISOU 446 CB ASP A 113 12133 13434 13241 -1549 49 2045 C ATOM 447 CG ASP A 113 -4.307 -21.892 -22.855 1.00100.99 C ANISOU 447 CG ASP A 113 12113 13291 12967 -1421 89 2094 C ATOM 448 OD1 ASP A 113 -3.165 -21.632 -23.294 1.00 99.64 O ANISOU 448 OD1 ASP A 113 11983 13144 12732 -1261 61 1984 O ATOM 449 OD2 ASP A 113 -4.565 -21.987 -21.635 1.00101.56 O ANISOU 449 OD2 ASP A 113 12242 13346 13002 -1493 140 2253 O ATOM 450 N LEU A 114 -7.446 -21.274 -26.007 1.00 65.73 N ANISOU 450 N LEU A 114 7210 8952 8811 -1649 -84 1841 N ATOM 451 CA LEU A 114 -8.593 -21.630 -26.842 1.00 67.29 C ANISOU 451 CA LEU A 114 7276 9156 9136 -1802 -179 1822 C ATOM 452 C LEU A 114 -8.303 -21.449 -28.326 1.00 66.81 C ANISOU 452 C LEU A 114 7294 9001 9089 -1739 -333 1659 C ATOM 453 O LEU A 114 -8.511 -22.371 -29.121 1.00 67.82 O ANISOU 453 O LEU A 114 7446 9016 9306 -1883 -466 1626 O ATOM 454 CB LEU A 114 -9.831 -20.829 -26.433 1.00 71.31 C ANISOU 454 CB LEU A 114 7504 9922 9666 -1816 -88 1869 C ATOM 455 CG LEU A 114 -10.613 -21.368 -25.233 1.00 72.70 C ANISOU 455 CG LEU A 114 7549 10205 9869 -1972 50 2049 C ATOM 456 CD1 LEU A 114 -11.815 -20.487 -24.943 1.00 74.57 C ANISOU 456 CD1 LEU A 114 7482 10714 10134 -1954 152 2077 C ATOM 457 CD2 LEU A 114 -11.051 -22.803 -25.491 1.00 73.52 C ANISOU 457 CD2 LEU A 114 7696 10134 10101 -2234 -48 2142 C ATOM 458 N LEU A 115 -7.802 -20.266 -28.676 1.00 40.95 N ANISOU 458 N LEU A 115 4070 5773 5715 -1537 -320 1560 N ATOM 459 CA LEU A 115 -7.353 -19.974 -30.031 1.00 40.40 C ANISOU 459 CA LEU A 115 4092 5631 5629 -1470 -448 1418 C ATOM 460 C LEU A 115 -6.519 -21.123 -30.588 1.00 40.17 C ANISOU 460 C LEU A 115 4290 5364 5610 -1510 -524 1369 C ATOM 461 O LEU A 115 -6.904 -21.749 -31.582 1.00 41.21 O ANISOU 461 O LEU A 115 4484 5399 5776 -1590 -654 1286 O ATOM 462 CB LEU A 115 -6.551 -18.669 -30.056 1.00 49.04 C ANISOU 462 CB LEU A 115 5210 6810 6613 -1261 -405 1347 C ATOM 463 CG LEU A 115 -7.316 -17.377 -29.762 1.00 49.97 C ANISOU 463 CG LEU A 115 5136 7126 6723 -1184 -366 1345 C ATOM 464 CD1 LEU A 115 -6.377 -16.179 -29.818 1.00 48.48 C ANISOU 464 CD1 LEU A 115 5021 6970 6429 -995 -342 1274 C ATOM 465 CD2 LEU A 115 -8.463 -17.208 -30.744 1.00 51.62 C ANISOU 465 CD2 LEU A 115 5210 7383 7018 -1263 -492 1314 C ATOM 466 N ILE A 116 -5.406 -21.423 -29.918 1.00 51.00 N ANISOU 466 N ILE A 116 5790 6641 6946 -1445 -449 1417 N ATOM 467 CA ILE A 116 -4.500 -22.477 -30.367 1.00 51.35 C ANISOU 467 CA ILE A 116 6049 6452 7009 -1442 -499 1376 C ATOM 468 C ILE A 116 -5.236 -23.806 -30.507 1.00 53.38 C ANISOU 468 C ILE A 116 6354 6548 7381 -1653 -578 1416 C ATOM 469 O ILE A 116 -4.991 -24.568 -31.442 1.00 54.69 O ANISOU 469 O ILE A 116 6676 6532 7573 -1692 -680 1314 O ATOM 470 CB ILE A 116 -3.305 -22.653 -29.402 1.00 79.44 C ANISOU 470 CB ILE A 116 9701 9956 10525 -1323 -409 1451 C ATOM 471 CG1 ILE A 116 -2.456 -21.382 -29.345 1.00 77.56 C ANISOU 471 CG1 ILE A 116 9438 9852 10179 -1136 -357 1400 C ATOM 472 CG2 ILE A 116 -2.444 -23.841 -29.816 1.00 80.55 C ANISOU 472 CG2 ILE A 116 10050 9842 10713 -1305 -454 1421 C ATOM 473 CD1 ILE A 116 -1.178 -21.550 -28.539 1.00 76.66 C ANISOU 473 CD1 ILE A 116 9406 9695 10026 -1019 -300 1467 C ATOM 474 N LEU A 117 -6.160 -24.068 -29.587 1.00 40.64 N ANISOU 474 N LEU A 117 4614 5000 5828 -1797 -528 1563 N ATOM 475 CA LEU A 117 -6.914 -25.315 -29.603 1.00 42.58 C ANISOU 475 CA LEU A 117 4893 5091 6193 -2033 -602 1633 C ATOM 476 C LEU A 117 -7.947 -25.341 -30.722 1.00 44.15 C ANISOU 476 C LEU A 117 5027 5291 6455 -2182 -752 1540 C ATOM 477 O LEU A 117 -8.239 -26.400 -31.277 1.00 45.82 O ANISOU 477 O LEU A 117 5394 5282 6731 -2317 -877 1488 O ATOM 478 CB LEU A 117 -7.596 -25.543 -28.253 1.00 47.61 C ANISOU 478 CB LEU A 117 5381 5840 6868 -2165 -495 1833 C ATOM 479 CG LEU A 117 -6.650 -25.899 -27.106 1.00 47.22 C ANISOU 479 CG LEU A 117 5445 5733 6763 -2080 -387 1956 C ATOM 480 CD1 LEU A 117 -7.362 -25.800 -25.771 1.00 49.40 C ANISOU 480 CD1 LEU A 117 5552 6197 7021 -2183 -255 2142 C ATOM 481 CD2 LEU A 117 -6.084 -27.294 -27.313 1.00 48.64 C ANISOU 481 CD2 LEU A 117 5870 5591 7021 -2143 -466 1983 C ATOM 482 N LEU A 118 -8.487 -24.174 -31.061 1.00 49.42 N ANISOU 482 N LEU A 118 5476 6199 7102 -2153 -750 1518 N ATOM 483 CA LEU A 118 -9.578 -24.106 -32.031 1.00 50.98 C ANISOU 483 CA LEU A 118 5572 6437 7360 -2295 -909 1454 C ATOM 484 C LEU A 118 -9.105 -23.856 -33.460 1.00 51.06 C ANISOU 484 C LEU A 118 5763 6347 7290 -2203 -1040 1266 C ATOM 485 O LEU A 118 -9.795 -24.207 -34.418 1.00 52.73 O ANISOU 485 O LEU A 118 6037 6459 7539 -2356 -1210 1193 O ATOM 486 CB LEU A 118 -10.610 -23.051 -31.615 1.00 38.76 C ANISOU 486 CB LEU A 118 3707 5187 5835 -2277 -863 1514 C ATOM 487 CG LEU A 118 -11.428 -23.376 -30.362 1.00 41.97 C ANISOU 487 CG LEU A 118 3890 5733 6326 -2411 -739 1698 C ATOM 488 CD1 LEU A 118 -12.442 -22.278 -30.067 1.00 42.81 C ANISOU 488 CD1 LEU A 118 3680 6135 6450 -2344 -684 1729 C ATOM 489 CD2 LEU A 118 -12.120 -24.722 -30.509 1.00 46.25 C ANISOU 489 CD2 LEU A 118 4431 6139 7004 -2717 -846 1780 C ATOM 490 N LEU A 119 -7.925 -23.263 -33.601 1.00 56.22 N ANISOU 490 N LEU A 119 6504 7032 7823 -1966 -962 1193 N ATOM 491 CA LEU A 119 -7.414 -22.905 -34.917 1.00 56.36 C ANISOU 491 CA LEU A 119 6673 7000 7741 -1868 -1057 1030 C ATOM 492 C LEU A 119 -6.169 -23.702 -35.290 1.00 56.74 C ANISOU 492 C LEU A 119 7010 6814 7732 -1785 -1039 935 C ATOM 493 O LEU A 119 -6.120 -24.334 -36.346 1.00 58.50 O ANISOU 493 O LEU A 119 7413 6893 7921 -1836 -1157 808 O ATOM 494 CB LEU A 119 -7.120 -21.404 -34.978 1.00 46.29 C ANISOU 494 CB LEU A 119 5295 5923 6370 -1674 -997 1009 C ATOM 495 CG LEU A 119 -8.293 -20.495 -34.604 1.00 46.49 C ANISOU 495 CG LEU A 119 5041 6175 6447 -1701 -1011 1081 C ATOM 496 CD1 LEU A 119 -7.886 -19.032 -34.659 1.00 44.86 C ANISOU 496 CD1 LEU A 119 4789 6109 6146 -1496 -962 1048 C ATOM 497 CD2 LEU A 119 -9.490 -20.756 -35.511 1.00 48.56 C ANISOU 497 CD2 LEU A 119 5226 6451 6775 -1881 -1204 1054 C ATOM 498 N ALA A 120 -5.167 -23.672 -34.417 1.00 49.49 N ANISOU 498 N ALA A 120 6139 5864 6801 -1649 -896 995 N ATOM 499 CA ALA A 120 -3.882 -24.304 -34.701 1.00 50.09 C ANISOU 499 CA ALA A 120 6450 5754 6830 -1514 -857 913 C ATOM 500 C ALA A 120 -3.962 -25.829 -34.736 1.00 52.38 C ANISOU 500 C ALA A 120 6932 5764 7207 -1628 -915 902 C ATOM 501 O ALA A 120 -3.357 -26.464 -35.598 1.00 54.23 O ANISOU 501 O ALA A 120 7390 5815 7401 -1556 -942 769 O ATOM 502 CB ALA A 120 -2.832 -23.846 -33.698 1.00 32.39 C ANISOU 502 CB ALA A 120 4172 3583 4552 -1329 -708 991 C ATOM 503 N MET A 121 -4.709 -26.410 -33.802 1.00 59.11 N ANISOU 503 N MET A 121 7706 6577 8176 -1805 -926 1041 N ATOM 504 CA MET A 121 -4.791 -27.868 -33.688 1.00 61.19 C ANISOU 504 CA MET A 121 8164 6547 8539 -1930 -986 1056 C ATOM 505 C MET A 121 -5.369 -28.627 -34.897 1.00 63.78 C ANISOU 505 C MET A 121 8659 6694 8882 -2088 -1160 905 C ATOM 506 O MET A 121 -4.774 -29.605 -35.335 1.00 65.72 O ANISOU 506 O MET A 121 9174 6677 9120 -2029 -1190 790 O ATOM 507 CB MET A 121 -5.487 -28.295 -32.388 1.00 57.23 C ANISOU 507 CB MET A 121 7545 6049 8151 -2103 -950 1268 C ATOM 508 CG MET A 121 -5.922 -29.754 -32.389 1.00 59.45 C ANISOU 508 CG MET A 121 8036 6002 8548 -2265 -1032 1301 C ATOM 509 SD MET A 121 -6.175 -30.450 -30.747 1.00 59.30 S ANISOU 509 SD MET A 121 7899 5983 8648 -2479 -977 1582 S ATOM 510 CE MET A 121 -4.487 -30.712 -30.216 1.00 57.37 C ANISOU 510 CE MET A 121 7681 5785 8332 -2205 -806 1692 C ATOM 511 N PRO A 122 -6.529 -28.199 -35.431 1.00 59.82 N ANISOU 511 N PRO A 122 8002 6328 8401 -2283 -1282 902 N ATOM 512 CA PRO A 122 -7.059 -28.925 -36.596 1.00 62.37 C ANISOU 512 CA PRO A 122 8499 6472 8728 -2458 -1477 759 C ATOM 513 C PRO A 122 -6.099 -28.881 -37.781 1.00 63.44 C ANISOU 513 C PRO A 122 8862 6542 8702 -2278 -1502 538 C ATOM 514 O PRO A 122 -5.777 -29.926 -38.363 1.00 65.91 O ANISOU 514 O PRO A 122 9442 6611 8992 -2347 -1616 389 O ATOM 515 CB PRO A 122 -8.334 -28.147 -36.940 1.00 43.27 C ANISOU 515 CB PRO A 122 5806 4284 6350 -2660 -1595 819 C ATOM 516 CG PRO A 122 -8.742 -27.514 -35.658 1.00 39.90 C ANISOU 516 CG PRO A 122 5114 4165 5883 -2490 -1448 913 C ATOM 517 CD PRO A 122 -7.459 -27.152 -34.973 1.00 37.96 C ANISOU 517 CD PRO A 122 4905 3869 5650 -2344 -1259 1016 C ATOM 518 N VAL A 123 -5.646 -27.675 -38.116 1.00 54.52 N ANISOU 518 N VAL A 123 7636 5625 7455 -2057 -1392 517 N ATOM 519 CA VAL A 123 -4.702 -27.456 -39.208 1.00 55.63 C ANISOU 519 CA VAL A 123 7972 5738 7428 -1873 -1375 334 C ATOM 520 C VAL A 123 -3.422 -28.273 -39.041 1.00 57.06 C ANISOU 520 C VAL A 123 8396 5680 7606 -1697 -1260 269 C ATOM 521 O VAL A 123 -2.971 -28.935 -39.980 1.00 59.74 O ANISOU 521 O VAL A 123 9004 5833 7863 -1653 -1301 90 O ATOM 522 CB VAL A 123 -4.335 -25.959 -39.345 1.00 43.58 C ANISOU 522 CB VAL A 123 6270 4497 5792 -1696 -1279 360 C ATOM 523 CG1 VAL A 123 -3.201 -25.779 -40.336 1.00 44.86 C ANISOU 523 CG1 VAL A 123 6628 4630 5788 -1486 -1204 209 C ATOM 524 CG2 VAL A 123 -5.555 -25.141 -39.765 1.00 42.89 C ANISOU 524 CG2 VAL A 123 5991 4617 5688 -1831 -1416 385 C ATOM 525 N GLU A 124 -2.844 -28.232 -37.845 1.00 49.30 N ANISOU 525 N GLU A 124 7320 4706 6708 -1589 -1120 414 N ATOM 526 CA GLU A 124 -1.616 -28.971 -37.583 1.00 50.62 C ANISOU 526 CA GLU A 124 7674 4664 6898 -1398 -1012 386 C ATOM 527 C GLU A 124 -1.831 -30.478 -37.645 1.00 53.12 C ANISOU 527 C GLU A 124 8235 4629 7321 -1523 -1107 344 C ATOM 528 O GLU A 124 -0.993 -31.210 -38.160 1.00 55.62 O ANISOU 528 O GLU A 124 8811 4715 7607 -1384 -1084 199 O ATOM 529 CB GLU A 124 -1.022 -28.597 -36.228 1.00 73.82 C ANISOU 529 CB GLU A 124 10439 7710 9898 -1275 -872 574 C ATOM 530 CG GLU A 124 0.149 -29.477 -35.845 1.00 75.25 C ANISOU 530 CG GLU A 124 10780 7685 10128 -1071 -778 577 C ATOM 531 CD GLU A 124 0.729 -29.151 -34.490 1.00 73.00 C ANISOU 531 CD GLU A 124 10340 7480 9916 -1004 -688 788 C ATOM 532 OE1 GLU A 124 0.328 -28.134 -33.883 1.00 70.20 O ANISOU 532 OE1 GLU A 124 9757 7390 9526 -1041 -654 893 O ATOM 533 OE2 GLU A 124 1.594 -29.923 -34.036 1.00 74.13 O ANISOU 533 OE2 GLU A 124 10604 7414 10146 -908 -658 848 O ATOM 534 N LEU A 125 -2.952 -30.938 -37.106 1.00 66.30 N ANISOU 534 N LEU A 125 9822 6253 9116 -1785 -1208 472 N ATOM 535 CA LEU A 125 -3.268 -32.355 -37.125 1.00 68.51 C ANISOU 535 CA LEU A 125 10331 6184 9516 -1950 -1316 462 C ATOM 536 C LEU A 125 -3.296 -32.809 -38.578 1.00 71.38 C ANISOU 536 C LEU A 125 10971 6352 9799 -2015 -1458 215 C ATOM 537 O LEU A 125 -2.486 -33.647 -38.993 1.00 73.84 O ANISOU 537 O LEU A 125 11582 6315 10158 -2014 -1505 117 O ATOM 538 CB LEU A 125 -4.609 -32.603 -36.438 1.00 67.59 C ANISOU 538 CB LEU A 125 10035 6107 9538 -2262 -1401 657 C ATOM 539 CG LEU A 125 -4.923 -34.036 -36.029 1.00 69.60 C ANISOU 539 CG LEU A 125 10499 6000 9944 -2466 -1504 711 C ATOM 540 CD1 LEU A 125 -3.694 -34.665 -35.400 1.00 70.26 C ANISOU 540 CD1 LEU A 125 10772 5842 10081 -2242 -1392 757 C ATOM 541 CD2 LEU A 125 -6.086 -34.050 -35.058 1.00 68.62 C ANISOU 541 CD2 LEU A 125 10139 5987 9948 -2773 -1550 941 C ATOM 542 N TYR A 126 -4.183 -32.200 -39.360 1.00 61.77 N ANISOU 542 N TYR A 126 9668 5350 8450 -2064 -1530 113 N ATOM 543 CA TYR A 126 -4.321 -32.551 -40.770 1.00 64.51 C ANISOU 543 CA TYR A 126 10278 5555 8676 -2131 -1676 -125 C ATOM 544 C TYR A 126 -3.014 -32.443 -41.554 1.00 64.24 C ANISOU 544 C TYR A 126 10468 5465 8474 -1820 -1545 -320 C ATOM 545 O TYR A 126 -2.456 -33.453 -41.981 1.00 67.26 O ANISOU 545 O TYR A 126 11180 5540 8833 -1760 -1563 -490 O ATOM 546 CB TYR A 126 -5.393 -31.689 -41.444 1.00 59.19 C ANISOU 546 CB TYR A 126 9422 5145 7921 -2314 -1827 -137 C ATOM 547 CG TYR A 126 -5.508 -31.911 -42.940 1.00 61.66 C ANISOU 547 CG TYR A 126 10004 5358 8068 -2382 -1992 -380 C ATOM 548 CD1 TYR A 126 -6.241 -32.975 -43.451 1.00 64.39 C ANISOU 548 CD1 TYR A 126 10559 5442 8466 -2654 -2213 -470 C ATOM 549 CD2 TYR A 126 -4.890 -31.050 -43.840 1.00 61.96 C ANISOU 549 CD2 TYR A 126 10098 5561 7882 -2190 -1935 -516 C ATOM 550 CE1 TYR A 126 -6.349 -33.180 -44.814 1.00 67.26 C ANISOU 550 CE1 TYR A 126 11192 5712 8651 -2725 -2380 -703 C ATOM 551 CE2 TYR A 126 -4.992 -31.247 -45.203 1.00 64.16 C ANISOU 551 CE2 TYR A 126 10644 5761 7975 -2253 -2085 -737 C ATOM 552 CZ TYR A 126 -5.723 -32.313 -45.684 1.00 66.05 C ANISOU 552 CZ TYR A 126 11099 5740 8258 -2517 -2311 -837 C ATOM 553 OH TYR A 126 -5.826 -32.513 -47.040 1.00 69.09 O ANISOU 553 OH TYR A 126 11774 6045 8433 -2589 -2475 -1069 O ATOM 554 N ASN A 127 -2.527 -31.219 -41.733 1.00 48.80 N ANISOU 554 N ASN A 127 8332 3803 6405 -1621 -1405 -294 N ATOM 555 CA ASN A 127 -1.424 -30.965 -42.659 1.00 49.71 C ANISOU 555 CA ASN A 127 8613 3936 6336 -1355 -1277 -469 C ATOM 556 C ASN A 127 -0.018 -31.253 -42.137 1.00 50.24 C ANISOU 556 C ASN A 127 8712 3925 6449 -1052 -1059 -442 C ATOM 557 O ASN A 127 0.926 -31.362 -42.920 1.00 52.18 O ANISOU 557 O ASN A 127 9095 4171 6559 -821 -932 -586 O ATOM 558 CB ASN A 127 -1.490 -29.531 -43.187 1.00 45.86 C ANISOU 558 CB ASN A 127 7941 3798 5685 -1317 -1257 -462 C ATOM 559 CG ASN A 127 -1.719 -29.474 -44.682 1.00 48.00 C ANISOU 559 CG ASN A 127 8428 4065 5745 -1383 -1382 -670 C ATOM 560 OD1 ASN A 127 -1.270 -30.346 -45.426 1.00 50.80 O ANISOU 560 OD1 ASN A 127 9104 4191 6005 -1318 -1380 -870 O ATOM 561 ND2 ASN A 127 -2.421 -28.444 -45.131 1.00 46.56 N ANISOU 561 ND2 ASN A 127 8082 4132 5478 -1504 -1494 -626 N ATOM 562 N PHE A 128 0.127 -31.367 -40.823 1.00 37.41 N ANISOU 562 N PHE A 128 6956 2247 5012 -1052 -1013 -249 N ATOM 563 CA PHE A 128 1.445 -31.596 -40.239 1.00 36.09 C ANISOU 563 CA PHE A 128 6786 2020 4904 -769 -832 -193 C ATOM 564 C PHE A 128 1.579 -32.982 -39.617 1.00 40.14 C ANISOU 564 C PHE A 128 7486 2172 5594 -770 -862 -153 C ATOM 565 O PHE A 128 2.689 -33.428 -39.329 1.00 40.66 O ANISOU 565 O PHE A 128 7633 2107 5709 -511 -737 -157 O ATOM 566 CB PHE A 128 1.784 -30.516 -39.207 1.00 43.08 C ANISOU 566 CB PHE A 128 7337 3208 5823 -702 -728 19 C ATOM 567 CG PHE A 128 2.064 -29.169 -39.806 1.00 42.13 C ANISOU 567 CG PHE A 128 7065 3405 5538 -627 -663 -19 C ATOM 568 CD1 PHE A 128 2.909 -29.044 -40.896 1.00 44.81 C ANISOU 568 CD1 PHE A 128 7550 3758 5717 -458 -581 -201 C ATOM 569 CD2 PHE A 128 1.480 -28.028 -39.280 1.00 38.67 C ANISOU 569 CD2 PHE A 128 6351 3243 5098 -723 -676 127 C ATOM 570 CE1 PHE A 128 3.169 -27.804 -41.451 1.00 44.09 C ANISOU 570 CE1 PHE A 128 7330 3950 5471 -406 -523 -215 C ATOM 571 CE2 PHE A 128 1.735 -26.785 -39.830 1.00 37.74 C ANISOU 571 CE2 PHE A 128 6117 3385 4838 -658 -628 101 C ATOM 572 CZ PHE A 128 2.581 -26.673 -40.918 1.00 40.46 C ANISOU 572 CZ PHE A 128 6607 3740 5028 -511 -556 -60 C ATOM 573 N ILE A 129 0.460 -33.670 -39.409 1.00 58.67 N ANISOU 573 N ILE A 129 9892 4357 8043 -1061 -1032 -102 N ATOM 574 CA ILE A 129 0.545 -35.015 -38.851 1.00 60.00 C ANISOU 574 CA ILE A 129 10259 4153 8385 -1106 -1084 -47 C ATOM 575 C ILE A 129 0.031 -36.096 -39.807 1.00 63.12 C ANISOU 575 C ILE A 129 11028 4195 8761 -1215 -1225 -275 C ATOM 576 O ILE A 129 0.646 -37.156 -39.941 1.00 65.49 O ANISOU 576 O ILE A 129 11607 4163 9113 -1043 -1191 -375 O ATOM 577 CB ILE A 129 -0.129 -35.096 -37.462 1.00 62.23 C ANISOU 577 CB ILE A 129 10350 4473 8824 -1368 -1159 220 C ATOM 578 CG1 ILE A 129 0.896 -34.788 -36.368 1.00 60.03 C ANISOU 578 CG1 ILE A 129 9848 4360 8602 -1192 -1011 443 C ATOM 579 CG2 ILE A 129 -0.748 -36.463 -37.225 1.00 64.14 C ANISOU 579 CG2 ILE A 129 10849 4302 9219 -1556 -1294 241 C ATOM 580 CD1 ILE A 129 0.306 -34.155 -35.141 1.00 57.51 C ANISOU 580 CD1 ILE A 129 9236 4457 8158 -1081 -902 478 C ATOM 581 N TRP A 130 -1.075 -35.818 -40.488 1.00 61.17 N ANISOU 581 N TRP A 130 10790 4014 8438 -1491 -1392 -361 N ATOM 582 CA TRP A 130 -1.724 -36.826 -41.327 1.00 65.58 C ANISOU 582 CA TRP A 130 11706 4243 8969 -1652 -1567 -576 C ATOM 583 C TRP A 130 -1.344 -36.777 -42.806 1.00 66.73 C ANISOU 583 C TRP A 130 12079 4394 8878 -1464 -1526 -873 C ATOM 584 O TRP A 130 -1.214 -37.816 -43.450 1.00 69.26 O ANISOU 584 O TRP A 130 12700 4447 9168 -1230 -1441 -1047 O ATOM 585 CB TRP A 130 -3.244 -36.765 -41.158 1.00 70.09 C ANISOU 585 CB TRP A 130 12177 4862 9591 -2079 -1802 -507 C ATOM 586 CG TRP A 130 -3.710 -37.461 -39.921 1.00 71.85 C ANISOU 586 CG TRP A 130 12287 4967 10046 -2305 -1859 -252 C ATOM 587 CD1 TRP A 130 -4.258 -36.888 -38.811 1.00 69.42 C ANISOU 587 CD1 TRP A 130 11603 4946 9825 -2455 -1837 8 C ATOM 588 CD2 TRP A 130 -3.643 -38.868 -39.658 1.00 76.93 C ANISOU 588 CD2 TRP A 130 13208 5167 10854 -2405 -1939 -228 C ATOM 589 NE1 TRP A 130 -4.547 -37.853 -37.877 1.00 72.64 N ANISOU 589 NE1 TRP A 130 12029 5141 10429 -2652 -1888 202 N ATOM 590 CE2 TRP A 130 -4.179 -39.075 -38.371 1.00 77.22 C ANISOU 590 CE2 TRP A 130 13008 5263 11067 -2633 -1960 70 C ATOM 591 CE3 TRP A 130 -3.188 -39.971 -40.387 1.00 81.64 C ANISOU 591 CE3 TRP A 130 14243 5313 11463 -2318 -1990 -431 C ATOM 592 CZ2 TRP A 130 -4.274 -40.344 -37.801 1.00 81.99 C ANISOU 592 CZ2 TRP A 130 13798 5493 11859 -2796 -2039 192 C ATOM 593 CZ3 TRP A 130 -3.282 -41.226 -39.817 1.00 86.37 C ANISOU 593 CZ3 TRP A 130 15035 5516 12263 -2467 -2078 -322 C ATOM 594 CH2 TRP A 130 -3.821 -41.402 -38.538 1.00 86.52 C ANISOU 594 CH2 TRP A 130 14809 5607 12456 -2713 -2106 -3 C ATOM 595 N VAL A 131 -1.177 -35.576 -43.344 1.00 57.74 N ANISOU 595 N VAL A 131 10804 3565 7568 -1559 -1582 -927 N ATOM 596 CA VAL A 131 -0.772 -35.425 -44.739 1.00 58.40 C ANISOU 596 CA VAL A 131 11097 3698 7394 -1408 -1545 -1189 C ATOM 597 C VAL A 131 0.197 -34.251 -44.894 1.00 52.77 C ANISOU 597 C VAL A 131 10169 3322 6561 -1106 -1304 -1146 C ATOM 598 O VAL A 131 -0.196 -33.082 -44.876 1.00 48.63 O ANISOU 598 O VAL A 131 9343 3143 5991 -1169 -1303 -1015 O ATOM 599 CB VAL A 131 -1.994 -35.313 -45.687 1.00 71.09 C ANISOU 599 CB VAL A 131 12760 5394 8858 -1711 -1791 -1298 C ATOM 600 CG1 VAL A 131 -3.047 -34.380 -45.102 1.00 68.25 C ANISOU 600 CG1 VAL A 131 11989 5358 8584 -1939 -1887 -1059 C ATOM 601 CG2 VAL A 131 -1.567 -34.856 -47.076 1.00 71.77 C ANISOU 601 CG2 VAL A 131 13015 5616 8640 -1546 -1732 -1526 C ATOM 602 N HIS A 132 1.476 -34.585 -45.032 1.00 60.15 N ANISOU 602 N HIS A 132 11256 4143 7457 -775 -1101 -1252 N ATOM 603 CA HIS A 132 2.547 -33.599 -44.981 1.00 56.52 C ANISOU 603 CA HIS A 132 10577 3975 6923 -487 -860 -1185 C ATOM 604 C HIS A 132 2.651 -32.784 -46.267 1.00 56.50 C ANISOU 604 C HIS A 132 10620 4215 6634 -439 -819 -1340 C ATOM 605 O HIS A 132 3.251 -31.707 -46.285 1.00 55.50 O ANISOU 605 O HIS A 132 10253 4404 6430 -314 -677 -1245 O ATOM 606 CB HIS A 132 3.872 -34.297 -44.667 1.00 73.43 C ANISOU 606 CB HIS A 132 12827 5925 9149 -144 -656 -1221 C ATOM 607 CG HIS A 132 3.761 -35.336 -43.593 1.00 72.66 C ANISOU 607 CG HIS A 132 12702 5583 9322 -167 -696 -1050 C ATOM 608 ND1 HIS A 132 3.928 -35.048 -42.255 1.00 72.70 N ANISOU 608 ND1 HIS A 132 12704 5465 9454 137 -531 -994 N ATOM 609 CD2 HIS A 132 3.483 -36.660 -43.660 1.00 71.86 C ANISOU 609 CD2 HIS A 132 12571 5346 9388 -458 -882 -908 C ATOM 610 CE1 HIS A 132 3.765 -36.150 -41.546 1.00 71.96 C ANISOU 610 CE1 HIS A 132 12602 5158 9583 33 -624 -822 C ATOM 611 NE2 HIS A 132 3.495 -37.143 -42.374 1.00 71.46 N ANISOU 611 NE2 HIS A 132 12523 5085 9544 -333 -827 -766 N ATOM 612 N HIS A 133 2.056 -33.303 -47.336 1.00 56.33 N ANISOU 612 N HIS A 133 10924 4034 6447 -552 -952 -1574 N ATOM 613 CA HIS A 133 2.038 -32.616 -48.620 1.00 56.84 C ANISOU 613 CA HIS A 133 11075 4312 6210 -547 -949 -1721 C ATOM 614 C HIS A 133 0.859 -33.093 -49.460 1.00 60.59 C ANISOU 614 C HIS A 133 11828 4628 6566 -834 -1229 -1894 C ATOM 615 O HIS A 133 0.539 -34.281 -49.463 1.00 65.04 O ANISOU 615 O HIS A 133 12662 4833 7217 -922 -1344 -2014 O ATOM 616 CB HIS A 133 3.352 -32.840 -49.374 1.00 54.68 C ANISOU 616 CB HIS A 133 10986 4031 5759 -198 -684 -1900 C ATOM 617 CG HIS A 133 3.547 -34.248 -49.842 1.00 61.01 C ANISOU 617 CG HIS A 133 12203 4432 6548 -87 -672 -2149 C ATOM 618 ND1 HIS A 133 3.828 -35.285 -48.980 1.00 65.93 N ANISOU 618 ND1 HIS A 133 13177 4989 6885 36 -604 -2436 N ATOM 619 CD2 HIS A 133 3.498 -34.792 -51.082 1.00 63.75 C ANISOU 619 CD2 HIS A 133 12690 4407 7124 -75 -720 -2156 C ATOM 620 CE1 HIS A 133 3.942 -36.408 -49.667 1.00 71.41 C ANISOU 620 CE1 HIS A 133 14215 5278 7638 129 -608 -2627 C ATOM 621 NE2 HIS A 133 3.749 -36.135 -50.945 1.00 70.19 N ANISOU 621 NE2 HIS A 133 13941 4923 7804 62 -685 -2455 N ATOM 622 N PRO A 134 0.207 -32.167 -50.181 1.00 66.46 N ANISOU 622 N PRO A 134 12515 5629 7110 -988 -1355 -1904 N ATOM 623 CA PRO A 134 0.553 -30.743 -50.223 1.00 61.95 C ANISOU 623 CA PRO A 134 11653 5454 6431 -898 -1237 -1761 C ATOM 624 C PRO A 134 -0.147 -29.940 -49.131 1.00 57.57 C ANISOU 624 C PRO A 134 10683 5097 6094 -1051 -1318 -1476 C ATOM 625 O PRO A 134 -1.080 -30.436 -48.499 1.00 58.32 O ANISOU 625 O PRO A 134 10712 5068 6381 -1281 -1502 -1396 O ATOM 626 CB PRO A 134 0.029 -30.315 -51.591 1.00 56.58 C ANISOU 626 CB PRO A 134 11163 4891 5443 -1030 -1395 -1911 C ATOM 627 CG PRO A 134 -1.180 -31.170 -51.790 1.00 61.45 C ANISOU 627 CG PRO A 134 11971 5262 6115 -1329 -1702 -2008 C ATOM 628 CD PRO A 134 -0.876 -32.497 -51.126 1.00 63.35 C ANISOU 628 CD PRO A 134 12376 5129 6564 -1264 -1642 -2071 C ATOM 629 N TRP A 135 0.311 -28.711 -48.916 1.00 60.00 N ANISOU 629 N TRP A 135 10720 5709 6366 -924 -1172 -1327 N ATOM 630 CA TRP A 135 -0.357 -27.791 -48.007 1.00 57.17 C ANISOU 630 CA TRP A 135 9989 5565 6168 -1045 -1237 -1081 C ATOM 631 C TRP A 135 -1.695 -27.397 -48.618 1.00 55.98 C ANISOU 631 C TRP A 135 9814 5513 5943 -1314 -1513 -1081 C ATOM 632 O TRP A 135 -1.788 -27.171 -49.824 1.00 56.19 O ANISOU 632 O TRP A 135 9992 5637 5722 -1328 -1579 -1195 O ATOM 633 CB TRP A 135 0.511 -26.556 -47.762 1.00 56.27 C ANISOU 633 CB TRP A 135 9647 5730 6003 -848 -1031 -953 C ATOM 634 CG TRP A 135 -0.122 -25.531 -46.861 1.00 53.00 C ANISOU 634 CG TRP A 135 8882 5533 5722 -946 -1088 -726 C ATOM 635 CD1 TRP A 135 -0.726 -24.369 -47.241 1.00 50.62 C ANISOU 635 CD1 TRP A 135 8448 5467 5318 -1025 -1183 -656 C ATOM 636 CD2 TRP A 135 -0.207 -25.577 -45.429 1.00 50.67 C ANISOU 636 CD2 TRP A 135 8343 5234 5676 -961 -1049 -544 C ATOM 637 NE1 TRP A 135 -1.182 -23.689 -46.135 1.00 47.31 N ANISOU 637 NE1 TRP A 135 7718 5182 5078 -1074 -1197 -456 N ATOM 638 CE2 TRP A 135 -0.877 -24.410 -45.012 1.00 47.16 C ANISOU 638 CE2 TRP A 135 7628 5029 5263 -1042 -1112 -388 C ATOM 639 CE3 TRP A 135 0.219 -26.492 -44.462 1.00 50.90 C ANISOU 639 CE3 TRP A 135 8369 5077 5896 -907 -970 -495 C ATOM 640 CZ2 TRP A 135 -1.130 -24.135 -43.668 1.00 44.08 C ANISOU 640 CZ2 TRP A 135 6974 4706 5069 -1070 -1083 -203 C ATOM 641 CZ3 TRP A 135 -0.034 -26.217 -43.130 1.00 47.62 C ANISOU 641 CZ3 TRP A 135 7689 4738 5668 -951 -954 -293 C ATOM 642 CH2 TRP A 135 -0.704 -25.050 -42.745 1.00 44.34 C ANISOU 642 CH2 TRP A 135 7014 4571 5261 -1032 -1003 -158 C ATOM 643 N ALA A 136 -2.731 -27.319 -47.790 1.00 44.57 N ANISOU 643 N ALA A 136 8168 4055 4711 -1527 -1672 -941 N ATOM 644 CA ALA A 136 -4.089 -27.150 -48.295 1.00 47.98 C ANISOU 644 CA ALA A 136 8570 4542 5119 -1804 -1961 -943 C ATOM 645 C ALA A 136 -4.780 -25.875 -47.813 1.00 45.57 C ANISOU 645 C ALA A 136 7933 4557 4826 -1838 -2013 -762 C ATOM 646 O ALA A 136 -5.961 -25.670 -48.092 1.00 48.35 O ANISOU 646 O ALA A 136 8261 5017 5092 -1999 -2236 -770 O ATOM 647 CB ALA A 136 -4.932 -28.371 -47.942 1.00 55.46 C ANISOU 647 CB ALA A 136 9506 5274 6292 -2045 -2121 -907 C ATOM 648 N PHE A 137 -4.056 -25.019 -47.101 1.00 64.39 N ANISOU 648 N PHE A 137 10066 7083 7318 -1682 -1820 -600 N ATOM 649 CA PHE A 137 -4.668 -23.819 -46.535 1.00 62.08 C ANISOU 649 CA PHE A 137 9466 7061 7061 -1695 -1856 -430 C ATOM 650 C PHE A 137 -4.168 -22.523 -47.166 1.00 61.13 C ANISOU 650 C PHE A 137 9401 7117 6709 -1539 -1784 -457 C ATOM 651 O PHE A 137 -4.498 -21.432 -46.702 1.00 61.95 O ANISOU 651 O PHE A 137 9747 7156 6635 -1407 -1662 -591 O ATOM 652 CB PHE A 137 -4.481 -23.785 -45.017 1.00 56.63 C ANISOU 652 CB PHE A 137 8494 6430 6590 -1630 -1706 -245 C ATOM 653 CG PHE A 137 -5.040 -24.987 -44.317 1.00 57.06 C ANISOU 653 CG PHE A 137 8518 6304 6856 -1775 -1744 -202 C ATOM 654 CD1 PHE A 137 -6.394 -25.080 -44.045 1.00 56.49 C ANISOU 654 CD1 PHE A 137 8267 6274 6922 -2008 -1926 -113 C ATOM 655 CD2 PHE A 137 -4.212 -26.028 -43.934 1.00 58.01 C ANISOU 655 CD2 PHE A 137 8785 6213 7041 -1679 -1600 -237 C ATOM 656 CE1 PHE A 137 -6.912 -26.187 -43.403 1.00 56.80 C ANISOU 656 CE1 PHE A 137 8278 6150 7151 -2166 -1955 -53 C ATOM 657 CE2 PHE A 137 -4.724 -27.138 -43.291 1.00 58.16 C ANISOU 657 CE2 PHE A 137 8797 6050 7251 -1823 -1643 -178 C ATOM 658 CZ PHE A 137 -6.075 -27.217 -43.025 1.00 57.54 C ANISOU 658 CZ PHE A 137 8546 6018 7299 -2079 -1816 -84 C ATOM 659 N GLY A 138 -3.376 -22.645 -48.225 1.00 66.55 N ANISOU 659 N GLY A 138 9867 8022 7395 -1553 -1855 -326 N ATOM 660 CA GLY A 138 -2.916 -21.485 -48.964 1.00 65.24 C ANISOU 660 CA GLY A 138 9748 8020 7020 -1429 -1804 -319 C ATOM 661 C GLY A 138 -1.890 -20.635 -48.237 1.00 64.27 C ANISOU 661 C GLY A 138 9588 7940 6890 -1213 -1525 -270 C ATOM 662 O GLY A 138 -1.464 -20.959 -47.126 1.00 64.44 O ANISOU 662 O GLY A 138 9531 7878 7076 -1149 -1382 -234 O ATOM 663 N ASP A 139 -1.505 -19.534 -48.875 1.00 60.94 N ANISOU 663 N ASP A 139 9224 7655 6275 -1114 -1459 -258 N ATOM 664 CA ASP A 139 -0.462 -18.654 -48.363 1.00 59.91 C ANISOU 664 CA ASP A 139 9034 7596 6133 -933 -1212 -194 C ATOM 665 C ASP A 139 -0.878 -17.979 -47.058 1.00 56.74 C ANISOU 665 C ASP A 139 8335 7275 5949 -918 -1186 -18 C ATOM 666 O ASP A 139 -0.123 -17.972 -46.082 1.00 56.05 O ANISOU 666 O ASP A 139 8150 7176 5969 -813 -1010 38 O ATOM 667 CB ASP A 139 -0.116 -17.597 -49.413 1.00 64.68 C ANISOU 667 CB ASP A 139 9751 8343 6484 -875 -1175 -190 C ATOM 668 CG ASP A 139 1.283 -17.049 -49.249 1.00 64.61 C ANISOU 668 CG ASP A 139 9721 8396 6434 -707 -908 -151 C ATOM 669 OD1 ASP A 139 2.224 -17.648 -49.811 1.00 66.67 O ANISOU 669 OD1 ASP A 139 10179 8666 6487 -632 -786 -251 O ATOM 670 OD2 ASP A 139 1.444 -16.018 -48.564 1.00 62.51 O ANISOU 670 OD2 ASP A 139 9238 8178 6337 -653 -821 -19 O ATOM 671 N ALA A 140 -2.083 -17.414 -47.049 1.00 45.00 N ANISOU 671 N ALA A 140 6707 5870 4520 -1018 -1368 65 N ATOM 672 CA ALA A 140 -2.604 -16.715 -45.878 1.00 42.15 C ANISOU 672 CA ALA A 140 6076 5584 4354 -1006 -1358 211 C ATOM 673 C ALA A 140 -2.743 -17.652 -44.682 1.00 42.53 C ANISOU 673 C ALA A 140 6028 5525 4605 -1042 -1303 221 C ATOM 674 O ALA A 140 -2.499 -17.261 -43.539 1.00 40.53 O ANISOU 674 O ALA A 140 5607 5308 4483 -982 -1196 321 O ATOM 675 CB ALA A 140 -3.942 -16.066 -46.202 1.00 26.75 C ANISOU 675 CB ALA A 140 3998 3734 2430 -1093 -1570 281 C ATOM 676 N GLY A 141 -3.135 -18.892 -44.953 1.00 47.34 N ANISOU 676 N GLY A 141 6763 5994 5230 -1151 -1386 120 N ATOM 677 CA GLY A 141 -3.230 -19.896 -43.911 1.00 47.98 C ANISOU 677 CA GLY A 141 6798 5943 5489 -1197 -1336 134 C ATOM 678 C GLY A 141 -1.854 -20.256 -43.392 1.00 48.42 C ANISOU 678 C GLY A 141 6928 5918 5550 -1041 -1121 120 C ATOM 679 O GLY A 141 -1.650 -20.397 -42.183 1.00 47.15 O ANISOU 679 O GLY A 141 6641 5736 5537 -1009 -1026 212 O ATOM 680 N CYS A 142 -0.906 -20.392 -44.316 1.00 47.84 N ANISOU 680 N CYS A 142 7056 5814 5309 -939 -1042 10 N ATOM 681 CA CYS A 142 0.472 -20.732 -43.978 1.00 49.08 C ANISOU 681 CA CYS A 142 7269 5913 5466 -768 -835 -7 C ATOM 682 C CYS A 142 1.109 -19.699 -43.052 1.00 46.04 C ANISOU 682 C CYS A 142 6675 5675 5145 -666 -710 141 C ATOM 683 O CYS A 142 1.673 -20.050 -42.015 1.00 45.54 O ANISOU 683 O CYS A 142 6529 5565 5208 -601 -610 207 O ATOM 684 CB CYS A 142 1.308 -20.879 -45.250 1.00 46.44 C ANISOU 684 CB CYS A 142 7162 5567 4916 -670 -759 -147 C ATOM 685 SG CYS A 142 3.067 -21.184 -44.959 1.00 48.47 S ANISOU 685 SG CYS A 142 7454 5785 5180 -435 -490 -165 S ATOM 686 N ARG A 143 1.017 -18.427 -43.429 1.00 56.45 N ANISOU 686 N ARG A 143 7922 7158 6367 -659 -731 195 N ATOM 687 CA ARG A 143 1.597 -17.348 -42.632 1.00 53.33 C ANISOU 687 CA ARG A 143 7356 6888 6018 -581 -634 323 C ATOM 688 C ARG A 143 0.825 -17.133 -41.328 1.00 50.44 C ANISOU 688 C ARG A 143 6799 6540 5825 -638 -682 430 C ATOM 689 O ARG A 143 1.417 -16.992 -40.250 1.00 48.76 O ANISOU 689 O ARG A 143 6480 6347 5699 -576 -583 512 O ATOM 690 CB ARG A 143 1.632 -16.051 -43.445 1.00 61.55 C ANISOU 690 CB ARG A 143 8401 8070 6914 -576 -665 356 C ATOM 691 CG ARG A 143 2.453 -16.140 -44.725 1.00 64.13 C ANISOU 691 CG ARG A 143 8909 8416 7040 -516 -584 272 C ATOM 692 CD ARG A 143 2.243 -14.914 -45.605 1.00 62.55 C ANISOU 692 CD ARG A 143 8731 8346 6688 -541 -643 325 C ATOM 693 NE ARG A 143 3.507 -14.292 -45.993 1.00 62.75 N ANISOU 693 NE ARG A 143 8805 8456 6582 -456 -476 347 N ATOM 694 CZ ARG A 143 4.211 -14.631 -47.068 1.00 65.29 C ANISOU 694 CZ ARG A 143 9310 8793 6705 -423 -404 254 C ATOM 695 NH1 ARG A 143 3.779 -15.593 -47.873 1.00 67.82 N ANISOU 695 NH1 ARG A 143 9811 9032 6925 -471 -502 117 N ATOM 696 NH2 ARG A 143 5.350 -14.008 -47.337 1.00 65.17 N ANISOU 696 NH2 ARG A 143 9299 8879 6582 -350 -231 297 N ATOM 697 N GLY A 144 -0.501 -17.123 -41.438 1.00 44.74 N ANISOU 697 N GLY A 144 6031 5822 5145 -758 -833 430 N ATOM 698 CA GLY A 144 -1.370 -16.887 -40.300 1.00 42.67 C ANISOU 698 CA GLY A 144 5576 5604 5030 -814 -868 528 C ATOM 699 C GLY A 144 -1.241 -17.932 -39.208 1.00 43.09 C ANISOU 699 C GLY A 144 5600 5557 5215 -834 -799 561 C ATOM 700 O GLY A 144 -1.384 -17.620 -38.025 1.00 41.15 O ANISOU 700 O GLY A 144 5209 5366 5059 -825 -748 658 O ATOM 701 N TYR A 145 -0.974 -19.172 -39.606 1.00 45.76 N ANISOU 701 N TYR A 145 6094 5738 5554 -860 -801 479 N ATOM 702 CA TYR A 145 -0.772 -20.260 -38.653 1.00 46.27 C ANISOU 702 CA TYR A 145 6164 5672 5742 -878 -746 519 C ATOM 703 C TYR A 145 0.388 -19.965 -37.704 1.00 44.76 C ANISOU 703 C TYR A 145 5914 5518 5574 -737 -598 601 C ATOM 704 O TYR A 145 0.204 -19.870 -36.485 1.00 42.80 O ANISOU 704 O TYR A 145 5541 5305 5413 -754 -565 711 O ATOM 705 CB TYR A 145 -0.526 -21.575 -39.400 1.00 47.71 C ANISOU 705 CB TYR A 145 6568 5648 5909 -901 -775 398 C ATOM 706 CG TYR A 145 -0.147 -22.737 -38.509 1.00 48.47 C ANISOU 706 CG TYR A 145 6714 5573 6126 -881 -710 440 C ATOM 707 CD1 TYR A 145 -1.119 -23.476 -37.848 1.00 48.24 C ANISOU 707 CD1 TYR A 145 6643 5456 6230 -1040 -781 511 C ATOM 708 CD2 TYR A 145 1.182 -23.100 -38.336 1.00 49.64 C ANISOU 708 CD2 TYR A 145 6946 5651 6262 -704 -581 423 C ATOM 709 CE1 TYR A 145 -0.777 -24.538 -37.034 1.00 48.88 C ANISOU 709 CE1 TYR A 145 6788 5365 6417 -1027 -732 569 C ATOM 710 CE2 TYR A 145 1.534 -24.157 -37.523 1.00 50.33 C ANISOU 710 CE2 TYR A 145 7083 5571 6467 -670 -538 476 C ATOM 711 CZ TYR A 145 0.552 -24.875 -36.875 1.00 49.83 C ANISOU 711 CZ TYR A 145 7004 5404 6524 -834 -617 551 C ATOM 712 OH TYR A 145 0.900 -25.933 -36.066 1.00 50.52 O ANISOU 712 OH TYR A 145 7160 5311 6724 -805 -584 622 O ATOM 713 N TYR A 146 1.581 -19.823 -38.274 1.00 58.54 N ANISOU 713 N TYR A 146 7743 7270 7232 -603 -512 550 N ATOM 714 CA TYR A 146 2.786 -19.568 -37.493 1.00 57.38 C ANISOU 714 CA TYR A 146 7530 7165 7109 -474 -390 627 C ATOM 715 C TYR A 146 2.724 -18.233 -36.757 1.00 53.65 C ANISOU 715 C TYR A 146 6893 6863 6629 -476 -382 727 C ATOM 716 O TYR A 146 3.200 -18.119 -35.620 1.00 51.86 O ANISOU 716 O TYR A 146 6579 6668 6458 -438 -330 822 O ATOM 717 CB TYR A 146 4.029 -19.644 -38.384 1.00 40.13 C ANISOU 717 CB TYR A 146 5442 4973 4831 -338 -293 553 C ATOM 718 CG TYR A 146 4.357 -21.047 -38.842 1.00 44.22 C ANISOU 718 CG TYR A 146 6134 5299 5370 -285 -266 452 C ATOM 719 CD1 TYR A 146 3.794 -21.574 -39.998 1.00 47.16 C ANISOU 719 CD1 TYR A 146 6683 5583 5651 -335 -327 308 C ATOM 720 CD2 TYR A 146 5.227 -21.849 -38.112 1.00 45.03 C ANISOU 720 CD2 TYR A 146 6238 5294 5578 -181 -193 500 C ATOM 721 CE1 TYR A 146 4.092 -22.859 -40.413 1.00 50.63 C ANISOU 721 CE1 TYR A 146 7314 5820 6103 -282 -305 195 C ATOM 722 CE2 TYR A 146 5.531 -23.133 -38.520 1.00 48.63 C ANISOU 722 CE2 TYR A 146 6870 5543 6062 -112 -169 402 C ATOM 723 CZ TYR A 146 4.961 -23.635 -39.670 1.00 51.36 C ANISOU 723 CZ TYR A 146 7408 5790 6315 -162 -221 241 C ATOM 724 OH TYR A 146 5.262 -24.914 -40.080 1.00 54.69 O ANISOU 724 OH TYR A 146 8038 5981 6759 -88 -200 123 O ATOM 725 N PHE A 147 2.131 -17.229 -37.401 1.00 44.08 N ANISOU 725 N PHE A 147 5656 5749 5345 -518 -446 704 N ATOM 726 CA PHE A 147 1.935 -15.936 -36.752 1.00 41.12 C ANISOU 726 CA PHE A 147 5152 5505 4968 -515 -451 782 C ATOM 727 C PHE A 147 1.107 -16.084 -35.479 1.00 39.81 C ANISOU 727 C PHE A 147 4875 5351 4902 -572 -464 854 C ATOM 728 O PHE A 147 1.477 -15.564 -34.425 1.00 38.12 O ANISOU 728 O PHE A 147 4585 5197 4703 -535 -413 927 O ATOM 729 CB PHE A 147 1.267 -14.938 -37.698 1.00 36.01 C ANISOU 729 CB PHE A 147 4511 4930 4241 -545 -537 750 C ATOM 730 CG PHE A 147 0.869 -13.647 -37.034 1.00 33.53 C ANISOU 730 CG PHE A 147 4081 4715 3943 -535 -558 818 C ATOM 731 CD1 PHE A 147 1.821 -12.686 -36.734 1.00 31.82 C ANISOU 731 CD1 PHE A 147 3851 4553 3685 -473 -503 862 C ATOM 732 CD2 PHE A 147 -0.455 -13.397 -36.709 1.00 33.44 C ANISOU 732 CD2 PHE A 147 3973 4738 3994 -586 -633 834 C ATOM 733 CE1 PHE A 147 1.460 -11.501 -36.124 1.00 30.29 C ANISOU 733 CE1 PHE A 147 3586 4419 3503 -459 -529 908 C ATOM 734 CE2 PHE A 147 -0.821 -12.213 -36.098 1.00 32.20 C ANISOU 734 CE2 PHE A 147 3724 4660 3852 -547 -640 881 C ATOM 735 CZ PHE A 147 0.138 -11.264 -35.806 1.00 30.70 C ANISOU 735 CZ PHE A 147 3558 4495 3612 -481 -590 910 C ATOM 736 N LEU A 148 -0.011 -16.797 -35.586 1.00 37.09 N ANISOU 736 N LEU A 148 4523 4955 4615 -672 -533 836 N ATOM 737 CA LEU A 148 -0.877 -17.047 -34.438 1.00 36.65 C ANISOU 737 CA LEU A 148 4352 4923 4650 -744 -529 914 C ATOM 738 C LEU A 148 -0.142 -17.823 -33.352 1.00 36.42 C ANISOU 738 C LEU A 148 4341 4829 4665 -721 -446 986 C ATOM 739 O LEU A 148 -0.271 -17.519 -32.161 1.00 35.38 O ANISOU 739 O LEU A 148 4120 4769 4552 -721 -398 1071 O ATOM 740 CB LEU A 148 -2.127 -17.815 -34.866 1.00 46.32 C ANISOU 740 CB LEU A 148 5561 6098 5939 -882 -625 890 C ATOM 741 CG LEU A 148 -3.099 -18.175 -33.742 1.00 46.54 C ANISOU 741 CG LEU A 148 5451 6165 6067 -981 -608 985 C ATOM 742 CD1 LEU A 148 -3.691 -16.916 -33.126 1.00 45.63 C ANISOU 742 CD1 LEU A 148 5173 6221 5942 -929 -573 1032 C ATOM 743 CD2 LEU A 148 -4.195 -19.096 -34.253 1.00 48.59 C ANISOU 743 CD2 LEU A 148 5695 6364 6403 -1146 -717 968 C ATOM 744 N ARG A 149 0.627 -18.824 -33.774 1.00 44.97 N ANISOU 744 N ARG A 149 5550 5776 5759 -689 -431 951 N ATOM 745 CA ARG A 149 1.424 -19.633 -32.858 1.00 45.08 C ANISOU 745 CA ARG A 149 5593 5709 5824 -648 -371 1029 C ATOM 746 C ARG A 149 2.332 -18.745 -32.006 1.00 43.04 C ANISOU 746 C ARG A 149 5264 5566 5523 -551 -309 1099 C ATOM 747 O ARG A 149 2.232 -18.725 -30.769 1.00 42.14 O ANISOU 747 O ARG A 149 5093 5493 5426 -568 -283 1200 O ATOM 748 CB ARG A 149 2.270 -20.632 -33.651 1.00121.87 C ANISOU 748 CB ARG A 149 15472 15267 15566 -583 -360 959 C ATOM 749 CG ARG A 149 2.691 -21.872 -32.879 1.00123.19 C ANISOU 749 CG ARG A 149 15692 15296 15819 -552 -329 1042 C ATOM 750 CD ARG A 149 1.528 -22.838 -32.703 1.00123.99 C ANISOU 750 CD ARG A 149 15825 15279 16006 -710 -386 1085 C ATOM 751 NE ARG A 149 1.934 -24.062 -32.020 1.00126.05 N ANISOU 751 NE ARG A 149 16210 15332 16352 -679 -379 1131 N ATOM 752 CZ ARG A 149 2.462 -25.118 -32.630 1.00127.93 C ANISOU 752 CZ ARG A 149 16608 15352 16647 -729 -431 1056 C ATOM 753 NH1 ARG A 149 2.652 -25.103 -33.943 1.00128.93 N ANISOU 753 NH1 ARG A 149 16786 15460 16743 -827 -502 929 N ATOM 754 NH2 ARG A 149 2.802 -26.190 -31.927 1.00128.85 N ANISOU 754 NH2 ARG A 149 16848 15259 16851 -682 -425 1107 N ATOM 755 N ASP A 150 3.206 -18.003 -32.681 1.00 38.65 N ANISOU 755 N ASP A 150 4718 5068 4901 -464 -290 1050 N ATOM 756 CA ASP A 150 4.143 -17.113 -32.001 1.00 36.90 C ANISOU 756 CA ASP A 150 4431 4951 4640 -394 -253 1111 C ATOM 757 C ASP A 150 3.438 -16.078 -31.129 1.00 35.21 C ANISOU 757 C ASP A 150 4134 4850 4397 -443 -268 1154 C ATOM 758 O ASP A 150 3.843 -15.840 -29.991 1.00 34.49 O ANISOU 758 O ASP A 150 4006 4806 4294 -431 -249 1232 O ATOM 759 CB ASP A 150 5.061 -16.420 -33.012 1.00 58.38 C ANISOU 759 CB ASP A 150 7166 7721 7295 -326 -232 1057 C ATOM 760 CG ASP A 150 6.152 -17.337 -33.533 1.00 60.55 C ANISOU 760 CG ASP A 150 7485 7929 7592 -225 -172 1046 C ATOM 761 OD1 ASP A 150 5.891 -18.550 -33.687 1.00 62.69 O ANISOU 761 OD1 ASP A 150 7827 8066 7926 -210 -166 1032 O ATOM 762 OD2 ASP A 150 7.273 -16.845 -33.780 1.00 60.52 O ANISOU 762 OD2 ASP A 150 7444 8002 7550 -160 -127 1056 O ATOM 763 N ALA A 151 2.379 -15.477 -31.664 1.00 41.85 N ANISOU 763 N ALA A 151 4949 5733 5219 -488 -306 1100 N ATOM 764 CA ALA A 151 1.627 -14.455 -30.942 1.00 41.31 C ANISOU 764 CA ALA A 151 4804 5765 5127 -503 -309 1122 C ATOM 765 C ALA A 151 1.081 -14.987 -29.622 1.00 41.83 C ANISOU 765 C ALA A 151 4823 5848 5222 -549 -270 1196 C ATOM 766 O ALA A 151 1.249 -14.364 -28.570 1.00 41.66 O ANISOU 766 O ALA A 151 4774 5902 5152 -528 -237 1236 O ATOM 767 CB ALA A 151 0.493 -13.917 -31.811 1.00 22.55 C ANISOU 767 CB ALA A 151 2397 3419 2753 -529 -365 1061 C ATOM 768 N CYS A 152 0.429 -16.144 -29.684 1.00 32.02 N ANISOU 768 N CYS A 152 3586 4530 4049 -622 -274 1215 N ATOM 769 CA CYS A 152 -0.129 -16.767 -28.490 1.00 32.71 C ANISOU 769 CA CYS A 152 3632 4633 4164 -690 -230 1308 C ATOM 770 C CYS A 152 0.959 -17.156 -27.493 1.00 32.11 C ANISOU 770 C CYS A 152 3608 4538 4055 -649 -195 1396 C ATOM 771 O CYS A 152 0.773 -17.029 -26.278 1.00 32.34 O ANISOU 771 O CYS A 152 3607 4646 4033 -666 -149 1470 O ATOM 772 CB CYS A 152 -0.976 -17.985 -28.859 1.00 30.10 C ANISOU 772 CB CYS A 152 3308 4203 3926 -804 -259 1321 C ATOM 773 SG CYS A 152 -2.533 -17.586 -29.689 1.00 31.37 S ANISOU 773 SG CYS A 152 3350 4432 4134 -891 -314 1263 S ATOM 774 N THR A 153 2.092 -17.629 -28.008 1.00 42.92 N ANISOU 774 N THR A 153 5051 5812 5444 -588 -216 1389 N ATOM 775 CA THR A 153 3.223 -17.967 -27.145 1.00 42.66 C ANISOU 775 CA THR A 153 5049 5765 5394 -537 -206 1485 C ATOM 776 C THR A 153 3.711 -16.746 -26.359 1.00 41.68 C ANISOU 776 C THR A 153 4888 5778 5171 -496 -204 1499 C ATOM 777 O THR A 153 3.836 -16.789 -25.125 1.00 41.77 O ANISOU 777 O THR A 153 4904 5841 5126 -507 -196 1589 O ATOM 778 CB THR A 153 4.397 -18.552 -27.952 1.00 86.53 C ANISOU 778 CB THR A 153 10664 11206 11006 -449 -221 1469 C ATOM 779 OG1 THR A 153 3.966 -19.734 -28.637 1.00 87.98 O ANISOU 779 OG1 THR A 153 10915 11248 11265 -484 -232 1411 O ATOM 780 CG2 THR A 153 5.556 -18.901 -27.030 1.00 86.89 C ANISOU 780 CG2 THR A 153 10731 11215 11069 -399 -227 1596 C ATOM 781 N TYR A 154 3.984 -15.663 -27.084 1.00 42.78 N ANISOU 781 N TYR A 154 5008 5969 5279 -460 -221 1411 N ATOM 782 CA TYR A 154 4.420 -14.409 -26.472 1.00 42.25 C ANISOU 782 CA TYR A 154 4926 6004 5123 -439 -235 1407 C ATOM 783 C TYR A 154 3.406 -13.902 -25.449 1.00 43.11 C ANISOU 783 C TYR A 154 5024 6194 5164 -475 -203 1415 C ATOM 784 O TYR A 154 3.778 -13.487 -24.347 1.00 43.42 O ANISOU 784 O TYR A 154 5088 6294 5115 -474 -206 1458 O ATOM 785 CB TYR A 154 4.655 -13.335 -27.539 1.00 39.63 C ANISOU 785 CB TYR A 154 4589 5690 4779 -413 -260 1319 C ATOM 786 CG TYR A 154 5.992 -13.424 -28.243 1.00 39.09 C ANISOU 786 CG TYR A 154 4520 5603 4730 -369 -275 1327 C ATOM 787 CD1 TYR A 154 7.172 -13.118 -27.575 1.00 38.94 C ANISOU 787 CD1 TYR A 154 4479 5633 4684 -354 -303 1392 C ATOM 788 CD2 TYR A 154 6.073 -13.791 -29.581 1.00 39.27 C ANISOU 788 CD2 TYR A 154 4558 5573 4789 -345 -260 1271 C ATOM 789 CE1 TYR A 154 8.396 -13.189 -28.215 1.00 39.09 C ANISOU 789 CE1 TYR A 154 4459 5660 4733 -312 -304 1412 C ATOM 790 CE2 TYR A 154 7.292 -13.867 -30.229 1.00 39.52 C ANISOU 790 CE2 TYR A 154 4575 5610 4829 -293 -244 1279 C ATOM 791 CZ TYR A 154 8.450 -13.564 -29.542 1.00 39.47 C ANISOU 791 CZ TYR A 154 4515 5664 4817 -275 -260 1356 C ATOM 792 OH TYR A 154 9.665 -13.637 -30.184 1.00 40.31 O ANISOU 792 OH TYR A 154 4570 5800 4946 -222 -231 1377 O ATOM 793 N ALA A 155 2.129 -13.938 -25.822 1.00 43.17 N ANISOU 793 N ALA A 155 4989 6208 5205 -506 -171 1372 N ATOM 794 CA ALA A 155 1.055 -13.508 -24.931 1.00 44.83 C ANISOU 794 CA ALA A 155 5162 6510 5361 -522 -111 1375 C ATOM 795 C ALA A 155 1.066 -14.300 -23.629 1.00 45.41 C ANISOU 795 C ALA A 155 5256 6613 5385 -568 -61 1485 C ATOM 796 O ALA A 155 0.966 -13.727 -22.541 1.00 46.60 O ANISOU 796 O ALA A 155 5430 6855 5422 -556 -18 1499 O ATOM 797 CB ALA A 155 -0.294 -13.637 -25.623 1.00 35.51 C ANISOU 797 CB ALA A 155 3894 5342 4257 -552 -91 1334 C ATOM 798 N THR A 156 1.201 -15.617 -23.751 1.00 47.27 N ANISOU 798 N THR A 156 5505 6759 5696 -618 -70 1564 N ATOM 799 CA THR A 156 1.247 -16.497 -22.588 1.00 47.85 C ANISOU 799 CA THR A 156 5613 6838 5728 -670 -35 1696 C ATOM 800 C THR A 156 2.430 -16.174 -21.680 1.00 47.43 C ANISOU 800 C THR A 156 5632 6824 5566 -622 -76 1748 C ATOM 801 O THR A 156 2.265 -16.005 -20.469 1.00 48.45 O ANISOU 801 O THR A 156 5795 7046 5568 -644 -38 1807 O ATOM 802 CB THR A 156 1.321 -17.977 -23.004 1.00 51.92 C ANISOU 802 CB THR A 156 6158 7207 6364 -724 -59 1772 C ATOM 803 OG1 THR A 156 0.187 -18.303 -23.816 1.00 52.60 O ANISOU 803 OG1 THR A 156 6181 7261 6544 -800 -42 1729 O ATOM 804 CG2 THR A 156 1.332 -18.875 -21.776 1.00 52.67 C ANISOU 804 CG2 THR A 156 6304 7296 6412 -782 -32 1934 C ATOM 805 N ALA A 157 3.620 -16.083 -22.269 1.00 44.35 N ANISOU 805 N ALA A 157 5259 6376 5217 -561 -155 1728 N ATOM 806 CA ALA A 157 4.828 -15.792 -21.497 1.00 44.12 C ANISOU 806 CA ALA A 157 5269 6388 5105 -527 -222 1787 C ATOM 807 C ALA A 157 4.727 -14.459 -20.755 1.00 44.67 C ANISOU 807 C ALA A 157 5368 6577 5026 -530 -224 1727 C ATOM 808 O ALA A 157 4.962 -14.386 -19.540 1.00 45.37 O ANISOU 808 O ALA A 157 5518 6735 4985 -550 -246 1793 O ATOM 809 CB ALA A 157 6.053 -15.809 -22.404 1.00 23.51 C ANISOU 809 CB ALA A 157 2632 3718 2583 -461 -290 1769 C ATOM 810 N LEU A 158 4.370 -13.410 -21.492 1.00 40.24 N ANISOU 810 N LEU A 158 4783 6031 4476 -509 -208 1599 N ATOM 811 CA LEU A 158 4.227 -12.077 -20.914 1.00 41.31 C ANISOU 811 CA LEU A 158 4968 6241 4484 -498 -214 1520 C ATOM 812 C LEU A 158 3.174 -12.051 -19.807 1.00 43.44 C ANISOU 812 C LEU A 158 5271 6597 4636 -512 -115 1526 C ATOM 813 O LEU A 158 3.353 -11.382 -18.784 1.00 44.76 O ANISOU 813 O LEU A 158 5527 6832 4646 -510 -123 1505 O ATOM 814 CB LEU A 158 3.894 -11.046 -21.996 1.00 23.32 C ANISOU 814 CB LEU A 158 2665 3933 2262 -461 -221 1396 C ATOM 815 CG LEU A 158 4.996 -10.767 -23.021 1.00 22.65 C ANISOU 815 CG LEU A 158 2561 3791 2253 -454 -305 1387 C ATOM 816 CD1 LEU A 158 4.558 -9.694 -24.008 1.00 21.39 C ANISOU 816 CD1 LEU A 158 2400 3604 2125 -429 -313 1283 C ATOM 817 CD2 LEU A 158 6.286 -10.370 -22.327 1.00 23.73 C ANISOU 817 CD2 LEU A 158 2738 3959 2320 -479 -397 1435 C ATOM 818 N ASN A 159 2.081 -12.781 -20.013 1.00 30.92 N ANISOU 818 N ASN A 159 3615 5014 3119 -534 -21 1555 N ATOM 819 CA ASN A 159 1.054 -12.904 -18.982 1.00 32.69 C ANISOU 819 CA ASN A 159 3841 5342 3238 -557 99 1587 C ATOM 820 C ASN A 159 1.586 -13.591 -17.728 1.00 34.09 C ANISOU 820 C ASN A 159 4107 5560 3285 -608 92 1720 C ATOM 821 O ASN A 159 1.211 -13.238 -16.607 1.00 35.74 O ANISOU 821 O ASN A 159 4384 5879 3318 -610 164 1723 O ATOM 822 CB ASN A 159 -0.174 -13.649 -19.510 1.00 64.19 C ANISOU 822 CB ASN A 159 7707 9330 7350 -600 189 1615 C ATOM 823 CG ASN A 159 -1.101 -12.754 -20.303 1.00 65.55 C ANISOU 823 CG ASN A 159 7788 9527 7592 -540 222 1489 C ATOM 824 OD1 ASN A 159 -1.564 -13.122 -21.381 1.00 64.87 O ANISOU 824 OD1 ASN A 159 7611 9382 7652 -562 195 1474 O ATOM 825 ND2 ASN A 159 -1.377 -11.570 -19.772 1.00 67.87 N ANISOU 825 ND2 ASN A 159 8115 9897 7775 -459 271 1395 N ATOM 826 N VAL A 160 2.461 -14.574 -17.923 1.00 61.51 N ANISOU 826 N VAL A 160 7589 8943 6836 -637 6 1830 N ATOM 827 CA VAL A 160 3.075 -15.278 -16.801 1.00 61.73 C ANISOU 827 CA VAL A 160 7704 8996 6754 -676 -33 1980 C ATOM 828 C VAL A 160 3.982 -14.351 -15.993 1.00 62.16 C ANISOU 828 C VAL A 160 7857 9122 6639 -653 -125 1947 C ATOM 829 O VAL A 160 3.876 -14.279 -14.764 1.00 63.60 O ANISOU 829 O VAL A 160 8138 9400 6625 -684 -106 2004 O ATOM 830 CB VAL A 160 3.868 -16.515 -17.269 1.00 41.65 C ANISOU 830 CB VAL A 160 5147 6319 4359 -681 -119 2102 C ATOM 831 CG1 VAL A 160 4.757 -17.037 -16.149 1.00 42.10 C ANISOU 831 CG1 VAL A 160 5294 6398 4303 -696 -202 2260 C ATOM 832 CG2 VAL A 160 2.917 -17.597 -17.749 1.00 41.76 C ANISOU 832 CG2 VAL A 160 5111 6250 4508 -739 -40 2155 C ATOM 833 N VAL A 161 4.867 -13.637 -16.685 1.00 41.37 N ANISOU 833 N VAL A 161 5203 6445 4070 -611 -228 1859 N ATOM 834 CA VAL A 161 5.758 -12.693 -16.012 1.00 41.84 C ANISOU 834 CA VAL A 161 5350 6558 3989 -615 -341 1823 C ATOM 835 C VAL A 161 4.957 -11.620 -15.275 1.00 44.07 C ANISOU 835 C VAL A 161 5735 6927 4082 -610 -265 1702 C ATOM 836 O VAL A 161 5.261 -11.271 -14.126 1.00 45.42 O ANISOU 836 O VAL A 161 6036 7174 4049 -640 -313 1715 O ATOM 837 CB VAL A 161 6.722 -12.014 -17.001 1.00 28.73 C ANISOU 837 CB VAL A 161 3632 4837 2449 -592 -449 1753 C ATOM 838 CG1 VAL A 161 7.730 -11.158 -16.252 1.00 29.88 C ANISOU 838 CG1 VAL A 161 3864 5033 2454 -629 -584 1724 C ATOM 839 CG2 VAL A 161 7.434 -13.056 -17.843 1.00 28.67 C ANISOU 839 CG2 VAL A 161 3523 4756 2616 -570 -502 1860 C ATOM 840 N SER A 162 3.924 -11.111 -15.939 1.00 48.49 N ANISOU 840 N SER A 162 6243 7475 4705 -564 -150 1584 N ATOM 841 CA SER A 162 3.064 -10.095 -15.346 1.00 51.20 C ANISOU 841 CA SER A 162 6671 7887 4894 -521 -55 1454 C ATOM 842 C SER A 162 2.370 -10.624 -14.094 1.00 53.09 C ANISOU 842 C SER A 162 6966 8249 4958 -543 76 1526 C ATOM 843 O SER A 162 2.241 -9.910 -13.099 1.00 55.44 O ANISOU 843 O SER A 162 7397 8627 5042 -519 125 1447 O ATOM 844 CB SER A 162 2.029 -9.603 -16.358 1.00 71.79 C ANISOU 844 CB SER A 162 9181 10458 7638 -448 35 1335 C ATOM 845 OG SER A 162 1.265 -8.545 -15.810 1.00 74.83 O ANISOU 845 OG SER A 162 9646 10896 7887 -374 127 1202 O ATOM 846 N LEU A 163 1.926 -11.877 -14.148 1.00 43.51 N ANISOU 846 N LEU A 163 5665 7043 3826 -594 137 1676 N ATOM 847 CA LEU A 163 1.326 -12.525 -12.986 1.00 45.06 C ANISOU 847 CA LEU A 163 5908 7355 3858 -642 261 1787 C ATOM 848 C LEU A 163 2.333 -12.645 -11.849 1.00 45.55 C ANISOU 848 C LEU A 163 6136 7462 3709 -690 148 1879 C ATOM 849 O LEU A 163 1.977 -12.512 -10.677 1.00 47.87 O ANISOU 849 O LEU A 163 6549 7881 3759 -707 234 1897 O ATOM 850 CB LEU A 163 0.775 -13.904 -13.353 1.00 45.70 C ANISOU 850 CB LEU A 163 5865 7400 4097 -710 327 1942 C ATOM 851 CG LEU A 163 -0.666 -13.942 -13.864 1.00 46.72 C ANISOU 851 CG LEU A 163 5842 7574 4334 -703 500 1897 C ATOM 852 CD1 LEU A 163 -1.038 -15.351 -14.298 1.00 45.61 C ANISOU 852 CD1 LEU A 163 5601 7369 4358 -805 522 2057 C ATOM 853 CD2 LEU A 163 -1.617 -13.440 -12.790 1.00 49.59 C ANISOU 853 CD2 LEU A 163 6240 8116 4485 -676 687 1860 C ATOM 854 N SER A 164 3.591 -12.899 -12.200 1.00 40.04 N ANISOU 854 N SER A 164 5439 6674 3098 -708 -46 1940 N ATOM 855 CA SER A 164 4.657 -12.978 -11.209 1.00 42.40 C ANISOU 855 CA SER A 164 5874 7017 3218 -753 -197 2033 C ATOM 856 C SER A 164 4.830 -11.640 -10.501 1.00 42.99 C ANISOU 856 C SER A 164 6104 7162 3068 -740 -237 1872 C ATOM 857 O SER A 164 4.890 -11.577 -9.270 1.00 45.81 O ANISOU 857 O SER A 164 6625 7624 3156 -778 -245 1904 O ATOM 858 CB SER A 164 5.971 -13.402 -11.865 1.00 60.08 C ANISOU 858 CB SER A 164 8038 9155 5634 -754 -394 2119 C ATOM 859 OG SER A 164 5.837 -14.658 -12.507 1.00 58.81 O ANISOU 859 OG SER A 164 7765 8903 5675 -750 -359 2248 O ATOM 860 N VAL A 165 4.900 -10.570 -11.288 1.00 43.47 N ANISOU 860 N VAL A 165 6133 7153 3230 -692 -265 1699 N ATOM 861 CA VAL A 165 5.038 -9.226 -10.733 1.00 45.33 C ANISOU 861 CA VAL A 165 6533 7408 3283 -679 -314 1525 C ATOM 862 C VAL A 165 3.851 -8.856 -9.840 1.00 48.28 C ANISOU 862 C VAL A 165 7028 7887 3429 -630 -115 1430 C ATOM 863 O VAL A 165 4.030 -8.388 -8.711 1.00 50.14 O ANISOU 863 O VAL A 165 7467 8196 3388 -652 -148 1379 O ATOM 864 CB VAL A 165 5.189 -8.174 -11.847 1.00 43.21 C ANISOU 864 CB VAL A 165 6205 7021 3189 -634 -359 1370 C ATOM 865 CG1 VAL A 165 5.284 -6.779 -11.251 1.00 45.72 C ANISOU 865 CG1 VAL A 165 6720 7327 3322 -615 -392 1179 C ATOM 866 CG2 VAL A 165 6.411 -8.478 -12.699 1.00 40.52 C ANISOU 866 CG2 VAL A 165 5758 6603 3035 -686 -548 1455 C ATOM 867 N GLU A 166 2.642 -9.077 -10.350 1.00 53.79 N ANISOU 867 N GLU A 166 7595 8603 4239 -563 92 1408 N ATOM 868 CA GLU A 166 1.422 -8.757 -9.612 1.00 56.73 C ANISOU 868 CA GLU A 166 8031 9094 4427 -493 318 1320 C ATOM 869 C GLU A 166 1.321 -9.539 -8.307 1.00 57.66 C ANISOU 869 C GLU A 166 8248 9362 4297 -562 399 1466 C ATOM 870 O GLU A 166 0.879 -9.003 -7.290 1.00 60.30 O ANISOU 870 O GLU A 166 8733 9814 4364 -521 531 1381 O ATOM 871 CB GLU A 166 0.182 -9.011 -10.474 1.00121.40 C ANISOU 871 CB GLU A 166 16011 17287 12826 -417 506 1291 C ATOM 872 CG GLU A 166 0.049 -8.078 -11.667 1.00121.83 C ANISOU 872 CG GLU A 166 16021 17226 13042 -313 473 1109 C ATOM 873 CD GLU A 166 -0.196 -6.637 -11.261 1.00124.10 C ANISOU 873 CD GLU A 166 16199 17580 13372 -186 696 1010 C ATOM 874 OE1 GLU A 166 -0.737 -6.410 -10.158 1.00125.52 O ANISOU 874 OE1 GLU A 166 16342 17915 13436 -181 893 1071 O ATOM 875 OE2 GLU A 166 0.152 -5.730 -12.047 1.00124.54 O ANISOU 875 OE2 GLU A 166 16198 17541 13581 -90 675 885 O ATOM 876 N LEU A 167 1.729 -10.804 -8.338 1.00 74.31 N ANISOU 876 N LEU A 167 10287 11462 6488 -659 325 1688 N ATOM 877 CA LEU A 167 1.715 -11.634 -7.139 1.00 75.27 C ANISOU 877 CA LEU A 167 10517 11710 6375 -738 374 1862 C ATOM 878 C LEU A 167 2.744 -11.126 -6.132 1.00 76.23 C ANISOU 878 C LEU A 167 10882 11874 6210 -776 198 1836 C ATOM 879 O LEU A 167 2.478 -11.086 -4.926 1.00 78.46 O ANISOU 879 O LEU A 167 11343 12298 6172 -795 289 1845 O ATOM 880 CB LEU A 167 1.985 -13.100 -7.485 1.00 71.03 C ANISOU 880 CB LEU A 167 9859 11111 6016 -825 313 2111 C ATOM 881 CG LEU A 167 1.856 -14.092 -6.326 1.00 72.22 C ANISOU 881 CG LEU A 167 10075 11382 5984 -912 430 2323 C ATOM 882 CD1 LEU A 167 0.463 -14.029 -5.719 1.00 74.02 C ANISOU 882 CD1 LEU A 167 10211 11731 6183 -895 731 2291 C ATOM 883 CD2 LEU A 167 2.179 -15.508 -6.780 1.00 70.38 C ANISOU 883 CD2 LEU A 167 9766 11036 5940 -990 314 2567 C ATOM 884 N TYR A 168 3.915 -10.739 -6.633 1.00 69.22 N ANISOU 884 N TYR A 168 9999 10872 5430 -795 -53 1805 N ATOM 885 CA TYR A 168 4.950 -10.157 -5.783 1.00 70.10 C ANISOU 885 CA TYR A 168 10321 11014 5298 -852 -265 1776 C ATOM 886 C TYR A 168 4.426 -8.921 -5.064 1.00 72.97 C ANISOU 886 C TYR A 168 10896 11432 5397 -799 -174 1534 C ATOM 887 O TYR A 168 4.577 -8.789 -3.850 1.00 74.97 O ANISOU 887 O TYR A 168 11380 11794 5310 -841 -200 1525 O ATOM 888 CB TYR A 168 6.195 -9.790 -6.594 1.00 54.18 C ANISOU 888 CB TYR A 168 8224 8871 3490 -884 -531 1772 C ATOM 889 CG TYR A 168 7.252 -9.063 -5.787 1.00 56.46 C ANISOU 889 CG TYR A 168 8708 9186 3559 -962 -776 1723 C ATOM 890 CD1 TYR A 168 8.187 -9.766 -5.039 1.00 58.97 C ANISOU 890 CD1 TYR A 168 9073 9566 3766 -1051 -980 1921 C ATOM 891 CD2 TYR A 168 7.314 -7.673 -5.773 1.00 56.45 C ANISOU 891 CD2 TYR A 168 8848 9136 3464 -953 -823 1485 C ATOM 892 CE1 TYR A 168 9.153 -9.109 -4.300 1.00 61.44 C ANISOU 892 CE1 TYR A 168 9554 9913 3877 -1141 -1230 1883 C ATOM 893 CE2 TYR A 168 8.276 -7.007 -5.037 1.00 58.95 C ANISOU 893 CE2 TYR A 168 9353 9465 3579 -1051 -1067 1436 C ATOM 894 CZ TYR A 168 9.193 -7.730 -4.303 1.00 61.46 C ANISOU 894 CZ TYR A 168 9700 9867 3786 -1151 -1275 1636 C ATOM 895 OH TYR A 168 10.154 -7.072 -3.569 1.00 64.40 O ANISOU 895 OH TYR A 168 10250 10261 3956 -1266 -1546 1594 O ATOM 896 N LEU A 169 3.813 -8.017 -5.822 1.00 57.43 N ANISOU 896 N LEU A 169 8862 9380 3579 -699 -73 1336 N ATOM 897 CA LEU A 169 3.244 -6.803 -5.246 1.00 59.84 C ANISOU 897 CA LEU A 169 9365 9699 3670 -614 25 1087 C ATOM 898 C LEU A 169 2.094 -7.129 -4.299 1.00 62.45 C ANISOU 898 C LEU A 169 9776 10205 3744 -553 311 1080 C ATOM 899 O LEU A 169 1.809 -6.372 -3.370 1.00 65.16 O ANISOU 899 O LEU A 169 10372 10618 3767 -517 363 930 O ATOM 900 CB LEU A 169 2.770 -5.852 -6.347 1.00 54.59 C ANISOU 900 CB LEU A 169 8590 8894 3256 -501 78 907 C ATOM 901 CG LEU A 169 3.860 -5.167 -7.174 1.00 52.55 C ANISOU 901 CG LEU A 169 8326 8466 3176 -557 -187 853 C ATOM 902 CD1 LEU A 169 3.242 -4.293 -8.256 1.00 51.87 C ANISOU 902 CD1 LEU A 169 8150 8246 3312 -441 -113 692 C ATOM 903 CD2 LEU A 169 4.775 -4.348 -6.277 1.00 55.50 C ANISOU 903 CD2 LEU A 169 8981 8821 3285 -641 -394 752 C ATOM 904 N ALA A 170 1.441 -8.262 -4.535 1.00 73.75 N ANISOU 904 N ALA A 170 10997 11711 5311 -549 498 1242 N ATOM 905 CA ALA A 170 0.325 -8.692 -3.702 1.00 76.06 C ANISOU 905 CA ALA A 170 11316 12193 5391 -506 795 1268 C ATOM 906 C ALA A 170 0.796 -9.203 -2.344 1.00 77.23 C ANISOU 906 C ALA A 170 11691 12484 5168 -611 759 1399 C ATOM 907 O ALA A 170 0.126 -8.996 -1.333 1.00 80.15 O ANISOU 907 O ALA A 170 12241 13005 5208 -563 945 1311 O ATOM 908 CB ALA A 170 -0.491 -9.759 -4.416 1.00 68.43 C ANISOU 908 CB ALA A 170 10053 11261 4685 -516 973 1433 C ATOM 909 N ILE A 171 1.947 -9.868 -2.318 1.00 74.27 N ANISOU 909 N ILE A 171 11313 12067 4839 -744 522 1611 N ATOM 910 CA ILE A 171 2.445 -10.456 -1.075 1.00 75.42 C ANISOU 910 CA ILE A 171 11666 12345 4643 -850 459 1775 C ATOM 911 C ILE A 171 3.437 -9.565 -0.323 1.00 76.87 C ANISOU 911 C ILE A 171 12152 12533 4523 -887 226 1644 C ATOM 912 O ILE A 171 3.673 -9.761 0.870 1.00 80.16 O ANISOU 912 O ILE A 171 12821 13100 4536 -913 286 1632 O ATOM 913 CB ILE A 171 3.084 -11.843 -1.309 1.00112.76 C ANISOU 913 CB ILE A 171 16266 17038 9539 -966 321 2096 C ATOM 914 CG1 ILE A 171 4.451 -11.704 -1.981 1.00113.69 C ANISOU 914 CG1 ILE A 171 16601 17306 9290 -1070 281 2294 C ATOM 915 CG2 ILE A 171 2.161 -12.729 -2.132 1.00110.47 C ANISOU 915 CG2 ILE A 171 15878 16571 9526 -991 5 2118 C ATOM 916 CD1 ILE A 171 5.181 -13.018 -2.146 1.00111.76 C ANISOU 916 CD1 ILE A 171 16251 17014 9200 -1166 166 2620 C ATOM 917 N CYS A 172 4.016 -8.589 -1.017 1.00 81.65 N ANISOU 917 N CYS A 172 12735 12977 5311 -900 -39 1547 N ATOM 918 CA CYS A 172 5.001 -7.703 -0.400 1.00 82.70 C ANISOU 918 CA CYS A 172 13131 13095 5197 -968 -305 1433 C ATOM 919 C CYS A 172 4.411 -6.360 0.019 1.00 85.50 C ANISOU 919 C CYS A 172 13728 13444 5315 -878 -195 1110 C ATOM 920 O CYS A 172 4.673 -5.878 1.122 1.00 87.77 O ANISOU 920 O CYS A 172 14325 13810 5212 -922 -270 1020 O ATOM 921 CB CYS A 172 6.201 -7.487 -1.324 1.00 82.39 C ANISOU 921 CB CYS A 172 12957 12895 5451 -1034 -625 1465 C ATOM 922 SG CYS A 172 7.438 -8.797 -1.245 1.00 79.44 S ANISOU 922 SG CYS A 172 12355 12519 5307 -1121 -802 1830 S ATOM 923 N HIS A 173 3.617 -5.756 -0.859 1.00121.54 N ANISOU 923 N HIS A 173 18160 17905 10114 -744 -28 934 N ATOM 924 CA HIS A 173 2.981 -4.480 -0.550 1.00124.17 C ANISOU 924 CA HIS A 173 18703 18189 10287 -621 83 617 C ATOM 925 C HIS A 173 1.472 -4.545 -0.759 1.00125.71 C ANISOU 925 C HIS A 173 18766 18461 10537 -440 476 542 C ATOM 926 O HIS A 173 0.947 -3.885 -1.653 1.00125.18 O ANISOU 926 O HIS A 173 18520 18273 10769 -327 554 439 O ATOM 927 CB HIS A 173 3.566 -3.368 -1.421 1.00 94.22 C ANISOU 927 CB HIS A 173 14896 14165 6737 -622 -137 455 C ATOM 928 CG HIS A 173 5.061 -3.291 -1.384 1.00 92.65 C ANISOU 928 CG HIS A 173 14758 13901 6545 -809 -524 547 C ATOM 929 ND1 HIS A 173 5.744 -2.496 -0.490 1.00 93.60 N ANISOU 929 ND1 HIS A 173 15187 13961 6416 -893 -750 381 N ATOM 930 CD2 HIS A 173 6.003 -3.908 -2.136 1.00 90.36 C ANISOU 930 CD2 HIS A 173 14250 13599 6485 -926 -727 788 C ATOM 931 CE1 HIS A 173 7.044 -2.627 -0.692 1.00 91.96 C ANISOU 931 CE1 HIS A 173 14923 13725 6294 -1065 -1082 529 C ATOM 932 NE2 HIS A 173 7.227 -3.478 -1.685 1.00 90.04 N ANISOU 932 NE2 HIS A 173 14357 13513 6342 -1074 -1065 777 N ATOM 933 N PRO A 174 0.768 -5.328 0.074 1.00122.46 N ANISOU 933 N PRO A 174 18430 18263 9834 -418 723 610 N ATOM 934 CA PRO A 174 -0.677 -5.507 -0.102 1.00123.76 C ANISOU 934 CA PRO A 174 18415 18558 10048 -274 1114 604 C ATOM 935 C PRO A 174 -1.453 -4.232 0.213 1.00125.13 C ANISOU 935 C PRO A 174 18598 18643 10300 -55 1282 304 C ATOM 936 O PRO A 174 -2.529 -4.016 -0.342 1.00125.61 O ANISOU 936 O PRO A 174 18391 18740 10594 67 1520 312 O ATOM 937 CB PRO A 174 -1.016 -6.598 0.917 1.00117.46 C ANISOU 937 CB PRO A 174 17826 18006 8798 -303 1304 670 C ATOM 938 CG PRO A 174 0.001 -6.431 1.986 1.00116.56 C ANISOU 938 CG PRO A 174 17920 17892 8478 -495 984 811 C ATOM 939 CD PRO A 174 1.263 -6.002 1.288 1.00115.05 C ANISOU 939 CD PRO A 174 17781 17469 8466 -536 632 686 C ATOM 940 N PHE A 175 -0.906 -3.401 1.094 1.00154.14 N ANISOU 940 N PHE A 175 22582 22200 13783 -4 1156 46 N ATOM 941 CA PHE A 175 -1.539 -2.137 1.452 1.00154.75 C ANISOU 941 CA PHE A 175 22691 22154 13951 219 1293 -239 C ATOM 942 C PHE A 175 -1.363 -1.103 0.343 1.00152.64 C ANISOU 942 C PHE A 175 22289 21623 14086 224 1070 -295 C ATOM 943 O PHE A 175 -2.198 -0.215 0.171 1.00153.03 O ANISOU 943 O PHE A 175 22323 21546 14275 412 1167 -494 O ATOM 944 CB PHE A 175 -0.995 -1.610 2.785 1.00210.16 C ANISOU 944 CB PHE A 175 30130 29176 20544 319 1354 -523 C ATOM 945 CG PHE A 175 0.507 -1.570 2.861 1.00213.79 C ANISOU 945 CG PHE A 175 30683 29920 20627 383 1683 -500 C ATOM 946 CD1 PHE A 175 1.226 -2.696 3.232 1.00213.12 C ANISOU 946 CD1 PHE A 175 30265 30038 20673 433 1990 -310 C ATOM 947 CD2 PHE A 175 1.198 -0.405 2.575 1.00217.99 C ANISOU 947 CD2 PHE A 175 31634 30521 20670 385 1691 -668 C ATOM 948 CE1 PHE A 175 2.606 -2.662 3.305 1.00216.52 C ANISOU 948 CE1 PHE A 175 30760 30747 20762 478 2313 -267 C ATOM 949 CE2 PHE A 175 2.579 -0.366 2.649 1.00221.45 C ANISOU 949 CE2 PHE A 175 32159 31240 20741 445 2018 -639 C ATOM 950 CZ PHE A 175 3.283 -1.496 3.014 1.00220.70 C ANISOU 950 CZ PHE A 175 31709 31356 20790 491 2338 -430 C ATOM 951 N LYS A 176 -0.273 -1.228 -0.408 1.00145.05 N ANISOU 951 N LYS A 176 21218 20585 13310 27 782 -106 N ATOM 952 CA LYS A 176 -0.043 -0.382 -1.572 1.00142.71 C ANISOU 952 CA LYS A 176 20694 20099 13433 22 636 -78 C ATOM 953 C LYS A 176 -0.700 -1.007 -2.798 1.00141.85 C ANISOU 953 C LYS A 176 20218 20088 13591 93 865 76 C ATOM 954 O LYS A 176 -0.882 -0.349 -3.822 1.00140.25 O ANISOU 954 O LYS A 176 19799 19764 13725 146 840 79 O ATOM 955 CB LYS A 176 1.457 -0.204 -1.822 1.00104.78 C ATOM 956 CG LYS A 176 2.209 0.508 -0.708 1.00104.78 C ATOM 957 CD LYS A 176 1.912 2.000 -0.683 1.00104.78 C ATOM 958 CE LYS A 176 2.765 2.710 0.361 1.00104.78 C ATOM 959 NZ LYS A 176 2.584 4.188 0.326 1.00104.78 N ATOM 960 N ALA A 177 -1.052 -2.285 -2.686 1.00139.51 N ANISOU 960 N ALA A 177 19863 20015 13131 79 1080 214 N ATOM 961 CA ALA A 177 -1.671 -3.014 -3.789 1.00139.12 C ANISOU 961 CA ALA A 177 19489 20082 13290 146 1333 338 C ATOM 962 C ALA A 177 -3.187 -2.858 -3.792 1.00141.76 C ANISOU 962 C ALA A 177 19837 20529 13497 369 1663 157 C ATOM 963 O ALA A 177 -3.814 -2.883 -4.849 1.00141.97 O ANISOU 963 O ALA A 177 19579 20655 13710 455 1886 221 O ATOM 964 CB ALA A 177 -1.292 -4.485 -3.738 1.00101.24 C ANISOU 964 CB ALA A 177 14587 15450 8429 -17 1376 623 C ATOM 965 N LYS A 178 -3.775 -2.710 -2.609 1.00177.61 N ANISOU 965 N LYS A 178 24707 25059 17716 464 1694 -69 N ATOM 966 CA LYS A 178 -5.210 -2.470 -2.510 1.00180.01 C ANISOU 966 CA LYS A 178 25048 25416 17931 727 1986 -295 C ATOM 967 C LYS A 178 -5.543 -1.085 -3.052 1.00179.11 C ANISOU 967 C LYS A 178 24862 25057 18133 870 1880 -456 C ATOM 968 O LYS A 178 -6.624 -0.866 -3.596 1.00180.31 O ANISOU 968 O LYS A 178 24880 25227 18404 1101 2102 -574 O ATOM 969 CB LYS A 178 -5.709 -2.652 -1.075 1.00145.80 C ATOM 970 CG LYS A 178 -5.757 -4.109 -0.640 1.00145.80 C ATOM 971 CD LYS A 178 -6.489 -4.285 0.678 1.00145.80 C ATOM 972 CE LYS A 178 -6.607 -5.758 1.039 1.00145.80 C ATOM 973 NZ LYS A 178 -7.365 -5.962 2.303 1.00145.80 N ATOM 974 N THR A 179 -4.607 -0.154 -2.902 1.00201.25 N ANISOU 974 N THR A 179 27754 27639 21070 731 1538 -450 N ATOM 975 CA THR A 179 -4.633 1.069 -3.691 1.00200.08 C ANISOU 975 CA THR A 179 27528 27251 21242 817 1400 -548 C ATOM 976 C THR A 179 -4.214 0.635 -5.088 1.00199.23 C ANISOU 976 C THR A 179 27006 27228 21464 876 1547 -395 C ATOM 977 O THR A 179 -3.055 0.773 -5.477 1.00200.38 O ANISOU 977 O THR A 179 27031 27329 21774 1089 1681 -507 O ATOM 978 CB THR A 179 -3.656 2.124 -3.147 1.00163.15 C ANISOU 978 CB THR A 179 22929 22375 16685 606 1025 -485 C ATOM 979 OG1 THR A 179 -2.324 1.596 -3.152 1.00165.19 O ANISOU 979 OG1 THR A 179 23573 22542 16649 540 860 -641 O ATOM 980 CG2 THR A 179 -4.034 2.520 -1.724 1.00161.03 C ANISOU 980 CG2 THR A 179 22535 21886 16763 679 911 -536 C ATOM 981 N LEU A 180 -5.178 0.109 -5.836 1.00170.46 N ANISOU 981 N LEU A 180 23157 23702 17911 687 1512 -138 N ATOM 982 CA LEU A 180 -4.903 -0.749 -6.984 1.00169.97 C ANISOU 982 CA LEU A 180 22716 23755 18110 702 1664 27 C ATOM 983 C LEU A 180 -4.800 -0.038 -8.330 1.00169.47 C ANISOU 983 C LEU A 180 22481 23538 18373 839 1617 -51 C ATOM 984 O LEU A 180 -5.419 1.004 -8.556 1.00171.36 O ANISOU 984 O LEU A 180 22523 23869 18717 1015 1833 -90 O ATOM 985 CB LEU A 180 -5.974 -1.846 -7.058 1.00132.60 C ANISOU 985 CB LEU A 180 17891 19282 13208 813 2019 37 C ATOM 986 CG LEU A 180 -5.884 -2.960 -8.103 1.00132.24 C ANISOU 986 CG LEU A 180 17484 19429 13333 742 2193 268 C ATOM 987 CD1 LEU A 180 -4.566 -3.710 -7.994 1.00133.48 C ANISOU 987 CD1 LEU A 180 17369 19664 13683 959 2420 196 C ATOM 988 CD2 LEU A 180 -7.059 -3.913 -7.954 1.00134.57 C ANISOU 988 CD2 LEU A 180 17848 19958 13326 633 2372 401 C ATOM 989 N MET A 181 -3.988 -0.618 -9.209 1.00177.44 N ANISOU 989 N MET A 181 23578 24322 19521 763 1336 -78 N ATOM 990 CA MET A 181 -4.021 -0.306 -10.624 1.00176.10 C ANISOU 990 CA MET A 181 23312 23970 19629 875 1242 -153 C ATOM 991 C MET A 181 -5.415 -0.692 -11.090 1.00176.37 C ANISOU 991 C MET A 181 23017 24123 19874 1014 1441 -101 C ATOM 992 O MET A 181 -5.742 -1.877 -11.138 1.00175.52 O ANISOU 992 O MET A 181 22668 24169 19854 902 1513 86 O ATOM 993 CB MET A 181 -2.989 -1.153 -11.368 1.00140.74 C ANISOU 993 CB MET A 181 18789 19339 15345 691 962 -37 C ATOM 994 CG MET A 181 -1.570 -1.048 -10.829 1.00140.33 C ANISOU 994 CG MET A 181 18990 19204 15126 515 743 -34 C ATOM 995 SD MET A 181 -0.519 -2.410 -11.379 1.00140.19 S ANISOU 995 SD MET A 181 18931 19390 14946 318 766 179 S ATOM 996 CE MET A 181 1.067 -1.902 -10.715 1.00137.03 C ANISOU 996 CE MET A 181 18187 18993 14885 220 719 399 C ATOM 997 N SER A 182 -6.232 0.306 -11.419 1.00130.99 N ANISOU 997 N SER A 182 17257 18292 14221 1250 1508 -257 N ATOM 998 CA SER A 182 -7.648 0.097 -11.738 1.00132.35 C ANISOU 998 CA SER A 182 17115 18608 14564 1419 1719 -227 C ATOM 999 C SER A 182 -7.905 -0.978 -12.795 1.00130.15 C ANISOU 999 C SER A 182 16523 18378 14552 1262 1632 -13 C ATOM 1000 O SER A 182 -7.023 -1.311 -13.589 1.00127.99 O ANISOU 1000 O SER A 182 16286 17952 14392 1110 1392 53 O ATOM 1001 CB SER A 182 -8.299 1.416 -12.169 1.00142.02 C ANISOU 1001 CB SER A 182 18378 19678 15906 1696 1727 -411 C ATOM 1002 OG SER A 182 -7.700 1.927 -13.348 1.00146.38 O ANISOU 1002 OG SER A 182 19226 20187 16207 1869 1843 -629 O ATOM 1003 N ARG A 183 -9.123 -1.516 -12.786 1.00 88.26 N ANISOU 1003 N ARG A 183 10909 13287 9338 1292 1832 93 N ATOM 1004 CA ARG A 183 -9.534 -2.543 -13.740 1.00 86.29 C ANISOU 1004 CA ARG A 183 10374 13092 9320 1121 1756 294 C ATOM 1005 C ARG A 183 -9.350 -2.087 -15.183 1.00 85.74 C ANISOU 1005 C ARG A 183 10250 12826 9500 1146 1527 279 C ATOM 1006 O ARG A 183 -8.963 -2.875 -16.047 1.00 83.66 O ANISOU 1006 O ARG A 183 9891 12515 9381 967 1369 410 O ATOM 1007 CB ARG A 183 -10.994 -2.945 -13.509 1.00117.86 C ANISOU 1007 CB ARG A 183 14036 17344 13402 1170 2003 389 C ATOM 1008 CG ARG A 183 -11.195 -4.045 -12.480 1.00117.96 C ANISOU 1008 CG ARG A 183 14075 17574 13171 1087 2232 462 C ATOM 1009 CD ARG A 183 -12.659 -4.459 -12.411 1.00119.40 C ANISOU 1009 CD ARG A 183 13917 18023 13427 1165 2511 539 C ATOM 1010 NE ARG A 183 -12.846 -5.718 -11.692 1.00119.09 N ANISOU 1010 NE ARG A 183 13779 18168 13304 934 2629 745 N ATOM 1011 CZ ARG A 183 -14.015 -6.339 -11.564 1.00119.80 C ANISOU 1011 CZ ARG A 183 13525 18478 13516 879 2810 895 C ATOM 1012 NH1 ARG A 183 -15.108 -5.820 -12.107 1.00120.76 N ANISOU 1012 NH1 ARG A 183 13347 18682 13855 1051 2888 859 N ATOM 1013 NH2 ARG A 183 -14.091 -7.481 -10.893 1.00119.67 N ANISOU 1013 NH2 ARG A 183 13458 18598 13412 646 2901 1092 N ATOM 1014 N SER A 184 -9.632 -0.813 -15.436 1.00128.26 N ANISOU 1014 N SER A 184 15720 18090 14925 1373 1512 118 N ATOM 1015 CA SER A 184 -9.480 -0.242 -16.770 1.00127.79 C ANISOU 1015 CA SER A 184 15661 17827 15067 1405 1288 102 C ATOM 1016 C SER A 184 -8.021 -0.276 -17.216 1.00126.32 C ANISOU 1016 C SER A 184 15719 17453 14826 1212 1050 118 C ATOM 1017 O SER A 184 -7.714 -0.674 -18.341 1.00124.73 O ANISOU 1017 O SER A 184 15439 17174 14780 1087 877 215 O ATOM 1018 CB SER A 184 -10.012 1.192 -16.803 1.00102.60 C ANISOU 1018 CB SER A 184 12557 14519 11906 1698 1322 -73 C ATOM 1019 OG SER A 184 -9.299 2.023 -15.904 1.00103.98 O ANISOU 1019 OG SER A 184 13079 14581 11848 1759 1341 -238 O ATOM 1020 N ARG A 185 -7.125 0.139 -16.325 1.00 97.41 N ANISOU 1020 N ARG A 185 12345 13729 10935 1183 1043 23 N ATOM 1021 CA ARG A 185 -5.696 0.132 -16.617 1.00 95.90 C ANISOU 1021 CA ARG A 185 12362 13386 10690 994 821 46 C ATOM 1022 C ARG A 185 -5.172 -1.292 -16.781 1.00 93.09 C ANISOU 1022 C ARG A 185 11884 13123 10361 759 768 232 C ATOM 1023 O ARG A 185 -4.243 -1.537 -17.552 1.00 91.24 O ANISOU 1023 O ARG A 185 11666 12781 10219 623 581 303 O ATOM 1024 CB ARG A 185 -4.919 0.863 -15.519 1.00126.19 C ANISOU 1024 CB ARG A 185 16523 17160 14264 1000 817 -91 C ATOM 1025 CG ARG A 185 -5.224 2.351 -15.426 1.00127.32 C ANISOU 1025 CG ARG A 185 16912 17046 14415 1072 655 -238 C ATOM 1026 CD ARG A 185 -4.511 2.993 -14.247 1.00126.81 C ANISOU 1026 CD ARG A 185 17166 16897 14118 950 543 -318 C ATOM 1027 NE ARG A 185 -4.857 4.404 -14.101 1.00128.56 N ANISOU 1027 NE ARG A 