HEADER SIGNALING PROTEIN, HYDROLASE 05-DEC-14 4RWS TITLE CRYSTAL STRUCTURE OF CXCR4 AND VIRAL CHEMOKINE ANTAGONIST VMIP-II TITLE 2 COMPLEX (PSI COMMUNITY TARGET) COMPND MOL_ID: 1; COMPND 2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4/ENDOLYSIN CHIMERIC PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CXCR4 RESIDUES 2-228, LYSOZYME RESIDUES 1002-1161, CXCR4 COMPND 5 RESIDUES 231-319; COMPND 6 SYNONYM: CXC-R4, CXCR-4, STROMAL CELL-DERIVED FACTOR 1 RECEPTOR, SDF- COMPND 7 1 RECEPTOR, FUSIN, LEUKOCYTE-DERIVED SEVEN TRANSMEMBRANE DOMAIN COMPND 8 RECEPTOR, LESTR, LCR1, FB22, NPYRL, HM89, LYSIS PROTEIN, MURAMIDASE, COMPND 9 ENDOLYSIN; COMPND 10 EC: 3.2.1.17; COMPND 11 ENGINEERED: YES; COMPND 12 MUTATION: YES; COMPND 13 MOL_ID: 2; COMPND 14 MOLECULE: VIRAL MACROPHAGE INFLAMMATORY PROTEIN 2; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: VIRAL MACROPHAGE INFLAMMATORY PROTEIN II, VMIP-II, VMIP-1B; COMPND 17 ENGINEERED: YES; COMPND 18 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_TAXID: 9606, 10665; SOURCE 4 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PFASTBAC; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8 STRAIN GK18; SOURCE 10 ORGANISM_COMMON: HHV-8; SOURCE 11 ORGANISM_TAXID: 868565; SOURCE 12 GENE: ORF K4; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS HUMAN CHEMOKINE-CHEMOKINE RECEPTOR COMPLEX, GPCR SIGNALING, PSI- KEYWDS 2 BIOLOGY, GPCR NETWORK, MEMBRANE PROTEIN, GPCR, CXCR4, VIRAL KEYWDS 3 ANTAGONIST CHEMOKINE VMIP-II, MEMBRANE, LIPIDIC CUBIC PHASE, T4L, KEYWDS 4 STRUCTURAL GENOMICS, SIGNALING PROTEIN, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR L.QIN,I.KUFAREVA,L.HOLDEN,C.WANG,Y.ZHENG,H.WU,G.FENALTI,G.W.HAN, AUTHOR 2 V.CHEREZOV,R.ABAGYAN,R.C.STEVENS,T.M.HANDEL,GPCR NETWORK (GPCR) REVDAT 5 22-NOV-17 4RWS 1 REMARK REVDAT 4 02-AUG-17 4RWS 1 SOURCE REMARK REVDAT 3 15-APR-15 4RWS 1 JRNL REVDAT 2 25-FEB-15 4RWS 1 JRNL REVDAT 1 11-FEB-15 4RWS 0 JRNL AUTH L.QIN,I.KUFAREVA,L.G.HOLDEN,C.WANG,Y.ZHENG,C.ZHAO,G.FENALTI, JRNL AUTH 2 H.WU,G.W.HAN,V.CHEREZOV,R.ABAGYAN,R.C.STEVENS,T.M.HANDEL JRNL TITL STRUCTURAL BIOLOGY. CRYSTAL STRUCTURE OF THE CHEMOKINE JRNL TITL 2 RECEPTOR CXCR4 IN COMPLEX WITH A VIRAL CHEMOKINE. JRNL REF SCIENCE V. 347 1117 2015 JRNL REFN ISSN 0036-8075 JRNL PMID 25612609 JRNL DOI 10.1126/SCIENCE.1261064 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 85.6 REMARK 3 NUMBER OF REFLECTIONS : 15153 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.251 REMARK 3 R VALUE (WORKING SET) : 0.249 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 767 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 3.3100 - 3.1000 0.86 1520 79 0.2504 0.2421 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 82.26 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.16 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 12.82150 REMARK 3 B22 (A**2) : -1.47950 REMARK 3 B33 (A**2) : -11.34200 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 4057 REMARK 3 ANGLE : 0.940 5535 REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL 594 REMARK 3 DIHEDRAL : NULL 1806 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|23 - A|303 } REMARK 3 ORIGIN FOR THE GROUP (A): 99.7894 2.4949 47.9252 REMARK 3 T TENSOR REMARK 3 T11: 0.2549 T22: -0.2657 REMARK 3 T33: -0.4269 T12: -0.0538 REMARK 3 T13: -0.0028 T23: -0.0361 REMARK 3 L TENSOR REMARK 3 L11: 1.3098 L22: 2.8554 REMARK 3 L33: 6.9762 L12: -0.0287 REMARK 3 L13: -1.5603 L23: 1.3744 REMARK 3 S TENSOR REMARK 3 S11: 0.0272 S12: -0.1203 S13: -0.0917 REMARK 3 S21: -0.0130 S22: 0.0710 S23: -0.3034 REMARK 3 S31: 0.0235 S32: 0.5794 S33: -0.0981 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1002 - A|1164 } REMARK 3 ORIGIN FOR THE GROUP (A): 86.7705 25.2500 82.4686 REMARK 3 T TENSOR REMARK 3 T11: 0.6079 T22: -0.3399 REMARK 3 T33: -0.6079 T12: -0.0860 REMARK 3 T13: 0.1059 T23: -0.0550 REMARK 3 L TENSOR REMARK 3 L11: 5.9286 L22: 5.4991 REMARK 3 L33: 3.5594 L12: -1.3641 REMARK 3 L13: 0.9960 L23: 0.5408 REMARK 3 S TENSOR REMARK 3 S11: 0.1015 S12: 0.2827 S13: -0.0150 REMARK 3 S21: -0.7653 S22: 0.0573 S23: -0.2909 REMARK 3 S31: -0.8946 S32: 0.4631 S33: -0.1587 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|1 - C|70 } REMARK 3 ORIGIN FOR THE GROUP (A): 100.4600 8.0975 10.0361 REMARK 3 T TENSOR REMARK 3 T11: 0.5890 T22: -0.2539 REMARK 3 T33: -0.4969 T12: -0.1526 REMARK 3 T13: 0.1134 T23: 0.0386 REMARK 3 L TENSOR REMARK 3 L11: 0.9662 L22: 9.1126 REMARK 3 L33: 8.8686 L12: 0.1236 REMARK 3 L13: -0.3782 L23: 5.1155 REMARK 3 S TENSOR REMARK 3 S11: 0.0263 S12: 0.0019 S13: -0.0116 REMARK 3 S21: 0.1181 S22: -0.0586 S23: 0.2515 REMARK 3 S31: -0.0536 S32: -0.2730 S33: 0.0323 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4RWS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000087892. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-MAR-14; 21-FEB-14 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 10 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-B; 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332; 1.0332 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL; ACCEL FIXED EXIT REMARK 200 DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; PIXEL REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; PSI REMARK 200 PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16747 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 8.800 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7 REMARK 200 DATA REDUNDANCY IN SHELL : 7.50 REMARK 200 R MERGE FOR SHELL (I) : 0.69000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3OE0, PDB ENTRY 2FHT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.01 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 5.5, 28% PEG REMARK 280 400, 120 MM AMMONIUM PHOSPHATE DIBASIC, 2-6% POLYPROPYLENE P400, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 41.16000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.91350 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 94.88300 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 41.16000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.91350 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 94.88300 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 41.16000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.91350 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 94.88300 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 41.16000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.91350 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 94.88300 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2600 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25900 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 GLU A 2 REMARK 465 GLY A 3 REMARK 465 ILE A 4 REMARK 465 SER A 5 REMARK 465 ILE A 6 REMARK 465 TYR A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 ASP A 10 REMARK 465 ASN A 11 REMARK 465 TYR A 12 REMARK 465 THR A 13 REMARK 465 GLU A 14 REMARK 465 GLU A 15 REMARK 465 MET A 16 REMARK 465 GLY A 17 REMARK 465 SER A 18 REMARK 465 GLY A 19 REMARK 465 ASP A 20 REMARK 465 TYR A 21 REMARK 465 ASP A 22 REMARK 465 LYS A 67 REMARK 465 LYS A 68 REMARK 465 LEU A 69 REMARK 465 ARG A 70 REMARK 465 PHE A 304 REMARK 465 LEU A 305 REMARK 465 GLY A 306 REMARK 465 ALA A 307 REMARK 465 LYS A 308 REMARK 465 PHE A 309 REMARK 465 LYS A 310 REMARK 465 THR A 311 REMARK 465 SER A 312 REMARK 465 ALA A 313 REMARK 465 GLN A 314 REMARK 465 HIS A 315 REMARK 465 ALA A 316 REMARK 465 LEU A 317 REMARK 465 THR A 318 REMARK 465 SER A 319 REMARK 465 GLY A 320 REMARK 465 ARG A 321 REMARK 465 PRO A 322 REMARK 465 LEU A 323 REMARK 465 GLU A 324 REMARK 465 VAL A 325 REMARK 465 LEU A 326 REMARK 465 PHE A 327 REMARK 465 GLN A 328 REMARK 465 ARG C 71 REMARK 465 TYR C 72 REMARK 465 PRO C 73 REMARK 465 TYR C 74 REMARK 465 ASP C 75 REMARK 465 VAL C 76 REMARK 465 PRO C 77 REMARK 465 ASP C 78 REMARK 465 TYR C 79 REMARK 465 ALA C 80 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 38 CG CD CE NZ REMARK 470 LYS A 75 CG CD CE NZ REMARK 470 ASN A 143 CG OD1 ND2 REMARK 470 LYS A 149 CG CD CE NZ REMARK 470 LYS A1019 CD CE NZ REMARK 470 ARG A1076 CG CD NE CZ NH1 NH2 REMARK 470 ILE A1078 CG1 CG2 CD1 REMARK 470 ARG A1080 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 LEU A1084 CG CD1 CD2 REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 THR A1115 OG1 CG2 REMARK 470 ARG A1119 CG CD NE CZ NH1 NH2 REMARK 470 GLN A1122 CD OE1 NE2 REMARK 470 GLN A1123 CG CD OE1 NE2 REMARK 470 LYS A1124 CG CD CE NZ REMARK 470 GLU A1128 CG CD OE1 OE2 REMARK 470 ASN A1132 CG OD1 ND2 REMARK 470 LYS A1135 CG CD CE NZ REMARK 470 ARG A1137 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1147 CD CE NZ REMARK 470 SER A1164 OG REMARK 470 GLN A 233 CG CD OE1 NE2 REMARK 470 ARG A 235 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 236 CE NZ REMARK 470 LYS A 239 CG CD CE NZ REMARK 470 LYS C 17 CG CD CE NZ REMARK 470 ARG C 18 CG CD NE CZ NH1 NH2 REMARK 470 LEU C 24 CG CD1 CD2 REMARK 470 LYS C 56 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 100 -114.40 -102.62 REMARK 500 ASN A 143 80.00 -156.02 REMARK 500 LYS A 154 -53.55 -126.42 REMARK 500 VAL A 160 -58.51 -123.97 REMARK 500 ASP A 181 -98.60 59.04 REMARK 500 MET A 205 -71.24 -73.70 REMARK 500 LEU A 208 -52.39 -147.35 REMARK 500 ASP A1010 -70.56 -76.41 REMARK 500 ASN A1055 36.13 -98.78 REMARK 500 ASP A1092 -151.33 -79.11 REMARK 500 PHE A1114 34.84 -97.42 REMARK 500 SER A1164 -127.83 -137.79 REMARK 500 HIS C 6 -71.02 -62.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ODU RELATED DB: PDB REMARK 900 CXCR4 WITH SMALL-MOLECULE ANTAGONIST IT1T IN P21 SPACEGROUP REMARK 900 RELATED ID: 3OE6 RELATED DB: PDB REMARK 900 CXCR4 WITH SMALL-MOLECULE ANTAGONIST IT1T IN I222 SPACEGROUP REMARK 900 RELATED ID: 3OE8 RELATED DB: PDB REMARK 900 CXCR4 WITH SMALL-MOLECULE ANTAGONIST IT1T IN P1 SPACEGROUP REMARK 900 RELATED ID: 3OE9 RELATED DB: PDB REMARK 900 CXCR4 WITH SMALL-MOLECULE IN P1 SPACEGROUP REMARK 900 RELATED ID: 3OE0 RELATED DB: PDB REMARK 900 CXCR4 WITH CYCLIC PEPTIDE ANTAGONISTS. REMARK 900 RELATED ID: GPCR-34 RELATED DB: TARGETTRACK DBREF 4RWS A 2 228 UNP P61073 CXCR4_HUMAN 2 228 DBREF 4RWS A 1002 1161 UNP P00720 LYS_BPT4 1002 1161 DBREF 4RWS A 231 319 UNP P61073 CXCR4_HUMAN 231 319 DBREF 4RWS C 1 71 UNP Q98157 VMI2_HHV8P 24 94 SEQADV 4RWS ASP A -8 UNP P61073 EXPRESSION TAG SEQADV 4RWS TYR A -7 UNP P61073 EXPRESSION TAG SEQADV 4RWS LYS A -6 UNP P61073 EXPRESSION TAG SEQADV 4RWS ASP A -5 UNP P61073 EXPRESSION TAG SEQADV 4RWS ASP A -4 UNP P61073 EXPRESSION TAG SEQADV 4RWS ASP A -3 UNP P61073 EXPRESSION TAG SEQADV 4RWS ASP A -2 UNP P61073 EXPRESSION TAG SEQADV 4RWS GLY A -1 UNP P61073 EXPRESSION TAG SEQADV 4RWS ALA A 0 UNP P61073 EXPRESSION TAG SEQADV 4RWS PRO A 1 UNP P61073 EXPRESSION TAG SEQADV 4RWS TRP A 125 UNP P61073 LEU 125 ENGINEERED MUTATION SEQADV 4RWS CYS A 187 UNP P61073 ASP 187 ENGINEERED MUTATION SEQADV 4RWS THR A 1054 UNP P00720 CYS 1054 ENGINEERED MUTATION SEQADV 4RWS ALA A 1097 UNP P00720 CYS 1097 ENGINEERED MUTATION SEQADV 4RWS SER A 1162 UNP P00720 LINKER SEQADV 4RWS GLY A 1163 UNP P00720 LINKER SEQADV 4RWS SER A 1164 UNP P00720 LINKER SEQADV 4RWS PRO A 240 UNP P61073 THR 240 ENGINEERED MUTATION SEQADV 4RWS GLY A 320 UNP P61073 EXPRESSION TAG SEQADV 4RWS ARG A 321 UNP P61073 EXPRESSION TAG SEQADV 4RWS PRO A 322 UNP P61073 EXPRESSION TAG SEQADV 4RWS LEU A 323 UNP P61073 EXPRESSION TAG SEQADV 4RWS GLU A 324 UNP P61073 EXPRESSION TAG SEQADV 4RWS VAL A 325 UNP P61073 EXPRESSION TAG SEQADV 4RWS LEU A 326 UNP P61073 EXPRESSION TAG SEQADV 4RWS PHE A 327 UNP P61073 EXPRESSION TAG SEQADV 4RWS GLN A 328 UNP P61073 EXPRESSION TAG SEQADV 4RWS CYS C 5 UNP Q98157 TRP 28 ENGINEERED MUTATION SEQADV 4RWS TYR C 72 UNP Q98157 EXPRESSION TAG SEQADV 4RWS PRO C 73 UNP Q98157 EXPRESSION TAG SEQADV 4RWS TYR C 74 UNP Q98157 EXPRESSION TAG SEQADV 4RWS ASP C 75 UNP Q98157 EXPRESSION TAG SEQADV 4RWS VAL C 76 UNP Q98157 EXPRESSION TAG SEQADV 4RWS PRO C 77 UNP Q98157 EXPRESSION TAG SEQADV 4RWS ASP C 78 UNP Q98157 EXPRESSION TAG SEQADV 4RWS TYR C 79 UNP Q98157 EXPRESSION TAG SEQADV 4RWS ALA C 80 UNP Q98157 EXPRESSION TAG SEQRES 1 A 498 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO GLU GLY ILE SEQRES 2 A 498 SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET GLY SEQRES 3 A 498 SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE ARG SEQRES 4 A 498 GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO THR SEQRES 5 A 498 ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY ASN SEQRES 6 A 498 GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS LEU SEQRES 7 A 498 ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER VAL SEQRES 8 A 498 ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP ALA SEQRES 9 A 498 VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE LEU SEQRES 10 A 498 CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU TYR SEQRES 11 A 498 SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP ARG SEQRES 12 A 498 TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG PRO SEQRES 13 A 498 ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY VAL SEQRES 14 A 498 TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE ILE SEQRES 15 A 498 PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE CYS SEQRES 16 A 498 CYS ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL PHE SEQRES 17 A 498 GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO GLY SEQRES 18 A 498 ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER LYS SEQRES 19 A 498 LEU SER HIS ASN ILE PHE GLU MET LEU ARG ILE ASP GLU SEQRES 20 A 498 GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR SEQRES 21 A 498 TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SEQRES 22 A 498 SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE SEQRES 23 A 498 GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA SEQRES 24 A 498 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG SEQRES 25 A 498 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SEQRES 26 A 498 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET SEQRES 27 A 498 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR SEQRES 28 A 498 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU SEQRES 29 A 498 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN SEQRES 30 A 498 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG SEQRES 31 A 498 THR GLY THR TRP ASP ALA TYR SER GLY SER GLY HIS GLN SEQRES 32 A 498 LYS ARG LYS ALA LEU LYS PRO THR VAL ILE LEU ILE LEU SEQRES 33 A 498 ALA PHE PHE ALA CYS TRP LEU PRO TYR TYR ILE GLY ILE SEQRES 34 A 498 SER ILE ASP SER PHE ILE LEU LEU GLU ILE ILE LYS GLN SEQRES 35 A 498 GLY CYS GLU PHE GLU ASN THR VAL HIS LYS TRP ILE SER SEQRES 36 A 498 ILE THR GLU ALA LEU ALA PHE PHE HIS CYS CYS LEU ASN SEQRES 37 A 498 PRO ILE LEU TYR ALA PHE LEU GLY ALA LYS PHE LYS THR SEQRES 38 A 498 SER ALA GLN HIS ALA LEU THR SER GLY ARG PRO LEU GLU SEQRES 39 A 498 VAL LEU PHE GLN SEQRES 1 C 80 LEU GLY ALA SER CYS HIS ARG PRO ASP LYS CYS CYS LEU SEQRES 2 C 80 GLY TYR GLN LYS ARG PRO LEU PRO GLN VAL LEU LEU SER SEQRES 3 C 80 SER TRP TYR PRO THR SER GLN LEU CYS SER LYS PRO GLY SEQRES 4 C 80 VAL ILE PHE LEU THR LYS ARG GLY ARG GLN VAL CYS ALA SEQRES 5 C 80 ASP LYS SER LYS ASP TRP VAL LYS LYS LEU MET GLN GLN SEQRES 6 C 80 LEU PRO VAL THR ALA ARG TYR PRO TYR ASP VAL PRO ASP SEQRES 7 C 80 TYR ALA HELIX 1 1 ARG A 30 GLY A 64 1 35 HELIX 2 2 MET A 72 ASP A 84 1 13 HELIX 3 3 ASP A 84 ILE A 89 1 6 HELIX 4 4 THR A 90 ALA A 100 1 11 HELIX 5 5 GLY A 105 VAL A 139 1 35 HELIX 6 6 HIS A 140 ASN A 143 5 4 HELIX 7 7 SER A 144 LYS A 154 1 11 HELIX 8 8 LYS A 154 VAL A 160 1 7 HELIX 9 9 VAL A 160 LEU A 167 1 8 HELIX 10 10 ILE A 169 PHE A 174 1 6 HELIX 11 11 ASN A 192 LEU A 208 1 17 HELIX 12 12 LEU A 208 GLU A 1011 1 31 HELIX 13 13 SER A 1038 GLY A 1051 1 14 HELIX 14 14 THR A 1059 LEU A 1079 1 21 HELIX 15 15 LEU A 1084 ASP A 1089 1 6 HELIX 16 16 ALA A 1093 MET A 1106 1 14 HELIX 17 17 GLY A 1107 ALA A 1112 1 6 HELIX 18 18 PHE A 1114 GLN A 1123 1 10 HELIX 19 19 ARG A 1125 ALA A 1134 1 10 HELIX 20 20 THR A 1142 GLY A 1156 1 15 HELIX 21 21 THR A 1157 TYR A 1161 5 5 HELIX 22 22 LEU A 238 LEU A 267 1 30 HELIX 23 23 GLY A 273 PHE A 292 1 20 HELIX 24 24 PHE A 293 CYS A 295 5 3 HELIX 25 25 CYS A 296 LEU A 301 1 6 HELIX 26 26 LYS C 56 LEU C 66 1 11 SHEET 1 A 2 ALA A 175 ALA A 180 0 SHEET 2 A 2 ARG A 183 ARG A 188 -1 O ILE A 185 N SER A 178 SHEET 1 B 3 TYR A1018 LYS A1019 0 SHEET 2 B 3 TYR A1025 ILE A1027 -1 O THR A1026 N TYR A1018 SHEET 3 B 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SHEET 1 C 3 LEU C 25 PRO C 30 0 SHEET 2 C 3 VAL C 40 THR C 44 -1 O ILE C 41 N TYR C 29 SHEET 3 C 3 GLN C 49 ALA C 52 -1 O VAL C 50 N PHE C 42 SSBOND 1 CYS A 28 CYS A 274 1555 1555 2.04 SSBOND 2 CYS A 109 CYS A 186 1555 1555 2.04 SSBOND 3 CYS A 187 CYS C 5 1555 1555 2.03 SSBOND 4 CYS C 11 CYS C 35 1555 1555 2.04 SSBOND 5 CYS C 12 CYS C 51 1555 1555 2.04 CRYST1 82.320 121.827 189.766 90.00 90.00 90.00 I 2 2 2 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 0.012148 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008208 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005270 0.00000 ATOM 1 N SER A 23 103.085 23.843 6.483 1.00137.99 N ANISOU 1 N SER A 23 37086 10114 5231 -637 5445 1604 N ATOM 2 CA SER A 23 101.791 23.604 7.117 1.00137.55 C ANISOU 2 CA SER A 23 37237 10014 5010 -15 4994 1704 C ATOM 3 C SER A 23 101.451 22.095 7.090 1.00139.65 C ANISOU 3 C SER A 23 37306 10505 5251 111 4737 1552 C ATOM 4 O SER A 23 100.893 21.604 6.102 1.00140.27 O ANISOU 4 O SER A 23 37378 10824 5095 444 4449 1612 O ATOM 5 CB SER A 23 100.704 24.430 6.429 1.00140.67 C ANISOU 5 CB SER A 23 37340 10742 5365 611 4521 1994 C ATOM 6 OG SER A 23 100.618 24.131 5.045 1.00147.08 O ANISOU 6 OG SER A 23 37386 12181 6316 680 4263 2048 O ATOM 7 N MET A 24 101.832 21.359 8.166 1.00135.73 N ANISOU 7 N MET A 24 37246 9625 4702 -197 4994 1345 N ATOM 8 CA MET A 24 101.617 19.907 8.293 1.00132.47 C ANISOU 8 CA MET A 24 36322 9549 4463 -156 4720 1180 C ATOM 9 C MET A 24 101.181 19.509 9.714 1.00130.65 C ANISOU 9 C MET A 24 35169 9671 4800 -53 4365 1107 C ATOM 10 O MET A 24 101.602 20.139 10.689 1.00129.47 O ANISOU 10 O MET A 24 34985 9340 4868 -317 4592 1081 O ATOM 11 CB MET A 24 102.888 19.122 7.910 1.00133.81 C ANISOU 11 CB MET A 24 36117 9852 4872 -824 5128 938 C ATOM 12 CG MET A 24 103.167 19.093 6.412 1.00139.96 C ANISOU 12 CG MET A 24 37132 10684 5364 -854 5253 976 C ATOM 13 SD MET A 24 104.708 18.251 5.976 1.00142.78 S ANISOU 13 SD MET A 24 36886 11290 6073 -1593 5731 687 S ATOM 14 CE MET A 24 104.675 18.431 4.215 1.00141.73 C ANISOU 14 CE MET A 24 36929 11305 5618 -1426 5704 807 C ATOM 15 N LYS A 25 100.341 18.451 9.823 1.00123.49 N ANISOU 15 N LYS A 25 33536 9269 4114 301 3823 1062 N ATOM 16 CA LYS A 25 99.846 17.964 11.116 1.00118.20 C ANISOU 16 CA LYS A 25 31992 8959 3961 414 3469 991 C ATOM 17 C LYS A 25 100.803 16.908 11.676 1.00118.09 C ANISOU 17 C LYS A 25 31113 9240 4516 -134 3623 740 C ATOM 18 O LYS A 25 101.114 15.933 10.995 1.00116.97 O ANISOU 18 O LYS A 25 30704 9316 4422 -278 3626 619 O ATOM 19 CB LYS A 25 98.407 17.413 11.005 1.00119.38 C ANISOU 19 CB LYS A 25 31819 9504 4035 1055 2826 1059 C ATOM 20 CG LYS A 25 97.767 17.010 12.336 1.00124.80 C ANISOU 20 CG LYS A 25 31685 10537 5197 1205 2467 1002 C ATOM 21 CD LYS A 25 97.738 18.147 13.366 1.00133.03 C ANISOU 21 CD LYS A 25 32974 11278 6294 1262 2600 1105 C ATOM 22 CE LYS A 25 97.190 17.705 14.695 1.00134.12 C ANISOU 22 CE LYS A 25 32294 11757 6908 1360 2285 1033 C ATOM 23 NZ LYS A 25 97.220 18.800 15.699 1.00141.00 N ANISOU 23 NZ LYS A 25 33425 12321 7828 1382 2443 1117 N ATOM 24 N GLU A 26 101.250 17.107 12.925 1.00112.28 N ANISOU 24 N GLU A 26 29960 8513 4189 -406 3742 664 N ATOM 25 CA GLU A 26 102.206 16.223 13.589 1.00108.49 C ANISOU 25 CA GLU A 26 28678 8308 4235 -887 3894 436 C ATOM 26 C GLU A 26 101.568 15.345 14.672 1.00107.82 C ANISOU 26 C GLU A 26 27715 8638 4614 -690 3450 373 C ATOM 27 O GLU A 26 100.584 15.756 15.292 1.00106.87 O ANISOU 27 O GLU A 26 27594 8531 4481 -307 3135 491 O ATOM 28 CB GLU A 26 103.327 17.046 14.235 1.00110.86 C ANISOU 28 CB GLU A 26 29111 8357 4654 -1416 4384 359 C ATOM 29 CG GLU A 26 104.323 17.628 13.256 1.00126.68 C ANISOU 29 CG GLU A 26 31785 10030 6319 -1832 4938 327 C ATOM 30 CD GLU A 26 105.508 18.254 13.957 1.00148.62 C ANISOU 30 CD GLU A 26 34520 12675 9273 -2451 5423 183 C ATOM 31 OE1 GLU A 26 106.463 17.512 14.279 1.00137.69 O ANISOU 31 OE1 GLU A 26 32447 11607 8260 -2855 5586 -39 O ATOM 32 OE2 GLU A 26 105.457 19.474 14.236 1.00143.00 O ANISOU 32 OE2 GLU A 26 34444 11563 8327 -2515 5624 283 O ATOM 33 N PRO A 27 102.153 14.155 14.957 1.00101.40 N ANISOU 33 N PRO A 27 26168 8154 4207 -949 3451 183 N ATOM 34 CA PRO A 27 101.616 13.319 16.040 1.00 96.92 C ANISOU 34 CA PRO A 27 24819 7938 4069 -803 3078 122 C ATOM 35 C PRO A 27 102.072 13.823 17.407 1.00 99.16 C ANISOU 35 C PRO A 27 24818 8188 4672 -1024 3195 86 C ATOM 36 O PRO A 27 103.003 14.627 17.489 1.00100.46 O ANISOU 36 O PRO A 27 25277 8113 4779 -1386 3602 56 O ATOM 37 CB PRO A 27 102.191 11.926 15.736 1.00 96.85 C ANISOU 37 CB PRO A 27 24278 8214 4307 -999 3105 -59 C ATOM 38 CG PRO A 27 103.035 12.077 14.490 1.00104.61 C ANISOU 38 CG PRO A 27 25743 9011 4994 -1244 3498 -97 C ATOM 39 CD PRO A 27 103.335 13.519 14.344 1.00103.51 C ANISOU 39 CD PRO A 27 26299 8480 4551 -1366 3809 14 C ATOM 40 N CYS A 28 101.421 13.353 18.479 1.00 92.88 N ANISOU 40 N CYS A 28 23459 7636 4193 -836 2853 76 N ATOM 41 CA CYS A 28 101.774 13.752 19.836 1.00 91.13 C ANISOU 41 CA CYS A 28 22937 7416 4274 -1019 2919 38 C ATOM 42 C CYS A 28 102.933 12.877 20.343 1.00 90.58 C ANISOU 42 C CYS A 28 22238 7584 4596 -1414 3095 -160 C ATOM 43 O CYS A 28 102.717 11.750 20.793 1.00 87.11 O ANISOU 43 O CYS A 28 21205 7443 4449 -1319 2851 -232 O ATOM 44 CB CYS A 28 100.561 13.683 20.760 1.00 89.95 C ANISOU 44 CB CYS A 28 22503 7414 4259 -636 2497 117 C ATOM 45 SG CYS A 28 100.862 14.318 22.430 1.00 92.74 S ANISOU 45 SG CYS A 28 22596 7727 4916 -818 2565 91 S ATOM 46 N PHE A 29 104.167 13.405 20.241 1.00 87.75 N ANISOU 46 N PHE A 29 22029 7098 4214 -1854 3533 -254 N ATOM 47 CA PHE A 29 105.403 12.739 20.660 1.00 86.06 C ANISOU 47 CA PHE A 29 21244 7134 4321 -2229 3748 -456 C ATOM 48 C PHE A 29 105.504 12.669 22.184 1.00 86.52 C ANISOU 48 C PHE A 29 20759 7377 4738 -2288 3608 -511 C ATOM 49 O PHE A 29 105.331 13.682 22.868 1.00 86.90 O ANISOU 49 O PHE A 29 21036 7246 4734 -2349 3643 -453 O ATOM 50 CB PHE A 29 106.634 13.463 20.085 1.00 91.53 C ANISOU 50 CB PHE A 29 22273 7667 4838 -2706 4272 -557 C ATOM 51 CG PHE A 29 106.884 13.231 18.614 1.00 95.49 C ANISOU 51 CG PHE A 29 23156 8072 5054 -2737 4478 -564 C ATOM 52 CD1 PHE A 29 107.769 12.247 18.189 1.00 98.39 C ANISOU 52 CD1 PHE A 29 23109 8698 5576 -2910 4645 -736 C ATOM 53 CD2 PHE A 29 106.251 14.009 17.652 1.00100.31 C ANISOU 53 CD2 PHE A 29 24565 8328 5218 -2570 4515 -399 C ATOM 54 CE1 PHE A 29 108.006 12.036 16.829 1.00101.79 C ANISOU 54 CE1 PHE A 29 23912 9033 5730 -2947 4855 -751 C ATOM 55 CE2 PHE A 29 106.486 13.794 16.291 1.00105.63 C ANISOU 55 CE2 PHE A 29 25622 8912 5602 -2603 4707 -405 C ATOM 56 CZ PHE A 29 107.363 12.811 15.889 1.00103.50 C ANISOU 56 CZ PHE A 29 24927 8898 5501 -2810 4884 -586 C ATOM 57 N ARG A 30 105.790 11.465 22.708 1.00 79.52 N ANISOU 57 N ARG A 30 19193 6830 4191 -2259 3461 -621 N ATOM 58 CA ARG A 30 105.921 11.199 24.144 1.00 76.13 C ANISOU 58 CA ARG A 30 18210 6615 4102 -2286 3306 -678 C ATOM 59 C ARG A 30 107.406 11.220 24.574 1.00 82.28 C ANISOU 59 C ARG A 30 18621 7591 5049 -2708 3622 -873 C ATOM 60 O ARG A 30 107.717 10.892 25.721 1.00 80.07 O ANISOU 60 O ARG A 30 17832 7546 5045 -2746 3511 -947 O ATOM 61 CB ARG A 30 105.274 9.839 24.508 1.00 70.26 C ANISOU 61 CB ARG A 30 16987 6111 3596 -1965 2942 -672 C ATOM 62 CG ARG A 30 103.870 9.569 23.942 1.00 71.85 C ANISOU 62 CG ARG A 30 17436 6229 3635 -1586 2631 -535 C ATOM 63 CD ARG A 30 102.787 10.529 24.403 1.00 70.56 C ANISOU 63 CD ARG A 30 17568 5901 3342 -1378 2438 -387 C ATOM 64 NE ARG A 30 101.475 10.142 23.882 1.00 71.25 N ANISOU 64 NE ARG A 30 17768 6017 3286 -1007 2117 -292 N ATOM 65 CZ ARG A 30 100.361 10.851 24.038 1.00 82.88 C ANISOU 65 CZ ARG A 30 19497 7398 4596 -723 1909 -162 C ATOM 66 NH1 ARG A 30 100.387 12.008 24.689 1.00 71.23 N ANISOU 66 NH1 ARG A 30 18262 5732 3070 -756 2006 -96 N ATOM 67 NH2 ARG A 30 99.215 10.416 23.532 1.00 67.50 N ANISOU 67 NH2 ARG A 30 17568 5563 2515 -402 1610 -111 N ATOM 68 N GLU A 31 108.312 11.626 23.656 1.00 83.37 N ANISOU 68 N GLU A 31 19018 7658 5003 -3026 4017 -964 N ATOM 69 CA GLU A 31 109.762 11.700 23.871 1.00 85.92 C ANISOU 69 CA GLU A 31 18995 8216 5436 -3464 4363 -1182 C ATOM 70 C GLU A 31 110.144 12.771 24.909 1.00 91.99 C ANISOU 70 C GLU A 31 19762 8958 6232 -3799 4480 -1241 C ATOM 71 O GLU A 31 111.183 12.630 25.558 1.00 92.34 O ANISOU 71 O GLU A 31 19291 9331 6464 -4086 4612 -1434 O ATOM 72 CB GLU A 31 110.497 11.983 22.549 1.00 91.12 C ANISOU 72 CB GLU A 31 20018 8766 5836 -3743 4785 -1261 C ATOM 73 CG GLU A 31 110.694 10.769 21.648 1.00101.86 C ANISOU 73 CG GLU A 31 21173 10294 7236 -3554 4784 -1311 C ATOM 74 CD GLU A 31 109.524 10.270 20.816 1.00123.15 C ANISOU 74 CD GLU A 31 24230 12790 9771 -3138 4518 -1138 C ATOM 75 OE1 GLU A 31 108.418 10.074 21.369 1.00113.19 O ANISOU 75 OE1 GLU A 31 22940 11483 8583 -2802 4121 -999 O ATOM 76 OE2 GLU A 31 109.748 9.986 19.617 1.00122.02 O ANISOU 76 OE2 GLU A 31 24345 12583 9436 -3158 4707 -1164 O ATOM 77 N GLU A 32 109.307 13.819 25.077 1.00 89.75 N ANISOU 77 N GLU A 32 20047 8304 5750 -3744 4426 -1086 N ATOM 78 CA GLU A 32 109.526 14.900 26.050 1.00 91.19 C ANISOU 78 CA GLU A 32 20345 8386 5918 -4046 4537 -1129 C ATOM 79 C GLU A 32 109.309 14.389 27.500 1.00 92.20 C ANISOU 79 C GLU A 32 19858 8797 6376 -3887 4194 -1150 C ATOM 80 O GLU A 32 109.801 15.006 28.451 1.00 92.58 O ANISOU 80 O GLU A 32 19775 8915 6485 -4197 4285 -1257 O ATOM 81 CB GLU A 32 108.624 16.120 25.758 1.00 94.13 C ANISOU 81 CB GLU A 32 21569 8240 5954 -3948 4580 -939 C ATOM 82 CG GLU A 32 107.125 15.850 25.707 1.00103.22 C ANISOU 82 CG GLU A 32 22901 9249 7069 -3339 4159 -706 C ATOM 83 CD GLU A 32 106.267 17.065 25.404 1.00128.50 C ANISOU 83 CD GLU A 32 26938 11971 9914 -3169 4200 -521 C ATOM 84 OE1 GLU A 32 106.316 18.045 26.183 1.00121.86 O ANISOU 84 OE1 GLU A 32 26345 10936 9021 -3352 4316 -527 O ATOM 85 OE2 GLU A 32 105.507 17.017 24.410 1.00126.26 O ANISOU 85 OE2 GLU A 32 27067 11514 9392 -2818 4097 -368 O ATOM 86 N ASN A 33 108.591 13.260 27.651 1.00 85.53 N ANISOU 86 N ASN A 33 18668 8111 5721 -3432 3820 -1060 N ATOM 87 CA ASN A 33 108.320 12.612 28.935 1.00 82.34 C ANISOU 87 CA ASN A 33 17716 7959 5610 -3238 3492 -1063 C ATOM 88 C ASN A 33 109.455 11.650 29.303 1.00 87.26 C ANISOU 88 C ASN A 33 17641 9031 6481 -3359 3530 -1252 C ATOM 89 O ASN A 33 109.692 11.410 30.487 1.00 85.72 O ANISOU 89 O ASN A 33 17000 9079 6489 -3365 3376 -1314 O ATOM 90 CB ASN A 33 106.983 11.855 28.880 1.00 78.40 C ANISOU 90 CB ASN A 33 17226 7400 5162 -2726 3107 -888 C ATOM 91 CG ASN A 33 105.783 12.674 28.456 1.00 93.18 C ANISOU 91 CG ASN A 33 19716 8907 6780 -2501 3019 -703 C ATOM 92 OD1 ASN A 33 105.779 13.910 28.495 1.00 88.38 O ANISOU 92 OD1 ASN A 33 19581 8028 5971 -2669 3201 -669 O ATOM 93 ND2 ASN A 33 104.722 11.991 28.059 1.00 80.69 N ANISOU 93 ND2 ASN A 33 18148 7324 5187 -2104 2736 -587 N ATOM 94 N ALA A 34 110.145 11.100 28.280 1.00 86.14 N ANISOU 94 N ALA A 34 17421 9004 6303 -3424 3733 -1342 N ATOM 95 CA ALA A 34 111.242 10.139 28.413 1.00 87.01 C ANISOU 95 CA ALA A 34 16901 9545 6612 -3467 3800 -1522 C ATOM 96 C ALA A 34 112.486 10.763 29.063 1.00 94.18 C ANISOU 96 C ALA A 34 17478 10745 7562 -3927 4042 -1742 C ATOM 97 O ALA A 34 113.054 10.151 29.971 1.00 93.36 O ANISOU 97 O ALA A 34 16768 11033 7673 -3868 3908 -1851 O ATOM 98 CB ALA A 34 111.606 9.574 27.048 1.00 89.38 C ANISOU 98 CB ALA A 34 17306 9844 6812 -3434 4006 -1564 C ATOM 99 N ASN A 35 112.911 11.964 28.605 1.00 94.33 N ANISOU 99 N ASN A 35 17903 10583 7354 -4389 4399 -1816 N ATOM 100 CA ASN A 35 114.092 12.650 29.142 1.00 97.78 C ANISOU 100 CA ASN A 35 18061 11301 7790 -4923 4673 -2059 C ATOM 101 C ASN A 35 113.820 13.201 30.553 1.00100.26 C ANISOU 101 C ASN A 35 18274 11637 8186 -4998 4468 -2053 C ATOM 102 O ASN A 35 114.764 13.336 31.334 1.00101.91 O ANISOU 102 O ASN A 35 17998 12241 8482 -5310 4537 -2267 O ATOM 103 CB ASN A 35 114.570 13.774 28.213 1.00103.58 C ANISOU 103 CB ASN A 35 19346 11782 8227 -5440 5153 -2144 C ATOM 104 CG ASN A 35 113.544 14.837 27.908 1.00129.30 C ANISOU 104 CG ASN A 35 23476 14432 11222 -5433 5184 -1936 C ATOM 105 OD1 ASN A 35 112.823 14.763 26.910 1.00125.70 O ANISOU 105 OD1 ASN A 35 23519 13641 10601 -5166 5173 -1758 O ATOM 106 ND2 ASN A 35 113.494 15.877 28.731 1.00120.71 N ANISOU 106 ND2 ASN A 35 22612 13194 10059 -5727 5242 -1964 N ATOM 107 N PHE A 36 112.541 13.506 30.877 1.00 93.61 N ANISOU 107 N PHE A 36 17862 10404 7301 -4705 4216 -1822 N ATOM 108 CA PHE A 36 112.108 14.008 32.187 1.00 91.96 C ANISOU 108 CA PHE A 36 17629 10158 7155 -4714 4011 -1788 C ATOM 109 C PHE A 36 112.367 12.953 33.276 1.00 93.24 C ANISOU 109 C PHE A 36 17044 10779 7604 -4475 3692 -1846 C ATOM 110 O PHE A 36 112.916 13.281 34.329 1.00 93.74 O ANISOU 110 O PHE A 36 16795 11094 7728 -4721 3669 -1986 O ATOM 111 CB PHE A 36 110.614 14.403 32.148 1.00 91.21 C ANISOU 111 CB PHE A 36 18124 9579 6953 -4357 3808 -1522 C ATOM 112 CG PHE A 36 109.996 14.753 33.485 1.00 91.00 C ANISOU 112 CG PHE A 36 18063 9505 7007 -4262 3563 -1462 C ATOM 113 CD1 PHE A 36 110.125 16.030 34.018 1.00 96.40 C ANISOU 113 CD1 PHE A 36 19111 9983 7535 -4633 3751 -1521 C ATOM 114 CD2 PHE A 36 109.265 13.810 34.200 1.00 89.46 C ANISOU 114 CD2 PHE A 36 17520 9448 7024 -3816 3170 -1352 C ATOM 115 CE1 PHE A 36 109.557 16.351 35.256 1.00 95.70 C ANISOU 115 CE1 PHE A 36 19007 9846 7510 -4541 3539 -1475 C ATOM 116 CE2 PHE A 36 108.704 14.130 35.440 1.00 90.77 C ANISOU 116 CE2 PHE A 36 17660 9575 7253 -3739 2966 -1305 C ATOM 117 CZ PHE A 36 108.848 15.400 35.956 1.00 90.98 C ANISOU 117 CZ PHE A 36 18029 9410 7129 -4088 3146 -1364 C ATOM 118 N ASN A 37 111.968 11.696 33.007 1.00 86.98 N ANISOU 118 N ASN A 37 16011 10078 6959 -4002 3455 -1742 N ATOM 119 CA ASN A 37 112.121 10.560 33.913 1.00 84.82 C ANISOU 119 CA ASN A 37 15132 10170 6928 -3692 3157 -1762 C ATOM 120 C ASN A 37 113.593 10.186 34.107 1.00 91.71 C ANISOU 120 C ASN A 37 15383 11578 7885 -3897 3297 -2013 C ATOM 121 O ASN A 37 113.987 9.877 35.227 1.00 91.31 O ANISOU 121 O ASN A 37 14865 11867 7961 -3845 3112 -2091 O ATOM 122 CB ASN A 37 111.343 9.347 33.386 1.00 82.35 C ANISOU 122 CB ASN A 37 14833 9756 6701 -3188 2942 -1602 C ATOM 123 CG ASN A 37 109.838 9.515 33.329 1.00101.43 C ANISOU 123 CG ASN A 37 17717 11764 9058 -2925 2736 -1375 C ATOM 124 OD1 ASN A 37 109.257 10.502 33.803 1.00 93.68 O ANISOU 124 OD1 ASN A 37 17053 10555 7987 -3032 2711 -1307 O ATOM 125 ND2 ASN A 37 109.163 8.527 32.762 1.00 92.54 N ANISOU 125 ND2 ASN A 37 16630 10558 7972 -2567 2582 -1266 N ATOM 126 N LYS A 38 114.405 10.255 33.031 1.00 91.14 N ANISOU 126 N LYS A 38 15304 11603 7723 -4129 3628 -2147 N ATOM 127 CA LYS A 38 115.830 9.902 33.011 1.00 94.49 C ANISOU 127 CA LYS A 38 15117 12578 8206 -4317 3809 -2409 C ATOM 128 C LYS A 38 116.715 10.817 33.900 1.00101.34 C ANISOU 128 C LYS A 38 15691 13779 9036 -4832 3929 -2642 C ATOM 129 O LYS A 38 117.875 10.470 34.138 1.00104.11 O ANISOU 129 O LYS A 38 15408 14697 9452 -4945 4002 -2877 O ATOM 130 CB LYS A 38 116.357 9.958 31.569 1.00 99.58 C ANISOU 130 CB LYS A 38 15938 13175 8722 -4508 4189 -2495 C ATOM 131 N ILE A 39 116.185 11.955 34.396 1.00 97.17 N ANISOU 131 N ILE A 39 15602 12928 8390 -5131 3948 -2593 N ATOM 132 CA ILE A 39 116.967 12.891 35.210 1.00100.23 C ANISOU 132 CA ILE A 39 15792 13583 8708 -5683 4084 -2827 C ATOM 133 C ILE A 39 116.439 12.936 36.664 1.00101.20 C ANISOU 133 C ILE A 39 15800 13733 8918 -5520 3722 -2753 C ATOM 134 O ILE A 39 117.239 12.822 37.596 1.00102.67 O ANISOU 134 O ILE A 39 15410 14433 9166 -5657 3623 -2948 O ATOM 135 CB ILE A 39 116.961 14.317 34.566 1.00106.12 C ANISOU 135 CB ILE A 39 17219 13913 9190 -6273 4500 -2879 C ATOM 136 CG1 ILE A 39 117.511 14.275 33.111 1.00109.34 C ANISOU 136 CG1 ILE A 39 17770 14290 9484 -6456 4887 -2956 C ATOM 137 CG2 ILE A 39 117.747 15.330 35.427 1.00110.61 C ANISOU 137 CG2 ILE A 39 17638 14728 9660 -6919 4670 -3147 C ATOM 138 CD1 ILE A 39 117.265 15.537 32.241 1.00119.54 C ANISOU 138 CD1 ILE A 39 19919 15023 10478 -6902 5292 -2923 C ATOM 139 N PHE A 40 115.117 13.111 36.851 1.00 93.58 N ANISOU 139 N PHE A 40 15363 12251 7941 -5232 3529 -2487 N ATOM 140 CA PHE A 40 114.495 13.278 38.166 1.00 91.06 C ANISOU 140 CA PHE A 40 15045 11878 7676 -5104 3232 -2404 C ATOM 141 C PHE A 40 114.215 11.961 38.914 1.00 91.23 C ANISOU 141 C PHE A 40 14599 12154 7909 -4538 2825 -2298 C ATOM 142 O PHE A 40 114.483 11.902 40.113 1.00 91.16 O ANISOU 142 O PHE A 40 14246 12439 7953 -4552 2629 -2375 O ATOM 143 CB PHE A 40 113.169 14.044 38.034 1.00 90.52 C ANISOU 143 CB PHE A 40 15737 11166 7490 -5012 3221 -2173 C ATOM 144 CG PHE A 40 113.327 15.499 37.655 1.00 95.33 C ANISOU 144 CG PHE A 40 16922 11447 7852 -5555 3593 -2257 C ATOM 145 CD1 PHE A 40 113.476 16.477 38.633 1.00100.19 C ANISOU 145 CD1 PHE A 40 17664 12032 8370 -5940 3649 -2372 C ATOM 146 CD2 PHE A 40 113.316 15.893 36.322 1.00 98.99 C ANISOU 146 CD2 PHE A 40 17857 11602 8152 -5683 3901 -2221 C ATOM 147 CE1 PHE A 40 113.622 17.823 38.283 1.00104.45 C ANISOU 147 CE1 PHE A 40 18816 12215 8655 -6458 4027 -2453 C ATOM 148 CE2 PHE A 40 113.463 17.239 35.972 1.00105.16 C ANISOU 148 CE2 PHE A 40 19255 12030 8670 -6182 4273 -2289 C ATOM 149 CZ PHE A 40 113.614 18.194 36.954 1.00105.11 C ANISOU 149 CZ PHE A 40 19392 11974 8572 -6570 4342 -2406 C ATOM 150 N LEU A 41 113.666 10.933 38.241 1.00 84.60 N ANISOU 150 N LEU A 41 13792 11187 7166 -4062 2706 -2128 N ATOM 151 CA LEU A 41 113.274 9.678 38.894 1.00 81.34 C ANISOU 151 CA LEU A 41 13070 10913 6924 -3530 2354 -2007 C ATOM 152 C LEU A 41 114.468 8.777 39.353 1.00 87.07 C ANISOU 152 C LEU A 41 13084 12246 7751 -3402 2269 -2178 C ATOM 153 O LEU A 41 114.260 8.099 40.362 1.00 85.21 O ANISOU 153 O LEU A 41 12618 12151 7606 -3078 1972 -2110 O ATOM 154 CB LEU A 41 112.348 8.834 38.002 1.00 78.32 C ANISOU 154 CB LEU A 41 12962 10209 6587 -3109 2278 -1800 C ATOM 155 CG LEU A 41 111.028 9.486 37.537 1.00 80.57 C ANISOU 155 CG LEU A 41 13891 9951 6772 -3082 2284 -1608 C ATOM 156 CD1 LEU A 41 110.146 8.476 36.848 1.00 78.20 C ANISOU 156 CD1 LEU A 41 13735 9453 6526 -2656 2146 -1439 C ATOM 157 CD2 LEU A 41 110.244 10.090 38.692 1.00 81.01 C ANISOU 157 CD2 LEU A 41 14115 9846 6821 -3084 2103 -1524 C ATOM 158 N PRO A 42 115.685 8.713 38.729 1.00 86.89 N ANISOU 158 N PRO A 42 12698 12611 7707 -3605 2505 -2395 N ATOM 159 CA PRO A 42 116.723 7.808 39.266 1.00 88.88 C ANISOU 159 CA PRO A 42 12251 13472 8046 -3372 2375 -2543 C ATOM 160 C PRO A 42 117.177 8.180 40.685 1.00 93.69 C ANISOU 160 C PRO A 42 12494 14464 8638 -3524 2185 -2670 C ATOM 161 O PRO A 42 117.503 7.283 41.460 1.00 93.72 O ANISOU 161 O PRO A 42 12073 14824 8713 -3130 1922 -2671 O ATOM 162 CB PRO A 42 117.882 7.960 38.275 1.00 94.82 C ANISOU 162 CB PRO A 42 12725 14555 8746 -3663 2723 -2779 C ATOM 163 CG PRO A 42 117.261 8.488 37.036 1.00 98.04 C ANISOU 163 CG PRO A 42 13751 14432 9067 -3856 2989 -2676 C ATOM 164 CD PRO A 42 116.179 9.397 37.517 1.00 90.92 C ANISOU 164 CD PRO A 42 13402 13045 8098 -4015 2901 -2517 C ATOM 165 N THR A 43 117.168 9.484 41.028 1.00 90.66 N ANISOU 165 N THR A 43 12325 13983 8137 -4075 2317 -2770 N ATOM 166 CA THR A 43 117.565 9.989 42.346 1.00 91.95 C ANISOU 166 CA THR A 43 12208 14480 8250 -4310 2163 -2913 C ATOM 167 C THR A 43 116.476 9.659 43.389 1.00 91.26 C ANISOU 167 C THR A 43 12352 14106 8216 -3929 1812 -2674 C ATOM 168 O THR A 43 116.817 9.209 44.483 1.00 91.65 O ANISOU 168 O THR A 43 12005 14535 8283 -3737 1544 -2720 O ATOM 169 CB THR A 43 117.841 11.506 42.276 1.00101.98 C ANISOU 169 CB THR A 43 13743 15652 9354 -5057 2468 -3099 C ATOM 170 OG1 THR A 43 118.736 11.775 41.196 1.00105.18 O ANISOU 170 OG1 THR A 43 14012 16251 9699 -5419 2834 -3301 O ATOM 171 CG2 THR A 43 118.423 12.065 43.572 1.00103.20 C ANISOU 171 CG2 THR A 43 13562 16223 9427 -5392 2345 -3310 C ATOM 172 N ILE A 44 115.182 9.876 43.045 1.00 83.39 N ANISOU 172 N ILE A 44 11982 12472 7228 -3814 1818 -2430 N ATOM 173 CA ILE A 44 114.018 9.648 43.919 1.00 79.15 C ANISOU 173 CA ILE A 44 11719 11620 6735 -3497 1540 -2207 C ATOM 174 C ILE A 44 113.908 8.149 44.277 1.00 81.13 C ANISOU 174 C ILE A 44 11678 12035 7112 -2892 1257 -2082 C ATOM 175 O ILE A 44 113.739 7.827 45.456 1.00 80.11 O ANISOU 175 O ILE A 44 11419 12028 6992 -2700 998 -2037 O ATOM 176 CB ILE A 44 112.700 10.180 43.270 1.00 78.89 C ANISOU 176 CB ILE A 44 12368 10934 6673 -3485 1638 -1999 C ATOM 177 CG1 ILE A 44 112.797 11.703 42.996 1.00 81.33 C ANISOU 177 CG1 ILE A 44 13061 11022 6817 -4049 1930 -2108 C ATOM 178 CG2 ILE A 44 111.471 9.863 44.146 1.00 75.77 C ANISOU 178 CG2 ILE A 44 12196 10263 6330 -3144 1365 -1787 C ATOM 179 CD1 ILE A 44 111.701 12.306 42.094 1.00 86.81 C ANISOU 179 CD1 ILE A 44 14434 11116 7435 -4025 2078 -1927 C ATOM 180 N TYR A 45 114.025 7.246 43.279 1.00 77.09 N ANISOU 180 N TYR A 45 11105 11513 6673 -2602 1322 -2031 N ATOM 181 CA TYR A 45 113.933 5.802 43.508 1.00 75.75 C ANISOU 181 CA TYR A 45 10748 11435 6597 -2032 1103 -1915 C ATOM 182 C TYR A 45 115.158 5.256 44.268 1.00 82.39 C ANISOU 182 C TYR A 45 10973 12903 7430 -1870 965 -2077 C ATOM 183 O TYR A 45 115.048 4.186 44.864 1.00 81.63 O ANISOU 183 O TYR A 45 10770 12877 7369 -1388 734 -1969 O ATOM 184 CB TYR A 45 113.755 5.027 42.193 1.00 76.27 C ANISOU 184 CB TYR A 45 10959 11302 6718 -1795 1239 -1838 C ATOM 185 CG TYR A 45 112.347 5.070 41.637 1.00 74.61 C ANISOU 185 CG TYR A 45 11314 10514 6520 -1732 1245 -1629 C ATOM 186 CD1 TYR A 45 112.038 5.845 40.524 1.00 76.35 C ANISOU 186 CD1 TYR A 45 11877 10454 6678 -2012 1481 -1628 C ATOM 187 CD2 TYR A 45 111.322 4.329 42.221 1.00 72.59 C ANISOU 187 CD2 TYR A 45 11250 10014 6315 -1392 1018 -1441 C ATOM 188 CE1 TYR A 45 110.745 5.883 40.002 1.00 74.26 C ANISOU 188 CE1 TYR A 45 12093 9723 6401 -1915 1458 -1447 C ATOM 189 CE2 TYR A 45 110.022 4.366 41.715 1.00 70.53 C ANISOU 189 CE2 TYR A 45 11442 9300 6056 -1347 1016 -1279 C ATOM 190 CZ TYR A 45 109.738 5.144 40.604 1.00 77.74 C ANISOU 190 CZ TYR A 45 12650 9984 6905 -1589 1219 -1283 C ATOM 191 OH TYR A 45 108.460 5.183 40.098 1.00 75.65 O ANISOU 191 OH TYR A 45 12792 9332 6617 -1508 1189 -1134 O ATOM 192 N SER A 46 116.298 5.982 44.272 1.00 81.95 N ANISOU 192 N SER A 46 10526 13308 7305 -2264 1104 -2339 N ATOM 193 CA SER A 46 117.507 5.559 44.987 1.00 85.37 C ANISOU 193 CA SER A 46 10303 14430 7703 -2125 960 -2527 C ATOM 194 C SER A 46 117.430 5.908 46.482 1.00 88.32 C ANISOU 194 C SER A 46 10581 14976 8001 -2184 692 -2544 C ATOM 195 O SER A 46 117.811 5.081 47.311 1.00 89.17 O ANISOU 195 O SER A 46 10361 15431 8088 -1759 425 -2531 O ATOM 196 CB SER A 46 118.752 6.189 44.373 1.00 93.32 C ANISOU 196 CB SER A 46 10883 15919 8655 -2568 1229 -2835 C ATOM 197 OG SER A 46 118.966 5.711 43.056 1.00102.00 O ANISOU 197 OG SER A 46 12003 16940 9811 -2446 1465 -2835 O ATOM 198 N ILE A 47 116.941 7.122 46.819 1.00 83.08 N ANISOU 198 N ILE A 47 10239 14056 7272 -2685 770 -2569 N ATOM 199 CA ILE A 47 116.815 7.618 48.195 1.00 82.94 C ANISOU 199 CA ILE A 47 10202 14151 7161 -2825 558 -2601 C ATOM 200 C ILE A 47 115.759 6.784 48.948 1.00 82.79 C ANISOU 200 C ILE A 47 10473 13795 7189 -2306 280 -2318 C ATOM 201 O ILE A 47 116.069 6.261 50.019 1.00 83.58 O ANISOU 201 O ILE A 47 10305 14220 7231 -2033 7 -2323 O ATOM 202 CB ILE A 47 116.480 9.143 48.221 1.00 85.84 C ANISOU 202 CB ILE A 47 10948 14230 7437 -3486 771 -2691 C ATOM 203 CG1 ILE A 47 117.645 9.973 47.617 1.00 90.89 C ANISOU 203 CG1 ILE A 47 11288 15255 7993 -4072 1065 -3010 C ATOM 204 CG2 ILE A 47 116.153 9.624 49.649 1.00 86.25 C ANISOU 204 CG2 ILE A 47 11086 14295 7389 -3597 557 -2693 C ATOM 205 CD1 ILE A 47 117.328 11.453 47.267 1.00 98.14 C ANISOU 205 CD1 ILE A 47 12715 15769 8803 -4736 1383 -3087 C ATOM 206 N ILE A 48 114.542 6.637 48.372 1.00 75.11 N ANISOU 206 N ILE A 48 10033 12203 6302 -2172 352 -2086 N ATOM 207 CA ILE A 48 113.407 5.901 48.953 1.00 71.35 C ANISOU 207 CA ILE A 48 9882 11358 5871 -1762 150 -1830 C ATOM 208 C ILE A 48 113.775 4.401 49.113 1.00 76.49 C ANISOU 208 C ILE A 48 10282 12225 6556 -1171 -33 -1751 C ATOM 209 O ILE A 48 113.332 3.784 50.086 1.00 75.14 O ANISOU 209 O ILE A 48 10205 11991 6353 -857 -257 -1618 O ATOM 210 CB ILE A 48 112.115 6.117 48.106 1.00 70.29 C ANISOU 210 CB ILE A 48 10298 10599 5809 -1794 299 -1649 C ATOM 211 CG1 ILE A 48 111.657 7.594 48.243 1.00 70.10 C ANISOU 211 CG1 ILE A 48 10592 10332 5711 -2280 438 -1697 C ATOM 212 CG2 ILE A 48 110.978 5.157 48.516 1.00 67.66 C ANISOU 212 CG2 ILE A 48 10243 9933 5531 -1369 125 -1410 C ATOM 213 CD1 ILE A 48 110.505 8.048 47.388 1.00 73.91 C ANISOU 213 CD1 ILE A 48 11588 10273 6220 -2334 592 -1554 C ATOM 214 N PHE A 49 114.618 3.839 48.215 1.00 75.39 N ANISOU 214 N PHE A 49 9847 12343 6457 -1018 74 -1840 N ATOM 215 CA PHE A 49 115.055 2.445 48.333 1.00 76.64 C ANISOU 215 CA PHE A 49 9794 12705 6621 -424 -73 -1777 C ATOM 216 C PHE A 49 115.975 2.271 49.550 1.00 84.04 C ANISOU 216 C PHE A 49 10277 14219 7437 -247 -326 -1889 C ATOM 217 O PHE A 49 115.728 1.377 50.356 1.00 83.47 O ANISOU 217 O PHE A 49 10295 14106 7314 214 -550 -1741 O ATOM 218 CB PHE A 49 115.760 1.954 47.054 1.00 80.17 C ANISOU 218 CB PHE A 49 10036 13297 7128 -301 129 -1863 C ATOM 219 CG PHE A 49 116.346 0.563 47.151 1.00 84.14 C ANISOU 219 CG PHE A 49 10315 14039 7614 339 3 -1822 C ATOM 220 CD1 PHE A 49 115.534 -0.559 47.054 1.00 84.96 C ANISOU 220 CD1 PHE A 49 10829 13700 7750 781 -51 -1594 C ATOM 221 CD2 PHE A 49 117.713 0.377 47.317 1.00 91.38 C ANISOU 221 CD2 PHE A 49 10622 15632 8468 501 -44 -2024 C ATOM 222 CE1 PHE A 49 116.074 -1.844 47.155 1.00 88.53 C ANISOU 222 CE1 PHE A 49 11160 14318 8159 1395 -143 -1550 C ATOM 223 CE2 PHE A 49 118.254 -0.909 47.410 1.00 96.88 C ANISOU 223 CE2 PHE A 49 11143 16541 9126 1166 -159 -1978 C ATOM 224 CZ PHE A 49 117.431 -2.011 47.324 1.00 92.60 C ANISOU 224 CZ PHE A 49 11089 15488 8606 1618 -199 -1732 C ATOM 225 N LEU A 50 117.015 3.121 49.681 1.00 84.12 N ANISOU 225 N LEU A 50 9820 14764 7378 -624 -284 -2155 N ATOM 226 CA LEU A 50 117.990 3.067 50.774 1.00 88.29 C ANISOU 226 CA LEU A 50 9835 15948 7764 -510 -531 -2312 C ATOM 227 C LEU A 50 117.349 3.370 52.136 1.00 91.10 C ANISOU 227 C LEU A 50 10431 16166 8019 -555 -768 -2216 C ATOM 228 O LEU A 50 117.677 2.693 53.109 1.00 92.65 O ANISOU 228 O LEU A 50 10444 16660 8097 -134 -1049 -2179 O ATOM 229 CB LEU A 50 119.150 4.047 50.526 1.00 92.57 C ANISOU 229 CB LEU A 50 9843 17081 8250 -1041 -389 -2656 C ATOM 230 CG LEU A 50 120.109 3.718 49.377 1.00100.26 C ANISOU 230 CG LEU A 50 10402 18411 9281 -980 -178 -2820 C ATOM 231 CD1 LEU A 50 120.938 4.926 49.002 1.00103.76 C ANISOU 231 CD1 LEU A 50 10498 19251 9676 -1698 61 -3149 C ATOM 232 CD2 LEU A 50 121.007 2.530 49.711 1.00106.63 C ANISOU 232 CD2 LEU A 50 10703 19784 10028 -298 -400 -2851 C ATOM 233 N THR A 51 116.441 4.365 52.205 1.00 84.78 N ANISOU 233 N THR A 51 10059 14911 7244 -1025 -650 -2170 N ATOM 234 CA THR A 51 115.761 4.764 53.445 1.00 83.37 C ANISOU 234 CA THR A 51 10149 14559 6970 -1117 -826 -2090 C ATOM 235 C THR A 51 114.745 3.680 53.867 1.00 84.37 C ANISOU 235 C THR A 51 10684 14249 7125 -586 -976 -1789 C ATOM 236 O THR A 51 114.572 3.433 55.061 1.00 84.42 O ANISOU 236 O THR A 51 10749 14317 7008 -398 -1208 -1720 O ATOM 237 CB THR A 51 115.079 6.136 53.267 1.00 89.85 C ANISOU 237 CB THR A 51 11338 14994 7807 -1733 -613 -2131 C ATOM 238 OG1 THR A 51 115.978 7.039 52.621 1.00 92.88 O ANISOU 238 OG1 THR A 51 11436 15688 8169 -2239 -398 -2398 O ATOM 239 CG2 THR A 51 114.607 6.742 54.585 1.00 88.14 C ANISOU 239 CG2 THR A 51 11322 14706 7463 -1910 -766 -2121 C ATOM 240 N GLY A 52 114.106 3.049 52.886 1.00 78.51 N ANISOU 240 N GLY A 52 10226 13083 6522 -379 -830 -1629 N ATOM 241 CA GLY A 52 113.111 2.007 53.108 1.00 75.81 C ANISOU 241 CA GLY A 52 10297 12298 6209 48 -909 -1369 C ATOM 242 C GLY A 52 113.659 0.619 53.380 1.00 82.69 C ANISOU 242 C GLY A 52 11030 13375 7014 672 -1076 -1291 C ATOM 243 O GLY A 52 112.898 -0.253 53.807 1.00 80.56 O ANISOU 243 O GLY A 52 11135 12757 6719 1007 -1154 -1087 O ATOM 244 N ILE A 53 114.970 0.383 53.124 1.00 84.03 N ANISOU 244 N ILE A 53 10682 14105 7141 844 -1114 -1457 N ATOM 245 CA ILE A 53 115.582 -0.933 53.343 1.00 87.05 C ANISOU 245 CA ILE A 53 10929 14711 7436 1515 -1268 -1389 C ATOM 246 C ILE A 53 116.428 -0.896 54.638 1.00 95.83 C ANISOU 246 C ILE A 53 11666 16408 8339 1704 -1571 -1483 C ATOM 247 O ILE A 53 116.441 -1.888 55.367 1.00 97.14 O ANISOU 247 O ILE A 53 11971 16571 8368 2261 -1770 -1336 O ATOM 248 CB ILE A 53 116.400 -1.437 52.113 1.00 92.13 C ANISOU 248 CB ILE A 53 11276 15568 8161 1719 -1102 -1487 C ATOM 249 CG1 ILE A 53 116.514 -2.979 52.102 1.00 94.17 C ANISOU 249 CG1 ILE A 53 11698 15722 8358 2465 -1178 -1324 C ATOM 250 CG2 ILE A 53 117.756 -0.718 51.920 1.00 97.02 C ANISOU 250 CG2 ILE A 53 11194 16922 8747 1481 -1085 -1792 C ATOM 251 CD1 ILE A 53 116.770 -3.622 50.712 1.00102.25 C ANISOU 251 CD1 ILE A 53 12723 16634 9496 2659 -938 -1339 C ATOM 252 N VAL A 54 117.107 0.235 54.928 1.00 94.74 N ANISOU 252 N VAL A 54 11095 16752 8151 1235 -1602 -1730 N ATOM 253 CA VAL A 54 117.913 0.395 56.143 1.00 98.99 C ANISOU 253 CA VAL A 54 11238 17903 8470 1332 -1900 -1859 C ATOM 254 C VAL A 54 116.945 0.639 57.308 1.00100.79 C ANISOU 254 C VAL A 54 11930 17766 8599 1233 -2042 -1704 C ATOM 255 O VAL A 54 117.095 0.024 58.364 1.00102.61 O ANISOU 255 O VAL A 54 12185 18167 8635 1660 -2315 -1616 O ATOM 256 CB VAL A 54 118.991 1.512 56.003 