185 17593 17151 14102 1100 698 -496 N ATOM 1028 CZ ARG A 185 -4.449 5.174 -13.097 1.00128.34 C ANISOU 1028 CZ ARG A 185 17871 17063 13828 1019 618 -599 C ATOM 1029 NH1 ARG A 185 -3.677 4.668 -12.145 1.00130.00 N ANISOU 1029 NH1 ARG A 185 18280 17308 13805 1173 778 -776 N ATOM 1030 NH2 ARG A 185 -4.812 6.449 -13.044 1.00126.38 N ANISOU 1030 NH2 ARG A 185 17728 16728 13563 786 379 -526 N ATOM 1031 N THR A 186 -5.775 -2.226 -16.052 1.00 64.20 N ANISOU 1031 N THR A 186 8107 9663 6623 718 940 315 N ATOM 1032 CA THR A 186 -5.408 -3.634 -16.157 1.00 61.37 C ANISOU 1032 CA THR A 186 7646 9378 6295 509 900 495 C ATOM 1033 C THR A 186 -5.798 -4.186 -17.523 1.00 60.08 C ANISOU 1033 C THR A 186 7249 9187 6392 459 822 594 C ATOM 1034 O THR A 186 -5.008 -4.874 -18.169 1.00 57.66 O ANISOU 1034 O THR A 186 6944 8806 6158 311 675 685 O ATOM 1035 CB THR A 186 -6.072 -4.479 -15.053 1.00 54.37 C ANISOU 1035 CB THR A 186 6688 8703 5267 471 1110 578 C ATOM 1036 OG1 THR A 186 -5.604 -4.045 -13.769 1.00 55.42 O ANISOU 1036 OG1 THR A 186 7074 8863 5120 496 1161 491 O ATOM 1037 CG2 THR A 186 -5.739 -5.952 -15.235 1.00 51.32 C ANISOU 1037 CG2 THR A 186 6205 8356 4941 260 1054 775 C ATOM 1038 N LYS A 187 -7.017 -3.879 -17.957 1.00 75.24 N ANISOU 1038 N LYS A 187 8971 11171 8445 589 918 571 N ATOM 1039 CA LYS A 187 -7.487 -4.286 -19.277 1.00 74.02 C ANISOU 1039 CA LYS A 187 8605 10994 8526 549 826 650 C ATOM 1040 C LYS A 187 -6.620 -3.664 -20.367 1.00 73.32 C ANISOU 1040 C LYS A 187 8635 10705 8516 539 607 610 C ATOM 1041 O LYS A 187 -6.293 -4.312 -21.366 1.00 70.99 O ANISOU 1041 O LYS A 187 8272 10361 8338 418 483 694 O ATOM 1042 CB LYS A 187 -8.952 -3.889 -19.476 1.00 86.11 C ANISOU 1042 CB LYS A 187 9900 12638 10180 713 951 626 C ATOM 1043 CG LYS A 187 -9.927 -4.612 -18.558 1.00 88.60 C ANISOU 1043 CG LYS A 187 10011 13182 10471 676 1167 716 C ATOM 1044 CD LYS A 187 -11.366 -4.209 -18.847 1.00 91.05 C ANISOU 1044 CD LYS A 187 10041 13621 10932 840 1282 704 C ATOM 1045 CE LYS A 187 -11.580 -2.717 -18.641 1.00 92.93 C ANISOU 1045 CE LYS A 187 10382 13826 11100 1120 1372 531 C ATOM 1046 NZ LYS A 187 -12.990 -2.312 -18.902 1.00 95.82 N ANISOU 1046 NZ LYS A 187 10451 14331 11625 1315 1495 525 N ATOM 1047 N LYS A 188 -6.250 -2.403 -20.163 1.00 56.94 N ANISOU 1047 N LYS A 188 6752 8512 6371 664 566 480 N ATOM 1048 CA LYS A 188 -5.356 -1.703 -21.077 1.00 56.37 C ANISOU 1048 CA LYS A 188 6819 8247 6352 639 367 452 C ATOM 1049 C LYS A 188 -4.006 -2.406 -21.150 1.00 53.46 C ANISOU 1049 C LYS A 188 6548 7835 5929 436 253 530 C ATOM 1050 O LYS A 188 -3.394 -2.484 -22.216 1.00 50.69 O ANISOU 1050 O LYS A 188 6194 7394 5672 355 113 580 O ATOM 1051 CB LYS A 188 -5.164 -0.250 -20.635 1.00 39.97 C ANISOU 1051 CB LYS A 188 4963 6034 4189 785 347 300 C ATOM 1052 CG LYS A 188 -6.348 0.661 -20.926 1.00 41.98 C ANISOU 1052 CG LYS A 188 5137 6268 4546 1021 409 220 C ATOM 1053 CD LYS A 188 -6.105 2.064 -20.390 1.00 44.06 C ANISOU 1053 CD LYS A 188 5666 6354 4720 1165 379 60 C ATOM 1054 CE LYS A 188 -7.202 3.028 -20.822 1.00 45.32 C ANISOU 1054 CE LYS A 188 5754 6456 5012 1423 413 -11 C ATOM 1055 NZ LYS A 188 -8.553 2.577 -20.390 1.00 46.34 N ANISOU 1055 NZ LYS A 188 5642 6801 5165 1577 638 -16 N ATOM 1056 N PHE A 189 -3.547 -2.918 -20.012 1.00 54.82 N ANISOU 1056 N PHE A 189 6803 8082 5945 364 318 547 N ATOM 1057 CA PHE A 189 -2.271 -3.621 -19.955 1.00 51.58 C ANISOU 1057 CA PHE A 189 6468 7644 5485 193 212 632 C ATOM 1058 C PHE A 189 -2.352 -4.979 -20.646 1.00 48.30 C ANISOU 1058 C PHE A 189 5877 7280 5194 82 204 768 C ATOM 1059 O PHE A 189 -1.394 -5.412 -21.287 1.00 44.34 O ANISOU 1059 O PHE A 189 5391 6709 4746 -17 86 828 O ATOM 1060 CB PHE A 189 -1.804 -3.787 -18.508 1.00 81.09 C ANISOU 1060 CB PHE A 189 10349 11451 9011 151 265 623 C ATOM 1061 CG PHE A 189 -0.423 -4.357 -18.381 1.00 77.22 C ANISOU 1061 CG PHE A 189 9933 10932 8475 -5 133 713 C ATOM 1062 CD1 PHE A 189 0.672 -3.655 -18.853 1.00 75.82 C ANISOU 1062 CD1 PHE A 189 9865 10629 8316 -56 -35 685 C ATOM 1063 CD2 PHE A 189 -0.215 -5.589 -17.784 1.00 74.89 C ANISOU 1063 CD2 PHE A 189 9590 10737 8129 -99 174 838 C ATOM 1064 CE1 PHE A 189 1.947 -4.169 -18.738 1.00 72.24 C ANISOU 1064 CE1 PHE A 189 9442 10169 7837 -188 -153 777 C ATOM 1065 CE2 PHE A 189 1.060 -6.109 -17.667 1.00 71.63 C ANISOU 1065 CE2 PHE A 189 9229 10297 7691 -217 46 928 C ATOM 1066 CZ PHE A 189 2.142 -5.398 -18.145 1.00 70.34 C ANISOU 1066 CZ PHE A 189 9146 10029 7553 -255 -114 896 C ATOM 1067 N ILE A 190 -3.496 -5.644 -20.514 1.00 52.32 N ANISOU 1067 N ILE A 190 6221 7908 5750 98 335 815 N ATOM 1068 CA ILE A 190 -3.734 -6.908 -21.202 1.00 49.57 C ANISOU 1068 CA ILE A 190 5718 7587 5530 -11 323 933 C ATOM 1069 C ILE A 190 -3.699 -6.686 -22.708 1.00 48.18 C ANISOU 1069 C ILE A 190 5483 7315 5510 -7 198 920 C ATOM 1070 O ILE A 190 -3.051 -7.434 -23.449 1.00 44.49 O ANISOU 1070 O ILE A 190 5010 6789 5106 -107 110 981 O ATOM 1071 CB ILE A 190 -5.097 -7.515 -20.819 1.00 67.07 C ANISOU 1071 CB ILE A 190 7750 9949 7782 -6 480 985 C ATOM 1072 CG1 ILE A 190 -5.145 -7.825 -19.323 1.00 67.62 C ANISOU 1072 CG1 ILE A 190 7887 10133 7672 -23 622 1015 C ATOM 1073 CG2 ILE A 190 -5.364 -8.778 -21.623 1.00 64.31 C ANISOU 1073 CG2 ILE A 190 7260 9597 7578 -140 439 1097 C ATOM 1074 CD1 ILE A 190 -4.140 -8.857 -18.882 1.00 64.47 C ANISOU 1074 CD1 ILE A 190 7584 9708 7203 -168 567 1127 C ATOM 1075 N SER A 191 -4.399 -5.645 -23.150 1.00 42.82 N ANISOU 1075 N SER A 191 4770 6617 4882 122 193 839 N ATOM 1076 CA SER A 191 -4.413 -5.269 -24.559 1.00 40.89 C ANISOU 1076 CA SER A 191 4490 6287 4761 137 66 831 C ATOM 1077 C SER A 191 -2.999 -4.968 -25.047 1.00 37.80 C ANISOU 1077 C SER A 191 4261 5769 4332 75 -63 827 C ATOM 1078 O SER A 191 -2.602 -5.392 -26.134 1.00 34.28 O ANISOU 1078 O SER A 191 3795 5274 3955 7 -153 868 O ATOM 1079 CB SER A 191 -5.320 -4.058 -24.777 1.00 53.22 C ANISOU 1079 CB SER A 191 6012 7838 6371 310 75 752 C ATOM 1080 OG SER A 191 -6.636 -4.320 -24.320 1.00 54.99 O ANISOU 1080 OG SER A 191 6043 8205 6645 376 206 765 O ATOM 1081 N ALA A 192 -2.243 -4.243 -24.228 1.00 38.25 N ANISOU 1081 N ALA A 192 4478 5781 4273 92 -68 778 N ATOM 1082 CA ALA A 192 -0.857 -3.916 -24.544 1.00 34.69 C ANISOU 1082 CA ALA A 192 4160 5230 3788 15 -186 787 C ATOM 1083 C ALA A 192 -0.019 -5.180 -24.717 1.00 30.93 C ANISOU 1083 C ALA A 192 3646 4782 3321 -113 -205 883 C ATOM 1084 O ALA A 192 0.809 -5.266 -25.625 1.00 27.70 O ANISOU 1084 O ALA A 192 3255 4316 2953 -172 -289 917 O ATOM 1085 CB ALA A 192 -0.263 -3.024 -23.463 1.00 20.91 C ANISOU 1085 CB ALA A 192 2590 3441 1913 35 -199 717 C ATOM 1086 N ILE A 193 -0.243 -6.156 -23.842 1.00 48.80 N ANISOU 1086 N ILE A 193 5862 7133 5548 -147 -120 931 N ATOM 1087 CA ILE A 193 0.459 -7.433 -23.910 1.00 45.64 C ANISOU 1087 CA ILE A 193 5430 6743 5170 -245 -134 1027 C ATOM 1088 C ILE A 193 0.132 -8.170 -25.206 1.00 43.91 C ANISOU 1088 C ILE A 193 5112 6492 5079 -274 -159 1056 C ATOM 1089 O ILE A 193 1.032 -8.642 -25.903 1.00 41.10 O ANISOU 1089 O ILE A 193 4774 6085 4758 -321 -217 1090 O ATOM 1090 CB ILE A 193 0.115 -8.334 -22.706 1.00 43.27 C ANISOU 1090 CB ILE A 193 5107 6530 4803 -278 -38 1089 C ATOM 1091 CG1 ILE A 193 0.752 -7.780 -21.431 1.00 44.39 C ANISOU 1091 CG1 ILE A 193 5381 6703 4782 -273 -39 1071 C ATOM 1092 CG2 ILE A 193 0.588 -9.760 -22.948 1.00 40.42 C ANISOU 1092 CG2 ILE A 193 4704 6150 4504 -363 -54 1195 C ATOM 1093 CD1 ILE A 193 0.490 -8.622 -20.202 1.00 45.17 C ANISOU 1093 CD1 ILE A 193 5484 6897 4781 -311 53 1146 C ATOM 1094 N TRP A 194 -1.156 -8.258 -25.525 1.00 51.79 N ANISOU 1094 N TRP A 194 6006 7529 6143 -244 -116 1039 N ATOM 1095 CA TRP A 194 -1.597 -8.915 -26.753 1.00 50.35 C ANISOU 1095 CA TRP A 194 5742 7319 6070 -283 -160 1055 C ATOM 1096 C TRP A 194 -0.992 -8.274 -28.000 1.00 48.19 C ANISOU 1096 C TRP A 194 5528 6968 5814 -266 -262 1019 C ATOM 1097 O TRP A 194 -0.469 -8.965 -28.880 1.00 45.94 O ANISOU 1097 O TRP A 194 5255 6639 5562 -319 -307 1038 O ATOM 1098 CB TRP A 194 -3.124 -8.899 -26.852 1.00 57.66 C ANISOU 1098 CB TRP A 194 6524 8316 7067 -258 -118 1047 C ATOM 1099 CG TRP A 194 -3.781 -10.047 -26.148 1.00 58.15 C ANISOU 1099 CG TRP A 194 6493 8443 7157 -341 -35 1119 C ATOM 1100 CD1 TRP A 194 -4.477 -10.005 -24.973 1.00 60.74 C ANISOU 1100 CD1 TRP A 194 6760 8876 7441 -326 89 1147 C ATOM 1101 CD2 TRP A 194 -3.801 -11.414 -26.577 1.00 56.23 C ANISOU 1101 CD2 TRP A 194 6222 8155 6987 -459 -66 1179 C ATOM 1102 NE1 TRP A 194 -4.930 -11.261 -24.646 1.00 60.14 N ANISOU 1102 NE1 TRP A 194 6610 8830 7412 -444 135 1239 N ATOM 1103 CE2 TRP A 194 -4.528 -12.143 -25.613 1.00 57.54 C ANISOU 1103 CE2 TRP A 194 6307 8394 7162 -527 33 1256 C ATOM 1104 CE3 TRP A 194 -3.275 -12.090 -27.682 1.00 53.92 C ANISOU 1104 CE3 TRP A 194 5982 7761 6745 -513 -162 1170 C ATOM 1105 CZ2 TRP A 194 -4.743 -13.515 -25.724 1.00 56.56 C ANISOU 1105 CZ2 TRP A 194 6158 8222 7111 -659 21 1331 C ATOM 1106 CZ3 TRP A 194 -3.488 -13.452 -27.788 1.00 53.39 C ANISOU 1106 CZ3 TRP A 194 5899 7643 6742 -624 -169 1222 C ATOM 1107 CH2 TRP A 194 -4.216 -14.150 -26.814 1.00 54.66 C ANISOU 1107 CH2 TRP A 194 5985 7856 6927 -703 -87 1306 C ATOM 1108 N LEU A 195 -1.064 -6.949 -28.064 1.00 41.77 N ANISOU 1108 N LEU A 195 4766 6134 4970 -190 -293 968 N ATOM 1109 CA LEU A 195 -0.545 -6.209 -29.209 1.00 39.81 C ANISOU 1109 CA LEU A 195 4586 5812 4726 -182 -387 953 C ATOM 1110 C LEU A 195 0.968 -6.350 -29.341 1.00 37.08 C ANISOU 1110 C LEU A 195 4325 5428 4335 -249 -414 986 C ATOM 1111 O LEU A 195 1.490 -6.516 -30.446 1.00 35.01 O ANISOU 1111 O LEU A 195 4081 5136 4084 -283 -458 1003 O ATOM 1112 CB LEU A 195 -0.944 -4.738 -29.112 1.00 64.03 C ANISOU 1112 CB LEU A 195 7708 8841 7781 -85 -418 901 C ATOM 1113 CG LEU A 195 -2.451 -4.504 -29.215 1.00 66.87 C ANISOU 1113 CG LEU A 195 7955 9244 8211 10 -404 875 C ATOM 1114 CD1 LEU A 195 -2.829 -3.152 -28.644 1.00 69.51 C ANISOU 1114 CD1 LEU A 195 8353 9531 8529 141 -402 813 C ATOM 1115 CD2 LEU A 195 -2.913 -4.626 -30.659 1.00 65.05 C ANISOU 1115 CD2 LEU A 195 7670 9001 8046 -9 -498 901 C ATOM 1116 N ALA A 196 1.666 -6.293 -28.211 1.00 33.01 N ANISOU 1116 N ALA A 196 3853 4927 3761 -268 -387 999 N ATOM 1117 CA ALA A 196 3.110 -6.494 -28.198 1.00 30.87 C ANISOU 1117 CA ALA A 196 3623 4644 3464 -331 -416 1046 C ATOM 1118 C ALA A 196 3.449 -7.895 -28.696 1.00 29.40 C ANISOU 1118 C ALA A 196 3377 4470 3325 -363 -386 1094 C ATOM 1119 O ALA A 196 4.450 -8.100 -29.387 1.00 27.84 O ANISOU 1119 O ALA A 196 3183 4259 3136 -388 -403 1124 O ATOM 1120 CB ALA A 196 3.666 -6.276 -26.800 1.00 16.40 C ANISOU 1120 CB ALA A 196 1841 2834 1555 -349 -416 1055 C ATOM 1121 N SER A 197 2.599 -8.854 -28.343 1.00 47.04 N ANISOU 1121 N SER A 197 5555 6725 5591 -361 -336 1101 N ATOM 1122 CA SER A 197 2.773 -10.236 -28.771 1.00 46.21 C ANISOU 1122 CA SER A 197 5420 6598 5540 -391 -315 1137 C ATOM 1123 C SER A 197 2.614 -10.355 -30.281 1.00 45.50 C ANISOU 1123 C SER A 197 5334 6468 5486 -393 -347 1097 C ATOM 1124 O SER A 197 3.381 -11.059 -30.942 1.00 44.81 O ANISOU 1124 O SER A 197 5267 6344 5413 -400 -342 1105 O ATOM 1125 CB SER A 197 1.764 -11.141 -28.067 1.00 35.79 C ANISOU 1125 CB SER A 197 4050 5299 4250 -415 -263 1163 C ATOM 1126 OG SER A 197 1.822 -10.955 -26.666 1.00 36.51 O ANISOU 1126 OG SER A 197 4156 5442 4276 -412 -226 1199 O ATOM 1127 N ALA A 198 1.614 -9.665 -30.820 1.00 39.54 N ANISOU 1127 N ALA A 198 4564 5722 4736 -376 -382 1054 N ATOM 1128 CA ALA A 198 1.399 -9.646 -32.263 1.00 39.00 C ANISOU 1128 CA ALA A 198 4516 5628 4674 -383 -436 1021 C ATOM 1129 C ALA A 198 2.605 -9.039 -32.977 1.00 37.65 C ANISOU 1129 C ALA A 198 4417 5440 4446 -379 -453 1029 C ATOM 1130 O ALA A 198 3.088 -9.579 -33.978 1.00 37.46 O ANISOU 1130 O ALA A 198 4432 5399 4402 -393 -458 1017 O ATOM 1131 CB ALA A 198 0.132 -8.874 -32.601 1.00 16.27 C ANISOU 1131 CB ALA A 198 1593 2770 1817 -353 -488 994 C ATOM 1132 N LEU A 199 3.086 -7.917 -32.447 1.00 26.51 N ANISOU 1132 N LEU A 199 3031 4038 3004 -368 -460 1050 N ATOM 1133 CA LEU A 199 4.253 -7.239 -33.003 1.00 25.58 C ANISOU 1133 CA LEU A 199 2964 3915 2842 -391 -474 1080 C ATOM 1134 C LEU A 199 5.473 -8.152 -33.009 1.00 25.23 C ANISOU 1134 C LEU A 199 2893 3892 2800 -406 -417 1116 C ATOM 1135 O LEU A 199 6.219 -8.199 -33.987 1.00 25.22 O ANISOU 1135 O LEU A 199 2909 3904 2770 -417 -396 1132 O ATOM 1136 CB LEU A 199 4.566 -5.971 -32.210 1.00 39.74 C ANISOU 1136 CB LEU A 199 4796 5694 4611 -400 -511 1094 C ATOM 1137 CG LEU A 199 3.524 -4.854 -32.251 1.00 40.81 C ANISOU 1137 CG LEU A 199 4977 5783 4744 -357 -569 1057 C ATOM 1138 CD1 LEU A 199 3.915 -3.737 -31.297 1.00 41.69 C ANISOU 1138 CD1 LEU A 199 5160 5851 4828 -365 -605 1054 C ATOM 1139 CD2 LEU A 199 3.351 -4.328 -33.667 1.00 40.47 C ANISOU 1139 CD2 LEU A 199 4979 5714 4685 -361 -622 1071 C ATOM 1140 N LEU A 200 5.675 -8.872 -31.911 1.00 29.21 N ANISOU 1140 N LEU A 200 3355 4407 3338 -398 -385 1137 N ATOM 1141 CA LEU A 200 6.793 -9.802 -31.812 1.00 29.38 C ANISOU 1141 CA LEU A 200 3339 4443 3382 -386 -339 1182 C ATOM 1142 C LEU A 200 6.576 -11.032 -32.691 1.00 30.22 C ANISOU 1142 C LEU A 200 3459 4508 3515 -353 -293 1147 C ATOM 1143 O LEU A 200 7.521 -11.759 -32.997 1.00 31.09 O ANISOU 1143 O LEU A 200 3550 4619 3645 -314 -242 1168 O ATOM 1144 CB LEU A 200 7.020 -10.217 -30.357 1.00 24.40 C ANISOU 1144 CB LEU A 200 2674 3827 2768 -385 -340 1231 C ATOM 1145 CG LEU A 200 7.542 -9.119 -29.424 1.00 24.40 C ANISOU 1145 CG LEU A 200 2680 3867 2723 -424 -393 1262 C ATOM 1146 CD1 LEU A 200 7.520 -9.583 -27.973 1.00 25.08 C ANISOU 1146 CD1 LEU A 200 2762 3973 2793 -425 -401 1299 C ATOM 1147 CD2 LEU A 200 8.947 -8.690 -29.829 1.00 24.37 C ANISOU 1147 CD2 LEU A 200 2633 3905 2722 -452 -409 1319 C ATOM 1148 N ALA A 201 5.329 -11.254 -33.099 1.00 35.42 N ANISOU 1148 N ALA A 201 4150 5129 4178 -366 -317 1090 N ATOM 1149 CA ALA A 201 4.994 -12.394 -33.948 1.00 36.81 C ANISOU 1149 CA ALA A 201 4370 5245 4371 -357 -298 1039 C ATOM 1150 C ALA A 201 5.035 -12.035 -35.430 1.00 37.39 C ANISOU 1150 C ALA A 201 4509 5327 4370 -357 -309 988 C ATOM 1151 O ALA A 201 4.961 -12.913 -36.291 1.00 39.18 O ANISOU 1151 O ALA A 201 4802 5504 4579 -350 -298 927 O ATOM 1152 CB ALA A 201 3.631 -12.949 -33.579 1.00 58.98 C ANISOU 1152 CB ALA A 201 7168 8013 7229 -398 -334 1016 C ATOM 1153 N ILE A 202 5.148 -10.741 -35.713 1.00 33.06 N ANISOU 1153 N ILE A 202 3962 4831 3768 -372 -335 1015 N ATOM 1154 CA ILE A 202 5.249 -10.235 -37.088 1.00 33.56 C ANISOU 1154 CA ILE A 202 4097 4914 3739 -384 -349 993 C ATOM 1155 C ILE A 202 6.225 -10.960 -38.045 1.00 35.42 C ANISOU 1155 C ILE A 202 4382 5161 3914 -350 -259 968 C ATOM 1156 O ILE A 202 5.842 -11.277 -39.172 1.00 36.92 O ANISOU 1156 O ILE A 202 4666 5339 4023 -356 -272 907 O ATOM 1157 CB ILE A 202 5.510 -8.703 -37.111 1.00 31.67 C ANISOU 1157 CB ILE A 202 3860 4711 3461 -413 -390 1053 C ATOM 1158 CG1 ILE A 202 4.270 -7.947 -36.631 1.00 30.99 C ANISOU 1158 CG1 ILE A 202 3767 4598 3410 -416 -484 1043 C ATOM 1159 CG2 ILE A 202 5.906 -8.233 -38.504 1.00 32.40 C ANISOU 1159 CG2 ILE A 202 4032 4834 3444 -433 -383 1064 C ATOM 1160 CD1 ILE A 202 4.412 -6.442 -36.696 1.00 30.40 C ANISOU 1160 CD1 ILE A 202 3724 4516 3308 -432 -537 1091 C ATOM 1161 N PRO A 203 7.475 -11.229 -37.609 1.00 36.07 N ANISOU 1161 N PRO A 203 4400 5276 4030 -307 -167 1012 N ATOM 1162 CA PRO A 203 8.445 -11.853 -38.523 1.00 38.57 C ANISOU 1162 CA PRO A 203 4747 5618 4292 -246 -55 983 C ATOM 1163 C PRO A 203 7.986 -13.157 -39.182 1.00 41.28 C ANISOU 1163 C PRO A 203 5199 5872 4616 -203 -39 871 C ATOM 1164 O PRO A 203 8.512 -13.513 -40.235 1.00 43.81 O ANISOU 1164 O PRO A 203 5605 6208 4836 -163 34 812 O ATOM 1165 CB PRO A 203 9.645 -12.131 -37.615 1.00 23.26 C ANISOU 1165 CB PRO A 203 2683 3713 2442 -190 16 1054 C ATOM 1166 CG PRO A 203 9.568 -11.082 -36.589 1.00 22.99 C ANISOU 1166 CG PRO A 203 2573 3713 2448 -261 -63 1136 C ATOM 1167 CD PRO A 203 8.104 -10.891 -36.318 1.00 22.38 C ANISOU 1167 CD PRO A 203 2560 3573 2371 -309 -165 1092 C ATOM 1168 N MET A 204 7.030 -13.855 -38.577 1.00 35.57 N ANISOU 1168 N MET A 204 4483 5054 3978 -219 -105 841 N ATOM 1169 CA MET A 204 6.532 -15.105 -39.143 1.00 38.63 C ANISOU 1169 CA MET A 204 4985 5328 4364 -204 -114 737 C ATOM 1170 C MET A 204 5.689 -14.877 -40.396 1.00 39.64 C ANISOU 1170 C MET A 204 5235 5454 4372 -267 -189 655 C ATOM 1171 O MET A 204 5.525 -15.781 -41.214 1.00 43.01 O ANISOU 1171 O MET A 204 5796 5801 4744 -256 -187 549 O ATOM 1172 CB MET A 204 5.742 -15.898 -38.100 1.00 45.68 C ANISOU 1172 CB MET A 204 5847 6126 5383 -241 -175 752 C ATOM 1173 CG MET A 204 6.621 -16.510 -37.031 1.00 45.88 C ANISOU 1173 CG MET A 204 5801 6120 5510 -166 -107 820 C ATOM 1174 SD MET A 204 7.926 -17.522 -37.757 1.00 50.63 S ANISOU 1174 SD MET A 204 6473 6663 6101 -15 23 759 S ATOM 1175 CE MET A 204 9.064 -17.650 -36.381 1.00 49.92 C ANISOU 1175 CE MET A 204 6236 6590 6139 71 66 892 C ATOM 1176 N LEU A 205 5.162 -13.666 -40.544 1.00 40.52 N ANISOU 1176 N LEU A 205 5313 5644 4439 -329 -267 705 N ATOM 1177 CA LEU A 205 4.365 -13.315 -41.715 1.00 41.21 C ANISOU 1177 CA LEU A 205 5505 5747 4405 -385 -360 655 C ATOM 1178 C LEU A 205 5.240 -13.185 -42.956 1.00 43.05 C ANISOU 1178 C LEU A 205 5847 6038 4470 -346 -268 626 C ATOM 1179 O LEU A 205 4.750 -13.243 -44.083 1.00 44.66 O ANISOU 1179 O LEU A 205 6189 6244 4536 -380 -325 560 O ATOM 1180 CB LEU A 205 3.606 -12.008 -41.473 1.00 21.66 C ANISOU 1180 CB LEU A 205 2959 3328 1944 -436 -469 732 C ATOM 1181 CG LEU A 205 2.512 -12.036 -40.404 1.00 21.03 C ANISOU 1181 CG LEU A 205 2773 3216 2001 -472 -557 751 C ATOM 1182 CD1 LEU A 205 1.917 -10.652 -40.212 1.00 21.72 C ANISOU 1182 CD1 LEU A 205 2797 3357 2099 -481 -642 818 C ATOM 1183 CD2 LEU A 205 1.431 -13.038 -40.781 1.00 21.70 C ANISOU 1183 CD2 LEU A 205 2908 3238 2101 -533 -650 671 C ATOM 1184 N PHE A 206 6.541 -13.013 -42.740 1.00 33.95 N ANISOU 1184 N PHE A 206 4628 4946 3324 -281 -126 683 N ATOM 1185 CA PHE A 206 7.487 -12.830 -43.834 1.00 35.67 C ANISOU 1185 CA PHE A 206 4915 5250 3386 -243 -3 677 C ATOM 1186 C PHE A 206 8.477 -13.988 -43.933 1.00 39.12 C ANISOU 1186 C PHE A 206 5370 5663 3831 -122 161 606 C ATOM 1187 O PHE A 206 9.124 -14.173 -44.963 1.00 41.60 O ANISOU 1187 O PHE A 206 5774 6033 3997 -68 282 555 O ATOM 1188 CB PHE A 206 8.246 -11.510 -43.665 1.00 44.95 C ANISOU 1188 CB PHE A 206 5985 6540 4554 -277 35 817 C ATOM 1189 CG PHE A 206 7.355 -10.300 -43.602 1.00 42.31 C ANISOU 1189 CG PHE A 206 5662 6208 4203 -372 -118 884 C ATOM 1190 CD1 PHE A 206 6.978 -9.642 -44.761 1.00 42.69 C ANISOU 1190 CD1 PHE A 206 5834 6300 4085 -422 -165 898 C ATOM 1191 CD2 PHE A 206 6.900 -9.817 -42.385 1.00 39.79 C ANISOU 1191 CD2 PHE A 206 5241 5848 4029 -398 -212 933 C ATOM 1192 CE1 PHE A 206 6.161 -8.530 -44.709 1.00 40.75 C ANISOU 1192 CE1 PHE A 206 5602 6041 3839 -486 -316 968 C ATOM 1193 CE2 PHE A 206 6.081 -8.704 -42.328 1.00 38.03 C ANISOU 1193 CE2 PHE A 206 5032 5615 3802 -454 -344 985 C ATOM 1194 CZ PHE A 206 5.711 -8.060 -43.492 1.00 38.57 C ANISOU 1194 CZ PHE A 206 5215 5712 3726 -493 -401 1007 C ATOM 1195 N THR A 207 8.593 -14.763 -42.857 1.00 41.61 N ANISOU 1195 N THR A 207 5601 5894 4313 -69 169 606 N ATOM 1196 CA THR A 207 9.521 -15.889 -42.815 1.00 45.22 C ANISOU 1196 CA THR A 207 6062 6305 4813 73 312 551 C ATOM 1197 C THR A 207 8.939 -17.114 -43.513 1.00 49.06 C ANISOU 1197 C THR A 207 6750 6637 5251 105 291 386 C ATOM 1198 O THR A 207 9.646 -17.837 -44.215 1.00 52.45 O ANISOU 1198 O THR A 207 7275 7039 5612 229 426 290 O ATOM 1199 CB THR A 207 9.886 -16.267 -41.366 1.00 45.44 C ANISOU 1199 CB THR A 207 5930 6296 5040 119 313 639 C ATOM 1200 OG1 THR A 207 10.384 -15.111 -40.680 1.00 41.84 O ANISOU 1200 OG1 THR A 207 5311 5965 4622 57 291 780 O ATOM 1201 CG2 THR A 207 10.947 -17.361 -41.346 1.00 48.93 C ANISOU 1201 CG2 THR A 207 6343 6712 5537 293 467 614 C ATOM 1202 N MET A 208 7.644 -17.338 -43.323 1.00 52.21 N ANISOU 1202 N MET A 208 7214 6937 5686 -8 123 351 N ATOM 1203 CA MET A 208 6.995 -18.533 -43.848 1.00 55.76 C ANISOU 1203 CA MET A 208 7853 7218 6116 -19 63 203 C ATOM 1204 C MET A 208 6.205 -18.245 -45.123 1.00 56.19 C ANISOU 1204 C MET A 208 8080 7295 5976 -111 -31 108 C ATOM 1205 O MET A 208 5.819 -17.104 -45.385 1.00 53.24 O ANISOU 1205 O MET A 208 7654 7039 5536 -201 -116 182 O ATOM 1206 CB MET A 208 6.077 -19.142 -42.787 1.00 29.68 C ANISOU 1206 CB MET A 208 4498 3789 2989 -105 -68 237 C ATOM 1207 CG MET A 208 6.748 -19.352 -41.439 1.00 29.12 C ANISOU 1207 CG MET A 208 4278 3693 3092 -25 2 342 C ATOM 1208 SD MET A 208 8.124 -20.516 -41.510 1.00 34.12 S ANISOU 1208 SD MET A 208 4991 4218 3756 185 173 270 S ATOM 1209 CE MET A 208 7.259 -22.031 -41.916 1.00 36.19 C ANISOU 1209 CE MET A 208 5510 4219 4019 134 76 102 C ATOM 1210 N GLY A 209 5.968 -19.290 -45.912 1.00 45.09 N ANISOU 1210 N GLY A 209 6893 5766 4473 -84 -28 -57 N ATOM 1211 CA GLY A 209 5.198 -19.160 -47.135 1.00 45.44 C ANISOU 1211 CA GLY A 209 7129 5825 4313 -180 -140 -159 C ATOM 1212 C GLY A 209 5.072 -20.467 -47.892 1.00 48.89 C ANISOU 1212 C GLY A 209 7832 6083 4663 -157 -152 -362 C ATOM 1213 O GLY A 209 5.423 -21.531 -47.381 1.00 51.10 O ANISOU 1213 O GLY A 209 8149 6202 5066 -63 -77 -422 O ATOM 1214 N LEU A 210 4.571 -20.388 -49.120 1.00 48.30 N ANISOU 1214 N LEU A 210 7959 6024 4371 -244 -258 -470 N ATOM 1215 CA LEU A 210 4.366 -21.576 -49.939 1.00 51.41 C ANISOU 1215 CA LEU A 210 8649 6240 4646 -242 -293 -686 C ATOM 1216 C LEU A 210 5.497 -21.792 -50.937 1.00 53.54 C ANISOU 1216 C LEU A 210 9101 6556 4686 -66 -66 -812 C ATOM 1217 O LEU A 210 5.955 -20.849 -51.584 1.00 52.42 O ANISOU 1217 O LEU A 210 8936 6620 4363 -41 25 -751 O ATOM 1218 CB LEU A 210 3.036 -21.485 -50.689 1.00 44.59 C ANISOU 1218 CB LEU A 210 7921 5361 3660 -449 -563 -746 C ATOM 1219 CG LEU A 210 1.773 -21.343 -49.839 1.00 42.97 C ANISOU 1219 CG LEU A 210 7538 5115 3676 -630 -791 -639 C ATOM 1220 CD1 LEU A 210 0.535 -21.457 -50.711 1.00 43.10 C ANISOU 1220 CD1 LEU A 210 7705 5101 3570 -826 -1062 -724 C ATOM 1221 CD2 LEU A 210 1.753 -22.384 -48.728 1.00 44.47 C ANISOU 1221 CD2 LEU A 210 7672 5107 4120 -612 -760 -640 C ATOM 1222 N GLN A 211 5.941 -23.040 -51.057 1.00 33.44 N ANISOU 1222 N GLN A 211 6740 3816 2148 61 33 -983 N ATOM 1223 CA GLN A 211 6.942 -23.405 -52.056 1.00 37.44 C ANISOU 1223 CA GLN A 211 7451 4352 2424 246 260 -1139 C ATOM 1224 C GLN A 211 6.634 -24.760 -52.679 1.00 41.90 C ANISOU 1224 C GLN A 211 8372 4654 2894 267 207 -1402 C ATOM 1225 O GLN A 211 6.163 -25.670 -52.000 1.00 41.38 O ANISOU 1225 O GLN A 211 8350 4349 3024 198 63 -1442 O ATOM 1226 CB GLN A 211 8.348 -23.420 -51.451 1.00 71.81 C ANISOU 1226 CB GLN A 211 11609 8769 6907 487 545 -1061 C ATOM 1227 CG GLN A 211 8.963 -22.045 -51.258 1.00 69.24 C ANISOU 1227 CG GLN A 211 10990 8726 6595 484 644 -836 C ATOM 1228 CD GLN A 211 10.444 -22.117 -50.943 1.00 70.27 C ANISOU 1228 CD GLN A 211 10967 8958 6776 723 944 -792 C ATOM 1229 OE1 GLN A 211 11.139 -21.100 -50.929 1.00 68.97 O ANISOU 1229 OE1 GLN A 211 10645 9034 6527 741 1082 -665 O ATOM 1230 NE2 GLN A 211 10.937 -23.325 -50.692 1.00 72.62 N ANISOU 1230 NE2 GLN A 211 11302 9069 7222 904 1040 -886 N ATOM 1231 N ASN A 212 6.896 -24.886 -53.975 1.00 46.81 N ANISOU 1231 N ASN A 212 9264 5315 3205 355 325 -1582 N ATOM 1232 CA ASN A 212 6.704 -26.154 -54.666 1.00 52.00 C ANISOU 1232 CA ASN A 212 10313 5718 3729 373 270 -1862 C ATOM 1233 C ASN A 212 7.999 -26.958 -54.686 1.00 55.00 C ANISOU 1233 C ASN A 212 10801 6005 4092 692 586 -2008 C ATOM 1234 O ASN A 212 8.847 -26.762 -55.556 1.00 57.40 O ANISOU 1234 O ASN A 212 11125 6505 4179 860 842 -2040 O ATOM 1235 CB ASN A 212 6.202 -25.923 -56.093 1.00 56.59 C ANISOU 1235 CB ASN A 212 11176 6386 3938 226 135 -1991 C ATOM 1236 CG ASN A 212 5.510 -27.143 -56.671 1.00 61.83 C ANISOU 1236 CG ASN A 212 12249 6760 4484 154 -31 -2271 C ATOM 1237 OD1 ASN A 212 6.153 -28.144 -56.985 1.00 62.85 O ANISOU 1237 OD1 ASN A 212 12474 6823 4582 -108 -351 -2292 O ATOM 1238 ND2 ASN A 212 4.193 -27.062 -56.822 1.00 65.72 N ANISOU 1238 ND2 ASN A 212 12982 7073 4915 385 179 -2489 N ATOM 1239 N LEU A 213 8.148 -27.861 -53.722 1.00 56.38 N ANISOU 1239 N LEU A 213 11037 5883 4503 781 573 -2085 N ATOM 1240 CA LEU A 213 9.389 -28.612 -53.561 1.00 59.41 C ANISOU 1240 CA LEU A 213 11489 6152 4932 1114 861 -2204 C ATOM 1241 C LEU A 213 9.407 -29.914 -54.358 1.00 65.89 C ANISOU 1241 C LEU A 213 12767 6634 5632 1187 832 -2526 C ATOM 1242 O LEU A 213 10.221 -30.799 -54.095 1.00 68.11 O ANISOU 1242 O LEU A 213 13127 6670 6081 1411 951 -2617 O ATOM 1243 CB LEU A 213 9.657 -28.897 -52.082 1.00 56.88 C ANISOU 1243 CB LEU A 213 10861 5751 5002 1217 902 -2013 C ATOM 1244 CG LEU A 213 9.859 -27.671 -51.189 1.00 50.62 C ANISOU 1244 CG LEU A 213 9625 5240 4368 1138 904 -1700 C ATOM 1245 CD1 LEU A 213 10.265 -28.090 -49.786 1.00 48.40 C ANISOU 1245 CD1 LEU A 213 9097 4880 4414 1311 1000 -1555 C ATOM 1246 CD2 LEU A 213 10.888 -26.727 -51.791 1.00 50.99 C ANISOU 1246 CD2 LEU A 213 9544 5642 4189 1203 1107 -1633 C ATOM 1247 N SER A 214 8.511 -30.029 -55.332 1.00 69.95 N ANISOU 1247 N SER A 214 13596 7128 5852 1002 663 -2698 N ATOM 1248 CA SER A 214 8.495 -31.195 -56.205 1.00 76.59 C ANISOU 1248 CA SER A 214 14916 7637 6548 1027 593 -3023 C ATOM 1249 C SER A 214 9.696 -31.170 -57.143 1.00 82.21 C ANISOU 1249 C SER A 214 15844 8292 7102 1408 947 -3249 C ATOM 1250 O SER A 214 10.417 -30.173 -57.208 1.00 86.92 O ANISOU 1250 O SER A 214 16748 8533 7747 1544 960 -3477 O ATOM 1251 CB SER A 214 7.196 -31.253 -57.008 1.00 78.17 C ANISOU 1251 CB SER A 214 15397 7875 6426 743 332 -3152 C ATOM 1252 OG SER A 214 7.029 -30.090 -57.799 1.00 73.06 O ANISOU 1252 OG SER A 214 14468 7427 5865 448 85 -2903 O ATOM 1253 N GLY A 215 9.908 -32.268 -57.861 1.00 80.78 N ANISOU 1253 N GLY A 215 15501 8458 6735 1578 1237 -3181 N ATOM 1254 CA GLY A 215 11.038 -32.391 -58.764 1.00 86.75 C ANISOU 1254 CA GLY A 215 16430 9229 7301 1942 1607 -3385 C ATOM 1255 C GLY A 215 11.070 -31.310 -59.826 1.00 89.85 C ANISOU 1255 C GLY A 215 16957 9941 7240 1908 1732 -3451 C ATOM 1256 O GLY A 215 12.055 -30.585 -59.957 1.00 90.93 O ANISOU 1256 O GLY A 215 16920 10368 7262 2122 2071 -3385 O ATOM 1257 N ASP A 216 9.984 -31.201 -60.584 1.00 92.82 N ANISOU 1257 N ASP A 216 17641 10270 7358 1625 1447 -3571 N ATOM 1258 CA ASP A 216 9.881 -30.189 -61.627 1.00 95.07 C ANISOU 1258 CA ASP A 216 18041 10871 7212 1518 1483 -3578 C ATOM 1259 C ASP A 216 9.525 -28.832 -61.033 1.00 88.35 C ANISOU 1259 C ASP A 216 16808 10291 6468 1247 1293 -3232 C ATOM 1260 O ASP A 216 9.737 -27.794 -61.660 1.00 88.62 O ANISOU 1260 O ASP A 216 16783 10650 6238 1185 1372 -3118 O ATOM 1261 CB ASP A 216 8.830 -30.597 -62.662 1.00151.93 C ATOM 1262 CG ASP A 216 9.130 -31.940 -63.299 1.00151.93 C ATOM 1263 OD1 ASP A 216 10.322 -32.302 -63.389 1.00151.93 O ATOM 1264 OD2 ASP A 216 8.175 -32.634 -63.710 1.00151.93 O ATOM 1265 N GLY A 217 8.984 -28.845 -59.819 1.00 81.57 N ANISOU 1265 N GLY A 217 15703 9289 5998 1090 1048 -3063 N ATOM 1266 CA GLY A 217 8.549 -27.626 -59.164 1.00 75.31 C ANISOU 1266 CA GLY A 217 14555 8712 5349 850 857 -2750 C ATOM 1267 C GLY A 217 7.205 -27.167 -59.692 1.00 76.08 C ANISOU 1267 C GLY A 217 14829 8785 5295 514 464 -2772 C ATOM 1268 O GLY A 217 6.799 -26.025 -59.476 1.00 72.00 O ANISOU 1268 O GLY A 217 14059 8448 4849 314 285 -2534 O ATOM 1269 N THR A 218 6.511 -28.065 -60.385 1.00 81.79 N ANISOU 1269 N THR A 218 15988 9276 5813 455 320 -3061 N ATOM 1270 CA THR A 218 5.231 -27.741 -61.005 1.00 84.04 C ANISOU 1270 CA THR A 218 16478 9551 5901 138 -60 -3108 C ATOM 1271 C THR A 218 4.117 -28.682 -60.551 1.00 83.25 C ANISOU 1271 C THR A 218 16404 9148 6079 -94 -419 -3139 C ATOM 1272 O THR A 218 2.950 -28.478 -60.882 1.00 82.87 O ANISOU 1272 O THR A 218 16319 9148 6021 -386 -762 -3052 O ATOM 1273 CB THR A 218 5.324 -27.788 -62.542 1.00 92.07 C ANISOU 1273 CB THR A 218 18001 10554 6426 171 -26 -3411 C ATOM 1274 OG1 THR A 218 5.734 -29.097 -62.957 1.00 96.64 O ANISOU 1274 OG1 THR A 218 18916 10780 7024 317 43 -3718 O ATOM 1275 CG2 THR A 218 6.330 -26.766 -63.049 1.00 93.57 C ANISOU 1275 CG2 THR A 218 18170 11068 6314 385 347 -3370 C ATOM 1276 N HIS A 219 4.482 -29.710 -59.791 1.00 83.49 N ANISOU 1276 N HIS A 219 16491 8868 6363 35 -341 -3250 N ATOM 1277 CA HIS A 219 3.509 -30.680 -59.299 1.00 84.17 C ANISOU 1277 CA HIS A 219 16667 8628 6688 -188 -661 -3307 C ATOM 1278 C HIS A 219 2.729 -30.104 -58.119 1.00 77.33 C ANISOU 1278 C HIS A 219 15340 7837 6204 -370 -830 -2988 C ATOM 1279 O HIS A 219 3.319 -29.722 -57.108 1.00 72.06 O ANISOU 1279 O HIS A 219 14337 7253 5789 -209 -625 -2794 O ATOM 1280 CB HIS A 219 4.212 -31.979 -58.897 1.00 87.32 C ANISOU 1280 CB HIS A 219 17303 8647 7228 22 -515 -3521 C ATOM 1281 CG HIS A 219 3.290 -33.152 -58.757 1.00 90.32 C ANISOU 1281 CG HIS A 219 17903 8645 7768 -220 -843 -3641 C ATOM 1282 ND1 HIS A 219 3.601 -34.403 -59.244 1.00 97.28 N ANISOU 1282 ND1 HIS A 219 19261 9156 8544 -148 -853 -3968 N ATOM 1283 CD2 HIS A 219 2.071 -33.266 -58.180 1.00 87.79 C ANISOU 1283 CD2 HIS A 219 17390 8250 7714 -536 -1165 -3474 C ATOM 1284 CE1 HIS A 219 2.611 -35.236 -58.978 1.00 98.89 C ANISOU 1284 CE1 HIS A 219 19563 9064 8945 -432 -1185 -3990 C ATOM 1285 NE2 HIS A 219 1.669 -34.571 -58.333 1.00 93.23 N ANISOU 1285 NE2 HIS A 219 18432 8535 8457 -673 -1372 -3687 N ATOM 1286 N PRO A 220 1.393 -30.038 -58.253 1.00 77.87 N ANISOU 1286 N PRO A 220 15391 7891 6305 -705 -1206 -2934 N ATOM 1287 CA PRO A 220 0.484 -29.489 -57.238 1.00 72.60 C ANISOU 1287 CA PRO A 220 14312 7307 5966 -906 -1397 -2651 C ATOM 1288 C PRO A 220 0.603 -30.183 -55.884 1.00 68.98 C ANISOU 1288 C PRO A 220 13655 6646 5908 -826 -1297 -2549 C ATOM 1289 O PRO A 220 0.262 -29.591 -54.861 1.00 63.29 O ANISOU 1289 O PRO A 220 12537 6073 5437 -845 -1274 -2288 O ATOM 1290 CB PRO A 220 -0.900 -29.755 -57.836 1.00 77.23 C ANISOU 1290 CB PRO A 220 15056 7779 6507 -1256 -1813 -2726 C ATOM 1291 CG PRO A 220 -0.671 -29.787 -59.308 1.00 83.87 C ANISOU 1291 CG PRO A 220 16355 8597 6916 -1257 -1861 -3002 C ATOM 1292 CD PRO A 220 0.673 -30.432 -59.478 1.00 84.46 C ANISOU 1292 CD PRO A 220 16590 8712 6790 -901 -1459 -3131 C ATOM 1293 N GLY A 221 1.074 -31.426 -55.884 1.00 72.75 N ANISOU 1293 N GLY A 221 14428 6778 6434 -736 -1247 -2756 N ATOM 1294 CA GLY A 221 1.252 -32.174 -54.653 1.00 70.43 C ANISOU 1294 CA GLY A 221 14006 6255 6502 -655 -1167 -2669 C ATOM 1295 C GLY A 221 2.507 -31.771 -53.902 1.00 65.33 C ANISOU 1295 C GLY A 221 13071 5774 5976 -345 -828 -2510 C ATOM 1296 O GLY A 221 2.695 -32.147 -52.745 1.00 61.44 O ANISOU 1296 O GLY A 221 12322 5225 5797 -317 -788 -2324 O ATOM 1297 N GLY A 222 3.367 -31.002 -54.562 1.00 65.81 N ANISOU 1297 N GLY A 222 13178 6049 5780 -123 -586 -2577 N ATOM 1298 CA GLY A 222 4.607 -30.550 -53.959 1.00 61.73 C ANISOU 1298 CA GLY A 222 12381 5722 5354 159 -266 -2428 C ATOM 1299 C GLY A 222 4.470 -29.198 -53.285 1.00 55.11 C ANISOU 1299 C GLY A 222 11099 5190 4651 56 -295 -2118 C ATOM 1300 O GLY A 222 5.433 -28.668 -52.733 1.00 51.23 O ANISOU 1300 O GLY A 222 10331 4839 4294 239 -80 -1958 O ATOM 1301 N LEU A 223 3.265 -28.640 -53.336 1.00 96.36 N ANISOU 1301 N LEU A 223 16257 10517 9838 -231 -568 -2037 N ATOM 1302 CA LEU A 223 2.985 -27.348 -52.722 1.00 93.30 C ANISOU 1302 CA LEU A 223 15476 10397 9575 -331 -617 -1760 C ATOM 1303 C LEU A 223 2.970 -27.461 -51.203 1.00 92.43 C ANISOU 1303 C LEU A 223 15083 10204 9831 -329 -607 -1573 C ATOM 1304 O LEU A 223 1.998 -27.937 -50.620 1.00 92.50 O ANISOU 1304 O LEU A 223 15117 10010 10020 -499 -796 -1568 O ATOM 1305 CB LEU A 223 1.641 -26.809 -53.212 1.00 59.21 C ANISOU 1305 CB LEU A 223 11156 6174 5166 -625 -931 -1724 C ATOM 1306 CG LEU A 223 1.198 -25.484 -52.592 1.00 55.81 C ANISOU 1306 CG LEU A 223 10356 6025 4822 -707 -983 -1461 C ATOM 1307 CD1 LEU A 223 2.173 -24.379 -52.962 1.00 54.76 C ANISOU 1307 CD1 LEU A 223 10141 6147 4516 -524 -746 -1390 C ATOM 1308 CD2 LEU A 223 -0.216 -25.130 -53.020 1.00 54.45 C ANISOU 1308 CD2 LEU A 223 10184 5924 4578 -976 -1308 -1434 C ATOM 1309 N VAL A 224 4.046 -27.018 -50.563 1.00 41.96 N ANISOU 1309 N VAL A 224 8425 3977 3539 -150 -391 -1412 N ATOM 1310 CA VAL A 224 4.160 -27.135 -49.114 1.00 40.96 C ANISOU 1310 CA VAL A 224 8043 3791 3726 -125 -363 -1232 C ATOM 1311 C VAL A 224 4.356 -25.789 -48.421 1.00 38.01 C ANISOU 1311 C VAL A 224 7309 3707 3425 -127 -308 -992 C ATOM 1312 O VAL A 224 4.863 -24.833 -49.015 1.00 36.76 O ANISOU 1312 O VAL A 224 7095 3779 3090 -71 -213 -963 O ATOM 1313 CB VAL A 224 5.315 -28.076 -48.715 1.00 36.83 C ANISOU 1313 CB VAL A 224 7590 3096 3309 145 -144 -1293 C ATOM 1314 CG1 VAL A 224 5.080 -29.474 -49.272 1.00 42.39 C ANISOU 1314 CG1 VAL A 224 8662 3450 3994 146 -215 -1524 C ATOM 1315 CG2 VAL A 224 6.647 -27.521 -49.197 1.00 37.08 C ANISOU 1315 CG2 VAL A 224 7582 3329 3176 395 130 -1318 C ATOM 1316 N CYS A 225 3.938 -25.728 -47.159 1.00 54.07 N ANISOU 1316 N CYS A 225 9117 5716 5709 -199 -371 -820 N ATOM 1317 CA CYS A 225 4.195 -24.576 -46.308 1.00 50.72 C ANISOU 1317 CA CYS A 225 8370 5523 5377 -188 -316 -604 C ATOM 1318 C CYS A 225 5.560 -24.751 -45.661 1.00 51.44 C ANISOU 1318 C CYS A 225 8352 5625 5566 48 -91 -540 C ATOM 1319 O CYS A 225 5.834 -25.776 -45.038 1.00 52.68 O ANISOU 1319 O CYS A 225 8547 5586 5884 125 -61 -544 O ATOM 1320 CB CYS A 225 3.114 -24.447 -45.237 1.00 50.46 C ANISOU 1320 CB CYS A 225 8157 5472 5542 -377 -485 -458 C ATOM 1321 SG CYS A 225 3.312 -23.024 -44.140 1.00 46.02 S ANISOU 1321 SG CYS A 225 7237 5175 5075 -373 -438 -218 S ATOM 1322 N THR A 226 6.415 -23.748 -45.813 1.00 43.16 N ANISOU 1322 N THR A 226 7167 4806 4425 155 56 -470 N ATOM 1323 CA THR A 226 7.814 -23.881 -45.438 1.00 44.08 C ANISOU 1323 CA THR A 226 7171 4966 4611 383 273 -419 C ATOM 1324 C THR A 226 8.439 -22.494 -45.276 1.00 41.45 C ANISOU 1324 C THR A 226 6596 4917 4237 395 360 -262 C ATOM 1325 O THR A 226 7.875 -21.499 -45.745 1.00 39.56 O ANISOU 1325 O THR A 226 6348 4821 3862 266 285 -236 O ATOM 1326 CB THR A 226 8.581 -24.685 -46.520 1.00 35.82 C ANISOU 1326 CB THR A 226 6356 3828 3424 579 439 -616 C ATOM 1327 OG1 THR A 226 9.843 -25.128 -46.009 1.00 36.98 O ANISOU 1327 OG1 THR A 226 6378 3978 3693 820 637 -565 O ATOM 1328 CG2 THR A 226 8.805 -23.835 -47.765 1.00 35.45 C ANISOU 1328 CG2 THR A 226 6395 3977 3095 570 512 -688 C ATOM 1329 N PRO A 227 9.587 -22.412 -44.581 1.00 44.70 N ANISOU 1329 N PRO A 227 6808 5400 4775 540 499 -144 N ATOM 1330 CA PRO A 227 10.333 -21.150 -44.584 1.00 42.19 C ANISOU 1330 CA PRO A 227 6283 5341 4406 549 592 -9 C ATOM 1331 C PRO A 227 10.756 -20.760 -45.997 1.00 43.08 C ANISOU 1331 C PRO A 227 6506 5583 4279 609 735 -102 C ATOM 1332 O PRO A 227 11.462 -21.519 -46.662 1.00 45.96 O ANISOU 1332 O PRO A 227 6990 5892 4581 784 894 -229 O ATOM 1333 CB PRO A 227 11.564 -21.476 -43.735 1.00 46.24 C ANISOU 1333 CB PRO A 227 6595 5876 5098 714 713 102 C ATOM 1334 CG PRO A 227 11.090 -22.521 -42.794 1.00 49.30 C ANISOU 1334 CG PRO A 227 7128 6012 5594 844 724 -3 C ATOM 1335 CD PRO A 227 10.115 -23.358 -43.580 1.00 49.65 C ANISOU 1335 CD PRO A 227 7374 5879 5614 669 536 -99 C ATOM 1336 N ILE A 228 10.314 -19.589 -46.446 1.00 61.91 N ANISOU 1336 N ILE A 228 8861 8135 6527 472 683 -36 N ATOM 1337 CA ILE A 228 10.683 -19.075 -47.760 1.00 62.55 C ANISOU 1337 CA ILE A 228 9065 8350 6349 493 800 -101 C ATOM 1338 C ILE A 228 11.904 -18.174 -47.642 1.00 61.27 C ANISOU 1338 C ILE A 228 8689 8418 6172 550 980 47 C ATOM 1339 O ILE A 228 12.112 -17.275 -48.457 1.00 61.35 O ANISOU 1339 O ILE A 228 8756 8583 5970 534 1083 51 O ATOM 1340 CB ILE A 228 9.534 -18.271 -48.389 1.00 34.13 C ANISOU 1340 CB ILE A 228 5595 4785 2586 298 614 -111 C ATOM 1341 CG1 ILE A 228 9.054 -17.188 -47.420 1.00 30.52 C ANISOU 1341 CG1 ILE A 228 4931 4410 2253 157 474 78 C ATOM 1342 CG2 ILE A 228 8.390 -19.195 -48.772 1.00 35.86 C ANISOU 1342 CG2 ILE A 228 6038 4798 2788 229 441 -272 C ATOM 1343 CD1 ILE A 228 7.999 -16.270 -47.998 1.00 30.10 C ANISOU 1343 CD1 ILE A 228 4974 4388 2075 -12 278 90 C ATOM 1344 N VAL A 229 12.712 -18.428 -46.620 1.00 56.86 N ANISOU 1344 N VAL A 229 7886 7886 5834 600 1009 180 N ATOM 1345 CA VAL A 229 13.843 -17.573 -46.291 1.00 55.61 C ANISOU 1345 CA VAL A 229 7492 7942 5696 629 1154 338 C ATOM 1346 C VAL A 229 15.111 -18.415 -46.145 1.00 58.14 C ANISOU 1346 C VAL A 229 7697 8280 6113 863 1367 319 C ATOM 1347 O VAL A 229 15.051 -19.560 -45.693 1.00 60.32 O ANISOU 1347 O VAL A 229 8067 8372 6479 998 1370 204 O ATOM 1348 CB VAL A 229 13.559 -16.788 -44.988 1.00 52.10 C ANISOU 1348 CB VAL A 229 6839 7540 5416 490 1005 520 C ATOM 1349 CG1 VAL A 229 14.765 -15.984 -44.562 1.00 51.99 C ANISOU 1349 CG1 VAL A 229 6662 7450 5642 588 994 575 C ATOM 1350 CG2 VAL A 229 12.357 -15.875 -45.173 1.00 50.28 C ANISOU 1350 CG2 VAL A 229 6457 7527 5120 405 1078 676 C ATOM 1351 N ASP A 230 16.251 -17.853 -46.545 1.00 48.74 N ANISOU 1351 N ASP A 230 6300 7308 4912 910 1541 438 N ATOM 1352 CA ASP A 230 17.535 -18.545 -46.438 1.00 51.21 C ANISOU 1352 CA ASP A 230 6457 7678 5323 1149 1757 439 C ATOM 1353 C ASP A 230 17.852 -18.974 -45.004 1.00 50.66 C ANISOU 1353 C ASP A 230 6206 7509 5535 1222 1663 525 C ATOM 1354 O ASP A 230 17.221 -18.516 -44.050 1.00 47.88 O ANISOU 1354 O ASP A 230 5808 7095 5288 1065 1453 615 O ATOM 1355 CB ASP A 230 18.669 -17.680 -47.000 1.00 97.97 C ANISOU 1355 CB ASP A 230 12160 13888 11175 1150 1960 574 C ATOM 1356 CG ASP A 230 18.773 -16.332 -46.312 1.00 94.55 C ANISOU 1356 CG ASP A 230 11521 13583 10821 926 1825 791 C ATOM 1357 OD1 ASP A 230 18.082 -15.386 -46.746 1.00 92.77 O ANISOU 1357 OD1 ASP A 230 11409 13392 10446 728 1732 822 O ATOM 1358 OD2 ASP A 230 19.547 -16.219 -45.339 1.00 93.75 O ANISOU 1358 OD2 ASP A 230 11155 13537 10927 949 1801 928 O ATOM 1359 N THR A 231 18.843 -19.851 -44.868 1.00 81.42 N ANISOU 1359 N THR A 231 10004 11390 9542 1473 1822 499 N ATOM 1360 CA THR A 231 19.158 -20.489 -43.591 1.00 81.55 C ANISOU 1360 CA THR A 231 9879 11292 9814 1577 1735 576 C ATOM 1361 C THR A 231 19.547 -19.510 -42.483 1.00 78.49 C ANISOU 1361 C THR A 231 9192 11061 9571 1443 1623 808 C ATOM 1362 O THR A 231 19.031 -19.592 -41.368 1.00 76.88 O ANISOU 1362 O THR A 231 8963 10743 9507 1377 1433 877 O ATOM 1363 CB THR A 231 20.279 -21.535 -43.756 1.00 82.40 C ANISOU 1363 CB THR A 231 9917 11376 10016 1905 1944 518 C ATOM 1364 OG1 THR A 231 19.901 -22.488 -44.758 1.00 85.06 O ANISOU 1364 OG1 THR A 231 10571 11541 10207 2034 2043 278 O ATOM 1365 CG2 THR A 231 20.533 -22.257 -42.443 1.00 82.49 C ANISOU 1365 CG2 THR A 231 9815 11239 10288 2018 1826 605 C ATOM 1366 N ALA A 232 20.452 -18.587 -42.794 1.00 70.54 N ANISOU 1366 N ALA A 232 7970 10313 8518 1391 1738 927 N ATOM 1367 CA ALA A 232 20.981 -17.654 -41.800 1.00 68.00 C ANISOU 1367 CA ALA A 232 7366 10144 8325 1252 1631 1142 C ATOM 1368 C ALA A 232 19.901 -16.789 -41.150 1.00 64.12 C ANISOU 1368 C ALA A 232 6973 9577 7813 989 1382 1186 C ATOM 1369 O ALA A 232 19.818 -16.697 -39.922 1.00 62.23 O ANISOU 1369 O ALA A 232 6633 9297 7715 930 1216 1286 O ATOM 1370 CB ALA A 232 22.064 -16.780 -42.421 1.00 61.38 C ANISOU 1370 CB ALA A 232 6307 9590 7424 1209 1804 1257 C ATOM 1371 N THR A 233 19.077 -16.157 -41.978 1.00 52.21 N ANISOU 1371 N THR A 233 5664 8053 6121 844 1359 1112 N ATOM 1372 CA THR A 233 18.025 -15.282 -41.480 1.00 48.58 C ANISOU 1372 CA THR A 233 5299 7526 5635 620 1142 1143 C ATOM 1373 C THR A 233 17.016 -16.069 -40.640 1.00 48.13 C ANISOU 1373 C THR A 233 5384 7245 5660 635 985 1064 C ATOM 1374 O THR A 233 16.572 -15.603 -39.587 1.00 45.10 O ANISOU 1374 O THR A 233 4985 6817 5336 502 811 1129 O ATOM 1375 CB THR A 233 17.306 -14.557 -42.634 1.00 52.60 C ANISOU 1375 CB THR A 233 5993 8062 5930 490 1150 1084 C ATOM 1376 OG1 THR A 233 18.273 -13.970 -43.515 1.00 54.88 O ANISOU 1376 OG1 THR A 233 6487 8275 6092 618 1264 911 O ATOM 1377 CG2 THR A 233 16.383 -13.473 -42.095 1.00 52.96 C ANISOU 1377 CG2 THR A 233 5891 8330 5902 399 1260 1216 C ATOM 1378 N LEU A 234 16.667 -17.265 -41.107 1.00 53.82 N ANISOU 1378 N LEU A 234 6249 7821 6377 796 1054 925 N ATOM 1379 CA LEU A 234 15.794 -18.164 -40.355 1.00 54.09 C ANISOU 1379 CA LEU A 234 6414 7634 6502 809 921 863 C ATOM 1380 C LEU A 234 16.381 -18.451 -38.976 1.00 53.09 C ANISOU 1380 C LEU A 234 6102 7501 6569 862 854 999 C ATOM 1381 O LEU A 234 15.673 -18.401 -37.963 1.00 50.94 O ANISOU 1381 O LEU A 234 5854 7140 6362 762 694 1044 O ATOM 1382 CB LEU A 234 15.577 -19.474 -41.115 1.00 30.70 C ANISOU 1382 CB LEU A 234 3658 4504 3504 972 1012 686 C ATOM 1383 CG LEU A 234 14.732 -20.515 -40.379 1.00 31.52 C ANISOU 1383 CG LEU A 234 3909 4356 3713 977 880 629 C ATOM 1384 CD1 LEU A 234 13.329 -19.983 -40.130 1.00 29.20 C ANISOU 1384 CD1 LEU A 234 3718 4008 3369 749 697 621 C ATOM 1385 CD2 LEU A 234 14.686 -21.831 -41.145 1.00 35.88 C ANISOU 1385 CD2 LEU A 234 4678 4722 4233 1143 974 448 C ATOM 1386 N LYS A 235 17.680 -18.741 -38.951 1.00 45.95 N ANISOU 1386 N LYS A 235 5006 6705 5748 1023 980 1070 N ATOM 1387 CA LYS A 235 18.406 -18.920 -37.700 1.00 45.04 C ANISOU 1387 CA LYS A 235 4683 6620 5807 1074 906 1223 C ATOM 1388 C LYS A 235 18.222 -17.692 -36.821 1.00 40.95 C ANISOU 1388 C LYS A 235 4061 6211 5287 850 747 1353 C ATOM 1389 O LYS A 235 18.016 -17.809 -35.616 1.00 39.05 O ANISOU 1389 O LYS A 235 3793 5912 5131 804 600 1433 O ATOM 1390 CB LYS A 235 19.899 -19.145 -37.955 1.00 37.37 C ANISOU 1390 CB LYS A 235 3473 5805 4921 1267 1070 1296 C ATOM 1391 CG LYS A 235 20.264 -20.509 -38.512 1.00 41.58 C ANISOU 1391 CG LYS A 235 4089 6209 5501 1547 1225 1179 C ATOM 1392 CD LYS A 235 21.772 -20.629 -38.695 1.00 43.98 C ANISOU 1392 CD LYS A 235 4106 6697 5908 1754 1392 1271 C ATOM 1393 CE LYS A 235 22.178 -22.022 -39.155 1.00 47.80 C ANISOU 1393 CE LYS A 235 4678 7037 6445 2071 1560 1143 C ATOM 1394 NZ LYS A 235 23.657 -22.147 -39.301 1.00 51.29 N ANISOU 1394 NZ LYS A 235 4808 7678 7002 2301 1740 1237 N ATOM 1395 N VAL A 236 18.286 -16.514 -37.433 1.00 47.49 N ANISOU 1395 N VAL A 236 4852 7187 6005 710 778 1372 N ATOM 1396 CA VAL A 236 18.132 -15.268 -36.688 1.00 43.91 C ANISOU 1396 CA VAL A 236 4329 6815 5540 498 630 1478 C ATOM 1397 C VAL A 236 16.755 -15.140 -36.025 1.00 41.27 C ANISOU 1397 C VAL A 236 4176 6331 5175 379 468 1426 C ATOM 1398 O VAL A 236 16.668 -14.968 -34.806 1.00 39.16 O ANISOU 1398 O VAL A 236 3861 6051 4968 310 332 1506 O ATOM 1399 CB VAL A 236 18.418 -14.037 -37.571 1.00 42.86 C ANISOU 1399 CB VAL A 236 4163 6832 5290 366 693 1506 C ATOM 1400 CG1 VAL A 236 18.106 -12.755 -36.819 1.00 39.43 C ANISOU 1400 CG1 VAL A 236 3733 6414 4834 146 521 1579 C ATOM 1401 CG2 VAL A 236 19.865 -14.047 -38.035 1.00 45.31 C ANISOU 1401 CG2 VAL A 236 4228 7338 5650 443 844 1606 C ATOM 1402 N VAL A 237 15.684 -15.237 -36.812 1.00 47.22 N ANISOU 1402 N VAL A 237 5133 6981 5828 357 483 1295 N ATOM 1403 CA VAL A 237 14.339 -15.080 -36.250 1.00 44.93 C ANISOU 1403 CA VAL A 237 4985 6572 5515 246 344 1249 C ATOM 1404 C VAL A 237 14.000 -16.181 -35.239 1.00 45.38 C ANISOU 1404 C VAL A 237 5068 6497 5679 306 279 1260 C ATOM 1405 O VAL A 237 13.295 -15.932 -34.255 1.00 43.12 O ANISOU 1405 O VAL A 237 4801 6174 5408 210 161 1297 O ATOM 1406 CB VAL A 237 13.234 -14.954 -37.341 1.00 22.62 C ANISOU 1406 CB VAL A 237 2350 3677 2566 203 356 1117 C ATOM 1407 CG1 VAL A 237 13.819 -14.417 -38.640 1.00 23.94 C ANISOU 1407 CG1 VAL A 237 2507 3975 2612 127 405 1134 C ATOM 1408 CG2 VAL A 237 12.523 -16.277 -37.575 1.00 22.12 C ANISOU 1408 CG2 VAL A 237 2406 3499 2497 341 447 998 C ATOM 1409 N ILE A 238 14.523 -17.384 -35.468 1.00 43.00 N ANISOU 1409 N ILE A 238 4773 6119 5447 473 363 1232 N ATOM 1410 CA ILE A 238 14.296 -18.494 -34.547 1.00 43.45 C ANISOU 1410 CA ILE A 238 4869 6029 5612 537 302 1260 C ATOM 1411 C ILE A 238 15.023 -18.247 -33.227 1.00 41.34 C ANISOU 1411 C ILE A 238 4433 5846 5427 528 219 1422 C ATOM 1412 O ILE A 238 14.489 -18.523 -32.149 1.00 39.64 O ANISOU 1412 O ILE A 238 4258 5562 5241 469 113 1477 O ATOM 1413 CB ILE A 238 14.729 -19.850 -35.153 1.00 59.13 C ANISOU 1413 CB ILE A 238 6926 7882 7660 737 409 1185 C ATOM 1414 CG1 ILE A 238 13.775 -20.265 -36.276 1.00 61.50 C ANISOU 1414 CG1 ILE A 238 7451 8048 7868 712 439 1011 C ATOM 1415 CG2 ILE A 238 14.755 -20.936 -34.090 1.00 59.06 C ANISOU 1415 CG2 ILE A 238 6926 7729 7785 818 340 1263 C ATOM 1416 CD1 ILE A 238 14.065 -21.639 -36.842 1.00 65.37 C ANISOU 1416 CD1 ILE A 238 8061 8379 8398 905 542 904 C ATOM 1417 N GLN A 239 16.242 -17.721 -33.320 1.00 46.76 N ANISOU 1417 N GLN A 239 4931 6695 6142 575 265 1505 N ATOM 1418 CA GLN A 239 17.002 -17.339 -32.136 1.00 45.11 C ANISOU 1418 CA GLN A 239 4553 6593 5995 538 160 1661 C ATOM 1419 C GLN A 239 16.241 -16.290 -31.337 1.00 41.84 C ANISOU 1419 C GLN A 239 4188 6211 5498 333 27 1683 C ATOM 1420 O GLN A 239 16.072 -16.420 -30.123 1.00 40.49 O ANISOU 1420 O GLN A 239 4020 6021 5344 290 -89 1760 O ATOM 1421 CB GLN A 239 18.376 -16.790 -32.524 1.00 70.79 C ANISOU 1421 CB GLN A 239 7573 10035 9286 583 227 1745 C ATOM 1422 CG GLN A 239 19.413 -17.846 -32.853 1.00 74.10 C ANISOU 1422 CG GLN A 239 7877 10454 9821 823 347 1766 C ATOM 1423 CD GLN A 239 20.719 -17.241 -33.333 1.00 75.56 C ANISOU 1423 CD GLN A 239 7816 10858 10036 857 450 1840 C ATOM 1424 OE1 GLN A 239 21.036 -16.092 -33.022 1.00 73.97 O ANISOU 1424 OE1 GLN A 239 7491 10808 9805 685 377 1928 O ATOM 1425 NE2 GLN A 239 21.481 -18.011 -34.102 1.00 78.87 N ANISOU 1425 NE2 GLN A 239 8165 11290 10511 1076 628 1802 N ATOM 1426 N VAL A 240 15.778 -15.254 -32.033 1.00 31.16 N ANISOU 1426 N VAL A 240 2886 4906 4047 217 48 1615 N ATOM 1427 CA VAL A 240 15.026 -14.174 -31.404 1.00 28.45 C ANISOU 1427 CA VAL A 240 2606 4577 3626 48 -64 1615 C ATOM 1428 C VAL A 240 13.785 -14.695 -30.687 1.00 27.42 C ANISOU 1428 C VAL A 240 2616 4318 3482 26 -122 1573 C ATOM 1429 O VAL A 240 13.507 -14.306 -29.552 1.00 26.51 O ANISOU 1429 O VAL A 240 2513 4217 3340 -54 -220 1621 O ATOM 1430 CB VAL A 240 14.624 -13.100 -32.433 1.00 19.46 C ANISOU 1430 CB VAL A 240 1526 3474 2394 -46 -30 1546 C ATOM 1431 CG1 VAL A 240 13.695 -12.072 -31.804 1.00 19.61 C ANISOU 1431 CG1 VAL A 240 1637 3467 2346 -182 -139 1525 C ATOM 1432 CG2 VAL A 240 15.866 -12.425 -33.000 1.00 20.36 C ANISOU 1432 CG2 VAL A 240 1491 3733 2512 -70 20 1619 C ATOM 1433 N ASN A 241 13.049 -15.585 -31.346 1.00 43.33 N ANISOU 1433 N ASN A 241 4740 6214 5510 90 -60 1486 N ATOM 1434 CA ASN A 241 11.864 -16.177 -30.736 1.00 42.63 C ANISOU 1434 CA ASN A 241 4766 6008 5425 53 -106 1461 C ATOM 1435 C ASN A 241 12.201 -17.037 -29.519 1.00 42.86 C ANISOU 1435 C ASN A 241 4768 5997 5521 98 -157 1572 C ATOM 1436 O ASN A 241 11.492 -17.006 -28.514 1.00 41.55 O ANISOU 1436 O ASN A 241 4650 5811 5327 21 -219 1609 O ATOM 1437 CB ASN A 241 11.074 -16.991 -31.762 1.00 47.71 C ANISOU 1437 CB ASN A 241 5534 6522 6074 89 -48 1347 C ATOM 1438 CG ASN A 241 9.809 -17.591 -31.178 1.00 47.21 C ANISOU 1438 CG ASN A 241 5567 6344 6027 22 -98 1335 C ATOM 1439 OD1 ASN A 241 9.754 -18.785 -30.875 1.00 48.60 O ANISOU 1439 OD1 ASN A 241 5792 6397 6276 75 -97 1364 O ATOM 1440 ND2 ASN A 241 8.785 -16.761 -31.011 1.00 44.88 N ANISOU 1440 ND2 ASN A 241 5294 6087 5671 -93 -141 1303 N ATOM 1441 N THR A 242 13.288 -17.797 -29.613 1.00 57.24 N ANISOU 1441 N THR A 242 6507 7814 7426 231 -126 1632 N ATOM 1442 CA THR A 242 13.718 -18.661 -28.519 1.00 57.57 C ANISOU 1442 CA THR A 242 6522 7813 7541 295 -188 1757 C ATOM 1443 C THR A 242 14.102 -17.837 -27.294 1.00 55.80 C ANISOU 1443 C THR A 242 6217 7722 7263 202 -301 1869 C ATOM 1444 O THR A 242 13.786 -18.207 -26.163 1.00 55.25 O ANISOU 1444 O THR A 242 6195 7621 7176 168 -378 1953 O ATOM 1445 CB THR A 242 14.907 -19.549 -28.933 1.00 58.77 C ANISOU 1445 CB THR A 242 6580 7942 7809 489 -131 1800 C ATOM 1446 OG1 THR A 242 14.564 -20.297 -30.106 1.00 60.99 O ANISOU 1446 OG1 THR A 242 6960 8102 8113 580 -16 1668 O ATOM 1447 CG2 THR A 242 15.272 -20.510 -27.809 1.00 59.27 C ANISOU 1447 CG2 THR A 242 6646 7916 7957 572 -207 1935 C ATOM 1448 N PHE A 243 14.774 -16.713 -27.524 1.00 49.16 N ANISOU 1448 N PHE A 243 5268 7025 6385 148 -316 1871 N ATOM 1449 CA PHE A 243 15.167 -15.831 -26.430 1.00 47.95 C ANISOU 1449 CA PHE A 243 5059 6989 6170 41 -440 1956 C ATOM 1450 C PHE A 243 13.973 -15.103 -25.818 1.00 46.30 C ANISOU 1450 C PHE A 243 4987 6767 5838 -97 -480 1894 C ATOM 1451 O PHE A 243 13.761 -15.150 -24.606 1.00 45.98 O ANISOU 1451 O PHE A 243 4999 6734 5737 -144 -559 1955 O ATOM 1452 CB PHE A 243 16.199 -14.802 -26.902 1.00 45.16 C ANISOU 1452 CB PHE A 243 4555 6780 5826 0 -452 1980 C ATOM 1453 CG PHE A 243 17.593 -15.345 -27.025 1.00 46.90 C ANISOU 1453 CG PHE A 243 4581 7074 6165 124 -445 2090 C ATOM 1454 CD1 PHE A 243 18.262 -15.827 -25.913 1.00 47.31 C ANISOU 1454 CD1 PHE A 243 4557 7159 6261 162 -564 2229 C ATOM 1455 CD2 PHE A 243 18.246 -15.346 -28.246 1.00 48.34 C ANISOU 1455 CD2 PHE A 243 4651 7307 6411 207 -318 2061 C ATOM 1456 CE1 PHE A 243 19.543 -16.320 -26.023 1.00 49.03 C ANISOU 1456 CE1 PHE A 243 4569 7454 6608 295 -566 2341 C ATOM 1457 CE2 PHE A 243 19.529 -15.836 -28.360 1.00 50.24 C ANISOU 1457 CE2 PHE A 243 4684 7634 6773 342 -293 2164 C ATOM 1458 CZ PHE A 243 20.180 -16.322 -27.246 1.00 50.53 C ANISOU 1458 CZ PHE A 243 4625 7698 6876 392 -423 2306 C ATOM 1459 N MET A 244 13.194 -14.438 -26.664 1.00 42.49 N ANISOU 1459 N MET A 244 4562 6269 5313 -149 -421 1777 N ATOM 1460 CA MET A 244 12.155 -13.525 -26.196 1.00 41.24 C ANISOU 1460 CA MET A 244 4507 6112 5051 -256 -451 1711 C ATOM 1461 C MET A 244 10.862 -14.203 -25.746 1.00 41.09 C ANISOU 1461 C MET A 244 4591 6012 5011 -259 -423 1689 C ATOM 1462 O MET A 244 10.129 -13.657 -24.923 1.00 40.65 O ANISOU 1462 O MET A 244 4597 5982 4866 -326 -453 1680 O ATOM 1463 CB MET A 244 11.854 -12.468 -27.263 1.00 53.29 C ANISOU 1463 CB MET A 244 6054 7643 6551 -297 -410 1611 C ATOM 1464 CG MET A 244 13.050 -11.596 -27.596 1.00 53.29 C ANISOU 1464 CG MET A 244 5967 7732 6546 -347 -448 1645 C ATOM 1465 SD MET A 244 13.724 -10.803 -26.124 1.00 53.17 S ANISOU 1465 SD MET A 244 5941 7793 6466 -452 -596 1719 S ATOM 1466 CE MET A 244 15.472 -10.794 -26.514 1.00 54.39 C ANISOU 1466 CE MET A 244 5901 8041 6721 -399 -631 1862 C ATOM 1467 N SER A 245 10.578 -15.385 -26.282 1.00 54.18 N ANISOU 1467 N SER A 245 6269 7569 6747 -192 -361 1680 N ATOM 1468 CA SER A 245 9.337 -16.072 -25.939 1.00 54.09 C ANISOU 1468 CA SER A 245 6343 7476 6732 -223 -334 1667 C ATOM 1469 C SER A 245 9.552 -17.191 -24.926 1.00 54.82 C ANISOU 1469 C SER A 245 6459 7517 6854 -198 -362 1791 C ATOM 1470 O SER A 245 8.591 -17.726 -24.373 1.00 54.85 O ANISOU 1470 O SER A 245 6528 7471 6841 -252 -345 1815 O ATOM 1471 CB SER A 245 8.653 -16.624 -27.193 1.00 48.85 C ANISOU 1471 CB SER A 245 5722 6712 6127 -204 -271 1569 C ATOM 1472 OG SER A 245 9.422 -17.659 -27.779 1.00 48.99 O ANISOU 1472 OG SER A 245 5804 6650 6161 -257 -257 1572 O ATOM 1473 N PHE A 246 10.810 -17.544 -24.678 1.00 55.34 N ANISOU 1473 N PHE A 246 6461 7599 6966 -119 -407 1884 N ATOM 1474 CA PHE A 246 11.109 -18.663 -23.790 1.00 56.24 C ANISOU 1474 CA PHE A 246 6602 7648 7119 -75 -449 2021 C ATOM 1475 C PHE A 246 12.138 -18.325 -22.712 1.00 56.38 C ANISOU 1475 C PHE A 246 6555 7778 7088 -70 -558 2149 C ATOM 1476 O PHE A 246 11.782 -18.127 -21.553 1.00 56.15 O ANISOU 1476 O PHE A 246 6585 7803 6947 -149 -613 2216 O ATOM 1477 CB PHE A 246 11.558 -19.885 -24.597 1.00 39.22 C ANISOU 1477 CB PHE A 246 4450 5343 5106 56 -407 2025 C ATOM 1478 CG PHE A 246 11.753 -21.122 -23.768 1.00 40.33 C ANISOU 1478 CG PHE A 246 4643 5374 5305 110 -454 2171 C ATOM 1479 CD1 PHE A 246 10.666 -21.780 -23.216 1.00 40.33 C ANISOU 1479 CD1 PHE A 246 4766 5271 5287 23 -446 2210 C ATOM 1480 CD2 PHE A 246 13.021 -21.631 -23.549 1.00 41.55 C ANISOU 1480 CD2 PHE A 246 4715 5530 5540 247 -511 2285 C ATOM 1481 CE1 PHE A 246 10.843 -22.918 -22.454 1.00 41.50 C ANISOU 1481 CE1 PHE A 246 4980 5301 5485 61 -496 2365 C ATOM 1482 CE2 PHE A 246 13.204 -22.769 -22.789 1.00 42.70 C ANISOU 1482 CE2 PHE A 246 4920 5558 5744 308 -570 2435 C ATOM 1483 CZ PHE A 246 12.114 -23.414 -22.242 1.00 42.66 C ANISOU 1483 CZ PHE A 246 5065 5433 5709 210 -563 2478 C ATOM 1484 N LEU A 247 13.408 -18.261 -23.104 1.00 43.97 N ANISOU 1484 N LEU A 247 4858 6256 5595 21 -589 2185 N ATOM 1485 CA LEU A 247 14.516 -18.083 -22.162 1.00 44.45 C ANISOU 1485 CA LEU A 247 4827 6421 5641 36 -718 2327 C ATOM 1486 C LEU A 247 14.369 -16.873 -21.233 1.00 43.57 C ANISOU 1486 C LEU A 247 4746 6444 5366 -111 -812 2328 C ATOM 1487 O LEU A 247 14.276 -17.028 -20.014 1.00 43.85 O ANISOU 1487 O LEU A 247 4848 6511 5302 -157 -902 2427 O ATOM 1488 CB LEU A 247 15.846 -18.004 -22.917 1.00 41.62 C ANISOU 1488 CB LEU A 247 4285 6124 5404 144 -716 2348 C ATOM 1489 CG LEU A 247 16.220 -19.242 -23.736 1.00 43.34 C ANISOU 1489 CG LEU A 247 4460 6221 5785 337 -650 2384 C ATOM 1490 CD1 LEU A 247 17.524 -19.020 -24.488 1.00 44.47 C ANISOU 1490 CD1 LEU A 247 4396 6467 6035 447 -619 2398 C ATOM 1491 CD2 LEU A 247 16.318 -20.466 -22.842 1.00 44.19 C ANISOU 1491 CD2 LEU A 247 4612 6251 5928 405 -745 2548 C ATOM 1492 N PHE A 248 14.350 -15.679 -21.816 1.00 50.83 N ANISOU 1492 N PHE A 248 5636 7430 6244 -183 -793 2216 N ATOM 1493 CA PHE A 248 14.275 -14.429 -21.055 1.00 50.32 C ANISOU 1493 CA PHE A 248 5619 7467 6033 -316 -885 2189 C ATOM 1494 C PHE A 248 13.062 -14.322 -20.103 1.00 50.15 C ANISOU 1494 C PHE A 248 5768 7429 5856 -388 -869 2154 C ATOM 1495 O PHE A 248 13.242 -14.182 -18.883 1.00 50.76 O ANISOU 1495 O PHE A 248 5907 7573 5804 -444 -971 2225 O ATOM 1496 CB PHE A 248 14.364 -13.228 -22.015 1.00 76.42 C ANISOU 1496 CB PHE A 248 8883 10806 9348 -372 -854 2075 C ATOM 1497 CG PHE A 248 14.283 -11.889 -21.340 1.00 76.22 C ANISOU 1497 CG PHE A 248 8927 10849 9187 -507 -955 2031 C ATOM 1498 CD1 PHE A 248 15.386 -11.352 -20.699 1.00 76.97 C ANISOU 1498 CD1 PHE A 248 8964 11039 9243 -576 -1116 2123 C ATOM 1499 CD2 PHE A 248 13.111 -11.153 -21.377 1.00 75.62 C ANISOU 1499 CD2 PHE A 248 8975 10731 9027 -561 -898 1895 C ATOM 1500 CE1 PHE A 248 15.317 -10.115 -20.089 1.00 77.19 C ANISOU 1500 CE1 PHE A 248 9088 11105 9138 -710 -1221 2065 C ATOM 1501 CE2 PHE A 248 13.034 -9.917 -20.769 1.00 75.93 C ANISOU 1501 CE2 PHE A 248 9106 10802 8943 -668 -988 1839 C ATOM 1502 CZ PHE A 248 14.138 -9.396 -20.124 1.00 76.76 C ANISOU 1502 CZ PHE A 248 9181 10986 8998 -749 -1151 1916 C ATOM 1503 N PRO A 249 11.827 -14.411 -20.642 1.00 51.66 N ANISOU 1503 N PRO A 249 6031 7547 6053 -385 -740 2051 N ATOM 1504 CA PRO A 249 10.680 -14.183 -19.755 1.00 51.84 C ANISOU 1504 CA PRO A 249 6183 7585 5931 -449 -704 2019 C ATOM 1505 C PRO A 249 10.489 -15.290 -18.719 1.00 52.69 C ANISOU 1505 C PRO A 249 6349 7682 5991 -446 -719 2159 C ATOM 1506 O PRO A 249 9.965 -15.018 -17.642 1.00 53.37 O ANISOU 1506 O PRO A 249 6535 7834 5909 -508 -730 2176 O ATOM 1507 CB PRO A 249 9.495 -14.157 -20.723 1.00 29.81 C ANISOU 1507 CB PRO A 249 3405 4723 3199 -438 -572 1902 C ATOM 1508 CG PRO A 249 9.915 -15.025 -21.837 1.00 29.05 C ANISOU 1508 CG PRO A 249 3229 4539 3267 -361 -540 1915 C ATOM 1509 CD PRO A 249 11.391 -14.802 -21.996 1.00 29.75 C ANISOU 1509 CD PRO A 249 3221 4681 3401 -327 -626 1968 C ATOM 1510 N MET A 250 10.905 -16.513 -19.035 1.00 55.41 N ANISOU 1510 N MET A 250 6649 7937 6470 -370 -714 2257 N ATOM 1511 CA MET A 250 10.778 -17.613 -18.082 1.00 56.39 C ANISOU 1511 CA MET A 250 6840 8025 6561 -368 -742 2415 C ATOM 1512 C MET A 250 11.877 -17.587 -17.026 1.00 57.23 C ANISOU 1512 C MET A 250 6941 8223 6581 -370 -902 2553 C ATOM 1513 O MET A 250 11.675 -18.048 -15.903 1.00 58.17 O ANISOU 1513 O MET A 250 7158 8371 6573 -412 -943 2672 O ATOM 1514 CB MET A 250 10.747 -18.968 -18.789 1.00 47.76 C ANISOU 1514 CB MET A 250 5729 6769 5649 -281 -696 2471 C ATOM 1515 CG MET A 250 9.423 -19.280 -19.460 1.00 47.38 C ANISOU 1515 CG MET A 250 5727 6624 5650 -321 -563 2376 C ATOM 1516 SD MET A 250 8.025 -19.161 -18.324 1.00 47.75 S ANISOU 1516 SD MET A 250 5877 6740 5524 -458 -492 2405 S ATOM 1517 CE MET A 250 7.253 -17.643 -18.883 1.00 46.77 C ANISOU 1517 CE MET A 250 5716 6714 5342 -497 -415 2194 C ATOM 1518 N LEU A 251 13.041 -17.056 -17.386 1.00 39.52 N ANISOU 1518 N LEU A 251 4577 6037 4401 -334 -997 2548 N ATOM 1519 CA LEU A 251 14.099 -16.854 -16.407 1.00 42.14 C ANISOU 1519 CA LEU A 251 4881 6478 4651 -357 -1179 2672 C ATOM 1520 C LEU A 251 13.631 -15.794 -15.419 1.00 42.71 C ANISOU 1520 C LEU A 251 5091 6657 4478 -490 -1222 2610 C ATOM 1521 O LEU A 251 13.718 -15.979 -14.197 1.00 45.24 O ANISOU 1521 O LEU A 251 5512 7041 4636 -537 -1319 2720 O ATOM 1522 CB LEU A 251 15.398 -16.421 -17.087 1.00 51.48 C ANISOU 1522 CB LEU A 251 5878 7720 5963 -317 -1260 2668 C ATOM 1523 CG LEU A 251 16.638 -16.342 -16.194 1.00 52.50 C ANISOU 1523 CG LEU A 251 5916 7962 6069 -325 -1471 2825 C ATOM 1524 CD1 LEU A 251 16.894 -17.675 -15.508 1.00 53.64 C ANISOU 1524 CD1 LEU A 251 6084 8055 6242 -232 -1535 3019 C ATOM 1525 CD2 LEU A 251 17.845 -15.920 -17.010 1.00 52.48 C ANISOU 1525 CD2 LEU A 251 5683 8020 6239 -276 -1510 2831 C ATOM 1526 N VAL A 252 13.116 -14.692 -15.959 1.00 46.60 N ANISOU 1526 N VAL A 252 5606 7162 4938 -543 -1147 2431 N ATOM 1527 CA VAL A 252 12.546 -13.633 -15.130 1.00 47.21 C ANISOU 1527 CA VAL A 252 5833 7313 4791 -644 -1162 2335 C ATOM 1528 C VAL A 252 11.433 -14.168 -14.229 1.00 48.15 C ANISOU 1528 C VAL A 252 6098 7439 4757 -660 -1066 2371 C ATOM 1529 O VAL A 252 11.406 -13.895 -13.029 1.00 49.42 O ANISOU 1529 O VAL A 252 6391 7688 4699 -724 -1134 2407 O ATOM 1530 CB VAL A 252 12.002 -12.477 -15.991 1.00 34.78 C ANISOU 1530 CB VAL A 252 4265 5712 3238 -666 -1073 2138 C ATOM 1531 CG1 VAL A 252 11.243 -11.481 -15.128 1.00 35.10 C ANISOU 1531 CG1 VAL A 252 4483 5799 3054 -732 -1052 2023 C ATOM 1532 CG2 VAL A 252 13.142 -11.791 -16.729 1.00 34.50 C ANISOU 1532 CG2 VAL A 252 4107 5690 3311 -688 -1178 2117 C ATOM 1533 N ALA A 253 10.530 -14.948 -14.813 1.00 51.41 N ANISOU 1533 N ALA A 253 6489 7766 5279 -615 -909 2369 N ATOM 1534 CA ALA A 253 9.390 -15.493 -14.082 1.00 52.35 C ANISOU 1534 CA ALA A 253 6715 7895 5280 -647 -791 2414 C ATOM 1535 C ALA A 253 9.819 -16.458 -12.982 1.00 53.44 C ANISOU 1535 C ALA A 253 6923 8055 5326 -663 -879 2626 C ATOM 1536 O ALA A 253 9.213 -16.499 -11.914 1.00 54.71 O ANISOU 1536 O ALA A 253 7212 8290 5283 -724 -829 2675 O ATOM 1537 CB ALA A 253 8.418 -16.176 -15.039 1.00 44.34 C ANISOU 1537 CB ALA A 253 5641 6775 4434 -617 -634 2377 C ATOM 1538 N SER A 254 10.859 -17.241 -13.252 1.00 54.29 N ANISOU 1538 N SER A 254 6947 8105 5578 -601 -1004 2758 N ATOM 1539 CA SER A 254 11.358 -18.206 -12.279 1.00 55.53 C ANISOU 1539 CA SER A 254 7167 8263 5669 -599 -1108 2982 C ATOM 1540 C SER A 254 12.038 -17.496 -11.112 1.00 56.57 C ANISOU 1540 C SER A 254 7370 8543 5581 -658 -1290 3034 C ATOM 1541 O SER A 254 11.856 -17.875 -9.950 1.00 57.94 O ANISOU 1541 O SER A 254 7671 8772 5573 -702 -1354 3188 O ATOM 1542 CB SER A 254 12.325 -19.191 -12.937 1.00 58.61 C ANISOU 1542 CB SER A 254 7439 8521 6309 -481 -1175 3106 C ATOM 1543 OG SER A 254 13.442 -18.518 -13.490 1.00 57.99 O ANISOU 1543 OG SER A 254 7209 8480 6344 -420 -1287 3061 O ATOM 1544 N ILE A 255 12.825 -16.470 -11.426 1.00 47.23 N ANISOU 1544 N ILE A 255 6125 7424 4398 -676 -1377 2906 N ATOM 1545 CA ILE A 255 13.448 -15.650 -10.391 1.00 49.79 C ANISOU 1545 CA ILE A 255 6531 7882 4505 -760 -1566 2925 C ATOM 1546 C ILE A 255 12.382 -15.002 -9.511 1.00 50.23 C ANISOU 1546 C ILE A 255 6802 8016 4269 -847 -1466 2817 C ATOM 1547 O ILE A 255 12.427 -15.090 -8.275 1.00 53.43 O ANISOU 1547 O ILE A 255 7364 8517 4421 -910 -1553 2909 O ATOM 1548 CB ILE A 255 14.332 -14.551 -11.006 1.00 48.67 C ANISOU 1548 CB ILE A 255 6269 7773 4450 -784 -1684 2812 C ATOM 1549 CG1 ILE A 255 15.564 -15.169 -11.669 1.00 49.28 C ANISOU 1549 CG1 ILE A 255 6120 7823 4782 -695 -1798 2948 C ATOM 1550 CG2 ILE A 255 14.744 -13.547 -9.945 1.00 51.18 C ANISOU 1550 CG2 ILE A 255 6721 8214 4512 -909 -1864 2776 C ATOM 1551 CD1 ILE A 255 16.448 -14.159 -12.370 1.00 48.37 C ANISOU 1551 CD1 ILE A 255 5848 7747 4785 -727 -1882 2858 C ATOM 1552 N LEU A 256 11.416 -14.364 -10.166 1.00 53.71 N ANISOU 1552 N LEU A 256 7248 8419 4741 -840 -1279 2624 N ATOM 1553 CA LEU A 256 10.317 -13.701 -9.476 1.00 54.96 C ANISOU 1553 CA LEU A 256 7582 8647 4654 -885 -1142 2499 C ATOM 1554 C LEU A 256 9.525 -14.671 -8.609 1.00 56.10 C ANISOU 1554 C LEU A 256 7825 8831 4661 -901 -1028 2647 C ATOM 1555 O LEU A 256 9.081 -14.312 -7.525 1.00 58.16 O ANISOU 1555 O LEU A 256 8264 9204 4632 -954 -994 2633 O ATOM 1556 CB LEU A 256 9.388 -13.009 -10.477 1.00 50.23 C ANISOU 1556 CB LEU A 256 6929 7988 4167 -845 -960 2293 C ATOM 1557 CG LEU A 256 9.934 -11.755 -11.165 1.00 49.58 C ANISOU 1557 CG LEU A 256 6802 7871 4164 -850 -1050 2130 C ATOM 1558 CD1 LEU A 256 8.929 -11.212 -12.173 1.00 49.26 C ANISOU 1558 CD1 LEU A 256 6722 7767 4228 -799 -870 1953 C ATOM 1559 CD2 LEU A 256 10.298 -10.692 -10.141 1.00 51.18 C ANISOU 1559 CD2 LEU A 256 7179 8153 4114 -931 -1198 2056 C ATOM 1560 N ASN A 257 9.354 -15.900 -9.087 1.00 64.40 N ANISOU 1560 N ASN A 257 8772 9785 5911 -861 -965 2787 N ATOM 1561 CA ASN A 257 8.638 -16.920 -8.324 1.00 65.53 C ANISOU 1561 CA ASN A 257 9004 9945 5951 -898 -867 2960 C ATOM 1562 C ASN A 257 9.436 -17.434 -7.131 1.00 66.92 C ANISOU 1562 C ASN A 257 9298 10186 5943 -937 -1050 3176 C ATOM 1563 O ASN A 257 8.863 -17.797 -6.102 1.00 68.53 O ANISOU 1563 O ASN A 257 9652 10473 5913 -1001 -981 3287 O ATOM 1564 CB ASN A 257 8.213 -18.081 -9.225 1.00 59.52 C ANISOU 1564 CB ASN A 257 8120 9028 5466 -859 -766 3042 C ATOM 1565 CG ASN A 257 6.953 -17.776 -10.012 1.00 59.05 C ANISOU 1565 CG ASN A 257 7996 8948 5494 -863 -544 2881 C ATOM 1566 OD1 ASN A 257 5.848 -18.108 -9.584 1.00 60.09 O ANISOU 1566 OD1 ASN A 257 8169 9117 5548 -921 -379 2931 O ATOM 1567 ND2 ASN A 257 7.112 -17.132 -11.163 1.00 57.65 N ANISOU 1567 ND2 ASN A 257 7708 8721 5478 -807 -542 2699 N ATOM 1568 N THR A 258 10.758 -17.471 -7.274 1.00 68.93 N ANISOU 1568 N THR A 258 9477 10416 6298 -899 -1283 3246 N ATOM 1569 CA THR A 258 11.629 -17.818 -6.158 1.00 71.37 C ANISOU 1569 CA THR A 258 9885 10802 6431 -933 -1501 3451 C ATOM 1570 C THR A 258 11.493 -16.762 -5.065 1.00 73.21 C ANISOU 1570 C THR A 258 10321 11206 6290 -1031 -1540 3354 C ATOM 1571 O THR A 258 11.281 -17.083 -3.886 1.00 76.03 O ANISOU 1571 O THR A 258 10863 11660 6366 -1095 -1554 3488 O ATOM 1572 CB THR A 258 13.103 -17.908 -6.596 1.00 60.89 C ANISOU 1572 CB THR A 258 8394 9442 5299 -868 -1750 3525 C ATOM 1573 OG1 THR A 258 13.257 -18.956 -7.562 1.00 59.28 O ANISOU 1573 OG1 THR A 258 8023 9072 5427 -753 -1700 3602 O ATOM 1574 CG2 THR A 258 14.000 -18.190 -5.400 1.00 65.69 C ANISOU 1574 CG2 THR A 258 9094 10145 5721 -904 -2005 3744 C ATOM 1575 N VAL A 259 11.604 -15.499 -5.471 1.00 61.48 N ANISOU 1575 N VAL A 259 8818 9748 4793 -1044 -1554 3118 N ATOM 1576 CA VAL A 259 11.433 -14.375 -4.556 1.00 63.25 C ANISOU 1576 CA VAL A 259 9254 10101 4675 -1126 -1586 2974 C ATOM 1577 C VAL A 259 10.051 -14.410 -3.904 1.00 63.98 C ANISOU 1577 C VAL A 259 9515 10266 4529 -1144 -1323 2931 C ATOM 1578 O VAL A 259 9.903 -14.109 -2.720 1.00 67.53 O ANISOU 1578 O VAL A 259 10187 10845 4626 -1209 -1347 2953 O ATOM 1579 CB VAL A 259 11.636 -13.026 -5.280 1.00 59.45 C ANISOU 1579 CB VAL A 259 8731 9589 4269 -1130 -1609 2714 C ATOM 1580 CG1 VAL A 259 11.407 -11.864 -4.328 1.00 61.42 C ANISOU 1580 CG1 VAL A 259 9237 9938 4162 -1203 -1623 2539 C ATOM 1581 CG2 VAL A 259 13.031 -12.954 -5.884 1.00 59.43 C ANISOU 1581 CG2 VAL A 259 8553 9550 4477 -1137 -1866 2771 C ATOM 1582 N ILE A 260 9.047 -14.794 -4.687 1.00 61.68 N ANISOU 1582 N ILE A 260 9111 9902 4425 -1089 -1072 2874 N ATOM 1583 CA ILE A 260 7.680 -14.919 -4.196 1.00 62.41 C ANISOU 1583 CA ILE A 260 9297 10071 4345 -1102 -797 2851 C ATOM 1584 C ILE A 260 7.584 -15.992 -3.116 1.00 66.62 C ANISOU 1584 C ILE A 260 9951 10678 4685 -1167 -794 3118 C ATOM 1585 O ILE A 260 6.936 -15.793 -2.090 1.00 69.44 O ANISOU 1585 O ILE A 260 10487 11179 4718 -1214 -662 3117 O ATOM 1586 CB ILE A 260 6.698 -15.235 -5.345 1.00 57.01 C ANISOU 1586 CB ILE A 260 8423 9288 3951 -1045 -570 2784 C ATOM 1587 CG1 ILE A 260 6.373 -13.964 -6.130 1.00 53.56 C ANISOU 1587 CG1 ILE A 260 7932 8823 3596 -984 -505 2500 C ATOM 1588 CG2 ILE A 260 5.412 -15.837 -4.809 1.00 58.71 C ANISOU 1588 CG2 ILE A 260 8679 9585 4043 -1081 -309 2864 C ATOM 1589 CD1 ILE A 260 5.617 -14.220 -7.416 1.00 50.04 C ANISOU 1589 CD1 ILE A 260 7280 8268 3466 -927 -354 2438 C ATOM 1590 N ALA A 261 8.243 -17.124 -3.348 1.00 83.83 N ANISOU 1590 N ALA A 261 12039 12754 7058 -1161 -935 3349 N ATOM 1591 CA ALA A 261 8.261 -18.208 -2.373 1.00 85.35 C ANISOU 1591 CA ALA A 261 12353 12986 7091 -1222 -968 3635 C ATOM 1592 C ALA A 261 8.905 -17.747 -1.069 1.00 87.37 C ANISOU 1592 C ALA A 261 12837 13403 6958 -1287 -1150 3689 C ATOM 1593 O ALA A 261 8.336 -17.921 0.016 1.00 89.51 O ANISOU 1593 O ALA A 261 13302 13807 6901 -1360 -1047 3786 O ATOM 1594 CB ALA A 261 8.997 -19.413 -2.935 1.00 69.82 C ANISOU 1594 CB ALA A 261 10252 10846 5432 -1175 -1118 3856 C ATOM 1595 N ASN A 262 10.089 -17.151 -1.183 1.00 81.26 N ANISOU 1595 N ASN A 262 12038 12627 6209 -1272 -1421 3627 N ATOM 1596 CA ASN A 262 10.806 -16.656 -0.010 1.00 85.16 C ANISOU 1596 CA ASN A 262 12747 13269 6341 -1349 -1645 3668 C ATOM 1597 C ASN A 262 10.010 -15.620 0.786 1.00 86.56 C ANISOU 1597 C ASN A 262 13161 13597 6130 -1402 -1481 3454 C ATOM 1598 O ASN A 262 9.923 -15.698 2.013 1.00 90.72 O ANISOU 1598 O ASN A 262 13931 14270 6268 -1476 -1499 3548 O ATOM 1599 CB ASN A 262 12.168 -16.085 -0.412 1.00 91.54 C ANISOU 1599 CB ASN A 262 13448 14047 7286 -1340 -1962 3619 C ATOM 1600 CG ASN A 262 13.089 -17.135 -1.004 1.00 90.78 C ANISOU 1600 CG ASN A 262 13125 13828 7541 -1264 -2131 3843 C ATOM 1601 OD1 ASN A 262 13.018 -18.312 -0.650 1.00 90.02 O ANISOU 1601 OD1 ASN A 262 