1.00106.50 C ANISOU 256 CB VAL A 54 11558 19519 9387 796 -1857 -2214 C ATOM 257 CG1 VAL A 54 119.708 1.782 57.327 1.00110.71 C ANISOU 257 CG1 VAL A 54 11706 20688 9672 814 -2182 -2367 C ATOM 258 CG2 VAL A 54 120.004 1.164 54.914 1.00109.41 C ANISOU 258 CG2 VAL A 54 11431 20308 9834 945 -1714 -2376 C ATOM 259 N GLY A 55 115.942 1.488 57.072 1.00 93.43 N ANISOU 259 N GLY A 55 11387 16321 7789 716 -1845 -1662 N ATOM 260 CA GLY A 55 114.914 1.848 58.040 1.00 90.86 C ANISOU 260 CA GLY A 55 11518 15606 7399 556 -1913 -1531 C ATOM 261 C GLY A 55 114.048 0.688 58.481 1.00 93.51 C ANISOU 261 C GLY A 55 12338 15490 7700 1063 -1994 -1241 C ATOM 262 O GLY A 55 114.130 0.269 59.639 1.00 95.15 O ANISOU 262 O GLY A 55 12614 15832 7707 1354 -2234 -1170 O ATOM 263 N ASN A 56 113.223 0.151 57.555 1.00 87.05 N ANISOU 263 N ASN A 56 11878 14140 7056 1154 -1788 -1081 N ATOM 264 CA ASN A 56 112.299 -0.965 57.806 1.00 85.33 C ANISOU 264 CA ASN A 56 12174 13429 6820 1548 -1795 -823 C ATOM 265 C ASN A 56 113.036 -2.272 58.141 1.00 93.52 C ANISOU 265 C ASN A 56 13146 14688 7698 2226 -1972 -741 C ATOM 266 O ASN A 56 112.456 -3.134 58.805 1.00 93.08 O ANISOU 266 O ASN A 56 13524 14316 7525 2560 -2040 -543 O ATOM 267 CB ASN A 56 111.383 -1.196 56.611 1.00 82.61 C ANISOU 267 CB ASN A 56 12145 12558 6684 1440 -1530 -727 C ATOM 268 CG ASN A 56 110.407 -0.076 56.372 1.00103.59 C ANISOU 268 CG ASN A 56 14996 14900 9462 896 -1369 -749 C ATOM 269 OD1 ASN A 56 109.468 0.145 57.151 1.00 94.45 O ANISOU 269 OD1 ASN A 56 14163 13464 8261 778 -1390 -655 O ATOM 270 ND2 ASN A 56 110.561 0.608 55.247 1.00 96.30 N ANISOU 270 ND2 ASN A 56 13919 13988 8682 586 -1186 -863 N ATOM 271 N GLY A 57 114.287 -2.397 57.689 1.00 93.91 N ANISOU 271 N GLY A 57 12679 15274 7731 2426 -2030 -895 N ATOM 272 CA GLY A 57 115.138 -3.550 57.967 1.00 98.26 C ANISOU 272 CA GLY A 57 13097 16125 8111 3128 -2207 -843 C ATOM 273 C GLY A 57 115.459 -3.669 59.444 1.00105.50 C ANISOU 273 C GLY A 57 13992 17347 8747 3395 -2525 -811 C ATOM 274 O GLY A 57 115.421 -4.769 60.000 1.00107.03 O ANISOU 274 O GLY A 57 14502 17404 8759 3986 -2650 -627 O ATOM 275 N LEU A 58 115.740 -2.520 60.094 1.00102.87 N ANISOU 275 N LEU A 58 13340 17394 8352 2944 -2644 -990 N ATOM 276 CA LEU A 58 116.035 -2.430 61.524 1.00105.84 C ANISOU 276 CA LEU A 58 13669 18103 8444 3091 -2955 -996 C ATOM 277 C LEU A 58 114.778 -2.645 62.370 1.00107.32 C ANISOU 277 C LEU A 58 14549 17671 8555 3069 -2945 -762 C ATOM 278 O LEU A 58 114.874 -3.263 63.428 1.00109.70 O ANISOU 278 O LEU A 58 15049 18043 8590 3495 -3173 -642 O ATOM 279 CB LEU A 58 116.664 -1.068 61.878 1.00107.40 C ANISOU 279 CB LEU A 58 13346 18860 8601 2515 -3042 -1290 C ATOM 280 CG LEU A 58 118.117 -0.827 61.457 1.00116.82 C ANISOU 280 CG LEU A 58 13749 20874 9764 2539 -3131 -1575 C ATOM 281 CD1 LEU A 58 118.449 0.649 61.488 1.00117.24 C ANISOU 281 CD1 LEU A 58 13429 21269 9847 1756 -3071 -1872 C ATOM 282 CD2 LEU A 58 119.095 -1.608 62.328 1.00125.32 C ANISOU 282 CD2 LEU A 58 14506 22575 10534 3213 -3502 -1587 C ATOM 283 N VAL A 59 113.608 -2.142 61.903 1.00 98.97 N ANISOU 283 N VAL A 59 13858 16034 7714 2590 -2679 -701 N ATOM 284 CA VAL A 59 112.312 -2.229 62.595 1.00 95.85 C ANISOU 284 CA VAL A 59 14078 15059 7282 2478 -2613 -512 C ATOM 285 C VAL A 59 111.934 -3.709 62.839 1.00101.23 C ANISOU 285 C VAL A 59 15258 15367 7838 3072 -2626 -257 C ATOM 286 O VAL A 59 111.655 -4.060 63.981 1.00102.23 O ANISOU 286 O VAL A 59 15716 15398 7730 3270 -2764 -133 O ATOM 287 CB VAL A 59 111.174 -1.478 61.838 1.00 94.35 C ANISOU 287 CB VAL A 59 14114 14376 7360 1921 -2313 -512 C ATOM 288 CG1 VAL A 59 109.829 -1.634 62.548 1.00 91.41 C ANISOU 288 CG1 VAL A 59 14326 13460 6946 1834 -2234 -334 C ATOM 289 CG2 VAL A 59 111.506 0.002 61.670 1.00 93.70 C ANISOU 289 CG2 VAL A 59 13660 14583 7357 1342 -2274 -748 C ATOM 290 N ILE A 60 111.959 -4.563 61.792 1.00 97.83 N ANISOU 290 N ILE A 60 14912 14723 7536 3346 -2471 -186 N ATOM 291 CA ILE A 60 111.602 -5.991 61.868 1.00 98.91 C ANISOU 291 CA ILE A 60 15585 14442 7555 3875 -2425 41 C ATOM 292 C ILE A 60 112.561 -6.737 62.842 1.00108.96 C ANISOU 292 C ILE A 60 16826 16087 8487 4540 -2725 105 C ATOM 293 O ILE A 60 112.097 -7.585 63.609 1.00109.73 O ANISOU 293 O ILE A 60 17492 15835 8367 4870 -2753 308 O ATOM 294 CB ILE A 60 111.599 -6.637 60.446 1.00100.91 C ANISOU 294 CB ILE A 60 15869 14461 8010 3998 -2195 54 C ATOM 295 CG1 ILE A 60 110.611 -5.887 59.507 1.00 96.07 C ANISOU 295 CG1 ILE A 60 15306 13501 7697 3369 -1928 -2 C ATOM 296 CG2 ILE A 60 111.257 -8.141 60.505 1.00103.20 C ANISOU 296 CG2 ILE A 60 16775 14282 8155 4527 -2117 275 C ATOM 297 CD1 ILE A 60 110.711 -6.203 57.997 1.00101.66 C ANISOU 297 CD1 ILE A 60 15924 14086 8615 3368 -1714 -48 C ATOM 298 N LEU A 61 113.866 -6.394 62.835 1.00109.71 N ANISOU 298 N LEU A 61 16269 16901 8516 4720 -2942 -76 N ATOM 299 CA LEU A 61 114.879 -7.015 63.699 1.00115.80 C ANISOU 299 CA LEU A 61 16898 18152 8950 5388 -3265 -48 C ATOM 300 C LEU A 61 114.719 -6.611 65.179 1.00121.48 C ANISOU 300 C LEU A 61 17758 19006 9395 5317 -3509 -17 C ATOM 301 O LEU A 61 115.012 -7.423 66.059 1.00124.88 O ANISOU 301 O LEU A 61 18457 19496 9495 5914 -3721 129 O ATOM 302 CB LEU A 61 116.301 -6.651 63.229 1.00119.71 C ANISOU 302 CB LEU A 61 16553 19467 9464 5525 -3422 -299 C ATOM 303 CG LEU A 61 116.774 -7.227 61.884 1.00124.96 C ANISOU 303 CG LEU A 61 17022 20143 10316 5786 -3234 -337 C ATOM 304 CD1 LEU A 61 118.013 -6.509 61.392 1.00128.01 C ANISOU 304 CD1 LEU A 61 16517 21348 10773 5657 -3323 -643 C ATOM 305 CD2 LEU A 61 117.029 -8.730 61.965 1.00131.35 C ANISOU 305 CD2 LEU A 61 18230 20764 10912 6668 -3281 -127 C ATOM 306 N VAL A 62 114.269 -5.372 65.446 1.00115.65 N ANISOU 306 N VAL A 62 16874 18300 8768 4616 -3473 -152 N ATOM 307 CA VAL A 62 114.095 -4.835 66.801 1.00116.81 C ANISOU 307 CA VAL A 62 17135 18579 8670 4454 -3676 -157 C ATOM 308 C VAL A 62 112.683 -5.186 67.339 1.00118.51 C ANISOU 308 C VAL A 62 18149 18027 8852 4335 -3493 78 C ATOM 309 O VAL A 62 112.563 -5.550 68.510 1.00120.43 O ANISOU 309 O VAL A 62 18749 18228 8781 4595 -3660 203 O ATOM 310 CB VAL A 62 114.358 -3.297 66.826 1.00119.36 C ANISOU 310 CB VAL A 62 16928 19317 9106 3750 -3702 -442 C ATOM 311 CG1 VAL A 62 113.939 -2.657 68.149 1.00119.34 C ANISOU 311 CG1 VAL A 62 17147 19314 8883 3474 -3839 -448 C ATOM 312 CG2 VAL A 62 115.824 -2.986 66.531 1.00123.59 C ANISOU 312 CG2 VAL A 62 16664 20699 9597 3856 -3908 -700 C ATOM 313 N MET A 63 111.637 -5.082 66.497 1.00111.05 N ANISOU 313 N MET A 63 17471 16516 8209 3947 -3155 127 N ATOM 314 CA MET A 63 110.247 -5.323 66.895 1.00108.27 C ANISOU 314 CA MET A 63 17788 15490 7860 3745 -2944 303 C ATOM 315 C MET A 63 109.949 -6.823 67.067 1.00114.94 C ANISOU 315 C MET A 63 19254 15895 8523 4299 -2882 553 C ATOM 316 O MET A 63 109.656 -7.250 68.186 1.00116.51 O ANISOU 316 O MET A 63 19912 15929 8430 4498 -2965 696 O ATOM 317 CB MET A 63 109.276 -4.712 65.867 1.00105.25 C ANISOU 317 CB MET A 63 17414 14730 7845 3176 -2623 247 C ATOM 318 CG MET A 63 107.912 -4.375 66.434 1.00105.93 C ANISOU 318 CG MET A 63 17954 14346 7949 2782 -2446 323 C ATOM 319 SD MET A 63 107.973 -3.153 67.772 1.00111.16 S ANISOU 319 SD MET A 63 18494 15317 8427 2448 -2629 206 S ATOM 320 CE MET A 63 108.580 -1.726 66.899 1.00106.27 C ANISOU 320 CE MET A 63 17207 15110 8063 1969 -2620 -71 C ATOM 321 N GLY A 64 110.007 -7.582 65.967 1.00111.76 N ANISOU 321 N GLY A 64 18907 15282 8276 4514 -2717 599 N ATOM 322 CA GLY A 64 109.715 -9.015 65.917 1.00113.67 C ANISOU 322 CA GLY A 64 19779 15041 8369 4993 -2594 817 C ATOM 323 C GLY A 64 110.477 -9.877 66.903 1.00123.78 C ANISOU 323 C GLY A 64 21309 16487 9233 5709 -2849 956 C ATOM 324 O GLY A 64 109.910 -10.810 67.480 1.00125.06 O ANISOU 324 O GLY A 64 22197 16156 9164 5959 -2753 1164 O ATOM 325 N TYR A 65 111.765 -9.560 67.103 1.00124.12 N ANISOU 325 N TYR A 65 20757 17242 9160 6038 -3171 833 N ATOM 326 CA TYR A 65 112.661 -10.269 68.018 1.00130.35 C ANISOU 326 CA TYR A 65 21649 18346 9531 6788 -3483 936 C ATOM 327 C TYR A 65 112.912 -9.402 69.262 1.00135.40 C ANISOU 327 C TYR A 65 22054 19442 9948 6619 -3783 852 C ATOM 328 O TYR A 65 112.340 -8.315 69.361 1.00130.87 O ANISOU 328 O TYR A 65 21302 18861 9561 5922 -3704 725 O ATOM 329 CB TYR A 65 113.986 -10.624 67.302 1.00135.69 C ANISOU 329 CB TYR A 65 21771 19574 10212 7346 -3641 837 C ATOM 330 CG TYR A 65 113.802 -11.205 65.915 1.00135.80 C ANISOU 330 CG TYR A 65 21874 19220 10504 7378 -3331 852 C ATOM 331 CD1 TYR A 65 113.881 -10.398 64.784 1.00134.19 C ANISOU 331 CD1 TYR A 65 21095 19205 10687 6867 -3189 642 C ATOM 332 CD2 TYR A 65 113.526 -12.557 65.734 1.00138.59 C ANISOU 332 CD2 TYR A 65 22944 19004 10711 7897 -3163 1075 C ATOM 333 CE1 TYR A 65 113.691 -10.920 63.506 1.00133.13 C ANISOU 333 CE1 TYR A 65 21063 18731 10788 6880 -2906 652 C ATOM 334 CE2 TYR A 65 113.336 -13.093 64.459 1.00137.82 C ANISOU 334 CE2 TYR A 65 22959 18554 10851 7895 -2869 1075 C ATOM 335 CZ TYR A 65 113.421 -12.269 63.347 1.00141.82 C ANISOU 335 CZ TYR A 65 22852 19289 11743 7389 -2752 862 C ATOM 336 OH TYR A 65 113.239 -12.785 62.086 1.00141.25 O ANISOU 336 OH TYR A 65 22899 18884 11885 7382 -2470 855 O ATOM 337 N GLN A 66 113.750 -9.895 70.208 1.00137.83 N ANISOU 337 N GLN A 66 22396 20136 9837 7277 -4124 924 N ATOM 338 CA GLN A 66 114.187 -9.265 71.469 1.00164.38 C ANISOU 338 CA GLN A 66 25550 24016 12891 7273 -4475 850 C ATOM 339 C GLN A 66 113.068 -8.429 72.130 1.00181.54 C ANISOU 339 C GLN A 66 28024 25834 15121 6543 -4331 842 C ATOM 340 O GLN A 66 111.945 -8.905 72.286 1.00136.45 O ANISOU 340 O GLN A 66 23032 19398 9414 6408 -4054 1031 O ATOM 341 CB GLN A 66 115.438 -8.382 71.240 1.00167.99 C ANISOU 341 CB GLN A 66 24996 25426 13407 7202 -4767 542 C ATOM 342 CG GLN A 66 115.249 -7.149 70.342 1.00177.14 C ANISOU 342 CG GLN A 66 25595 26700 15012 6363 -4569 284 C ATOM 343 CD GLN A 66 116.477 -6.814 69.531 1.00196.92 C ANISOU 343 CD GLN A 66 27226 29946 17650 6445 -4695 31 C ATOM 344 OE1 GLN A 66 117.026 -7.651 68.802 1.00193.83 O ANISOU 344 OE1 GLN A 66 26734 29623 17290 6987 -4671 78 O ATOM 345 NE2 GLN A 66 116.877 -5.553 69.559 1.00188.05 N ANISOU 345 NE2 GLN A 66 25476 29348 16627 5850 -4779 -257 N ATOM 346 N SER A 71 104.304 -2.826 73.267 1.00108.57 N ANISOU 346 N SER A 71 20257 13866 7129 1899 -2426 580 N ATOM 347 CA SER A 71 103.141 -1.975 73.026 1.00104.44 C ANISOU 347 CA SER A 71 19761 13072 6849 1379 -2137 500 C ATOM 348 C SER A 71 102.137 -2.663 72.078 1.00105.10 C ANISOU 348 C SER A 71 20050 12701 7182 1316 -1821 591 C ATOM 349 O SER A 71 102.480 -3.647 71.415 1.00105.45 O ANISOU 349 O SER A 71 20139 12667 7261 1624 -1827 683 O ATOM 350 CB SER A 71 103.576 -0.626 72.459 1.00106.53 C ANISOU 350 CB SER A 71 19482 13664 7329 1038 -2192 279 C ATOM 351 OG SER A 71 102.474 0.217 72.160 1.00111.99 O ANISOU 351 OG SER A 71 20214 14094 8246 605 -1917 209 O ATOM 352 N MET A 72 100.896 -2.135 72.029 1.00 98.27 N ANISOU 352 N MET A 72 19304 11560 6475 921 -1545 551 N ATOM 353 CA MET A 72 99.790 -2.656 71.222 1.00 95.25 C ANISOU 353 CA MET A 72 19084 10796 6311 780 -1238 599 C ATOM 354 C MET A 72 99.854 -2.180 69.765 1.00 94.59 C ANISOU 354 C MET A 72 18562 10796 6581 642 -1188 493 C ATOM 355 O MET A 72 99.650 -2.992 68.860 1.00 93.23 O ANISOU 355 O MET A 72 18441 10443 6540 733 -1075 548 O ATOM 356 CB MET A 72 98.444 -2.241 71.836 1.00 96.47 C ANISOU 356 CB MET A 72 19491 10703 6461 437 -978 578 C ATOM 357 CG MET A 72 97.590 -3.411 72.259 1.00101.52 C ANISOU 357 CG MET A 72 20663 10958 6952 472 -753 713 C ATOM 358 SD MET A 72 96.961 -4.381 70.867 1.00104.07 S ANISOU 358 SD MET A 72 21017 11000 7526 433 -516 743 S ATOM 359 CE MET A 72 96.263 -5.734 71.739 1.00103.85 C ANISOU 359 CE MET A 72 21712 10550 7196 475 -286 896 C ATOM 360 N THR A 73 100.117 -0.873 69.538 1.00 88.62 N ANISOU 360 N THR A 73 17428 10286 5956 410 -1252 340 N ATOM 361 CA THR A 73 100.203 -0.276 68.197 1.00 85.28 C ANISOU 361 CA THR A 73 16628 9941 5836 262 -1198 237 C ATOM 362 C THR A 73 101.459 -0.766 67.456 1.00 88.60 C ANISOU 362 C THR A 73 16774 10602 6288 537 -1380 236 C ATOM 363 O THR A 73 101.471 -0.768 66.224 1.00 86.51 O ANISOU 363 O THR A 73 16305 10313 6253 498 -1300 200 O ATOM 364 CB THR A 73 100.187 1.260 68.264 1.00 93.21 C ANISOU 364 CB THR A 73 17401 11102 6914 -56 -1194 80 C ATOM 365 OG1 THR A 73 101.220 1.711 69.142 1.00 96.87 O ANISOU 365 OG1 THR A 73 17761 11885 7162 -21 -1430 13 O ATOM 366 CG2 THR A 73 98.835 1.818 68.702 1.00 90.21 C ANISOU 366 CG2 THR A 73 17241 10475 6560 -306 -967 65 C ATOM 367 N ASP A 74 102.494 -1.201 68.207 1.00 87.03 N ANISOU 367 N ASP A 74 16574 10651 5843 837 -1624 272 N ATOM 368 CA ASP A 74 103.756 -1.735 67.687 1.00 88.16 C ANISOU 368 CA ASP A 74 16444 11086 5965 1174 -1818 267 C ATOM 369 C ASP A 74 103.536 -3.029 66.887 1.00 89.98 C ANISOU 369 C ASP A 74 16887 11031 6271 1448 -1695 399 C ATOM 370 O ASP A 74 104.334 -3.332 65.997 1.00 89.89 O ANISOU 370 O ASP A 74 16607 11192 6357 1644 -1757 369 O ATOM 371 CB ASP A 74 104.738 -1.996 68.841 1.00 94.15 C ANISOU 371 CB ASP A 74 17211 12172 6388 1487 -2112 291 C ATOM 372 CG ASP A 74 105.312 -0.755 69.508 1.00103.84 C ANISOU 372 CG ASP A 74 18135 13800 7518 1233 -2285 117 C ATOM 373 OD1 ASP A 74 104.796 0.357 69.249 1.00101.76 O ANISOU 373 OD1 ASP A 74 17765 13474 7426 793 -2141 -4 O ATOM 374 OD2 ASP A 74 106.245 -0.900 70.327 1.00112.32 O ANISOU 374 OD2 ASP A 74 19113 15243 8320 1480 -2562 99 O ATOM 375 N LYS A 75 102.452 -3.777 67.202 1.00 84.78 N ANISOU 375 N LYS A 75 16719 9937 5555 1432 -1499 528 N ATOM 376 CA LYS A 75 102.059 -5.010 66.515 1.00 83.90 C ANISOU 376 CA LYS A 75 16907 9482 5488 1605 -1330 639 C ATOM 377 C LYS A 75 101.594 -4.690 65.088 1.00 82.42 C ANISOU 377 C LYS A 75 16469 9215 5631 1345 -1158 548 C ATOM 378 O LYS A 75 101.970 -5.399 64.154 1.00 82.07 O ANISOU 378 O LYS A 75 16394 9120 5668 1540 -1128 570 O ATOM 379 CB LYS A 75 100.960 -5.745 67.299 1.00 87.12 C ANISOU 379 CB LYS A 75 17904 9467 5731 1540 -1133 763 C ATOM 380 N TYR A 76 100.804 -3.604 64.923 1.00 74.84 N ANISOU 380 N TYR A 76 15344 8251 4841 935 -1050 446 N ATOM 381 CA TYR A 76 100.323 -3.131 63.621 1.00 71.01 C ANISOU 381 CA TYR A 76 14622 7722 4639 694 -909 357 C ATOM 382 C TYR A 76 101.461 -2.530 62.808 1.00 74.18 C ANISOU 382 C TYR A 76 14577 8450 5157 749 -1047 258 C ATOM 383 O TYR A 76 101.452 -2.631 61.580 1.00 72.37 O ANISOU 383 O TYR A 76 14206 8182 5110 717 -962 222 O ATOM 384 CB TYR A 76 99.203 -2.098 63.779 1.00 69.47 C ANISOU 384 CB TYR A 76 14399 7452 4544 318 -771 284 C ATOM 385 CG TYR A 76 97.913 -2.659 64.329 1.00 70.85 C ANISOU 385 CG TYR A 76 14945 7323 4651 192 -572 344 C ATOM 386 CD1 TYR A 76 97.051 -3.397 63.523 1.00 71.92 C ANISOU 386 CD1 TYR A 76 15207 7225 4893 103 -377 355 C ATOM 387 CD2 TYR A 76 97.514 -2.389 65.634 1.00 72.53 C ANISOU 387 CD2 TYR A 76 15367 7504 4688 116 -560 366 C ATOM 388 CE1 TYR A 76 95.854 -3.906 64.020 1.00 72.94 C ANISOU 388 CE1 TYR A 76 15646 7115 4953 -71 -169 379 C ATOM 389 CE2 TYR A 76 96.310 -2.879 66.138 1.00 73.67 C ANISOU 389 CE2 TYR A 76 15836 7389 4765 -37 -343 402 C ATOM 390 CZ TYR A 76 95.482 -3.636 65.326 1.00 80.30 C ANISOU 390 CZ TYR A 76 16775 8021 5716 -144 -143 402 C ATOM 391 OH TYR A 76 94.293 -4.121 65.811 1.00 82.45 O ANISOU 391 OH TYR A 76 17336 8077 5915 -348 93 408 O ATOM 392 N ARG A 77 102.444 -1.912 63.495 1.00 72.14 N ANISOU 392 N ARG A 77 14099 8532 4779 807 -1253 199 N ATOM 393 CA ARG A 77 103.620 -1.319 62.858 1.00 72.49 C ANISOU 393 CA ARG A 77 13695 8947 4899 818 -1378 75 C ATOM 394 C ARG A 77 104.562 -2.429 62.365 1.00 78.66 C ANISOU 394 C ARG A 77 14405 9842 5642 1235 -1466 127 C ATOM 395 O ARG A 77 105.308 -2.196 61.416 1.00 78.36 O ANISOU 395 O ARG A 77 14022 10022 5729 1241 -1479 32 O ATOM 396 CB ARG A 77 104.348 -0.340 63.792 1.00 74.30 C ANISOU 396 CB ARG A 77 13708 9535 4986 703 -1561 -35 C ATOM 397 CG ARG A 77 103.532 0.924 64.068 1.00 81.37 C ANISOU 397 CG ARG A 77 14653 10322 5941 281 -1445 -115 C ATOM 398 CD ARG A 77 104.384 2.133 64.401 1.00 92.38 C ANISOU 398 CD ARG A 77 15751 12075 7273 48 -1562 -289 C ATOM 399 NE ARG A 77 105.071 2.015 65.687 1.00106.07 N ANISOU 399 NE ARG A 77 17480 14087 8736 183 -1792 -302 N ATOM 400 CZ ARG A 77 105.868 2.949 66.196 1.00123.34 C ANISOU 400 CZ ARG A 77 19423 16634 10805 -23 -1926 -468 C ATOM 401 NH1 ARG A 77 106.098 4.073 65.525 1.00111.09 N ANISOU 401 NH1 ARG A 77 17650 15174 9386 -388 -1826 -633 N ATOM 402 NH2 ARG A 77 106.453 2.762 67.370 1.00112.35 N ANISOU 402 NH2 ARG A 77 18031 15517 9141 125 -2157 -479 N ATOM 403 N LEU A 78 104.495 -3.638 62.973 1.00 77.27 N ANISOU 403 N LEU A 78 14589 9490 5280 1585 -1498 276 N ATOM 404 CA LEU A 78 105.254 -4.816 62.539 1.00 79.60 C ANISOU 404 CA LEU A 78 14929 9806 5509 2046 -1548 349 C ATOM 405 C LEU A 78 104.640 -5.343 61.232 1.00 81.63 C ANISOU 405 C LEU A 78 15306 9737 5973 1966 -1313 366 C ATOM 406 O LEU A 78 105.374 -5.733 60.322 1.00 82.01 O ANISOU 406 O LEU A 78 15164 9901 6093 2177 -1316 334 O ATOM 407 CB LEU A 78 105.273 -5.902 63.637 1.00 82.84 C ANISOU 407 CB LEU A 78 15799 10057 5618 2442 -1627 517 C ATOM 408 CG LEU A 78 106.026 -7.211 63.332 1.00 90.78 C ANISOU 408 CG LEU A 78 16967 11028 6496 3008 -1671 618 C ATOM 409 CD1 LEU A 78 107.539 -7.007 63.335 1.00 94.05 C ANISOU 409 CD1 LEU A 78 16875 12025 6834 3355 -1940 529 C ATOM 410 CD2 LEU A 78 105.665 -8.286 64.333 1.00 95.94 C ANISOU 410 CD2 LEU A 78 18256 11345 6852 3316 -1655 808 C ATOM 411 N HIS A 79 103.287 -5.323 61.148 1.00 75.78 N ANISOU 411 N HIS A 79 14857 8621 5316 1650 -1109 399 N ATOM 412 CA HIS A 79 102.496 -5.710 59.974 1.00 73.49 C ANISOU 412 CA HIS A 79 14679 8037 5205 1487 -888 391 C ATOM 413 C HIS A 79 102.702 -4.727 58.824 1.00 74.74 C ANISOU 413 C HIS A 79 14408 8394 5597 1253 -866 255 C ATOM 414 O HIS A 79 102.622 -5.116 57.657 1.00 73.26 O ANISOU 414 O HIS A 79 14205 8097 5534 1252 -752 233 O ATOM 415 CB HIS A 79 101.000 -5.774 60.327 1.00 72.62 C ANISOU 415 CB HIS A 79 14902 7588 5100 1175 -702 425 C ATOM 416 CG HIS A 79 100.585 -7.014 61.048 1.00 78.30 C ANISOU 416 CG HIS A 79 16158 7981 5611 1340 -611 555 C ATOM 417 ND1 HIS A 79 100.789 -7.162 62.406 1.00 82.29 N ANISOU 417 ND1 HIS A 79 16891 8500 5877 1503 -715 642 N ATOM 418 CD2 HIS A 79 99.941 -8.108 60.580 1.00 80.53 C ANISOU 418 CD2 HIS A 79 16823 7902 5874 1326 -407 602 C ATOM 419 CE1 HIS A 79 100.291 -8.348 62.715 1.00 83.62 C ANISOU 419 CE1 HIS A 79 17595 8294 5882 1602 -562 752 C ATOM 420 NE2 HIS A 79 99.768 -8.953 61.649 1.00 83.05 N ANISOU 420 NE2 HIS A 79 17637 7982 5936 1482 -365 725 N ATOM 421 N LEU A 80 102.938 -3.449 59.165 1.00 70.58 N ANISOU 421 N LEU A 80 13583 8130 5106 1037 -959 162 N ATOM 422 CA LEU A 80 103.147 -2.365 58.212 1.00 68.73 C ANISOU 422 CA LEU A 80 13001 8062 5050 785 -924 33 C ATOM 423 C LEU A 80 104.582 -2.377 57.682 1.00 74.84 C ANISOU 423 C LEU A 80 13423 9182 5833 976 -1028 -44 C ATOM 424 O LEU A 80 104.767 -2.247 56.475 1.00 73.59 O ANISOU 424 O LEU A 80 13108 9037 5817 907 -932 -105 O ATOM 425 CB LEU A 80 102.830 -1.013 58.880 1.00 67.73 C ANISOU 425 CB LEU A 80 12780 8035 4918 473 -951 -39 C ATOM 426 CG LEU A 80 102.612 0.193 57.963 1.00 70.26 C ANISOU 426 CG LEU A 80 12912 8383 5400 159 -850 -148 C ATOM 427 CD1 LEU A 80 101.218 0.170 57.353 1.00 67.90 C ANISOU 427 CD1 LEU A 80 12814 7771 5213 14 -679 -110 C ATOM 428 CD2 LEU A 80 102.764 1.485 58.736 1.00 73.05 C ANISOU 428 CD2 LEU A 80 13171 8892 5693 -80 -903 -237 C ATOM 429 N SER A 81 105.588 -2.557 58.572 1.00 74.76 N ANISOU 429 N SER A 81 13278 9474 5653 1225 -1223 -48 N ATOM 430 CA SER A 81 107.014 -2.567 58.221 1.00 77.48 C ANISOU 430 CA SER A 81 13216 10245 5977 1428 -1341 -147 C ATOM 431 C SER A 81 107.423 -3.808 57.402 1.00 83.31 C ANISOU 431 C SER A 81 14018 10904 6733 1821 -1287 -86 C ATOM 432 O SER A 81 108.521 -3.813 56.845 1.00 84.88 O ANISOU 432 O SER A 81 13852 11444 6953 1975 -1333 -183 O ATOM 433 CB SER A 81 107.883 -2.491 59.472 1.00 84.58 C ANISOU 433 CB SER A 81 13955 11525 6658 1622 -1589 -171 C ATOM 434 OG SER A 81 107.663 -3.593 60.337 1.00 95.89 O ANISOU 434 OG SER A 81 15761 12776 7897 2006 -1669 -6 O ATOM 435 N VAL A 82 106.566 -4.846 57.331 1.00 79.68 N ANISOU 435 N VAL A 82 14020 10004 6250 1965 -1172 58 N ATOM 436 CA VAL A 82 106.861 -6.054 56.556 1.00 81.17 C ANISOU 436 CA VAL A 82 14364 10041 6435 2319 -1086 115 C ATOM 437 C VAL A 82 106.179 -5.922 55.163 1.00 82.11 C ANISOU 437 C VAL A 82 14517 9916 6766 2026 -866 67 C ATOM 438 O VAL A 82 106.750 -6.371 54.166 1.00 82.46 O ANISOU 438 O VAL A 82 14459 10003 6869 2195 -795 27 O ATOM 439 CB VAL A 82 106.469 -7.366 57.306 1.00 87.28 C ANISOU 439 CB VAL A 82 15682 10472 7007 2668 -1076 289 C ATOM 440 CG1 VAL A 82 104.958 -7.518 57.485 1.00 84.63 C ANISOU 440 CG1 VAL A 82 15790 9667 6698 2339 -903 361 C ATOM 441 CG2 VAL A 82 107.066 -8.599 56.632 1.00 89.74 C ANISOU 441 CG2 VAL A 82 16154 10680 7264 3127 -1011 338 C ATOM 442 N ALA A 83 104.994 -5.266 55.103 1.00 75.61 N ANISOU 442 N ALA A 83 13815 8873 6040 1608 -769 61 N ATOM 443 CA ALA A 83 104.224 -5.045 53.874 1.00 72.71 C ANISOU 443 CA ALA A 83 13481 8305 5840 1326 -593 15 C ATOM 444 C ALA A 83 104.909 -4.028 52.959 1.00 76.05 C ANISOU 444 C ALA A 83 13496 9010 6391 1157 -585 -117 C ATOM 445 O ALA A 83 104.865 -4.196 51.739 1.00 75.10 O ANISOU 445 O ALA A 83 13364 8805 6366 1114 -460 -156 O ATOM 446 CB ALA A 83 102.818 -4.574 54.210 1.00 70.89 C ANISOU 446 CB ALA A 83 13447 7844 5645 987 -523 37 C ATOM 447 N ASP A 84 105.538 -2.983 53.538 1.00 73.17 N ANISOU 447 N ASP A 84 12828 8967 6008 1036 -699 -195 N ATOM 448 CA ASP A 84 106.229 -1.955 52.759 1.00 72.96 C ANISOU 448 CA ASP A 84 12449 9200 6072 819 -662 -335 C ATOM 449 C ASP A 84 107.631 -2.440 52.341 1.00 79.23 C ANISOU 449 C ASP A 84 12936 10325 6842 1100 -698 -408 C ATOM 450 O ASP A 84 108.072 -2.083 51.249 1.00 78.73 O ANISOU 450 O ASP A 84 12681 10362 6869 979 -583 -505 O ATOM 451 CB ASP A 84 106.312 -0.610 53.515 1.00 74.83 C ANISOU 451 CB ASP A 84 12525 9626 6280 514 -732 -415 C ATOM 452 CG ASP A 84 106.944 -0.611 54.901 1.00 90.37 C ANISOU 452 CG ASP A 84 14378 11865 8094 648 -929 -422 C ATOM 453 OD1 ASP A 84 107.837 -1.449 55.151 1.00 94.39 O ANISOU 453 OD1 ASP A 84 14756 12595 8513 1008 -1041 -412 O ATOM 454 OD2 ASP A 84 106.587 0.271 55.717 1.00 96.05 O ANISOU 454 OD2 ASP A 84 15133 12596 8764 406 -973 -447 O ATOM 455 N LEU A 85 108.310 -3.264 53.189 1.00 78.10 N ANISOU 455 N LEU A 85 12759 10354 6560 1497 -849 -361 N ATOM 456 CA LEU A 85 109.646 -3.828 52.922 1.00 81.16 C ANISOU 456 CA LEU A 85 12836 11105 6897 1864 -905 -428 C ATOM 457 C LEU A 85 109.615 -4.724 51.684 1.00 84.71 C ANISOU 457 C LEU A 85 13433 11332 7423 2054 -731 -401 C ATOM 458 O LEU A 85 110.562 -4.716 50.894 1.00 86.03 O ANISOU 458 O LEU A 85 13281 11777 7631 2146 -673 -514 O ATOM 459 CB LEU A 85 110.160 -4.622 54.134 1.00 84.39 C ANISOU 459 CB LEU A 85 13285 11676 7106 2324 -1114 -347 C ATOM 460 CG LEU A 85 111.581 -5.178 54.025 1.00 93.49 C ANISOU 460 CG LEU A 85 14066 13286 8169 2783 -1213 -422 C ATOM 461 CD1 LEU A 85 112.529 -4.441 54.943 1.00 96.55 C ANISOU 461 CD1 LEU A 85 13983 14260 8441 2758 -1437 -552 C ATOM 462 CD2 LEU A 85 111.607 -6.661 54.314 1.00 98.16 C ANISOU 462 CD2 LEU A 85 15027 13656 8612 3383 -1246 -259 C ATOM 463 N LEU A 86 108.509 -5.478 51.515 1.00 79.32 N ANISOU 463 N LEU A 86 13234 10156 6746 2078 -632 -270 N ATOM 464 CA LEU A 86 108.258 -6.371 50.383 1.00 78.89 C ANISOU 464 CA LEU A 86 13422 9811 6742 2199 -453 -244 C ATOM 465 C LEU A 86 108.191 -5.561 49.075 1.00 80.42 C ANISOU 465 C LEU A 86 13428 10037 7090 1843 -304 -359 C ATOM 466 O LEU A 86 108.543 -6.078 48.016 1.00 80.77 O ANISOU 466 O LEU A 86 13477 10043 7169 1968 -172 -399 O ATOM 467 CB LEU A 86 106.945 -7.143 50.628 1.00 77.47 C ANISOU 467 CB LEU A 86 13790 9123 6520 2158 -379 -111 C ATOM 468 CG LEU A 86 106.659 -8.375 49.760 1.00 83.00 C ANISOU 468 CG LEU A 86 14863 9471 7201 2339 -206 -70 C ATOM 469 CD1 LEU A 86 107.579 -9.538 50.124 1.00 87.21 C ANISOU 469 CD1 LEU A 86 15527 10031 7579 2918 -241 -8 C ATOM 470 CD2 LEU A 86 105.224 -8.826 49.935 1.00 83.73 C ANISOU 470 CD2 LEU A 86 15425 9117 7270 2107 -111 7 C ATOM 471 N PHE A 87 107.774 -4.282 49.171 1.00 74.52 N ANISOU 471 N PHE A 87 12549 9355 6411 1422 -318 -411 N ATOM 472 CA PHE A 87 107.681 -3.350 48.051 1.00 72.65 C ANISOU 472 CA PHE A 87 12187 9136 6282 1075 -184 -508 C ATOM 473 C PHE A 87 109.010 -2.575 47.864 1.00 78.40 C ANISOU 473 C PHE A 87 12449 10321 7018 1002 -183 -663 C ATOM 474 O PHE A 87 109.252 -2.061 46.772 1.00 77.74 O ANISOU 474 O PHE A 87 12264 10277 6997 799 -33 -753 O ATOM 475 CB PHE A 87 106.500 -2.377 48.251 1.00 71.50 C ANISOU 475 CB PHE A 87 12203 8788 6175 697 -180 -479 C ATOM 476 CG PHE A 87 106.362 -1.329 47.172 1.00 71.88 C ANISOU 476 CG PHE A 87 12189 8828 6293 370 -50 -559 C ATOM 477 CD1 PHE A 87 105.900 -1.667 45.904 1.00 74.31 C ANISOU 477 CD1 PHE A 87 12667 8927 6642 342 84 -554 C ATOM 478 CD2 PHE A 87 106.717 -0.008 47.414 1.00 74.07 C ANISOU 478 CD2 PHE A 87 12281 9294 6569 88 -52 -644 C ATOM 479 CE1 PHE A 87 105.809 -0.705 44.895 1.00 74.38 C ANISOU 479 CE1 PHE A 87 12661 8922 6679 75 202 -617 C ATOM 480 CE2 PHE A 87 106.615 0.956 46.409 1.00 76.24 C ANISOU 480 CE2 PHE A 87 12576 9517 6873 -196 91 -708 C ATOM 481 CZ PHE A 87 106.162 0.601 45.156 1.00 73.51 C ANISOU 481 CZ PHE A 87 12403 8969 6559 -183 211 -686 C ATOM 482 N VAL A 88 109.863 -2.494 48.909 1.00 77.25 N ANISOU 482 N VAL A 88 12024 10536 6791 1149 -344 -705 N ATOM 483 CA VAL A 88 111.158 -1.796 48.830 1.00 79.59 C ANISOU 483 CA VAL A 88 11824 11341 7075 1048 -350 -887 C ATOM 484 C VAL A 88 112.101 -2.612 47.918 1.00 85.33 C ANISOU 484 C VAL A 88 12350 12258 7815 1365 -250 -953 C ATOM 485 O VAL A 88 112.752 -2.031 47.051 1.00 85.54 O ANISOU 485 O VAL A 88 12107 12503 7890 1147 -101 -1102 O ATOM 486 CB VAL A 88 111.786 -1.512 50.228 1.00 85.87 C ANISOU 486 CB VAL A 88 12350 12523 7752 1116 -575 -934 C ATOM 487 CG1 VAL A 88 113.207 -0.964 50.107 1.00 89.33 C ANISOU 487 CG1 VAL A 88 12218 13563 8160 1029 -580 -1155 C ATOM 488 CG2 VAL A 88 110.924 -0.543 51.031 1.00 83.26 C ANISOU 488 CG2 VAL A 88 12209 12017 7407 748 -631 -900 C ATOM 489 N ILE A 89 112.118 -3.953 48.069 1.00 83.02 N ANISOU 489 N ILE A 89 12241 11838 7466 1867 -299 -842 N ATOM 490 CA ILE A 89 112.944 -4.857 47.251 1.00 85.50 C ANISOU 490 CA ILE A 89 12433 12280 7773 2249 -195 -890 C ATOM 491 C ILE A 89 112.366 -4.951 45.809 1.00 86.86 C ANISOU 491 C ILE A 89 12869 12088 8046 2055 51 -888 C ATOM 492 O ILE A 89 113.027 -5.490 44.920 1.00 88.55 O ANISOU 492 O ILE A 89 12980 12395 8268 2268 191 -956 O ATOM 493 CB ILE A 89 113.097 -6.268 47.901 1.00 91.09 C ANISOU 493 CB ILE A 89 13356 12899 8353 2879 -309 -758 C ATOM 494 CG1 ILE A 89 111.722 -6.944 48.173 1.00 88.73 C ANISOU 494 CG1 ILE A 89 13699 11981 8032 2885 -294 -563 C ATOM 495 CG2 ILE A 89 113.959 -6.181 49.172 1.00 95.14 C ANISOU 495 CG2 ILE A 89 13516 13900 8733 3145 -561 -792 C ATOM 496 CD1 ILE A 89 111.751 -8.443 48.565 1.00 98.28 C ANISOU 496 CD1 ILE A 89 15290 12954 9097 3468 -319 -424 C ATOM 497 N THR A 90 111.159 -4.391 45.590 1.00 79.37 N ANISOU 497 N THR A 90 12238 10762 7157 1664 98 -820 N ATOM 498 CA THR A 90 110.438 -4.339 44.314 1.00 76.75 C ANISOU 498 CA THR A 90 12174 10095 6891 1439 287 -814 C ATOM 499 C THR A 90 110.802 -3.020 43.570 1.00 79.85 C ANISOU 499 C THR A 90 12321 10681 7337 1009 412 -951 C ATOM 500 O THR A 90 110.746 -2.990 42.339 1.00 79.11 O ANISOU 500 O THR A 90 12322 10466 7269 897 594 -993 O ATOM 501 CB THR A 90 108.922 -4.476 44.600 1.00 81.25 C ANISOU 501 CB THR A 90 13192 10214 7466 1296 243 -674 C ATOM 502 OG1 THR A 90 108.681 -5.734 45.233 1.00 82.21 O ANISOU 502 OG1 THR A 90 13579 10144 7515 1661 176 -563 O ATOM 503 CG2 THR A 90 108.053 -4.369 43.360 1.00 77.34 C ANISOU 503 CG2 THR A 90 12961 9413 7012 1056 394 -672 C ATOM 504 N LEU A 91 111.219 -1.964 44.318 1.00 76.68 N ANISOU 504 N LEU A 91 11637 10573 6925 768 330 -1028 N ATOM 505 CA LEU A 91 111.599 -0.640 43.795 1.00 76.52 C ANISOU 505 CA LEU A 91 11435 10719 6921 319 464 -1165 C ATOM 506 C LEU A 91 112.744 -0.687 42.742 1.00 83.12 C ANISOU 506 C LEU A 91 11973 11845 7762 317 664 -1326 C ATOM 507 O LEU A 91 112.610 0.067 41.776 1.00 82.06 O ANISOU 507 O LEU A 91 11948 11594 7636 -23 856 -1380 O ATOM 508 CB LEU A 91 112.014 0.330 44.915 1.00 77.53 C ANISOU 508 CB LEU A 91 11303 11149 7007 87 343 -1247 C ATOM 509 CG LEU A 91 110.906 0.884 45.822 1.00 79.42 C ANISOU 509 CG LEU A 91 11827 11115 7232 -78 214 -1133 C ATOM 510 CD1 LEU A 91 111.497 1.577 47.032 1.00 81.34 C ANISOU 510 CD1 LEU A 91 11792 11704 7408 -223 76 -1227 C ATOM 511 CD2 LEU A 91 109.986 1.849 45.070 1.00 79.09 C ANISOU 511 CD2 LEU A 91 12109 10728 7214 -442 360 -1103 C ATOM 512 N PRO A 92 113.839 -1.511 42.833 1.00 82.96 N ANISOU 512 N PRO A 92 11606 12193 7723 688 647 -1407 N ATOM 513 CA PRO A 92 114.861 -1.484 41.762 1.00 85.55 C ANISOU 513 CA PRO A 92 11645 12802 8057 652 876 -1577 C ATOM 514 C PRO A 92 114.288 -1.779 40.371 1.00 87.71 C ANISOU 514 C PRO A 92 12296 12675 8357 606 1089 -1525 C ATOM 515 O PRO A 92 114.818 -1.267 39.386 1.00 88.24 O ANISOU 515 O PRO A 92 12249 12859 8419 357 1320 -1656 O ATOM 516 CB PRO A 92 115.842 -2.583 42.177 1.00 91.00 C ANISOU 516 CB PRO A 92 11996 13867 8712 1208 783 -1620 C ATOM 517 CG PRO A 92 115.680 -2.701 43.631 1.00 95.40 C ANISOU 517 CG PRO A 92 12509 14518 9220 1385 496 -1538 C ATOM 518 CD PRO A 92 114.225 -2.469 43.891 1.00 86.41 C ANISOU 518 CD PRO A 92 11897 12825 8109 1178 432 -1354 C ATOM 519 N PHE A 93 113.195 -2.574 40.296 1.00 82.09 N ANISOU 519 N PHE A 93 12040 11499 7653 809 1019 -1347 N ATOM 520 CA PHE A 93 112.505 -2.906 39.046 1.00 80.51 C ANISOU 520 CA PHE A 93 12228 10909 7452 759 1182 -1297 C ATOM 521 C PHE A 93 111.702 -1.701 38.543 1.00 81.86 C ANISOU 521 C PHE A 93 12630 10857 7617 279 1247 -1279 C ATOM 522 O PHE A 93 111.667 -1.459 37.334 1.00 81.50 O ANISOU 522 O PHE A 93 12730 10694 7540 112 1442 -1322 O ATOM 523 CB PHE A 93 111.583 -4.128 39.220 1.00 80.91 C ANISOU 523 CB PHE A 93 12679 10572 7491 1077 1084 -1142 C ATOM 524 CG PHE A 93 112.263 -5.391 39.696 1.00 85.34 C ANISOU 524 CG PHE A 93 13151 11253 8021 1606 1034 -1129 C ATOM 525 CD1 PHE A 93 112.121 -5.824 41.008 1.00 88.66 C ANISOU 525 CD1 PHE A 93 13584 11689 8415 1855 821 -1032 C ATOM 526 CD2 PHE A 93 113.051 -6.144 38.834 1.00 90.35 C ANISOU 526 CD2 PHE A 93 13721 11977 8632 1885 1211 -1211 C ATOM 527 CE1 PHE A 93 112.748 -6.994 41.448 1.00 92.62 C ANISOU 527 CE1 PHE A 93 14066 12276 8851 2399 775 -1005 C ATOM 528 CE2 PHE A 93 113.685 -7.310 39.276 1.00 96.26 C ANISOU 528 CE2 PHE A 93 14424 12821 9328 2441 1172 -1192 C ATOM 529 CZ PHE A 93 113.528 -7.728 40.580 1.00 94.59 C ANISOU 529 CZ PHE A 93 14256 12608 9076 2706 948 -1083 C ATOM 530 N TRP A 94 111.065 -0.948 39.472 1.00 76.47 N ANISOU 530 N TRP A 94 12005 10109 6941 86 1090 -1212 N ATOM 531 CA TRP A 94 110.279 0.258 39.182 1.00 74.21 C ANISOU 531 CA TRP A 94 11957 9611 6629 -307 1131 -1183 C ATOM 532 C TRP A 94 111.156 1.373 38.601 1.00 80.31 C ANISOU 532 C TRP A 94 12558 10597 7359 -664 1341 -1335 C ATOM 533 O TRP A 94 110.695 2.111 37.728 1.00 79.12 O ANISOU 533 O TRP A 94 12690 10222 7149 -918 1478 -1322 O ATOM 534 CB TRP A 94 109.567 0.766 40.447 1.00 71.03 C ANISOU 534 CB TRP A 94 11613 9140 6236 -383 931 -1098 C ATOM 535 CG TRP A 94 108.264 0.083 40.730 1.00 69.27 C ANISOU 535 CG TRP A 94 11707 8585 6027 -213 790 -943 C ATOM 536 CD1 TRP A 94 108.084 -1.124 41.338 1.00 72.25 C ANISOU 536 CD1 TRP A 94 12116 8911 6422 112 670 -871 C ATOM 537 CD2 TRP A 94 106.954 0.587 40.440 1.00 66.58 C ANISOU 537 CD2 TRP A 94 11697 7936 5663 -369 768 -855 C ATOM 538 NE1 TRP A 94 106.742 -1.415 41.425 1.00 69.27 N ANISOU 538 NE1 TRP A 94 12062 8214 6041 108 596 -759 N ATOM 539 CE2 TRP A 94 106.024 -0.381 40.882 1.00 69.02 C ANISOU 539 CE2 TRP A 94 12181 8053 5990 -170 641 -752 C ATOM 540 CE3 TRP A 94 106.472 1.762 39.837 1.00 66.89 C ANISOU 540 CE3 TRP A 94 11919 7847 5648 -642 851 -855 C ATOM 541 CZ2 TRP A 94 104.643 -0.212 40.737 1.00 66.12 C ANISOU 541 CZ2 TRP A 94 12085 7436 5602 -254 586 -673 C ATOM 542 CZ3 TRP A 94 105.102 1.929 39.698 1.00 66.22 C ANISOU 542 CZ3 TRP A 94 12124 7503 5534 -657 776 -756 C ATOM 543 CH2 TRP A 94 104.204 0.953 40.151 1.00 65.53 C ANISOU 543 CH2 TRP A 94 12127 7293 5480 -474 640 -677 C ATOM 544 N ALA A 95 112.413 1.484 39.082 1.00 79.88 N ANISOU 544 N ALA A 95 12050 10987 7314 -683 1368 -1486 N ATOM 545 CA ALA A 95 113.390 2.483 38.645 1.00 82.39 C ANISOU 545 CA ALA A 95 12141 11580 7582 -1069 1591 -1674 C ATOM 546 C ALA A 95 113.834 2.247 37.192 1.00 88.13 C ANISOU 546 C ALA A 95 12917 12288 8278 -1097 1864 -1749 C ATOM 547 O ALA A 95 113.919 3.210 36.430 1.00 88.39 O ANISOU 547 O ALA A 95 13115 12234 8235 -1484 2087 -1814 O ATOM 548 CB ALA A 95 114.601 2.462 39.565 1.00 86.36 C ANISOU 548 CB ALA A 95 12080 12638 8096 -1041 1523 -1838 C ATOM 549 N VAL A 96 114.103 0.976 36.812 1.00 85.54 N ANISOU 549 N VAL A 96 12500 12012 7990 -684 1862 -1737 N ATOM 550 CA VAL A 96 114.559 0.576 35.474 1.00 87.06 C ANISOU 550 CA VAL A 96 12733 12198 8148 -646 2119 -1814 C ATOM 551 C VAL A 96 113.414 0.759 34.451 1.00 88.51 C ANISOU 551 C VAL A 96 13488 11873 8268 -770 2189 -1684 C ATOM 552 O VAL A 96 113.660 1.308 33.379 1.00 89.21 O ANISOU 552 O VAL A 96 13710 11912 8274 -1030 2439 -1757 O ATOM 553 CB VAL A 96 115.105 -0.884 35.470 1.00 92.73 C ANISOU 553 CB VAL A 96 13245 13079 8910 -114 2086 -1829 C ATOM 554 CG1 VAL A 96 115.455 -1.360 34.060 1.00 94.11 C ANISOU 554 CG1 VAL A 96 13528 13190 9041 -53 2360 -1899 C ATOM 555 CG2 VAL A 96 116.317 -1.019 36.388 1.00 96.03 C ANISOU 555 CG2 VAL A 96 13059 14072 9357 52 2014 -1972 C ATOM 556 N ASP A 97 112.183 0.316 34.786 1.00 82.16 N ANISOU 556 N ASP A 97 13010 10723 7484 -596 1972 -1506 N ATOM 557 CA ASP A 97 111.001 0.402 33.916 1.00 79.77 C ANISOU 557 CA ASP A 97 13201 10000 7109 -668 1980 -1390 C ATOM 558 C ASP A 97 110.640 1.859 33.570 1.00 83.12 C ANISOU 558 C ASP A 97 13856 10290 7437 -1069 2070 -1381 C ATOM 559 O ASP A 97 110.219 2.129 32.444 1.00 82.58 O ANISOU 559 O ASP A 97 14124 9996 7255 -1177 2196 -1355 O ATOM 560 CB ASP A 97 109.794 -0.281 34.589 1.00 78.86 C ANISOU 560 CB ASP A 97 13293 9635 7036 -447 1718 -1235 C ATOM 561 CG ASP A 97 108.516 -0.285 33.765 1.00 87.69 C ANISOU 561 CG ASP A 97 14853 10395 8071 -500 1687 -1137 C ATOM 562 OD1 ASP A 97 108.497 -0.940 32.699 1.00 89.06 O ANISOU 562 OD1 ASP A 97 15195 10460 8184 -419 1802 -1162 O ATOM 563 OD2 ASP A 97 107.524 0.331 34.209 1.00 92.00 O ANISOU 563 OD2 ASP A 97 15563 10791 8602 -605 1541 -1043 O ATOM 564 N ALA A 98 110.809 2.782 34.530 1.00 79.70 N ANISOU 564 N ALA A 98 13279 9979 7023 -1275 2011 -1402 N ATOM 565 CA ALA A 98 110.478 4.196 34.371 1.00 79.31 C ANISOU 565 CA ALA A 98 13499 9769 6867 -1637 2103 -1389 C ATOM 566 C ALA A 98 111.477 4.952 33.478 1.00 86.21 C ANISOU 566 C ALA A 98 14364 10759 7635 -1979 2438 -1541 C ATOM 567 O ALA A 98 111.064 5.906 32.815 1.00 85.83 O ANISOU 567 O ALA A 98 14721 10448 7442 -2217 2575 -1502 O ATOM 568 CB ALA A 98 110.420 4.866 35.731 1.00 79.46 C ANISOU 568 CB ALA A 98 13379 9883 6930 -1755 1956 -1386 C ATOM 569 N VAL A 99 112.773 4.559 33.465 1.00 85.72 N ANISOU 569 N VAL A 99 13854 11090 7625 -1999 2580 -1717 N ATOM 570 CA VAL A 99 113.784 5.285 32.682 1.00 88.98 C ANISOU 570 CA VAL A 99 14209 11665 7936 -2379 2932 -1894 C ATOM 571 C VAL A 99 114.228 4.483 31.434 1.00 94.40 C ANISOU 571 C VAL A 99 14893 12383 8592 -2233 3135 -1951 C ATOM 572 O VAL A 99 114.367 5.085 30.368 1.00 95.54 O ANISOU 572 O VAL A 99 15328 12382 8589 -2505 3412 -1992 O ATOM 573 CB VAL A 99 115.033 5.714 33.514 1.00 96.05 C ANISOU 573 CB VAL A 99 14562 13058 8873 -2635 3010 -2111 C ATOM 574 CG1 VAL A 99 114.651 6.690 34.619 1.00 94.85 C ANISOU 574 CG1 VAL A 99 14489 12843 8705 -2875 2872 -2082 C ATOM 575 CG2 VAL A 99 115.805 4.524 34.089 1.00 97.15 C ANISOU 575 CG2 VAL A 99 14118 13644 9150 -2251 2871 -2195 C ATOM 576 N ALA A 100 114.466 3.163 31.563 1.00 90.87 N ANISOU 576 N ALA A 100 14164 12104 8258 -1808 3019 -1954 N ATOM 577 CA ALA A 100 114.958 2.333 30.464 1.00 92.52 C ANISOU 577 CA ALA A 100 14353 12361 8439 -1636 3221 -2025 C ATOM 578 C ALA A 100 113.829 1.485 29.843 1.00 93.44 C ANISOU 578 C ALA A 100 14912 12063 8526 -1336 3091 -1852 C ATOM 579 O ALA A 100 112.919 2.052 29.235 1.00 91.19 O ANISOU 579 O ALA A 100 15098 11425 8123 -1494 3092 -1744 O ATOM 580 CB ALA A 100 116.092 1.440 30.955 1.00 96.03 C ANISOU 580 CB ALA A 100 14205 13286 8996 -1346 3223 -2170 C ATOM 581 N ASN A 101 113.906 0.143 29.972 1.00 89.96 N ANISOU 581 N ASN A 101 14336 11674 8169 -907 2991 -1839 N ATOM 582 CA ASN A 101 112.963 -0.815 29.392 1.00 87.83 C ANISOU 582 CA ASN A 101 14454 11053 7864 -648 2899 -1720 C ATOM 583 C ASN A 101 112.718 -1.991 30.354 1.00 90.52 C ANISOU 583 C ASN A 101 14673 11399 8322 -231 2656 -1648 C ATOM 584 O ASN A 101 113.465 -2.156 31.322 1.00 91.52 O ANISOU 584 O ASN A 101 14387 11841 8544 -80 2585 -1702 O ATOM 585 CB ASN A 101 113.544 -1.318 28.049 1.00 91.02 C ANISOU 585 CB ASN A 101 14951 11457 8174 -603 3193 -1826 C ATOM 586 CG ASN A 101 112.608 -2.062 27.119 1.00111.64 C ANISOU 586 CG ASN A 101 18042 13693 10684 -471 3169 -1742 C ATOM 587 OD1 ASN A 101 111.418 -2.263 27.390 1.00103.78 O ANISOU 587 OD1 ASN A 101 17322 12429 9682 -417 2926 -1605 O ATOM 588 ND2 ASN A 101 113.125 -2.451 25.964 1.00105.19 N ANISOU 588 ND2 ASN A 101 17328 12870 9768 -449 3435 -1841 N ATOM 589 N TRP A 102 111.665 -2.792 30.100 1.00 84.76 N ANISOU 589 N TRP A 102 14319 10326 7562 -63 2530 -1535 N ATOM 590 CA TRP A 102 111.359 -3.972 30.903 1.00 83.81 C ANISOU 590 CA TRP A 102 14199 10129 7514 301 2347 -1466 C ATOM 591 C TRP A 102 112.092 -5.173 30.300 1.00 89.95 C ANISOU 591 C TRP A 102 14968 10941 8270 635 2524 -1551 C ATOM 592 O TRP A 102 111.735 -5.621 29.209 1.00 89.80 O ANISOU 592 O TRP A 102 15284 10686 8152 622 2651 -1566 O ATOM 593 CB TRP A 102 109.841 -4.215 30.999 1.00 79.53 C ANISOU 593 CB TRP A 102 14061 9220 6939 259 2146 -1328 C ATOM 594 CG TRP A 102 109.499 -5.378 31.881 1.00 80.20 C ANISOU 594 CG TRP A 102 14198 9195 7078 570 1990 -1261 C ATOM 595 CD1 TRP A 102 109.325 -6.674 31.495 1.00 84.13 C ANISOU 595 CD1 TRP A 102 14954 9484 7528 813 2046 -1265 C ATOM 596 CD2 TRP A 102 109.416 -5.371 33.312 1.00 79.13 C ANISOU 596 CD2 TRP A 102 13881 9152 7033 678 1786 -1188 C ATOM 597 NE1 TRP A 102 109.097 -7.469 32.593 1.00 83.37 N ANISOU 597 NE1 TRP A 102 14885 9313 7479 1059 1899 -1191 N ATOM 598 CE2 TRP A 102 109.150 -6.696 33.723 1.00 83.52 C ANISOU 598 CE2 TRP A 102 14627 9524 7582 991 1731 -1139 C ATOM 599 CE3 TRP A 102 109.510 -4.365 34.289 1.00 79.36 C ANISOU 599 CE3 TRP A 102 13650 9375 7127 526 1655 -1162 C ATOM 600 CZ2 TRP A 102 108.987 -7.044 35.068 1.00 82.37 C ANISOU 600 CZ2 TRP A 102 14423 9389 7486 1167 1548 -1054 C ATOM 601 CZ3 TRP A 102 109.350 -4.712 35.622 1.00 80.27 C ANISOU 601 CZ3 TRP A 102 13677 9523 7300 700 1461 -1088 C ATOM 602 CH2 TRP A 102 109.084 -6.035 36.000 1.00 81.43 C ANISOU 602 CH2 TRP A 102 14020 9487 7432 1022 1407 -1028 C ATOM 603 N TYR A 103 113.128 -5.672 30.997 1.00 88.71 N ANISOU 603 N TYR A 103 14429 11091 8184 951 2533 -1613 N ATOM 604 CA TYR A 103 113.953 -6.798 30.539 1.00 91.78 C ANISOU 604 CA TYR A 103 14767 11557 8546 1352 2709 -1700 C ATOM 605 C TYR A 103 113.672 -8.094 31.304 1.00 95.83 C ANISOU 605 C TYR A 103 15454 11888 9069 1809 2561 -1605 C ATOM 606 O TYR A 103 113.835 -9.186 30.760 1.00 97.34 O ANISOU 606 O TYR A 103 15878 11911 9196 2120 2699 -1630 O ATOM 607 CB TYR A 103 115.454 -6.471 30.707 1.00 96.61 C ANISOU 607 CB TYR A 103 14789 12715 9202 1449 2850 -1863 C ATOM 608 CG TYR A 103 115.893 -5.095 30.251 1.00 98.54 C ANISOU 608 CG TYR A 103 14802 13202 9436 956 3005 -1975 C ATOM 609 CD1 TYR A 103 116.161 -4.835 28.910 1.00101.83 C ANISOU 609 CD1 TYR A 103 15354 13573 9763 741 3304 -2075 C ATOM 610 CD2 TYR A 103 116.147 -4.084 31.173 1.00 98.79 C ANISOU 610 CD2 TYR A 103 14489 13521 9527 707 2881 -1998 C ATOM 611 CE1 TYR A 103 116.602 -3.581 28.489 1.00103.31 C ANISOU 611 CE1 TYR A 103 15388 13954 9913 272 3486 -2181 C ATOM 612 CE2 TYR A 103 116.599 -2.829 30.766 1.00100.57 C ANISOU 612 CE2 TYR A 103 14551 13942 9719 224 3063 -2117 C ATOM 613 CZ TYR A 103 116.820 -2.580 29.422 1.00109.30 C ANISOU 613 CZ TYR A 103 15835 14965 10729 5 3373 -2204 C ATOM 614 OH TYR A 103 117.259 -1.344 29.015 1.00111.80 O ANISOU 614 OH TYR A 103 16061 15433 10985 -494 3586 -2318 O ATOM 615 N PHE A 104 113.275 -7.946 32.574 1.00 90.79 N ANISOU 615 N PHE A 104 14736 11270 8492 1841 2302 -1499 N ATOM 616 CA PHE A 104 113.066 -8.940 33.628 1.00 91.03 C ANISOU 616 CA PHE A 104 14887 11176 8523 2236 2132 -1394 C ATOM 617 C PHE A 104 112.143 -10.125 33.234 1.00 94.58 C ANISOU 617 C PHE A 104 15937 11112 8887 2368 2169 -1318 C ATOM 618 O PHE A 104 112.301 -11.204 33.810 1.00 96.17 O ANISOU 618 O PHE A 104 16299 11195 9046 2793 2142 -1265 O ATOM 619 CB PHE A 104 112.492 -8.241 34.868 1.00 90.16 C ANISOU 619 CB PHE A 104 14670 11111 8475 2053 1865 -1292 C ATOM 620 CG PHE A 104 113.263 -6.979 35.193 1.00 92.16 C ANISOU 620 CG PHE A 104 14406 11821 8790 1814 1843 -1383 C ATOM 621 CD1 PHE A 104 114.544 -7.045 35.731 1.00 98.78 C ANISOU 621 CD1 PHE A 104 14749 13137 9644 2093 1841 -1482 C ATOM 622 CD2 PHE A 104 112.736 -5.728 34.899 1.00 91.88 C ANISOU 622 CD2 PHE A 104 14389 11748 8772 1310 1845 -1387 C ATOM 623 CE1 PHE A 104 115.273 -5.880 35.990 1.00100.64 C ANISOU 623 CE1 PHE A 104 14502 13817 9919 1801 1845 -1603 C ATOM 624 CE2 PHE A 104 113.463 -4.563 35.163 1.00 95.59 C ANISOU 624 CE2 PHE A 104 14447 12598 9274 1041 1867 -1489 C ATOM 625 CZ PHE A 104 114.725 -4.647 35.709 1.00 97.11 C ANISOU 625 CZ PHE A 104 14136 13273 9488 1254 1872 -1607 C ATOM 626 N GLY A 105 111.231 -9.939 32.280 1.00 89.03 N ANISOU 626 N GLY A 105 15572 10121 8135 2018 2234 -1321 N ATOM 627 CA GLY A 105 110.363 -11.019 31.816 1.00 88.72 C ANISOU 627 CA GLY A 105 16083 9632 7994 2061 2286 -1290 C ATOM 628 C GLY A 105 108.923 -10.996 32.286 1.00 89.46 C ANISOU 628 C GLY A 105 16475 9440 8076 1784 2099 -1191 C ATOM 629 O GLY A 105 108.515 -10.098 33.028 1.00 86.74 O ANISOU 629 O GLY A 105 15924 9225 7809 1576 1913 -1126 O ATOM 630 N ASN A 106 108.150 -12.016 31.864 1.00 86.23 N ANISOU 630 N ASN A 106 16558 8647 7557 1772 2165 -1194 N ATOM 631 CA ASN A 106 106.720 -12.169 32.140 1.00 83.72 C ANISOU 631 CA ASN A 106 16547 8064 7199 1476 2031 -1142 C ATOM 632 C ASN A 106 106.433 -12.672 33.571 1.00 87.34 C ANISOU 632 C ASN A 106 17079 8420 7687 1639 1897 -1035 C ATOM 633 O ASN A 106 105.383 -12.324 34.115 1.00 84.50 O ANISOU 633 O ASN A 106 16760 8001 7347 1361 1743 -983 O ATOM 634 CB ASN A 106 106.091 -13.132 31.131 1.00 85.14 C ANISOU 634 CB ASN A 106 17224 7900 7226 1367 2180 -1224 C ATOM 635 CG ASN A 106 104.655 -12.816 30.784 1.00102.36 C ANISOU 635 CG ASN A 106 19575 9972 9347 912 2061 -1242 C ATOM 636 OD1 ASN A 106 104.310 -11.691 30.407 1.00 93.74 O ANISOU 636 OD1 ASN A 106 18258 9076 8281 659 1955 -1242 O ATOM 637 ND2 ASN A 106 103.804 -13.827 30.803 1.00 94.73 N ANISOU 637 ND2 ASN A 106 19031 8693 8269 801 2096 -1276 N ATOM 638 N PHE A 107 107.333 -13.493 34.169 1.00 86.66 N ANISOU 638 N PHE A 107 17027 8316 7583 2105 1961 -1002 N ATOM 639 CA PHE A 107 107.147 -14.018 35.532 1.00 86.85 C ANISOU 639 CA PHE A 107 17177 8226 7596 2309 1846 -888 C ATOM 640 C PHE A 107 107.306 -12.895 36.566 1.00 87.74 C ANISOU 640 C PHE A 107 16816 8687 7833 2244 1623 -818 C ATOM 641 O PHE A 107 106.476 -12.781 37.471 1.00 85.41 O ANISOU 641 O PHE A 107 16610 8294 7546 2083 1482 -738 O ATOM 642 CB PHE A 107 108.121 -15.176 35.842 1.00 92.91 C ANISOU 642 CB PHE A 107 18137 8892 8273 2896 1969 -863 C ATOM 643 CG PHE A 107 108.035 -15.702 37.261 1.00 95.62 C ANISOU 643 CG PHE A 107 18643 9121 8569 3163 1851 -731 C ATOM 644 CD1 PHE A 107 107.038 -16.598 37.631 1.00 99.25 C ANISOU 644 CD1 PHE A 107 19685 9117 8907 3048 1901 -679 C ATOM 645 CD2 PHE A 107 108.957 -15.304 38.225 1.00 98.77 C ANISOU 645 CD2 PHE A 107 18625 9886 9019 3509 1698 -671 C ATOM 646 CE1 PHE A 107 106.954 -17.074 38.944 1.00101.29 C ANISOU 646 CE1 PHE A 107 20147 9245 9095 3284 1813 -550 C ATOM 647 CE2 PHE A 107 108.869 -15.778 39.537 1.00102.67 C ANISOU 647 CE2 PHE A 107 19300 10274 9436 3768 1579 -541 C ATOM 648 CZ PHE A 107 107.872 -16.662 39.887 1.00101.05 C ANISOU 648 CZ PHE A 107 19716 9570 9107 3664 1645 -472 C ATOM 649 N LEU A 108 108.374 -12.082 36.432 1.00 84.29 N ANISOU 649 N LEU A 108 15889 8658 7480 2345 1611 -866 N ATOM 650 CA LEU A 108 108.660 -10.947 37.313 1.00 82.42 C ANISOU 650 CA LEU A 108 15192 8778 7345 2249 1426 -834 C ATOM 651 C LEU A 108 107.584 -9.866 37.159 1.00 82.52 C ANISOU 651 C LEU A 108 15179 8762 7412 1736 1331 -824 C ATOM 652 O LEU A 108 107.299 -9.153 38.121 1.00 80.11 O ANISOU 652 O LEU A 108 14698 8578 7161 1612 1162 -765 O ATOM 653 CB LEU A 108 110.062 -10.352 37.030 1.00 84.35 C ANISOU 653 CB LEU A 108 14932 9475 7643 2402 1484 -932 C ATOM 654 CG LEU A 108 111.338 -11.059 37.569 1.00 92.90 C ANISOU 654 CG LEU A 108 15805 10805 8690 2969 1496 -947 C ATOM 655 CD1 LEU A 108 111.381 -11.099 39.090 1.00 93.29 C ANISOU 655 CD1 LEU A 108 15755 10964 8726 3173 1268 -843 C ATOM 656 CD2 LEU A 108 111.578 -12.427 36.938 1.00 98.27 C ANISOU 656 CD2 LEU A 108 16868 11207 9262 3363 1688 -960 C ATOM 657 N CYS A 109 106.969 -9.776 35.956 1.00 78.43 N ANISOU 657 N CYS A 109 14859 8082 6857 1468 1435 -882 N ATOM 658 CA CYS A 109 105.904 -8.833 35.610 1.00 75.42 C ANISOU 658 CA CYS A 109 14499 7669 6489 1046 1353 -878 C ATOM 659 C CYS A 109 104.674 -9.077 36.489 1.00 77.50 C ANISOU 659 C CYS A 109 14964 7741 6743 915 1210 -800 C ATOM 660 O CYS A 109 104.093 -8.117 36.999 1.00 74.97 O ANISOU 660 O CYS A 109 14491 7522 6473 703 1071 -759 O ATOM 661 CB CYS A 109 105.555 -8.938 34.127 1.00 75.98 C ANISOU 661 CB CYS A 109 14787 7608 6475 871 