12943 13620 7642 -1205 -1993 3985 O ATOM 1602 ND2 ASN A 262 13.961 -16.712 -1.912 1.00 91.25 N ANISOU 1602 ND2 ASN A 262 13084 13904 7684 -1265 -2431 3874 N ATOM 1603 N LYS A 263 9.426 -14.660 0.078 1.00101.85 N ANISOU 1603 N LYS A 263 15036 15496 8168 -1353 -1317 3167 N ATOM 1604 CA LYS A 263 8.645 -13.602 0.712 1.00103.86 C ANISOU 1604 CA LYS A 263 15498 15865 8099 -1362 -1137 2928 C ATOM 1605 C LYS A 263 7.344 -14.129 1.312 1.00105.57 C ANISOU 1605 C LYS A 263 15800 16192 8122 -1368 -820 3016 C ATOM 1606 O LYS A 263 6.826 -13.566 2.276 1.00108.05 O ANISOU 1606 O LYS A 263 16351 16660 8043 -1393 -699 2925 O ATOM 1607 CB LYS A 263 8.355 -12.476 -0.281 1.00104.39 C ANISOU 1607 CB LYS A 263 15450 15836 8377 -1284 -1028 2629 C ATOM 1608 CG LYS A 263 9.568 -11.627 -0.622 1.00103.54 C ANISOU 1608 CG LYS A 263 15291 15641 8411 -1305 -1322 2522 C ATOM 1609 CD LYS A 263 10.068 -10.873 0.599 1.00104.77 C ANISOU 1609 CD LYS A 263 15722 15897 8188 -1401 -1549 2453 C ATOM 1610 CE LYS A 263 11.315 -10.065 0.278 1.00104.08 C ANISOU 1610 CE LYS A 263 15563 15726 8257 -1451 -1849 2358 C ATOM 1611 NZ LYS A 263 12.452 -10.940 -0.123 1.00105.31 N ANISOU 1611 NZ LYS A 263 15949 15981 8085 -1580 -2157 2378 N ATOM 1612 N LEU A 264 6.814 -15.201 0.732 1.00 84.56 N ANISOU 1612 N LEU A 264 12945 13451 5732 -1351 -680 3190 N ATOM 1613 CA LEU A 264 5.636 -15.856 1.284 1.00 86.88 C ANISOU 1613 CA LEU A 264 13285 13845 5878 -1389 -396 3326 C ATOM 1614 C LEU A 264 6.013 -16.525 2.595 1.00 92.56 C ANISOU 1614 C LEU A 264 14241 14693 6234 -1488 -507 3576 C ATOM 1615 O LEU A 264 5.261 -16.477 3.568 1.00 96.11 O ANISOU 1615 O LEU A 264 14873 15319 6323 -1533 -304 3588 O ATOM 1616 CB LEU A 264 5.080 -16.896 0.312 1.00111.96 C ANISOU 1616 CB LEU A 264 16215 16880 9445 -1379 -276 3476 C ATOM 1617 CG LEU A 264 3.859 -17.670 0.817 1.00113.59 C ANISOU 1617 CG LEU A 264 16442 17184 9535 -1451 15 3644 C ATOM 1618 CD1 LEU A 264 2.629 -16.773 0.866 1.00115.23 C ANISOU 1618 CD1 LEU A 264 16677 17558 9549 -1415 334 3416 C ATOM 1619 CD2 LEU A 264 3.601 -18.904 -0.033 1.00111.94 C ANISOU 1619 CD2 LEU A 264 16009 16801 9723 -1469 76 3801 C ATOM 1620 N THR A 265 7.186 -17.152 2.609 1.00 94.38 N ANISOU 1620 N THR A 265 14464 14843 6555 -1514 -827 3782 N ATOM 1621 CA THR A 265 7.719 -17.759 3.824 1.00 99.11 C ANISOU 1621 CA THR A 265 15293 15556 6811 -1604 -992 4038 C ATOM 1622 C THR A 265 7.886 -16.708 4.923 1.00102.33 C ANISOU 1622 C THR A 265 15988 16154 6740 -1647 -1044 3861 C ATOM 1623 O THR A 265 7.437 -16.899 6.059 1.00107.24 O ANISOU 1623 O THR A 265 16857 16945 6947 -1724 -980 3983 O ATOM 1624 CB THR A 265 9.069 -18.453 3.553 1.00113.04 C ANISOU 1624 CB THR A 265 16975 17198 8778 -1596 -1365 4269 C ATOM 1625 OG1 THR A 265 8.862 -19.599 2.717 1.00111.65 O ANISOU 1625 OG1 THR A 265 16714 16978 8731 -1552 -1604 4072 O ATOM 1626 CG2 THR A 265 9.719 -18.896 4.850 1.00111.25 C ANISOU 1626 CG2 THR A 265 16513 16767 8990 -1545 -1306 4447 C ATOM 1627 N VAL A 266 8.522 -15.593 4.569 1.00150.71 N ANISOU 1627 N VAL A 266 22097 22244 12920 -1604 -1162 3573 N ATOM 1628 CA VAL A 266 8.718 -14.483 5.496 1.00152.83 C ANISOU 1628 CA VAL A 266 22654 22653 12760 -1641 -1220 3353 C ATOM 1629 C VAL A 266 7.384 -13.947 6.017 1.00155.18 C ANISOU 1629 C VAL A 266 23113 23096 12753 -1613 -825 3185 C ATOM 1630 O VAL A 266 7.246 -13.648 7.204 1.00158.27 O ANISOU 1630 O VAL A 266 23811 23663 12662 -1668 -799 3166 O ATOM 1631 CB VAL A 266 9.518 -13.335 4.839 1.00124.08 C ANISOU 1631 CB VAL A 266 18946 18904 9294 -1609 -1414 3072 C ATOM 1632 CG1 VAL A 266 9.612 -12.137 5.772 1.00126.58 C ANISOU 1632 CG1 VAL A 266 19547 19314 9235 -1612 -1335 2751 C ATOM 1633 CG2 VAL A 266 10.906 -13.815 4.444 1.00122.84 C ANISOU 1633 CG2 VAL A 266 18742 18704 9228 -1675 -1855 3227 C ATOM 1634 N MET A 267 6.402 -13.841 5.126 1.00 95.26 N ANISOU 1634 N MET A 267 15311 15443 5441 -1524 -517 3071 N ATOM 1635 CA MET A 267 5.075 -13.357 5.498 1.00 96.09 C ANISOU 1635 CA MET A 267 15498 15682 5330 -1464 -123 2887 C ATOM 1636 C MET A 267 4.384 -14.297 6.481 1.00100.86 C ANISOU 1636 C MET A 267 16209 16475 5639 -1533 124 3127 C ATOM 1637 O MET A 267 3.781 -13.851 7.457 1.00103.66 O ANISOU 1637 O MET A 267 16714 17006 5666 -1500 420 2997 O ATOM 1638 CB MET A 267 4.200 -13.168 4.257 1.00138.79 C ANISOU 1638 CB MET A 267 20616 20970 11149 -1347 100 2710 C ATOM 1639 CG MET A 267 2.776 -12.743 4.574 1.00138.64 C ANISOU 1639 CG MET A 267 20429 21026 11223 -1335 471 2830 C ATOM 1640 SD MET A 267 1.727 -12.629 3.113 1.00138.65 S ANISOU 1640 SD MET A 267 20221 20995 11465 -1173 787 2510 S ATOM 1641 CE MET A 267 0.159 -12.195 3.861 1.00138.30 C ANISOU 1641 CE MET A 267 19943 21049 11557 -1219 1142 2749 C ATOM 1642 N VAL A 268 4.470 -15.597 6.213 1.00125.13 N ANISOU 1642 N VAL A 268 19213 19509 8823 -1625 3 3481 N ATOM 1643 CA VAL A 268 3.904 -16.605 7.102 1.00127.53 C ANISOU 1643 CA VAL A 268 19631 19972 8855 -1723 195 3763 C ATOM 1644 C VAL A 268 4.568 -16.528 8.473 1.00131.34 C ANISOU 1644 C VAL A 268 20490 20649 8766 -1768 138 3746 C ATOM 1645 O VAL A 268 3.906 -16.650 9.505 1.00134.89 O ANISOU 1645 O VAL A 268 21057 21228 8968 -1777 385 3837 O ATOM 1646 CB VAL A 268 4.056 -18.029 6.518 1.00105.52 C ANISOU 1646 CB VAL A 268 16713 17045 6334 -1806 23 4152 C ATOM 1647 CG1 VAL A 268 3.723 -19.085 7.562 1.00109.74 C ANISOU 1647 CG1 VAL A 268 17346 17673 6677 -1885 232 4415 C ATOM 1648 CG2 VAL A 268 3.173 -18.196 5.289 1.00 99.67 C ANISOU 1648 CG2 VAL A 268 15621 16087 6162 -1745 81 4128 C ATOM 1649 N HIS A 269 5.878 -16.302 8.477 1.00225.32 N ANISOU 1649 N HIS A 269 32550 32518 20546 -1754 -180 3575 N ATOM 1650 CA HIS A 269 6.624 -16.185 9.726 1.00229.47 C ANISOU 1650 CA HIS A 269 33406 33160 20623 -1744 -264 3466 C ATOM 1651 C HIS A 269 6.295 -14.897 10.477 1.00232.55 C ANISOU 1651 C HIS A 269 33969 33726 20665 -1671 113 3181 C ATOM 1652 O HIS A 269 6.496 -14.809 11.688 1.00236.69 O ANISOU 1652 O HIS A 269 34676 34406 20852 -1651 319 3223 O ATOM 1653 CB HIS A 269 8.126 -16.271 9.460 1.00258.31 C ANISOU 1653 CB HIS A 269 37149 36722 24276 -1760 -699 3322 C ATOM 1654 CG HIS A 269 8.559 -17.586 8.893 1.00258.60 C ANISOU 1654 CG HIS A 269 37031 36616 24609 -1806 -1080 3594 C ATOM 1655 ND1 HIS A 269 7.691 -18.642 8.721 1.00256.21 N ANISOU 1655 ND1 HIS A 269 36425 36171 24752 -1807 -1101 3795 N ATOM 1656 CD2 HIS A 269 9.767 -18.015 8.457 1.00261.21 C ANISOU 1656 CD2 HIS A 269 37458 36927 24865 -1838 -1454 3690 C ATOM 1657 CE1 HIS A 269 8.346 -19.667 8.204 1.00257.41 C ANISOU 1657 CE1 HIS A 269 36499 36216 25091 -1821 -1456 3999 C ATOM 1658 NE2 HIS A 269 9.607 -19.314 8.039 1.00260.43 N ANISOU 1658 NE2 HIS A 269 37107 36677 25169 -1843 -1677 3945 N ATOM 1659 N GLN A 270 5.791 -13.902 9.755 1.00118.93 N ANISOU 1659 N GLN A 270 19520 19309 6358 -1618 210 2892 N ATOM 1660 CA GLN A 270 5.426 -12.627 10.361 1.00121.78 C ANISOU 1660 CA GLN A 270 20025 19811 6436 -1510 574 2585 C ATOM 1661 C GLN A 270 4.149 -12.752 11.185 1.00120.74 C ANISOU 1661 C GLN A 270 19687 19805 6383 -1466 1043 2700 C ATOM 1662 O GLN A 270 3.078 -13.039 10.650 1.00120.26 O ANISOU 1662 O GLN A 270 19479 19745 6468 -1321 1345 2464 O ATOM 1663 CB GLN A 270 5.254 -11.553 9.284 1.00 20.00 C ATOM 1664 N PRO A 297 -5.991 -13.602 7.520 1.00194.64 N ANISOU 1664 N PRO A 297 27136 29558 17261 -963 3319 2553 N ATOM 1665 CA PRO A 297 -7.319 -14.141 7.211 1.00193.57 C ANISOU 1665 CA PRO A 297 26958 29471 17119 -1205 3298 2969 C ATOM 1666 C PRO A 297 -7.266 -15.117 6.041 1.00189.99 C ANISOU 1666 C PRO A 297 26104 28874 17210 -1296 3284 3155 C ATOM 1667 O PRO A 297 -6.379 -15.970 5.991 1.00187.30 O ANISOU 1667 O PRO A 297 25748 28337 17078 -1443 2995 3378 O ATOM 1668 CB PRO A 297 -8.116 -12.895 6.816 1.00150.53 C ANISOU 1668 CB PRO A 297 21587 24372 11236 -1227 3725 3061 C ATOM 1669 CG PRO A 297 -7.421 -11.770 7.500 1.00153.33 C ANISOU 1669 CG PRO A 297 21868 24852 11540 -972 4031 2702 C ATOM 1670 CD PRO A 297 -5.968 -12.130 7.480 1.00151.92 C ANISOU 1670 CD PRO A 297 21836 24425 11462 -816 3718 2371 C ATOM 1671 N GLY A 298 -8.206 -14.987 5.111 1.00143.51 N ANISOU 1671 N GLY A 298 19902 23082 11545 -1205 3585 3061 N ATOM 1672 CA GLY A 298 -8.224 -15.822 3.925 1.00140.78 C ANISOU 1672 CA GLY A 298 19179 22597 11716 -1285 3557 3192 C ATOM 1673 C GLY A 298 -7.235 -15.328 2.888 1.00137.20 C ANISOU 1673 C GLY A 298 18679 21822 11630 -1212 3191 3033 C ATOM 1674 O GLY A 298 -6.980 -16.000 1.886 1.00134.53 O ANISOU 1674 O GLY A 298 18191 21280 11645 -1335 2987 3200 O ATOM 1675 N ARG A 299 -6.678 -14.146 3.135 1.00163.59 N ANISOU 1675 N ARG A 299 22165 25115 14875 -1013 3114 2704 N ATOM 1676 CA ARG A 299 -5.705 -13.549 2.229 1.00160.74 C ANISOU 1676 CA ARG A 299 21788 24472 14812 -937 2782 2533 C ATOM 1677 C ARG A 299 -4.452 -14.411 2.138 1.00158.32 C ANISOU 1677 C ARG A 299 21651 23986 14516 -1084 2411 2716 C ATOM 1678 O ARG A 299 -3.874 -14.562 1.066 1.00155.27 O ANISOU 1678 O ARG A 299 21158 23365 14471 -1089 2151 2703 O ATOM 1679 CB ARG A 299 -5.345 -12.128 2.675 1.00200.18 C ANISOU 1679 CB ARG A 299 26964 29452 19642 -720 2769 2163 C ATOM 1680 CG ARG A 299 -4.431 -11.395 1.703 1.00199.33 C ANISOU 1680 CG ARG A 299 27187 29206 19342 -748 2415 2091 C ATOM 1681 CD ARG A 299 -4.339 -9.904 2.005 1.00199.19 C ANISOU 1681 CD ARG A 299 27270 29049 19363 -569 2295 1739 C ATOM 1682 NE ARG A 299 -3.605 -9.622 3.235 1.00199.46 N ANISOU 1682 NE ARG A 299 27663 29030 19091 -607 2026 1657 N ATOM 1683 CZ ARG A 299 -4.144 -9.077 4.321 1.00198.31 C ANISOU 1683 CZ ARG A 299 27605 28676 19067 -571 1730 1480 C ATOM 1684 NH1 ARG A 299 -5.428 -8.748 4.334 1.00196.83 N ANISOU 1684 NH1 ARG A 299 27188 28313 19286 -487 1676 1370 N ATOM 1685 NH2 ARG A 299 -3.397 -8.855 5.394 1.00198.70 N ANISOU 1685 NH2 ARG A 299 27971 28699 18827 -633 1480 1425 N ATOM 1686 N VAL A 300 -4.042 -14.981 3.266 1.00110.36 N ANISOU 1686 N VAL A 300 15839 18032 8063 -1193 2388 2889 N ATOM 1687 CA VAL A 300 -2.880 -15.862 3.300 1.00108.47 C ANISOU 1687 CA VAL A 300 15748 17641 7826 -1322 2038 3096 C ATOM 1688 C VAL A 300 -3.152 -17.151 2.526 1.00106.06 C ANISOU 1688 C VAL A 300 15210 17193 7895 -1463 1981 3383 C ATOM 1689 O VAL A 300 -2.286 -17.648 1.803 1.00103.11 O ANISOU 1689 O VAL A 300 14797 16587 7795 -1485 1681 3442 O ATOM 1690 CB VAL A 300 -2.477 -16.204 4.747 1.00102.57 C ANISOU 1690 CB VAL A 300 15326 17074 6571 -1419 2041 3257 C ATOM 1691 CG1 VAL A 300 -1.260 -17.117 4.763 1.00102.46 C ANISOU 1691 CG1 VAL A 300 15410 16910 6608 -1562 1698 3548 C ATOM 1692 CG2 VAL A 300 -2.202 -14.932 5.532 1.00104.38 C ANISOU 1692 CG2 VAL A 300 15846 17389 6423 -1296 2001 2961 C ATOM 1693 N GLN A 301 -4.363 -17.682 2.677 1.00129.47 N ANISOU 1693 N GLN A 301 18018 20295 10878 -1556 2276 3555 N ATOM 1694 CA GLN A 301 -4.773 -18.887 1.962 1.00127.70 C ANISOU 1694 CA GLN A 301 17593 19927 11000 -1711 2235 3824 C ATOM 1695 C GLN A 301 -4.746 -18.661 0.453 1.00125.02 C ANISOU 1695 C GLN A 301 16982 19382 11139 -1633 2143 3660 C ATOM 1696 O GLN A 301 -4.109 -19.414 -0.290 1.00122.43 O ANISOU 1696 O GLN A 301 16594 18811 11112 -1690 1906 3769 O ATOM 1697 CB GLN A 301 -6.180 -19.311 2.393 1.00146.34 C ANISOU 1697 CB GLN A 301 19831 22494 13278 -1854 2580 4042 C ATOM 1698 CG GLN A 301 -6.341 -19.569 3.885 1.00149.41 C ANISOU 1698 CG GLN A 301 20476 23056 13235 -1994 2659 4311 C ATOM 1699 CD GLN A 301 -5.985 -20.991 4.286 1.00151.38 C ANISOU 1699 CD GLN A 301 20684 23651 13181 -2003 3093 4312 C ATOM 1700 OE1 GLN A 301 -6.186 -21.391 5.433 1.00152.07 O ANISOU 1700 OE1 GLN A 301 20471 23830 13478 -1981 3351 4244 O ATOM 1701 NE2 GLN A 301 -5.458 -21.763 3.340 1.00152.49 N ANISOU 1701 NE2 GLN A 301 21122 23962 12854 -2023 3169 4376 N ATOM 1702 N ALA A 302 -5.439 -17.615 0.011 1.00 98.04 N ANISOU 1702 N ALA A 302 13412 16061 7777 -1488 2332 3397 N ATOM 1703 CA ALA A 302 -5.500 -17.274 -1.407 1.00 95.85 C ANISOU 1703 CA ALA A 302 12887 15612 7919 -1404 2253 3229 C ATOM 1704 C ALA A 302 -4.115 -16.969 -1.968 1.00 93.30 C ANISOU 1704 C ALA A 302 12671 15047 7731 -1331 1898 3111 C ATOM 1705 O ALA A 302 -3.808 -17.315 -3.111 1.00 90.75 O ANISOU 1705 O ALA A 302 12201 14516 7766 -1345 1736 3120 O ATOM 1706 CB ALA A 302 -6.437 -16.095 -1.629 1.00138.19 C ANISOU 1706 CB ALA A 302 18107 21128 13271 -1232 2498 2964 C ATOM 1707 N LEU A 303 -3.282 -16.325 -1.157 1.00107.83 N ANISOU 1707 N LEU A 303 14772 16926 9273 -1261 1782 3002 N ATOM 1708 CA LEU A 303 -1.918 -16.002 -1.559 1.00105.80 C ANISOU 1708 CA LEU A 303 14618 16476 9105 -1206 1449 2902 C ATOM 1709 C LEU A 303 -1.089 -17.263 -1.773 1.00103.90 C ANISOU 1709 C LEU A 303 14405 16071 9003 -1324 1201 3163 C ATOM 1710 O LEU A 303 -0.412 -17.397 -2.790 1.00101.41 O ANISOU 1710 O LEU A 303 13999 15552 8980 -1291 988 3127 O ATOM 1711 CB LEU A 303 -1.246 -15.092 -0.529 1.00 92.44 C ANISOU 1711 CB LEU A 303 13205 14878 7042 -1130 1378 2732 C ATOM 1712 CG LEU A 303 -1.156 -13.606 -0.887 1.00 89.90 C ANISOU 1712 CG LEU A 303 12877 14520 6763 -963 1384 2388 C ATOM 1713 CD1 LEU A 303 -2.486 -13.072 -1.398 1.00 90.29 C ANISOU 1713 CD1 LEU A 303 12727 14672 6906 -863 1707 2260 C ATOM 1714 CD2 LEU A 303 -0.679 -12.798 0.310 1.00 92.17 C ANISOU 1714 CD2 LEU A 303 13481 14886 6654 -918 1304 2231 C ATOM 1715 N ARG A 304 -1.145 -18.181 -0.811 1.00 95.48 N ANISOU 1715 N ARG A 304 13468 15089 7722 -1452 1234 3430 N ATOM 1716 CA ARG A 304 -0.427 -19.448 -0.919 1.00 94.05 C ANISOU 1716 CA ARG A 304 13318 14733 7684 -1548 1005 3697 C ATOM 1717 C ARG A 304 -0.890 -20.216 -2.152 1.00 91.99 C ANISOU 1717 C ARG A 304 12815 14286 7852 -1591 1024 3768 C ATOM 1718 O ARG A 304 -0.071 -20.752 -2.913 1.00 89.76 O ANISOU 1718 O ARG A 304 12496 13780 7831 -1577 794 3826 O ATOM 1719 CB ARG A 304 -0.638 -20.296 0.337 1.00109.64 C ANISOU 1719 CB ARG A 304 15485 16828 9347 -1685 1048 3994 C ATOM 1720 CG ARG A 304 0.170 -21.584 0.352 1.00108.54 C ANISOU 1720 CG ARG A 304 15442 16505 9295 -1741 749 4251 C ATOM 1721 CD ARG A 304 -0.203 -22.467 1.533 1.00110.53 C ANISOU 1721 CD ARG A 304 15928 16883 9186 -1864 753 4542 C ATOM 1722 NE ARG A 304 -0.006 -21.796 2.815 1.00112.30 N ANISOU 1722 NE ARG A 304 16329 17387 8954 -1854 917 4427 N ATOM 1723 CZ ARG A 304 1.126 -21.827 3.511 1.00114.19 C ANISOU 1723 CZ ARG A 304 16839 17763 8784 -1916 841 4584 C ATOM 1724 NH1 ARG A 304 2.174 -22.496 3.048 1.00115.05 N ANISOU 1724 NH1 ARG A 304 17058 17754 8904 -1988 590 4880 N ATOM 1725 NH2 ARG A 304 1.211 -21.188 4.670 1.00115.97 N ANISOU 1725 NH2 ARG A 304 17238 18241 8586 -1897 1009 4443 N ATOM 1726 N ARG A 305 -2.208 -20.261 -2.343 1.00 88.25 N ANISOU 1726 N ARG A 305 12172 13909 7449 -1638 1297 3753 N ATOM 1727 CA ARG A 305 -2.789 -20.880 -3.528 1.00 86.26 C ANISOU 1727 CA ARG A 305 11690 13494 7591 -1695 1316 3796 C ATOM 1728 C ARG A 305 -2.188 -20.287 -4.797 1.00 81.27 C ANISOU 1728 C ARG A 305 10944 12696 7241 -1557 1155 3552 C ATOM 1729 O ARG A 305 -1.693 -21.018 -5.650 1.00 79.21 O ANISOU 1729 O ARG A 305 10605 12212 7278 -1577 1004 3602 O ATOM 1730 CB ARG A 305 -4.313 -20.723 -3.543 1.00104.17 C ANISOU 1730 CB ARG A 305 13769 15936 9876 -1768 1633 3804 C ATOM 1731 CG ARG A 305 -5.045 -21.644 -2.582 1.00108.56 C ANISOU 1731 CG ARG A 305 14396 16645 10206 -1945 1816 4091 C ATOM 1732 CD ARG A 305 -6.504 -21.815 -2.984 1.00110.46 C ANISOU 1732 CD ARG A 305 14390 17063 10516 -2025 2130 4107 C ATOM 1733 NE ARG A 305 -7.268 -20.577 -2.849 1.00110.63 N ANISOU 1733 NE ARG A 305 14335 17312 10390 -1858 2336 3842 N ATOM 1734 CZ ARG A 305 -8.031 -20.283 -1.802 1.00113.26 C ANISOU 1734 CZ ARG A 305 14482 17888 10665 -1881 2656 3843 C ATOM 1735 NH1 ARG A 305 -8.138 -21.140 -0.796 1.00116.01 N ANISOU 1735 NH1 ARG A 305 14694 18296 11089 -2095 2805 4109 N ATOM 1736 NH2 ARG A 305 -8.691 -19.134 -1.762 1.00113.47 N ANISOU 1736 NH2 ARG A 305 14456 18094 10566 -1689 2830 3585 N ATOM 1737 N GLY A 306 -2.217 -18.962 -4.903 1.00 70.12 N ANISOU 1737 N GLY A 306 9539 11385 5718 -1416 1190 3290 N ATOM 1738 CA GLY A 306 -1.656 -18.273 -6.053 1.00 65.44 C ANISOU 1738 CA GLY A 306 8863 10650 5348 -1290 1039 3064 C ATOM 1739 C GLY A 306 -0.189 -18.588 -6.278 1.00 63.94 C ANISOU 1739 C GLY A 306 8772 10280 5241 -1269 742 3118 C ATOM 1740 O GLY A 306 0.255 -18.722 -7.419 1.00 60.80 O ANISOU 1740 O GLY A 306 8264 9703 5133 -1229 615 3062 O ATOM 1741 N VAL A 307 0.559 -18.710 -5.186 1.00 63.19 N ANISOU 1741 N VAL A 307 8882 10246 4883 -1292 633 3228 N ATOM 1742 CA VAL A 307 1.977 -19.045 -5.252 1.00 62.60 C ANISOU 1742 CA VAL A 307 8885 10031 4871 -1268 345 3308 C ATOM 1743 C VAL A 307 2.189 -20.420 -5.872 1.00 62.54 C ANISOU 1743 C VAL A 307 8798 9820 5146 -1319 261 3510 C ATOM 1744 O VAL A 307 2.923 -20.560 -6.855 1.00 59.80 O ANISOU 1744 O VAL A 307 8369 9300 5055 -1248 101 3463 O ATOM 1745 CB VAL A 307 2.631 -19.018 -3.856 1.00 65.23 C ANISOU 1745 CB VAL A 307 9451 10486 4847 -1306 240 3433 C ATOM 1746 CG1 VAL A 307 4.030 -19.615 -3.908 1.00 65.39 C ANISOU 1746 CG1 VAL A 307 9512 10367 4964 -1284 -66 3565 C ATOM 1747 CG2 VAL A 307 2.670 -17.600 -3.315 1.00 65.27 C ANISOU 1747 CG2 VAL A 307 9574 10656 4569 -1247 282 3201 C ATOM 1748 N LEU A 308 1.544 -21.432 -5.294 1.00 68.05 N ANISOU 1748 N LEU A 308 9527 10533 5795 -1442 380 3733 N ATOM 1749 CA LEU A 308 1.670 -22.797 -5.802 1.00 68.59 C ANISOU 1749 CA LEU A 308 9558 10381 6121 -1503 302 3934 C ATOM 1750 C LEU A 308 1.216 -22.902 -7.260 1.00 64.95 C ANISOU 1750 C LEU A 308 8902 9765 6011 -1477 338 3789 C ATOM 1751 O LEU A 308 1.894 -23.522 -8.089 1.00 63.41 O ANISOU 1751 O LEU A 308 8678 9349 6066 -1430 184 3813 O ATOM 1752 CB LEU A 308 0.895 -23.782 -4.921 1.00131.07 C ANISOU 1752 CB LEU A 308 17548 18343 13909 -1671 438 4205 C ATOM 1753 CG LEU A 308 1.622 -24.357 -3.700 1.00132.57 C ANISOU 1753 CG LEU A 308 17958 18563 13848 -1719 316 4468 C ATOM 1754 CD1 LEU A 308 2.925 -25.030 -4.114 1.00131.39 C ANISOU 1754 CD1 LEU A 308 17849 18160 13911 -1648 40 4594 C ATOM 1755 CD2 LEU A 308 1.876 -23.294 -2.644 1.00133.84 C ANISOU 1755 CD2 LEU A 308 18258 18961 13632 -1667 301 4375 C ATOM 1756 N VAL A 309 0.078 -22.281 -7.565 1.00 78.43 N ANISOU 1756 N VAL A 309 10479 11594 7727 -1497 539 3638 N ATOM 1757 CA VAL A 309 -0.448 -22.245 -8.927 1.00 77.00 C ANISOU 1757 CA VAL A 309 10114 11296 7846 -1479 566 3491 C ATOM 1758 C VAL A 309 0.574 -21.678 -9.895 1.00 74.91 C ANISOU 1758 C VAL A 309 9822 10913 7728 -1329 390 3306 C ATOM 1759 O VAL A 309 0.941 -22.332 -10.864 1.00 73.50 O ANISOU 1759 O VAL A 309 9591 10531 7802 -1310 288 3302 O ATOM 1760 CB VAL A 309 -1.719 -21.381 -9.035 1.00 68.79 C ANISOU 1760 CB VAL A 309 8926 10443 6769 -1487 791 3340 C ATOM 1761 CG1 VAL A 309 -2.083 -21.154 -10.498 1.00 67.23 C ANISOU 1761 CG1 VAL A 309 8554 10137 6854 -1432 765 3152 C ATOM 1762 CG2 VAL A 309 -2.863 -22.032 -8.310 1.00 70.70 C ANISOU 1762 CG2 VAL A 309 9124 10789 6950 -1656 988 3529 C ATOM 1763 N LEU A 310 1.032 -20.461 -9.618 1.00 55.85 N ANISOU 1763 N LEU A 310 7452 8624 5144 -1230 358 3153 N ATOM 1764 CA LEU A 310 1.956 -19.768 -10.506 1.00 52.40 C ANISOU 1764 CA LEU A 310 6978 8104 4829 -1107 207 2980 C ATOM 1765 C LEU A 310 3.253 -20.549 -10.693 1.00 52.60 C ANISOU 1765 C LEU A 310 7051 7963 4972 -1069 -1 3104 C ATOM 1766 O LEU A 310 3.794 -20.612 -11.800 1.00 50.08 O ANISOU 1766 O LEU A 310 6649 7504 4877 -997 -88 3022 O ATOM 1767 CB LEU A 310 2.249 -18.366 -9.977 1.00 58.94 C ANISOU 1767 CB LEU A 310 7877 9086 5433 -1037 196 2820 C ATOM 1768 CG LEU A 310 2.980 -17.434 -10.941 1.00 57.40 C ANISOU 1768 CG LEU A 310 7629 8821 5358 -935 65 2632 C ATOM 1769 CD1 LEU A 310 2.184 -17.263 -12.225 1.00 56.16 C ANISOU 1769 CD1 LEU A 310 7312 8583 5443 -904 140 2498 C ATOM 1770 CD2 LEU A 310 3.221 -16.100 -10.273 1.00 58.65 C ANISOU 1770 CD2 LEU A 310 7889 9113 5284 -893 53 2482 C ATOM 1771 N ARG A 311 3.742 -21.145 -9.608 1.00 53.12 N ANISOU 1771 N ARG A 311 7249 8053 4880 -1109 -77 3307 N ATOM 1772 CA ARG A 311 4.923 -22.000 -9.676 1.00 53.95 C ANISOU 1772 CA ARG A 311 7392 8007 5101 -1055 -277 3454 C ATOM 1773 C ARG A 311 4.680 -23.140 -10.660 1.00 53.40 C ANISOU 1773 C ARG A 311 7263 7706 5321 -1062 -269 3522 C ATOM 1774 O ARG A 311 5.498 -23.398 -11.554 1.00 51.84 O ANISOU 1774 O ARG A 311 7013 7352 5330 -957 -387 3489 O ATOM 1775 CB ARG A 311 5.261 -22.563 -8.293 1.00 73.79 C ANISOU 1775 CB ARG A 311 10067 10590 7380 -1107 -357 3688 C ATOM 1776 CG ARG A 311 6.539 -23.388 -8.248 1.00 73.71 C ANISOU 1776 CG ARG A 311 10090 10442 7476 -1030 -583 3859 C ATOM 1777 CD ARG A 311 6.742 -24.016 -6.877 1.00 75.68 C ANISOU 1777 CD ARG A 311 10508 10725 7523 -1107 -640 4141 C ATOM 1778 NE ARG A 311 6.686 -23.027 -5.804 1.00 77.04 N ANISOU 1778 NE ARG A 311 10797 11143 7331 -1168 -620 4123 N ATOM 1779 CZ ARG A 311 6.810 -23.315 -4.512 1.00 78.96 C ANISOU 1779 CZ ARG A 311 11211 11473 7318 -1231 -695 4344 C ATOM 1780 NH1 ARG A 311 7.001 -24.569 -4.124 1.00 79.70 N ANISOU 1780 NH1 ARG A 311 11370 11418 7496 -1242 -798 4618 N ATOM 1781 NH2 ARG A 311 6.743 -22.347 -3.608 1.00 80.33 N ANISOU 1781 NH2 ARG A 311 11509 11874 7141 -1282 -668 4290 N ATOM 1782 N ALA A 312 3.539 -23.806 -10.498 1.00 53.69 N ANISOU 1782 N ALA A 312 7307 7724 5368 -1190 -123 3610 N ATOM 1783 CA ALA A 312 3.159 -24.914 -11.370 1.00 53.60 C ANISOU 1783 CA ALA A 312 7264 7482 5619 -1233 -115 3667 C ATOM 1784 C ALA A 312 3.045 -24.489 -12.834 1.00 49.51 C ANISOU 1784 C ALA A 312 6612 6882 5318 -1160 -106 3429 C ATOM 1785 O ALA A 312 3.413 -25.241 -13.736 1.00 48.64 O ANISOU 1785 O ALA A 312 6500 6555 5427 -1105 -187 3421 O ATOM 1786 CB ALA A 312 1.856 -25.541 -10.894 1.00 56.39 C ANISOU 1786 CB ALA A 312 7631 7866 5931 -1419 44 3802 C ATOM 1787 N VAL A 313 2.538 -23.281 -13.059 1.00 47.30 N ANISOU 1787 N VAL A 313 6236 6771 4965 -1151 -8 3238 N ATOM 1788 CA VAL A 313 2.365 -22.751 -14.407 1.00 43.66 C ANISOU 1788 CA VAL A 313 5656 6257 4674 -1087 -4 3020 C ATOM 1789 C VAL A 313 3.712 -22.467 -15.063 1.00 41.68 C ANISOU 1789 C VAL A 313 5404 5923 4508 -936 -151 2942 C ATOM 1790 O VAL A 313 3.926 -22.795 -16.233 1.00 39.84 O ANISOU 1790 O VAL A 313 5130 5538 4472 -881 -189 2859 O ATOM 1791 CB VAL A 313 1.512 -21.466 -14.402 1.00 42.02 C ANISOU 1791 CB VAL A 313 5358 6250 4358 -1087 118 2846 C ATOM 1792 CG1 VAL A 313 1.434 -20.873 -15.802 1.00 38.45 C ANISOU 1792 CG1 VAL A 313 4801 5741 4065 -1010 93 2637 C ATOM 1793 CG2 VAL A 313 0.120 -21.759 -13.867 1.00 44.09 C ANISOU 1793 CG2 VAL A 313 5570 6609 4573 -1225 288 2915 C ATOM 1794 N VAL A 314 4.618 -21.859 -14.304 1.00 47.42 N ANISOU 1794 N VAL A 314 6177 6761 5079 -876 -234 2970 N ATOM 1795 CA VAL A 314 5.961 -21.580 -14.801 1.00 46.21 C ANISOU 1795 CA VAL A 314 5992 6563 5001 -747 -374 2921 C ATOM 1796 C VAL A 314 6.695 -22.874 -15.144 1.00 47.19 C ANISOU 1796 C VAL A 314 6140 6481 5308 -678 -468 3051 C ATOM 1797 O VAL A 314 7.240 -23.019 -16.244 1.00 45.48 O ANISOU 1797 O VAL A 314 5860 6150 5271 -580 -497 2955 O ATOM 1798 CB VAL A 314 6.793 -20.771 -13.783 1.00 42.31 C ANISOU 1798 CB VAL A 314 5546 6231 4299 -726 -472 2954 C ATOM 1799 CG1 VAL A 314 8.233 -20.638 -14.257 1.00 41.74 C ANISOU 1799 CG1 VAL A 314 5411 6117 4332 -609 -629 2948 C ATOM 1800 CG2 VAL A 314 6.173 -19.402 -13.562 1.00 40.97 C ANISOU 1800 CG2 VAL A 314 5370 6231 3965 -761 -389 2784 C ATOM 1801 N ILE A 315 6.697 -23.815 -14.202 1.00 45.46 N ANISOU 1801 N ILE A 315 6025 6208 5037 -721 -508 3269 N ATOM 1802 CA ILE A 315 7.355 -25.101 -14.414 1.00 47.01 C ANISOU 1802 CA ILE A 315 6266 6183 5412 -637 -603 3406 C ATOM 1803 C ILE A 315 6.777 -25.831 -15.626 1.00 45.62 C ANISOU 1803 C ILE A 315 6085 5793 5457 -646 -534 3322 C ATOM 1804 O ILE A 315 7.521 -26.337 -16.469 1.00 44.90 O ANISOU 1804 O ILE A 315 5979 5534 5548 -512 -590 3281 O ATOM 1805 CB ILE A 315 7.258 -26.009 -13.168 1.00 51.32 C ANISOU 1805 CB ILE A 315 6949 6694 5858 -692 -668 3682 C ATOM 1806 CG1 ILE A 315 7.982 -25.368 -11.983 1.00 53.15 C ANISOU 1806 CG1 ILE A 315 7230 6669 6295 -570 -782 3821 C ATOM 1807 CG2 ILE A 315 7.845 -27.383 -13.458 1.00 52.94 C ANISOU 1807 CG2 ILE A 315 7228 6918 5968 -882 -532 3764 C ATOM 1808 CD1 ILE A 315 7.901 -26.177 -10.705 1.00 52.54 C ANISOU 1808 CD1 ILE A 315 7055 6601 6306 -369 -914 3788 C ATOM 1809 N ALA A 316 5.451 -25.868 -15.713 1.00 65.59 N ANISOU 1809 N ALA A 316 8620 8335 7964 -801 -412 3289 N ATOM 1810 CA ALA A 316 4.777 -26.525 -16.829 1.00 65.80 C ANISOU 1810 CA ALA A 316 8647 8171 8182 -846 -365 3203 C ATOM 1811 C ALA A 316 5.126 -25.865 -18.159 1.00 64.60 C ANISOU 1811 C ALA A 316 8400 8013 8131 -735 -364 2965 C ATOM 1812 O ALA A 316 5.327 -26.549 -19.161 1.00 65.13 O ANISOU 1812 O ALA A 316 8498 7878 8370 -675 -387 2896 O ATOM 1813 CB ALA A 316 3.272 -26.530 -16.618 1.00 45.52 C ANISOU 1813 CB ALA A 316 6060 5671 5564 -1049 -243 3218 C ATOM 1814 N PHE A 317 5.197 -24.537 -18.162 1.00 49.82 N ANISOU 1814 N PHE A 317 6430 6356 6141 -708 -336 2840 N ATOM 1815 CA PHE A 317 5.545 -23.796 -19.369 1.00 48.71 C ANISOU 1815 CA PHE A 317 6203 6232 6070 -615 -333 2634 C ATOM 1816 C PHE A 317 6.954 -24.157 -19.817 1.00 48.96 C ANISOU 1816 C PHE A 317 6233 6163 6207 -442 -420 2641 C ATOM 1817 O PHE A 317 7.178 -24.479 -20.986 1.00 49.23 O ANISOU 1817 O PHE A 317 6260 6069 6374 -364 -411 2527 O ATOM 1818 CB PHE A 317 5.434 -22.287 -19.131 1.00 54.60 C ANISOU 1818 CB PHE A 317 6869 7211 6665 -623 -302 2528 C ATOM 1819 CG PHE A 317 5.573 -21.461 -20.382 1.00 53.51 C ANISOU 1819 CG PHE A 317 6651 7093 6588 -561 -289 2330 C ATOM 1820 CD1 PHE A 317 6.822 -21.103 -20.862 1.00 53.03 C ANISOU 1820 CD1 PHE A 317 6547 7039 6562 -437 -351 2284 C ATOM 1821 CD2 PHE A 317 4.452 -21.040 -21.076 1.00 53.19 C ANISOU 1821 CD2 PHE A 317 6568 7076 6567 -632 -217 2207 C ATOM 1822 CE1 PHE A 317 6.951 -20.341 -22.008 1.00 52.21 C ANISOU 1822 CE1 PHE A 317 6380 6959 6497 -394 -332 2122 C ATOM 1823 CE2 PHE A 317 4.574 -20.279 -22.224 1.00 52.34 C ANISOU 1823 CE2 PHE A 317 6403 6984 6499 -579 -216 2043 C ATOM 1824 CZ PHE A 317 5.825 -19.929 -22.689 1.00 51.81 C ANISOU 1824 CZ PHE A 317 6314 6918 6452 -464 -268 2003 C ATOM 1825 N VAL A 318 7.897 -24.106 -18.881 1.00 46.64 N ANISOU 1825 N VAL A 318 5940 5938 5843 -378 -503 2775 N ATOM 1826 CA VAL A 318 9.288 -24.432 -19.175 1.00 47.20 C ANISOU 1826 CA VAL A 318 5970 5943 6020 -201 -588 2809 C ATOM 1827 C VAL A 318 9.430 -25.850 -19.724 1.00 48.83 C ANISOU 1827 C VAL A 318 6261 5880 6414 -116 -594 2852 C ATOM 1828 O VAL A 318 10.026 -26.054 -20.783 1.00 49.39 O ANISOU 1828 O VAL A 318 6296 5856 6614 20 -577 2741 O ATOM 1829 CB VAL A 318 10.181 -24.278 -17.930 1.00 40.42 C ANISOU 1829 CB VAL A 318 5100 5199 5057 -166 -706 2984 C ATOM 1830 CG1 VAL A 318 11.587 -24.779 -18.220 1.00 41.45 C ANISOU 1830 CG1 VAL A 318 5157 5263 5332 29 -796 3042 C ATOM 1831 CG2 VAL A 318 10.211 -22.827 -17.476 1.00 39.45 C ANISOU 1831 CG2 VAL A 318 4918 5322 4749 -241 -716 2914 C ATOM 1832 N VAL A 319 8.869 -26.820 -19.006 1.00 51.82 N ANISOU 1832 N VAL A 319 6764 6127 6797 -199 -611 3011 N ATOM 1833 CA VAL A 319 8.959 -28.223 -19.404 1.00 53.61 C ANISOU 1833 CA VAL A 319 7110 6057 7202 -129 -634 3068 C ATOM 1834 C VAL A 319 8.316 -28.487 -20.765 1.00 52.54 C ANISOU 1834 C VAL A 319 7011 5773 7179 -156 -557 2868 C ATOM 1835 O VAL A 319 8.904 -29.153 -21.618 1.00 53.18 O ANISOU 1835 O VAL A 319 7139 5660 7406 -5 -564 2796 O ATOM 1836 CB VAL A 319 8.320 -29.155 -18.351 1.00 46.55 C ANISOU 1836 CB VAL A 319 6360 5047 6281 -259 -668 3295 C ATOM 1837 CG1 VAL A 319 8.258 -30.586 -18.869 1.00 48.59 C ANISOU 1837 CG1 VAL A 319 6769 4956 6736 -202 -698 3341 C ATOM 1838 CG2 VAL A 319 9.099 -29.093 -17.047 1.00 49.17 C ANISOU 1838 CG2 VAL A 319 6684 5508 6489 -218 -767 3506 C ATOM 1839 N CYS A 320 7.113 -27.958 -20.967 1.00 67.09 N ANISOU 1839 N CYS A 320 8832 7713 8948 -338 -486 2776 N ATOM 1840 CA CYS A 320 6.388 -28.184 -22.214 1.00 67.59 C ANISOU 1840 CA CYS A 320 8929 7652 9099 -394 -439 2597 C ATOM 1841 C CYS A 320 7.060 -27.522 -23.414 1.00 67.29 C ANISOU 1841 C CYS A 320 8814 7669 9085 -248 -411 2390 C ATOM 1842 O CYS A 320 7.120 -28.103 -24.497 1.00 68.74 O ANISOU 1842 O CYS A 320 9074 7679 9367 -198 -399 2258 O ATOM 1843 CB CYS A 320 4.941 -27.701 -22.099 1.00 46.98 C ANISOU 1843 CB CYS A 320 6277 5163 6410 -619 -380 2569 C ATOM 1844 SG CYS A 320 3.895 -28.703 -21.020 1.00 48.22 S ANISOU 1844 SG CYS A 320 6536 5209 6575 -838 -381 2790 S ATOM 1845 N TRP A 321 7.567 -26.309 -23.221 1.00 40.57 N ANISOU 1845 N TRP A 321 5293 4522 5598 -191 -402 2363 N ATOM 1846 CA TRP A 321 8.118 -25.542 -24.335 1.00 40.21 C ANISOU 1846 CA TRP A 321 5164 4559 5555 -88 -366 2187 C ATOM 1847 C TRP A 321 9.613 -25.764 -24.575 1.00 41.40 C ANISOU 1847 C TRP A 321 5269 4680 5782 134 -383 2201 C ATOM 1848 O TRP A 321 10.155 -25.305 -25.581 1.00 41.84 O ANISOU 1848 O TRP A 321 5267 4775 5853 230 -334 2063 O ATOM 1849 CB TRP A 321 7.818 -24.049 -24.166 1.00 42.46 C ANISOU 1849 CB TRP A 321 5330 5102 5701 -166 -344 2129 C ATOM 1850 CG TRP A 321 6.386 -23.701 -24.428 1.00 41.69 C ANISOU 1850 CG TRP A 321 5241 5041 5558 -332 -303 2048 C ATOM 1851 CD1 TRP A 321 5.401 -23.519 -23.500 1.00 41.05 C ANISOU 1851 CD1 TRP A 321 5152 5047 5399 -476 -286 2127 C ATOM 1852 CD2 TRP A 321 5.773 -23.499 -25.708 1.00 41.86 C ANISOU 1852 CD2 TRP A 321 5268 5029 5609 -364 -273 1878 C ATOM 1853 NE1 TRP A 321 4.215 -23.211 -24.122 1.00 40.80 N ANISOU 1853 NE1 TRP A 321 5095 5042 5367 -587 -247 2021 N ATOM 1854 CE2 TRP A 321 4.417 -23.195 -25.478 1.00 41.18 C ANISOU 1854 CE2 TRP A 321 5156 5012 5479 -527 -253 1871 C ATOM 1855 CE3 TRP A 321 6.240 -23.546 -27.027 1.00 42.88 C ANISOU 1855 CE3 TRP A 321 5421 5086 5785 -268 -259 1736 C ATOM 1856 CZ2 TRP A 321 3.523 -22.940 -26.516 1.00 41.28 C ANISOU 1856 CZ2 TRP A 321 5155 5022 5508 -598 -246 1735 C ATOM 1857 CZ3 TRP A 321 5.350 -23.290 -28.056 1.00 43.02 C ANISOU 1857 CZ3 TRP A 321 5455 5097 5793 -348 -249 1596 C ATOM 1858 CH2 TRP A 321 4.008 -22.991 -27.794 1.00 42.11 C ANISOU 1858 CH2 TRP A 321 5304 5049 5648 -513 -256 1601 C ATOM 1859 N LEU A 322 10.276 -26.467 -23.662 1.00 51.80 N ANISOU 1859 N LEU A 322 6601 5939 7143 217 -449 2378 N ATOM 1860 CA LEU A 322 11.710 -26.723 -23.816 1.00 53.13 C ANISOU 1860 CA LEU A 322 6691 6094 7403 444 -470 2415 C ATOM 1861 C LEU A 322 12.084 -27.561 -25.053 1.00 55.67 C ANISOU 1861 C LEU A 322 7085 6203 7864 613 -406 2288 C ATOM 1862 O LEU A 322 12.923 -27.133 -25.842 1.00 56.37 O ANISOU 1862 O LEU A 322 7067 6377 7975 752 -345 2187 O ATOM 1863 CB LEU A 322 12.327 -27.315 -22.540 1.00 46.90 C ANISOU 1863 CB LEU A 322 5899 5288 6636 505 -578 2650 C ATOM 1864 CG LEU A 322 13.843 -27.533 -22.570 1.00 48.38 C ANISOU 1864 CG LEU A 322 5966 5480 6936 753 -616 2716 C ATOM 1865 CD1 LEU A 322 14.567 -26.218 -22.816 1.00 47.13 C ANISOU 1865 CD1 LEU A 322 5596 5608 6704 762 -622 2681 C ATOM 1866 CD2 LEU A 322 14.327 -28.181 -21.284 1.00 49.30 C ANISOU 1866 CD2 LEU A 322 6127 5505 7100 822 -741 2959 C ATOM 1867 N PRO A 323 11.473 -28.750 -25.230 1.00 60.67 N ANISOU 1867 N PRO A 323 7909 6558 8586 597 -414 2290 N ATOM 1868 CA PRO A 323 11.867 -29.549 -26.398 1.00 63.51 C ANISOU 1868 CA PRO A 323 8371 6699 9063 770 -354 2146 C ATOM 1869 C PRO A 323 11.421 -28.914 -27.714 1.00 63.73 C ANISOU 1869 C PRO A 323 8401 6792 9022 720 -263 1909 C ATOM 1870 O PRO A 323 12.042 -29.148 -28.751 1.00 66.00 O ANISOU 1870 O PRO A 323 8710 7014 9353 896 -185 1770 O ATOM 1871 CB PRO A 323 11.125 -30.875 -26.183 1.00 55.83 C ANISOU 1871 CB PRO A 323 7630 5405 8179 695 -406 2201 C ATOM 1872 CG PRO A 323 10.733 -30.881 -24.746 1.00 54.16 C ANISOU 1872 CG PRO A 323 7400 5254 7922 559 -494 2438 C ATOM 1873 CD PRO A 323 10.474 -29.456 -24.412 1.00 51.28 C ANISOU 1873 CD PRO A 323 6859 5228 7395 427 -475 2427 C ATOM 1874 N TYR A 324 10.351 -28.127 -27.662 1.00 46.77 N ANISOU 1874 N TYR A 324 6232 4778 6760 492 -270 1868 N ATOM 1875 CA TYR A 324 9.816 -27.450 -28.840 1.00 46.79 C ANISOU 1875 CA TYR A 324 6235 4858 6684 423 -211 1668 C ATOM 1876 C TYR A 324 10.858 -26.549 -29.493 1.00 46.83 C ANISOU 1876 C TYR A 324 6090 5060 6642 567 -136 1595 C ATOM 1877 O TYR A 324 11.101 -26.638 -30.698 1.00 48.97 O ANISOU 1877 O TYR A 324 6411 5291 6903 658 -60 1434 O ATOM 1878 CB TYR A 324 8.576 -26.636 -28.456 1.00 53.20 C ANISOU 1878 CB TYR A 324 7007 5813 7396 177 -242 1679 C ATOM 1879 CG TYR A 324 8.055 -25.715 -29.540 1.00 52.78 C ANISOU 1879 CG TYR A 324 6926 5878 7253 107 -204 1505 C ATOM 1880 CD1 TYR A 324 7.227 -26.191 -30.547 1.00 54.66 C ANISOU 1880 CD1 TYR A 324 7301 5967 7500 37 -209 1359 C ATOM 1881 CD2 TYR A 324 8.377 -24.364 -29.543 1.00 50.66 C ANISOU 1881 CD2 TYR A 324 6504 5859 6885 99 -181 1494 C ATOM 1882 CE1 TYR A 324 6.742 -25.350 -31.534 1.00 54.45 C ANISOU 1882 CE1 TYR A 324 7254 6055 7381 -28 -194 1216 C ATOM 1883 CE2 TYR A 324 7.898 -23.517 -30.523 1.00 50.31 C ANISOU 1883 CE2 TYR A 324 6446 5911 6761 38 -158 1356 C ATOM 1884 CZ TYR A 324 7.081 -24.014 -31.516 1.00 52.22 C ANISOU 1884 CZ TYR A 324 6818 6019 7007 -20 -166 1222 C ATOM 1885 OH TYR A 324 6.604 -23.168 -32.492 1.00 52.02 O ANISOU 1885 OH TYR A 324 6783 6095 6890 -79 -161 1100 O ATOM 1886 N HIS A 325 11.475 -25.689 -28.690 1.00 49.95 N ANISOU 1886 N HIS A 325 6309 5670 6998 575 -160 1716 N ATOM 1887 CA HIS A 325 12.488 -24.766 -29.188 1.00 49.81 C ANISOU 1887 CA HIS A 325 6127 5855 6945 676 -102 1680 C ATOM 1888 C HIS A 325 13.757 -25.493 -29.623 1.00 52.59 C ANISOU 1888 C HIS A 325 6438 6137 7408 934 -38 1682 C ATOM 1889 O HIS A 325 14.467 -25.035 -30.519 1.00 53.79 O ANISOU 1889 O HIS A 325 6501 6396 7539 1036 60 1593 O ATOM 1890 CB HIS A 325 12.817 -23.705 -28.136 1.00 68.35 C ANISOU 1890 CB HIS A 325 8312 8430 9226 594 -169 1813 C ATOM 1891 CG HIS A 325 11.708 -22.729 -27.897 1.00 65.79 C ANISOU 1891 CG HIS A 325 8004 8213 8780 382 -197 1777 C ATOM 1892 ND1 HIS A 325 11.466 -21.659 -28.732 1.00 65.13 N ANISOU 1892 ND1 HIS A 325 7892 8239 8615 317 -151 1650 N ATOM 1893 CD2 HIS A 325 10.778 -22.658 -26.916 1.00 63.98 C ANISOU 1893 CD2 HIS A 325 7814 7999 8496 235 -259 1855 C ATOM 1894 CE1 HIS A 325 10.433 -20.973 -28.276 1.00 62.90 C ANISOU 1894 CE1 HIS A 325 7625 8024 8249 154 -190 1647 C ATOM 1895 NE2 HIS A 325 9.997 -21.558 -27.176 1.00 62.27 N ANISOU 1895 NE2 HIS A 325 7582 7898 8180 103 -244 1765 N ATOM 1896 N VAL A 326 14.037 -26.624 -28.985 1.00 40.26 N ANISOU 1896 N VAL A 326 4937 4397 5964 1045 -88 1793 N ATOM 1897 CA VAL A 326 15.191 -27.439 -29.348 1.00 43.08 C ANISOU 1897 CA VAL A 326 5258 4658 6450 1324 -29 1801 C ATOM 1898 C VAL A 326 15.020 -27.998 -30.758 1.00 46.12 C ANISOU 1898 C VAL A 326 5798 4883 6843 1432 95 1583 C ATOM 1899 O VAL A 326 15.976 -28.067 -31.532 1.00 48.17 O ANISOU 1899 O VAL A 326 5969 5203 7128 1636 215 1510 O ATOM 1900 CB VAL A 326 15.410 -28.593 -28.344 1.00 40.11 C ANISOU 1900 CB VAL A 326 4957 4078 6205 1421 -127 1971 C ATOM 1901 CG1 VAL A 326 16.499 -29.539 -28.833 1.00 43.42 C ANISOU 1901 CG1 VAL A 326 5371 4347 6777 1742 -56 1952 C ATOM 1902 CG2 VAL A 326 15.761 -28.041 -26.972 1.00 41.14 C ANISOU 1902 CG2 VAL A 326 4928 4393 6310 1349 -251 2193 C ATOM 1903 N ARG A 327 13.791 -28.377 -31.092 1.00 57.63 N ANISOU 1903 N ARG A 327 7482 6147 8267 1286 67 1479 N ATOM 1904 CA ARG A 327 13.494 -28.945 -32.401 1.00 60.72 C ANISOU 1904 CA ARG A 327 8065 6366 8637 1351 155 1258 C ATOM 1905 C ARG A 327 13.637 -27.916 -33.521 1.00 61.03 C ANISOU 1905 C ARG A 327 8025 6629 8535 1330 262 1111 C ATOM 1906 O ARG A 327 14.172 -28.217 -34.588 1.00 63.99 O ANISOU 1906 O ARG A 327 8454 6968 8889 1503 389 964 O ATOM 1907 CB ARG A 327 12.083 -29.533 -32.421 1.00 51.62 C ANISOU 1907 CB ARG A 327 7153 4984 7475 1143 66 1197 C ATOM 1908 CG ARG A 327 11.721 -30.199 -33.735 1.00 54.91 C ANISOU 1908 CG ARG A 327 7799 5210 7853 1177 123 957 C ATOM 1909 CD ARG A 327 10.275 -30.644 -33.746 1.00 54.85 C ANISOU 1909 CD ARG A 327 7995 5008 7837 923 8 911 C ATOM 1910 NE ARG A 327 9.359 -29.543 -33.464 1.00 51.62 N ANISOU 1910 NE ARG A 327 7461 4821 7332 660 -56 968 N ATOM 1911 CZ ARG A 327 8.956 -28.656 -34.367 1.00 51.24 C ANISOU 1911 CZ ARG A 327 7373 4949 7146 563 -31 844 C ATOM 1912 NH1 ARG A 327 9.391 -28.733 -35.617 1.00 53.96 N ANISOU 1912 NH1 ARG A 327 7801 5289 7412 688 58 661 N ATOM 1913 NH2 ARG A 327 8.117 -27.688 -34.022 1.00 48.17 N ANISOU 1913 NH2 ARG A 327 6868 4743 6692 351 -92 908 N ATOM 1914 N ARG A 328 13.149 -26.703 -33.277 1.00 53.54 N ANISOU 1914 N ARG A 328 6960 5903 7481 1123 215 1155 N ATOM 1915 CA ARG A 328 13.206 -25.645 -34.281 1.00 53.66 C ANISOU 1915 CA ARG A 328 6906 6126 7357 1076 296 1047 C ATOM 1916 C ARG A 328 14.638 -25.168 -34.501 1.00 54.42 C ANISOU 1916 C ARG A 328 6792 6416 7468 1260 411 1091 C ATOM 1917 O ARG A 328 15.004 -24.758 -35.602 1.00 56.43 O ANISOU 1917 O ARG A 328 7044 6761 7637 1330 538 973 O ATOM 1918 CB ARG A 328 12.295 -24.479 -33.891 1.00 56.53 C ANISOU 1918 CB ARG A 328 7203 6651 7625 825 206 1095 C ATOM 1919 CG ARG A 328 10.820 -24.839 -33.903 1.00 56.20 C ANISOU 1919 CG ARG A 328 7341 6465 7547 638 124 1014 C ATOM 1920 CD ARG A 328 9.957 -23.735 -33.320 1.00 52.45 C ANISOU 1920 CD ARG A 328 6779 6134 7016 426 36 1095 C ATOM 1921 NE ARG A 328 9.817 -22.589 -34.213 1.00 51.81 N ANISOU 1921 NE ARG A 328 6658 6219 6809 341 54 1010 N ATOM 1922 CZ ARG A 328 10.105 -21.337 -33.872 1.00 49.72 C ANISOU 1922 CZ ARG A 328 6238 6166 6488 328 70 1069 C ATOM 1923 NH1 ARG A 328 10.555 -21.065 -32.654 1.00 48.14 N ANISOU 1923 NH1 ARG A 328 5897 6053 6340 386 64 1206 N ATOM 1924 NH2 ARG A 328 9.943 -20.355 -34.748 1.00 49.27 N ANISOU 1924 NH2 ARG A 328 6174 6225 6320 250 77 998 N ATOM 1925 N LEU A 329 15.443 -25.224 -33.445 1.00 54.52 N ANISOU 1925 N LEU A 329 6624 6506 7583 1330 364 1272 N ATOM 1926 CA LEU A 329 16.868 -24.950 -33.565 1.00 55.41 C ANISOU 1926 CA LEU A 329 6506 6798 7748 1513 459 1340 C ATOM 1927 C LEU A 329 17.525 -26.087 -34.338 1.00 59.33 C ANISOU 1927 C LEU A 329 7073 7141 8328 1798 596 1242 C ATOM 1928 O LEU A 329 18.435 -25.867 -35.134 1.00 61.34 O ANISOU 1928 O LEU A 329 7208 7534 8564 1949 754 1190 O ATOM 1929 CB LEU A 329 17.513 -24.805 -32.185 1.00 46.10 C ANISOU 1929 CB LEU A 329 5131 5718 6668 1518 340 1563 C ATOM 1930 CG LEU A 329 17.200 -23.529 -31.399 1.00 42.44 C ANISOU 1930 CG LEU A 329 4568 5444 6113 1272 221 1660 C ATOM 1931 CD1 LEU A 329 17.827 -23.580 -30.013 1.00 40.87 C ANISOU 1931 CD1 LEU A 329 4224 5309 5996 1287 88 1869 C ATOM 1932 CD2 LEU A 329 17.677 -22.300 -32.158 1.00 42.21 C ANISOU 1932 CD2 LEU A 329 4395 5654 5990 1204 301 1619 C ATOM 1933 N MET A 330 17.046 -27.303 -34.097 1.00 58.73 N ANISOU 1933 N MET A 330 7199 6771 8343 1871 542 1219 N ATOM 1934 CA MET A 330 17.549 -28.491 -34.777 1.00 62.39 C ANISOU 1934 CA MET A 330 7790 7022 8892 2150 658 1105 C ATOM 1935 C MET A 330 17.208 -28.449 -36.265 1.00 65.01 C ANISOU 1935 C MET A 330 8295 7330 9076 2163 802 857 C ATOM 1936 O MET A 330 17.936 -28.991 -37.097 1.00 67.96 O ANISOU 1936 O MET A 330 8681 7679 9460 2416 973 746 O ATOM 1937 CB MET A 330 16.962 -29.750 -34.130 1.00 76.94 C ANISOU 1937 CB MET A 330 9862 8519 10852 2166 538 1134 C ATOM 1938 CG MET A 330 17.337 -31.059 -34.805 1.00 80.77 C ANISOU 1938 CG MET A 330 10546 8714 11429 2446 637 993 C ATOM 1939 SD MET A 330 16.583 -32.492 -34.009 1.00 81.25 S ANISOU 1939 SD MET A 330 10922 8333 11617 2394 471 1030 S ATOM 1940 CE MET A 330 17.174 -33.819 -35.058 1.00 86.00 C ANISOU 1940 CE MET A 330 11809 8604 12262 2697 618 771 C ATOM 1941 N PHE A 331 16.098 -27.793 -36.589 1.00 65.80 N ANISOU 1941 N PHE A 331 8523 7445 9030 1894 732 776 N ATOM 1942 CA PHE A 331 15.615 -27.712 -37.964 1.00 68.21 C ANISOU 1942 CA PHE A 331 9017 7731 9167 1861 826 551 C ATOM 1943 C PHE A 331 16.568 -26.952 -38.882 1.00 69.56 C ANISOU 1943 C PHE A 331 9027 8172 9231 1974 1016 508 C ATOM 1944 O PHE A 331 16.703 -27.288 -40.058 1.00 72.68 O ANISOU 1944 O PHE A 331 9565 8521 9529 2116 1168 326 O ATOM 1945 CB PHE A 331 14.226 -27.063 -37.999 1.00 52.46 C ANISOU 1945 CB PHE A 331 7129 5750 7053 1541 686 518 C ATOM 1946 CG PHE A 331 13.676 -26.868 -39.387 1.00 54.75 C ANISOU 1946 CG PHE A 331 7606 6045 7153 1479 745 308 C ATOM 1947 CD1 PHE A 331 13.018 -27.900 -40.035 1.00 57.36 C ANISOU 1947 CD1 PHE A 331 8242 6100 7453 1495 725 122 C ATOM 1948 CD2 PHE A 331 13.805 -25.650 -40.037 1.00 54.09 C ANISOU 1948 CD2 PHE A 331 7410 6231 6913 1392 806 302 C ATOM 1949 CE1 PHE A 331 12.507 -27.725 -41.304 1.00 59.41 C ANISOU 1949 CE1 PHE A 331 8688 6370 7516 1428 758 -72 C ATOM 1950 CE2 PHE A 331 13.296 -25.469 -41.307 1.00 55.94 C ANISOU 1950 CE2 PHE A 331 7827 6476 6953 1333 847 125 C ATOM 1951 CZ PHE A 331 12.646 -26.509 -41.941 1.00 58.71 C ANISOU 1951 CZ PHE A 331 8480 6567 7261 1351 820 -65 C ATOM 1952 N CYS A 332 17.232 -25.934 -38.345 1.00 61.42 N ANISOU 1952 N CYS A 332 7710 7422 8206 1900 1010 675 N ATOM 1953 CA CYS A 332 18.037 -25.044 -39.174 1.00 62.27 C ANISOU 1953 CA CYS A 332 7652 7807 8202 1938 1175 664 C ATOM 1954 C CYS A 332 19.538 -25.096 -38.890 1.00 62.99 C ANISOU 1954 C CYS A 332 7453 8059 8423 2176 1307 785 C ATOM 1955 O CYS A 332 20.336 -24.605 -39.687 1.00 64.59 O ANISOU 1955 O CYS A 332 7532 8463 8549 2268 1495 756 O ATOM 1956 CB CYS A 332 17.532 -23.605 -39.045 1.00 68.79 C ANISOU 1956 CB CYS A 332 8376 8843 8920 1654 1078 751 C ATOM 1957 SG CYS A 332 17.477 -22.980 -37.351 1.00 64.11 S ANISOU 1957 SG CYS A 332 7564 8332 8464 1508 880 993 S ATOM 1958 N TYR A 333 19.924 -25.688 -37.763 1.00 70.91 N ANISOU 1958 N TYR A 333 8337 8985 9620 2273 1208 932 N ATOM 1959 CA TYR A 333 21.336 -25.714 -37.378 1.00 71.33 C ANISOU 1959 CA TYR A 333 8075 9208 9819 2490 1297 1076 C ATOM 1960 C TYR A 333 22.095 -26.956 -37.844 1.00 74.75 C ANISOU 1960 C TYR A 333 8554 9494 10353 2858 1469 978 C ATOM 1961 O TYR A 333 23.326 -26.952 -37.896 1.00 75.97 O ANISOU 1961 O TYR A 333 8444 9833 10589 3074 1624 1042 O ATOM 1962 CB TYR A 333 21.501 -25.519 -35.868 1.00 82.91 C ANISOU 1962 CB TYR A 333 9355 10712 11433 2414 1092 1309 C ATOM 1963 CG TYR A 333 21.697 -24.075 -35.468 1.00 80.06 C ANISOU 1963 CG TYR A 333 8754 10649 11017 2183 1019 1453 C ATOM 1964 CD1 TYR A 333 22.962 -23.502 -35.474 1.00 80.53 C ANISOU 1964 CD1 TYR A 333 8476 10978 11141 2267 1106 1577 C ATOM 1965 CD2 TYR A 333 20.621 -23.282 -35.091 1.00 76.99 C ANISOU 1965 CD2 TYR A 333 8471 10264 10515 1880 864 1463 C ATOM 1966 CE1 TYR A 333 23.152 -22.184 -35.113 1.00 78.06 C ANISOU 1966 CE1 TYR A 333 7963 10912 10782 2035 1023 1706 C ATOM 1967 CE2 TYR A 333 20.802 -21.959 -34.727 1.00 74.35 C ANISOU 1967 CE2 TYR A 333 7949 10168 10130 1676 793 1580 C ATOM 1968 CZ TYR A 333 22.070 -21.418 -34.741 1.00 74.95 C ANISOU 1968 CZ TYR A 333 7716 10490 10272 1743 865 1700 C ATOM 1969 OH TYR A 333 22.259 -20.105 -34.382 1.00 72.50 O ANISOU 1969 OH TYR A 333 7238 10392 9916 1520 777 1814 O ATOM 1970 N ILE A 334 21.368 -28.015 -38.179 1.00 75.98 N ANISOU 1970 N ILE A 334 9042 9317 10512 2930 1443 822 N ATOM 1971 CA ILE A 334 22.002 -29.221 -38.696 1.00 79.32 C ANISOU 1971 CA ILE A 334 9576 9551 11012 3286 1611 686 C ATOM 1972 C ILE A 334 22.326 -29.059 -40.178 1.00 81.81 C ANISOU 1972 C ILE A 334 10005 9954 11124 3359 1852 462 C ATOM 1973 O ILE A 334 21.447 -28.749 -40.982 1.00 82.29 O ANISOU 1973 O ILE A 334 10358 9908 11001 3181 1823 290 O ATOM 1974 CB ILE A 334 21.123 -30.470 -38.492 1.00 59.60 C ANISOU 1974 CB ILE A 334 7425 6627 8595 3324 1481 599 C ATOM 1975 CG1 ILE A 334 20.897 -30.725 -37.001 1.00 57.26 C ANISOU 1975 CG1 ILE A 334 7023 6247 8486 3267 1256 841 C ATOM 1976 CG2 ILE A 334 21.766 -31.688 -39.141 1.00 63.17 C ANISOU 1976 CG2 ILE A 334 8033 6854 9115 3705 1661 429 C ATOM 1977 CD1 ILE A 334 20.234 -32.050 -36.705 1.00 58.25 C ANISOU 1977 CD1 ILE A 334 7464 5949 8721 3323 1135 798 C ATOM 1978 N SER A 335 23.590 -29.270 -40.531 1.00106.10 N ANISOU 1978 N SER A 335 12844 13242 14228 3617 2089 473 N ATOM 1979 CA SER A 335 24.044 -29.101 -41.908 1.00108.16 C ANISOU 1979 CA SER A 335 13187 13636 14273 3694 2349 281 C ATOM 1980 C SER A 335 23.448 -30.151 -42.842 1.00110.97 C ANISOU 1980 C SER A 335 13939 13665 14559 3914 2457 -3 C ATOM 1981 O SER A 335 22.949 -31.184 -42.395 1.00111.61 O ANISOU 1981 O SER A 335 14193 13413 14801 4052 2352 -35 O ATOM 1982 CB SER A 335 25.573 -29.139 -41.978 1.00130.02 C ANISOU 1982 CB SER A 335 15554 16752 17095 3902 2591 392 C ATOM 1983 OG SER A 335 26.076 -30.368 -41.485 1.00131.75 O ANISOU 1983 OG SER A 335 15853 17127 17079 3958 2859 222 O ATOM 1984 N ASP A 336 23.513 -29.876 -44.141 1.00 98.41 N ANISOU 1984 N ASP A 336 12508 12165 12720 3937 2663 -205 N ATOM 1985 CA ASP A 336 22.922 -30.745 -45.154 1.00100.99 C ANISOU 1985 CA ASP A 336 13264 12192 12915 4095 2755 -510 C ATOM 1986 C ASP A 336 23.579 -32.122 -45.209 1.00103.61 C ANISOU 1986 C ASP A 336 13630 12300 13436 4540 2899 -592 C ATOM 1987 O ASP A 336 22.921 -33.122 -45.497 1.00105.27 O ANISOU 1987 O ASP A 336 14216 12116 13666 4639 2835 -781 O ATOM 1988 CB ASP A 336 22.995 -30.081 -46.532 1.00121.92 C ANISOU 1988 CB ASP A 336 16028 15054 15241 4070 2984 -686 C ATOM 1989 CG ASP A 336 22.269 -28.750 -46.577 1.00118.83 C ANISOU 1989 CG ASP A 336 15502 14959 14689 3689 2889 -551 C ATOM 1990 OD1 ASP A 336 22.179 -28.082 -45.525 1.00116.19 O ANISOU 1990 OD1 ASP A 336 14915 14724 14509 3491 2697 -311 O ATOM 1991 OD2 ASP A 336 21.787 -28.371 -47.666 1.00118.99 O ANISOU 1991 OD2 ASP A 336 15685 15107 14420 3593 3003 -685 O ATOM 1992 N GLU A 337 24.878 -32.167 -44.931 1.00120.81 N ANISOU 1992 N GLU A 337 15414 14725 15765 4805 3085 -445 N ATOM 1993 CA GLU A 337 25.629 -33.416 -44.999 1.00123.53 C ANISOU 1993 CA GLU A 337 15736 14899 16299 5276 3253 -509 C ATOM 1994 C GLU A 337 25.355 -34.326 -43.803 1.00123.23 C ANISOU 1994 C GLU A 337 15778 14497 16546 5348 2999 -405 C ATOM 1995 O GLU A 337 25.580 -35.534 -43.870 1.00125.77 O ANISOU 1995 O GLU A 337 16308 14492 16988 5683 3062 -541 O ATOM 1996 CB GLU A 337 27.129 -33.136 -45.115 1.00218.55 C ANISOU 1996 CB GLU A 337 27263 27334 28440 5521 3502 -340 C ATOM 1997 CG GLU A 337 27.527 -32.417 -46.394 1.00216.03 C ANISOU 1997 CG GLU A 337 26496 27314 28272 5282 3322 6 C ATOM 1998 CD GLU A 337 29.024 -32.202 -46.498 1.00216.35 C ANISOU 1998 CD GLU A 337 26024 27775 28402 5477 3564 172 C ATOM 1999 OE1 GLU A 337 29.739 -32.513 -45.522 1.00218.70 O ANISOU 1999 OE1 GLU A 337 26297 28140 28659 5829 3891 25 O ATOM 2000 OE2 GLU A 337 29.486 -31.724 -47.556 1.00214.26 O ANISOU 2000 OE2 GLU A 337 25381 27780 28247 5275 3428 447 O ATOM 2001 N GLN A 338 24.867 -33.742 -42.714 1.00122.94 N ANISOU 2001 N GLN A 338 15592 14508 16610 5037 2715 -163 N ATOM 2002 CA GLN A 338 24.587 -34.506 -41.502 1.00122.29 C ANISOU 2002 CA GLN A 338 15574 14114 16777 5064 2464 -25 C ATOM 2003 C GLN A 338 23.185 -35.108 -41.509 1.00122.40 C ANISOU 2003 C GLN A 338 16081 13703 16720 4868 2273 -191 C ATOM 2004 O GLN A 338 22.924 -36.098 -40.824 1.00123.03 O ANISOU 2004 O GLN A 338 16341 13419 16986 4983 2135 -166 O ATOM 2005 CB GLN A 338 24.781 -33.635 -40.258 1.00152.27 C ANISOU 2005 CB GLN A 338 19015 18148 20694 4819 2247 304 C ATOM 2006 CG GLN A 338 26.229 -33.273 -39.975 1.00152.24 C ANISOU 2006 CG GLN A 338 18508 18484 20854 5039 2360 520 C ATOM 2007 CD GLN A 338 26.387 -32.433 -38.723 1.00149.87 C ANISOU 2007 CD GLN A 338 17891 18637 20415 4770 2402 637 C ATOM 2008 OE1 GLN A 338 25.970 -31.275 -38.681 1.00148.91 O ANISOU 2008 OE1 GLN A 338 17925 18608 20046 4544 2469 495 O ATOM 2009 NE2 GLN A 338 26.989 -33.015 -37.692 1.00148.97 N ANISOU 2009 NE2 GLN A 338 17340 18801 20463 4783 2345 905 N ATOM 2010 N TRP A 339 22.286 -34.509 -42.284 1.00 88.44 N ANISOU 2010 N TRP A 339 11993 9452 12159 4565 2253 -346 N ATOM 2011 CA TRP A 339 20.908 -34.984 -42.361 1.00 88.43 C ANISOU 2011 CA TRP A 339 12427 9090 12085 4329 2055 -493 C ATOM 2012 C TRP A 339 20.798 -36.358 -43.017 1.00 91.71 C ANISOU 2012 C TRP A 339 13246 9086 12514 4611 2142 -762 C ATOM 2013 O TRP A 339 20.887 -36.485 -44.238 1.00 94.01 O ANISOU 2013 O TRP A 339 13631 9423 12668 4859 2398 -982 O ATOM 2014 CB TRP A 339 20.025 -33.978 -43.104 1.00 78.87 C ANISOU 2014 CB TRP A 339 11327 8053 10588 3965 2017 -598 C ATOM 2015 CG TRP A 339 19.532 -32.855 -42.245 1.00 75.48 C ANISOU 2015 CG TRP A 339 10659 7860 10162 3601 1821 -360 C ATOM 2016 CD1 TRP A 339 19.965 -31.561 -42.258 1.00 73.77 C ANISOU 2016 CD1 TRP A 339 10114 8056 9861 3480 1884 -223 C ATOM 2017 CD2 TRP A 339 18.512 -32.928 -41.243 1.00 73.40 C ANISOU 2017 CD2 TRP A 339 10476 7425 9988 3315 1540 -236 C ATOM 2018 NE1 TRP A 339 19.276 -30.822 -41.327 1.00 70.81 N ANISOU 2018 NE1 TRP A 339 9628 7761 9515 3153 1655 -38 N ATOM 2019 CE2 TRP A 339 18.378 -31.638 -40.690 1.00 70.44 C ANISOU 2019 CE2 TRP A 339 9818 7377 9569 3052 1453 -42 C ATOM 2020 CE3 TRP A 339 17.697 -33.957 -40.761 1.00 73.73 C ANISOU 2020 CE3 TRP A 339 10806 7068 10141 3250 1359 -266 C ATOM 2021 CZ2 TRP A 339 17.463 -31.349 -39.679 1.00 67.70 C ANISOU 2021 CZ2 TRP A 339 9463 6985 9275 2753 1212 109 C ATOM 2022 CZ3 TRP A 339 16.791 -33.670 -39.758 1.00 71.03 C ANISOU 2022 CZ3 TRP A 339 10437 6698 9855 2932 1120 -95 C ATOM 2023 CH2 TRP A 339 16.681 -32.376 -39.227 1.00 68.00 C ANISOU 2023 CH2 TRP A 339 9764 6660 9415 2699 1058 84 C ATOM 2024 N THR A 340 20.605 -37.385 -42.195 1.00118.32 N ANISOU 2024 N THR A 340 16868 12044 16044 4567 1930 -743 N ATOM 2025 CA THR A 340 20.386 -38.736 -42.694 1.00121.32 C ANISOU 2025 CA THR A 340 17684 11956 16456 4790 1961 -995 C ATOM 2026 C THR A 340 18.897 -39.059 -42.667 1.00120.76 C ANISOU 2026 C THR A 340 18003 11556 16324 4417 1697 -1083 C ATOM 2027 O THR A 340 18.083 -38.226 -42.268 1.00118.08 O ANISOU 2027 O THR A 340 17567 11385 15914 4019 1521 -953 O ATOM 2028 CB THR A 340 21.144 -39.781 -41.852 1.00109.53 C ANISOU 2028 CB THR A 340 16138 10204 15276 5168 1962 -872 C ATOM 2029 OG1 THR A 340 20.638 -39.779 -40.511 1.00107.11 O ANISOU 2029 OG1 THR A 340 15716 9823 15158 4948 1688 -574 O ATOM 2030 CG2 THR A 340 22.633 -39.470 -41.829 1.00110.34 C ANISOU 2030 CG2 THR A 340 15824 10640 15460 5555 2223 -780 C ATOM 2031 N THR A 341 18.543 -40.266 -43.096 1.00 97.85 N ANISOU 2031 N THR A 341 15539 8184 13455 4547 1670 -1305 N ATOM 2032 CA THR A 341 17.158 -40.719 -43.036 1.00 97.60 C ANISOU 2032 CA THR A 341 15884 7803 13397 4193 1408 -1384 C ATOM 2033 C THR A 341 16.741 -40.881 -41.578 1.00 95.44 C ANISOU 2033 C THR A 341 15481 7417 13362 3991 1158 -1063 C ATOM 2034 O THR A 341 15.600 -40.578 -41.199 1.00 93.36 O ANISOU 2034 O THR A 341 15262 7152 13057 3570 942 -978 O ATOM 2035 CB THR A 341 16.969 -42.056 -43.775 1.00 93.29 C ANISOU 2035 CB THR A 341 15852 6737 12857 4398 1428 -1689 C ATOM 2036 OG1 THR A 341 17.766 -43.069 -43.148 1.00 98.48 O ANISOU 2036 OG1 THR A 341 16511 7107 13802 4770 1459 -1591 O ATOM 2037 CG2 THR A 341 17.382 -41.924 -45.235 1.00 96.97 C ANISOU 2037 CG2 THR A 341 16471 7317 13058 4622 1696 -2021 C ATOM 2038 N PHE A 342 17.684 -41.353 -40.768 1.00 87.58 N ANISOU 2038 N PHE A 342 14316 6348 12613 4303 1195 -878 N ATOM 2039 CA PHE A 342 17.475 -41.512 -39.335 1.00 85.93 C ANISOU 2039 CA PHE A 342 13986 6039 12625 4166 977 -555 C ATOM 2040 C PHE A 342 17.095 -40.190 -38.685 1.00 78.40 C ANISOU 2040 C PHE A 342 12662 5529 11597 3827 887 -315 C ATOM 2041 O PHE A 342 16.112 -40.117 -37.956 1.00 75.23 O ANISOU 2041 O PHE A 342 12305 5063 11217 3472 674 -169 O ATOM 2042 CB PHE A 342 18.727 -42.076 -38.662 1.00112.77 C ANISOU 2042 CB PHE A 342 17225 9342 16279 4606 1050 -396 C ATOM 2043 CG PHE A 342 18.697 -41.992 -37.160 1.00110.53 C ANISOU 2043 CG PHE A 342 16731 9080 16187 4484 847 -23 C ATOM 2044 CD1 PHE A 342 17.942 -42.886 -36.418 1.00110.87 C ANISOU 2044 CD1 PHE A 342 17057 8704 16364 4316 621 82 C ATOM 2045 CD2 PHE A 342 19.424 -41.020 -36.491 1.00108.14 C ANISOU 2045 CD2 PHE A 342 15956 9215 15919 4525 877 229 C ATOM 2046 CE1 PHE A 342 17.911 -42.811 -35.039 1.00108.84 C ANISOU 2046 CE1 PHE A 342 16623 8480 16253 4200 443 433 C ATOM 2047 CE2 PHE A 342 19.397 -40.940 -35.113 1.00106.08 C ANISOU 2047 CE2 PHE A 342 15525 8980 15802 4410 684 564 C ATOM 2048 CZ PHE A 342 18.640 -41.837 -34.386 1.00106.44 C ANISOU 2048 CZ PHE A 342 15862 8620 15962 4253 473 668 C ATOM 2049 N LEU A 343 17.877 -39.149 -38.954 1.00104.79 N ANISOU 2049 N LEU A 343 15645 9320 14851 3937 1058 -275 N ATOM 2050 CA LEU A 343 17.614 -37.830 -38.386 1.00101.29 C ANISOU 2050 CA LEU A 343 14859 9299 14327 3642 988 -69 C ATOM 2051 C LEU A 343 16.311 -37.234 -38.909 1.00100.07 C ANISOU 2051 C LEU A 343 14851 9211 13960 3228 890 -185 C ATOM 2052 O LEU A 343 15.710 -36.379 -38.262 1.00 97.11 O ANISOU 2052 O LEU A 343 14300 9046 13553 2921 760 -11 O ATOM 2053 CB LEU A 343 18.781 -36.877 -38.657 1.00 96.39 C ANISOU 2053 CB LEU A 343 13850 9117 13656 3844 1196 -22 C ATOM 2054 CG LEU A 343 20.031 -37.073 -37.798 1.00 96.78 C ANISOU 2054 CG LEU A 343 13613 9223 13934 4190 1249 185 C ATOM 2055 CD1 LEU A 343 21.080 -36.025 -38.137 1.00 96.43 C ANISOU 2055 CD1 LEU A 343 13169 9638 13830 4336 1453 228 C ATOM 2056 CD2 LEU A 343 19.676 -37.019 -36.319 1.00 94.34 C ANISOU 2056 CD2 LEU A 343 13178 8888 13778 4016 1007 496 C ATOM 2057 N PHE A 344 15.882 -37.696 -40.079 1.00 88.31 N ANISOU 2057 N PHE A 344 13685 7546 12323 3231 951 -482 N ATOM 2058 CA PHE A 344 14.638 -37.244 -40.690 1.00 87.55 C ANISOU 2058 CA PHE A 344 13750 7492 12026 2858 843 -609 C ATOM 2059 C PHE A 344 13.446 -37.818 -39.926 1.00 86.55 C ANISOU 2059 C PHE A 344 13809 7073 12003 2544 583 -516 C ATOM 2060 O PHE A 344 12.624 -37.075 -39.356 1.00 83.89 O ANISOU 2060 O PHE A 344 13329 6918 11629 2206 444 -371 O ATOM 2061 CB PHE A 344 14.598 -37.695 -42.152 1.00 65.93 C ANISOU 2061 CB PHE A 344 11338 4617 9096 2974 969 -957 C ATOM 2062 CG PHE A 344 13.620 -36.938 -43.006 1.00 62.66 C ANISOU 2062 CG PHE A 344 11029 4349 8430 2641 893 -1093 C ATOM 2063 CD1 PHE A 344 13.958 -35.708 -43.544 1.00 59.21 C ANISOU 2063 CD1 PHE A 344 10360 4339 7799 2603 1017 -1090 C ATOM 2064 CD2 PHE A 344 12.373 -37.469 -43.292 1.00 63.80 C ANISOU 2064 CD2 PHE A 344 11508 4198 8535 2366 690 -1219 C ATOM 2065 CE1 PHE A 344 13.066 -35.014 -44.339 1.00 57.36 C ANISOU 2065 CE1 PHE A 344 10227 4232 7335 2312 934 -1202 C ATOM 2066 CE2 PHE A 344 11.477 -36.780 -44.087 1.00 61.41 C ANISOU 2066 CE2 PHE A 344 11286 4039 8007 2068 602 -1335 C ATOM 2067 CZ PHE A 344 11.823 -35.550 -44.610 1.00 58.18 C ANISOU 2067 CZ PHE A 344 10648 4054 7404 2052 723 -1325 C ATOM 2068 N ASP A 345 13.367 -39.147 -39.910 1.00 75.92 N ANISOU 2068 N ASP A 345 12781 5272 10796 2663 525 -594 N ATOM 2069 CA ASP A 345 12.303 -39.848 -39.198 1.00 75.40 C ANISOU 2069 CA ASP A 345 12919 4888 10841 2366 286 -504 C ATOM 2070 C ASP A 345 12.270 -39.419 -37.733 1.00 72.38 C ANISOU 2070 C ASP A 345 12237 4666 10601 2236 183 -147 C ATOM 2071 O ASP A 345 11.203 -39.129 -37.177 1.00 70.16 O ANISOU 2071 O ASP A 345 11921 4428 10309 1868 21 -20 O ATOM 2072 CB ASP A 345 12.505 -41.360 -39.299 1.00149.94 C ANISOU 2072 CB ASP A 345 22747 13791 20432 2566 255 -624 C ATOM 2073 CG ASP A 345 12.658 -41.833 -40.732 1.00153.02 C ANISOU 2073 CG ASP A 345 23460 14011 20668 2747 379 -998 C ATOM 2074 OD1 ASP A 345 11.963 -41.289 -41.615 1.00152.54 O ANISOU 2074 OD1 ASP A 345 23443 14140 20374 2549 385 -1172 O ATOM 2075 OD2 ASP A 345 13.473 -42.748 -40.978 1.00155.85 O ANISOU 2075 OD2 ASP A 345 24035 14046 21132 3099 470 -1120 O ATOM 2076 N PHE A 346 13.451 -39.368 -37.123 1.00 78.07 N ANISOU 2076 N PHE A 346 12730 5491 11445 2544 281 12 N ATOM 2077 CA PHE A 346 13.594 -38.905 -35.750 1.00 75.38 C ANISOU 2077 CA PHE A 346 12098 5334 11212 2462 194 345 C ATOM 2078 C PHE A 346 13.072 -37.486 -35.595 1.00 70.89 C ANISOU 2078 C PHE A 346 11251 5204 10483 2174 177 424 C ATOM 2079 O PHE A 346 12.416 -37.177 -34.607 1.00 68.31 O ANISOU 2079 O PHE A 346 10816 4959 10181 1919 45 635 O ATOM 2080 CB PHE A 346 15.054 -38.975 -35.293 1.00 82.37 C ANISOU 2080 CB PHE A 346 12753 6313 12230 2858 305 478 C ATOM 2081 CG PHE A 346 15.310 -38.311 -33.968 1.00 79.36 C ANISOU 2081 CG PHE A 346 12036 6213 11905 2772 223 800 C ATOM 2082 CD1 PHE A 346 15.061 -38.985 -32.785 1.00 80.25 C ANISOU 2082 CD1 PHE A 346 12210 6124 12159 2678 53 1044 C ATOM 2083 CD2 PHE A 346 15.809 -37.018 -33.906 1.00 76.28 C ANISOU 2083 CD2 PHE A 346 11289 6281 11414 2774 311 862 C ATOM 2084 CE1 PHE A 346 15.294 -38.383 -31.565 1.00 78.01 C ANISOU 2084 CE1 PHE A 346 11643 6103 11894 2595 -27 1330 C ATOM 2085 CE2 PHE A 346 16.043 -36.408 -32.686 1.00 73.89 C ANISOU 2085 CE2 PHE A 346 10706 6223 11145 2685 221 1140 C ATOM 2086 CZ PHE A 346 15.786 -37.092 -31.514 1.00 74.73 C ANISOU 2086 CZ PHE A 346 10883 6137 11373 2601 53 1368 C ATOM 2087 N TYR A 347 13.365 -36.628 -36.570 1.00 52.96 N ANISOU 2087 N TYR A 347 8872 3208 8041 2225 318 258 N ATOM 2088 CA TYR A 347 12.894 -35.248 -36.521 1.00 47.11 C ANISOU 2088 CA TYR A 347 7892 2861 7147 1972 305 316 C ATOM 2089 C TYR A 347 11.377 -35.193 -36.487 1.00 45.03 C ANISOU 2089 C TYR A 347 7771 2518 6821 1583 140 298 C ATOM 2090 O TYR A 347 10.797 -34.378 -35.770 1.00 41.31 O ANISOU 2090 O TYR A 347 7108 2267 6322 1348 59 461 O ATOM 2091 CB TYR A 347 13.403 -34.431 -37.712 1.00 51.64 C ANISOU 2091 CB TYR A 347 8381 3700 7540 2081 480 132 C ATOM 2092 CG TYR A 347 12.815 -33.036 -37.770 1.00 47.25 C ANISOU 2092 CG TYR A 347 7614 3511 6830 1819 452 187 C ATOM 2093 CD1 TYR A 347 13.347 -32.008 -37.004 1.00 44.65 C ANISOU 2093 CD1 TYR A 347 6943 3507 6514 1831 482 384 C ATOM 2094 CD2 TYR A 347 11.719 -32.752 -38.578 1.00 46.02 C ANISOU 2094 CD2 TYR A 347 7605 3362 6520 1558 380 44 C ATOM 2095 CE1 TYR A 347 12.810 -30.735 -37.044 1.00 40.93 C ANISOU 2095 CE1 TYR A 347 6306 3337 5911 1603 452 427 C ATOM 2096 CE2 TYR A 347 11.174 -31.482 -38.622 1.00 43.28 C ANISOU 2096 CE2 TYR A 347 7070 3329 6045 1343 349 100 C ATOM 2097 CZ TYR A 347 11.725 -30.478 -37.854 1.00 40.81 C ANISOU 2097 CZ TYR A 347 6441 3314 5752 1372 391 287 C ATOM 2098 OH TYR A 347 11.188 -29.212 -37.897 1.00 38.44 O ANISOU 2098 OH TYR A 347 5980 3294 5332 1169 357 334 O ATOM 2099 N HIS A 348 10.729 -36.052 -37.265 1.00 53.25 N ANISOU 2099 N HIS A 348 9144 3251 7838 1514 88 95 N ATOM 2100 CA HIS A 348 9.269 -36.009 -37.324 1.00 52.07 C ANISOU 2100 CA HIS A 348 9101 3052 7634 1129 -77 77 C ATOM 2101 C HIS A 348 8.565 -36.662 -36.121 1.00 52.49 C ANISOU 2101 C HIS A 348 9192 2903 7850 924 -237 295 C ATOM 2102 O HIS A 348 7.536 -36.158 -35.647 1.00 50.19 O ANISOU 2102 O HIS A 348 8801 2740 7530 606 -345 402 O ATOM 2103 CB HIS A 348 8.764 -36.553 -38.661 1.00 60.26 C ANISOU 2103 CB HIS A 348 10465 3873 8557 1077 -100 -220 C ATOM 2104 CG HIS A 348 9.212 -35.743 -39.838 1.00 58.87 C ANISOU 2104 CG HIS A 348 10244 3955 8170 1195 43 -412 C ATOM 2105 ND1 HIS A 348 10.456 -35.891 -40.413 1.00 61.07 N ANISOU 2105 ND1 HIS A 348 10545 4245 8414 1556 242 -534 N ATOM 2106 CD2 HIS A 348 8.591 -34.761 -40.533 1.00 56.26 C ANISOU 2106 CD2 HIS A 348 9836 3891 7649 1001 22 -485 C ATOM 2107 CE1 HIS A 348 10.578 -35.041 -41.418 1.00 59.89 C ANISOU 2107 CE1 HIS A 348 10345 4360 8049 1563 344 -672 C ATOM 2108 NE2 HIS A 348 9.460 -34.345 -41.512 1.00 57.57 N ANISOU 2108 NE2 HIS A 348 10001 4216 7658 1230 203 -643 N ATOM 2109 N TYR A 349 9.114 -37.766 -35.619 1.00 63.30 N ANISOU 2109 N TYR A 349 10685 3976 9390 1115 -244 380 N ATOM 2110 CA TYR A 349 8.590 -38.350 -34.384 1.00 62.03 C ANISOU 2110 CA TYR A 349 10542 3651 9374 935 -382 630 C ATOM 2111 C TYR A 349 8.770 -37.359 -33.233 1.00 58.56 C ANISOU 2111 C TYR A 349 9748 3584 8917 884 -368 890 C ATOM 2112 O TYR A 349 7.884 -37.188 -32.385 1.00 56.09 O ANISOU 2112 O TYR A 349 9359 3343 8610 601 -465 1068 O ATOM 2113 CB TYR A 349 9.279 -39.677 -34.059 1.00 59.70 C ANISOU 2113 CB TYR A 349 10472 2943 9268 1174 -401 679 C ATOM 2114 CG TYR A 349 8.837 -40.839 -34.925 1.00 64.87 C ANISOU 2114 CG TYR A 349 11541 3140 9968 1138 -470 461 C ATOM 2115 CD1 TYR A 349 7.540 -41.331 -34.851 1.00 66.65 C ANISOU 2115 CD1 TYR A 349 11945 3158 10221 759 -640 486 C ATOM 2116 CD2 TYR A 349 9.720 -41.457 -35.802 1.00 68.61 C ANISOU 2116 CD2 TYR A 349 12225 3386 10455 1482 -365 229 C ATOM 2117 CE1 TYR A 349 7.132 -42.396 -35.635 1.00 71.89 C ANISOU 2117 CE1 TYR A 349 13002 3385 10926 699 -728 283 C ATOM 2118 CE2 TYR A 349 9.319 -42.523 -36.590 1.00 73.91 C ANISOU 2118 CE2 TYR A 349 13311 3616 11156 1449 -437 9 C ATOM 2119 CZ TYR A 349 8.025 -42.986 -36.502 1.00 75.49 C ANISOU 2119 CZ TYR A 349 13698 3601 11384 1047 -630 37 C ATOM 2120 OH TYR A 349 7.625 -44.044 -37.284 1.00 81.24 O ANISOU 2120 OH TYR A 349 14853 3874 12141 989 -724 -186 O ATOM 2121 N PHE A 350 9.922 -36.698 -33.226 1.00 55.62 N ANISOU 2121 N PHE A 350 9162 3455 8515 1156 -243 905 N ATOM 2122 CA PHE A 350 10.223 -35.668 -32.242 1.00 52.34 C ANISOU 2122 CA PHE A 350 8419 3405 8060 1125 -230 1116 C ATOM 2123 C PHE A 350 9.263 -34.497 -32.400 1.00 49.65 C ANISOU 2123 C PHE A 350 7947 3350 7566 825 -253 1087 C ATOM 2124 O PHE A 350 8.908 -33.843 -31.422 1.00 46.51 O ANISOU 2124 O PHE A 350 7381 3145 7145 654 -304 1274 O ATOM 2125 CB PHE A 350 11.669 -35.195 -32.397 1.00 74.95 C ANISOU 2125 CB PHE A 350 11080 6486 10912 1446 -93 1095 C ATOM 2126 CG PHE A 350 12.142 -34.301 -31.289 1.00 71.74 C ANISOU 2126 CG PHE A 350 10372 6382 10504 1453 -109 1333 C ATOM 2127 CD1 PHE A 350 12.013 -34.690 -29.968 1.00 69.71 C ANISOU 2127 CD1 PHE A 350 10097 6092 10297 1297 -233 1573 C ATOM 2128 CD2 PHE A 350 12.739 -33.083 -31.569 1.00 70.88 C ANISOU 2128 CD2 PHE A 350 10007 6592 10330 1601 -5 1320 C ATOM 2129 CE1 PHE A 350 12.453 -33.874 -28.944 1.00 66.96 C ANISOU 2129 CE1 PHE A 350 9499 6020 9921 1298 -260 1778 C ATOM 2130 CE2 PHE A 350 13.184 -32.262 -30.548 1.00 68.05 C ANISOU 2130 CE2 PHE A 350 9389 6500 9965 1587 -43 1529 C ATOM 2131 CZ PHE A 350 13.040 -32.659 -29.235 1.00 66.12 C ANISOU 2131 CZ PHE A 350 9148 6216 9757 1440 -175 1750 C ATOM 2132 N TYR A 351 8.845 -34.239 -33.637 1.00 47.64 N ANISOU 2132 N TYR A 351 7780 3119 7201 773 -217 851 N ATOM 2133 CA TYR A 351 7.844 -33.213 -33.906 1.00 45.45 C ANISOU 2133 CA TYR A 351 7402 3078 6790 503 -255 808 C ATOM 2134 C TYR A 351 6.554 -33.581 -33.192 1.00 43.90 C ANISOU 2134 C TYR A 351 7257 2775 6649 193 -390 933 C ATOM 2135 O TYR A 351 5.964 -32.755 -32.476 1.00 40.88 O ANISOU 2135 O TYR A 351 6678 2636 6219 13 -415 1065 O ATOM 2136 CB TYR A 351 7.600 -33.073 -35.412 1.00 49.95 C ANISOU 2136 CB TYR A 351 8118 3623 7236 499 -224 536 C ATOM 2137 CG TYR A 351 6.548 -32.050 -35.783 1.00 47.93 C ANISOU 2137 CG TYR A 351 7753 3614 6844 249 -273 493 C ATOM 2138 CD1 TYR A 351 6.890 -30.722 -35.996 1.00 46.63 C ANISOU 2138 CD1 TYR A 351 7374 3788 6557 301 -191 490 C ATOM 2139 CD2 TYR A 351 5.214 -32.414 -35.928 1.00 47.42 C ANISOU 2139 CD2 TYR A 351 7795 3438 6785 -39 -411 465 C ATOM 2140 CE1 TYR A 351 5.936 -29.784 -36.335 1.00 44.83 C ANISOU 2140 CE1 TYR A 351 7054 3765 6215 97 -244 458 C ATOM 2141 CE2 TYR A 351 4.252 -31.483 -36.268 1.00 45.62 C ANISOU 2141 CE2 TYR A 351 7446 3440 6448 -243 -464 436 C ATOM 2142 CZ TYR A 351 4.618 -30.169 -36.470 1.00 44.30 C ANISOU 2142 CZ TYR A 351 7080 3593 6160 -162 -380 431 C ATOM 2143 OH TYR A 351 3.666 -29.235 -36.809 1.00 42.53 O ANISOU 2143 OH TYR A 351 6744 3579 5836 -344 -440 409 O ATOM 2144 N MET A 352 6.129 -34.828 -33.389 1.00 66.57 N ANISOU 2144 N MET A 352 10394 5277 9623 134 -470 891 N ATOM 2145 CA MET A 352 4.958 -35.355 -32.692 1.00 65.45 C ANISOU 2145 CA MET A 352 10306 5009 9552 -176 -596 1028 C ATOM 2146 C MET A 352 5.066 -35.123 -31.186 1.00 62.82 C ANISOU 2146 C MET A 352 9787 4818 9262 -216 -595 1319 C ATOM 2147 O MET A 352 4.139 -34.600 -30.559 1.00 60.39 O ANISOU 2147 O MET A 352 9332 4698 8914 -462 -627 1439 O ATOM 2148 CB MET A 352 4.787 -36.849 -32.973 1.00 68.34 C ANISOU 2148 CB MET A 352 11006 4912 10047 -204 -684 970 C ATOM 2149 CG MET A 352 4.471 -37.189 -34.417 1.00 70.89 C ANISOU 2149 CG MET A 352 11564 5062 10310 -231 -718 675 C ATOM 2150 SD MET A 352 4.262 -38.963 -34.664 1.00 74.37 S ANISOU 2150 SD MET A 352 12438 4910 10908 -233 -826 594 S ATOM 2151 CE MET A 352 3.817 -39.017 -36.398 1.00 76.63 C ANISOU 2151 CE MET A 352 12958 5099 11057 -349 -890 240 C ATOM 2152 N LEU A 353 6.210 -35.499 -30.619 1.00 47.85 N ANISOU 2152 N LEU A 353 7892 2846 7440 37 -556 1430 N ATOM 2153 CA LEU A 353 6.435 -35.368 -29.179 1.00 48.30 C ANISOU 2153 CA LEU A 353 7808 3020 7523 16 -572 1711 C ATOM 2154 C LEU A 353 6.326 -33.916 -28.700 1.00 44.44 C ANISOU 2154 C LEU A 353 7027 2965 6892 -52 -520 1770 C ATOM 2155 O LEU A 353 5.478 -33.588 -27.860 1.00 44.47 O ANISOU 2155 O LEU A 353 6937 3107 6853 -275 -548 1921 O ATOM 2156 CB LEU A 353 7.801 -35.955 -28.803 1.00 57.86 C ANISOU 2156 CB LEU A 353 9057 4091 8836 334 -554 1806 C ATOM 2157 CG LEU A 353 8.042 -36.439 -27.368 1.00 56.42 C ANISOU 2157 CG LEU A 353 8797 3946 8693 340 -606 2111 C ATOM 2158 CD1 LEU A 353 9.220 -37.402 -27.335 1.00 59.14 C ANISOU 2158 CD1 LEU A 353 9318 3950 9202 590 -646 2193 C ATOM 2159 CD2 LEU A 353 8.286 -35.283 -26.411 1.00 53.71 C ANISOU 2159 CD2 LEU A 353 8166 4004 8238 428 -555 2194 C ATOM 2160 N THR A 354 7.188 -33.056 -29.237 1.00 47.38 N ANISOU 2160 N THR A 354 7266 3545 7189 140 -437 1649 N ATOM 2161 CA THR A 354 7.257 -31.655 -28.825 1.00 44.29 C ANISOU 2161 CA THR A 354 6622 3535 6671 104 -394 1692 C ATOM 2162 C THR A 354 5.923 -30.933 -28.970 1.00 42.44 C ANISOU 2162 C THR A 354 6322 3455 6346 -171 -412 1648 C ATOM 2163 O THR A 354 5.512 -30.188 -28.078 1.00 40.06 O ANISOU 2163 O THR A 354 5873 3369 5979 -293 -412 1778 O ATOM 2164 CB THR A 354 8.321 -30.877 -29.625 1.00 51.50 C ANISOU 2164 CB THR A 354 7423 4618 7525 325 -303 1551 C ATOM 2165 OG1 THR A 354 7.977 -30.881 -31.016 1.00 53.56 O ANISOU 2165 OG1 THR A 354 7799 4804 7746 313 -273 1316 O ATOM 2166 CG2 THR A 354 9.692 -31.504 -29.445 1.00 53.28 C ANISOU 2166 CG2 THR A 354 7652 4741 7851 616 -274 1611 C ATOM 2167 N ASN A 355 5.247 -31.151 -30.093 1.00 40.12 N ANISOU 2167 N ASN A 355 6141 3056 6047 -259 -431 1462 N ATOM 2168 CA ASN A 355 3.965 -30.494 -30.315 1.00 38.55 C ANISOU 2168 CA ASN A 355 5858 3011 5778 -505 -462 1422 C ATOM 2169 C ASN A 355 2.862 -31.038 -29.405 1.00 39.13 C ANISOU 2169 C ASN A 355 5941 3012 5912 -753 -523 1590 C ATOM 2170 O ASN A 355 1.990 -30.286 -28.948 1.00 38.28 O ANISOU 2170 O ASN A 355 5673 3122 5747 -924 -517 1653 O ATOM 2171 CB ASN A 355 3.570 -30.569 -31.786 1.00 58.68 C ANISOU 2171 CB ASN A 355 8523 5478 8293 -542 -490 1189 C ATOM 2172 CG ASN A 355 4.382 -29.625 -32.655 1.00 58.68 C ANISOU 2172 CG ASN A 355 8451 5665 8181 -361 -412 1044 C ATOM 2173 OD1 ASN A 355 3.908 -28.559 -33.040 1.00 57.33 O ANISOU 2173 OD1 ASN A 355 8179 5694 7911 -448 -417 970 O ATOM 2174 ND2 ASN A 355 5.616 -30.009 -32.954 1.00 60.34 N ANISOU 2174 ND2 ASN A 355 8704 5812 8411 -106 -337 1016 N ATOM 2175 N ALA A 356 2.910 -32.342 -29.136 1.00 38.97 N ANISOU 2175 N ALA A 356 6108 2688 6012 -766 -573 1671 N ATOM 2176 CA ALA A 356 2.020 -32.936 -28.144 1.00 42.25 C ANISOU 2176 CA ALA A 356 6538 3030 6487 -1001 -620 1873 C ATOM 2177 C ALA A 356 2.211 -32.231 -26.805 1.00 41.75 C ANISOU 2177 C ALA A 356 6289 3230 6344 -991 -560 2076 C ATOM 2178 O ALA A 356 1.240 -31.907 -26.115 1.00 42.50 O ANISOU 2178 O ALA A 356 6265 3485 6397 -1200 -544 2189 O ATOM 2179 CB ALA A 356 2.284 -34.425 -28.005 1.00 45.31 C ANISOU 2179 CB ALA A 356 7177 3023 7015 -983 -686 1945 C ATOM 2180 N LEU A 357 3.469 -31.979 -26.454 1.00 54.93 N ANISOU 2180 N LEU A 357 7928 4957 7986 -746 -525 2116 N ATOM 2181 CA LEU A 357 3.783 -31.230 -25.240 1.00 52.70 C ANISOU 2181 CA LEU A 357 7489 4931 7604 -725 -487 2286 C ATOM 2182 C LEU A 357 3.236 -29.806 -25.293 1.00 50.30 C ANISOU 2182 C LEU A 357 6983 4961 7168 -798 -429 2206 C ATOM 2183 O LEU A 357 2.773 -29.273 -24.282 1.00 48.75 O ANISOU 2183 O LEU A 357 6679 4965 6881 -896 -395 2334 O ATOM 2184 CB LEU A 357 5.292 -31.206 -24.988 1.00 39.26 C ANISOU 2184 CB LEU A 357 5776 3232 5907 -450 -486 2330 C ATOM 2185 CG LEU A 357 5.903 -32.474 -24.390 1.00 43.01 C ANISOU 2185 CG LEU A 357 6416 3422 6503 -351 -548 2488 C ATOM 2186 CD1 LEU A 357 7.388 -32.285 -24.133 1.00 42.93 C ANISOU 2186 CD1 LEU A 357 6337 3473 6502 -69 -552 2534 C ATOM 2187 CD2 LEU A 357 5.178 -32.858 -23.111 1.00 46.19 C ANISOU 2187 CD2 LEU A 357 6858 3809 6884 -555 -581 2735 C ATOM 2188 N VAL A 358 3.295 -29.194 -26.474 1.00 53.34 N ANISOU 2188 N VAL A 358 7335 5398 7534 -741 -415 1996 N ATOM 2189 CA VAL A 358 2.747 -27.855 -26.672 1.00 51.29 C ANISOU 2189 CA VAL A 358 6904 5420 7165 -799 -374 1913 C ATOM 2190 C VAL A 358 1.260 -27.825 -26.338 1.00 51.01 C ANISOU 2190 C VAL A 358 6804 5450 7127 -1048 -375 1968 C ATOM 2191 O VAL A 358 0.792 -26.935 -25.623 1.00 49.42 O ANISOU 2191 O VAL A 358 6457 5485 6836 -1106 -323 2031 O ATOM 2192 CB VAL A 358 2.962 -27.357 -28.118 1.00 38.17 C ANISOU 2192 CB VAL A 358 5245 3775 5484 -710 -372 1691 C ATOM 2193 CG1 VAL A 358 2.127 -26.115 -28.391 1.00 36.35 C ANISOU 2193 CG1 VAL A 358 4860 3789 5161 -800 -354 1620 C ATOM 2194 CG2 VAL A 358 4.438 -27.084 -28.377 1.00 38.37 C ANISOU 2194 CG2 VAL A 358 5269 3819 5492 -466 -338 1651 C ATOM 2195 N TYR A 359 0.517 -28.804 -26.844 1.00 53.43 N ANISOU 2195 N TYR A 359 7217 5549 7535 -1196 -434 1943 N ATOM 2196 CA TYR A 359 -0.913 -28.863 -26.554 1.00 53.54 C ANISOU 2196 CA TYR A 359 7140 5634 7569 -1450 -439 2011 C ATOM 2197 C TYR A 359 -1.199 -29.251 -25.102 1.00 53.43 C ANISOU 2197 C TYR A 359 7098 5658 7544 -1558 -392 2252 C ATOM 2198 O TYR A 359 -2.229 -28.864 -24.539 1.00 53.09 O ANISOU 2198 O TYR A 359 6905 5804 7464 -1717 -337 2335 O ATOM 2199 CB TYR A 359 -1.634 -29.784 -27.538 1.00 79.44 C ANISOU 2199 CB TYR A 359 10538 8684 10962 -1610 -537 1921 C ATOM 2200 CG TYR A 359 -1.659 -29.224 -28.941 1.00 79.69 C ANISOU 2200 CG TYR A 359 10575 8742 10962 -1544 -582 1687 C ATOM 2201 CD1 TYR A 359 -2.376 -28.068 -29.234 1.00 78.24 C ANISOU 2201 CD1 TYR A 359 10200 8825 10705 -1575 -564 1621 C ATOM 2202 CD2 TYR A 359 -0.962 -29.842 -29.970 1.00 81.65 C ANISOU 2202 CD2 TYR A 359 11032 8748 11243 -1440 -638 1536 C ATOM 2203 CE1 TYR A 359 -2.401 -27.548 -30.513 1.00 78.58 C ANISOU 2203 CE1 TYR A 359 10259 8894 10703 -1520 -616 1429 C ATOM 2204 CE2 TYR A 359 -0.979 -29.329 -31.251 1.00 82.19 C ANISOU 2204 CE2 TYR A 359 11123 8856 11252 -1386 -672 1329 C ATOM 2205 CZ TYR A 359 -1.700 -28.183 -31.517 1.00 80.56 C ANISOU 2205 CZ TYR A 359 10725 8918 10967 -1434 -668 1285 C ATOM 2206 OH TYR A 359 -1.720 -27.671 -32.792 1.00 81.20 O ANISOU 2206 OH TYR A 359 10840 9039 10974 -1386 -713 1099 O ATOM 2207 N VAL A 360 -0.283 -30.008 -24.499 1.00 52.72 N ANISOU 2207 N VAL A 360 7150 5403 7480 -1461 -407 2372 N ATOM 2208 CA VAL A 360 -0.354 -30.283 -23.067 1.00 52.62 C ANISOU 2208 CA VAL A 360 7131 5445 7419 -1534 -365 2614 C ATOM 2209 C VAL A 360 -0.298 -28.962 -22.306 1.00 50.60 C ANISOU 2209 C VAL A 360 6703 5530 6994 -1467 -275 2634 C ATOM 2210 O VAL A 360 -1.068 -28.734 -21.370 1.00 50.53 O ANISOU 2210 O VAL A 360 6607 5690 6904 -1603 -201 2768 O ATOM 2211 CB VAL A 360 0.789 -31.210 -22.596 1.00 51.38 C ANISOU 2211 CB VAL A 360 7155 5055 7312 -1397 -420 2738 C ATOM 2212 CG1 VAL A 360 0.917 -31.178 -21.080 1.00 52.14 C ANISOU 2212 CG1 VAL A 360 7232 5278 7301 -1428 -381 2983 C ATOM 2213 CG2 VAL A 360 0.563 -32.632 -23.086 1.00 53.80 C ANISOU 2213 CG2 VAL A 360 7663 4992 7786 -1496 -504 2758 C ATOM 2214 N SER A 361 0.609 -28.086 -22.732 1.00 43.84 N ANISOU 2214 N SER A 361 5806 4770 6080 -1263 -277 2496 N ATOM 2215 CA SER A 361 0.700 -26.741 -22.174 1.00 42.05 C ANISOU 2215 CA SER A 361 5440 4839 5699 -1199 -210 2476 C ATOM 2216 C SER A 361 -0.585 -25.967 -22.432 1.00 41.68 C ANISOU 2216 C SER A 361 5240 4976 5620 -1326 -147 2398 C ATOM 2217 O SER A 361 -1.015 -25.162 -21.604 1.00 41.17 O ANISOU 2217 O SER A 361 5072 5140 5432 -1345 -65 2440 O ATOM 2218 CB SER A 361 1.883 -25.986 -22.779 1.00 48.40 C ANISOU 2218 CB SER A 361 6228 5686 6475 -984 -237 2337 C ATOM 2219 OG SER A 361 1.852 -24.613 -22.423 1.00 46.88 O ANISOU 2219 OG SER A 361 5915 5752 6145 -947 -188 2290 O ATOM 2220 N ALA A 362 -1.192 -26.212 -23.589 1.00 60.48 N ANISOU 2220 N ALA A 362 7612 7257 8110 -1406 -189 2283 N ATOM 2221 CA ALA A 362 -2.436 -25.539 -23.946 1.00 60.51 C ANISOU 2221 CA ALA A 362 7452 7428 8110 -1520 -153 2215 C ATOM 2222 C ALA A 362 -3.616 -26.018 -23.101 1.00 61.85 C ANISOU 2222 C ALA A 362 7544 7653 8303 -1739 -93 2381 C ATOM 2223 O ALA A 362 -4.640 -25.340 -23.014 1.00 62.16 O ANISOU 2223 O ALA A 362 7406 7883 8330 -1824 -34 2365 O ATOM 2224 CB ALA A 362 -2.735 -25.721 -25.425 1.00103.34 C ANISOU 2224 CB ALA A 362 12895 12740 13630 -1541 -243 2044 C ATOM 2225 N ALA A 363 -3.471 -27.182 -22.474 1.00 49.72 N ANISOU 2225 N ALA A 363 6134 5952 6805 -1828 -105 2552 N ATOM 2226 CA ALA A 363 -4.570 -27.757 -21.698 1.00 51.22 C ANISOU 2226 CA ALA A 363 6261 6181 7021 -2064 -44 2737 C ATOM 2227 C ALA A 363 -4.307 -27.867 -20.191 1.00 51.41 C ANISOU 2227 C ALA A 363 6314 6312 6908 -2072 54 2947 C ATOM 2228 O ALA A 363 -5.179 -28.303 -19.440 1.00 53.79 O ANISOU 2228 O ALA A 363 6541 6703 7193 -2262 142 3113 O ATOM 2229 CB ALA A 363 -4.955 -29.117 -22.265 1.00 61.07 C ANISOU 2229 CB ALA A 363 7637 7127 8440 -2242 -151 2785 C ATOM 2230 N ILE A 364 -3.119 -27.464 -19.749 1.00 64.51 N ANISOU 2230 N ILE A 364 8074 7976 8462 -1876 39 2947 N ATOM 2231 CA ILE A 364 -2.716 -27.681 -18.357 1.00 64.93 C ANISOU 2231 CA ILE A 364 8200 8095 8374 -1881 93 3154 C ATOM 2232 C ILE A 364 -3.346 -26.723 -17.333 1.00 64.98 C ANISOU 2232 C ILE A 364 8073 8432 8185 -1901 248 3192 C ATOM 2233 O ILE A 364 -3.721 -27.145 -16.238 1.00 66.19 O ANISOU 2233 O ILE A 364 8252 8664 8233 -2018 332 3393 O ATOM 2234 CB ILE A 364 -1.171 -27.700 -18.201 1.00 47.54 C ANISOU 2234 CB ILE A 364 6145 5788 6131 -1670 -2 3157 C ATOM 2235 CG1 ILE A 364 -0.778 -28.074 -16.770 1.00 50.72 C ANISOU 2235 CG1 ILE A 364 6647 6232 6391 -1692 16 3397 C ATOM 2236 CG2 ILE A 364 -0.559 -26.366 -18.601 1.00 43.67 C ANISOU 2236 CG2 ILE A 364 5573 5458 5560 -1475 -5 2958 C ATOM 2237 CD1 ILE A 364 -1.236 -29.458 -16.349 1.00 55.03 C ANISOU 2237 CD1 ILE A 364 7298 6597 7015 -1892 11 3626 C ATOM 2238 N ASN A 365 -3.476 -25.449 -17.695 1.00 52.44 N ANISOU 2238 N ASN A 365 6356 7028 6541 -1787 290 3001 N ATOM 2239 CA ASN A 365 -3.921 -24.418 -16.750 1.00 52.79 C ANISOU 2239 CA ASN A 365 6303 7367 6390 -1754 435 2998 C ATOM 2240 C ASN A 365 -5.281 -24.624 -16.056 1.00 54.78 C ANISOU 2240 C ASN A 365 6424 7791 6599 -1936 601 3132 C ATOM 2241 O ASN A 365 -5.363 -24.501 -14.832 1.00 56.80 O ANISOU 2241 O ASN A 365 6715 8207 6662 -1955 717 3257 O ATOM 2242 CB ASN A 365 -3.833 -23.018 -17.376 1.00 66.04 C ANISOU 2242 CB ASN A 365 7882 9167 8042 -1591 436 2762 C ATOM 2243 CG ASN A 365 -2.405 -22.585 -17.636 1.00 64.32 C ANISOU 2243 CG ASN A 365 7781 8857 7799 -1412 312 2663 C ATOM 2244 OD1 ASN A 365 -2.066 -22.154 -18.737 1.00 63.07 O ANISOU 2244 OD1 ASN A 365 7609 8596 7758 -1337 224 2517 O ATOM 2245 ND2 ASN A 365 -1.559 -22.695 -16.620 1.00 64.45 N ANISOU 2245 ND2 ASN A 365 7908 8924 7656 -1350 303 2750 N ATOM 2246 N PRO A 366 -6.349 -24.927 -16.821 1.00 73.78 N ANISOU 2246 N PRO A 366 8677 10181 9176 -2077 615 3111 N ATOM 2247 CA PRO A 366 -7.648 -25.110 -16.159 1.00 75.81 C ANISOU 2247 CA PRO A 366 8769 10628 9407 -2258 784 3253 C ATOM 2248 C PRO A 366 -7.661 -26.300 -15.204 1.00 77.02 C ANISOU 2248 C PRO A 366 9044 10706 9513 -2441 821 3527 C ATOM 2249 O PRO A 366 -8.431 -26.304 -14.244 1.00 78.65 O ANISOU 2249 O PRO A 366 9163 11123 9598 -2549 1001 3675 O ATOM 2250 CB PRO A 366 -8.603 -25.370 -17.329 1.00 55.21 C ANISOU 2250 CB PRO A 366 5989 7959 7029 -2390 725 3187 C ATOM 2251 CG PRO A 366 -7.932 -24.759 -18.511 1.00 50.64 C ANISOU 2251 CG PRO A 366 5451 7266 6524 -2213 577 2953 C ATOM 2252 CD PRO A 366 -6.475 -25.006 -18.288 1.00 48.88 C ANISOU 2252 CD PRO A 366 5475 6871 6226 -2079 484 2955 C ATOM 2253 N ILE A 367 -6.823 -27.296 -15.474 1.00 95.10 N ANISOU 2253 N ILE A 367 11537 12698 11897 -2466 660 3598 N ATOM 2254 CA ILE A 367 -6.721 -28.468 -14.612 1.00 96.36 C ANISOU 2254 CA ILE A 367 11850 12740 12023 -2625 664 3871 C ATOM 2255 C ILE A 367 -6.128 -28.092 -13.257 1.00 96.49 C ANISOU 2255 C ILE A 367 11975 12923 11762 -2522 746 3977 C ATOM 2256 O ILE A 367 -6.590 -28.556 -12.214 1.00 98.11 O ANISOU 2256 O ILE A 367 12203 13238 11836 -2669 868 4202 O ATOM 2257 CB ILE A 367 -5.864 -29.571 -15.265 1.00 63.40 C ANISOU 2257 CB ILE A 367 7888 8178 8021 -2624 458 3900 C ATOM 2258 CG1 ILE A 367 -6.477 -30.001 -16.599 1.00 62.66 C ANISOU 2258 CG1 ILE A 367 7723 7907 8177 -2732 362 3774 C ATOM 2259 CG2 ILE A 367 -5.722 -30.765 -14.332 1.00 68.12 C ANISOU 2259 CG2 ILE A 367 8660 8629 8592 -2783 449 4201 C ATOM 2260 CD1 ILE A 367 -5.692 -31.079 -17.314 1.00 62.42 C ANISOU 2260 CD1 ILE A 367 7919 7484 8314 -2707 171 3760 C ATOM 2261 N LEU A 368 -5.109 -27.239 -13.282 1.00 77.01 N ANISOU 2261 N LEU A 368 9579 10484 9199 -2282 676 3817 N ATOM 2262 CA LEU A 368 -4.447 -26.794 -12.061 1.00 77.15 C ANISOU 2262 CA LEU A 368 9715 10655 8946 -2179 714 3887 C ATOM 2263 C LEU A 368 -5.386 -25.972 -11.185 1.00 78.56 C ANISOU 2263 C LEU A 368 9773 11173 8903 -2210 943 3890 C ATOM 2264 O LEU A 368 -5.377 -26.102 -9.962 1.00 79.79 O ANISOU 2264 O LEU A 368 10033 11464 8822 -2250 1030 4053 O ATOM 2265 CB LEU A 368 -3.197 -25.976 -12.396 1.00 57.64 C ANISOU 2265 CB LEU A 368 7309 8148 6442 -1935 579 3695 C ATOM 2266 CG LEU A 368 -2.071 -26.705 -13.132 1.00 56.30 C ANISOU 2266 CG LEU A 368 7267 7674 6449 -1854 372 3700 C ATOM 2267 CD1 LEU A 368 -0.927 -25.750 -13.441 1.00 52.67 C ANISOU 2267 CD1 LEU A 368 6827 7240 5946 -1628 268 3520 C ATOM 2268 CD2 LEU A 368 -1.579 -27.892 -12.324 1.00 60.19 C ANISOU 2268 CD2 LEU A 368 7943 8022 6904 -1930 306 3977 C ATOM 2269 N TYR A 369 -6.195 -25.129 -11.822 1.00 87.48 N ANISOU 2269 N TYR A 369 10691 12444 10105 -2181 1041 3708 N ATOM 2270 CA TYR A 369 -7.128 -24.258 -11.111 1.00 89.14 C ANISOU 2270 CA TYR A 369 10763 12976 10130 -2170 1274 3677 C ATOM 2271 C TYR A 369 -8.132 -25.061 -10.288 1.00 91.48 C ANISOU 2271 C TYR A 369 11008 13399 10354 -2397 1456 3937 C ATOM 2272 O TYR A 369 -8.458 -24.696 -9.158 1.00 93.08 O ANISOU 2272 O TYR A 369 11228 13848 10293 -2388 1642 4004 O ATOM 2273 CB TYR A 369 -7.877 -23.357 -12.095 1.00 64.61 C ANISOU 2273 CB TYR A 369 7417 9961 7170 -2094 1322 3455 C ATOM 2274 CG TYR A 369 -6.992 -22.466 -12.938 1.00 59.55 C ANISOU 2274 CG TYR A 369 6820 9225 6579 -1879 1169 3205 C ATOM 2275 CD1 TYR A 369 -5.737 -22.070 -12.492 1.00 57.78 C ANISOU 2275 CD1 TYR A 369 6799 8954 6200 -1736 1067 3157 C ATOM 2276 CD2 TYR A 369 -7.418 -22.015 -14.183 1.00 56.88 C ANISOU 2276 CD2 TYR A 369 6317 8853 6441 -1832 1118 3030 C ATOM 2277 CE1 TYR A 369 -4.930 -21.254 -13.264 1.00 53.60 C ANISOU 2277 CE1 TYR A 369 6296 8346 5722 -1563 934 2948 C ATOM 2278 CE2 TYR A 369 -6.621 -21.198 -14.962 1.00 52.64 C ANISOU 2278 CE2 TYR A 369 5827 8232 5939 -1650 986 2822 C ATOM 2279 CZ TYR A 369 -5.378 -20.822 -14.498 1.00 51.05 C ANISOU 2279 CZ TYR A 369 5819 7986 5590 -1522 902 2784 C ATOM 2280 OH TYR A 369 -4.578 -20.012 -15.269 1.00 47.26 O ANISOU 2280 OH TYR A 369 5373 7432 5151 -1364 778 2594 O ATOM 2281 N ASN A 370 -8.616 -26.157 -10.866 1.00 80.29 N ANISOU 2281 N ASN A 370 9535 11811 9161 -2609 1403 4083 N ATOM 2282 CA ASN A 370 -9.599 -27.010 -10.208 1.00 85.69 C ANISOU 2282 CA ASN A 370 10162 12588 9809 -2867 1561 4358 C ATOM 2283 C ASN A 370 -9.034 -27.777 -9.018 1.00 88.84 C ANISOU 2283 C ASN A 370 10818 12943 9995 -2936 1556 4613 C ATOM 2284 O ASN A 370 -9.737 -28.020 -8.037 1.00 92.92 O ANISOU 2284 O ASN A 370 11323 13696 10287 -3033 1765 4782 O ATOM 2285 CB ASN A 370 -10.209 -27.991 -11.210 1.00104.36 C ANISOU 2285 CB ASN A 370 12422 14742 12487 -3100 1468 4444 C ATOM 2286 CG ASN A 370 -11.282 -27.355 -12.070 1.00104.72 C ANISOU 2286 CG ASN A 370 12153 14926 12707 -3115 1531 4281 C ATOM 2287 OD1 ASN A 370 -10.989 -26.665 -13.046 1.00103.90 O ANISOU 2287 OD1 ASN A 370 11951 14962 12564 -2895 1559 4043 O ATOM 2288 ND2 ASN A 370 -12.537 -27.594 -11.714 1.00106.18 N ANISOU 2288 ND2 ASN A 370 12180 15070 13091 -3386 1544 4421 N ATOM 2289 N LEU A 371 -7.765 -28.156 -9.111 1.00 82.92 N ANISOU 2289 N LEU A 371 10297 11896 9313 -2878 1321 4645 N ATOM 2290 CA LEU A 371 -7.121 -28.940 -8.064 1.00 86.25 C ANISOU 2290 CA LEU A 371 10971 12222 9578 -2944 1264 4911 C ATOM 2291 C LEU A 371 -6.891 -28.134 -6.790 1.00 87.77 C ANISOU 2291 C LEU A 371 11266 12698 9386 -2849 1391 4952 C ATOM 2292 O LEU A 371 -7.261 -28.563 -5.698 1.00 92.61 O ANISOU 2292 O LEU A 371 11979 13407 9801 -2997 1498 5217 O ATOM 2293 CB LEU A 371 -5.792 -29.507 -8.568 1.00 79.24 C ANISOU 2293 CB LEU A 371 10285 10984 8839 -2823 981 4890 C ATOM 2294 CG LEU A 371 -5.878 -30.593 -9.641 1.00 80.40 C ANISOU 2294 CG LEU A 371 10494 10762 9293 -2969 829 4998 C ATOM 2295 CD1 LEU A 371 -4.500 -30.902 -10.197 1.00 80.17 C ANISOU 2295 CD1 LEU A 371 10239 10727 9496 -3129 894 4902 C ATOM 2296 CD2 LEU A 371 -6.522 -31.850 -9.074 1.00 76.80 C ANISOU 2296 CD2 LEU A 371 10183 10017 8980 -2757 585 4870 C ATOM 2297 N VAL A 372 -6.283 -26.963 -6.940 1.00 93.89 N ANISOU 2297 N VAL A 372 12028 13601 10044 -2613 1376 4693 N ATOM 2298 CA VAL A 372 -5.872 -26.150 -5.800 1.00 94.86 C ANISOU 2298 CA VAL A 372 12288 13962 9794 -2509 1457 4692 C ATOM 2299 C VAL A 372 -7.037 -25.426 -5.119 1.00 96.98 C ANISOU 2299 C VAL A 372 12415 14587 9845 -2549 1774 4667 C ATOM 2300 O VAL A 372 -7.090 -25.338 -3.891 1.00 99.08 O ANISOU 2300 O VAL A 372 12800 15041 9804 -2621 1915 4842 O ATOM 2301 CB VAL A 372 -4.789 -25.130 -6.218 1.00 75.84 C ANISOU 2301 CB VAL A 372 9951 11523 7342 -2254 1290 4431 C ATOM 2302 CG1 VAL A 372 -5.296 -24.258 -7.352 1.00 71.27 C ANISOU 2302 CG1 VAL A 372 9158 10939 6982 -2143 1304 4139 C ATOM 2303 CG2 VAL A 372 -4.350 -24.283 -5.032 1.00 77.33 C ANISOU 2303 CG2 VAL A 372 10278 11967 7136 -2162 1374 4393 C ATOM 2304 N SER A 373 -7.973 -24.919 -5.915 1.00 91.42 N ANISOU 2304 N SER A 373 11459 13981 9294 -2492 1888 4455 N ATOM 2305 CA SER A 373 -9.065 -24.112 -5.386 1.00 93.55 C ANISOU 2305 CA SER A 373 11565 14593 9387 -2473 2195 4391 C ATOM 2306 C SER A 373 -10.386 -24.871 -5.400 1.00 95.17 C ANISOU 2306 C SER A 373 11524 14892 9746 -2706 2387 4572 C ATOM 2307 O SER A 373 -10.833 -25.339 -6.447 1.00 94.24 O ANISOU 2307 O SER A 373 11225 14621 9962 -2789 2299 4544 O ATOM 2308 CB SER A 373 -9.199 -22.809 -6.178 1.00 81.05 C ANISOU 2308 CB SER A 373 9854 13084 7856 -2233 2206 4044 C ATOM 2309 OG SER A 373 -10.235 -21.998 -5.654 1.00 83.54 O ANISOU 2309 OG SER A 373 9980 13711 8052 -2192 2509 3975 O ATOM 2310 N ALA A 374 -11.005 -24.987 -4.230 1.00128.89 N ANISOU 2310 N ALA A 374 15787 19424 13761 -2822 2649 4761 N ATOM 2311 CA ALA A 374 -12.292 -25.657 -4.107 1.00130.83 C ANISOU 2311 CA ALA A 374 15779 19806 14122 -3066 2863 4964 C ATOM 2312 C ALA A 374 -13.398 -24.817 -4.736 1.00131.45 C ANISOU 2312 C ALA A 374 15494 20075 14376 -2979 3024 4758 C ATOM 2313 O ALA A 374 -14.336 -25.352 -5.326 1.00132.28 O ANISOU 2313 O ALA A 374 15330 20198 14732 -3173 3085 4868 O ATOM 2314 CB ALA A 374 -12.605 -25.943 -2.648 1.00160.02 C ANISOU 2314 CB ALA A 374 19564 23770 17464 -3194 3128 5216 C ATOM 2315 N ASN A 375 -13.276 -23.499 -4.607 1.00151.21 N ANISOU 2315 N ASN A 375 17992 22710 16753 -2690 3079 4467 N ATOM 2316 CA ASN A 375 -14.262 -22.572 -5.152 1.00152.17 C ANISOU 2316 CA ASN A 375 17783 23015 17019 -2560 3232 4265 C ATOM 2317 C ASN A 375 -14.368 -22.678 -6.668 1.00150.13 C ANISOU 2317 C ASN A 375 17352 22522 17169 -2572 2993 4146 C ATOM 2318 O ASN A 375 -15.429 -23.009 -7.207 1.00151.13 O ANISOU 2318 O ASN A 375 17153 22740 17530 -2681 3075 4183 O ATOM 2319 CB ASN A 375 -13.915 -21.135 -4.758 1.00149.57 C ANISOU 2319 CB ASN A 375 17546 22841 16443 -2237 3328 3979 C ATOM 2320 CG ASN A 375 -13.650 -20.986 -3.274 1.00151.60 C ANISOU 2320 CG ASN A 375 18053 23293 16253 -2209 3513 4060 C ATOM 2321 OD1 ASN A 375 -14.574 -20.808 -2.481 1.00154.43 O ANISOU 2321 OD1 ASN A 375 18290 23971 16416 -2185 3845 4090 O ATOM 2322 ND2 ASN A 375 -12.380 -21.056 -2.890 1.00150.33 N ANISOU 2322 ND2 ASN A 375 18241 22953 15923 -2205 3298 4095 N ATOM 2323 N PHE A 376 -13.255 -22.405 -7.346 1.00163.36 N ANISOU 2323 N PHE A 376 19242 23908 18921 -2465 2699 4008 N ATOM 2324 CA PHE A 376 -13.197 -22.457 -8.803 1.00161.46 C ANISOU 2324 CA PHE A 376 18888 23432 19027 -2468 2463 3886 C ATOM 2325 C PHE A 376 -13.604 -23.829 -9.323 1.00161.63 C ANISOU 2325 C PHE A 376 18822 23303 19288 -2782 2387 4124 C ATOM 2326 O PHE A 376 -14.136 -23.947 -10.422 1.00161.81 O ANISOU 2326 O PHE A 376 18610 23279 19591 -2871 2321 4086 O ATOM 2327 CB PHE A 376 -11.793 -22.104 -9.303 1.00132.97 C ANISOU 2327 CB PHE A 376 15546 19552 15423 -2307 2185 3727 C ATOM 2328 CG PHE A 376 -11.689 -22.006 -10.801 1.00132.24 C ANISOU 2328 CG PHE A 376 15523 19561 15160 -2018 2210 3465 C ATOM 2329 CD1 PHE A 376 -11.931 -20.804 -11.446 1.00131.71 C ANISOU 2329 CD1 PHE A 376 15311 19471 15263 -1854 2143 3224 C ATOM 2330 CD2 PHE A 376 -11.348 -23.112 -11.564 1.00132.27 C ANISOU 2330 CD2 PHE A 376 15755 19672 14828 -1920 2285 3463 C ATOM 2331 CE1 PHE A 376 -11.837 -20.708 -12.821 1.00131.32 C ANISOU 2331 CE1 PHE A 376 15345 19484 15067 -1600 2155 2992 C ATOM 2332 CE2 PHE A 376 -11.255 -23.022 -12.940 1.00131.85 C ANISOU 2332 CE2 PHE A 376 15789 19686 14621 -1673 2291 3216 C ATOM 2333 CZ PHE A 376 -11.498 -21.818 -13.569 1.00131.40 C ANISOU 2333 CZ PHE A 376 15588 19587 14752 -1514 2228 2981 C ATOM 2334 N ARG A 377 -13.344 -24.862 -8.530 1.00104.94 N ANISOU 2334 N ARG A 377 11844 16045 11984 -2956 2387 4377 N ATOM 2335 CA ARG A 377 -13.752 -26.214 -8.880 1.00105.48 C ANISOU 2335 CA ARG A 377 11887 15942 12249 -3274 2316 4633 C ATOM 2336 C ARG A 377 -15.270 -26.340 -8.812 1.00108.31 C ANISOU 2336 C ARG A 377 11903 16573 12679 -3480 2564 4781 C ATOM 2337 O ARG A 377 -15.895 -26.928 -9.696 1.00109.23 O ANISOU 2337 O ARG A 377 11893 16570 13041 -3754 2496 4936 O ATOM 2338 CB ARG A 377 -13.088 -27.223 -7.944 1.00117.83 C ANISOU 2338 CB ARG A 377 13773 17364 13632 -3380 2263 4878 C ATOM 2339 CG ARG A 377 -13.491 -28.666 -8.178 1.00119.60 C ANISOU 2339 CG ARG A 377 14031 17381 14029 -3715 2194 5175 C ATOM 2340 CD ARG A 377 -12.537 -29.603 -7.459 1.00119.19 C ANISOU 2340 CD ARG A 377 14344 17119 13824 -3742 2068 5372 C ATOM 2341 NE ARG A 377 -12.313 -29.189 -6.077 1.00120.33 N ANISOU 2341 NE ARG A 377 14592 17544 13584 -3701 2279 5499 N ATOM 2342 CZ ARG A 377 -11.218 -29.473 -5.381 1.00120.29 C ANISOU 2342 CZ ARG A 377 14889 17477 13340 -3565 2181 5533 C ATOM 2343 NH1 ARG A 377 -10.239 -30.170 -5.940 1.00119.22 N ANISOU 2343 NH1 ARG A 377 14952 17017 13329 -3444 1888 5455 N ATOM 2344 NH2 ARG A 377 -11.097 -29.054 -4.129 1.00121.57 N ANISOU 2344 NH2 ARG A 377 15148 17914 13131 -3545 2376 5642 N ATOM 2345 N GLN A 378 -15.856 -25.772 -7.762 1.00177.15 N ANISOU 2345 N GLN A 378 20465 25656 21187 -3346 2851 4726 N ATOM 2346 CA GLN A 378 -17.304 -25.792 -7.583 1.00179.82 C ANISOU 2346 CA GLN A 378 20427 26305 21593 -3497 3119 4847 C ATOM 2347 C GLN A 378 -18.025 -25.034 -8.693 1.00179.59 C ANISOU 2347 C GLN A 378 20058 26330 21847 -3402 3068 4637 C ATOM 2348 O GLN A 378 -19.099 -25.443 -9.133 1.00180.76 O ANISOU 2348 O GLN A 378 19897 26553 22231 -3628 3102 4761 O ATOM 2349 CB GLN A 378 -17.693 -25.220 -6.217 1.00204.89 C ANISOU 2349 CB GLN A 378 23582 29862 24407 -3389 3480 4894 C ATOM 2350 CG GLN A 378 -17.399 -26.144 -5.047 1.00206.44 C ANISOU 2350 CG GLN A 378 23493 30374 24573 -3124 3703 4661 C ATOM 2351 CD GLN A 378 -17.688 -25.497 -3.707 1.00208.73 C ANISOU 2351 CD GLN A 378 23339 30904 25067 -3274 3903 4763 C ATOM 2352 OE1 GLN A 378 -18.013 -24.312 -3.632 1.00209.95 O ANISOU 2352 OE1 GLN A 378 23474 31056 25242 -3508 3985 4954 O ATOM 2353 NE2 GLN A 378 -17.571 -26.276 -2.638 1.00209.55 N ANISOU 2353 NE2 GLN A 378 23118 31154 25348 -3103 3938 4581 N ATOM 2354 N VAL A 379 -17.433 -23.931 -9.145 1.00210.18 N ANISOU 2354 N VAL A 379 23993 30162 25705 -3085 2969 4332 N ATOM 2355 CA VAL A 379 -18.039 -23.134 -10.210 1.00210.22 C ANISOU 2355 CA VAL A 379 23690 30230 25953 -2968 2920 4136 C ATOM 2356 C VAL A 379 -17.837 -23.795 -11.583 1.00208.37 C ANISOU 2356 C VAL A 379 23451 29679 26042 -3117 2589 4107 C ATOM 2357 O VAL A 379 -18.736 -23.791 -12.441 1.00208.98 O ANISOU 2357 O VAL A 379 23219 29820 26364 -3168 2541 4061 O ATOM 2358 CB VAL A 379 -17.497 -21.690 -10.211 1.00 94.34 C ANISOU 2358 CB VAL A 379 9069 15629 11147 -2577 2945 3828 C ATOM 2359 CG1 VAL A 379 -18.417 -20.785 -10.997 1.00 98.06 C ANISOU 2359 CG1 VAL A 379 9403 16476 11376 -2422 3311 3819 C ATOM 2360 CG2 VAL A 379 -17.373 -21.173 -8.788 1.00 89.64 C ANISOU 2360 CG2 VAL A 379 8889 14777 10391 -2439 2751 3713 C ATOM 2361 N PHE A 380 -16.652 -24.371 -11.772 1.00143.93 N ANISOU 2361 N PHE A 380 15630 21182 17877 -3177 2359 4131 N ATOM 2362 CA PHE A 380 -16.329 -25.135 -12.972 1.00142.33 C ANISOU 2362 CA PHE A 380 15467 20660 17953 -3319 2057 4099 C ATOM 2363 C PHE A 380 -17.335 -26.267 -13.130 1.00144.18 C ANISOU 2363 C PHE A 380 15473 20929 18379 -3688 2093 4345 C ATOM 2364 O PHE A 380 -17.810 -26.541 -14.232 1.00144.46 O ANISOU 2364 O PHE A 380 15265 20959 18666 -3797 1983 4299 O ATOM 2365 CB PHE A 380 -14.911 -25.706 -12.864 1.00156.53 C ANISOU 2365 CB PHE A 380 17673 22105 19695 -3301 1845 4103 C ATOM 2366 CG PHE A 380 -14.370 -26.260 -14.155 1.00154.99 C ANISOU 2366 CG PHE A 380 17570 21557 19761 -3409 1544 4040 C ATOM 2367 CD1 PHE A 380 -14.763 -27.508 -14.611 1.00153.14 C ANISOU 2367 CD1 PHE A 380 17674 21005 19505 -3331 1348 3996 C ATOM 2368 CD2 PHE A 380 -13.455 -25.537 -14.905 1.00155.62 C ANISOU 2368 CD2 PHE A 380 17404 21627 20097 -3580 1454 4021 C ATOM 2369 CE1 PHE A 380 -14.267 -28.019 -15.795 1.00152.05 C ANISOU 2369 CE1 PHE A 380 17643 20544 19582 -3406 1096 3921 C ATOM 2370 CE2 PHE A 380 -12.955 -26.044 -16.091 1.00154.45 C ANISOU 2370 CE2 PHE A 380 17379 21152 20153 -3677 1179 3946 C ATOM 2371 CZ PHE A 380 -13.361 -27.287 -16.535 1.00152.71 C ANISOU 2371 CZ PHE A 380 17513 20613 19895 -3582 1012 3889 C ATOM 2372 N LEU A 381 -17.652 -26.922 -12.018 1.00106.29 N ANISOU 2372 N LEU A 381 10755 16176 13455 -3892 2240 4616 N ATOM 2373 CA LEU A 381 -18.640 -27.992 -12.018 1.00108.31 C ANISOU 2373 CA LEU A 381 10810 16465 13878 -4277 2287 4887 C ATOM 2374 C LEU A 381 -20.058 -27.429 -12.056 1.00110.52 C ANISOU 2374 C LEU A 381 10606 17128 14259 -4310 2492 4893 C ATOM 2375 O LEU A 381 -21.005 -28.142 -12.381 1.00112.35 O ANISOU 2375 O LEU A 381 10605 17339 14746 -4564 2409 4974 O ATOM 2376 CB LEU A 381 -18.457 -28.902 -10.800 1.00108.26 C ANISOU 2376 CB LEU A 381 10987 16472 13673 -4465 2442 5191 C ATOM 2377 CG LEU A 381 -17.155 -29.704 -10.751 1.00106.58 C ANISOU 2377 CG LEU A 381 11219 15847 13429 -4509 2211 5260 C ATOM 2378 CD1 LEU A 381 -17.126 -30.610 -9.531 1.00109.61 C ANISOU 2378 CD1 LEU A 381 11803 16241 13601 -4628 2352 5511 C ATOM 2379 CD2 LEU A 381 -16.972 -30.510 -12.030 1.00106.23 C ANISOU 2379 CD2 LEU A 381 11227 15428 13708 -4731 1911 5263 C ATOM 2380 N SER A 382 -20.201 -26.151 -11.719 1.00345.43 N ANISOU 2380 N SER A 382 40233 47201 43815 -4020 2738 4771 N ATOM 2381 CA SER A 382 -21.499 -25.492 -11.796 1.00347.73 C ANISOU 2381 CA SER A 382 40054 47874 44195 -3982 2954 4760 C ATOM 2382 C SER A 382 -21.907 -25.331 -13.252 1.00346.98 C ANISOU 2382 C SER A 382 39726 47712 44401 -3935 2722 4574 C ATOM 2383 O SER A 382 -23.059 -25.580 -13.611 1.00348.79 O ANISOU 2383 O SER A 382 39576 48108 44843 -4082 2750 4640 O ATOM 2384 CB SER A 382 -21.463 -24.125 -11.108 1.00204.30 C ANISOU 2384 CB SER A 382 21866 30017 25743 -3627 3251 4624 C ATOM 2385 OG SER A 382 -20.953 -24.222 -9.788 1.00204.17 O ANISOU 2385 OG SER A 382 22161 30014 25402 -3626 3404 4743 O ATOM 2386 N THR A 383 -20.960 -24.914 -14.089 1.00170.59 N ANISOU 2386 N THR A 383 17636 25112 22069 -3712 2475 4321 N ATOM 2387 CA THR A 383 -21.223 -24.796 -15.524 1.00169.79 C ANISOU 2387 CA THR A 383 17373 24927 22213 -3647 2234 4134 C ATOM 2388 C THR A 383 -21.487 -26.149 -16.158 1.00169.51 C ANISOU 2388 C THR A 383 17294 24660 22453 -4008 1965 4241 C ATOM 2389 O THR A 383 -22.547 -26.384 -16.742 1.00169.94 O ANISOU 2389 O THR A 383 17052 24783 22734 -4075 1840 4193 O ATOM 2390 CB THR A 383 -20.021 -24.169 -16.267 1.00130.13 C ANISOU 2390 CB THR A 383 12660 19683 17100 -3328 2053 3852 C ATOM 2391 OG1 THR A 383 -18.857 -24.259 -15.436 1.00128.61 O ANISOU 2391 OG1 THR A 383 12863 19328 16674 -3278 2079 3882 O ATOM 2392 CG2 THR A 383 -20.285 -22.704 -16.580 1.00130.86 C ANISOU 2392 CG2 THR A 383 12585 20025 17112 -2966 2199 3654 C ATOM 2393 N LEU A 384 -20.489 -27.022 -16.055 1.00137.75 N ANISOU 2393 N LEU A 384 13578 20351 18409 -4237 1862 4383 N ATOM 2394 CA LEU A 384 -20.538 -28.352 -16.654 1.00137.73 C ANISOU 2394 CA LEU A 384 13593 20083 18652 -4594 1604 4481 C ATOM 2395 C LEU A 384 -21.769 -29.128 -16.191 1.00140.48 C ANISOU 2395 C LEU A 384 13527 20667 19180 -4918 1703 4701 C ATOM 2396 O LEU A 384 -21.709 -29.882 -15.225 1.00141.76 O ANISOU 2396 O LEU A 384 13502 21128 19229 -4856 1996 4783 O ATOM 2397 CB LEU A 384 -19.263 -29.123 -16.309 1.00132.83 C ANISOU 2397 CB LEU A 384 13404 19100 17965 -4746 1499 4602 C ATOM 2398 CG LEU A 384 -18.661 -30.013 -17.391 1.00126.19 C ANISOU 2398 CG LEU A 384 12982 17970 16994 -4460 1347 4392 C ATOM 2399 CD1 LEU A 384 -17.242 -30.424 -17.018 1.00127.12 C ANISOU 2399 CD1 LEU A 384 13472 17805 17023 -4585 1311 4565 C ATOM 2400 CD2 LEU A 384 -19.526 -31.242 -17.629 1.00122.41 C ANISOU 2400 CD2 LEU A 384 12568 17248 16693 -4409 1040 4156 C TER 2401 LEU A 384 ATOM 2402 N SER B 49 -0.214 36.891 -38.393 1.00125.03 N ATOM 2403 CA SER B 49 0.588 37.153 -39.582 1.00125.03 C ATOM 2404 C SER B 49 0.158 36.273 -40.750 1.00125.03 C ATOM 2405 O SER B 49 -1.007 35.889 -40.855 1.00125.03 O ATOM 2406 CB SER B 49 2.075 36.939 -39.286 1.00118.93 C ATOM 2407 OG SER B 49 2.544 37.868 -38.325 1.00118.93 O ATOM 2408 N GLY B 50 1.107 35.958 -41.625 1.00162.91 N ATOM 2409 CA GLY B 50 0.834 35.129 -42.785 1.00162.91 C ATOM 2410 C GLY B 50 1.936 34.119 -43.045 1.00162.91 C ATOM 2411 O GLY B 50 3.043 34.262 -42.526 1.00162.91 O ATOM 2412 N PRO B 51 1.641 33.087 -43.852 1.00213.07 N ATOM 2413 CA PRO B 51 0.335 32.848 -44.478 1.00213.07 C ATOM 2414 C PRO B 51 -0.663 32.238 -43.497 1.00213.07 C ATOM 2415 O PRO B 51 -0.330 32.047 -42.327 1.00213.07 O ATOM 2416 CB PRO B 51 0.665 31.844 -45.582 1.00 88.90 C ATOM 2417 CG PRO B 51 1.825 31.086 -45.044 1.00 88.90 C ATOM 2418 CD PRO B 51 2.638 32.080 -44.261 1.00 88.90 C ATOM 2419 N ASN B 52 -1.867 31.932 -43.972 1.00124.48 N ANISOU 2419 N ASN B 52 22537 7964 16799 473 -4782 3327 N ATOM 2420 CA ASN B 52 -2.923 31.409 -43.107 1.00120.73 C ANISOU 2420 CA ASN B 52 21756 7959 16158 303 -4701 3514 C ATOM 2421 C ASN B 52 -2.747 29.943 -42.720 1.00116.14 C ANISOU 2421 C ASN B 52 20972 7642 15515 263 -4560 3329 C ATOM 2422 O ASN B 52 -3.697 29.161 -42.754 1.00114.60 O ANISOU 2422 O ASN B 52 20822 7448 15276 -48 -4486 3222 O ATOM 2423 CB ASN B 52 -4.300 31.627 -43.740 1.00155.37 C ANISOU 2423 CB ASN B 52 26186 12447 20400 -194 -4711 3811 C ATOM 2424 CG ASN B 52 -4.742 33.076 -43.690 1.00156.11 C ANISOU 2424 CG ASN B 52 26461 12364 20489 -600 -4699 3755 C ATOM 2425 OD1 ASN B 52 -3.923 33.984 -43.542 1.00153.04 O ANISOU 2425 OD1 ASN B 52 25929 12215 20004 -887 -4588 3725 O ATOM 2426 ND2 ASN B 52 -6.045 33.301 -43.808 1.00160.44 N ANISOU 2426 ND2 ASN B 52 27317 12497 21146 -629 -4821 3745 N ATOM 2427 N SER B 53 -1.523 29.580 -42.355 1.00279.01 N ANISOU 2427 N SER B 53 41241 28647 36123 565 -4441 3222 N ATOM 2428 CA SER B 53 -1.238 28.261 -41.811 1.00275.07 C ANISOU 2428 CA SER B 53 40367 28611 35534 533 -4197 2989 C ATOM 2429 C SER B 53 -0.774 28.429 -40.372 1.00276.82 C ANISOU 2429 C SER B 53 40683 28684 35811 543 -4110 2668 C ATOM 2430 O SER B 53 0.389 28.184 -40.050 1.00275.46 O ANISOU 2430 O SER B 53 40484 28631 35546 188 -4025 2623 O ATOM 2431 CB SER B 53 -0.163 27.557 -42.638 1.00 99.33 C ANISOU 2431 CB SER B 53 17920 6739 13081 95 -4094 3167 C ATOM 2432 OG SER B 53 1.027 28.324 -42.686 1.00101.65 O ANISOU 2432 OG SER B 53 18209 7122 13291 38 -4191 3481 O ATOM 2433 N ASP B 54 -1.693 28.857 -39.512 1.00124.27 N ANISOU 2433 N ASP B 54 21469 9113 16635 956 -4130 2444 N ATOM 2434 CA ASP B 54 -1.364 29.172 -38.124 1.00125.14 C ANISOU 2434 CA ASP B 54 21736 9033 16779 987 -4063 2130 C ATOM 2435 C ASP B 54 -1.025 27.939 -37.285 1.00121.53 C ANISOU 2435 C ASP B 54 20926 9019 16230 1021 -3818 1873 C ATOM 2436 O ASP B 54 -1.727 27.611 -36.329 1.00122.78 O ANISOU 2436 O ASP B 54 21048 9159 16442 1357 -3717 1596 O ATOM 2437 CB ASP B 54 -2.497 29.970 -37.470 1.00162.71 C ANISOU 2437 CB ASP B 54 26783 13326 21712 1424 -4164 1973 C ATOM 2438 CG ASP B 54 -3.845 29.295 -37.614 1.00168.23 C ANISOU 2438 CG ASP B 54 27910 13498 22510 1354 -4425 2206 C ATOM 2439 OD1 ASP B 54 -3.945 28.330 -38.401 1.00171.09 O ANISOU 2439 OD1 ASP B 54 28632 13495 22879 1090 -4525 2174 O ATOM 2440 OD2 ASP B 54 -4.804 29.735 -36.947 1.00169.93 O ANISOU 2440 OD2 ASP B 54 28110 13659 22795 1551 -4544 2431 O ATOM 2441 N LEU B 55 0.059 27.262 -37.649 1.00 92.11 N ANISOU 2441 N LEU B 55 16948 5690 12362 674 -3717 1978 N ATOM 2442 CA LEU B 55 0.557 26.136 -36.870 1.00 85.95 C ANISOU 2442 CA LEU B 55 15870 5306 11482 616 -3504 1773 C ATOM 2443 C LEU B 55 1.728 26.601 -36.013 1.00 86.37 C ANISOU 2443 C LEU B 55 16132 5200 11486 303 -3519 1653 C ATOM 2444 O LEU B 55 2.516 25.792 -35.524 1.00 82.58 O ANISOU 2444 O LEU B 55 15467 5016 10894 -7 -3425 1667 O ATOM 2445 CB LEU B 55 0.991 24.984 -37.781 1.00 92.93 C ANISOU 2445 CB LEU B 55 16395 6671 12244 407 -3399 1946 C ATOM 2446 CG LEU B 55 -0.077 24.259 -38.609 1.00 90.40 C ANISOU 2446 CG LEU B 55 15743 6675 11930 696 -3315 1961 C ATOM 2447 CD1 LEU B 55 -1.367 24.104 -37.813 1.00 95.11 C ANISOU 2447 CD1 LEU B 55 16466 7044 12627 936 -3489 2137 C ATOM 2448 CD2 LEU B 55 -0.343 24.975 -39.924 1.00 85.99 C ANISOU 2448 CD2 LEU B 55 14883 6563 11229 439 -3205 2092 C ATOM 2449 N ASP B 56 1.826 27.914 -35.833 1.00 89.94 N ANISOU 2449 N ASP B 56 16971 5179 12024 395 -3646 1528 N ATOM 2450 CA ASP B 56 2.915 28.519 -35.076 1.00 92.14 C ANISOU 2450 CA ASP B 56 17525 5216 12265 57 -3731 1452 C ATOM 2451 C ASP B 56 2.816 28.201 -33.588 1.00 91.83 C ANISOU 2451 C ASP B 56 17607 5080 12205 239 -3657 1080 C ATOM 2452 O ASP B 56 1.761 28.369 -32.977 1.00 91.59 O ANISOU 2452 O ASP B 56 17533 5047 12218 676 -3559 881 O ATOM 2453 CB ASP B 56 2.921 30.036 -35.276 1.00110.10 C ANISOU 2453 CB ASP B 56 20225 6969 14639 -80 -3976 1633 C ATOM 2454 CG ASP B 56 2.988 30.433 -36.737 1.00110.79 C ANISOU 2454 CG ASP B 56 20497 6728 14870 374 -4064 1627 C ATOM 2455 OD1 ASP B 56 1.918 30.575 -37.364 1.00109.17 O ANISOU 2455 OD1 ASP B 56 20188 6590 14703 804 -3945 1386 O ATOM 2456 OD2 ASP B 56 4.111 30.607 -37.257 1.00114.50 O ANISOU 2456 OD2 ASP B 56 21205 6882 15418 303 -4249 1876 O ATOM 2457 N VAL B 57 3.921 27.742 -33.010 1.00 92.19 N ANISOU 2457 N VAL B 57 17791 5065 12171 -109 -3704 995 N ATOM 2458 CA VAL B 57 3.985 27.485 -31.578 1.00 92.00 C ANISOU 2458 CA VAL B 57 17894 4983 12077 -12 -3644 651 C ATOM 2459 C VAL B 57 4.541 28.702 -30.848 1.00 98.49 C ANISOU 2459 C VAL B 57 19202 5304 12915 -237 -3856 559 C ATOM 2460 O VAL B 57 5.685 29.101 -31.066 1.00101.65 O ANISOU 2460 O VAL B 57 19750 5520 13353 -620 -4031 788 O ATOM 2461 CB VAL B 57 4.855 26.258 -31.259 1.00 85.66 C ANISOU 2461 CB VAL B 57 16751 4670 11127 -228 -3490 593 C ATOM 2462 CG1 VAL B 57 5.064 26.135 -29.760 1.00 86.10 C ANISOU 2462 CG1 VAL B 57 16798 4774 11142 -770 -3608 803 C ATOM 2463 CG2 VAL B 57 4.217 24.997 -31.822 1.00 79.52 C ANISOU 2463 CG2 VAL B 57 15511 4372 10331 -32 -3287 673 C ATOM 2464 N ASN B 58 3.723 29.289 -29.980 1.00157.26 N ANISOU 2464 N ASN B 58 26902 12523 20325 1 -3838 224 N ATOM 2465 CA ASN B 58 4.096 30.514 -29.283 1.00159.50 C ANISOU 2465 CA ASN B 58 27696 12291 20617 -169 -4047 84 C ATOM 2466 C ASN B 58 4.946 30.277 -28.037 1.00158.55 C ANISOU 2466 C ASN B 58 27612 12294 20337 -524 -4075 -72 C ATOM 2467 O ASN B 58 4.446 30.327 -26.914 1.00160.14 O ANISOU 2467 O ASN B 58 28113 12274 20457 -415 -4097 -387 O ATOM 2468 CB ASN B 58 2.850 31.326 -28.923 1.00182.83 C ANISOU 2468 CB ASN B 58 30992 14842 23632 329 -4037 -200 C ATOM 2469 CG ASN B 58 2.084 31.790 -30.148 1.00187.90 C ANISOU 2469 CG ASN B 58 31660 15275 24459 666 -4072 -28 C ATOM 2470 OD1 ASN B 58 2.664 32.001 -31.213 1.00191.81 O ANISOU 2470 OD1 ASN B 58 32266 15558 25055 438 -4251 268 O ATOM 2471 ND2 ASN B 58 0.774 31.951 -30.002 1.00187.91 N ANISOU 2471 ND2 ASN B 58 31543 15351 24502 1207 -3900 -196 N ATOM 2472 N THR B 59 6.233 30.021 -28.247 1.00103.02 N ANISOU 2472 N THR B 59 20277 5613 13254 -944 -4079 151 N ATOM 2473 CA THR B 59 7.184 29.899 -27.149 1.00102.85 C ANISOU 2473 CA THR B 59 20271 5704 13104 -1335 -4151 63 C ATOM 2474 C THR B 59 8.290 30.937 -27.312 1.00109.83 C ANISOU 2474 C THR B 59 21521 6156 14052 -1774 -4443 181 C ATOM 2475 O THR B 59 8.882 31.060 -28.385 1.00111.00 O ANISOU 2475 O THR B 59 21603 6270 14304 -2036 -4531 506 O ATOM 2476 CB THR B 59 7.797 28.489 -27.078 1.00 95.90 C ANISOU 2476 CB THR B 59 18872 5413 12153 -1566 -4016 248 C ATOM 2477 OG1 THR B 59 8.343 28.138 -28.355 1.00 95.52 O ANISOU 2477 OG1 THR B 59 18645 5438 12210 -1762 -4045 610 O ATOM 2478 CG2 THR B 59 6.740 27.468 -26.687 1.00 89.32 C ANISOU 2478 CG2 THR B 59 17697 4991 11248 -1167 -3741 117 C ATOM 2479 N ASP B 60 8.559 31.682 -26.244 1.00119.55 N ANISOU 2479 N ASP B 60 23154 7054 15216 -1857 -4592 -85 N ATOM 2480 CA ASP B 60 9.500 32.799 -26.293 1.00126.50 C ANISOU 2480 CA ASP B 60 24442 7464 16160 -2277 -4896 -16 C ATOM 2481 C ASP B 60 10.922 32.383 -26.665 1.00125.63 C ANISOU 2481 C ASP B 60 24070 7608 16056 -2870 -5002 290 C ATOM 2482 O ASP B 60 11.307 31.224 -26.508 1.00119.89 O ANISOU 2482 O ASP B 60 22900 7412 15242 -2973 -4859 354 O ATOM 2483 CB ASP B 60 9.501 33.559 -24.964 1.00126.90 C ANISOU 2483 CB ASP B 60 24888 7244 16085 -2240 -4997 -394 C ATOM 2484 CG ASP B 60 9.801 32.662 -23.779 1.00124.11 C ANISOU 2484 CG ASP B 60 24378 7238 15540 -2400 -4957 -569 C ATOM 2485 OD1 ASP B 60 8.848 32.098 -23.203 1.00119.51 O ANISOU 2485 OD1 ASP B 60 23624 6945 14839 -2011 -4721 -777 O ATOM 2486 OD2 ASP B 60 10.989 32.523 -23.422 1.00125.55 O ANISOU 2486 OD2 ASP B 60 24523 7503 15678 -2892 -5129 -475 O ATOM 2487 N ILE B 61 11.694 33.348 -27.155 1.00125.67 N ANISOU 2487 N ILE B 61 24196 7415 16138 -3186 -5170 483 N ATOM 2488 CA ILE B 61 13.057 33.103 -27.614 1.00125.39 C ANISOU 2488 CA ILE B 61 23881 7641 16119 -3730 -5250 795 C ATOM 2489 C ILE B 61 13.983 32.728 -26.458 1.00125.15 C ANISOU 2489 C ILE B 61 23757 7831 15964 -4043 -5329 661 C ATOM 2490 O ILE B 61 14.920 31.952 -26.633 1.00122.71 O ANISOU 2490 O ILE B 61 23071 7909 15645 -4364 -5302 864 O ATOM 2491 CB ILE B 61 13.625 34.335 -28.350 1.00130.03 C ANISOU 2491 CB ILE B 61 24644 7960 16801 -3986 -5414 995 C ATOM 2492 CG1 ILE B 61 12.598 34.881 -29.345 1.00131.11 C ANISOU 2492 CG1 ILE B 61 24936 7828 17051 -3643 -5367 1093 C ATOM 2493 CG2 ILE B 61 14.930 33.991 -29.056 1.00129.56 C ANISOU 2493 CG2 ILE B 61 24234 8223 16769 -4501 -5447 1355 C ATOM 2494 CD1 ILE B 61 13.073 36.096 -30.111 1.00135.25 C ANISOU 2494 CD1 ILE B 61 25923 7872 17596 -3303 -5445 805 C ATOM 2495 N TYR B 62 13.712 33.286 -25.282 1.00127.92 N ANISOU 2495 N TYR B 62 24444 7947 16211 -3934 -5422 321 N ATOM 2496 CA TYR B 62 14.500 33.006 -24.084 1.00128.40 C ANISOU 2496 CA TYR B 62 24466 8192 16130 -4211 -5525 173 C ATOM 2497 C TYR B 62 14.521 31.512 -23.769 1.00123.42 C ANISOU 2497 C TYR B 62 23508 7979 15407 -4154 -5379 123 C ATOM 2498 O TYR B 62 15.588 30.909 -23.607 1.00122.26 O ANISOU 2498 O TYR B 62 23066 8172 15214 -4510 -5433 237 O ATOM 2499 CB TYR B 62 13.938 33.795 -22.897 1.00148.58 C ANISOU 2499 CB TYR B 62 27482 10405 18564 -4031 -5625 -208 C ATOM 2500 CG TYR B 62 14.580 33.479 -21.563 1.00149.74 C ANISOU 2500 CG TYR B 62 27622 10747 18525 -4246 -5722 -400 C ATOM 2501 CD1 TYR B 62 15.809 34.023 -21.215 1.00151.44 C ANISOU 2501 CD1 TYR B 62 27755 11049 18734 -4743 -5930 -252 C ATOM 2502 CD2 TYR B 62 13.946 32.650 -20.645 1.00149.35 C ANISOU 2502 CD2 TYR B 62 27643 10806 18298 -3944 -5605 -722 C ATOM 2503 CE1 TYR B 62 16.395 33.741 -19.995 1.00152.63 C ANISOU 2503 CE1 TYR B 62 27890 11388 18713 -4931 -6035 -410 C ATOM 2504 CE2 TYR B 62 14.525 32.363 -19.423 1.00150.53 C ANISOU 2504 CE2 TYR B 62 27790 11149 18255 -4135 -5700 -886 C ATOM 2505 CZ TYR B 62 15.749 32.911 -19.103 1.00152.14 C ANISOU 2505 CZ TYR B 62 27909 11433 18463 -4627 -5923 -725 C ATOM 2506 OH TYR B 62 16.328 32.629 -17.887 1.00153.43 O ANISOU 2506 OH TYR B 62 28060 11799 18435 -4811 -6032 -871 O ATOM 2507 N SER B 63 13.332 30.923 -23.694 1.00137.36 N ANISOU 2507 N SER B 63 25251 9797 17142 -3663 -5160 -33 N ATOM 2508 CA SER B 63 13.191 29.499 -23.419 1.00130.39 C ANISOU 2508 CA SER B 63 23900 9496 16144 -3470 -4907 -61 C ATOM 2509 C SER B 63 13.816 28.657 -24.526 1.00126.20 C ANISOU 2509 C SER B 63 22842 9403 15704 -3674 -4795 314 C ATOM 2510 O SER B 63 14.389 27.603 -24.260 1.00122.90 O ANISOU 2510 O SER B 63 22042 9442 15210 -3801 -4714 372 O ATOM 2511 CB SER B 63 11.716 29.131 -23.247 1.00110.12 C ANISOU 2511 CB SER B 63 21345 6963 13532 -2860 -4652 -277 C ATOM 2512 OG SER B 63 10.969 29.464 -24.405 1.00109.37 O ANISOU 2512 OG SER B 63 21205 6752 13598 -2641 -4565 -95 O ATOM 2513 N LYS B 64 13.706 29.126 -25.765 1.00107.93 N ANISOU 2513 N LYS B 64 20525 6939 13545 -3697 -4793 569 N ATOM 2514 CA LYS B 64 14.284 28.419 -26.902 1.00104.48 C ANISOU 2514 CA LYS B 64 19636 6881 13181 -3895 -4685 929 C ATOM 2515 C LYS B 64 15.807 28.365 -26.816 1.00107.12 C ANISOU 2515 C LYS B 64 19799 7376 13524 -4453 -4842 1112 C ATOM 2516 O LYS B 64 16.414 27.325 -27.067 1.00102.83 O ANISOU 2516 O LYS B 64 18799 7319 12954 -4563 -4713 1256 O ATOM 2517 CB LYS B 64 13.853 29.066 -28.221 1.00106.82 C ANISOU 2517 CB LYS B 64 20046 6922 13618 -3860 -4697 1170 C ATOM 2518 CG LYS B 64 12.394 28.840 -28.582 1.00103.23 C ANISOU 2518 CG LYS B 64 19589 6453 13179 -3317 -4507 1091 C ATOM 2519 CD LYS B 64 12.091 29.363 -29.979 1.00107.04 C ANISOU 2519 CD LYS B 64 20250 6625 13796 -3322 -4580 1339 C ATOM 2520 CE LYS B 64 10.662 29.053 -30.393 1.00101.96 C ANISOU 2520 CE LYS B 64 19333 6242 13167 -2952 -4360 1448 C ATOM 2521 NZ LYS B 64 10.371 29.529 -31.771 1.00 99.54 N ANISOU 2521 NZ LYS B 64 19108 5877 12836 -2409 -4243 1153 N ATOM 2522 N VAL B 65 16.416 29.491 -26.457 1.00114.64 N ANISOU 2522 N VAL B 65 21120 7912 14524 -4802 -5127 1109 N ATOM 2523 CA VAL B 65 17.866 29.577 -26.322 1.00117.56 C ANISOU 2523 CA VAL B 65 21310 8446 14910 -5328 -5288 1286 C ATOM 2524 C VAL B 65 18.351 28.754 -25.133 1.00116.12 C ANISOU 2524 C VAL B 65 20971 8550 14601 -5421 -5327 1107 C ATOM 2525 O VAL B 65 19.364 28.057 -25.221 1.00115.10 O ANISOU 2525 O VAL B 65 20435 8814 14483 -5720 -5324 1301 O ATOM 2526 CB VAL B 65 18.339 31.041 -26.179 1.00123.06 C ANISOU 2526 CB VAL B 65 22327 8796 15636 -5529 -5503 1282 C ATOM 2527 CG1 VAL B 65 19.829 31.099 -25.874 1.00125.21 C ANISOU 2527 CG1 VAL B 65 22354 9315 15906 -6013 -5647 1444 C ATOM 2528 CG2 VAL B 65 18.024 31.825 -27.443 1.00124.58 C ANISOU 2528 CG2 VAL B 65 22627 8756 15951 -5476 -5470 1502 C ATOM 2529 N LEU B 66 17.620 28.833 -24.024 1.00117.26 N ANISOU 2529 N LEU B 66 21401 8546 14606 -5118 -5334 741 N ATOM 2530 CA LEU B 66 17.956 28.051 -22.837 1.00115.47 C ANISOU 2530 CA LEU B 66 21042 8617 14215 -5136 -5350 553 C ATOM 2531 C LEU B 66 17.922 26.554 -23.143 1.00107.78 C ANISOU 2531 C LEU B 66 19504 8241 13206 -4948 -5069 668 C ATOM 2532 O LEU B 66 18.879 25.825 -22.860 1.00106.98 O ANISOU 2532 O LEU B 66 19065 8504 13080 -5204 -5107 782 O ATOM 2533 CB LEU B 66 16.995 28.378 -21.691 1.00115.03 C ANISOU 2533 CB LEU B 66 21424 8286 13995 -4792 -5365 136 C ATOM 2534 CG LEU B 66 17.265 27.686 -20.354 1.00113.69 C ANISOU 2534 CG LEU B 66 21188 8397 13613 -4774 -5379 -86 C ATOM 2535 CD1 LEU B 66 18.644 28.051 -19.830 1.00119.23 C ANISOU 2535 CD1 LEU B 66 21890 9115 14297 -5325 -5693 -7 C ATOM 2536 CD2 LEU B 66 16.189 28.044 -19.340 1.00115.17 C ANISOU 2536 CD2 LEU B 66 21826 8308 13626 -4391 -5344 -495 C ATOM 2537 N VAL B 67 16.816 26.109 -23.731 1.00100.19 N ANISOU 2537 N VAL B 67 18446 7370 12253 -4501 -4800 641 N ATOM 2538 CA VAL B 67 16.640 24.708 -24.099 1.00 92.68 C ANISOU 2538 CA VAL B 67 17000 6941 11275 -4296 -4528 737 C ATOM 2539 C VAL B 67 17.695 24.256 -25.106 1.00 92.03 C ANISOU 2539 C VAL B 67 16496 7158 11313 -4609 -4493 1104 C ATOM 2540 O VAL B 67 18.225 23.153 -25.002 1.00 88.26 O ANISOU 2540 O VAL B 67 15603 7124 10806 -4639 -4377 1196 O ATOM 2541 CB VAL B 67 15.219 24.446 -24.649 1.00 94.26 C ANISOU 2541 CB VAL B 67 17200 7138 11476 -3781 -4272 647 C ATOM 2542 CG1 VAL B 67 15.142 23.097 -25.346 1.00 88.93 C ANISOU 2542 CG1 VAL B 67 16022 6975 10792 -3615 -4009 776 C ATOM 2543 CG2 VAL B 67 14.201 24.524 -23.523 1.00 94.98 C ANISOU 2543 CG2 VAL B 67 17631 7025 11434 -3441 -4255 280 C ATOM 2544 N THR B 68 18.006 25.118 -26.069 1.00 96.20 N ANISOU 2544 N THR B 68 17140 7438 11973 -4838 -4589 1316 N ATOM 2545 CA THR B 68 19.048 24.826 -27.048 1.00 96.80 C ANISOU 2545 CA THR B 68 16847 7779 12156 -5164 -4553 1673 C ATOM 2546 C THR B 68 20.394 24.618 -26.359 1.00100.00 C ANISOU 2546 C THR B 68 17052 8385 12561 -5593 -4726 1753 C ATOM 2547 O THR B 68 21.125 23.679 -26.677 1.00 97.66 O ANISOU 2547 O THR B 68 16292 8527 12290 -5699 -4607 1943 O ATOM 2548 CB THR B 68 19.180 25.954 -28.091 1.00101.75 C ANISOU 2548 CB THR B 68 17691 8061 12908 -5361 -4645 1892 C ATOM 2549 OG1 THR B 68 17.933 26.123 -28.777 1.00 98.89 O ANISOU 2549 OG1 THR B 68 17468 7553 12552 -4952 -4489 1850 O ATOM 2550 CG2 THR B 68 20.269 25.628 -29.102 1.00102.97 C ANISOU 2550 CG2 THR B 68 17454 8518 13152 -5716 -4589 2267 C ATOM 2551 N ALA B 69 20.708 25.493 -25.408 1.00121.43 N ANISOU 2551 N ALA B 69 20119 10772 15247 -5829 -5013 1603 N ATOM 2552 CA ALA B 69 21.958 25.409 -24.659 1.00124.26 C ANISOU 2552 CA ALA B 69 20325 11287 15602 -6256 -5231 1662 C ATOM 2553 C ALA B 69 22.045 24.111 -23.858 1.00120.37 C ANISOU 2553 C ALA B 69 19510 11235 14988 -6081 -5124 1550 C ATOM 2554 O ALA B 69 23.068 23.419 -23.890 1.00120.17 O ANISOU 2554 O ALA B 69 19066 11587 15005 -6318 -5137 1740 O ATOM 2555 CB ALA B 69 22.108 26.612 -23.741 1.00115.61 C ANISOU 2555 CB ALA B 69 19693 9779 14454 -6426 -5523 1472 C ATOM 2556 N ILE B 70 20.970 23.789 -23.143 1.00100.90 N ANISOU 2556 N ILE B 70 17237 8723 12377 -5660 -5017 1253 N ATOM 2557 CA ILE B 70 20.899 22.541 -22.387 1.00 96.16 C ANISOU 2557 CA ILE B 70 16369 8517 11648 -5455 -4896 1145 C ATOM 2558 C ILE B 70 21.103 21.344 -23.313 1.00 90.62 C ANISOU 2558 C ILE B 70 15128 8274 11027 -5346 -4627 1387 C ATOM 2559 O ILE B 70 21.856 20.419 -22.999 1.00 89.55 O ANISOU 2559 O ILE B 70 14626 8519 10882 -5443 -4616 1482 O ATOM 2560 CB ILE B 70 19.547 22.400 -21.657 1.00 92.67 C ANISOU 2560 CB ILE B 70 16218 7949 11045 -4990 -4770 809 C ATOM 2561 CG1 ILE B 70 19.364 23.536 -20.647 1.00 98.65 C ANISOU 2561 CG1 ILE B 70 17513 8283 11684 -5079 -5028 531 C ATOM 2562 CG2 ILE B 70 19.449 21.053 -20.960 1.00 87.34 C ANISOU 2562 CG2 ILE B 70 15231 7705 10248 -4764 -4603 747 C ATOM 2563 CD1 ILE B 70 18.045 23.490 -19.907 1.00 96.18 C ANISOU 2563 CD1 ILE B 70 17493 7851 11199 -4623 -4891 192 C ATOM 2564 N TYR B 71 20.435 21.385 -24.462 1.00 87.91 N ANISOU 2564 N TYR B 71 14754 7885 10763 -5142 -4422 1486 N ATOM 2565 CA TYR B 71 20.546 20.346 -25.479 1.00 83.26 C ANISOU 2565 CA TYR B 71 13708 7687 10240 -5032 -4161 1703 C ATOM 2566 C TYR B 71 21.980 20.181 -25.974 1.00 86.58 C ANISOU 2566 C TYR B 71 13763 8360 10774 -5437 -4222 2005 C ATOM 2567 O TYR B 71 22.429 19.065 -26.222 1.00 83.72 O ANISOU 2567 O TYR B 71 12975 8409 10425 -5393 -4073 2122 O ATOM 2568 CB TYR B 71 19.629 20.662 -26.664 1.00 80.71 C ANISOU 2568 CB TYR B 71 13475 7219 9971 -4801 -3984 1768 C ATOM 2569 CG TYR B 71 18.216 20.141 -26.523 1.00 75.12 C ANISOU 2569 CG TYR B 71 12872 6496 9177 -4312 -3798 1543 C ATOM 2570 CD1 TYR B 71 17.553 20.185 -25.303 1.00 73.75 C ANISOU 2570 CD1 TYR B 71 12863 6284 8874 -4119 -3830 1261 C ATOM 2571 CD2 TYR B 71 17.541 19.616 -27.617 1.00 71.66 C ANISOU 2571 CD2 TYR B 71 12357 6096 8777 -4054 -3591 1622 C ATOM 2572 CE1 TYR B 71 16.262 19.713 -25.176 1.00 69.01 C ANISOU 2572 CE1 TYR B 71 12328 5691 8202 -3684 -3646 1072 C ATOM 2573 CE2 TYR B 71 16.249 19.144 -27.500 1.00 66.97 C ANISOU 2573 CE2 TYR B 71 11825 5502 8119 -3626 -3432 1432 C ATOM 2574 CZ TYR B 71 15.615 19.194 -26.278 1.00 65.59 C ANISOU 2574 CZ TYR B 71 11792 5298 7833 -3444 -3452 1162 C ATOM 2575 OH TYR B 71 14.328 18.725 -26.157 1.00 61.26 O ANISOU 2575 OH TYR B 71 11279 4769 7228 -3030 -3280 988 O ATOM 2576 N LEU B 72 22.691 21.295 -26.120 1.00 92.78 N ANISOU 2576 N LEU B 72 14711 8894 11648 -5826 -4434 2137 N ATOM 2577 CA LEU B 72 24.073 21.258 -26.588 1.00 96.90 C ANISOU 2577 CA LEU B 72 14880 9648 12291 -6246 -4499 2441 C ATOM 2578 C LEU B 72 25.013 20.691 -25.527 1.00 98.72 C ANISOU 2578 C LEU B 72 14876 10136 12498 -6442 -4660 2422 C ATOM 2579 O LEU B 72 25.904 19.897 -25.838 1.00 98.94 O ANISOU 2579 O LEU B 72 14433 10557 12602 -6576 -4584 2640 O ATOM 2580 CB LEU B 72 24.537 22.649 -27.027 1.00103.90 C ANISOU 2580 CB LEU B 72 16025 10173 13280 -6641 -4704 2592 C ATOM 2581 CG LEU B 72 23.858 23.225 -28.273 1.00103.32 C ANISOU 2581 CG LEU B 72 16132 9876 13249 -6514 -4560 2699 C ATOM 2582 CD1 LEU B 72 24.458 24.573 -28.651 1.00109.99 C ANISOU 2582 CD1 LEU B 72 17205 10403 14183 -6887 -4757 2860 C ATOM 2583 CD2 LEU B 72 23.944 22.249 -29.438 1.00 99.20 C ANISOU 2583 CD2 LEU B 72 15175 9764 12751 -6366 -4240 2917 C ATOM 2584 N ALA B 73 24.813 21.100 -24.276 1.00100.42 N ANISOU 2584 N ALA B 73 15421 10133 12600 -6448 -4884 2162 N ATOM 2585 CA ALA B 73 25.612 20.580 -23.170 1.00102.50 C ANISOU 2585 CA ALA B 73 15510 10625 12812 -6620 -5070 2126 C ATOM 2586 C ALA B 73 25.424 19.071 -23.032 1.00 96.26 C ANISOU 2586 C ALA B 73 14341 10270 11964 -6285 -4834 2114 C ATOM 2587 O ALA B 73 26.396 18.313 -22.945 1.00 97.26 O ANISOU 2587 O ALA B 73 14043 10761 12149 -6429 -4855 2283 O ATOM 2588 CB ALA B 73 25.247 21.284 -21.873 1.00105.66 C ANISOU 2588 CB ALA B 73 16402 10684 13061 -6655 -5340 1821 C ATOM 2589 N LEU B 74 24.165 18.642 -23.023 1.00 98.39 N ANISOU 2589 N LEU B 74 14760 10494 12132 -5838 -4613 1922 N ATOM 2590 CA LEU B 74 23.838 17.223 -22.964 1.00 96.09 C ANISOU 2590 CA LEU B 74 14153 10570 11788 -5505 -4376 1904 C ATOM 2591 C LEU B 74 24.374 16.493 -24.193 1.00 94.93 C ANISOU 2591 C LEU B 74 13541 10745 11785 -5501 -4146 2184 C ATOM 2592 O LEU B 74 24.712 15.310 -24.125 1.00 93.43 O ANISOU 2592 O LEU B 74 12989 10911 11599 -5355 -4006 2249 O ATOM 2593 CB LEU B 74 22.325 17.024 -22.845 1.00 78.97 C ANISOU 2593 CB LEU B 74 12250 8259 9496 -5055 -4188 1655 C ATOM 2594 CG LEU B 74 21.675 17.517 -21.550 1.00 80.37 C ANISOU 2594 CG LEU B 74 12868 8173 9497 -4970 -4348 1346 C ATOM 2595 CD1 LEU B 74 20.161 17.432 -21.646 1.00 75.44 C ANISOU 2595 CD1 LEU B 74 12461 7417 8786 -4524 -4125 1137 C ATOM 2596 CD2 LEU B 74 22.186 16.723 -20.357 1.00 81.36 C ANISOU 2596 CD2 LEU B 74 12865 8543 9503 -5029 -4474 1289 C ATOM 2597 N PHE B 75 24.456 17.209 -25.310 1.00 84.36 N ANISOU 2597 N PHE B 75 12229 9269 10553 -5657 -4105 2350 N ATOM 2598 CA PHE B 75 24.987 16.645 -26.545 1.00 83.50 C ANISOU 2598 CA PHE B 75 11716 9451 10560 -5678 -3880 2617 C ATOM 2599 C PHE B 75 26.467 16.326 -26.411 1.00 88.00 C ANISOU 2599 C PHE B 75 11873 10324 11236 -6013 -3983 2845 C ATOM 2600 O PHE B 75 26.880 15.193 -26.639 1.00 85.95 O ANISOU 2600 O PHE B 75 11198 10442 11018 -5892 -3806 2958 O ATOM 2601 CB PHE B 75 24.770 17.596 -27.724 1.00 85.18 C ANISOU 2601 CB PHE B 75 12102 9429 10835 -5774 -3820 2745 C ATOM 2602 CG PHE B 75 25.322 17.085 -29.025 1.00 84.82 C ANISOU 2602 CG PHE B 75 11673 9681 10871 -5795 -3573 3015 C ATOM 2603 CD1 PHE B 75 24.595 16.196 -29.801 1.00 79.19 C ANISOU 2603 CD1 PHE B 75 10850 9130 10111 -5421 -3279 2987 C ATOM 2604 CD2 PHE B 75 26.568 17.493 -29.474 1.00 90.52 C ANISOU 2604 CD2 PHE B 75 12150 10530 11713 -6194 -3631 3294 C ATOM 2605 CE1 PHE B 75 25.101 15.724 -30.998 1.00 79.32 C ANISOU 2605 CE1 PHE B 75 10545 9417 10176 -5432 -3045 3215 C ATOM 2606 CE2 PHE B 75 27.079 17.024 -30.668 1.00 90.59 C ANISOU 2606 CE2 PHE B 75 11813 10831 11778 -6200 -3377 3536 C ATOM 2607 CZ PHE B 75 26.344 16.138 -31.431 1.00 84.99 C ANISOU 2607 CZ PHE B 75 11024 10269 10998 -5811 -3082 3486 C ATOM 2608 N VAL B 76 27.266 17.326 -26.051 1.00 94.52 N ANISOU 2608 N VAL B 76 12810 10983 12118 -6434 -4275 2915 N ATOM 2609 CA VAL B 76 28.704 17.114 -25.925 1.00 99.57 C ANISOU 2609 CA VAL B 76 13034 11920 12879 -6783 -4399 3147 C ATOM 2610 C VAL B 76 29.042 16.120 -24.810 1.00 98.28 C ANISOU 2610 C VAL B 76 12652 12029 12660 -6662 -4475 3058 C ATOM 2611 O VAL B 76 29.834 15.198 -25.019 1.00 98.17 O ANISOU 2611 O VAL B 76 12157 12410 12733 -6634 -4357 3233 O ATOM 2612 CB VAL B 76 29.489 18.440 -25.754 1.00106.37 C ANISOU 2612 CB VAL B 76 14068 12547 13799 -7227 -4690 3233 C ATOM 2613 CG1 VAL B 76 29.534 19.202 -27.071 1.00107.69 C ANISOU 2613 CG1 VAL B 76 14273 12596 14047 -7337 -4550 3427 C ATOM 2614 CG2 VAL B 76 28.881 19.298 -24.657 1.00107.63 C ANISOU 2614 CG2 VAL B 76 14776 12290 13830 -7249 -4965 2943 C ATOM 2615 N VAL B 77 28.422 16.291 -23.644 1.00101.55 N ANISOU 2615 N VAL B 77 13428 12234 12923 -6568 -4658 2788 N ATOM 2616 CA VAL B 77 28.672 15.396 -22.516 1.00100.93 C ANISOU 2616 CA VAL B 77 13197 12389 12762 -6467 -4757 2704 C ATOM 2617 C VAL B 77 28.281 13.956 -22.847 1.00 96.04 C ANISOU 2617 C VAL B 77 12294 12072 12126 -6036 -4434 2705 C ATOM 2618 O VAL B 77 29.054 13.021 -22.616 1.00 96.06 O ANISOU 2618 O VAL B 77 11903 12418 12178 -6008 -4424 2824 O ATOM 2619 CB VAL B 77 27.928 15.855 -21.244 1.00 97.25 C ANISOU 2619 CB VAL B 77 13229 11628 12095 -6419 -4981 2393 C ATOM 2620 CG1 VAL B 77 28.047 14.806 -20.148 1.00 96.23 C ANISOU 2620 CG1 VAL B 77 12956 11756 11850 -6275 -5051 2315 C ATOM 2621 CG2 VAL B 77 28.471 17.193 -20.767 1.00104.61 C ANISOU 2621 CG2 VAL B 77 14446 12262 13041 -6871 -5341 2381 C ATOM 2622 N GLY B 78 27.087 13.788 -23.406 1.00 87.64 N ANISOU 2622 N GLY B 78 11428 10870 11001 -5704 -4180 2581 N ATOM 2623 CA GLY B 78 26.587 12.473 -23.761 1.00 81.60 C ANISOU 2623 CA GLY B 78 10450 10341 10214 -5302 -3881 2560 C ATOM 2624 C GLY B 78 27.401 11.787 -24.842 1.00 81.63 C ANISOU 2624 C GLY B 78 9969 10675 10372 -5303 -3667 2821 C ATOM 2625 O GLY B 78 27.779 10.623 -24.699 1.00 80.13 O ANISOU 2625 O GLY B 78 9452 10787 10209 -5136 -3565 2878 O ATOM 2626 N THR B 79 27.668 12.507 -25.927 1.00 91.50 N ANISOU 2626 N THR B 79 11185 11863 11718 -5483 -3593 2980 N ATOM 2627 CA THR B 79 28.421 11.951 -27.047 1.00 91.43 C ANISOU 2627 CA THR B 79 10740 12163 11836 -5488 -3360 3225 C ATOM 2628 C THR B 79 29.850 11.596 -26.653 1.00 92.91 C ANISOU 2628 C THR B 79 10487 12665 12148 -5723 -3484 3425 C ATOM 2629 O THR B 79 30.312 10.488 -26.924 1.00 92.39 O ANISOU 2629 O THR B 79 10027 12928 12146 -5547 -3300 3529 O ATOM 2630 CB THR B 79 28.444 12.900 -28.261 1.00 83.61 C ANISOU 2630 CB THR B 79 9832 11037 10900 -5671 -3269 3372 C ATOM 2631 OG1 THR B 79 28.806 14.219 -27.833 1.00 89.07 O ANISOU 2631 OG1 THR B 79 10752 11468 11621 -6069 -3565 3404 O ATOM 2632 CG2 THR B 79 27.078 12.942 -28.930 1.00 78.39 C ANISOU 2632 CG2 THR B 79 9490 10160 10135 -5365 -3080 3221 C ATOM 2633 N VAL B 80 30.545 12.533 -26.013 1.00 94.76 N ANISOU 2633 N VAL B 80 10788 12794 12425 -6119 -3802 3480 N ATOM 2634 CA VAL B 80 31.910 12.277 -25.562 1.00100.05 C ANISOU 2634 CA VAL B 80 11030 13764 13222 -6370 -3965 3677 C ATOM 2635 C VAL B 80 31.950 11.108 -24.581 1.00 97.79 C ANISOU 2635 C VAL B 80 10595 13680 12882 -6113 -4007 3582 C ATOM 2636 O VAL B 80 32.742 10.178 -24.745 1.00 98.74 O ANISOU 2636 O VAL B 80 10250 14153 13112 -6029 -3904 3745 O ATOM 2637 CB VAL B 80 32.550 13.525 -24.917 1.00103.40 C ANISOU 2637 CB VAL B 80 11628 13997 13662 -6791 -4315 3705 C ATOM 2638 CG1 VAL B 80 33.827 13.154 -24.177 1.00106.36 C ANISOU 2638 CG1 VAL B 80 11645 14664 14104 -6869 -4458 3826 C ATOM 2639 CG2 VAL B 80 32.829 14.585 -25.973 1.00105.59 C ANISOU 2639 CG2 VAL B 80 11974 14137 14007 -7003 -4231 3853 C ATOM 2640 N GLY B 81 31.079 11.152 -23.576 1.00 99.94 N ANISOU 2640 N GLY B 81 11266 13725 12980 -5976 -4145 3323 N ATOM 2641 CA GLY B 81 31.012 10.102 -22.575 1.00 98.31 C ANISOU 2641 CA GLY B 81 10982 13679 12693 -5749 -4203 3231 C ATOM 2642 C GLY B 81 30.773 8.721 -23.160 1.00 93.97 C ANISOU 2642 C GLY B 81 10157 13372 12176 -5341 -3871 3263 C ATOM 2643 O GLY B 81 31.528 7.785 -22.890 1.00 94.97 O ANISOU 2643 O GLY B 81 9932 13784 12367 -5252 -3885 3370 O ATOM 2644 N ASN B 82 29.727 8.597 -23.970 1.00 91.61 N ANISOU 2644 N ASN B 82 10017 12953 11837 -5095 -3583 3176 N ATOM 2645 CA ASN B 82 29.372 7.314 -24.569 1.00 89.98 C ANISOU 2645 CA ASN B 82 9611 12932 11645 -4708 -3270 3176 C ATOM 2646 C ASN B 82 30.397 6.808 -25.584 1.00 90.78 C ANISOU 2646 C ASN B 82 9228 13342 11924 -4718 -3072 3422 C ATOM 2647 O ASN B 82 30.626 5.603 -25.692 1.00 90.37 O ANISOU 2647 O ASN B 82 8885 13528 11924 -4470 -2926 3474 O ATOM 2648 CB ASN B 82 27.978 7.376 -25.201 1.00 73.48 C ANISOU 2648 CB ASN B 82 7858 10615 9445 -4449 -3052 2994 C ATOM 2649 CG ASN B 82 26.879 7.556 -24.171 1.00 70.64 C ANISOU 2649 CG ASN B 82 7908 10021 8910 -4319 -3171 2739 C ATOM 2650 OD1 ASN B 82 26.475 6.602 -23.505 1.00 67.96 O ANISOU 2650 OD1 ASN B 82 7553 9768 8501 -4072 -3124 2652 O ATOM 2651 ND2 ASN B 82 26.386 8.782 -24.039 1.00 71.61 N ANISOU 2651 ND2 ASN B 82 8407 9841 8959 -4481 -3316 2623 N ATOM 2652 N SER B 83 31.011 7.726 -26.325 1.00 81.75 N ANISOU 2652 N SER B 83 8005 12190 10868 -4996 -3055 3576 N ATOM 2653 CA SER B 83 32.033 7.350 -27.298 1.00 84.74 C ANISOU 2653 CA SER B 83 7914 12879 11404 -5032 -2854 3821 C ATOM 2654 C SER B 83 33.293 6.839 -26.607 1.00 89.66 C ANISOU 2654 C SER B 83 8104 13800 12164 -5150 -3021 3988 C ATOM 2655 O SER B 83 33.835 5.794 -26.978 1.00 89.99 O ANISOU 2655 O SER B 83 7751 14136 12306 -4942 -2833 4100 O ATOM 2656 CB SER B 83 32.375 8.525 -28.216 1.00 88.29 C ANISOU 2656 CB SER B 83 8390 13251 11905 -5350 -2821 3969 C ATOM 2657 OG SER B 83 31.247 8.924 -28.974 1.00 92.21 O ANISOU 2657 OG SER B 83 9108 13530 12397 -5732 -3161 3965 O ATOM 2658 N VAL B 84 33.756 7.580 -25.604 1.00111.25 N ANISOU 2658 N VAL B 84 10922 16447 14899 -5477 -3384 4000 N ATOM 2659 CA VAL B 84 34.922 7.168 -24.828 1.00113.07 C ANISOU 2659 CA VAL B 84 10765 16945 15249 -5620 -3609 4157 C ATOM 2660 C VAL B 84 34.634 5.855 -24.101 1.00112.06 C ANISOU 2660 C VAL B 84 10574 16932 15070 -5255 -3598 4062 C ATOM 2661 O VAL B 84 35.520 5.014 -23.944 1.00113.25 O ANISOU 2661 O VAL B 84 10279 17391 15357 -5169 -3589 4225 O ATOM 2662 CB VAL B 84 35.361 8.264 -23.829 1.00119.19 C ANISOU 2662 CB VAL B 84 11789 17527 15969 -5961 -3978 4120 C ATOM 2663 CG1 VAL B 84 36.484 7.763 -22.934 1.00120.27 C ANISOU 2663 CG1 VAL B 84 11683 17867 16147 -5952 -4184 4192 C ATOM 2664 CG2 VAL B 84 35.805 9.512 -24.576 1.00120.35 C ANISOU 2664 CG2 VAL B 84 11940 17598 16187 -6255 -3947 4252 C ATOM 2665 N THR B 85 33.386 5.677 -23.677 1.00 93.81 N ANISOU 2665 N THR B 85 8702 14374 12569 -5035 -3592 3809 N ATOM 2666 CA THR B 85 32.960 4.426 -23.056 1.00 90.71 C ANISOU 2666 CA THR B 85 8296 14060 12110 -4683 -3553 3719 C ATOM 2667 C THR B 85 33.066 3.263 -24.040 1.00 89.12 C ANISOU 2667 C THR B 85 7761 14079 12023 -4345 -3198 3808 C ATOM 2668 O THR B 85 33.622 2.210 -23.717 1.00 90.08 O ANISOU 2668 O THR B 85 7580 14420 12226 -4164 -3199 3900 O ATOM 2669 CB THR B 85 31.513 4.517 -22.534 1.00 81.57 C ANISOU 2669 CB THR B 85 7665 12601 10728 -4502 -3546 3437 C ATOM 2670 OG1 THR B 85 31.430 5.526 -21.520 1.00 84.04 O ANISOU 2670 OG1 THR B 85 8314 12698 10920 -4792 -3866 3330 O ATOM 2671 CG2 THR B 85 31.070 3.183 -21.954 1.00 78.82 C ANISOU 2671 CG2 THR B 85 7296 12341 10312 -4169 -3509 3370 C ATOM 2672 N LEU B 86 32.534 3.463 -25.243 1.00 84.49 N ANISOU 2672 N LEU B 86 7245 13421 11436 -4257 -2903 3780 N ATOM 2673 CA LEU B 86 32.575 2.441 -26.285 1.00 84.18 C ANISOU 2673 CA LEU B 86 6936 13568 11481 -3948 -2551 3842 C ATOM 2674 C LEU B 86 34.004 2.085 -26.681 1.00 88.05 C ANISOU 2674 C LEU B 86 6868 14406 12181 -4025 -2512 4104 C ATOM 2675 O LEU B 86 34.306 0.925 -26.960 1.00 87.95 O ANISOU 2675 O LEU B 86 6565 14595 12258 -3730 -2331 4162 O ATOM 2676 CB LEU B 86 31.785 2.891 -27.517 1.00 76.87 C ANISOU 2676 CB LEU B 86 6216 12502 10491 -3898 -2279 3773 C ATOM 2677 CG LEU B 86 30.267 2.727 -27.446 1.00 70.28 C ANISOU 2677 CG LEU B 86 5817 11400 9483 -3651 -2182 3524 C ATOM 2678 CD1 LEU B 86 29.611 3.267 -28.703 1.00 68.10 C ANISOU 2678 CD1 LEU B 86 5698 11020 9159 -3626 -1940 3494 C ATOM 2679 CD2 LEU B 86 29.901 1.269 -27.238 1.00 67.10 C ANISOU 2679 CD2 LEU B 86 5338 11083 9074 -3273 -2054 3451 C ATOM 2680 N PHE B 87 34.880 3.085 -26.708 1.00111.77 N ANISOU 2680 N PHE B 87 9720 17476 15272 -4419 -2680 4265 N ATOM 2681 CA PHE B 87 36.283 2.846 -27.025 1.00114.15 C ANISOU 2681 CA PHE B 87 9456 18128 15786 -4534 -2664 4534 C ATOM 2682 C PHE B 87 36.976 2.132 -25.869 1.00115.32 C ANISOU 2682 C PHE B 87 9389 18425 16000 -4433 -2889 4583 C ATOM 2683 O PHE B 87 37.922 1.371 -26.072 1.00117.05 O ANISOU 2683 O PHE B 87 9209 18900 16364 -4252 -2763 4721 O ATOM 2684 CB PHE B 87 36.999 4.159 -27.345 1.00197.89 C ATOM 2685 CG PHE B 87 38.415 3.979 -27.814 1.00197.89 C ATOM 2686 CD1 PHE B 87 38.689 3.730 -29.148 1.00197.89 C ATOM 2687 CD2 PHE B 87 39.471 4.059 -26.921 1.00197.89 C ATOM 2688 CE1 PHE B 87 39.991 3.563 -29.583 1.00197.89 C ATOM 2689 CE2 PHE B 87 40.773 3.893 -27.349 1.00197.89 C ATOM 2690 CZ PHE B 87 41.034 3.645 -28.682 1.00197.89 C ATOM 2691 N THR B 88 36.494 2.384 -24.656 1.00109.13 N ANISOU 2691 N THR B 88 8909 17463 15092 -4526 -3212 4457 N ATOM 2692 CA THR B 88 37.037 1.755 -23.458 1.00110.51 C ANISOU 2692 CA THR B 88 8976 17734 15280 -4437 -3450 4486 C ATOM 2693 C THR B 88 36.703 0.268 -23.430 1.00108.72 C ANISOU 2693 C THR B 88 8620 17616 15075 -4018 -3307 4463 C ATOM 2694 O THR B 88 37.553 -0.566 -23.113 1.00110.47 O ANISOU 2694 O THR B 88 8549 18023 15402 -3833 -3333 4573 O ATOM 2695 CB THR B 88 36.491 2.421 -22.178 1.00125.64 C ANISOU 2695 CB THR B 88 11312 19413 17012 -4669 -3830 4341 C ATOM 2696 OG1 THR B 88 36.952 3.776 -22.108 1.00126.68 O ANISOU 2696 OG1 THR B 88 11601 19405 17128 -5050 -3964 4351 O ATOM 2697 CG2 THR B 88 36.950 1.669 -20.938 1.00127.10 C ANISOU 2697 CG2 THR B 88 11390 19710 17195 -4601 -4080 4391 C ATOM 2698 N LEU B 89 35.461 -0.058 -23.775 1.00132.15 N ANISOU 2698 N LEU B 89 11961 20357 17892 -3770 -3076 4250 N ATOM 2699 CA LEU B 89 34.996 -1.441 -23.752 1.00131.13 C ANISOU 2699 CA LEU B 89 11853 20229 17741 -3336 -2890 4171 C ATOM 2700 C LEU B 89 35.674 -2.304 -24.815 1.00132.12 C ANISOU 2700 C LEU B 89 11552 20592 18055 -3076 -2571 4305 C ATOM 2701 O LEU B 89 35.681 -3.531 -24.717 1.00132.26 O ANISOU 2701 O LEU B 89 11431 20689 18132 -2744 -2486 4321 O ATOM 2702 CB LEU B 89 33.476 -1.494 -23.917 1.00115.89 C ANISOU 2702 CB LEU B 89 10429 17997 15610 -3179 -2737 3913 C ATOM 2703 CG LEU B 89 32.682 -0.786 -22.817 1.00114.82 C ANISOU 2703 CG LEU B 89 10741 17620 15268 -3342 -3008 3747 C ATOM 2704 CD1 LEU B 89 31.196 -0.809 -23.124 1.00112.45 C ANISOU 2704 CD1 LEU B 89 10866 17065 14798 -3128 -2820 3511 C ATOM 2705 CD2 LEU B 89 32.964 -1.418 -21.463 1.00115.56 C ANISOU 2705 CD2 LEU B 89 10772 17801 15334 -3335 -3304 3803 C ATOM 2706 N ALA B 90 36.242 -1.658 -25.828 1.00119.96 N ANISOU 2706 N ALA B 90 9819 19159 16602 -3224 -2390 4402 N ATOM 2707 CA ALA B 90 36.928 -2.370 -26.901 1.00121.18 C ANISOU 2707 CA ALA B 90 9556 19565 16922 -2999 -2068 4532 C ATOM 2708 C ALA B 90 38.431 -2.438 -26.648 1.00123.92 C ANISOU 2708 C ALA B 90 9371 20226 17487 -3026 -2196 4773 C ATOM 2709 O ALA B 90 39.226 -2.490 -27.587 1.00125.68 O ANISOU 2709 O ALA B 90 9309 20623 17822 -3059 -2012 4894 O ATOM 2710 CB ALA B 90 36.642 -1.712 -28.242 1.00 93.45 C ANISOU 2710 CB ALA B 90 6045 16065 13396 -3155 -1816 4557 C ATOM 2711 N ARG B 91 38.813 -2.438 -25.375 1.00149.57 N ANISOU 2711 N ARG B 91 12629 23463 20738 -2949 -2470 4779 N ATOM 2712 CA ARG B 91 40.219 -2.498 -24.994 1.00152.25 C ANISOU 2712 CA ARG B 91 12631 23991 21227 -2901 -2583 4935 C ATOM 2713 C ARG B 91 40.392 -3.136 -23.620 1.00152.26 C ANISOU 2713 C ARG B 91 12669 23966 21218 -2667 -2786 4924 C ATOM 2714 O ARG B 91 40.182 -4.337 -23.452 1.00153.58 O ANISOU 2714 O ARG B 91 12532 24288 21536 -2395 -2724 5028 O ATOM 2715 CB ARG B 91 40.837 -1.098 -25.005 1.00 20.00 C ATOM 2716 N LEU B 98 33.953 -12.643 -16.559 1.00159.28 N ANISOU 2716 N LEU B 98 15241 23916 21363 -868 -3642 4700 N ATOM 2717 CA LEU B 98 32.704 -12.475 -15.825 1.00156.57 C ANISOU 2717 CA LEU B 98 15375 23306 20807 -843 -3449 4464 C ATOM 2718 C LEU B 98 32.146 -11.069 -16.017 1.00154.72 C ANISOU 2718 C LEU B 98 15381 23010 20395 -1180 -3463 4285 C ATOM 2719 O LEU B 98 30.931 -10.869 -16.031 1.00152.72 O ANISOU 2719 O LEU B 98 15419 22574 20035 -1167 -3229 4081 O ATOM 2720 CB LEU B 98 32.902 -12.766 -14.333 1.00161.59 C ANISOU 2720 CB LEU B 98 16315 23821 21259 -764 -3613 4484 C ATOM 2721 CG LEU B 98 33.035 -14.229 -13.894 1.00158.89 C ANISOU 2721 CG LEU B 98 16275 23238 20856 -524 -3338 4348 C ATOM 2722 CD1 LEU B 98 34.391 -14.820 -14.261 1.00159.63 C ANISOU 2722 CD1 LEU B 98 16112 23322 21219 -191 -3067 4392 C ATOM 2723 CD2 LEU B 98 32.779 -14.363 -12.400 1.00158.23 C ANISOU 2723 CD2 LEU B 98 16445 23072 20604 -468 -3522 4422 C ATOM 2724 N GLN B 99 33.042 -10.100 -16.167 1.00197.74 N ANISOU 2724 N GLN B 99 20708 28605 25817 -1483 -3755 4368 N ATOM 2725 CA GLN B 99 32.650 -8.714 -16.388 1.00196.55 C ANISOU 2725 CA GLN B 99 20744 28399 25537 -1821 -3801 4224 C ATOM 2726 C GLN B 99 32.544 -8.429 -17.884 1.00196.04 C ANISOU 2726 C GLN B 99 20558 28320 25609 -1809 -3480 4149 C ATOM 2727 O GLN B 99 31.861 -7.493 -18.302 1.00194.73 O ANISOU 2727 O GLN B 99 20644 28020 25322 -1993 -3406 3983 O ATOM 2728 CB GLN B 99 33.665 -7.768 -15.739 1.00170.67 C ANISOU 2728 CB GLN B 99 17280 25302 22264 -2144 -4185 4364 C ATOM 2729 CG GLN B 99 33.294 -6.294 -15.810 1.00169.79 C ANISOU 2729 CG GLN B 99 17447 25088 21979 -2516 -4308 4210 C ATOM 2730 CD GLN B 99 34.379 -5.393 -15.253 1.00171.74 C ANISOU 2730 CD GLN B 99 17379 25514 22362 -2827 -4525 4349 C ATOM 2731 OE1 GLN B 99 35.365 -5.865 -14.689 1.00173.79 O ANISOU 2731 OE1 GLN B 99 17246 25943 22845 -2727 -4489 4518 O ATOM 2732 NE2 GLN B 99 34.202 -4.086 -15.413 1.00171.32 N ANISOU 2732 NE2 GLN B 99 17577 25351 22167 -3169 -4670 4225 N ATOM 2733 N SER B 100 33.214 -9.256 -18.682 1.00384.55 N ANISOU 2733 N SER B 100 44055 52331 49728 -1576 -3287 4273 N ATOM 2734 CA SER B 100 33.280 -9.068 -20.130 1.00384.40 C ANISOU 2734 CA SER B 100 43889 52334 49833 -1536 -2965 4225 C ATOM 2735 C SER B 100 31.907 -9.071 -20.799 1.00381.41 C ANISOU 2735 C SER B 100 43879 51712 49329 -1392 -2664 3995 C ATOM 2736 O SER B 100 31.692 -8.377 -21.792 1.00380.51 O ANISOU 2736 O SER B 100 43803 51561 49215 -1475 -2464 3904 O ATOM 2737 CB SER B 100 34.170 -10.141 -20.763 1.00125.03 C ANISOU 2737 CB SER B 100 10558 19691 17255 -1272 -2815 4404 C ATOM 2738 OG SER B 100 35.477 -10.108 -20.217 1.00129.36 O ANISOU 2738 OG SER B 100 10719 20487 17942 -1395 -3099 4635 O ATOM 2739 N THR B 101 30.983 -9.853 -20.251 1.00102.86 N ANISOU 2739 N THR B 101 8863 16274 13946 -1188 -2642 3916 N ATOM 2740 CA THR B 101 29.636 -9.945 -20.801 1.00100.98 C ANISOU 2740 CA THR B 101 8961 15811 13597 -1055 -2382 3709 C ATOM 2741 C THR B 101 28.818 -8.707 -20.454 1.00 