1489 -960 C ATOM 662 SG CYS A 109 104.366 -7.700 33.548 1.00 77.15 S ANISOU 662 SG CYS A 109 14943 7774 6596 440 1379 -957 S ATOM 663 N LYS A 110 104.299 -10.356 36.682 1.00 75.23 N ANISOU 663 N LYS A 110 15037 7169 6378 1038 1267 -786 N ATOM 664 CA LYS A 110 103.171 -10.741 37.531 1.00 74.04 C ANISOU 664 CA LYS A 110 15110 6825 6198 895 1179 -730 C ATOM 665 C LYS A 110 103.546 -10.579 39.005 1.00 77.86 C ANISOU 665 C LYS A 110 15434 7416 6732 1088 1055 -628 C ATOM 666 O LYS A 110 102.745 -10.052 39.776 1.00 75.57 O ANISOU 666 O LYS A 110 15088 7152 6475 888 929 -581 O ATOM 667 CB LYS A 110 102.716 -12.183 37.245 1.00 78.43 C ANISOU 667 CB LYS A 110 16162 7013 6624 924 1325 -765 C ATOM 668 CG LYS A 110 102.110 -12.381 35.865 1.00 89.82 C ANISOU 668 CG LYS A 110 17800 8343 7985 661 1425 -882 C ATOM 669 CD LYS A 110 101.508 -13.769 35.704 1.00100.36 C ANISOU 669 CD LYS A 110 19658 9300 9173 595 1573 -937 C ATOM 670 CE LYS A 110 100.837 -13.972 34.365 1.00110.64 C ANISOU 670 CE LYS A 110 21149 10519 10369 290 1653 -1076 C ATOM 671 NZ LYS A 110 101.809 -13.990 33.239 1.00122.96 N ANISOU 671 NZ LYS A 110 22694 12119 11906 477 1783 -1132 N ATOM 672 N ALA A 111 104.779 -11.003 39.376 1.00 76.58 N ANISOU 672 N ALA A 111 15182 7350 6565 1493 1086 -603 N ATOM 673 CA ALA A 111 105.345 -10.958 40.729 1.00 76.90 C ANISOU 673 CA ALA A 111 15067 7536 6617 1756 958 -515 C ATOM 674 C ALA A 111 105.391 -9.527 41.295 1.00 77.72 C ANISOU 674 C ALA A 111 14741 7964 6824 1551 794 -506 C ATOM 675 O ALA A 111 105.038 -9.334 42.458 1.00 76.28 O ANISOU 675 O ALA A 111 14549 7793 6639 1533 664 -431 O ATOM 676 CB ALA A 111 106.746 -11.552 40.723 1.00 80.95 C ANISOU 676 CB ALA A 111 15477 8190 7092 2247 1018 -524 C ATOM 677 N VAL A 112 105.808 -8.535 40.479 1.00 73.14 N ANISOU 677 N VAL A 112 13857 7617 6315 1383 822 -586 N ATOM 678 CA VAL A 112 105.891 -7.124 40.880 1.00 71.07 C ANISOU 678 CA VAL A 112 13251 7623 6129 1156 710 -595 C ATOM 679 C VAL A 112 104.454 -6.556 41.022 1.00 72.40 C ANISOU 679 C VAL A 112 13573 7628 6309 814 637 -556 C ATOM 680 O VAL A 112 104.175 -5.863 42.006 1.00 70.76 O ANISOU 680 O VAL A 112 13246 7509 6129 719 513 -511 O ATOM 681 CB VAL A 112 106.769 -6.299 39.890 1.00 75.17 C ANISOU 681 CB VAL A 112 13485 8391 6687 1058 813 -700 C ATOM 682 CG1 VAL A 112 106.565 -4.796 40.051 1.00 73.05 C ANISOU 682 CG1 VAL A 112 13012 8278 6464 726 750 -716 C ATOM 683 CG2 VAL A 112 108.247 -6.652 40.043 1.00 77.98 C ANISOU 683 CG2 VAL A 112 13553 9035 7040 1390 856 -758 C ATOM 684 N HIS A 113 103.550 -6.884 40.070 1.00 68.48 N ANISOU 684 N HIS A 113 13328 6916 5774 647 712 -584 N ATOM 685 CA HIS A 113 102.152 -6.436 40.064 1.00 66.38 C ANISOU 685 CA HIS A 113 13172 6549 5500 358 644 -571 C ATOM 686 C HIS A 113 101.362 -6.945 41.278 1.00 70.27 C ANISOU 686 C HIS A 113 13811 6913 5976 350 568 -505 C ATOM 687 O HIS A 113 100.507 -6.213 41.778 1.00 68.44 O ANISOU 687 O HIS A 113 13515 6724 5766 162 477 -483 O ATOM 688 CB HIS A 113 101.439 -6.884 38.784 1.00 67.32 C ANISOU 688 CB HIS A 113 13517 6512 5549 213 732 -638 C ATOM 689 CG HIS A 113 101.326 -5.800 37.762 1.00 69.78 C ANISOU 689 CG HIS A 113 13719 6942 5853 44 734 -679 C ATOM 690 ND1 HIS A 113 102.241 -5.678 36.736 1.00 72.58 N ANISOU 690 ND1 HIS A 113 14031 7357 6189 101 855 -733 N ATOM 691 CD2 HIS A 113 100.412 -4.807 37.656 1.00 69.98 C ANISOU 691 CD2 HIS A 113 13698 7026 5866 -152 641 -669 C ATOM 692 CE1 HIS A 113 101.851 -4.627 36.032 1.00 71.08 C ANISOU 692 CE1 HIS A 113 13811 7232 5964 -81 836 -747 C ATOM 693 NE2 HIS A 113 100.759 -4.067 36.553 1.00 69.88 N ANISOU 693 NE2 HIS A 113 13659 7082 5812 -211 700 -704 N ATOM 694 N VAL A 114 101.638 -8.181 41.742 1.00 68.68 N ANISOU 694 N VAL A 114 13835 6542 5718 564 623 -473 N ATOM 695 CA VAL A 114 100.963 -8.793 42.894 1.00 68.79 C ANISOU 695 CA VAL A 114 14064 6390 5682 559 591 -408 C ATOM 696 C VAL A 114 101.406 -8.057 44.177 1.00 72.25 C ANISOU 696 C VAL A 114 14268 7024 6162 658 450 -334 C ATOM 697 O VAL A 114 100.542 -7.623 44.940 1.00 70.71 O ANISOU 697 O VAL A 114 14072 6822 5973 476 382 -305 O ATOM 698 CB VAL A 114 101.218 -10.329 42.964 1.00 75.42 C ANISOU 698 CB VAL A 114 15300 6945 6411 787 718 -388 C ATOM 699 CG1 VAL A 114 100.858 -10.913 44.329 1.00 76.11 C ANISOU 699 CG1 VAL A 114 15627 6870 6421 856 695 -297 C ATOM 700 CG2 VAL A 114 100.462 -11.059 41.858 1.00 75.83 C ANISOU 700 CG2 VAL A 114 15648 6767 6396 579 862 -480 C ATOM 701 N ILE A 115 102.735 -7.880 44.381 1.00 70.02 N ANISOU 701 N ILE A 115 13761 6947 5896 929 411 -324 N ATOM 702 CA ILE A 115 103.333 -7.200 45.544 1.00 69.84 C ANISOU 702 CA ILE A 115 13486 7163 5889 1025 268 -281 C ATOM 703 C ILE A 115 102.802 -5.752 45.633 1.00 71.25 C ANISOU 703 C ILE A 115 13443 7487 6143 701 197 -308 C ATOM 704 O ILE A 115 102.510 -5.285 46.737 1.00 69.98 O ANISOU 704 O ILE A 115 13241 7377 5972 644 97 -264 O ATOM 705 CB ILE A 115 104.892 -7.249 45.478 1.00 75.20 C ANISOU 705 CB ILE A 115 13894 8114 6563 1342 250 -313 C ATOM 706 CG1 ILE A 115 105.400 -8.702 45.677 1.00 78.46 C ANISOU 706 CG1 ILE A 115 14570 8374 6868 1764 299 -260 C ATOM 707 CG2 ILE A 115 105.536 -6.311 46.518 1.00 76.19 C ANISOU 707 CG2 ILE A 115 13679 8569 6700 1349 93 -315 C ATOM 708 CD1 ILE A 115 106.888 -8.960 45.341 1.00 88.28 C ANISOU 708 CD1 ILE A 115 15553 9893 8097 2141 315 -312 C ATOM 709 N TYR A 116 102.645 -5.073 44.478 1.00 67.21 N ANISOU 709 N TYR A 116 12840 7014 5682 508 260 -376 N ATOM 710 CA TYR A 116 102.136 -3.700 44.396 1.00 65.34 C ANISOU 710 CA TYR A 116 12469 6870 5489 243 220 -397 C ATOM 711 C TYR A 116 100.669 -3.638 44.859 1.00 66.70 C ANISOU 711 C TYR A 116 12807 6891 5646 78 180 -360 C ATOM 712 O TYR A 116 100.319 -2.722 45.600 1.00 65.41 O ANISOU 712 O TYR A 116 12558 6800 5496 -29 110 -341 O ATOM 713 CB TYR A 116 102.287 -3.144 42.966 1.00 66.72 C ANISOU 713 CB TYR A 116 12596 7075 5677 122 314 -465 C ATOM 714 CG TYR A 116 101.910 -1.684 42.808 1.00 67.90 C ANISOU 714 CG TYR A 116 12667 7295 5837 -102 295 -479 C ATOM 715 CD1 TYR A 116 102.577 -0.688 43.518 1.00 70.10 C ANISOU 715 CD1 TYR A 116 12759 7744 6131 -166 259 -492 C ATOM 716 CD2 TYR A 116 100.958 -1.289 41.873 1.00 68.03 C ANISOU 716 CD2 TYR A 116 12816 7210 5821 -238 321 -488 C ATOM 717 CE1 TYR A 116 102.260 0.660 43.349 1.00 70.19 C ANISOU 717 CE1 TYR A 116 12777 7765 6126 -366 274 -505 C ATOM 718 CE2 TYR A 116 100.637 0.057 41.689 1.00 68.41 C ANISOU 718 CE2 TYR A 116 12853 7291 5847 -382 315 -488 C ATOM 719 CZ TYR A 116 101.288 1.028 42.434 1.00 76.04 C ANISOU 719 CZ TYR A 116 13692 8370 6830 -448 306 -493 C ATOM 720 OH TYR A 116 100.973 2.356 42.259 1.00 76.54 O ANISOU 720 OH TYR A 116 13823 8412 6846 -587 329 -491 O ATOM 721 N THR A 117 99.840 -4.633 44.470 1.00 62.44 N ANISOU 721 N THR A 117 12502 6155 5068 48 238 -365 N ATOM 722 CA THR A 117 98.427 -4.736 44.858 1.00 60.95 C ANISOU 722 CA THR A 117 12440 5865 4855 -132 225 -362 C ATOM 723 C THR A 117 98.327 -5.002 46.374 1.00 64.06 C ANISOU 723 C THR A 117 12897 6220 5222 -76 179 -293 C ATOM 724 O THR A 117 97.519 -4.357 47.041 1.00 62.71 O ANISOU 724 O THR A 117 12676 6091 5058 -212 134 -284 O ATOM 725 CB THR A 117 97.727 -5.828 44.030 1.00 69.13 C ANISOU 725 CB THR A 117 13706 6727 5833 -218 320 -417 C ATOM 726 OG1 THR A 117 97.865 -5.503 42.649 1.00 69.10 O ANISOU 726 OG1 THR A 117 13646 6777 5832 -260 348 -479 O ATOM 727 CG2 THR A 117 96.244 -5.975 44.366 1.00 66.93 C ANISOU 727 CG2 THR A 117 13507 6404 5518 -450 321 -452 C ATOM 728 N VAL A 118 99.164 -5.921 46.912 1.00 61.26 N ANISOU 728 N VAL A 118 12665 5792 4820 154 192 -243 N ATOM 729 CA VAL A 118 99.201 -6.270 48.339 1.00 61.52 C ANISOU 729 CA VAL A 118 12812 5775 4788 256 146 -165 C ATOM 730 C VAL A 118 99.501 -4.997 49.163 1.00 63.23 C ANISOU 730 C VAL A 118 12766 6218 5042 225 22 -149 C ATOM 731 O VAL A 118 98.687 -4.626 50.004 1.00 61.80 O ANISOU 731 O VAL A 118 12624 6015 4843 88 -1 -129 O ATOM 732 CB VAL A 118 100.217 -7.415 48.644 1.00 67.96 C ANISOU 732 CB VAL A 118 13808 6498 5516 597 165 -106 C ATOM 733 CG1 VAL A 118 100.428 -7.603 50.146 1.00 68.86 C ANISOU 733 CG1 VAL A 118 14021 6609 5533 753 82 -14 C ATOM 734 CG2 VAL A 118 99.782 -8.729 48.004 1.00 69.17 C ANISOU 734 CG2 VAL A 118 14332 6352 5599 601 321 -121 C ATOM 735 N ASN A 119 100.626 -4.311 48.868 1.00 59.49 N ANISOU 735 N ASN A 119 12030 5961 4611 316 -35 -178 N ATOM 736 CA ASN A 119 101.097 -3.102 49.551 1.00 58.67 C ANISOU 736 CA ASN A 119 11689 6079 4524 254 -133 -192 C ATOM 737 C ASN A 119 100.074 -1.941 49.481 1.00 59.98 C ANISOU 737 C ASN A 119 11825 6231 4732 -14 -122 -218 C ATOM 738 O ASN A 119 100.001 -1.158 50.429 1.00 59.19 O ANISOU 738 O ASN A 119 11670 6209 4611 -85 -184 -211 O ATOM 739 CB ASN A 119 102.435 -2.647 48.948 1.00 60.84 C ANISOU 739 CB ASN A 119 11694 6592 4832 327 -143 -259 C ATOM 740 CG ASN A 119 103.109 -1.482 49.645 1.00 85.30 C ANISOU 740 CG ASN A 119 14548 9942 7922 229 -228 -305 C ATOM 741 OD1 ASN A 119 103.551 -0.524 49.004 1.00 80.79 O ANISOU 741 OD1 ASN A 119 13807 9500 7390 65 -182 -384 O ATOM 742 ND2 ASN A 119 103.208 -1.528 50.968 1.00 77.65 N ANISOU 742 ND2 ASN A 119 13587 9038 6877 301 -340 -264 N ATOM 743 N LEU A 120 99.294 -1.832 48.383 1.00 55.03 N ANISOU 743 N LEU A 120 11249 5516 4144 -136 -48 -252 N ATOM 744 CA LEU A 120 98.299 -0.766 48.216 1.00 53.30 C ANISOU 744 CA LEU A 120 11011 5299 3942 -312 -44 -273 C ATOM 745 C LEU A 120 97.097 -0.921 49.151 1.00 56.40 C ANISOU 745 C LEU A 120 11507 5617 4305 -383 -51 -247 C ATOM 746 O LEU A 120 96.593 0.090 49.641 1.00 55.20 O ANISOU 746 O LEU A 120 11311 5512 4150 -461 -71 -251 O ATOM 747 CB LEU A 120 97.778 -0.692 46.768 1.00 52.95 C ANISOU 747 CB LEU A 120 10991 5215 3911 -376 13 -316 C ATOM 748 CG LEU A 120 98.606 0.094 45.744 1.00 57.83 C ANISOU 748 CG LEU A 120 11522 5909 4542 -390 49 -351 C ATOM 749 CD1 LEU A 120 98.092 -0.149 44.335 1.00 57.87 C ANISOU 749 CD1 LEU A 120 11605 5856 4527 -418 98 -385 C ATOM 750 CD2 LEU A 120 98.614 1.594 46.047 1.00 60.02 C ANISOU 750 CD2 LEU A 120 11754 6246 4806 -487 38 -355 C ATOM 751 N TYR A 121 96.619 -2.160 49.373 1.00 53.70 N ANISOU 751 N TYR A 121 11325 5150 3930 -369 -9 -231 N ATOM 752 CA TYR A 121 95.435 -2.391 50.199 1.00 53.66 C ANISOU 752 CA TYR A 121 11420 5083 3886 -484 24 -229 C ATOM 753 C TYR A 121 95.790 -2.809 51.638 1.00 57.84 C ANISOU 753 C TYR A 121 12072 5557 4346 -407 4 -160 C ATOM 754 O TYR A 121 94.998 -2.536 52.543 1.00 57.14 O ANISOU 754 O TYR A 121 12022 5465 4224 -506 22 -156 O ATOM 755 CB TYR A 121 94.519 -3.450 49.562 1.00 55.78 C ANISOU 755 CB TYR A 121 11823 5242 4128 -601 118 -280 C ATOM 756 CG TYR A 121 94.008 -3.046 48.195 1.00 57.57 C ANISOU 756 CG TYR A 121 11932 5554 4388 -679 117 -356 C ATOM 757 CD1 TYR A 121 93.087 -2.011 48.049 1.00 59.06 C ANISOU 757 CD1 TYR A 121 11968 5885 4588 -751 82 -396 C ATOM 758 CD2 TYR A 121 94.426 -3.712 47.047 1.00 58.97 C ANISOU 758 CD2 TYR A 121 12174 5671 4562 -652 151 -387 C ATOM 759 CE1 TYR A 121 92.623 -1.627 46.791 1.00 60.21 C ANISOU 759 CE1 TYR A 121 12026 6124 4728 -775 59 -456 C ATOM 760 CE2 TYR A 121 93.969 -3.337 45.784 1.00 59.67 C ANISOU 760 CE2 TYR A 121 12177 5845 4650 -716 139 -455 C ATOM 761 CZ TYR A 121 93.065 -2.294 45.660 1.00 66.62 C ANISOU 761 CZ TYR A 121 12906 6880 5528 -770 82 -485 C ATOM 762 OH TYR A 121 92.601 -1.924 44.420 1.00 67.59 O ANISOU 762 OH TYR A 121 12965 7101 5616 -789 50 -543 O ATOM 763 N SER A 122 96.958 -3.446 51.860 1.00 55.17 N ANISOU 763 N SER A 122 11795 5196 3969 -210 -36 -109 N ATOM 764 CA SER A 122 97.352 -3.869 53.206 1.00 56.00 C ANISOU 764 CA SER A 122 12041 5266 3971 -85 -80 -34 C ATOM 765 C SER A 122 97.697 -2.653 54.078 1.00 58.76 C ANISOU 765 C SER A 122 12216 5795 4315 -107 -186 -35 C ATOM 766 O SER A 122 97.143 -2.537 55.170 1.00 58.81 O ANISOU 766 O SER A 122 12332 5762 4251 -169 -182 -7 O ATOM 767 CB SER A 122 98.522 -4.851 53.170 1.00 61.16 C ANISOU 767 CB SER A 122 12791 5885 4560 200 -113 18 C ATOM 768 OG SER A 122 99.675 -4.293 52.563 1.00 69.80 O ANISOU 768 OG SER A 122 13610 7192 5717 317 -193 -19 O ATOM 769 N SER A 123 98.556 -1.732 53.579 1.00 53.93 N ANISOU 769 N SER A 123 11359 5367 3764 -95 -253 -81 N ATOM 770 CA SER A 123 98.996 -0.537 54.308 1.00 53.21 C ANISOU 770 CA SER A 123 11122 5443 3652 -162 -335 -108 C ATOM 771 C SER A 123 97.826 0.385 54.686 1.00 55.27 C ANISOU 771 C SER A 123 11428 5649 3924 -352 -282 -128 C ATOM 772 O SER A 123 97.788 0.857 55.822 1.00 55.22 O ANISOU 772 O SER A 123 11460 5679 3843 -389 -322 -121 O ATOM 773 CB SER A 123 100.014 0.253 53.491 1.00 56.42 C ANISOU 773 CB SER A 123 11293 6028 4117 -189 -359 -180 C ATOM 774 OG SER A 123 99.452 0.739 52.283 1.00 64.18 O ANISOU 774 OG SER A 123 12259 6942 5185 -309 -268 -217 O ATOM 775 N VAL A 124 96.869 0.607 53.758 1.00 50.26 N ANISOU 775 N VAL A 124 10792 4942 3361 -447 -196 -158 N ATOM 776 CA VAL A 124 95.722 1.497 53.962 1.00 49.08 C ANISOU 776 CA VAL A 124 10655 4774 3218 -564 -143 -186 C ATOM 777 C VAL A 124 94.697 0.860 54.951 1.00 53.35 C ANISOU 777 C VAL A 124 11333 5236 3702 -607 -88 -163 C ATOM 778 O VAL A 124 93.955 1.606 55.596 1.00 52.96 O ANISOU 778 O VAL A 124 11293 5203 3627 -673 -52 -183 O ATOM 779 CB VAL A 124 95.052 1.886 52.614 1.00 51.99 C ANISOU 779 CB VAL A 124 10961 5141 3652 -598 -93 -228 C ATOM 780 CG1 VAL A 124 94.214 0.749 52.025 1.00 51.84 C ANISOU 780 CG1 VAL A 124 10984 5066 3649 -620 -41 -240 C ATOM 781 CG2 VAL A 124 94.230 3.167 52.746 1.00 51.43 C ANISOU 781 CG2 VAL A 124 10883 5092 3567 -638 -62 -256 C ATOM 782 N TRP A 125 94.666 -0.481 55.085 1.00 50.46 N ANISOU 782 N TRP A 125 11103 4771 3300 -575 -57 -127 N ATOM 783 CA TRP A 125 93.726 -1.121 56.006 1.00 51.09 C ANISOU 783 CA TRP A 125 11354 4754 3302 -661 34 -114 C ATOM 784 C TRP A 125 94.383 -1.390 57.376 1.00 54.79 C ANISOU 784 C TRP A 125 11988 5183 3646 -572 -19 -40 C ATOM 785 O TRP A 125 93.657 -1.567 58.358 1.00 54.72 O ANISOU 785 O TRP A 125 12130 5109 3552 -658 59 -29 O ATOM 786 CB TRP A 125 93.135 -2.401 55.414 1.00 50.85 C ANISOU 786 CB TRP A 125 11455 4599 3265 -734 140 -132 C ATOM 787 CG TRP A 125 91.975 -2.093 54.517 1.00 51.52 C ANISOU 787 CG TRP A 125 11385 4770 3421 -885 205 -229 C ATOM 788 CD1 TRP A 125 92.011 -1.910 53.166 1.00 53.82 C ANISOU 788 CD1 TRP A 125 11536 5127 3788 -871 173 -276 C ATOM 789 CD2 TRP A 125 90.641 -1.765 54.931 1.00 51.86 C ANISOU 789 CD2 TRP A 125 11359 4896 3450 -1041 296 -300 C ATOM 790 NE1 TRP A 125 90.766 -1.554 52.703 1.00 53.46 N ANISOU 790 NE1 TRP A 125 11346 5207 3761 -991 217 -367 N ATOM 791 CE2 TRP A 125 89.904 -1.459 53.765 1.00 55.69 C ANISOU 791 CE2 TRP A 125 11644 5520 3997 -1093 296 -390 C ATOM 792 CE3 TRP A 125 89.985 -1.731 56.175 1.00 53.98 C ANISOU 792 CE3 TRP A 125 11712 5154 3645 -1135 385 -304 C ATOM 793 CZ2 TRP A 125 88.544 -1.125 53.804 1.00 55.79 C ANISOU 793 CZ2 TRP A 125 11496 5699 4002 -1210 365 -491 C ATOM 794 CZ3 TRP A 125 88.639 -1.401 56.212 1.00 56.11 C ANISOU 794 CZ3 TRP A 125 11829 5569 3920 -1276 483 -408 C ATOM 795 CH2 TRP A 125 87.931 -1.106 55.038 1.00 56.69 C ANISOU 795 CH2 TRP A 125 11662 5817 4058 -1302 466 -504 C ATOM 796 N ILE A 126 95.733 -1.357 57.457 1.00 50.96 N ANISOU 796 N ILE A 126 11455 4772 3135 -403 -151 -1 N ATOM 797 CA ILE A 126 96.464 -1.498 58.723 1.00 51.69 C ANISOU 797 CA ILE A 126 11661 4897 3083 -282 -247 60 C ATOM 798 C ILE A 126 96.234 -0.195 59.507 1.00 54.06 C ANISOU 798 C ILE A 126 11879 5301 3360 -407 -273 15 C ATOM 799 O ILE A 126 95.951 -0.244 60.705 1.00 54.61 O ANISOU 799 O ILE A 126 12116 5332 3302 -427 -264 47 O ATOM 800 CB ILE A 126 97.968 -1.851 58.502 1.00 55.79 C ANISOU 800 CB ILE A 126 12085 5542 3572 -45 -393 87 C ATOM 801 CG1 ILE A 126 98.107 -3.342 58.105 1.00 57.23 C ANISOU 801 CG1 ILE A 126 12483 5551 3712 135 -342 154 C ATOM 802 CG2 ILE A 126 98.814 -1.560 59.759 1.00 58.11 C ANISOU 802 CG2 ILE A 126 12377 5991 3711 67 -546 112 C ATOM 803 CD1 ILE A 126 99.442 -3.752 57.461 1.00 64.82 C ANISOU 803 CD1 ILE A 126 13307 6638 4683 397 -442 160 C ATOM 804 N LEU A 127 96.264 0.952 58.797 1.00 48.58 N ANISOU 804 N LEU A 127 10979 4705 2773 -499 -277 -58 N ATOM 805 CA LEU A 127 96.002 2.281 59.354 1.00 47.82 C ANISOU 805 CA LEU A 127 10850 4665 2656 -619 -266 -112 C ATOM 806 C LEU A 127 94.539 2.393 59.801 1.00 51.47 C ANISOU 806 C LEU A 127 11423 5025 3108 -712 -127 -122 C ATOM 807 O LEU A 127 94.262 3.054 60.802 1.00 51.61 O ANISOU 807 O LEU A 127 11522 5047 3042 -770 -103 -139 O ATOM 808 CB LEU A 127 96.337 3.388 58.333 1.00 46.86 C ANISOU 808 CB LEU A 127 10562 4612 2629 -682 -265 -181 C ATOM 809 CG LEU A 127 97.792 3.489 57.842 1.00 51.83 C ANISOU 809 CG LEU A 127 11034 5389 3270 -649 -368 -209 C ATOM 810 CD1 LEU A 127 97.892 4.375 56.630 1.00 50.94 C ANISOU 810 CD1 LEU A 127 10826 5281 3249 -733 -308 -267 C ATOM 811 CD2 LEU A 127 98.737 3.969 58.934 1.00 55.77 C ANISOU 811 CD2 LEU A 127 11504 6042 3643 -689 -478 -246 C ATOM 812 N ALA A 128 93.613 1.726 59.073 1.00 47.70 N ANISOU 812 N ALA A 128 10937 4481 2704 -737 -27 -126 N ATOM 813 CA ALA A 128 92.182 1.674 59.395 1.00 47.89 C ANISOU 813 CA ALA A 128 11003 4473 2721 -840 118 -162 C ATOM 814 C ALA A 128 91.948 0.888 60.691 1.00 53.75 C ANISOU 814 C ALA A 128 11974 5124 3324 -885 180 -118 C ATOM 815 O ALA A 128 91.107 1.281 61.501 1.00 54.15 O ANISOU 815 O ALA A 128 12075 5179 3319 -970 284 -152 O ATOM 816 CB ALA A 128 91.405 1.046 58.249 1.00 48.31 C ANISOU 816 CB ALA A 128 10963 4529 2863 -887 189 -203 C ATOM 817 N PHE A 129 92.720 -0.205 60.891 1.00 50.88 N ANISOU 817 N PHE A 129 11774 4671 2887 -803 125 -40 N ATOM 818 CA PHE A 129 92.679 -1.057 62.079 1.00 52.00 C ANISOU 818 CA PHE A 129 12215 4686 2856 -801 174 28 C ATOM 819 C PHE A 129 93.347 -0.356 63.263 1.00 55.58 C ANISOU 819 C PHE A 129 12731 5209 3180 -734 61 56 C ATOM 820 O PHE A 129 92.959 -0.608 64.405 1.00 56.57 O ANISOU 820 O PHE A 129 13090 5254 3150 -781 134 87 O ATOM 821 CB PHE A 129 93.341 -2.409 61.792 1.00 54.96 C ANISOU 821 CB PHE A 129 12784 4926 3173 -668 146 109 C ATOM 822 CG PHE A 129 92.371 -3.495 61.386 1.00 57.45 C ANISOU 822 CG PHE A 129 13271 5072 3487 -823 343 88 C ATOM 823 CD1 PHE A 129 91.681 -3.423 60.180 1.00 59.43 C ANISOU 823 CD1 PHE A 129 13310 5380 3892 -956 413 -7 C ATOM 824 CD2 PHE A 129 92.179 -4.613 62.188 1.00 62.12 C ANISOU 824 CD2 PHE A 129 14263 5442 3896 -845 463 155 C ATOM 825 CE1 PHE A 129 90.780 -4.424 59.809 1.00 61.57 C ANISOU 825 CE1 PHE A 129 13723 5528 4143 -1154 598 -58 C ATOM 826 CE2 PHE A 129 91.289 -5.624 61.809 1.00 66.19 C ANISOU 826 CE2 PHE A 129 14972 5787 4392 -1053 678 112 C ATOM 827 CZ PHE A 129 90.597 -5.523 60.621 1.00 63.17 C ANISOU 827 CZ PHE A 129 14331 5499 4172 -1224 741 -6 C ATOM 828 N ILE A 130 94.325 0.542 62.990 1.00 50.86 N ANISOU 828 N ILE A 130 11934 4763 2627 -659 -100 31 N ATOM 829 CA ILE A 130 95.001 1.365 64.003 1.00 51.26 C ANISOU 829 CA ILE A 130 12000 4923 2552 -648 -215 19 C ATOM 830 C ILE A 130 93.965 2.367 64.542 1.00 54.59 C ANISOU 830 C ILE A 130 12451 5322 2970 -808 -79 -49 C ATOM 831 O ILE A 130 93.882 2.566 65.757 1.00 55.29 O ANISOU 831 O ILE A 130 12713 5396 2897 -843 -70 -43 O ATOM 832 CB ILE A 130 96.283 2.051 63.433 1.00 53.93 C ANISOU 832 CB ILE A 130 12098 5451 2944 -595 -386 -27 C ATOM 833 CG1 ILE A 130 97.411 1.016 63.256 1.00 55.71 C ANISOU 833 CG1 ILE A 130 12303 5748 3116 -380 -534 39 C ATOM 834 CG2 ILE A 130 96.766 3.191 64.334 1.00 55.11 C ANISOU 834 CG2 ILE A 130 12234 5727 2979 -689 -465 -93 C ATOM 835 CD1 ILE A 130 98.649 1.481 62.452 1.00 64.37 C ANISOU 835 CD1 ILE A 130 13103 7066 4290 -334 -667 -24 C ATOM 836 N SER A 131 93.144 2.943 63.632 1.00 49.71 N ANISOU 836 N SER A 131 11677 4701 2509 -876 30 -113 N ATOM 837 CA SER A 131 92.065 3.882 63.949 1.00 49.51 C ANISOU 837 CA SER A 131 11652 4669 2493 -961 175 -182 C ATOM 838 C SER A 131 90.995 3.204 64.807 1.00 54.51 C ANISOU 838 C SER A 131 12443 5230 3038 -1037 340 -175 C ATOM 839 O SER A 131 90.484 3.828 65.737 1.00 55.44 O ANISOU 839 O SER A 131 12658 5342 3063 -1090 433 -213 O ATOM 840 CB SER A 131 91.437 4.438 62.674 1.00 52.24 C ANISOU 840 CB SER A 131 11797 5051 3002 -944 233 -238 C ATOM 841 OG SER A 131 92.390 5.087 61.847 1.00 60.81 O ANISOU 841 OG SER A 131 12778 6176 4151 -902 119 -247 O ATOM 842 N LEU A 132 90.677 1.924 64.508 1.00 50.54 N ANISOU 842 N LEU A 132 11995 4660 2547 -1064 399 -136 N ATOM 843 CA LEU A 132 89.697 1.134 65.259 1.00 51.49 C ANISOU 843 CA LEU A 132 12298 4696 2568 -1195 591 -139 C ATOM 844 C LEU A 132 90.229 0.789 66.653 1.00 56.84 C ANISOU 844 C LEU A 132 13298 5276 3023 -1175 563 -60 C ATOM 845 O LEU A 132 89.447 0.751 67.606 1.00 57.73 O ANISOU 845 O LEU A 132 13575 5341 3017 -1292 731 -83 O ATOM 846 CB LEU A 132 89.327 -0.151 64.502 1.00 51.78 C ANISOU 846 CB LEU A 132 12363 4658 2654 -1268 674 -131 C ATOM 847 CG LEU A 132 88.503 0.006 63.220 1.00 55.45 C ANISOU 847 CG LEU A 132 12528 5244 3295 -1333 734 -231 C ATOM 848 CD1 LEU A 132 88.569 -1.250 62.376 1.00 55.87 C ANISOU 848 CD1 LEU A 132 12640 5206 3380 -1391 757 -217 C ATOM 849 CD2 LEU A 132 87.056 0.384 63.518 1.00 58.74 C ANISOU 849 CD2 LEU A 132 12816 5786 3718 -1482 935 -349 C ATOM 850 N ASP A 133 91.557 0.552 66.766 1.00 53.51 N ANISOU 850 N ASP A 133 12953 4851 2528 -1015 350 24 N ATOM 851 CA ASP A 133 92.251 0.231 68.022 1.00 55.08 C ANISOU 851 CA ASP A 133 13441 5003 2485 -931 258 106 C ATOM 852 C ASP A 133 92.206 1.427 68.979 1.00 57.80 C ANISOU 852 C ASP A 133 13796 5432 2734 -994 246 47 C ATOM 853 O ASP A 133 91.991 1.233 70.176 1.00 58.74 O ANISOU 853 O ASP A 133 14196 5480 2644 -1031 309 78 O ATOM 854 CB ASP A 133 93.715 -0.190 67.749 1.00 57.54 C ANISOU 854 CB ASP A 133 13726 5382 2754 -703 4 183 C ATOM 855 CG ASP A 133 94.575 -0.497 68.973 1.00 70.71 C ANISOU 855 CG ASP A 133 15647 7073 4148 -548 -152 265 C ATOM 856 OD1 ASP A 133 94.022 -0.982 69.988 1.00 73.02 O ANISOU 856 OD1 ASP A 133 16284 7216 4246 -592 -31 318 O ATOM 857 OD2 ASP A 133 95.808 -0.309 68.894 1.00 77.42 O ANISOU 857 OD2 ASP A 133 16351 8106 4961 -379 -394 273 O ATOM 858 N ARG A 134 92.399 2.653 68.451 1.00 52.24 N ANISOU 858 N ARG A 134 12835 4852 2161 -1016 186 -41 N ATOM 859 CA ARG A 134 92.368 3.877 69.253 1.00 52.25 C ANISOU 859 CA ARG A 134 12877 4904 2071 -1090 196 -115 C ATOM 860 C ARG A 134 90.941 4.176 69.711 1.00 55.92 C ANISOU 860 C ARG A 134 13420 5295 2532 -1201 459 -173 C ATOM 861 O ARG A 134 90.766 4.669 70.823 1.00 56.80 O ANISOU 861 O ARG A 134 13719 5385 2477 -1258 519 -202 O ATOM 862 CB ARG A 134 92.955 5.081 68.489 1.00 50.97 C ANISOU 862 CB ARG A 134 12488 4847 2033 -1098 99 -196 C ATOM 863 CG ARG A 134 94.447 4.987 68.105 1.00 60.51 C ANISOU 863 CG ARG A 134 13566 6192 3232 -1029 -147 -180 C ATOM 864 CD ARG A 134 95.414 4.897 69.280 1.00 71.21 C ANISOU 864 CD ARG A 134 15056 7657 4342 -1007 -325 -167 C ATOM 865 NE ARG A 134 95.535 3.528 69.784 1.00 80.07 N ANISOU 865 NE ARG A 134 16356 8733 5333 -854 -379 -44 N ATOM 866 CZ ARG A 134 96.161 3.187 70.906 1.00 95.86 C ANISOU 866 CZ ARG A 134 18544 10803 7076 -772 -523 0 C ATOM 867 NH1 ARG A 134 96.716 4.117 71.674 1.00 84.90 N ANISOU 867 NH1 ARG A 134 17157 9566 5536 -866 -634 -87 N ATOM 868 NH2 ARG A 134 96.222 1.917 71.279 1.00 83.94 N ANISOU 868 NH2 ARG A 134 17259 9204 5431 -596 -550 128 N ATOM 869 N TYR A 135 89.929 3.845 68.878 1.00 51.14 N ANISOU 869 N TYR A 135 12661 4680 2091 -1232 617 -202 N ATOM 870 CA TYR A 135 88.511 4.026 69.201 1.00 51.50 C ANISOU 870 CA TYR A 135 12697 4726 2143 -1329 876 -279 C ATOM 871 C TYR A 135 88.126 3.164 70.419 1.00 57.86 C ANISOU 871 C TYR A 135 13811 5430 2744 -1441 1019 -240 C ATOM 872 O TYR A 135 87.411 3.643 71.295 1.00 58.74 O ANISOU 872 O TYR A 135 14023 5542 2755 -1515 1192 -301 O ATOM 873 CB TYR A 135 87.623 3.694 67.978 1.00 51.50 C ANISOU 873 CB TYR A 135 12423 4803 2343 -1346 974 -331 C ATOM 874 CG TYR A 135 86.260 3.126 68.321 1.00 54.51 C ANISOU 874 CG TYR A 135 12797 5216 2697 -1499 1240 -401 C ATOM 875 CD1 TYR A 135 85.244 3.942 68.809 1.00 57.35 C ANISOU 875 CD1 TYR A 135 13076 5675 3038 -1514 1426 -508 C ATOM 876 CD2 TYR A 135 85.984 1.773 68.148 1.00 56.10 C ANISOU 876 CD2 TYR A 135 13081 5355 2881 -1642 1328 -377 C ATOM 877 CE1 TYR A 135 83.998 3.418 69.153 1.00 59.79 C ANISOU 877 CE1 TYR A 135 13335 6068 3316 -1681 1689 -598 C ATOM 878 CE2 TYR A 135 84.740 1.239 68.482 1.00 58.86 C ANISOU 878 CE2 TYR A 135 13423 5753 3189 -1852 1601 -469 C ATOM 879 CZ TYR A 135 83.747 2.068 68.977 1.00 66.24 C ANISOU 879 CZ TYR A 135 14218 6836 4113 -1877 1779 -586 C ATOM 880 OH TYR A 135 82.516 1.548 69.296 1.00 67.91 O ANISOU 880 OH TYR A 135 14371 7150 4283 -2106 2065 -703 O ATOM 881 N LEU A 136 88.592 1.908 70.467 1.00 55.46 N ANISOU 881 N LEU A 136 13692 5020 2360 -1441 966 -139 N ATOM 882 CA LEU A 136 88.286 0.990 71.566 1.00 57.94 C ANISOU 882 CA LEU A 136 14382 5187 2445 -1540 1113 -82 C ATOM 883 C LEU A 136 89.048 1.370 72.844 1.00 64.00 C ANISOU 883 C LEU A 136 15430 5924 2962 -1467 990 -27 C ATOM 884 O LEU A 136 88.509 1.219 73.941 1.00 65.37 O ANISOU 884 O LEU A 136 15886 6014 2938 -1573 1164 -28 O ATOM 885 CB LEU A 136 88.623 -0.458 71.165 1.00 58.58 C ANISOU 885 CB LEU A 136 14647 5120 2490 -1521 1094 20 C ATOM 886 CG LEU A 136 87.802 -1.077 70.027 1.00 62.48 C ANISOU 886 CG LEU A 136 14948 5619 3173 -1658 1247 -45 C ATOM 887 CD1 LEU A 136 88.512 -2.271 69.439 1.00 62.93 C ANISOU 887 CD1 LEU A 136 15174 5525 3212 -1567 1155 59 C ATOM 888 CD2 LEU A 136 86.392 -1.451 70.482 1.00 66.41 C ANISOU 888 CD2 LEU A 136 15523 6095 3614 -1942 1592 -143 C ATOM 889 N ALA A 137 90.284 1.881 72.695 1.00 60.44 N ANISOU 889 N ALA A 137 14890 5567 2509 -1309 700 4 N ATOM 890 CA ALA A 137 91.161 2.272 73.799 1.00 61.88 C ANISOU 890 CA ALA A 137 15278 5788 2445 -1242 528 34 C ATOM 891 C ALA A 137 90.752 3.605 74.444 1.00 66.42 C ANISOU 891 C ALA A 137 15842 6418 2978 -1353 617 -84 C ATOM 892 O ALA A 137 91.138 3.852 75.587 1.00 68.21 O ANISOU 892 O ALA A 137 16317 6647 2952 -1363 555 -78 O ATOM 893 CB ALA A 137 92.594 2.377 73.303 1.00 62.03 C ANISOU 893 CB ALA A 137 15128 5953 2489 -1073 201 67 C ATOM 894 N ILE A 138 90.005 4.467 73.724 1.00 61.47 N ANISOU 894 N ILE A 138 14955 5831 2570 -1410 755 -191 N ATOM 895 CA ILE A 138 89.619 5.785 74.233 1.00 61.67 C ANISOU 895 CA ILE A 138 14999 5878 2556 -1471 858 -305 C ATOM 896 C ILE A 138 88.107 5.817 74.571 1.00 67.14 C ANISOU 896 C ILE A 138 15722 6526 3264 -1555 1197 -372 C ATOM 897 O ILE A 138 87.764 6.227 75.682 1.00 68.37 O ANISOU 897 O ILE A 138 16109 6637 3230 -1621 1329 -416 O ATOM 898 CB ILE A 138 90.022 6.911 73.213 1.00 62.80 C ANISOU 898 CB ILE A 138 14875 6096 2891 -1423 758 -379 C ATOM 899 CG1 ILE A 138 91.492 7.375 73.416 1.00 63.37 C ANISOU 899 CG1 ILE A 138 14978 6249 2851 -1430 482 -384 C ATOM 900 CG2 ILE A 138 89.102 8.136 73.271 1.00 63.55 C ANISOU 900 CG2 ILE A 138 14955 6162 3029 -1434 971 -497 C ATOM 901 CD1 ILE A 138 92.624 6.449 72.932 1.00 70.04 C ANISOU 901 CD1 ILE A 138 15710 7190 3713 -1339 223 -291 C ATOM 902 N VAL A 139 87.223 5.403 73.638 1.00 63.56 N ANISOU 902 N VAL A 139 15021 6112 3017 -1560 1336 -397 N ATOM 903 CA VAL A 139 85.767 5.473 73.826 1.00 64.99 C ANISOU 903 CA VAL A 139 15126 6338 3230 -1639 1653 -496 C ATOM 904 C VAL A 139 85.288 4.364 74.793 1.00 72.77 C ANISOU 904 C VAL A 139 16394 7233 4023 -1811 1845 -460 C ATOM 905 O VAL A 139 84.485 4.658 75.686 1.00 74.04 O ANISOU 905 O VAL A 139 16675 7396 4061 -1900 2088 -536 O ATOM 906 CB VAL A 139 85.002 5.409 72.471 1.00 67.43 C ANISOU 906 CB VAL A 139 15036 6783 3800 -1596 1713 -557 C ATOM 907 CG1 VAL A 139 83.491 5.535 72.664 1.00 68.90 C ANISOU 907 CG1 VAL A 139 15066 7104 4010 -1662 2028 -689 C ATOM 908 CG2 VAL A 139 85.499 6.488 71.514 1.00 65.39 C ANISOU 908 CG2 VAL A 139 14575 6575 3696 -1417 1538 -576 C ATOM 909 N HIS A 140 85.770 3.117 74.630 1.00 71.01 N ANISOU 909 N HIS A 140 16313 6911 3755 -1852 1760 -348 N ATOM 910 CA HIS A 140 85.319 2.003 75.467 1.00 74.10 C ANISOU 910 CA HIS A 140 17049 7165 3942 -2026 1968 -304 C ATOM 911 C HIS A 140 86.477 1.409 76.295 1.00 81.24 C ANISOU 911 C HIS A 140 18386 7902 4578 -1937 1769 -146 C ATOM 912 O HIS A 140 86.573 0.190 76.433 1.00 82.67 O ANISOU 912 O HIS A 140 18853 7923 4633 -1982 1817 -47 O ATOM 913 CB HIS A 140 84.678 0.923 74.582 1.00 74.95 C ANISOU 913 CB HIS A 140 17028 7268 4184 -2167 2110 -322 C ATOM 914 CG HIS A 140 83.593 1.452 73.701 1.00 77.69 C ANISOU 914 CG HIS A 140 16904 7842 4774 -2222 2257 -483 C ATOM 915 ND1 HIS A 140 82.310 1.644 74.175 1.00 81.54 N ANISOU 915 ND1 HIS A 140 17296 8454 5233 -2393 2582 -628 N ATOM 916 CD2 HIS A 140 83.646 1.839 72.406 1.00 77.35 C ANISOU 916 CD2 HIS A 140 16466 7945 4979 -2101 2110 -522 C ATOM 917 CE1 HIS A 140 81.621 2.129 73.155 1.00 80.15 C ANISOU 917 CE1 HIS A 140 16649 8520 5286 -2343 2603 -750 C ATOM 918 NE2 HIS A 140 82.383 2.263 72.070 1.00 77.94 N ANISOU 918 NE2 HIS A 140 16199 8245 5170 -2169 2322 -685 N ATOM 919 N ALA A 141 87.308 2.280 76.896 1.00 78.79 N ANISOU 919 N ALA A 141 18151 7635 4150 -1813 1562 -133 N ATOM 920 CA ALA A 141 88.482 1.926 77.704 1.00 80.54 C ANISOU 920 CA ALA A 141 18711 7792 4097 -1687 1315 -8 C ATOM 921 C ALA A 141 88.148 1.076 78.950 1.00 89.21 C ANISOU 921 C ALA A 141 20330 8705 4860 -1774 1495 70 C ATOM 922 O ALA A 141 89.026 0.341 79.410 1.00 90.46 O ANISOU 922 O ALA A 141 20807 8778 4784 -1625 1305 211 O ATOM 923 CB ALA A 141 89.186 3.192 78.155 1.00 81.04 C ANISOU 923 CB ALA A 141 18716 7984 4092 -1625 1120 -70 C ATOM 924 N THR A 142 86.905 1.185 79.492 1.00 88.13 N ANISOU 924 N THR A 142 20286 8519 4682 -1994 1862 -23 N ATOM 925 CA THR A 142 86.409 0.502 80.706 1.00 91.55 C ANISOU 925 CA THR A 142 21227 8768 4788 -2139 2113 23 C ATOM 926 C THR A 142 86.822 -0.993 80.725 1.00 96.76 C ANISOU 926 C THR A 142 22287 9204 5272 -2091 2086 195 C ATOM 927 O THR A 142 87.356 -1.458 81.735 1.00 98.94 O ANISOU 927 O THR A 142 23061 9337 5195 -1999 2015 319 O ATOM 928 CB THR A 142 84.872 0.642 80.817 1.00102.11 C ANISOU 928 CB THR A 142 22453 10133 6209 -2417 2561 -132 C ATOM 929 OG1 THR A 142 84.495 2.005 80.606 1.00101.30 O ANISOU 929 OG1 THR A 142 21964 10233 6294 -2383 2577 -284 O ATOM 930 CG2 THR A 142 84.326 0.159 82.163 1.00103.94 C ANISOU 930 CG2 THR A 142 23209 10193 6090 -2604 2862 -115 C ATOM 931 N ASN A 143 86.584 -1.721 79.611 1.00 91.55 N ANISOU 931 N ASN A 143 21441 8509 4837 -2135 2140 199 N ATOM 932 CA ASN A 143 86.930 -3.136 79.437 1.00 92.62 C ANISOU 932 CA ASN A 143 21958 8398 4836 -2085 2145 348 C ATOM 933 C ASN A 143 87.068 -3.430 77.938 1.00 92.98 C ANISOU 933 C ASN A 143 21607 8510 5210 -2037 2043 326 C ATOM 934 O ASN A 143 86.137 -3.941 77.306 1.00 92.63 O ANISOU 934 O ASN A 143 21459 8426 5312 -2290 2314 239 O ATOM 935 CB ASN A 143 85.892 -4.047 80.108 1.00 97.12 C ANISOU 935 CB ASN A 143 22992 8723 5189 -2400 2586 340 C ATOM 936 N SER A 144 88.233 -3.067 77.366 1.00 86.66 N ANISOU 936 N SER A 144 20567 7842 4519 -1734 1655 387 N ATOM 937 CA SER A 144 88.513 -3.220 75.938 1.00 83.48 C ANISOU 937 CA SER A 144 19779 7520 4418 -1654 1524 368 C ATOM 938 C SER A 144 89.764 -4.066 75.655 1.00 86.71 C ANISOU 938 C SER A 144 20391 7829 4724 -1333 1251 533 C ATOM 939 O SER A 144 90.150 -4.174 74.490 1.00 84.48 O ANISOU 939 O SER A 144 19804 7619 4675 -1234 1121 523 O ATOM 940 CB SER A 144 88.691 -1.851 75.288 1.00 83.83 C ANISOU 940 CB SER A 144 19259 7854 4738 -1600 1346 252 C ATOM 941 OG SER A 144 89.761 -1.128 75.874 1.00 92.58 O ANISOU 941 OG SER A 144 20375 9080 5720 -1394 1051 293 O ATOM 942 N GLN A 145 90.372 -4.690 76.684 1.00 85.11 N ANISOU 942 N GLN A 145 20709 7467 4164 -1147 1173 683 N ATOM 943 CA GLN A 145 91.575 -5.510 76.504 1.00 85.69 C ANISOU 943 CA GLN A 145 20992 7469 4097 -765 906 845 C ATOM 944 C GLN A 145 91.281 -6.745 75.621 1.00 88.07 C ANISOU 944 C GLN A 145 21488 7504 4470 -800 1091 892 C ATOM 945 O GLN A 145 92.160 -7.164 74.868 1.00 87.27 O ANISOU 945 O GLN A 145 21296 7425 4438 -512 879 961 O ATOM 946 CB GLN A 145 92.157 -5.945 77.861 1.00 91.02 C ANISOU 946 CB GLN A 145 22234 8026 4323 -533 802 999 C ATOM 947 CG GLN A 145 93.638 -6.340 77.811 1.00112.23 C ANISOU 947 CG GLN A 145 24968 10818 6856 -32 403 1137 C ATOM 948 CD GLN A 145 94.553 -5.155 77.598 1.00132.53 C ANISOU 948 CD GLN A 145 26955 13824 9575 96 38 1043 C ATOM 949 OE1 GLN A 145 94.877 -4.414 78.533 1.00130.88 O ANISOU 949 OE1 GLN A 145 26745 13801 9183 111 -116 1013 O ATOM 950 NE2 GLN A 145 95.005 -4.959 76.367 1.00120.81 N ANISOU 950 NE2 GLN A 145 24990 12507 8407 165 -93 984 N ATOM 951 N ARG A 146 90.045 -7.293 75.690 1.00 84.00 N ANISOU 951 N ARG A 146 21220 6760 3937 -1176 1497 834 N ATOM 952 CA ARG A 146 89.614 -8.445 74.893 1.00 83.78 C ANISOU 952 CA ARG A 146 21410 6466 3956 -1315 1729 839 C ATOM 953 C ARG A 146 89.368 -8.016 73.415 1.00 82.43 C ANISOU 953 C ARG A 146 20599 6517 4205 -1432 1686 692 C ATOM 954 O ARG A 146 90.051 -8.584 72.561 1.00 81.46 O ANISOU 954 O ARG A 146 20467 6330 4153 -1216 1548 753 O ATOM 955 CB ARG A 146 88.363 -9.120 75.499 1.00 86.00 C ANISOU 955 CB ARG A 146 22149 6471 4058 -1750 2197 789 C ATOM 956 CG ARG A 146 87.885 -10.354 74.737 1.00 94.68 C ANISOU 956 CG ARG A 146 23542 7270 5163 -1968 2475 771 C ATOM 957 CD ARG A 146 86.579 -10.890 75.282 1.00102.77 C ANISOU 957 CD ARG A 146 24927 8089 6034 -2494 2968 669 C ATOM 958 NE ARG A 146 86.105 -12.045 74.518 1.00110.67 N ANISOU 958 NE ARG A 146 26206 8811 7031 -2772 3251 619 N ATOM 959 CZ ARG A 146 85.236 -11.979 73.514 1.00123.51 C ANISOU 959 CZ ARG A 146 27371 10618 8939 -3156 3416 404 C ATOM 960 NH1 ARG A 146 84.726 -10.812 73.142 1.00108.64 N ANISOU 960 NH1 ARG A 146 24732 9188 7361 -3260 3325 236 N ATOM 961 NH2 ARG A 146 84.864 -13.083 72.879 1.00111.78 N ANISOU 961 NH2 ARG A 146 26202 8861 7406 -3431 3676 352 N ATOM 962 N PRO A 147 88.468 -7.042 73.063 1.00 75.65 N ANISOU 962 N PRO A 147 19221 5919 3605 -1718 1787 507 N ATOM 963 CA PRO A 147 88.280 -6.698 71.638 1.00 72.10 C ANISOU 963 CA PRO A 147 18222 5668 3507 -1779 1726 387 C ATOM 964 C PRO A 147 89.550 -6.181 70.954 1.00 72.32 C ANISOU 964 C PRO A 147 17928 5869 3679 -1405 1337 449 C ATOM 965 O PRO A 147 89.725 -6.470 69.772 1.00 70.33 O ANISOU 965 O PRO A 147 17469 5638 3616 -1370 1285 422 O ATOM 966 CB PRO A 147 87.217 -5.598 71.672 1.00 72.52 C ANISOU 966 CB PRO A 147 17833 5988 3732 -2038 1860 208 C ATOM 967 CG PRO A 147 86.487 -5.818 72.936 1.00 79.93 C ANISOU 967 CG PRO A 147 19153 6796 4422 -2260 2139 199 C ATOM 968 CD PRO A 147 87.540 -6.257 73.905 1.00 77.40 C ANISOU 968 CD PRO A 147 19354 6262 3792 -1975 1978 397 C ATOM 969 N ARG A 148 90.431 -5.445 71.680 1.00 67.94 N ANISOU 969 N ARG A 148 17337 5451 3024 -1155 1080 514 N ATOM 970 CA ARG A 148 91.692 -4.918 71.135 1.00 65.67 C ANISOU 970 CA ARG A 148 16733 5371 2846 -841 724 548 C ATOM 971 C ARG A 148 92.688 -6.043 70.823 1.00 71.05 C ANISOU 971 C ARG A 148 17680 5905 3411 -522 588 689 C ATOM 972 O ARG A 148 93.433 -5.926 69.847 1.00 69.35 O ANISOU 972 O ARG A 148 17151 5829 3371 -346 402 679 O ATOM 973 CB ARG A 148 92.346 -3.908 72.083 1.00 64.90 C ANISOU 973 CB ARG A 148 16559 5473 2626 -715 507 554 C ATOM 974 CG ARG A 148 91.725 -2.516 72.027 1.00 72.43 C ANISOU 974 CG ARG A 148 17130 6628 3762 -927 557 402 C ATOM 975 CD ARG A 148 92.347 -1.569 73.040 1.00 83.60 C ANISOU 975 CD ARG A 148 18549 8198 5015 -850 376 394 C ATOM 976 NE ARG A 148 93.754 -1.275 72.753 1.00 92.90 N ANISOU 976 NE ARG A 148 19521 9580 6196 -603 35 420 N ATOM 977 CZ ARG A 148 94.589 -0.691 73.609 1.00110.55 C ANISOU 977 CZ ARG A 148 21777 11987 8241 -505 -183 417 C ATOM 978 NH1 ARG A 148 95.849 -0.465 73.264 1.00 98.40 N ANISOU 978 NH1 ARG A 148 19990 10685 6713 -314 -478 410 N ATOM 979 NH2 ARG A 148 94.174 -0.346 74.823 1.00100.02 N ANISOU 979 NH2 ARG A 148 20706 10610 6688 -612 -102 405 N ATOM 980 N LYS A 149 92.697 -7.123 71.639 1.00 70.34 N ANISOU 980 N LYS A 149 18193 5524 3012 -433 698 820 N ATOM 981 CA LYS A 149 93.574 -8.279 71.435 1.00 72.07 C ANISOU 981 CA LYS A 149 18765 5550 3068 -76 602 968 C ATOM 982 C LYS A 149 93.101 -9.087 70.229 1.00 75.02 C ANISOU 982 C LYS A 149 19165 5726 3613 -223 804 925 C ATOM 983 O LYS A 149 93.883 -9.290 69.302 1.00 73.46 O ANISOU 983 O LYS A 149 18773 5599 3541 23 640 942 O ATOM 984 CB LYS A 149 93.638 -9.163 72.690 1.00 78.59 C ANISOU 984 CB LYS A 149 20309 6078 3473 70 688 1128 C ATOM 985 N LEU A 150 91.809 -9.492 70.220 1.00 72.43 N ANISOU 985 N LEU A 150 19039 5189 3292 -652 1165 844 N ATOM 986 CA LEU A 150 91.141 -10.271 69.166 1.00 72.41 C ANISOU 986 CA LEU A 150 19090 5004 3419 -907 1406 762 C ATOM 987 C LEU A 150 91.335 -9.657 67.775 1.00 73.06 C ANISOU 987 C LEU A 150 18543 5362 3853 -896 1248 651 C ATOM 988 O LEU A 150 91.531 -10.394 66.808 1.00 72.83 O ANISOU 988 O LEU A 150 18584 5200 3889 -850 1284 649 O ATOM 989 CB LEU A 150 89.631 -10.374 69.464 1.00 73.47 C ANISOU 989 CB LEU A 150 19325 5050 3541 -1449 1788 625 C ATOM 990 CG LEU A 150 89.108 -11.632 70.184 1.00 82.70 C ANISOU 990 CG LEU A 150 21264 5775 4383 -1647 2136 688 C ATOM 991 CD1 LEU A 150 89.669 -11.772 71.600 1.00 85.54 C ANISOU 991 CD1 LEU A 150 22135 5973 4392 -1372 2069 870 C ATOM 992 CD2 LEU A 150 87.594 -11.613 70.258 1.00 86.03 C ANISOU 992 CD2 LEU A 150 21614 6221 4854 -2245 2516 493 C ATOM 993 N LEU A 151 91.302 -8.315 67.691 1.00 66.85 N ANISOU 993 N LEU A 151 17200 4933 3268 -930 1087 562 N ATOM 994 CA LEU A 151 91.448 -7.543 66.461 1.00 63.36 C ANISOU 994 CA LEU A 151 16179 4758 3135 -927 942 459 C ATOM 995 C LEU A 151 92.888 -7.600 65.922 1.00 66.75 C ANISOU 995 C LEU A 151 16496 5268 3598 -516 655 548 C ATOM 996 O LEU A 151 93.076 -7.851 64.732 1.00 65.38 O ANISOU 996 O LEU A 151 16148 5106 3586 -487 636 508 O ATOM 997 CB LEU A 151 91.040 -6.081 66.725 1.00 61.23 C ANISOU 997 CB LEU A 151 15473 4788 3003 -1048 877 359 C ATOM 998 CG LEU A 151 90.694 -5.219 65.513 1.00 63.24 C ANISOU 998 CG LEU A 151 15193 5283 3553 -1149 831 226 C ATOM 999 CD1 LEU A 151 89.314 -5.572 64.958 1.00 63.70 C ANISOU 999 CD1 LEU A 151 15184 5322 3698 -1499 1097 93 C ATOM 1000 CD2 LEU A 151 90.709 -3.751 65.881 1.00 64.24 C ANISOU 1000 CD2 LEU A 151 14996 5654 3757 -1132 715 172 C ATOM 1001 N ALA A 152 93.890 -7.367 66.789 1.00 64.53 N ANISOU 1001 N ALA A 152 16294 5073 3153 -207 434 652 N ATOM 1002 CA ALA A 152 95.310 -7.335 66.428 1.00 64.61 C ANISOU 1002 CA ALA A 152 16131 5249 3170 191 147 713 C ATOM 1003 C ALA A 152 95.933 -8.739 66.281 1.00 71.68 C ANISOU 1003 C ALA A 152 17462 5887 3888 516 160 843 C ATOM 1004 O ALA A 152 96.936 -8.882 65.575 1.00 70.89 O ANISOU 1004 O ALA A 152 17171 5911 3853 817 -11 862 O ATOM 1005 CB ALA A 152 96.084 -6.555 67.479 1.00 66.01 C ANISOU 1005 CB ALA A 152 16207 5668 3205 371 -95 747 C ATOM 1006 N GLU A 153 95.372 -9.755 66.958 1.00 71.66 N ANISOU 1006 N GLU A 153 18065 5519 3643 467 377 930 N ATOM 1007 CA GLU A 153 95.916 -11.116 66.934 1.00 75.07 C ANISOU 1007 CA GLU A 153 19037 5635 3852 801 423 1069 C ATOM 1008 C GLU A 153 95.256 -12.014 65.879 1.00 79.65 C ANISOU 1008 C GLU A 153 19826 5910 4527 576 700 1013 C ATOM 1009 O GLU A 153 95.936 -12.894 65.346 1.00 81.02 O ANISOU 1009 O GLU A 153 20243 5913 4630 896 685 1086 O ATOM 1010 CB GLU A 153 95.761 -11.789 68.309 1.00 80.16 C ANISOU 1010 CB GLU A 153 20349 5994 4115 900 521 1211 C ATOM 1011 CG GLU A 153 96.606 -11.175 69.417 1.00 92.25 C ANISOU 1011 CG GLU A 153 21797 7794 5458 1222 219 1293 C ATOM 1012 CD GLU A 153 96.286 -11.628 70.832 1.00119.47 C ANISOU 1012 CD GLU A 153 25875 10991 8526 1248 323 1417 C ATOM 1013 OE1 GLU A 153 95.667 -12.705 70.999 1.00119.97 O ANISOU 1013 OE1 GLU A 153 26585 10598 8400 1143 627 1488 O ATOM 1014 OE2 GLU A 153 96.668 -10.904 71.780 1.00113.58 O ANISOU 1014 OE2 GLU A 153 25005 10497 7651 1356 112 1436 O ATOM 1015 N LYS A 154 93.946 -11.830 65.598 1.00 75.07 N ANISOU 1015 N LYS A 154 19165 5275 4083 42 955 873 N ATOM 1016 CA LYS A 154 93.227 -12.718 64.681 1.00 75.55 C ANISOU 1016 CA LYS A 154 19448 5065 4194 -244 1233 792 C ATOM 1017 C LYS A 154 92.499 -11.984 63.533 1.00 75.94 C ANISOU 1017 C LYS A 154 18898 5379 4575 -608 1260 595 C ATOM 1018 O LYS A 154 92.709 -12.354 62.378 1.00 75.09 O ANISOU 1018 O LYS A 154 18702 5241 4588 -579 1263 547 O ATOM 1019 CB LYS A 154 92.195 -13.548 65.469 1.00 81.19 C ANISOU 1019 CB LYS A 154 20779 5405 4665 -594 1591 795 C ATOM 1020 CG LYS A 154 92.826 -14.598 66.392 1.00100.79 C ANISOU 1020 CG LYS A 154 24039 7494 6764 -234 1637 1001 C ATOM 1021 CD LYS A 154 91.870 -15.137 67.467 1.00114.14 C ANISOU 1021 CD LYS A 154 26330 8859 8179 -582 1972 1018 C ATOM 1022 CE LYS A 154 91.666 -14.210 68.651 1.00124.60 C ANISOU 1022 CE LYS A 154 27485 10414 9444 -628 1880 1036 C ATOM 1023 NZ LYS A 154 92.909 -14.029 69.453 1.00134.69 N ANISOU 1023 NZ LYS A 154 28873 11777 10527 -35 1548 1227 N ATOM 1024 N VAL A 155 91.640 -10.983 63.841 1.00 70.44 N ANISOU 1024 N VAL A 155 17828 4933 4002 -922 1286 484 N ATOM 1025 CA VAL A 155 90.797 -10.256 62.872 1.00 67.61 C ANISOU 1025 CA VAL A 155 16936 4840 3915 -1245 1319 300 C ATOM 1026 C VAL A 155 91.666 -9.502 61.818 1.00 69.33 C ANISOU 1026 C VAL A 155 16658 5323 4360 -986 1044 288 C ATOM 1027 O VAL A 155 91.194 -9.306 60.695 1.00 67.43 O ANISOU 1027 O VAL A 155 16114 5205 4301 -1166 1072 164 O ATOM 1028 CB VAL A 155 89.812 -9.278 63.583 1.00 70.40 C ANISOU 1028 CB VAL A 155 17019 5415 4314 -1521 1388 205 C ATOM 1029 CG1 VAL A 155 88.858 -8.608 62.593 1.00 68.24 C ANISOU 1029 CG1 VAL A 155 16227 5420 4280 -1805 1430 16 C ATOM 1030 CG2 VAL A 155 89.008 -9.993 64.665 1.00 73.23 C ANISOU 1030 CG2 VAL A 155 17865 5525 4433 -1789 1681 211 C ATOM 1031 N VAL A 156 92.922 -9.128 62.156 1.00 66.24 N ANISOU 1031 N VAL A 156 16197 5033 3939 -583 789 405 N ATOM 1032 CA VAL A 156 93.828 -8.407 61.249 1.00 64.25 C ANISOU 1032 CA VAL A 156 15497 5039 3877 -365 555 386 C ATOM 1033 C VAL A 156 94.155 -9.290 60.004 1.00 70.31 C ANISOU 1033 C VAL A 156 16348 5666 4699 -283 604 371 C ATOM 1034 O VAL A 156 94.189 -8.765 58.894 1.00 67.91 O ANISOU 1034 O VAL A 156 15671 5538 4593 -338 544 283 O ATOM 1035 CB VAL A 156 95.125 -7.916 61.964 1.00 68.24 C ANISOU 1035 CB VAL A 156 15913 5716 4301 9 291 487 C ATOM 1036 CG1 VAL A 156 95.998 -9.070 62.456 1.00 71.22 C ANISOU 1036 CG1 VAL A 156 16738 5884 4440 382 254 633 C ATOM 1037 CG2 VAL A 156 95.928 -6.957 61.087 1.00 65.72 C ANISOU 1037 CG2 VAL A 156 15081 5707 4184 121 90 427 C ATOM 1038 N TYR A 157 94.349 -10.608 60.185 1.00 70.96 N ANISOU 1038 N TYR A 157 16961 5411 4588 -158 732 455 N ATOM 1039 CA TYR A 157 94.672 -11.517 59.085 1.00 72.22 C ANISOU 1039 CA TYR A 157 17283 5392 4766 -65 807 441 C ATOM 1040 C TYR A 157 93.455 -11.759 58.189 1.00 77.14 C ANISOU 1040 C TYR A 157 17875 5945 5489 -530 1024 282 C ATOM 1041 O TYR A 157 93.582 -11.689 56.965 1.00 75.75 O ANISOU 1041 O TYR A 157 17463 5858 5460 -549 993 201 O ATOM 1042 CB TYR A 157 95.211 -12.855 59.618 1.00 77.14 C ANISOU 1042 CB TYR A 157 18563 5632 5114 233 902 583 C ATOM 1043 CG TYR A 157 96.500 -12.715 60.397 1.00 80.02 C ANISOU 1043 CG TYR A 157 18932 6119 5352 763 654 732 C ATOM 1044 CD1 TYR A 157 97.728 -12.646 59.746 1.00 81.94 C ANISOU 1044 CD1 TYR A 157 18917 6551 5666 1173 458 757 C ATOM 1045 CD2 TYR A 157 96.495 -12.669 61.788 1.00 82.33 C ANISOU 1045 CD2 TYR A 157 19476 6370 5436 852 616 836 C ATOM 1046 CE1 TYR A 157 98.919 -12.513 60.458 1.00 84.41 C ANISOU 1046 CE1 TYR A 157 19167 7056 5851 1657 214 866 C ATOM 1047 CE2 TYR A 157 97.679 -12.538 62.512 1.00 84.71 C ANISOU 1047 CE2 TYR A 157 19755 6839 5594 1343 360 958 C ATOM 1048 CZ TYR A 157 98.890 -12.463 61.842 1.00 92.16 C ANISOU 1048 CZ TYR A 157 20389 8015 6615 1746 152 967 C ATOM 1049 OH TYR A 157 100.063 -12.339 62.547 1.00 95.19 O ANISOU 1049 OH TYR A 157 20687 8636 6844 2228 -113 1060 O ATOM 1050 N VAL A 158 92.282 -12.014 58.804 1.00 75.58 N ANISOU 1050 N VAL A 158 17893 5624 5199 -914 1242 223 N ATOM 1051 CA VAL A 158 91.008 -12.306 58.134 1.00 75.96 C ANISOU 1051 CA VAL A 158 17907 5654 5298 -1409 1466 42 C ATOM 1052 C VAL A 158 90.491 -11.055 57.376 1.00 76.97 C ANISOU 1052 C VAL A 158 17360 6209 5678 -1562 1330 -93 C ATOM 1053 O VAL A 158 90.030 -11.184 56.240 1.00 76.22 O ANISOU 1053 O VAL A 158 17096 6189 5676 -1761 1374 -225 O ATOM 1054 CB VAL A 158 89.951 -12.824 59.155 1.00 82.39 C ANISOU 1054 CB VAL A 158 19094 6280 5929 -1779 1742 5 C ATOM 1055 CG1 VAL A 158 88.627 -13.169 58.473 1.00 83.19 C ANISOU 1055 CG1 VAL A 158 19118 6424 6067 -2332 1982 -217 C ATOM 1056 CG2 VAL A 158 90.476 -14.032 59.928 1.00 85.71 C ANISOU 1056 CG2 VAL A 158 20267 6237 6063 -1596 1886 159 C ATOM 1057 N GLY A 159 90.585 -9.884 58.004 1.00 71.67 N ANISOU 1057 N GLY A 159 16354 5793 5085 -1454 1170 -58 N ATOM 1058 CA GLY A 159 90.088 -8.633 57.441 1.00 69.07 C ANISOU 1058 CA GLY A 159 15465 5826 4953 -1549 1055 -165 C ATOM 1059 C GLY A 159 91.032 -7.782 56.610 1.00 70.75 C ANISOU 1059 C GLY A 159 15328 6230 5323 -1268 815 -134 C ATOM 1060 O GLY A 159 90.574 -6.810 56.000 1.00 68.46 O ANISOU 1060 O GLY A 159 14645 6196 5172 -1344 744 -221 O ATOM 1061 N VAL A 160 92.349 -8.100 56.586 1.00 67.62 N ANISOU 1061 N VAL A 160 15070 5732 4892 -933 697 -15 N ATOM 1062 CA VAL A 160 93.316 -7.294 55.826 1.00 65.50 C ANISOU 1062 CA VAL A 160 14464 5662 4760 -701 497 -2 C ATOM 1063 C VAL A 160 94.082 -8.178 54.821 1.00 70.66 C ANISOU 1063 C VAL A 160 15252 6182 5413 -534 505 13 C ATOM 1064 O VAL A 160 94.037 -7.883 53.627 1.00 69.22 O ANISOU 1064 O VAL A 160 14843 6108 5350 -590 482 -65 O ATOM 1065 CB VAL A 160 94.308 -6.506 56.738 1.00 68.78 C ANISOU 1065 CB VAL A 160 14765 6215 5153 -449 315 91 C ATOM 1066 CG1 VAL A 160 95.396 -5.803 55.928 1.00 67.17 C ANISOU 1066 CG1 VAL A 160 14244 6209 5067 -256 148 85 C ATOM 1067 CG2 VAL A 160 93.576 -5.504 57.625 1.00 67.78 C ANISOU 1067 CG2 VAL A 160 14501 6219 5031 -611 312 63 C ATOM 1068 N TRP A 161 94.787 -9.227 55.292 1.00 69.58 N ANISOU 1068 N TRP A 161 15500 5811 5125 -301 541 115 N ATOM 1069 CA TRP A 161 95.635 -10.073 54.445 1.00 70.55 C ANISOU 1069 CA TRP A 161 15779 5799 5226 -63 554 139 C