98.97 C ANISOU 2741 C THR B 101 9075 15402 13127 -1306 -2431 3531 C ATOM 2742 O THR B 101 27.962 -8.280 -21.228 1.00 97.77 O ANISOU 2742 O THR B 101 9082 15133 12934 -1298 -2213 3385 O ATOM 2743 CB THR B 101 28.898 -11.173 -20.260 1.00 99.81 C ANISOU 2743 CB THR B 101 8984 15536 13406 -791 -2357 3694 C ATOM 2744 OG1 THR B 101 28.663 -10.999 -18.859 1.00 98.73 O ANISOU 2744 OG1 THR B 101 9109 15335 13069 -934 -2610 3678 O ATOM 2745 CG2 THR B 101 29.722 -12.433 -20.490 1.00102.21 C ANISOU 2745 CG2 THR B 101 8943 15971 13924 -537 -2366 3886 C ATOM 2746 N VAL B 102 29.081 -8.143 -19.279 1.00102.20 N ANISOU 2746 N VAL B 102 9629 15810 13393 -1516 -2724 3541 N ATOM 2747 CA VAL B 102 28.407 -6.928 -18.837 1.00100.59 C ANISOU 2747 CA VAL B 102 9779 15458 12984 -1750 -2800 3371 C ATOM 2748 C VAL B 102 28.811 -5.761 -19.736 1.00100.70 C ANISOU 2748 C VAL B 102 9724 15484 13054 -1972 -2752 3344 C ATOM 2749 O VAL B 102 28.011 -4.861 -20.013 1.00 99.12 O ANISOU 2749 O VAL B 102 9813 15116 12731 -2074 -2685 3178 O ATOM 2750 CB VAL B 102 28.752 -6.605 -17.369 1.00100.55 C ANISOU 2750 CB VAL B 102 9933 15467 12806 -1931 -3141 3393 C ATOM 2751 CG1 VAL B 102 27.966 -5.397 -16.885 1.00 99.50 C ANISOU 2751 CG1 VAL B 102 9918 15306 12583 -2276 -3330 3329 C ATOM 2752 CG2 VAL B 102 28.473 -7.811 -16.485 1.00 99.72 C ANISOU 2752 CG2 VAL B 102 10190 15209 12492 -1803 -3109 3269 C ATOM 2753 N ASP B 103 30.057 -5.798 -20.200 1.00 96.94 N ANISOU 2753 N ASP B 103 8853 15209 12774 -2032 -2771 3519 N ATOM 2754 CA ASP B 103 30.582 -4.790 -21.114 1.00 97.39 C ANISOU 2754 CA ASP B 103 8793 15305 12906 -2246 -2707 3538 C ATOM 2755 C ASP B 103 29.778 -4.740 -22.411 1.00 96.21 C ANISOU 2755 C ASP B 103 8770 15037 12751 -2112 -2370 3411 C ATOM 2756 O ASP B 103 29.686 -3.694 -23.053 1.00 95.99 O ANISOU 2756 O ASP B 103 8822 14950 12702 -2302 -2321 3368 O ATOM 2757 CB ASP B 103 32.057 -5.062 -21.420 1.00128.43 C ANISOU 2757 CB ASP B 103 12223 19511 17063 -2299 -2753 3774 C ATOM 2758 CG ASP B 103 32.958 -4.814 -20.224 1.00129.84 C ANISOU 2758 CG ASP B 103 12266 19818 17248 -2510 -3136 3912 C ATOM 2759 OD1 ASP B 103 32.454 -4.830 -19.082 1.00129.13 O ANISOU 2759 OD1 ASP B 103 12506 19591 16965 -2685 -3368 3808 O ATOM 2760 OD2 ASP B 103 34.173 -4.604 -20.427 1.00131.81 O ANISOU 2760 OD2 ASP B 103 12078 20312 17691 -2498 -3205 4122 O ATOM 2761 N TYR B 104 29.201 -5.875 -22.792 1.00 79.74 N ANISOU 2761 N TYR B 104 6706 12910 10684 -1795 -2152 3359 N ATOM 2762 CA TYR B 104 28.353 -5.943 -23.977 1.00 78.67 C ANISOU 2762 CA TYR B 104 6730 12647 10514 -1662 -1858 3221 C ATOM 2763 C TYR B 104 27.062 -5.155 -23.770 1.00 76.79 C ANISOU 2763 C TYR B 104 6920 12176 10081 -1757 -1889 3027 C ATOM 2764 O TYR B 104 26.654 -4.376 -24.634 1.00 76.11 O ANISOU 2764 O TYR B 104 6964 11998 9956 -1830 -1765 2944 O ATOM 2765 CB TYR B 104 28.040 -7.399 -24.334 1.00109.96 C ANISOU 2765 CB TYR B 104 10635 16604 14541 -1312 -1649 3204 C ATOM 2766 CG TYR B 104 29.208 -8.149 -24.938 1.00111.88 C ANISOU 2766 CG TYR B 104 10461 17062 14987 -1168 -1538 3367 C ATOM 2767 CD1 TYR B 104 30.153 -7.492 -25.714 1.00112.34 C ANISOU 2767 CD1 TYR B 104 10392 17179 15115 -1072 -1256 3356 C ATOM 2768 CD2 TYR B 104 29.365 -9.514 -24.732 1.00113.33 C ANISOU 2768 CD2 TYR B 104 10374 17399 15286 -1121 -1715 3536 C ATOM 2769 CE1 TYR B 104 31.222 -8.172 -26.269 1.00114.24 C ANISOU 2769 CE1 TYR B 104 10244 17627 15535 -919 -1127 3497 C ATOM 2770 CE2 TYR B 104 30.431 -10.203 -25.282 1.00115.25 C ANISOU 2770 CE2 TYR B 104 10212 17848 15732 -963 -1605 3688 C ATOM 2771 CZ TYR B 104 31.356 -9.527 -26.050 1.00115.73 C ANISOU 2771 CZ TYR B 104 10149 17965 15859 -856 -1298 3662 C ATOM 2772 OH TYR B 104 32.418 -10.207 -26.601 1.00117.80 O ANISOU 2772 OH TYR B 104 10000 18442 16316 -677 -1161 3805 O ATOM 2773 N TYR B 105 26.425 -5.362 -22.620 1.00 76.04 N ANISOU 2773 N TYR B 105 7040 11991 9860 -1745 -2051 2963 N ATOM 2774 CA TYR B 105 25.215 -4.625 -22.270 1.00 74.14 C ANISOU 2774 CA TYR B 105 7190 11547 9433 -1819 -2084 2780 C ATOM 2775 C TYR B 105 25.502 -3.130 -22.185 1.00 74.10 C ANISOU 2775 C TYR B 105 7285 11492 9377 -2123 -2247 2757 C ATOM 2776 O TYR B 105 24.739 -2.309 -22.702 1.00 72.98 O ANISOU 2776 O TYR B 105 7363 11197 9170 -2179 -2165 2635 O ATOM 2777 CB TYR B 105 24.641 -5.125 -20.943 1.00 66.44 C ANISOU 2777 CB TYR B 105 6400 10523 8322 -1754 -2221 2737 C ATOM 2778 CG TYR B 105 24.182 -6.566 -20.967 1.00 66.23 C ANISOU 2778 CG TYR B 105 6359 10484 8323 -1471 -2064 2740 C ATOM 2779 CD1 TYR B 105 22.945 -6.912 -21.497 1.00 64.69 C ANISOU 2779 CD1 TYR B 105 6377 10139 8064 -1331 -1866 2593 C ATOM 2780 CD2 TYR B 105 24.980 -7.579 -20.448 1.00 67.69 C ANISOU 2780 CD2 TYR B 105 6317 10796 8606 -1349 -2131 2897 C ATOM 2781 CE1 TYR B 105 22.521 -8.228 -21.518 1.00 64.74 C ANISOU 2781 CE1 TYR B 105 6383 10114 8101 -1101 -1738 2599 C ATOM 2782 CE2 TYR B 105 24.564 -8.898 -20.464 1.00 67.74 C ANISOU 2782 CE2 TYR B 105 6336 10757 8646 -1097 -1999 2904 C ATOM 2783 CZ TYR B 105 23.333 -9.216 -21.001 1.00 66.34 C ANISOU 2783 CZ TYR B 105 6385 10420 8400 -986 -1803 2752 C ATOM 2784 OH TYR B 105 22.909 -10.524 -21.022 1.00 66.60 O ANISOU 2784 OH TYR B 105 6444 10391 8472 -762 -1686 2762 O ATOM 2785 N LEU B 106 26.611 -2.789 -21.535 1.00 76.47 N ANISOU 2785 N LEU B 106 7426 11914 9713 -2320 -2491 2883 N ATOM 2786 CA LEU B 106 27.036 -1.397 -21.415 1.00 77.00 C ANISOU 2786 CA LEU B 106 7579 11930 9748 -2642 -2683 2879 C ATOM 2787 C LEU B 106 27.258 -0.762 -22.785 1.00 77.30 C ANISOU 2787 C LEU B 106 7506 11967 9896 -2736 -2522 2922 C ATOM 2788 O LEU B 106 26.876 0.387 -23.019 1.00 76.92 O ANISOU 2788 O LEU B 106 7680 11760 9786 -2919 -2567 2842 O ATOM 2789 CB LEU B 106 28.310 -1.294 -20.573 1.00 64.06 C ANISOU 2789 CB LEU B 106 5722 10459 8159 -2844 -2980 3037 C ATOM 2790 CG LEU B 106 28.141 -1.038 -19.073 1.00 65.87 C ANISOU 2790 CG LEU B 106 6184 10638 8205 -2933 -3263 2973 C ATOM 2791 CD1 LEU B 106 27.270 -2.101 -18.419 1.00 62.44 C ANISOU 2791 CD1 LEU B 106 5962 10129 7634 -2658 -3155 2861 C ATOM 2792 CD2 LEU B 106 29.496 -0.958 -18.388 1.00 71.64 C ANISOU 2792 CD2 LEU B 106 6610 11588 9021 -3076 -3537 3172 C ATOM 2793 N GLY B 107 27.876 -1.521 -23.685 1.00 66.87 N ANISOU 2793 N GLY B 107 5855 10821 8732 -2599 -2329 3050 N ATOM 2794 CA GLY B 107 28.125 -1.058 -25.037 1.00 67.25 C ANISOU 2794 CA GLY B 107 5779 10905 8868 -2661 -2138 3108 C ATOM 2795 C GLY B 107 26.833 -0.847 -25.799 1.00 65.63 C ANISOU 2795 C GLY B 107 5873 10502 8562 -2538 -1934 2942 C ATOM 2796 O GLY B 107 26.707 0.099 -26.578 1.00 65.48 O ANISOU 2796 O GLY B 107 5938 10406 8534 -2683 -1878 2941 O ATOM 2797 N SER B 108 25.871 -1.735 -25.572 1.00 56.98 N ANISOU 2797 N SER B 108 4931 9324 7393 -2278 -1833 2815 N ATOM 2798 CA SER B 108 24.556 -1.612 -26.187 1.00 53.80 C ANISOU 2798 CA SER B 108 4806 8739 6894 -2155 -1667 2654 C ATOM 2799 C SER B 108 23.869 -0.334 -25.718 1.00 52.95 C ANISOU 2799 C SER B 108 5029 8422 6665 -2333 -1820 2535 C ATOM 2800 O SER B 108 23.290 0.402 -26.521 1.00 52.21 O ANISOU 2800 O SER B 108 5102 8197 6536 -2365 -1734 2473 O ATOM 2801 CB SER B 108 23.692 -2.828 -25.855 1.00 47.85 C ANISOU 2801 CB SER B 108 4138 7946 6096 -1873 -1562 2555 C ATOM 2802 OG SER B 108 22.431 -2.744 -26.496 1.00 46.01 O ANISOU 2802 OG SER B 108 4171 7540 5770 -1777 -1438 2399 O ATOM 2803 N LEU B 109 23.942 -0.079 -24.415 1.00 47.58 N ANISOU 2803 N LEU B 109 4454 7710 5917 -2441 -2052 2506 N ATOM 2804 CA LEU B 109 23.384 1.140 -23.836 1.00 47.52 C ANISOU 2804 CA LEU B 109 4775 7494 5786 -2601 -2210 2378 C ATOM 2805 C LEU B 109 24.025 2.384 -24.446 1.00 50.24 C ANISOU 2805 C LEU B 109 5105 7792 6191 -2883 -2299 2459 C ATOM 2806 O LEU B 109 23.328 3.316 -24.860 1.00 49.03 O ANISOU 2806 O LEU B 109 5209 7436 5984 -2946 -2294 2365 O ATOM 2807 CB LEU B 109 23.577 1.147 -22.317 1.00 50.16 C ANISOU 2807 CB LEU B 109 5216 7827 6014 -2670 -2447 2337 C ATOM 2808 CG LEU B 109 22.803 0.100 -21.513 1.00 47.94 C ANISOU 2808 CG LEU B 109 5038 7547 5629 -2428 -2384 2244 C ATOM 2809 CD1 LEU B 109 23.225 0.127 -20.053 1.00 51.13 C ANISOU 2809 CD1 LEU B 109 5508 7997 5921 -2525 -2633 2248 C ATOM 2810 CD2 LEU B 109 21.306 0.329 -21.645 1.00 44.23 C ANISOU 2810 CD2 LEU B 109 4876 6880 5047 -2291 -2249 2052 C ATOM 2811 N ALA B 110 25.354 2.386 -24.504 1.00 53.53 N ANISOU 2811 N ALA B 110 5209 8399 6731 -3049 -2379 2646 N ATOM 2812 CA ALA B 110 26.101 3.508 -25.062 1.00 57.17 C ANISOU 2812 CA ALA B 110 5608 8846 7266 -3353 -2468 2761 C ATOM 2813 C ALA B 110 25.739 3.755 -26.524 1.00 55.39 C ANISOU 2813 C ALA B 110 5388 8581 7079 -3307 -2227 2789 C ATOM 2814 O ALA B 110 25.625 4.903 -26.958 1.00 56.68 O ANISOU 2814 O ALA B 110 5712 8590 7234 -3508 -2280 2800 O ATOM 2815 CB ALA B 110 27.596 3.275 -24.915 1.00 61.99 C ANISOU 2815 CB ALA B 110 5818 9716 8019 -3517 -2575 2977 C ATOM 2816 N LEU B 111 25.559 2.674 -27.277 1.00 53.72 N ANISOU 2816 N LEU B 111 5015 8497 6900 -3044 -1973 2803 N ATOM 2817 CA LEU B 111 25.159 2.777 -28.676 1.00 52.31 C ANISOU 2817 CA LEU B 111 4858 8293 6722 -2970 -1737 2816 C ATOM 2818 C LEU B 111 23.765 3.386 -28.790 1.00 49.16 C ANISOU 2818 C LEU B 111 4856 7620 6202 -2902 -1734 2637 C ATOM 2819 O LEU B 111 23.525 4.271 -29.618 1.00 49.47 O ANISOU 2819 O LEU B 111 5031 7541 6226 -3010 -1700 2660 O ATOM 2820 CB LEU B 111 25.190 1.403 -29.348 1.00 75.07 C ANISOU 2820 CB LEU B 111 7523 11353 9644 -2683 -1484 2834 C ATOM 2821 CG LEU B 111 24.853 1.373 -30.840 1.00 73.89 C ANISOU 2821 CG LEU B 111 7405 11202 9468 -2579 -1229 2833 C ATOM 2822 CD1 LEU B 111 25.829 2.231 -31.626 1.00 75.06 C ANISOU 2822 CD1 LEU B 111 7402 11444 9671 -2824 -1191 3013 C ATOM 2823 CD2 LEU B 111 24.847 -0.056 -31.362 1.00 73.20 C ANISOU 2823 CD2 LEU B 111 7145 11260 9405 -2283 -1004 2813 C ATOM 2824 N SER B 112 22.852 2.910 -27.947 1.00 56.58 N ANISOU 2824 N SER B 112 5974 8466 7059 -2721 -1769 2473 N ATOM 2825 CA SER B 112 21.483 3.414 -27.936 1.00 55.05 C ANISOU 2825 CA SER B 112 6126 8033 6760 -2623 -1761 2298 C ATOM 2826 C SER B 112 21.446 4.900 -27.591 1.00 55.64 C ANISOU 2826 C SER B 112 6450 7892 6799 -2857 -1959 2265 C ATOM 2827 O SER B 112 20.583 5.635 -28.072 1.00 54.96 O ANISOU 2827 O SER B 112 6613 7604 6666 -2823 -1936 2180 O ATOM 2828 CB SER B 112 20.617 2.621 -26.955 1.00 49.64 C ANISOU 2828 CB SER B 112 5550 7319 5993 -2412 -1766 2148 C ATOM 2829 OG SER B 112 21.054 2.804 -25.620 1.00 50.02 O ANISOU 2829 OG SER B 112 5635 7371 6002 -2531 -1978 2132 O ATOM 2830 N ASP B 113 22.387 5.336 -26.758 1.00 60.85 N ANISOU 2830 N ASP B 113 7049 8586 7486 -3094 -2168 2334 N ATOM 2831 CA ASP B 113 22.508 6.751 -26.423 1.00 61.90 C ANISOU 2831 CA ASP B 113 7430 8496 7591 -3347 -2381 2303 C ATOM 2832 C ASP B 113 23.045 7.552 -27.608 1.00 63.54 C ANISOU 2832 C ASP B 113 7571 8682 7889 -3566 -2355 2469 C ATOM 2833 O ASP B 113 22.494 8.597 -27.968 1.00 64.01 O ANISOU 2833 O ASP B 113 7905 8493 7922 -3653 -2409 2426 O ATOM 2834 CB ASP B 113 23.419 6.941 -25.208 1.00124.13 C ANISOU 2834 CB ASP B 113 15286 16420 15460 -3548 -2641 2314 C ATOM 2835 CG ASP B 113 22.862 6.295 -23.954 1.00122.94 C ANISOU 2835 CG ASP B 113 15280 16253 15179 -3362 -2690 2143 C ATOM 2836 OD1 ASP B 113 21.626 6.146 -23.857 1.00121.09 O ANISOU 2836 OD1 ASP B 113 15084 16028 14898 -3074 -2500 2049 O ATOM 2837 OD2 ASP B 113 23.662 5.940 -23.062 1.00123.90 O ANISOU 2837 OD2 ASP B 113 15482 16358 15238 -3516 -2923 2109 O ATOM 2838 N LEU B 114 24.121 7.052 -28.210 1.00 68.44 N ANISOU 2838 N LEU B 114 7827 9562 8615 -3646 -2265 2666 N ATOM 2839 CA LEU B 114 24.765 7.736 -29.327 1.00 69.47 C ANISOU 2839 CA LEU B 114 7848 9724 8823 -3864 -2210 2854 C ATOM 2840 C LEU B 114 23.840 7.906 -30.528 1.00 68.48 C ANISOU 2840 C LEU B 114 7888 9485 8648 -3718 -2013 2827 C ATOM 2841 O LEU B 114 23.882 8.934 -31.203 1.00 69.26 O ANISOU 2841 O LEU B 114 8109 9450 8756 -3908 -2040 2918 O ATOM 2842 CB LEU B 114 26.047 7.012 -29.749 1.00 70.04 C ANISOU 2842 CB LEU B 114 7462 10139 9012 -3920 -2101 3061 C ATOM 2843 CG LEU B 114 27.286 7.266 -28.891 1.00 71.82 C ANISOU 2843 CG LEU B 114 7468 10490 9331 -4201 -2331 3187 C ATOM 2844 CD1 LEU B 114 28.515 6.633 -29.521 1.00 73.86 C ANISOU 2844 CD1 LEU B 114 7241 11104 9721 -4213 -2181 3402 C ATOM 2845 CD2 LEU B 114 27.498 8.758 -28.685 1.00 74.76 C ANISOU 2845 CD2 LEU B 114 8034 10653 9719 -4578 -2554 3245 C ATOM 2846 N LEU B 115 23.010 6.901 -30.795 1.00 66.99 N ANISOU 2846 N LEU B 115 7706 9346 8402 -3392 -1832 2711 N ATOM 2847 CA LEU B 115 22.057 6.984 -31.899 1.00 65.80 C ANISOU 2847 CA LEU B 115 7711 9100 8192 -3238 -1666 2675 C ATOM 2848 C LEU B 115 21.089 8.150 -31.708 1.00 66.22 C ANISOU 2848 C LEU B 115 8154 8820 8188 -3274 -1806 2564 C ATOM 2849 O LEU B 115 20.873 8.950 -32.624 1.00 66.49 O ANISOU 2849 O LEU B 115 8321 8730 8214 -3363 -1786 2642 O ATOM 2850 CB LEU B 115 21.284 5.672 -32.054 1.00 65.88 C ANISOU 2850 CB LEU B 115 7666 9210 8156 -2899 -1482 2556 C ATOM 2851 CG LEU B 115 22.082 4.482 -32.589 1.00 65.24 C ANISOU 2851 CG LEU B 115 7241 9424 8123 -2803 -1285 2659 C ATOM 2852 CD1 LEU B 115 21.206 3.240 -32.687 1.00 62.90 C ANISOU 2852 CD1 LEU B 115 6956 9165 7779 -2482 -1134 2521 C ATOM 2853 CD2 LEU B 115 22.700 4.817 -33.938 1.00 65.60 C ANISOU 2853 CD2 LEU B 115 7175 9571 8177 -2923 -1140 2831 C ATOM 2854 N ILE B 116 20.518 8.241 -30.510 1.00 63.16 N ANISOU 2854 N ILE B 116 7953 8287 7757 -3196 -1944 2386 N ATOM 2855 CA ILE B 116 19.608 9.325 -30.159 1.00 63.49 C ANISOU 2855 CA ILE B 116 8367 8006 7748 -3189 -2071 2253 C ATOM 2856 C ILE B 116 20.297 10.683 -30.248 1.00 65.36 C ANISOU 2856 C ILE B 116 8739 8062 8030 -3522 -2263 2357 C ATOM 2857 O ILE B 116 19.773 11.617 -30.859 1.00 66.09 O ANISOU 2857 O ILE B 116 9078 7914 8117 -3558 -2300 2362 O ATOM 2858 CB ILE B 116 19.047 9.146 -28.733 1.00 54.32 C ANISOU 2858 CB ILE B 116 7367 6757 6515 -3040 -2162 2037 C ATOM 2859 CG1 ILE B 116 18.183 7.886 -28.655 1.00 51.69 C ANISOU 2859 CG1 ILE B 116 6940 6562 6141 -2719 -1974 1939 C ATOM 2860 CG2 ILE B 116 18.244 10.369 -28.319 1.00 55.17 C ANISOU 2860 CG2 ILE B 116 7861 6526 6577 -3036 -2296 1895 C ATOM 2861 CD1 ILE B 116 16.961 7.929 -29.545 1.00 50.69 C ANISOU 2861 CD1 ILE B 116 6979 6356 5927 -2557 -2026 1737 C ATOM 2862 N LEU B 117 21.478 10.782 -29.646 1.00 80.73 N ANISOU 2862 N LEU B 117 10521 10122 10031 -3774 -2395 2452 N ATOM 2863 CA LEU B 117 22.207 12.047 -29.594 1.00 82.66 C ANISOU 2863 CA LEU B 117 10882 10196 10328 -4133 -2604 2556 C ATOM 2864 C LEU B 117 22.644 12.551 -30.969 1.00 83.37 C ANISOU 2864 C LEU B 117 10897 10300 10478 -4304 -2510 2780 C ATOM 2865 O LEU B 117 22.612 13.753 -31.234 1.00 84.64 O ANISOU 2865 O LEU B 117 11319 10187 10651 -4479 -2629 2820 O ATOM 2866 CB LEU B 117 23.421 11.923 -28.672 1.00 66.43 C ANISOU 2866 CB LEU B 117 8619 8301 8323 -4377 -2776 2625 C ATOM 2867 CG LEU B 117 23.097 11.709 -27.193 1.00 65.47 C ANISOU 2867 CG LEU B 117 8663 8099 8114 -4303 -2947 2413 C ATOM 2868 CD1 LEU B 117 24.349 11.349 -26.414 1.00 68.56 C ANISOU 2868 CD1 LEU B 117 8769 8730 8553 -4498 -3089 2512 C ATOM 2869 CD2 LEU B 117 22.440 12.950 -26.612 1.00 67.38 C ANISOU 2869 CD2 LEU B 117 9354 7951 8297 -4411 -3157 2262 C ATOM 2870 N LEU B 118 23.047 11.634 -31.841 1.00 87.95 N ANISOU 2870 N LEU B 118 11137 11193 11089 -4248 -2293 2928 N ATOM 2871 CA LEU B 118 23.565 12.012 -33.152 1.00 88.52 C ANISOU 2871 CA LEU B 118 11109 11333 11193 -4412 -2172 3156 C ATOM 2872 C LEU B 118 22.472 12.191 -34.204 1.00 87.56 C ANISOU 2872 C LEU B 118 11218 11062 10991 -4218 -2041 3124 C ATOM 2873 O LEU B 118 22.596 13.032 -35.095 1.00 88.52 O ANISOU 2873 O LEU B 118 11464 11057 11114 -4396 -2053 3274 O ATOM 2874 CB LEU B 118 24.603 10.995 -33.638 1.00 66.24 C ANISOU 2874 CB LEU B 118 7835 8914 8421 -4414 -1971 3319 C ATOM 2875 CG LEU B 118 25.933 10.943 -32.882 1.00 70.15 C ANISOU 2875 CG LEU B 118 8029 9600 9026 -4666 -2098 3438 C ATOM 2876 CD1 LEU B 118 26.843 9.876 -33.470 1.00 71.13 C ANISOU 2876 CD1 LEU B 118 7698 10123 9205 -4602 -1861 3594 C ATOM 2877 CD2 LEU B 118 26.616 12.300 -32.895 1.00 76.01 C ANISOU 2877 CD2 LEU B 118 8865 10179 9835 -5092 -2306 3594 C ATOM 2878 N LEU B 119 21.402 11.408 -34.102 1.00 77.92 N ANISOU 2878 N LEU B 119 10050 9857 9700 -3866 -1929 2943 N ATOM 2879 CA LEU B 119 20.350 11.443 -35.117 1.00 76.80 C ANISOU 2879 CA LEU B 119 10077 9623 9482 -3667 -1805 2920 C ATOM 2880 C LEU B 119 19.102 12.217 -34.689 1.00 77.20 C ANISOU 2880 C LEU B 119 10506 9326 9500 -3528 -1944 2744 C ATOM 2881 O LEU B 119 18.610 13.069 -35.431 1.00 77.73 O ANISOU 2881 O LEU B 119 10799 9186 9550 -3556 -1980 2805 O ATOM 2882 CB LEU B 119 19.969 10.023 -35.547 1.00 62.57 C ANISOU 2882 CB LEU B 119 8071 8076 7627 -3376 -1572 2858 C ATOM 2883 CG LEU B 119 21.110 9.183 -36.126 1.00 62.31 C ANISOU 2883 CG LEU B 119 7669 8389 7619 -3443 -1390 3016 C ATOM 2884 CD1 LEU B 119 20.600 7.839 -36.619 1.00 60.04 C ANISOU 2884 CD1 LEU B 119 7250 8292 7273 -3133 -1176 2922 C ATOM 2885 CD2 LEU B 119 21.819 9.939 -37.239 1.00 64.11 C ANISOU 2885 CD2 LEU B 119 7865 8659 7837 -3683 -1325 3255 C ATOM 2886 N ALA B 120 18.595 11.923 -33.496 1.00 66.99 N ANISOU 2886 N ALA B 120 9281 7975 8198 -3370 -2017 2533 N ATOM 2887 CA ALA B 120 17.331 12.501 -33.044 1.00 67.40 C ANISOU 2887 CA ALA B 120 9653 7742 8215 -3173 -2102 2343 C ATOM 2888 C ALA B 120 17.449 13.964 -32.618 1.00 69.46 C ANISOU 2888 C ALA B 120 10228 7657 8508 -3369 -2329 2331 C ATOM 2889 O ALA B 120 16.529 14.753 -32.833 1.00 70.28 O ANISOU 2889 O ALA B 120 10614 7488 8602 -3247 -2384 2262 O ATOM 2890 CB ALA B 120 16.736 11.667 -31.918 1.00 45.16 C ANISOU 2890 CB ALA B 120 6801 4998 5360 -2936 -2075 2128 C ATOM 2891 N MET B 121 18.580 14.321 -32.017 1.00 76.94 N ANISOU 2891 N MET B 121 11128 8606 9499 -3668 -2474 2398 N ATOM 2892 CA MET B 121 18.768 15.671 -31.481 1.00 78.99 C ANISOU 2892 CA MET B 121 11707 8519 9789 -3881 -2715 2368 C ATOM 2893 C MET B 121 18.712 16.820 -32.501 1.00 80.41 C ANISOU 2893 C MET B 121 12085 8458 10011 -4045 -2770 2540 C ATOM 2894 O MET B 121 17.952 17.767 -32.305 1.00 81.68 O ANISOU 2894 O MET B 121 12599 8266 10171 -3964 -2884 2440 O ATOM 2895 CB MET B 121 20.036 15.759 -30.621 1.00 78.67 C ANISOU 2895 CB MET B 121 11568 8542 9783 -4189 -2886 2397 C ATOM 2896 CG MET B 121 20.465 17.183 -30.310 1.00 80.99 C ANISOU 2896 CG MET B 121 12208 8460 10105 -4451 -3154 2369 C ATOM 2897 SD MET B 121 21.400 17.323 -28.777 1.00 82.13 S ANISOU 2897 SD MET B 121 12256 8672 10277 -4827 -3399 2385 S ATOM 2898 CE MET B 121 20.111 17.032 -27.570 1.00 80.87 C ANISOU 2898 CE MET B 121 12164 8574 9991 -4518 -3404 2074 C ATOM 2899 N PRO B 122 19.510 16.751 -33.586 1.00 77.93 N ANISOU 2899 N PRO B 122 11550 8328 9730 -4267 -2684 2804 N ATOM 2900 CA PRO B 122 19.471 17.890 -34.512 1.00 80.33 C ANISOU 2900 CA PRO B 122 12063 8395 10062 -4449 -2746 2989 C ATOM 2901 C PRO B 122 18.126 18.028 -35.222 1.00 78.87 C ANISOU 2901 C PRO B 122 12089 8052 9826 -4143 -2671 2939 C ATOM 2902 O PRO B 122 17.708 19.145 -35.526 1.00 81.48 O ANISOU 2902 O PRO B 122 12727 8050 10179 -4207 -2795 3001 O ATOM 2903 CB PRO B 122 20.574 17.557 -35.522 1.00 74.05 C ANISOU 2903 CB PRO B 122 10931 7922 9284 -4690 -2602 3273 C ATOM 2904 CG PRO B 122 20.693 16.075 -35.477 1.00 69.64 C ANISOU 2904 CG PRO B 122 10015 7756 8689 -4481 -2400 3204 C ATOM 2905 CD PRO B 122 20.441 15.704 -34.047 1.00 66.77 C ANISOU 2905 CD PRO B 122 9707 7335 8328 -4348 -2516 2951 C ATOM 2906 N VAL B 123 17.462 16.904 -35.477 1.00 64.43 N ANISOU 2906 N VAL B 123 10095 6450 7933 -3820 -2484 2836 N ATOM 2907 CA VAL B 123 16.152 16.914 -36.119 1.00 62.39 C ANISOU 2907 CA VAL B 123 10001 6075 7629 -3514 -2426 2775 C ATOM 2908 C VAL B 123 15.103 17.561 -35.217 1.00 61.53 C ANISOU 2908 C VAL B 123 10208 5626 7544 -3311 -2573 2542 C ATOM 2909 O VAL B 123 14.335 18.419 -35.656 1.00 63.44 O ANISOU 2909 O VAL B 123 10726 5577 7804 -3221 -2658 2556 O ATOM 2910 CB VAL B 123 15.700 15.488 -36.498 1.00 57.65 C ANISOU 2910 CB VAL B 123 9135 5810 6960 -3242 -2202 2712 C ATOM 2911 CG1 VAL B 123 14.249 15.489 -36.954 1.00 55.44 C ANISOU 2911 CG1 VAL B 123 9019 5400 6645 -2910 -2182 2601 C ATOM 2912 CG2 VAL B 123 16.607 14.915 -37.576 1.00 59.09 C ANISOU 2912 CG2 VAL B 123 9065 6289 7098 -3390 -2035 2940 C ATOM 2913 N GLU B 124 15.080 17.148 -33.954 1.00 62.34 N ANISOU 2913 N GLU B 124 10273 5771 7642 -3233 -2599 2333 N ATOM 2914 CA GLU B 124 14.138 17.698 -32.986 1.00 61.59 C ANISOU 2914 CA GLU B 124 10462 5391 7547 -3022 -2706 2088 C ATOM 2915 C GLU B 124 14.429 19.164 -32.685 1.00 66.83 C ANISOU 2915 C GLU B 124 11478 5649 8265 -3233 -2938 2094 C ATOM 2916 O GLU B 124 13.516 19.987 -32.632 1.00 68.13 O ANISOU 2916 O GLU B 124 11951 5485 8451 -3055 -3020 1992 O ATOM 2917 CB GLU B 124 14.163 16.889 -31.686 1.00 62.45 C ANISOU 2917 CB GLU B 124 10448 5669 7609 -2918 -2671 1880 C ATOM 2918 CG GLU B 124 13.358 17.514 -30.557 1.00 63.79 C ANISOU 2918 CG GLU B 124 10911 5571 7754 -2706 -2757 1617 C ATOM 2919 CD GLU B 124 13.501 16.765 -29.248 1.00 62.78 C ANISOU 2919 CD GLU B 124 10705 5593 7556 -2685 -2756 1439 C ATOM 2920 OE1 GLU B 124 13.939 15.597 -29.269 1.00 60.58 O ANISOU 2920 OE1 GLU B 124 10107 5655 7253 -2716 -2644 1499 O ATOM 2921 OE2 GLU B 124 13.176 17.349 -28.195 1.00 64.26 O ANISOU 2921 OE2 GLU B 124 11164 5548 7703 -2630 -2868 1240 O ATOM 2922 N LEU B 125 15.705 19.484 -32.488 1.00 67.07 N ANISOU 2922 N LEU B 125 11460 5698 8326 -3613 -3048 2217 N ATOM 2923 CA LEU B 125 16.111 20.846 -32.151 1.00 72.85 C ANISOU 2923 CA LEU B 125 12525 6039 9113 -3873 -3290 2232 C ATOM 2924 C LEU B 125 15.725 21.833 -33.250 1.00 76.42 C ANISOU 2924 C LEU B 125 13213 6204 9616 -3896 -3342 2400 C ATOM 2925 O LEU B 125 15.502 23.014 -32.987 1.00 80.39 O ANISOU 2925 O LEU B 125 14097 6280 10165 -3924 -3525 2338 O ATOM 2926 CB LEU B 125 17.618 20.907 -31.881 1.00 76.34 C ANISOU 2926 CB LEU B 125 12802 6612 9591 -4315 -3393 2382 C ATOM 2927 CG LEU B 125 18.159 22.168 -31.204 1.00 82.69 C ANISOU 2927 CG LEU B 125 13937 7032 10449 -4638 -3676 2372 C ATOM 2928 CD1 LEU B 125 17.418 22.436 -29.906 1.00 82.28 C ANISOU 2928 CD1 LEU B 125 14220 6697 10345 -4426 -3798 2038 C ATOM 2929 CD2 LEU B 125 19.655 22.047 -30.953 1.00 85.87 C ANISOU 2929 CD2 LEU B 125 14091 7644 10890 -5066 -3769 2524 C ATOM 2930 N TYR B 126 15.633 21.336 -34.479 1.00 76.19 N ANISOU 2930 N TYR B 126 12972 6403 9571 -3875 -3182 2610 N ATOM 2931 CA TYR B 126 15.256 22.169 -35.614 1.00 79.49 C ANISOU 2931 CA TYR B 126 13591 6598 10014 -3890 -3218 2802 C ATOM 2932 C TYR B 126 13.745 22.238 -35.818 1.00 77.23 C ANISOU 2932 C TYR B 126 13484 6143 9716 -3455 -3191 2657 C ATOM 2933 O TYR B 126 13.182 23.323 -35.967 1.00 80.58 O ANISOU 2933 O TYR B 126 14265 6154 10196 -3382 -3346 2622 O ATOM 2934 CB TYR B 126 15.930 21.668 -36.894 1.00 78.97 C ANISOU 2934 CB TYR B 126 13236 6864 9905 -4054 -3054 3091 C ATOM 2935 CG TYR B 126 15.433 22.348 -38.152 1.00 82.23 C ANISOU 2935 CG TYR B 126 13837 7099 10306 -4058 -3073 3310 C ATOM 2936 CD1 TYR B 126 15.842 23.633 -38.479 1.00 88.62 C ANISOU 2936 CD1 TYR B 126 14882 7614 11173 -4391 -3237 3524 C ATOM 2937 CD2 TYR B 126 14.553 21.703 -39.012 1.00 79.32 C ANISOU 2937 CD2 TYR B 126 13416 6856 9865 -3743 -2942 3315 C ATOM 2938 CE1 TYR B 126 15.388 24.257 -39.626 1.00 91.92 C ANISOU 2938 CE1 TYR B 126 15487 7866 11570 -4399 -3262 3746 C ATOM 2939 CE2 TYR B 126 14.095 22.319 -40.161 1.00 82.59 C ANISOU 2939 CE2 TYR B 126 14011 7118 10253 -3747 -2978 3526 C ATOM 2940 CZ TYR B 126 14.516 23.596 -40.463 1.00 88.84 C ANISOU 2940 CZ TYR B 126 15042 7616 11095 -4069 -3134 3746 C ATOM 2941 OH TYR B 126 14.063 24.214 -41.606 1.00 92.39 O ANISOU 2941 OH TYR B 126 15686 7910 11508 -4075 -3177 3977 O ATOM 2942 N ASN B 127 13.093 21.080 -35.824 1.00 71.01 N ANISOU 2942 N ASN B 127 12443 5672 8866 -3166 -3000 2575 N ATOM 2943 CA ASN B 127 11.683 21.004 -36.197 1.00 69.13 C ANISOU 2943 CA ASN B 127 12299 5346 8622 -2775 -2960 2488 C ATOM 2944 C ASN B 127 10.691 20.893 -35.039 1.00 66.42 C ANISOU 2944 C ASN B 127 12060 4881 8295 -2439 -2970 2175 C ATOM 2945 O ASN B 127 9.481 20.899 -35.257 1.00 65.53 O ANISOU 2945 O ASN B 127 12027 4672 8200 -2108 -2953 2098 O ATOM 2946 CB ASN B 127 11.453 19.863 -37.193 1.00 65.74 C ANISOU 2946 CB ASN B 127 11565 5300 8114 -2649 -2761 2587 C ATOM 2947 CG ASN B 127 11.200 20.364 -38.602 1.00 68.74 C ANISOU 2947 CG ASN B 127 12058 5588 8472 -2643 -2788 2816 C ATOM 2948 OD1 ASN B 127 10.591 21.415 -38.799 1.00 71.79 O ANISOU 2948 OD1 ASN B 127 12741 5619 8915 -2537 -2935 2829 O ATOM 2949 ND2 ASN B 127 11.668 19.613 -39.591 1.00 68.20 N ANISOU 2949 ND2 ASN B 127 11765 5836 8313 -2747 -2645 2997 N ATOM 2950 N PHE B 128 11.195 20.794 -33.814 1.00 65.41 N ANISOU 2950 N PHE B 128 11925 4772 8155 -2523 -2999 2001 N ATOM 2951 CA PHE B 128 10.317 20.644 -32.658 1.00 63.02 C ANISOU 2951 CA PHE B 128 11720 4385 7839 -2218 -2984 1702 C ATOM 2952 C PHE B 128 10.558 21.708 -31.588 1.00 67.00 C ANISOU 2952 C PHE B 128 12577 4515 8367 -2320 -3173 1548 C ATOM 2953 O PHE B 128 9.748 21.872 -30.675 1.00 66.68 O ANISOU 2953 O PHE B 128 12719 4300 8315 -2045 -3180 1302 O ATOM 2954 CB PHE B 128 10.452 19.241 -32.059 1.00 57.50 C ANISOU 2954 CB PHE B 128 10694 4088 7065 -2139 -2817 1586 C ATOM 2955 CG PHE B 128 9.905 18.153 -32.937 1.00 53.64 C ANISOU 2955 CG PHE B 128 9912 3917 6553 -1949 -2631 1660 C ATOM 2956 CD1 PHE B 128 8.701 18.319 -33.601 1.00 53.66 C ANISOU 2956 CD1 PHE B 128 9979 3826 6586 -1671 -2607 1668 C ATOM 2957 CD2 PHE B 128 10.597 16.966 -33.104 1.00 50.55 C ANISOU 2957 CD2 PHE B 128 9187 3910 6112 -2047 -2494 1723 C ATOM 2958 CE1 PHE B 128 8.196 17.320 -34.410 1.00 50.71 C ANISOU 2958 CE1 PHE B 128 9348 3737 6181 -1519 -2461 1730 C ATOM 2959 CE2 PHE B 128 10.097 15.963 -33.912 1.00 47.66 C ANISOU 2959 CE2 PHE B 128 8582 3808 5716 -1881 -2334 1775 C ATOM 2960 CZ PHE B 128 8.894 16.140 -34.566 1.00 47.76 C ANISOU 2960 CZ PHE B 128 8670 3726 5748 -1629 -2323 1776 C ATOM 2961 N ILE B 129 11.669 22.428 -31.704 1.00 71.23 N ANISOU 2961 N ILE B 129 13207 4928 8929 -2720 -3322 1689 N ATOM 2962 CA ILE B 129 11.992 23.493 -30.758 1.00 75.98 C ANISOU 2962 CA ILE B 129 14171 5148 9549 -2870 -3533 1552 C ATOM 2963 C ILE B 129 11.947 24.866 -31.429 1.00 82.23 C ANISOU 2963 C ILE B 129 15317 5490 10438 -2990 -3713 1693 C ATOM 2964 O ILE B 129 11.327 25.797 -30.914 1.00 85.44 O ANISOU 2964 O ILE B 129 16096 5489 10878 -2818 -3830 1521 O ATOM 2965 CB ILE B 129 13.369 23.270 -30.077 1.00 77.06 C ANISOU 2965 CB ILE B 129 14190 5440 9650 -3263 -3619 1574 C ATOM 2966 CG1 ILE B 129 13.224 22.389 -28.833 1.00 72.85 C ANISOU 2966 CG1 ILE B 129 13525 5142 9010 -3098 -3533 1323 C ATOM 2967 CG2 ILE B 129 13.992 24.593 -29.664 1.00 84.04 C ANISOU 2967 CG2 ILE B 129 15454 5896 10581 -3570 -3888 1563 C ATOM 2968 CD1 ILE B 129 12.901 20.942 -29.118 1.00 66.31 C ANISOU 2968 CD1 ILE B 129 12284 4773 8138 -2891 -3287 1354 C ATOM 2969 N TRP B 130 12.595 24.984 -32.585 1.00101.59 N ANISOU 2969 N TRP B 130 17659 8012 12929 -3273 -3727 2008 N ATOM 2970 CA TRP B 130 12.658 26.259 -33.295 1.00103.62 C ANISOU 2970 CA TRP B 130 18248 7850 13274 -3443 -3906 2188 C ATOM 2971 C TRP B 130 11.596 26.379 -34.385 1.00103.89 C ANISOU 2971 C TRP B 130 18356 7778 13339 -3128 -3852 2287 C ATOM 2972 O TRP B 130 10.550 26.992 -34.176 1.00105.47 O ANISOU 2972 O TRP B 130 18864 7617 13592 -2838 -3935 2140 O ATOM 2973 CB TRP B 130 14.055 26.483 -33.881 1.00 94.17 C ANISOU 2973 CB TRP B 130 16922 6759 12099 -3953 -3963 2499 C ATOM 2974 CG TRP B 130 15.098 26.776 -32.843 1.00 96.92 C ANISOU 2974 CG TRP B 130 17305 7063 12456 -4315 -4113 2431 C ATOM 2975 CD1 TRP B 130 15.964 25.888 -32.276 1.00 94.68 C ANISOU 2975 CD1 TRP B 130 16663 7182 12130 -4535 -4044 2460 C ATOM 2976 CD2 TRP B 130 15.381 28.048 -32.245 1.00102.95 C ANISOU 2976 CD2 TRP B 130 18495 7346 13275 -4499 -4375 2319 C ATOM 2977 NE1 TRP B 130 16.769 26.526 -31.364 1.00 98.94 N ANISOU 2977 NE1 TRP B 130 17360 7540 12693 -4856 -4258 2385 N ATOM 2978 CE2 TRP B 130 16.431 27.854 -31.326 1.00104.10 C ANISOU 2978 CE2 TRP B 130 18506 7646 13399 -4850 -4466 2290 C ATOM 2979 CE3 TRP B 130 14.848 29.332 -32.399 1.00107.94 C ANISOU 2979 CE3 TRP B 130 19618 7420 13974 -4396 -4552 2240 C ATOM 2980 CZ2 TRP B 130 16.959 28.894 -30.564 1.00110.08 C ANISOU 2980 CZ2 TRP B 130 19613 8026 14189 -5123 -4736 2177 C ATOM 2981 CZ3 TRP B 130 15.373 30.363 -31.642 1.00113.86 C ANISOU 2981 CZ3 TRP B 130 20730 7774 14759 -4652 -4806 2118 C ATOM 2982 CH2 TRP B 130 16.418 30.138 -30.736 1.00114.62 C ANISOU 2982 CH2 TRP B 130 20677 8057 14816 -5011 -4892 2081 C ATOM 2983 N VAL B 131 11.872 25.799 -35.549 1.00 88.59 N ANISOU 2983 N VAL B 131 16139 6158 11364 -3177 -3717 2532 N ATOM 2984 CA VAL B 131 10.938 25.858 -36.669 1.00 88.69 C ANISOU 2984 CA VAL B 131 16201 6112 11387 -2903 -3681 2649 C ATOM 2985 C VAL B 131 9.903 24.741 -36.569 1.00 82.25 C ANISOU 2985 C VAL B 131 15085 5656 10508 -2519 -3478 2507 C ATOM 2986 O VAL B 131 10.139 23.621 -37.016 1.00 78.59 O ANISOU 2986 O VAL B 131 14277 5619 9966 -2581 -3311 2598 O ATOM 2987 CB VAL B 131 11.672 25.760 -38.019 1.00 91.97 C ANISOU 2987 CB VAL B 131 16575 6589 11780 -3199 -3687 3028 C ATOM 2988 CG1 VAL B 131 10.700 25.984 -39.168 1.00 99.43 C ANISOU 2988 CG1 VAL B 131 17918 7044 12814 -3472 -3922 3182 C ATOM 2989 CG2 VAL B 131 12.807 26.767 -38.075 1.00 89.75 C ANISOU 2989 CG2 VAL B 131 15914 6767 11421 -3511 -3535 3161 C ATOM 2990 N HIS B 132 8.753 25.055 -35.982 1.00 81.34 N ANISOU 2990 N HIS B 132 15109 5361 10436 -2118 -3491 2284 N ATOM 2991 CA HIS B 132 7.716 24.056 -35.740 1.00 75.62 C ANISOU 2991 CA HIS B 132 14111 4952 9668 -1760 -3312 2119 C ATOM 2992 C HIS B 132 6.998 23.631 -37.020 1.00 74.79 C ANISOU 2992 C HIS B 132 13864 5006 9546 -1582 -3249 2295 C ATOM 2993 O HIS B 132 6.371 22.573 -37.069 1.00 70.15 O ANISOU 2993 O HIS B 132 12986 4762 8908 -1388 -3093 2228 O ATOM 2994 CB HIS B 132 6.708 24.578 -34.714 1.00 94.80 C ANISOU 2994 CB HIS B 132 16712 7163 12146 -1406 -3329 1807 C ATOM 2995 CG HIS B 132 7.339 25.065 -33.447 1.00 95.37 C ANISOU 2995 CG HIS B 132 16926 7113 12195 -1564 -3384 1604 C ATOM 2996 ND1 HIS B 132 7.577 24.242 -32.368 1.00 96.02 N ANISOU 2996 ND1 HIS B 132 17103 7115 12265 -1285 -3344 1294 N ATOM 2997 CD2 HIS B 132 7.786 26.293 -33.090 1.00 96.22 C ANISOU 2997 CD2 HIS B 132 17096 7180 12282 -1980 -3481 1672 C ATOM 2998 CE1 HIS B 132 8.142 24.941 -31.399 1.00 96.27 C ANISOU 2998 CE1 HIS B 132 17272 7054 12251 -1523 -3424 1171 C ATOM 2999 NE2 HIS B 132 8.280 26.188 -31.812 1.00 96.53 N ANISOU 2999 NE2 HIS B 132 17280 7107 12289 -1950 -3519 1398 N ATOM 3000 N HIS B 133 7.093 24.462 -38.053 1.00 80.55 N ANISOU 3000 N HIS B 133 14814 5480 10313 -1662 -3386 2524 N ATOM 3001 CA HIS B 133 6.461 24.173 -39.337 1.00 80.67 C ANISOU 3001 CA HIS B 133 14732 5630 10288 -1533 -3361 2722 C ATOM 3002 C HIS B 133 7.125 24.968 -40.458 1.00 86.00 C ANISOU 3002 C HIS B 133 15599 6131 10945 -1839 -3483 3052 C ATOM 3003 O HIS B 133 7.525 26.113 -40.253 1.00 90.83 O ANISOU 3003 O HIS B 133 16525 6351 11636 -2007 -3645 3103 O ATOM 3004 CB HIS B 133 4.959 24.478 -39.284 1.00106.73 C ANISOU 3004 CB HIS B 133 18135 8742 13677 -1079 -3422 2604 C ATOM 3005 CG HIS B 133 4.639 25.926 -39.082 1.00109.88 C ANISOU 3005 CG HIS B 133 18947 8603 14200 -1001 -3625 2597 C ATOM 3006 ND1 HIS B 133 3.632 26.567 -39.771 1.00112.27 N ANISOU 3006 ND1 HIS B 133 19436 8649 14572 -792 -3764 2743 N ATOM 3007 CD2 HIS B 133 5.185 26.857 -38.264 1.00111.00 C ANISOU 3007 CD2 HIS B 133 19368 8398 14410 -1100 -3724 2457 C ATOM 3008 CE1 HIS B 133 3.576 27.831 -39.391 1.00114.76 C ANISOU 3008 CE1 HIS B 133 20131 8469 15003 -754 -3932 2696 C ATOM 3009 NE2 HIS B 133 4.507 28.032 -38.476 1.00114.08 N ANISOU 3009 NE2 HIS B 133 20117 8315 14914 -943 -3910 2514 N ATOM 3010 N PRO B 134 7.249 24.361 -41.650 1.00 84.63 N ANISOU 3010 N PRO B 134 15254 6244 10658 -1924 -3403 3278 N ATOM 3011 CA PRO B 134 6.809 22.999 -41.969 1.00 79.55 C ANISOU 3011 CA PRO B 134 14264 6047 9912 -1756 -3223 3223 C ATOM 3012 C PRO B 134 7.872 21.951 -41.654 1.00 75.69 C ANISOU 3012 C PRO B 134 13476 5943 9341 -1986 -3035 3174 C ATOM 3013 O PRO B 134 9.008 22.299 -41.334 1.00 77.56 O ANISOU 3013 O PRO B 134 13749 6139 9583 -2321 -3047 3255 O ATOM 3014 CB PRO B 134 6.587 23.067 -43.478 1.00 82.39 C ANISOU 3014 CB PRO B 134 14663 6473 10170 -1805 -3258 3516 C ATOM 3015 CG PRO B 134 7.619 24.035 -43.943 1.00 87.72 C ANISOU 3015 CG PRO B 134 15569 6919 10842 -2179 -3356 3766 C ATOM 3016 CD PRO B 134 7.757 25.062 -42.843 1.00 89.93 C ANISOU 3016 CD PRO B 134 16106 6781 11284 -2193 -3500 3619 C ATOM 3017 N TRP B 135 7.498 20.679 -41.746 1.00 70.81 N ANISOU 3017 N TRP B 135 12562 5683 8659 -1808 -2874 3048 N ATOM 3018 CA TRP B 135 8.440 19.584 -41.552 1.00 67.41 C ANISOU 3018 CA TRP B 135 11838 5627 8150 -1987 -2690 3016 C ATOM 3019 C TRP B 135 9.393 19.505 -42.740 1.00 69.82 C ANISOU 3019 C TRP B 135 12078 6118 8333 -2281 -2620 3295 C ATOM 3020 O TRP B 135 8.960 19.462 -43.893 1.00 71.22 O ANISOU 3020 O TRP B 135 12285 6362 8416 -2221 -2619 3448 O ATOM 3021 CB TRP B 135 7.689 18.263 -41.374 1.00 62.25 C ANISOU 3021 CB TRP B 135 10916 5277 7459 -1715 -2547 2830 C ATOM 3022 CG TRP B 135 8.585 17.075 -41.199 1.00 59.07 C ANISOU 3022 CG TRP B 135 10219 5244 6981 -1860 -2360 2801 C ATOM 3023 CD1 TRP B 135 8.913 16.151 -42.147 1.00 58.17 C ANISOU 3023 CD1 TRP B 135 9912 5448 6742 -1912 -2219 2905 C ATOM 3024 CD2 TRP B 135 9.271 16.681 -40.002 1.00 56.74 C ANISOU 3024 CD2 TRP B 135 9800 5032 6728 -1958 -2300 2657 C ATOM 3025 NE1 TRP B 135 9.760 15.207 -41.617 1.00 55.52 N ANISOU 3025 NE1 TRP B 135 9333 5376 6385 -2019 -2067 2835 N ATOM 3026 CE2 TRP B 135 9.995 15.510 -40.302 1.00 54.58 C ANISOU 3026 CE2 TRP B 135 9244 5126 6369 -2053 -2122 2693 C ATOM 3027 CE3 TRP B 135 9.341 17.206 -38.708 1.00 56.57 C ANISOU 3027 CE3 TRP B 135 9892 4807 6796 -1968 -2386 2499 C ATOM 3028 CZ2 TRP B 135 10.777 14.853 -39.355 1.00 52.32 C ANISOU 3028 CZ2 TRP B 135 8769 5008 6103 -2152 -2038 2595 C ATOM 3029 CZ3 TRP B 135 10.120 16.554 -37.771 1.00 54.23 C ANISOU 3029 CZ3 TRP B 135 9417 4690 6496 -2085 -2309 2400 C ATOM 3030 CH2 TRP B 135 10.826 15.389 -38.098 1.00 52.15 C ANISOU 3030 CH2 TRP B 135 8857 4793 6165 -2173 -2142 2457 C ATOM 3031 N ALA B 136 10.691 19.487 -42.456 1.00 70.57 N ANISOU 3031 N ALA B 136 12078 6311 8422 -2597 -2560 3364 N ATOM 3032 CA ALA B 136 11.699 19.587 -43.506 1.00 73.88 C ANISOU 3032 CA ALA B 136 12453 6878 8741 -2910 -2489 3647 C ATOM 3033 C ALA B 136 12.566 18.338 -43.654 1.00 71.05 C ANISOU 3033 C ALA B 136 11751 6981 8264 -2958 -2249 3656 C ATOM 3034 O ALA B 136 13.684 18.415 -44.163 1.00 73.31 O ANISOU 3034 O ALA B 136 11985 7450 8420 -3110 -2147 3870 O ATOM 3035 CB ALA B 136 12.577 20.813 -43.274 1.00 78.04 C ANISOU 3035 CB ALA B 136 13105 7195 9351 -3268 -2593 3771 C ATOM 3036 N PHE B 137 12.055 17.191 -43.219 1.00 80.16 N ANISOU 3036 N PHE B 137 12685 8317 9455 -2822 -2154 3426 N ATOM 3037 CA PHE B 137 12.822 15.951 -43.307 1.00 77.97 C ANISOU 3037 CA PHE B 137 12088 8445 9094 -2869 -1933 3422 C ATOM 3038 C PHE B 137 12.077 14.831 -44.029 1.00 75.71 C ANISOU 3038 C PHE B 137 11690 8389 8689 -2616 -1808 3352 C ATOM 3039 O PHE B 137 12.594 13.723 -44.164 1.00 73.86 O ANISOU 3039 O PHE B 137 11206 8460 8396 -2589 -1629 3292 O ATOM 3040 CB PHE B 137 13.272 15.489 -41.920 1.00 61.21 C ANISOU 3040 CB PHE B 137 9781 6408 7068 -2887 -1901 3241 C ATOM 3041 CG PHE B 137 14.174 16.463 -41.222 1.00 64.07 C ANISOU 3041 CG PHE B 137 10261 6542 7541 -3143 -2051 3283 C ATOM 3042 CD1 PHE B 137 15.479 16.646 -41.650 1.00 67.60 C ANISOU 3042 CD1 PHE B 137 10602 7092 7989 -3490 -2015 3490 C ATOM 3043 CD2 PHE B 137 13.721 17.195 -40.138 1.00 63.63 C ANISOU 3043 CD2 PHE B 137 10420 6171 7584 -3041 -2226 3112 C ATOM 3044 CE1 PHE B 137 16.313 17.544 -41.012 1.00 70.73 C ANISOU 3044 CE1 PHE B 137 11108 7273 8493 -3756 -2177 3531 C ATOM 3045 CE2 PHE B 137 14.551 18.094 -39.494 1.00 66.66 C ANISOU 3045 CE2 PHE B 137 10944 6328 8059 -3288 -2381 3134 C ATOM 3046 CZ PHE B 137 15.849 18.268 -39.932 1.00 70.27 C ANISOU 3046 CZ PHE B 137 11296 6880 8523 -3658 -2369 3346 C ATOM 3047 N GLY B 138 10.867 15.123 -44.491 1.00 61.96 N ANISOU 3047 N GLY B 138 10134 6492 6915 -2432 -1916 3362 N ATOM 3048 CA GLY B 138 10.100 14.168 -45.269 1.00 60.01 C ANISOU 3048 CA GLY B 138 9808 6445 6551 -2218 -1837 3310 C ATOM 3049 C GLY B 138 9.376 13.118 -44.450 1.00 55.20 C ANISOU 3049 C GLY B 138 9036 5935 6003 -1956 -1792 3044 C ATOM 3050 O GLY B 138 9.587 12.990 -43.240 1.00 52.99 O ANISOU 3050 O GLY B 138 8687 5603 5842 -1932 -1797 2891 O ATOM 3051 N ASP B 139 8.519 12.360 -45.127 1.00 55.17 N ANISOU 3051 N ASP B 139 8979 6079 5905 -1776 -1754 2997 N ATOM 3052 CA ASP B 139 7.720 11.319 -44.493 1.00 51.11 C ANISOU 3052 CA ASP B 139 8308 5671 5441 -1541 -1711 2769 C ATOM 3053 C ASP B 139 8.609 10.247 -43.865 1.00 48.30 C ANISOU 3053 C ASP B 139 7714 5551 5085 -1600 -1528 2665 C ATOM 3054 O ASP B 139 8.385 9.824 -42.725 1.00 45.30 O ANISOU 3054 O ASP B 139 7228 5178 4807 -1485 -1511 2487 O ATOM 3055 CB ASP B 139 6.779 10.689 -45.522 1.00 71.72 C ANISOU 3055 CB ASP B 139 10922 8392 7938 -1386 -1730 2773 C ATOM 3056 CG ASP B 139 5.607 9.975 -44.882 1.00 70.63 C ANISOU 3056 CG ASP B 139 10656 8301 7881 -1141 -1739 2561 C ATOM 3057 OD1 ASP B 139 4.565 10.626 -44.652 1.00 71.44 O ANISOU 3057 OD1 ASP B 139 10832 8293 8020 -968 -1879 2549 O ATOM 3058 OD2 ASP B 139 5.724 8.762 -44.615 1.00 69.16 O ANISOU 3058 OD2 ASP B 139 10287 8266 7725 -1123 -1609 2420 O ATOM 3059 N ALA B 140 9.621 9.819 -44.615 1.00 69.19 N ANISOU 3059 N ALA B 140 10277 8396 7617 -1769 -1388 2785 N ATOM 3060 CA ALA B 140 10.565 8.814 -44.141 1.00 67.93 C ANISOU 3060 CA ALA B 140 9884 8459 7466 -1820 -1213 2713 C ATOM 3061 C ALA B 140 11.398 9.347 -42.980 1.00 68.48 C ANISOU 3061 C ALA B 140 9907 8434 7679 -1936 -1253 2686 C ATOM 3062 O ALA B 140 11.834 8.586 -42.116 1.00 67.31 O ANISOU 3062 O ALA B 140 9588 8392 7595 -1890 -1182 2558 O ATOM 3063 CB ALA B 140 11.464 8.354 -45.277 1.00 48.42 C ANISOU 3063 CB ALA B 140 7341 6213 4845 -1968 -1046 2863 C ATOM 3064 N GLY B 141 11.616 10.658 -42.970 1.00 69.54 N ANISOU 3064 N GLY B 141 10210 8355 7859 -2095 -1381 2810 N ATOM 3065 CA GLY B 141 12.311 11.305 -41.874 1.00 70.74 C ANISOU 3065 CA GLY B 141 10368 8372 8138 -2221 -1464 2778 C ATOM 3066 C GLY B 141 11.471 11.273 -40.613 1.00 70.54 C ANISOU 3066 C GLY B 141 10400 8194 8208 -2010 -1559 2559 C ATOM 3067 O GLY B 141 11.980 11.012 -39.524 1.00 70.56 O ANISOU 3067 O GLY B 141 10308 8224 8279 -2020 -1554 2442 O ATOM 3068 N CYS B 142 10.177 11.536 -40.767 1.00 46.45 N ANISOU 3068 N CYS B 142 7497 4999 5154 -1812 -1644 2510 N ATOM 3069 CA CYS B 142 9.242 11.485 -39.646 1.00 44.09 C ANISOU 3069 CA CYS B 142 7245 4568 4940 -1582 -1713 2310 C ATOM 3070 C CYS B 142 9.159 10.078 -39.053 1.00 40.25 C ANISOU 3070 C CYS B 142 6532 4305 4455 -1453 -1584 2145 C ATOM 3071 O CYS B 142 9.492 9.851 -37.872 1.00 38.45 O ANISOU 3071 O CYS B 142 6276 4043 4289 -1414 -1593 2008 O ATOM 3072 CB CYS B 142 7.853 11.933 -40.107 1.00 78.52 C ANISOU 3072 CB CYS B 142 11746 8791 9299 -1379 -1808 2315 C ATOM 3073 SG CYS B 142 6.545 11.739 -38.878 1.00 79.24 S ANISOU 3073 SG CYS B 142 11861 8750 9499 -1066 -1865 2081 S ATOM 3074 N ARG B 143 8.707 9.142 -39.888 1.00 44.83 N ANISOU 3074 N ARG B 143 6971 5104 4956 -1393 -1469 2161 N ATOM 3075 CA ARG B 143 8.552 7.746 -39.494 1.00 41.83 C ANISOU 3075 CA ARG B 143 6393 4920 4581 -1276 -1351 2020 C ATOM 3076 C ARG B 143 9.844 7.185 -38.911 1.00 41.11 C ANISOU 3076 C ARG B 143 6147 4966 4505 -1419 -1260 2023 C ATOM 3077 O ARG B 143 9.832 6.525 -37.871 1.00 39.14 O ANISOU 3077 O ARG B 143 5803 4763 4305 -1351 -1232 1897 O ATOM 3078 CB ARG B 143 8.116 6.900 -40.692 1.00 62.12 C ANISOU 3078 CB ARG B 143 8884 7661 7057 -1193 -1268 2036 C ATOM 3079 CG ARG B 143 6.751 7.258 -41.254 1.00 63.00 C ANISOU 3079 CG ARG B 143 9107 7673 7158 -1036 -1375 2028 C ATOM 3080 CD ARG B 143 6.458 6.451 -42.511 1.00 62.22 C ANISOU 3080 CD ARG B 143 8956 7745 6939 -1000 -1316 2056 C ATOM 3081 NE ARG B 143 5.147 5.809 -42.463 1.00 62.31 N ANISOU 3081 NE ARG B 143 8933 7759 6982 -807 -1375 1950 N ATOM 3082 CZ ARG B 143 4.032 6.341 -42.952 1.00 63.80 C ANISOU 3082 CZ ARG B 143 9228 7843 7169 -710 -1516 1996 C ATOM 3083 NH1 ARG B 143 4.060 7.533 -43.533 1.00 65.18 N ANISOU 3083 NH1 ARG B 143 9578 7881 7305 -785 -1614 2149 N ATOM 3084 NH2 ARG B 143 2.886 5.680 -42.860 1.00 64.18 N ANISOU 3084 NH2 ARG B 143 9199 7923 7262 -544 -1566 1904 N ATOM 3085 N GLY B 144 10.956 7.462 -39.585 1.00 58.07 N ANISOU 3085 N GLY B 144 8265 7190 6611 -1619 -1216 2181 N ATOM 3086 CA GLY B 144 12.258 7.000 -39.140 1.00 57.93 C ANISOU 3086 CA GLY B 144 8065 7330 6616 -1758 -1130 2215 C ATOM 3087 C GLY B 144 12.649 7.584 -37.797 1.00 59.21 C ANISOU 3087 C GLY B 144 8256 7374 6869 -1849 -1240 2165 C ATOM 3088 O GLY B 144 13.226 6.891 -36.958 1.00 58.74 O ANISOU 3088 O GLY B 144 8034 7441 6844 -1871 -1196 2119 O ATOM 3089 N TYR B 145 12.335 8.861 -37.599 1.00 50.44 N ANISOU 3089 N TYR B 145 7366 6010 5790 -1900 -1394 2174 N ATOM 3090 CA TYR B 145 12.586 9.540 -36.330 1.00 52.35 C ANISOU 3090 CA TYR B 145 7693 6100 6098 -1991 -1521 2107 C ATOM 3091 C TYR B 145 11.877 8.825 -35.183 1.00 51.02 C ANISOU 3091 C TYR B 145 7478 5964 5945 -1801 -1505 1905 C ATOM 3092 O TYR B 145 12.521 8.345 -34.235 1.00 50.93 O ANISOU 3092 O TYR B 145 7349 6054 5948 -1867 -1500 1867 O ATOM 3093 CB TYR B 145 12.124 11.000 -36.418 1.00 52.83 C ANISOU 3093 CB TYR B 145 8043 5844 6186 -2031 -1685 2128 C ATOM 3094 CG TYR B 145 12.170 11.775 -35.119 1.00 55.35 C ANISOU 3094 CG TYR B 145 8520 5955 6556 -2079 -1829 2011 C ATOM 3095 CD1 TYR B 145 13.362 12.315 -34.651 1.00 57.88 C ANISOU 3095 CD1 TYR B 145 8855 6230 6907 -2361 -1925 2092 C ATOM 3096 CD2 TYR B 145 11.015 11.988 -34.375 1.00 55.47 C ANISOU 3096 CD2 TYR B 145 8674 5820 6582 -1848 -1871 1818 C ATOM 3097 CE1 TYR B 145 13.405 13.031 -33.468 1.00 59.90 C ANISOU 3097 CE1 TYR B 145 9286 6284 7189 -2418 -2075 1970 C ATOM 3098 CE2 TYR B 145 11.048 12.702 -33.192 1.00 57.68 C ANISOU 3098 CE2 TYR B 145 9128 5907 6880 -1882 -1993 1691 C ATOM 3099 CZ TYR B 145 12.245 13.221 -32.743 1.00 59.58 C ANISOU 3099 CZ TYR B 145 9410 6091 7138 -2170 -2104 1762 C ATOM 3100 OH TYR B 145 12.283 13.934 -31.565 1.00 61.27 O ANISOU 3100 OH TYR B 145 9826 6102 7350 -2216 -2242 1622 O ATOM 3101 N TYR B 146 10.553 8.739 -35.277 1.00 57.51 N ANISOU 3101 N TYR B 146 8380 6712 6760 -1568 -1497 1793 N ATOM 3102 CA TYR B 146 9.777 8.127 -34.196 1.00 56.59 C ANISOU 3102 CA TYR B 146 8230 6623 6651 -1383 -1467 1613 C ATOM 3103 C TYR B 146 10.117 6.646 -33.974 1.00 54.00 C ANISOU 3103 C TYR B 146 7657 6556 6304 -1343 -1329 1597 C ATOM 3104 O TYR B 146 10.250 6.192 -32.826 1.00 53.61 O ANISOU 3104 O TYR B 146 7548 6567 6256 -1305 -1314 1503 O ATOM 3105 CB TYR B 146 8.277 8.342 -34.412 1.00 44.04 C ANISOU 3105 CB TYR B 146 6742 4919 5073 -1147 -1479 1522 C ATOM 3106 CG TYR B 146 7.853 9.775 -34.175 1.00 47.34 C ANISOU 3106 CG TYR B 146 7417 5046 5525 -1126 -1618 1495 C ATOM 3107 CD1 TYR B 146 7.870 10.706 -35.205 1.00 48.69 C ANISOU 3107 CD1 TYR B 146 7722 5072 5706 -1171 -1697 1623 C ATOM 3108 CD2 TYR B 146 7.455 10.200 -32.914 1.00 49.42 C ANISOU 3108 CD2 TYR B 146 7808 5169 5800 -1054 -1671 1340 C ATOM 3109 CE1 TYR B 146 7.493 12.018 -34.988 1.00 52.04 C ANISOU 3109 CE1 TYR B 146 8400 5199 6175 -1139 -1833 1603 C ATOM 3110 CE2 TYR B 146 7.075 11.508 -32.686 1.00 52.86 C ANISOU 3110 CE2 TYR B 146 8502 5314 6270 -1014 -1795 1298 C ATOM 3111 CZ TYR B 146 7.096 12.415 -33.726 1.00 54.17 C ANISOU 3111 CZ TYR B 146 8796 5318 6468 -1053 -1880 1431 C ATOM 3112 OH TYR B 146 6.717 13.722 -33.505 1.00 57.81 O ANISOU 3112 OH TYR B 146 9531 5458 6975 -1001 -2012 1394 O ATOM 3113 N PHE B 147 10.276 5.909 -35.072 1.00 47.88 N ANISOU 3113 N PHE B 147 6763 5927 5502 -1349 -1232 1691 N ATOM 3114 CA PHE B 147 10.674 4.504 -35.012 1.00 46.06 C ANISOU 3114 CA PHE B 147 6321 5919 5260 -1308 -1100 1681 C ATOM 3115 C PHE B 147 12.000 4.336 -34.280 1.00 46.78 C ANISOU 3115 C PHE B 147 6289 6107 5378 -1456 -1101 1729 C ATOM 3116 O PHE B 147 12.135 3.463 -33.420 1.00 46.09 O ANISOU 3116 O PHE B 147 6092 6116 5304 -1396 -1064 1663 O ATOM 3117 CB PHE B 147 10.771 3.907 -36.420 1.00 43.63 C ANISOU 3117 CB PHE B 147 5943 5733 4902 -1302 -997 1768 C ATOM 3118 CG PHE B 147 11.335 2.514 -36.453 1.00 42.64 C ANISOU 3118 CG PHE B 147 5620 5814 4770 -1266 -858 1762 C ATOM 3119 CD1 PHE B 147 10.525 1.420 -36.204 1.00 41.44 C ANISOU 3119 CD1 PHE B 147 5410 5714 4624 -1103 -802 1648 C ATOM 3120 CD2 PHE B 147 12.672 2.299 -36.746 1.00 43.46 C ANISOU 3120 CD2 PHE B 147 5590 6055 4870 -1394 -782 1876 C ATOM 3121 CE1 PHE B 147 11.038 0.140 -36.235 1.00 41.16 C ANISOU 3121 CE1 PHE B 147 5218 5832 4590 -1061 -683 1641 C ATOM 3122 CE2 PHE B 147 13.192 1.021 -36.775 1.00 43.21 C ANISOU 3122 CE2 PHE B 147 5380 6196 4842 -1329 -651 1864 C ATOM 3123 CZ PHE B 147 12.373 -0.060 -36.521 1.00 42.10 C ANISOU 3123 CZ PHE B 147 5216 6075 4708 -1160 -607 1743 C ATOM 3124 N LEU B 148 12.975 5.171 -34.627 1.00 41.53 N ANISOU 3124 N LEU B 148 5638 5418 4723 -1659 -1153 1859 N ATOM 3125 CA LEU B 148 14.285 5.124 -33.987 1.00 42.96 C ANISOU 3125 CA LEU B 148 5681 5699 4942 -1828 -1179 1929 C ATOM 3126 C LEU B 148 14.180 5.402 -32.493 1.00 43.96 C ANISOU 3126 C LEU B 148 5887 5731 5083 -1836 -1305 1818 C ATOM 3127 O LEU B 148 14.775 4.685 -31.677 1.00 44.12 O ANISOU 3127 O LEU B 148 5762 5881 5118 -1852 -1302 1810 O ATOM 3128 CB LEU B 148 15.244 6.123 -34.636 1.00 48.63 C ANISOU 3128 CB LEU B 148 6412 6390 5675 -2072 -1228 2099 C ATOM 3129 CG LEU B 148 16.627 6.223 -33.990 1.00 50.66 C ANISOU 3129 CG LEU B 148 6504 6758 5989 -2282 -1279 2196 C ATOM 3130 CD1 LEU B 148 17.331 4.873 -34.007 1.00 49.76 C ANISOU 3130 CD1 LEU B 148 6099 6914 5893 -2210 -1124 2237 C ATOM 3131 CD2 LEU B 148 17.468 7.279 -34.689 1.00 53.04 C ANISOU 3131 CD2 LEU B 148 6837 7005 6311 -2547 -1338 2373 C ATOM 3132 N ARG B 149 13.424 6.440 -32.137 1.00 45.97 N ANISOU 3132 N ARG B 149 6383 5760 5325 -1813 -1416 1731 N ATOM 3133 CA ARG B 149 13.219 6.767 -30.727 1.00 47.19 C ANISOU 3133 CA ARG B 149 6657 5812 5462 -1807 -1527 1602 C ATOM 3134 C ARG B 149 12.661 5.576 -29.948 1.00 44.78 C ANISOU 3134 C ARG B 149 6257 5633 5126 -1618 -1439 1488 C ATOM 3135 O ARG B 149 13.263 5.130 -28.959 1.00 44.88 O ANISOU 3135 O ARG B 149 6200 5733 5121 -1667 -1477 1469 O ATOM 3136 CB ARG B 149 12.302 7.982 -30.570 1.00112.74 C ANISOU 3136 CB ARG B 149 15246 13838 13753 -1756 -1630 1507 C ATOM 3137 CG ARG B 149 12.901 9.277 -31.082 1.00114.23 C ANISOU 3137 CG ARG B 149 15591 13843 13970 -1992 -1781 1596 C ATOM 3138 CD ARG B 149 12.034 10.471 -30.715 1.00116.70 C ANISOU 3138 CD ARG B 149 16216 13852 14273 -1922 -1900 1465 C ATOM 3139 NE ARG B 149 12.050 10.752 -29.282 1.00119.19 N ANISOU 3139 NE ARG B 149 16705 13974 14609 -2178 -2080 1513 N ATOM 3140 CZ ARG B 149 12.852 11.641 -28.703 1.00121.11 C ANISOU 3140 CZ ARG B 149 17123 14079 14816 -2240 -2213 1383 C ATOM 3141 NH1 ARG B 149 13.708 12.341 -29.434 1.00120.79 N ANISOU 3141 NH1 ARG B 149 17103 14089 14704 -2055 -2169 1204 N ATOM 3142 NH2 ARG B 149 12.799 11.831 -27.392 1.00123.33 N ANISOU 3142 NH2 ARG B 149 17569 14170 15122 -2500 -2393 1433 N ATOM 3143 N ASP B 150 11.522 5.057 -30.406 1.00 46.43 N ANISOU 3143 N ASP B 150 6460 5855 5328 -1416 -1332 1428 N ATOM 3144 CA ASP B 150 10.896 3.906 -29.757 1.00 44.73 C ANISOU 3144 CA ASP B 150 6159 5749 5090 -1249 -1242 1334 C ATOM 3145 C ASP B 150 11.851 2.720 -29.634 1.00 43.74 C ANISOU 3145 C ASP B 150 5811 5828 4980 -1293 -1177 1412 C ATOM 3146 O ASP B 150 11.998 2.144 -28.551 1.00 43.55 O ANISOU 3146 O ASP B 150 5744 5873 4931 -1269 -1185 1371 O ATOM 3147 CB ASP B 150 9.621 3.490 -30.495 1.00 30.71 C ANISOU 3147 CB ASP B 150 4379 3966 3322 -1062 -1147 1286 C ATOM 3148 CG ASP B 150 8.386 4.206 -29.975 1.00 31.73 C ANISOU 3148 CG ASP B 150 4686 3930 3439 -933 -1190 1166 C ATOM 3149 OD1 ASP B 150 8.530 5.310 -29.404 1.00 33.86 O ANISOU 3149 OD1 ASP B 150 5131 4036 3699 -1000 -1299 1136 O ATOM 3150 OD2 ASP B 150 7.272 3.658 -30.138 1.00 31.51 O ANISOU 3150 OD2 ASP B 150 4620 3934 3419 -763 -1114 1100 O ATOM 3151 N ALA B 151 12.507 2.377 -30.740 1.00 38.13 N ANISOU 3151 N ALA B 151 4968 5214 4305 -1348 -1110 1529 N ATOM 3152 CA ALA B 151 13.449 1.262 -30.766 1.00 38.10 C ANISOU 3152 CA ALA B 151 4747 5400 4332 -1358 -1032 1605 C ATOM 3153 C ALA B 151 14.538 1.419 -29.709 1.00 39.68 C ANISOU 3153 C ALA B 151 4880 5652 4546 -1498 -1139 1654 C ATOM 3154 O ALA B 151 14.834 0.478 -28.967 1.00 39.49 O ANISOU 3154 O ALA B 151 4736 5740 4531 -1448 -1123 1657 O ATOM 3155 CB ALA B 151 14.066 1.123 -32.148 1.00 25.59 C ANISOU 3155 CB ALA B 151 3053 3904 2768 -1402 -936 1717 C ATOM 3156 N CYS B 152 15.123 2.611 -29.637 1.00 38.65 N ANISOU 3156 N CYS B 152 4836 5430 4418 -1681 -1266 1698 N ATOM 3157 CA CYS B 152 16.166 2.881 -28.653 1.00 40.32 C ANISOU 3157 CA CYS B 152 4992 5685 4640 -1849 -1404 1749 C ATOM 3158 C CYS B 152 15.645 2.762 -27.220 1.00 39.72 C ANISOU 3158 C CYS B 152 5038 5561 4491 -1789 -1490 1623 C ATOM 3159 O CYS B 152 16.329 2.214 -26.349 1.00 40.24 O ANISOU 3159 O CYS B 152 4992 5744 4552 -1830 -1551 1659 O ATOM 3160 CB CYS B 152 16.794 4.257 -28.887 1.00 59.37 C ANISOU 3160 CB CYS B 152 7502 7983 7074 -2084 -1537 1820 C ATOM 3161 SG CYS B 152 17.876 4.335 -30.333 1.00 60.72 S ANISOU 3161 SG CYS B 152 7466 8284 7322 -2230 -1445 2026 S ATOM 3162 N THR B 153 14.436 3.267 -26.982 1.00 48.66 N ANISOU 3162 N THR B 153 6393 6533 5562 -1682 -1491 1481 N ATOM 3163 CA THR B 153 13.817 3.147 -25.661 1.00 48.48 C ANISOU 3163 CA THR B 153 6501 6476 5445 -1608 -1540 1352 C ATOM 3164 C THR B 153 13.670 1.683 -25.244 1.00 47.07 C ANISOU 3164 C THR B 153 6172 6460 5255 -1464 -1430 1357 C ATOM 3165 O THR B 153 14.100 1.286 -24.152 1.00 47.52 O ANISOU 3165 O THR B 153 6218 6589 5251 -1486 -1496 1351 O ATOM 3166 CB THR B 153 12.429 3.816 -25.611 1.00105.44 C ANISOU 3166 CB THR B 153 13955 13503 12604 -1481 -1524 1198 C ATOM 3167 OG1 THR B 153 11.564 3.209 -26.579 1.00103.98 O ANISOU 3167 OG1 THR B 153 13706 13344 12459 -1301 -1369 1184 O ATOM 3168 CG2 THR B 153 12.540 5.303 -25.895 1.00107.44 C ANISOU 3168 CG2 THR B 153 14393 13554 12874 -1612 -1645 1192 C ATOM 3169 N TYR B 154 13.064 0.888 -26.124 1.00 37.59 N ANISOU 3169 N TYR B 154 4870 5306 4105 -1325 -1277 1372 N ATOM 3170 CA TYR B 154 12.864 -0.537 -25.866 1.00 36.78 C ANISOU 3170 CA TYR B 154 4636 5329 4009 -1196 -1171 1384 C ATOM 3171 C TYR B 154 14.183 -1.255 -25.606 1.00 37.72 C ANISOU 3171 C TYR B 154 4565 5595 4172 -1269 -1210 1509 C ATOM 3172 O TYR B 154 14.301 -2.033 -24.654 1.00 38.10 O ANISOU 3172 O TYR B 154 4578 5714 4182 -1229 -1230 1518 O ATOM 3173 CB TYR B 154 12.131 -1.205 -27.032 1.00 41.00 C ANISOU 3173 CB TYR B 154 5104 5873 4599 -1069 -1023 1381 C ATOM 3174 CG TYR B 154 10.654 -0.895 -27.095 1.00 40.47 C ANISOU 3174 CG TYR B 154 5169 5710 4497 -944 -972 1263 C ATOM 3175 CD1 TYR B 154 9.796 -1.312 -26.084 1.00 40.76 C ANISOU 3175 CD1 TYR B 154 5239 5766 4481 -846 -931 1191 C ATOM 3176 CD2 TYR B 154 10.113 -0.201 -28.172 1.00 40.22 C ANISOU 3176 CD2 TYR B 154 5213 5579 4487 -922 -964 1238 C ATOM 3177 CE1 TYR B 154 8.445 -1.040 -26.136 1.00 41.11 C ANISOU 3177 CE1 TYR B 154 5365 5747 4508 -728 -872 1093 C ATOM 3178 CE2 TYR B 154 8.761 0.080 -28.233 1.00 40.51 C ANISOU 3178 CE2 TYR B 154 5338 5542 4510 -794 -926 1142 C ATOM 3179 CZ TYR B 154 7.931 -0.344 -27.212 1.00 41.12 C ANISOU 3179 CZ TYR B 154 5422 5654 4548 -695 -874 1067 C ATOM 3180 OH TYR B 154 6.583 -0.072 -27.264 1.00 42.20 O ANISOU 3180 OH TYR B 154 5609 5740 4684 -564 -825 980 O ATOM 3181 N ALA B 155 15.170 -0.987 -26.457 1.00 47.45 N ANISOU 3181 N ALA B 155 5669 6879 5482 -1373 -1219 1617 N ATOM 3182 CA ALA B 155 16.492 -1.587 -26.312 1.00 49.10 C ANISOU 3182 CA ALA B 155 5657 7242 5756 -1432 -1250 1749 C ATOM 3183 C ALA B 155 17.086 -1.268 -24.945 1.00 50.32 C ANISOU 3183 C ALA B 155 5844 7418 5856 -1552 -1436 1765 C ATOM 3184 O ALA B 155 17.605 -2.154 -24.259 1.00 51.13 O ANISOU 3184 O ALA B 155 5820 7636 5971 -1519 -1470 1832 O ATOM 3185 CB ALA B 155 17.416 -1.111 -27.421 1.00 35.77 C ANISOU 3185 CB ALA B 155 3827 5612 4150 -1543 -1222 1863 C ATOM 3186 N THR B 156 16.992 -0.001 -24.551 1.00 48.43 N ANISOU 3186 N THR B 156 5792 7056 5551 -1689 -1566 1700 N ATOM 3187 CA THR B 156 17.510 0.442 -23.261 1.00 49.69 C ANISOU 3187 CA THR B 156 6031 7216 5631 -1825 -1765 1691 C ATOM 3188 C THR B 156 16.840 -0.289 -22.101 1.00 48.90 C ANISOU 3188 C THR B 156 6029 7137 5414 -1696 -1758 1612 C ATOM 3189 O THR B 156 17.519 -0.836 -21.225 1.00 49.86 O ANISOU 3189 O THR B 156 6071 7370 5504 -1732 -1861 1682 O ATOM 3190 CB THR B 156 17.322 1.957 -23.072 1.00 72.71 C ANISOU 3190 CB THR B 156 9190 9951 8487 -1980 -1899 1603 C ATOM 3191 OG1 THR B 156 17.933 2.654 -24.165 1.00 74.05 O ANISOU 3191 OG1 THR B 156 9270 10104 8764 -2133 -1917 1706 O ATOM 3192 CG2 THR B 156 17.957 2.415 -21.767 1.00 74.01 C ANISOU 3192 CG2 THR B 156 9465 10110 8546 -2131 -2119 1575 C ATOM 3193 N ALA B 157 15.509 -0.299 -22.104 1.00 48.42 N ANISOU 3193 N ALA B 157 6129 6978 5289 -1547 -1637 1481 N ATOM 3194 CA ALA B 157 14.749 -0.948 -21.037 1.00 48.09 C ANISOU 3194 CA ALA B 157 6185 6960 5125 -1430 -1600 1410 C ATOM 3195 C ALA B 157 15.082 -2.435 -20.919 1.00 48.03 C ANISOU 3195 C ALA B 157 5980 7099 5168 -1339 -1538 1527 C ATOM 3196 O ALA B 157 15.363 -2.939 -19.824 1.00 48.75 O ANISOU 3196 O ALA B 157 6089 7263 5168 -1344 -1613 1560 O ATOM 3197 CB ALA B 157 13.257 -0.753 -21.255 1.00 29.43 C ANISOU 3197 CB ALA B 157 3970 4490 2721 -1280 -1456 1271 C ATOM 3198 N LEU B 158 15.057 -3.131 -22.052 1.00 50.20 N ANISOU 3198 N LEU B 158 6086 7408 5581 -1255 -1406 1590 N ATOM 3199 CA LEU B 158 15.361 -4.559 -22.076 1.00 50.74 C ANISOU 3199 CA LEU B 158 5986 7578 5715 -1147 -1336 1690 C ATOM 3200 C LEU B 158 16.785 -4.840 -21.599 1.00 52.57 C ANISOU 3200 C LEU B 158 6051 7932 5991 -1232 -1477 1835 C ATOM 3201 O LEU B 158 17.029 -5.827 -20.902 1.00 53.44 O ANISOU 3201 O LEU B 158 6097 8115 6094 -1166 -1502 1913 O ATOM 3202 CB LEU B 158 15.139 -5.138 -23.475 1.00 39.74 C ANISOU 3202 CB LEU B 158 4476 6176 4447 -1041 -1169 1704 C ATOM 3203 CG LEU B 158 13.693 -5.161 -23.976 1.00 38.20 C ANISOU 3203 CG LEU B 158 4405 5884 4225 -940 -1037 1584 C ATOM 3204 CD1 LEU B 158 13.614 -5.794 -25.355 1.00 38.11 C ANISOU 3204 CD1 LEU B 158 4286 5873 4320 -853 -901 1601 C ATOM 3205 CD2 LEU B 158 12.791 -5.892 -22.991 1.00 38.27 C ANISOU 3205 CD2 LEU B 158 4499 5889 4151 -859 -1003 1547 C ATOM 3206 N ASN B 159 17.719 -3.970 -21.972 1.00 46.30 N ANISOU 3206 N ASN B 159 5181 7162 5249 -1383 -1577 1883 N ATOM 3207 CA ASN B 159 19.094 -4.093 -21.495 1.00 48.36 C ANISOU 3207 CA ASN B 159 5262 7555 5560 -1488 -1737 2027 C ATOM 3208 C ASN B 159 19.204 -3.902 -19.984 1.00 48.76 C ANISOU 3208 C ASN B 159 5449 7620 5457 -1572 -1931 2014 C ATOM 3209 O ASN B 159 19.999 -4.573 -19.322 1.00 50.08 O ANISOU 3209 O ASN B 159 5484 7906 5637 -1572 -2042 2138 O ATOM 3210 CB ASN B 159 20.021 -3.118 -22.224 1.00 55.98 C ANISOU 3210 CB ASN B 159 6113 8544 6611 -1666 -1805 2087 C ATOM 3211 CG ASN B 159 20.432 -3.619 -23.592 1.00 56.78 C ANISOU 3211 CG ASN B 159 5987 8717 6868 -1586 -1632 2169 C ATOM 3212 OD1 ASN B 159 20.288 -2.917 -24.590 1.00 56.57 O ANISOU 3212 OD1 ASN B 159 5975 8643 6875 -1654 -1563 2152 O ATOM 3213 ND2 ASN B 159 20.951 -4.839 -23.645 1.00 58.00 N ANISOU 3213 ND2 ASN B 159 5945 8982 7110 -1434 -1558 2261 N ATOM 3214 N VAL B 160 18.401 -2.986 -19.446 1.00 61.42 N ANISOU 3214 N VAL B 160 7325 9103 6909 -1631 -1971 1865 N ATOM 3215 CA VAL B 160 18.373 -2.747 -18.005 1.00 62.05 C ANISOU 3215 CA VAL B 160 7587 9188 6799 -1703 -2137 1822 C ATOM 3216 C VAL B 160 17.842 -3.968 -17.258 1.00 61.81 C ANISOU 3216 C VAL B 160 7577 9217 6689 -1546 -2063 1851 C ATOM 3217 O VAL B 160 18.433 -4.408 -16.267 1.00 63.00 O ANISOU 3217 O VAL B 160 7710 9466 6761 -1585 -2212 1942 O ATOM 3218 CB VAL B 160 17.528 -1.505 -17.647 1.00 41.78 C ANISOU 3218 CB VAL B 160 5331 6462 4081 -1765 -2161 1629 C ATOM 3219 CG1 VAL B 160 17.307 -1.422 -16.144 1.00 43.70 C ANISOU 3219 CG1 VAL B 160 5796 6717 4090 -1790 -2276 1558 C ATOM 3220 CG2 VAL B 160 18.203 -0.242 -18.157 1.00 42.97 C ANISOU 3220 CG2 VAL B 160 5497 6538 4292 -1967 -2298 1621 C ATOM 3221 N VAL B 161 16.730 -4.518 -17.741 1.00 48.54 N ANISOU 3221 N VAL B 161 5934 7478 5031 -1382 -1846 1787 N ATOM 3222 CA VAL B 161 16.162 -5.720 -17.134 1.00 48.54 C ANISOU 3222 CA VAL B 161 5953 7517 4970 -1248 -1759 1826 C ATOM 3223 C VAL B 161 17.149 -6.885 -17.208 1.00 49.71 C ANISOU 3223 C VAL B 161 5870 7771 5246 -1194 -1801 2016 C ATOM 3224 O VAL B 161 17.333 -7.627 -16.235 1.00 50.63 O ANISOU 3224 O VAL B 161 6007 7951 5276 -1172 -1879 2107 O ATOM 3225 CB VAL B 161 14.834 -6.124 -17.803 1.00 36.88 C ANISOU 3225 CB VAL B 161 4522 5960 3531 -1103 -1525 1736 C ATOM 3226 CG1 VAL B 161 14.290 -7.398 -17.175 1.00 37.03 C ANISOU 3226 CG1 VAL B 161 4554 6015 3501 -995 -1442 1799 C ATOM 3227 CG2 VAL B 161 13.821 -4.998 -17.684 1.00 35.79 C ANISOU 3227 CG2 VAL B 161 4598 5723 3279 -1121 -1480 1556 C ATOM 3228 N SER B 162 17.790 -7.029 -18.364 1.00 37.72 N ANISOU 3228 N SER B 162 4136 6271 3926 -1164 -1747 2079 N ATOM 3229 CA SER B 162 18.792 -8.070 -18.564 1.00 39.04 C ANISOU 3229 CA SER B 162 4066 6529 4237 -1079 -1767 2249 C ATOM 3230 C SER B 162 19.954 -7.929 -17.584 1.00 42.85 C ANISOU 3230 C SER B 162 4452 7135 4693 -1195 -2014 2380 C ATOM 3231 O SER B 162 20.427 -8.920 -17.026 1.00 44.84 O ANISOU 3231 O SER B 162 4588 7463 4987 -1116 -2083 2527 O ATOM 3232 CB SER B 162 19.312 -8.046 -20.002 1.00 40.35 C ANISOU 3232 CB SER B 162 4030 6699 4600 -1017 -1634 2270 C ATOM 3233 OG SER B 162 18.284 -8.373 -20.921 1.00 40.81 O ANISOU 3233 OG SER B 162 4033 6783 4687 -1174 -1705 2255 O ATOM 3234 N LEU B 163 20.411 -6.697 -17.378 1.00 54.47 N ANISOU 3234 N LEU B 163 5979 8618 6099 -1387 -2163 2332 N ATOM 3235 CA LEU B 163 21.479 -6.434 -16.416 1.00 56.14 C ANISOU 3235 CA LEU B 163 6121 8945 6264 -1537 -2433 2443 C ATOM 3236 C LEU B 163 21.029 -6.736 -14.989 1.00 57.47 C ANISOU 3236 C LEU B 163 6502 9125 6208 -1542 -2552 2440 C ATOM 3237 O LEU B 163 21.825 -7.178 -14.156 1.00 60.63 O ANISOU 3237 O LEU B 163 6809 9640 6586 -1568 -2742 2590 O ATOM 3238 CB LEU B 163 21.975 -4.990 -16.528 1.00 49.45 C ANISOU 3238 CB LEU B 163 5319 8076 5394 -1768 -2571 2378 C ATOM 3239 CG LEU B 163 23.041 -4.725 -17.593 1.00 50.31 C ANISOU 3239 CG LEU B 163 5126 8266 5722 -1842 -2575 2488 C ATOM 3240 CD1 LEU B 163 23.398 -3.248 -17.639 1.00 51.67 C ANISOU 3240 CD1 LEU B 163 5388 8383 5859 -2099 -2716 2424 C ATOM 3241 CD2 LEU B 163 24.277 -5.571 -17.328 1.00 53.89 C ANISOU 3241 CD2 LEU B 163 5272 8905 6298 -1822 -2714 2703 C ATOM 3242 N SER B 164 19.749 -6.497 -14.713 1.00 64.48 N ANISOU 3242 N SER B 164 7668 9906 6924 -1511 -2436 2279 N ATOM 3243 CA SER B 164 19.180 -6.825 -13.411 1.00 64.81 C ANISOU 3243 CA SER B 164 7931 9967 6728 -1502 -2496 2268 C ATOM 3244 C SER B 164 19.232 -8.331 -13.177 1.00 65.32 C ANISOU 3244 C SER B 164 7884 10084 6849 -1343 -2441 2432 C ATOM 3245 O SER B 164 19.634 -8.791 -12.105 1.00 66.55 O ANISOU 3245 O SER B 164 8073 10327 6887 -1365 -2605 2555 O ATOM 3246 CB SER B 164 17.740 -6.319 -13.306 1.00 57.24 C ANISOU 3246 CB SER B 164 7251 8895 5604 -1469 -2328 2063 C ATOM 3247 OG SER B 164 17.677 -4.915 -13.485 1.00 57.07 O ANISOU 3247 OG SER B 164 7358 8793 5535 -1598 -2386 1908 O ATOM 3248 N VAL B 165 18.832 -9.091 -14.193 1.00 52.46 N ANISOU 3248 N VAL B 165 6143 8393 5399 -1187 -2220 2436 N ATOM 3249 CA VAL B 165 18.870 -10.548 -14.121 1.00 52.93 C ANISOU 3249 CA VAL B 165 6112 8458 5543 -1028 -2153 2582 C ATOM 3250 C VAL B 165 20.299 -11.059 -13.937 1.00 55.55 C ANISOU 3250 C VAL B 165 6205 8898 6003 -1008 -2339 2788 C ATOM 3251 O VAL B 165 20.561 -11.905 -13.078 1.00 57.80 O ANISOU 3251 O VAL B 165 6506 9228 6228 -962 -2447 2937 O ATOM 3252 CB VAL B 165 18.260 -11.190 -15.383 1.00 52.93 C ANISOU 3252 CB VAL B 165 6032 8354 5726 -881 -1900 2530 C ATOM 3253 CG1 VAL B 165 18.423 -12.702 -15.344 1.00 53.74 C ANISOU 3253 CG1 VAL B 165 6037 8435 5947 -720 -1856 2685 C ATOM 3254 CG2 VAL B 165 16.794 -10.811 -15.514 1.00 50.47 C ANISOU 3254 CG2 VAL B 165 5931 7949 5297 -881 -1726 2355 C ATOM 3255 N GLU B 166 21.217 -10.535 -14.745 1.00 55.19 N ANISOU 3255 N GLU B 166 5931 8903 6136 -1043 -2376 2810 N ATOM 3256 CA GLU B 166 22.620 -10.933 -14.683 1.00 58.22 C ANISOU 3256 CA GLU B 166 6034 9410 6678 -1008 -2534 3009 C ATOM 3257 C GLU B 166 23.220 -10.665 -13.307 1.00 62.00 C ANISOU 3257 C GLU B 166 6543 10011 7004 -1161 -2845 3112 C ATOM 3258 O GLU B 166 23.907 -11.518 -12.742 1.00 65.02 O ANISOU 3258 O GLU B 166 6765 10487 7452 -1095 -2999 3308 O ATOM 3259 CB GLU B 166 23.437 -10.206 -15.755 1.00 74.40 C ANISOU 3259 CB GLU B 166 7816 11509 8943 -1026 -2479 3010 C ATOM 3260 CG GLU B 166 23.127 -10.621 -17.187 1.00 74.31 C ANISOU 3260 CG GLU B 166 7705 11415 9113 -828 -2205 2973 C ATOM 3261 CD GLU B 166 23.857 -11.881 -17.613 1.00 76.04 C ANISOU 3261 CD GLU B 166 7574 11745 9572 -752 -2184 3090 C ATOM 3262 OE1 GLU B 166 24.226 -12.693 -16.738 1.00 77.32 O ANISOU 3262 OE1 GLU B 166 7539 12057 9780 -845 -2392 3227 O ATOM 3263 OE2 GLU B 166 24.068 -12.055 -18.832 1.00 76.28 O ANISOU 3263 OE2 GLU B 166 7522 11720 9738 -599 -1959 3046 O ATOM 3264 N LEU B 167 22.956 -9.477 -12.771 1.00 58.74 N ANISOU 3264 N LEU B 167 6346 9589 6385 -1360 -2947 2978 N ATOM 3265 CA LEU B 167 23.473 -9.103 -11.461 1.00 63.14 C ANISOU 3265 CA LEU B 167 6987 10251 6755 -1527 -3255 3047 C ATOM 3266 C LEU B 167 22.865 -9.973 -10.364 1.00 64.44 C ANISOU 3266 C LEU B 167 7353 10416 6717 -1445 -3284 3116 C ATOM 3267 O LEU B 167 23.551 -10.361 -9.416 1.00 68.62 O ANISOU 3267 O LEU B 167 7839 11057 7177 -1476 -3527 3286 O ATOM 3268 CB LEU B 167 23.202 -7.624 -11.176 1.00 63.27 C ANISOU 3268 CB LEU B 167 7227 10224 6589 -1754 -3347 2858 C ATOM 3269 CG LEU B 167 23.833 -7.069 -9.897 1.00 68.31 C ANISOU 3269 CG LEU B 167 7886 10973 7096 -1986 -3706 2915 C ATOM 3270 CD1 LEU B 167 25.344 -7.244 -9.924 1.00 71.26 C ANISOU 3270 CD1 LEU B 167 8513 11394 7169 -2008 -3865 2948 C ATOM 3271 CD2 LEU B 167 23.464 -5.610 -9.705 1.00 68.13 C ANISOU 3271 CD2 LEU B 167 8011 10869 7005 -2204 -3766 2729 C ATOM 3272 N TYR B 168 21.577 -10.278 -10.501 1.00 61.16 N ANISOU 3272 N TYR B 168 7149 9882 6205 -1349 -3042 2997 N ATOM 3273 CA TYR B 168 20.898 -11.149 -9.548 1.00 62.26 C ANISOU 3273 CA TYR B 168 7479 10019 6159 -1276 -3023 3073 C ATOM 3274 C TYR B 168 21.536 -12.534 -9.521 1.00 64.07 C ANISOU 3274 C TYR B 168 7500 10278 6567 -1115 -3072 3319 C ATOM 3275 O TYR B 168 21.841 -13.065 -8.454 1.00 67.75 O ANISOU 3275 O TYR B 168 8026 10816 6900 -1119 -3254 3486 O ATOM 3276 CB TYR B 168 19.409 -11.267 -9.884 1.00 69.37 C ANISOU 3276 CB TYR B 168 8574 10794 6989 -1197 -2723 2917 C ATOM 3277 CG TYR B 168 18.674 -12.282 -9.036 1.00 70.02 C ANISOU 3277 CG TYR B 168 8824 10869 6912 -1123 -2658 3015 C ATOM 3278 CD1 TYR B 168 18.142 -11.930 -7.803 1.00 70.55 C ANISOU 3278 CD1 TYR B 168 9176 10989 6640 -1221 -2708 2967 C ATOM 3279 CD2 TYR B 168 18.514 -13.595 -9.468 1.00 70.37 C ANISOU 3279 CD2 TYR B 168 8756 10846 7135 -961 -2539 3156 C ATOM 3280 CE1 TYR B 168 17.471 -12.853 -7.025 1.00 71.54 C ANISOU 3280 CE1 TYR B 168 9453 11121 6608 -1170 -2635 3076 C ATOM 3281 CE2 TYR B 168 17.850 -14.525 -8.695 1.00 71.14 C ANISOU 3281 CE2 TYR B 168 9013 10925 7093 -917 -2484 3266 C ATOM 3282 CZ TYR B 168 17.328 -14.148 -7.476 1.00 71.59 C ANISOU 3282 CZ TYR B 168 9336 11056 6811 -1027 -2527 3234 C ATOM 3283 OH TYR B 168 16.662 -15.072 -6.703 1.00 72.56 O ANISOU 3283 OH TYR B 168 9614 11173 6782 -998 -2459 3362 O ATOM 3284 N LEU B 169 21.728 -13.115 -10.700 1.00 73.53 N ANISOU 3284 N LEU B 169 8466 11413 8057 -966 -2910 3340 N ATOM 3285 CA LEU B 169 22.314 -14.447 -10.808 1.00 75.18 C ANISOU 3285 CA LEU B 169 8474 11620 8471 -778 -2932 3552 C ATOM 3286 C LEU B 169 23.774 -14.455 -10.370 1.00 79.72 C ANISOU 3286 C LEU B 169 8823 12355 9110 -816 -3236 3744 C ATOM 3287 O LEU B 169 24.286 -15.475 -9.906 1.00 82.87 O ANISOU 3287 O LEU B 169 9150 12783 9553 -702 -3365 3957 O ATOM 3288 CB LEU B 169 22.189 -14.974 -12.238 1.00 60.05 C ANISOU 3288 CB LEU B 169 6371 9605 6839 -614 -2689 3497 C ATOM 3289 CG LEU B 169 20.755 -15.175 -12.726 1.00 56.05 C ANISOU 3289 CG LEU B 169 6046 8931 6318 -535 -2409 3363 C ATOM 3290 CD1 LEU B 169 20.734 -15.652 -14.168 1.00 53.38 C ANISOU 3290 CD1 LEU B 169 5528 8507 6247 -381 -2205 3310 C ATOM 3291 CD2 LEU B 169 20.018 -16.150 -11.821 1.00 57.48 C ANISOU 3291 CD2 LEU B 169 6398 9044 6400 -462 -2408 3491 C ATOM 3292 N ALA B 170 24.439 -13.315 -10.518 1.00 68.99 N ANISOU 3292 N ALA B 170 7350 11097 7766 -982 -3359 3679 N ATOM 3293 CA ALA B 170 25.835 -13.195 -10.121 1.00 73.83 C ANISOU 3293 CA ALA B 170 7716 11883 8453 -1057 -3663 3855 C ATOM 3294 C ALA B 170 25.971 -13.071 -8.607 1.00 78.15 C ANISOU 3294 C ALA B 170 8454 12518 8720 -1183 -3961 3958 C ATOM 3295 O ALA B 170 26.955 -13.527 -8.027 1.00 82.70 O ANISOU 3295 O ALA B 170 8854 13212 9354 -1145 -4205 4185 O ATOM 3296 CB ALA B 170 26.486 -12.007 -10.812 1.00 73.70 C ANISOU 3296 CB ALA B 170 7549 11939 8516 -1242 -3713 3755 C ATOM 3297 N ILE B 171 24.979 -12.456 -7.969 1.00 79.88 N ANISOU 3297 N ILE B 171 9034 12687 8630 -1325 -3939 3792 N ATOM 3298 CA ILE B 171 25.035 -12.228 -6.527 1.00 84.07 C ANISOU 3298 CA ILE B 171 9799 13306 8839 -1465 -4207 3855 C ATOM 3299 C ILE B 171 24.443 -13.387 -5.717 1.00 85.28 C ANISOU 3299 C ILE B 171 10101 13429 8874 -1317 -4178 4014 C ATOM 3300 O ILE B 171 24.852 -13.632 -4.581 1.00 90.10 O ANISOU 3300 O ILE B 171 10743 14146 9344 -1353 -4452 4204 O ATOM 3301 CB ILE B 171 24.366 -10.884 -6.133 1.00 82.96 C ANISOU 3301 CB ILE B 171 10000 13132 8388 -1677 -4206 3602 C ATOM 3302 CG1 ILE B 171 24.752 -10.480 -4.709 1.00 88.07 C ANISOU 3302 CG1 ILE B 171 10886 13890 8685 -1835 -4514 3663 C ATOM 3303 CG2 ILE B 171 22.854 -10.955 -6.283 1.00 78.26 C ANISOU 3303 CG2 ILE B 171 9648 12386 7700 -1584 -3854 3414 C ATOM 3304 CD1 ILE B 171 24.199 -9.138 -4.291 1.00 88.01 C ANISOU 3304 CD1 ILE B 171 11225 13848 8367 -2034 -4534 3404 C ATOM 3305 N CYS B 172 23.492 -14.107 -6.306 1.00 84.62 N ANISOU 3305 N CYS B 172 10108 13197 8849 -1164 -3860 3950 N ATOM 3306 CA CYS B 172 22.886 -15.254 -5.636 1.00 85.76 C ANISOU 3306 CA CYS B 172 10408 13290 8889 -1045 -3811 4104 C ATOM 3307 C CYS B 172 23.756 -16.498 -5.763 1.00 88.61 C ANISOU 3307 C CYS B 172 10510 13657 9501 -859 -3936 4383 C ATOM 3308 O CYS B 172 23.680 -17.408 -4.937 1.00 92.53 O ANISOU 3308 O CYS B 172 11098 14190 9868 -831 -4109 4596 O ATOM 3309 CB CYS B 172 21.484 -15.528 -6.182 1.00 80.56 C ANISOU 3309 CB CYS B 172 9905 12468 8236 -959 -3448 3962 C ATOM 3310 SG CYS B 172 20.219 -14.399 -5.565 1.00 78.69 S ANISOU 3310 SG CYS B 172 10000 12223 7675 -1131 -3289 3664 S ATOM 3311 N HIS B 173 24.583 -16.531 -6.802 1.00 97.39 N ANISOU 3311 N HIS B 173 11305 14733 10965 -722 -3844 4386 N ATOM 3312 CA HIS B 173 25.524 -17.626 -6.997 1.00 99.87 C ANISOU 3312 CA HIS B 173 11359 15042 11544 -506 -3937 4633 C ATOM 3313 C HIS B 173 26.929 -17.066 -7.200 1.00101.65 C ANISOU 3313 C HIS B 173 11197 15416 12009 -503 -4100 4693 C ATOM 3314 O HIS B 173 27.485 -17.163 -8.290 1.00100.80 O ANISOU 3314 O HIS B 173 10829 15263 12208 -332 -3938 4684 O ATOM 3315 CB HIS B 173 25.112 -18.469 -8.204 1.00121.11 C ANISOU 3315 CB HIS B 173 14024 17529 14465 -280 -3624 4598 C ATOM 3316 CG HIS B 173 23.662 -18.842 -8.211 1.00120.01 C ANISOU 3316 CG HIS B 173 14224 17243 14131 -310 -3417 4508 C ATOM 3317 ND1 HIS B 173 23.181 -19.979 -7.597 1.00117.07 N ANISOU 3317 ND1 HIS B 173 13908 16721 13854 -261 -3102 4316 N ATOM 3318 CD2 HIS B 173 22.586 -18.227 -8.758 1.00121.63 C ANISOU 3318 CD2 HIS B 173 14719 17447 14050 -392 -3479 4593 C ATOM 3319 CE1 HIS B 173 21.873 -20.049 -7.766 1.00116.95 C ANISOU 3319 CE1 HIS B 173 14178 16620 13638 -314 -2981 4290 C ATOM 3320 NE2 HIS B 173 21.486 -18.998 -8.466 1.00119.71 N ANISOU 3320 NE2 HIS B 173 14675 17059 13750 -393 -3192 4457 N ATOM 3321 N PRO B 174 27.512 -16.488 -6.137 1.00150.30 N ANISOU 3321 N PRO B 174 17316 21764 18029 -694 -4426 4765 N ATOM 3322 CA PRO B 174 28.763 -15.725 -6.224 1.00152.53 C ANISOU 3322 CA PRO B 174 17227 22213 18514 -761 -4596 4812 C ATOM 3323 C PRO B 174 29.962 -16.558 -6.670 1.00154.94 C ANISOU 3323 C PRO B 174 17129 22556 19186 -494 -4610 5026 C ATOM 3324 O PRO B 174 30.954 -15.998 -7.138 1.00155.09 O ANISOU 3324 O PRO B 174 16808 22661 19458 -470 -4558 5011 O ATOM 3325 CB PRO B 174 28.978 -15.238 -4.784 1.00101.59 C ANISOU 3325 CB PRO B 174 10878 15903 11817 -991 -4947 4861 C ATOM 3326 CG PRO B 174 27.650 -15.382 -4.113 1.00100.89 C ANISOU 3326 CG PRO B 174 11248 15743 11342 -1091 -4934 4782 C ATOM 3327 CD PRO B 174 27.025 -16.575 -4.751 1.00 98.16 C ANISOU 3327 CD PRO B 174 11016 15229 11051 -865 -4664 4822 C ATOM 3328 N PHE B 175 29.874 -17.875 -6.525 1.00133.98 N ANISOU 3328 N PHE B 175 14528 19819 16557 -291 -4647 5204 N ATOM 3329 CA PHE B 175 30.985 -18.753 -6.877 1.00136.16 C ANISOU 3329 CA PHE B 175 14478 20082 17173 -1 -4630 5371 C ATOM 3330 C PHE B 175 30.845 -19.317 -8.287 1.00135.48 C ANISOU 3330 C PHE B 175 14328 19826 17322 266 -4314 5341 C ATOM 3331 O PHE B 175 31.692 -19.077 -9.148 1.00136.85 O ANISOU 3331 O PHE B 175 14159 20023 17813 480 -4223 5395 O ATOM 3332 CB PHE B 175 31.102 -19.898 -5.868 1.00149.50 C ANISOU 3332 CB PHE B 175 16278 21735 18790 91 -4821 5549 C ATOM 3333 CG PHE B 175 31.298 -19.440 -4.454 1.00150.28 C ANISOU 3333 CG PHE B 175 16432 21994 18672 -154 -5122 5560 C ATOM 3334 CD1 PHE B 175 32.567 -19.183 -3.965 1.00150.81 C ANISOU 3334 CD1 PHE B 175 16785 22032 18484 -194 -5290 5653 C ATOM 3335 CD2 PHE B 175 30.212 -19.265 -3.612 1.00150.51 C ANISOU 3335 CD2 PHE B 175 16247 22198 18740 -358 -5234 5475 C ATOM 3336 CE1 PHE B 175 32.751 -18.760 -2.662 1.00151.67 C ANISOU 3336 CE1 PHE B 175 16962 22285 18379 -416 -5569 5654 C ATOM 3337 CE2 PHE B 175 30.389 -18.843 -2.309 1.00151.41 C ANISOU 3337 CE2 PHE B 175 16432 22441 18656 -593 -5520 5478 C ATOM 3338 CZ PHE B 175 31.660 -18.590 -1.833 1.00151.97 C ANISOU 3338 CZ PHE B 175 16789 22484 18468 -616 -5690 5562 C ATOM 3339 N LYS B 176 29.773 -20.067 -8.516 1.00169.46 N ANISOU 3339 N LYS B 176 18996 23931 21461 244 -4092 5190 N ATOM 3340 CA LYS B 176 29.574 -20.734 -9.797 1.00168.77 C ANISOU 3340 CA LYS B 176 18950 23625 21553 451 -3744 5069 C ATOM 3341 C LYS B 176 28.483 -20.094 -10.645 1.00167.03 C ANISOU 3341 C LYS B 176 18635 23424 21406 368 -3502 4811 C ATOM 3342 O LYS B 176 27.614 -20.785 -11.178 1.00166.91 O ANISOU 3342 O LYS B 176 18521 23295 21602 554 -3244 4721 O ATOM 3343 CB LYS B 176 29.273 -22.218 -9.591 1.00177.24 C ATOM 3344 CG LYS B 176 30.457 -23.018 -9.082 1.00177.24 C ATOM 3345 CD LYS B 176 30.126 -24.495 -8.996 1.00177.24 C ATOM 3346 CE LYS B 176 31.333 -25.301 -8.552 1.00177.24 C ATOM 3347 NZ LYS B 176 31.020 -26.751 -8.451 1.00177.24 N ATOM 3348 N ALA B 177 28.527 -18.774 -10.766 1.00182.54 N ANISOU 3348 N ALA B 177 20647 25526 23184 87 -3597 4697 N ATOM 3349 CA ALA B 177 27.668 -18.088 -11.714 1.00180.88 C ANISOU 3349 CA ALA B 177 20382 25331 23013 -25 -3397 4467 C ATOM 3350 C ALA B 177 28.309 -18.190 -13.085 1.00182.05 C ANISOU 3350 C ALA B 177 20105 25624 23442 49 -3384 4517 C ATOM 3351 O ALA B 177 27.613 -18.185 -14.102 1.00180.57 O ANISOU 3351 O ALA B 177 19854 25461 23294 -48 -3225 4354 O ATOM 3352 CB ALA B 177 27.494 -16.630 -11.327 1.00155.89 C ANISOU 3352 CB ALA B 177 17432 22235 19563 -343 -3507 4327 C ATOM 3353 N LYS B 178 29.637 -18.316 -13.090 1.00183.11 N ANISOU 3353 N LYS B 178 19941 25861 23771 224 -3542 4749 N ATOM 3354 CA LYS B 178 30.442 -18.123 -14.290 1.00184.56 C ANISOU 3354 CA LYS B 178 19689 26202 24235 315 -3491 4802 C ATOM 3355 C LYS B 178 29.951 -16.833 -14.911 1.00184.46 C ANISOU 3355 C LYS B 178 19631 26053 24405 540 -3112 4659 C ATOM 3356 O LYS B 178 30.223 -15.736 -14.420 1.00184.77 O ANISOU 3356 O LYS B 178 19398 26207 24601 547 -2975 4612 O ATOM 3357 CB LYS B 178 30.251 -19.273 -15.284 1.00122.23 C ATOM 3358 CG LYS B 178 30.437 -20.667 -14.711 1.00122.23 C ATOM 3359 CD LYS B 178 30.103 -21.718 -15.763 1.00122.23 C ATOM 3360 CE LYS B 178 30.268 -23.131 -15.228 1.00122.23 C ATOM 3361 NZ LYS B 178 29.904 -24.146 -16.255 1.00122.23 N ATOM 3362 N THR B 179 29.210 -16.990 -15.999 1.00210.20 N ANISOU 3362 N THR B 179 23158 29070 27638 714 -2947 4598 N ATOM 3363 CA THR B 179 28.302 -15.965 -16.480 1.00209.35 C ANISOU 3363 CA THR B 179 23077 28808 27658 897 -2601 4431 C ATOM 3364 C THR B 179 27.204 -16.702 -17.234 1.00207.11 C ANISOU 3364 C THR B 179 22900 28540 27253 669 -2433 4197 C ATOM 3365 O THR B 179 27.427 -17.805 -17.738 1.00207.26 O ANISOU 3365 O THR B 179 22706 28642 27403 701 -2263 4126 O ATOM 3366 CB THR B 179 28.991 -14.919 -17.373 1.00108.92 C ANISOU 3366 CB THR B 179 10685 15807 14894 1051 -2489 4395 C ATOM 3367 OG1 THR B 179 30.269 -14.578 -16.821 1.00111.34 O ANISOU 3367 OG1 THR B 179 10892 16065 15349 1301 -2622 4618 O ATOM 3368 CG2 THR B 179 28.138 -13.666 -17.447 1.00108.07 C ANISOU 3368 CG2 THR B 179 10656 15532 14876 1186 -2150 4188 C ATOM 3369 N LEU B 180 26.023 -16.099 -17.288 1.00108.64 N ANISOU 3369 N LEU B 180 10759 15992 14526 447 -2483 4089 N ATOM 3370 CA LEU B 180 24.821 -16.758 -17.786 1.00105.47 C ANISOU 3370 CA LEU B 180 10502 15595 13977 209 -2384 3883 C ATOM 3371 C LEU B 180 24.996 -17.419 -19.148 1.00103.18 C ANISOU 3371 C LEU B 180 10157 15243 13801 297 -2078 3718 C ATOM 3372 O LEU B 180 24.416 -18.470 -19.418 1.00102.10 O ANISOU 3372 O LEU B 180 9966 15192 13636 128 -2027 3620 O ATOM 3373 CB LEU B 180 23.671 -15.754 -17.840 1.00 74.23 C ANISOU 3373 CB LEU B 180 6390 11850 9961 -47 -2609 3934 C ATOM 3374 CG LEU B 180 22.275 -16.324 -18.082 1.00 71.37 C ANISOU 3374 CG LEU B 180 6265 11472 9379 -337 -2624 3755 C ATOM 3375 CD1 LEU B 180 21.999 -17.461 -17.112 1.00 72.79 C ANISOU 3375 CD1 LEU B 180 6208 11817 9632 -523 -2685 3757 C ATOM 3376 CD2 LEU B 180 21.254 -15.220 -17.920 1.00 72.68 C ANISOU 3376 CD2 LEU B 180 6693 11630 9291 -493 -2857 3780 C ATOM 3377 N MET B 181 25.808 -16.807 -20.001 1.00 95.54 N ANISOU 3377 N MET B 181 9243 14114 12945 546 -1884 3684 N ATOM 3378 CA MET B 181 25.986 -17.308 -21.354 1.00 95.66 C ANISOU 3378 CA MET B 181 9232 14060 13054 656 -1594 3527 C ATOM 3379 C MET B 181 27.439 -17.272 -21.789 1.00 96.58 C ANISOU 3379 C MET B 181 9006 14372 13320 679 -1508 3549 C ATOM 3380 O MET B 181 28.300 -16.694 -21.122 1.00 95.90 O ANISOU 3380 O MET B 181 8764 14470 13205 472 -1642 3604 O ATOM 3381 CB MET B 181 25.192 -16.459 -22.343 1.00 88.23 C ANISOU 3381 CB MET B 181 8590 13003 11930 482 -1477 3316 C ATOM 3382 CG MET B 181 23.700 -16.418 -22.124 1.00 87.38 C ANISOU 3382 CG MET B 181 8804 12714 11683 464 -1508 3284 C ATOM 3383 SD MET B 181 22.996 -14.940 -22.877 1.00 86.55 S ANISOU 3383 SD MET B 181 8832 12691 11365 243 -1795 3387 S ATOM 3384 CE MET B 181 21.344 -15.511 -23.252 1.00 84.99 C ANISOU 3384 CE MET B 181 8690 12588 11015 -37 -1798 3225 C ATOM 3385 N SER B 182 27.696 -17.896 -22.932 1.00116.55 N ANISOU 3385 N SER B 182 11425 16855 16003 927 -1279 3506 N ATOM 3386 CA SER B 182 28.965 -17.741 -23.613 1.00117.82 C ANISOU 3386 CA SER B 182 11235 17212 16317 999 -1156 3546 C ATOM 3387 C SER B 182 28.942 -16.377 -24.284 1.00116.26 C ANISOU 3387 C SER B 182 11015 17139 16017 724 -1107 3459 C ATOM 3388 O SER B 182 27.886 -15.751 -24.392 1.00114.23 O ANISOU 3388 O SER B 182 11048 16760 15592 564 -1062 3301 O ATOM 3389 CB SER B 182 29.149 -18.845 -24.654 1.00135.08 C ANISOU 3389 CB SER B 182 13403 19291 18631 1313 -873 3457 C ATOM 3390 OG SER B 182 29.072 -20.129 -24.057 1.00138.05 O ANISOU 3390 OG SER B 182 13751 19558 19146 1594 -922 3563 O ATOM 3391 N ARG B 183 30.103 -15.913 -24.730 1.00138.04 N ANISOU 3391 N ARG B 183 13419 20140 18888 667 -1123 3575 N ATOM 3392 CA ARG B 183 30.199 -14.602 -25.360 1.00136.88 C ANISOU 3392 CA ARG B 183 13226 20117 18666 389 -1095 3530 C ATOM 3393 C ARG B 183 29.363 -14.532 -26.637 1.00136.09 C ANISOU 3393 C ARG B 183 13303 19912 18493 425 -802 3337 C ATOM 3394 O ARG B 183 28.685 -13.533 -26.895 1.00134.49 O ANISOU 3394 O ARG B 183 13264 19683 18152 190 -793 3240 O ATOM 3395 CB ARG B 183 31.661 -14.251 -25.643 1.00146.25 C ANISOU 3395 CB ARG B 183 13955 21590 20021 353 -1126 3711 C ATOM 3396 CG ARG B 183 32.513 -14.155 -24.386 1.00147.05 C ANISOU 3396 CG ARG B 183 13858 21832 20180 242 -1462 3913 C ATOM 3397 CD ARG B 183 33.948 -13.770 -24.705 1.00149.20 C ANISOU 3397 CD ARG B 183 13619 22400 20668 268 -1464 4109 C ATOM 3398 NE ARG B 183 34.755 -13.666 -23.492 1.00149.59 N ANISOU 3398 NE ARG B 183 13503 22623 20711 -50 -1782 4257 N ATOM 3399 CZ ARG B 183 36.045 -13.344 -23.472 1.00151.04 C ANISOU 3399 CZ ARG B 183 13266 23077 21043 -174 -1816 4417 C ATOM 3400 NH1 ARG B 183 36.687 -13.090 -24.605 1.00152.15 N ANISOU 3400 NH1 ARG B 183 13101 23363 21345 10 -1525 4452 N ATOM 3401 NH2 ARG B 183 36.694 -13.275 -22.317 1.00151.52 N ANISOU 3401 NH2 ARG B 183 13214 23268 21086 -491 -2139 4541 N ATOM 3402 N SER B 184 29.402 -15.606 -27.420 1.00138.57 N ANISOU 3402 N SER B 184 13600 20156 18896 727 -576 3281 N ATOM 3403 CA SER B 184 28.614 -15.698 -28.644 1.00138.02 C ANISOU 3403 CA SER B 184 13723 19976 18743 789 -309 3091 C ATOM 3404 C SER B 184 27.119 -15.650 -28.340 1.00136.14 C ANISOU 3404 C SER B 184 13900 19498 18330 683 -359 2933 C ATOM 3405 O SER B 184 26.363 -14.949 -29.014 1.00134.71 O ANISOU 3405 O SER B 184 13896 19269 18019 542 -268 2803 O ATOM 3406 CB SER B 184 28.955 -16.981 -29.405 1.00114.16 C ANISOU 3406 CB SER B 184 10622 16907 15847 1151 -80 3054 C ATOM 3407 OG SER B 184 28.629 -18.130 -28.642 1.00114.18 O ANISOU 3407 OG SER B 184 10768 16716 15901 1339 -173 3063 O ATOM 3408 N ARG B 185 26.699 -16.393 -27.321 1.00 82.18 N ANISOU 3408 N ARG B 185 7207 12521 11495 754 -503 2960 N ATOM 3409 CA ARG B 185 25.299 -16.409 -26.911 1.00 80.62 C ANISOU 3409 CA ARG B 185 7369 12119 11142 653 -558 2837 C ATOM 3410 C ARG B 185 24.857 -15.051 -26.381 1.00 78.74 C ANISOU 3410 C ARG B 185 7221 11939 10759 343 -701 2818 C ATOM 3411 O ARG B 185 23.727 -14.624 -26.616 1.00 77.31 O ANISOU 3411 O ARG B 185 7292 11639 10442 233 -661 2677 O ATOM 3412 CB ARG B 185 25.057 -17.472 -25.840 1.00145.50 C ANISOU 3412 CB ARG B 185 15688 20208 19388 764 -698 2914 C ATOM 3413 CG ARG B 185 25.147 -18.902 -26.334 1.00146.25 C ANISOU 3413 CG ARG B 185 15986 20070 19513 974 -558 2814 C ATOM 3414 CD ARG B 185 24.802 -19.872 -25.219 1.00148.89 C ANISOU 3414 CD ARG B 185 16136 20408 20028 1274 -404 2841 C ATOM 3415 NE ARG B 185 24.896 -21.264 -25.649 1.00149.00 N ANISOU 3415 NE ARG B 185 16117 20466 20029 1316 -165 2702 N ATOM 3416 CZ ARG B 185 24.702 -22.305 -24.846 1.00151.05 C ANISOU 3416 CZ ARG B 185 16237 20743 20410 1575 24 2681 C ATOM 3417 NH1 ARG B 185 24.404 -22.112 -23.569 1.00152.54 N ANISOU 3417 NH1 ARG B 185 16296 20895 20767 1830 -4 2791 N ATOM 3418 NH2 ARG B 185 24.807 -23.540 -25.318 1.00151.67 N ANISOU 3418 NH2 ARG B 185 16316 20876 20436 1590 244 2552 N ATOM 3419 N THR B 186 25.748 -14.383 -25.656 1.00 75.91 N ANISOU 3419 N THR B 186 6653 11755 10434 207 -876 2961 N ATOM 3420 CA THR B 186 25.445 -13.074 -25.091 1.00 74.44 C ANISOU 3420 CA THR B 186 6554 11611 10117 -89 -1031 2945 C ATOM 3421 C THR B 186 25.268 -12.043 -26.201 1.00 73.66 C ANISOU 3421 C THR B 186 6478 11537 9974 -215 -884 2848 C ATOM 3422 O THR B 186 24.340 -11.233 -26.165 1.00 72.15 O ANISOU 3422 O THR B 186 6526 11246 9643 -372 -908 2733 O ATOM 3423 CB THR B 186 26.544 -12.608 -24.117 1.00 93.77 C ANISOU 3423 CB THR B 186 8761 14246 12622 -222 -1269 3124 C ATOM 3424 OG1 THR B 186 26.765 -13.619 -23.125 1.00 94.30 O ANISOU 3424 OG1 THR B 186 8845 14286 12699 -123 -1436 3223 O ATOM 3425 CG2 THR B 186 26.136 -11.313 -23.432 1.00 92.40 C ANISOU 3425 CG2 THR B 186 8710 14087 12309 -537 -1431 3086 C ATOM 3426 N LYS B 187 26.157 -12.084 -27.190 1.00 63.08 N ANISOU 3426 N LYS B 187 4887 10331 8748 -134 -726 2901 N ATOM 3427 CA LYS B 187 26.043 -11.202 -28.347 1.00 62.23 C ANISOU 3427 CA LYS B 187 4797 10256 8589 -243 -568 2832 C ATOM 3428 C LYS B 187 24.759 -11.491 -29.121 1.00 60.91 C ANISOU 3428 C LYS B 187 4936 9898 8308 -166 -412 2643 C ATOM 3429 O LYS B 187 24.070 -10.569 -29.570 1.00 59.17 O ANISOU 3429 O LYS B 187 4888 9619 7973 -326 -398 2557 O ATOM 3430 CB LYS B 187 27.264 -11.344 -29.257 1.00 91.71 C ANISOU 3430 CB LYS B 187 8200 14187 12457 -136 -389 2929 C ATOM 3431 CG LYS B 187 28.553 -10.818 -28.643 1.00 92.79 C ANISOU 3431 CG LYS B 187 7994 14551 12710 -279 -537 3128 C ATOM 3432 CD LYS B 187 29.742 -11.012 -29.571 1.00 94.47 C ANISOU 3432 CD LYS B 187 7859 14982 13054 -173 -322 3225 C ATOM 3433 CE LYS B 187 30.012 -12.485 -29.828 1.00 96.19 C ANISOU 3433 CE LYS B 187 7965 15193 13389 201 -157 3217 C ATOM 3434 NZ LYS B 187 31.204 -12.690 -30.698 1.00 98.09 N ANISOU 3434 NZ LYS B 187 7852 15664 13754 333 77 3306 N ATOM 3435 N LYS B 188 24.445 -12.777 -29.269 1.00 73.18 N ANISOU 3435 N LYS B 188 6558 11345 9901 76 -313 2585 N ATOM 3436 CA LYS B 188 23.195 -13.206 -29.888 1.00 72.24 C ANISOU 3436 CA LYS B 188 6723 11040 9686 146 -193 2412 C ATOM 3437 C LYS B 188 21.995 -12.626 -29.149 1.00 70.45 C ANISOU 3437 C LYS B 188 6754 10683 9332 -18 -340 2338 C ATOM 3438 O LYS B 188 20.993 -12.253 -29.763 1.00 68.70 O ANISOU 3438 O LYS B 188 6732 10362 9008 -74 -276 2212 O ATOM 3439 CB LYS B 188 23.094 -14.734 -29.896 1.00 60.20 C ANISOU 3439 CB LYS B 188 5233 9400 8240 414 -102 2377 C ATOM 3440 CG LYS B 188 23.891 -15.425 -30.991 1.00 61.98 C ANISOU 3440 CG LYS B 188 5284 9704 8559 626 113 2377 C ATOM 3441 CD LYS B 188 23.715 -16.936 -30.914 1.00 63.83 C ANISOU 3441 CD LYS B 188 5605 9775 8871 895 186 2324 C ATOM 3442 CE LYS B 188 24.392 -17.642 -32.079 1.00 65.78 C ANISOU 3442 CE LYS B 188 5735 10074 9182 1127 431 2277 C ATOM 3443 NZ LYS B 188 25.854 -17.359 -32.133 1.00 66.92 N ANISOU 3443 NZ LYS B 188 5505 10469 9452 1180 467 2437 N ATOM 3444 N PHE B 189 22.104 -12.556 -27.826 1.00 49.18 N ANISOU 3444 N PHE B 189 4052 7998 6638 -85 -534 2420 N ATOM 3445 CA PHE B 189 21.018 -12.056 -26.993 1.00 47.92 C ANISOU 3445 CA PHE B 189 4128 7734 6348 -224 -661 2353 C ATOM 3446 C PHE B 189 20.883 -10.541 -27.096 1.00 46.02 C ANISOU 3446 C PHE B 189 3943 7526 6018 -449 -723 2318 C ATOM 3447 O PHE B 189 19.774 -10.011 -27.047 1.00 43.51 O ANISOU 3447 O PHE B 189 3844 7098 5592 -520 -725 2203 O ATOM 3448 CB PHE B 189 21.209 -12.480 -25.536 1.00 44.26 C ANISOU 3448 CB PHE B 189 3657 7279 5879 -230 -846 2452 C ATOM 3449 CG PHE B 189 20.101 -12.032 -24.627 1.00 42.01 C ANISOU 3449 CG PHE B 189 3621 6897 5443 -344 -943 2377 C ATOM 3450 CD1 PHE B 189 18.808 -12.490 -24.817 1.00 41.12 C ANISOU 3450 CD1 PHE B 189 3709 6639 5276 -277 -845 2266 C ATOM 3451 CD2 PHE B 189 20.354 -11.165 -23.577 1.00 40.68 C ANISOU 3451 CD2 PHE B 189 3486 6787 5183 -520 -1130 2413 C ATOM 3452 CE1 PHE B 189 17.788 -12.086 -23.985 1.00 38.82 C ANISOU 3452 CE1 PHE B 189 3620 6281 4849 -369 -908 2202 C ATOM 3453 CE2 PHE B 189 19.337 -10.758 -22.739 1.00 39.38 C ANISOU 3453 CE2 PHE B 189 3557 6541 4865 -603 -1194 2330 C ATOM 3454 CZ PHE B 189 18.052 -11.218 -22.944 1.00 37.51 C ANISOU 3454 CZ PHE B 189 3492 6177 4582 -520 -1071 2229 C ATOM 3455 N ILE B 190 22.011 -9.850 -27.230 1.00 55.59 N ANISOU 3455 N ILE B 190 4952 8886 7286 -559 -779 2424 N ATOM 3456 CA ILE B 190 21.996 -8.409 -27.458 1.00 54.11 C ANISOU 3456 CA ILE B 190 4817 8711 7032 -783 -839 2406 C ATOM 3457 C ILE B 190 21.301 -8.116 -28.783 1.00 52.07 C ANISOU 3457 C ILE B 190 4671 8386 6728 -764 -660 2303 C ATOM 3458 O ILE B 190 20.410 -7.259 -28.864 1.00 49.80 O ANISOU 3458 O ILE B 190 4588 7993 6342 -874 -694 2214 O ATOM 3459 CB ILE B 190 23.423 -7.828 -27.488 1.00 57.73 C ANISOU 3459 CB ILE B 190 5001 9351 7582 -917 -915 2562 C ATOM 3460 CG1 ILE B 190 24.119 -8.054 -26.144 1.00 59.02 C ANISOU 3460 CG1 ILE B 190 5050 9591 7781 -955 -1131 2674 C ATOM 3461 CG2 ILE B 190 23.393 -6.347 -27.826 1.00 56.72 C ANISOU 3461 CG2 ILE B 190 4953 9205 7392 -1163 -974 2549 C ATOM 3462 CD1 ILE B 190 23.430 -7.379 -24.978 1.00 57.82 C ANISOU 3462 CD1 ILE B 190 5141 9338 7488 -1114 -1335 2609 C ATOM 3463 N SER B 191 21.711 -8.847 -29.816 1.00 48.53 N ANISOU 3463 N SER B 191 4097 7996 6345 -610 -473 2314 N ATOM 3464 CA SER B 191 21.102 -8.727 -31.133 1.00 47.13 C ANISOU 3464 CA SER B 191 4031 7770 6106 -578 -301 2220 C ATOM 3465 C SER B 191 19.601 -8.995 -31.063 1.00 45.33 C ANISOU 3465 C SER B 191 4075 7360 5788 -523 -299 2070 C ATOM 3466 O SER B 191 18.805 -8.281 -31.674 1.00 43.35 O ANISOU 3466 O SER B 191 3981 7038 5449 -594 -274 1993 O ATOM 3467 CB SER B 191 21.766 -9.692 -32.116 1.00 54.78 C ANISOU 3467 CB SER B 191 4839 8829 7143 -390 -95 2239 C ATOM 3468 OG SER B 191 23.155 -9.431 -32.229 1.00 56.34 O ANISOU 3468 OG SER B 191 4747 9223 7435 -436 -75 2388 O ATOM 3469 N ALA B 192 19.223 -10.020 -30.306 1.00 32.79 N ANISOU 3469 N ALA B 192 2531 5702 4227 -401 -331 2045 N ATOM 3470 CA ALA B 192 17.819 -10.373 -30.131 1.00 31.55 C ANISOU 3470 CA ALA B 192 2598 5389 4001 -361 -332 1923 C ATOM 3471 C ALA B 192 17.045 -9.244 -29.454 1.00 29.00 C ANISOU 3471 C ALA B 192 2425 5010 3586 -517 -460 1881 C ATOM 3472 O ALA B 192 15.899 -8.963 -29.810 1.00 27.42 O ANISOU 3472 O ALA B 192 2389 4713 3318 -526 -435 1778 O ATOM 3473 CB ALA B 192 17.692 -11.662 -29.334 1.00 39.00 C ANISOU 3473 CB ALA B 192 3545 6276 4997 -227 -350 1939 C ATOM 3474 N ILE B 193 17.681 -8.600 -28.479 1.00 42.84 N ANISOU 3474 N ILE B 193 4120 6822 5336 -633 -604 1958 N ATOM 3475 CA ILE B 193 17.085 -7.463 -27.788 1.00 40.75 C ANISOU 3475 CA ILE B 193 4010 6494 4977 -775 -728 1909 C ATOM 3476 C ILE B 193 16.836 -6.314 -28.760 1.00 39.31 C ANISOU 3476 C ILE B 193 3898 6277 4759 -874 -700 1869 C ATOM 3477 O ILE B 193 15.749 -5.731 -28.781 1.00 37.46 O ANISOU 3477 O ILE B 193 3843 5935 4455 -891 -711 1771 O ATOM 3478 CB ILE B 193 17.977 -6.977 -26.623 1.00 57.58 C ANISOU 3478 CB ILE B 193 6076 8698 7104 -897 -905 1997 C ATOM 3479 CG1 ILE B 193 17.911 -7.963 -25.453 1.00 58.54 C ANISOU 3479 CG1 ILE B 193 6194 8830 7218 -811 -964 2032 C ATOM 3480 CG2 ILE B 193 17.559 -5.591 -26.161 1.00 55.81 C ANISOU 3480 CG2 ILE B 193 6028 8397 6780 -1055 -1025 1931 C ATOM 3481 CD1 ILE B 193 18.734 -7.550 -24.251 1.00 59.41 C ANISOU 3481 CD1 ILE B 193 6259 9016 7297 -932 -1162 2118 C ATOM 3482 N TRP B 194 17.842 -6.001 -29.574 1.00 49.92 N ANISOU 3482 N TRP B 194 5093 7719 6156 -936 -660 1958 N ATOM 3483 CA TRP B 194 17.710 -4.933 -30.565 1.00 48.91 C ANISOU 3483 CA TRP B 194 5029 7563 5991 -1042 -631 1951 C ATOM 3484 C TRP B 194 16.614 -5.213 -31.594 1.00 47.58 C ANISOU 3484 C TRP B 194 4992 7315 5772 -936 -506 1851 C ATOM 3485 O TRP B 194 15.802 -4.335 -31.911 1.00 46.01 O ANISOU 3485 O TRP B 194 4953 7017 5510 -993 -539 1797 O ATOM 3486 CB TRP B 194 19.043 -4.678 -31.272 1.00 60.04 C ANISOU 3486 CB TRP B 194 6228 9121 7465 -1126 -580 2086 C ATOM 3487 CG TRP B 194 19.936 -3.720 -30.542 1.00 61.18 C ANISOU 3487 CG TRP B 194 6305 9306 7635 -1335 -747 2182 C ATOM 3488 CD1 TRP B 194 21.027 -4.027 -29.781 1.00 63.40 C ANISOU 3488 CD1 TRP B 194 6382 9714 7995 -1382 -837 2291 C ATOM 3489 CD2 TRP B 194 19.809 -2.294 -30.502 1.00 60.68 C ANISOU 3489 CD2 TRP B 194 6389 9144 7522 -1533 -865 2179 C ATOM 3490 NE1 TRP B 194 21.589 -2.880 -29.272 1.00 64.41 N ANISOU 3490 NE1 TRP B 194 6519 9834 8119 -1617 -1011 2351 N ATOM 3491 CE2 TRP B 194 20.860 -1.802 -29.700 1.00 62.86 C ANISOU 3491 CE2 TRP B 194 6550 9488 7846 -1713 -1027 2280 C ATOM 3492 CE3 TRP B 194 18.910 -1.385 -31.069 1.00 59.01 C ANISOU 3492 CE3 TRP B 194 6401 8783 7238 -1573 -861 2105 C ATOM 3493 CZ2 TRP B 194 21.036 -0.442 -29.452 1.00 63.61 C ANISOU 3493 CZ2 TRP B 194 6766 9488 7914 -1942 -1182 2297 C ATOM 3494 CZ3 TRP B 194 19.085 -0.037 -30.821 1.00 59.67 C ANISOU 3494 CZ3 TRP B 194 6603 8768 7302 -1777 -1007 2129 C ATOM 3495 CH2 TRP B 194 20.140 0.422 -30.018 1.00 62.03 C ANISOU 3495 CH2 TRP B 194 6803 9119 7645 -1965 -1164 2219 C ATOM 3496 N LEU B 195 16.596 -6.437 -32.112 1.00 40.91 N ANISOU 3496 N LEU B 195 4086 6502 4954 -778 -376 1828 N ATOM 3497 CA LEU B 195 15.603 -6.834 -33.104 1.00 39.94 C ANISOU 3497 CA LEU B 195 4086 6310 4778 -686 -274 1730 C ATOM 3498 C LEU B 195 14.191 -6.792 -32.531 1.00 38.51 C ANISOU 3498 C LEU B 195 4075 5999 4556 -661 -344 1625 C ATOM 3499 O LEU B 195 13.256 -6.319 -33.186 1.00 37.00 O ANISOU 3499 O LEU B 195 4011 5739 4309 -667 -338 1561 O ATOM 3500 CB LEU B 195 15.920 -8.225 -33.653 1.00 35.65 C ANISOU 3500 CB LEU B 195 3460 5812 4275 -525 -133 1714 C ATOM 3501 CG LEU B 195 17.230 -8.312 -34.439 1.00 37.31 C ANISOU 3501 CG LEU B 195 3498 6166 4513 -511 -10 1800 C ATOM 3502 CD1 LEU B 195 17.582 -9.755 -34.763 1.00 39.74 C ANISOU 3502 CD1 LEU B 195 3716 6501 4883 -318 114 1780 C ATOM 3503 CD2 LEU B 195 17.143 -7.481 -35.710 1.00 36.49 C ANISOU 3503 CD2 LEU B 195 3473 6082 4309 -573 72 1789 C ATOM 3504 N ALA B 196 14.047 -7.281 -31.304 1.00 37.25 N ANISOU 3504 N ALA B 196 3911 5820 4424 -632 -408 1619 N ATOM 3505 CA ALA B 196 12.763 -7.237 -30.618 1.00 35.79 C ANISOU 3505 CA ALA B 196 3862 5538 4199 -612 -456 1533 C ATOM 3506 C ALA B 196 12.333 -5.790 -30.418 1.00 33.83 C ANISOU 3506 C ALA B 196 3724 5234 3895 -713 -548 1505 C ATOM 3507 O ALA B 196 11.149 -5.466 -30.511 1.00 32.54 O ANISOU 3507 O ALA B 196 3675 4993 3697 -685 -556 1425 O ATOM 3508 CB ALA B 196 12.843 -7.960 -29.284 1.00 21.30 C ANISOU 3508 CB ALA B 196 2001 3712 2383 -576 -499 1555 C ATOM 3509 N SER B 197 13.307 -4.925 -30.148 1.00 42.68 N ANISOU 3509 N SER B 197 4807 6392 5018 -829 -623 1575 N ATOM 3510 CA SER B 197 13.047 -3.500 -29.971 1.00 41.61 C ANISOU 3510 CA SER B 197 4796 6175 4837 -935 -722 1552 C ATOM 3511 C SER B 197 12.516 -2.877 -31.256 1.00 40.73 C ANISOU 3511 C SER B 197 4758 6009 4708 -942 -681 1539 C ATOM 3512 O SER B 197 11.588 -2.066 -31.227 1.00 39.79 O ANISOU 3512 O SER B 197 4782 5780 4555 -943 -733 1478 O ATOM 3513 CB SER B 197 14.320 -2.779 -29.529 1.00 35.68 C ANISOU 3513 CB SER B 197 3982 5471 4102 -1088 -825 1643 C ATOM 3514 OG SER B 197 14.882 -3.411 -28.394 1.00 36.57 O ANISOU 3514 OG SER B 197 4018 5651 4225 -1082 -881 1672 O ATOM 3515 N ALA B 198 13.114 -3.258 -32.382 1.00 43.72 N ANISOU 3515 N ALA B 198 5040 6468 5102 -934 -584 1598 N ATOM 3516 CA ALA B 198 12.645 -2.794 -33.684 1.00 42.91 C ANISOU 3516 CA ALA B 198 5012 6335 4956 -939 -538 1598 C ATOM 3517 C ALA B 198 11.216 -3.271 -33.939 1.00 41.87 C ANISOU 3517 C ALA B 198 4977 6134 4798 -818 -517 1493 C ATOM 3518 O ALA B 198 10.355 -2.496 -34.371 1.00 41.18 O ANISOU 3518 O ALA B 198 5005 5969 4673 -822 -557 1470 O ATOM 3519 CB ALA B 198 13.573 -3.276 -34.785 1.00 51.67 C ANISOU 3519 CB ALA B 198 5999 7568 6065 -943 -415 1675 C ATOM 3520 N LEU B 199 10.975 -4.550 -33.661 1.00 30.06 N ANISOU 3520 N LEU B 199 3427 4665 3330 -717 -465 1442 N ATOM 3521 CA LEU B 199 9.651 -5.143 -33.828 1.00 29.80 C ANISOU 3521 CA LEU B 199 3458 4577 3287 -625 -452 1351 C ATOM 3522 C LEU B 199 8.600 -4.414 -32.995 1.00 29.05 C ANISOU 3522 C LEU B 199 3449 4400 3190 -616 -536 1296 C ATOM 3523 O LEU B 199 7.468 -4.223 -33.436 1.00 28.99 O ANISOU 3523 O LEU B 199 3503 4342 3171 -570 -555 1245 O ATOM 3524 CB LEU B 199 9.677 -6.627 -33.456 1.00 49.44 C ANISOU 3524 CB LEU B 199 5875 7093 5816 -543 -385 1324 C ATOM 3525 CG LEU B 199 10.462 -7.551 -34.388 1.00 51.02 C ANISOU 3525 CG LEU B 199 6012 7352 6021 -500 -282 1344 C ATOM 3526 CD1 LEU B 199 10.490 -8.969 -33.838 1.00 52.95 C ANISOU 3526 CD1 LEU B 199 6213 7582 6322 -414 -238 1319 C ATOM 3527 CD2 LEU B 199 9.873 -7.523 -35.790 1.00 50.95 C ANISOU 3527 CD2 LEU B 199 6085 7330 5942 -490 -248 1302 C ATOM 3528 N LEU B 200 8.982 -4.008 -31.788 1.00 46.01 N ANISOU 3528 N LEU B 200 5597 6540 5344 -652 -586 1304 N ATOM 3529 CA LEU B 200 8.083 -3.264 -30.911 1.00 46.02 C ANISOU 3529 CA LEU B 200 5690 6468 5328 -626 -645 1237 C ATOM 3530 C LEU B 200 7.941 -1.814 -31.365 1.00 45.84 C ANISOU 3530 C LEU B 200 5784 6347 5286 -664 -722 1232 C ATOM 3531 O LEU B 200 6.960 -1.144 -31.037 1.00 46.58 O ANISOU 3531 O LEU B 200 5964 6361 5371 -604 -758 1164 O ATOM 3532 CB LEU B 200 8.581 -3.314 -29.465 1.00 33.11 C ANISOU 3532 CB LEU B 200 4050 4857 3675 -654 -677 1237 C ATOM 3533 CG LEU B 200 8.574 -4.686 -28.787 1.00 33.88 C ANISOU 3533 CG LEU B 200 4064 5023 3786 -601 -616 1244 C ATOM 3534 CD1 LEU B 200 9.229 -4.610 -27.421 1.00 34.34 C ANISOU 3534 CD1 LEU B 200 4120 5120 3807 -651 -672 1276 C ATOM 3535 CD2 LEU B 200 7.154 -5.225 -28.678 1.00 34.73 C ANISOU 3535 CD2 LEU B 200 4192 5110 3893 -513 -566 1173 C ATOM 3536 N ALA B 201 8.925 -1.334 -32.120 1.00 44.12 N ANISOU 3536 N ALA B 201 5567 6133 5063 -758 -740 1312 N ATOM 3537 CA ALA B 201 8.922 0.047 -32.595 1.00 44.44 C ANISOU 3537 CA ALA B 201 5734 6062 5089 -818 -823 1335 C ATOM 3538 C ALA B 201 8.191 0.184 -33.926 1.00 44.33 C ANISOU 3538 C ALA B 201 5762 6021 5059 -768 -811 1348 C ATOM 3539 O ALA B 201 7.938 1.297 -34.390 1.00 44.95 O ANISOU 3539 O ALA B 201 5957 5994 5126 -800 -885 1380 O ATOM 3540 CB ALA B 201 10.344 0.574 -32.711 1.00 22.76 C ANISOU 3540 CB ALA B 201 2970 3335 2344 -981 -861 1438 C ATOM 3541 N ILE B 202 7.863 -0.954 -34.533 1.00 44.31 N ANISOU 3541 N ILE B 202 5681 6103 5052 -697 -733 1327 N ATOM 3542 CA ILE B 202 7.115 -0.996 -35.797 1.00 44.52 C ANISOU 3542 CA ILE B 202 5747 6123 5044 -655 -736 1332 C ATOM 3543 C ILE B 202 5.869 -0.085 -35.911 1.00 45.35 C ANISOU 3543 C ILE B 202 5952 6117 5163 -581 -831 1301 C ATOM 3544 O ILE B 202 5.724 0.611 -36.916 1.00 45.74 O ANISOU 3544 O ILE B 202 6083 6121 5173 -599 -885 1358 O ATOM 3545 CB ILE B 202 6.757 -2.456 -36.201 1.00 31.75 C ANISOU 3545 CB ILE B 202 4046 4596 3421 -593 -654 1287 C ATOM 3546 CG1 ILE B 202 8.022 -3.229 -36.578 1.00 31.74 C ANISOU 3546 CG1 ILE B 202 3973 4692 3394 -644 -556 1336 C ATOM 3547 CG2 ILE B 202 5.766 -2.476 -37.352 1.00 32.45 C ANISOU 3547 CG2 ILE B 202 4189 4671 3471 -547 -694 1270 C ATOM 3548 CD1 ILE B 202 7.755 -4.627 -37.088 1.00 32.62 C ANISOU 3548 CD1 ILE B 202 4036 4859 3499 -578 -477 1281 C ATOM 3549 N PRO B 203 4.975 -0.078 -34.895 1.00 41.94 N ANISOU 3549 N PRO B 203 5509 5645 4781 -489 -848 1218 N ATOM 3550 CA PRO B 203 3.758 0.744 -34.997 1.00 43.62 C ANISOU 3550 CA PRO B 203 5790 5759 5022 -387 -928 1187 C ATOM 3551 C PRO B 203 3.983 2.216 -35.344 1.00 44.28 C ANISOU 3551 C PRO B 203 6027 5700 5095 -425 -1026 1246 C ATOM 3552 O PRO B 203 3.095 2.837 -35.927 1.00 45.65 O ANISOU 3552 O PRO B 203 6263 5799 5282 -350 -1103 1265 O ATOM 3553 CB PRO B 203 3.154 0.638 -33.596 1.00 26.15 C ANISOU 3553 CB PRO B 203 3544 3539 2853 -297 -897 1093 C ATOM 3554 CG PRO B 203 3.572 -0.686 -33.128 1.00 25.18 C ANISOU 3554 CG PRO B 203 3306 3538 2724 -333 -803 1079 C ATOM 3555 CD PRO B 203 4.958 -0.896 -33.667 1.00 23.71 C ANISOU 3555 CD PRO B 203 3118 3392 2500 -458 -786 1155 C ATOM 3556 N MET B 204 5.145 2.761 -35.000 1.00 45.65 N ANISOU 3556 N MET B 204 6260 5832 5252 -547 -1035 1285 N ATOM 3557 CA MET B 204 5.439 4.162 -35.289 1.00 46.80 C ANISOU 3557 CA MET B 204 6568 5819 5395 -615 -1137 1350 C ATOM 3558 C MET B 204 5.600 4.426 -36.785 1.00 46.58 C ANISOU 3558 C MET B 204 6585 5796 5319 -681 -1165 1474 C ATOM 3559 O MET B 204 5.505 5.567 -37.236 1.00 48.07 O ANISOU 3559 O MET B 204 6920 5835 5508 -701 -1264 1541 O ATOM 3560 CB MET B 204 6.682 4.622 -34.525 1.00 38.89 C ANISOU 3560 CB MET B 204 5602 4786 4388 -769 -1153 1373 C ATOM 3561 CG MET B 204 6.436 4.822 -33.047 1.00 40.04 C ANISOU 3561 CG MET B 204 5790 4871 4553 -711 -1169 1252 C ATOM 3562 SD MET B 204 5.049 5.936 -32.757 1.00 43.28 S ANISOU 3562 SD MET B 204 6371 5070 5001 -530 -1248 1156 S ATOM 3563 CE MET B 204 4.902 5.841 -30.975 1.00 44.64 C ANISOU 3563 CE MET B 204 6547 5261 5153 -448 -1199 997 C ATOM 3564 N LEU B 205 5.843 3.366 -37.549 1.00 36.85 N ANISOU 3564 N LEU B 205 5242 4725 4034 -710 -1078 1505 N ATOM 3565 CA LEU B 205 5.976 3.475 -38.997 1.00 36.96 C ANISOU 3565 CA LEU B 205 5304 4773 3965 -764 -1085 1611 C ATOM 3566 C LEU B 205 4.616 3.659 -39.662 1.00 37.97 C ANISOU 3566 C LEU B 205 5485 4851 4089 -634 -1175 1596 C ATOM 3567 O LEU B 205 4.524 4.163 -40.781 1.00 38.65 O ANISOU 3567 O LEU B 205 5668 4913 4102 -666 -1235 1695 O ATOM 3568 CB LEU B 205 6.667 2.233 -39.564 1.00 32.82 C ANISOU 3568 CB LEU B 205 4661 4435 3374 -811 -953 1619 C ATOM 3569 CG LEU B 205 8.116 2.006 -39.132 1.00 32.72 C ANISOU 3569 CG LEU B 205 4566 4502 3363 -939 -863 1671 C ATOM 3570 CD1 LEU B 205 8.639 0.686 -39.670 1.00 32.27 C ANISOU 3570 CD1 LEU B 205 4391 4618 3252 -930 -722 1660 C ATOM 3571 CD2 LEU B 205 8.990 3.162 -39.597 1.00 34.70 C ANISOU 3571 CD2 LEU B 205 4910 4694 3582 -1097 -905 1814 C ATOM 3572 N PHE B 206 3.562 3.243 -38.966 1.00 37.27 N ANISOU 3572 N PHE B 206 5326 4759 4077 -491 -1186 1484 N ATOM 3573 CA PHE B 206 2.206 3.340 -39.494 1.00 38.69 C ANISOU 3573 CA PHE B 206 5506 4915 4278 -358 -1277 1470 C ATOM 3574 C PHE B 206 1.362 4.347 -38.714 1.00 40.85 C ANISOU 3574 C PHE B 206 5835 5033 4652 -223 -1361 1430 C ATOM 3575 O PHE B 206 0.249 4.679 -39.120 1.00 42.55 O ANISOU 3575 O PHE B 206 6071 5194 4901 -106 -1464 1452 O ATOM 3576 CB PHE B 206 1.521 1.970 -39.476 1.00 50.89 C ANISOU 3576 CB PHE B 206 6896 6603 5837 -299 -1219 1384 C ATOM 3577 CG PHE B 206 2.200 0.937 -40.331 1.00 49.66 C ANISOU 3577 CG PHE B 206 6712 6576 5580 -398 -1144 1402 C ATOM 3578 CD1 PHE B 206 1.850 0.784 -41.663 1.00 50.24 C ANISOU 3578 CD1 PHE B 206 6840 6693 5558 -414 -1205 1450 C ATOM 3579 CD2 PHE B 206 3.178 0.112 -39.801 1.00 48.36 C ANISOU 3579 CD2 PHE B 206 6477 6487 5410 -463 -1015 1369 C ATOM 3580 CE1 PHE B 206 2.468 -0.165 -42.450 1.00 49.79 C ANISOU 3580 CE1 PHE B 206 6782 6748 5390 -490 -1122 1446 C ATOM 3581 CE2 PHE B 206 3.799 -0.841 -40.584 1.00 47.94 C ANISOU 3581 CE2 PHE B 206 6405 6541 5271 -524 -932 1374 C ATOM 3582 CZ PHE B 206 3.443 -0.979 -41.911 1.00 48.78 C ANISOU 3582 CZ PHE B 206 6580 6683 5270 -535 -977 1403 C ATOM 3583 N THR B 207 1.893 4.828 -37.594 1.00 50.57 N ANISOU 3583 N THR B 207 7093 6194 5927 -231 -1321 1368 N ATOM 3584 CA THR B 207 1.168 5.771 -36.748 1.00 53.31 C ANISOU 3584 CA THR B 207 7514 6385 6356 -88 -1376 1302 C ATOM 3585 C THR B 207 1.479 7.215 -37.130 1.00 54.80 C ANISOU 3585 C THR B 207 7915 6359 6548 -122 -1497 1387 C ATOM 3586 O THR B 207 0.587 8.061 -37.182 1.00 57.54 O ANISOU 3586 O THR B 207 8345 6557 6960 33 -1587 1376 O ATOM 3587 CB THR B 207 1.510 5.572 -35.258 1.00 36.03 C ANISOU 3587 CB THR B 207 5299 4204 4186 -83 -1289 1185 C ATOM 3588 OG1 THR B 207 1.345 4.194 -34.904 1.00 34.78 O ANISOU 3588 OG1 THR B 207 4958 4237 4018 -85 -1177 1135 O ATOM 3589 CG2 THR B 207 0.611 6.434 -34.382 1.00 39.62 C ANISOU 3589 CG2 THR B 207 5818 4526 4710 105 -1314 1084 C ATOM 3590 N MET B 208 2.751 7.491 -37.398 1.00 37.64 N ANISOU 3590 N MET B 208 5824 4168 4311 -324 -1499 1482 N ATOM 3591 CA MET B 208 3.192 8.847 -37.704 1.00 39.29 C ANISOU 3591 CA MET B 208 6244 4162 4522 -405 -1612 1581 C ATOM 3592 C MET B 208 3.286 9.087 -39.207 1.00 40.36 C ANISOU 3592 C MET B 208 6442 4304 4589 -476 -1677 1750 C ATOM 3593 O MET B 208 3.598 8.175 -39.973 1.00 39.66 O ANISOU 3593 O MET B 208 6245 4409 4416 -543 -1606 1797 O ATOM 3594 CB MET B 208 4.544 9.125 -37.043 1.00 40.10 C ANISOU 3594 CB MET B 208 6400 4231 4605 -612 -1588 1597 C ATOM 3595 CG MET B 208 4.558 8.878 -35.541 1.00 40.21 C ANISOU 3595 CG MET B 208 6389 4232 4656 -561 -1544 1438 C ATOM 3596 SD MET B 208 3.379 9.916 -34.656 1.00 44.40 S ANISOU 3596 SD MET B 208 7094 4508 5268 -331 -1631 1310 S ATOM 3597 CE MET B 208 4.007 11.544 -35.055 1.00 44.56 C ANISOU 3597 CE MET B 208 6957 4686 5286 -199 -1496 1121 C ATOM 3598 N GLY B 209 3.016 10.320 -39.624 1.00 61.91 N ANISOU 3598 N GLY B 209 9365 6811 7345 -456 -1813 1840 N ATOM 3599 CA GLY B 209 3.105 10.678 -41.028 1.00 62.01 C ANISOU 3599 CA GLY B 209 9473 6811 7277 -530 -1891 2022 C ATOM 3600 C GLY B 209 2.993 12.172 -41.261 1.00 64.92 C ANISOU 3600 C GLY B 209 10087 6883 7694 -519 -2052 2128 C ATOM 3601 O GLY B 209 3.012 12.962 -40.319 1.00 67.08 O ANISOU 3601 O GLY B 209 10472 6946 8066 -463 -2100 2046 O ATOM 3602 N LEU B 210 2.876 12.560 -42.525 1.00 47.01 N ANISOU 3602 N LEU B 210 7924 4589 5346 -572 -2140 2311 N ATOM 3603 CA LEU B 210 2.763 13.968 -42.884 1.00 50.93 C ANISOU 3603 CA LEU B 210 8675 4792 5885 -568 -2309 2446 C ATOM 3604 C LEU B 210 1.312 14.374 -43.106 1.00 52.37 C ANISOU 3604 C LEU B 210 8888 4859 6151 -280 -2449 2431 C ATOM 3605 O LEU B 210 0.520 13.605 -43.653 1.00 51.65 O ANISOU 3605 O LEU B 210 8650 4954 6020 -164 -2452 2421 O ATOM 3606 CB LEU B 210 3.577 14.265 -44.144 1.00 54.02 C ANISOU 3606 CB LEU B 210 9185 5206 6134 -805 -2333 2688 C ATOM 3607 CG LEU B 210 5.090 14.062 -44.057 1.00 53.71 C ANISOU 3607 CG LEU B 210 9113 5268 6026 -1102 -2203 2747 C ATOM 3608 CD1 LEU B 210 5.765 14.532 -45.334 1.00 57.71 C ANISOU 3608 CD1 LEU B 210 9768 5756 6403 -1323 -2236 3010 C ATOM 3609 CD2 LEU B 210 5.659 14.786 -42.846 1.00 53.31 C ANISOU 3609 CD2 LEU B 210 9131 5020 6104 -1167 -2222 2653 C ATOM 3610 N GLN B 211 0.967 15.582 -42.672 1.00 66.04 N ANISOU 3610 N GLN B 211 10811 6276 8006 -163 -2571 2424 N ATOM 3611 CA GLN B 211 -0.360 16.136 -42.926 1.00 68.46 C ANISOU 3611 CA GLN B 211 11167 6430 8414 125 -2721 2438 C ATOM 3612 C GLN B 211 -0.289 17.627 -43.227 1.00 71.08 C ANISOU 3612 C GLN B 211 11818 6396 8793 95 -2891 2593 C ATOM 3613 O GLN B 211 0.482 18.357 -42.607 1.00 71.69 O ANISOU 3613 O GLN B 211 12062 6305 8873 -104 -2880 2609 O ATOM 3614 CB GLN B 211 -1.299 15.890 -41.742 1.00 79.67 C ANISOU 3614 CB GLN B 211 12455 7838 9978 402 -2663 2203 C ATOM 3615 CG GLN B 211 -1.865 14.483 -41.669 1.00 77.53 C ANISOU 3615 CG GLN B 211 11869 7910 9681 467 -2530 2081 C ATOM 3616 CD GLN B 211 -2.973 14.355 -40.641 1.00 79.62 C ANISOU 3616 CD GLN B 211 11990 8174 10090 775 -2497 1904 C ATOM 3617 OE1 GLN B 211 -3.442 13.253 -40.351 1.00 79.01 O ANISOU 3617 OE1 GLN B 211 11665 8328 10027 884 -2455 1855 O ATOM 3618 NE2 GLN B 211 -3.400 15.485 -40.085 1.00 82.32 N ANISOU 3618 NE2 GLN B 211 12488 8254 10537 912 -2513 1805 N ATOM 3619 N ASN B 212 -1.097 18.074 -44.183 1.00 65.54 N ANISOU 3619 N ASN B 212 11204 5564 8136 283 -3063 2715 N ATOM 3620 CA ASN B 212 -1.162 19.490 -44.517 1.00 70.68 C ANISOU 3620 CA ASN B 212 12177 5861 8818 240 -3242 2906 C ATOM 3621 C ASN B 212 -2.268 20.182 -43.727 1.00 73.25 C ANISOU 3621 C ASN B 212 12652 5833 9345 543 -3353 2802 C ATOM 3622 O ASN B 212 -3.426 20.203 -44.146 1.00 76.41 O ANISOU 3622 O ASN B 212 13342 5886 9806 469 -3439 2848 O ATOM 3623 CB ASN B 212 -1.378 19.682 -46.019 1.00 73.84 C ANISOU 3623 CB ASN B 212 12627 6330 9100 208 -3381 3165 C ATOM 3624 CG ASN B 212 -0.839 21.007 -46.517 1.00 79.23 C ANISOU 3624 CG ASN B 212 13652 6691 9762 60 -3543 3417 C ATOM 3625 OD1 ASN B 212 -1.483 22.045 -46.375 1.00 80.51 O ANISOU 3625 OD1 ASN B 212 13893 6944 9752 -236 -3523 3615 O ATOM 3626 ND2 ASN B 212 0.353 20.979 -47.103 1.00 82.85 N ANISOU 3626 ND2 ASN B 212 14317 6768 10392 271 -3700 3419 N ATOM 3627 N LEU B 213 -1.903 20.750 -42.582 1.00 72.51 N ANISOU 3627 N LEU B 213 12363 5828 9360 879 -3345 2662 N ATOM 3628 CA LEU B 213 -2.875 21.366 -41.685 1.00 75.31 C ANISOU 3628 CA LEU B 213 12827 5879 9910 1222 -3425 2551 C ATOM 3629 C LEU B 213 -3.166 22.822 -42.037 1.00 81.56 C ANISOU 3629 C LEU B 213 13941 6286 10762 1278 -3660 2768 C ATOM 3630 O LEU B 213 -3.399 23.648 -41.156 1.00 84.43 O ANISOU 3630 O LEU B 213 14274 6671 11135 1419 -3813 2942 O ATOM 3631 CB LEU B 213 -2.401 21.264 -40.234 1.00 73.05 C ANISOU 3631 CB LEU B 213 12627 5450 9679 1210 -3295 2307 C ATOM 3632 CG LEU B 213 -2.186 19.848 -39.699 1.00 67.10 C ANISOU 3632 CG LEU B 213 11604 5032 8859 1126 -3065 2100 C ATOM 3633 CD1 LEU B 213 -1.787 19.881 -38.233 1.00 66.38 C ANISOU 3633 CD1 LEU B 213 11628 4760 8835 1210 -2976 1853 C ATOM 3634 CD2 LEU B 213 -3.435 19.003 -39.900 1.00 64.71 C ANISOU 3634 CD2 LEU B 213 10948 5062 8577 1340 -2994 2042 C ATOM 3635 N SER B 214 -3.151 23.132 -43.329 1.00 87.70 N ANISOU 3635 N SER B 214 15037 6704 11582 1160 -3703 2760 N ATOM 3636 CA SER B 214 -3.502 24.467 -43.791 1.00 94.06 C ANISOU 3636 CA SER B 214 16204 7080 12452 1173 -3927 2966 C ATOM 3637 C SER B 214 -5.017 24.604 -43.874 1.00 98.57 C ANISOU 3637 C SER B 214 16829 7416 13207 1623 -4089 2979 C ATOM 3638 O SER B 214 -5.746 23.632 -43.676 1.00103.60 O ANISOU 3638 O SER B 214 17790 7604 13970 1741 -4228 3006 O ATOM 3639 CB SER B 214 -2.873 24.742 -45.157 1.00 92.16 C ANISOU 3639 CB SER B 214 16047 6928 12042 850 -4018 3290 C ATOM 3640 OG SER B 214 -1.463 24.620 -45.105 1.00 87.55 O ANISOU 3640 OG SER B 214 15289 6693 11284 509 -3837 3275 O ATOM 3641 N GLY B 215 -5.486 25.814 -44.162 1.00 93.25 N ANISOU 3641 N GLY B 215 15837 7035 12557 1872 -4079 2963 N ATOM 3642 CA GLY B 215 -6.910 26.067 -44.289 1.00 97.82 C ANISOU 3642 CA GLY B 215 16404 7449 13315 2302 -4239 3006 C ATOM 3643 C GLY B 215 -7.520 25.287 -45.437 1.00 98.86 C ANISOU 3643 C GLY B 215 16354 7840 13369 2318 -4380 3244 C ATOM 3644 O GLY B 215 -8.578 24.675 -45.293 1.00 98.84 O ANISOU 3644 O GLY B 215 16060 8036 13459 2615 -4401 3197 O ATOM 3645 N ASP B 216 -6.843 25.308 -46.581 1.00101.84 N ANISOU 3645 N ASP B 216 16904 8224 13566 1984 -4478 3504 N ATOM 3646 CA ASP B 216 -7.294 24.573 -47.755 1.00102.77 C ANISOU 3646 CA ASP B 216 16889 8613 13546 1932 -4606 3731 C ATOM 3647 C ASP B 216 -6.570 23.235 -47.862 1.00 97.03 C ANISOU 3647 C ASP B 216 15934 8336 12598 1615 -4417 3676 C ATOM 3648 O ASP B 216 -7.046 22.309 -48.518 1.00 96.36 O ANISOU 3648 O ASP B 216 15647 8567 12401 1605 -4465 3756 O ATOM 3649 CB ASP B 216 -7.071 25.401 -49.023 1.00115.02 C ANISOU 3649 CB ASP B 216 18795 9893 15014 1789 -4839 4073 C ATOM 3650 CG ASP B 216 -5.630 25.847 -49.182 1.00115.24 C ANISOU 3650 CG ASP B 216 19133 9704 14948 1411 -4769 4138 C ATOM 3651 OD1 ASP B 216 -4.910 25.917 -48.165 1.00110.51 O ANISOU 3651 OD1 ASP B 216 18422 9322 14244 1144 -4545 3992 O ATOM 3652 OD2 ASP B 216 -5.217 26.134 -50.325 1.00119.12 O ANISOU 3652 OD2 ASP B 216 19908 9876 15475 1358 -4876 4289 O ATOM 3653 N GLY B 217 -5.416 23.143 -47.209 1.00 91.54 N ANISOU 3653 N GLY B 217 15280 7657 11843 1359 -4213 3537 N ATOM 3654 CA GLY B 217 -4.637 21.918 -47.197 1.00 86.29 C ANISOU 3654 CA GLY B 217 14408 7386 10991 1076 -4015 3468 C ATOM 3655 C GLY B 217 -3.756 21.763 -48.421 1.00 87.67 C ANISOU 3655 C GLY B 217 14749 7629 10930 704 -4036 3715 C ATOM 3656 O GLY B 217 -3.462 20.644 -48.844 1.00 84.17 O ANISOU 3656 O GLY B 217 14153 7515 10311 475 -3881 3689 O ATOM 3657 N THR B 218 -3.331 22.888 -48.991 1.00 93.16 N ANISOU 3657 N THR B 218 15763 8011 11621 651 -4220 3961 N ATOM 3658 CA THR B 218 -2.505 22.869 -50.195 1.00 95.53 C ANISOU 3658 CA THR B 218 16235 8373 11687 314 -4253 4238 C ATOM 3659 C THR B 218 -1.177 23.595 -49.999 1.00 96.53 C ANISOU 3659 C THR B 218 16598 8288 11789 -14 -4176 4310 C ATOM 3660 O THR B 218 -0.223 23.367 -50.743 1.00 96.64 O ANISOU 3660 O THR B 218 16650 8470 11597 -350 -4086 4465 O ATOM 3661 CB THR B 218 -3.238 23.494 -51.396 1.00101.73 C ANISOU 3661 CB THR B 218 17221 8993 12440 429 -4531 4532 C ATOM 3662 OG1 THR B 218 -3.451 24.889 -51.151 1.00105.81 O ANISOU 3662 OG1 THR B 218 17995 9046 13162 577 -4670 4575 O ATOM 3663 CG2 THR B 218 -4.577 22.811 -51.622 1.00101.37 C ANISOU 3663 CG2 THR B 218 16925 9166 12425 738 -4639 4481 C ATOM 3664 N HIS B 219 -1.118 24.463 -48.994 1.00 97.61 N ANISOU 3664 N HIS B 219 16890 8062 12134 83 -4210 4195 N ATOM 3665 CA HIS B 219 0.087 25.243 -48.728 1.00 99.89 C ANISOU 3665 CA HIS B 219 17447 8080 12428 -228 -4200 4289 C ATOM 3666 C HIS B 219 1.199 24.366 -48.161 1.00 94.98 C ANISOU 3666 C HIS B 219 16648 7716 11723 -522 -3952 4141 C ATOM 3667 O HIS B 219 0.987 23.640 -47.190 1.00 90.32 O ANISOU 3667 O HIS B 219 15852 7250 11217 -393 -3818 3853 O ATOM 3668 CB HIS B 219 -0.219 26.394 -47.769 1.00103.14 C ANISOU 3668 CB HIS B 219 18110 7994 13083 -23 -4335 4192 C ATOM 3669 CG HIS B 219 0.789 27.500 -47.812 1.00107.13 C ANISOU 3669 CG HIS B 219 18947 8152 13606 -334 -4398 4339 C ATOM 3670 ND1 HIS B 219 0.550 28.701 -48.445 1.00111.30 N ANISOU 3670 ND1 HIS B 219 19727 8287 14272 -220 -4539 4380 N ATOM 3671 CD2 HIS B 219 2.041 27.586 -47.304 1.00106.45 C ANISOU 3671 CD2 HIS B 219 18895 8128 13423 -760 -4284 4399 C ATOM 3672 CE1 HIS B 219 1.610 29.480 -48.322 1.00113.04 C ANISOU 3672 CE1 HIS B 219 20138 8335 14477 -574 -4522 4460 C ATOM 3673 NE2 HIS B 219 2.529 28.827 -47.636 1.00110.17 N ANISOU 3673 NE2 HIS B 219 19633 8251 13975 -908 -4368 4474 N ATOM 3674 N PRO B 220 2.393 24.434 -48.773 1.00 96.35 N ANISOU 3674 N PRO B 220 16895 7984 11731 -915 -3889 4353 N ATOM 3675 CA PRO B 220 3.565 23.635 -48.391 1.00 92.69 C ANISOU 3675 CA PRO B 220 16257 7784 11178 -1225 -3663 4274 C ATOM 3676 C PRO B 220 4.038 23.914 -46.967 1.00 90.56 C ANISOU 3676 C PRO B 220 15987 7343 11076 -1242 -3610 4029 C ATOM 3677 O PRO B 220 4.719 23.078 -46.372 1.00 85.82 O ANISOU 3677 O PRO B 220 15142 7020 10446 -1324 -3422 3850 O ATOM 3678 CB PRO B 220 4.637 24.087 -49.390 1.00 97.31 C ANISOU 3678 CB PRO B 220 17036 8312 11626 -1616 -3682 4603 C ATOM 3679 CG PRO B 220 3.871 24.609 -50.562 1.00102.08 C ANISOU 3679 CG PRO B 220 17845 8771 12169 -1508 -3873 4850 C ATOM 3680 CD PRO B 220 2.662 25.264 -49.961 1.00101.66 C ANISOU 3680 CD PRO B 220 17776 8595 12257 -1059 -4023 4708 C ATOM 3681 N GLY B 221 3.685 25.079 -46.434 1.00 94.35 N ANISOU 3681 N GLY B 221 16759 7365 11723 -1165 -3780 4021 N ATOM 3682 CA GLY B 221 4.069 25.448 -45.085 1.00 93.24 C ANISOU 3682 CA GLY B 221 16682 7021 11723 -1192 -3759 3790 C ATOM 3683 C GLY B 221 3.269 24.709 -44.029 1.00 87.97 C ANISOU 3683 C GLY B 221 15784 6510 11131 -875 -3647 3446 C ATOM 3684 O GLY B 221 3.696 24.598 -42.880 1.00 85.19 O ANISOU 3684 O GLY B 221 15366 6189 10814 -956 -3550 3239 O ATOM 3685 N GLY B 222 2.104 24.199 -44.421 1.00 86.92 N ANISOU 3685 N GLY B 222 15524 6484 11020 -523 -3667 3397 N ATOM 3686 CA GLY B 222 1.237 23.483 -43.504 1.00 82.36 C ANISOU 3686 CA GLY B 222 14706 6076 10513 -218 -3554 3099 C ATOM 3687 C GLY B 222 1.582 22.011 -43.400 1.00 76.51 C ANISOU 3687 C GLY B 222 13616 5806 9649 -338 -3336 2996 C ATOM 3688 O GLY B 222 0.943 21.265 -42.658 1.00 72.50 O ANISOU 3688 O GLY B 222 12911 5447 9187 -158 -3218 2748 O ATOM 3689 N LEU B 223 2.598 21.593 -44.148 1.00 90.26 N ANISOU 3689 N LEU B 223 15287 7779 11229 -634 -3275 3189 N ATOM 3690 CA LEU B 223 3.045 20.206 -44.130 1.00 85.71 C ANISOU 3690 CA LEU B 223 14398 7634 10533 -746 -3070 3106 C ATOM 3691 C LEU B 223 3.811 19.910 -42.846 1.00 83.60 C ANISOU 3691 C LEU B 223 14056 7399 10310 -875 -2947 2912 C ATOM 3692 O LEU B 223 4.948 20.348 -42.679 1.00 84.85 O ANISOU 3692 O LEU B 223 14343 7434 10463 -1161 -2963 2993 O ATOM 3693 CB LEU B 223 3.930 19.913 -45.342 1.00 72.85 C ANISOU 3693 CB LEU B 223 12748 6216 8718 -1036 -3020 3355 C ATOM 3694 CG LEU B 223 4.364 18.457 -45.507 1.00 68.59 C ANISOU 3694 CG LEU B 223 11901 6119 8041 -1112 -2813 3287 C ATOM 3695 CD1 LEU B 223 3.149 17.568 -45.715 1.00 65.92 C ANISOU 3695 CD1 LEU B 223 11376 5961 7709 -807 -2805 3147 C ATOM 3696 CD2 LEU B 223 5.347 18.310 -46.658 1.00 70.81 C ANISOU 3696 CD2 LEU B 223 12199 6579 8125 -1385 -2755 3535 C ATOM 3697 N VAL B 224 3.184 19.165 -41.941 1.00 67.81 N ANISOU 3697 N VAL B 224 11843 5571 8350 -674 -2836 2668 N ATOM 3698 CA VAL B 224 3.795 18.870 -40.649 1.00 65.14 C ANISOU 3698 CA VAL B 224 11440 5266 8045 -757 -2735 2471 C ATOM 3699 C VAL B 224 3.842 17.374 -40.350 1.00 60.33 C ANISOU 3699 C VAL B 224 10501 5052 7371 -729 -2545 2339 C ATOM 3700 O VAL B 224 3.081 16.588 -40.921 1.00 58.79 O ANISOU 3700 O VAL B 224 10134 5062 7140 -567 -2499 2334 O ATOM 3701 CB VAL B 224 3.053 19.583 -39.499 1.00 63.64 C ANISOU 3701 CB VAL B 224 11406 4783 7991 -512 -2804 2261 C ATOM 3702 CG1 VAL B 224 3.072 21.094 -39.702 1.00 69.13 C ANISOU 3702 CG1 VAL B 224 12467 5036 8763 -568 -2995 2368 C ATOM 3703 CG2 VAL B 224 1.625 19.071 -39.387 1.00 62.29 C ANISOU 3703 CG2 VAL B 224 11100 4688 7881 -125 -2784 2145 C ATOM 3704 N CYS B 225 4.744 16.994 -39.449 1.00 75.38 N ANISOU 3704 N CYS B 225 12327 7050 9263 -895 -2451 2238 N ATOM 3705 CA CYS B 225 4.852 15.617 -38.983 1.00 72.57 C ANISOU 3705 CA CYS B 225 11684 7029 8862 -865 -2279 2106 C ATOM 3706 C CYS B 225 3.957 15.418 -37.764 1.00 73.71 C ANISOU 3706 C CYS B 225 11788 7136 9082 -596 -2248 1863 C ATOM 3707 O CYS B 225 4.159 16.043 -36.723 1.00 76.16 O ANISOU 3707 O CYS B 225 12257 7237 9445 -585 -2296 1743 O ATOM 3708 CB CYS B 225 6.304 15.284 -38.638 1.00 68.90 C ANISOU 3708 CB CYS B 225 11139 6690 8349 -1163 -2204 2133 C ATOM 3709 SG CYS B 225 6.569 13.595 -38.052 1.00 65.08 S ANISOU 3709 SG CYS B 225 10318 6597 7813 -1139 -2003 2001 S ATOM 3710 N THR B 226 2.970 14.539 -37.902 1.00 46.57 N ANISOU 3710 N THR B 226 8144 3909 5640 -390 -2163 1789 N ATOM 3711 CA THR B 226 1.936 14.368 -36.889 1.00 44.85 C ANISOU 3711 CA THR B 226 7867 3677 5495 -114 -2120 1584 C ATOM 3712 C THR B 226 1.396 12.937 -36.933 1.00 41.69 C ANISOU 3712 C THR B 226 7173 3602 5068 -15 -1988 1526 C ATOM 3713 O THR B 226 1.586 12.231 -37.929 1.00 41.43 O ANISOU 3713 O THR B 226 7023 3749 4969 -102 -1969 1643 O ATOM 3714 CB THR B 226 0.781 15.372 -37.133 1.00 55.83 C ANISOU 3714 CB THR B 226 9419 4807 6987 143 -2248 1587 C ATOM 3715 OG1 THR B 226 -0.103 15.401 -36.005 1.00 58.16 O ANISOU 3715 OG1 THR B 226 9684 5060 7354 408 -2189 1377 O ATOM 3716 CG2 THR B 226 -0.004 14.999 -38.384 1.00 56.04 C ANISOU 3716 CG2 THR B 226 9335 4949 7010 246 -2299 1726 C ATOM 3717 N PRO B 227 0.750 12.485 -35.842 1.00 59.25 N ANISOU 3717 N PRO B 227 9287 5899 7329 153 -1893 1342 N ATOM 3718 CA PRO B 227 0.031 11.210 -35.919 1.00 57.65 C ANISOU 3718 CA PRO B 227 8814 5968 7122 262 -1785 1294 C ATOM 3719 C PRO B 227 -1.066 11.275 -36.978 1.00 58.54 C ANISOU 3719 C PRO B 227 8864 6093 7287 435 -1868 1373 C ATOM 3720 O PRO B 227 -1.914 12.168 -36.935 1.00 61.65 O ANISOU 3720 O PRO B 227 9351 6303 7772 642 -1953 1354 O ATOM 3721 CB PRO B 227 -0.590 11.078 -34.528 1.00 51.45 C ANISOU 3721 CB PRO B 227 7976 5196 6374 426 -1684 1098 C ATOM 3722 CG PRO B 227 0.334 11.827 -33.639 1.00 54.62 C ANISOU 3722 CG PRO B 227 8647 5300 6804 466 -1760 1030 C ATOM 3723 CD PRO B 227 0.827 12.989 -34.458 1.00 53.33 C ANISOU 3723 CD PRO B 227 8654 5009 6598 203 -1866 1175 C ATOM 3724 N ILE B 228 -1.040 10.339 -37.921 1.00 61.66 N ANISOU 3724 N ILE B 228 9108 6699 7623 355 -1853 1459 N ATOM 3725 CA ILE B 228 -2.001 10.326 -39.018 1.00 62.24 C ANISOU 3725 CA ILE B 228 9123 6807 7719 475 -1960 1553 C ATOM 3726 C ILE B 228 -3.103 9.297 -38.798 1.00 62.48 C ANISOU 3726 C ILE B 228 8893 7040 7808 632 -1900 1462 C ATOM 3727 O ILE B 228 -3.772 8.879 -39.743 1.00 62.57 O ANISOU 3727 O ILE B 228 8807 7139 7829 698 -1989 1534 O ATOM 3728 CB ILE B 228 -1.313 10.035 -40.362 1.00 44.43 C ANISOU 3728 CB ILE B 228 6902 4646 5334 275 -2006 1714 C ATOM 3729 CG1 ILE B 228 -0.475 8.758 -40.259 1.00 41.57 C ANISOU 3729 CG1 ILE B 228 6394 4519 4881 107 -1854 1667 C ATOM 3730 CG2 ILE B 228 -0.451 11.214 -40.783 1.00 46.77 C ANISOU 3730 CG2 ILE B 228 7450 4736 5586 127 -2088 1848 C ATOM 3731 CD1 ILE B 228 0.226 8.374 -41.545 1.00 42.45 C ANISOU 3731 CD1 ILE B 228 6540 4741 4848 -76 -1861 1801 C ATOM 3732 N VAL B 229 -3.287 8.888 -37.549 1.00 54.34 N ANISOU 3732 N VAL B 229 7751 6086 6809 676 -1757 1314 N ATOM 3733 CA VAL B 229 -4.307 7.904 -37.217 1.00 54.87 C ANISOU 3733 CA VAL B 229 7564 6349 6937 799 -1681 1236 C ATOM 3734 C VAL B 229 -5.298 8.492 -36.211 1.00 58.78 C ANISOU 3734 C VAL B 229 8018 6763 7554 1063 -1650 1132 C ATOM 3735 O VAL B 229 -5.008 9.498 -35.559 1.00 60.86 O ANISOU 3735 O VAL B 229 8474 6812 7838 1141 -1665 1084 O ATOM 3736 CB VAL B 229 -3.675 6.609 -36.660 1.00 51.16 C ANISOU 3736 CB VAL B 229 6971 6063 6404 655 -1521 1161 C ATOM 3737 CG1 VAL B 229 -3.405 6.740 -35.164 1.00 47.59 C ANISOU 3737 CG1 VAL B 229 6541 5702 5839 428 -1530 1250 C ATOM 3738 CG2 VAL B 229 -4.554 5.406 -36.969 1.00 51.95 C ANISOU 3738 CG2 VAL B 229 7178 6076 6487 637 -1423 1056 C ATOM 3739 N ASP B 230 -6.468 7.869 -36.096 1.00 51.79 N ANISOU 3739 N ASP B 230 6883 6048 6748 1200 -1604 1095 N ATOM 3740 CA ASP B 230 -7.516 8.356 -35.202 1.00 55.47 C ANISOU 3740 CA ASP B 230 7261 6481 7333 1473 -1545 1000 C ATOM 3741 C ASP B 230 -7.088 8.351 -33.733 1.00 56.82 C ANISOU 3741 C ASP B 230 7497 6633 7461 1485 -1369 846 C ATOM 3742 O ASP B 230 -6.127 7.677 -33.356 1.00 54.80 O ANISOU 3742 O ASP B 230 7286 6437 7097 1276 -1294 823 O ATOM 3743 CB ASP B 230 -8.807 7.552 -35.388 1.00 85.27 C ANISOU 3743 CB ASP B 230 10711 10481 11204 1581 -1530 1016 C ATOM 3744 CG ASP B 230 -8.580 6.055 -35.312 1.00 83.12 C ANISOU 3744 CG ASP B 230 10266 10443 10871 1385 -1420 999 C ATOM 3745 OD1 ASP B 230 -8.316 5.442 -36.368 1.00 80.29 O ANISOU 3745 OD1 ASP B 230 9895 10160 10452 1203 -1506 1085 O ATOM 3746 OD2 ASP B 230 -8.670 5.493 -34.199 1.00 84.39 O ANISOU 3746 OD2 ASP B 230 10321 10706 11037 1415 -1246 899 O ATOM 3747 N THR B 231 -7.818 9.103 -32.915 1.00 75.32 N ANISOU 3747 N THR B 231 9844 8894 9880 1740 -1305 741 N ATOM 3748 CA THR B 231 -7.470 9.306 -31.510 1.00 77.23 C ANISOU 3748 CA THR B 231 10199 9089 10057 1778 -1150 582 C ATOM 3749 C THR B 231 -7.409 8.004 -30.713 1.00 76.30 C ANISOU 3749 C THR B 231 9898 9228 9867 1656 -976 534 C ATOM 3750 O THR B 231 -6.517 7.818 -29.886 1.00 76.12 O ANISOU 3750 O THR B 231 10004 9193 9726 1520 -902 465 O ATOM 3751 CB THR B 231 -8.457 10.273 -30.825 1.00 85.18 C ANISOU 3751 CB THR B 231 11222 9986 11156 2117 -1089 466 C ATOM 3752 OG1 THR B 231 -8.556 11.480 -31.591 1.00 86.24 O ANISOU 3752 OG1 THR B 231 11547 9851 11370 2242 -1265 521 O ATOM 3753 CG2 THR B 231 -7.992 10.611 -29.417 1.00 86.79 C ANISOU 3753 CG2 THR B 231 11600 10123 11254 2146 -939 287 C ATOM 3754 N ALA B 232 -8.358 7.108 -30.964 1.00 76.77 N ANISOU 3754 N ALA B 232 9657 9512 9997 1694 -928 581 N ATOM 3755 CA ALA B 232 -8.407 5.831 -30.259 1.00 75.87 C ANISOU 3755 CA ALA B 232 9361 9633 9832 1580 -769 555 C ATOM 3756 C ALA B 232 -7.157 4.993 -30.521 1.00 72.95 C ANISOU 3756 C ALA B 232 9074 9294 9348 1286 -793 606 C ATOM 3757 O ALA B 232 -6.526 4.493 -29.587 1.00 72.76 O ANISOU 3757 O ALA B 232 9095 9323 9226 1187 -679 548 O ATOM 3758 CB ALA B 232 -9.659 5.057 -30.647 1.00 29.79 C ANISOU 3758 CB ALA B 232 3193 4012 4114 1641 -751 621 C ATOM 3759 N THR B 233 -6.807 4.851 -31.796 1.00 43.76 N ANISOU 3759 N THR B 233 5400 5569 5659 1158 -941 717 N ATOM 3760 CA THR B 233 -5.633 4.086 -32.199 1.00 40.11 C ANISOU 3760 CA THR B 233 4998 5144 5100 904 -957 770 C ATOM 3761 C THR B 233 -4.361 4.687 -31.607 1.00 39.37 C ANISOU 3761 C THR B 233 5150 4898 4910 809 -962 734 C ATOM 3762 O THR B 233 -3.470 3.961 -31.158 1.00 36.90 O ANISOU 3762 O THR B 233 4858 4646 4516 639 -909 737 O ATOM 3763 CB THR B 233 -5.502 4.020 -33.735 1.00 36.77 C ANISOU 3763 CB THR B 233 4564 4723 4684 807 -1105 889 C ATOM 3764 OG1 THR B 233 -6.765 3.665 -34.314 1.00 38.21 O ANISOU 3764 OG1 THR B 233 4882 4732 4904 915 -1242 934 O ATOM 3765 CG2 THR B 233 -4.449 2.997 -34.140 1.00 34.96 C ANISOU 3765 CG2 THR B 233 4085 4672 4525 824 -1113 924 C ATOM 3766 N LEU B 234 -4.288 6.015 -31.604 1.00 48.44 N ANISOU 3766 N LEU B 234 6483 5842 6078 917 -1036 707 N ATOM 3767 CA LEU B 234 -3.147 6.720 -31.030 1.00 47.79 C ANISOU 3767 CA LEU B 234 6645 5595 5916 818 -1062 668 C ATOM 3768 C LEU B 234 -3.026 6.429 -29.539 1.00 49.23 C ANISOU 3768 C LEU B 234 6842 5835 6026 834 -925 540 C ATOM 3769 O LEU B 234 -1.935 6.132 -29.042 1.00 46.82 O ANISOU 3769 O LEU B 234 6622 5539 5629 659 -915 533 O ATOM 3770 CB LEU B 234 -3.265 8.227 -31.265 1.00 41.98 C ANISOU 3770 CB LEU B 234 6122 4600 5230 942 -1179 658 C ATOM 3771 CG LEU B 234 -2.100 9.061 -30.724 1.00 41.80 C ANISOU 3771 CG LEU B 234 6374 4372 5137 828 -1232 612 C ATOM 3772 CD1 LEU B 234 -0.791 8.626 -31.367 1.00 37.60 C ANISOU 3772 CD1 LEU B 234 5876 3872 4539 540 -1291 731 C ATOM 3773 CD2 LEU B 234 -2.339 10.548 -30.938 1.00 44.91 C ANISOU 3773 CD2 LEU B 234 6991 4477 5595 973 -1350 596 C ATOM 3774 N LYS B 235 -4.154 6.517 -28.835 1.00 52.83 N ANISOU 3774 N LYS B 235 7206 6346 6520 1047 -818 447 N ATOM 3775 CA LYS B 235 -4.214 6.155 -27.424 1.00 53.89 C ANISOU 3775 CA LYS B 235 7340 6572 6564 1078 -664 331 C ATOM 3776 C LYS B 235 -3.677 4.745 -27.237 1.00 50.80 C ANISOU 3776 C LYS B 235 6806 6385 6113 884 -596 392 C ATOM 3777 O LYS B 235 -2.898 4.483 -26.324 1.00 49.63 O ANISOU 3777 O LYS B 235 6744 6263 5850 779 -549 350 O ATOM 3778 CB LYS B 235 -5.652 6.216 -26.900 1.00 51.72 C ANISOU 3778 CB LYS B 235 6924 6379 6348 1340 -530 249 C ATOM 3779 CG LYS B 235 -6.215 7.610 -26.693 1.00 54.61 C ANISOU 3779 CG LYS B 235 7456 6531 6760 1583 -561 149 C ATOM 3780 CD LYS B 235 -7.582 7.533 -26.024 1.00 56.81 C ANISOU 3780 CD LYS B 235 7555 6933 7098 1857 -393 68 C ATOM 3781 CE LYS B 235 -8.219 8.906 -25.862 1.00 59.47 C ANISOU 3781 CE LYS B 235 8062 7043 7489 2139 -412 -44 C ATOM 3782 NZ LYS B 235 -9.557 8.819 -25.208 1.00 61.33 N ANISOU 3782 NZ LYS B 235 8091 7421 7790 2432 -225 -122 N ATOM 3783 N VAL B 236 -4.092 3.842 -28.120 1.00 52.01 N ANISOU 3783 N VAL B 236 6751 6669 6341 838 -606 493 N ATOM 3784 CA VAL B 236 -3.672 2.448 -28.043 1.00 49.11 C ANISOU 3784 CA VAL B 236 6255 6469 5936 668 -549 554 C ATOM 3785 C VAL B 236 -2.157 2.278 -28.182 1.00 45.10 C ANISOU 3785 C VAL B 236 5877 5909 5349 464 -617 600 C ATOM 3786 O VAL B 236 -1.517 1.693 -27.310 1.00 43.43 O ANISOU 3786 O VAL B 236 5678 5766 5055 370 -555 588 O ATOM 3787 CB VAL B 236 -4.404 1.580 -29.087 1.00 33.42 C ANISOU 3787 CB VAL B 236 4055 4597 4045 649 -575 642 C ATOM 3788 CG1 VAL B 236 -3.751 0.217 -29.198 1.00 30.01 C ANISOU 3788 CG1 VAL B 236 3551 4275 3576 461 -546 704 C ATOM 3789 CG2 VAL B 236 -5.874 1.442 -28.720 1.00 36.08 C ANISOU 3789 CG2 VAL B 236 4195 5048 4466 816 -484 614 C ATOM 3790 N VAL B 237 -1.582 2.799 -29.263 1.00 55.12 N ANISOU 3790 N VAL B 237 7236 7067 6643 397 -743 664 N ATOM 3791 CA VAL B 237 -0.148 2.639 -29.500 1.00 51.04 C ANISOU 3791 CA VAL B 237 6805 6524 6066 203 -798 725 C ATOM 3792 C VAL B 237 0.700 3.332 -28.427 1.00 51.19 C ANISOU 3792 C VAL B 237 6998 6449 6003 152 -813 661 C ATOM 3793 O VAL B 237 1.741 2.808 -28.009 1.00 48.40 O ANISOU 3793 O VAL B 237 6649 6153 5591 6 -810 690 O ATOM 3794 CB VAL B 237 0.267 3.089 -30.930 1.00 37.13 C ANISOU 3794 CB VAL B 237 5098 4678 4333 133 -914 822 C ATOM 3795 CG1 VAL B 237 -0.646 2.449 -31.970 1.00 36.81 C ANISOU 3795 CG1 VAL B 237 4903 4741 4343 160 -915 878 C ATOM 3796 CG2 VAL B 237 0.238 4.601 -31.069 1.00 39.52 C ANISOU 3796 CG2 VAL B 237 5575 4778 4662 218 -1012 803 C ATOM 3797 N ILE B 238 0.240 4.494 -27.966 1.00 53.94 N ANISOU 3797 N ILE B 238 7491 6654 6351 279 -837 569 N ATOM 3798 CA ILE B 238 0.953 5.243 -26.937 1.00 54.74 C ANISOU 3798 CA ILE B 238 7794 6643 6363 232 -870 485 C ATOM 3799 C ILE B 238 0.920 4.497 -25.607 1.00 54.75 C ANISOU 3799 C ILE B 238 7749 6789 6264 236 -754 416 C ATOM 3800 O ILE B 238 1.932 4.409 -24.909 1.00 52.87 O ANISOU 3800 O ILE B 238 7596 6558 5934 96 -791 412 O ATOM 3801 CB ILE B 238 0.374 6.665 -26.757 1.00 60.03 C ANISOU 3801 CB ILE B 238 8661 7094 7052 390 -920 383 C ATOM 3802 CG1 ILE B 238 0.713 7.537 -27.967 1.00 59.56 C ANISOU 3802 CG1 ILE B 238 8710 6855 7067 329 -1069 475 C ATOM 3803 CG2 ILE B 238 0.915 7.314 -25.493 1.00 61.22 C ANISOU 3803 CG2 ILE B 238 9030 7145 7087 364 -933 255 C ATOM 3804 CD1 ILE B 238 0.290 8.980 -27.815 1.00 61.07 C ANISOU 3804 CD1 ILE B 238 9114 6792 7297 491 -1138 390 C ATOM 3805 N GLN B 239 -0.247 3.958 -25.265 1.00 54.33 N ANISOU 3805 N GLN B 239 7555 6860 6229 387 -621 378 N ATOM 3806 CA GLN B 239 -0.392 3.152 -24.059 1.00 54.52 C ANISOU 3806 CA GLN B 239 7517 7044 6155 384 -494 342 C ATOM 3807 C GLN B 239 0.503 1.923 -24.124 1.00 50.52 C ANISOU 3807 C GLN B 239 6906 6661 5626 196 -506 455 C ATOM 3808 O GLN B 239 1.154 1.573 -23.142 1.00 49.37 O ANISOU 3808 O GLN B 239 6823 6565 5368 108 -500 446 O ATOM 3809 CB GLN B 239 -1.846 2.721 -23.863 1.00 36.97 C ANISOU 3809 CB GLN B 239 5117 4951 3980 556 -343 317 C ATOM 3810 CG GLN B 239 -2.758 3.806 -23.319 1.00 41.66 C ANISOU 3810 CG GLN B 239 5803 5463 4562 781 -279 180 C ATOM 3811 CD GLN B 239 -4.222 3.425 -23.415 1.00 44.36 C ANISOU 3811 CD GLN B 239 5914 5948 4994 953 -140 184 C ATOM 3812 OE1 GLN B 239 -4.569 2.244 -23.429 1.00 43.23 O ANISOU 3812 OE1 GLN B 239 5565 5986 4874 882 -62 267 O ATOM 3813 NE2 GLN B 239 -5.089 4.426 -23.494 1.00 47.16 N ANISOU 3813 NE2 GLN B 239 6292 6215 5411 1179 -115 99 N ATOM 3814 N VAL B 240 0.531 1.273 -25.284 1.00 35.36 N ANISOU 3814 N VAL B 240 4838 4788 3809 144 -528 559 N ATOM 3815 CA VAL B 240 1.377 0.100 -25.478 1.00 31.70 C ANISOU 3815 CA VAL B 240 4279 4422 3343 -6 -534 660 C ATOM 3816 C VAL B 240 2.849 0.443 -25.258 1.00 29.33 C ANISOU 3816 C VAL B 240 4096 4065 2984 -152 -637 690 C ATOM 3817 O VAL B 240 3.573 -0.293 -24.581 1.00 27.87 O ANISOU 3817 O VAL B 240 3884 3963 2742 -242 -629 731 O ATOM 3818 CB VAL B 240 1.175 -0.529 -26.874 1.00 37.98 C ANISOU 3818 CB VAL B 240 4940 5246 4245 -29 -552 744 C ATOM 3819 CG1 VAL B 240 2.252 -1.568 -27.156 1.00 34.88 C ANISOU 3819 CG1 VAL B 240 4482 4922 3849 -165 -559 833 C ATOM 3820 CG2 VAL B 240 -0.208 -1.155 -26.972 1.00 40.36 C ANISOU 3820 CG2 VAL B 240 5092 5635 4610 76 -466 732 C ATOM 3821 N ASN B 241 3.282 1.571 -25.812 1.00 41.36 N ANISOU 3821 N ASN B 241 5744 5444 4527 -182 -742 681 N ATOM 3822 CA ASN B 241 4.655 2.021 -25.609 1.00 39.84 C ANISOU 3822 CA ASN B 241 5650 5197 4292 -344 -851 717 C ATOM 3823 C ASN B 241 4.959 2.352 -24.147 1.00 41.29 C ANISOU 3823 C ASN B 241 5973 5365 4352 -367 -875 631 C ATOM 3824 O ASN B 241 6.034 2.034 -23.641 1.00 39.97 O ANISOU 3824 O ASN B 241 5808 5249 4132 -506 -938 679 O ATOM 3825 CB ASN B 241 4.968 3.228 -26.495 1.00 50.43 C ANISOU 3825 CB ASN B 241 7107 6373 5683 -389 -960 738 C ATOM 3826 CG ASN B 241 6.392 3.725 -26.320 1.00 49.51 C ANISOU 3826 CG ASN B 241 7071 6205 5536 -586 -1079 791 C ATOM 3827 OD1 ASN B 241 6.652 4.645 -25.543 1.00 51.43 O ANISOU 3827 OD1 ASN B 241 7501 6315 5727 -627 -1169 719 O ATOM 3828 ND2 ASN B 241 7.325 3.110 -27.040 1.00 47.11 N ANISOU 3828 ND2 ASN B 241 6625 6008 5268 -710 -1082 915 N ATOM 3829 N THR B 242 4.005 2.989 -23.476 1.00 69.51 N ANISOU 3829 N THR B 242 9661 8877 7874 -221 -824 502 N ATOM 3830 CA THR B 242 4.172 3.380 -22.080 1.00 71.27 C ANISOU 3830 CA THR B 242 10057 9076 7948 -223 -837 393 C ATOM 3831 C THR B 242 4.279 2.158 -21.173 1.00 70.33 C ANISOU 3831 C THR B 242 9843 9147 7733 -255 -758 429 C ATOM 3832 O THR B 242 5.084 2.132 -20.242 1.00 70.07 O ANISOU 3832 O THR B 242 9910 9137 7578 -362 -832 419 O ATOM 3833 CB THR B 242 3.005 4.268 -21.608 1.00 74.22 C ANISOU 3833 CB THR B 242 10565 9352 8285 -19 -762 235 C ATOM 3834 OG1 THR B 242 2.883 5.401 -22.478 1.00 75.43 O ANISOU 3834 OG1 THR B 242 10793 9317 8549 35 -837 223 O ATOM 3835 CG2 THR B 242 3.237 4.750 -20.185 1.00 75.93 C ANISOU 3835 CG2 THR B 242 11020 9508 8323 -29 -793 99 C ATOM 3836 N PHE B 243 3.467 1.144 -21.454 1.00 56.91 N ANISOU 3836 N PHE B 243 7955 7578 6089 -174 -625 481 N ATOM 3837 CA PHE B 243 3.484 -0.087 -20.673 1.00 56.22 C ANISOU 3837 CA PHE B 243 7777 7656 5927 -206 -547 539 C ATOM 3838 C PHE B 243 4.733 -0.922 -20.946 1.00 53.10 C ANISOU 3838 C PHE B 243 7289 7317 5569 -362 -637 677 C ATOM 3839 O PHE B 243 5.377 -1.408 -20.017 1.00 52.76 O ANISOU 3839 O PHE B 243 7289 7335 5420 -448 -688 710 O ATOM 3840 CB PHE B 243 2.235 -0.930 -20.952 1.00 65.63 C ANISOU 3840 CB PHE B 243 8796 8954 7184 -94 -387 563 C ATOM 3841 CG PHE B 243 0.994 -0.434 -20.261 1.00 69.32 C ANISOU 3841 CG PHE B 243 9315 9438 7586 70 -258 443 C ATOM 3842 CD1 PHE B 243 0.956 -0.312 -18.883 1.00 70.80 C ANISOU 3842 CD1 PHE B 243 9634 9681 7586 90 -197 371 C ATOM 3843 CD2 PHE B 243 -0.144 -0.120 -20.987 1.00 71.42 C ANISOU 3843 CD2 PHE B 243 9489 9677 7971 211 -194 407 C ATOM 3844 CE1 PHE B 243 -0.183 0.132 -18.244 1.00 73.94 C ANISOU 3844 CE1 PHE B 243 10071 10108 7912 259 -48 254 C ATOM 3845 CE2 PHE B 243 -1.287 0.325 -20.352 1.00 74.90 C ANISOU 3845 CE2 PHE B 243 9944 10147 8365 384 -60 301 C ATOM 3846 CZ PHE B 243 -1.306 0.451 -18.979 1.00 75.95 C ANISOU 3846 CZ PHE B 243 10210 10339 8309 413 27 220 C ATOM 3847 N MET B 244 5.075 -1.083 -22.221 1.00 41.63 N ANISOU 3847 N MET B 244 5709 5848 4262 -389 -655 756 N ATOM 3848 CA MET B 244 6.150 -1.995 -22.610 1.00 39.41 C ANISOU 3848 CA MET B 244 5308 5632 4034 -497 -702 884 C ATOM 3849 C MET B 244 7.558 -1.420 -22.455 1.00 38.67 C ANISOU 3849 C MET B 244 5276 5503 3913 -638 -851 922 C ATOM 3850 O MET B 244 8.508 -2.161 -22.202 1.00 37.98 O ANISOU 3850 O MET B 244 5105 5498 3826 -718 -897 1019 O ATOM 3851 CB MET B 244 5.942 -2.500 -24.042 1.00 67.75 C ANISOU 3851 CB MET B 244 8761 9218 7763 -475 -662 942 C ATOM 3852 CG MET B 244 4.767 -3.452 -24.197 1.00 68.54 C ANISOU 3852 CG MET B 244 8758 9377 7906 -381 -541 939 C ATOM 3853 SD MET B 244 4.850 -4.855 -23.066 1.00 69.07 S ANISOU 3853 SD MET B 244 8770 9561 7912 -397 -472 1003 S ATOM 3854 CE MET B 244 3.521 -4.455 -21.932 1.00 71.58 C ANISOU 3854 CE MET B 244 9152 9912 8132 -296 -365 904 C ATOM 3855 N SER B 245 7.696 -0.108 -22.607 1.00 67.15 N ANISOU 3855 N SER B 245 9021 8982 7508 -671 -935 854 N ATOM 3856 CA SER B 245 9.015 0.514 -22.558 1.00 66.86 C ANISOU 3856 CA SER B 245 9032 8905 7464 -837 -1089 901 C ATOM 3857 C SER B 245 9.327 1.160 -21.211 1.00 68.49 C ANISOU 3857 C SER B 245 9426 9074 7522 -902 -1194 819 C ATOM 3858 O SER B 245 10.476 1.507 -20.937 1.00 68.66 O ANISOU 3858 O SER B 245 9476 9085 7526 -1065 -1344 866 O ATOM 3859 CB SER B 245 9.165 1.549 -23.676 1.00 64.00 C ANISOU 3859 CB SER B 245 8712 8414 7192 -883 -1142 911 C ATOM 3860 OG SER B 245 8.250 2.619 -23.507 1.00 64.32 O ANISOU 3860 OG SER B 245 8796 8412 7230 -1069 -1293 964 O ATOM 3861 N PHE B 246 8.310 1.321 -20.370 1.00 55.90 N ANISOU 3861 N PHE B 246 7958 7466 5813 -781 -1116 696 N ATOM 3862 CA PHE B 246 8.498 2.014 -19.098 1.00 57.77 C ANISOU 3862 CA PHE B 246 8417 7657 5876 -828 -1207 589 C ATOM 3863 C PHE B 246 7.998 1.222 -17.889 1.00 58.63 C ANISOU 3863 C PHE B 246 8550 7900 5825 -755 -1113 559 C ATOM 3864 O PHE B 246 8.797 0.654 -17.148 1.00 58.27 O ANISOU 3864 O PHE B 246 8490 7958 5692 -858 -1197 632 O ATOM 3865 CB PHE B 246 7.843 3.399 -19.140 1.00 51.59 C ANISOU 3865 CB PHE B 246 7858 6675 5069 -757 -1223 429 C ATOM 3866 CG PHE B 246 8.146 4.251 -17.939 1.00 53.67 C ANISOU 3866 CG PHE B 246 8392 6853 5148 -819 -1335 296 C ATOM 3867 CD1 PHE B 246 9.385 4.856 -17.796 1.00 53.63 C ANISOU 3867 CD1 PHE B 246 8472 6785 5120 -1039 -1550 331 C ATOM 3868 CD2 PHE B 246 7.189 4.455 -16.960 1.00 55.96 C ANISOU 3868 CD2 PHE B 246 8852 7132 5280 -661 -1226 134 C ATOM 3869 CE1 PHE B 246 9.665 5.643 -16.693 1.00 55.68 C ANISOU 3869 CE1 PHE B 246 9004 6954 5197 -1114 -1678 197 C ATOM 3870 CE2 PHE B 246 7.461 5.241 -15.856 1.00 57.91 C ANISOU 3870 CE2 PHE B 246 9380 7293 5329 -713 -1328 -9 C ATOM 3871 CZ PHE B 246 8.701 5.836 -15.722 1.00 57.70 C ANISOU 3871 CZ PHE B 246 9460 7187 5276 -946 -1566 18 C ATOM 3872 N LEU B 247 6.682 1.190 -17.699 1.00 51.50 N ANISOU 3872 N LEU B 247 7675 7006 4886 -579 -942 465 N ATOM 3873 CA LEU B 247 6.071 0.608 -16.501 1.00 52.87 C ANISOU 3873 CA LEU B 247 7897 7306 4884 -510 -829 430 C ATOM 3874 C LEU B 247 6.514 -0.824 -16.185 1.00 51.36 