ATOM 1070 C TRP A 161 94.833 -11.009 53.526 1.00 75.44 C ANISOU 1070 C TRP A 161 16649 6192 5824 -326 764 42 C ATOM 1071 O TRP A 161 95.253 -11.194 52.383 1.00 74.50 O ANISOU 1071 O TRP A 161 16452 6082 5772 -250 758 -4 O ATOM 1072 CB TRP A 161 96.600 -10.903 55.296 1.00 71.93 C ANISOU 1072 CB TRP A 161 16319 5796 5214 328 526 283 C ATOM 1073 CG TRP A 161 97.519 -10.052 56.122 1.00 72.38 C ANISOU 1073 CG TRP A 161 16105 6128 5270 596 297 356 C ATOM 1074 CD1 TRP A 161 97.413 -9.792 57.455 1.00 75.90 C ANISOU 1074 CD1 TRP A 161 16650 6594 5594 617 240 426 C ATOM 1075 CD2 TRP A 161 98.607 -9.248 55.641 1.00 71.03 C ANISOU 1075 CD2 TRP A 161 15490 6281 5219 807 105 334 C ATOM 1076 NE1 TRP A 161 98.404 -8.923 57.849 1.00 74.83 N ANISOU 1076 NE1 TRP A 161 16169 6778 5485 841 9 448 N ATOM 1077 CE2 TRP A 161 99.149 -8.569 56.755 1.00 75.17 C ANISOU 1077 CE2 TRP A 161 15865 7018 5678 943 -70 386 C ATOM 1078 CE3 TRP A 161 99.198 -9.058 54.379 1.00 71.37 C ANISOU 1078 CE3 TRP A 161 15262 6456 5400 875 79 266 C ATOM 1079 CZ2 TRP A 161 100.256 -7.717 56.647 1.00 73.96 C ANISOU 1079 CZ2 TRP A 161 15287 7221 5595 1112 -264 356 C ATOM 1080 CZ3 TRP A 161 100.291 -8.211 54.274 1.00 72.31 C ANISOU 1080 CZ3 TRP A 161 14969 6913 5591 1050 -97 246 C ATOM 1081 CH2 TRP A 161 100.811 -7.554 55.398 1.00 73.35 C ANISOU 1081 CH2 TRP A 161 14944 7267 5657 1152 -264 283 C ATOM 1082 N ILE A 162 93.708 -11.591 53.998 1.00 73.85 N ANISOU 1082 N ILE A 162 16742 5801 5518 -657 959 -6 N ATOM 1083 CA ILE A 162 92.875 -12.490 53.181 1.00 75.37 C ANISOU 1083 CA ILE A 162 17174 5800 5663 -988 1174 -133 C ATOM 1084 C ILE A 162 92.252 -11.682 51.995 1.00 76.86 C ANISOU 1084 C ILE A 162 16874 6300 6030 -1227 1104 -289 C ATOM 1085 O ILE A 162 92.453 -12.126 50.862 1.00 76.89 O ANISOU 1085 O ILE A 162 16922 6244 6050 -1231 1136 -352 O ATOM 1086 CB ILE A 162 91.790 -13.255 54.009 1.00 81.17 C ANISOU 1086 CB ILE A 162 18318 6297 6228 -1354 1425 -177 C ATOM 1087 CG1 ILE A 162 92.415 -14.166 55.112 1.00 84.64 C ANISOU 1087 CG1 ILE A 162 19357 6365 6439 -1087 1515 -8 C ATOM 1088 CG2 ILE A 162 90.808 -14.042 53.117 1.00 83.47 C ANISOU 1088 CG2 ILE A 162 18772 6469 6474 -1803 1649 -363 C ATOM 1089 CD1 ILE A 162 93.396 -15.342 54.658 1.00 95.27 C ANISOU 1089 CD1 ILE A 162 21203 7350 7646 -737 1585 80 C ATOM 1090 N PRO A 163 91.570 -10.509 52.173 1.00 71.05 N ANISOU 1090 N PRO A 163 15701 5886 5409 -1377 1004 -345 N ATOM 1091 CA PRO A 163 91.024 -9.804 50.998 1.00 69.12 C ANISOU 1091 CA PRO A 163 15054 5918 5292 -1529 928 -476 C ATOM 1092 C PRO A 163 92.108 -9.223 50.082 1.00 70.94 C ANISOU 1092 C PRO A 163 15067 6257 5631 -1229 760 -426 C ATOM 1093 O PRO A 163 91.876 -9.163 48.877 1.00 70.15 O ANISOU 1093 O PRO A 163 14832 6248 5572 -1323 747 -523 O ATOM 1094 CB PRO A 163 90.181 -8.680 51.611 1.00 69.56 C ANISOU 1094 CB PRO A 163 14762 6255 5412 -1652 865 -513 C ATOM 1095 CG PRO A 163 89.951 -9.086 53.024 1.00 75.49 C ANISOU 1095 CG PRO A 163 15786 6846 6051 -1716 982 -453 C ATOM 1096 CD PRO A 163 91.202 -9.796 53.413 1.00 71.96 C ANISOU 1096 CD PRO A 163 15704 6118 5520 -1405 969 -299 C ATOM 1097 N ALA A 164 93.282 -8.820 50.635 1.00 66.49 N ANISOU 1097 N ALA A 164 14469 5700 5094 -891 639 -291 N ATOM 1098 CA ALA A 164 94.401 -8.257 49.859 1.00 64.87 C ANISOU 1098 CA ALA A 164 14045 5621 4982 -633 506 -258 C ATOM 1099 C ALA A 164 94.983 -9.289 48.891 1.00 69.67 C ANISOU 1099 C ALA A 164 14879 6045 5548 -527 591 -276 C ATOM 1100 O ALA A 164 95.277 -8.943 47.746 1.00 68.33 O ANISOU 1100 O ALA A 164 14528 5985 5449 -504 552 -329 O ATOM 1101 CB ALA A 164 95.492 -7.746 50.785 1.00 65.25 C ANISOU 1101 CB ALA A 164 14010 5747 5036 -344 379 -142 C ATOM 1102 N LEU A 165 95.122 -10.553 49.339 1.00 68.33 N ANISOU 1102 N LEU A 165 15147 5574 5242 -460 724 -233 N ATOM 1103 CA LEU A 165 95.624 -11.650 48.510 1.00 69.91 C ANISOU 1103 CA LEU A 165 15654 5540 5370 -343 842 -251 C ATOM 1104 C LEU A 165 94.534 -12.125 47.534 1.00 74.22 C ANISOU 1104 C LEU A 165 16304 6008 5886 -735 980 -409 C ATOM 1105 O LEU A 165 94.855 -12.746 46.520 1.00 74.90 O ANISOU 1105 O LEU A 165 16547 5969 5940 -698 1058 -463 O ATOM 1106 CB LEU A 165 96.127 -12.818 49.379 1.00 72.81 C ANISOU 1106 CB LEU A 165 16525 5575 5564 -101 949 -142 C ATOM 1107 CG LEU A 165 97.412 -12.574 50.187 1.00 77.79 C ANISOU 1107 CG LEU A 165 17074 6303 6179 373 796 4 C ATOM 1108 CD1 LEU A 165 97.549 -13.576 51.311 1.00 80.81 C ANISOU 1108 CD1 LEU A 165 17974 6377 6353 567 885 122 C ATOM 1109 CD2 LEU A 165 98.653 -12.581 49.299 1.00 80.59 C ANISOU 1109 CD2 LEU A 165 17263 6768 6591 721 734 7 C ATOM 1110 N LEU A 166 93.256 -11.812 47.832 1.00 70.13 N ANISOU 1110 N LEU A 166 15675 5600 5371 -1108 1008 -498 N ATOM 1111 CA LEU A 166 92.102 -12.147 46.995 1.00 70.75 C ANISOU 1111 CA LEU A 166 15758 5712 5410 -1522 1110 -679 C ATOM 1112 C LEU A 166 91.917 -11.119 45.869 1.00 72.45 C ANISOU 1112 C LEU A 166 15523 6264 5742 -1551 951 -758 C ATOM 1113 O LEU A 166 91.198 -11.391 44.906 1.00 72.69 O ANISOU 1113 O LEU A 166 15532 6360 5727 -1817 995 -910 O ATOM 1114 CB LEU A 166 90.828 -12.232 47.855 1.00 71.79 C ANISOU 1114 CB LEU A 166 15913 5882 5482 -1892 1211 -756 C ATOM 1115 CG LEU A 166 90.239 -13.630 48.091 1.00 80.07 C ANISOU 1115 CG LEU A 166 17481 6594 6346 -2211 1483 -841 C ATOM 1116 CD1 LEU A 166 91.181 -14.524 48.898 1.00 81.92 C ANISOU 1116 CD1 LEU A 166 18256 6411 6460 -1914 1593 -674 C ATOM 1117 CD2 LEU A 166 88.910 -13.535 48.807 1.00 83.74 C ANISOU 1117 CD2 LEU A 166 17853 7197 6767 -2633 1586 -956 C ATOM 1118 N LEU A 167 92.566 -9.944 45.991 1.00 66.93 N ANISOU 1118 N LEU A 167 14493 5771 5165 -1289 774 -660 N ATOM 1119 CA LEU A 167 92.507 -8.864 45.000 1.00 65.06 C ANISOU 1119 CA LEU A 167 13894 5811 5014 -1267 633 -704 C ATOM 1120 C LEU A 167 93.703 -8.922 44.037 1.00 68.47 C ANISOU 1120 C LEU A 167 14356 6187 5472 -1025 615 -668 C ATOM 1121 O LEU A 167 93.812 -8.071 43.152 1.00 66.79 O ANISOU 1121 O LEU A 167 13910 6159 5308 -990 522 -693 O ATOM 1122 CB LEU A 167 92.459 -7.488 45.693 1.00 63.16 C ANISOU 1122 CB LEU A 167 13331 5799 4867 -1167 491 -634 C ATOM 1123 CG LEU A 167 91.164 -7.120 46.422 1.00 68.13 C ANISOU 1123 CG LEU A 167 13826 6576 5483 -1389 494 -693 C ATOM 1124 CD1 LEU A 167 91.414 -6.049 47.457 1.00 66.79 C ANISOU 1124 CD1 LEU A 167 13490 6507 5380 -1235 403 -592 C ATOM 1125 CD2 LEU A 167 90.059 -6.715 45.450 1.00 70.98 C ANISOU 1125 CD2 LEU A 167 13954 7190 5826 -1576 446 -835 C ATOM 1126 N THR A 168 94.588 -9.924 44.205 1.00 66.43 N ANISOU 1126 N THR A 168 14404 5673 5164 -841 717 -613 N ATOM 1127 CA THR A 168 95.766 -10.107 43.353 1.00 66.50 C ANISOU 1127 CA THR A 168 14444 5636 5188 -587 731 -591 C ATOM 1128 C THR A 168 95.434 -11.049 42.181 1.00 72.22 C ANISOU 1128 C THR A 168 15426 6199 5816 -745 864 -712 C ATOM 1129 O THR A 168 96.261 -11.200 41.281 1.00 72.06 O ANISOU 1129 O THR A 168 15434 6149 5795 -575 898 -723 O ATOM 1130 CB THR A 168 96.965 -10.628 44.160 1.00 74.86 C ANISOU 1130 CB THR A 168 15658 6556 6230 -228 755 -470 C ATOM 1131 OG1 THR A 168 96.642 -11.889 44.745 1.00 76.75 O ANISOU 1131 OG1 THR A 168 16344 6480 6339 -257 900 -457 O ATOM 1132 CG2 THR A 168 97.421 -9.651 45.227 1.00 71.80 C ANISOU 1132 CG2 THR A 168 14993 6367 5919 -79 607 -371 C ATOM 1133 N ILE A 169 94.214 -11.649 42.178 1.00 70.29 N ANISOU 1133 N ILE A 169 15352 5874 5479 -1099 949 -824 N ATOM 1134 CA ILE A 169 93.713 -12.558 41.135 1.00 72.27 C ANISOU 1134 CA ILE A 169 15863 5988 5609 -1345 1080 -975 C ATOM 1135 C ILE A 169 93.813 -11.854 39.745 1.00 75.44 C ANISOU 1135 C ILE A 169 16012 6615 6038 -1343 980 -1044 C ATOM 1136 O ILE A 169 94.387 -12.477 38.848 1.00 76.41 O ANISOU 1136 O ILE A 169 16353 6581 6098 -1267 1078 -1086 O ATOM 1137 CB ILE A 169 92.266 -13.075 41.431 1.00 77.02 C ANISOU 1137 CB ILE A 169 16575 6581 6110 -1805 1167 -1117 C ATOM 1138 CG1 ILE A 169 92.209 -13.835 42.785 1.00 78.82 C ANISOU 1138 CG1 ILE A 169 17140 6531 6276 -1821 1309 -1044 C ATOM 1139 CG2 ILE A 169 91.740 -13.962 40.282 1.00 80.25 C ANISOU 1139 CG2 ILE A 169 17230 6890 6373 -2115 1294 -1308 C ATOM 1140 CD1 ILE A 169 90.798 -14.281 43.272 1.00 87.25 C ANISOU 1140 CD1 ILE A 169 18300 7608 7245 -2313 1429 -1188 C ATOM 1141 N PRO A 170 93.378 -10.574 39.539 1.00 70.13 N ANISOU 1141 N PRO A 170 14933 6274 5439 -1377 801 -1044 N ATOM 1142 CA PRO A 170 93.533 -9.958 38.205 1.00 69.50 C ANISOU 1142 CA PRO A 170 14703 6360 5343 -1346 724 -1093 C ATOM 1143 C PRO A 170 94.996 -9.698 37.813 1.00 72.95 C ANISOU 1143 C PRO A 170 15139 6733 5844 -1018 749 -996 C ATOM 1144 O PRO A 170 95.282 -9.604 36.619 1.00 73.02 O ANISOU 1144 O PRO A 170 15169 6774 5803 -1003 765 -1049 O ATOM 1145 CB PRO A 170 92.777 -8.634 38.334 1.00 69.57 C ANISOU 1145 CB PRO A 170 14342 6693 5399 -1390 541 -1082 C ATOM 1146 CG PRO A 170 91.902 -8.793 39.519 1.00 74.17 C ANISOU 1146 CG PRO A 170 14882 7303 5996 -1552 546 -1094 C ATOM 1147 CD PRO A 170 92.671 -9.652 40.451 1.00 70.19 C ANISOU 1147 CD PRO A 170 14651 6501 5517 -1437 678 -1006 C ATOM 1148 N ASP A 171 95.921 -9.609 38.797 1.00 68.90 N ANISOU 1148 N ASP A 171 14596 6156 5425 -764 757 -868 N ATOM 1149 CA ASP A 171 97.353 -9.405 38.542 1.00 68.69 C ANISOU 1149 CA ASP A 171 14510 6131 5456 -459 789 -800 C ATOM 1150 C ASP A 171 98.019 -10.718 38.068 1.00 74.87 C ANISOU 1150 C ASP A 171 15632 6656 6159 -319 965 -835 C ATOM 1151 O ASP A 171 99.166 -10.697 37.617 1.00 74.90 O ANISOU 1151 O ASP A 171 15591 6680 6189 -70 1022 -814 O ATOM 1152 CB ASP A 171 98.063 -8.857 39.787 1.00 69.67 C ANISOU 1152 CB ASP A 171 14448 6341 5683 -250 715 -677 C ATOM 1153 CG ASP A 171 97.533 -7.510 40.223 1.00 78.97 C ANISOU 1153 CG ASP A 171 15333 7742 6929 -362 568 -645 C ATOM 1154 OD1 ASP A 171 96.533 -7.482 40.969 1.00 79.30 O ANISOU 1154 OD1 ASP A 171 15380 7788 6963 -516 521 -644 O ATOM 1155 OD2 ASP A 171 98.117 -6.483 39.815 1.00 84.43 O ANISOU 1155 OD2 ASP A 171 15815 8595 7670 -301 523 -628 O ATOM 1156 N PHE A 172 97.299 -11.852 38.175 1.00 73.08 N ANISOU 1156 N PHE A 172 15756 6187 5823 -486 1073 -898 N ATOM 1157 CA PHE A 172 97.750 -13.160 37.703 1.00 75.45 C ANISOU 1157 CA PHE A 172 16477 6181 6012 -384 1269 -945 C ATOM 1158 C PHE A 172 97.160 -13.458 36.320 1.00 80.59 C ANISOU 1158 C PHE A 172 17267 6803 6551 -656 1335 -1104 C ATOM 1159 O PHE A 172 97.699 -14.297 35.596 1.00 82.34 O ANISOU 1159 O PHE A 172 17790 6813 6682 -551 1498 -1158 O ATOM 1160 CB PHE A 172 97.373 -14.281 38.692 1.00 79.10 C ANISOU 1160 CB PHE A 172 17342 6331 6381 -418 1388 -922 C ATOM 1161 CG PHE A 172 98.176 -14.364 39.971 1.00 80.69 C ANISOU 1161 CG PHE A 172 17556 6477 6626 -56 1362 -763 C ATOM 1162 CD1 PHE A 172 99.456 -14.905 39.973 1.00 85.43 C ANISOU 1162 CD1 PHE A 172 18294 6962 7203 396 1440 -693 C ATOM 1163 CD2 PHE A 172 97.612 -14.005 41.188 1.00 81.73 C ANISOU 1163 CD2 PHE A 172 17593 6669 6790 -156 1270 -694 C ATOM 1164 CE1 PHE A 172 100.187 -15.013 41.161 1.00 86.98 C ANISOU 1164 CE1 PHE A 172 18493 7149 7406 761 1389 -553 C ATOM 1165 CE2 PHE A 172 98.343 -14.111 42.376 1.00 85.04 C ANISOU 1165 CE2 PHE A 172 18050 7044 7215 181 1233 -550 C ATOM 1166 CZ PHE A 172 99.623 -14.621 42.355 1.00 84.91 C ANISOU 1166 CZ PHE A 172 18149 6946 7168 643 1280 -480 C ATOM 1167 N ILE A 173 96.058 -12.769 35.956 1.00 76.16 N ANISOU 1167 N ILE A 173 16489 6470 5978 -980 1205 -1184 N ATOM 1168 CA ILE A 173 95.346 -12.972 34.691 1.00 77.28 C ANISOU 1168 CA ILE A 173 16721 6657 5985 -1265 1220 -1348 C ATOM 1169 C ILE A 173 95.743 -11.914 33.639 1.00 80.65 C ANISOU 1169 C ILE A 173 16884 7325 6433 -1164 1114 -1340 C ATOM 1170 O ILE A 173 96.112 -12.287 32.523 1.00 81.59 O ANISOU 1170 O ILE A 173 17181 7365 6454 -1155 1209 -1417 O ATOM 1171 CB ILE A 173 93.794 -12.951 34.909 1.00 80.62 C ANISOU 1171 CB ILE A 173 17062 7232 6338 -1682 1135 -1468 C ATOM 1172 CG1 ILE A 173 93.343 -13.929 36.022 1.00 82.39 C ANISOU 1172 CG1 ILE A 173 17563 7214 6527 -1840 1269 -1480 C ATOM 1173 CG2 ILE A 173 93.035 -13.214 33.589 1.00 83.01 C ANISOU 1173 CG2 ILE A 173 17439 7634 6468 -1988 1127 -1664 C ATOM 1174 CD1 ILE A 173 91.888 -13.744 36.515 1.00 88.56 C ANISOU 1174 CD1 ILE A 173 18163 8212 7275 -2233 1193 -1588 C ATOM 1175 N PHE A 174 95.630 -10.614 33.978 1.00 75.46 N ANISOU 1175 N PHE A 174 15857 6935 5879 -1103 939 -1252 N ATOM 1176 CA PHE A 174 95.815 -9.513 33.032 1.00 74.54 C ANISOU 1176 CA PHE A 174 15544 7029 5748 -1050 844 -1242 C ATOM 1177 C PHE A 174 97.236 -8.909 33.027 1.00 77.48 C ANISOU 1177 C PHE A 174 15804 7408 6228 -756 900 -1132 C ATOM 1178 O PHE A 174 97.605 -8.313 32.011 1.00 77.26 O ANISOU 1178 O PHE A 174 15744 7464 6146 -727 910 -1146 O ATOM 1179 CB PHE A 174 94.800 -8.395 33.333 1.00 75.07 C ANISOU 1179 CB PHE A 174 15325 7370 5829 -1155 639 -1222 C ATOM 1180 CG PHE A 174 93.375 -8.901 33.420 1.00 78.00 C ANISOU 1180 CG PHE A 174 15708 7828 6099 -1453 576 -1352 C ATOM 1181 CD1 PHE A 174 92.669 -9.251 32.272 1.00 82.92 C ANISOU 1181 CD1 PHE A 174 16423 8542 6541 -1662 548 -1508 C ATOM 1182 CD2 PHE A 174 92.746 -9.047 34.650 1.00 79.87 C ANISOU 1182 CD2 PHE A 174 15859 8081 6406 -1550 553 -1337 C ATOM 1183 CE1 PHE A 174 91.364 -9.746 32.357 1.00 85.45 C ANISOU 1183 CE1 PHE A 174 16710 9000 6756 -1980 496 -1664 C ATOM 1184 CE2 PHE A 174 91.438 -9.537 34.733 1.00 84.28 C ANISOU 1184 CE2 PHE A 174 16402 8756 6866 -1869 525 -1486 C ATOM 1185 CZ PHE A 174 90.755 -9.880 33.586 1.00 84.31 C ANISOU 1185 CZ PHE A 174 16457 8884 6694 -2092 494 -1656 C ATOM 1186 N ALA A 175 98.026 -9.053 34.110 1.00 73.51 N ANISOU 1186 N ALA A 175 15239 6839 5851 -555 940 -1036 N ATOM 1187 CA ALA A 175 99.384 -8.495 34.139 1.00 73.12 C ANISOU 1187 CA ALA A 175 15023 6867 5894 -308 992 -966 C ATOM 1188 C ALA A 175 100.353 -9.373 33.341 1.00 79.49 C ANISOU 1188 C ALA A 175 16021 7536 6648 -143 1184 -1021 C ATOM 1189 O ALA A 175 100.576 -10.531 33.699 1.00 80.63 O ANISOU 1189 O ALA A 175 16391 7475 6768 -18 1287 -1031 O ATOM 1190 CB ALA A 175 99.871 -8.333 35.569 1.00 73.15 C ANISOU 1190 CB ALA A 175 14862 6909 6023 -145 940 -863 C ATOM 1191 N ASN A 176 100.893 -8.820 32.233 1.00 76.79 N ANISOU 1191 N ASN A 176 15625 7287 6265 -138 1249 -1060 N ATOM 1192 CA ASN A 176 101.838 -9.477 31.316 1.00 78.76 C ANISOU 1192 CA ASN A 176 16023 7446 6455 12 1451 -1127 C ATOM 1193 C ASN A 176 102.540 -8.436 30.417 1.00 82.36 C ANISOU 1193 C ASN A 176 16312 8081 6900 0 1510 -1141 C ATOM 1194 O ASN A 176 102.001 -7.351 30.183 1.00 80.03 O ANISOU 1194 O ASN A 176 15921 7907 6581 -173 1397 -1114 O ATOM 1195 CB ASN A 176 101.147 -10.562 30.457 1.00 81.50 C ANISOU 1195 CB ASN A 176 16757 7569 6640 -125 1537 -1238 C ATOM 1196 CG ASN A 176 99.775 -10.218 29.916 1.00104.48 C ANISOU 1196 CG ASN A 176 19728 10535 9436 -452 1394 -1296 C ATOM 1197 OD1 ASN A 176 99.458 -9.067 29.588 1.00 98.26 O ANISOU 1197 OD1 ASN A 176 18754 9944 8637 -544 1269 -1267 O ATOM 1198 ND2 ASN A 176 98.933 -11.233 29.791 1.00 97.04 N ANISOU 1198 ND2 ASN A 176 19066 9425 8381 -631 1418 -1391 N ATOM 1199 N VAL A 177 103.754 -8.780 29.936 1.00 81.30 N ANISOU 1199 N VAL A 177 16163 7958 6769 197 1707 -1186 N ATOM 1200 CA VAL A 177 104.619 -7.930 29.102 1.00 81.96 C ANISOU 1200 CA VAL A 177 16099 8205 6835 180 1831 -1219 C ATOM 1201 C VAL A 177 104.053 -7.838 27.668 1.00 87.17 C ANISOU 1201 C VAL A 177 17032 8778 7310 -14 1884 -1288 C ATOM 1202 O VAL A 177 103.542 -8.827 27.135 1.00 87.88 O ANISOU 1202 O VAL A 177 17420 8681 7288 -41 1923 -1356 O ATOM 1203 CB VAL A 177 106.090 -8.444 29.090 1.00 88.15 C ANISOU 1203 CB VAL A 177 16744 9074 7676 470 2039 -1269 C ATOM 1204 CG1 VAL A 177 107.033 -7.435 28.435 1.00 88.68 C ANISOU 1204 CG1 VAL A 177 16586 9366 7741 398 2182 -1316 C ATOM 1205 CG2 VAL A 177 106.576 -8.762 30.500 1.00 88.04 C ANISOU 1205 CG2 VAL A 177 16508 9146 7799 718 1958 -1206 C ATOM 1206 N SER A 178 104.161 -6.638 27.056 1.00 83.78 N ANISOU 1206 N SER A 178 16531 8474 6826 -157 1893 -1275 N ATOM 1207 CA SER A 178 103.703 -6.334 25.699 1.00 84.47 C ANISOU 1207 CA SER A 178 16875 8513 6708 -318 1930 -1322 C ATOM 1208 C SER A 178 104.616 -5.310 25.022 1.00 89.56 C ANISOU 1208 C SER A 178 17452 9269 7306 -370 2103 -1328 C ATOM 1209 O SER A 178 105.128 -4.406 25.684 1.00 87.97 O ANISOU 1209 O SER A 178 17004 9207 7216 -388 2102 -1276 O ATOM 1210 CB SER A 178 102.271 -5.809 25.729 1.00 86.62 C ANISOU 1210 CB SER A 178 17230 8790 6889 -483 1676 -1274 C ATOM 1211 OG SER A 178 101.779 -5.527 24.429 1.00 97.37 O ANISOU 1211 OG SER A 178 18845 10133 8019 -602 1674 -1316 O ATOM 1212 N GLU A 179 104.803 -5.452 23.698 1.00 88.91 N ANISOU 1212 N GLU A 179 17620 9121 7040 -424 2266 -1403 N ATOM 1213 CA GLU A 179 105.618 -4.542 22.889 1.00 90.49 C ANISOU 1213 CA GLU A 179 17839 9395 7149 -515 2475 -1423 C ATOM 1214 C GLU A 179 104.774 -3.318 22.505 1.00 93.89 C ANISOU 1214 C GLU A 179 18442 9813 7419 -684 2331 -1338 C ATOM 1215 O GLU A 179 103.632 -3.469 22.064 1.00 93.19 O ANISOU 1215 O GLU A 179 18578 9652 7176 -720 2144 -1323 O ATOM 1216 CB GLU A 179 106.182 -5.267 21.644 1.00 94.58 C ANISOU 1216 CB GLU A 179 18586 9833 7517 -485 2731 -1542 C ATOM 1217 CG GLU A 179 106.954 -4.389 20.659 1.00107.90 C ANISOU 1217 CG GLU A 179 20358 11574 9064 -617 2983 -1577 C ATOM 1218 CD GLU A 179 108.144 -3.596 21.176 1.00131.40 C ANISOU 1218 CD GLU A 179 22994 14749 12183 -658 3167 -1589 C ATOM 1219 OE1 GLU A 179 108.932 -4.142 21.982 1.00130.02 O ANISOU 1219 OE1 GLU A 179 22477 14716 12211 -490 3225 -1635 O ATOM 1220 OE2 GLU A 179 108.310 -2.436 20.736 1.00125.34 O ANISOU 1220 OE2 GLU A 179 22324 14001 11299 -861 3266 -1563 O ATOM 1221 N ALA A 180 105.338 -2.109 22.693 1.00 90.55 N ANISOU 1221 N ALA A 180 17919 9471 7016 -782 2422 -1291 N ATOM 1222 CA ALA A 180 104.644 -0.860 22.389 1.00 90.01 C ANISOU 1222 CA ALA A 180 18065 9355 6778 -897 2318 -1195 C ATOM 1223 C ALA A 180 105.575 0.176 21.739 1.00 95.62 C ANISOU 1223 C ALA A 180 18896 10062 7371 -1057 2606 -1209 C ATOM 1224 O ALA A 180 106.364 0.830 22.430 1.00 95.55 O ANISOU 1224 O ALA A 180 18657 10152 7497 -1150 2729 -1216 O ATOM 1225 CB ALA A 180 104.030 -0.285 23.660 1.00 88.47 C ANISOU 1225 CB ALA A 180 17677 9209 6728 -874 2082 -1096 C ATOM 1226 N ASP A 181 105.461 0.281 20.416 1.00 93.51 N ANISOU 1226 N ASP A 181 19013 9688 6829 -1113 2717 -1225 N ATOM 1227 CA ASP A 181 106.205 1.240 19.608 1.00 95.60 C ANISOU 1227 CA ASP A 181 19538 9893 6894 -1288 3014 -1239 C ATOM 1228 C ASP A 181 107.673 0.925 19.862 1.00100.31 C ANISOU 1228 C ASP A 181 19839 10631 7645 -1406 3366 -1364 C ATOM 1229 O ASP A 181 108.246 0.014 19.262 1.00102.09 O ANISOU 1229 O ASP A 181 20147 10863 7779 -1431 3621 -1470 O ATOM 1230 CB ASP A 181 105.802 2.670 19.976 1.00 97.41 C ANISOU 1230 CB ASP A 181 20004 10024 6985 -1379 2950 -1109 C ATOM 1231 CG ASP A 181 104.557 3.131 19.245 1.00107.88 C ANISOU 1231 CG ASP A 181 21734 11224 8030 -1256 2692 -995 C ATOM 1232 OD1 ASP A 181 103.730 2.270 18.875 1.00108.13 O ANISOU 1232 OD1 ASP A 181 21767 11293 8024 -1117 2472 -1018 O ATOM 1233 OD2 ASP A 181 104.404 4.353 19.040 1.00113.94 O ANISOU 1233 OD2 ASP A 181 22822 11868 8603 -1294 2710 -890 O ATOM 1234 N ASP A 182 108.270 1.702 20.754 1.00 95.49 N ANISOU 1234 N ASP A 182 18884 10157 7240 -1487 3388 -1365 N ATOM 1235 CA ASP A 182 109.718 1.763 20.969 1.00 96.97 C ANISOU 1235 CA ASP A 182 18733 10557 7553 -1625 3704 -1504 C ATOM 1236 C ASP A 182 110.270 0.690 21.921 1.00 98.94 C ANISOU 1236 C ASP A 182 18466 11038 8090 -1414 3636 -1582 C ATOM 1237 O ASP A 182 111.352 0.161 21.660 1.00100.97 O ANISOU 1237 O ASP A 182 18483 11478 8403 -1384 3887 -1723 O ATOM 1238 CB ASP A 182 110.092 3.148 21.526 1.00 99.39 C ANISOU 1238 CB ASP A 182 19009 10899 7857 -1902 3805 -1485 C ATOM 1239 CG ASP A 182 109.670 4.297 20.633 1.00112.35 C ANISOU 1239 CG ASP A 182 21220 12281 9187 -2096 3919 -1401 C ATOM 1240 OD1 ASP A 182 110.452 4.663 19.727 1.00116.02 O ANISOU 1240 OD1 ASP A 182 21869 12727 9484 -2319 4277 -1488 O ATOM 1241 OD2 ASP A 182 108.554 4.824 20.833 1.00117.17 O ANISOU 1241 OD2 ASP A 182 22107 12708 9704 -2008 3660 -1248 O ATOM 1242 N ARG A 183 109.574 0.407 23.033 1.00 91.56 N ANISOU 1242 N ARG A 183 17364 10105 7318 -1255 3316 -1494 N ATOM 1243 CA ARG A 183 110.054 -0.539 24.047 1.00 90.27 C ANISOU 1243 CA ARG A 183 16766 10136 7398 -1030 3232 -1543 C ATOM 1244 C ARG A 183 108.941 -1.481 24.558 1.00 90.23 C ANISOU 1244 C ARG A 183 16841 9984 7458 -792 2918 -1451 C ATOM 1245 O ARG A 183 107.789 -1.381 24.131 1.00 88.36 O ANISOU 1245 O ARG A 183 16936 9547 7089 -821 2755 -1368 O ATOM 1246 CB ARG A 183 110.658 0.245 25.234 1.00 90.06 C ANISOU 1246 CB ARG A 183 16358 10337 7526 -1149 3211 -1558 C ATOM 1247 CG ARG A 183 109.753 1.343 25.797 1.00 97.45 C ANISOU 1247 CG ARG A 183 17468 11131 8425 -1307 3015 -1429 C ATOM 1248 CD ARG A 183 110.362 2.088 26.977 1.00105.53 C ANISOU 1248 CD ARG A 183 18144 12369 9583 -1451 3005 -1462 C ATOM 1249 NE ARG A 183 110.481 1.244 28.170 1.00110.19 N ANISOU 1249 NE ARG A 183 18351 13135 10382 -1202 2802 -1462 N ATOM 1250 CZ ARG A 183 109.560 1.150 29.124 1.00119.50 C ANISOU 1250 CZ ARG A 183 19544 14219 11641 -1084 2510 -1344 C ATOM 1251 NH1 ARG A 183 109.748 0.341 30.158 1.00104.30 N ANISOU 1251 NH1 ARG A 183 17314 12439 9875 -854 2356 -1345 N ATOM 1252 NH2 ARG A 183 108.446 1.868 29.056 1.00104.68 N ANISOU 1252 NH2 ARG A 183 17995 12110 9669 -1177 2376 -1226 N ATOM 1253 N TYR A 184 109.313 -2.402 25.475 1.00 85.55 N ANISOU 1253 N TYR A 184 15942 9510 7051 -557 2844 -1477 N ATOM 1254 CA TYR A 184 108.415 -3.363 26.124 1.00 83.00 C ANISOU 1254 CA TYR A 184 15682 9054 6799 -355 2594 -1406 C ATOM 1255 C TYR A 184 107.817 -2.748 27.388 1.00 82.92 C ANISOU 1255 C TYR A 184 15527 9079 6902 -402 2342 -1302 C ATOM 1256 O TYR A 184 108.505 -1.997 28.086 1.00 82.56 O ANISOU 1256 O TYR A 184 15196 9228 6946 -480 2372 -1314 O ATOM 1257 CB TYR A 184 109.155 -4.670 26.466 1.00 85.85 C ANISOU 1257 CB TYR A 184 15871 9483 7265 -45 2671 -1475 C ATOM 1258 CG TYR A 184 109.763 -5.383 25.277 1.00 90.56 C ANISOU 1258 CG TYR A 184 16618 10037 7754 48 2937 -1588 C ATOM 1259 CD1 TYR A 184 109.044 -6.346 24.574 1.00 92.73 C ANISOU 1259 CD1 TYR A 184 17275 10048 7909 116 2927 -1597 C ATOM 1260 CD2 TYR A 184 111.070 -5.122 24.876 1.00 94.16 C ANISOU 1260 CD2 TYR A 184 16825 10734 8218 52 3214 -1705 C ATOM 1261 CE1 TYR A 184 109.606 -7.019 23.489 1.00 96.13 C ANISOU 1261 CE1 TYR A 184 17877 10420 8226 206 3186 -1708 C ATOM 1262 CE2 TYR A 184 111.640 -5.783 23.789 1.00 97.79 C ANISOU 1262 CE2 TYR A 184 17422 11161 8573 152 3481 -1817 C ATOM 1263 CZ TYR A 184 110.905 -6.734 23.100 1.00104.91 C ANISOU 1263 CZ TYR A 184 18744 11764 9354 241 3466 -1812 C ATOM 1264 OH TYR A 184 111.463 -7.396 22.032 1.00108.26 O ANISOU 1264 OH TYR A 184 19336 12136 9662 342 3742 -1929 O ATOM 1265 N ILE A 185 106.542 -3.054 27.684 1.00 76.32 N ANISOU 1265 N ILE A 185 14875 8074 6048 -377 2106 -1217 N ATOM 1266 CA ILE A 185 105.861 -2.512 28.863 1.00 73.32 C ANISOU 1266 CA ILE A 185 14383 7715 5761 -412 1876 -1121 C ATOM 1267 C ILE A 185 105.163 -3.644 29.644 1.00 76.40 C ANISOU 1267 C ILE A 185 14787 8012 6229 -249 1704 -1087 C ATOM 1268 O ILE A 185 104.489 -4.491 29.052 1.00 76.20 O ANISOU 1268 O ILE A 185 15006 7831 6116 -225 1684 -1110 O ATOM 1269 CB ILE A 185 104.856 -1.366 28.516 1.00 74.75 C ANISOU 1269 CB ILE A 185 14778 7809 5813 -594 1765 -1045 C ATOM 1270 CG1 ILE A 185 103.839 -1.774 27.412 1.00 74.95 C ANISOU 1270 CG1 ILE A 185 15137 7684 5655 -606 1703 -1048 C ATOM 1271 CG2 ILE A 185 105.606 -0.073 28.149 1.00 76.32 C ANISOU 1271 CG2 ILE A 185 14977 8075 5947 -777 1941 -1059 C ATOM 1272 CD1 ILE A 185 102.600 -0.883 27.265 1.00 78.94 C ANISOU 1272 CD1 ILE A 185 15822 8143 6030 -678 1512 -965 C ATOM 1273 N CYS A 186 105.358 -3.655 30.976 1.00 72.28 N ANISOU 1273 N CYS A 186 14026 7585 5852 -160 1596 -1042 N ATOM 1274 CA CYS A 186 104.747 -4.605 31.909 1.00 71.24 C ANISOU 1274 CA CYS A 186 13924 7358 5786 -24 1449 -997 C ATOM 1275 C CYS A 186 103.502 -3.951 32.515 1.00 72.13 C ANISOU 1275 C CYS A 186 14076 7431 5900 -171 1242 -917 C ATOM 1276 O CYS A 186 103.621 -3.097 33.398 1.00 70.70 O ANISOU 1276 O CYS A 186 13709 7361 5793 -213 1164 -868 O ATOM 1277 CB CYS A 186 105.747 -5.039 32.978 1.00 72.64 C ANISOU 1277 CB CYS A 186 13841 7675 6086 200 1459 -995 C ATOM 1278 SG CYS A 186 105.009 -5.948 34.360 1.00 75.71 S ANISOU 1278 SG CYS A 186 14301 7933 6532 346 1278 -910 S ATOM 1279 N CYS A 187 102.311 -4.296 31.986 1.00 67.69 N ANISOU 1279 N CYS A 187 13746 6735 5237 -259 1161 -922 N ATOM 1280 CA CYS A 187 101.044 -3.686 32.401 1.00 65.54 C ANISOU 1280 CA CYS A 187 13491 6470 4942 -378 972 -868 C ATOM 1281 C CYS A 187 99.932 -4.727 32.512 1.00 69.04 C ANISOU 1281 C CYS A 187 14079 6809 5343 -420 883 -899 C ATOM 1282 O CYS A 187 100.110 -5.880 32.120 1.00 69.85 O ANISOU 1282 O CYS A 187 14340 6790 5409 -382 981 -963 O ATOM 1283 CB CYS A 187 100.644 -2.594 31.410 1.00 65.75 C ANISOU 1283 CB CYS A 187 13623 6530 4831 -488 957 -860 C ATOM 1284 SG CYS A 187 101.975 -1.446 30.973 1.00 70.35 S ANISOU 1284 SG CYS A 187 14142 7182 5404 -524 1143 -856 S ATOM 1285 N ARG A 188 98.761 -4.282 33.011 1.00 64.54 N ANISOU 1285 N ARG A 188 13466 6293 4761 -515 716 -869 N ATOM 1286 CA ARG A 188 97.534 -5.067 33.122 1.00 64.68 C ANISOU 1286 CA ARG A 188 13575 6278 4722 -631 628 -925 C ATOM 1287 C ARG A 188 96.670 -4.773 31.897 1.00 70.54 C ANISOU 1287 C ARG A 188 14416 7099 5285 -742 556 -991 C ATOM 1288 O ARG A 188 96.194 -3.646 31.733 1.00 69.66 O ANISOU 1288 O ARG A 188 14230 7117 5121 -730 444 -946 O ATOM 1289 CB ARG A 188 96.794 -4.771 34.443 1.00 62.26 C ANISOU 1289 CB ARG A 188 13118 6036 4504 -661 502 -871 C ATOM 1290 CG ARG A 188 97.387 -5.513 35.638 1.00 68.74 C ANISOU 1290 CG ARG A 188 13925 6748 5444 -571 562 -829 C ATOM 1291 CD ARG A 188 96.799 -5.123 36.984 1.00 72.66 C ANISOU 1291 CD ARG A 188 14284 7304 6018 -596 457 -769 C ATOM 1292 NE ARG A 188 95.343 -5.273 37.045 1.00 75.43 N ANISOU 1292 NE ARG A 188 14642 7714 6303 -776 371 -829 N ATOM 1293 CZ ARG A 188 94.628 -5.212 38.164 1.00 84.07 C ANISOU 1293 CZ ARG A 188 15653 8849 7442 -838 313 -808 C ATOM 1294 NH1 ARG A 188 95.229 -5.057 39.337 1.00 69.96 N ANISOU 1294 NH1 ARG A 188 13810 7018 5754 -728 320 -718 N ATOM 1295 NH2 ARG A 188 93.308 -5.337 38.122 1.00 68.64 N ANISOU 1295 NH2 ARG A 188 13658 7004 5417 -1016 250 -891 N ATOM 1296 N PHE A 189 96.531 -5.765 31.003 1.00 69.51 N ANISOU 1296 N PHE A 189 14484 6886 5040 -825 625 -1097 N ATOM 1297 CA PHE A 189 95.770 -5.615 29.766 1.00 70.94 C ANISOU 1297 CA PHE A 189 14775 7164 5017 -931 548 -1179 C ATOM 1298 C PHE A 189 94.459 -6.386 29.863 1.00 75.28 C ANISOU 1298 C PHE A 189 15334 7787 5480 -1136 444 -1299 C ATOM 1299 O PHE A 189 94.457 -7.609 30.029 1.00 75.54 O ANISOU 1299 O PHE A 189 15519 7666 5518 -1251 551 -1383 O ATOM 1300 CB PHE A 189 96.597 -6.070 28.552 1.00 74.61 C ANISOU 1300 CB PHE A 189 15465 7509 5376 -911 714 -1237 C ATOM 1301 CG PHE A 189 97.865 -5.272 28.353 1.00 76.16 C ANISOU 1301 CG PHE A 189 15626 7680 5634 -759 843 -1151 C ATOM 1302 CD1 PHE A 189 99.082 -5.737 28.838 1.00 79.59 C ANISOU 1302 CD1 PHE A 189 16016 8010 6215 -636 1016 -1131 C ATOM 1303 CD2 PHE A 189 97.839 -4.044 27.701 1.00 78.71 C ANISOU 1303 CD2 PHE A 189 15963 8096 5849 -738 797 -1097 C ATOM 1304 CE1 PHE A 189 100.253 -4.993 28.662 1.00 80.66 C ANISOU 1304 CE1 PHE A 189 16065 8183 6400 -542 1146 -1085 C ATOM 1305 CE2 PHE A 189 99.010 -3.300 27.528 1.00 81.67 C ANISOU 1305 CE2 PHE A 189 16322 8443 6264 -665 953 -1040 C ATOM 1306 CZ PHE A 189 100.209 -3.783 28.004 1.00 79.84 C ANISOU 1306 CZ PHE A 189 15990 8155 6191 -592 1129 -1047 C ATOM 1307 N TYR A 190 93.344 -5.642 29.779 1.00 71.81 N ANISOU 1307 N TYR A 190 14741 7594 4951 -1178 244 -1313 N ATOM 1308 CA TYR A 190 91.974 -6.144 29.884 1.00 72.91 C ANISOU 1308 CA TYR A 190 14789 7917 4996 -1391 118 -1448 C ATOM 1309 C TYR A 190 91.383 -6.434 28.492 1.00 78.58 C ANISOU 1309 C TYR A 190 15623 8774 5459 -1520 44 -1596 C ATOM 1310 O TYR A 190 91.785 -5.771 27.532 1.00 78.34 O ANISOU 1310 O TYR A 190 15691 8764 5313 -1378 20 -1547 O ATOM 1311 CB TYR A 190 91.096 -5.125 30.635 1.00 73.37 C ANISOU 1311 CB TYR A 190 14560 8225 5094 -1313 -65 -1391 C ATOM 1312 CG TYR A 190 91.621 -4.740 32.002 1.00 73.05 C ANISOU 1312 CG TYR A 190 14413 8067 5276 -1198 -7 -1254 C ATOM 1313 CD1 TYR A 190 92.375 -3.584 32.182 1.00 73.55 C ANISOU 1313 CD1 TYR A 190 14448 8086 5411 -976 -4 -1103 C ATOM 1314 CD2 TYR A 190 91.365 -5.531 33.118 1.00 73.58 C ANISOU 1314 CD2 TYR A 190 14439 8062 5458 -1334 55 -1284 C ATOM 1315 CE1 TYR A 190 92.855 -3.219 33.438 1.00 72.40 C ANISOU 1315 CE1 TYR A 190 14202 7860 5449 -895 38 -997 C ATOM 1316 CE2 TYR A 190 91.847 -5.181 34.379 1.00 72.72 C ANISOU 1316 CE2 TYR A 190 14247 7858 5525 -1221 94 -1160 C ATOM 1317 CZ TYR A 190 92.589 -4.020 34.534 1.00 78.19 C ANISOU 1317 CZ TYR A 190 14879 8542 6289 -1003 74 -1023 C ATOM 1318 OH TYR A 190 93.062 -3.660 35.771 1.00 77.52 O ANISOU 1318 OH TYR A 190 14708 8390 6357 -916 101 -920 O ATOM 1319 N PRO A 191 90.423 -7.393 28.354 1.00 76.95 N ANISOU 1319 N PRO A 191 15422 8676 5139 -1813 12 -1786 N ATOM 1320 CA PRO A 191 89.865 -7.694 27.020 1.00 79.51 C ANISOU 1320 CA PRO A 191 15851 9166 5194 -1962 -73 -1950 C ATOM 1321 C PRO A 191 89.079 -6.531 26.397 1.00 84.16 C ANISOU 1321 C PRO A 191 16238 10133 5607 -1805 -340 -1935 C ATOM 1322 O PRO A 191 89.082 -6.403 25.170 1.00 85.30 O ANISOU 1322 O PRO A 191 16531 10355 5526 -1777 -404 -1984 O ATOM 1323 CB PRO A 191 88.929 -8.879 27.284 1.00 83.46 C ANISOU 1323 CB PRO A 191 16345 9737 5628 -2355 -47 -2169 C ATOM 1324 CG PRO A 191 88.615 -8.813 28.733 1.00 86.25 C ANISOU 1324 CG PRO A 191 16490 10096 6185 -2373 -32 -2109 C ATOM 1325 CD PRO A 191 89.850 -8.287 29.382 1.00 78.74 C ANISOU 1325 CD PRO A 191 15597 8865 5453 -2056 76 -1875 C ATOM 1326 N ASN A 192 88.407 -5.696 27.225 1.00 79.77 N ANISOU 1326 N ASN A 192 15375 9805 5130 -1677 -492 -1867 N ATOM 1327 CA ASN A 192 87.627 -4.542 26.762 1.00 80.55 C ANISOU 1327 CA ASN A 192 15292 10259 5055 -1447 -747 -1836 C ATOM 1328 C ASN A 192 87.593 -3.437 27.843 1.00 81.85 C ANISOU 1328 C ASN A 192 15263 10447 5391 -1184 -793 -1661 C ATOM 1329 O ASN A 192 88.032 -3.666 28.971 1.00 79.07 O ANISOU 1329 O ASN A 192 14871 9890 5281 -1238 -651 -1596 O ATOM 1330 CB ASN A 192 86.204 -4.957 26.349 1.00 84.62 C ANISOU 1330 CB ASN A 192 15569 11232 5352 -1652 -955 -2070 C ATOM 1331 CG ASN A 192 85.429 -5.703 27.400 1.00109.02 C ANISOU 1331 CG ASN A 192 18404 14453 8566 -1955 -919 -2214 C ATOM 1332 OD1 ASN A 192 84.929 -5.123 28.363 1.00103.82 O ANISOU 1332 OD1 ASN A 192 17469 13953 8027 -1841 -984 -2158 O ATOM 1333 ND2 ASN A 192 85.267 -7.004 27.208 1.00102.49 N ANISOU 1333 ND2 ASN A 192 17695 13561 7686 -2365 -800 -2415 N ATOM 1334 N ASP A 193 87.084 -2.239 27.474 1.00 79.31 N ANISOU 1334 N ASP A 193 14860 10359 4916 -881 -988 -1585 N ATOM 1335 CA ASP A 193 86.999 -1.038 28.314 1.00 77.77 C ANISOU 1335 CA ASP A 193 14549 10179 4821 -588 -1035 -1421 C ATOM 1336 C ASP A 193 86.078 -1.203 29.538 1.00 81.13 C ANISOU 1336 C ASP A 193 14613 10827 5384 -676 -1088 -1494 C ATOM 1337 O ASP A 193 86.269 -0.475 30.516 1.00 78.89 O ANISOU 1337 O ASP A 193 14276 10441 5259 -513 -1044 -1361 O ATOM 1338 CB ASP A 193 86.508 0.162 27.489 1.00 81.82 C ANISOU 1338 CB ASP A 193 15118 10901 5068 -224 -1237 -1347 C ATOM 1339 CG ASP A 193 87.515 0.679 26.478 1.00 93.58 C ANISOU 1339 CG ASP A 193 17018 12111 6428 -85 -1144 -1219 C ATOM 1340 OD1 ASP A 193 88.664 0.980 26.881 1.00 91.90 O ANISOU 1340 OD1 ASP A 193 16993 11534 6392 -82 -930 -1084 O ATOM 1341 OD2 ASP A 193 87.134 0.855 25.299 1.00102.29 O ANISOU 1341 OD2 ASP A 193 18248 13385 7234 30 -1289 -1257 O ATOM 1342 N LEU A 194 85.094 -2.132 29.495 1.00 79.47 N ANISOU 1342 N LEU A 194 14171 10921 5103 -957 -1164 -1716 N ATOM 1343 CA LEU A 194 84.172 -2.373 30.615 1.00 79.56 C ANISOU 1343 CA LEU A 194 13836 11169 5225 -1100 -1181 -1817 C ATOM 1344 C LEU A 194 84.921 -2.971 31.822 1.00 80.49 C ANISOU 1344 C LEU A 194 14056 10903 5623 -1289 -937 -1749 C ATOM 1345 O LEU A 194 84.562 -2.667 32.960 1.00 78.88 O ANISOU 1345 O LEU A 194 13660 10755 5554 -1256 -916 -1715 O ATOM 1346 CB LEU A 194 82.999 -3.280 30.210 1.00 83.06 C ANISOU 1346 CB LEU A 194 14021 12036 5502 -1432 -1286 -2103 C ATOM 1347 CG LEU A 194 81.772 -2.606 29.573 1.00 91.22 C ANISOU 1347 CG LEU A 194 14721 13662 6278 -1220 -1585 -2214 C ATOM 1348 CD1 LEU A 194 82.059 -2.091 28.164 1.00 92.61 C ANISOU 1348 CD1 LEU A 194 15127 13862 6198 -955 -1737 -2152 C ATOM 1349 CD2 LEU A 194 80.609 -3.573 29.504 1.00 97.30 C ANISOU 1349 CD2 LEU A 194 15150 14889 6930 -1639 -1650 -2533 C ATOM 1350 N TRP A 195 85.971 -3.784 31.573 1.00 76.01 N ANISOU 1350 N TRP A 195 13801 9956 5124 -1447 -755 -1724 N ATOM 1351 CA TRP A 195 86.828 -4.355 32.616 1.00 73.48 C ANISOU 1351 CA TRP A 195 13624 9261 5033 -1549 -537 -1641 C ATOM 1352 C TRP A 195 87.749 -3.282 33.192 1.00 74.12 C ANISOU 1352 C TRP A 195 13763 9137 5262 -1236 -502 -1413 C ATOM 1353 O TRP A 195 88.026 -3.287 34.390 1.00 71.96 O ANISOU 1353 O TRP A 195 13452 8725 5164 -1239 -413 -1338 O ATOM 1354 CB TRP A 195 87.660 -5.523 32.071 1.00 72.52 C ANISOU 1354 CB TRP A 195 13823 8829 4904 -1741 -363 -1691 C ATOM 1355 CG TRP A 195 86.869 -6.753 31.754 1.00 76.43 C ANISOU 1355 CG TRP A 195 14338 9428 5273 -2131 -327 -1926 C ATOM 1356 CD1 TRP A 195 86.136 -6.987 30.629 1.00 82.10 C ANISOU 1356 CD1 TRP A 195 15013 10423 5759 -2283 -450 -2107 C ATOM 1357 CD2 TRP A 195 86.798 -7.951 32.538 1.00 76.92 C ANISOU 1357 CD2 TRP A 195 14528 9291 5407 -2442 -137 -2015 C ATOM 1358 NE1 TRP A 195 85.581 -8.245 30.678 1.00 83.96 N ANISOU 1358 NE1 TRP A 195 15314 10662 5923 -2713 -343 -2323 N ATOM 1359 CE2 TRP A 195 85.972 -8.861 31.839 1.00 84.14 C ANISOU 1359 CE2 TRP A 195 15471 10369 6128 -2818 -135 -2266 C ATOM 1360 CE3 TRP A 195 87.338 -8.341 33.777 1.00 76.68 C ANISOU 1360 CE3 TRP A 195 14615 8959 5560 -2442 33 -1910 C ATOM 1361 CZ2 TRP A 195 85.673 -10.135 32.336 1.00 85.20 C ANISOU 1361 CZ2 TRP A 195 15786 10336 6248 -3219 62 -2415 C ATOM 1362 CZ3 TRP A 195 87.042 -9.605 34.267 1.00 79.84 C ANISOU 1362 CZ3 TRP A 195 15207 9190 5939 -2789 214 -2037 C ATOM 1363 CH2 TRP A 195 86.220 -10.486 33.551 1.00 83.75 C ANISOU 1363 CH2 TRP A 195 15764 9814 6241 -3186 244 -2288 C ATOM 1364 N VAL A 196 88.221 -2.361 32.328 1.00 70.33 N ANISOU 1364 N VAL A 196 13400 8635 4686 -990 -563 -1312 N ATOM 1365 CA VAL A 196 89.123 -1.258 32.677 1.00 68.01 C ANISOU 1365 CA VAL A 196 13205 8150 4487 -740 -512 -1121 C ATOM 1366 C VAL A 196 88.437 -0.322 33.691 1.00 71.34 C ANISOU 1366 C VAL A 196 13420 8720 4965 -584 -599 -1060 C ATOM 1367 O VAL A 196 89.045 0.013 34.705 1.00 69.01 O ANISOU 1367 O VAL A 196 13137 8246 4837 -544 -504 -957 O ATOM 1368 CB VAL A 196 89.590 -0.467 31.415 1.00 72.46 C ANISOU 1368 CB VAL A 196 13982 8672 4877 -552 -543 -1051 C ATOM 1369 CG1 VAL A 196 90.595 0.626 31.778 1.00 70.56 C ANISOU 1369 CG1 VAL A 196 13880 8206 4722 -374 -440 -878 C ATOM 1370 CG2 VAL A 196 90.180 -1.394 30.355 1.00 73.06 C ANISOU 1370 CG2 VAL A 196 14260 8625 4873 -703 -451 -1129 C ATOM 1371 N VAL A 197 87.169 0.056 33.425 1.00 69.74 N ANISOU 1371 N VAL A 197 13019 8869 4611 -491 -780 -1140 N ATOM 1372 CA VAL A 197 86.393 1.006 34.223 1.00 69.63 C ANISOU 1372 CA VAL A 197 12808 9040 4608 -283 -870 -1097 C ATOM 1373 C VAL A 197 85.826 0.342 35.527 1.00 72.59 C ANISOU 1373 C VAL A 197 12937 9502 5142 -499 -811 -1183 C ATOM 1374 O VAL A 197 85.578 1.080 36.483 1.00 71.65 O ANISOU 1374 O VAL A 197 12717 9407 5098 -352 -808 -1115 O ATOM 1375 CB VAL A 197 85.264 1.647 33.363 1.00 76.60 C ANISOU 1375 CB VAL A 197 13556 10312 5238 -39 -1094 -1157 C ATOM 1376 CG1 VAL A 197 84.096 0.694 33.116 1.00 79.00 C ANISOU 1376 CG1 VAL A 197 13545 11025 5447 -268 -1209 -1389 C ATOM 1377 CG2 VAL A 197 84.783 2.969 33.952 1.00 76.84 C ANISOU 1377 CG2 VAL A 197 13522 10433 5239 324 -1164 -1053 C ATOM 1378 N VAL A 198 85.645 -1.004 35.592 1.00 69.37 N ANISOU 1378 N VAL A 198 12482 9107 4769 -849 -739 -1328 N ATOM 1379 CA VAL A 198 85.122 -1.615 36.829 1.00 69.01 C ANISOU 1379 CA VAL A 198 12268 9107 4845 -1073 -651 -1403 C ATOM 1380 C VAL A 198 86.261 -1.749 37.855 1.00 70.22 C ANISOU 1380 C VAL A 198 12624 8860 5195 -1085 -481 -1255 C ATOM 1381 O VAL A 198 86.008 -1.528 39.037 1.00 69.36 O ANISOU 1381 O VAL A 198 12413 8757 5185 -1084 -436 -1224 O ATOM 1382 CB VAL A 198 84.352 -2.957 36.687 1.00 75.04 C ANISOU 1382 CB VAL A 198 12931 10035 5545 -1478 -608 -1628 C ATOM 1383 CG1 VAL A 198 83.014 -2.754 35.992 1.00 78.09 C ANISOU 1383 CG1 VAL A 198 12989 10943 5738 -1485 -796 -1811 C ATOM 1384 CG2 VAL A 198 85.175 -4.050 36.011 1.00 74.70 C ANISOU 1384 CG2 VAL A 198 13198 9696 5487 -1689 -491 -1658 C ATOM 1385 N PHE A 199 87.497 -2.075 37.415 1.00 65.46 N ANISOU 1385 N PHE A 199 12289 7948 4635 -1078 -393 -1173 N ATOM 1386 CA PHE A 199 88.642 -2.183 38.323 1.00 63.32 C ANISOU 1386 CA PHE A 199 12171 7361 4527 -1049 -260 -1044 C ATOM 1387 C PHE A 199 89.190 -0.790 38.651 1.00 66.24 C ANISOU 1387 C PHE A 199 12545 7679 4944 -785 -294 -894 C ATOM 1388 O PHE A 199 89.891 -0.628 39.653 1.00 64.39 O ANISOU 1388 O PHE A 199 12352 7281 4833 -756 -220 -803 O ATOM 1389 CB PHE A 199 89.743 -3.088 37.753 1.00 64.83 C ANISOU 1389 CB PHE A 199 12605 7290 4735 -1117 -145 -1035 C ATOM 1390 CG PHE A 199 89.382 -4.554 37.791 1.00 67.75 C ANISOU 1390 CG PHE A 199 13073 7595 5076 -1393 -50 -1164 C ATOM 1391 CD1 PHE A 199 89.423 -5.268 38.983 1.00 70.59 C ANISOU 1391 CD1 PHE A 199 13498 7804 5520 -1508 63 -1153 C ATOM 1392 CD2 PHE A 199 89.022 -5.229 36.631 1.00 71.67 C ANISOU 1392 CD2 PHE A 199 13644 8153 5432 -1549 -57 -1301 C ATOM 1393 CE1 PHE A 199 89.074 -6.620 39.020 1.00 73.25 C ANISOU 1393 CE1 PHE A 199 14004 8029 5799 -1783 186 -1273 C ATOM 1394 CE2 PHE A 199 88.688 -6.585 36.666 1.00 76.22 C ANISOU 1394 CE2 PHE A 199 14368 8633 5959 -1844 62 -1437 C ATOM 1395 CZ PHE A 199 88.720 -7.272 37.860 1.00 74.24 C ANISOU 1395 CZ PHE A 199 14215 8203 5791 -1962 194 -1419 C ATOM 1396 N GLN A 200 88.836 0.214 37.824 1.00 63.96 N ANISOU 1396 N GLN A 200 12238 7531 4532 -597 -403 -874 N ATOM 1397 CA GLN A 200 89.189 1.621 38.013 1.00 63.17 C ANISOU 1397 CA GLN A 200 12207 7369 4426 -358 -419 -747 C ATOM 1398 C GLN A 200 88.387 2.176 39.193 1.00 66.99 C ANISOU 1398 C GLN A 200 12524 7974 4956 -286 -449 -739 C ATOM 1399 O GLN A 200 88.944 2.897 40.016 1.00 65.36 O ANISOU 1399 O GLN A 200 12391 7617 4828 -211 -388 -642 O ATOM 1400 CB GLN A 200 88.916 2.411 36.715 1.00 66.07 C ANISOU 1400 CB GLN A 200 12673 7832 4597 -162 -517 -731 C ATOM 1401 CG GLN A 200 89.417 3.855 36.688 1.00 83.30 C ANISOU 1401 CG GLN A 200 15053 9869 6727 68 -490 -596 C ATOM 1402 CD GLN A 200 89.135 4.540 35.364 1.00105.07 C ANISOU 1402 CD GLN A 200 17981 12690 9252 275 -576 -571 C ATOM 1403 OE1 GLN A 200 89.371 3.994 34.276 1.00101.35 O ANISOU 1403 OE1 GLN A 200 17597 12223 8689 205 -586 -614 O ATOM 1404 NE2 GLN A 200 88.675 5.782 35.428 1.00 97.74 N ANISOU 1404 NE2 GLN A 200 17153 11781 8202 556 -626 -494 N ATOM 1405 N PHE A 201 87.091 1.795 39.286 1.00 65.20 N ANISOU 1405 N PHE A 201 12062 8038 4673 -337 -530 -861 N ATOM 1406 CA PHE A 201 86.146 2.206 40.328 1.00 65.66 C ANISOU 1406 CA PHE A 201 11913 8277 4757 -278 -548 -890 C ATOM 1407 C PHE A 201 86.270 1.311 41.582 1.00 68.18 C ANISOU 1407 C PHE A 201 12192 8490 5223 -535 -422 -917 C ATOM 1408 O PHE A 201 85.943 1.771 42.680 1.00 67.44 O ANISOU 1408 O PHE A 201 12022 8421 5183 -486 -385 -893 O ATOM 1409 CB PHE A 201 84.706 2.174 39.773 1.00 70.36 C ANISOU 1409 CB PHE A 201 12229 9300 5205 -224 -687 -1036 C ATOM 1410 CG PHE A 201 83.587 2.557 40.718 1.00 73.42 C ANISOU 1410 CG PHE A 201 12339 9961 5598 -148 -702 -1102 C ATOM 1411 CD1 PHE A 201 83.582 3.793 41.357 1.00 76.34 C ANISOU 1411 CD1 PHE A 201 12764 10268 5974 152 -694 -990 C ATOM 1412 CD2 PHE A 201 82.485 1.728 40.885 1.00 77.78 C ANISOU 1412 CD2 PHE A 201 12575 10856 6121 -378 -713 -1296 C ATOM 1413 CE1 PHE A 201 82.536 4.151 42.215 1.00 78.78 C ANISOU 1413 CE1 PHE A 201 12815 10838 6278 248 -691 -1059 C ATOM 1414 CE2 PHE A 201 81.435 2.091 41.734 1.00 82.25 C ANISOU 1414 CE2 PHE A 201 12850 11716 6685 -310 -708 -1375 C ATOM 1415 CZ PHE A 201 81.464 3.302 42.388 1.00 79.86 C ANISOU 1415 CZ PHE A 201 12601 11342 6400 26 -700 -1252 C ATOM 1416 N GLN A 202 86.757 0.057 41.423 1.00 64.13 N ANISOU 1416 N GLN A 202 11778 7836 4754 -786 -344 -962 N ATOM 1417 CA GLN A 202 86.964 -0.892 42.526 1.00 63.25 C ANISOU 1417 CA GLN A 202 11721 7568 4741 -1006 -213 -972 C ATOM 1418 C GLN A 202 88.132 -0.431 43.418 1.00 65.12 C ANISOU 1418 C GLN A 202 12116 7539 5087 -890 -155 -816 C ATOM 1419 O GLN A 202 88.052 -0.557 44.640 1.00 64.26 O ANISOU 1419 O GLN A 202 12005 7376 5035 -949 -90 -793 O ATOM 1420 CB GLN A 202 87.225 -2.310 41.985 1.00 65.15 C ANISOU 1420 CB GLN A 202 12104 7688 4960 -1252 -136 -1053 C ATOM 1421 CG GLN A 202 87.237 -3.403 43.055 1.00 77.97 C ANISOU 1421 CG GLN A 202 13846 9145 6634 -1482 13 -1076 C ATOM 1422 CD GLN A 202 88.459 -4.285 42.969 1.00 94.03 C ANISOU 1422 CD GLN A 202 16178 10845 8703 -1491 109 -1005 C ATOM 1423 OE1 GLN A 202 88.367 -5.484 42.689 1.00 90.60 O ANISOU 1423 OE1 GLN A 202 15912 10296 8214 -1700 209 -1091 O ATOM 1424 NE2 GLN A 202 89.634 -3.716 43.218 1.00 83.57 N ANISOU 1424 NE2 GLN A 202 14930 9366 7457 -1264 91 -859 N ATOM 1425 N HIS A 203 89.205 0.106 42.797 1.00 60.68 N ANISOU 1425 N HIS A 203 11685 6834 4534 -745 -173 -723 N ATOM 1426 CA HIS A 203 90.400 0.613 43.475 1.00 58.90 C ANISOU 1426 CA HIS A 203 11572 6416 4391 -658 -128 -606 C ATOM 1427 C HIS A 203 90.071 1.841 44.336 1.00 60.89 C ANISOU 1427 C HIS A 203 11772 6716 4647 -538 -149 -556 C ATOM 1428 O HIS A 203 90.629 1.980 45.425 1.00 59.54 O ANISOU 1428 O HIS A 203 11644 6441 4539 -552 -106 -501 O ATOM 1429 CB HIS A 203 91.489 0.961 42.445 1.00 59.57 C ANISOU 1429 CB HIS A 203 11776 6399 4460 -576 -122 -558 C ATOM 1430 CG HIS A 203 92.717 1.578 43.041 1.00 62.34 C ANISOU 1430 CG HIS A 203 12191 6618 4875 -524 -75 -472 C ATOM 1431 ND1 HIS A 203 93.688 0.806 43.652 1.00 63.90 N ANISOU 1431 ND1 HIS A 203 12415 6715 5149 -567 -23 -450 N ATOM 1432 CD2 HIS A 203 93.091 2.879 43.098 1.00 64.17 C ANISOU 1432 CD2 HIS A 203 12474 6824 5085 -440 -70 -420 C ATOM 1433 CE1 HIS A 203 94.615 1.657 44.063 1.00 63.04 C ANISOU 1433 CE1 HIS A 203 12312 6574 5067 -526 -6 -400 C ATOM 1434 NE2 HIS A 203 94.299 2.916 43.752 1.00 63.47 N ANISOU 1434 NE2 HIS A 203 12400 6650 5064 -480 -18 -385 N ATOM 1435 N ILE A 204 89.172 2.720 43.849 1.00 57.44 N ANISOU 1435 N ILE A 204 11262 6440 4122 -397 -218 -578 N ATOM 1436 CA ILE A 204 88.752 3.948 44.537 1.00 57.18 C ANISOU 1436 CA ILE A 204 11221 6441 4063 -234 -224 -537 C ATOM 1437 C ILE A 204 87.983 3.579 45.831 1.00 60.33 C ANISOU 1437 C ILE A 204 11481 6931 4510 -325 -183 -585 C ATOM 1438 O ILE A 204 88.171 4.245 46.850 1.00 59.28 O ANISOU 1438 O ILE A 204 11406 6716 4403 -277 -138 -534 O ATOM 1439 CB ILE A 204 87.905 4.868 43.597 1.00 61.92 C ANISOU 1439 CB ILE A 204 11799 7204 4523 6 -312 -550 C ATOM 1440 CG1 ILE A 204 88.681 5.213 42.300 1.00 62.37 C ANISOU 1440 CG1 ILE A 204 12052 7142 4504 78 -330 -498 C ATOM 1441 CG2 ILE A 204 87.473 6.159 44.313 1.00 63.19 C ANISOU 1441 CG2 ILE A 204 12008 7362 4638 223 -296 -504 C ATOM 1442 CD1 ILE A 204 87.844 5.871 41.150 1.00 72.51 C ANISOU 1442 CD1 ILE A 204 13352 8594 5604 329 -439 -509 C ATOM 1443 N MET A 205 87.153 2.516 45.798 1.00 57.13 N ANISOU 1443 N MET A 205 10920 6686 4102 -489 -179 -692 N ATOM 1444 CA MET A 205 86.378 2.085 46.963 1.00 57.24 C ANISOU 1444 CA MET A 205 10817 6790 4141 -623 -105 -754 C ATOM 1445 C MET A 205 87.273 1.401 48.009 1.00 58.64 C ANISOU 1445 C MET A 205 11168 6718 4394 -773 -13 -688 C ATOM 1446 O MET A 205 87.544 1.999 49.048 1.00 57.17 O ANISOU 1446 O MET A 205 11043 6449 4231 -713 20 -624 O ATOM 1447 CB MET A 205 85.224 1.147 46.555 1.00 61.63 C ANISOU 1447 CB MET A 205 11165 7604 4646 -814 -101 -915 C ATOM 1448 CG MET A 205 84.045 1.863 45.927 1.00 67.54 C ANISOU 1448 CG MET A 205 11651 8712 5298 -639 -202 -1008 C ATOM 1449 SD MET A 205 83.155 2.925 47.098 1.00 73.08 S ANISOU 1449 SD MET A 205 12191 9587 5991 -444 -162 -1017 S ATOM 1450 CE MET A 205 81.880 3.563 46.050 1.00 72.77 C ANISOU 1450 CE MET A 205 11836 10007 5806 -176 -313 -1132 C ATOM 1451 N VAL A 206 87.752 0.178 47.707 1.00 54.94 N ANISOU 1451 N VAL A 206 10805 6129 3942 -938 25 -702 N ATOM 1452 CA VAL A 206 88.556 -0.711 48.561 1.00 54.15 C ANISOU 1452 CA VAL A 206 10899 5801 3876 -1040 104 -643 C ATOM 1453 C VAL A 206 89.877 -0.038 49.042 1.00 56.66 C ANISOU 1453 C VAL A 206 11327 5964 4238 -880 67 -516 C ATOM 1454 O VAL A 206 90.297 -0.295 50.174 1.00 56.50 O ANISOU 1454 O VAL A 206 11410 5836 4221 -899 104 -462 O ATOM 1455 CB VAL A 206 88.875 -2.046 47.822 1.00 58.51 C ANISOU 1455 CB VAL A 206 11584 6237 4411 -1175 149 -681 C ATOM 1456 CG1 VAL A 206 89.599 -3.034 48.733 1.00 58.40 C ANISOU 1456 CG1 VAL A 206 11815 5978 4395 -1224 238 -615 C ATOM 1457 CG2 VAL A 206 87.605 -2.689 47.268 1.00 60.17 C ANISOU 1457 CG2 VAL A 206 11681 6624 4556 -1393 188 -839 C ATOM 1458 N GLY A 207 90.505 0.790 48.205 1.00 51.94 N ANISOU 1458 N GLY A 207 10714 5370 3652 -746 1 -481 N ATOM 1459 CA GLY A 207 91.779 1.415 48.551 1.00 50.65 C ANISOU 1459 CA GLY A 207 10625 5102 3517 -658 -18 -399 C ATOM 1460 C GLY A 207 91.824 2.899 48.854 1.00 54.00 C ANISOU 1460 C GLY A 207 11046 5549 3923 -568 -35 -371 C ATOM 1461 O GLY A 207 92.919 3.424 49.082 1.00 53.04 O ANISOU 1461 O GLY A 207 10983 5360 3812 -553 -38 -330 O ATOM 1462 N LEU A 208 90.667 3.603 48.867 1.00 51.15 N ANISOU 1462 N LEU A 208 10625 5292 3520 -506 -36 -404 N ATOM 1463 CA LEU A 208 90.680 5.044 49.137 1.00 51.02 C ANISOU 1463 CA LEU A 208 10679 5247 3460 -391 -28 -375 C ATOM 1464 C LEU A 208 89.412 5.516 49.883 1.00 55.30 C ANISOU 1464 C LEU A 208 11153 5897 3963 -317 -1 -410 C ATOM 1465 O LEU A 208 89.555 6.191 50.904 1.00 54.98 O ANISOU 1465 O LEU A 208 11198 5787 3905 -306 42 -389 O ATOM 1466 CB LEU A 208 90.841 5.837 47.819 1.00 51.48 C ANISOU 1466 CB LEU A 208 10811 5288 3461 -272 -50 -361 C ATOM 1467 CG LEU A 208 91.015 7.365 47.905 1.00 56.97 C ANISOU 1467 CG LEU A 208 11688 5879 4077 -157 -8 -323 C ATOM 1468 CD1 LEU A 208 92.340 7.751 48.575 1.00 56.71 C ANISOU 1468 CD1 LEU A 208 11773 5706 4068 -299 45 -301 C ATOM 1469 CD2 LEU A 208 90.951 7.988 46.525 1.00 60.08 C ANISOU 1469 CD2 LEU A 208 12201 6250 4378 -20 -21 -305 C ATOM 1470 N ILE A 209 88.198 5.196 49.377 1.00 52.40 N ANISOU 1470 N ILE A 209 10619 5721 3567 -271 -23 -480 N ATOM 1471 CA ILE A 209 86.945 5.649 49.992 1.00 53.31 C ANISOU 1471 CA ILE A 209 10610 6005 3639 -174 10 -537 C ATOM 1472 C ILE A 209 86.654 4.832 51.267 1.00 57.07 C ANISOU 1472 C ILE A 209 11035 6493 4155 -370 95 -573 C ATOM 1473 O ILE A 209 86.616 5.433 52.337 1.00 57.16 O ANISOU 1473 O ILE A 209 11120 6447 4149 -336 156 -552 O ATOM 1474 CB ILE A 209 85.728 5.625 49.016 1.00 58.04 C ANISOU 1474 CB ILE A 209 10990 6887 4174 -48 -54 -625 C ATOM 1475 CG1 ILE A 209 85.931 6.644 47.865 1.00 58.91 C ANISOU 1475 CG1 ILE A 209 11222 6965 4198 212 -132 -570 C ATOM 1476 CG2 ILE A 209 84.403 5.905 49.766 1.00 60.45 C ANISOU 1476 CG2 ILE A 209 11089 7436 4441 35 -5 -713 C ATOM 1477 CD1 ILE A 209 84.804 6.701 46.787 1.00 69.14 C ANISOU 1477 CD1 ILE A 209 12313 8570 5388 401 -238 -648 C ATOM 1478 N LEU A 210 86.444 3.500 51.161 1.00 53.25 N ANISOU 1478 N LEU A 210 10475 6059 3699 -579 116 -628 N ATOM 1479 CA LEU A 210 86.086 2.631 52.294 1.00 53.40 C ANISOU 1479 CA LEU A 210 10502 6065 3721 -786 225 -664 C ATOM 1480 C LEU A 210 87.097 2.732 53.465 1.00 55.51 C ANISOU 1480 C LEU A 210 10995 6102 3996 -805 254 -562 C ATOM 1481 O LEU A 210 86.610 2.927 54.581 1.00 55.73 O ANISOU 1481 O LEU A 210 11038 6149 3990 -840 339 -579 O ATOM 1482 CB LEU A 210 85.921 1.160 51.883 1.00 54.11 C ANISOU 1482 CB LEU A 210 10586 6158 3814 -1026 265 -728 C ATOM 1483 CG LEU A 210 84.898 0.878 50.773 1.00 60.51 C ANISOU 1483 CG LEU A 210 11160 7238 4595 -1080 234 -863 C ATOM 1484 CD1 LEU A 210 84.820 -0.604 50.470 1.00 61.68 C ANISOU 1484 CD1 LEU A 210 11375 7334 4726 -1373 307 -937 C ATOM 1485 CD2 LEU A 210 83.520 1.447 51.106 1.00 64.71 C ANISOU 1485 CD2 LEU A 210 11414 8090 5082 -1036 270 -979 C ATOM 1486 N PRO A 211 88.454 2.675 53.297 1.00 50.18 N ANISOU 1486 N PRO A 211 10472 5248 3347 -775 187 -471 N ATOM 1487 CA PRO A 211 89.329 2.848 54.477 1.00 49.14 C ANISOU 1487 CA PRO A 211 10502 4976 3192 -782 190 -399 C ATOM 1488 C PRO A 211 89.254 4.273 55.027 1.00 51.60 C ANISOU 1488 C PRO A 211 10839 5296 3470 -677 197 -393 C ATOM 1489 O PRO A 211 89.389 4.467 56.234 1.00 51.41 O ANISOU 1489 O PRO A 211 10918 5218 3396 -714 234 -376 O ATOM 1490 CB PRO A 211 90.733 2.527 53.950 1.00 50.10 C ANISOU 1490 CB PRO A 211 10696 4994 3345 -752 106 -336 C ATOM 1491 CG PRO A 211 90.536 1.926 52.609 1.00 54.69 C ANISOU 1491 CG PRO A 211 11201 5612 3965 -761 91 -370 C ATOM 1492 CD PRO A 211 89.262 2.477 52.076 1.00 50.89 C ANISOU 1492 CD PRO A 211 10574 5290 3474 -732 109 -444 C ATOM 1493 N GLY A 212 88.999 5.237 54.136 1.00 47.04 N ANISOU 1493 N GLY A 212 10208 4769 2895 -541 172 -410 N ATOM 1494 CA GLY A 212 88.838 6.650 54.458 1.00 46.66 C ANISOU 1494 CA GLY A 212 10246 4691 2792 -410 203 -408 C ATOM 1495 C GLY A 212 87.640 6.913 55.348 1.00 50.32 C ANISOU 1495 C GLY A 212 10655 5253 3211 -365 297 -462 C ATOM 1496 O GLY A 212 87.715 7.777 56.221 1.00 50.19 O ANISOU 1496 O GLY A 212 10778 5155 3137 -324 354 -456 O ATOM 1497 N ILE A 213 86.533 6.153 55.151 1.00 47.00 N ANISOU 1497 N ILE A 213 10028 5022 2808 -398 330 -533 N ATOM 1498 CA ILE A 213 85.308 6.251 55.962 1.00 48.06 C ANISOU 1498 CA ILE A 213 10045 5313 2902 -385 444 -614 C ATOM 1499 C ILE A 213 85.614 5.737 57.381 1.00 51.31 C ANISOU 1499 C ILE A 213 10603 5605 3287 -574 530 -593 C ATOM 1500 O ILE A 213 85.259 6.401 58.351 1.00 51.47 O ANISOU 1500 O ILE A 213 10692 5616 3248 -525 621 -611 O ATOM 1501 CB ILE A 213 84.087 5.494 55.330 1.00 52.54 C ANISOU 1501 CB ILE A 213 10312 6170 3483 -435 465 -729 C ATOM 1502 CG1 ILE A 213 83.860 5.795 53.818 1.00 53.43 C ANISOU 1502 CG1 ILE A 213 10282 6424 3596 -257 342 -748 C ATOM 1503 CG2 ILE A 213 82.797 5.661 56.151 1.00 55.16 C ANISOU 1503 CG2 ILE A 213 10465 6725 3768 -424 603 -839 C ATOM 1504 CD1 ILE A 213 83.616 7.290 53.370 1.00 62.56 C ANISOU 1504 CD1 ILE A 213 11479 7607 4684 111 300 -720 C ATOM 1505 N VAL A 214 86.296 4.572 57.484 1.00 46.88 N ANISOU 1505 N VAL A 214 10126 4940 2748 -761 504 -550 N ATOM 1506 CA VAL A 214 86.677 3.897 58.733 1.00 46.69 C ANISOU 1506 CA VAL A 214 10288 4786 2666 -915 564 -511 C ATOM 1507 C VAL A 214 87.583 4.819 59.581 1.00 49.81 C ANISOU 1507 C VAL A 214 10874 5047 3004 -843 520 -448 C ATOM 1508 O VAL A 214 87.322 4.970 60.772 1.00 50.25 O ANISOU 1508 O VAL A 214 11043 5073 2976 -892 608 -456 O ATOM 1509 CB VAL A 214 87.363 2.528 58.447 1.00 50.10 C ANISOU 1509 CB VAL A 214 10816 5107 3112 -1042 523 -461 C ATOM 1510 CG1 VAL A 214 87.903 1.877 59.721 1.00 50.32 C ANISOU 1510 CG1 VAL A 214 11099 4978 3043 -1130 559 -393 C ATOM 1511 CG2 VAL A 214 86.408 1.576 57.729 1.00 50.89 C ANISOU 1511 CG2 VAL A 214 10775 5323 3239 -1184 599 -551 C ATOM 1512 N ILE A 215 88.609 5.445 58.971 1.00 45.10 N ANISOU 1512 N ILE A 215 10316 4383 2437 -758 401 -402 N ATOM 1513 CA ILE A 215 89.546 6.334 59.669 1.00 44.73 C ANISOU 1513 CA ILE A 215 10435 4236 2323 -748 358 -373 C ATOM 1514 C ILE A 215 88.819 7.639 60.078 1.00 50.14 C ANISOU 1514 C ILE A 215 11180 4918 2951 -653 459 -424 C ATOM 1515 O ILE A 215 88.973 8.073 61.223 1.00 50.14 O ANISOU 1515 O ILE A 215 11339 4856 2856 -701 505 -432 O ATOM 1516 CB ILE A 215 90.808 6.607 58.799 1.00 46.73 C ANISOU 1516 CB ILE A 215 10687 4448 2619 -733 237 -340 C ATOM 1517 CG1 ILE A 215 91.574 5.284 58.536 1.00 46.67 C ANISOU 1517 CG1 ILE A 215 10638 4445 2649 -781 149 -291 C ATOM 1518 CG2 ILE A 215 91.735 7.637 59.462 1.00 47.66 C ANISOU 1518 CG2 ILE A 215 10954 4501 2653 -782 210 -350 C ATOM 1519 CD1 ILE A 215 92.573 5.284 57.363 1.00 53.31 C ANISOU 1519 CD1 ILE A 215 11403 5294 3558 -752 59 -277 C ATOM 1520 N LEU A 216 88.012 8.231 59.168 1.00 48.01 N ANISOU 1520 N LEU A 216 10802 4719 2719 -494 495 -459 N ATOM 1521 CA LEU A 216 87.266 9.472 59.419 1.00 49.66 C ANISOU 1521 CA LEU A 216 11088 4921 2861 -322 598 -503 C ATOM 1522 C LEU A 216 86.215 9.286 60.532 1.00 55.66 C ANISOU 1522 C LEU A 216 11805 5773 3570 -334 736 -561 C ATOM 1523 O LEU A 216 86.161 10.121 61.437 1.00 56.49 O ANISOU 1523 O LEU A 216 12094 5787 3581 -297 826 -581 O ATOM 1524 CB LEU A 216 86.583 9.973 58.129 1.00 50.39 C ANISOU 1524 CB LEU A 216 11061 5106 2980 -89 583 -518 C ATOM 1525 CG LEU A 216 85.804 11.295 58.186 1.00 57.39 C ANISOU 1525 CG LEU A 216 12054 5976 3775 188 682 -550 C ATOM 1526 CD1 LEU A 216 86.739 12.496 58.348 1.00 57.83 C ANISOU 1526 CD1 LEU A 216 12474 5757 3743 195 712 -516 C ATOM 1527 CD2 LEU A 216 84.969 11.478 56.930 1.00 61.13 C ANISOU 1527 CD2 LEU A 216 12350 6619 4256 455 638 -566 C ATOM 1528 N SER A 217 85.401 8.202 60.470 1.00 52.67 N ANISOU 1528 N SER A 217 11205 5569 3239 -415 774 -602 N ATOM 1529 CA SER A 217 84.351 7.908 61.454 1.00 54.13 C ANISOU 1529 CA SER A 217 11320 5874 3374 -475 938 -677 C ATOM 1530 C SER A 217 84.941 7.606 62.844 1.00 58.77 C ANISOU 1530 C SER A 217 12159 6301 3870 -659 986 -638 C ATOM 1531 O SER A 217 84.271 7.883 63.838 1.00 59.93 O ANISOU 1531 O SER A 217 12358 6477 3935 -667 1140 -693 O ATOM 1532 CB SER A 217 83.473 6.748 60.995 1.00 58.07 C ANISOU 1532 CB SER A 217 11546 6590 3928 -602 981 -747 C ATOM 1533 OG SER A 217 84.231 5.592 60.679 1.00 65.38 O ANISOU 1533 OG SER A 217 12530 7415 4896 -797 895 -687 O ATOM 1534 N CYS A 218 86.184 7.068 62.915 1.00 54.54 N ANISOU 1534 N CYS A 218 11774 5618 3332 -779 854 -550 N ATOM 1535 CA CYS A 218 86.884 6.794 64.179 1.00 54.78 C ANISOU 1535 CA CYS A 218 12050 5520 3244 -909 850 -504 C ATOM 1536 C CYS A 218 87.298 8.113 64.824 1.00 59.92 C ANISOU 1536 C CYS A 218 12888 6077 3801 -846 855 -520 C ATOM 1537 O CYS A 218 86.928 8.372 65.966 1.00 60.83 O ANISOU 1537 O CYS A 218 13151 6163 3799 -887 972 -552 O ATOM 1538 CB CYS A 218 88.090 5.881 63.968 1.00 53.90 C ANISOU 1538 CB CYS A 218 12005 5331 3142 -985 686 -415 C ATOM 1539 SG CYS A 218 87.679 4.128 63.793 1.00 58.08 S ANISOU 1539 SG CYS A 218 12507 5869 3693 -1116 739 -391 S ATOM 1540 N TYR A 219 88.036 8.958 64.071 1.00 56.23 N ANISOU 1540 N TYR A 219 12441 5553 3372 -769 753 -508 N ATOM 1541 CA TYR A 219 88.518 10.271 64.497 1.00 56.95 C ANISOU 1541 CA TYR A 219 12750 5525 3365 -751 772 -539 C ATOM 1542 C TYR A 219 87.364 11.157 64.991 1.00 63.02 C ANISOU 1542 C TYR A 219 13596 6280 4067 -612 967 -609 C ATOM 1543 O TYR A 219 87.493 11.771 66.050 1.00 63.57 O ANISOU 1543 O TYR A 219 13899 6253 4001 -667 1042 -645 O ATOM 1544 CB TYR A 219 89.263 10.958 63.333 1.00 57.38 C ANISOU 1544 CB TYR A 219 12804 5520 3478 -704 684 -528 C ATOM 1545 CG TYR A 219 89.556 12.430 63.542 1.00 60.44 C ANISOU 1545 CG TYR A 219 13458 5750 3757 -689 759 -578 C ATOM 1546 CD1 TYR A 219 90.624 12.844 64.333 1.00 63.04 C ANISOU 1546 CD1 TYR A 219 13982 6005 3967 -894 714 -610 C ATOM 1547 CD2 TYR A 219 88.795 13.409 62.908 1.00 62.13 C ANISOU 1547 CD2 TYR A 219 13750 5891 3967 -469 874 -600 C ATOM 1548 CE1 TYR A 219 90.901 14.198 64.524 1.00 65.36 C ANISOU 1548 CE1 TYR A 219 14567 6127 4140 -937 810 -677 C ATOM 1549 CE2 TYR A 219 89.061 14.765 63.092 1.00 64.55 C ANISOU 1549 CE2 TYR A 219 14387 5993 4147 -455 976 -644 C ATOM 1550 CZ TYR A 219 90.119 15.155 63.898 1.00 73.14 C ANISOU 1550 CZ TYR A 219 15691 6981 5119 -719 956 -689 C ATOM 1551 OH TYR A 219 90.393 16.492 64.073 1.00 76.69 O ANISOU 1551 OH TYR A 219 16509 7204 5424 -760 1082 -752 O ATOM 1552 N CYS A 220 86.242 11.194 64.240 1.00 60.66 N ANISOU 1552 N CYS A 220 13093 6104 3850 -420 1044 -638 N ATOM 1553 CA CYS A 220 85.069 12.023 64.520 1.00 62.80 C ANISOU 1553 CA CYS A 220 13373 6421 4066 -204 1223 -711 C ATOM 1554 C CYS A 220 84.308 11.557 65.781 1.00 67.97 C ANISOU 1554 C CYS A 220 14017 7160 4649 -298 1382 -767 C ATOM 1555 O CYS A 220 83.536 12.354 66.321 1.00 69.74 O ANISOU 1555 O CYS A 220 14316 7391 4792 -139 1552 -836 O ATOM 1556 CB CYS A 220 84.137 12.058 63.315 1.00 63.76 C ANISOU 1556 CB CYS A 220 13216 6729 4280 42 1221 -734 C ATOM 1557 SG CYS A 220 83.841 13.724 62.663 1.00 69.45 S ANISOU 1557 SG CYS A 220 14132 7332 4925 428 1280 -744 S ATOM 1558 N ILE A 221 84.508 10.310 66.253 1.00 63.59 N ANISOU 1558 N ILE A 221 13409 6649 4103 -536 1351 -738 N ATOM 1559 CA ILE A 221 83.812 9.851 67.463 1.00 64.95 C ANISOU 1559 CA ILE A 221 13627 6872 4179 -657 1529 -787 C ATOM 1560 C ILE A 221 84.824 9.790 68.642 1.00 67.05 C ANISOU 1560 C ILE A 221 14233 6950 4293 -837 1480 -736 C ATOM 1561 O ILE A 221 84.392 9.751 69.795 1.00 68.09 O ANISOU 1561 O ILE A 221 14513 7065 4293 -915 1635 -774 O ATOM 1562 CB ILE A 221 83.028 8.517 67.281 1.00 68.85 C ANISOU 1562 CB ILE A 221 13869 7551 4738 -802 1602 -816 C ATOM 1563 CG1 ILE A 221 83.944 7.303 66.969 1.00 67.91 C ANISOU 1563 CG1 ILE A 221 13798 7348 4658 -991 1440 -717 C ATOM 1564 CG2 ILE A 221 81.890 8.699 66.254 1.00 70.71 C ANISOU 1564 CG2 ILE A 221 13731 8050 5085 -623 1658 -908 C ATOM 1565 CD1 ILE A 221 83.224 5.965 66.637 1.00 77.11 C ANISOU 1565 CD1 ILE A 221 14778 8645 5875 -1167 1526 -753 C ATOM 1566 N ILE A 222 86.146 9.854 68.356 1.00 60.93 N ANISOU 1566 N ILE A 222 13570 6064 3519 -893 1268 -663 N ATOM 1567 CA ILE A 222 87.201 9.890 69.379 1.00 60.36 C ANISOU 1567 CA ILE A 222 13771 5878 3285 -1039 1174 -632 C ATOM 1568 C ILE A 222 87.250 11.318 69.963 1.00 64.42 C ANISOU 1568 C ILE A 222 14522 6280 3675 -1000 1263 -708 C ATOM 1569 O ILE A 222 87.294 11.467 71.186 1.00 65.48 O ANISOU 1569 O ILE A 222 14891 6358 3631 -1097 1331 -736 O ATOM 1570 CB ILE A 222 88.580 9.414 68.826 1.00 61.81 C ANISOU 1570 CB ILE A 222 13920 6056 3509 -1105 919 -555 C ATOM 1571 CG1 ILE A 222 88.578 7.880 68.610 1.00 61.47 C ANISOU 1571 CG1 ILE A 222 13767 6069 3521 -1150 861 -476 C ATOM 1572 CG2 ILE A 222 89.737 9.814 69.767 1.00 63.15 C ANISOU 1572 CG2 ILE A 222 14324 6175 3496 -1226 795 -560 C ATOM 1573 CD1 ILE A 222 89.714 7.326 67.717 1.00 66.95 C ANISOU 1573 CD1 ILE A 222 14348 6786 4302 -1137 640 -406 C ATOM 1574 N ILE A 223 87.210 12.358 69.093 1.00 59.99 N ANISOU 1574 N ILE A 223 13946 5664 3183 -856 1279 -741 N ATOM 1575 CA ILE A 223 87.219 13.769 69.514 1.00 60.96 C ANISOU 1575 CA ILE A 223 14357 5627 3177 -805 1396 -817 C ATOM 1576 C ILE A 223 85.878 14.101 70.209 1.00 65.58 C ANISOU 1576 C ILE A 223 14988 6231 3698 -650 1652 -885 C ATOM 1577 O ILE A 223 85.868 14.918 71.131 1.00 66.68 O ANISOU 1577 O ILE A 223 15430 6236 3669 -674 1777 -951 O ATOM 1578 CB ILE A 223 87.534 14.771 68.361 1.00 63.82 C ANISOU 1578 CB ILE A 223 14769 5879 3600 -680 1373 -823 C ATOM 1579 CG1 ILE A 223 86.483 14.720 67.212 1.00 64.11 C ANISOU 1579 CG1 ILE A 223 14550 6020 3790 -387 1428 -803 C ATOM 1580 CG2 ILE A 223 88.974 14.580 67.851 1.00 63.11 C ANISOU 1580 CG2 ILE A 223 14664 5777 3540 -886 1157 -787 C ATOM 1581 CD1 ILE A 223 86.552 15.852 66.147 1.00 72.41 C ANISOU 1581 CD1 ILE A 223 15738 6927 4847 -183 1453 -802 C ATOM 1582 N SER A 224 84.771 13.434 69.790 1.00 61.32 N ANISOU 1582 N SER A 224 14137 5881 3280 -517 1735 -887 N ATOM 1583 CA SER A 224 83.423 13.572 70.359 1.00 62.69 C ANISOU 1583 CA SER A 224 14241 6166 3412 -375 1985 -971 C ATOM 1584 C SER A 224 83.409 13.097 71.821 1.00 65.89 C ANISOU 1584 C SER A 224 14836 6542 3657 -597 2091 -992 C ATOM 1585 O SER A 224 82.745 13.711 72.660 1.00 67.57 O ANISOU 1585 O SER A 224 15201 6726 3747 -520 2309 -1075 O ATOM 1586 CB SER A 224 82.413 12.783 69.528 1.00 66.02 C ANISOU 1586 CB SER A 224 14229 6861 3994 -272 2013 -987 C ATOM 1587 OG SER A 224 81.090 12.912 70.024 1.00 76.97 O ANISOU 1587 OG SER A 224 15476 8427 5344 -141 2261 -1095 O ATOM 1588 N LYS A 225 84.165 12.016 72.116 1.00 59.75 N ANISOU 1588 N LYS A 225 14080 5759 2861 -844 1939 -913 N ATOM 1589 CA LYS A 225 84.329 11.439 73.450 1.00 59.86 C ANISOU 1589 CA LYS A 225 14326 5727 2692 -1052 1994 -904 C ATOM 1590 C LYS A 225 85.239 12.346 74.287 1.00 63.42 C ANISOU 1590 C LYS A 225 15149 6001 2947 -1125 1933 -924 C ATOM 1591 O LYS A 225 84.883 12.686 75.416 1.00 65.03 O ANISOU 1591 O LYS A 225 15596 6145 2967 -1172 2102 -985 O ATOM 1592 CB LYS A 225 84.896 10.002 73.349 1.00 60.69 C ANISOU 1592 CB LYS A 225 14369 5867 2823 -1223 1832 -798 C ATOM 1593 CG LYS A 225 85.208 9.303 74.680 1.00 74.06 C ANISOU 1593 CG LYS A 225 16362 7487 4290 -1408 1853 -756 C ATOM 1594 CD LYS A 225 83.970 8.949 75.504 1.00 84.79 C ANISOU 1594 CD LYS A 225 17766 8892 5559 -1480 2166 -823 C ATOM 1595 CE LYS A 225 84.344 8.310 76.817 1.00 94.75 C ANISOU 1595 CE LYS A 225 19397 10045 6558 -1653 2185 -768 C ATOM 1596 NZ LYS A 225 83.145 8.004 77.638 1.00106.41 N ANISOU 1596 NZ LYS A 225 20945 11556 7929 -1758 2529 -844 N ATOM 1597 N LEU A 226 86.394 12.751 73.712 1.00 57.86 N ANISOU 1597 N LEU A 226 14483 5230 2271 -1158 1706 -892 N ATOM 1598 CA LEU A 226 87.403 13.620 74.324 1.00 58.29 C ANISOU 1598 CA LEU A 226 14848 5156 2145 -1287 1619 -937 C ATOM 1599 C LEU A 226 86.808 14.964 74.784 1.00 64.11 C ANISOU 1599 C LEU A 226 15851 5742 2767 -1195 1857 -1052 C ATOM 1600 O LEU A 226 87.135 15.426 75.881 1.00 64.86 O ANISOU 1600 O LEU A 226 16266 5742 2634 -1337 1900 -1116 O ATOM 1601 CB LEU A 226 88.541 13.868 73.321 1.00 56.69 C ANISOU 1601 CB LEU A 226 14550 4951 2040 -1333 1389 -910 C ATOM 1602 CG LEU A 226 89.899 13.225 73.630 1.00 60.87 C ANISOU 1602 CG LEU A 226 15078 5570 2481 -1529 1113 -866 C ATOM 1603 CD1 LEU A 226 89.798 11.718 73.771 1.00 60.18 C ANISOU 1603 CD1 LEU A 226 14838 5599 2429 -1511 1026 -755 C ATOM 1604 CD2 LEU A 226 90.908 13.554 72.551 1.00 62.24 C ANISOU 1604 CD2 LEU A 226 15113 5770 2766 -1574 938 -868 C ATOM 1605 N SER A 227 85.928 15.571 73.960 1.00 61.23 N ANISOU 1605 N SER A 227 15370 5358 2534 -935 2010 -1079 N ATOM 1606 CA SER A 227 85.260 16.837 74.272 1.00 63.38 C ANISOU 1606 CA SER A 227 15904 5475 2701 -756 2259 -1179 C ATOM 1607 C SER A 227 84.161 16.634 75.326 1.00 69.16 C ANISOU 1607 C SER A 227 16670 6274 3333 -695 2510 -1239 C ATOM 1608 O SER A 227 83.891 17.554 76.101 1.00 71.28 O ANISOU 1608 O SER A 227 17268 6390 3425 -645 2708 -1331 O ATOM 1609 CB SER A 227 84.674 17.467 73.012 1.00 66.67 C ANISOU 1609 CB SER A 227 16183 5879 3271 -430 2320 -1174 C ATOM 1610 OG SER A 227 83.688 16.635 72.423 1.00 75.32 O ANISOU 1610 OG SER A 227 16848 7228 4544 -253 2345 -1141 O ATOM 1611 N HIS A 228 83.534 15.436 75.354 1.00 64.63 N ANISOU 1611 N HIS A 228 15781 5918 2857 -721 2528 -1198 N ATOM 1612 CA HIS A 228 82.488 15.094 76.322 1.00 66.46 C ANISOU 1612 CA HIS A 228 16010 6246 2996 -720 2788 -1262 C ATOM 1613 C HIS A 228 83.090 14.884 77.718 1.00 72.71 C ANISOU 1613 C HIS A 228 17171 6922 3535 -994 2786 -1265 C ATOM 1614 O HIS A 228 82.447 15.224 78.715 1.00 74.60 O ANISOU 1614 O HIS A 228 17611 7125 3609 -985 3036 -1351 O ATOM 1615 CB HIS A 228 81.712 13.842 75.881 1.00 66.08 C ANISOU 1615 CB HIS A 228 15543 6456 3110 -741 2820 -1233 C ATOM 1616 CG HIS A 228 80.664 13.405 76.859 1.00 71.41 C ANISOU 1616 CG HIS A 228 16202 7248 3682 -808 3112 -1313 C ATOM 1617 ND1 HIS A 228 80.905 12.392 77.767 1.00 73.15 N ANISOU 1617 ND1 HIS A 228 16581 7446 3768 -1101 3124 -1268 N ATOM 1618 CD2 HIS A 228 79.421 13.897 77.073 1.00 75.34 C ANISOU 1618 CD2 HIS A 228 16569 7886 4171 -607 3412 -1440 C ATOM 1619 CE1 HIS A 228 79.793 12.272 78.473 1.00 74.96 C ANISOU 1619 CE1 HIS A 228 16772 7790 3920 -1115 3445 -1370 C ATOM 1620 NE2 HIS A 228 78.875 13.161 78.096 1.00 76.77 N ANISOU 1620 NE2 HIS A 228 16799 8143 4228 -822 3627 -1485 N ATOM 1621 N ASN A1002 84.319 14.329 77.781 1.00 49.06 N ANISOU 1621 N ASN A1002 12067 3713 2859 417 -249 -1909 N ATOM 1622 CA ASN A1002 85.035 14.057 79.031 1.00 47.52 C ANISOU 1622 CA ASN A1002 11591 3529 2937 307 -114 -1711 C ATOM 1623 C ASN A1002 85.381 15.351 79.776 1.00 50.01 C ANISOU 1623 C ASN A1002 12030 3998 2974 146 113 -1451 C ATOM 1624 O ASN A1002 85.432 15.330 81.004 1.00 48.21 O ANISOU 1624 O ASN A1002 11615 3763 2942 74 134 -1226 O ATOM 1625 CB ASN A1002 86.305 13.246 78.770 1.00 49.27 C ANISOU 1625 CB ASN A1002 11644 3810 3268 345 -2 -1926 C ATOM 1626 CG ASN A1002 86.059 11.836 78.282 1.00 69.83 C ANISOU 1626 CG ASN A1002 14070 6205 6258 512 -246 -2194 C ATOM 1627 OD1 ASN A1002 85.026 11.234 78.582 1.00 66.68 O ANISOU 1627 OD1 ASN A1002 13637 5857 5840 615 -185 -2499 O ATOM 1628 ND2 ASN A1002 86.995 11.265 77.525 1.00 59.54 N ANISOU 1628 ND2 ASN A1002 12633 4651 5339 544 -523 -2104 N ATOM 1629 N ILE A1003 85.596 16.467 79.045 1.00 47.30 N ANISOU 1629 N ILE A1003 12014 3780 2178 94 268 -1478 N ATOM 1630 CA ILE A1003 85.879 17.781 79.638 1.00 46.00 C ANISOU 1630 CA ILE A1003 12001 3703 1774 -66 456 -1265 C ATOM 1631 C ILE A1003 84.555 18.341 80.190 1.00 48.82 C ANISOU 1631 C ILE A1003 12443 3944 2163 -26 296 -1080 C ATOM 1632 O ILE A1003 84.555 18.962 81.258 1.00 47.22 O ANISOU 1632 O ILE A1003 12203 3762 1977 -114 366 -894 O ATOM 1633 CB ILE A1003 86.565 18.755 78.630 1.00 50.76 C ANISOU 1633 CB ILE A1003 12922 4432 1931 -150 689 -1322 C ATOM 1634 CG1 ILE A1003 87.754 18.073 77.912 1.00 53.60 C ANISOU 1634 CG1 ILE A1003 13168 4937 2260 -144 867 -1548 C ATOM 1635 CG2 ILE A1003 87.003 20.063 79.323 1.00 50.17 C ANISOU 1635 CG2 ILE A1003 12963 4393 1708 -350 875 -1118 C ATOM 1636 CD1 ILE A1003 88.322 18.807 76.686 1.00 65.57 C ANISOU 1636 CD1 ILE A1003 14996 6603 3315 -191 1120 -1611 C ATOM 1637 N PHE A1004 83.428 18.089 79.472 1.00 45.86 N ANISOU 1637 N PHE A1004 12158 3458 1809 123 66 -1160 N ATOM 1638 CA PHE A1004 82.082 18.524 79.858 1.00 44.66 C ANISOU 1638 CA PHE A1004 12034 3199 1738 196 -103 -1020 C ATOM 1639 C PHE A1004 81.673 17.885 81.184 1.00 46.65 C ANISOU 1639 C PHE A1004 11932 3401 2393 180 -143 -851 C ATOM 1640 O PHE A1004 81.168 18.594 82.049 1.00 45.52 O ANISOU 1640 O PHE A1004 11793 3273 2229 165 -94 -667 O ATOM 1641 CB PHE A1004 81.049 18.207 78.760 1.00 48.17 C ANISOU 1641 CB PHE A1004 12578 3542 2181 366 -385 -1183 C ATOM 1642 CG PHE A1004 79.614 18.542 79.105 1.00 49.47 C ANISOU 1642 CG PHE A1004 12693 3597 2506 460 -585 -1066 C ATOM 1643 CD1 PHE A1004 79.150 19.851 79.032 1.00 52.17 C ANISOU 1643 CD1 PHE A1004 13314 3942 2566 495 -566 -953 C ATOM 1644 CD2 PHE A1004 78.714 17.542 79.458 1.00 52.08 C ANISOU 1644 CD2 PHE A1004 12681 3802 3305 519 -795 -1073 C ATOM 1645 CE1 PHE A1004 77.822 20.158 79.347 1.00 53.27 C ANISOU 1645 CE1 PHE A1004 13368 3991 2880 614 -746 -869 C ATOM 1646 CE2 PHE A1004 77.385 17.850 79.766 1.00 55.12 C ANISOU 1646 CE2 PHE A1004 12964 4108 3872 604 -953 -969 C ATOM 1647 CZ PHE A1004 76.947 19.155 79.703 1.00 52.89 C ANISOU 1647 CZ PHE A1004 12944 3859 3294 666 -929 -882 C ATOM 1648 N GLU A1005 81.912 16.573 81.355 1.00 43.00 N ANISOU 1648 N GLU A1005 11178 2877 2284 195 -217 -906 N ATOM 1649 CA GLU A1005 81.580 15.868 82.595 1.00 42.00 C ANISOU 1649 CA GLU A1005 10724 2696 2538 175 -238 -689 C ATOM 1650 C GLU A1005 82.561 16.237 83.717 1.00 43.16 C ANISOU 1650 C GLU A1005 10827 3001 2571 68 -25 -521 C ATOM 1651 O GLU A1005 82.185 16.167 84.886 1.00 41.88 O ANISOU 1651 O GLU A1005 10507 2868 2536 59 7 -284 O ATOM 1652 CB GLU A1005 81.553 14.345 82.386 1.00 44.88 C ANISOU 1652 CB GLU A1005 10811 2888 3353 223 -407 -782 C ATOM 1653 CG GLU A1005 80.352 13.863 81.586 1.00 56.72 C ANISOU 1653 CG GLU A1005 12265 4197 5088 320 -680 -923 C ATOM 1654 CD GLU A1005 78.983 14.117 82.192 1.00 77.93 C ANISOU 1654 CD GLU A1005 14818 6822 7970 331 -755 -708 C ATOM 1655 OE1 GLU A1005 78.816 13.904 83.416 1.00 73.58 O ANISOU 1655 OE1 GLU A1005 14046 6286 7624 272 -638 -412 O ATOM 1656 OE2 GLU A1005 78.063 14.495 81.430 1.00 72.25 O ANISOU 1656 OE2 GLU A1005 14202 6052 7199 415 -934 -835 O ATOM 1657 N MET A1006 83.797 16.646 83.357 1.00 39.01 N ANISOU 1657 N MET A1006 10431 2594 1796 -9 120 -648 N ATOM 1658 CA MET A1006 84.849 17.067 84.286 1.00 37.96 C ANISOU 1658 CA MET A1006 10253 2617 1555 -120 282 -551 C ATOM 1659 C MET A1006 84.480 18.398 84.947 1.00 41.90 C ANISOU 1659 C MET A1006 10944 3188 1789 -173 365 -426 C ATOM 1660 O MET A1006 84.635 18.549 86.160 1.00 41.41 O ANISOU 1660 O MET A1006 10782 3221 1731 -200 404 -275 O ATOM 1661 CB MET A1006 86.187 17.193 83.539 1.00 40.82 C ANISOU 1661 CB MET A1006 10673 3074 1765 -199 418 -750 C ATOM 1662 CG MET A1006 87.370 17.490 84.425 1.00 43.92 C ANISOU 1662 CG MET A1006 10947 3618 2124 -319 541 -695 C ATOM 1663 SD MET A1006 88.365 18.838 83.758 1.00 48.32 S ANISOU 1663 SD MET A1006 11744 4288 2327 -505 774 -817 S ATOM 1664 CE MET A1006 89.788 18.681 84.763 1.00 45.60 C ANISOU 1664 CE MET A1006 11108 4102 2116 -615 831 -813 C ATOM 1665 N LEU A1007 84.000 19.358 84.144 1.00 39.13 N ANISOU 1665 N LEU A1007 10884 2787 1198 -167 377 -497 N ATOM 1666 CA LEU A1007 83.611 20.680 84.621 1.00 38.85 C ANISOU 1666 CA LEU A1007 11063 2761 938 -192 436 -417 C ATOM 1667 C LEU A1007 82.166 20.672 85.167 1.00 43.58 C ANISOU 1667 C LEU A1007 11595 3304 1662 -48 330 -291 C ATOM 1668 O LEU A1007 81.800 21.583 85.911 1.00 42.94 O ANISOU 1668 O LEU A1007 11610 3253 1453 -29 382 -221 O ATOM 1669 CB LEU A1007 83.785 21.717 83.508 1.00 39.44 C ANISOU 1669 CB LEU A1007 11488 2775 723 -242 494 -512 C ATOM 1670 CG LEU A1007 85.194 22.311 83.456 1.00 44.41 C ANISOU 1670 CG LEU A1007 12198 3484 1193 -441 685 -564 C ATOM 1671 CD1 LEU A1007 85.605 22.666 82.060 1.00 45.99 C ANISOU 1671 CD1 LEU A1007 12643 3658 1174 -494 779 -648 C ATOM 1672 CD2 LEU A1007 85.338 23.490 84.401 1.00 46.38 C ANISOU 1672 CD2 LEU A1007 12561 3726 1336 -536 745 -500 C ATOM 1673 N ARG A1008 81.381 19.614 84.861 1.00 41.17 N ANISOU 1673 N ARG A1008 11088 2914 1639 51 188 -277 N ATOM 1674 CA ARG A1008 80.028 19.405 85.388 1.00 41.68 C ANISOU 1674 CA ARG A1008 10987 2933 1916 167 107 -142 C ATOM 1675 C ARG A1008 80.126 19.134 86.894 1.00 46.86 C ANISOU 1675 C ARG A1008 11431 3722 2652 148 228 72 C ATOM 1676 O ARG A1008 79.273 19.568 87.672 1.00 47.04 O ANISOU 1676 O ARG A1008 11408 3803 2660 226 284 199 O ATOM 1677 CB ARG A1008 79.349 18.239 84.648 1.00 42.50 C ANISOU 1677 CB ARG A1008 10892 2889 2368 231 -90 -200 C ATOM 1678 CG ARG A1008 77.860 18.089 84.908 1.00 54.65 C ANISOU 1678 CG ARG A1008 12238 4354 4173 335 -194 -92 C ATOM 1679 CD ARG A1008 77.343 16.816 84.279 1.00 67.35 C ANISOU 1679 CD ARG A1008 13600 5787 6204 357 -411 -164 C ATOM 1680 NE ARG A1008 75.897 16.670 84.435 1.00 79.77 N ANISOU 1680 NE ARG A1008 14938 7276 8092 434 -524 -76 N ATOM 1681 CZ ARG A1008 75.219 15.564 84.143 1.00 97.65 C ANISOU 1681 CZ ARG A1008 16904 9362 10837 431 -718 -95 C ATOM 1682 NH1 ARG A1008 75.854 14.481 83.709 1.00 86.36 N ANISOU 1682 NH1 ARG A1008 15394 7798 9619 374 -827 -208 N ATOM 1683 NH2 ARG A1008 73.904 15.521 84.309 1.00 87.14 N ANISOU 1683 NH2 ARG A1008 15321 7969 9818 485 -805 -11 N ATOM 1684 N ILE A1009 81.204 18.420 87.283 1.00 43.73 N ANISOU 1684 N ILE A1009 10909 3390 2316 64 268 105 N ATOM 1685 CA ILE A1009 81.576 18.052 88.647 1.00 43.75 C ANISOU 1685 CA ILE A1009 10741 3541 2342 51 352 313 C ATOM 1686 C ILE A1009 82.135 19.285 89.375 1.00 47.90 C ANISOU 1686 C ILE A1009 11470 4237 2492 13 464 274 C ATOM 1687 O ILE A1009 81.729 19.557 90.507 1.00 48.40 O ANISOU 1687 O ILE A1009 11500 4443 2449 77 537 421 O ATOM 1688 CB ILE A1009 82.610 16.880 88.599 1.00 47.01 C ANISOU 1688 CB ILE A1009 10967 3926 2968 0 297 320 C ATOM 1689 CG1 ILE A1009 81.928 15.566 88.149 1.00 48.31 C ANISOU 1689 CG1 ILE A1009 10897 3883 3577 48 166 381 C ATOM 1690 CG2 ILE A1009 83.329 16.696 89.946 1.00 48.76 C ANISOU 1690 CG2 ILE A1009 11083 4333 3112 -12 355 509 C ATOM 1691 CD1 ILE A1009 82.875 14.404 87.769 1.00 56.61 C ANISOU 1691 CD1 ILE A1009 11791 4825 4891 34 75 303 C ATOM 1692 N ASP A1010 83.068 20.016 88.728 1.00 43.95 N ANISOU 1692 N ASP A1010 11176 3724 1800 -92 482 72 N ATOM 1693 CA ASP A1010 83.756 21.165 89.308 1.00 43.93 C ANISOU 1693 CA ASP A1010 11353 3827 1512 -170 555 -7 C ATOM 1694 C ASP A1010 82.871 22.425 89.343 1.00 48.55 C ANISOU 1694 C ASP A1010 12183 4354 1911 -102 585 -54 C ATOM 1695 O ASP A1010 82.482 22.838 90.436 1.00 49.35 O ANISOU 1695 O ASP A1010 12285 4572 1894 -20 624 4 O ATOM 1696 CB ASP A1010 85.056 21.455 88.543 1.00 45.56 C ANISOU 1696 CB ASP A1010 11646 4011 1655 -337 587 -182 C ATOM 1697 CG ASP A1010 86.162 20.434 88.758 1.00 53.53 C ANISOU 1697 CG ASP A1010 12400 5115 2825 -390 564 -177 C ATOM 1698 OD1 ASP A1010 86.163 19.768 89.815 1.00 54.04 O ANISOU 1698 OD1 ASP A1010 12273 5290 2970 -320 513 -23 O ATOM 1699 OD2 ASP A1010 87.071 20.360 87.911 1.00 58.91 O ANISOU 1699 OD2 ASP A1010 13076 5774 3533 -493 609 -319 O ATOM 1700 N GLU A1011 82.576 23.040 88.182 1.00 44.85 N ANISOU 1700 N GLU A1011 11932 3713 1394 -113 563 -159 N ATOM 1701 CA GLU A1011 81.785 24.270 88.090 1.00 45.17 C ANISOU 1701 CA GLU A1011 12226 3648 1291 -30 561 -206 C ATOM 1702 C GLU A1011 80.294 24.009 88.402 1.00 48.75 C ANISOU 1702 C GLU A1011 12546 4101 1875 179 519 -103 C ATOM 1703 O GLU A1011 79.717 24.726 89.215 1.00 49.03 O ANISOU 1703 O GLU A1011 12629 4185 1815 292 568 -101 O ATOM 1704 CB GLU A1011 81.950 24.908 86.691 1.00 47.04 C ANISOU 1704 CB GLU A1011 12744 3697 1433 -94 535 -296 C ATOM 1705 CG GLU A1011 81.026 26.075 86.348 1.00 60.60 C ANISOU 1705 CG GLU A1011 14737 5242 3047 27 483 -316 C ATOM 1706 CD GLU A1011 81.159 27.401 87.080 1.00 88.05 C ANISOU 1706 CD GLU A1011 18423 8652 6381 13 532 -380 C ATOM 1707 OE1 GLU A1011 81.542 27.413 88.273 1.00 80.38 O ANISOU 1707 OE1 GLU A1011 17332 7827 5381 -13 588 -411 O ATOM 1708 OE2 GLU A1011 80.797 28.432 86.469 1.00 87.86 O ANISOU 1708 OE2 GLU A1011 18694 8416 6274 56 488 -404 O ATOM 1709 N GLY A1012 79.695 23.016 87.749 1.00 45.09 N ANISOU 1709 N GLY A1012 11903 3582 1646 232 430 -46 N ATOM 1710 CA GLY A1012 78.285 22.684 87.924 1.00 45.39 C ANISOU 1710 CA GLY A1012 11750 3603 1892 399 382 50 C ATOM 1711 C GLY A1012 77.439 23.067 86.726 1.00 48.86 C ANISOU 1711 C GLY A1012 12324 3863 2377 501 221 -43 C ATOM 1712 O GLY A1012 77.637 24.133 86.135 1.00 47.96 O ANISOU 1712 O GLY A1012 12537 3647 2038 506 193 -144 O ATOM 1713 N LEU A1013 76.486 22.192 86.364 1.00 46.04 N ANISOU 1713 N LEU A1013 11713 3452 2329 583 93 0 N ATOM 1714 CA LEU A1013 75.588 22.399 85.228 1.00 46.89 C ANISOU 1714 CA LEU A1013 11898 3407 2512 706 -127 -101 C ATOM 1715 C LEU A1013 74.267 23.038 85.678 1.00 52.45 C ANISOU 1715 C LEU A1013 12500 4108 3320 902 -142 -58 C ATOM 1716 O LEU A1013 73.661 22.611 86.665 1.00 52.54 O ANISOU 1716 O LEU A1013 12189 4231 3543 942 -21 76 O ATOM 1717 CB LEU A1013 75.317 21.064 84.505 1.00 47.39 C ANISOU 1717 CB LEU A1013 11719 3391 2896 684 -312 -139 C ATOM 1718 CG LEU A1013 74.536 21.115 83.183 1.00 53.37 C ANISOU 1718 CG LEU A1013 12568 4005 3704 809 -609 -294 C ATOM 1719 CD1 LEU A1013 75.344 21.787 82.089 1.00 53.23 C ANISOU 1719 CD1 LEU A1013 12995 3951 3279 790 -654 -428 C ATOM 1720 CD2 LEU A1013 74.154 19.723 82.733 1.00 56.85 C ANISOU 1720 CD2 LEU A1013 12697 4360 4543 789 -806 -356 C ATOM 1721 N ARG A1014 73.828 24.059 84.928 1.00 50.41 N ANISOU 1721 N ARG A1014 12517 3725 2913 1035 -282 -158 N ATOM 1722 CA ARG A1014 72.594 24.805 85.165 1.00 52.11 C ANISOU 1722 CA ARG A1014 12668 3906 3226 1264 -336 -162 C ATOM 1723 C ARG A1014 71.843 24.958 83.840 1.00 58.59 C ANISOU 1723 C ARG A1014 13589 4561 4111 1409 -666 -259 C ATOM 1724 O ARG A1014 72.369 25.532 82.884 1.00 58.25 O ANISOU 1724 O ARG A1014 13944 4405 3784 1398 -780 -323 O ATOM 1725 CB ARG A1014 72.904 26.158 85.822 1.00 51.27 C ANISOU 1725 CB ARG A1014 12851 3795 2836 1322 -179 -190 C ATOM 1726 CG ARG A1014 73.187 26.006 87.313 1.00 58.65 C ANISOU 1726 CG ARG A1014 13599 4942 3744 1274 102 -115 C ATOM 1727 CD ARG A1014 74.235 26.956 87.854 1.00 62.34 C ANISOU 1727 CD ARG A1014 14394 5414 3880 1187 237 -188 C ATOM 1728 NE ARG A1014 75.592 26.624 87.417 1.00 61.44 N ANISOU 1728 NE ARG A1014 14439 5283 3622 934 245 -193 N ATOM 1729 CZ ARG A1014 76.696 27.104 87.981 1.00 69.07 C ANISOU 1729 CZ ARG A1014 15577 6294 4374 789 364 -242 C ATOM 1730 NH1 ARG A1014 77.888 26.754 87.523 1.00 54.79 N ANISOU 1730 NH1 ARG A1014 13851 4481 2487 566 376 -249 N ATOM 1731 NH2 ARG A1014 76.616 27.924 89.021 1.00 53.27 N ANISOU 1731 NH2 ARG A1014 13642 4350 2246 875 467 -310 N ATOM 1732 N LEU A1015 70.626 24.390 83.779 1.00 57.44 N ANISOU 1732 N LEU A1015 13066 4412 4345 1539 -823 -259 N ATOM 1733 CA LEU A1015 69.774 24.377 82.585 1.00 59.51 C ANISOU 1733 CA LEU A1015 13340 4542 4731 1699 -1201 -373 C ATOM 1734 C LEU A1015 68.825 25.597 82.544 1.00 66.19 C ANISOU 1734 C LEU A1015 14285 5309 5558 1979 -1314 -400 C ATOM 1735 O LEU A1015 67.926 25.657 81.700 1.00 68.02 O ANISOU 1735 O LEU A1015 14466 5445 5935 2164 -1655 -484 O ATOM 1736 CB LEU A1015 68.960 23.067 82.544 1.00 60.78 C ANISOU 1736 CB LEU A1015 12981 4714 5398 1673 -1350 -382 C ATOM 1737 CG LEU A1015 69.745 21.745 82.561 1.00 63.91 C ANISOU 1737 CG LEU A1015 13232 5130 5921 1430 -1290 -365 C ATOM 1738 CD1 LEU A1015 68.812 20.568 82.707 1.00 66.09 C ANISOU 1738 CD1 LEU A1015 12962 5365 6785 1399 -1416 -341 C ATOM 1739 CD2 LEU A1015 70.613 21.576 81.318 1.00 65.94 C ANISOU 1739 CD2 LEU A1015 13862 5313 5878 1374 -1480 -528 C ATOM 1740 N LYS A1016 69.048 26.568 83.447 1.00 62.95 N ANISOU 1740 N LYS A1016 14019 4927 4972 2026 -1057 -354 N ATOM 1741 CA LYS A1016 68.279 27.811 83.568 1.00 65.33 C ANISOU 1741 CA LYS A1016 14439 5128 5254 2305 -1119 -397 C ATOM 1742 C LYS A1016 69.220 29.016 83.549 1.00 69.00 C ANISOU 1742 C LYS A1016 15450 5457 5309 2270 -1020 -402 C ATOM 1743 O LYS A1016 70.381 28.880 83.953 1.00 66.52 O ANISOU 1743 O LYS A1016 15282 5209 4784 2025 -793 -368 O ATOM 1744 CB LYS A1016 67.440 27.820 84.872 1.00 69.20 C ANISOU 1744 CB LYS A1016 14494 5783 6017 2437 -877 -373 C ATOM 1745 CG LYS A1016 66.634 26.551 85.189 1.00 85.99 C ANISOU 1745 CG LYS A1016 16012 8062 8597 2393 -855 -303 C ATOM 1746 CD LYS A1016 65.436 26.322 84.269 1.00 99.27 C ANISOU 1746 CD LYS A1016 17433 9641 10644 2575 -1239 -382 C ATOM 1747 CE LYS A1016 64.746 25.002 84.534 1.00110.64 C ANISOU 1747 CE LYS A1016 18259 11185 12593 2465 -1226 -311 C ATOM 1748 NZ LYS A1016 65.582 23.834 84.138 1.00116.94 N ANISOU 1748 NZ LYS A1016 19080 11956 13395 2171 -1274 -275 N ATOM 1749 N ILE A1017 68.728 30.198 83.114 1.00 67.79 N ANISOU 1749 N ILE A1017 15580 5095 5082 2512 -1198 -440 N ATOM 1750 CA ILE A1017 69.536 31.423 83.125 1.00 67.59 C ANISOU 1750 CA ILE A1017 16064 4873 4744 2476 -1114 -432 C ATOM 1751 C ILE A1017 69.679 31.857 84.596 1.00 71.14 C ANISOU 1751 C ILE A1017 16397 5418 5214 2484 -800 -500 C ATOM 1752 O ILE A1017 68.678 32.040 85.297 1.00 72.07 O ANISOU 1752 O ILE A1017 16222 5609 5551 2733 -758 -571 O ATOM 1753 CB ILE A1017 68.978 32.554 82.206 1.00 73.79 C ANISOU 1753 CB ILE A1017 17217 5357 5464 2741 -1419 -420 C ATOM 1754 CG1 ILE A1017 68.898 32.082 80.731 1.00 75.11 C ANISOU 1754 CG1 ILE A1017 17541 5481 5517 2743 -1743 -355 C ATOM 1755 CG2 ILE A1017 69.831 33.837 82.333 1.00 74.79 C ANISOU 1755 CG2 ILE A1017 17853 5226 5337 2669 -1304 -390 C ATOM 1756 CD1 ILE A1017 68.226 33.058 79.710 1.00 86.55 C ANISOU 1756 CD1 ILE A1017 19342 6660 6884 3046 -2114 -302 C ATOM 1757 N TYR A1018 70.931 31.951 85.062 1.00 66.15 N ANISOU 1757 N TYR A1018 15964 4819 4352 2215 -579 -494 N ATOM 1758 CA TYR A1018 71.268 32.328 86.431 1.00 66.02 C ANISOU 1758 CA TYR A1018 15894 4915 4277 2197 -312 -586 C ATOM 1759 C TYR A1018 72.218 33.532 86.431 1.00 71.64 C ANISOU 1759 C TYR A1018 17086 5368 4765 2089 -287 -650 C ATOM 1760 O TYR A1018 72.840 33.827 85.408 1.00 70.57 O ANISOU 1760 O TYR A1018 17287 5023 4503 1940 -400 -561 O ATOM 1761 CB TYR A1018 71.892 31.128 87.184 1.00 64.36 C ANISOU 1761 CB TYR A1018 15377 5024 4051 1961 -89 -526 C ATOM 1762 CG TYR A1018 73.289 30.738 86.740 1.00 63.20 C ANISOU 1762 CG TYR A1018 15427 4870 3717 1623 -55 -467 C ATOM 1763 CD1 TYR A1018 73.487 29.879 85.663 1.00 63.83 C ANISOU 1763 CD1 TYR A1018 15477 4945 3831 1499 -184 -380 C ATOM 1764 CD2 TYR A1018 74.411 31.170 87.443 1.00 63.18 C ANISOU 1764 CD2 TYR A1018 15597 4890 3520 1437 105 -529 C ATOM 1765 CE1 TYR A1018 74.770 29.511 85.256 1.00 62.82 C ANISOU 1765 CE1 TYR A1018 15496 4834 3538 1215 -120 -348 C ATOM 1766 CE2 TYR A1018 75.697 30.805 87.050 1.00 62.22 C ANISOU 1766 CE2 TYR A1018 15595 4778 3270 1132 149 -484 C ATOM 1767 CZ TYR A1018 75.873 29.970 85.960 1.00 68.31 C ANISOU 1767 CZ TYR A1018 16330 5552 4072 1029 57 -388 C ATOM 1768 OH TYR A1018 77.143 29.601 85.586 1.00 68.22 O ANISOU 1768 OH TYR A1018 16403 5575 3942 754 132 -364 O ATOM 1769 N LYS A1019 72.338 34.212 87.582 1.00 71.07 N ANISOU 1769 N LYS A1019 17043 5315 4646 2158 -132 -807 N ATOM 1770 CA LYS A1019 73.233 35.357 87.721 1.00 72.85 C ANISOU 1770 CA LYS A1019 17684 5268 4728 2038 -122 -907 C ATOM 1771 C LYS A1019 74.595 34.898 88.244 1.00 77.03 C ANISOU 1771 C LYS A1019 18205 5970 5093 1682 48 -914 C ATOM 1772 O LYS A1019 74.673 34.090 89.171 1.00 75.02 O ANISOU 1772 O LYS A1019 17639 6060 4806 1655 203 -939 O ATOM 1773 CB LYS A1019 72.635 36.444 88.633 1.00 78.06 C ANISOU 1773 CB LYS A1019 18413 5806 5439 2334 -101 -1142 C ATOM 1774 CG LYS A1019 71.448 37.184 88.026 1.00 90.51 C ANISOU 1774 CG LYS A1019 20079 7110 7202 2697 -310 -1154 C ATOM 1775 N ASP A1020 75.663 35.423 87.626 1.00 76.07 N ANISOU 1775 N ASP A1020 18417 5606 4880 1413 17 -871 N ATOM 1776 CA ASP A1020 77.074 35.180 87.939 1.00 75.54 C ANISOU 1776 CA ASP A1020 18369 5634 4698 1055 142 -888 C ATOM 1777 C ASP A1020 77.450 35.848 89.280 1.00 82.17 C ANISOU 1777 C ASP A1020 19235 6496 5490 1064 210 -1140 C ATOM 1778 O ASP A1020 76.651 36.615 89.828 1.00 84.11 O ANISOU 1778 O ASP A1020 19547 6632 5778 1348 169 -1307 O ATOM 1779 CB ASP A1020 77.929 35.742 86.773 1.00 78.66 C ANISOU 1779 CB ASP A1020 19119 5718 5052 796 99 -755 C ATOM 1780 CG ASP A1020 79.440 35.608 86.864 1.00 91.43 C ANISOU 1780 CG ASP A1020 20752 7385 6604 402 227 -758 C ATOM 1781 OD1 ASP A1020 79.917 34.622 87.475 1.00 90.67 O ANISOU 1781 OD1 ASP A1020 20347 7630 6476 300 323 -793 O ATOM 1782 OD2 ASP A1020 80.145 36.466 86.286 1.00 98.86 O ANISOU 1782 OD2 ASP A1020 21998 8015 7548 193 231 -702 O ATOM 1783 N THR A1021 78.665 35.558 89.804 1.00 78.90 N ANISOU 1783 N THR A1021 18761 6230 4987 777 294 -1197 N ATOM 1784 CA THR A1021 79.209 36.143 91.039 1.00 81.05 C ANISOU 1784 CA THR A1021 19070 6542 5182 749 311 -1466 C ATOM 1785 C THR A1021 79.368 37.668 90.830 1.00 89.40 C ANISOU 1785 C THR A1021 20520 7108 6339 728 196 -1623 C ATOM 1786 O THR A1021 79.192 38.444 91.773 1.00 91.39 O ANISOU 1786 O THR A1021 20863 7288 6573 885 152 -1911 O ATOM 1787 CB THR A1021 80.536 35.448 91.414 1.00 88.51 C ANISOU 1787 CB THR A1021 19854 7728 6047 427 370 -1461 C ATOM 1788 OG1 THR A1021 80.333 34.034 91.447 1.00 86.02 O ANISOU 1788 OG1 THR A1021 19206 7785 5694 458 456 -1274 O ATOM 1789 CG2 THR A1021 81.093 35.907 92.761 1.00 89.30 C ANISOU 1789 CG2 THR A1021 19958 7940 6032 418 341 -1758 C ATOM 1790 N GLU A1022 79.654 38.078 89.574 1.00 87.25 N ANISOU 1790 N GLU A1022 20492 6492 6167 552 149 -1426 N ATOM 1791 CA GLU A1022 79.796 39.473 89.150 1.00 90.88 C ANISOU 1791 CA GLU A1022 21348 6415 6766 500 43 -1471 C ATOM 1792 C GLU A1022 78.417 40.075 88.784 1.00 96.39 C ANISOU 1792 C GLU A1022 22208 6868 7548 903 -80 -1449 C ATOM 1793 O GLU A1022 78.300 41.296 88.645 1.00 99.49 O ANISOU 1793 O GLU A1022 22928 6790 8082 965 -198 -1526 O ATOM 1794 CB GLU A1022 80.774 39.586 87.969 1.00 92.49 C ANISOU 1794 CB GLU A1022 21735 6398 7009 118 90 -1209 C ATOM 1795 CG GLU A1022 82.198 39.183 88.313 1.00103.10 C ANISOU 1795 CG GLU A1022 22909 7923 8342 -282 200 -1262 C ATOM 1796 CD GLU A1022 83.184 39.298 87.169 1.00126.43 C ANISOU 1796 CD GLU A1022 26000 10695 11341 -661 306 -1006 C ATOM 1797 OE1 GLU A1022 83.587 40.437 86.842 1.00125.51 O ANISOU 1797 OE1 GLU A1022 26184 10123 11380 -842 280 -974 O ATOM 1798 OE2 GLU A1022 83.581 38.244 86.622 1.00118.55 O ANISOU 1798 OE2 GLU A1022 24800 10009 10235 -781 430 -840 O ATOM 1799 N GLY A1023 77.402 39.214 88.650 1.00 90.69 N ANISOU 1799 N GLY A1023 21235 6446 6777 1170 -68 -1351 N ATOM 1800 CA GLY A1023 76.022 39.606 88.374 1.00 92.13 C ANISOU 1800 CA GLY A1023 21459 6483 7064 1583 -193 -1347 C ATOM 1801 C GLY A1023 75.534 39.525 86.941 1.00 95.62 C ANISOU 1801 C GLY A1023 22046 6748 7537 1639 -326 -1049 C ATOM 1802 O GLY A1023 74.427 39.991 86.655 1.00 97.57 O ANISOU 1802 O GLY A1023 22355 6819 7899 1991 -482 -1049 O ATOM 1803 N TYR A1024 76.335 38.938 86.028 1.00 89.56 N ANISOU 1803 N TYR A1024 21330 6042 6655 1324 -278 -810 N ATOM 1804 CA TYR A1024 75.963 38.820 84.613 1.00 89.43 C ANISOU 1804 CA TYR A1024 21491 5902 6585 1373 -410 -534 C ATOM 1805 C TYR A1024 75.121 37.563 84.371 1.00 89.84 C ANISOU 1805 C TYR A1024 21176 6334 6626 1554 -457 -488 C ATOM 1806 O TYR A1024 75.260 36.584 85.106 1.00 86.58 O ANISOU 1806 O TYR A1024 20391 6293 6214 1485 -318 -577 O ATOM 1807 CB TYR A1024 77.210 38.802 83.706 1.00 90.44 C ANISOU 1807 CB TYR A1024 21858 5940 6566 970 -307 -315 C ATOM 1808 CG TYR A1024 78.184 39.938 83.944 1.00 94.73 C ANISOU 1808 CG TYR A1024 22702 6109 7181 703 -236 -340 C ATOM 1809 CD1 TYR A1024 77.826 41.259 83.682 1.00100.89 C ANISOU 1809 CD1 TYR A1024 23873 6374 8086 833 -382 -291 C ATOM 1810 CD2 TYR A1024 79.489 39.688 84.359 1.00 94.23 C ANISOU 1810 CD2 TYR A1024 22528 6176 7100 310 -42 -400 C ATOM 1811 CE1 TYR A1024 78.723 42.307 83.885 1.00104.57 C ANISOU 1811 CE1 TYR A1024 24607 6440 8684 558 -331 -313 C ATOM 1812 CE2 TYR A1024 80.399 40.727 84.551 1.00 98.00 C ANISOU 1812 CE2 TYR A1024 23244 6289 7704 31 4 -433 C ATOM 1813 CZ TYR A1024 80.010 42.036 84.318 1.00109.40 C ANISOU 1813 CZ TYR A1024 25075 7196 9295 143 -137 -390 C ATOM 1814 OH TYR A1024 80.904 43.062 84.509 1.00113.45 O ANISOU 1814 OH TYR A1024 25812 7298 9995 -159 -104 -425 O ATOM 1815 N TYR A1025 74.246 37.588 83.343 1.00 87.09 N ANISOU 1815 N TYR A1025 20931 5876 6282 1785 -676 -343 N ATOM 1816 CA TYR A1025 73.394 36.445 83.009 1.00 84.92 C ANISOU 1816 CA TYR A1025 20306 5906 6052 1951 -778 -320 C ATOM 1817 C TYR A1025 74.230 35.349 82.356 1.00 85.82 C ANISOU 1817 C TYR A1025 20351 6260 5997 1655 -689 -208 C ATOM 1818 O TYR A1025 74.889 35.580 81.339 1.00 86.19 O ANISOU 1818 O TYR A1025 20733 6174 5842 1492 -704 -45 O ATOM 1819 CB TYR A1025 72.222 36.851 82.112 1.00 88.77 C ANISOU 1819 CB TYR A1025 20922 6200 6606 2303 -1095 -237 C ATOM 1820 CG TYR A1025 71.253 37.805 82.773 1.00 93.06 C ANISOU 1820 CG TYR A1025 21449 6536 7373 2662 -1195 -382 C ATOM 1821 CD1 TYR A1025 71.331 39.176 82.548 1.00 98.48 C ANISOU 1821 CD1 TYR A1025 22583 6767 8066 2757 -1301 -340 C ATOM 1822 CD2 TYR A1025 70.253 37.338 83.621 1.00 93.43 C ANISOU 1822 CD2 TYR A1025 21023 6831 7646 2914 -1168 -555 C ATOM 1823 CE1 TYR A1025 70.437 40.059 83.149 1.00102.26 C ANISOU 1823 CE1 TYR A1025 23046 7034 8776 3125 -1404 -511 C ATOM 1824 CE2 TYR A1025 69.362 38.213 84.238 1.00 97.33 C ANISOU 1824 CE2 TYR A1025 21475 7163 8343 3275 -1228 -719 C ATOM 1825 CZ TYR A1025 69.449 39.572 83.989 1.00108.09 C ANISOU 1825 CZ TYR A1025 23294 8063 9713 3397 -1362 -717 C ATOM 1826 OH TYR A1025 68.558 40.431 84.583 1.00112.73 O ANISOU 1826 OH TYR A1025 23835 8472 10525 3791 -1434 -914 O ATOM 1827 N THR A1026 74.225 34.165 82.987 1.00 79.39 N ANISOU 1827 N THR A1026 19100 5797 5267 1591 -574 -291 N ATOM 1828 CA THR A1026 75.006 32.992 82.596 1.00 76.47 C ANISOU 1828 CA THR A1026 18583 5670 4803 1338 -478 -240 C ATOM 1829 C THR A1026 74.075 31.761 82.509 1.00 78.59 C ANISOU 1829 C THR A1026 18437 6172 5253 1492 -600 -269 C ATOM 1830 O THR A1026 72.975 31.785 83.066 1.00 78.85 O ANISOU 1830 O THR A1026 18222 6237 5501 1738 -673 -329 O ATOM 1831 CB THR A1026 76.141 32.803 83.638 1.00 83.18 C ANISOU 1831 CB THR A1026 19310 6665 5630 1063 -211 -311 C ATOM 1832 OG1 THR A1026 76.668 34.074 84.036 1.00 85.00 O ANISOU 1832 OG1 THR A1026 19841 6646 5809 985 -144 -352 O ATOM 1833 CG2 THR A1026 77.269 31.925 83.144 1.00 79.77 C ANISOU 1833 CG2 THR A1026 18830 6396 5082 771 -92 -256 C ATOM 1834 N ILE A1027 74.512 30.702 81.792 1.00 73.49 N ANISOU 1834 N ILE A1027 17704 5673 4546 1348 -620 -239 N ATOM 1835 CA ILE A1027 73.782 29.436 81.625 1.00 72.32 C ANISOU 1835 CA ILE A1027 17166 5701 4612 1436 -754 -280 C ATOM 1836 C ILE A1027 74.814 28.307 81.341 1.00 73.93 C ANISOU 1836 C ILE A1027 17269 6070 4750 1182 -642 -291 C ATOM 1837 O ILE A1027 75.932 28.598 80.910 1.00 73.32 O ANISOU 1837 O ILE A1027 17470 5967 4421 989 -512 -260 O ATOM 1838 CB ILE A1027 72.681 29.547 80.520 1.00 77.80 C ANISOU 1838 CB ILE A1027 17944 6281 5334 1700 -1110 -285 C ATOM 1839 CG1 ILE A1027 71.592 28.453 80.681 1.00 78.09 C ANISOU 1839 CG1 ILE A1027 17478 6452 5741 1833 -1274 -361 C ATOM 1840 CG2 ILE A1027 73.268 29.638 79.093 1.00 79.64 C ANISOU 1840 CG2 ILE A1027 18589 6446 5225 1640 -1232 -235 C ATOM 1841 CD1 ILE A1027 70.284 28.673 79.934 1.00 86.67 C ANISOU 1841 CD1 ILE A1027 18529 7437 6966 2138 -1651 -402 C ATOM 1842 N GLY A1028 74.431 27.056 81.614 1.00 69.16 N ANISOU 1842 N GLY A1028 16251 5618 4410 1185 -681 -332 N ATOM 1843 CA GLY A1028 75.270 25.878 81.409 1.00 67.31 C ANISOU 1843 CA GLY A1028 15868 5511 4196 994 -609 -366 C ATOM 1844 C GLY A1028 76.447 25.816 82.358 1.00 69.07 C ANISOU 1844 C GLY A1028 16040 5843 4363 772 -318 -330 C ATOM 1845 O GLY A1028 76.285 26.036 83.562 1.00 68.21 O ANISOU 1845 O GLY A1028 15770 5795 4350 783 -188 -287 O ATOM 1846 N ILE A1029 77.645 25.537 81.816 1.00 64.87 N ANISOU 1846 N ILE A1029 15640 5353 3655 586 -217 -360 N ATOM 1847 CA ILE A1029 78.885 25.474 82.593 1.00 63.14 C ANISOU 1847 CA ILE A1029 15361 5239 3391 370 23 -345 C ATOM 1848 C ILE A1029 79.652 26.802 82.353 1.00 67.78 C ANISOU 1848 C ILE A1029 16333 5718 3702 248 146 -322 C ATOM 1849 O ILE A1029 80.544 26.889 81.501 1.00 68.05 O ANISOU 1849 O ILE A1029 16557 5749 3551 107 232 -328 O ATOM 1850 CB ILE A1029 79.726 24.196 82.272 1.00 65.30 C ANISOU 1850 CB ILE A1029 15435 5632 3744 249 65 -405 C ATOM 1851 CG1 ILE A1029 78.907 22.914 82.573 1.00 65.11 C ANISOU 1851 CG1 ILE A1029 15028 5642 4068 355 -74 -407 C ATOM 1852 CG2 ILE A1029 81.054 24.194 83.054 1.00 65.26 C ANISOU 1852 CG2 ILE A1029 15353 5740 3704 42 283 -395 C ATOM 1853 CD1 ILE A1029 79.573 21.587 82.239 1.00 70.87 C ANISOU 1853 CD1 ILE A1029 15553 6425 4951 281 -85 -487 C ATOM 1854 N GLY A1030 79.242 27.825 83.098 1.00 64.61 N ANISOU 1854 N GLY A1030 16034 5218 3296 311 159 -299 N ATOM 1855 CA GLY A1030 79.827 29.160 83.065 1.00 65.82 C ANISOU 1855 CA GLY A1030 16530 5199 3278 200 248 -280 C ATOM 1856 C GLY A1030 79.852 29.859 81.720 1.00 71.95 C ANISOU 1856 C GLY A1030 17703 5788 3848 200 193 -198 C ATOM 1857 O GLY A1030 80.782 30.627 81.454 1.00 73.31 O ANISOU 1857 O GLY A1030 18123 5848 3884 -5 335 -145 O ATOM 1858 N HIS A1031 78.838 29.612 80.863 1.00 68.93 N ANISOU 1858 N HIS A1031 17382 5368 3442 424 -20 -175 N ATOM 1859 CA HIS A1031 78.746 30.252 79.548 1.00 71.01 C ANISOU 1859 CA HIS A1031 18056 5475 3449 476 -111 -69 C ATOM 1860 C HIS A1031 78.048 31.607 79.688 1.00 75.61 C ANISOU 1860 C HIS A1031 18922 5772 4034 629 -223 10 C ATOM 1861 O HIS A1031 76.828 31.660 79.882 1.00 75.65 O ANISOU 1861 O HIS A1031 18827 5728 4188 905 -438 -29 O ATOM 1862 CB HIS A1031 78.026 29.352 78.523 1.00 72.50 C ANISOU 1862 CB HIS A1031 18198 5765 3585 666 -343 -114 C ATOM 1863 CG HIS A1031 77.710 30.043 77.231 1.00 79.28 C ANISOU 1863 CG HIS A1031 19500 6484 4138 795 -499 4 C ATOM 1864 ND1 HIS A1031 78.667 30.209 76.247 1.00 82.88 N ANISOU 1864 ND1 HIS A1031 20270 6974 4246 638 -339 102 N ATOM 1865 CD2 HIS A1031 76.551 30.604 76.811 1.00 83.23 C ANISOU 1865 CD2 HIS A1031 20169 6827 4627 1076 -795 54 C ATOM 1866 CE1 HIS A1031 78.065 30.860 75.266 1.00 85.51 C ANISOU 1866 CE1 HIS A1031 20988 7173 4329 827 -542 233 C ATOM 1867 NE2 HIS A1031 76.791 31.121 75.561 1.00 86.18 N ANISOU 1867 NE2 HIS A1031 21000 7128 4616 1101 -844 