C ANISOU 3874 C LEU B 247 7541 7284 4690 -576 -815 597 C ATOM 3875 O LEU B 247 7.132 -1.075 -15.149 1.00 51.76 O ANISOU 3875 O LEU B 247 7676 7411 4582 -659 -893 628 O ATOM 3876 CB LEU B 247 4.543 0.676 -16.597 1.00 50.87 C ANISOU 3876 CB LEU B 247 7624 7065 4638 -307 -619 336 C ATOM 3877 CG LEU B 247 3.944 2.084 -16.635 1.00 53.71 C ANISOU 3877 CG LEU B 247 8197 7285 4924 -178 -587 138 C ATOM 3878 CD1 LEU B 247 2.429 2.028 -16.713 1.00 54.76 C ANISOU 3878 CD1 LEU B 247 8605 7386 4813 -243 -679 24 C ATOM 3879 CD2 LEU B 247 4.387 2.883 -15.419 1.00 53.73 C ANISOU 3879 CD2 LEU B 247 8223 7095 5096 -170 -684 111 C ATOM 3880 N PHE B 248 6.194 -1.751 -17.081 1.00 65.09 N ANISOU 3880 N PHE B 248 9062 9068 6601 -538 -729 703 N ATOM 3881 CA PHE B 248 6.498 -3.171 -16.888 1.00 64.05 C ANISOU 3881 CA PHE B 248 8781 9064 6493 -574 -700 858 C ATOM 3882 C PHE B 248 7.996 -3.488 -16.676 1.00 63.05 C ANISOU 3882 C PHE B 248 8628 8971 6358 -715 -879 975 C ATOM 3883 O PHE B 248 8.367 -4.061 -15.638 1.00 63.74 O ANISOU 3883 O PHE B 248 8757 9152 6310 -757 -918 1041 O ATOM 3884 CB PHE B 248 5.887 -3.999 -18.033 1.00 95.69 C ANISOU 3884 CB PHE B 248 12587 13073 10697 -512 -594 924 C ATOM 3885 CG PHE B 248 6.129 -5.478 -17.924 1.00 95.07 C ANISOU 3885 CG PHE B 248 12374 13083 10663 -536 -558 1073 C ATOM 3886 CD1 PHE B 248 5.390 -6.252 -17.045 1.00 96.20 C ANISOU 3886 CD1 PHE B 248 12534 13319 10697 -511 -455 1110 C ATOM 3887 CD2 PHE B 248 7.074 -6.098 -18.725 1.00 93.72 C ANISOU 3887 CD2 PHE B 248 12067 12897 10644 -577 -617 1177 C ATOM 3888 CE1 PHE B 248 5.602 -7.612 -16.953 1.00 95.93 C ANISOU 3888 CE1 PHE B 248 12397 13337 10715 -538 -433 1257 C ATOM 3889 CE2 PHE B 248 7.291 -7.459 -18.638 1.00 93.78 C ANISOU 3889 CE2 PHE B 248 11971 12955 10704 -580 -587 1304 C ATOM 3890 CZ PHE B 248 6.553 -8.216 -17.750 1.00 94.83 C ANISOU 3890 CZ PHE B 248 12136 13155 10738 -565 -504 1348 C ATOM 3891 N PRO B 249 8.864 -3.101 -17.635 1.00 56.21 N ANISOU 3891 N PRO B 249 7688 8041 5629 -789 -991 1013 N ATOM 3892 CA PRO B 249 10.272 -3.482 -17.474 1.00 55.82 C ANISOU 3892 CA PRO B 249 7558 8052 5598 -910 -1146 1144 C ATOM 3893 C PRO B 249 10.950 -2.806 -16.282 1.00 57.09 C ANISOU 3893 C PRO B 249 7890 8225 5574 -1023 -1316 1107 C ATOM 3894 O PRO B 249 11.798 -3.429 -15.642 1.00 57.48 O ANISOU 3894 O PRO B 249 7893 8372 5575 -1095 -1428 1222 O ATOM 3895 CB PRO B 249 10.910 -3.014 -18.786 1.00 32.57 C ANISOU 3895 CB PRO B 249 4498 5044 2831 -963 -1197 1177 C ATOM 3896 CG PRO B 249 10.062 -1.892 -19.231 1.00 31.32 C ANISOU 3896 CG PRO B 249 4468 4758 2675 -920 -1152 1036 C ATOM 3897 CD PRO B 249 8.664 -2.272 -18.839 1.00 30.26 C ANISOU 3897 CD PRO B 249 4386 4638 2474 -774 -987 954 C ATOM 3898 N MET B 250 10.586 -1.561 -15.987 1.00 46.55 N ANISOU 3898 N MET B 250 6763 6787 4138 -1036 -1346 947 N ATOM 3899 CA MET B 250 11.163 -0.865 -14.840 1.00 48.06 C ANISOU 3899 CA MET B 250 7161 6968 4131 -1151 -1517 882 C ATOM 3900 C MET B 250 10.613 -1.397 -13.521 1.00 49.36 C ANISOU 3900 C MET B 250 7457 7236 4062 -1097 -1456 854 C ATOM 3901 O MET B 250 11.269 -1.300 -12.486 1.00 50.39 O ANISOU 3901 O MET B 250 7703 7423 4019 -1205 -1614 872 O ATOM 3902 CB MET B 250 10.952 0.647 -14.932 1.00 56.74 C ANISOU 3902 CB MET B 250 8476 7891 5194 -1178 -1573 707 C ATOM 3903 CG MET B 250 11.833 1.337 -15.955 1.00 56.03 C ANISOU 3903 CG MET B 250 8305 7705 5281 -1312 -1709 761 C ATOM 3904 SD MET B 250 13.589 1.015 -15.702 1.00 56.05 S ANISOU 3904 SD MET B 250 8165 7826 5308 -1539 -1955 940 S ATOM 3905 CE MET B 250 13.925 -0.138 -17.033 1.00 53.99 C ANISOU 3905 CE MET B 250 7540 7665 5309 -1483 -1840 1133 C ATOM 3906 N LEU B 251 9.407 -1.955 -13.561 1.00 53.01 N ANISOU 3906 N LEU B 251 7902 7730 4512 -940 -1231 817 N ATOM 3907 CA LEU B 251 8.838 -2.599 -12.385 1.00 54.36 C ANISOU 3907 CA LEU B 251 8166 8022 4469 -891 -1136 824 C ATOM 3908 C LEU B 251 9.650 -3.855 -12.088 1.00 53.66 C ANISOU 3908 C LEU B 251 7932 8058 4400 -959 -1215 1038 C ATOM 3909 O LEU B 251 10.094 -4.078 -10.950 1.00 54.89 O ANISOU 3909 O LEU B 251 8204 8303 4348 -1027 -1314 1085 O ATOM 3910 CB LEU B 251 7.371 -2.953 -12.628 1.00 68.58 C ANISOU 3910 CB LEU B 251 9918 9841 6296 -724 -871 769 C ATOM 3911 CG LEU B 251 6.439 -2.950 -11.416 1.00 70.58 C ANISOU 3911 CG LEU B 251 10289 10218 6308 -661 -720 744 C ATOM 3912 CD1 LEU B 251 6.560 -1.641 -10.658 1.00 72.59 C ANISOU 3912 CD1 LEU B 251 10843 10459 6279 -697 -809 593 C ATOM 3913 CD2 LEU B 251 5.003 -3.178 -11.860 1.00 71.50 C ANISOU 3913 CD2 LEU B 251 10330 10345 6492 -500 -464 672 C ATOM 3914 N VAL B 252 9.851 -4.662 -13.130 1.00 44.80 N ANISOU 3914 N VAL B 252 6568 6932 3520 -935 -1179 1165 N ATOM 3915 CA VAL B 252 10.679 -5.861 -13.025 1.00 44.48 C ANISOU 3915 CA VAL B 252 6378 6980 3540 -972 -1254 1370 C ATOM 3916 C VAL B 252 12.078 -5.530 -12.505 1.00 45.34 C ANISOU 3916 C VAL B 252 6510 7128 3590 -1111 -1515 1439 C ATOM 3917 O VAL B 252 12.563 -6.145 -11.550 1.00 47.77 O ANISOU 3917 O VAL B 252 6847 7535 3769 -1153 -1616 1557 O ATOM 3918 CB VAL B 252 10.803 -6.580 -14.386 1.00 34.57 C ANISOU 3918 CB VAL B 252 4881 5688 2567 -916 -1183 1462 C ATOM 3919 CG1 VAL B 252 11.793 -7.733 -14.294 1.00 36.05 C ANISOU 3919 CG1 VAL B 252 4921 5942 2836 -939 -1285 1662 C ATOM 3920 CG2 VAL B 252 9.442 -7.072 -14.852 1.00 32.43 C ANISOU 3920 CG2 VAL B 252 4572 5398 2354 -801 -955 1426 C ATOM 3921 N ALA B 253 12.712 -4.545 -13.133 1.00 52.45 N ANISOU 3921 N ALA B 253 7395 7952 4579 -1194 -1633 1376 N ATOM 3922 CA ALA B 253 14.057 -4.123 -12.756 1.00 53.22 C ANISOU 3922 CA ALA B 253 7479 8087 4653 -1353 -1895 1445 C ATOM 3923 C ALA B 253 14.108 -3.597 -11.324 1.00 54.96 C ANISOU 3923 C ALA B 253 7965 8342 4575 -1445 -2038 1368 C ATOM 3924 O ALA B 253 15.106 -3.776 -10.628 1.00 56.82 O ANISOU 3924 O ALA B 253 8187 8665 4734 -1561 -2257 1477 O ATOM 3925 CB ALA B 253 14.576 -3.072 -13.727 1.00 42.58 C ANISOU 3925 CB ALA B 253 6069 6644 3468 -1440 -1970 1395 C ATOM 3926 N SER B 254 13.032 -2.949 -10.890 1.00 70.61 N ANISOU 3926 N SER B 254 10185 10259 6383 -1384 -1915 1179 N ATOM 3927 CA SER B 254 12.955 -2.423 -9.530 1.00 72.60 C ANISOU 3927 CA SER B 254 10733 10530 6319 -1455 -2024 1066 C ATOM 3928 C SER B 254 12.919 -3.558 -8.514 1.00 73.62 C ANISOU 3928 C SER B 254 10913 10813 6246 -1413 -1975 1172 C ATOM 3929 O SER B 254 13.680 -3.559 -7.540 1.00 75.67 O ANISOU 3929 O SER B 254 11371 11141 6239 -1505 -2130 1160 O ATOM 3930 CB SER B 254 11.722 -1.534 -9.365 1.00 54.65 C ANISOU 3930 CB SER B 254 8704 8127 3933 -1377 -1889 813 C ATOM 3931 OG SER B 254 11.740 -0.464 -10.293 1.00 52.86 O ANISOU 3931 OG SER B 254 8426 7919 3737 -1189 -1596 782 O ATOM 3932 N ILE B 255 12.028 -4.520 -8.746 1.00 57.02 N ANISOU 3932 N ILE B 255 8645 8759 4261 -1285 -1769 1280 N ATOM 3933 CA ILE B 255 11.936 -5.693 -7.880 1.00 57.92 C ANISOU 3933 CA ILE B 255 8782 9007 4217 -1259 -1727 1427 C ATOM 3934 C ILE B 255 13.278 -6.417 -7.807 1.00 58.49 C ANISOU 3934 C ILE B 255 8701 9154 4368 -1348 -1965 1653 C ATOM 3935 O ILE B 255 13.804 -6.687 -6.715 1.00 61.30 O ANISOU 3935 O ILE B 255 9177 9615 4501 -1422 -2122 1745 O ATOM 3936 CB ILE B 255 10.867 -6.681 -8.383 1.00 47.45 C ANISOU 3936 CB ILE B 255 7319 7689 3022 -1118 -1449 1487 C ATOM 3937 CG1 ILE B 255 9.490 -6.016 -8.406 1.00 46.12 C ANISOU 3937 CG1 ILE B 255 7290 7491 2742 -1018 -1209 1287 C ATOM 3938 CG2 ILE B 255 10.839 -7.927 -7.513 1.00 49.60 C ANISOU 3938 CG2 ILE B 255 7572 8076 3197 -1117 -1442 1697 C ATOM 3939 CD1 ILE B 255 8.412 -6.882 -9.019 1.00 43.49 C ANISOU 3939 CD1 ILE B 255 6794 7165 2567 -900 -950 1338 C ATOM 3940 N LEU B 256 13.832 -6.711 -8.980 1.00 66.61 N ANISOU 3940 N LEU B 256 9464 10135 5709 -1333 -1992 1744 N ATOM 3941 CA LEU B 256 15.112 -7.404 -9.078 1.00 66.85 C ANISOU 3941 CA LEU B 256 9296 10234 5868 -1381 -2194 1959 C ATOM 3942 C LEU B 256 16.223 -6.670 -8.330 1.00 68.10 C ANISOU 3942 C LEU B 256 9534 10450 5891 -1553 -2504 1967 C ATOM 3943 O LEU B 256 16.978 -7.285 -7.582 1.00 69.23 O ANISOU 3943 O LEU B 256 9627 10700 5978 -1601 -2698 2145 O ATOM 3944 CB LEU B 256 15.500 -7.622 -10.543 1.00 49.20 C ANISOU 3944 CB LEU B 256 6773 7939 3982 -1323 -2137 2016 C ATOM 3945 CG LEU B 256 14.636 -8.624 -11.313 1.00 46.15 C ANISOU 3945 CG LEU B 256 6275 7502 3758 -1167 -1883 2053 C ATOM 3946 CD1 LEU B 256 15.164 -8.831 -12.726 1.00 43.91 C ANISOU 3946 CD1 LEU B 256 5737 7165 3782 -1117 -1846 2092 C ATOM 3947 CD2 LEU B 256 14.556 -9.944 -10.570 1.00 47.97 C ANISOU 3947 CD2 LEU B 256 6506 7796 3924 -1111 -1877 2236 C ATOM 3948 N ASN B 257 16.308 -5.357 -8.520 1.00 55.92 N ANISOU 3948 N ASN B 257 8121 8828 4298 -1651 -2567 1780 N ATOM 3949 CA ASN B 257 17.315 -4.551 -7.832 1.00 59.90 C ANISOU 3949 CA ASN B 257 8725 9366 4670 -1846 -2878 1767 C ATOM 3950 C ASN B 257 17.127 -4.510 -6.317 1.00 63.84 C ANISOU 3950 C ASN B 257 9525 9944 4786 -1903 -2985 1730 C ATOM 3951 O ASN B 257 18.103 -4.443 -5.566 1.00 68.06 O ANISOU 3951 O ASN B 257 10097 10567 5199 -2052 -3279 1816 O ATOM 3952 CB ASN B 257 17.365 -3.132 -8.404 1.00 59.06 C ANISOU 3952 CB ASN B 257 8702 9118 4620 -1948 -2919 1575 C ATOM 3953 CG ASN B 257 18.120 -3.062 -9.717 1.00 57.30 C ANISOU 3953 CG ASN B 257 8166 8867 4737 -1985 -2950 1672 C ATOM 3954 OD1 ASN B 257 19.287 -2.670 -9.754 1.00 60.01 O ANISOU 3954 OD1 ASN B 257 8395 9255 5151 -2155 -3200 1758 O ATOM 3955 ND2 ASN B 257 17.459 -3.451 -10.802 1.00 53.09 N ANISOU 3955 ND2 ASN B 257 7488 8272 4410 -1833 -2696 1665 N ATOM 3956 N THR B 258 15.875 -4.547 -5.870 1.00 62.75 N ANISOU 3956 N THR B 258 9599 9789 4454 -1788 -2746 1607 N ATOM 3957 CA THR B 258 15.589 -4.620 -4.440 1.00 66.53 C ANISOU 3957 CA THR B 258 10370 10363 4544 -1818 -2789 1579 C ATOM 3958 C THR B 258 16.120 -5.932 -3.863 1.00 68.79 C ANISOU 3958 C THR B 258 10540 10799 4797 -1811 -2890 1857 C ATOM 3959 O THR B 258 16.837 -5.943 -2.849 1.00 73.42 O ANISOU 3959 O THR B 258 11255 11490 5152 -1932 -3148 1937 O ATOM 3960 CB THR B 258 14.079 -4.512 -4.156 1.00 64.80 C ANISOU 3960 CB THR B 258 10346 10117 4156 -1671 -2458 1412 C ATOM 3961 OG1 THR B 258 13.594 -3.239 -4.603 1.00 63.12 O ANISOU 3961 OG1 THR B 258 10261 9754 3969 -1655 -2378 1153 O ATOM 3962 CG2 THR B 258 13.804 -4.658 -2.665 1.00 69.13 C ANISOU 3962 CG2 THR B 258 11198 10790 4278 -1698 -2475 1396 C ATOM 3963 N VAL B 259 15.772 -7.035 -4.522 1.00 66.22 N ANISOU 3963 N VAL B 259 9983 10472 4706 -1672 -2700 2006 N ATOM 3964 CA VAL B 259 16.246 -8.350 -4.096 1.00 68.20 C ANISOU 3964 CA VAL B 259 10115 10825 4972 -1641 -2781 2284 C ATOM 3965 C VAL B 259 17.775 -8.406 -4.090 1.00 71.11 C ANISOU 3965 C VAL B 259 10308 11255 5453 -1748 -3130 2448 C ATOM 3966 O VAL B 259 18.383 -8.955 -3.168 1.00 75.30 O ANISOU 3966 O VAL B 259 10888 11901 5819 -1803 -3345 2623 O ATOM 3967 CB VAL B 259 15.687 -9.474 -4.989 1.00 64.01 C ANISOU 3967 CB VAL B 259 9354 10236 4729 -1479 -2536 2397 C ATOM 3968 CG1 VAL B 259 16.146 -10.830 -4.482 1.00 66.35 C ANISOU 3968 CG1 VAL B 259 9534 10601 5073 -1440 -2644 2689 C ATOM 3969 CG2 VAL B 259 14.170 -9.411 -5.030 1.00 61.75 C ANISOU 3969 CG2 VAL B 259 9211 9916 4335 -1389 -2207 2266 C ATOM 3970 N ILE B 260 18.387 -7.823 -5.117 1.00 86.80 N ANISOU 3970 N ILE B 260 12085 13176 7719 -1783 -3187 2399 N ATOM 3971 CA ILE B 260 19.841 -7.739 -5.211 1.00 87.68 C ANISOU 3971 CA ILE B 260 11983 13357 7973 -1895 -3500 2543 C ATOM 3972 C ILE B 260 20.423 -6.958 -4.035 1.00 89.51 C ANISOU 3972 C ILE B 260 12444 13670 7896 -2097 -3816 2501 C ATOM 3973 O ILE B 260 21.464 -7.326 -3.490 1.00 90.95 O ANISOU 3973 O ILE B 260 12523 13973 8059 -2176 -4106 2695 O ATOM 3974 CB ILE B 260 20.282 -7.089 -6.542 1.00 68.63 C ANISOU 3974 CB ILE B 260 9335 10861 5881 -1920 -3467 2471 C ATOM 3975 CG1 ILE B 260 19.978 -8.023 -7.713 1.00 64.99 C ANISOU 3975 CG1 ILE B 260 8581 10362 5749 -1732 -3249 2585 C ATOM 3976 CG2 ILE B 260 21.765 -6.765 -6.524 1.00 72.36 C ANISOU 3976 CG2 ILE B 260 9648 11417 6430 -2102 -3809 2565 C ATOM 3977 CD1 ILE B 260 20.196 -7.390 -9.068 1.00 61.72 C ANISOU 3977 CD1 ILE B 260 7984 9862 5606 -1734 -3142 2491 C ATOM 3978 N ALA B 261 19.738 -5.888 -3.641 1.00 76.71 N ANISOU 3978 N ALA B 261 11140 11977 6032 -2174 -3765 2245 N ATOM 3979 CA ALA B 261 20.159 -5.096 -2.490 1.00 81.85 C ANISOU 3979 CA ALA B 261 12073 12678 6349 -2369 -4053 2159 C ATOM 3980 C ALA B 261 20.148 -5.937 -1.216 1.00 85.97 C ANISOU 3980 C ALA B 261 12764 13349 6553 -2366 -4160 2307 C ATOM 3981 O ALA B 261 21.122 -5.941 -0.453 1.00 90.99 O ANISOU 3981 O ALA B 261 13416 14098 7059 -2515 -4510 2430 O ATOM 3982 CB ALA B 261 19.270 -3.873 -2.331 1.00 81.03 C ANISOU 3982 CB ALA B 261 12307 12439 6043 -2402 -3924 1834 C ATOM 3983 N ASN B 262 19.047 -6.652 -0.993 1.00 84.20 N ANISOU 3983 N ASN B 262 12661 13131 6203 -2206 -3866 2307 N ATOM 3984 CA ASN B 262 18.952 -7.546 0.161 1.00 88.13 C ANISOU 3984 CA ASN B 262 13335 13766 6383 -2199 -3930 2465 C ATOM 3985 C ASN B 262 20.070 -8.590 0.176 1.00 90.38 C ANISOU 3985 C ASN B 262 13345 14154 6842 -2190 -4165 2805 C ATOM 3986 O ASN B 262 20.748 -8.783 1.194 1.00 95.75 O ANISOU 3986 O ASN B 262 14133 14964 7286 -2297 -4466 2948 O ATOM 3987 CB ASN B 262 17.585 -8.232 0.203 1.00 96.57 C ANISOU 3987 CB ASN B 262 14524 14820 7347 -2034 -3538 2432 C ATOM 3988 CG ASN B 262 16.450 -7.255 0.442 1.00100.65 C ANISOU 3988 CG ASN B 262 15288 15481 7473 -2050 -3573 2570 C ATOM 3989 OD1 ASN B 262 16.626 -6.232 1.105 1.00105.75 O ANISOU 3989 OD1 ASN B 262 16095 16232 7850 -2190 -3887 2630 O ATOM 3990 ND2 ASN B 262 15.276 -7.568 -0.096 1.00 99.19 N ANISOU 3990 ND2 ASN B 262 15133 15305 7247 -1920 -3256 2631 N ATOM 3991 N LYS B 263 20.262 -9.249 -0.964 1.00 87.10 N ANISOU 3991 N LYS B 263 12579 13675 6838 -2055 -4037 2929 N ATOM 3992 CA LYS B 263 21.317 -10.246 -1.116 1.00 88.97 C ANISOU 3992 CA LYS B 263 12529 13984 7292 -1997 -4221 3242 C ATOM 3993 C LYS B 263 22.697 -9.644 -0.872 1.00 93.02 C ANISOU 3993 C LYS B 263 12894 14590 7859 -2162 -4628 3318 C ATOM 3994 O LYS B 263 23.611 -10.335 -0.427 1.00 97.15 O ANISOU 3994 O LYS B 263 13302 15229 8384 -2171 -4896 3569 O ATOM 3995 CB LYS B 263 21.265 -10.875 -2.511 1.00 87.04 C ANISOU 3995 CB LYS B 263 11960 13633 7478 -1812 -3979 3307 C ATOM 3996 CG LYS B 263 20.022 -11.706 -2.781 1.00 88.64 C ANISOU 3996 CG LYS B 263 11931 13871 7878 -1678 -4066 3622 C ATOM 3997 CD LYS B 263 19.955 -12.918 -1.868 1.00 85.91 C ANISOU 3997 CD LYS B 263 11629 13428 7584 -1507 -3751 3683 C ATOM 3998 CE LYS B 263 18.767 -13.804 -2.213 1.00 87.54 C ANISOU 3998 CE LYS B 263 12207 13676 7378 -1560 -3650 3641 C ATOM 3999 NZ LYS B 263 17.472 -13.078 -2.086 1.00 86.73 N ANISOU 3999 NZ LYS B 263 12129 13511 7313 -1428 -3432 3801 N ATOM 4000 N LEU B 264 22.841 -8.355 -1.168 1.00 91.45 N ANISOU 4000 N LEU B 264 12695 14336 7715 -2295 -4675 3106 N ATOM 4001 CA LEU B 264 24.102 -7.654 -0.957 1.00 95.55 C ANISOU 4001 CA LEU B 264 13089 14936 8277 -2499 -5060 3151 C ATOM 4002 C LEU B 264 24.340 -7.405 0.526 1.00100.09 C ANISOU 4002 C LEU B 264 13956 15579 8494 -2630 -5289 3113 C ATOM 4003 O LEU B 264 25.459 -7.562 1.016 1.00102.96 O ANISOU 4003 O LEU B 264 14157 16018 8946 -2690 -5545 3245 O ATOM 4004 CB LEU B 264 24.120 -6.330 -1.724 1.00 93.18 C ANISOU 4004 CB LEU B 264 12773 14520 8111 -2621 -5016 2910 C ATOM 4005 CG LEU B 264 25.402 -5.503 -1.596 1.00 97.05 C ANISOU 4005 CG LEU B 264 13114 15066 8695 -2869 -5383 2932 C ATOM 4006 CD1 LEU B 264 26.598 -6.276 -2.132 1.00100.47 C ANISOU 4006 CD1 LEU B 264 13919 15467 8788 -3069 -5576 2732 C ATOM 4007 CD2 LEU B 264 25.259 -4.168 -2.308 1.00 98.76 C ANISOU 4007 CD2 LEU B 264 12915 15406 9203 -2815 -5547 3215 C ATOM 4008 N THR B 265 23.285 -7.010 1.236 1.00100.50 N ANISOU 4008 N THR B 265 14432 15597 8158 -2658 -5167 2911 N ATOM 4009 CA THR B 265 23.370 -6.829 2.683 1.00104.47 C ANISOU 4009 CA THR B 265 15243 16153 8298 -2751 -5324 2844 C ATOM 4010 C THR B 265 23.752 -8.146 3.356 1.00106.41 C ANISOU 4010 C THR B 265 15400 16507 8523 -2641 -5392 3120 C ATOM 4011 O THR B 265 24.663 -8.196 4.195 1.00110.09 O ANISOU 4011 O THR B 265 15875 17048 8908 -2727 -5662 3193 O ATOM 4012 CB THR B 265 22.038 -6.328 3.270 1.00114.32 C ANISOU 4012 CB THR B 265 16956 17356 9126 -2750 -5111 2583 C ATOM 4013 OG1 THR B 265 21.687 -5.075 2.670 1.00112.83 O ANISOU 4013 OG1 THR B 265 16869 17040 8961 -2839 -5057 2320 O ATOM 4014 CG2 THR B 265 22.152 -6.150 4.777 1.00118.59 C ANISOU 4014 CG2 THR B 265 17821 17959 9280 -2843 -5273 2502 C ATOM 4015 N VAL B 266 23.056 -9.213 2.975 1.00104.11 N ANISOU 4015 N VAL B 266 15022 16214 8322 -2454 -5157 3281 N ATOM 4016 CA VAL B 266 23.373 -10.544 3.480 1.00105.87 C ANISOU 4016 CA VAL B 266 15162 16504 8560 -2335 -5208 3557 C ATOM 4017 C VAL B 266 24.821 -10.908 3.157 1.00107.31 C ANISOU 4017 C VAL B 266 14952 16729 9091 -2328 -5481 3763 C ATOM 4018 O VAL B 266 25.534 -11.457 3.997 1.00110.84 O ANISOU 4018 O VAL B 266 15398 17255 9463 -2343 -5704 3905 O ATOM 4019 CB VAL B 266 22.426 -11.610 2.894 1.00103.09 C ANISOU 4019 CB VAL B 266 14768 16106 8294 -2143 -4901 3698 C ATOM 4020 CG1 VAL B 266 22.848 -13.003 3.332 1.00104.33 C ANISOU 4020 CG1 VAL B 266 14696 16280 8662 -2001 -4991 4016 C ATOM 4021 CG2 VAL B 266 20.990 -11.329 3.308 1.00103.40 C ANISOU 4021 CG2 VAL B 266 15207 16158 7920 -2141 -4660 3581 C ATOM 4022 N MET B 267 25.256 -10.573 1.946 1.00104.84 N ANISOU 4022 N MET B 267 14306 16375 9153 -2305 -5461 3776 N ATOM 4023 CA MET B 267 26.605 -10.902 1.494 1.00106.05 C ANISOU 4023 CA MET B 267 14043 16580 9674 -2266 -5662 3977 C ATOM 4024 C MET B 267 27.701 -10.181 2.271 1.00109.59 C ANISOU 4024 C MET B 267 14447 17103 10091 -2476 -5991 3925 C ATOM 4025 O MET B 267 28.741 -10.769 2.559 1.00112.21 O ANISOU 4025 O MET B 267 14515 17516 10604 -2451 -6205 4119 O ATOM 4026 CB MET B 267 26.763 -10.629 -0.002 1.00102.55 C ANISOU 4026 CB MET B 267 13251 16083 9629 -2161 -5502 4011 C ATOM 4027 CG MET B 267 26.886 -11.885 -0.844 1.00102.91 C ANISOU 4027 CG MET B 267 13007 16162 9933 -2297 -5658 3962 C ATOM 4028 SD MET B 267 27.491 -11.527 -2.501 1.00100.45 S ANISOU 4028 SD MET B 267 12177 15846 10143 -2092 -5518 4139 S ATOM 4029 CE MET B 267 28.992 -10.630 -2.114 1.00101.25 C ANISOU 4029 CE MET B 267 12024 15999 10450 -2321 -5679 4039 C ATOM 4030 N VAL B 268 27.484 -8.911 2.601 1.00110.06 N ANISOU 4030 N VAL B 268 14765 17127 9925 -2679 -6036 3664 N ATOM 4031 CA VAL B 268 28.479 -8.176 3.377 1.00113.90 C ANISOU 4031 CA VAL B 268 15274 17667 10336 -2900 -6356 3606 C ATOM 4032 C VAL B 268 28.458 -8.627 4.836 1.00117.75 C ANISOU 4032 C VAL B 268 16041 18230 10470 -2917 -6509 3654 C ATOM 4033 O VAL B 268 29.497 -8.644 5.504 1.00121.65 O ANISOU 4033 O VAL B 268 16470 18806 10947 -3038 -6811 3724 O ATOM 4034 CB VAL B 268 28.323 -6.636 3.261 1.00113.46 C ANISOU 4034 CB VAL B 268 15425 17517 10168 -3119 -6375 3306 C ATOM 4035 CG1 VAL B 268 28.452 -6.197 1.809 1.00109.89 C ANISOU 4035 CG1 VAL B 268 14690 16996 10067 -3109 -6232 3278 C ATOM 4036 CG2 VAL B 268 27.004 -6.166 3.850 1.00113.02 C ANISOU 4036 CG2 VAL B 268 15872 17390 9681 -3125 -6205 3064 C ATOM 4037 N HIS B 269 27.280 -9.013 5.321 1.00149.39 N ANISOU 4037 N HIS B 269 20355 22217 14188 -2801 -6297 3626 N ATOM 4038 CA HIS B 269 27.179 -9.577 6.664 1.00153.25 C ANISOU 4038 CA HIS B 269 21080 22790 14357 -2782 -6408 3722 C ATOM 4039 C HIS B 269 27.896 -10.923 6.749 1.00154.56 C ANISOU 4039 C HIS B 269 20945 23018 14763 -2613 -6493 4059 C ATOM 4040 O HIS B 269 28.408 -11.297 7.804 1.00157.95 O ANISOU 4040 O HIS B 269 21497 23525 14993 -2594 -6640 4195 O ATOM 4041 CB HIS B 269 25.719 -9.708 7.098 1.00122.04 C ANISOU 4041 CB HIS B 269 17550 18811 10011 -2721 -6134 3591 C ATOM 4042 CG HIS B 269 25.135 -8.436 7.630 1.00122.71 C ANISOU 4042 CG HIS B 269 18002 18851 9772 -2879 -6101 3254 C ATOM 4043 ND1 HIS B 269 25.907 -7.341 7.946 1.00120.62 N ANISOU 4043 ND1 HIS B 269 17696 18485 9651 -2977 -6064 3041 N ATOM 4044 CD2 HIS B 269 23.855 -8.087 7.901 1.00125.53 C ANISOU 4044 CD2 HIS B 269 18785 19243 9669 -2945 -6099 3091 C ATOM 4045 CE1 HIS B 269 25.129 -6.369 8.390 1.00122.11 C ANISOU 4045 CE1 HIS B 269 18278 18629 9492 -3091 -6044 2754 C ATOM 4046 NE2 HIS B 269 23.880 -6.796 8.372 1.00125.12 N ANISOU 4046 NE2 HIS B 269 18944 19098 9498 -3068 -6058 2772 N ATOM 4047 N GLN B 270 27.932 -11.646 5.634 1.00118.64 N ANISOU 4047 N GLN B 270 16013 18429 10637 -2479 -6396 4190 N ATOM 4048 CA GLN B 270 28.695 -12.886 5.550 1.00119.86 C ANISOU 4048 CA GLN B 270 15836 18625 11083 -2306 -6494 4493 C ATOM 4049 C GLN B 270 30.180 -12.575 5.402 1.00122.30 C ANISOU 4049 C GLN B 270 15782 19017 11670 -2397 -6786 4570 C ATOM 4050 O GLN B 270 31.035 -13.337 5.851 1.00124.89 O ANISOU 4050 O GLN B 270 15869 19412 12172 -2292 -6955 4808 O ATOM 4051 CB GLN B 270 28.229 -13.730 4.362 1.00115.91 C ANISOU 4051 CB GLN B 270 15120 18029 10890 -2080 -6212 4598 C ATOM 4052 CG GLN B 270 26.823 -14.288 4.493 1.00113.71 C ANISOU 4052 CG GLN B 270 15150 17670 10385 -1982 -5916 4568 C ATOM 4053 CD GLN B 270 26.349 -14.964 3.220 1.00109.84 C ANISOU 4053 CD GLN B 270 14449 17073 10212 -1786 -5649 4650 C ATOM 4054 OE1 GLN B 270 25.192 -15.372 3.113 1.00107.76 O ANISOU 4054 OE1 GLN B 270 14384 16734 9824 -1712 -5388 4633 O ATOM 4055 NE2 GLN B 270 27.243 -15.083 2.245 1.00109.12 N ANISOU 4055 NE2 GLN B 270 13948 16980 10532 -1702 -5705 4741 N ATOM 4056 N ALA B 271 30.474 -11.446 4.767 1.00121.94 N ANISOU 4056 N ALA B 271 15696 18963 11673 -2594 -6838 4374 N ATOM 4057 CA ALA B 271 31.848 -11.045 4.493 1.00124.31 C ANISOU 4057 CA ALA B 271 15650 19345 12238 -2719 -7094 4436 C ATOM 4058 C ALA B 271 32.534 -10.527 5.748 1.00129.64 C ANISOU 4058 C ALA B 271 16413 20132 12714 -2837 -7438 4520 C ATOM 4059 O ALA B 271 33.762 -10.513 5.832 1.00132.43 O ANISOU 4059 O ALA B 271 16433 20584 13301 -2789 -7641 4735 O ATOM 4060 CB ALA B 271 31.882 -9.991 3.393 1.00122.61 C ANISOU 4060 CB ALA B 271 15452 19075 12060 -2938 -7077 4197 C ATOM 4061 N ALA B 272 31.737 -10.097 6.720 1.00131.96 N ANISOU 4061 N ALA B 272 17157 20413 12568 -2981 -7498 4347 N ATOM 4062 CA ALA B 272 32.276 -9.617 7.988 1.00137.07 C ANISOU 4062 CA ALA B 272 17960 21164 12956 -3070 -7799 4427 C ATOM 4063 C ALA B 272 32.951 -10.738 8.781 1.00137.89 C ANISOU 4063 C ALA B 272 18029 21306 13055 -2824 -7763 4690 C ATOM 4064 O ALA B 272 33.753 -10.477 9.677 1.00134.44 O ANISOU 4064 O ALA B 272 17614 20788 12677 -2627 -7472 4734 O ATOM 4065 CB ALA B 272 31.181 -8.963 8.817 1.00137.47 C ANISOU 4065 CB ALA B 272 18532 21184 12516 -3244 -7815 4166 C ATOM 4066 N PHE B 291 32.625 -11.983 8.444 1.00141.66 N ANISOU 4066 N PHE B 291 18454 21899 13472 -2842 -8066 4871 N ATOM 4067 CA PHE B 291 33.174 -13.137 9.149 1.00143.25 C ANISOU 4067 CA PHE B 291 18582 22134 13714 -2612 -8091 5156 C ATOM 4068 C PHE B 291 33.933 -14.075 8.213 1.00141.39 C ANISOU 4068 C PHE B 291 17863 21874 13987 -2380 -8003 5365 C ATOM 4069 O PHE B 291 34.227 -15.215 8.575 1.00142.56 O ANISOU 4069 O PHE B 291 17914 22018 14234 -2160 -8010 5606 O ATOM 4070 CB PHE B 291 32.061 -13.903 9.868 1.00141.89 C ANISOU 4070 CB PHE B 291 18821 21895 13198 -2504 -7847 5134 C ATOM 4071 CG PHE B 291 31.360 -13.102 10.929 1.00143.52 C ANISOU 4071 CG PHE B 291 19512 22126 12895 -2701 -7870 4901 C ATOM 4072 CD1 PHE B 291 30.313 -12.257 10.600 1.00140.10 C ANISOU 4072 CD1 PHE B 291 19335 21605 12293 -2768 -7601 4624 C ATOM 4073 CD2 PHE B 291 31.748 -13.194 12.256 1.00148.75 C ANISOU 4073 CD2 PHE B 291 20379 22900 13239 -2804 -8157 4957 C ATOM 4074 CE1 PHE B 291 29.666 -11.520 11.573 1.00141.89 C ANISOU 4074 CE1 PHE B 291 20013 21851 12050 -2922 -7603 4396 C ATOM 4075 CE2 PHE B 291 31.105 -12.459 13.234 1.00150.53 C ANISOU 4075 CE2 PHE B 291 21062 23150 12985 -2970 -8164 4731 C ATOM 4076 CZ PHE B 291 30.062 -11.620 12.891 1.00147.13 C ANISOU 4076 CZ PHE B 291 20883 22626 12395 -3021 -7879 4445 C ATOM 4077 N ASN B 292 34.244 -13.585 7.015 1.00138.75 N ANISOU 4077 N ASN B 292 17239 21515 13965 -2427 -7916 5268 N ATOM 4078 CA ASN B 292 34.979 -14.354 6.012 1.00137.34 C ANISOU 4078 CA ASN B 292 16574 21332 14276 -2224 -7831 5436 C ATOM 4079 C ASN B 292 34.291 -15.674 5.662 1.00134.46 C ANISOU 4079 C ASN B 292 16201 20852 14037 -1920 -7552 5563 C ATOM 4080 O ASN B 292 34.922 -16.731 5.655 1.00135.87 O ANISOU 4080 O ASN B 292 16101 21039 14487 -1694 -7591 5796 O ATOM 4081 CB ASN B 292 36.426 -14.596 6.466 1.00134.40 C ATOM 4082 CG ASN B 292 37.348 -14.977 5.319 1.00134.40 C ATOM 4083 OD1 ASN B 292 38.204 -14.191 4.911 1.00134.40 O ATOM 4084 ND2 ASN B 292 37.187 -16.191 4.802 1.00134.40 N ATOM 4085 N MET B 293 32.995 -15.606 5.376 1.00130.65 N ANISOU 4085 N MET B 293 16024 20253 13364 -1915 -7270 5408 N ATOM 4086 CA MET B 293 32.232 -16.794 5.011 1.00127.93 C ANISOU 4086 CA MET B 293 15708 19781 13117 -1659 -6996 5515 C ATOM 4087 C MET B 293 31.650 -16.675 3.607 1.00122.84 C ANISOU 4087 C MET B 293 14954 19036 12682 -1609 -6687 5374 C ATOM 4088 O MET B 293 30.545 -17.149 3.340 1.00119.81 O ANISOU 4088 O MET B 293 14825 18548 12151 -1566 -6429 5291 O ATOM 4089 CB MET B 293 31.117 -17.056 6.026 1.00128.32 C ANISOU 4089 CB MET B 293 16229 19785 12741 -1673 -6912 5500 C ATOM 4090 CG MET B 293 31.615 -17.462 7.405 1.00133.40 C ANISOU 4090 CG MET B 293 17069 20541 13078 -1773 -7212 5588 C ATOM 4091 SD MET B 293 30.273 -17.848 8.545 1.00133.94 S ANISOU 4091 SD MET B 293 17679 20567 12645 -1773 -7060 5584 S ATOM 4092 CE MET B 293 29.387 -16.292 8.561 1.00132.37 C ANISOU 4092 CE MET B 293 17349 20217 12729 -1457 -6849 5850 C ATOM 4093 N THR B 294 32.401 -16.038 2.714 1.00122.20 N ANISOU 4093 N THR B 294 14489 18997 12942 -1618 -6710 5357 N ATOM 4094 CA THR B 294 31.978 -15.880 1.327 1.00117.70 C ANISOU 4094 CA THR B 294 13790 18348 12581 -1577 -6435 5231 C ATOM 4095 C THR B 294 33.163 -15.591 0.407 1.00117.95 C ANISOU 4095 C THR B 294 13316 18441 13056 -1493 -6458 5315 C ATOM 4096 O THR B 294 34.302 -15.936 0.720 1.00121.38 O ANISOU 4096 O THR B 294 13483 18961 13676 -1399 -6644 5503 O ATOM 4097 CB THR B 294 30.917 -14.768 1.178 1.00 90.45 C ATOM 4098 OG1 THR B 294 30.594 -14.593 -0.207 1.00 90.45 O ATOM 4099 CG2 THR B 294 31.430 -13.453 1.748 1.00 90.45 C ATOM 4100 N ILE B 295 32.881 -14.957 -0.726 1.00115.05 N ANISOU 4100 N ILE B 295 12819 18039 12855 -1522 -6259 5179 N ATOM 4101 CA ILE B 295 33.901 -14.652 -1.725 1.00115.21 C ANISOU 4101 CA ILE B 295 12368 18132 13274 -1464 -6240 5237 C ATOM 4102 C ILE B 295 34.922 -13.622 -1.245 1.00118.59 C ANISOU 4102 C ILE B 295 12648 18707 13704 -1720 -6521 5217 C ATOM 4103 O ILE B 295 34.775 -13.033 -0.174 1.00120.22 O ANISOU 4103 O ILE B 295 13154 18934 13592 -1954 -6710 5117 O ATOM 4104 CB ILE B 295 33.261 -14.158 -3.035 1.00 94.73 C ATOM 4105 CG1 ILE B 295 32.228 -13.070 -2.739 1.00 94.73 C ATOM 4106 CG2 ILE B 295 32.610 -15.314 -3.777 1.00 94.73 C ATOM 4107 CD1 ILE B 295 31.402 -12.663 -3.938 1.00 94.73 C ATOM 4108 N GLU B 296 35.958 -13.416 -2.054 1.00220.61 N ANISOU 4108 N GLU B 296 25114 31730 26980 -1676 -6540 5312 N ATOM 4109 CA GLU B 296 37.035 -12.486 -1.730 1.00224.07 C ANISOU 4109 CA GLU B 296 25363 32311 27464 -1927 -6796 5317 C ATOM 4110 C GLU B 296 36.536 -11.043 -1.677 1.00222.54 C ANISOU 4110 C GLU B 296 25415 32076 27064 -2259 -6813 5075 C ATOM 4111 O GLU B 296 35.608 -10.682 -2.400 1.00218.50 O ANISOU 4111 O GLU B 296 25015 31463 26543 -2262 -6571 4926 O ATOM 4112 CB GLU B 296 38.175 -12.617 -2.746 1.00175.01 C ATOM 4113 CG GLU B 296 38.988 -13.900 -2.622 1.00175.01 C ATOM 4114 CD GLU B 296 38.257 -15.119 -3.155 1.00175.01 C ATOM 4115 OE1 GLU B 296 37.241 -14.946 -3.860 1.00175.01 O ATOM 4116 OE2 GLU B 296 38.701 -16.251 -2.868 1.00175.01 O ATOM 4117 N PRO B 297 37.153 -10.217 -0.813 1.00148.20 N ANISOU 4117 N PRO B 297 16092 22730 17487 -2534 -7107 5038 N ATOM 4118 CA PRO B 297 36.778 -8.810 -0.622 1.00147.03 C ANISOU 4118 CA PRO B 297 16267 22513 17085 -2855 -7172 4797 C ATOM 4119 C PRO B 297 36.703 -8.011 -1.922 1.00143.55 C ANISOU 4119 C PRO B 297 15682 22028 16833 -2972 -6993 4675 C ATOM 4120 O PRO B 297 35.781 -7.213 -2.087 1.00140.18 O ANISOU 4120 O PRO B 297 15572 21468 16220 -3070 -6863 4462 O ATOM 4121 CB PRO B 297 37.907 -8.272 0.259 1.00100.74 C ATOM 4122 CG PRO B 297 38.351 -9.450 1.042 1.00100.74 C ATOM 4123 CD PRO B 297 38.233 -10.622 0.106 1.00100.74 C ATOM 4124 N GLY B 298 37.657 -8.221 -2.825 1.00147.48 N ANISOU 4124 N GLY B 298 15705 22639 17691 -2960 -6984 4811 N ATOM 4125 CA GLY B 298 37.685 -7.503 -4.088 1.00144.68 C ANISOU 4125 CA GLY B 298 15184 22262 17527 -3081 -6818 4724 C ATOM 4126 C GLY B 298 36.460 -7.774 -4.940 1.00138.71 C ANISOU 4126 C GLY B 298 14571 21375 16758 -2923 -6487 4603 C ATOM 4127 O GLY B 298 35.864 -6.854 -5.508 1.00136.27 O ANISOU 4127 O GLY B 298 14420 20967 16387 -3094 -6393 4426 O ATOM 4128 N ARG B 299 36.085 -9.047 -5.023 1.00113.73 N ANISOU 4128 N ARG B 299 11361 18199 13653 -2596 -6322 4702 N ATOM 4129 CA ARG B 299 34.899 -9.460 -5.761 1.00109.07 C ANISOU 4129 CA ARG B 299 10915 17486 13041 -2424 -6019 4607 C ATOM 4130 C ARG B 299 33.645 -8.840 -5.151 1.00107.15 C ANISOU 4130 C ARG B 299 11208 17101 12402 -2549 -6023 4395 C ATOM 4131 O ARG B 299 32.713 -8.471 -5.866 1.00103.55 O ANISOU 4131 O ARG B 299 10912 16540 11891 -2541 -5815 4248 O ATOM 4132 CB ARG B 299 34.786 -10.986 -5.763 1.00156.61 C ANISOU 4132 CB ARG B 299 16782 23508 19216 -2050 -5862 4773 C ATOM 4133 CG ARG B 299 33.571 -11.529 -6.494 1.00155.37 C ANISOU 4133 CG ARG B 299 16744 23225 19064 -1873 -5551 4688 C ATOM 4134 CD ARG B 299 33.707 -11.410 -8.001 1.00155.39 C ANISOU 4134 CD ARG B 299 16448 23234 19359 -1516 -5359 4854 C ATOM 4135 NE ARG B 299 32.514 -11.906 -8.681 1.00153.17 N ANISOU 4135 NE ARG B 299 16386 22807 19004 -1338 -5116 4793 N ATOM 4136 CZ ARG B 299 32.294 -13.185 -8.967 1.00152.11 C ANISOU 4136 CZ ARG B 299 16051 22632 19112 -1093 -4858 4830 C ATOM 4137 NH1 ARG B 299 33.188 -14.106 -8.635 1.00150.23 N ANISOU 4137 NH1 ARG B 299 16076 22222 18785 -957 -4618 4733 N ATOM 4138 NH2 ARG B 299 31.177 -13.545 -9.585 1.00153.09 N ANISOU 4138 NH2 ARG B 299 15746 22860 19564 -981 -4783 4920 N ATOM 4139 N VAL B 300 33.634 -8.728 -3.826 1.00128.03 N ANISOU 4139 N VAL B 300 14130 19751 14765 -2651 -6251 4378 N ATOM 4140 CA VAL B 300 32.521 -8.110 -3.114 1.00126.77 C ANISOU 4140 CA VAL B 300 14480 19474 14213 -2776 -6250 4163 C ATOM 4141 C VAL B 300 32.431 -6.624 -3.449 1.00125.91 C ANISOU 4141 C VAL B 300 14476 19298 14069 -3058 -6281 3956 C ATOM 4142 O VAL B 300 31.341 -6.088 -3.649 1.00123.47 O ANISOU 4142 O VAL B 300 14428 18865 13623 -3084 -6112 3767 O ATOM 4143 CB VAL B 300 32.657 -8.287 -1.587 1.00112.09 C ANISOU 4143 CB VAL B 300 12891 17651 12049 -2850 -6499 4180 C ATOM 4144 CG1 VAL B 300 31.500 -7.615 -0.863 1.00112.04 C ANISOU 4144 CG1 VAL B 300 13398 17538 11633 -3062 -6543 3911 C ATOM 4145 CG2 VAL B 300 32.725 -9.761 -1.227 1.00112.00 C ANISOU 4145 CG2 VAL B 300 12896 17655 12005 -2570 -6425 4354 C ATOM 4146 N GLN B 301 33.585 -5.965 -3.514 1.00111.12 N ANISOU 4146 N GLN B 301 12369 17500 12350 -3260 -6483 4008 N ATOM 4147 CA GLN B 301 33.640 -4.548 -3.856 1.00111.30 C ANISOU 4147 CA GLN B 301 12501 17439 12350 -3555 -6543 3830 C ATOM 4148 C GLN B 301 33.147 -4.303 -5.278 1.00107.50 C ANISOU 4148 C GLN B 301 11875 16892 12076 -3513 -6273 3773 C ATOM 4149 O GLN B 301 32.353 -3.393 -5.520 1.00105.80 O ANISOU 4149 O GLN B 301 11945 16528 11725 -3659 -6214 3559 O ATOM 4150 CB GLN B 301 35.062 -4.006 -3.691 1.00142.10 C ANISOU 4150 CB GLN B 301 16155 21446 16390 -3782 -6822 3935 C ATOM 4151 CG GLN B 301 35.578 -4.025 -2.260 1.00146.12 C ANISOU 4151 CG GLN B 301 16942 21974 16601 -3898 -7113 3910 C ATOM 4152 CD GLN B 301 34.810 -3.089 -1.346 1.00149.92 C ANISOU 4152 CD GLN B 301 17075 22643 17242 -3838 -7317 4166 C ATOM 4153 OE1 GLN B 301 34.218 -2.108 -1.795 1.00151.33 O ANISOU 4153 OE1 GLN B 301 16801 22938 17757 -3842 -7327 4332 O ATOM 4154 NE2 GLN B 301 34.817 -3.390 -0.052 1.00151.74 N ANISOU 4154 NE2 GLN B 301 17516 22909 17227 -3766 -7466 4206 N ATOM 4155 N ALA B 302 33.623 -5.119 -6.215 1.00106.33 N ANISOU 4155 N ALA B 302 11298 16849 12252 -3306 -6110 3958 N ATOM 4156 CA ALA B 302 33.208 -5.010 -7.610 1.00102.84 C ANISOU 4156 CA ALA B 302 10704 16367 12006 -3232 -5839 3924 C ATOM 4157 C ALA B 302 31.709 -5.255 -7.756 1.00 98.95 C ANISOU 4157 C ALA B 302 10566 15735 11294 -3097 -5644 3767 C ATOM 4158 O ALA B 302 31.010 -4.526 -8.468 1.00 96.44 O ANISOU 4158 O ALA B 302 10372 15312 10959 -3172 -5509 3617 O ATOM 4159 CB ALA B 302 33.990 -5.988 -8.473 1.00102.80 C ANISOU 4159 CB ALA B 302 10193 16507 12362 -2988 -5686 4148 C ATOM 4160 N LEU B 303 31.225 -6.286 -7.070 1.00 98.69 N ANISOU 4160 N LEU B 303 10704 15703 11092 -2905 -5631 3810 N ATOM 4161 CA LEU B 303 29.811 -6.634 -7.096 1.00 95.38 C ANISOU 4161 CA LEU B 303 10613 15170 10456 -2767 -5436 3688 C ATOM 4162 C LEU B 303 28.974 -5.482 -6.551 1.00 94.55 C ANISOU 4162 C LEU B 303 10995 14913 10015 -2957 -5456 3409 C ATOM 4163 O LEU B 303 27.919 -5.155 -7.096 1.00 89.54 O ANISOU 4163 O LEU B 303 10557 14108 9357 -2880 -5154 3205 O ATOM 4164 CB LEU B 303 29.566 -7.904 -6.279 1.00 95.76 C ANISOU 4164 CB LEU B 303 10727 15250 10409 -2531 -5408 3823 C ATOM 4165 CG LEU B 303 28.336 -8.736 -6.642 1.00 92.46 C ANISOU 4165 CG LEU B 303 10070 14807 10253 -2206 -5114 3939 C ATOM 4166 CD1 LEU B 303 28.409 -9.187 -8.092 1.00 93.94 C ANISOU 4166 CD1 LEU B 303 9749 15119 10824 -2156 -5132 4110 C ATOM 4167 CD2 LEU B 303 28.218 -9.931 -5.715 1.00 93.99 C ANISOU 4167 CD2 LEU B 303 10353 15023 10334 -2015 -5155 4103 C ATOM 4168 N ARG B 304 29.460 -4.864 -5.478 1.00104.27 N ANISOU 4168 N ARG B 304 12441 16159 11018 -3154 -5726 3356 N ATOM 4169 CA ARG B 304 28.786 -3.719 -4.876 1.00104.31 C ANISOU 4169 CA ARG B 304 12915 16023 10694 -3338 -5779 3086 C ATOM 4170 C ARG B 304 28.753 -2.540 -5.844 1.00103.59 C ANISOU 4170 C ARG B 304 12803 15824 10734 -3531 -5766 2948 C ATOM 4171 O ARG B 304 27.752 -1.820 -5.929 1.00101.71 O ANISOU 4171 O ARG B 304 12907 15404 10334 -3555 -5622 2701 O ATOM 4172 CB ARG B 304 29.475 -3.315 -3.570 1.00127.14 C ANISOU 4172 CB ARG B 304 16030 18938 13340 -3499 -6056 3046 C ATOM 4173 CG ARG B 304 28.807 -2.156 -2.849 1.00129.50 C ANISOU 4173 CG ARG B 304 16001 19337 13866 -3666 -6307 3193 C ATOM 4174 CD ARG B 304 29.386 -1.963 -1.457 1.00133.14 C ANISOU 4174 CD ARG B 304 16718 19800 14069 -3869 -6601 3121 C ATOM 4175 NE ARG B 304 30.800 -1.599 -1.491 1.00133.14 N ANISOU 4175 NE ARG B 304 17245 19635 13707 -3981 -6594 2826 N ATOM 4176 CZ ARG B 304 31.251 -0.349 -1.444 1.00135.89 C ANISOU 4176 CZ ARG B 304 17862 19918 13850 -4215 -6829 2681 C ATOM 4177 NH1 ARG B 304 30.397 0.662 -1.361 1.00139.37 N ANISOU 4177 NH1 ARG B 304 18089 20455 14411 -4383 -7106 2817 N ATOM 4178 NH2 ARG B 304 32.555 -0.110 -1.479 1.00135.97 N ANISOU 4178 NH2 ARG B 304 18362 19766 13535 -4274 -6784 2397 N ATOM 4179 N ARG B 305 29.852 -2.346 -6.569 1.00 99.03 N ANISOU 4179 N ARG B 305 11831 15322 10474 -3639 -5853 3088 N ATOM 4180 CA ARG B 305 29.912 -1.320 -7.603 1.00 98.29 C ANISOU 4180 CA ARG B 305 11683 15128 10534 -3824 -5820 2995 C ATOM 4181 C ARG B 305 28.833 -1.567 -8.648 1.00 91.91 C ANISOU 4181 C ARG B 305 10869 14200 9854 -3593 -5407 2904 C ATOM 4182 O ARG B 305 28.132 -0.642 -9.061 1.00 89.26 O ANISOU 4182 O ARG B 305 10776 13666 9475 -3656 -5270 2693 O ATOM 4183 CB ARG B 305 31.292 -1.285 -8.268 1.00127.31 C ANISOU 4183 CB ARG B 305 14904 18926 14541 -3958 -5929 3188 C ATOM 4184 CG ARG B 305 32.408 -0.774 -7.371 1.00129.98 C ANISOU 4184 CG ARG B 305 15298 19292 14797 -4193 -6243 3203 C ATOM 4185 CD ARG B 305 33.637 -0.390 -8.181 1.00131.80 C ANISOU 4185 CD ARG B 305 15069 19651 15358 -4336 -6333 3400 C ATOM 4186 NE ARG B 305 34.247 -1.535 -8.852 1.00131.99 N ANISOU 4186 NE ARG B 305 14627 19882 15639 -4090 -6227 3650 N ATOM 4187 CZ ARG B 305 35.292 -2.207 -8.380 1.00134.01 C ANISOU 4187 CZ ARG B 305 14456 20304 16156 -4143 -6316 3856 C ATOM 4188 NH1 ARG B 305 35.848 -1.850 -7.231 1.00136.31 N ANISOU 4188 NH1 ARG B 305 14720 20586 16484 -4455 -6522 3855 N ATOM 4189 NH2 ARG B 305 35.783 -3.235 -9.059 1.00134.29 N ANISOU 4189 NH2 ARG B 305 14097 20508 16416 -3878 -6197 4062 N ATOM 4190 N GLY B 306 28.698 -2.824 -9.063 1.00 89.14 N ANISOU 4190 N GLY B 306 10265 13938 9667 -3303 -5185 3048 N ATOM 4191 CA GLY B 306 27.661 -3.205 -10.005 1.00 82.79 C ANISOU 4191 CA GLY B 306 9470 13007 8977 -3057 -4770 2953 C ATOM 4192 C GLY B 306 26.272 -2.899 -9.477 1.00 79.42 C ANISOU 4192 C GLY B 306 9504 12394 8276 -2969 -4593 2705 C ATOM 4193 O GLY B 306 25.423 -2.373 -10.203 1.00 75.29 O ANISOU 4193 O GLY B 306 9104 11710 7793 -2917 -4350 2539 O ATOM 4194 N VAL B 307 26.047 -3.223 -8.206 1.00 81.58 N ANISOU 4194 N VAL B 307 10023 12704 8268 -2948 -4716 2691 N ATOM 4195 CA VAL B 307 24.764 -2.969 -7.556 1.00 79.35 C ANISOU 4195 CA VAL B 307 10171 12284 7695 -2865 -4554 2469 C ATOM 4196 C VAL B 307 24.408 -1.486 -7.563 1.00 79.63 C ANISOU 4196 C VAL B 307 10512 12145 7596 -3053 -4603 2218 C ATOM 4197 O VAL B 307 23.326 -1.100 -8.013 1.00 75.70 O ANISOU 4197 O VAL B 307 10215 11483 7062 -2945 -4343 2024 O ATOM 4198 CB VAL B 307 24.752 -3.482 -6.100 1.00 82.89 C ANISOU 4198 CB VAL B 307 10830 12835 7832 -2856 -4723 2522 C ATOM 4199 CG1 VAL B 307 23.467 -3.068 -5.401 1.00 81.44 C ANISOU 4199 CG1 VAL B 307 11099 12527 7319 -2800 -4559 2278 C ATOM 4200 CG2 VAL B 307 24.920 -4.992 -6.065 1.00 82.42 C ANISOU 4200 CG2 VAL B 307 10518 12901 7896 -2639 -4648 2764 C ATOM 4201 N LEU B 308 25.324 -0.660 -7.065 1.00 84.64 N ANISOU 4201 N LEU B 308 11182 12811 8168 -3336 -4952 2229 N ATOM 4202 CA LEU B 308 25.096 0.780 -6.997 1.00 85.96 C ANISOU 4202 CA LEU B 308 11664 12789 8208 -3544 -5052 1997 C ATOM 4203 C LEU B 308 24.900 1.405 -8.377 1.00 82.01 C ANISOU 4203 C LEU B 308 11047 12139 7975 -3532 -4840 1936 C ATOM 4204 O LEU B 308 23.987 2.213 -8.575 1.00 79.70 O ANISOU 4204 O LEU B 308 11055 11635 7594 -3497 -4687 1706 O ATOM 4205 CB LEU B 308 26.239 1.474 -6.253 1.00 92.72 C ANISOU 4205 CB LEU B 308 12520 13716 8995 -3881 -5498 2058 C ATOM 4206 CG LEU B 308 26.326 1.190 -4.752 1.00 97.65 C ANISOU 4206 CG LEU B 308 13474 14398 9229 -3975 -5763 1997 C ATOM 4207 CD1 LEU B 308 27.535 1.878 -4.139 1.00102.73 C ANISOU 4207 CD1 LEU B 308 14022 15092 9919 -4260 -6121 2075 C ATOM 4208 CD2 LEU B 308 25.047 1.622 -4.052 1.00 96.88 C ANISOU 4208 CD2 LEU B 308 13912 14087 8811 -3941 -5641 1670 C ATOM 4209 N VAL B 309 25.752 1.025 -9.326 1.00 81.49 N ANISOU 4209 N VAL B 309 10544 12188 8230 -3547 -4824 2147 N ATOM 4210 CA VAL B 309 25.648 1.532 -10.692 1.00 78.01 C ANISOU 4210 CA VAL B 309 9962 11638 8041 -3535 -4616 2127 C ATOM 4211 C VAL B 309 24.297 1.188 -11.310 1.00 71.98 C ANISOU 4211 C VAL B 309 9337 10748 7264 -3244 -4234 1988 C ATOM 4212 O VAL B 309 23.602 2.066 -11.821 1.00 69.73 O ANISOU 4212 O VAL B 309 9260 10263 6972 -3250 -4110 1814 O ATOM 4213 CB VAL B 309 26.779 0.994 -11.597 1.00 78.46 C ANISOU 4213 CB VAL B 309 9503 11883 8427 -3541 -4604 2391 C ATOM 4214 CG1 VAL B 309 26.442 1.214 -13.064 1.00 74.08 C ANISOU 4214 CG1 VAL B 309 8823 11232 8093 -3453 -4310 2370 C ATOM 4215 CG2 VAL B 309 28.100 1.659 -11.247 1.00 84.61 C ANISOU 4215 CG2 VAL B 309 10105 12770 9272 -3873 -4972 2526 C ATOM 4216 N LEU B 310 23.925 -0.088 -11.246 1.00 69.75 N ANISOU 4216 N LEU B 310 8943 10577 6983 -2996 -4065 2072 N ATOM 4217 CA LEU B 310 22.664 -0.541 -11.825 1.00 64.45 C ANISOU 4217 CA LEU B 310 8357 9811 6320 -2732 -3714 1967 C ATOM 4218 C LEU B 310 21.465 0.136 -11.167 1.00 63.55 C ANISOU 4218 C LEU B 310 8677 9525 5943 -2698 -3641 1710 C ATOM 4219 O LEU B 310 20.511 0.522 -11.846 1.00 59.92 O ANISOU 4219 O LEU B 310 8320 8917 5530 -2590 -3417 1573 O ATOM 4220 CB LEU B 310 22.538 -2.060 -11.722 1.00 63.23 C ANISOU 4220 CB LEU B 310 8034 9795 6195 -2505 -3587 2112 C ATOM 4221 CG LEU B 310 21.317 -2.660 -12.418 1.00 58.11 C ANISOU 4221 CG LEU B 310 7409 9065 5605 -2251 -3235 2038 C ATOM 4222 CD1 LEU B 310 21.287 -2.259 -13.885 1.00 55.07 C ANISOU 4222 CD1 LEU B 310 6843 8610 5471 -2229 -3071 2033 C ATOM 4223 CD2 LEU B 310 21.316 -4.169 -12.273 1.00 57.64 C ANISOU 4223 CD2 LEU B 310 7201 9120 5579 -2059 -3143 2192 C ATOM 4224 N ARG B 311 21.523 0.278 -9.846 1.00 70.62 N ANISOU 4224 N ARG B 311 9826 10448 6557 -2783 -3830 1646 N ATOM 4225 CA ARG B 311 20.471 0.958 -9.098 1.00 70.54 C ANISOU 4225 CA ARG B 311 10240 10288 6272 -2744 -3759 1389 C ATOM 4226 C ARG B 311 20.308 2.389 -9.599 1.00 70.71 C ANISOU 4226 C ARG B 311 10444 10089 6332 -2880 -3807 1214 C ATOM 4227 O ARG B 311 19.195 2.829 -9.914 1.00 68.08 O ANISOU 4227 O ARG B 311 10326 9591 5951 -2746 -3602 1022 O ATOM 4228 CB ARG B 311 20.798 0.958 -7.602 1.00 72.75 C ANISOU 4228 CB ARG B 311 10772 10651 6217 -2836 -3979 1356 C ATOM 4229 CG ARG B 311 19.717 1.559 -6.718 1.00 72.28 C ANISOU 4229 CG ARG B 311 10660 10760 6045 -2657 -3868 1480 C ATOM 4230 CD ARG B 311 20.160 1.605 -5.265 1.00 76.41 C ANISOU 4230 CD ARG B 311 11537 11330 6163 -2709 -4001 1384 C ATOM 4231 NE ARG B 311 20.620 0.301 -4.794 1.00 82.06 N ANISOU 4231 NE ARG B 311 12318 12093 6765 -2981 -4402 1419 N ATOM 4232 CZ ARG B 311 21.155 0.084 -3.597 1.00 86.31 C ANISOU 4232 CZ ARG B 311 12865 12808 7121 -3056 -4636 1565 C ATOM 4233 NH1 ARG B 311 21.301 1.085 -2.739 1.00 85.45 N ANISOU 4233 NH1 ARG B 311 12707 12829 6928 -2877 -4498 1698 N ATOM 4234 NH2 ARG B 311 21.547 -1.136 -3.255 1.00 91.73 N ANISOU 4234 NH2 ARG B 311 13603 13535 7713 -3322 -5023 1591 N ATOM 4235 N ALA B 312 21.429 3.103 -9.680 1.00 70.63 N ANISOU 4235 N ALA B 312 10337 10076 6423 -3147 -4082 1291 N ATOM 4236 CA ALA B 312 21.439 4.477 -10.172 1.00 71.41 C ANISOU 4236 CA ALA B 312 10605 9948 6579 -3313 -4158 1156 C ATOM 4237 C ALA B 312 20.867 4.570 -11.584 1.00 66.32 C ANISOU 4237 C ALA B 312 9824 9198 6176 -3164 -3875 1155 C ATOM 4238 O ALA B 312 20.138 5.510 -11.903 1.00 65.06 O ANISOU 4238 O ALA B 312 9918 8811 5992 -3130 -3786 971 O ATOM 4239 CB ALA B 312 22.849 5.044 -10.131 1.00 76.61 C ANISOU 4239 CB ALA B 312 11116 10653 7340 -3648 -4501 1290 C ATOM 4240 N VAL B 313 21.198 3.591 -12.421 1.00 68.97 N ANISOU 4240 N VAL B 313 9771 9695 6737 -3062 -3736 1358 N ATOM 4241 CA VAL B 313 20.692 3.547 -13.790 1.00 64.49 C ANISOU 4241 CA VAL B 313 9061 9058 6384 -2920 -3472 1374 C ATOM 4242 C VAL B 313 19.174 3.393 -13.817 1.00 61.50 C ANISOU 4242 C VAL B 313 8892 8574 5901 -2650 -3200 1199 C ATOM 4243 O VAL B 313 18.483 4.115 -14.539 1.00 59.99 O ANISOU 4243 O VAL B 313 8815 8205 5772 -2590 -3070 1089 O ATOM 4244 CB VAL B 313 21.342 2.405 -14.601 1.00 57.51 C ANISOU 4244 CB VAL B 313 7740 8380 5730 -2841 -3369 1610 C ATOM 4245 CG1 VAL B 313 20.616 2.205 -15.922 1.00 52.85 C ANISOU 4245 CG1 VAL B 313 7045 7722 5311 -2671 -3082 1604 C ATOM 4246 CG2 VAL B 313 22.816 2.694 -14.838 1.00 61.39 C ANISOU 4246 CG2 VAL B 313 7971 8988 6367 -3098 -3606 1795 C ATOM 4247 N VAL B 314 18.665 2.453 -13.025 1.00 59.55 N ANISOU 4247 N VAL B 314 8688 8439 5497 -2495 -3122 1187 N ATOM 4248 CA VAL B 314 17.225 2.222 -12.930 1.00 57.36 C ANISOU 4248 CA VAL B 314 8575 8100 5119 -2249 -2860 1042 C ATOM 4249 C VAL B 314 16.490 3.481 -12.477 1.00 58.69 C ANISOU 4249 C VAL B 314 9127 8056 5115 -2255 -2872 791 C ATOM 4250 O VAL B 314 15.536 3.927 -13.129 1.00 58.18 O ANISOU 4250 O VAL B 314 9142 7850 5114 -2112 -2686 676 O ATOM 4251 CB VAL B 314 16.898 1.065 -11.962 1.00 52.15 C ANISOU 4251 CB VAL B 314 7911 7607 4295 -2124 -2796 1092 C ATOM 4252 CG1 VAL B 314 15.396 0.970 -11.733 1.00 49.68 C ANISOU 4252 CG1 VAL B 314 7783 7236 3856 -1903 -2536 933 C ATOM 4253 CG2 VAL B 314 17.444 -0.250 -12.498 1.00 50.91 C ANISOU 4253 CG2 VAL B 314 7391 7619 4332 -2062 -2744 1326 C ATOM 4254 N ILE B 315 16.947 4.054 -11.365 1.00 57.05 N ANISOU 4254 N ILE B 315 9164 7823 4690 -2415 -3102 704 N ATOM 4255 CA ILE B 315 16.337 5.265 -10.820 1.00 58.84 C ANISOU 4255 CA ILE B 315 9795 7832 4729 -2418 -3132 445 C ATOM 4256 C ILE B 315 16.343 6.402 -11.837 1.00 58.09 C ANISOU 4256 C ILE B 315 9754 7499 4819 -2494 -3160 385 C ATOM 4257 O ILE B 315 15.311 7.034 -12.083 1.00 56.62 O ANISOU 4257 O ILE B 315 9780 7123 4610 -2341 -3013 205 O ATOM 4258 CB ILE B 315 17.055 5.736 -9.540 1.00 64.51 C ANISOU 4258 CB ILE B 315 10779 8557 5175 -2616 -3418 365 C ATOM 4259 CG1 ILE B 315 16.986 4.657 -8.459 1.00 65.53 C ANISOU 4259 CG1 ILE B 315 10903 8914 5081 -2528 -3382 422 C ATOM 4260 CG2 ILE B 315 16.445 7.033 -9.028 1.00 66.86 C ANISOU 4260 CG2 ILE B 315 11522 8597 5283 -2612 -3446 74 C ATOM 4261 CD1 ILE B 315 17.725 5.021 -7.189 1.00 63.05 C ANISOU 4261 CD1 ILE B 315 10732 8606 4617 -2244 -3065 286 C ATOM 4262 N ALA B 316 17.509 6.652 -12.427 1.00 61.15 N ANISOU 4262 N ALA B 316 9934 7903 5396 -2724 -3341 551 N ATOM 4263 CA ALA B 316 17.657 7.721 -13.408 1.00 60.91 C ANISOU 4263 CA ALA B 316 9938 7658 5546 -2835 -3382 537 C ATOM 4264 C ALA B 316 16.729 7.515 -14.600 1.00 55.75 C ANISOU 4264 C ALA B 316 9163 6955 5062 -2597 -3090 547 C ATOM 4265 O ALA B 316 16.143 8.472 -15.109 1.00 55.04 O ANISOU 4265 O ALA B 316 9263 6629 5018 -2553 -3044 430 O ATOM 4266 CB ALA B 316 19.102 7.828 -13.870 1.00 61.38 C ANISOU 4266 CB ALA B 316 9733 7802 5785 -3126 -3597 754 C ATOM 4267 N PHE B 317 16.595 6.266 -15.037 1.00 51.52 N ANISOU 4267 N PHE B 317 8325 6633 4616 -2443 -2907 686 N ATOM 4268 CA PHE B 317 15.709 5.942 -16.150 1.00 46.94 C ANISOU 4268 CA PHE B 317 7618 6031 4184 -2226 -2645 702 C ATOM 4269 C PHE B 317 14.263 6.270 -15.798 1.00 45.43 C ANISOU 4269 C PHE B 317 7689 5708 3863 -1993 -2479 485 C ATOM 4270 O PHE B 317 13.577 6.967 -16.552 1.00 43.58 O ANISOU 4270 O PHE B 317 7537 5301 3719 -1895 -2385 413 O ATOM 4271 CB PHE B 317 15.830 4.466 -16.539 1.00 64.92 C ANISOU 4271 CB PHE B 317 9557 8552 6557 -2112 -2498 873 C ATOM 4272 CG PHE B 317 15.085 4.105 -17.799 1.00 63.12 C ANISOU 4272 CG PHE B 317 9174 8313 6496 -1938 -2267 911 C ATOM 4273 CD1 PHE B 317 13.749 3.738 -17.754 1.00 62.43 C ANISOU 4273 CD1 PHE B 317 9162 8202 6358 -1698 -2059 800 C ATOM 4274 CD2 PHE B 317 15.723 4.134 -19.027 1.00 62.39 C ANISOU 4274 CD2 PHE B 317 8858 8247 6603 -2021 -2260 1061 C ATOM 4275 CE1 PHE B 317 13.066 3.405 -18.908 1.00 60.90 C ANISOU 4275 CE1 PHE B 317 8829 8001 6311 -1554 -1876 836 C ATOM 4276 CE2 PHE B 317 15.045 3.802 -20.185 1.00 60.82 C ANISOU 4276 CE2 PHE B 317 8541 8039 6528 -1868 -2062 1089 C ATOM 4277 CZ PHE B 317 13.715 3.437 -20.125 1.00 59.98 C ANISOU 4277 CZ PHE B 317 8518 7900 6371 -1640 -1884 975 C ATOM 4278 N VAL B 318 13.809 5.765 -14.653 1.00 61.38 N ANISOU 4278 N VAL B 318 9833 7819 5669 -1900 -2442 393 N ATOM 4279 CA VAL B 318 12.441 6.006 -14.201 1.00 62.38 C ANISOU 4279 CA VAL B 318 10186 7859 5658 -1667 -2261 191 C ATOM 4280 C VAL B 318 12.133 7.498 -14.108 1.00 64.70 C ANISOU 4280 C VAL B 318 10817 7865 5904 -1685 -2345 -10 C ATOM 4281 O VAL B 318 11.141 7.976 -14.669 1.00 65.24 O ANISOU 4281 O VAL B 318 10949 7789 6050 -1501 -2196 -103 O ATOM 4282 CB VAL B 318 12.170 5.350 -12.834 1.00 46.44 C ANISOU 4282 CB VAL B 318 8279 5993 3374 -1606 -2227 129 C ATOM 4283 CG1 VAL B 318 10.798 5.754 -12.316 1.00 46.08 C ANISOU 4283 CG1 VAL B 318 8469 5865 3175 -1369 -2026 -90 C ATOM 4284 CG2 VAL B 318 12.283 3.837 -12.940 1.00 44.60 C ANISOU 4284 CG2 VAL B 318 7737 6012 3197 -1559 -2126 327 C ATOM 4285 N VAL B 319 13.000 8.229 -13.412 1.00 57.95 N ANISOU 4285 N VAL B 319 10176 6915 4927 -1908 -2600 -70 N ATOM 4286 CA VAL B 319 12.813 9.662 -13.204 1.00 60.67 C ANISOU 4286 CA VAL B 319 10889 6953 5208 -1946 -2710 -274 C ATOM 4287 C VAL B 319 12.818 10.453 -14.511 1.00 60.39 C ANISOU 4287 C VAL B 319 10808 6710 5425 -1983 -2725 -215 C ATOM 4288 O VAL B 319 11.931 11.273 -14.752 1.00 61.91 O ANISOU 4288 O VAL B 319 11220 6668 5636 -1826 -2650 -369 O ATOM 4289 CB VAL B 319 13.891 10.241 -12.263 1.00 59.51 C ANISOU 4289 CB VAL B 319 10975 6745 4892 -2230 -3022 -332 C ATOM 4290 CG1 VAL B 319 13.777 11.756 -12.186 1.00 63.07 C ANISOU 4290 CG1 VAL B 319 11831 6836 5298 -2283 -3151 -546 C ATOM 4291 CG2 VAL B 319 13.774 9.621 -10.880 1.00 61.65 C ANISOU 4291 CG2 VAL B 319 11353 7203 4868 -2183 -3015 -407 C ATOM 4292 N CYS B 320 13.816 10.203 -15.353 1.00 71.49 N ANISOU 4292 N CYS B 320 11929 8209 7023 -2179 -2815 15 N ATOM 4293 CA CYS B 320 13.954 10.945 -16.602 1.00 71.60 C ANISOU 4293 CA CYS B 320 11895 8050 7258 -2249 -2837 102 C ATOM 4294 C CYS B 320 12.840 10.641 -17.599 1.00 70.56 C ANISOU 4294 C CYS B 320 11643 7916 7252 -1967 -2576 113 C ATOM 4295 O CYS B 320 12.423 11.519 -18.357 1.00 71.71 O ANISOU 4295 O CYS B 320 11913 7832 7503 -1920 -2568 80 O ATOM 4296 CB CYS B 320 15.315 10.677 -17.246 1.00 66.54 C ANISOU 4296 CB CYS B 320 10954 7551 6776 -2525 -2969 355 C ATOM 4297 SG CYS B 320 16.719 11.387 -16.361 1.00 68.60 S ANISOU 4297 SG CYS B 320 11355 7745 6964 -2928 -3340 371 S ATOM 4298 N TRP B 321 12.355 9.403 -17.596 1.00 45.20 N ANISOU 4298 N TRP B 321 8195 4950 4031 -1788 -2380 168 N ATOM 4299 CA TRP B 321 11.353 8.992 -18.576 1.00 44.10 C ANISOU 4299 CA TRP B 321 7899 4840 4019 -1553 -2154 202 C ATOM 4300 C TRP B 321 9.907 9.156 -18.109 1.00 45.54 C ANISOU 4300 C TRP B 321 8247 4950 4106 -1258 -1981 6 C ATOM 4301 O TRP B 321 8.987 9.106 -18.924 1.00 45.46 O ANISOU 4301 O TRP B 321 8144 4921 4209 -1065 -1826 16 O ATOM 4302 CB TRP B 321 11.604 7.555 -19.043 1.00 54.92 C ANISOU 4302 CB TRP B 321 8902 6493 5470 -1532 -2036 385 C ATOM 4303 CG TRP B 321 12.764 7.436 -19.977 1.00 53.77 C ANISOU 4303 CG TRP B 321 8541 6408 5480 -1743 -2131 589 C ATOM 4304 CD1 TRP B 321 14.031 7.039 -19.666 1.00 53.37 C ANISOU 4304 CD1 TRP B 321 8342 6503 5430 -1954 -2267 718 C ATOM 4305 CD2 TRP B 321 12.766 7.726 -21.379 1.00 53.31 C ANISOU 4305 CD2 TRP B 321 8384 6279 5592 -1762 -2092 695 C ATOM 4306 NE1 TRP B 321 14.822 7.059 -20.789 1.00 52.82 N ANISOU 4306 NE1 TRP B 321 8072 6468 5529 -2094 -2293 894 N ATOM 4307 CE2 TRP B 321 14.069 7.478 -21.854 1.00 52.68 C ANISOU 4307 CE2 TRP B 321 8093 6318 5603 -1986 -2185 883 C ATOM 4308 CE3 TRP B 321 11.792 8.170 -22.280 1.00 53.69 C ANISOU 4308 CE3 TRP B 321 8496 6184 5717 -1607 -1991 659 C ATOM 4309 CZ2 TRP B 321 14.424 7.659 -23.188 1.00 52.39 C ANISOU 4309 CZ2 TRP B 321 7923 6268 5714 -2065 -2157 1029 C ATOM 4310 CZ3 TRP B 321 12.145 8.349 -23.604 1.00 53.18 C ANISOU 4310 CZ3 TRP B 321 8314 6097 5794 -1691 -1989 809 C ATOM 4311 CH2 TRP B 321 13.450 8.094 -24.045 1.00 52.53 C ANISOU 4311 CH2 TRP B 321 8036 6140 5782 -1921 -2061 989 C ATOM 4312 N LEU B 322 9.706 9.357 -16.810 1.00 57.29 N ANISOU 4312 N LEU B 322 9975 6409 5383 -1222 -2006 -168 N ATOM 4313 CA LEU B 322 8.350 9.508 -16.276 1.00 59.15 C ANISOU 4313 CA LEU B 322 10357 6601 5516 -930 -1816 -359 C ATOM 4314 C LEU B 322 7.546 10.686 -16.861 1.00 61.48 C ANISOU 4314 C LEU B 322 10837 6611 5911 -769 -1791 -477 C ATOM 4315 O LEU B 322 6.439 10.476 -17.359 1.00 62.05 O ANISOU 4315 O LEU B 322 10794 6713 6070 -522 -1601 -489 O ATOM 4316 CB LEU B 322 8.349 9.550 -14.743 1.00 60.28 C ANISOU 4316 CB LEU B 322 10743 6782 5377 -922 -1834 -530 C ATOM 4317 CG LEU B 322 6.972 9.696 -14.092 1.00 62.49 C ANISOU 4317 CG LEU B 322 11164 7048 5531 -610 -1606 -730 C ATOM 4318 CD1 LEU B 322 6.098 8.490 -14.400 1.00 60.90 C ANISOU 4318 CD1 LEU B 322 10649 7121 5370 -444 -1359 -624 C ATOM 4319 CD2 LEU B 322 7.105 9.900 -12.590 1.00 64.73 C ANISOU 4319 CD2 LEU B 322 11784 7301 5511 -624 -1656 -933 C ATOM 4320 N PRO B 323 8.089 11.921 -16.810 1.00 76.67 N ANISOU 4320 N PRO B 323 13046 8252 7834 -910 -1993 -555 N ATOM 4321 CA PRO B 323 7.287 13.040 -17.325 1.00 79.06 C ANISOU 4321 CA PRO B 323 13542 8260 8240 -736 -1975 -660 C ATOM 4322 C PRO B 323 7.092 12.964 -18.837 1.00 78.12 C ANISOU 4322 C PRO B 323 13180 8140 8363 -704 -1930 -470 C ATOM 4323 O PRO B 323 6.113 13.498 -19.361 1.00 79.94 O ANISOU 4323 O PRO B 323 13460 8228 8688 -469 -1841 -525 O ATOM 4324 CB PRO B 323 8.135 14.271 -16.978 1.00 48.23 C ANISOU 4324 CB PRO B 323 9980 4052 4293 -967 -2239 -741 C ATOM 4325 CG PRO B 323 9.092 13.811 -15.934 1.00 50.79 C ANISOU 4325 CG PRO B 323 10350 4526 4421 -1185 -2360 -764 C ATOM 4326 CD PRO B 323 9.381 12.392 -16.281 1.00 46.67 C ANISOU 4326 CD PRO B 323 9418 4370 3945 -1225 -2255 -556 C ATOM 4327 N TYR B 324 8.024 12.309 -19.521 1.00 42.22 N ANISOU 4327 N TYR B 324 8378 3757 3908 -930 -1994 -250 N ATOM 4328 CA TYR B 324 7.950 12.132 -20.968 1.00 40.81 C ANISOU 4328 CA TYR B 324 7970 3612 3926 -925 -1950 -62 C ATOM 4329 C TYR B 324 6.693 11.367 -21.370 1.00 40.56 C ANISOU 4329 C TYR B 324 7736 3733 3942 -633 -1722 -66 C ATOM 4330 O TYR B 324 5.959 11.789 -22.266 1.00 41.94 O ANISOU 4330 O TYR B 324 7902 3796 4240 -483 -1681 -43 O ATOM 4331 CB TYR B 324 9.200 11.409 -21.475 1.00 64.44 C ANISOU 4331 CB TYR B 324 10706 6803 6974 -1195 -2021 155 C ATOM 4332 CG TYR B 324 9.118 10.947 -22.912 1.00 62.88 C ANISOU 4332 CG TYR B 324 10257 6695 6940 -1185 -1944 345 C ATOM 4333 CD1 TYR B 324 9.347 11.829 -23.959 1.00 63.96 C ANISOU 4333 CD1 TYR B 324 10470 6640 7192 -1288 -2041 443 C ATOM 4334 CD2 TYR B 324 8.828 9.624 -23.220 1.00 60.19 C ANISOU 4334 CD2 TYR B 324 9622 6623 6624 -1085 -1781 428 C ATOM 4335 CE1 TYR B 324 9.280 11.409 -25.273 1.00 62.50 C ANISOU 4335 CE1 TYR B 324 10076 6548 7122 -1283 -1970 614 C ATOM 4336 CE2 TYR B 324 8.758 9.193 -24.529 1.00 58.46 C ANISOU 4336 CE2 TYR B 324 9201 6481 6528 -1078 -1717 582 C ATOM 4337 CZ TYR B 324 8.985 10.090 -25.554 1.00 59.63 C ANISOU 4337 CZ TYR B 324 9432 6456 6769 -1174 -1808 673 C ATOM 4338 OH TYR B 324 8.917 9.664 -26.862 1.00 57.88 O ANISOU 4338 OH TYR B 324 9030 6322 6638 -1169 -1742 824 O ATOM 4339 N HIS B 325 6.444 10.250 -20.693 1.00 55.72 N ANISOU 4339 N HIS B 325 9497 5910 5767 -564 -1588 -84 N ATOM 4340 CA HIS B 325 5.276 9.423 -20.983 1.00 55.63 C ANISOU 4340 CA HIS B 325 9276 6064 5797 -322 -1377 -79 C ATOM 4341 C HIS B 325 3.972 10.113 -20.594 1.00 59.34 C ANISOU 4341 C HIS B 325 9908 6401 6239 -34 -1271 -266 C ATOM 4342 O HIS B 325 2.940 9.911 -21.234 1.00 60.57 O ANISOU 4342 O HIS B 325 9915 6600 6500 171 -1145 -247 O ATOM 4343 CB HIS B 325 5.385 8.066 -20.283 1.00 49.42 C ANISOU 4343 CB HIS B 325 8300 5565 4912 -346 -1270 -39 C ATOM 4344 CG HIS B 325 6.419 7.161 -20.876 1.00 45.85 C ANISOU 4344 CG HIS B 325 7623 5272 4528 -554 -1329 157 C ATOM 4345 ND1 HIS B 325 6.188 6.410 -22.009 1.00 43.87 N ANISOU 4345 ND1 HIS B 325 7132 5115 4424 -533 -1262 299 N ATOM 4346 CD2 HIS B 325 7.687 6.884 -20.494 1.00 44.18 C ANISOU 4346 CD2 HIS B 325 7387 5143 4256 -774 -1447 232 C ATOM 4347 CE1 HIS B 325 7.270 5.709 -22.298 1.00 41.08 C ANISOU 4347 CE1 HIS B 325 6624 4890 4097 -716 -1317 442 C ATOM 4348 NE2 HIS B 325 8.195 5.979 -21.394 1.00 41.39 N ANISOU 4348 NE2 HIS B 325 6773 4931 4023 -861 -1431 414 N ATOM 4349 N VAL B 326 4.025 10.925 -19.542 1.00 45.31 N ANISOU 4349 N VAL B 326 8433 4466 4320 -15 -1324 -449 N ATOM 4350 CA VAL B 326 2.854 11.671 -19.087 1.00 48.78 C ANISOU 4350 CA VAL B 326 9056 4759 4722 278 -1216 -649 C ATOM 4351 C VAL B 326 2.393 12.655 -20.155 1.00 50.74 C ANISOU 4351 C VAL B 326 9375 4749 5156 395 -1281 -629 C ATOM 4352 O VAL B 326 1.195 12.803 -20.407 1.00 52.86 O ANISOU 4352 O VAL B 326 9575 5005 5504 680 -1147 -679 O ATOM 4353 CB VAL B 326 3.145 12.442 -17.783 1.00 36.88 C ANISOU 4353 CB VAL B 326 7911 3101 3001 258 -1281 -866 C ATOM 4354 CG1 VAL B 326 1.955 13.309 -17.394 1.00 40.12 C ANISOU 4354 CG1 VAL B 326 8543 3308 3393 581 -1176 -1085 C ATOM 4355 CG2 VAL B 326 3.489 11.478 -16.663 1.00 37.24 C ANISOU 4355 CG2 VAL B 326 7896 3418 2836 192 -1196 -891 C ATOM 4356 N ARG B 327 3.355 13.321 -20.784 1.00 53.02 N ANISOU 4356 N ARG B 327 9785 4841 5516 166 -1491 -537 N ATOM 4357 CA ARG B 327 3.058 14.306 -21.815 1.00 54.61 C ANISOU 4357 CA ARG B 327 10085 4779 5885 233 -1583 -485 C ATOM 4358 C ARG B 327 2.412 13.667 -23.042 1.00 54.08 C ANISOU 4358 C ARG B 327 9703 4868 5977 342 -1492 -314 C ATOM 4359 O ARG B 327 1.482 14.226 -23.626 1.00 56.05 O ANISOU 4359 O ARG B 327 9974 4982 6340 570 -1470 -326 O ATOM 4360 CB ARG B 327 4.329 15.046 -22.226 1.00 64.42 C ANISOU 4360 CB ARG B 327 11497 5817 7162 -90 -1821 -385 C ATOM 4361 CG ARG B 327 4.102 16.085 -23.305 1.00 65.89 C ANISOU 4361 CG ARG B 327 11807 5716 7511 -56 -1932 -301 C ATOM 4362 CD ARG B 327 5.411 16.649 -23.810 1.00 65.02 C ANISOU 4362 CD ARG B 327 11821 5446 7436 -418 -2151 -164 C ATOM 4363 NE ARG B 327 6.320 15.601 -24.263 1.00 61.95 N ANISOU 4363 NE ARG B 327 11131 5354 7050 -672 -2145 33 N ATOM 4364 CZ ARG B 327 6.261 15.025 -25.460 1.00 60.38 C ANISOU 4364 CZ ARG B 327 10673 5312 6954 -691 -2088 233 C ATOM 4365 NH1 ARG B 327 5.331 15.393 -26.332 1.00 61.50 N ANISOU 4365 NH1 ARG B 327 10814 5352 7201 -487 -2054 275 N ATOM 4366 NH2 ARG B 327 7.131 14.080 -25.787 1.00 57.63 N ANISOU 4366 NH2 ARG B 327 10072 5224 6598 -904 -2071 387 N ATOM 4367 N ARG B 328 2.908 12.496 -23.429 1.00 50.18 N ANISOU 4367 N ARG B 328 8925 4652 5489 181 -1451 -157 N ATOM 4368 CA ARG B 328 2.381 11.791 -24.592 1.00 49.42 C ANISOU 4368 CA ARG B 328 8542 4715 5518 253 -1377 -3 C ATOM 4369 C ARG B 328 0.961 11.292 -24.342 1.00 51.18 C ANISOU 4369 C ARG B 328 8609 5077 5758 556 -1190 -87 C ATOM 4370 O ARG B 328 0.127 11.289 -25.248 1.00 51.65 O ANISOU 4370 O ARG B 328 8543 5137 5943 712 -1165 -23 O ATOM 4371 CB ARG B 328 3.300 10.633 -24.982 1.00 77.58 C ANISOU 4371 CB ARG B 328 11870 8532 9075 20 -1370 161 C ATOM 4372 CG ARG B 328 4.655 11.084 -25.493 1.00 75.71 C ANISOU 4372 CG ARG B 328 11695 8197 8873 -262 -1534 304 C ATOM 4373 CD ARG B 328 5.562 9.910 -25.831 1.00 71.56 C ANISOU 4373 CD ARG B 328 10949 7923 8316 -472 -1513 428 C ATOM 4374 NE ARG B 328 5.075 9.131 -26.966 1.00 68.57 N ANISOU 4374 NE ARG B 328 10326 7708 8021 -454 -1439 573 N ATOM 4375 CZ ARG B 328 4.606 7.891 -26.875 1.00 66.42 C ANISOU 4375 CZ ARG B 328 9833 7661 7744 -355 -1300 579 C ATOM 4376 NH1 ARG B 328 4.564 7.280 -25.698 1.00 66.88 N ANISOU 4376 NH1 ARG B 328 9869 7822 7722 -266 -1209 468 N ATOM 4377 NH2 ARG B 328 4.184 7.259 -27.964 1.00 64.07 N ANISOU 4377 NH2 ARG B 328 9350 7482 7513 -354 -1254 698 N ATOM 4378 N LEU B 329 0.692 10.872 -23.110 1.00 59.23 N ANISOU 4378 N LEU B 329 9631 6224 6647 628 -1063 -220 N ATOM 4379 CA LEU B 329 -0.657 10.487 -22.713 1.00 61.28 C ANISOU 4379 CA LEU B 329 9754 6618 6912 911 -868 -310 C ATOM 4380 C LEU B 329 -1.550 11.720 -22.683 1.00 64.18 C ANISOU 4380 C LEU B 329 10307 6736 7340 1185 -869 -443 C ATOM 4381 O LEU B 329 -2.732 11.657 -23.018 1.00 65.75 O ANISOU 4381 O LEU B 329 10343 6990 7649 1431 -770 -440 O ATOM 4382 CB LEU B 329 -0.645 9.817 -21.338 1.00 57.51 C ANISOU 4382 CB LEU B 329 9277 6323 6250 909 -729 -417 C ATOM 4383 CG LEU B 329 0.039 8.453 -21.238 1.00 54.08 C ANISOU 4383 CG LEU B 329 8624 6158 5767 701 -695 -283 C ATOM 4384 CD1 LEU B 329 0.047 7.962 -19.800 1.00 53.61 C ANISOU 4384 CD1 LEU B 329 8624 6243 5502 696 -583 -385 C ATOM 4385 CD2 LEU B 329 -0.644 7.446 -22.147 1.00 53.88 C ANISOU 4385 CD2 LEU B 329 8268 6325 5878 767 -596 -151 C ATOM 4386 N MET B 330 -0.966 12.844 -22.280 1.00 73.76 N ANISOU 4386 N MET B 330 11865 7670 8490 1139 -993 -558 N ATOM 4387 CA MET B 330 -1.677 14.115 -22.225 1.00 76.50 C ANISOU 4387 CA MET B 330 12451 7719 8897 1393 -1020 -695 C ATOM 4388 C MET B 330 -2.067 14.588 -23.621 1.00 77.06 C ANISOU 4388 C MET B 330 12450 7654 9176 1465 -1126 -543 C ATOM 4389 O MET B 330 -3.116 15.206 -23.810 1.00 79.41 O ANISOU 4389 O MET B 330 12767 7827 9579 1769 -1086 -603 O ATOM 4390 CB MET B 330 -0.807 15.170 -21.537 1.00 84.46 C ANISOU 4390 CB MET B 330 13871 8426 9794 1261 -1173 -830 C ATOM 4391 CG MET B 330 -1.343 16.588 -21.621 1.00 87.48 C ANISOU 4391 CG MET B 330 14559 8435 10245 1502 -1233 -973 C ATOM 4392 SD MET B 330 -0.195 17.812 -20.961 1.00 87.76 S ANISOU 4392 SD MET B 330 15097 8079 10167 1273 -1464 -1108 S ATOM 4393 CE MET B 330 -1.076 19.329 -21.323 1.00 90.98 C ANISOU 4393 CE MET B 330 15795 8032 10741 1576 -1548 -1194 C ATOM 4394 N PHE B 331 -1.218 14.282 -24.596 1.00 93.21 N ANISOU 4394 N PHE B 331 14409 9734 11274 1193 -1258 -342 N ATOM 4395 CA PHE B 331 -1.416 14.731 -25.970 1.00 93.32 C ANISOU 4395 CA PHE B 331 14376 9633 11450 1209 -1377 -173 C ATOM 4396 C PHE B 331 -2.678 14.159 -26.614 1.00 94.29 C ANISOU 4396 C PHE B 331 14203 9935 11689 1462 -1268 -116 C ATOM 4397 O PHE B 331 -3.275 14.790 -27.485 1.00 96.10 O ANISOU 4397 O PHE B 331 14464 10001 12049 1648 -1340 -70 O ATOM 4398 CB PHE B 331 -0.188 14.385 -26.822 1.00 47.87 C ANISOU 4398 CB PHE B 331 8550 3948 5690 857 -1494 30 C ATOM 4399 CG PHE B 331 -0.353 14.692 -28.286 1.00 47.61 C ANISOU 4399 CG PHE B 331 8469 3835 5785 846 -1606 220 C ATOM 4400 CD1 PHE B 331 -0.236 15.992 -28.751 1.00 49.15 C ANISOU 4400 CD1 PHE B 331 8941 3693 6040 811 -1778 267 C ATOM 4401 CD2 PHE B 331 -0.617 13.682 -29.199 1.00 45.79 C ANISOU 4401 CD2 PHE B 331 7937 3858 5602 855 -1549 358 C ATOM 4402 CE1 PHE B 331 -0.383 16.280 -30.093 1.00 49.11 C ANISOU 4402 CE1 PHE B 331 8908 3621 6132 793 -1884 460 C ATOM 4403 CE2 PHE B 331 -0.767 13.965 -30.544 1.00 45.37 C ANISOU 4403 CE2 PHE B 331 7862 3743 5636 839 -1660 532 C ATOM 4404 CZ PHE B 331 -0.649 15.266 -30.991 1.00 47.11 C ANISOU 4404 CZ PHE B 331 8354 3641 5905 809 -1824 590 C ATOM 4405 N CYS B 332 -3.088 12.972 -26.182 1.00 68.38 N ANISOU 4405 N CYS B 332 10634 6983 8364 1461 -1109 -109 N ATOM 4406 CA CYS B 332 -4.203 12.288 -26.828 1.00 68.90 C ANISOU 4406 CA CYS B 332 10384 7251 8543 1635 -1026 -29 C ATOM 4407 C CYS B 332 -5.388 12.009 -25.905 1.00 71.06 C ANISOU 4407 C CYS B 332 10528 7649 8822 1935 -827 -175 C ATOM 4408 O CYS B 332 -6.380 11.421 -26.331 1.00 72.03 O ANISOU 4408 O CYS B 332 10411 7886 9069 2132 -777 -125 O ATOM 4409 CB CYS B 332 -3.722 10.984 -27.467 1.00 79.58 C ANISOU 4409 CB CYS B 332 11475 8884 9875 1405 -1003 119 C ATOM 4410 SG CYS B 332 -2.957 9.823 -26.316 1.00 77.36 S ANISOU 4410 SG CYS B 332 11134 8832 9425 1224 -862 52 S ATOM 4411 N TYR B 333 -5.289 12.423 -24.646 1.00 75.36 N ANISOU 4411 N TYR B 333 11226 8184 9225 1966 -714 -350 N ATOM 4412 CA TYR B 333 -6.376 12.186 -23.696 1.00 77.04 C ANISOU 4412 CA TYR B 333 11315 8550 9409 2235 -489 -489 C ATOM 4413 C TYR B 333 -7.192 13.437 -23.380 1.00 79.80 C ANISOU 4413 C TYR B 333 11835 8665 9822 2587 -459 -643 C ATOM 4414 O TYR B 333 -8.311 13.344 -22.874 1.00 81.33 O ANISOU 4414 O TYR B 333 11849 8995 10059 2871 -274 -717 O ATOM 4415 CB TYR B 333 -5.854 11.545 -22.407 1.00 77.77 C ANISOU 4415 CB TYR B 333 11466 8797 9288 2111 -352 -595 C ATOM 4416 CG TYR B 333 -5.981 10.040 -22.390 1.00 76.19 C ANISOU 4416 CG TYR B 333 10940 8945 9065 1971 -237 -476 C ATOM 4417 CD1 TYR B 333 -7.197 9.434 -22.104 1.00 77.10 C ANISOU 4417 CD1 TYR B 333 10785 9302 9209 2158 -25 -492 C ATOM 4418 CD2 TYR B 333 -4.890 9.225 -22.662 1.00 73.71 C ANISOU 4418 CD2 TYR B 333 10585 8712 8712 1653 -338 -341 C ATOM 4419 CE1 TYR B 333 -7.324 8.061 -22.087 1.00 75.63 C ANISOU 4419 CE1 TYR B 333 10321 9407 9010 2012 68 -375 C ATOM 4420 CE2 TYR B 333 -5.008 7.847 -22.648 1.00 72.39 C ANISOU 4420 CE2 TYR B 333 10147 8827 8532 1535 -240 -237 C ATOM 4421 CZ TYR B 333 -6.228 7.271 -22.359 1.00 73.38 C ANISOU 4421 CZ TYR B 333 10031 9167 8685 1705 -45 -253 C ATOM 4422 OH TYR B 333 -6.356 5.901 -22.341 1.00 71.97 O ANISOU 4422 OH TYR B 333 9602 9244 8501 1570 41 -141 O ATOM 4423 N ILE B 334 -6.632 14.604 -23.677 1.00 66.69 N ANISOU 4423 N ILE B 334 10516 6649 8174 2572 -635 -688 N ATOM 4424 CA ILE B 334 -7.355 15.855 -23.484 1.00 69.38 C ANISOU 4424 CA ILE B 334 11053 6714 8595 2917 -631 -829 C ATOM 4425 C ILE B 334 -8.269 16.124 -24.675 1.00 70.34 C ANISOU 4425 C ILE B 334 10972 6804 8951 3117 -711 -680 C ATOM 4426 O ILE B 334 -7.821 16.129 -25.822 1.00 69.36 O ANISOU 4426 O ILE B 334 10857 6587 8912 2940 -913 -496 O ATOM 4427 CB ILE B 334 -6.396 17.045 -23.290 1.00 67.43 C ANISOU 4427 CB ILE B 334 11275 6056 8288 2818 -813 -927 C ATOM 4428 CG1 ILE B 334 -5.540 16.846 -22.038 1.00 66.80 C ANISOU 4428 CG1 ILE B 334 11411 6004 7966 2632 -756 -1090 C ATOM 4429 CG2 ILE B 334 -7.172 18.348 -23.193 1.00 70.36 C ANISOU 4429 CG2 ILE B 334 11864 6106 8765 3199 -821 -1069 C ATOM 4430 CD1 ILE B 334 -4.671 18.037 -21.699 1.00 67.57 C ANISOU 4430 CD1 ILE B 334 11985 5694 7995 2542 -933 -1220 C ATOM 4431 N SER B 335 -9.551 16.342 -24.396 1.00165.17 N ANISOU 4431 N SER B 335 22792 18908 21058 3487 -551 -753 N ATOM 4432 CA SER B 335 -10.535 16.595 -25.444 1.00166.11 C ANISOU 4432 CA SER B 335 22683 19026 21406 3711 -628 -612 C ATOM 4433 C SER B 335 -10.247 17.901 -26.178 1.00167.42 C ANISOU 4433 C SER B 335 23170 18760 21682 3820 -853 -592 C ATOM 4434 O SER B 335 -9.555 18.776 -25.657 1.00168.45 O ANISOU 4434 O SER B 335 23696 18577 21732 3837 -891 -749 O ATOM 4435 CB SER B 335 -11.949 16.621 -24.860 1.00182.69 C ATOM 4436 OG SER B 335 -12.916 16.831 -25.874 1.00182.69 O ATOM 4437 N ASP B 336 -10.788 18.024 -27.386 1.00132.43 N ANISOU 4437 N ASP B 336 18582 14308 17428 3883 -1013 -393 N ATOM 4438 CA ASP B 336 -10.547 19.189 -28.234 1.00133.61 C ANISOU 4438 CA ASP B 336 19018 14054 17693 3975 -1246 -324 C ATOM 4439 C ASP B 336 -10.991 20.495 -27.580 1.00136.74 C ANISOU 4439 C ASP B 336 19624 14162 18169 4406 -1181 -523 C ATOM 4440 O ASP B 336 -10.264 21.488 -27.606 1.00137.91 O ANISOU 4440 O ASP B 336 20175 13889 18335 4436 -1333 -570 O ATOM 4441 CB ASP B 336 -11.245 19.019 -29.585 1.00100.64 C ANISOU 4441 CB ASP B 336 14596 9963 13681 3994 -1417 -65 C ATOM 4442 CG ASP B 336 -10.719 17.831 -30.368 1.00 97.65 C ANISOU 4442 CG ASP B 336 13928 9944 13230 3653 -1419 97 C ATOM 4443 OD1 ASP B 336 -10.271 16.851 -29.734 1.00 96.54 O ANISOU 4443 OD1 ASP B 336 13701 10033 12949 3470 -1254 9 O ATOM 4444 OD2 ASP B 336 -10.752 17.877 -31.616 1.00 96.40 O ANISOU 4444 OD2 ASP B 336 13646 9832 13150 3575 -1592 311 O ATOM 4445 N GLU B 337 -12.184 20.488 -26.995 1.00127.21 N ANISOU 4445 N GLU B 337 18142 13178 17011 4738 -948 -639 N ATOM 4446 CA GLU B 337 -12.725 21.682 -26.356 1.00130.32 C ANISOU 4446 CA GLU B 337 18697 13341 17477 