202 N ATOM 1868 N LEU A1032 78.833 32.699 79.603 1.00 72.61 N ANISOU 1868 N LEU A1032 18872 5185 3533 447 -75 117 N ATOM 1869 CA LEU A1032 78.330 34.070 79.717 1.00 74.28 C ANISOU 1869 CA LEU A1032 19396 5053 3774 569 -175 195 C ATOM 1870 C LEU A1032 77.609 34.462 78.421 1.00 79.31 C ANISOU 1870 C LEU A1032 20388 5534 4213 788 -403 365 C ATOM 1871 O LEU A1032 78.165 34.314 77.328 1.00 80.17 O ANISOU 1871 O LEU A1032 20733 5692 4038 678 -343 507 O ATOM 1872 CB LEU A1032 79.480 35.044 80.042 1.00 75.62 C ANISOU 1872 CB LEU A1032 19780 5015 3936 261 47 253 C ATOM 1873 CG LEU A1032 79.095 36.494 80.345 1.00 83.11 C ANISOU 1873 CG LEU A1032 21039 5547 4991 355 -47 293 C ATOM 1874 CD1 LEU A1032 79.807 36.999 81.577 1.00 82.76 C ANISOU 1874 CD1 LEU A1032 20887 5422 5134 153 94 125 C ATOM 1875 CD2 LEU A1032 79.363 37.400 79.152 1.00 89.59 C ANISOU 1875 CD2 LEU A1032 22359 6057 5624 280 -50 583 C ATOM 1876 N LEU A1033 76.364 34.946 78.558 1.00 75.86 N ANISOU 1876 N LEU A1033 19978 4934 3912 1121 -668 342 N ATOM 1877 CA LEU A1033 75.526 35.356 77.434 1.00 78.38 C ANISOU 1877 CA LEU A1033 20611 5096 4075 1394 -962 490 C ATOM 1878 C LEU A1033 75.826 36.819 77.068 1.00 85.24 C ANISOU 1878 C LEU A1033 21998 5550 4838 1357 -948 721 C ATOM 1879 O LEU A1033 76.275 37.075 75.949 1.00 87.65 O ANISOU 1879 O LEU A1033 22689 5788 4826 1274 -929 962 O ATOM 1880 CB LEU A1033 74.029 35.148 77.756 1.00 78.44 C ANISOU 1880 CB LEU A1033 20340 5126 4338 1783 -1271 349 C ATOM 1881 CG LEU A1033 73.561 33.698 77.991 1.00 80.10 C ANISOU 1881 CG LEU A1033 20036 5691 4708 1830 -1328 165 C ATOM 1882 CD1 LEU A1033 72.224 33.660 78.699 1.00 80.39 C ANISOU 1882 CD1 LEU A1033 19714 5732 5097 2140 -1513 29 C ATOM 1883 CD2 LEU A1033 73.506 32.897 76.692 1.00 83.30 C ANISOU 1883 CD2 LEU A1033 20527 6250 4873 1868 -1517 194 C ATOM 1884 N THR A1034 75.611 37.764 78.014 1.00 81.45 N ANISOU 1884 N THR A1034 21537 4790 4622 1415 -943 648 N ATOM 1885 CA THR A1034 75.865 39.202 77.838 1.00 84.74 C ANISOU 1885 CA THR A1034 22420 4729 5047 1377 -948 837 C ATOM 1886 C THR A1034 76.290 39.892 79.139 1.00 87.17 C ANISOU 1886 C THR A1034 22637 4840 5642 1238 -792 648 C ATOM 1887 O THR A1034 75.917 39.464 80.236 1.00 83.98 O ANISOU 1887 O THR A1034 21841 4635 5432 1340 -773 365 O ATOM 1888 CB THR A1034 74.626 39.952 77.288 1.00 96.70 C ANISOU 1888 CB THR A1034 24195 5948 6598 1808 -1320 949 C ATOM 1889 OG1 THR A1034 73.436 39.483 77.927 1.00 93.79 O ANISOU 1889 OG1 THR A1034 23414 5749 6474 2154 -1518 690 O ATOM 1890 CG2 THR A1034 74.494 39.867 75.777 1.00 98.93 C ANISOU 1890 CG2 THR A1034 24840 6241 6509 1897 -1491 1249 C ATOM 1891 N LYS A1035 77.033 41.005 78.993 1.00 86.14 N ANISOU 1891 N LYS A1035 22892 4302 5536 1017 -695 812 N ATOM 1892 CA LYS A1035 77.454 41.879 80.088 1.00 86.36 C ANISOU 1892 CA LYS A1035 22929 4037 5846 889 -610 625 C ATOM 1893 C LYS A1035 76.300 42.839 80.432 1.00 91.88 C ANISOU 1893 C LYS A1035 23775 4361 6776 1309 -888 526 C ATOM 1894 O LYS A1035 76.347 43.546 81.443 1.00 92.53 O ANISOU 1894 O LYS A1035 23837 4211 7109 1329 -881 280 O ATOM 1895 CB LYS A1035 78.736 42.652 79.707 1.00 91.72 C ANISOU 1895 CB LYS A1035 23937 4394 6519 448 -405 850 C ATOM 1896 CG LYS A1035 79.985 41.795 79.473 1.00101.52 C ANISOU 1896 CG LYS A1035 24988 5998 7587 23 -94 909 C ATOM 1897 CD LYS A1035 80.641 41.318 80.765 1.00107.07 C ANISOU 1897 CD LYS A1035 25267 6951 8464 -175 50 560 C ATOM 1898 CE LYS A1035 81.912 40.555 80.490 1.00116.46 C ANISOU 1898 CE LYS A1035 26266 8453 9529 -577 337 626 C ATOM 1899 NZ LYS A1035 82.574 40.117 81.746 1.00123.79 N ANISOU 1899 NZ LYS A1035 26795 9616 10625 -750 431 303 N ATOM 1900 N SER A1036 75.261 42.838 79.566 1.00 89.03 N ANISOU 1900 N SER A1036 23551 3953 6324 1668 -1152 695 N ATOM 1901 CA SER A1036 74.031 43.624 79.624 1.00 91.69 C ANISOU 1901 CA SER A1036 24007 3970 6863 2139 -1463 645 C ATOM 1902 C SER A1036 73.207 43.321 80.885 1.00 92.62 C ANISOU 1902 C SER A1036 23657 4309 7226 2426 -1487 230 C ATOM 1903 O SER A1036 73.080 42.149 81.256 1.00 88.27 O ANISOU 1903 O SER A1036 22664 4261 6612 2401 -1381 87 O ATOM 1904 CB SER A1036 73.183 43.339 78.386 1.00 96.92 C ANISOU 1904 CB SER A1036 24807 4692 7324 2432 -1747 898 C ATOM 1905 OG SER A1036 71.929 44.000 78.422 1.00109.22 O ANISOU 1905 OG SER A1036 26413 5983 9104 2927 -2082 838 O ATOM 1906 N PRO A1037 72.592 44.349 81.525 1.00 91.56 N ANISOU 1906 N PRO A1037 23612 3803 7373 2724 -1621 42 N ATOM 1907 CA PRO A1037 71.771 44.084 82.721 1.00 89.81 C ANISOU 1907 CA PRO A1037 22944 3835 7346 3029 -1600 -352 C ATOM 1908 C PRO A1037 70.372 43.556 82.369 1.00 92.63 C ANISOU 1908 C PRO A1037 23011 4415 7771 3474 -1826 -356 C ATOM 1909 O PRO A1037 69.612 43.210 83.276 1.00 91.42 O ANISOU 1909 O PRO A1037 22428 4531 7776 3726 -1773 -639 O ATOM 1910 CB PRO A1037 71.681 45.456 83.413 1.00 95.85 C ANISOU 1910 CB PRO A1037 23958 4082 8378 3199 -1668 -567 C ATOM 1911 CG PRO A1037 72.476 46.413 82.566 1.00103.67 C ANISOU 1911 CG PRO A1037 25517 4510 9361 2945 -1736 -252 C ATOM 1912 CD PRO A1037 72.622 45.792 81.220 1.00 98.28 C ANISOU 1912 CD PRO A1037 24968 3983 8390 2807 -1783 172 C ATOM 1913 N SER A1038 70.035 43.485 81.064 1.00 89.43 N ANISOU 1913 N SER A1038 22824 3917 7239 3568 -2076 -45 N ATOM 1914 CA SER A1038 68.740 43.013 80.577 1.00 89.41 C ANISOU 1914 CA SER A1038 22561 4093 7317 3976 -2363 -41 C ATOM 1915 C SER A1038 68.709 41.486 80.458 1.00 87.39 C ANISOU 1915 C SER A1038 21861 4410 6931 3820 -2269 -62 C ATOM 1916 O SER A1038 69.638 40.881 79.913 1.00 84.41 O ANISOU 1916 O SER A1038 21606 4191 6276 3453 -2140 104 O ATOM 1917 CB SER A1038 68.415 43.649 79.229 1.00 96.76 C ANISOU 1917 CB SER A1038 23961 4664 8140 4166 -2724 291 C ATOM 1918 OG SER A1038 67.179 43.189 78.708 1.00105.80 O ANISOU 1918 OG SER A1038 24845 5986 9369 4564 -3061 278 O ATOM 1919 N LEU A1039 67.630 40.875 80.982 1.00 82.29 N ANISOU 1919 N LEU A1039 20683 4060 6523 4105 -2326 -271 N ATOM 1920 CA LEU A1039 67.381 39.434 80.944 1.00 78.20 C ANISOU 1920 CA LEU A1039 19683 4032 5999 4007 -2278 -309 C ATOM 1921 C LEU A1039 66.956 39.019 79.530 1.00 83.40 C ANISOU 1921 C LEU A1039 20455 4705 6527 4111 -2645 -117 C ATOM 1922 O LEU A1039 67.475 38.027 79.018 1.00 80.42 O ANISOU 1922 O LEU A1039 20023 4587 5948 3845 -2596 -43 O ATOM 1923 CB LEU A1039 66.311 39.044 81.991 1.00 78.05 C ANISOU 1923 CB LEU A1039 19055 4276 6326 4280 -2201 -567 C ATOM 1924 CG LEU A1039 65.758 37.603 81.986 1.00 80.06 C ANISOU 1924 CG LEU A1039 18735 4973 6709 4240 -2198 -599 C ATOM 1925 CD1 LEU A1039 66.839 36.569 82.274 1.00 75.37 C ANISOU 1925 CD1 LEU A1039 18049 4669 5918 3785 -1895 -556 C ATOM 1926 CD2 LEU A1039 64.633 37.453 82.987 1.00 83.60 C ANISOU 1926 CD2 LEU A1039 18614 5624 7527 4537 -2101 -805 C ATOM 1927 N ASN A1040 66.035 39.788 78.900 1.00 84.34 N ANISOU 1927 N ASN A1040 20749 4544 6754 4516 -3031 -54 N ATOM 1928 CA ASN A1040 65.528 39.547 77.544 1.00 86.54 C ANISOU 1928 CA ASN A1040 21182 4817 6884 4692 -3459 116 C ATOM 1929 C ASN A1040 66.645 39.625 76.500 1.00 90.98 C ANISOU 1929 C ASN A1040 22325 5285 6957 4389 -3432 408 C ATOM 1930 O ASN A1040 66.574 38.908 75.500 1.00 90.89 O ANISOU 1930 O ASN A1040 22356 5470 6709 4379 -3647 492 O ATOM 1931 CB ASN A1040 64.420 40.537 77.186 1.00 91.70 C ANISOU 1931 CB ASN A1040 21957 5138 7745 5205 -3878 141 C ATOM 1932 CG ASN A1040 63.085 40.254 77.835 1.00111.87 C ANISOU 1932 CG ASN A1040 23863 7865 10778 5574 -4006 -132 C ATOM 1933 OD1 ASN A1040 62.673 39.100 78.014 1.00102.61 O ANISOU 1933 OD1 ASN A1040 22146 7084 9755 5508 -3978 -271 O ATOM 1934 ND2 ASN A1040 62.334 41.308 78.113 1.00107.17 N ANISOU 1934 ND2 ASN A1040 23305 6956 10458 5988 -4176 -201 N ATOM 1935 N ALA A1041 67.671 40.479 76.733 1.00 87.99 N ANISOU 1935 N ALA A1041 22375 4618 6438 4141 -3164 545 N ATOM 1936 CA ALA A1041 68.833 40.623 75.847 1.00 88.32 C ANISOU 1936 CA ALA A1041 22940 4573 6044 3808 -3040 846 C ATOM 1937 C ALA A1041 69.661 39.334 75.839 1.00 88.17 C ANISOU 1937 C ALA A1041 22675 5001 5825 3423 -2761 774 C ATOM 1938 O ALA A1041 70.083 38.880 74.773 1.00 88.34 O ANISOU 1938 O ALA A1041 22932 5161 5473 3309 -2814 944 O ATOM 1939 CB ALA A1041 69.690 41.802 76.283 1.00 90.34 C ANISOU 1939 CB ALA A1041 23592 4406 6328 3605 -2798 966 C ATOM 1940 N ALA A1042 69.858 38.732 77.027 1.00 80.90 N ANISOU 1940 N ALA A1042 21283 4313 5143 3257 -2475 518 N ATOM 1941 CA ALA A1042 70.582 37.477 77.201 1.00 76.50 C ANISOU 1941 CA ALA A1042 20429 4155 4484 2927 -2221 427 C ATOM 1942 C ALA A1042 69.736 36.296 76.726 1.00 80.20 C ANISOU 1942 C ALA A1042 20524 4939 5011 3097 -2478 313 C ATOM 1943 O ALA A1042 70.283 35.336 76.178 1.00 78.08 O ANISOU 1943 O ALA A1042 20215 4920 4533 2893 -2422 316 O ATOM 1944 CB ALA A1042 70.963 37.297 78.658 1.00 73.90 C ANISOU 1944 CB ALA A1042 19743 3943 4392 2749 -1884 220 C ATOM 1945 N LYS A1043 68.399 36.376 76.937 1.00 78.74 N ANISOU 1945 N LYS A1043 20046 4729 5144 3476 -2768 190 N ATOM 1946 CA LYS A1043 67.415 35.362 76.542 1.00 78.83 C ANISOU 1946 CA LYS A1043 19642 4984 5326 3666 -3071 58 C ATOM 1947 C LYS A1043 67.390 35.238 75.012 1.00 86.20 C ANISOU 1947 C LYS A1043 20954 5909 5891 3758 -3430 193 C ATOM 1948 O LYS A1043 67.376 34.120 74.499 1.00 84.65 O ANISOU 1948 O LYS A1043 20560 5972 5629 3682 -3542 91 O ATOM 1949 CB LYS A1043 66.023 35.715 77.102 1.00 83.15 C ANISOU 1949 CB LYS A1043 19811 5464 6319 4062 -3286 -82 C ATOM 1950 CG LYS A1043 64.983 34.600 76.977 1.00 90.75 C ANISOU 1950 CG LYS A1043 20191 6689 7600 4204 -3539 -251 C ATOM 1951 CD LYS A1043 63.643 34.937 77.645 1.00 97.64 C ANISOU 1951 CD LYS A1043 20603 7530 8964 4573 -3674 -393 C ATOM 1952 CE LYS A1043 63.670 34.876 79.157 1.00 98.37 C ANISOU 1952 CE LYS A1043 20300 7750 9326 4480 -3218 -509 C ATOM 1953 NZ LYS A1043 62.333 35.153 79.740 1.00107.34 N ANISOU 1953 NZ LYS A1043 20954 8901 10928 4859 -3318 -654 N ATOM 1954 N SER A1044 67.429 36.386 74.296 1.00 87.31 N ANISOU 1954 N SER A1044 21660 5741 5772 3920 -3605 425 N ATOM 1955 CA SER A1044 67.465 36.451 72.832 1.00 90.99 C ANISOU 1955 CA SER A1044 22595 6192 5785 4033 -3926 612 C ATOM 1956 C SER A1044 68.819 35.960 72.305 1.00 93.34 C ANISOU 1956 C SER A1044 23180 6662 5622 3640 -3605 722 C ATOM 1957 O SER A1044 68.857 35.278 71.280 1.00 94.41 O ANISOU 1957 O SER A1044 23435 7012 5426 3670 -3802 711 O ATOM 1958 CB SER A1044 67.190 37.871 72.347 1.00 99.82 C ANISOU 1958 CB SER A1044 24251 6902 6775 4299 -4149 887 C ATOM 1959 OG SER A1044 65.912 38.320 72.765 1.00111.75 O ANISOU 1959 OG SER A1044 25480 8256 8722 4711 -4472 762 O ATOM 1960 N GLU A1045 69.922 36.291 73.022 1.00 87.32 N ANISOU 1960 N GLU A1045 22501 5823 4853 3285 -3119 796 N ATOM 1961 CA GLU A1045 71.298 35.879 72.712 1.00 85.31 C ANISOU 1961 CA GLU A1045 22436 5731 4247 2885 -2741 885 C ATOM 1962 C GLU A1045 71.434 34.360 72.773 1.00 85.41 C ANISOU 1962 C GLU A1045 21998 6142 4312 2756 -2689 618 C ATOM 1963 O GLU A1045 72.190 33.777 71.996 1.00 84.86 O ANISOU 1963 O GLU A1045 22096 6273 3873 2593 -2582 644 O ATOM 1964 CB GLU A1045 72.290 36.537 73.685 1.00 84.70 C ANISOU 1964 CB GLU A1045 22405 5476 4301 2558 -2291 951 C ATOM 1965 CG GLU A1045 73.081 37.685 73.081 1.00 99.70 C ANISOU 1965 CG GLU A1045 24918 7069 5893 2414 -2145 1304 C ATOM 1966 CD GLU A1045 74.211 37.294 72.147 1.00122.72 C ANISOU 1966 CD GLU A1045 28111 10183 8333 2126 -1892 1479 C ATOM 1967 OE1 GLU A1045 75.010 36.400 72.512 1.00117.77 O ANISOU 1967 OE1 GLU A1045 27178 9845 7724 1842 -1593 1310 O ATOM 1968 OE2 GLU A1045 74.342 37.935 71.080 1.00119.92 O ANISOU 1968 OE2 GLU A1045 28290 9687 7589 2186 -1965 1803 O ATOM 1969 N LEU A1046 70.686 33.732 73.699 1.00 79.58 N ANISOU 1969 N LEU A1046 20686 5507 4045 2839 -2756 369 N ATOM 1970 CA LEU A1046 70.623 32.288 73.902 1.00 76.59 C ANISOU 1970 CA LEU A1046 19816 5435 3848 2741 -2747 124 C ATOM 1971 C LEU A1046 69.864 31.631 72.742 1.00 83.62 C ANISOU 1971 C LEU A1046 20713 6449 4609 2985 -3214 16 C ATOM 1972 O LEU A1046 70.332 30.625 72.211 1.00 82.21 O ANISOU 1972 O LEU A1046 20482 6490 4265 2857 -3200 -110 O ATOM 1973 CB LEU A1046 69.944 31.988 75.256 1.00 74.08 C ANISOU 1973 CB LEU A1046 18917 5148 4080 2776 -2672 -39 C ATOM 1974 CG LEU A1046 69.745 30.525 75.663 1.00 76.05 C ANISOU 1974 CG LEU A1046 18601 5657 4637 2673 -2654 -249 C ATOM 1975 CD1 LEU A1046 71.076 29.831 75.929 1.00 72.88 C ANISOU 1975 CD1 LEU A1046 18183 5413 4094 2306 -2274 -259 C ATOM 1976 CD2 LEU A1046 68.868 30.433 76.893 1.00 77.49 C ANISOU 1976 CD2 LEU A1046 18262 5856 5326 2771 -2600 -336 C ATOM 1977 N ASP A1047 68.712 32.219 72.340 1.00 84.41 N ANISOU 1977 N ASP A1047 20882 6403 4787 3353 -3648 44 N ATOM 1978 CA ASP A1047 67.860 31.748 71.238 1.00 88.16 C ANISOU 1978 CA ASP A1047 21373 6972 5152 3639 -4186 -72 C ATOM 1979 C ASP A1047 68.605 31.789 69.902 1.00 94.82 C ANISOU 1979 C ASP A1047 22813 7904 5310 3616 -4240 56 C ATOM 1980 O ASP A1047 68.366 30.938 69.049 1.00 95.62 O ANISOU 1980 O ASP A1047 22887 8204 5239 3716 -4550 -134 O ATOM 1981 CB ASP A1047 66.576 32.596 71.140 1.00 94.08 C ANISOU 1981 CB ASP A1047 22117 7514 6114 4053 -4624 -25 C ATOM 1982 CG ASP A1047 65.697 32.607 72.380 1.00103.25 C ANISOU 1982 CG ASP A1047 22674 8619 7936 4143 -4582 -164 C ATOM 1983 OD1 ASP A1047 65.830 31.688 73.214 1.00 99.86 O ANISOU 1983 OD1 ASP A1047 21746 8358 7838 3917 -4322 -328 O ATOM 1984 OD2 ASP A1047 64.874 33.538 72.514 1.00112.93 O ANISOU 1984 OD2 ASP A1047 23929 9635 9344 4454 -4800 -98 O ATOM 1985 N LYS A1048 69.500 32.779 69.731 1.00 92.96 N ANISOU 1985 N LYS A1048 23107 7520 4692 3482 -3932 371 N ATOM 1986 CA LYS A1048 70.323 32.975 68.539 1.00 96.21 C ANISOU 1986 CA LYS A1048 24119 8018 4418 3426 -3861 575 C ATOM 1987 C LYS A1048 71.454 31.932 68.502 1.00 98.11 C ANISOU 1987 C LYS A1048 24234 8550 4494 3089 -3474 420 C ATOM 1988 O LYS A1048 71.723 31.367 67.441 1.00100.19 O ANISOU 1988 O LYS A1048 24727 9044 4296 3141 -3581 348 O ATOM 1989 CB LYS A1048 70.886 34.410 68.524 1.00100.78 C ANISOU 1989 CB LYS A1048 25231 8290 4770 3350 -3613 994 C ATOM 1990 CG LYS A1048 71.559 34.823 67.211 1.00120.22 C ANISOU 1990 CG LYS A1048 28372 10805 6500 3345 -3562 1307 C ATOM 1991 CD LYS A1048 72.030 36.287 67.203 1.00132.64 C ANISOU 1991 CD LYS A1048 30463 12003 7933 3259 -3340 1767 C ATOM 1992 CE LYS A1048 73.241 36.563 68.069 1.00140.06 C ANISOU 1992 CE LYS A1048 31318 12844 9055 2797 -2730 1847 C ATOM 1993 NZ LYS A1048 73.631 37.996 68.026 1.00152.18 N ANISOU 1993 NZ LYS A1048 33345 13955 10520 2710 -2567 2280 N ATOM 1994 N ALA A1049 72.099 31.674 69.659 1.00 90.80 N ANISOU 1994 N ALA A1049 22945 7621 3936 2774 -3045 351 N ATOM 1995 CA ALA A1049 73.194 30.711 69.804 1.00 88.07 C ANISOU 1995 CA ALA A1049 22414 7516 3532 2460 -2669 204 C ATOM 1996 C ALA A1049 72.707 29.263 69.627 1.00 92.34 C ANISOU 1996 C ALA A1049 22532 8284 4269 2549 -2938 -172 C ATOM 1997 O ALA A1049 73.425 28.454 69.035 1.00 92.31 O ANISOU 1997 O ALA A1049 22576 8503 3993 2447 -2822 -314 O ATOM 1998 CB ALA A1049 73.852 30.872 71.165 1.00 84.31 C ANISOU 1998 CB ALA A1049 21642 6954 3437 2156 -2235 231 C ATOM 1999 N ILE A1050 71.494 28.947 70.129 1.00 88.93 N ANISOU 1999 N ILE A1050 21675 7782 4333 2739 -3290 -339 N ATOM 2000 CA ILE A1050 70.885 27.614 70.044 1.00 88.55 C ANISOU 2000 CA ILE A1050 21169 7874 4600 2810 -3588 -686 C ATOM 2001 C ILE A1050 70.161 27.452 68.684 1.00 98.31 C ANISOU 2001 C ILE A1050 22662 9187 5505 3133 -4144 -820 C ATOM 2002 O ILE A1050 70.398 26.463 67.987 1.00 98.91 O ANISOU 2002 O ILE A1050 22722 9446 5412 3134 -4273 -1080 O ATOM 2003 CB ILE A1050 69.918 27.367 71.251 1.00 89.17 C ANISOU 2003 CB ILE A1050 20631 7848 5400 2836 -3667 -772 C ATOM 2004 CG1 ILE A1050 70.662 27.366 72.623 1.00 84.84 C ANISOU 2004 CG1 ILE A1050 19824 7283 5131 2531 -3137 -677 C ATOM 2005 CG2 ILE A1050 69.050 26.107 71.078 1.00 90.71 C ANISOU 2005 CG2 ILE A1050 20341 8122 6002 2932 -4059 -1095 C ATOM 2006 CD1 ILE A1050 71.754 26.246 72.880 1.00 89.09 C ANISOU 2006 CD1 ILE A1050 20168 7986 5696 2231 -2815 -802 C ATOM 2007 N GLY A1051 69.298 28.410 68.341 1.00 98.84 N ANISOU 2007 N GLY A1051 22959 9108 5486 3421 -4485 -662 N ATOM 2008 CA GLY A1051 68.488 28.386 67.125 1.00104.39 C ANISOU 2008 CA GLY A1051 23905 9872 5887 3776 -5085 -767 C ATOM 2009 C GLY A1051 67.012 28.266 67.453 1.00110.41 C ANISOU 2009 C GLY A1051 24188 10524 7239 4032 -5588 -934 C ATOM 2010 O GLY A1051 66.160 28.775 66.720 1.00114.86 O ANISOU 2010 O GLY A1051 24958 11037 7645 4379 -6098 -906 O ATOM 2011 N ARG A1052 66.714 27.588 68.575 1.00103.68 N ANISOU 2011 N ARG A1052 22676 9642 7075 3861 -5435 -1091 N ATOM 2012 CA ARG A1052 65.387 27.334 69.140 1.00104.42 C ANISOU 2012 CA ARG A1052 22161 9652 7862 4020 -5771 -1247 C ATOM 2013 C ARG A1052 64.960 28.502 70.042 1.00107.73 C ANISOU 2013 C ARG A1052 22523 9877 8533 4113 -5597 -995 C ATOM 2014 O ARG A1052 65.793 29.046 70.771 1.00103.95 O ANISOU 2014 O ARG A1052 22202 9335 7958 3900 -5078 -786 O ATOM 2015 CB ARG A1052 65.440 26.007 69.935 1.00101.46 C ANISOU 2015 CB ARG A1052 21143 9347 8059 3746 -5587 -1479 C ATOM 2016 CG ARG A1052 64.248 25.692 70.835 1.00112.12 C ANISOU 2016 CG ARG A1052 21770 10621 10208 3797 -5723 -1571 C ATOM 2017 CD ARG A1052 64.642 24.668 71.881 1.00118.46 C ANISOU 2017 CD ARG A1052 22070 11464 11476 3455 -5316 -1624 C ATOM 2018 NE ARG A1052 63.756 24.710 73.045 1.00127.34 N ANISOU 2018 NE ARG A1052 22593 12532 13259 3457 -5196 -1561 N ATOM 2019 CZ ARG A1052 64.030 24.150 74.220 1.00139.25 C ANISOU 2019 CZ ARG A1052 23695 14069 15143 3191 -4752 -1488 C ATOM 2020 NH1 ARG A1052 65.180 23.514 74.409 1.00123.98 N ANISOU 2020 NH1 ARG A1052 21882 12195 13029 2906 -4415 -1472 N ATOM 2021 NH2 ARG A1052 63.167 24.242 75.222 1.00126.79 N ANISOU 2021 NH2 ARG A1052 21593 12478 14105 3227 -4631 -1417 N ATOM 2022 N ASN A1053 63.663 28.868 70.005 1.00107.96 N ANISOU 2022 N ASN A1053 22299 9811 8910 4441 -6045 -1048 N ATOM 2023 CA ASN A1053 63.101 29.923 70.850 1.00108.02 C ANISOU 2023 CA ASN A1053 22187 9633 9221 4596 -5930 -878 C ATOM 2024 C ASN A1053 62.920 29.373 72.275 1.00108.24 C ANISOU 2024 C ASN A1053 21539 9706 9882 4380 -5533 -961 C ATOM 2025 O ASN A1053 61.910 28.727 72.569 1.00109.13 O ANISOU 2025 O ASN A1053 21029 9870 10565 4463 -5760 -1148 O ATOM 2026 CB ASN A1053 61.776 30.448 70.263 1.00115.09 C ANISOU 2026 CB ASN A1053 23015 10432 10283 5055 -6567 -928 C ATOM 2027 CG ASN A1053 61.074 31.505 71.092 1.00140.62 C ANISOU 2027 CG ASN A1053 26074 13468 13887 5281 -6496 -807 C ATOM 2028 OD1 ASN A1053 61.694 32.359 71.742 1.00132.82 O ANISOU 2028 OD1 ASN A1053 25359 12337 12770 5186 -6059 -599 O ATOM 2029 ND2 ASN A1053 59.750 31.497 71.051 1.00136.87 N ANISOU 2029 ND2 ASN A1053 25138 12974 13893 5606 -6955 -961 N ATOM 2030 N THR A1054 63.929 29.592 73.141 1.00100.71 N ANISOU 2030 N THR A1054 20704 8746 8816 4093 -4942 -813 N ATOM 2031 CA THR A1054 63.934 29.111 74.528 1.00 97.04 C ANISOU 2031 CA THR A1054 19693 8354 8822 3879 -4513 -846 C ATOM 2032 C THR A1054 63.477 30.206 75.497 1.00101.59 C ANISOU 2032 C THR A1054 20188 8804 9608 4047 -4315 -740 C ATOM 2033 O THR A1054 63.798 31.383 75.306 1.00102.29 O ANISOU 2033 O THR A1054 20786 8710 9371 4165 -4287 -587 O ATOM 2034 CB THR A1054 65.329 28.598 74.939 1.00 99.97 C ANISOU 2034 CB THR A1054 20209 8825 8951 3479 -4023 -787 C ATOM 2035 OG1 THR A1054 66.288 29.649 74.820 1.00 98.89 O ANISOU 2035 OG1 THR A1054 20674 8577 8324 3418 -3780 -588 O ATOM 2036 CG2 THR A1054 65.783 27.396 74.130 1.00 98.54 C ANISOU 2036 CG2 THR A1054 20025 8775 8640 3319 -4169 -941 C ATOM 2037 N ASN A1055 62.747 29.805 76.552 1.00 97.65 N ANISOU 2037 N ASN A1055 19049 8396 9658 4053 -4155 -821 N ATOM 2038 CA ASN A1055 62.259 30.711 77.594 1.00 97.99 C ANISOU 2038 CA ASN A1055 18930 8372 9928 4230 -3921 -781 C ATOM 2039 C ASN A1055 63.198 30.643 78.818 1.00 97.24 C ANISOU 2039 C ASN A1055 18820 8372 9754 3929 -3317 -708 C ATOM 2040 O ASN A1055 62.751 30.743 79.965 1.00 96.65 O ANISOU 2040 O ASN A1055 18357 8385 9982 3980 -3032 -732 O ATOM 2041 CB ASN A1055 60.810 30.361 77.967 1.00101.81 C ANISOU 2041 CB ASN A1055 18703 8939 11043 4461 -4108 -914 C ATOM 2042 CG ASN A1055 59.832 31.487 77.735 1.00126.25 C ANISOU 2042 CG ASN A1055 21838 11864 14267 4914 -4424 -941 C ATOM 2043 OD1 ASN A1055 59.867 32.527 78.405 1.00119.70 O ANISOU 2043 OD1 ASN A1055 21170 10920 13390 5066 -4189 -894 O ATOM 2044 ND2 ASN A1055 58.906 31.284 76.809 1.00121.37 N ANISOU 2044 ND2 ASN A1055 21044 11220 13851 5159 -4989 -1044 N ATOM 2045 N GLY A1056 64.494 30.489 78.541 1.00 90.60 N ANISOU 2045 N GLY A1056 18405 7532 8486 3636 -3135 -625 N ATOM 2046 CA GLY A1056 65.541 30.370 79.548 1.00 86.55 C ANISOU 2046 CA GLY A1056 17924 7112 7848 3334 -2631 -564 C ATOM 2047 C GLY A1056 65.898 28.933 79.879 1.00 87.62 C ANISOU 2047 C GLY A1056 17677 7464 8151 3043 -2464 -591 C ATOM 2048 O GLY A1056 66.900 28.687 80.555 1.00 84.15 O ANISOU 2048 O GLY A1056 17294 7113 7564 2778 -2100 -533 O ATOM 2049 N VAL A1057 65.074 27.974 79.403 1.00 85.56 N ANISOU 2049 N VAL A1057 17014 7266 8231 3095 -2759 -686 N ATOM 2050 CA VAL A1057 65.242 26.534 79.625 1.00 83.57 C ANISOU 2050 CA VAL A1057 16357 7153 8244 2843 -2675 -718 C ATOM 2051 C VAL A1057 66.029 25.912 78.461 1.00 86.02 C ANISOU 2051 C VAL A1057 16985 7440 8258 2701 -2883 -793 C ATOM 2052 O VAL A1057 65.703 26.150 77.298 1.00 88.29 O ANISOU 2052 O VAL A1057 17521 7648 8377 2879 -3291 -882 O ATOM 2053 CB VAL A1057 63.891 25.783 79.849 1.00 90.33 C ANISOU 2053 CB VAL A1057 16532 8060 9731 2945 -2859 -791 C ATOM 2054 CG1 VAL A1057 63.299 26.102 81.215 1.00 90.61 C ANISOU 2054 CG1 VAL A1057 16167 8203 10058 3014 -2497 -697 C ATOM 2055 CG2 VAL A1057 62.872 26.059 78.739 1.00 94.28 C ANISOU 2055 CG2 VAL A1057 17021 8451 10351 3240 -3421 -934 C ATOM 2056 N ILE A1058 67.080 25.137 78.782 1.00 79.04 N ANISOU 2056 N ILE A1058 16106 6641 7286 2405 -2603 -764 N ATOM 2057 CA ILE A1058 67.903 24.429 77.791 1.00 78.17 C ANISOU 2057 CA ILE A1058 16241 6539 6921 2268 -2732 -867 C ATOM 2058 C ILE A1058 68.095 22.969 78.252 1.00 80.35 C ANISOU 2058 C ILE A1058 16070 6877 7581 2044 -2630 -915 C ATOM 2059 O ILE A1058 67.892 22.665 79.429 1.00 78.70 O ANISOU 2059 O ILE A1058 15476 6723 7704 1948 -2359 -793 O ATOM 2060 CB ILE A1058 69.274 25.113 77.480 1.00 79.39 C ANISOU 2060 CB ILE A1058 16978 6698 6487 2145 -2492 -782 C ATOM 2061 CG1 ILE A1058 70.228 25.120 78.701 1.00 76.38 C ANISOU 2061 CG1 ILE A1058 16533 6395 6095 1902 -2008 -654 C ATOM 2062 CG2 ILE A1058 69.093 26.506 76.848 1.00 82.21 C ANISOU 2062 CG2 ILE A1058 17823 6934 6478 2356 -2636 -704 C ATOM 2063 CD1 ILE A1058 71.695 25.433 78.382 1.00 81.94 C ANISOU 2063 CD1 ILE A1058 17674 7122 6337 1709 -1772 -608 C ATOM 2064 N THR A1059 68.477 22.076 77.324 1.00 77.29 N ANISOU 2064 N THR A1059 15751 6477 7140 1978 -2847 -1091 N ATOM 2065 CA THR A1059 68.716 20.664 77.634 1.00 76.19 C ANISOU 2065 CA THR A1059 15231 6332 7385 1778 -2797 -1157 C ATOM 2066 C THR A1059 70.216 20.431 77.854 1.00 76.67 C ANISOU 2066 C THR A1059 15535 6465 7130 1567 -2448 -1104 C ATOM 2067 O THR A1059 71.030 21.267 77.452 1.00 75.39 O ANISOU 2067 O THR A1059 15846 6356 6444 1574 -2320 -1073 O ATOM 2068 CB THR A1059 68.163 19.754 76.523 1.00 87.29 C ANISOU 2068 CB THR A1059 16512 7650 9004 1855 -3286 -1445 C ATOM 2069 OG1 THR A1059 68.853 20.016 75.302 1.00 87.02 O ANISOU 2069 OG1 THR A1059 17009 7657 8397 1938 -3444 -1607 O ATOM 2070 CG2 THR A1059 66.657 19.902 76.328 1.00 89.67 C ANISOU 2070 CG2 THR A1059 16490 7880 9701 2054 -3674 -1518 C ATOM 2071 N LYS A1060 70.573 19.290 78.487 1.00 71.86 N ANISOU 2071 N LYS A1060 14584 5845 6876 1379 -2301 -1079 N ATOM 2072 CA LYS A1060 71.950 18.858 78.774 1.00 69.05 C ANISOU 2072 CA LYS A1060 14348 5550 6338 1191 -2006 -1044 C ATOM 2073 C LYS A1060 72.790 18.832 77.478 1.00 72.98 C ANISOU 2073 C LYS A1060 15262 6074 6394 1223 -2125 -1270 C ATOM 2074 O LYS A1060 73.960 19.222 77.500 1.00 70.78 O ANISOU 2074 O LYS A1060 15267 5894 5733 1127 -1847 -1219 O ATOM 2075 CB LYS A1060 71.929 17.468 79.445 1.00 71.55 C ANISOU 2075 CB LYS A1060 14195 5788 7204 1041 -1966 -1006 C ATOM 2076 CG LYS A1060 73.294 16.908 79.837 1.00 84.31 C ANISOU 2076 CG LYS A1060 15864 7450 8718 874 -1697 -962 C ATOM 2077 CD LYS A1060 73.173 15.487 80.380 1.00 96.04 C ANISOU 2077 CD LYS A1060 16905 8797 10790 756 -1725 -912 C ATOM 2078 CE LYS A1060 74.507 14.801 80.574 1.00106.37 C ANISOU 2078 CE LYS A1060 18257 10116 12042 638 -1549 -921 C ATOM 2079 NZ LYS A1060 75.186 14.495 79.284 1.00116.78 N ANISOU 2079 NZ LYS A1060 19835 11410 13126 699 -1721 -1267 N ATOM 2080 N ASP A1061 72.168 18.398 76.358 1.00 72.05 N ANISOU 2080 N ASP A1061 15166 5886 6323 1365 -2539 -1528 N ATOM 2081 CA ASP A1061 72.772 18.326 75.025 1.00 73.35 C ANISOU 2081 CA ASP A1061 15727 6109 6033 1450 -2693 -1776 C ATOM 2082 C ASP A1061 73.068 19.737 74.504 1.00 75.93 C ANISOU 2082 C ASP A1061 16581 6539 5728 1544 -2596 -1653 C ATOM 2083 O ASP A1061 74.184 19.990 74.048 1.00 74.87 O ANISOU 2083 O ASP A1061 16792 6516 5138 1481 -2368 -1657 O ATOM 2084 CB ASP A1061 71.850 17.565 74.050 1.00 79.30 C ANISOU 2084 CB ASP A1061 16356 6765 7008 1610 -3219 -2098 C ATOM 2085 CG ASP A1061 71.483 16.155 74.485 1.00 92.26 C ANISOU 2085 CG ASP A1061 17469 8234 9352 1502 -3359 -2225 C ATOM 2086 OD1 ASP A1061 71.728 15.210 73.703 1.00 95.17 O ANISOU 2086 OD1 ASP A1061 17842 8541 9778 1534 -3593 -2553 O ATOM 2087 OD2 ASP A1061 70.944 15.997 75.606 1.00 97.70 O ANISOU 2087 OD2 ASP A1061 17745 8842 10536 1392 -3228 -1994 O ATOM 2088 N GLU A1062 72.076 20.658 74.609 1.00 72.67 N ANISOU 2088 N GLU A1062 16207 6075 5329 1691 -2751 -1526 N ATOM 2089 CA GLU A1062 72.184 22.069 74.209 1.00 72.81 C ANISOU 2089 CA GLU A1062 16709 6117 4840 1797 -2696 -1363 C ATOM 2090 C GLU A1062 73.257 22.776 75.034 1.00 73.10 C ANISOU 2090 C GLU A1062 16898 6192 4683 1596 -2204 -1131 C ATOM 2091 O GLU A1062 73.987 23.613 74.501 1.00 73.09 O ANISOU 2091 O GLU A1062 17350 6225 4195 1574 -2052 -1034 O ATOM 2092 CB GLU A1062 70.836 22.792 74.362 1.00 75.84 C ANISOU 2092 CB GLU A1062 16996 6399 5421 2011 -2970 -1288 C ATOM 2093 CG GLU A1062 69.810 22.434 73.299 1.00 89.96 C ANISOU 2093 CG GLU A1062 18756 8155 7269 2253 -3527 -1515 C ATOM 2094 CD GLU A1062 68.409 22.977 73.520 1.00110.51 C ANISOU 2094 CD GLU A1062 21132 10662 10197 2472 -3826 -1472 C ATOM 2095 OE1 GLU A1062 67.957 23.022 74.687 1.00100.14 O ANISOU 2095 OE1 GLU A1062 19412 9309 9328 2409 -3630 -1348 O ATOM 2096 OE2 GLU A1062 67.734 23.289 72.512 1.00108.22 O ANISOU 2096 OE2 GLU A1062 21041 10352 9725 2726 -4274 -1579 O ATOM 2097 N ALA A1063 73.358 22.411 76.331 1.00 66.72 N ANISOU 2097 N ALA A1063 15706 5383 4262 1443 -1963 -1038 N ATOM 2098 CA ALA A1063 74.347 22.919 77.282 1.00 63.58 C ANISOU 2098 CA ALA A1063 15367 5033 3756 1249 -1541 -862 C ATOM 2099 C ALA A1063 75.756 22.457 76.907 1.00 66.38 C ANISOU 2099 C ALA A1063 15864 5491 3865 1072 -1320 -928 C ATOM 2100 O ALA A1063 76.718 23.184 77.159 1.00 64.85 O ANISOU 2100 O ALA A1063 15892 5338 3410 931 -1026 -810 O ATOM 2101 CB ALA A1063 74.002 22.452 78.684 1.00 62.33 C ANISOU 2101 CB ALA A1063 14747 4885 4049 1173 -1400 -769 C ATOM 2102 N GLU A1064 75.872 21.256 76.297 1.00 63.55 N ANISOU 2102 N GLU A1064 15359 5165 3623 1084 -1471 -1140 N ATOM 2103 CA GLU A1064 77.148 20.697 75.858 1.00 62.97 C ANISOU 2103 CA GLU A1064 15375 5199 3351 964 -1279 -1256 C ATOM 2104 C GLU A1064 77.593 21.371 74.557 1.00 69.15 C ANISOU 2104 C GLU A1064 16657 6066 3552 1034 -1272 -1302 C ATOM 2105 O GLU A1064 78.789 21.607 74.389 1.00 68.66 O ANISOU 2105 O GLU A1064 16769 6115 3206 895 -957 -1266 O ATOM 2106 CB GLU A1064 77.064 19.174 75.692 1.00 64.88 C ANISOU 2106 CB GLU A1064 15283 5409 3959 984 -1457 -1494 C ATOM 2107 CG GLU A1064 78.435 18.516 75.627 1.00 74.55 C ANISOU 2107 CG GLU A1064 16481 6734 5112 858 -1205 -1599 C ATOM 2108 CD GLU A1064 78.490 17.001 75.601 1.00 96.04 C ANISOU 2108 CD GLU A1064 18864 9375 8253 874 -1355 -1828 C ATOM 2109 OE1 GLU A1064 77.538 16.349 76.087 1.00 89.38 O ANISOU 2109 OE1 GLU A1064 17689 8371 7902 898 -1582 -1819 O ATOM 2110 OE2 GLU A1064 79.529 16.467 75.149 1.00 92.38 O ANISOU 2110 OE2 GLU A1064 18443 8997 7661 853 -1220 -2004 O ATOM 2111 N LYS A1065 76.637 21.701 73.656 1.00 68.21 N ANISOU 2111 N LYS A1065 16758 5905 3255 1252 -1613 -1362 N ATOM 2112 CA LYS A1065 76.924 22.389 72.392 1.00 71.08 C ANISOU 2112 CA LYS A1065 17641 6355 3011 1354 -1635 -1353 C ATOM 2113 C LYS A1065 77.525 23.771 72.665 1.00 74.99 C ANISOU 2113 C LYS A1065 18458 6822 3211 1223 -1308 -1038 C ATOM 2114 O LYS A1065 78.501 24.137 72.011 1.00 76.13 O ANISOU 2114 O LYS A1065 18924 7079 2923 1134 -1051 -975 O ATOM 2115 CB LYS A1065 75.672 22.515 71.508 1.00 76.70 C ANISOU 2115 CB LYS A1065 18508 7016 3619 1640 -2126 -1453 C ATOM 2116 CG LYS A1065 75.228 21.209 70.855 1.00 92.83 C ANISOU 2116 CG LYS A1065 20348 9094 5830 1776 -2490 -1827 C ATOM 2117 CD LYS A1065 74.200 21.477 69.766 1.00106.46 C ANISOU 2117 CD LYS A1065 22331 10818 7299 2070 -2985 -1941 C ATOM 2118 CE LYS A1065 73.803 20.238 69.004 1.00118.66 C ANISOU 2118 CE LYS A1065 23724 12397 8966 2215 -3391 -2367 C ATOM 2119 NZ LYS A1065 72.955 20.574 67.827 1.00131.58 N ANISOU 2119 NZ LYS A1065 25687 14080 10226 2519 -3888 -2493 N ATOM 2120 N LEU A1066 76.971 24.508 73.661 1.00 70.06 N ANISOU 2120 N LEU A1066 17725 6045 2849 1204 -1299 -853 N ATOM 2121 CA LEU A1066 77.459 25.828 74.084 1.00 69.52 C ANISOU 2121 CA LEU A1066 17921 5883 2610 1076 -1030 -588 C ATOM 2122 C LEU A1066 78.813 25.708 74.767 1.00 71.58 C ANISOU 2122 C LEU A1066 18055 6229 2913 781 -611 -554 C ATOM 2123 O LEU A1066 79.648 26.605 74.633 1.00 71.89 O ANISOU 2123 O LEU A1066 18378 6243 2693 623 -345 -388 O ATOM 2124 CB LEU A1066 76.465 26.532 75.033 1.00 68.49 C ANISOU 2124 CB LEU A1066 17661 5574 2787 1173 -1152 -479 C ATOM 2125 CG LEU A1066 75.117 26.996 74.469 1.00 75.72 C ANISOU 2125 CG LEU A1066 18713 6369 3689 1478 -1558 -466 C ATOM 2126 CD1 LEU A1066 74.206 27.472 75.580 1.00 74.58 C ANISOU 2126 CD1 LEU A1066 18312 6093 3934 1571 -1616 -412 C ATOM 2127 CD2 LEU A1066 75.285 28.106 73.436 1.00 81.51 C ANISOU 2127 CD2 LEU A1066 20028 7013 3927 1560 -1596 -281 C ATOM 2128 N PHE A1067 79.020 24.598 75.505 1.00 66.41 N ANISOU 2128 N PHE A1067 16960 5657 2615 706 -568 -698 N ATOM 2129 CA PHE A1067 80.254 24.300 76.230 1.00 64.65 C ANISOU 2129 CA PHE A1067 16541 5530 2493 462 -236 -694 C ATOM 2130 C PHE A1067 81.411 24.091 75.253 1.00 70.40 C ANISOU 2130 C PHE A1067 17452 6412 2887 364 -19 -764 C ATOM 2131 O PHE A1067 82.468 24.698 75.433 1.00 70.14 O ANISOU 2131 O PHE A1067 17509 6414 2725 152 296 -652 O ATOM 2132 CB PHE A1067 80.073 23.065 77.133 1.00 64.34 C ANISOU 2132 CB PHE A1067 16010 5526 2909 457 -301 -808 C ATOM 2133 CG PHE A1067 81.337 22.620 77.829 1.00 64.52 C ANISOU 2133 CG PHE A1067 15814 5658 3042 250 -21 -817 C ATOM 2134 CD1 PHE A1067 81.786 23.269 78.972 1.00 65.97 C ANISOU 2134 CD1 PHE A1067 15929 5835 3304 99 165 -677 C ATOM 2135 CD2 PHE A1067 82.082 21.555 77.337 1.00 67.52 C ANISOU 2135 CD2 PHE A1067 16054 6149 3454 229 31 -995 C ATOM 2136 CE1 PHE A1067 82.965 22.870 79.601 1.00 65.91 C ANISOU 2136 CE1 PHE A1067 15708 5938 3396 -77 375 -696 C ATOM 2137 CE2 PHE A1067 83.262 21.158 77.966 1.00 69.27 C ANISOU 2137 CE2 PHE A1067 16051 6468 3800 64 265 -1006 C ATOM 2138 CZ PHE A1067 83.691 21.812 79.098 1.00 65.60 C ANISOU 2138 CZ PHE A1067 15511 6005 3411 -91 422 -848 C ATOM 2139 N ASN A1068 81.203 23.245 74.222 1.00 68.91 N ANISOU 2139 N ASN A1068 17300 6316 2566 522 -189 -967 N ATOM 2140 CA ASN A1068 82.187 22.930 73.184 1.00 71.23 C ANISOU 2140 CA ASN A1068 17763 6799 2501 493 12 -1084 C ATOM 2141 C ASN A1068 82.647 24.208 72.467 1.00 77.98 C ANISOU 2141 C ASN A1068 19092 7676 2861 414 238 -846 C ATOM 2142 O ASN A1068 83.831 24.332 72.155 1.00 78.73 O ANISOU 2142 O ASN A1068 19249 7916 2751 244 603 -814 O ATOM 2143 CB ASN A1068 81.606 21.925 72.183 1.00 74.14 C ANISOU 2143 CB ASN A1068 18148 7239 2783 739 -297 -1376 C ATOM 2144 CG ASN A1068 81.235 20.574 72.769 1.00 94.71 C ANISOU 2144 CG ASN A1068 20286 9781 5918 793 -512 -1611 C ATOM 2145 OD1 ASN A1068 81.693 20.168 73.849 1.00 87.96 O ANISOU 2145 OD1 ASN A1068 19080 8892 5450 644 -363 -1569 O ATOM 2146 ND2 ASN A1068 80.394 19.837 72.059 1.00 87.29 N ANISOU 2146 ND2 ASN A1068 19336 8812 5018 1010 -888 -1859 N ATOM 2147 N GLN A1069 81.721 25.169 72.266 1.00 76.06 N ANISOU 2147 N GLN A1069 19156 7271 2474 529 33 -660 N ATOM 2148 CA GLN A1069 81.979 26.477 71.653 1.00 79.03 C ANISOU 2148 CA GLN A1069 20013 7582 2432 467 197 -368 C ATOM 2149 C GLN A1069 82.906 27.324 72.535 1.00 81.81 C ANISOU 2149 C GLN A1069 20312 7831 2942 150 558 -164 C ATOM 2150 O GLN A1069 83.743 28.059 72.008 1.00 83.99 O ANISOU 2150 O GLN A1069 20865 8126 2922 -24 867 34 O ATOM 2151 CB GLN A1069 80.660 27.230 71.406 1.00 81.81 C ANISOU 2151 CB GLN A1069 20641 7733 2709 704 -179 -234 C ATOM 2152 CG GLN A1069 79.796 26.633 70.293 1.00102.90 C ANISOU 2152 CG GLN A1069 23468 10509 5119 1021 -566 -409 C ATOM 2153 CD GLN A1069 78.395 27.208 70.223 1.00124.84 C ANISOU 2153 CD GLN A1069 26385 13092 7958 1281 -1006 -328 C ATOM 2154 OE1 GLN A1069 78.017 28.130 70.960 1.00120.53 O ANISOU 2154 OE1 GLN A1069 25854 12316 7624 1252 -1012 -130 O ATOM 2155 NE2 GLN A1069 77.581 26.655 69.335 1.00117.76 N ANISOU 2155 NE2 GLN A1069 25569 12281 6894 1562 -1410 -515 N ATOM 2156 N ASP A1070 82.752 27.215 73.873 1.00 75.04 N ANISOU 2156 N ASP A1070 19095 6870 2548 73 515 -213 N ATOM 2157 CA ASP A1070 83.564 27.943 74.850 1.00 73.80 C ANISOU 2157 CA ASP A1070 18844 6616 2582 -205 780 -90 C ATOM 2158 C ASP A1070 84.967 27.344 74.968 1.00 77.02 C ANISOU 2158 C ASP A1070 18991 7231 3041 -440 1113 -187 C ATOM 2159 O ASP A1070 85.913 28.080 75.255 1.00 77.40 O ANISOU 2159 O ASP A1070 19067 7236 3107 -708 1392 -62 O ATOM 2160 CB ASP A1070 82.887 27.962 76.230 1.00 72.58 C ANISOU 2160 CB ASP A1070 18406 6334 2836 -160 605 -138 C ATOM 2161 CG ASP A1070 81.706 28.909 76.378 1.00 84.05 C ANISOU 2161 CG ASP A1070 20088 7544 4304 20 363 -18 C ATOM 2162 OD1 ASP A1070 81.198 29.403 75.344 1.00 86.90 O ANISOU 2162 OD1 ASP A1070 20819 7821 4378 167 233 95 O ATOM 2163 OD2 ASP A1070 81.285 29.151 77.528 1.00 89.79 O ANISOU 2163 OD2 ASP A1070 20626 8176 5316 39 299 -42 O ATOM 2164 N VAL A1071 85.102 26.018 74.752 1.00 72.56 N ANISOU 2164 N VAL A1071 18154 6871 2544 -337 1068 -424 N ATOM 2165 CA VAL A1071 86.390 25.317 74.810 1.00 72.33 C ANISOU 2165 CA VAL A1071 17841 7049 2594 -500 1353 -555 C ATOM 2166 C VAL A1071 87.231 25.763 73.599 1.00 80.00 C ANISOU 2166 C VAL A1071 19104 8158 3135 -601 1681 -465 C ATOM 2167 O VAL A1071 88.401 26.101 73.779 1.00 80.76 O ANISOU 2167 O VAL A1071 19086 8324 3274 -863 2025 -400 O ATOM 2168 CB VAL A1071 86.237 23.772 74.896 1.00 74.67 C ANISOU 2168 CB VAL A1071 17781 7470 3118 -328 1186 -839 C ATOM 2169 CG1 VAL A1071 87.596 23.072 74.896 1.00 75.17 C ANISOU 2169 CG1 VAL A1071 17554 7737 3272 -457 1474 -987 C ATOM 2170 CG2 VAL A1071 85.448 23.371 76.137 1.00 70.92 C ANISOU 2170 CG2 VAL A1071 17013 6863 3069 -263 922 -854 C ATOM 2171 N ASP A1072 86.618 25.828 72.392 1.00 78.97 N ANISOU 2171 N ASP A1072 19351 8071 2584 -397 1574 -443 N ATOM 2172 CA ASP A1072 87.270 26.281 71.157 1.00 83.50 C ANISOU 2172 CA ASP A1072 20273 8803 2650 -453 1888 -312 C ATOM 2173 C ASP A1072 87.902 27.661 71.348 1.00 88.88 C ANISOU 2173 C ASP A1072 21148 9327 3294 -764 2193 40 C ATOM 2174 O ASP A1072 89.063 27.853 70.988 1.00 91.18 O ANISOU 2174 O ASP A1072 21407 9770 3468 -991 2621 121 O ATOM 2175 CB ASP A1072 86.267 26.322 69.986 1.00 88.36 C ANISOU 2175 CB ASP A1072 21329 9444 2798 -149 1620 -297 C ATOM 2176 CG ASP A1072 85.782 24.978 69.471 1.00100.52 C ANISOU 2176 CG ASP A1072 22738 11160 4294 148 1345 -678 C ATOM 2177 OD1 ASP A1072 86.002 23.955 70.162 1.00 98.78 O ANISOU 2177 OD1 ASP A1072 22063 10973 4496 142 1294 -942 O ATOM 2178 OD2 ASP A1072 85.174 24.948 68.379 1.00109.98 O ANISOU 2178 OD2 ASP A1072 24297 12446 5045 392 1153 -714 O ATOM 2179 N ALA A1073 87.145 28.598 71.955 1.00 84.11 N ANISOU 2179 N ALA A1073 20708 8407 2842 -776 1975 229 N ATOM 2180 CA ALA A1073 87.569 29.966 72.247 1.00 85.67 C ANISOU 2180 CA ALA A1073 21104 8354 3092 -1053 2175 541 C ATOM 2181 C ALA A1073 88.746 29.987 73.229 1.00 88.08 C ANISOU 2181 C ALA A1073 20995 8678 3795 -1390 2442 474 C ATOM 2182 O ALA A1073 89.684 30.763 73.037 1.00 91.03 O ANISOU 2182 O ALA A1073 21443 9000 4143 -1695 2788 676 O ATOM 2183 CB ALA A1073 86.401 30.756 72.817 1.00 85.00 C ANISOU 2183 CB ALA A1073 21211 7926 3157 -919 1816 649 C ATOM 2184 N ALA A1074 88.700 29.121 74.260 1.00 80.15 N ANISOU 2184 N ALA A1074 19546 7746 3160 -1334 2274 203 N ATOM 2185 CA ALA A1074 89.734 28.999 75.288 1.00 78.45 C ANISOU 2185 CA ALA A1074 18904 7576 3326 -1593 2434 99 C ATOM 2186 C ALA A1074 91.028 28.408 74.718 1.00 84.33 C ANISOU 2186 C ALA A1074 19413 8617 4013 -1745 2811 15 C ATOM 2187 O ALA A1074 92.111 28.857 75.093 1.00 85.35 O ANISOU 2187 O ALA A1074 19340 8747 4341 -2057 3073 63 O ATOM 2188 CB ALA A1074 89.229 28.131 76.431 1.00 74.72 C ANISOU 2188 CB ALA A1074 18072 7131 3188 -1433 2132 -129 C ATOM 2189 N VAL A1075 90.910 27.408 73.814 1.00 81.36 N ANISOU 2189 N VAL A1075 19041 8489 3384 -1515 2828 -137 N ATOM 2190 CA VAL A1075 92.041 26.723 73.180 1.00 83.57 C ANISOU 2190 CA VAL A1075 19093 9085 3575 -1578 3185 -272 C ATOM 2191 C VAL A1075 92.744 27.699 72.221 1.00 92.42 C ANISOU 2191 C VAL A1075 20506 10250 4359 -1811 3624 12 C ATOM 2192 O VAL A1075 93.958 27.874 72.337 1.00 93.94 O ANISOU 2192 O VAL A1075 20422 10553 4718 -2095 3993 37 O ATOM 2193 CB VAL A1075 91.605 25.410 72.464 1.00 87.26 C ANISOU 2193 CB VAL A1075 19530 9770 3855 -1228 3038 -556 C ATOM 2194 CG1 VAL A1075 92.729 24.830 71.608 1.00 90.88 C ANISOU 2194 CG1 VAL A1075 19835 10567 4128 -1248 3448 -703 C ATOM 2195 CG2 VAL A1075 91.118 24.370 73.470 1.00 82.57 C ANISOU 2195 CG2 VAL A1075 18568 9117 3686 -1061 2671 -804 C ATOM 2196 N ARG A1076 91.976 28.354 71.314 1.00 91.62 N ANISOU 2196 N ARG A1076 20948 10053 3812 -1696 3576 249 N ATOM 2197 CA ARG A1076 92.468 29.319 70.317 1.00 97.05 C ANISOU 2197 CA ARG A1076 22008 10756 4109 -1887 3975 602 C ATOM 2198 C ARG A1076 93.228 30.488 70.970 1.00102.43 C ANISOU 2198 C ARG A1076 22607 11180 5134 -2325 4210 865 C ATOM 2199 O ARG A1076 94.194 30.985 70.389 1.00106.79 O ANISOU 2199 O ARG A1076 23181 11825 5570 -2603 4685 1084 O ATOM 2200 CB ARG A1076 91.307 29.867 69.476 1.00 98.91 C ANISOU 2200 CB ARG A1076 22857 10855 3869 -1646 3741 831 C ATOM 2201 N GLY A1077 92.792 30.894 72.163 1.00 95.36 N ANISOU 2201 N GLY A1077 21602 9971 4659 -2383 3884 826 N ATOM 2202 CA GLY A1077 93.417 31.960 72.936 1.00 96.32 C ANISOU 2202 CA GLY A1077 21625 9804 5167 -2771 4000 987 C ATOM 2203 C GLY A1077 94.681 31.521 73.650 1.00100.24 C ANISOU 2203 C GLY A1077 21526 10478 6083 -3031 4209 774 C ATOM 2204 O GLY A1077 95.612 32.318 73.799 1.00103.15 O ANISOU 2204 O GLY A1077 21779 10730 6686 -3422 4491 929 O ATOM 2205 N ILE A1078 94.722 30.246 74.097 1.00 93.56 N ANISOU 2205 N ILE A1078 20285 9894 5368 -2817 4052 423 N ATOM 2206 CA ILE A1078 95.855 29.650 74.815 1.00 93.03 C ANISOU 2206 CA ILE A1078 19621 10021 5705 -2982 4173 187 C ATOM 2207 C ILE A1078 97.064 29.478 73.884 1.00102.07 C ANISOU 2207 C ILE A1078 20577 11465 6740 -3164 4710 229 C ATOM 2208 O ILE A1078 98.186 29.792 74.287 1.00103.69 O ANISOU 2208 O ILE A1078 20405 11697 7296 -3497 4947 224 O ATOM 2209 CB ILE A1078 95.455 28.294 75.442 1.00 91.47 C ANISOU 2209 CB ILE A1078 19116 9989 5648 -2655 3841 -149 C ATOM 2210 N LEU A1079 96.833 29.002 72.640 1.00101.28 N ANISOU 2210 N LEU A1079 20730 11602 6148 -2941 4902 255 N ATOM 2211 CA LEU A1079 97.885 28.780 71.640 1.00106.67 C ANISOU 2211 CA LEU A1079 21274 12628 6626 -3050 5456 283 C ATOM 2212 C LEU A1079 98.400 30.125 71.062 1.00116.92 C ANISOU 2212 C LEU A1079 22831 13789 7803 -3443 5888 727 C ATOM 2213 O LEU A1079 99.408 30.132 70.350 1.00121.69 O ANISOU 2213 O LEU A1079 23266 14664 8307 -3625 6425 812 O ATOM 2214 CB LEU A1079 97.404 27.838 70.508 1.00107.67 C ANISOU 2214 CB LEU A1079 21635 13063 6212 -2645 5488 131 C ATOM 2215 CG LEU A1079 96.117 28.183 69.745 1.00112.42 C ANISOU 2215 CG LEU A1079 22900 13538 6278 -2392 5253 317 C ATOM 2216 CD1 LEU A1079 96.416 28.975 68.477 1.00119.21 C ANISOU 2216 CD1 LEU A1079 24189 14512 6595 -2516 5721 692 C ATOM 2217 CD2 LEU A1079 95.380 26.919 69.349 1.00112.48 C ANISOU 2217 CD2 LEU A1079 22946 13740 6052 -1931 4949 -40 C ATOM 2218 N ARG A1080 97.720 31.246 71.382 1.00113.38 N ANISOU 2218 N ARG A1080 22772 12913 7395 -3572 5666 1011 N ATOM 2219 CA ARG A1080 98.102 32.598 70.965 1.00118.62 C ANISOU 2219 CA ARG A1080 23711 13325 8034 -3959 5999 1465 C ATOM 2220 C ARG A1080 99.022 33.243 72.017 1.00123.26 C ANISOU 2220 C ARG A1080 23856 13681 9295 -4411 6049 1446 C ATOM 2221 O ARG A1080 99.799 34.140 71.682 1.00128.33 O ANISOU 2221 O ARG A1080 24493 14200 10064 -4824 6454 1757 O ATOM 2222 CB ARG A1080 96.856 33.465 70.732 1.00118.51 C ANISOU 2222 CB ARG A1080 24363 12925 7739 -3822 5690 1762 C ATOM 2223 N ASN A1081 98.929 32.776 73.283 1.00114.72 N ANISOU 2223 N ASN A1081 22404 12543 8640 -4331 5628 1086 N ATOM 2224 CA ASN A1081 99.730 33.245 74.417 1.00114.69 C ANISOU 2224 CA ASN A1081 21958 12356 9264 -4689 5554 969 C ATOM 2225 C ASN A1081 101.130 32.620 74.347 1.00121.63 C ANISOU 2225 C ASN A1081 22194 13611 10407 -4882 5936 798 C ATOM 2226 O ASN A1081 101.250 31.399 74.239 1.00119.17 O ANISOU 2226 O ASN A1081 21611 13675 9995 -4588 5929 520 O ATOM 2227 CB ASN A1081 99.023 32.899 75.738 1.00108.72 C ANISOU 2227 CB ASN A1081 21100 11463 8746 -4459 4957 658 C ATOM 2228 CG ASN A1081 99.635 33.504 76.980 1.00129.30 C ANISOU 2228 CG ASN A1081 23367 13841 11920 -4773 4770 519 C ATOM 2229 OD1 ASN A1081 100.759 33.184 77.383 1.00124.60 O ANISOU 2229 OD1 ASN A1081 22217 13438 11689 -4982 4897 340 O ATOM 2230 ND2 ASN A1081 98.863 34.330 77.668 1.00118.87 N ANISOU 2230 ND2 ASN A1081 22357 12120 10688 -4768 4415 551 N ATOM 2231 N ALA A1082 102.180 33.464 74.418 1.00123.36 N ANISOU 2231 N ALA A1082 22152 13707 11012 -5376 6256 956 N ATOM 2232 CA ALA A1082 103.594 33.076 74.331 1.00127.18 C ANISOU 2232 CA ALA A1082 21978 14517 11827 -5628 6664 833 C ATOM 2233 C ALA A1082 104.057 32.197 75.517 1.00127.44 C ANISOU 2233 C ALA A1082 21393 14719 12310 -5513 6302 367 C ATOM 2234 O ALA A1082 105.036 31.462 75.368 1.00129.10 O ANISOU 2234 O ALA A1082 21053 15298 12700 -5528 6567 180 O ATOM 2235 CB ALA A1082 104.465 34.321 74.263 1.00134.31 C ANISOU 2235 CB ALA A1082 22758 15152 13123 -6218 7008 1128 C ATOM 2236 N LYS A1083 103.375 32.279 76.676 1.00119.19 N ANISOU 2236 N LYS A1083 20435 13418 11432 -5384 5713 191 N ATOM 2237 CA LYS A1083 103.726 31.514 77.877 1.00115.87 C ANISOU 2237 CA LYS A1083 19505 13135 11386 -5258 5321 -200 C ATOM 2238 C LYS A1083 102.818 30.276 78.074 1.00113.90 C ANISOU 2238 C LYS A1083 19367 13073 10838 -4715 4983 -406 C ATOM 2239 O LYS A1083 103.120 29.442 78.932 1.00110.96 O ANISOU 2239 O LYS A1083 18577 12864 10718 -4556 4703 -693 O ATOM 2240 CB LYS A1083 103.643 32.416 79.117 1.00117.65 C ANISOU 2240 CB LYS A1083 19728 12984 11989 -5478 4899 -274 C ATOM 2241 N LEU A1084 101.731 30.150 77.280 1.00108.82 N ANISOU 2241 N LEU A1084 19269 12394 9684 -4440 4997 -250 N ATOM 2242 CA LEU A1084 100.780 29.035 77.380 1.00103.61 C ANISOU 2242 CA LEU A1084 18735 11859 8773 -3957 4679 -423 C ATOM 2243 C LEU A1084 100.849 28.078 76.166 1.00108.73 C ANISOU 2243 C LEU A1084 19397 12844 9071 -3705 4990 -473 C ATOM 2244 O LEU A1084 100.535 26.895 76.321 1.00105.35 O ANISOU 2244 O LEU A1084 18828 12581 8618 -3353 4773 -713 O ATOM 2245 CB LEU A1084 99.350 29.573 77.519 1.00100.33 C ANISOU 2245 CB LEU A1084 18906 11130 8086 -3791 4352 -274 C ATOM 2246 N LYS A1085 101.243 28.582 74.975 1.00109.90 N ANISOU 2246 N LYS A1085 19727 13085 8944 -3875 5490 -248 N ATOM 2247 CA LYS A1085 101.346 27.788 73.744 1.00111.90 C ANISOU 2247 CA LYS A1085 20040 13687 8789 -3635 5828 -306 C ATOM 2248 C LYS A1085 102.473 26.720 73.806 1.00117.00 C ANISOU 2248 C LYS A1085 20029 14702 9722 -3565 6026 -633 C ATOM 2249 O LYS A1085 102.193 25.598 73.382 1.00115.32 O ANISOU 2249 O LYS A1085 19803 14705 9309 -3182 5965 -874 O ATOM 2250 CB LYS A1085 101.574 28.682 72.517 1.00120.26 C ANISOU 2250 CB LYS A1085 21455 14781 9458 -3858 6355 58 C ATOM 2251 N PRO A1086 103.721 26.984 74.305 1.00116.34 N ANISOU 2251 N PRO A1086 19382 14691 10129 -3897 6233 -678 N ATOM 2252 CA PRO A1086 104.742 25.915 74.305 1.00117.93 C ANISOU 2252 CA PRO A1086 18952 15253 10604 -3768 6403 -1004 C ATOM 2253 C PRO A1086 104.478 24.820 75.349 1.00116.19 C ANISOU 2253 C PRO A1086 18455 15013 10680 -3440 5852 -1328 C ATOM 2254 O PRO A1086 105.180 23.806 75.362 1.00116.89 O ANISOU 2254 O PRO A1086 18062 15360 10992 -3249 5912 -1614 O ATOM 2255 CB PRO A1086 106.037 26.665 74.630 1.00124.51 C ANISOU 2255 CB PRO A1086 19274 16112 11922 -4245 6710 -928 C ATOM 2256 CG PRO A1086 105.602 27.837 75.420 1.00127.19 C ANISOU 2256 CG PRO A1086 19874 16028 12424 -4551 6409 -706 C ATOM 2257 CD PRO A1086 104.279 28.245 74.844 1.00120.31 C ANISOU 2257 CD PRO A1086 19775 14945 10993 -4393 6311 -461 C ATOM 2258 N VAL A1087 103.459 25.016 76.201 1.00107.28 N ANISOU 2258 N VAL A1087 17633 13580 9549 -3361 5335 -1269 N ATOM 2259 CA VAL A1087 103.077 24.078 77.254 1.00102.37 C ANISOU 2259 CA VAL A1087 16821 12907 9167 -3072 4812 -1489 C ATOM 2260 C VAL A1087 101.939 23.170 76.751 1.00102.78 C ANISOU 2260 C VAL A1087 17235 12952 8864 -2645 4619 -1568 C ATOM 2261 O VAL A1087 102.004 21.957 76.951 1.00101.12 O ANISOU 2261 O VAL A1087 16757 12849 8815 -2343 4441 -1814 O ATOM 2262 CB VAL A1087 102.671 24.819 78.561 1.00103.18 C ANISOU 2262 CB VAL A1087 17005 12716 9483 -3237 4384 -1390 C ATOM 2263 CG1 VAL A1087 102.517 23.840 79.721 1.00 99.39 C ANISOU 2263 CG1 VAL A1087 16248 12245 9272 -2971 3904 -1586 C ATOM 2264 CG2 VAL A1087 103.677 25.912 78.922 1.00106.82 C ANISOU 2264 CG2 VAL A1087 