5195 -837 -849 C ATOM 4447 C GLU B 337 -11.998 22.013 -25.057 1.00130.94 C ANISOU 4447 C GLU B 337 19182 13225 17342 5145 -727 -1124 C ATOM 4448 O GLU B 337 -12.004 23.160 -24.608 1.00133.48 O ANISOU 4448 O GLU B 337 19822 13206 17688 5443 -711 -1315 O ATOM 4449 CB GLU B 337 -14.226 21.527 -26.100 1.00237.82 C ATOM 4450 CG GLU B 337 -15.065 21.448 -27.364 1.00237.82 C ATOM 4451 CD GLU B 337 -16.553 21.421 -27.076 1.00237.82 C ATOM 4452 OE1 GLU B 337 -16.929 21.338 -25.888 1.00237.82 O ATOM 4453 OE2 GLU B 337 -17.346 21.486 -28.039 1.00237.82 O ATOM 4454 N GLN B 338 -11.371 21.007 -24.456 1.00135.08 N ANISOU 4454 N GLN B 338 19708 13961 17657 4770 -664 -1144 N ATOM 4455 CA GLN B 338 -10.618 21.209 -23.225 1.00135.34 C ANISOU 4455 CA GLN B 338 20109 13856 17458 4672 -580 -1389 C ATOM 4456 C GLN B 338 -9.281 21.891 -23.499 1.00134.78 C ANISOU 4456 C GLN B 338 20495 13380 17337 4375 -855 -1371 C ATOM 4457 O GLN B 338 -8.722 22.552 -22.625 1.00135.80 O ANISOU 4457 O GLN B 338 21033 13234 17330 4376 -860 -1592 O ATOM 4458 CB GLN B 338 -10.394 19.881 -22.499 1.00128.25 C ATOM 4459 CG GLN B 338 -11.661 19.243 -21.958 1.00128.25 C ATOM 4460 CD GLN B 338 -11.379 18.000 -21.135 1.00128.25 C ATOM 4461 OE1 GLN B 338 -11.171 16.915 -21.679 1.00128.25 O ATOM 4462 NE2 GLN B 338 -11.368 18.154 -19.815 1.00128.25 N ATOM 4463 N TRP B 339 -8.775 21.727 -24.717 1.00131.87 N ANISOU 4463 N TRP B 339 20056 12980 17067 4109 -1081 -1108 N ATOM 4464 CA TRP B 339 -7.511 22.344 -25.108 1.00131.25 C ANISOU 4464 CA TRP B 339 20363 12546 16960 3797 -1343 -1044 C ATOM 4465 C TRP B 339 -7.623 23.862 -25.206 1.00133.93 C ANISOU 4465 C TRP B 339 21107 12368 17414 4056 -1480 -1141 C ATOM 4466 O TRP B 339 -8.178 24.393 -26.168 1.00135.75 O ANISOU 4466 O TRP B 339 21245 12492 17841 4396 -1509 -1073 O ATOM 4467 CB TRP B 339 -7.014 21.774 -26.439 1.00 73.52 C ANISOU 4467 CB TRP B 339 12862 5349 9725 3482 -1525 -727 C ATOM 4468 CG TRP B 339 -6.264 20.487 -26.304 1.00 70.73 C ANISOU 4468 CG TRP B 339 12303 5351 9221 3090 -1471 -645 C ATOM 4469 CD1 TRP B 339 -6.724 19.235 -26.589 1.00 69.21 C ANISOU 4469 CD1 TRP B 339 11681 5586 9031 3043 -1350 -530 C ATOM 4470 CD2 TRP B 339 -4.916 20.325 -25.849 1.00 69.15 C ANISOU 4470 CD2 TRP B 339 12319 5098 8859 2695 -1550 -666 C ATOM 4471 NE1 TRP B 339 -5.747 18.303 -26.341 1.00 66.86 N ANISOU 4471 NE1 TRP B 339 11331 5490 8583 2665 -1340 -483 N ATOM 4472 CE2 TRP B 339 -4.627 18.947 -25.884 1.00 66.72 C ANISOU 4472 CE2 TRP B 339 11688 5197 8465 2451 -1461 -560 C ATOM 4473 CE3 TRP B 339 -3.926 21.212 -25.415 1.00 69.54 C ANISOU 4473 CE3 TRP B 339 12799 4789 8834 2520 -1699 -760 C ATOM 4474 CZ2 TRP B 339 -3.389 18.434 -25.503 1.00 64.58 C ANISOU 4474 CZ2 TRP B 339 11493 4999 8045 2065 -1509 -539 C ATOM 4475 CZ3 TRP B 339 -2.698 20.700 -25.035 1.00 67.39 C ANISOU 4475 CZ3 TRP B 339 12590 4605 8412 2111 -1756 -736 C ATOM 4476 CH2 TRP B 339 -2.440 19.324 -25.082 1.00 64.88 C ANISOU 4476 CH2 TRP B 339 11926 4709 8019 1900 -1658 -624 C ATOM 4477 N THR B 340 -7.092 24.555 -24.204 1.00123.65 N ANISOU 4477 N THR B 340 20257 10734 15988 3890 -1577 -1297 N ATOM 4478 CA THR B 340 -7.047 26.011 -24.221 1.00126.13 C ANISOU 4478 CA THR B 340 21026 10499 16396 4077 -1734 -1398 C ATOM 4479 C THR B 340 -5.691 26.478 -24.738 1.00124.98 C ANISOU 4479 C THR B 340 21215 10052 16218 3619 -2017 -1271 C ATOM 4480 O THR B 340 -4.802 25.663 -24.986 1.00122.26 O ANISOU 4480 O THR B 340 20710 9953 15788 3198 -2070 -1105 O ATOM 4481 CB THR B 340 -7.281 26.600 -22.818 1.00115.62 C ANISOU 4481 CB THR B 340 20001 8987 14940 4362 -1573 -1771 C ATOM 4482 OG1 THR B 340 -6.244 26.160 -21.932 1.00113.38 O ANISOU 4482 OG1 THR B 340 19869 8809 14399 4013 -1544 -1905 O ATOM 4483 CG2 THR B 340 -8.631 26.158 -22.272 1.00116.87 C ANISOU 4483 CG2 THR B 340 19814 9458 15132 4828 -1265 -1891 C ATOM 4484 N THR B 341 -5.537 27.788 -24.902 1.00123.32 N ANISOU 4484 N THR B 341 21464 9306 16085 3704 -2196 -1344 N ATOM 4485 CA THR B 341 -4.261 28.359 -25.324 1.00122.52 C ANISOU 4485 CA THR B 341 21708 8881 15962 3262 -2469 -1228 C ATOM 4486 C THR B 341 -3.203 28.109 -24.254 1.00121.33 C ANISOU 4486 C THR B 341 21721 8806 15573 2911 -2452 -1401 C ATOM 4487 O THR B 341 -2.038 27.820 -24.558 1.00119.21 O ANISOU 4487 O THR B 341 21446 8607 15240 2432 -2593 -1236 O ATOM 4488 CB THR B 341 -4.376 29.874 -25.573 1.00108.05 C ANISOU 4488 CB THR B 341 20372 6417 14266 3449 -2663 -1293 C ATOM 4489 OG1 THR B 341 -4.677 30.541 -24.341 1.00113.18 O ANISOU 4489 OG1 THR B 341 21342 6839 14824 3736 -2550 -1669 O ATOM 4490 CG2 THR B 341 -5.473 30.168 -26.588 1.00110.60 C ANISOU 4490 CG2 THR B 341 20538 6656 14830 3827 -2697 -1115 C ATOM 4491 N PHE B 342 -3.627 28.219 -22.997 1.00106.06 N ANISOU 4491 N PHE B 342 19921 6875 13502 3162 -2274 -1729 N ATOM 4492 CA PHE B 342 -2.758 27.960 -21.858 1.00105.17 C ANISOU 4492 CA PHE B 342 19988 6835 13140 2878 -2256 -1923 C ATOM 4493 C PHE B 342 -2.222 26.537 -21.889 1.00 98.52 C ANISOU 4493 C PHE B 342 18717 6534 12180 2552 -2168 -1763 C ATOM 4494 O PHE B 342 -1.033 26.315 -21.691 1.00 96.65 O ANISOU 4494 O PHE B 342 18561 6327 11834 2106 -2309 -1700 O ATOM 4495 CB PHE B 342 -3.497 28.208 -20.540 1.00114.92 C ANISOU 4495 CB PHE B 342 21409 8025 14227 3264 -2040 -2301 C ATOM 4496 CG PHE B 342 -2.781 27.667 -19.333 1.00113.35 C ANISOU 4496 CG PHE B 342 21306 8024 13735 3010 -1977 -2488 C ATOM 4497 CD1 PHE B 342 -1.690 28.335 -18.801 1.00116.96 C ANISOU 4497 CD1 PHE B 342 22224 8150 14064 2682 -2203 -2609 C ATOM 4498 CD2 PHE B 342 -3.202 26.493 -18.728 1.00108.71 C ANISOU 4498 CD2 PHE B 342 20352 7950 13001 3085 -1709 -2530 C ATOM 4499 CE1 PHE B 342 -1.031 27.840 -17.691 1.00115.99 C ANISOU 4499 CE1 PHE B 342 22189 8218 13664 2444 -2171 -2771 C ATOM 4500 CE2 PHE B 342 -2.547 25.994 -17.619 1.00107.66 C ANISOU 4500 CE2 PHE B 342 20316 7999 12588 2853 -1665 -2683 C ATOM 4501 CZ PHE B 342 -1.460 26.668 -17.100 1.00111.33 C ANISOU 4501 CZ PHE B 342 21236 8142 12919 2537 -1902 -2805 C ATOM 4502 N LEU B 343 -3.106 25.576 -22.137 1.00107.16 N ANISOU 4502 N LEU B 343 19355 8052 13310 2776 -1941 -1695 N ATOM 4503 CA LEU B 343 -2.709 24.174 -22.194 1.00104.21 C ANISOU 4503 CA LEU B 343 18571 8182 12843 2508 -1844 -1544 C ATOM 4504 C LEU B 343 -1.817 23.892 -23.399 1.00102.00 C ANISOU 4504 C LEU B 343 18155 7945 12657 2112 -2042 -1221 C ATOM 4505 O LEU B 343 -1.027 22.954 -23.387 1.00 99.43 O ANISOU 4505 O LEU B 343 17637 7910 12231 1772 -2043 -1113 O ATOM 4506 CB LEU B 343 -3.938 23.261 -22.215 1.00 98.09 C ANISOU 4506 CB LEU B 343 17347 7808 12113 2836 -1577 -1526 C ATOM 4507 CG LEU B 343 -4.731 23.168 -20.910 1.00 99.54 C ANISOU 4507 CG LEU B 343 17555 8112 12154 3168 -1312 -1819 C ATOM 4508 CD1 LEU B 343 -5.876 22.179 -21.049 1.00 99.43 C ANISOU 4508 CD1 LEU B 343 17050 8510 12218 3444 -1064 -1748 C ATOM 4509 CD2 LEU B 343 -3.819 22.779 -19.757 1.00 98.07 C ANISOU 4509 CD2 LEU B 343 17506 8063 11692 2887 -1278 -1962 C ATOM 4510 N PHE B 344 -1.952 24.717 -24.432 1.00 80.96 N ANISOU 4510 N PHE B 344 15597 4985 10180 2169 -2204 -1066 N ATOM 4511 CA PHE B 344 -1.141 24.609 -25.638 1.00 78.80 C ANISOU 4511 CA PHE B 344 15231 4719 9990 1818 -2385 -753 C ATOM 4512 C PHE B 344 0.298 25.017 -25.327 1.00 80.27 C ANISOU 4512 C PHE B 344 15715 4699 10083 1368 -2582 -742 C ATOM 4513 O PHE B 344 1.245 24.221 -25.473 1.00 75.99 O ANISOU 4513 O PHE B 344 14982 4420 9471 993 -2609 -591 O ATOM 4514 CB PHE B 344 -1.726 25.526 -26.716 1.00 86.12 C ANISOU 4514 CB PHE B 344 16250 5347 11125 2029 -2512 -604 C ATOM 4515 CG PHE B 344 -1.283 25.199 -28.115 1.00 83.88 C ANISOU 4515 CG PHE B 344 15796 5154 10919 1749 -2645 -261 C ATOM 4516 CD1 PHE B 344 -1.955 24.246 -28.863 1.00 79.48 C ANISOU 4516 CD1 PHE B 344 14806 4991 10401 1815 -2539 -91 C ATOM 4517 CD2 PHE B 344 -0.215 25.865 -28.692 1.00 86.90 C ANISOU 4517 CD2 PHE B 344 16465 5220 11332 1421 -2877 -107 C ATOM 4518 CE1 PHE B 344 -1.558 23.951 -30.152 1.00 78.05 C ANISOU 4518 CE1 PHE B 344 14496 4895 10264 1570 -2654 209 C ATOM 4519 CE2 PHE B 344 0.186 25.574 -29.982 1.00 85.43 C ANISOU 4519 CE2 PHE B 344 16130 5132 11198 1171 -2977 212 C ATOM 4520 CZ PHE B 344 -0.486 24.614 -30.712 1.00 80.99 C ANISOU 4520 CZ PHE B 344 15151 4971 10652 1254 -2861 362 C ATOM 4521 N ASP B 345 0.448 26.266 -24.891 1.00 87.81 N ANISOU 4521 N ASP B 345 17136 5181 11045 1411 -2721 -907 N ATOM 4522 CA ASP B 345 1.755 26.804 -24.530 1.00 90.54 C ANISOU 4522 CA ASP B 345 17802 5278 11320 980 -2939 -906 C ATOM 4523 C ASP B 345 2.427 25.936 -23.467 1.00 87.17 C ANISOU 4523 C ASP B 345 17280 5159 10679 747 -2866 -1035 C ATOM 4524 O ASP B 345 3.601 25.571 -23.595 1.00 85.42 O ANISOU 4524 O ASP B 345 16997 5049 10407 307 -2988 -889 O ATOM 4525 CB ASP B 345 1.616 28.244 -24.031 1.00133.31 C ANISOU 4525 CB ASP B 345 23765 10116 16771 1120 -3086 -1114 C ATOM 4526 CG ASP B 345 0.838 29.122 -24.994 1.00135.11 C ANISOU 4526 CG ASP B 345 24107 10014 17217 1408 -3159 -997 C ATOM 4527 OD1 ASP B 345 0.860 28.835 -26.210 1.00133.73 O ANISOU 4527 OD1 ASP B 345 23696 9957 17161 1295 -3212 -685 O ATOM 4528 OD2 ASP B 345 0.206 30.099 -24.538 1.00137.94 O ANISOU 4528 OD2 ASP B 345 24798 9993 17620 1758 -3164 -1218 O ATOM 4529 N PHE B 346 1.666 25.599 -22.428 1.00 83.47 N ANISOU 4529 N PHE B 346 16786 4844 10085 1053 -2662 -1295 N ATOM 4530 CA PHE B 346 2.147 24.723 -21.366 1.00 80.52 C ANISOU 4530 CA PHE B 346 16318 4785 9492 888 -2572 -1420 C ATOM 4531 C PHE B 346 2.580 23.376 -21.925 1.00 73.12 C ANISOU 4531 C PHE B 346 14901 4326 8555 652 -2503 -1166 C ATOM 4532 O PHE B 346 3.571 22.811 -21.473 1.00 71.25 O ANISOU 4532 O PHE B 346 14609 4265 8197 310 -2568 -1130 O ATOM 4533 CB PHE B 346 1.072 24.520 -20.293 1.00 84.85 C ANISOU 4533 CB PHE B 346 16874 5455 9910 1302 -2320 -1708 C ATOM 4534 CG PHE B 346 1.427 23.481 -19.263 1.00 81.17 C ANISOU 4534 CG PHE B 346 16236 5390 9216 1170 -2191 -1788 C ATOM 4535 CD1 PHE B 346 2.263 23.795 -18.203 1.00 84.25 C ANISOU 4535 CD1 PHE B 346 16938 5678 9398 932 -2310 -1963 C ATOM 4536 CD2 PHE B 346 0.919 22.193 -19.350 1.00 75.11 C ANISOU 4536 CD2 PHE B 346 15007 5092 8442 1274 -1967 -1682 C ATOM 4537 CE1 PHE B 346 2.589 22.845 -17.255 1.00 81.41 C ANISOU 4537 CE1 PHE B 346 16428 5686 8820 813 -2208 -2019 C ATOM 4538 CE2 PHE B 346 1.243 21.240 -18.405 1.00 72.16 C ANISOU 4538 CE2 PHE B 346 14490 5067 7862 1152 -1856 -1737 C ATOM 4539 CZ PHE B 346 2.078 21.566 -17.356 1.00 75.34 C ANISOU 4539 CZ PHE B 346 15202 5373 8051 929 -1977 -1900 C ATOM 4540 N TYR B 347 1.836 22.867 -22.904 1.00 72.85 N ANISOU 4540 N TYR B 347 14525 4495 8657 841 -2381 -995 N ATOM 4541 CA TYR B 347 2.184 21.596 -23.533 1.00 68.26 C ANISOU 4541 CA TYR B 347 13510 4339 8086 642 -2313 -760 C ATOM 4542 C TYR B 347 3.542 21.676 -24.213 1.00 67.22 C ANISOU 4542 C TYR B 347 13404 4144 7991 191 -2523 -536 C ATOM 4543 O TYR B 347 4.332 20.734 -24.146 1.00 64.20 O ANISOU 4543 O TYR B 347 12806 4053 7534 -90 -2516 -435 O ATOM 4544 CB TYR B 347 1.128 21.161 -24.551 1.00 69.85 C ANISOU 4544 CB TYR B 347 13393 4713 8435 908 -2187 -616 C ATOM 4545 CG TYR B 347 1.483 19.882 -25.276 1.00 65.16 C ANISOU 4545 CG TYR B 347 12387 4522 7850 707 -2127 -385 C ATOM 4546 CD1 TYR B 347 1.282 18.647 -24.674 1.00 62.92 C ANISOU 4546 CD1 TYR B 347 11807 4632 7470 755 -1935 -430 C ATOM 4547 CD2 TYR B 347 2.031 19.910 -26.554 1.00 64.41 C ANISOU 4547 CD2 TYR B 347 12217 4407 7851 470 -2256 -123 C ATOM 4548 CE1 TYR B 347 1.608 17.475 -25.325 1.00 60.22 C ANISOU 4548 CE1 TYR B 347 11116 4625 7139 584 -1884 -234 C ATOM 4549 CE2 TYR B 347 2.362 18.741 -27.213 1.00 60.53 C ANISOU 4549 CE2 TYR B 347 11372 4272 7354 305 -2189 65 C ATOM 4550 CZ TYR B 347 2.148 17.526 -26.593 1.00 58.82 C ANISOU 4550 CZ TYR B 347 10878 4418 7054 369 -2008 2 C ATOM 4551 OH TYR B 347 2.476 16.357 -27.242 1.00 55.91 O ANISOU 4551 OH TYR B 347 10184 4375 6686 217 -1945 176 O ATOM 4552 N HIS B 348 3.815 22.797 -24.873 1.00 85.73 N ANISOU 4552 N HIS B 348 16014 6105 10456 122 -2707 -451 N ATOM 4553 CA HIS B 348 5.090 22.924 -25.580 1.00 84.43 C ANISOU 4553 CA HIS B 348 15851 5890 10339 -310 -2891 -206 C ATOM 4554 C HIS B 348 6.296 23.208 -24.669 1.00 84.13 C ANISOU 4554 C HIS B 348 16030 5741 10194 -682 -3056 -279 C ATOM 4555 O HIS B 348 7.390 22.666 -24.886 1.00 82.26 O ANISOU 4555 O HIS B 348 15644 5651 9960 -1062 -3144 -80 O ATOM 4556 CB HIS B 348 4.978 23.930 -26.726 1.00 72.24 C ANISOU 4556 CB HIS B 348 14481 4006 8961 -287 -3029 -36 C ATOM 4557 CG HIS B 348 4.023 23.504 -27.797 1.00 69.41 C ANISOU 4557 CG HIS B 348 13841 3831 8703 -27 -2907 116 C ATOM 4558 ND1 HIS B 348 2.661 23.685 -27.693 1.00 69.86 N ANISOU 4558 ND1 HIS B 348 13885 3844 8813 429 -2791 -20 N ATOM 4559 CD2 HIS B 348 4.230 22.879 -28.981 1.00 66.55 C ANISOU 4559 CD2 HIS B 348 13188 3710 8386 -163 -2886 387 C ATOM 4560 CE1 HIS B 348 2.071 23.203 -28.773 1.00 67.40 C ANISOU 4560 CE1 HIS B 348 13289 3736 8585 546 -2728 169 C ATOM 4561 NE2 HIS B 348 3.001 22.709 -29.570 1.00 65.38 N ANISOU 4561 NE2 HIS B 348 12878 3650 8315 194 -2783 410 N ATOM 4562 N TYR B 349 6.102 24.038 -23.648 1.00 76.81 N ANISOU 4562 N TYR B 349 15450 4568 9169 -575 -3100 -562 N ATOM 4563 CA TYR B 349 7.159 24.247 -22.659 1.00 79.44 C ANISOU 4563 CA TYR B 349 15971 4846 9367 -920 -3259 -658 C ATOM 4564 C TYR B 349 7.455 22.933 -21.932 1.00 74.21 C ANISOU 4564 C TYR B 349 14979 4665 8553 -993 -3123 -678 C ATOM 4565 O TYR B 349 8.614 22.591 -21.664 1.00 73.88 O ANISOU 4565 O TYR B 349 14834 4780 8457 -1369 -3239 -573 O ATOM 4566 CB TYR B 349 6.774 25.340 -21.656 1.00 83.53 C ANISOU 4566 CB TYR B 349 16988 4953 9796 -771 -3345 -979 C ATOM 4567 CG TYR B 349 6.757 26.741 -22.232 1.00 90.10 C ANISOU 4567 CG TYR B 349 18220 5243 10771 -812 -3552 -955 C ATOM 4568 CD1 TYR B 349 7.914 27.319 -22.737 1.00 93.61 C ANISOU 4568 CD1 TYR B 349 18805 5485 11278 -1278 -3812 -780 C ATOM 4569 CD2 TYR B 349 5.589 27.493 -22.251 1.00 93.28 C ANISOU 4569 CD2 TYR B 349 18854 5333 11255 -385 -3490 -1098 C ATOM 4570 CE1 TYR B 349 7.905 28.600 -23.260 1.00 99.99 C ANISOU 4570 CE1 TYR B 349 19996 5777 12220 -1335 -4010 -742 C ATOM 4571 CE2 TYR B 349 5.570 28.775 -22.771 1.00 99.70 C ANISOU 4571 CE2 TYR B 349 20051 5622 12206 -410 -3690 -1067 C ATOM 4572 CZ TYR B 349 6.731 29.324 -23.274 1.00102.98 C ANISOU 4572 CZ TYR B 349 20625 5828 12675 -895 -3952 -887 C ATOM 4573 OH TYR B 349 6.717 30.600 -23.793 1.00109.72 O ANISOU 4573 OH TYR B 349 21879 6140 13670 -938 -4158 -841 O ATOM 4574 N PHE B 350 6.393 22.192 -21.631 1.00 68.18 N ANISOU 4574 N PHE B 350 14038 4135 7730 -627 -2879 -797 N ATOM 4575 CA PHE B 350 6.522 20.891 -20.989 1.00 63.23 C ANISOU 4575 CA PHE B 350 13102 3954 6968 -640 -2726 -808 C ATOM 4576 C PHE B 350 7.194 19.906 -21.933 1.00 58.56 C ANISOU 4576 C PHE B 350 12111 3680 6461 -900 -2725 -508 C ATOM 4577 O PHE B 350 7.858 18.970 -21.492 1.00 56.44 O ANISOU 4577 O PHE B 350 11655 3693 6095 -1101 -2724 -461 O ATOM 4578 CB PHE B 350 5.151 20.366 -20.559 1.00 74.11 C ANISOU 4578 CB PHE B 350 14329 5517 8313 -201 -2453 -938 C ATOM 4579 CG PHE B 350 5.211 19.174 -19.650 1.00 72.52 C ANISOU 4579 CG PHE B 350 13922 5698 7933 -188 -2300 -1009 C ATOM 4580 CD1 PHE B 350 5.846 19.256 -18.422 1.00 71.70 C ANISOU 4580 CD1 PHE B 350 13935 5650 7657 -464 -2422 -1072 C ATOM 4581 CD2 PHE B 350 4.616 17.978 -20.014 1.00 71.98 C ANISOU 4581 CD2 PHE B 350 13545 5931 7871 89 -2048 -998 C ATOM 4582 CE1 PHE B 350 5.899 18.164 -17.582 1.00 70.26 C ANISOU 4582 CE1 PHE B 350 13578 5812 7303 -450 -2293 -1118 C ATOM 4583 CE2 PHE B 350 4.663 16.884 -19.177 1.00 70.56 C ANISOU 4583 CE2 PHE B 350 13191 6088 7528 89 -1909 -1044 C ATOM 4584 CZ PHE B 350 5.306 16.976 -17.960 1.00 69.63 C ANISOU 4584 CZ PHE B 350 13206 6018 7231 -173 -2030 -1101 C ATOM 4585 N TYR B 351 7.014 20.117 -23.234 1.00 70.07 N ANISOU 4585 N TYR B 351 13447 5087 8090 -881 -2725 -305 N ATOM 4586 CA TYR B 351 7.705 19.314 -24.233 1.00 67.54 C ANISOU 4586 CA TYR B 351 12783 5034 7846 -1120 -2719 -23 C ATOM 4587 C TYR B 351 9.200 19.555 -24.102 1.00 66.80 C ANISOU 4587 C TYR B 351 12733 4924 7726 -1562 -2915 79 C ATOM 4588 O TYR B 351 9.993 18.604 -24.042 1.00 64.51 O ANISOU 4588 O TYR B 351 12152 4960 7400 -1749 -2883 195 O ATOM 4589 CB TYR B 351 7.227 19.667 -25.642 1.00 63.66 C ANISOU 4589 CB TYR B 351 12257 4415 7517 -1053 -2727 165 C ATOM 4590 CG TYR B 351 7.957 18.933 -26.744 1.00 61.22 C ANISOU 4590 CG TYR B 351 11610 4386 7267 -1261 -2692 444 C ATOM 4591 CD1 TYR B 351 7.533 17.680 -27.167 1.00 59.40 C ANISOU 4591 CD1 TYR B 351 11038 4492 7042 -1088 -2500 508 C ATOM 4592 CD2 TYR B 351 9.065 19.496 -27.367 1.00 60.87 C ANISOU 4592 CD2 TYR B 351 11591 4266 7270 -1633 -2844 642 C ATOM 4593 CE1 TYR B 351 8.194 17.005 -28.176 1.00 57.11 C ANISOU 4593 CE1 TYR B 351 10466 4445 6789 -1260 -2457 740 C ATOM 4594 CE2 TYR B 351 9.734 18.830 -28.376 1.00 58.82 C ANISOU 4594 CE2 TYR B 351 11024 4274 7050 -1803 -2784 888 C ATOM 4595 CZ TYR B 351 9.294 17.585 -28.777 1.00 56.87 C ANISOU 4595 CZ TYR B 351 10465 4348 6794 -1605 -2589 926 C ATOM 4596 OH TYR B 351 9.955 16.916 -29.780 1.00 54.79 O ANISOU 4596 OH TYR B 351 9923 4340 6555 -1758 -2521 1149 O ATOM 4597 N MET B 352 9.570 20.834 -24.053 1.00 86.12 N ANISOU 4597 N MET B 352 15542 6980 10201 -1724 -3125 36 N ATOM 4598 CA MET B 352 10.958 21.225 -23.818 1.00 86.04 C ANISOU 4598 CA MET B 352 15606 6908 10177 -2165 -3344 124 C ATOM 4599 C MET B 352 11.521 20.508 -22.595 1.00 84.97 C ANISOU 4599 C MET B 352 15400 7010 9876 -2258 -3354 -6 C ATOM 4600 O MET B 352 12.567 19.857 -22.673 1.00 83.11 O ANISOU 4600 O MET B 352 14911 7030 9637 -2548 -3409 154 O ATOM 4601 CB MET B 352 11.070 22.739 -23.624 1.00 73.61 C ANISOU 4601 CB MET B 352 14504 4826 8638 -2283 -3573 33 C ATOM 4602 CG MET B 352 10.710 23.568 -24.846 1.00 75.70 C ANISOU 4602 CG MET B 352 14873 4816 9071 -2252 -3613 202 C ATOM 4603 SD MET B 352 10.812 25.339 -24.512 1.00 84.43 S ANISOU 4603 SD MET B 352 16586 5272 10221 -2344 -3881 67 S ATOM 4604 CE MET B 352 10.474 26.017 -26.135 1.00 86.13 C ANISOU 4604 CE MET B 352 16808 5280 10638 -2374 -3918 374 C ATOM 4605 N LEU B 353 10.807 20.613 -21.476 1.00 68.62 N ANISOU 4605 N LEU B 353 13542 4868 7662 -1998 -3291 -287 N ATOM 4606 CA LEU B 353 11.246 19.997 -20.222 1.00 68.62 C ANISOU 4606 CA LEU B 353 13521 5081 7471 -2075 -3308 -419 C ATOM 4607 C LEU B 353 11.438 18.482 -20.324 1.00 62.91 C ANISOU 4607 C LEU B 353 12331 4839 6733 -2068 -3144 -266 C ATOM 4608 O LEU B 353 12.526 17.964 -20.049 1.00 63.34 O ANISOU 4608 O LEU B 353 12215 5100 6751 -2353 -3249 -155 O ATOM 4609 CB LEU B 353 10.262 20.321 -19.094 1.00 69.16 C ANISOU 4609 CB LEU B 353 13891 5018 7369 -1753 -3219 -746 C ATOM 4610 CG LEU B 353 10.571 19.700 -17.730 1.00 70.66 C ANISOU 4610 CG LEU B 353 14155 5372 7318 -1847 -3268 -904 C ATOM 4611 CD1 LEU B 353 11.932 20.159 -17.227 1.00 76.39 C ANISOU 4611 CD1 LEU B 353 15098 5924 8001 -2279 -3592 -894 C ATOM 4612 CD2 LEU B 353 9.480 20.043 -16.728 1.00 72.40 C ANISOU 4612 CD2 LEU B 353 14663 5490 7355 -1492 -3128 -1223 C ATOM 4613 N THR B 354 10.377 17.782 -20.718 1.00 65.06 N ANISOU 4613 N THR B 354 12397 5279 7042 -1742 -2898 -257 N ATOM 4614 CA THR B 354 10.390 16.324 -20.800 1.00 62.31 C ANISOU 4614 CA THR B 354 11642 5351 6682 -1691 -2727 -137 C ATOM 4615 C THR B 354 11.478 15.799 -21.726 1.00 60.31 C ANISOU 4615 C THR B 354 11084 5283 6549 -1982 -2788 144 C ATOM 4616 O THR B 354 12.229 14.896 -21.356 1.00 58.46 O ANISOU 4616 O THR B 354 10619 5329 6265 -2120 -2791 226 O ATOM 4617 CB THR B 354 9.034 15.766 -21.272 1.00 57.22 C ANISOU 4617 CB THR B 354 10833 4814 6092 -1322 -2476 -152 C ATOM 4618 OG1 THR B 354 8.692 16.341 -22.540 1.00 57.82 O ANISOU 4618 OG1 THR B 354 10886 4739 6341 -1296 -2485 -13 O ATOM 4619 CG2 THR B 354 7.947 16.079 -20.260 1.00 59.36 C ANISOU 4619 CG2 THR B 354 11351 4955 6248 -1008 -2376 -421 C ATOM 4620 N ASN B 355 11.562 16.360 -22.929 1.00 62.58 N ANISOU 4620 N ASN B 355 11371 5418 6988 -2066 -2832 297 N ATOM 4621 CA ASN B 355 12.581 15.920 -23.877 1.00 60.98 C ANISOU 4621 CA ASN B 355 10873 5403 6891 -2324 -2855 566 C ATOM 4622 C ASN B 355 13.998 16.247 -23.399 1.00 61.46 C ANISOU 4622 C ASN B 355 10959 5455 6936 -2716 -3079 638 C ATOM 4623 O ASN B 355 14.939 15.475 -23.630 1.00 60.26 O ANISOU 4623 O ASN B 355 10493 5579 6824 -2905 -3076 819 O ATOM 4624 CB ASN B 355 12.310 16.492 -25.269 1.00 60.70 C ANISOU 4624 CB ASN B 355 10843 5222 6998 -2314 -2834 722 C ATOM 4625 CG ASN B 355 11.176 15.776 -25.982 1.00 59.58 C ANISOU 4625 CG ASN B 355 10529 5220 6888 -1986 -2613 732 C ATOM 4626 OD1 ASN B 355 11.404 15.007 -26.914 1.00 57.71 O ANISOU 4626 OD1 ASN B 355 10015 5200 6712 -2015 -2511 914 O ATOM 4627 ND2 ASN B 355 9.947 16.016 -25.538 1.00 60.89 N ANISOU 4627 ND2 ASN B 355 10856 5269 7011 -1673 -2537 532 N ATOM 4628 N ALA B 356 14.143 17.383 -22.719 1.00 58.53 N ANISOU 4628 N ALA B 356 10960 4768 6511 -2832 -3277 491 N ATOM 4629 CA ALA B 356 15.413 17.721 -22.085 1.00 63.31 C ANISOU 4629 CA ALA B 356 11614 5358 7083 -3210 -3520 527 C ATOM 4630 C ALA B 356 15.805 16.628 -21.095 1.00 61.70 C ANISOU 4630 C ALA B 356 11205 5488 6751 -3204 -3494 486 C ATOM 4631 O ALA B 356 16.958 16.194 -21.058 1.00 63.04 O ANISOU 4631 O ALA B 356 11127 5873 6952 -3472 -3593 652 O ATOM 4632 CB ALA B 356 15.327 19.069 -21.387 1.00 72.16 C ANISOU 4632 CB ALA B 356 13218 6061 8137 -3297 -3735 326 C ATOM 4633 N LEU B 357 14.835 16.181 -20.302 1.00 61.62 N ANISOU 4633 N LEU B 357 11286 5528 6601 -2891 -3353 281 N ATOM 4634 CA LEU B 357 15.062 15.086 -19.362 1.00 60.19 C ANISOU 4634 CA LEU B 357 10923 5662 6286 -2852 -3308 253 C ATOM 4635 C LEU B 357 15.412 13.788 -20.087 1.00 56.05 C ANISOU 4635 C LEU B 357 9930 5497 5869 -2838 -3155 486 C ATOM 4636 O LEU B 357 16.189 12.974 -19.583 1.00 56.51 O ANISOU 4636 O LEU B 357 9774 5813 5887 -2957 -3205 572 O ATOM 4637 CB LEU B 357 13.839 14.874 -18.468 1.00 72.81 C ANISOU 4637 CB LEU B 357 12703 7249 7713 -2509 -3150 6 C ATOM 4638 CG LEU B 357 13.613 15.905 -17.362 1.00 77.30 C ANISOU 4638 CG LEU B 357 13734 7535 8104 -2513 -3295 -263 C ATOM 4639 CD1 LEU B 357 12.389 15.543 -16.539 1.00 75.97 C ANISOU 4639 CD1 LEU B 357 13688 7416 7764 -2150 -3086 -485 C ATOM 4640 CD2 LEU B 357 14.845 16.017 -16.478 1.00 81.27 C ANISOU 4640 CD2 LEU B 357 14302 8086 8492 -2855 -3565 -254 C ATOM 4641 N VAL B 358 14.829 13.597 -21.267 1.00 66.25 N ANISOU 4641 N VAL B 358 11080 6799 7294 -2684 -2978 584 N ATOM 4642 CA VAL B 358 15.141 12.435 -22.092 1.00 63.84 C ANISOU 4642 CA VAL B 358 10367 6801 7090 -2661 -2826 789 C ATOM 4643 C VAL B 358 16.617 12.438 -22.477 1.00 63.98 C ANISOU 4643 C VAL B 358 10170 6937 7204 -3004 -2968 1008 C ATOM 4644 O VAL B 358 17.303 11.417 -22.367 1.00 62.59 O ANISOU 4644 O VAL B 358 9690 7052 7042 -3050 -2935 1126 O ATOM 4645 CB VAL B 358 14.276 12.395 -23.368 1.00 55.65 C ANISOU 4645 CB VAL B 358 9261 5721 6162 -2464 -2643 849 C ATOM 4646 CG1 VAL B 358 14.792 11.340 -24.334 1.00 53.50 C ANISOU 4646 CG1 VAL B 358 8604 5732 5990 -2499 -2516 1067 C ATOM 4647 CG2 VAL B 358 12.819 12.141 -23.016 1.00 55.41 C ANISOU 4647 CG2 VAL B 358 9332 5661 6058 -2108 -2475 666 C ATOM 4648 N TYR B 359 17.111 13.591 -22.917 1.00 54.51 N ANISOU 4648 N TYR B 359 9122 5510 6078 -3245 -3126 1070 N ATOM 4649 CA TYR B 359 18.527 13.701 -23.263 1.00 58.04 C ANISOU 4649 CA TYR B 359 9351 6074 6626 -3596 -3260 1292 C ATOM 4650 C TYR B 359 19.431 13.603 -22.032 1.00 61.77 C ANISOU 4650 C TYR B 359 9818 6636 7017 -3811 -3478 1260 C ATOM 4651 O TYR B 359 20.571 13.134 -22.123 1.00 63.66 O ANISOU 4651 O TYR B 359 9746 7110 7329 -4023 -3545 1448 O ATOM 4652 CB TYR B 359 18.801 14.974 -24.064 1.00 80.87 C ANISOU 4652 CB TYR B 359 12408 8695 9621 -3823 -3372 1391 C ATOM 4653 CG TYR B 359 18.200 14.933 -25.450 1.00 80.12 C ANISOU 4653 CG TYR B 359 12248 8579 9612 -3660 -3171 1493 C ATOM 4654 CD1 TYR B 359 18.667 14.032 -26.401 1.00 78.48 C ANISOU 4654 CD1 TYR B 359 11665 8676 9478 -3635 -2990 1687 C ATOM 4655 CD2 TYR B 359 17.152 15.774 -25.803 1.00 81.25 C ANISOU 4655 CD2 TYR B 359 12716 8399 9757 -3516 -3167 1390 C ATOM 4656 CE1 TYR B 359 18.117 13.982 -27.668 1.00 77.93 C ANISOU 4656 CE1 TYR B 359 11557 8594 9459 -3495 -2820 1774 C ATOM 4657 CE2 TYR B 359 16.596 15.730 -27.068 1.00 80.74 C ANISOU 4657 CE2 TYR B 359 12595 8323 9759 -3371 -3008 1494 C ATOM 4658 CZ TYR B 359 17.083 14.833 -27.995 1.00 79.03 C ANISOU 4658 CZ TYR B 359 12015 8418 9592 -3371 -2839 1684 C ATOM 4659 OH TYR B 359 16.534 14.786 -29.255 1.00 78.62 O ANISOU 4659 OH TYR B 359 11929 8361 9579 -3236 -2694 1782 O ATOM 4660 N VAL B 360 18.915 14.037 -20.883 1.00 69.86 N ANISOU 4660 N VAL B 360 11179 7483 7882 -3744 -3587 1022 N ATOM 4661 CA VAL B 360 19.609 13.836 -19.614 1.00 70.99 C ANISOU 4661 CA VAL B 360 11346 7728 7900 -3905 -3789 966 C ATOM 4662 C VAL B 360 19.792 12.341 -19.368 1.00 68.52 C ANISOU 4662 C VAL B 360 10678 7794 7563 -3758 -3655 1053 C ATOM 4663 O VAL B 360 20.860 11.895 -18.945 1.00 70.27 O ANISOU 4663 O VAL B 360 10673 8226 7798 -3955 -3797 1183 O ATOM 4664 CB VAL B 360 18.845 14.471 -18.430 1.00 67.09 C ANISOU 4664 CB VAL B 360 11310 6986 7198 -3803 -3884 667 C ATOM 4665 CG1 VAL B 360 19.422 14.003 -17.102 1.00 69.70 C ANISOU 4665 CG1 VAL B 360 11640 7491 7352 -3895 -4042 606 C ATOM 4666 CG2 VAL B 360 18.883 15.988 -18.523 1.00 71.88 C ANISOU 4666 CG2 VAL B 360 12290 7194 7827 -4010 -4088 582 C ATOM 4667 N SER B 361 18.745 11.571 -19.651 1.00 64.36 N ANISOU 4667 N SER B 361 10098 7345 7012 -3413 -3390 991 N ATOM 4668 CA SER B 361 18.822 10.117 -19.557 1.00 62.12 C ANISOU 4668 CA SER B 361 9490 7386 6727 -3254 -3240 1082 C ATOM 4669 C SER B 361 19.822 9.574 -20.569 1.00 61.43 C ANISOU 4669 C SER B 361 8994 7517 6829 -3380 -3195 1346 C ATOM 4670 O SER B 361 20.506 8.584 -20.313 1.00 60.66 O ANISOU 4670 O SER B 361 8610 7686 6754 -3382 -3190 1465 O ATOM 4671 CB SER B 361 17.451 9.485 -19.799 1.00 92.65 C ANISOU 4671 CB SER B 361 13386 11262 10554 -2888 -2966 973 C ATOM 4672 OG SER B 361 17.532 8.070 -19.803 1.00 90.52 O ANISOU 4672 OG SER B 361 12801 11279 10316 -2750 -2816 1083 O ATOM 4673 N ALA B 362 19.900 10.227 -21.722 1.00 61.53 N ANISOU 4673 N ALA B 362 8990 7415 6975 -3475 -3158 1441 N ATOM 4674 CA ALA B 362 20.823 9.806 -22.769 1.00 61.62 C ANISOU 4674 CA ALA B 362 8630 7632 7154 -3592 -3086 1687 C ATOM 4675 C ALA B 362 22.272 10.162 -22.441 1.00 65.55 C ANISOU 4675 C ALA B 362 8969 8222 7717 -3952 -3325 1842 C ATOM 4676 O ALA B 362 23.198 9.676 -23.091 1.00 66.18 O ANISOU 4676 O ALA B 362 8684 8534 7929 -4048 -3271 2055 O ATOM 4677 CB ALA B 362 20.418 10.412 -24.107 1.00 77.31 C ANISOU 4677 CB ALA B 362 10663 9478 9234 -3575 -2957 1749 C ATOM 4678 N ALA B 363 22.467 11.007 -21.432 1.00 78.03 N ANISOU 4678 N ALA B 363 10818 9625 9204 -4151 -3588 1732 N ATOM 4679 CA ALA B 363 23.810 11.469 -21.087 1.00 81.31 C ANISOU 4679 CA ALA B 363 11104 10107 9683 -4532 -3856 1874 C ATOM 4680 C ALA B 363 24.254 11.110 -19.665 1.00 83.06 C ANISOU 4680 C ALA B 363 11325 10455 9780 -4598 -4070 1816 C ATOM 4681 O ALA B 363 25.378 11.418 -19.269 1.00 86.58 O ANISOU 4681 O ALA B 363 11598 11016 10283 -4901 -4303 1953 O ATOM 4682 CB ALA B 363 23.918 12.971 -21.308 1.00 73.67 C ANISOU 4682 CB ALA B 363 10442 8811 8739 -4815 -4044 1843 C ATOM 4683 N ILE B 364 23.380 10.457 -18.905 1.00 70.19 N ANISOU 4683 N ILE B 364 9878 8816 7975 -4324 -3994 1627 N ATOM 4684 CA ILE B 364 23.653 10.189 -17.492 1.00 73.02 C ANISOU 4684 CA ILE B 364 10326 9256 8162 -4378 -4204 1545 C ATOM 4685 C ILE B 364 24.571 8.983 -17.246 1.00 73.68 C ANISOU 4685 C ILE B 364 9986 9703 8308 -4375 -4229 1744 C ATOM 4686 O ILE B 364 25.416 9.015 -16.350 1.00 78.24 O ANISOU 4686 O ILE B 364 10528 10377 8820 -4580 -4502 1786 O ATOM 4687 CB ILE B 364 22.340 10.044 -16.674 1.00 69.35 C ANISOU 4687 CB ILE B 364 10222 8662 7467 -4090 -4102 1279 C ATOM 4688 CG1 ILE B 364 22.642 9.828 -15.189 1.00 73.17 C ANISOU 4688 CG1 ILE B 364 10861 9209 7731 -4178 -4338 1186 C ATOM 4689 CG2 ILE B 364 21.477 8.916 -17.218 1.00 63.40 C ANISOU 4689 CG2 ILE B 364 9287 8059 6741 -3725 -3770 1295 C ATOM 4690 CD1 ILE B 364 23.385 10.980 -14.541 1.00 79.64 C ANISOU 4690 CD1 ILE B 364 11900 9861 8498 -4554 -4696 1142 C ATOM 4691 N ASN B 365 24.415 7.937 -18.052 1.00 70.30 N ANISOU 4691 N ASN B 365 9244 9463 8003 -4143 -3959 1866 N ATOM 4692 CA ASN B 365 25.117 6.669 -17.826 1.00 70.54 C ANISOU 4692 CA ASN B 365 8896 9814 8094 -4062 -3944 2035 C ATOM 4693 C ASN B 365 26.654 6.704 -17.729 1.00 75.92 C ANISOU 4693 C ASN B 365 9242 10696 8909 -4361 -4185 2260 C ATOM 4694 O ASN B 365 27.216 6.116 -16.804 1.00 78.57 O ANISOU 4694 O ASN B 365 9473 11199 9182 -4393 -4367 2315 O ATOM 4695 CB ASN B 365 24.658 5.603 -18.831 1.00 92.35 C ANISOU 4695 CB ASN B 365 11411 12703 10973 -3758 -3603 2109 C ATOM 4696 CG ASN B 365 23.198 5.241 -18.666 1.00 90.29 C ANISOU 4696 CG ASN B 365 11413 12319 10573 -3448 -3395 1912 C ATOM 4697 OD1 ASN B 365 22.424 5.279 -19.622 1.00 89.09 O ANISOU 4697 OD1 ASN B 365 11339 12046 10464 -3313 -3186 1851 O ATOM 4698 ND2 ASN B 365 22.813 4.887 -17.445 1.00 89.97 N ANISOU 4698 ND2 ASN B 365 11503 12322 10361 -3341 -3457 1823 N ATOM 4699 N PRO B 366 27.339 7.378 -18.675 1.00 76.40 N ANISOU 4699 N PRO B 366 9120 10755 9153 -4582 -4190 2405 N ATOM 4700 CA PRO B 366 28.805 7.407 -18.578 1.00 82.17 C ANISOU 4700 CA PRO B 366 9493 11703 10025 -4875 -4416 2633 C ATOM 4701 C PRO B 366 29.296 8.098 -17.309 1.00 87.73 C ANISOU 4701 C PRO B 366 10417 12321 10597 -5181 -4818 2566 C ATOM 4702 O PRO B 366 30.335 7.723 -16.768 1.00 92.35 O ANISOU 4702 O PRO B 366 10725 13128 11237 -5351 -5048 2724 O ATOM 4703 CB PRO B 366 29.221 8.221 -19.808 1.00 95.79 C ANISOU 4703 CB PRO B 366 11072 13389 11937 -5073 -4327 2771 C ATOM 4704 CG PRO B 366 28.093 8.065 -20.764 1.00 89.74 C ANISOU 4704 CG PRO B 366 10442 12497 11158 -4780 -3983 2672 C ATOM 4705 CD PRO B 366 26.866 8.032 -19.909 1.00 86.47 C ANISOU 4705 CD PRO B 366 10461 11870 10523 -4575 -3988 2403 C ATOM 4706 N ILE B 367 28.548 9.094 -16.845 1.00 87.97 N ANISOU 4706 N ILE B 367 10942 12031 10454 -5242 -4907 2331 N ATOM 4707 CA ILE B 367 28.902 9.825 -15.635 1.00 93.34 C ANISOU 4707 CA ILE B 367 11914 12585 10966 -5517 -5282 2218 C ATOM 4708 C ILE B 367 28.794 8.928 -14.405 1.00 93.50 C ANISOU 4708 C ILE B 367 11977 12760 10788 -5358 -5381 2154 C ATOM 4709 O ILE B 367 29.634 8.987 -13.506 1.00 98.93 O ANISOU 4709 O ILE B 367 12614 13561 11415 -5592 -5711 2215 O ATOM 4710 CB ILE B 367 28.000 11.062 -15.447 1.00 92.79 C ANISOU 4710 CB ILE B 367 12401 12107 10746 -5560 -5314 1951 C ATOM 4711 CG1 ILE B 367 28.016 11.930 -16.708 1.00 92.92 C ANISOU 4711 CG1 ILE B 367 12400 11950 10957 -5718 -5226 2034 C ATOM 4712 CG2 ILE B 367 28.435 11.871 -14.235 1.00 98.92 C ANISOU 4712 CG2 ILE B 367 13515 12741 11331 -5846 -5709 1812 C ATOM 4713 CD1 ILE B 367 27.132 13.154 -16.620 1.00 92.83 C ANISOU 4713 CD1 ILE B 367 12926 11515 10830 -5729 -5247 1789 C ATOM 4714 N LEU B 368 27.759 8.094 -14.376 1.00 87.55 N ANISOU 4714 N LEU B 368 11316 12016 9933 -4972 -5102 2043 N ATOM 4715 CA LEU B 368 27.523 7.194 -13.251 1.00 87.38 C ANISOU 4715 CA LEU B 368 11350 12137 9715 -4794 -5150 1996 C ATOM 4716 C LEU B 368 28.624 6.146 -13.124 1.00 89.64 C ANISOU 4716 C LEU B 368 11150 12768 10141 -4811 -5246 2267 C ATOM 4717 O LEU B 368 28.926 5.681 -12.025 1.00 93.11 O ANISOU 4717 O LEU B 368 11604 13337 10437 -4866 -5486 2295 O ATOM 4718 CB LEU B 368 26.165 6.504 -13.394 1.00 80.99 C ANISOU 4718 CB LEU B 368 10692 11272 8808 -4390 -4800 1854 C ATOM 4719 CG LEU B 368 24.931 7.406 -13.369 1.00 78.86 C ANISOU 4719 CG LEU B 368 10906 10684 8373 -4304 -4694 1570 C ATOM 4720 CD1 LEU B 368 23.667 6.583 -13.553 1.00 72.95 C ANISOU 4720 CD1 LEU B 368 10219 9940 7560 -3911 -4349 1473 C ATOM 4721 CD2 LEU B 368 24.876 8.201 -12.075 1.00 83.61 C ANISOU 4721 CD2 LEU B 368 11922 11146 8699 -4478 -4984 1380 C ATOM 4722 N TYR B 369 29.219 5.780 -14.254 1.00100.30 N ANISOU 4722 N TYR B 369 12078 14269 11764 -4749 -5054 2467 N ATOM 4723 CA TYR B 369 30.278 4.778 -14.276 1.00101.03 C ANISOU 4723 CA TYR B 369 11671 14688 12029 -4724 -5105 2732 C ATOM 4724 C TYR B 369 31.554 5.321 -13.638 1.00103.80 C ANISOU 4724 C TYR B 369 11865 15158 12417 -5108 -5519 2871 C ATOM 4725 O TYR B 369 32.254 4.607 -12.921 1.00105.60 O ANISOU 4725 O TYR B 369 11877 15598 12649 -5075 -5667 3006 O ATOM 4726 CB TYR B 369 30.567 4.335 -15.711 1.00 87.46 C ANISOU 4726 CB TYR B 369 9559 13086 10588 -4600 -4803 2895 C ATOM 4727 CG TYR B 369 29.378 3.754 -16.445 1.00 80.52 C ANISOU 4727 CG TYR B 369 8793 12112 9690 -4235 -4412 2778 C ATOM 4728 CD1 TYR B 369 28.324 3.167 -15.758 1.00 77.23 C ANISOU 4728 CD1 TYR B 369 8648 11624 9073 -3979 -4328 2620 C ATOM 4729 CD2 TYR B 369 29.313 3.792 -17.831 1.00 77.67 C ANISOU 4729 CD2 TYR B 369 8267 11742 9504 -4160 -4132 2834 C ATOM 4730 CE1 TYR B 369 27.238 2.636 -16.434 1.00 71.36 C ANISOU 4730 CE1 TYR B 369 7991 10800 8325 -3670 -3989 2523 C ATOM 4731 CE2 TYR B 369 28.233 3.264 -18.515 1.00 71.74 C ANISOU 4731 CE2 TYR B 369 7621 10906 8731 -3845 -3803 2727 C ATOM 4732 CZ TYR B 369 27.199 2.688 -17.812 1.00 68.65 C ANISOU 4732 CZ TYR B 369 7481 10441 8159 -3607 -3740 2573 C ATOM 4733 OH TYR B 369 26.122 2.163 -18.487 1.00 63.21 O ANISOU 4733 OH TYR B 369 6881 9676 7461 -3317 -3430 2476 O ATOM 4734 N ASN B 370 31.846 6.591 -13.902 1.00116.06 N ANISOU 4734 N ASN B 370 13550 16539 14006 -5434 -5658 2833 N ATOM 4735 CA ASN B 370 33.050 7.234 -13.384 1.00118.75 C ANISOU 4735 CA ASN B 370 13830 16895 14394 -5709 -5902 2920 C ATOM 4736 C ASN B 370 32.995 7.496 -11.881 1.00120.34 C ANISOU 4736 C ASN B 370 14404 17002 14317 -5763 -6165 2758 C ATOM 4737 O ASN B 370 34.012 7.414 -11.193 1.00122.81 O ANISOU 4737 O ASN B 370 14545 17476 14641 -5826 -6346 2878 O ATOM 4738 CB ASN B 370 33.319 8.544 -14.130 1.00108.42 C ANISOU 4738 CB ASN B 370 12632 15375 13189 -6006 -5929 2908 C ATOM 4739 CG ASN B 370 33.855 8.319 -15.531 1.00107.85 C ANISOU 4739 CG ASN B 370 12108 15459 13410 -6018 -5704 3136 C ATOM 4740 OD1 ASN B 370 33.101 8.029 -16.459 1.00104.98 O ANISOU 4740 OD1 ASN B 370 11458 15281 13148 -5766 -5464 3227 O ATOM 4741 ND2 ASN B 370 35.166 8.457 -15.690 1.00110.78 N ANISOU 4741 ND2 ASN B 370 12426 15756 13909 -6308 -5770 3232 N ATOM 4742 N LEU B 371 31.806 7.810 -11.379 1.00199.60 N ANISOU 4742 N LEU B 371 24957 26781 24101 -5733 -6178 2482 N ATOM 4743 CA LEU B 371 31.626 8.117 -9.964 1.00200.61 C ANISOU 4743 CA LEU B 371 25513 26786 23926 -5782 -6396 2286 C ATOM 4744 C LEU B 371 31.867 6.903 -9.072 1.00200.59 C ANISOU 4744 C LEU B 371 25384 27028 23805 -5591 -6448 2365 C ATOM 4745 O LEU B 371 32.455 7.019 -7.996 1.00202.56 O ANISOU 4745 O LEU B 371 25722 27311 23931 -5709 -6684 2363 O ATOM 4746 CB LEU B 371 30.225 8.678 -9.708 1.00106.39 C ANISOU 4746 CB LEU B 371 14128 14554 11739 -5700 -6324 1971 C ATOM 4747 CG LEU B 371 29.904 10.033 -10.339 1.00108.14 C ANISOU 4747 CG LEU B 371 14685 14435 11971 -5940 -6400 1815 C ATOM 4748 CD1 LEU B 371 28.478 10.451 -10.013 1.00106.37 C ANISOU 4748 CD1 LEU B 371 14997 13926 11495 -5794 -6306 1495 C ATOM 4749 CD2 LEU B 371 30.896 11.087 -9.874 1.00113.20 C ANISOU 4749 CD2 LEU B 371 15443 15004 12565 -6228 -6697 1813 C ATOM 4750 N VAL B 372 31.409 5.740 -9.522 1.00150.88 N ANISOU 4750 N VAL B 372 18889 20893 17546 -5298 -6231 2442 N ATOM 4751 CA VAL B 372 31.507 4.523 -8.724 1.00150.69 C ANISOU 4751 CA VAL B 372 18782 21071 17403 -5083 -6253 2519 C ATOM 4752 C VAL B 372 32.825 3.787 -8.947 1.00152.20 C ANISOU 4752 C VAL B 372 18457 21534 17839 -5091 -6333 2813 C ATOM 4753 O VAL B 372 33.601 3.589 -8.012 1.00153.87 O ANISOU 4753 O VAL B 372 18671 21846 17947 -5112 -6530 2868 O ATOM 4754 CB VAL B 372 30.338 3.564 -9.015 1.00106.10 C ANISOU 4754 CB VAL B 372 13147 15472 11692 -4756 -5991 2492 C ATOM 4755 CG1 VAL B 372 30.463 2.309 -8.168 1.00106.25 C ANISOU 4755 CG1 VAL B 372 13089 15684 11597 -4541 -6012 2598 C ATOM 4756 CG2 VAL B 372 29.008 4.257 -8.758 1.00103.48 C ANISOU 4756 CG2 VAL B 372 13333 14861 11122 -4682 -5842 2185 C ATOM 4757 N SER B 373 33.069 3.381 -10.189 1.00106.12 N ANISOU 4757 N SER B 373 12183 15816 12320 -5066 -6176 3000 N ATOM 4758 CA SER B 373 34.273 2.628 -10.524 1.00108.12 C ANISOU 4758 CA SER B 373 11919 16337 12824 -5023 -6203 3277 C ATOM 4759 C SER B 373 35.491 3.534 -10.648 1.00112.02 C ANISOU 4759 C SER B 373 12217 16850 13496 -5339 -6362 3387 C ATOM 4760 O SER B 373 35.464 4.531 -11.369 1.00111.66 O ANISOU 4760 O SER B 373 12140 16705 13580 -5496 -6270 3378 O ATOM 4761 CB SER B 373 34.074 1.841 -11.821 1.00131.40 C ANISOU 4761 CB SER B 373 14477 19441 16009 -4751 -5902 3426 C ATOM 4762 OG SER B 373 35.278 1.214 -12.224 1.00133.41 O ANISOU 4762 OG SER B 373 14224 19939 16527 -4702 -5902 3683 O ATOM 4763 N ALA B 374 36.558 3.179 -9.941 1.00124.63 N ANISOU 4763 N ALA B 374 13683 18575 15093 -5436 -6605 3500 N ATOM 4764 CA ALA B 374 37.800 3.938 -9.995 1.00128.96 C ANISOU 4764 CA ALA B 374 14022 19170 15806 -5740 -6782 3627 C ATOM 4765 C ALA B 374 38.625 3.543 -11.216 1.00129.11 C ANISOU 4765 C ALA B 374 13475 19403 16178 -5683 -6585 3875 C ATOM 4766 O ALA B 374 39.221 4.394 -11.874 1.00131.48 O ANISOU 4766 O ALA B 374 13621 19698 16636 -5931 -6613 3959 O ATOM 4767 CB ALA B 374 38.602 3.733 -8.721 1.00124.75 C ANISOU 4767 CB ALA B 374 13489 18737 15173 -5840 -7101 3687 C ATOM 4768 N ASN B 375 38.649 2.246 -11.512 1.00195.38 N ANISOU 4768 N ASN B 375 21569 27980 24687 -5347 -6378 3992 N ATOM 4769 CA ASN B 375 39.396 1.725 -12.652 1.00196.21 C ANISOU 4769 CA ASN B 375 21137 28302 25112 -5231 -6154 4213 C ATOM 4770 C ASN B 375 38.855 2.254 -13.975 1.00193.45 C ANISOU 4770 C ASN B 375 20792 27854 24856 -5261 -5880 4165 C ATOM 4771 O ASN B 375 39.606 2.778 -14.805 1.00195.06 O ANISOU 4771 O ASN B 375 20718 28134 25261 -5412 -5795 4294 O ATOM 4772 CB ASN B 375 39.363 0.195 -12.652 1.00160.56 C ANISOU 4772 CB ASN B 375 16350 23975 20679 -4835 -6008 4328 C ATOM 4773 CG ASN B 375 39.736 -0.396 -11.306 1.00163.18 C ANISOU 4773 CG ASN B 375 16762 24367 20871 -4773 -6271 4355 C ATOM 4774 OD1 ASN B 375 40.910 -0.628 -11.020 1.00167.68 O ANISOU 4774 OD1 ASN B 375 16997 25126 21585 -4777 -6403 4541 O ATOM 4775 ND2 ASN B 375 38.733 -0.647 -10.471 1.00160.54 N ANISOU 4775 ND2 ASN B 375 16873 23878 20247 -4711 -6344 4174 N ATOM 4776 N PHE B 376 37.545 2.118 -14.161 1.00169.96 N ANISOU 4776 N PHE B 376 18138 24715 21725 -5118 -5743 3982 N ATOM 4777 CA PHE B 376 36.883 2.598 -15.368 1.00168.06 C ANISOU 4777 CA PHE B 376 17941 24368 21549 -5121 -5487 3921 C ATOM 4778 C PHE B 376 37.056 4.103 -15.519 1.00169.14 C ANISOU 4778 C PHE B 376 18278 24315 21674 -5493 -5596 3862 C ATOM 4779 O PHE B 376 37.087 4.617 -16.632 1.00168.95 O ANISOU 4779 O PHE B 376 18103 24288 21803 -5570 -5408 3931 O ATOM 4780 CB PHE B 376 35.394 2.239 -15.355 1.00139.52 C ANISOU 4780 CB PHE B 376 14677 20597 17738 -4919 -5373 3720 C ATOM 4781 CG PHE B 376 34.663 2.640 -16.608 1.00137.96 C ANISOU 4781 CG PHE B 376 14449 20339 17632 -4852 -5083 3688 C ATOM 4782 CD1 PHE B 376 34.639 1.801 -17.709 1.00136.84 C ANISOU 4782 CD1 PHE B 376 13973 20373 17647 -4554 -4801 3798 C ATOM 4783 CD2 PHE B 376 34.001 3.855 -16.684 1.00137.79 C ANISOU 4783 CD2 PHE B 376 14742 20072 17540 -5082 -5093 3546 C ATOM 4784 CE1 PHE B 376 33.970 2.165 -18.863 1.00135.53 C ANISOU 4784 CE1 PHE B 376 13865 20094 17536 -4421 -4441 3725 C ATOM 4785 CE2 PHE B 376 33.331 4.226 -17.836 1.00136.47 C ANISOU 4785 CE2 PHE B 376 14598 19810 17444 -4969 -4769 3503 C ATOM 4786 CZ PHE B 376 33.315 3.379 -18.926 1.00135.33 C ANISOU 4786 CZ PHE B 376 14169 19818 17430 -4630 -4429 3585 C ATOM 4787 N ARG B 377 37.162 4.803 -14.394 1.00140.14 N ANISOU 4787 N ARG B 377 14961 20473 17812 -5719 -5894 3735 N ATOM 4788 CA ARG B 377 37.397 6.241 -14.411 1.00141.62 C ANISOU 4788 CA ARG B 377 15378 20448 17985 -6075 -6029 3674 C ATOM 4789 C ARG B 377 38.824 6.542 -14.855 1.00145.15 C ANISOU 4789 C ARG B 377 15387 21083 18679 -6270 -6059 3925 C ATOM 4790 O ARG B 377 39.067 7.495 -15.598 1.00146.40 O ANISOU 4790 O ARG B 377 15551 21141 18932 -6501 -6020 3965 O ATOM 4791 CB ARG B 377 37.127 6.846 -13.032 1.00116.58 C ANISOU 4791 CB ARG B 377 12694 17057 14543 -6246 -6343 3470 C ATOM 4792 CG ARG B 377 37.423 8.333 -12.931 1.00121.71 C ANISOU 4792 CG ARG B 377 13213 17816 15214 -6462 -6641 3585 C ATOM 4793 CD ARG B 377 36.826 8.922 -11.664 1.00124.03 C ANISOU 4793 CD ARG B 377 14035 17856 15235 -6667 -6937 3363 C ATOM 4794 NE ARG B 377 37.202 8.159 -10.478 1.00121.88 N ANISOU 4794 NE ARG B 377 14082 17538 14692 -6440 -6959 3177 N ATOM 4795 CZ ARG B 377 36.698 8.367 -9.266 1.00121.63 C ANISOU 4795 CZ ARG B 377 14608 17231 14377 -6486 -7055 2898 C ATOM 4796 NH1 ARG B 377 35.792 9.316 -9.078 1.00123.36 N ANISOU 4796 NH1 ARG B 377 15141 17171 14559 -6744 -7149 2767 N ATOM 4797 NH2 ARG B 377 37.098 7.625 -8.243 1.00119.90 N ANISOU 4797 NH2 ARG B 377 14640 17010 13905 -6264 -7047 2752 N ATOM 4798 N GLN B 378 39.764 5.720 -14.396 1.00172.75 N ANISOU 4798 N GLN B 378 18501 24855 22282 -6163 -6120 4101 N ATOM 4799 CA GLN B 378 41.159 5.846 -14.802 1.00177.55 C ANISOU 4799 CA GLN B 378 18656 25679 23125 -6318 -6152 4346 C ATOM 4800 C GLN B 378 41.299 5.660 -16.307 1.00176.31 C ANISOU 4800 C GLN B 378 18126 25670 23195 -6199 -5795 4493 C ATOM 4801 O GLN B 378 41.960 6.452 -16.978 1.00178.80 O ANISOU 4801 O GLN B 378 18316 25986 23635 -6434 -5753 4597 O ATOM 4802 CB GLN B 378 42.034 4.831 -14.063 1.00198.57 C ATOM 4803 CG GLN B 378 42.249 5.143 -12.592 1.00198.57 C ATOM 4804 CD GLN B 378 43.068 4.080 -11.885 1.00198.57 C ATOM 4805 OE1 GLN B 378 43.370 3.031 -12.454 1.00198.57 O ATOM 4806 NE2 GLN B 378 43.431 4.347 -10.636 1.00198.57 N ATOM 4807 N VAL B 379 40.667 4.614 -16.833 1.00145.05 N ANISOU 4807 N VAL B 379 14001 21832 19279 -5835 -5533 4502 N ATOM 4808 CA VAL B 379 40.718 4.344 -18.266 1.00143.78 C ANISOU 4808 CA VAL B 379 13504 21813 19310 -5694 -5171 4623 C ATOM 4809 C VAL B 379 39.977 5.423 -19.057 1.00141.35 C ANISOU 4809 C VAL B 379 13488 21272 18945 -5846 -5032 4512 C ATOM 4810 O VAL B 379 40.402 5.812 -20.146 1.00141.86 O ANISOU 4810 O VAL B 379 13329 21416 19154 -5902 -4809 4632 O ATOM 4811 CB VAL B 379 40.130 2.959 -18.604 1.00154.90 C ANISOU 4811 CB VAL B 379 14693 23386 20777 -5255 -4919 4646 C ATOM 4812 CG1 VAL B 379 40.355 2.631 -20.071 1.00158.17 C ANISOU 4812 CG1 VAL B 379 14670 24082 21348 -5092 -4967 4834 C ATOM 4813 CG2 VAL B 379 40.754 1.891 -17.722 1.00151.70 C ANISOU 4813 CG2 VAL B 379 14695 22798 20148 -5096 -4984 4436 C ATOM 4814 N PHE B 380 38.873 5.906 -18.495 1.00156.43 N ANISOU 4814 N PHE B 380 15906 22893 20638 -5909 -5162 4283 N ATOM 4815 CA PHE B 380 38.058 6.937 -19.132 1.00154.79 C ANISOU 4815 CA PHE B 380 16026 22422 20365 -6052 -5067 4161 C ATOM 4816 C PHE B 380 38.847 8.230 -19.294 1.00157.58 C ANISOU 4816 C PHE B 380 16418 22676 20779 -6434 -5200 4242 C ATOM 4817 O PHE B 380 38.828 8.849 -20.357 1.00157.71 O ANISOU 4817 O PHE B 380 16344 22681 20900 -6524 -5004 4329 O ATOM 4818 CB PHE B 380 36.791 7.198 -18.312 1.00110.73 C ANISOU 4818 CB PHE B 380 10993 16547 14532 -6030 -5206 3886 C ATOM 4819 CG PHE B 380 35.796 8.098 -18.992 1.00108.98 C ANISOU 4819 CG PHE B 380 11135 16027 14246 -6154 -5124 3747 C ATOM 4820 CD1 PHE B 380 34.821 7.569 -19.822 1.00105.32 C ANISOU 4820 CD1 PHE B 380 10696 15535 13785 -5941 -4850 3690 C ATOM 4821 CD2 PHE B 380 35.827 9.468 -18.792 1.00111.54 C ANISOU 4821 CD2 PHE B 380 11786 16086 14508 -6479 -5329 3676 C ATOM 4822 CE1 PHE B 380 33.902 8.391 -20.446 1.00104.33 C ANISOU 4822 CE1 PHE B 380 10908 15125 13606 -6051 -4784 3571 C ATOM 4823 CE2 PHE B 380 34.911 10.295 -19.413 1.00110.18 C ANISOU 4823 CE2 PHE B 380 11963 15614 14285 -6574 -5259 3554 C ATOM 4824 CZ PHE B 380 33.947 9.756 -20.241 1.00106.45 C ANISOU 4824 CZ PHE B 380 11507 15119 13820 -6359 -4987 3505 C ATOM 4825 N LEU B 381 39.538 8.634 -18.233 1.00119.47 N ANISOU 4825 N LEU B 381 11741 17773 15876 -6662 -5536 4213 N ATOM 4826 CA LEU B 381 40.340 9.852 -18.267 1.00123.71 C ANISOU 4826 CA LEU B 381 12331 18205 16468 -7043 -5702 4289 C ATOM 4827 C LEU B 381 41.610 9.656 -19.089 1.00126.65 C ANISOU 4827 C LEU B 381 12152 18881 17088 -7098 -5551 4575 C ATOM 4828 O LEU B 381 42.117 10.600 -19.695 1.00128.79 O ANISOU 4828 O LEU B 381 12402 19089 17441 -7342 -5509 4670 O ATOM 4829 CB LEU B 381 40.687 10.321 -16.851 1.00155.15 C ANISOU 4829 CB LEU B 381 16551 22078 20320 -7255 -6097 4207 C ATOM 4830 CG LEU B 381 39.712 11.296 -16.183 1.00153.55 C ANISOU 4830 CG LEU B 381 16970 21524 19850 -7275 -6265 3905 C ATOM 4831 CD1 LEU B 381 38.321 10.695 -16.046 1.00152.90 C ANISOU 4831 CD1 LEU B 381 17253 21109 19732 -7432 -6197 3792 C ATOM 4832 CD2 LEU B 381 40.243 11.734 -14.826 1.00157.31 C ANISOU 4832 CD2 LEU B 381 17653 21928 20190 -7476 -6642 3834 C ATOM 4833 N SER B 382 42.120 8.428 -19.107 1.00160.39 N ANISOU 4833 N SER B 382 15987 23479 21476 -6859 -5463 4710 N ATOM 4834 CA SER B 382 43.303 8.108 -19.897 1.00163.86 C ANISOU 4834 CA SER B 382 15876 24234 22150 -6853 -5288 4970 C ATOM 4835 C SER B 382 42.983 8.159 -21.387 1.00161.39 C ANISOU 4835 C SER B 382 15453 23953 21917 -6752 -4902 5021 C ATOM 4836 O SER B 382 43.846 8.468 -22.208 1.00164.56 O ANISOU 4836 O SER B 382 15613 24462 22450 -6920 -4789 5191 O ATOM 4837 CB SER B 382 43.845 6.728 -19.523 1.00130.37 C ANISOU 4837 CB SER B 382 11222 20304 18009 -6558 -5258 5078 C ATOM 4838 OG SER B 382 44.192 6.670 -18.151 1.00131.55 O ANISOU 4838 OG SER B 382 11550 20397 18036 -6593 -5596 4995 O ATOM 4839 N THR B 383 41.735 7.853 -21.728 1.00139.88 N ANISOU 4839 N THR B 383 12907 21138 19102 -6483 -4702 4877 N ATOM 4840 CA THR B 383 41.289 7.875 -23.116 1.00137.29 C ANISOU 4840 CA THR B 383 12523 20821 18818 -6377 -4340 4905 C ATOM 4841 C THR B 383 40.869 9.283 -23.531 1.00137.41 C ANISOU 4841 C THR B 383 12899 20545 18765 -6695 -4388 4857 C ATOM 4842 O THR B 383 41.116 9.710 -24.660 1.00137.86 O ANISOU 4842 O THR B 383 12836 20648 18894 -6752 -4150 4969 O ATOM 4843 CB THR B 383 40.113 6.903 -23.341 1.00135.78 C ANISOU 4843 CB THR B 383 12448 20598 18546 -6019 -4136 4758 C ATOM 4844 OG1 THR B 383 40.498 5.583 -22.939 1.00134.31 O ANISOU 4844 OG1 THR B 383 12573 20256 18204 -5966 -4395 4579 O ATOM 4845 CG2 THR B 383 39.705 6.882 -24.806 1.00136.03 C ANISOU 4845 CG2 THR B 383 12001 20965 18722 -5668 -3854 4886 C ATOM 4846 N LEU B 384 40.242 10.001 -22.605 1.00325.55 N ANISOU 4846 N LEU B 384 37186 44066 42444 -6887 -4694 4685 N ATOM 4847 CA LEU B 384 39.762 11.355 -22.863 1.00326.13 C ANISOU 4847 CA LEU B 384 37655 43812 42448 -7185 -4788 4621 C ATOM 4848 C LEU B 384 40.924 12.301 -23.154 1.00331.73 C ANISOU 4848 C LEU B 384 38141 44611 43291 -7504 -4853 4834 C ATOM 4849 O LEU B 384 40.789 13.245 -23.932 1.00332.38 O ANISOU 4849 O LEU B 384 38286 44597 43408 -7658 -4723 4909 O ATOM 4850 CB LEU B 384 38.941 11.861 -21.670 1.00125.67 C ANISOU 4850 CB LEU B 384 12798 18082 16866 -7293 -5113 4375 C ATOM 4851 CG LEU B 384 38.010 13.063 -21.858 1.00127.01 C ANISOU 4851 CG LEU B 384 13473 17845 16938 -7589 -5299 4253 C ATOM 4852 CD1 LEU B 384 36.854 12.983 -20.875 1.00125.03 C ANISOU 4852 CD1 LEU B 384 13725 17306 16473 -7527 -5511 3962 C ATOM 4853 CD2 LEU B 384 38.750 14.382 -21.685 1.00132.72 C ANISOU 4853 CD2 LEU B 384 14130 18559 17736 -7958 -5537 4391 C ATOM 4854 N ALA B 385 42.068 12.035 -22.531 1.00195.61 N ANISOU 4854 N ALA B 385 20642 27557 26124 -7607 -5062 4939 N ATOM 4855 CA ALA B 385 43.254 12.864 -22.718 1.00201.60 C ANISOU 4855 CA ALA B 385 21156 28424 27018 -7925 -5155 5150 C ATOM 4856 C ALA B 385 43.983 12.525 -24.016 1.00202.74 C ANISOU 4856 C ALA B 385 20834 28867 27331 -7841 -4795 5374 C ATOM 4857 O ALA B 385 45.061 13.059 -24.286 1.00207.13 O ANISOU 4857 O ALA B 385 21277 29447 27974 -8112 -4779 5535 O ATOM 4858 CB ALA B 385 44.192 12.723 -21.528 1.00139.59 C ANISOU 4858 CB ALA B 385 13093 20733 19210 -8020 -5451 5216 C ATOM 4859 N CYS B 386 43.386 11.637 -24.808 1.00197.10 N ANISOU 4859 N CYS B 386 19861 28375 26652 -7464 -4502 5380 N ATOM 4860 CA CYS B 386 43.943 11.214 -26.092 1.00197.83 C ANISOU 4860 CA CYS B 386 19520 28763 26883 -7328 -4126 5565 C ATOM 4861 C CYS B 386 45.353 10.645 -25.953 1.00196.23 C ANISOU 4861 C CYS B 386 19540 28394 26623 -7400 -3892 5558 C ATOM 4862 O CYS B 386 45.606 9.789 -25.105 1.00194.24 O ANISOU 4862 O CYS B 386 19776 27789 26236 -7524 -4018 5404 O ATOM 4863 CB CYS B 386 43.927 12.368 -27.100 1.00143.99 C ATOM 4864 SG CYS B 386 42.285 13.052 -27.431 1.00143.99 S TER 4865 CYS B 386 ATOM 4866 N ARG C 8 18.293 -35.932 -47.347 1.00100.25 N ANISOU 4866 N ARG C 8 15589 9910 12593 4019 2171 -1726 N ATOM 4867 CA ARG C 8 17.391 -34.806 -47.555 1.00 93.50 C ANISOU 4867 CA ARG C 8 14706 9274 11546 3594 2010 -1676 C ATOM 4868 C ARG C 8 17.177 -34.022 -46.264 1.00 88.01 C ANISOU 4868 C ARG C 8 13616 8798 11024 3370 1850 -1335 C ATOM 4869 O ARG C 8 17.615 -34.440 -45.193 1.00 87.90 O ANISOU 4869 O ARG C 8 13423 8695 11279 3486 1799 -1148 O ATOM 4870 CB ARG C 8 16.050 -35.288 -48.109 1.00 68.96 C ATOM 4871 CG ARG C 8 15.357 -36.315 -47.233 1.00 68.96 C ATOM 4872 CD ARG C 8 14.022 -36.729 -47.826 1.00 68.96 C ATOM 4873 NE ARG C 8 13.349 -37.737 -47.010 1.00 68.96 N ATOM 4874 CZ ARG C 8 12.154 -38.248 -47.289 1.00 68.96 C ATOM 4875 NH1 ARG C 8 11.496 -37.846 -48.368 1.00 68.96 N ATOM 4876 NH2 ARG C 8 11.617 -39.160 -46.490 1.00 68.96 N ATOM 4877 N ARG C 9 16.499 -32.885 -46.376 1.00 98.91 N ANISOU 4877 N ARG C 9 14879 10459 12243 3055 1766 -1259 N ATOM 4878 CA ARG C 9 16.268 -32.008 -45.235 1.00 96.23 C ANISOU 4878 CA ARG C 9 14197 10335 12032 2830 1618 -964 C ATOM 4879 C ARG C 9 14.776 -31.749 -45.051 1.00 93.75 C ANISOU 4879 C ARG C 9 14021 9947 11652 2430 1347 -954 C ATOM 4880 O ARG C 9 14.058 -31.530 -46.028 1.00 93.72 O ANISOU 4880 O ARG C 9 14252 9933 11423 2282 1311 -1134 O ATOM 4881 CB ARG C 9 17.006 -30.683 -45.441 1.00 78.29 C ANISOU 4881 CB ARG C 9 11583 8509 9655 2846 1788 -842 C ATOM 4882 CG ARG C 9 17.099 -29.801 -44.208 1.00 77.94 C ANISOU 4882 CG ARG C 9 11172 8692 9749 2667 1664 -544 C ATOM 4883 CD ARG C 9 17.682 -28.440 -44.554 1.00 80.98 C ANISOU 4883 CD ARG C 9 11271 9488 10007 2641 1816 -445 C ATOM 4884 NE ARG C 9 18.038 -27.675 -43.363 1.00 77.78 N ANISOU 4884 NE ARG C 9 10524 9283 9743 2500 1705 -173 N ATOM 4885 CZ ARG C 9 19.256 -27.650 -42.831 1.00 77.02 C ANISOU 4885 CZ ARG C 9 10102 9357 9803 2669 1801 -1 C ATOM 4886 NH1 ARG C 9 20.237 -28.348 -43.387 1.00 73.63 N ANISOU 4886 NH1 ARG C 9 9618 8932 9426 3004 2024 -64 N ATOM 4887 NH2 ARG C 9 19.494 -26.926 -41.745 1.00 78.14 N ANISOU 4887 NH2 ARG C 9 9973 9667 10049 2508 1672 230 N ATOM 4888 N PRO C 10 14.302 -31.782 -43.794 1.00 84.23 N ANISOU 4888 N PRO C 10 12666 8698 10639 2258 1155 -740 N ATOM 4889 CA PRO C 10 12.897 -31.502 -43.478 1.00 81.38 C ANISOU 4889 CA PRO C 10 12381 8297 10243 1888 912 -703 C ATOM 4890 C PRO C 10 12.458 -30.123 -43.961 1.00 76.15 C ANISOU 4890 C PRO C 10 11596 7963 9374 1680 901 -683 C ATOM 4891 O PRO C 10 13.260 -29.189 -43.983 1.00 75.71 O ANISOU 4891 O PRO C 10 11292 8206 9268 1764 1044 -590 O ATOM 4892 CB PRO C 10 12.869 -31.551 -41.948 1.00 70.42 C ANISOU 4892 CB PRO C 10 10773 6892 9090 1812 785 -440 C ATOM 4893 CG PRO C 10 13.977 -32.466 -41.586 1.00 73.01 C ANISOU 4893 CG PRO C 10 11081 7060 9598 2139 895 -406 C ATOM 4894 CD PRO C 10 15.057 -32.205 -42.602 1.00 78.04 C ANISOU 4894 CD PRO C 10 11670 7864 10118 2417 1150 -533 C ATOM 4895 N TYR C 11 11.192 -30.007 -44.349 1.00 47.45 N ANISOU 4895 N TYR C 11 8133 4265 5632 1406 723 -762 N ATOM 4896 CA TYR C 11 10.639 -28.737 -44.803 1.00 46.86 C ANISOU 4896 CA TYR C 11 7961 4467 5377 1196 672 -731 C ATOM 4897 C TYR C 11 9.570 -28.238 -43.836 1.00 45.93 C ANISOU 4897 C TYR C 11 7694 4388 5369 919 458 -556 C ATOM 4898 O TYR C 11 9.061 -27.125 -43.973 1.00 42.26 O ANISOU 4898 O TYR C 11 7125 4135 4798 741 387 -500 O ATOM 4899 CB TYR C 11 10.061 -28.874 -46.216 1.00 39.10 C ANISOU 4899 CB TYR C 11 7288 3426 4143 1120 642 -971 C ATOM 4900 CG TYR C 11 9.049 -29.990 -46.370 1.00 41.71 C ANISOU 4900 CG TYR C 11 7930 3410 4509 992 458 -1120 C ATOM 4901 CD1 TYR C 11 7.694 -29.761 -46.157 1.00 39.82 C ANISOU 4901 CD1 TYR C 11 7706 3142 4280 674 210 -1077 C ATOM 4902 CD2 TYR C 11 9.449 -31.272 -46.735 1.00 46.10 C ANISOU 4902 CD2 TYR C 11 8759 3661 5095 1188 530 -1301 C ATOM 4903 CE1 TYR C 11 6.766 -30.779 -46.297 1.00 42.14 C ANISOU 4903 CE1 TYR C 11 8269 3126 4617 526 29 -1198 C ATOM 4904 CE2 TYR C 11 8.529 -32.296 -46.879 1.00 49.10 C ANISOU 4904 CE2 TYR C 11 9443 3700 5514 1046 345 -1436 C ATOM 4905 CZ TYR C 11 7.190 -32.043 -46.658 1.00 47.12 C ANISOU 4905 CZ TYR C 11 9190 3439 5274 700 91 -1378 C ATOM 4906 OH TYR C 11 6.271 -33.057 -46.799 1.00 51.13 O ANISOU 4906 OH TYR C 11 9983 3614 5830 528 -105 -1498 O ATOM 4907 N ILE C 12 9.238 -29.072 -42.856 1.00 60.99 N ANISOU 4907 N ILE C 12 9596 6089 7486 893 364 -465 N ATOM 4908 CA ILE C 12 8.224 -28.731 -41.865 1.00 55.10 C ANISOU 4908 CA ILE C 12 8724 5363 6848 641 182 -302 C ATOM 4909 C ILE C 12 8.849 -28.171 -40.591 1.00 51.49 C ANISOU 4909 C ILE C 12 7970 5057 6534 692 218 -65 C ATOM 4910 O ILE C 12 9.575 -28.869 -39.883 1.00 50.15 O ANISOU 4910 O ILE C 12 7765 4788 6500 880 290 2 O ATOM 4911 CB ILE C 12 7.350 -29.949 -41.510 1.00 48.18 C ANISOU 4911 CB ILE C 12 8060 4154 6093 515 29 -343 C ATOM 4912 CG1 ILE C 12 6.579 -30.426 -42.743 1.00 49.60 C ANISOU 4912 CG1 ILE C 12 8548 4176 6124 419 -50 -583 C ATOM 4913 CG2 ILE C 12 6.394 -29.605 -40.373 1.00 48.88 C ANISOU 4913 CG2 ILE C 12 7986 4294 6292 262 -126 -156 C ATOM 4914 CD1 ILE C 12 5.685 -31.621 -42.486 1.00 49.25 C ANISOU 4914 CD1 ILE C 12 8739 3776 6198 278 -209 -637 C ATOM 4915 N LEU C 13 8.567 -26.903 -40.309 1.00 47.78 N ANISOU 4915 N LEU C 13 7300 4825 6031 530 158 58 N ATOM 4916 CA LEU C 13 9.069 -26.255 -39.104 1.00 45.78 C ANISOU 4916 CA LEU C 13 6792 4715 5889 534 161 272 C ATOM 4917 C LEU C 13 8.048 -26.378 -37.977 1.00 43.87 C ANISOU 4917 C LEU C 13 6517 4413 5740 318 8 388 C ATOM 4918 O LEU C 13 6.844 -26.476 -38.217 1.00 43.77 O ANISOU 4918 O LEU C 13 6618 4315 5698 135 -104 316 O ATOM 4919 CB LEU C 13 9.381 -24.780 -39.378 1.00 50.21 C ANISOU 4919 CB LEU C 13 7150 5584 6343 525 221 334 C ATOM 4920 CG LEU C 13 9.937 -23.945 -38.221 1.00 50.45 C ANISOU 4920 CG LEU C 13 7027 5755 6386 739 379 391 C ATOM 4921 CD1 LEU C 13 11.257 -24.514 -37.725 1.00 49.54 C ANISOU 4921 CD1 LEU C 13 6744 5920 6157 673 413 447 C ATOM 4922 CD2 LEU C 13 10.097 -22.490 -38.638 1.00 49.00 C ANISOU 4922 CD2 LEU C 13 6709 5531 6378 825 365 557 C ATOM 4923 OXT LEU C 13 8.393 -26.380 -36.795 1.00 50.72 O ANISOU 4923 OXT LEU C 13 7236 5327 6707 317 -6 559 O TER 4924 LEU C 13 ATOM 4925 N ARG D 8 -8.112 24.960 -30.372 1.00 88.09 N ANISOU 4925 N ARG D 8 15176 6168 12125 3739 -2275 -126 N ATOM 4926 CA ARG D 8 -6.819 24.699 -30.992 1.00 83.32 C ANISOU 4926 CA ARG D 8 14448 5761 11446 3297 -2382 123 C ATOM 4927 C ARG D 8 -6.123 23.521 -30.320 1.00 77.72 C ANISOU 4927 C ARG D 8 13682 5308 10539 2940 -2258 32 C ATOM 4928 O ARG D 8 -6.006 23.477 -29.097 1.00 78.68 O ANISOU 4928 O ARG D 8 14070 5262 10561 2876 -2219 -173 O ATOM 4929 CB ARG D 8 -5.930 25.941 -30.923 1.00 85.29 C ANISOU 4929 CB ARG D 8 15046 5616 11745 3095 -2652 320 C ATOM 4930 CG ARG D 8 -4.605 25.789 -31.644 1.00 89.75 C ANISOU 4930 CG ARG D 8 16111 5686 12305 3093 -2743 153 C ATOM 4931 CD ARG D 8 -3.727 27.008 -31.438 1.00 87.09 C ANISOU 4931 CD ARG D 8 15943 5348 11797 2614 -2769 124 C ATOM 4932 NE ARG D 8 -2.453 26.882 -32.139 1.00 87.13 N ANISOU 4932 NE ARG D 8 16052 5250 11801 2226 -2970 410 N ATOM 4933 CZ ARG D 8 -1.459 27.759 -32.047 1.00 91.17 C ANISOU 4933 CZ ARG D 8 16977 5333 12328 2014 -3163 456 C ATOM 4934 NH1 ARG D 8 -1.587 28.830 -31.277 1.00 96.84 N ANISOU 4934 NH1 ARG D 8 18067 5665 13062 2155 -3196 216 N ATOM 4935 NH2 ARG D 8 -0.336 27.564 -32.721 1.00 91.12 N ANISOU 4935 NH2 ARG D 8 17021 5285 12314 1653 -3319 741 N ATOM 4936 N ARG D 9 -5.662 22.569 -31.125 1.00 92.86 N ANISOU 4936 N ARG D 9 15261 7624 12398 2715 -2207 182 N ATOM 4937 CA ARG D 9 -5.053 21.354 -30.596 1.00 87.83 C ANISOU 4937 CA ARG D 9 14519 7261 11589 2402 -2088 122 C ATOM 4938 C ARG D 9 -3.654 21.134 -31.168 1.00 83.73 C ANISOU 4938 C ARG D 9 14088 6725 10999 1952 -2234 320 C ATOM 4939 O ARG D 9 -3.437 21.304 -32.368 1.00 84.81 O ANISOU 4939 O ARG D 9 14195 6830 11199 1871 -2369 551 O ATOM 4940 CB ARG D 9 -5.941 20.146 -30.907 1.00 86.73 C ANISOU 4940 CB ARG D 9 13932 7591 11430 2477 -1897 125 C ATOM 4941 CG ARG D 9 -5.795 18.995 -29.929 1.00 90.31 C ANISOU 4941 CG ARG D 9 14108 8266 11938 2377 -1972 377 C ATOM 4942 CD ARG D 9 -6.696 17.830 -30.298 1.00 91.57 C ANISOU 4942 CD ARG D 9 13845 8850 12098 2471 -1796 361 C ATOM 4943 NE ARG D 9 -6.901 16.928 -29.169 1.00 91.03 N ANISOU 4943 NE ARG D 9 13694 9008 11884 2295 -1626 238 N ATOM 4944 CZ ARG D 9 -6.075 15.941 -28.838 1.00 91.16 C ANISOU 4944 CZ ARG D 9 13653 9123 11861 2480 -1436 37 C ATOM 4945 NH1 ARG D 9 -4.978 15.724 -29.551 1.00 92.35 N ANISOU 4945 NH1 ARG D 9 13801 9174 12114 2861 -1371 -75 N ATOM 4946 NH2 ARG D 9 -6.345 15.171 -27.793 1.00 93.58 N ANISOU 4946 NH2 ARG D 9 13900 9633 12022 2294 -1304 -44 N ATOM 4947 N PRO D 10 -2.696 20.761 -30.304 1.00 65.55 N ANISOU 4947 N PRO D 10 11895 4451 8562 1662 -2209 237 N ATOM 4948 CA PRO D 10 -1.319 20.476 -30.722 1.00 64.67 C ANISOU 4948 CA PRO D 10 11832 4357 8382 1227 -2321 414 C ATOM 4949 C PRO D 10 -1.242 19.330 -31.726 1.00 62.29 C ANISOU 4949 C PRO D 10 11182 4422 8066 1088 -2275 619 C ATOM 4950 O PRO D 10 -2.094 18.440 -31.718 1.00 60.04 O ANISOU 4950 O PRO D 10 10596 4436 7780 1251 -2130 580 O ATOM 4951 CB PRO D 10 -0.636 20.069 -29.413 1.00 55.36 C ANISOU 4951 CB PRO D 10 10720 3253 7062 1030 -2251 246 C ATOM 4952 CG PRO D 10 -1.427 20.741 -28.355 1.00 58.10 C ANISOU 4952 CG PRO D 10 11260 3413 7403 1337 -2183 -24 C ATOM 4953 CD PRO D 10 -2.846 20.708 -28.840 1.00 58.63 C ANISOU 4953 CD PRO D 10 11117 3577 7582 1741 -2078 -35 C ATOM 4954 N TYR D 11 -0.225 19.360 -32.581 1.00 74.41 N ANISOU 4954 N TYR D 11 12766 5925 9582 785 -2394 836 N ATOM 4955 CA TYR D 11 -0.025 18.318 -33.581 1.00 70.20 C ANISOU 4955 CA TYR D 11 11946 5719 9009 636 -2351 1022 C ATOM 4956 C TYR D 11 1.330 17.643 -33.396 1.00 68.64 C ANISOU 4956 C TYR D 11 11669 5715 8699 274 -2302 1063 C ATOM 4957 O TYR D 11 1.628 16.637 -34.041 1.00 66.15 O ANISOU 4957 O TYR D 11 11122 5681 8334 137 -2242 1191 O ATOM 4958 CB TYR D 11 -0.138 18.899 -34.993 1.00 54.33 C ANISOU 4958 CB TYR D 11 10020 3571 7050 601 -2504 1263 C ATOM 4959 CG TYR D 11 0.748 20.103 -35.239 1.00 58.53 C ANISOU 4959 CG TYR D 11 10895 3749 7594 382 -2672 1368 C ATOM 4960 CD1 TYR D 11 2.058 19.949 -35.679 1.00 58.33 C ANISOU 4960 CD1 TYR D 11 10878 3796 7489 -6 -2702 1535 C ATOM 4961 CD2 TYR D 11 0.272 21.392 -35.035 1.00 63.19 C ANISOU 4961 CD2 TYR D 11 11798 3927 8283 563 -2797 1303 C ATOM 4962 CE1 TYR D 11 2.869 21.045 -35.906 1.00 62.58 C ANISOU 4962 CE1 TYR D 11 11715 4016 8045 -237 -2857 1650 C ATOM 4963 CE2 TYR D 11 1.075 22.494 -35.259 1.00 67.51 C ANISOU 4963 CE2 TYR D 11 12677 4125 8850 341 -2964 1406 C ATOM 4964 CZ TYR D 11 2.373 22.315 -35.695 1.00 67.14 C ANISOU 4964 CZ TYR D 11 12620 4168 8722 -73 -2996 1586 C ATOM 4965 OH TYR D 11 3.176 23.410 -35.918 1.00 71.83 O ANISOU 4965 OH TYR D 11 13530 4420 9342 -325 -3163 1707 O ATOM 4966 N ILE D 12 2.145 18.206 -32.510 1.00 61.12 N ANISOU 4966 N ILE D 12 10910 4606 7707 128 -2335 952 N ATOM 4967 CA ILE D 12 3.479 17.679 -32.245 1.00 61.17 C ANISOU 4967 CA ILE D 12 10837 4784 7622 -208 -2310 992 C ATOM 4968 C ILE D 12 3.461 16.648 -31.121 1.00 58.67 C ANISOU 4968 C ILE D 12 10395 4668 7228 -151 -2175 791 C ATOM 4969 O ILE D 12 3.026 16.937 -30.007 1.00 59.14 O ANISOU 4969 O ILE D 12 10636 4563 7272 -16 -2177 593 O ATOM 4970 CB ILE D 12 4.465 18.806 -31.880 1.00 50.34 C ANISOU 4970 CB ILE D 12 9761 3116 6253 -487 -2477 1043 C ATOM 4971 CG1 ILE D 12 4.580 19.806 -33.033 1.00 54.35 C ANISOU 4971 CG1 ILE D 12 10405 3421 6824 -581 -2611 1274 C ATOM 4972 CG2 ILE D 12 5.826 18.229 -31.526 1.00 48.51 C ANISOU 4972 CG2 ILE D 12 9405 3086 5939 -825 -2456 1086 C ATOM 4973 CD1 ILE D 12 5.490 20.979 -32.739 1.00 58.91 C ANISOU 4973 CD1 ILE D 12 11289 3673 7423 -866 -2788 1343 C ATOM 4974 N LEU D 13 3.935 15.443 -31.422 1.00 69.03 N ANISOU 4974 N LEU D 13 11415 6328 8485 -247 -2056 843 N ATOM 4975 CA LEU D 13 3.993 14.374 -30.433 1.00 69.24 C ANISOU 4975 CA LEU D 13 11326 6554 8428 -240 -1941 692 C ATOM 4976 C LEU D 13 5.423 14.181 -29.932 1.00 68.15 C ANISOU 4976 C LEU D 13 11141 6530 8225 -576 -1977 768 C ATOM 4977 O LEU D 13 5.654 13.741 -28.805 1.00 68.58 O ANISOU 4977 O LEU D 13 11156 6702 8200 -624 -1932 660 O ATOM 4978 CB LEU D 13 3.456 13.068 -31.026 1.00 60.21 C ANISOU 4978 CB LEU D 13 9881 5713 7281 -56 -1772 673 C ATOM 4979 CG LEU D 13 3.422 11.841 -30.110 1.00 57.38 C ANISOU 4979 CG LEU D 13 9248 5649 6902 -208 -1702 822 C ATOM 4980 CD1 LEU D 13 2.606 12.127 -28.856 1.00 56.71 C ANISOU 4980 CD1 LEU D 13 8920 5808 6819 -13 -1550 761 C ATOM 4981 CD2 LEU D 13 2.864 10.638 -30.854 1.00 56.00 C ANISOU 4981 CD2 LEU D 13 9077 5429 6772 -303 -1782 1019 C ATOM 4982 OXT LEU D 13 6.389 14.463 -30.643 1.00 62.16 O ANISOU 4982 OXT LEU D 13 10369 5758 7489 -805 -2051 949 O TER 4983 LEU D 13 HETATM 4984 N GLY A1385 12.541 -11.046 -45.867 1.00 67.79 N HETATM 4985 CA GLY A1385 13.236 -10.573 -44.684 1.00 67.79 C HETATM 4986 C GLY A1385 12.676 -11.164 -43.404 1.00 67.79 C HETATM 4987 O GLY A1385 11.512 -11.560 -43.346 1.00 67.79 O HETATM 4988 OXT GLY A1385 13.372 -11.260 -42.393 1.00 80.91 O HETATM 4989 N GLY A1386 -11.468 -11.881 -17.481 1.00102.99 N HETATM 4990 CA GLY A1386 -12.112 -12.206 -18.740 1.00102.99 C HETATM 4991 C GLY A1386 -11.176 -12.069 -19.926 1.00102.99 C HETATM 4992 O GLY A1386 -10.131 -11.423 -19.838 1.00102.99 O HETATM 4993 OXT GLY A1386 -11.438 -12.601 -21.005 1.00 90.22 O HETATM 4994 N GLY A1387 1.647 -3.518 -14.296 1.00 92.58 N HETATM 4995 CA GLY A1387 1.084 -2.582 -15.251 1.00 92.58 C HETATM 4996 C GLY A1387 -0.424 -2.471 -15.138 1.00 92.58 C HETATM 4997 O GLY A1387 -1.023 -1.494 -15.589 1.00 92.58 O HETATM 4998 OXT GLY A1387 -1.087 -3.354 -14.592 1.00125.09 O HETATM 4999 N GLY A1388 -3.712 -9.416 -31.147 1.00 98.67 N HETATM 5000 CA GLY A1388 -4.513 -10.620 -31.033 1.00 98.67 C HETATM 5001 C GLY A1388 -3.978 -11.759 -31.878 1.00 98.67 C HETATM 5002 O GLY A1388 -3.159 -11.552 -32.774 1.00 98.67 O HETATM 5003 OXT GLY A1388 -4.350 -12.918 -31.690 1.00 76.64 O HETATM 5004 N GLY A1389 15.965 -24.658 -25.493 1.00 89.24 N HETATM 5005 CA GLY A1389 16.839 -23.567 -25.104 1.00 89.24 C HETATM 5006 C GLY A1389 18.249 -23.739 -25.632 1.00 89.24 C HETATM 5007 O GLY A1389 18.674 -24.849 -25.952 1.00 89.24 O HETATM 5008 OXT GLY A1389 19.003 -22.773 -25.753 1.00107.17 O HETATM 5009 N GLY A1390 -2.471 -13.581 -41.903 1.00 72.53 N HETATM 5010 CA GLY A1390 -2.046 -13.915 -43.250 1.00 72.53 C HETATM 5011 C GLY A1390 -1.640 -12.688 -44.045 1.00 72.53 C HETATM 5012 O GLY A1390 -1.547 -12.729 -45.273 1.00 72.53 O HETATM 5013 OXT GLY A1390 -1.399 -11.618 -43.483 1.00144.30 O HETATM 5014 N GLY A1391 10.216 -8.214 -40.224 1.00 89.54 N HETATM 5015 CA GLY A1391 9.574 -7.095 -40.888 1.00 89.54 C HETATM 5016 C GLY A1391 9.479 -7.282 -42.390 1.00 89.54 C HETATM 5017 O GLY A1391 10.162 -8.132 -42.965 1.00 89.54 O HETATM 5018 OXT GLY A1391 8.718 -6.589 -43.069 1.00101.46 O HETATM 5019 N GLY A1392 4.066 -29.680 -13.083 1.00 77.23 N HETATM 5020 CA GLY A1392 4.890 -29.119 -12.029 1.00 77.23 C HETATM 5021 C GLY A1392 5.422 -30.176 -11.080 1.00 77.23 C HETATM 5022 O GLY A1392 4.911 -31.295 -11.025 1.00 77.23 O HETATM 5023 OXT GLY A1392 6.379 -29.942 -10.341 1.00 68.96 O HETATM 5024 N GLY B1387 20.165 -0.164 -34.327 1.00 94.64 N HETATM 5025 CA GLY B1387 19.062 0.742 -34.593 1.00 94.64 C HETATM 5026 C GLY B1387 17.751 0.010 -34.808 1.00 94.64 C HETATM 5027 O GLY B1387 17.702 -1.222 -34.797 1.00 94.64 O HETATM 5028 OXT GLY B1387 16.702 0.628 -34.999 1.00 79.73 O HETATM 5029 N GLY B1388 36.439 -1.882 -13.651 1.00104.40 N HETATM 5030 CA GLY B1388 35.825 -1.937 -12.338 1.00104.40 C HETATM 5031 C GLY B1388 34.333 -2.201 -12.408 1.00104.40 C HETATM 5032 O GLY B1388 33.806 -2.598 -13.448 1.00104.40 O HETATM 5033 OXT GLY B1388 33.611 -2.028 -11.427 1.00 96.81 O HETATM 5034 N GLY B1389 17.996 -13.115 -20.235 1.00108.73 N HETATM 5035 CA GLY B1389 19.014 -14.117 -20.490 1.00108.73 C HETATM 5036 C GLY B1389 18.471 -15.317 -21.241 1.00108.73 C HETATM 5037 O GLY B1389 17.717 -15.172 -22.205 1.00108.73 O HETATM 5038 OXT GLY B1389 18.769 -16.463 -20.905 1.00143.49 O CONECT 685 1321 CONECT 1321 685 CONECT 4984 4985 CONECT 4985 4984 4986 CONECT 4986 4985 4987 4988 CONECT 4987 4986 CONECT 4988 4986 CONECT 4989 4990 CONECT 4990 4989 4991 CONECT 4991 4990 4992 4993 CONECT 4992 4991 CONECT 4993 4991 CONECT 4994 4995 CONECT 4995 4994 4996 CONECT 4996 4995 4997 4998 CONECT 4997 4996 CONECT 4998 4996 CONECT 4999 5000 CONECT 5000 4999 5001 CONECT 5001 5000 5002 5003 CONECT 5002 5001 CONECT 5003 5001 CONECT 5004 5005 CONECT 5005 5004 5006 CONECT 5006 5005 5007 5008 CONECT 5007 5006 CONECT 5008 5006 CONECT 5009 5010 CONECT 5010 5009 5011 CONECT 5011 5010 5012 5013 CONECT 5012 5011 CONECT 5013 5011 CONECT 5014 5015 CONECT 5015 5014 5016 CONECT 5016 5015 5017 5018 CONECT 5017 5016 CONECT 5018 5016 CONECT 5019 5020 CONECT 5020 5019 5021 CONECT 5021 5020 5022 5023 CONECT 5022 5021 CONECT 5023 5021 CONECT 3073 3709 CONECT 3709 3073 CONECT 5024 5025 CONECT 5025 5024 5026 CONECT 5026 5025 5027 5028 CONECT 5027 5026 CONECT 5028 5026 CONECT 5029 5030 CONECT 5030 5029 5031 CONECT 5031 5030 5032 5033 CONECT 5032 5031 CONECT 5033 5031 CONECT 5034 5035 CONECT 5035 5034 5036 CONECT 5036 5035 5037 5038 CONECT 5037 5036 CONECT 5038 5036 MASTER 393 0 11 23 4 0 10 9 5034 4 59 54 END