17201 13119 10267 -3701 4559 -1309 C ATOM 2265 N TYR A1088 100.913 23.766 76.100 1.00 98.24 N ANISOU 2265 N TYR A1088 17254 12228 7845 -2623 4632 -1362 N ATOM 2266 CA TYR A1088 99.704 23.108 75.592 1.00 95.33 C ANISOU 2266 CA TYR A1088 17275 11812 7134 -2258 4408 -1417 C ATOM 2267 C TYR A1088 100.018 21.904 74.677 1.00101.93 C ANISOU 2267 C TYR A1088 17958 12927 7846 -1956 4586 -1700 C ATOM 2268 O TYR A1088 99.353 20.876 74.811 1.00 98.92 O ANISOU 2268 O TYR A1088 17583 12495 7505 -1629 4256 -1892 O ATOM 2269 CB TYR A1088 98.827 24.118 74.829 1.00 96.82 C ANISOU 2269 CB TYR A1088 18086 11850 6852 -2327 4487 -1134 C ATOM 2270 CG TYR A1088 97.451 23.594 74.473 1.00 95.33 C ANISOU 2270 CG TYR A1088 18293 11565 6365 -1975 4155 -1181 C ATOM 2271 CD1 TYR A1088 97.196 23.034 73.225 1.00 99.51 C ANISOU 2271 CD1 TYR A1088 19047 12279 6482 -1728 4297 -1295 C ATOM 2272 CD2 TYR A1088 96.400 23.665 75.383 1.00 91.44 C ANISOU 2272 CD2 TYR A1088 17933 10808 6003 -1885 3697 -1128 C ATOM 2273 CE1 TYR A1088 95.934 22.544 72.894 1.00 97.92 C ANISOU 2273 CE1 TYR A1088 19175 11979 6051 -1414 3945 -1371 C ATOM 2274 CE2 TYR A1088 95.133 23.178 75.065 1.00 90.10 C ANISOU 2274 CE2 TYR A1088 18062 10546 5624 -1581 3390 -1174 C ATOM 2275 CZ TYR A1088 94.903 22.622 73.817 1.00 99.85 C ANISOU 2275 CZ TYR A1088 19502 11944 6494 -1355 3493 -1301 C ATOM 2276 OH TYR A1088 93.660 22.131 73.497 1.00 99.10 O ANISOU 2276 OH TYR A1088 19669 11749 6234 -1064 3147 -1379 O ATOM 2277 N ASP A1089 100.998 22.028 73.758 1.00104.10 N ANISOU 2277 N ASP A1089 18093 13480 7981 -2061 5108 -1732 N ATOM 2278 CA ASP A1089 101.359 20.949 72.827 1.00107.09 C ANISOU 2278 CA ASP A1089 18334 14152 8203 -1755 5326 -2042 C ATOM 2279 C ASP A1089 102.123 19.815 73.537 1.00110.78 C ANISOU 2279 C ASP A1089 18177 14705 9208 -1591 5185 -2368 C ATOM 2280 O ASP A1089 102.039 18.666 73.100 1.00111.09 O ANISOU 2280 O ASP A1089 18134 14846 9229 -1233 5118 -2683 O ATOM 2281 CB ASP A1089 102.199 21.484 71.650 1.00115.40 C ANISOU 2281 CB ASP A1089 19419 15516 8913 -1916 5986 -1956 C ATOM 2282 CG ASP A1089 103.543 22.089 72.021 1.00129.47 C ANISOU 2282 CG ASP A1089 20698 17415 11079 -2303 6367 -1858 C ATOM 2283 OD1 ASP A1089 103.580 22.943 72.933 1.00128.13 O ANISOU 2283 OD1 ASP A1089 20476 17000 11208 -2624 6197 -1637 O ATOM 2284 OD2 ASP A1089 104.546 21.756 71.355 1.00140.71 O ANISOU 2284 OD2 ASP A1089 21785 19181 12496 -2288 6848 -2011 O ATOM 2285 N SER A1090 102.860 20.141 74.618 1.00106.78 N ANISOU 2285 N SER A1090 17243 14142 9185 -1838 5109 -2304 N ATOM 2286 CA SER A1090 103.650 19.184 75.400 1.00106.65 C ANISOU 2286 CA SER A1090 16620 14196 9705 -1699 4937 -2562 C ATOM 2287 C SER A1090 102.758 18.262 76.254 1.00105.19 C ANISOU 2287 C SER A1090 16487 13768 9712 -1404 4345 -2645 C ATOM 2288 O SER A1090 103.156 17.132 76.546 1.00105.18 O ANISOU 2288 O SER A1090 16109 13807 10048 -1143 4187 -2894 O ATOM 2289 CB SER A1090 104.633 19.923 76.304 1.00111.51 C ANISOU 2289 CB SER A1090 16809 14822 10739 -2063 4981 -2452 C ATOM 2290 OG SER A1090 105.520 20.737 75.553 1.00125.18 O ANISOU 2290 OG SER A1090 18419 16760 12384 -2372 5551 -2358 O ATOM 2291 N LEU A1091 101.567 18.748 76.653 1.00 97.19 N ANISOU 2291 N LEU A1091 15924 12495 8510 -1443 4033 -2421 N ATOM 2292 CA LEU A1091 100.607 18.013 77.484 1.00 92.35 C ANISOU 2292 CA LEU A1091 15388 11645 8056 -1212 3513 -2425 C ATOM 2293 C LEU A1091 99.872 16.922 76.687 1.00 95.67 C ANISOU 2293 C LEU A1091 15991 12029 8330 -845 3403 -2638 C ATOM 2294 O LEU A1091 99.857 16.955 75.454 1.00 97.74 O ANISOU 2294 O LEU A1091 16468 12438 8229 -772 3695 -2751 O ATOM 2295 CB LEU A1091 99.573 18.984 78.098 1.00 88.62 C ANISOU 2295 CB LEU A1091 15319 10938 7415 -1379 3279 -2128 C ATOM 2296 CG LEU A1091 100.087 20.090 79.032 1.00 93.17 C ANISOU 2296 CG LEU A1091 15781 11474 8147 -1723 3277 -1946 C ATOM 2297 CD1 LEU A1091 99.003 21.104 79.311 1.00 90.56 C ANISOU 2297 CD1 LEU A1091 15926 10915 7567 -1843 3122 -1700 C ATOM 2298 CD2 LEU A1091 100.640 19.528 80.341 1.00 94.81 C ANISOU 2298 CD2 LEU A1091 15537 11686 8799 -1679 2974 -2015 C ATOM 2299 N ASP A1092 99.240 15.969 77.410 1.00 89.28 N ANISOU 2299 N ASP A1092 15107 11014 7801 -618 2970 -2684 N ATOM 2300 CA ASP A1092 98.459 14.856 76.853 1.00 88.66 C ANISOU 2300 CA ASP A1092 15161 10814 7712 -284 2763 -2893 C ATOM 2301 C ASP A1092 97.056 15.344 76.433 1.00 88.87 C ANISOU 2301 C ASP A1092 15721 10687 7360 -283 2615 -2747 C ATOM 2302 O ASP A1092 96.904 16.508 76.074 1.00 88.41 O ANISOU 2302 O ASP A1092 15964 10692 6936 -493 2816 -2558 O ATOM 2303 CB ASP A1092 98.352 13.713 77.890 1.00 89.10 C ANISOU 2303 CB ASP A1092 14906 10666 8283 -92 2359 -2927 C ATOM 2304 CG ASP A1092 99.677 13.166 78.381 1.00103.58 C ANISOU 2304 CG ASP A1092 16202 12624 10530 -44 2420 -3064 C ATOM 2305 OD1 ASP A1092 99.943 11.965 78.153 1.00106.38 O ANISOU 2305 OD1 ASP A1092 16325 12924 11172 245 2325 -3329 O ATOM 2306 OD2 ASP A1092 100.442 13.934 79.007 1.00110.19 O ANISOU 2306 OD2 ASP A1092 16839 13592 11435 -285 2534 -2920 O ATOM 2307 N ALA A1093 96.041 14.461 76.464 1.00 82.91 N ANISOU 2307 N ALA A1093 15064 9711 6726 -50 2258 -2831 N ATOM 2308 CA ALA A1093 94.662 14.816 76.131 1.00 80.25 C ANISOU 2308 CA ALA A1093 15161 9218 6113 -22 2058 -2717 C ATOM 2309 C ALA A1093 93.886 15.191 77.395 1.00 78.94 C ANISOU 2309 C ALA A1093 15012 8844 6135 -140 1778 -2400 C ATOM 2310 O ALA A1093 93.004 16.051 77.338 1.00 76.66 O ANISOU 2310 O ALA A1093 15059 8485 5583 -229 1723 -2209 O ATOM 2311 CB ALA A1093 93.980 13.665 75.409 1.00 82.18 C ANISOU 2311 CB ALA A1093 15470 9338 6416 282 1822 -3016 C ATOM 2312 N VAL A1094 94.230 14.549 78.536 1.00 73.77 N ANISOU 2312 N VAL A1094 14001 8107 5922 -120 1607 -2341 N ATOM 2313 CA VAL A1094 93.608 14.771 79.849 1.00 70.26 C ANISOU 2313 CA VAL A1094 13532 7515 5650 -201 1364 -2047 C ATOM 2314 C VAL A1094 94.290 15.951 80.572 1.00 72.80 C ANISOU 2314 C VAL A1094 13825 7972 5864 -465 1526 -1861 C ATOM 2315 O VAL A1094 93.612 16.681 81.297 1.00 70.02 O ANISOU 2315 O VAL A1094 13640 7542 5421 -568 1417 -1636 O ATOM 2316 CB VAL A1094 93.596 13.505 80.754 1.00 73.90 C ANISOU 2316 CB VAL A1094 13663 7819 6596 -40 1086 -2026 C ATOM 2317 CG1 VAL A1094 92.545 12.501 80.289 1.00 73.79 C ANISOU 2317 CG1 VAL A1094 13723 7566 6749 167 843 -2130 C ATOM 2318 CG2 VAL A1094 94.974 12.852 80.852 1.00 76.29 C ANISOU 2318 CG2 VAL A1094 13578 8239 7171 26 1179 -2201 C ATOM 2319 N ARG A1095 95.614 16.138 80.372 1.00 71.15 N ANISOU 2319 N ARG A1095 13386 7959 5688 -569 1780 -1979 N ATOM 2320 CA ARG A1095 96.373 17.230 80.989 1.00 70.82 C ANISOU 2320 CA ARG A1095 13269 8029 5608 -843 1919 -1852 C ATOM 2321 C ARG A1095 95.967 18.580 80.380 1.00 74.09 C ANISOU 2321 C ARG A1095 14090 8433 5626 -1047 2119 -1728 C ATOM 2322 O ARG A1095 96.040 19.599 81.071 1.00 73.00 O ANISOU 2322 O ARG A1095 14021 8264 5453 -1261 2113 -1571 O ATOM 2323 CB ARG A1095 97.883 17.007 80.861 1.00 73.90 C ANISOU 2323 CB ARG A1095 13248 8628 6204 -902 2138 -2026 C ATOM 2324 CG ARG A1095 98.417 15.968 81.837 1.00 82.12 C ANISOU 2324 CG ARG A1095 13864 9662 7674 -744 1885 -2075 C ATOM 2325 CD ARG A1095 99.930 15.920 81.833 1.00 92.40 C ANISOU 2325 CD ARG A1095 14718 11179 9210 -819 2075 -2238 C ATOM 2326 NE ARG A1095 100.449 15.104 82.931 1.00 97.68 N ANISOU 2326 NE ARG A1095 14999 11837 10279 -677 1775 -2236 N ATOM 2327 CZ ARG A1095 100.728 13.807 82.844 1.00111.32 C ANISOU 2327 CZ ARG A1095 16460 13522 12316 -389 1654 -2389 C ATOM 2328 NH1 ARG A1095 100.526 13.153 81.705 1.00 99.62 N ANISOU 2328 NH1 ARG A1095 15053 12008 10792 -207 1805 -2607 N ATOM 2329 NH2 ARG A1095 101.192 13.149 83.896 1.00 97.34 N ANISOU 2329 NH2 ARG A1095 14365 11726 10894 -263 1359 -2332 N ATOM 2330 N ARG A1096 95.513 18.579 79.105 1.00 71.22 N ANISOU 2330 N ARG A1096 14015 8080 4965 -961 2263 -1803 N ATOM 2331 CA ARG A1096 95.001 19.767 78.418 1.00 71.14 C ANISOU 2331 CA ARG A1096 14444 8032 4555 -1101 2416 -1652 C ATOM 2332 C ARG A1096 93.654 20.163 79.017 1.00 71.59 C ANISOU 2332 C ARG A1096 14775 7868 4557 -1054 2112 -1472 C ATOM 2333 O ARG A1096 93.428 21.346 79.263 1.00 70.61 O ANISOU 2333 O ARG A1096 14882 7659 4288 -1232 2150 -1291 O ATOM 2334 CB ARG A1096 94.872 19.537 76.902 1.00 73.47 C ANISOU 2334 CB ARG A1096 14978 8433 4505 -967 2612 -1787 C ATOM 2335 CG ARG A1096 96.180 19.627 76.139 1.00 85.68 C ANISOU 2335 CG ARG A1096 16355 10236 5964 -1076 3049 -1900 C ATOM 2336 CD ARG A1096 95.958 19.316 74.673 1.00 96.42 C ANISOU 2336 CD ARG A1096 17988 11735 6913 -889 3224 -2051 C ATOM 2337 NE ARG A1096 97.210 19.320 73.914 1.00107.40 N ANISOU 2337 NE ARG A1096 19192 13417 8197 -963 3695 -2171 N ATOM 2338 CZ ARG A1096 97.298 19.070 72.611 1.00122.03 C ANISOU 2338 CZ ARG A1096 21242 15480 9645 -805 3947 -2326 C ATOM 2339 NH1 ARG A1096 96.210 18.791 71.904 1.00107.14 N ANISOU 2339 NH1 ARG A1096 19754 13529 7425 -563 3723 -2402 N ATOM 2340 NH2 ARG A1096 98.478 19.096 72.006 1.00111.82 N ANISOU 2340 NH2 ARG A1096 19734 14482 8272 -880 4425 -2420 N ATOM 2341 N ALA A1097 92.780 19.159 79.285 1.00 66.42 N ANISOU 2341 N ALA A1097 14065 7107 4063 -815 1814 -1526 N ATOM 2342 CA ALA A1097 91.452 19.317 79.891 1.00 63.62 C ANISOU 2342 CA ALA A1097 13882 6567 3723 -736 1532 -1372 C ATOM 2343 C ALA A1097 91.551 19.982 81.272 1.00 67.00 C ANISOU 2343 C ALA A1097 14221 6964 4272 -883 1463 -1197 C ATOM 2344 O ALA A1097 90.705 20.813 81.616 1.00 65.58 O ANISOU 2344 O ALA A1097 14284 6672 3962 -911 1378 -1052 O ATOM 2345 CB ALA A1097 90.769 17.963 80.009 1.00 63.30 C ANISOU 2345 CB ALA A1097 13676 6430 3947 -497 1268 -1464 C ATOM 2346 N ALA A1098 92.607 19.633 82.042 1.00 64.20 N ANISOU 2346 N ALA A1098 13520 6718 4154 -955 1487 -1236 N ATOM 2347 CA ALA A1098 92.895 20.189 83.363 1.00 63.11 C ANISOU 2347 CA ALA A1098 13272 6597 4109 -1079 1400 -1125 C ATOM 2348 C ALA A1098 93.375 21.638 83.249 1.00 68.47 C ANISOU 2348 C ALA A1098 14133 7274 4607 -1344 1584 -1090 C ATOM 2349 O ALA A1098 93.094 22.436 84.143 1.00 67.29 O ANISOU 2349 O ALA A1098 14083 7060 4424 -1425 1480 -1001 O ATOM 2350 CB ALA A1098 93.936 19.340 84.071 1.00 64.72 C ANISOU 2350 CB ALA A1098 13052 6928 4611 -1053 1338 -1197 C ATOM 2351 N LEU A1099 94.075 21.983 82.146 1.00 67.65 N ANISOU 2351 N LEU A1099 14082 7231 4390 -1475 1866 -1157 N ATOM 2352 CA LEU A1099 94.561 23.340 81.889 1.00 69.65 C ANISOU 2352 CA LEU A1099 14511 7441 4512 -1759 2078 -1085 C ATOM 2353 C LEU A1099 93.396 24.240 81.442 1.00 73.64 C ANISOU 2353 C LEU A1099 15500 7747 4734 -1736 2046 -935 C ATOM 2354 O LEU A1099 93.347 25.403 81.843 1.00 73.78 O ANISOU 2354 O LEU A1099 15695 7621 4715 -1911 2047 -841 O ATOM 2355 CB LEU A1099 95.691 23.330 80.839 1.00 73.10 C ANISOU 2355 CB LEU A1099 14818 8032 4923 -1903 2437 -1164 C ATOM 2356 CG LEU A1099 96.475 24.637 80.633 1.00 80.55 C ANISOU 2356 CG LEU A1099 15829 8936 5839 -2259 2704 -1070 C ATOM 2357 CD1 LEU A1099 97.344 24.971 81.846 1.00 81.24 C ANISOU 2357 CD1 LEU A1099 15574 9040 6254 -2460 2595 -1133 C ATOM 2358 CD2 LEU A1099 97.357 24.542 79.410 1.00 86.37 C ANISOU 2358 CD2 LEU A1099 16487 9852 6480 -2359 3116 -1104 C ATOM 2359 N ILE A1100 92.453 23.687 80.636 1.00 69.84 N ANISOU 2359 N ILE A1100 15217 7238 4080 -1505 1981 -934 N ATOM 2360 CA ILE A1100 91.238 24.359 80.142 1.00 69.34 C ANISOU 2360 CA ILE A1100 15583 6999 3763 -1413 1890 -807 C ATOM 2361 C ILE A1100 90.322 24.657 81.351 1.00 71.79 C ANISOU 2361 C ILE A1100 15918 7172 4188 -1335 1623 -738 C ATOM 2362 O ILE A1100 89.694 25.717 81.400 1.00 71.52 O ANISOU 2362 O ILE A1100 16186 6964 4026 -1363 1581 -628 O ATOM 2363 CB ILE A1100 90.536 23.495 79.042 1.00 72.47 C ANISOU 2363 CB ILE A1100 16102 7438 3996 -1162 1827 -886 C ATOM 2364 CG1 ILE A1100 91.414 23.418 77.762 1.00 76.33 C ANISOU 2364 CG1 ILE A1100 16651 8091 4261 -1226 2141 -954 C ATOM 2365 CG2 ILE A1100 89.132 24.026 78.696 1.00 72.17 C ANISOU 2365 CG2 ILE A1100 16440 7222 3759 -1011 1631 -773 C ATOM 2366 CD1 ILE A1100 91.046 22.307 76.731 1.00 84.44 C ANISOU 2366 CD1 ILE A1100 17706 9224 5152 -961 2082 -1142 C ATOM 2367 N ASN A1101 90.294 23.733 82.336 1.00 67.32 N ANISOU 2367 N ASN A1101 15032 6688 3857 -1229 1459 -796 N ATOM 2368 CA ASN A1101 89.540 23.842 83.586 1.00 65.65 C ANISOU 2368 CA ASN A1101 14785 6423 3738 -1139 1251 -730 C ATOM 2369 C ASN A1101 90.016 25.062 84.386 1.00 71.79 C ANISOU 2369 C ASN A1101 15639 7148 4491 -1335 1283 -715 C ATOM 2370 O ASN A1101 89.187 25.790 84.935 1.00 71.33 O ANISOU 2370 O ASN A1101 15773 6969 4360 -1275 1177 -662 O ATOM 2371 CB ASN A1101 89.702 22.555 84.401 1.00 65.66 C ANISOU 2371 CB ASN A1101 14418 6549 3980 -1020 1122 -756 C ATOM 2372 CG ASN A1101 88.819 22.452 85.620 1.00 88.39 C ANISOU 2372 CG ASN A1101 17252 9415 6915 -891 941 -649 C ATOM 2373 OD1 ASN A1101 89.002 23.147 86.628 1.00 83.42 O ANISOU 2373 OD1 ASN A1101 16635 8819 6240 -959 910 -630 O ATOM 2374 ND2 ASN A1101 87.889 21.512 85.582 1.00 79.07 N ANISOU 2374 ND2 ASN A1101 15991 8201 5851 -701 822 -587 N ATOM 2375 N MET A1102 91.350 25.291 84.425 1.00 70.52 N ANISOU 2375 N MET A1102 15310 7068 4415 -1565 1423 -788 N ATOM 2376 CA MET A1102 91.988 26.424 85.108 1.00 71.93 C ANISOU 2376 CA MET A1102 15519 7179 4633 -1795 1438 -821 C ATOM 2377 C MET A1102 91.650 27.748 84.408 1.00 77.10 C ANISOU 2377 C MET A1102 16574 7586 5134 -1925 1548 -734 C ATOM 2378 O MET A1102 91.528 28.772 85.079 1.00 77.77 O ANISOU 2378 O MET A1102 16805 7511 5232 -2013 1466 -753 O ATOM 2379 CB MET A1102 93.515 26.239 85.174 1.00 76.44 C ANISOU 2379 CB MET A1102 15750 7899 5395 -2018 1559 -927 C ATOM 2380 CG MET A1102 93.955 25.070 86.032 1.00 79.34 C ANISOU 2380 CG MET A1102 15723 8481 5942 -1888 1401 -1004 C ATOM 2381 SD MET A1102 95.754 24.895 86.145 1.00 86.63 S ANISOU 2381 SD MET A1102 16193 9584 7137 -2121 1503 -1153 S ATOM 2382 CE MET A1102 96.113 25.998 87.482 1.00 84.62 C ANISOU 2382 CE MET A1102 15933 9278 6940 -2301 1296 -1237 C ATOM 2383 N VAL A1103 91.508 27.721 83.064 1.00 73.96 N ANISOU 2383 N VAL A1103 16368 7150 4581 -1920 1721 -645 N ATOM 2384 CA VAL A1103 91.163 28.875 82.222 1.00 75.47 C ANISOU 2384 CA VAL A1103 16976 7105 4593 -2014 1831 -500 C ATOM 2385 C VAL A1103 89.692 29.260 82.492 1.00 77.32 C ANISOU 2385 C VAL A1103 17495 7160 4723 -1767 1599 -442 C ATOM 2386 O VAL A1103 89.399 30.446 82.622 1.00 78.31 O ANISOU 2386 O VAL A1103 17899 7032 4825 -1837 1569 -378 O ATOM 2387 CB VAL A1103 91.440 28.586 80.718 1.00 81.22 C ANISOU 2387 CB VAL A1103 17826 7916 5119 -2033 2076 -415 C ATOM 2388 CG1 VAL A1103 90.871 29.673 79.809 1.00 83.20 C ANISOU 2388 CG1 VAL A1103 18564 7926 5123 -2058 2145 -208 C ATOM 2389 CG2 VAL A1103 92.934 28.412 80.461 1.00 83.48 C ANISOU 2389 CG2 VAL A1103 17818 8374 5527 -2297 2363 -469 C ATOM 2390 N PHE A1104 88.785 28.268 82.610 1.00 71.24 N ANISOU 2390 N PHE A1104 16628 6502 3939 -1484 1434 -473 N ATOM 2391 CA PHE A1104 87.370 28.505 82.926 1.00 69.72 C ANISOU 2391 CA PHE A1104 16609 6181 3700 -1236 1224 -433 C ATOM 2392 C PHE A1104 87.191 29.069 84.344 1.00 72.58 C ANISOU 2392 C PHE A1104 16913 6494 4172 -1229 1109 -500 C ATOM 2393 O PHE A1104 86.254 29.834 84.591 1.00 72.42 O ANISOU 2393 O PHE A1104 17112 6297 4106 -1094 1001 -477 O ATOM 2394 CB PHE A1104 86.555 27.209 82.794 1.00 69.56 C ANISOU 2394 CB PHE A1104 16409 6301 3719 -980 1089 -457 C ATOM 2395 CG PHE A1104 85.959 26.951 81.433 1.00 72.10 C ANISOU 2395 CG PHE A1104 16934 6586 3873 -847 1063 -415 C ATOM 2396 CD1 PHE A1104 86.610 26.140 80.512 1.00 76.20 C ANISOU 2396 CD1 PHE A1104 17374 7251 4329 -879 1177 -475 C ATOM 2397 CD2 PHE A1104 84.724 27.486 81.085 1.00 74.86 C ANISOU 2397 CD2 PHE A1104 17546 6772 4126 -658 900 -343 C ATOM 2398 CE1 PHE A1104 86.047 25.884 79.258 1.00 78.39 C ANISOU 2398 CE1 PHE A1104 17862 7522 4399 -728 1122 -475 C ATOM 2399 CE2 PHE A1104 84.163 27.235 79.829 1.00 79.03 C ANISOU 2399 CE2 PHE A1104 18268 7285 4474 -512 821 -321 C ATOM 2400 CZ PHE A1104 84.828 26.433 78.925 1.00 77.94 C ANISOU 2400 CZ PHE A1104 18078 7306 4230 -549 927 -393 C ATOM 2401 N GLN A1105 88.096 28.688 85.263 1.00 68.28 N ANISOU 2401 N GLN A1105 16072 6116 3756 -1348 1120 -601 N ATOM 2402 CA GLN A1105 88.081 29.076 86.671 1.00 67.85 C ANISOU 2402 CA GLN A1105 15938 6087 3753 -1329 999 -700 C ATOM 2403 C GLN A1105 88.751 30.447 86.916 1.00 74.36 C ANISOU 2403 C GLN A1105 16938 6705 4610 -1568 1025 -786 C ATOM 2404 O GLN A1105 88.208 31.240 87.685 1.00 74.68 O ANISOU 2404 O GLN A1105 17132 6621 4623 -1482 908 -867 O ATOM 2405 CB GLN A1105 88.801 27.997 87.498 1.00 68.05 C ANISOU 2405 CB GLN A1105 15575 6395 3886 -1335 958 -759 C ATOM 2406 CG GLN A1105 88.619 28.118 89.012 1.00 73.57 C ANISOU 2406 CG GLN A1105 16188 7208 4560 -1234 807 -839 C ATOM 2407 CD GLN A1105 89.505 27.180 89.802 1.00 83.01 C ANISOU 2407 CD GLN A1105 17034 8667 5841 -1257 742 -874 C ATOM 2408 OE1 GLN A1105 90.039 27.550 90.843 1.00 75.63 O ANISOU 2408 OE1 GLN A1105 16032 7822 4880 -1308 633 -994 O ATOM 2409 NE2 GLN A1105 89.719 25.959 89.320 1.00 74.93 N ANISOU 2409 NE2 GLN A1105 15785 7760 4927 -1210 781 -788 N ATOM 2410 N MET A1106 89.926 30.710 86.304 1.00 72.74 N ANISOU 2410 N MET A1106 16688 6461 4489 -1866 1182 -782 N ATOM 2411 CA MET A1106 90.691 31.943 86.531 1.00 75.66 C ANISOU 2411 CA MET A1106 17163 6609 4975 -2152 1208 -860 C ATOM 2412 C MET A1106 90.719 32.885 85.316 1.00 82.36 C ANISOU 2412 C MET A1106 18347 7153 5794 -2324 1383 -688 C ATOM 2413 O MET A1106 90.559 34.095 85.486 1.00 84.17 O ANISOU 2413 O MET A1106 18840 7058 6082 -2416 1329 -700 O ATOM 2414 CB MET A1106 92.140 31.607 86.915 1.00 79.26 C ANISOU 2414 CB MET A1106 17246 7249 5622 -2409 1256 -980 C ATOM 2415 CG MET A1106 92.271 30.896 88.244 1.00 81.58 C ANISOU 2415 CG MET A1106 17247 7809 5940 -2267 1044 -1140 C ATOM 2416 SD MET A1106 93.961 30.356 88.595 1.00 87.58 S ANISOU 2416 SD MET A1106 17523 8808 6944 -2517 1054 -1275 S ATOM 2417 CE MET A1106 94.126 29.065 87.440 1.00 82.57 C ANISOU 2417 CE MET A1106 16705 8364 6303 -2439 1273 -1124 C ATOM 2418 N GLY A1107 90.972 32.339 84.131 1.00 79.30 N ANISOU 2418 N GLY A1107 17952 6867 5312 -2366 1589 -535 N ATOM 2419 CA GLY A1107 91.077 33.115 82.901 1.00 82.08 C ANISOU 2419 CA GLY A1107 18626 6992 5570 -2525 1792 -320 C ATOM 2420 C GLY A1107 92.446 32.993 82.270 1.00 88.85 C ANISOU 2420 C GLY A1107 19278 7967 6516 -2853 2095 -269 C ATOM 2421 O GLY A1107 93.402 32.587 82.938 1.00 88.31 O ANISOU 2421 O GLY A1107 18813 8081 6660 -3003 2105 -436 O ATOM 2422 N GLU A1108 92.547 33.358 80.976 1.00 88.58 N ANISOU 2422 N GLU A1108 19506 7843 6306 -2955 2347 -30 N ATOM 2423 CA GLU A1108 93.779 33.307 80.178 1.00 92.06 C ANISOU 2423 CA GLU A1108 19786 8411 6780 -3261 2719 68 C ATOM 2424 C GLU A1108 94.924 34.081 80.851 1.00 99.08 C ANISOU 2424 C GLU A1108 20436 9157 8053 -3669 2794 -4 C ATOM 2425 O GLU A1108 96.044 33.572 80.908 1.00 99.66 O ANISOU 2425 O GLU A1108 20085 9474 8307 -3859 2968 -106 O ATOM 2426 CB GLU A1108 93.547 33.863 78.758 1.00 96.79 C ANISOU 2426 CB GLU A1108 20820 8881 7077 -3300 2969 393 C ATOM 2427 CG GLU A1108 92.726 32.970 77.833 1.00107.11 C ANISOU 2427 CG GLU A1108 22301 10410 7986 -2941 2947 437 C ATOM 2428 CD GLU A1108 91.228 32.846 78.062 1.00127.46 C ANISOU 2428 CD GLU A1108 25125 12878 10425 -2556 2572 402 C ATOM 2429 OE1 GLU A1108 90.676 33.575 78.920 1.00122.85 O ANISOU 2429 OE1 GLU A1108 24647 12020 10012 -2528 2337 369 O ATOM 2430 OE2 GLU A1108 90.599 32.029 77.352 1.00120.69 O ANISOU 2430 OE2 GLU A1108 24348 12209 9299 -2276 2514 389 O ATOM 2431 N THR A1109 94.629 35.286 81.379 1.00 97.53 N ANISOU 2431 N THR A1109 20488 8557 8010 -3787 2633 17 N ATOM 2432 CA THR A1109 95.594 36.158 82.055 1.00100.99 C ANISOU 2432 CA THR A1109 20743 8777 8852 -4179 2632 -85 C ATOM 2433 C THR A1109 96.033 35.522 83.392 1.00103.32 C ANISOU 2433 C THR A1109 20584 9318 9357 -4129 2370 -449 C ATOM 2434 O THR A1109 97.213 35.596 83.741 1.00105.52 O ANISOU 2434 O THR A1109 20481 9661 9951 -4440 2435 -574 O ATOM 2435 CB THR A1109 94.984 37.560 82.264 1.00111.26 C ANISOU 2435 CB THR A1109 22482 9543 10249 -4242 2471 -4 C ATOM 2436 OG1 THR A1109 94.318 37.981 81.071 1.00112.32 O ANISOU 2436 OG1 THR A1109 23084 9483 10107 -4162 2634 353 O ATOM 2437 CG2 THR A1109 96.023 38.604 82.673 1.00114.78 C ANISOU 2437 CG2 THR A1109 22795 9670 11147 -4714 2511 -62 C ATOM 2438 N GLY A1110 95.085 34.899 84.097 1.00 96.07 N ANISOU 2438 N GLY A1110 19701 8541 8262 -3740 2083 -593 N ATOM 2439 CA GLY A1110 95.307 34.246 85.385 1.00 94.02 C ANISOU 2439 CA GLY A1110 19088 8531 8105 -3619 1815 -884 C ATOM 2440 C GLY A1110 96.225 33.041 85.335 1.00 97.79 C ANISOU 2440 C GLY A1110 19082 9413 8659 -3640 1921 -954 C ATOM 2441 O GLY A1110 97.139 32.928 86.157 1.00 98.58 O ANISOU 2441 O GLY A1110 18811 9638 9006 -3786 1800 -1158 O ATOM 2442 N VAL A1111 95.987 32.134 84.363 1.00 93.24 N ANISOU 2442 N VAL A1111 18508 9039 7881 -3475 2121 -808 N ATOM 2443 CA VAL A1111 96.760 30.900 84.147 1.00 92.73 C ANISOU 2443 CA VAL A1111 18015 9340 7880 -3433 2241 -877 C ATOM 2444 C VAL A1111 98.184 31.271 83.663 1.00101.62 C ANISOU 2444 C VAL A1111 18846 10497 9268 -3833 2542 -872 C ATOM 2445 O VAL A1111 99.146 30.598 84.044 1.00102.03 O ANISOU 2445 O VAL A1111 18419 10800 9547 -3886 2536 -1033 O ATOM 2446 CB VAL A1111 96.036 29.938 83.158 1.00 94.26 C ANISOU 2446 CB VAL A1111 18347 9684 7785 -3140 2359 -760 C ATOM 2447 CG1 VAL A1111 96.839 28.661 82.910 1.00 94.00 C ANISOU 2447 CG1 VAL A1111 17879 9990 7847 -3071 2477 -868 C ATOM 2448 CG2 VAL A1111 94.642 29.585 83.664 1.00 90.16 C ANISOU 2448 CG2 VAL A1111 18050 9122 7084 -2782 2067 -761 C ATOM 2449 N ALA A1112 98.314 32.368 82.879 1.00101.86 N ANISOU 2449 N ALA A1112 19146 10257 9297 -4115 2794 -675 N ATOM 2450 CA ALA A1112 99.587 32.880 82.354 1.00106.95 C ANISOU 2450 CA ALA A1112 19539 10887 10210 -4542 3136 -609 C ATOM 2451 C ALA A1112 100.546 33.329 83.481 1.00113.72 C ANISOU 2451 C ALA A1112 19996 11686 11526 -4826 2932 -848 C ATOM 2452 O ALA A1112 101.756 33.401 83.255 1.00117.31 O ANISOU 2452 O ALA A1112 20041 12238 12293 -5148 3167 -874 O ATOM 2453 CB ALA A1112 99.329 34.044 81.411 1.00110.98 C ANISOU 2453 CB ALA A1112 20503 11053 10613 -4767 3398 -294 C ATOM 2454 N GLY A1113 99.997 33.601 84.668 1.00108.55 N ANISOU 2454 N GLY A1113 19446 10900 10897 -4691 2500 -1036 N ATOM 2455 CA GLY A1113 100.752 34.015 85.847 1.00110.82 C ANISOU 2455 CA GLY A1113 19415 11142 11550 -4891 2208 -1317 C ATOM 2456 C GLY A1113 101.461 32.892 86.584 1.00114.26 C ANISOU 2456 C GLY A1113 19316 11986 12112 -4755 2024 -1550 C ATOM 2457 O GLY A1113 102.127 33.142 87.593 1.00116.00 O ANISOU 2457 O GLY A1113 19245 12220 12609 -4888 1733 -1804 O ATOM 2458 N PHE A1114 101.327 31.646 86.089 1.00108.40 N ANISOU 2458 N PHE A1114 18446 11562 11177 -4476 2161 -1477 N ATOM 2459 CA PHE A1114 101.954 30.451 86.658 1.00107.60 C ANISOU 2459 CA PHE A1114 17856 11829 11198 -4296 2003 -1653 C ATOM 2460 C PHE A1114 103.257 30.107 85.907 1.00115.97 C ANISOU 2460 C PHE A1114 18420 13087 12557 -4528 2349 -1665 C ATOM 2461 O PHE A1114 103.602 28.928 85.785 1.00114.59 O ANISOU 2461 O PHE A1114 17920 13215 12403 -4308 2381 -1725 O ATOM 2462 CB PHE A1114 100.972 29.263 86.614 1.00104.45 C ANISOU 2462 CB PHE A1114 17613 11609 10465 -3833 1918 -1581 C ATOM 2463 CG PHE A1114 99.832 29.327 87.604 1.00102.68 C ANISOU 2463 CG PHE A1114 17710 11302 10003 -3562 1555 -1604 C ATOM 2464 CD1 PHE A1114 99.924 28.692 88.836 1.00104.67 C ANISOU 2464 CD1 PHE A1114 17740 11751 10278 -3359 1194 -1751 C ATOM 2465 CD2 PHE A1114 98.656 29.999 87.293 1.00103.10 C ANISOU 2465 CD2 PHE A1114 18280 11099 9793 -3488 1586 -1464 C ATOM 2466 CE1 PHE A1114 98.864 28.739 89.747 1.00102.96 C ANISOU 2466 CE1 PHE A1114 17814 11501 9805 -3102 916 -1752 C ATOM 2467 CE2 PHE A1114 97.599 30.051 88.207 1.00103.21 C ANISOU 2467 CE2 PHE A1114 18549 11067 9600 -3224 1293 -1497 C ATOM 2468 CZ PHE A1114 97.708 29.416 89.426 1.00100.35 C ANISOU 2468 CZ PHE A1114 17961 10928 9241 -3038 983 -1637 C ATOM 2469 N THR A1115 104.000 31.148 85.449 1.00117.88 N ANISOU 2469 N THR A1115 18577 13144 13069 -4977 2606 -1612 N ATOM 2470 CA THR A1115 105.261 31.068 84.692 1.00122.66 C ANISOU 2470 CA THR A1115 18701 13910 13992 -5274 3013 -1595 C ATOM 2471 C THR A1115 106.302 30.146 85.357 1.00128.31 C ANISOU 2471 C THR A1115 18739 14967 15045 -5194 2825 -1865 C ATOM 2472 O THR A1115 107.074 29.494 84.651 1.00129.99 O ANISOU 2472 O THR A1115 18553 15442 15394 -5204 3160 -1869 O ATOM 2473 CB THR A1115 105.861 32.465 84.531 1.00135.95 C ANISOU 2473 CB THR A1115 20369 15275 16012 -5806 3180 -1523 C ATOM 2474 N ASN A1116 106.309 30.092 86.703 1.00124.33 N ANISOU 2474 N ASN A1116 18115 14471 14652 -5088 2288 -2092 N ATOM 2475 CA ASN A1116 107.210 29.256 87.497 1.00125.63 C ANISOU 2475 CA ASN A1116 17685 14939 15110 -4966 1997 -2340 C ATOM 2476 C ASN A1116 106.806 27.778 87.407 1.00125.82 C ANISOU 2476 C ASN A1116 17677 15236 14893 -4478 1954 -2312 C ATOM 2477 O ASN A1116 107.673 26.915 87.265 1.00127.21 O ANISOU 2477 O ASN A1116 17334 15679 15319 -4388 2020 -2418 O ATOM 2478 CB ASN A1116 107.208 29.714 88.965 1.00127.21 C ANISOU 2478 CB ASN A1116 17876 15061 15398 -4969 1407 -2570 C ATOM 2479 CG ASN A1116 107.509 31.182 89.180 1.00156.28 C ANISOU 2479 CG ASN A1116 21628 18409 19342 -5426 1357 -2654 C ATOM 2480 OD1 ASN A1116 108.423 31.762 88.581 1.00155.80 O ANISOU 2480 OD1 ASN A1116 21245 18265 19687 -5849 1658 -2642 O ATOM 2481 ND2 ASN A1116 106.768 31.805 90.086 1.00147.31 N ANISOU 2481 ND2 ASN A1116 20893 17070 18009 -5349 968 -2756 N ATOM 2482 N SER A1117 105.487 27.501 87.482 1.00117.66 N ANISOU 2482 N SER A1117 17178 14111 13415 -4167 1842 -2174 N ATOM 2483 CA SER A1117 104.896 26.161 87.454 1.00113.79 C ANISOU 2483 CA SER A1117 16735 13795 12704 -3715 1761 -2124 C ATOM 2484 C SER A1117 104.791 25.586 86.031 1.00117.50 C ANISOU 2484 C SER A1117 17254 14336 13053 -3632 2230 -2008 C ATOM 2485 O SER A1117 104.946 24.374 85.864 1.00116.26 O ANISOU 2485 O SER A1117 16863 14373 12939 -3340 2225 -2064 O ATOM 2486 CB SER A1117 103.508 26.189 88.084 1.00112.87 C ANISOU 2486 CB SER A1117 17143 13540 12205 -3461 1479 -2019 C ATOM 2487 OG SER A1117 103.563 26.627 89.431 1.00122.35 O ANISOU 2487 OG SER A1117 18322 14724 13440 -3475 1045 -2150 O ATOM 2488 N LEU A1118 104.516 26.440 85.020 1.00115.16 N ANISOU 2488 N LEU A1118 17285 13877 12594 -3865 2614 -1851 N ATOM 2489 CA LEU A1118 104.383 26.041 83.610 1.00115.34 C ANISOU 2489 CA LEU A1118 17429 13983 12410 -3793 3070 -1740 C ATOM 2490 C LEU A1118 105.726 25.566 83.022 1.00123.65 C ANISOU 2490 C LEU A1118 17897 15310 13775 -3895 3411 -1868 C ATOM 2491 O LEU A1118 105.723 24.765 82.086 1.00123.28 O ANISOU 2491 O LEU A1118 17824 15434 13582 -3688 3693 -1882 O ATOM 2492 CB LEU A1118 103.824 27.199 82.755 1.00116.15 C ANISOU 2492 CB LEU A1118 18040 13843 12247 -4033 3370 -1504 C ATOM 2493 CG LEU A1118 102.357 27.604 82.981 1.00116.54 C ANISOU 2493 CG LEU A1118 18709 13632 11937 -3868 3127 -1364 C ATOM 2494 CD1 LEU A1118 102.082 28.985 82.427 1.00118.66 C ANISOU 2494 CD1 LEU A1118 19389 13607 12090 -4174 3339 -1150 C ATOM 2495 CD2 LEU A1118 101.388 26.584 82.392 1.00115.32 C ANISOU 2495 CD2 LEU A1118 18807 13567 11443 -3463 3122 -1321 C ATOM 2496 N ARG A1119 106.861 26.057 83.574 1.00124.36 N ANISOU 2496 N ARG A1119 17501 15444 14305 -4202 3372 -1988 N ATOM 2497 CA ARG A1119 108.221 25.696 83.156 1.00129.19 C ANISOU 2497 CA ARG A1119 17460 16325 15303 -4327 3677 -2130 C ATOM 2498 C ARG A1119 108.532 24.239 83.521 1.00131.91 C ANISOU 2498 C ARG A1119 17405 16921 15793 -3907 3448 -2340 C ATOM 2499 O ARG A1119 109.111 23.517 82.707 1.00133.87 O ANISOU 2499 O ARG A1119 17341 17401 16123 -3783 3792 -2431 O ATOM 2500 CB ARG A1119 109.252 26.639 83.795 1.00134.14 C ANISOU 2500 CB ARG A1119 17661 16893 16414 -4769 3596 -2220 C ATOM 2501 N MET A1120 108.135 23.811 84.738 1.00125.16 N ANISOU 2501 N MET A1120 16578 16014 14961 -3672 2877 -2408 N ATOM 2502 CA MET A1120 108.317 22.444 85.236 1.00123.87 C ANISOU 2502 CA MET A1120 16104 16022 14940 -3257 2579 -2549 C ATOM 2503 C MET A1120 107.317 21.489 84.582 1.00123.55 C ANISOU 2503 C MET A1120 16438 15952 14555 -2877 2661 -2471 C ATOM 2504 O MET A1120 107.583 20.288 84.494 1.00123.35 O ANISOU 2504 O MET A1120 16134 16057 14678 -2549 2602 -2594 O ATOM 2505 CB MET A1120 108.163 22.392 86.766 1.00124.63 C ANISOU 2505 CB MET A1120 16174 16070 15110 -3149 1954 -2585 C ATOM 2506 CG MET A1120 109.266 23.107 87.524 1.00132.72 C ANISOU 2506 CG MET A1120 16733 17158 16535 -3455 1757 -2747 C ATOM 2507 SD MET A1120 109.005 23.124 89.319 1.00135.51 S ANISOU 2507 SD MET A1120 17154 17489 16845 -3299 1002 -2803 S ATOM 2508 CE MET A1120 107.652 24.285 89.447 1.00128.33 C ANISOU 2508 CE MET A1120 17024 16274 15462 -3456 1001 -2630 C ATOM 2509 N LEU A1121 106.167 22.032 84.129 1.00116.72 N ANISOU 2509 N LEU A1121 16192 14892 13263 -2916 2768 -2282 N ATOM 2510 CA LEU A1121 105.077 21.300 83.481 1.00112.96 C ANISOU 2510 CA LEU A1121 16125 14351 12445 -2600 2813 -2208 C ATOM 2511 C LEU A1121 105.502 20.797 82.087 1.00119.51 C ANISOU 2511 C LEU A1121 16836 15351 13221 -2524 3293 -2309 C ATOM 2512 O LEU A1121 104.981 19.781 81.624 1.00117.54 O ANISOU 2512 O LEU A1121 16700 15113 12848 -2183 3270 -2376 O ATOM 2513 CB LEU A1121 103.836 22.207 83.378 1.00109.73 C ANISOU 2513 CB LEU A1121 16360 13699 11634 -2702 2792 -1993 C ATOM 2514 CG LEU A1121 102.464 21.525 83.365 1.00109.79 C ANISOU 2514 CG LEU A1121 16782 13580 11355 -2366 2581 -1904 C ATOM 2515 CD1 LEU A1121 102.149 20.878 84.713 1.00107.46 C ANISOU 2515 CD1 LEU A1121 16381 13254 11195 -2148 2095 -1899 C ATOM 2516 CD2 LEU A1121 101.373 22.526 83.059 1.00110.00 C ANISOU 2516 CD2 LEU A1121 17386 13393 11016 -2482 2630 -1712 C ATOM 2517 N GLN A1122 106.460 21.499 81.437 1.00120.53 N ANISOU 2517 N GLN A1122 16724 15615 13456 -2840 3731 -2328 N ATOM 2518 CA GLN A1122 107.027 21.140 80.127 1.00124.06 C ANISOU 2518 CA GLN A1122 17012 16291 13833 -2796 4263 -2427 C ATOM 2519 C GLN A1122 108.189 20.165 80.287 1.00131.20 C ANISOU 2519 C GLN A1122 17218 17443 15189 -2619 4279 -2706 C ATOM 2520 O GLN A1122 108.384 19.295 79.440 1.00132.40 O ANISOU 2520 O GLN A1122 17252 17767 15287 -2350 4531 -2880 O ATOM 2521 CB GLN A1122 107.508 22.388 79.365 1.00129.41 C ANISOU 2521 CB GLN A1122 17751 17003 14416 -3238 4775 -2262 C ATOM 2522 CG GLN A1122 106.396 23.311 78.905 1.00142.62 C ANISOU 2522 CG GLN A1122 20140 18439 15611 -3369 4842 -1979 C ATOM 2523 N GLN A1123 108.959 20.318 81.381 1.00129.12 N ANISOU 2523 N GLN A1123 16491 17197 15372 -2750 3982 -2772 N ATOM 2524 CA GLN A1123 110.119 19.490 81.704 1.00132.55 C ANISOU 2524 CA GLN A1123 16209 17850 16304 -2590 3914 -3027 C ATOM 2525 C GLN A1123 109.715 18.066 82.137 1.00133.44 C ANISOU 2525 C GLN A1123 16296 17918 16487 -2077 3504 -3149 C ATOM 2526 O GLN A1123 110.600 17.245 82.400 1.00136.02 O ANISOU 2526 O GLN A1123 16057 18394 17232 -1866 3399 -3360 O ATOM 2527 CB GLN A1123 110.937 20.158 82.814 1.00136.08 C ANISOU 2527 CB GLN A1123 16229 18301 17173 -2881 3625 -3049 C ATOM 2528 N LYS A1124 108.391 17.795 82.238 1.00124.62 N ANISOU 2528 N LYS A1124 15768 16576 15007 -1887 3262 -3003 N ATOM 2529 CA LYS A1124 107.747 16.520 82.603 1.00121.51 C ANISOU 2529 CA LYS A1124 15469 16055 14643 -1444 2883 -3042 C ATOM 2530 C LYS A1124 108.078 16.071 84.055 1.00124.62 C ANISOU 2530 C LYS A1124 15550 16410 15391 -1315 2324 -3020 C ATOM 2531 O LYS A1124 108.009 14.870 84.350 1.00124.22 O ANISOU 2531 O LYS A1124 15363 16298 15537 -940 2051 -3083 O ATOM 2532 CB LYS A1124 108.134 15.402 81.616 1.00126.88 C ANISOU 2532 CB LYS A1124 15915 16858 15437 -1114 3138 -3309 C ATOM 2533 N ARG A1125 108.370 17.028 84.962 1.00120.64 N ANISOU 2533 N ARG A1125 14977 15918 14943 -1609 2130 -2924 N ATOM 2534 CA ARG A1125 108.620 16.736 86.381 1.00120.25 C ANISOU 2534 CA ARG A1125 14706 15861 15123 -1493 1572 -2888 C ATOM 2535 C ARG A1125 107.290 16.923 87.120 1.00119.45 C ANISOU 2535 C ARG A1125 15191 15549 14646 -1445 1256 -2631 C ATOM 2536 O ARG A1125 107.139 17.843 87.926 1.00118.65 O ANISOU 2536 O ARG A1125 15240 15422 14419 -1664 1057 -2542 O ATOM 2537 CB ARG A1125 109.758 17.617 86.966 1.00124.02 C ANISOU 2537 CB ARG A1125 14732 16496 15895 -1814 1500 -2994 C ATOM 2538 CG ARG A1125 110.870 18.009 85.985 1.00136.62 C ANISOU 2538 CG ARG A1125 15866 18285 17759 -2059 2011 -3185 C ATOM 2539 CD ARG A1125 111.843 18.922 86.680 1.00147.90 C ANISOU 2539 CD ARG A1125 16874 19811 19511 -2409 1866 -3270 C ATOM 2540 NE ARG A1125 112.521 19.841 85.768 1.00158.44 N ANISOU 2540 NE ARG A1125 17994 21236 20969 -2828 2418 -3324 N ATOM 2541 CZ ARG A1125 113.745 20.312 85.975 1.00176.30 C ANISOU 2541 CZ ARG A1125 19627 23653 23707 -3101 2454 -3484 C ATOM 2542 NH1 ARG A1125 114.455 19.901 87.019 1.00165.27 N ANISOU 2542 NH1 ARG A1125 17741 22358 22695 -2960 1943 -3641 N ATOM 2543 NH2 ARG A1125 114.290 21.160 85.114 1.00166.04 N ANISOU 2543 NH2 ARG A1125 18157 22413 22517 -3510 3004 -3478 N ATOM 2544 N TRP A1126 106.302 16.051 86.795 1.00112.96 N ANISOU 2544 N TRP A1126 14691 14572 13655 -1155 1228 -2534 N ATOM 2545 CA TRP A1126 104.919 16.079 87.288 1.00108.24 C ANISOU 2545 CA TRP A1126 14630 13776 12720 -1079 1011 -2286 C ATOM 2546 C TRP A1126 104.817 15.927 88.812 1.00111.41 C ANISOU 2546 C TRP A1126 15004 14176 13149 -973 512 -2128 C ATOM 2547 O TRP A1126 103.868 16.473 89.393 1.00108.12 O ANISOU 2547 O TRP A1126 14997 13669 12413 -1037 381 -1940 O ATOM 2548 CB TRP A1126 104.072 14.978 86.614 1.00105.08 C ANISOU 2548 CB TRP A1126 14437 13211 12275 -776 1056 -2259 C ATOM 2549 CG TRP A1126 103.999 15.081 85.111 1.00106.56 C ANISOU 2549 CG TRP A1126 14746 13415 12328 -826 1511 -2418 C ATOM 2550 CD1 TRP A1126 103.343 16.028 84.383 1.00107.81 C ANISOU 2550 CD1 TRP A1126 15321 13534 12109 -1046 1789 -2354 C ATOM 2551 CD2 TRP A1126 104.573 14.174 84.161 1.00109.23 C ANISOU 2551 CD2 TRP A1126 14809 13819 12873 -615 1724 -2670 C ATOM 2552 NE1 TRP A1126 103.524 15.803 83.038 1.00109.01 N ANISOU 2552 NE1 TRP A1126 15480 13757 12181 -1000 2170 -2531 N ATOM 2553 CE2 TRP A1126 104.262 14.661 82.872 1.00113.18 C ANISOU 2553 CE2 TRP A1126 15589 14359 13055 -731 2148 -2749 C ATOM 2554 CE3 TRP A1126 105.330 12.994 84.273 1.00113.44 C ANISOU 2554 CE3 TRP A1126 14893 14381 13829 -313 1591 -2847 C ATOM 2555 CZ2 TRP A1126 104.683 14.012 81.702 1.00115.47 C ANISOU 2555 CZ2 TRP A1126 15733 14753 13388 -554 2460 -3019 C ATOM 2556 CZ3 TRP A1126 105.749 12.353 83.113 1.00117.80 C ANISOU 2556 CZ3 TRP A1126 15277 15004 14478 -135 1898 -3136 C ATOM 2557 CH2 TRP A1126 105.425 12.861 81.847 1.00118.49 C ANISOU 2557 CH2 TRP A1126 15659 15166 14197 -255 2336 -3231 C ATOM 2558 N ASP A1127 105.741 15.191 89.465 1.00110.85 N ANISOU 2558 N ASP A1127 14475 14216 13426 -785 229 -2195 N ATOM 2559 CA ASP A1127 105.716 15.026 90.927 1.00110.91 C ANISOU 2559 CA ASP A1127 14466 14264 13411 -658 -265 -2029 C ATOM 2560 C ASP A1127 106.327 16.231 91.625 1.00116.32 C ANISOU 2560 C ASP A1127 15049 15108 14037 -950 -397 -2126 C ATOM 2561 O ASP A1127 105.934 16.542 92.749 1.00115.24 O ANISOU 2561 O ASP A1127 15120 14999 13665 -926 -732 -1988 O ATOM 2562 CB ASP A1127 106.447 13.748 91.383 1.00115.88 C ANISOU 2562 CB ASP A1127 14668 14930 14432 -309 -574 -2037 C ATOM 2563 CG ASP A1127 105.664 12.459 91.224 1.00123.95 C ANISOU 2563 CG ASP A1127 15856 15726 15515 28 -643 -1856 C ATOM 2564 OD1 ASP A1127 104.490 12.522 90.806 1.00120.67 O ANISOU 2564 OD1 ASP A1127 15880 15139 14830 -7 -472 -1723 O ATOM 2565 OD2 ASP A1127 106.218 11.385 91.545 1.00132.71 O ANISOU 2565 OD2 ASP A1127 16643 16807 16974 329 -895 -1845 O ATOM 2566 N GLU A1128 107.287 16.907 90.955 1.00115.40 N ANISOU 2566 N GLU A1128 14609 15097 14141 -1227 -126 -2370 N ATOM 2567 CA GLU A1128 107.999 18.083 91.455 1.00117.70 C ANISOU 2567 CA GLU A1128 14729 15500 14493 -1561 -221 -2514 C ATOM 2568 C GLU A1128 107.190 19.365 91.241 1.00118.67 C ANISOU 2568 C GLU A1128 15353 15481 14257 -1879 -15 -2450 C ATOM 2569 O GLU A1128 107.323 20.312 92.017 1.00119.43 O ANISOU 2569 O GLU A1128 15507 15591 14280 -2084 -237 -2511 O ATOM 2570 CB GLU A1128 109.359 18.213 90.752 1.00123.72 C ANISOU 2570 CB GLU A1128 14886 16411 15711 -1742 32 -2774 C ATOM 2571 N ALA A1129 106.364 19.402 90.178 1.00111.86 N ANISOU 2571 N ALA A1129 14851 14470 13180 -1905 384 -2350 N ATOM 2572 CA ALA A1129 105.531 20.555 89.852 1.00109.14 C ANISOU 2572 CA ALA A1129 15002 13961 12507 -2162 589 -2266 C ATOM 2573 C ALA A1129 104.295 20.623 90.762 1.00109.00 C ANISOU 2573 C ALA A1129 15462 13839 12114 -1998 295 -2080 C ATOM 2574 O ALA A1129 103.986 21.705 91.260 1.00108.53 O ANISOU 2574 O ALA A1129 15657 13708 11871 -2192 207 -2090 O ATOM 2575 CB ALA A1129 105.110 20.505 88.393 1.00108.50 C ANISOU 2575 CB ALA A1129 15125 13788 12310 -2203 1078 -2222 C ATOM 2576 N ALA A1130 103.612 19.478 90.984 1.00102.68 N ANISOU 2576 N ALA A1130 14763 13021 11229 -1646 155 -1917 N ATOM 2577 CA ALA A1130 102.403 19.353 91.805 1.00 99.18 C ANISOU 2577 CA ALA A1130 14723 12506 10455 -1461 -68 -1700 C ATOM 2578 C ALA A1130 102.629 19.798 93.260 1.00104.00 C ANISOU 2578 C ALA A1130 15318 13249 10948 -1454 -473 -1713 C ATOM 2579 O ALA A1130 101.756 20.462 93.820 1.00101.91 O ANISOU 2579 O ALA A1130 15439 12935 10348 -1472 -544 -1634 O ATOM 2580 CB ALA A1130 101.905 17.917 91.788 1.00 98.50 C ANISOU 2580 CB ALA A1130 14615 12377 10433 -1113 -150 -1524 C ATOM 2581 N VAL A1131 103.794 19.453 93.857 1.00103.55 N ANISOU 2581 N VAL A1131 14816 13373 11156 -1409 -746 -1838 N ATOM 2582 CA VAL A1131 104.150 19.829 95.234 1.00105.52 C ANISOU 2582 CA VAL A1131 15017 13788 11286 -1380 -1187 -1894 C ATOM 2583 C VAL A1131 104.490 21.350 95.257 1.00109.97 C ANISOU 2583 C VAL A1131 15641 14314 11828 -1759 -1149 -2144 C ATOM 2584 O VAL A1131 104.226 22.018 96.260 1.00110.28 O ANISOU 2584 O VAL A1131 15898 14406 11599 -1767 -1428 -2199 O ATOM 2585 CB VAL A1131 105.295 18.936 95.819 1.00113.36 C ANISOU 2585 CB VAL A1131 15498 14980 12593 -1185 -1537 -1950 C ATOM 2586 CG1 VAL A1131 106.599 19.050 95.027 1.00116.33 C ANISOU 2586 CG1 VAL A1131 15338 15403 13460 -1390 -1378 -2219 C ATOM 2587 CG2 VAL A1131 105.527 19.198 97.307 1.00115.99 C ANISOU 2587 CG2 VAL A1131 15848 15513 12710 -1082 -2051 -1975 C ATOM 2588 N ASN A1132 105.014 21.887 94.134 1.00106.50 N ANISOU 2588 N ASN A1132 15040 13770 11656 -2065 -786 -2283 N ATOM 2589 CA ASN A1132 105.369 23.298 93.981 1.00107.95 C ANISOU 2589 CA ASN A1132 15259 13846 11910 -2466 -694 -2481 C ATOM 2590 C ASN A1132 104.143 24.153 93.612 1.00107.58 C ANISOU 2590 C ASN A1132 15801 13558 11517 -2566 -463 -2368 C ATOM 2591 O ASN A1132 104.193 25.377 93.753 1.00108.68 O ANISOU 2591 O ASN A1132 16088 13557 11647 -2844 -476 -2507 O ATOM 2592 CB ASN A1132 106.456 23.459 92.922 1.00111.56 C ANISOU 2592 CB ASN A1132 15277 14302 12808 -2751 -360 -2615 C ATOM 2593 N LEU A1133 103.052 23.510 93.146 1.00 99.25 N ANISOU 2593 N LEU A1133 15061 12432 10217 -2333 -278 -2131 N ATOM 2594 CA LEU A1133 101.803 24.171 92.755 1.00 95.52 C ANISOU 2594 CA LEU A1133 15121 11745 9429 -2363 -78 -2006 C ATOM 2595 C LEU A1133 100.763 24.065 93.883 1.00 96.53 C ANISOU 2595 C LEU A1133 15574 11916 9187 -2094 -356 -1898 C ATOM 2596 O LEU A1133 99.808 24.842 93.903 1.00 94.44 O ANISOU 2596 O LEU A1133 15720 11496 8668 -2119 -285 -1863 O ATOM 2597 CB LEU A1133 101.266 23.544 91.456 1.00 92.93 C ANISOU 2597 CB LEU A1133 14899 11323 9087 -2283 294 -1842 C ATOM 2598 CG LEU A1133 100.695 24.481 90.382 1.00 96.66 C ANISOU 2598 CG LEU A1133 15728 11564 9435 -2494 643 -1792 C ATOM 2599 CD1 LEU A1133 100.756 23.836 89.014 1.00 96.21 C ANISOU 2599 CD1 LEU A1133 15607 11503 9444 -2465 997 -1725 C ATOM 2600 CD2 LEU A1133 99.272 24.913 90.693 1.00 96.18 C ANISOU 2600 CD2 LEU A1133 16168 11351 9025 -2361 578 -1663 C ATOM 2601 N ALA A1134 100.963 23.124 94.833 1.00 93.10 N ANISOU 2601 N ALA A1134 14953 11700 8722 -1828 -663 -1835 N ATOM 2602 CA ALA A1134 100.078 22.925 95.987 1.00 91.70 C ANISOU 2602 CA ALA A1134 15044 11627 8170 -1558 -905 -1696 C ATOM 2603 C ALA A1134 100.217 24.067 97.003 1.00 97.43 C ANISOU 2603 C ALA A1134 15917 12410 8693 -1656 -1169 -1925 C ATOM 2604 O ALA A1134 99.288 24.313 97.776 1.00 96.38 O ANISOU 2604 O ALA A1134 16119 12322 8180 -1484 -1261 -1859 O ATOM 2605 CB ALA A1134 100.385 21.597 96.662 1.00 93.38 C ANISOU 2605 CB ALA A1134 15007 12048 8425 -1263 -1153 -1529 C ATOM 2606 N LYS A1135 101.375 24.761 96.990 1.00 96.72 N ANISOU 2606 N LYS A1135 15557 12315 8876 -1931 -1285 -2212 N ATOM 2607 CA LYS A1135 101.712 25.873 97.880 1.00 99.47 C ANISOU 2607 CA LYS A1135 15981 12682 9132 -2068 -1582 -2512 C ATOM 2608 C LYS A1135 101.090 27.212 97.415 1.00101.72 C ANISOU 2608 C LYS A1135 16639 12654 9355 -2305 -1370 -2625 C ATOM 2609 O LYS A1135 101.159 28.194 98.161 1.00104.19 O ANISOU 2609 O LYS A1135 17096 12924 9566 -2390 -1613 -2891 O ATOM 2610 CB LYS A1135 103.240 26.020 97.971 1.00106.39 C ANISOU 2610 CB LYS A1135 16350 13645 10427 -2296 -1800 -2777 C ATOM 2611 N SER A1136 100.476 27.248 96.209 1.00 94.10 N ANISOU 2611 N SER A1136 15846 11463 8446 -2386 -953 -2436 N ATOM 2612 CA SER A1136 99.857 28.447 95.624 1.00 92.87 C ANISOU 2612 CA SER A1136 16055 10978 8255 -2587 -736 -2481 C ATOM 2613 C SER A1136 98.610 28.905 96.400 1.00 94.23 C ANISOU 2613 C SER A1136 16680 11117 8005 -2348 -844 -2484 C ATOM 2614 O SER A1136 97.975 28.103 97.090 1.00 92.04 O ANISOU 2614 O SER A1136 16468 11070 7431 -2015 -947 -2337 O ATOM 2615 CB SER A1136 99.473 28.193 94.169 1.00 93.65 C ANISOU 2615 CB SER A1136 16230 10904 8449 -2659 -302 -2245 C ATOM 2616 OG SER A1136 98.489 27.179 94.048 1.00 98.69 O ANISOU 2616 OG SER A1136 17001 11641 8856 -2332 -216 -1991 O ATOM 2617 N ARG A1137 98.258 30.203 96.255 1.00 91.14 N ANISOU 2617 N ARG A1137 16592 10425 7612 -2520 -799 -2638 N ATOM 2618 CA ARG A1137 97.089 30.835 96.880 1.00 89.98 C ANISOU 2618 CA ARG A1137 16875 10200 7114 -2307 -866 -2697 C ATOM 2619 C ARG A1137 95.787 30.322 96.249 1.00 88.59 C ANISOU 2619 C ARG A1137 16937 9982 6742 -2074 -580 -2377 C ATOM 2620 O ARG A1137 94.734 30.386 96.883 1.00 87.18 O ANISOU 2620 O ARG A1137 17015 9870 6241 -1796 -619 -2353 O ATOM 2621 CB ARG A1137 97.173 32.363 96.756 1.00 92.91 C ANISOU 2621 CB ARG A1137 17474 10189 7638 -2570 -897 -2960 C ATOM 2622 N TRP A1138 95.873 29.816 95.000 1.00 82.33 N ANISOU 2622 N TRP A1138 16041 9094 6146 -2184 -297 -2152 N ATOM 2623 CA TRP A1138 94.777 29.237 94.221 1.00 78.10 C ANISOU 2623 CA TRP A1138 15671 8509 5493 -1998 -53 -1870 C ATOM 2624 C TRP A1138 94.239 27.968 94.903 1.00 79.62 C ANISOU 2624 C TRP A1138 15755 9006 5492 -1664 -136 -1691 C ATOM 2625 O TRP A1138 93.025 27.746 94.904 1.00 76.96 O ANISOU 2625 O TRP A1138 15618 8656 4966 -1439 -48 -1531 O ATOM 2626 CB TRP A1138 95.269 28.929 92.793 1.00 75.88 C ANISOU 2626 CB TRP A1138 15258 8113 5459 -2200 220 -1736 C ATOM 2627 CG TRP A1138 94.381 28.023 91.989 1.00 73.33 C ANISOU 2627 CG TRP A1138 15005 7806 5052 -1999 406 -1484 C ATOM 2628 CD1 TRP A1138 93.173 28.334 91.438 1.00 74.36 C ANISOU 2628 CD1 TRP A1138 15462 7756 5033 -1880 526 -1361 C ATOM 2629 CD2 TRP A1138 94.675 26.682 91.581 1.00 71.78 C ANISOU 2629 CD2 TRP A1138 14528 7786 4959 -1900 469 -1357 C ATOM 2630 NE1 TRP A1138 92.677 27.255 90.745 1.00 71.30 N ANISOU 2630 NE1 TRP A1138 15010 7438 4645 -1721 639 -1176 N ATOM 2631 CE2 TRP A1138 93.579 26.227 90.815 1.00 72.98 C ANISOU 2631 CE2 TRP A1138 14863 7852 5014 -1731 612 -1176 C ATOM 2632 CE3 TRP A1138 95.755 25.809 91.801 1.00 74.15 C ANISOU 2632 CE3 TRP A1138 14427 8294 5451 -1919 392 -1397 C ATOM 2633 CZ2 TRP A1138 93.530 24.939 90.269 1.00 70.79 C ANISOU 2633 CZ2 TRP A1138 14398 7670 4830 -1595 675 -1056 C ATOM 2634 CZ3 TRP A1138 95.703 24.532 91.265 1.00 74.07 C ANISOU 2634 CZ3 TRP A1138 14237 8372 5533 -1763 471 -1262 C ATOM 2635 CH2 TRP A1138 94.603 24.109 90.506 1.00 72.12 C ANISOU 2635 CH2 TRP A1138 14194 8016 5191 -1612 610 -1104 C ATOM 2636 N TYR A1139 95.143 27.152 95.486 1.00 77.08 N ANISOU 2636 N TYR A1139 15103 8941 5244 -1635 -310 -1705 N ATOM 2637 CA TYR A1139 94.808 25.915 96.191 1.00 75.78 C ANISOU 2637 CA TYR A1139 14815 9044 4933 -1341 -412 -1497 C ATOM 2638 C TYR A1139 94.016 26.223 97.467 1.00 80.61 C ANISOU 2638 C TYR A1139 15657 9815 5156 -1104 -562 -1516 C ATOM 2639 O TYR A1139 93.110 25.467 97.806 1.00 78.67 O ANISOU 2639 O TYR A1139 15464 9692 4733 -853 -503 -1264 O ATOM 2640 CB TYR A1139 96.082 25.113 96.520 1.00 78.91 C ANISOU 2640 CB TYR A1139 14811 9647 5524 -1367 -602 -1526 C ATOM 2641 CG TYR A1139 95.815 23.774 97.175 1.00 80.36 C ANISOU 2641 CG TYR A1139 14868 10058 5606 -1070 -713 -1261 C ATOM 2642 CD1 TYR A1139 95.498 22.653 96.412 1.00 80.15 C ANISOU 2642 CD1 TYR A1139 14724 9967 5761 -976 -547 -1016 C ATOM 2643 CD2 TYR A1139 95.907 23.619 98.555 1.00 83.52 C ANISOU 2643 CD2 TYR A1139 15274 10730 5731 -880 -997 -1252 C ATOM 2644 CE1 TYR A1139 95.246 21.419 97.009 1.00 81.19 C ANISOU 2644 CE1 TYR A1139 14743 10246 5860 -721 -652 -743 C ATOM 2645 CE2 TYR A1139 95.658 22.389 99.164 1.00 84.51 C ANISOU 2645 CE2 TYR A1139 15305 11045 5762 -612 -1085 -943 C ATOM 2646 CZ TYR A1139 95.331 21.290 98.386 1.00 89.68 C ANISOU 2646 CZ TYR A1139 15834 11580 6661 -546 -909 -678 C ATOM 2647 OH TYR A1139 95.093 20.072 98.978 1.00 91.07 O ANISOU 2647 OH TYR A1139 15916 11883 6805 -302 -1001 -348 O ATOM 2648 N ASN A1140 94.356 27.324 98.165 1.00 80.29 N ANISOU 2648 N ASN A1140 15741 9771 4994 -1185 -747 -1822 N ATOM 2649 CA ASN A1140 93.680 27.743 99.397 1.00 81.93 C ANISOU 2649 CA ASN A1140 16188 10155 4788 -946 -889 -1917 C ATOM 2650 C ASN A1140 92.480 28.666 99.090 1.00 84.44 C ANISOU 2650 C ASN A1140 16859 10237 4987 -891 -696 -1967 C ATOM 2651 O ASN A1140 91.766 29.065 100.011 1.00 85.35 O ANISOU 2651 O ASN A1140 17187 10485 4757 -664 -750 -2060 O ATOM 2652 CB ASN A1140 94.661 28.430 100.346 1.00 87.51 C ANISOU 2652 CB ASN A1140 16850 10982 5417 -1026 -1238 -2283 C ATOM 2653 CG ASN A1140 95.675 27.478 100.925 1.00113.74 C ANISOU 2653 CG ASN A1140 19841 14606 8768 -977 -1493 -2223 C ATOM 2654 OD1 ASN A1140 95.439 26.836 101.955 1.00109.29 O ANISOU 2654 OD1 ASN A1140 19299 14372 7855 -691 -1643 -2089 O ATOM 2655 ND2 ASN A1140 96.812 27.340 100.259 1.00106.71 N ANISOU 2655 ND2 ASN A1140 18630 13619 8296 -1240 -1533 -2295 N ATOM 2656 N GLN A1141 92.252 28.986 97.804 1.00 78.83 N ANISOU 2656 N GLN A1141 16211 9197 4544 -1069 -472 -1903 N ATOM 2657 CA GLN A1141 91.114 29.798 97.369 1.00 77.62 C ANISOU 2657 CA GLN A1141 16374 8790 4327 -1000 -306 -1914 C ATOM 2658 C GLN A1141 89.893 28.881 97.243 1.00 78.04 C ANISOU 2658 C GLN A1141 16433 8961 4259 -732 -126 -1592 C ATOM 2659 O GLN A1141 88.786 29.237 97.652 1.00 77.69 O ANISOU 2659 O GLN A1141 16582 8930 4006 -509 -60 -1592 O ATOM 2660 CB GLN A1141 91.439 30.515 96.041 1.00 78.52 C ANISOU 2660 CB GLN A1141 16566 8513 4755 -1299 -169 -1946 C ATOM 2661 CG GLN A1141 90.615 31.774 95.781 1.00 95.89 C ANISOU 2661 CG GLN A1141 19127 10383 6925 -1278 -113 -2067 C ATOM 2662 CD GLN A1141 91.030 32.925 96.667 1.00119.46 C ANISOU 2662 CD GLN A1141 22252 13272 9865 -1342 -335 -2444 C ATOM 2663 OE1 GLN A1141 92.074 33.556 96.462 1.00117.69 O ANISOU 2663 OE1 GLN A1141 21970 12859 9889 -1657 -428 -2623 O ATOM 2664 NE2 GLN A1141 90.215 33.229 97.666 1.00112.08 N ANISOU 2664 NE2 GLN A1141 21493 12463 8628 -1044 -418 -2590 N ATOM 2665 N THR A1142 90.136 27.676 96.699 1.00 72.02 N ANISOU 2665 N THR A1142 15425 8278 3661 -755 -54 -1336 N ATOM 2666 CA THR A1142 89.197 26.574 96.488 1.00 69.19 C ANISOU 2666 CA THR A1142 14984 8003 3303 -560 85 -1016 C ATOM 2667 C THR A1142 90.029 25.275 96.645 1.00 71.86 C ANISOU 2667 C THR A1142 15003 8532 3768 -569 1 -850 C ATOM 2668 O THR A1142 90.919 25.029 95.830 1.00 70.98 O ANISOU 2668 O THR A1142 14733 8319 3916 -759 7 -890 O ATOM 2669 CB THR A1142 88.439 26.719 95.140 1.00 74.23 C ANISOU 2669 CB THR A1142 15734 8351 4117 -605 271 -928 C ATOM 2670 OG1 THR A1142 87.761 25.497 94.840 1.00 72.21 O ANISOU 2670 OG1 THR A1142 15322 8158 3956 -467 357 -649 O ATOM 2671 CG2 THR A1142 89.345 27.101 93.975 1.00 71.88 C ANISOU 2671 CG2 THR A1142 15432 7829 4049 -889 316 -1029 C ATOM 2672 N PRO A1143 89.824 24.475 97.719 1.00 68.33 N ANISOU 2672 N PRO A1143 14460 8364 3137 -359 -79 -666 N ATOM 2673 CA PRO A1143 90.690 23.299 97.920 1.00 68.30 C ANISOU 2673 CA PRO A1143 14167 8506 3276 -350 -204 -509 C ATOM 2674 C PRO A1143 90.214 22.017 97.219 1.00 69.10 C ANISOU 2674 C PRO A1143 14103 8512 3641 -286 -79 -204 C ATOM 2675 O PRO A1143 91.068 21.241 96.793 1.00 68.58 O ANISOU 2675 O PRO A1143 13803 8417 3837 -351 -146 -173 O ATOM 2676 CB PRO A1143 90.675 23.098 99.437 1.00 72.90 C ANISOU 2676 CB PRO A1143 14772 9426 3502 -141 -364 -425 C ATOM 2677 CG PRO A1143 89.459 23.818 99.933 1.00 77.72 C ANISOU 2677 CG PRO A1143 15650 10084 3797 12 -228 -443 C ATOM 2678 CD PRO A1143 88.864 24.639 98.830 1.00 71.06 C ANISOU 2678 CD PRO A1143 14957 8918 3125 -112 -55 -589 C ATOM 2679 N ASN A1144 88.888 21.784 97.116 1.00 63.63 N ANISOU 2679 N ASN A1144 13503 7761 2913 -155 84 -4 N ATOM 2680 CA ASN A1144 88.301 20.576 96.524 1.00 61.49 C ANISOU 2680 CA ASN A1144 13072 7370 2920 -95 172 270 C ATOM 2681 C ASN A1144 88.475 20.524 94.993 1.00 61.71 C ANISOU 2681 C ASN A1144 13071 7124 3252 -246 244 137 C ATOM 2682 O ASN A1144 88.753 19.453 94.457 1.00 60.39 O ANISOU 2682 O ASN A1144 12706 6872 3369 -243 222 236 O ATOM 2683 CB ASN A1144 86.812 20.479 96.875 1.00 62.09 C ANISOU 2683 CB ASN A1144 13228 7468 2897 65 323 489 C ATOM 2684 CG ASN A1144 86.523 20.279 98.351 1.00 84.66 C ANISOU 2684 CG ASN A1144 16097 10633 5438 247 315 702 C ATOM 2685 OD1 ASN A1144 87.305 19.683 99.104 1.00 77.53 O ANISOU 2685 OD1 ASN A1144 15089 9909 4459 294 170 825 O ATOM 2686 ND2 ASN A1144 85.358 20.726 98.788 1.00 78.36 N ANISOU 2686 ND2 ASN A1144 15416 9917 4440 376 478 768 N ATOM 2687 N ARG A1145 88.305 21.658 94.297 1.00 56.97 N ANISOU 2687 N ARG A1145 12680 6383 2581 -358 325 -82 N ATOM 2688 CA ARG A1145 88.448 21.722 92.841 1.00 55.14 C ANISOU 2688 CA ARG A1145 12476 5929 2544 -488 410 -194 C ATOM 2689 C ARG A1145 89.934 21.663 92.452 1.00 60.12 C ANISOU 2689 C ARG A1145 12956 6582 3303 -661 374 -355 C ATOM 2690 O ARG A1145 90.276 20.954 91.507 1.00 59.24 O ANISOU 2690 O ARG A1145 12714 6387 3408 -693 423 -366 O ATOM 2691 CB ARG A1145 87.776 22.995 92.288 1.00 53.77 C ANISOU 2691 CB ARG A1145 12603 5595 2232 -536 500 -323 C ATOM 2692 CG ARG A1145 87.765 23.118 90.765 1.00 58.81 C ANISOU 2692 CG ARG A1145 13334 6023 2990 -638 592 -394 C ATOM 2693 CD ARG A1145 86.795 24.191 90.317 1.00 63.74 C ANISOU 2693 CD ARG A1145 14258 6477 3483 -608 644 -433 C ATOM 2694 NE ARG A1145 86.923 24.498 88.891 1.00 66.42 N ANISOU 2694 NE ARG A1145 14746 6635 3854 -713 721 -493 N ATOM 2695 CZ ARG A1145 86.082 25.273 88.212 1.00 78.56 C ANISOU 2695 CZ ARG A1145 16550 7994 5304 -668 742 -494 C ATOM 2696 NH1 ARG A1145 85.015 25.790 88.807 1.00 67.06 N ANISOU 2696 NH1 ARG A1145 15203 6503 3773 -509 697 -464 N ATOM 2697 NH2 ARG A1145 86.289 25.516 86.926 1.00 64.12 N ANISOU 2697 NH2 ARG A1145 14877 6034 3450 -757 811 -520 N ATOM 2698 N ALA A1146 90.805 22.379 93.196 1.00 58.56 N ANISOU 2698 N ALA A1146 12755 6506 2990 -759 282 -501 N ATOM 2699 CA ALA A1146 92.249 22.452 92.953 1.00 59.76 C ANISOU 2699 CA ALA A1146 12712 6700 3293 -942 242 -672 C ATOM 2700 C ALA A1146 92.942 21.098 93.116 1.00 64.02 C ANISOU 2700 C ALA A1146 12917 7357 4052 -847 143 -574 C ATOM 2701 O ALA A1146 93.791 20.770 92.282 1.00 64.13 O ANISOU 2701 O ALA A1146 12743 7332 4292 -949 211 -679 O ATOM 2702 CB ALA A1146 92.889 23.456 93.893 1.00 62.71 C ANISOU 2702 CB ALA A1146 13130 7176 3519 -1044 101 -854 C ATOM 2703 N LYS A1147 92.587 20.314 94.170 1.00 60.46 N ANISOU 2703 N LYS A1147 12391 7045 3537 -642 -3 -364 N ATOM 2704 CA LYS A1147 93.203 19.008 94.435 1.00 61.05 C ANISOU 2704 CA LYS A1147 12166 7194 3835 -522 -136 -230 C ATOM 2705 C LYS A1147 92.882 18.015 93.290 1.00 62.89 C ANISOU 2705 C LYS A1147 12301 7225 4368 -476 -17 -165 C ATOM 2706 O LYS A1147 93.751 17.221 92.935 1.00 63.57 O ANISOU 2706 O LYS A1147 12126 7300 4726 -453 -67 -218 O ATOM 2707 CB LYS A1147 92.802 18.423 95.811 1.00 64.77 C ANISOU 2707 CB LYS A1147 12631 7842 4138 -311 -301 47 C ATOM 2708 CG LYS A1147 91.333 18.050 96.004 1.00 77.71 C ANISOU 2708 CG LYS A1147 14421 9417 5688 -171 -186 328 C ATOM 2709 N ARG A1148 91.674 18.103 92.687 1.00 56.79 N ANISOU 2709 N ARG A1148 11728 6295 3557 -452 122 -96 N ATOM 2710 CA ARG A1148 91.253 17.246 91.575 1.00 55.23 C ANISOU 2710 CA ARG A1148 11473 5897 3615 -404 198 -85 C ATOM 2711 C ARG A1148 92.005 17.592 90.288 1.00 60.39 C ANISOU 2711 C ARG A1148 12117 6490 4338 -544 333 -360 C ATOM 2712 O ARG A1148 92.313 16.692 89.507 1.00 60.45 O ANISOU 2712 O ARG A1148 11967 6412 4590 -486 350 -431 O ATOM 2713 CB ARG A1148 89.741 17.353 91.325 1.00 51.74 C ANISOU 2713 CB ARG A1148 11230 5322 3105 -342 270 40 C ATOM 2714 CG ARG A1148 88.871 16.721 92.396 1.00 57.64 C ANISOU 2714 CG ARG A1148 11929 6109 3864 -194 201 357 C ATOM 2715 CD ARG A1148 87.422 16.603 91.954 1.00 61.23 C ANISOU 2715 CD ARG A1148 12475 6405 4385 -140 273 462 C ATOM 2716 NE ARG A1148 86.760 17.900 91.796 1.00 66.71 N ANISOU 2716 NE ARG A1148 13428 7118 4802 -184 373 351 N ATOM 2717 CZ ARG A1148 86.054 18.506 92.746 1.00 83.36 C ANISOU 2717 CZ ARG A1148 15643 9353 6678 -118 417 468 C ATOM 2718 NH1 ARG A1148 85.913 17.942 93.940 1.00 75.24 N ANISOU 2718 NH1 ARG A1148 14498 8481 5607 -16 392 725 N ATOM 2719 NH2 ARG A1148 85.484 19.679 92.511 1.00 69.34 N ANISOU 2719 NH2 ARG A1148 14098 7551 4698 -136 491 333 N ATOM 2720 N VAL A1149 92.289 18.891 90.067 1.00 57.64 N ANISOU 2720 N VAL A1149 11944 6178 3779 -723 440 -510 N ATOM 2721 CA VAL A1149 92.993 19.380 88.880 1.00 58.25 C ANISOU 2721 CA VAL A1149 12042 6217 3873 -888 622 -718 C ATOM 2722 C VAL A1149 94.506 19.092 89.021 1.00 65.31 C ANISOU 2722 C VAL A1149 12600 7253 4960 -965 605 -853 C ATOM 2723 O VAL A1149 95.119 18.649 88.045 1.00 65.68 O ANISOU 2723 O VAL A1149 12502 7295 5159 -981 742 -986 O ATOM 2724 CB VAL A1149 92.713 20.893 88.624 1.00 61.64 C ANISOU 2724 CB VAL A1149 12787 6584 4050 -1066 741 -777 C ATOM 2725 CG1 VAL A1149 93.561 21.446 87.479 1.00 62.79 C ANISOU 2725 CG1 VAL A1149 12947 6706 4203 -1269 962 -932 C ATOM 2726 CG2 VAL A1149 91.234 21.139 88.343 1.00 59.54 C ANISOU 2726 CG2 VAL A1149 12817 6174 3632 -958 750 -667 C ATOM 2727 N ILE A1150 95.097 19.324 90.219 1.00 63.87 N ANISOU 2727 N ILE A1150 12284 7215 4770 -989 431 -838 N ATOM 2728 CA ILE A1150 96.536 19.136 90.427 1.00 66.60 C ANISOU 2728 CA ILE A1150 12275 7706 5325 -1061 370 -981 C ATOM 2729 C ILE A1150 96.904 17.625 90.377 1.00 71.83 C ANISOU 2729 C ILE A1150 12627 8381 6283 -840 269 -935 C ATOM 2730 O ILE A1150 97.959 17.307 89.828 1.00 73.20 O ANISOU 2730 O ILE A1150 12510 8613 6689 -875 345 -1106 O ATOM 2731 CB ILE A1150 97.081 19.818 91.727 1.00 71.47 C ANISOU 2731 CB ILE A1150 12832 8477 5845 -1134 148 -1016 C ATOM 2732 CG1 ILE A1150 98.617 19.996 91.695 1.00 75.05 C ANISOU 2732 CG1 ILE A1150 12915 9059 6540 -1295 119 -1230 C ATOM 2733 CG2 ILE A1150 96.617 19.157 93.026 1.00 72.38 C ANISOU 2733 CG2 ILE A1150 12947 8694 5858 -897 -124 -806 C ATOM 2734 CD1 ILE A1150 99.159 20.785 90.500 1.00 83.38 C ANISOU 2734 CD1 ILE A1150 13960 10043 7679 -1573 434 -1402 C ATOM 2735 N THR A1151 96.037 16.714 90.887 1.00 67.94 N ANISOU 2735 N THR A1151 12187 7815 5812 -619 122 -706 N ATOM 2736 CA THR A1151 96.298 15.265 90.859 1.00 69.08 C ANISOU 2736 CA THR A1151 12068 7896 6283 -404 2 -637 C ATOM 2737 C THR A1151 96.150 14.765 89.401 1.00 72.93 C ANISOU 2737 C THR A1151 12553 8224 6933 -378 201 -803 C ATOM 2738 O THR A1151 96.805 13.788 89.029 1.00 74.33 O ANISOU 2738 O THR A1151 12459 8364 7421 -245 168 -907 O ATOM 2739 CB THR A1151 95.386 14.509 91.851 1.00 75.91 C ANISOU 2739 CB THR A1151 13004 8701 7138 -213 -192 -299 C ATOM 2740 OG1 THR A1151 95.479 15.130 93.135 1.00 76.49 O ANISOU 2740 OG1 THR A1151 13144 8972 6948 -230 -342 -178 O ATOM 2741 CG2 THR A1151 95.755 13.034 91.995 1.00 75.85 C ANISOU 2741 CG2 THR A1151 12720 8588 7511 6 -363 -186 C ATOM 2742 N THR A1152 95.338 15.465 88.575 1.00 67.92 N ANISOU 2742 N THR A1152 12224 7508 6076 -485 393 -853 N ATOM 2743 CA THR A1152 95.148 15.147 87.157 1.00 67.76 C ANISOU 2743 CA THR A1152 12267 7377 6104 -458 571 -1032 C ATOM 2744 C THR A1152 96.452 15.511 86.407 1.00 74.02 C ANISOU 2744 C THR A1152 12876 8319 6930 -582 788 -1291 C ATOM 2745 O THR A1152 96.892 14.720 85.578 1.00 75.08 O ANISOU 2745 O THR A1152 12843 8436 7247 -465 872 -1474 O ATOM 2746 CB THR A1152 93.895 15.852 86.601 1.00 73.14 C ANISOU 2746 CB THR A1152 13336 7949 6506 -517 664 -979 C ATOM 2747 OG1 THR A1152 92.754 15.374 87.318 1.00 71.27 O ANISOU 2747 OG1 THR A1152 13173 7591 6314 -392 483 -744 O ATOM 2748 CG2 THR A1152 93.680 15.603 85.110 1.00 71.27 C ANISOU 2748 CG2 THR A1152 13210 7630 6239 -475 818 -1176 C ATOM 2749 N PHE A1153 97.085 16.666 86.729 1.00 71.55 N ANISOU 2749 N PHE A1153 12567 8146 6473 -813 877 -1317 N ATOM 2750 CA PHE A1153 98.361 17.082 86.125 1.00 74.30 C ANISOU 2750 CA PHE A1153 12687 8645 6898 -977 1107 -1525 C ATOM 2751 C PHE A1153 99.521 16.192 86.591 1.00 81.19 C ANISOU 2751 C PHE A1153 13075 9635 8137 -854 977 -1629 C ATOM 2752 O PHE A1153 100.440 15.926 85.816 1.00 83.32 O ANISOU 2752 O PHE A1153 13080 10005 8572 -857 1181 -1837 O ATOM 2753 CB PHE A1153 98.693 18.550 86.448 1.00 76.67 C ANISOU 2753 CB PHE A1153 13096 9008 7027 -1282 1194 -1511 C ATOM 2754 CG PHE A1153 98.085 19.607 85.554 1.00 77.56 C ANISOU 2754 CG PHE A1153 13605 9025 6838 -1458 1443 -1482 C ATOM 2755 CD1 PHE A1153 98.586 19.834 84.277 1.00 82.82 C ANISOU 2755 CD1 PHE A1153 14275 9741 7450 -1568 1788 -1594 C ATOM 2756 CD2 PHE A1153 97.093 20.455 86.030 1.00 77.66 C ANISOU 2756 CD2 PHE A1153 13980 8912 6614 -1514 1343 -1336 C ATOM 2757 CE1 PHE A1153 98.051 20.838 83.464 1.00 83.51 C ANISOU 2757 CE1 PHE A1153 14757 9736 7238 -1724 2004 -1518 C ATOM 2758 CE2 PHE A1153 96.569 21.469 85.222 1.00 80.19 C ANISOU 2758 CE2 PHE A1153 14668 9117 6683 -1660 1543 -1293 C ATOM 2759 CZ PHE A1153 97.049 21.650 83.943 1.00 80.25 C ANISOU 2759 CZ PHE A1153 14705 9159 6628 -1766 1862 -1364 C ATOM 2760 N ARG A1154 99.475 15.757 87.863 1.00 77.99 N ANISOU 2760 N ARG A1154 12558 9233 7840 -732 644 -1475 N ATOM 2761 CA ARG A1154 100.465 14.912 88.536 1.00 80.76 C ANISOU 2761 CA ARG A1154 12479 9678 8528 -575 422 -1511 C ATOM 2762 C ARG A1154 100.510 13.495 87.929 1.00 86.55 C ANISOU 2762 C ARG A1154 13032 10287 9566 -293 408 -1587 C ATOM 2763 O ARG A1154 101.598 12.998 87.632 1.00 89.19 O ANISOU 2763 O ARG A1154 12980 10713 10198 -210 447 -1789 O ATOM 2764 CB ARG A1154 100.118 14.843 90.039 1.00 80.46 C ANISOU 2764 CB ARG A1154 12497 9662 8412 -490 62 -1258 C ATOM 2765 CG ARG A1154 100.856 13.805 90.877 1.00 93.20 C ANISOU 2765 CG ARG A1154 13752 11329 10331 -254 -253 -1193 C ATOM 2766 CD ARG A1154 100.184 13.690 92.231 1.00103.84 C ANISOU 2766 CD ARG A1154 15281 12687 11485 -145 -555 -873 C ATOM 2767 NE ARG A1154 100.601 12.494 92.962 1.00116.89 N ANISOU 2767 NE ARG A1154 16681 14323 13407 134 -865 -709 N ATOM 2768 CZ ARG A1154 100.087 12.108 94.127 1.00132.51 C ANISOU 2768 CZ ARG A1154 18787 16311 15249 286 -1127 -371 C ATOM 2769 NH1 ARG A1154 99.126 12.821 94.704 1.00117.75 N ANISOU 2769 NH1 ARG A1154 17273 14493 12971 196 -1098 -196 N ATOM 2770 NH2 ARG A1154 100.522 11.005 94.719 1.00122.60 N ANISOU 2770 NH2 ARG A1154 17309 15016 14257 545 -1408 -193 N ATOM 2771 N THR A1155 99.342 12.847 87.767 1.00 81.66 N ANISOU 2771 N THR A1155 12666 9448 8912 -144 340 -1445 N ATOM 2772 CA THR A1155 99.247 11.470 87.273 1.00 82.91 C ANISOU 2772 CA THR A1155 12687 9416 9398 127 268 -1519 C ATOM 2773 C THR A1155 99.038 11.394 85.753 1.00 87.82 C ANISOU 2773 C THR A1155 13428 9984 9956 135 553 -1796 C ATOM 2774 O THR A1155 99.669 10.563 85.096 1.00 89.99 O ANISOU 2774 O THR A1155 13458 10235 10500 314 608 -2046 O ATOM 2775 CB THR A1155 98.096 10.722 87.975 1.00 88.67 C ANISOU 2775 CB THR A1155 13589 9906 10197 273 9 -1204 C ATOM 2776 OG1 THR A1155 96.866 11.419 87.755 1.00 84.24 O ANISOU 2776 OG1 THR A1155 13418 9284 9306 137 111 -1092 O ATOM 2777 CG2 THR A1155 98.336 10.537 89.471 1.00 88.40 C ANISOU 2777 CG2 THR A1155 13433 9936 10219 339 -285 -906 C ATOM 2778 N GLY A1156 98.147 12.228 85.223 1.00 82.82 N ANISOU 2778 N GLY A1156 13176 9334 8958 -24 713 -1759 N ATOM 2779 CA GLY A1156 97.781 12.214 83.812 1.00 83.29 C ANISOU 2779 CA GLY A1156 13429 9355 8863 -1 943 -1985 C ATOM 2780 C GLY A1156 96.670 11.214 83.575 1.00 87.38 C ANISOU 2780 C GLY A1156 14088 9590 9523 203 742 -1961 C ATOM 2781 O GLY A1156 96.656 10.527 82.550 1.00 88.63 O ANISOU 2781 O GLY A1156 14238 9670 9767 362 801 -2233 O ATOM 2782 N THR A1157 95.745 11.111 84.555 1.00 82.70 N ANISOU 2782 N THR A1157 13605 8846 8972 201 503 -1643 N ATOM 2783 CA THR A1157 94.600 10.196 84.554 1.00 82.32 C ANISOU 2783 CA THR A1157 13649 8500 9129 346 291 -1542 C ATOM 2784 C THR A1157 93.297 10.963 84.776 1.00 84.97 C ANISOU 2784 C THR A1157 14311 8794 9182 216 277 -1315 C ATOM 2785 O THR A1157 93.246 11.876 85.605 1.00 83.03 O ANISOU 2785 O THR A1157 14151 8691 8705 72 306 -1104 O ATOM 2786 CB THR A1157 94.764 9.105 85.632 1.00 90.44 C ANISOU 2786 CB THR A1157 14416 9363 10584 500 18 -1319 C ATOM 2787 OG1 THR A1157 94.884 9.715 86.919 1.00 89.16 O ANISOU 2787 OG1 THR A1157 14247 9358 10271 393 -46 -1003 O ATOM 2788 CG2 THR A1157 95.955 8.194 85.379 1.00 91.88 C ANISOU 2788 CG2 THR A1157 14257 9526 11129 689 -19 -1559 C ATOM 2789 N TRP A1158 92.238 10.562 84.055 1.00 82.71 N ANISOU 2789 N TRP A1158 14184 8303 8940 286 207 -1384 N ATOM 2790 CA TRP A1158 90.900 11.149 84.147 1.00 81.13 C ANISOU 2790 CA TRP A1158 14246 8035 8545 205 168 -1203 C ATOM 2791 C TRP A1158 90.118 10.480 85.305 1.00 84.10 C ANISOU 2791 C TRP A1158 14507 8231 9214 247 -37 -848 C ATOM 2792 O TRP A1158 89.008 10.906 85.634 1.00 82.04 O ANISOU 2792 O TRP A1158 14393 7933 8846 189 -61 -648 O ATOM 2793 CB TRP A1158 90.174 10.999 82.791 1.00 81.08 C ANISOU 2793 CB TRP A1158 14430 7909 8468 272 155 -1468 C ATOM 2794 CG TRP A1158 88.811 11.624 82.719 1.00 80.82 C ANISOU 2794 CG TRP A1158 14644 7811 8252 213 97 -1330 C ATOM 2795 CD1 TRP A1158 88.512 12.955 82.785 1.00 82.16 C ANISOU 2795 CD1 TRP A1158 15062 8136 8018 81 230 -1223 C ATOM 2796 CD2 TRP A1158 87.569 10.944 82.486 1.00 81.25 C ANISOU 2796 CD2 TRP A1158 14700 7609 8562 295 -124 -1317 C ATOM 2797 NE1 TRP A1158 87.153 13.141 82.670 1.00 80.95 N ANISOU 2797 NE1 TRP A1158 15054 7856 7846 101 106 -1132 N ATOM 2798 CE2 TRP A1158 86.550 11.923 82.476 1.00 83.68 C ANISOU 2798 CE2 TRP A1158 15237 7961 8596 219 -109 -1188 C ATOM 2799 CE3 TRP A1158 87.213 9.595 82.307 1.00 84.54 C ANISOU 2799 CE3 TRP A1158 14926 7734 9462 420 -349 -1406 C ATOM 2800 CZ2 TRP A1158 85.200 11.597 82.290 1.00 83.22 C ANISOU 2800 CZ2 TRP A1158 15189 7702 8730 266 -307 -1149 C ATOM 2801 CZ3 TRP A1158 85.877 9.274 82.121 1.00 86.33 C ANISOU 2801 CZ3 TRP A1158 15171 7737 9892 437 -547 -1365 C ATOM 2802 CH2 TRP A1158 84.887 10.267 82.110 1.00 85.28 C ANISOU 2802 CH2 TRP A1158 15235 7690 9477 360 -523 -1239 C ATOM 2803 N ASP A1159 90.746 9.482 85.967 1.00 82.26 N ANISOU 2803 N ASP A1159 14005 7909 9343 353 -165 -746 N ATOM 2804 CA ASP A1159 90.195 8.713 87.087 1.00 82.56 C ANISOU 2804 CA ASP A1159 13914 7775 9679 403 -339 -360 C ATOM 2805 C ASP A1159 90.220 9.512 88.416 1.00 83.90 C ANISOU 2805 C ASP A1159 14138 8191 9550 313 -292 -20 C ATOM 2806 O ASP A1159 89.777 8.994 89.445 1.00 84.28 O ANISOU 2806 O ASP A1159 14110 8165 9745 353 -394 351 O ATOM 2807 CB ASP A1159 90.962 7.390 87.247 1.00 87.60 C ANISOU 2807 CB ASP A1159 14273 8214 10798 573 -507 -374 C ATOM 2808 CG ASP A1159 90.728 6.420 86.103 1.00101.44 C ANISOU 2808 CG ASP A1159 15969 9654 12918 695 -607 -694 C ATOM 2809 OD1 ASP A1159 91.685 6.154 85.343 1.00103.98 O ANISOU 2809 OD1 ASP A1159 16194 10010 13302 803 -567 -1061 O ATOM 2810 OD2 ASP A1159 89.587 5.920 85.971 1.00108.08 O ANISOU 2810 OD2 ASP A1159 16849 10220 13998 688 -728 -597 O ATOM 2811 N ALA A1160 90.687 10.773 88.389 1.00 78.15 N ANISOU 2811 N ALA A1160 13552 7742 8398 192 -137 -142 N ATOM 2812 CA ALA A1160 90.666 11.658 89.557 1.00 76.76 C ANISOU 2812 CA ALA A1160 13466 7799 7901 112 -108 91 C ATOM 2813 C ALA A1160 89.234 12.171 89.797 1.00 77.65 C ANISOU 2813 C ALA A1160 13785 7880 7840 67 -54 280 C ATOM 2814 O ALA A1160 88.902 12.615 90.898 1.00 76.48 O ANISOU 2814 O ALA A1160 13697 7881 7482 57 -45 528 O ATOM 2815 CB ALA A1160 91.630 12.819 89.352 1.00 77.06 C ANISOU 2815 CB ALA A1160 13573 8080 7627 -20 21 -144 C ATOM 2816 N TYR A1161 88.393 12.077 88.743 1.00 73.02 N ANISOU 2816 N TYR A1161 13291 7110 7343 64 -30 137 N ATOM 2817 CA TYR A1161 86.984 12.468 88.672 1.00 71.37 C ANISOU 2817 CA TYR A1161 13227 6831 7058 43 -1 246 C ATOM 2818 C TYR A1161 86.077 11.248 88.511 1.00 77.86 C ANISOU 2818 C TYR A1161 13888 7363 8333 116 -133 376 C ATOM 2819 O TYR A1161 84.965 11.235 89.041 1.00 77.44 O ANISOU 2819 O TYR A1161 13820 7265 8339 110 -125 628 O ATOM 2820 CB TYR A1161 86.766 13.428 87.490 1.00 70.31 C ANISOU 2820 CB TYR A1161 13335 6717 6662 -18 90 -47 C ATOM 2821 CG TYR A1161 87.393 14.793 87.670 1.00 69.82 C ANISOU 2821 CG TYR A1161 13461 6881 6185 -129 233 -127 C ATOM 2822 CD1 TYR A1161 86.633 15.878 88.091 1.00 70.33 C ANISOU 2822 CD1 TYR A1161 13727 7021 5974 -168 297 -33 C ATOM 2823 CD2 TYR A1161 88.742 15.006 87.395 1.00 70.87 C ANISOU 2823 CD2 TYR A1161 13551 7132 6243 -195 303 -313 C ATOM 2824 CE1 TYR A1161 87.202 17.139 88.250 1.00 70.14 C ANISOU 2824 CE1 TYR A1161 13882 7144 5622 -278 403 -125 C ATOM 2825 CE2 TYR A1161 89.324 16.261 87.560 1.00 71.13 C ANISOU 2825 CE2 TYR A1161 13732 7331 5964 -332 423 -384 C ATOM 2826 CZ TYR A1161 88.547 17.328 87.977 1.00 76.38 C ANISOU 2826 CZ TYR A1161 14625 8026 6370 -377 461 -294 C ATOM 2827 OH TYR A1161 89.114 18.567 88.149 1.00 76.41 O ANISOU 2827 OH TYR A1161 14780 8137 6118 -519 554 -379 O ATOM 2828 N SER A1162 86.548 10.239 87.755 1.00 77.05 N ANISOU 2828 N SER A1162 13650 7054 8573 185 -249 180 N ATOM 2829 CA SER A1162 85.825 9.002 87.467 1.00 79.34 C ANISOU 2829 CA SER A1162 13772 6999 9374 245 -418 229 C ATOM 2830 C SER A1162 86.085 7.952 88.547 1.00 86.97 C ANISOU 2830 C SER A1162 14510 7835 10698 297 -508 590 C ATOM 2831 O SER A1162 87.233 7.726 88.929 1.00 87.38 O ANISOU 2831 O SER A1162 14483 7977 10742 357 -528 592 O ATOM 2832 CB SER A1162 86.233 8.464 86.098 1.00 83.97 C ANISOU 2832 CB SER A1162 14354 7419 10132 322 -513 -213 C ATOM 2833 OG SER A1162 85.515 7.292 85.747 1.00 95.39 O ANISOU 2833 OG SER A1162 15646 8491 12105 377 -718 -234 O ATOM 2834 N GLY A1163 85.014 7.323 89.022 1.00 86.17 N ANISOU 2834 N GLY A1163 14293 7522 10926 274 -564 909 N ATOM 2835 CA GLY A1163 85.087 6.278 90.036 1.00 89.31 C ANISOU 2835 CA GLY A1163 14494 7751 11689 313 -641 1336 C ATOM 2836 C GLY A1163 85.176 4.899 89.416 1.00 97.38 C ANISOU 2836 C GLY A1163 15328 8320 13352 382 -861 1218 C ATOM 2837 O GLY A1163 84.252 4.094 89.566 1.00 99.38 O ANISOU 2837 O GLY A1163 15436 8249 14076 335 -945 1457 O ATOM 2838 N SER A1164 86.288 4.624 88.700 1.00 95.04 N ANISOU 2838 N SER A1164 15017 7987 13106 493 -948 831 N ATOM 2839 CA SER A1164 86.512 3.347 88.018 1.00 98.25 C ANISOU 2839 CA SER A1164 15260 7963 14106 603 -1169 612 C ATOM 2840 C SER A1164 87.977 2.868 88.210 1.00104.40 C ANISOU 2840 C SER A1164 15929 8765 14973 768 -1234 523 C ATOM 2841 O SER A1164 88.442 2.796 89.350 1.00104.65 O ANISOU 2841 O SER A1164 15901 8911 14951 795 -1229 922 O ATOM 2842 CB SER A1164 86.162 3.473 86.536 1.00101.43 C ANISOU 2842 CB SER A1164 15757 8274 14508 616 -1225 59 C ATOM 2843 N GLY A 231 88.667 2.544 87.109 1.00124.97 N ANISOU 2843 N GLY A 231 27307 12949 7225 -1976 1661 108 N ATOM 2844 CA GLY A 231 90.038 2.039 87.097 1.00125.55 C ANISOU 2844 CA GLY A 231 27462 13114 7128 -1706 1209 249 C ATOM 2845 C GLY A 231 91.130 3.036 87.435 1.00129.65 C ANISOU 2845 C GLY A 231 27844 13894 7523 -1623 827 168 C ATOM 2846 O GLY A 231 90.876 4.049 88.092 1.00129.81 O ANISOU 2846 O GLY A 231 27924 13957 7443 -1784 920 28 O ATOM 2847 N HIS A 232 92.379 2.714 87.030 1.00126.17 N ANISOU 2847 N HIS A 232 27241 13641 7058 -1377 402 248 N ATOM 2848 CA HIS A 232 93.576 3.534 87.279 1.00126.77 C ANISOU 2848 CA HIS A 232 27133 14034 6999 -1312 -2 158 C ATOM 2849 C HIS A 232 94.608 3.384 86.155 1.00128.67 C ANISOU 2849 C HIS A 232 26902 14508 7479 -1121 -341 176 C ATOM 2850 O HIS A 232 94.656 2.335 85.508 1.00127.68 O ANISOU 2850 O HIS A 232 26759 14288 7465 -928 -352 322 O ATOM 2851 CB HIS A 232 94.252 3.159 88.621 1.00132.05 C ANISOU 2851 CB HIS A 232 28276 14778 7120 -1165 -237 241 C ATOM 2852 CG HIS A 232 93.337 2.613 89.674 1.00138.07 C ANISOU 2852 CG HIS A 232 29647 15238 7575 -1239 88 328 C ATOM 2853 ND1 HIS A 232 93.062 1.259 89.754 1.00141.36 N ANISOU 2853 ND1 HIS A 232 30450 15404 7857 -1076 208 535 N ATOM 2854 CD2 HIS A 232 92.664 3.254 90.657 1.00141.37 C ANISOU 2854 CD2 HIS A 232 30366 15560 7789 -1471 335 228 C ATOM 2855 CE1 HIS A 232 92.235 1.120 90.776 1.00143.17 C ANISOU 2855 CE1 HIS A 232 31195 15400 7805 -1237 528 552 C ATOM 2856 NE2 HIS A 232 91.964 2.292 91.350 1.00143.56 N ANISOU 2856 NE2 HIS A 232 31196 15544 7807 -1467 613 370 N ATOM 2857 N GLN A 233 95.460 4.422 85.965 1.00124.65 N ANISOU 2857 N GLN A 233 26042 14301 7017 -1193 -602 18 N ATOM 2858 CA GLN A 233 96.582 4.515 85.012 1.00123.25 C ANISOU 2858 CA GLN A 233 25382 14422 7026 -1067 -935 -16 C ATOM 2859 C GLN A 233 96.190 4.078 83.569 1.00122.87 C ANISOU 2859 C GLN A 233 25013 14244 7428 -1013 -790 41 C ATOM 2860 O GLN A 233 96.946 3.355 82.910 1.00122.32 O ANISOU 2860 O GLN A 233 24747 14300 7429 -769 -1013 131 O ATOM 2861 CB GLN A 233 97.770 3.668 85.510 1.00128.06 C ANISOU 2861 CB GLN A 233 26085 15284 7290 -730 -1345 100 C ATOM 2862 N LYS A 234 95.036 4.556 83.074 1.00116.23 N ANISOU 2862 N LYS A 234 24105 13181 6876 -1224 -429 -24 N ATOM 2863 CA LYS A 234 94.564 4.224 81.729 1.00112.67 C ANISOU 2863 CA LYS A 234 23355 12626 6830 -1201 -285 9 C ATOM 2864 C LYS A 234 94.978 5.338 80.743 1.00114.10 C ANISOU 2864 C LYS A 234 23076 12977 7302 -1313 -369 -144 C ATOM 2865 O LYS A 234 94.142 6.135 80.305 1.00112.14 O ANISOU 2865 O LYS A 234 22718 12614 7274 -1478 -119 -243 O ATOM 2866 CB LYS A 234 93.040 3.991 81.721 1.00114.09 C ANISOU 2866 CB LYS A 234 23702 12514 7132 -1339 147 23 C ATOM 2867 CG LYS A 234 92.598 2.753 82.495 1.00128.39 C ANISOU 2867 CG LYS A 234 25983 14116 8683 -1268 284 178 C ATOM 2868 CD LYS A 234 91.098 2.540 82.398 1.00136.06 C ANISOU 2868 CD LYS A 234 27043 14859 9793 -1464 732 152 C ATOM 2869 CE LYS A 234 90.664 1.285 83.111 1.00147.58 C ANISOU 2869 CE LYS A 234 29006 16083 10986 -1452 911 294 C ATOM 2870 NZ LYS A 234 89.203 1.054 82.973 1.00155.18 N ANISOU 2870 NZ LYS A 234 29999 16876 12088 -1697 1366 235 N ATOM 2871 N ARG A 235 96.283 5.390 80.409 1.00110.64 N ANISOU 2871 N ARG A 235 22380 12820 6839 -1212 -713 -167 N ATOM 2872 CA ARG A 235 96.849 6.390 79.497 1.00108.57 C ANISOU 2872 CA ARG A 235 21714 12730 6806 -1345 -801 -315 C ATOM 2873 C ARG A 235 97.165 5.769 78.131 1.00109.45 C ANISOU 2873 C ARG A 235 21488 12881 7216 -1188 -866 -245 C ATOM 2874 O ARG A 235 97.800 4.713 78.067 1.00110.24 O ANISOU 2874 O ARG A 235 21573 13077 7235 -935 -1060 -124 O ATOM 2875 CB ARG A 235 98.115 7.017 80.102 1.00111.71 C ANISOU 2875 CB ARG A 235 22024 13470 6950 -1421 -1116 -443 C ATOM 2876 N LYS A 236 96.704 6.425 77.043 1.00102.34 N ANISOU 2876 N LYS A 236 20349 11893 6641 -1313 -697 -317 N ATOM 2877 CA LYS A 236 96.905 5.977 75.657 1.00 99.46 C ANISOU 2877 CA LYS A 236 19671 11547 6572 -1202 -724 -271 C ATOM 2878 C LYS A 236 97.419 7.119 74.771 1.00100.98 C ANISOU 2878 C LYS A 236 19556 11864 6948 -1370 -756 -420 C ATOM 2879 O LYS A 236 96.975 8.261 74.915 1.00100.37 O ANISOU 2879 O LYS A 236 19556 11697 6884 -1575 -601 -537 O ATOM 2880 CB LYS A 236 95.607 5.398 75.052 1.00 99.74 C ANISOU 2880 CB LYS A 236 19766 11309 6823 -1168 -442 -184 C ATOM 2881 CG LYS A 236 95.173 4.032 75.596 1.00115.07 C ANISOU 2881 CG LYS A 236 21999 13099 8621 -1019 -382 -28 C ATOM 2882 CD LYS A 236 94.285 4.116 76.838 1.00126.73 C ANISOU 2882 CD LYS A 236 23850 14421 9880 -1129 -181 -27 C ATOM 2883 N ALA A 237 98.344 6.798 73.842 1.00 95.97 N ANISOU 2883 N ALA A 237 18607 11417 6441 -1276 -932 -415 N ATOM 2884 CA ALA A 237 98.942 7.757 72.908 1.00 94.40 C ANISOU 2884 CA ALA A 237 18123 11339 6403 -1446 -953 -551 C ATOM 2885 C ALA A 237 98.075 7.925 71.658 1.00 94.01 C ANISOU 2885 C ALA A 237 17990 11063 6664 -1448 -726 -523 C ATOM 2886 O ALA A 237 97.543 6.941 71.138 1.00 92.41 O ANISOU 2886 O ALA A 237 17771 10746 6593 -1268 -669 -397 O ATOM 2887 CB ALA A 237 100.340 7.306 72.515 1.00 96.43 C ANISOU 2887 CB ALA A 237 18063 11939 6636 -1343 -1231 -572 C ATOM 2888 N LEU A 238 97.944 9.173 71.176 1.00 88.74 N ANISOU 2888 N LEU A 238 17300 10329 6089 -1651 -598 -646 N ATOM 2889 CA LEU A 238 97.140 9.512 69.999 1.00 85.57 C ANISOU 2889 CA LEU A 238 16839 9732 5941 -1633 -398 -631 C ATOM 2890 C LEU A 238 97.976 10.286 68.963 1.00 87.54 C ANISOU 2890 C LEU A 238 16894 10070 6295 -1772 -429 -732 C ATOM 2891 O LEU A 238 97.718 10.160 67.764 1.00 85.26 O ANISOU 2891 O LEU A 238 16474 9707 6214 -1692 -359 -689 O ATOM 2892 CB LEU A 238 95.920 10.344 70.442 1.00 85.48 C ANISOU 2892 CB LEU A 238 17087 9484 5906 -1690 -150 -667 C ATOM 2893 CG LEU A 238 94.709 10.393 69.503 1.00 88.18 C ANISOU 2893 CG LEU A 238 17394 9645 6466 -1568 57 -619 C ATOM 2894 CD1 LEU A 238 93.421 10.402 70.291 1.00 88.72 C ANISOU 2894 CD1 LEU A 238 17660 9576 6475 -1515 256 -605 C ATOM 2895 CD2 LEU A 238 94.765 11.590 68.559 1.00 90.17 C ANISOU 2895 CD2 LEU A 238 17637 9809 6816 -1638 154 -702 C ATOM 2896 N LYS A 239 98.970 11.075 69.432 1.00 84.91 N ANISOU 2896 N LYS A 239 16556 9905 5800 -2005 -524 -877 N ATOM 2897 CA LYS A 239 99.866 11.910 68.625 1.00 84.67 C ANISOU 2897 CA LYS A 239 16379 9975 5815 -2228 -525 -1011 C ATOM 2898 C LYS A 239 100.672 11.103 67.563 1.00 86.44 C ANISOU 2898 C LYS A 239 16244 10407 6194 -2113 -659 -969 C ATOM 2899 O LYS A 239 100.723 11.591 66.434 1.00 85.02 O ANISOU 2899 O LYS A 239 16001 10141 6160 -2190 -544 -1001 O ATOM 2900 CB LYS A 239 100.850 12.681 69.516 1.00 90.20 C ANISOU 2900 CB LYS A 239 17112 10892 6269 -2536 -626 -1196 C ATOM 2901 N PRO A 240 101.303 9.919 67.826 1.00 82.45 N ANISOU 2901 N PRO A 240 15528 10151 5647 -1910 -882 -898 N ATOM 2902 CA PRO A 240 102.055 9.249 66.744 1.00 81.31 C ANISOU 2902 CA PRO A 240 15059 10184 5650 -1787 -973 -874 C ATOM 2903 C PRO A 240 101.151 8.716 65.626 1.00 80.52 C ANISOU 2903 C PRO A 240 14984 9821 5789 -1601 -826 -738 C ATOM 2904 O PRO A 240 101.565 8.710 64.466 1.00 79.23 O ANISOU 2904 O PRO A 240 14630 9702 5771 -1608 -799 -758 O ATOM 2905 CB PRO A 240 102.764 8.092 67.462 1.00 84.94 C ANISOU 2905 CB PRO A 240 15380 10924 5968 -1539 -1230 -811 C ATOM 2906 CG PRO A 240 102.691 8.418 68.918 1.00 91.39 C ANISOU 2906 CG PRO A 240 16406 11791 6528 -1627 -1306 -853 C ATOM 2907 CD PRO A 240 101.403 9.147 69.081 1.00 85.30 C ANISOU 2907 CD PRO A 240 15968 10638 5805 -1757 -1053 -836 C ATOM 2908 N THR A 241 99.917 8.295 65.980 1.00 74.52 N ANISOU 2908 N THR A 241 14452 8809 5053 -1461 -723 -619 N ATOM 2909 CA THR A 241 98.907 7.744 65.074 1.00 71.31 C ANISOU 2909 CA THR A 241 14071 8184 4839 -1308 -588 -510 C ATOM 2910 C THR A 241 98.411 8.812 64.084 1.00 72.31 C ANISOU 2910 C THR A 241 14226 8151 5095 -1429 -411 -566 C ATOM 2911 O THR A 241 98.534 8.607 62.877 1.00 70.82 O ANISOU 2911 O THR A 241 13897 7957 5056 -1377 -388 -546 O ATOM 2912 CB THR A 241 97.736 7.165 65.894 1.00 79.26 C ANISOU 2912 CB THR A 241 15305 9016 5793 -1202 -505 -415 C ATOM 2913 OG1 THR A 241 98.208 6.050 66.650 1.00 81.40 O ANISOU 2913 OG1 THR A 241 15607 9391 5932 -1051 -657 -336 O ATOM 2914 CG2 THR A 241 96.551 6.737 65.030 1.00 74.89 C ANISOU 2914 CG2 THR A 241 14761 8275 5418 -1108 -345 -344 C ATOM 2915 N VAL A 242 97.863 9.938 64.594 1.00 67.95 N ANISOU 2915 N VAL A 242 13892 7461 4465 -1566 -281 -633 N ATOM 2916 CA VAL A 242 97.282 11.027 63.798 1.00 66.46 C ANISOU 2916 CA VAL A 242 13825 7077 4348 -1623 -97 -674 C ATOM 2917 C VAL A 242 98.349 11.592 62.802 1.00 69.08 C ANISOU 2917 C VAL A 242 14043 7486 4719 -1785 -107 -756 C ATOM 2918 O VAL A 242 97.974 11.964 61.690 1.00 67.52 O ANISOU 2918 O VAL A 242 13878 7149 4626 -1740 6 -736 O ATOM 2919 CB VAL A 242 96.662 12.135 64.705 1.00 71.50 C ANISOU 2919 CB VAL A 242 14768 7552 4847 -1720 45 -741 C ATOM 2920 CG1 VAL A 242 97.707 12.864 65.548 1.00 73.67 C ANISOU 2920 CG1 VAL A 242 15128 7933 4930 -1996 -16 -877 C ATOM 2921 CG2 VAL A 242 95.808 13.119 63.906 1.00 70.91 C ANISOU 2921 CG2 VAL A 242 14870 7242 4832 -1658 247 -748 C ATOM 2922 N ILE A 243 99.654 11.577 63.171 1.00 66.21 N ANISOU 2922 N ILE A 243 13526 7370 4261 -1960 -245 -850 N ATOM 2923 CA ILE A 243 100.753 12.046 62.317 1.00 66.47 C ANISOU 2923 CA ILE A 243 13408 7534 4315 -2162 -240 -957 C ATOM 2924 C ILE A 243 100.962 11.043 61.163 1.00 68.08 C ANISOU 2924 C ILE A 243 13355 7819 4694 -1966 -295 -870 C ATOM 2925 O ILE A 243 100.982 11.465 60.006 1.00 67.35 O ANISOU 2925 O ILE A 243 13276 7624 4689 -2017 -177 -882 O ATOM 2926 CB ILE A 243 102.065 12.286 63.130 1.00 72.32 C ANISOU 2926 CB ILE A 243 13996 8598 4885 -2418 -379 -1115 C ATOM 2927 CG1 ILE A 243 101.906 13.508 64.072 1.00 74.59 C ANISOU 2927 CG1 ILE A 243 14594 8762 4983 -2694 -276 -1238 C ATOM 2928 CG2 ILE A 243 103.280 12.479 62.198 1.00 74.12 C ANISOU 2928 CG2 ILE A 243 13959 9053 5150 -2615 -384 -1235 C ATOM 2929 CD1 ILE A 243 103.030 13.714 65.137 1.00 84.95 C ANISOU 2929 CD1 ILE A 243 15777 10420 6079 -2958 -439 -1409 C ATOM 2930 N LEU A 244 101.088 9.734 61.474 1.00 63.20 N ANISOU 2930 N LEU A 244 12559 7352 4104 -1737 -458 -779 N ATOM 2931 CA LEU A 244 101.324 8.663 60.500 1.00 61.47 C ANISOU 2931 CA LEU A 244 12131 7201 4025 -1534 -510 -701 C ATOM 2932 C LEU A 244 100.225 8.600 59.416 1.00 61.51 C ANISOU 2932 C LEU A 244 12249 6941 4182 -1423 -364 -612 C ATOM 2933 O LEU A 244 100.569 8.446 58.245 1.00 60.45 O ANISOU 2933 O LEU A 244 11995 6826 4148 -1405 -330 -614 O ATOM 2934 CB LEU A 244 101.427 7.298 61.215 1.00 61.87 C ANISOU 2934 CB LEU A 244 12108 7367 4034 -1279 -676 -603 C ATOM 2935 CG LEU A 244 101.780 6.057 60.364 1.00 66.05 C ANISOU 2935 CG LEU A 244 12464 7961 4671 -1039 -734 -525 C ATOM 2936 CD1 LEU A 244 103.187 6.150 59.774 1.00 67.82 C ANISOU 2936 CD1 LEU A 244 12379 8488 4902 -1091 -806 -632 C ATOM 2937 CD2 LEU A 244 101.676 4.798 61.188 1.00 69.20 C ANISOU 2937 CD2 LEU A 244 12933 8373 4986 -779 -853 -412 C ATOM 2938 N ILE A 245 98.932 8.718 59.798 1.00 56.10 N ANISOU 2938 N ILE A 245 11771 6046 3497 -1348 -279 -548 N ATOM 2939 CA ILE A 245 97.793 8.652 58.870 1.00 53.80 C ANISOU 2939 CA ILE A 245 11549 5571 3323 -1225 -165 -481 C ATOM 2940 C ILE A 245 97.770 9.924 57.976 1.00 58.34 C ANISOU 2940 C ILE A 245 12240 6024 3903 -1332 -33 -538 C ATOM 2941 O ILE A 245 97.623 9.785 56.758 1.00 57.15 O ANISOU 2941 O ILE A 245 12042 5829 3843 -1260 6 -509 O ATOM 2942 CB ILE A 245 96.441 8.430 59.627 1.00 55.92 C ANISOU 2942 CB ILE A 245 11956 5720 3572 -1122 -107 -426 C ATOM 2943 CG1 ILE A 245 96.220 6.930 59.966 1.00 55.59 C ANISOU 2943 CG1 ILE A 245 11846 5723 3554 -993 -181 -344 C ATOM 2944 CG2 ILE A 245 95.226 8.942 58.842 1.00 55.27 C ANISOU 2944 CG2 ILE A 245 11950 5496 3556 -1032 26 -411 C ATOM 2945 CD1 ILE A 245 96.937 6.359 61.174 1.00 61.45 C ANISOU 2945 CD1 ILE A 245 12608 6571 4169 -991 -303 -329 C ATOM 2946 N LEU A 246 97.934 11.134 58.561 1.00 56.58 N ANISOU 2946 N LEU A 246 12208 5729 3561 -1506 45 -621 N ATOM 2947 CA LEU A 246 97.937 12.387 57.790 1.00 57.33 C ANISOU 2947 CA LEU A 246 12514 5652 3617 -1612 200 -671 C ATOM 2948 C LEU A 246 99.121 12.441 56.814 1.00 62.02 C ANISOU 2948 C LEU A 246 12977 6350 4240 -1775 203 -730 C ATOM 2949 O LEU A 246 98.925 12.817 55.656 1.00 61.24 O ANISOU 2949 O LEU A 246 12979 6118 4173 -1738 306 -707 O ATOM 2950 CB LEU A 246 97.960 13.626 58.703 1.00 59.21 C ANISOU 2950 CB LEU A 246 13039 5764 3692 -1798 305 -762 C ATOM 2951 CG LEU A 246 96.631 14.022 59.354 1.00 63.82 C ANISOU 2951 CG LEU A 246 13852 6167 4231 -1621 393 -718 C ATOM 2952 CD1 LEU A 246 96.850 15.026 60.462 1.00 65.85 C ANISOU 2952 CD1 LEU A 246 14376 6333 4312 -1825 474 -821 C ATOM 2953 CD2 LEU A 246 95.637 14.568 58.326 1.00 66.11 C ANISOU 2953 CD2 LEU A 246 14314 6252 4552 -1399 523 -657 C ATOM 2954 N ALA A 247 100.328 12.028 57.268 1.00 59.76 N ANISOU 2954 N ALA A 247 12452 6325 3928 -1932 89 -809 N ATOM 2955 CA ALA A 247 101.545 12.002 56.451 1.00 60.53 C ANISOU 2955 CA ALA A 247 12351 6598 4048 -2097 94 -893 C ATOM 2956 C ALA A 247 101.448 10.951 55.330 1.00 62.57 C ANISOU 2956 C ALA A 247 12427 6892 4456 -1869 55 -798 C ATOM 2957 O ALA A 247 102.106 11.112 54.302 1.00 62.93 O ANISOU 2957 O ALA A 247 12403 6978 4529 -1971 131 -846 O ATOM 2958 CB ALA A 247 102.760 11.730 57.321 1.00 63.17 C ANISOU 2958 CB ALA A 247 12418 7278 4306 -2258 -47 -1008 C ATOM 2959 N PHE A 248 100.615 9.901 55.515 1.00 57.00 N ANISOU 2959 N PHE A 248 11672 6155 3830 -1591 -39 -676 N ATOM 2960 CA PHE A 248 100.384 8.858 54.514 1.00 55.41 C ANISOU 2960 CA PHE A 248 11349 5953 3750 -1388 -66 -594 C ATOM 2961 C PHE A 248 99.605 9.438 53.328 1.00 58.29 C ANISOU 2961 C PHE A 248 11896 6105 4146 -1352 66 -559 C ATOM 2962 O PHE A 248 100.021 9.250 52.183 1.00 57.63 O ANISOU 2962 O PHE A 248 11748 6038 4109 -1351 107 -564 O ATOM 2963 CB PHE A 248 99.640 7.654 55.127 1.00 56.17 C ANISOU 2963 CB PHE A 248 11411 6043 3887 -1165 -168 -494 C ATOM 2964 CG PHE A 248 99.279 6.556 54.152 1.00 56.76 C ANISOU 2964 CG PHE A 248 11415 6083 4067 -989 -175 -423 C ATOM 2965 CD1 PHE A 248 98.019 6.511 53.564 1.00 58.67 C ANISOU 2965 CD1 PHE A 248 11768 6168 4354 -903 -111 -372 C ATOM 2966 CD2 PHE A 248 100.192 5.558 53.834 1.00 59.59 C ANISOU 2966 CD2 PHE A 248 11595 6584 4461 -900 -246 -422 C ATOM 2967 CE1 PHE A 248 97.687 5.498 52.660 1.00 58.80 C ANISOU 2967 CE1 PHE A 248 11730 6165 4445 -787 -116 -331 C ATOM 2968 CE2 PHE A 248 99.858 4.543 52.932 1.00 61.61 C ANISOU 2968 CE2 PHE A 248 11837 6776 4795 -754 -232 -368 C ATOM 2969 CZ PHE A 248 98.607 4.519 52.353 1.00 58.38 C ANISOU 2969 CZ PHE A 248 11552 6205 4426 -725 -167 -328 C ATOM 2970 N PHE A 249 98.490 10.150 53.604 1.00 54.53 N ANISOU 2970 N PHE A 249 11652 5443 3625 -1297 133 -525 N ATOM 2971 CA PHE A 249 97.655 10.760 52.568 1.00 54.00 C ANISOU 2971 CA PHE A 249 11776 5193 3548 -1194 236 -485 C ATOM 2972 C PHE A 249 98.353 11.975 51.952 1.00 59.39 C ANISOU 2972 C PHE A 249 12670 5761 4135 -1386 380 -549 C ATOM 2973 O PHE A 249 98.020 12.346 50.827 1.00 59.19 O ANISOU 2973 O PHE A 249 12798 5605 4086 -1305 460 -513 O ATOM 2974 CB PHE A 249 96.270 11.150 53.111 1.00 55.60 C ANISOU 2974 CB PHE A 249 12135 5276 3713 -1028 262 -440 C ATOM 2975 CG PHE A 249 95.446 9.980 53.605 1.00 56.17 C ANISOU 2975 CG PHE A 249 12028 5449 3864 -880 166 -391 C ATOM 2976 CD1 PHE A 249 95.105 8.935 52.750 1.00 58.46 C ANISOU 2976 CD1 PHE A 249 12162 5806 4243 -770 111 -351 C ATOM 2977 CD2 PHE A 249 94.952 9.956 54.903 1.00 58.42 C ANISOU 2977 CD2 PHE A 249 12341 5743 4114 -876 157 -394 C ATOM 2978 CE1 PHE A 249 94.342 7.855 53.207 1.00 58.64 C ANISOU 2978 CE1 PHE A 249 12064 5899 4317 -694 59 -324 C ATOM 2979 CE2 PHE A 249 94.173 8.884 55.352 1.00 60.50 C ANISOU 2979 CE2 PHE A 249 12479 6079 4429 -783 108 -358 C ATOM 2980 CZ PHE A 249 93.876 7.840 54.503 1.00 57.73 C ANISOU 2980 CZ PHE A 249 11983 5787 4165 -706 66 -326 C ATOM 2981 N ALA A 250 99.345 12.560 52.661 1.00 57.41 N ANISOU 2981 N ALA A 250 12436 5568 3810 -1659 417 -653 N ATOM 2982 CA ALA A 250 100.147 13.691 52.187 1.00 59.25 C ANISOU 2982 CA ALA A 250 12878 5702 3931 -1940 587 -749 C ATOM 2983 C ALA A 250 101.028 13.279 51.004 1.00 63.62 C ANISOU 2983 C ALA A 250 13263 6370 4538 -2024 620 -777 C ATOM 2984 O ALA A 250 101.295 14.101 50.127 1.00 64.47 O ANISOU 2984 O ALA A 250 13615 6320 4560 -2167 795 -809 O ATOM 2985 CB ALA A 250 101.010 14.230 53.316 1.00 61.77 C ANISOU 2985 CB ALA A 250 13183 6132 4155 -2253 598 -884 C ATOM 2986 N CYS A 251 101.464 12.003 50.982 1.00 59.47 N ANISOU 2986 N CYS A 251 12360 6099 4136 -1923 471 -765 N ATOM 2987 CA CYS A 251 102.297 11.422 49.927 1.00 59.60 C ANISOU 2987 CA CYS A 251 12173 6259 4215 -1954 494 -795 C ATOM 2988 C CYS A 251 101.449 11.095 48.688 1.00 62.52 C ANISOU 2988 C CYS A 251 12671 6458 4627 -1724 523 -684 C ATOM 2989 O CYS A 251 101.934 11.245 47.566 1.00 62.79 O ANISOU 2989 O CYS A 251 12748 6468 4642 -1803 637 -710 O ATOM 2990 CB CYS A 251 103.021 10.178 50.438 1.00 59.59 C ANISOU 2990 CB CYS A 251 11768 6572 4304 -1867 326 -817 C ATOM 2991 SG CYS A 251 104.139 10.481 51.831 1.00 65.57 S ANISOU 2991 SG CYS A 251 12309 7628 4978 -2111 248 -965 S ATOM 2992 N TRP A 252 100.194 10.642 48.895 1.00 57.82 N ANISOU 2992 N TRP A 252 12125 5771 4074 -1458 425 -576 N ATOM 2993 CA TRP A 252 99.283 10.250 47.819 1.00 56.83 C ANISOU 2993 CA TRP A 252 12074 5545 3974 -1237 415 -490 C ATOM 2994 C TRP A 252 98.474 11.429 47.243 1.00 62.03 C ANISOU 2994 C TRP A 252 13099 5964 4506 -1169 523 -448 C ATOM 2995 O TRP A 252 98.085 11.355 46.074 1.00 61.45 O ANISOU 2995 O TRP A 252 13120 5826 4403 -1042 544 -402 O ATOM 2996 CB TRP A 252 98.309 9.165 48.300 1.00 53.95 C ANISOU 2996 CB TRP A 252 11560 5243 3697 -1020 269 -424 C ATOM 2997 CG TRP A 252 98.958 7.825 48.480 1.00 54.45 C ANISOU 2997 CG TRP A 252 11352 5477 3858 -997 177 -433 C ATOM 2998 CD1 TRP A 252 99.260 7.211 49.660 1.00 57.35 C ANISOU 2998 CD1 TRP A 252 11575 5960 4257 -993 84 -439 C ATOM 2999 CD2 TRP A 252 99.459 6.970 47.442 1.00 54.26 C ANISOU 2999 CD2 TRP A 252 11214 5515 3888 -953 182 -438 C ATOM 3000 NE1 TRP A 252 99.880 6.006 49.422 1.00 56.80 N ANISOU 3000 NE1 TRP A 252 11323 6007 4250 -912 28 -436 N ATOM 3001 CE2 TRP A 252 100.023 5.836 48.069 1.00 58.22 C ANISOU 3001 CE2 TRP A 252 11512 6156 4452 -892 94 -442 C ATOM 3002 CE3 TRP A 252 99.470 7.042 46.037 1.00 55.67 C ANISOU 3002 CE3 TRP A 252 11474 5633 4046 -939 258 -437 C ATOM 3003 CZ2 TRP A 252 100.593 4.784 47.341 1.00 57.82 C ANISOU 3003 CZ2 TRP A 252 11342 6175 4453 -805 91 -448 C ATOM 3004 CZ3 TRP A 252 100.039 6.003 45.317 1.00 57.22 C ANISOU 3004 CZ3 TRP A 252 11534 5910 4299 -888 256 -452 C ATOM 3005 CH2 TRP A 252 100.590 4.889 45.966 1.00 57.95 C ANISOU 3005 CH2 TRP A 252 11426 6130 4461 -816 179 -459 C ATOM 3006 N LEU A 253 98.230 12.499 48.037 1.00 59.98 N ANISOU 3006 N LEU A 253 13071 5569 4150 -1229 593 -464 N ATOM 3007 CA LEU A 253 97.449 13.676 47.621 1.00 61.06 C ANISOU 3007 CA LEU A 253 13614 5449 4136 -1105 706 -417 C ATOM 3008 C LEU A 253 97.944 14.264 46.263 1.00 66.63 C ANISOU 3008 C LEU A 253 14583 6004 4729 -1180 856 -414 C ATOM 3009 O LEU A 253 97.082 14.431 45.400 1.00 66.53 O ANISOU 3009 O LEU A 253 14750 5887 4640 -916 846 -330 O ATOM 3010 CB LEU A 253 97.452 14.783 48.699 1.00 62.41 C ANISOU 3010 CB LEU A 253 14044 5469 4200 -1226 807 -462 C ATOM 3011 CG LEU A 253 96.536 15.999 48.464 1.00 68.58 C ANISOU 3011 CG LEU A 253 15294 5958 4807 -1021 929 -404 C ATOM 3012 CD1 LEU A 253 95.058 15.624 48.588 1.00 67.72 C ANISOU 3012 CD1 LEU A 253 15084 5913 4733 -614 799 -319 C ATOM 3013 CD2 LEU A 253 96.856 17.112 49.441 1.00 72.68 C ANISOU 3013 CD2 LEU A 253 16124 6290 5199 -1229 1077 -477 C ATOM 3014 N PRO A 254 99.258 14.546 45.999 1.00 64.52 N ANISOU 3014 N PRO A 254 14334 5747 4432 -1522 993 -507 N ATOM 3015 CA PRO A 254 99.629 15.108 44.683 1.00 65.98 C ANISOU 3015 CA PRO A 254 14818 5764 4488 -1598 1166 -500 C ATOM 3016 C PRO A 254 99.494 14.100 43.529 1.00 68.84 C ANISOU 3016 C PRO A 254 14987 6246 4922 -1423 1077 -447 C ATOM 3017 O PRO A 254 99.412 14.518 42.372 1.00 69.20 O ANISOU 3017 O PRO A 254 15326 6131 4835 -1372 1184 -404 O ATOM 3018 CB PRO A 254 101.097 15.518 44.867 1.00 69.50 C ANISOU 3018 CB PRO A 254 15232 6271 4904 -2061 1337 -651 C ATOM 3019 CG PRO A 254 101.339 15.506 46.341 1.00 73.63 C ANISOU 3019 CG PRO A 254 15551 6937 5488 -2200 1256 -729 C ATOM 3020 CD PRO A 254 100.451 14.432 46.863 1.00 66.54 C ANISOU 3020 CD PRO A 254 14351 6190 4743 -1861 1008 -637 C ATOM 3021 N TYR A 255 99.459 12.789 43.836 1.00 63.94 N ANISOU 3021 N TYR A 255 13928 5881 4484 -1332 894 -449 N ATOM 3022 CA TYR A 255 99.319 11.740 42.828 1.00 62.89 C ANISOU 3022 CA TYR A 255 13623 5854 4417 -1185 814 -415 C ATOM 3023 C TYR A 255 97.845 11.576 42.413 1.00 67.06 C ANISOU 3023 C TYR A 255 14245 6331 4902 -845 687 -316 C ATOM 3024 O TYR A 255 97.581 11.386 41.225 1.00 66.96 O ANISOU 3024 O TYR A 255 14330 6292 4821 -731 686 -280 O ATOM 3025 CB TYR A 255 99.898 10.408 43.336 1.00 62.38 C ANISOU 3025 CB TYR A 255 13119 6048 4536 -1218 697 -463 C ATOM 3026 CG TYR A 255 99.707 9.249 42.383 1.00 62.84 C ANISOU 3026 CG TYR A 255 13035 6186 4654 -1069 627 -437 C ATOM 3027 CD1 TYR A 255 100.423 9.172 41.192 1.00 65.66 C ANISOU 3027 CD1 TYR A 255 13444 6538 4967 -1152 747 -470 C ATOM 3028 CD2 TYR A 255 98.840 8.206 42.690 1.00 62.07 C ANISOU 3028 CD2 TYR A 255 12769 6168 4646 -878 464 -396 C ATOM 3029 CE1 TYR A 255 100.248 8.108 40.309 1.00 65.76 C ANISOU 3029 CE1 TYR A 255 13359 6608 5018 -1023 694 -457 C ATOM 3030 CE2 TYR A 255 98.677 7.122 41.829 1.00 62.47 C ANISOU 3030 CE2 TYR A 255 12727 6275 4734 -782 417 -392 C ATOM 3031 CZ TYR A 255 99.374 7.082 40.633 1.00 70.38 C ANISOU 3031 CZ TYR A 255 13796 7259 5687 -842 526 -420 C ATOM 3032 OH TYR A 255 99.204 6.020 39.776 1.00 70.38 O ANISOU 3032 OH TYR A 255 13738 7298 5707 -753 491 -426 O ATOM 3033 N TYR A 256 96.895 11.663 43.372 1.00 63.74 N ANISOU 3033 N TYR A 256 13784 5926 4508 -692 584 -285 N ATOM 3034 CA TYR A 256 95.464 11.535 43.081 1.00 63.68 C ANISOU 3034 CA TYR A 256 13795 5946 4456 -378 463 -220 C ATOM 3035 C TYR A 256 94.917 12.806 42.395 1.00 69.37 C ANISOU 3035 C TYR A 256 14943 6458 4957 -188 545 -158 C ATOM 3036 O TYR A 256 93.862 12.732 41.762 1.00 69.38 O ANISOU 3036 O TYR A 256 14967 6519 4877 101 440 -110 O ATOM 3037 CB TYR A 256 94.651 11.205 44.343 1.00 64.34 C ANISOU 3037 CB TYR A 256 13678 6139 4631 -289 356 -225 C ATOM 3038 CG TYR A 256 94.726 9.738 44.719 1.00 65.30 C ANISOU 3038 CG TYR A 256 13434 6456 4920 -357 245 -257 C ATOM 3039 CD1 TYR A 256 93.923 8.793 44.083 1.00 66.98 C ANISOU 3039 CD1 TYR A 256 13489 6800 5160 -232 140 -256 C ATOM 3040 CD2 TYR A 256 95.600 9.293 45.705 1.00 65.62 C ANISOU 3040 CD2 TYR A 256 13319 6547 5066 -543 249 -294 C ATOM 3041 CE1 TYR A 256 94.000 7.439 44.411 1.00 66.85 C ANISOU 3041 CE1 TYR A 256 13224 6906 5271 -311 74 -287 C ATOM 3042 CE2 TYR A 256 95.682 7.942 46.045 1.00 65.62 C ANISOU 3042 CE2 TYR A 256 13064 6683 5187 -563 162 -308 C ATOM 3043 CZ TYR A 256 94.880 7.018 45.395 1.00 73.39 C ANISOU 3043 CZ TYR A 256 13951 7740 6195 -456 91 -302 C ATOM 3044 OH TYR A 256 94.953 5.685 45.730 1.00 74.53 O ANISOU 3044 OH TYR A 256 13924 7964 6432 -491 39 -318 O ATOM 3045 N ILE A 257 95.646 13.946 42.481 1.00 67.43 N ANISOU 3045 N ILE A 257 15049 5977 4593 -353 735 -166 N ATOM 3046 CA ILE A 257 95.293 15.200 41.799 1.00 69.75 C ANISOU 3046 CA ILE A 257 15863 5999 4640 -185 859 -98 C ATOM 3047 C ILE A 257 95.541 15.007 40.287 1.00 74.09 C ANISOU 3047 C ILE A 257 16547 6519 5084 -154 888 -65 C ATOM 3048 O ILE A 257 94.697 15.392 39.476 1.00 74.93 O ANISOU 3048 O ILE A 257 16903 6556 5010 173 841 18 O ATOM 3049 CB ILE A 257 96.070 16.428 42.387 1.00 74.76 C ANISOU 3049 CB ILE A 257 16885 6357 5163 -447 1095 -138 C ATOM 3050 CG1 ILE A 257 95.606 16.794 43.831 1.00 74.96 C ANISOU 3050 CG1 ILE A 257 16876 6371 5233 -409 1069 -160 C ATOM 3051 CG2 ILE A 257 96.047 17.663 41.457 1.00 78.43 C ANISOU 3051 CG2 ILE A 257 17989 6470 5340 -359 1292 -72 C ATOM 3052 CD1 ILE A 257 94.093 17.219 44.056 1.00 83.38 C ANISOU 3052 CD1 ILE A 257 18075 7402 6204 67 978 -76 C ATOM 3053 N GLY A 258 96.674 14.382 39.950 1.00 69.94 N ANISOU 3053 N GLY A 258 15837 6073 4662 -466 956 -135 N ATOM 3054 CA GLY A 258 97.088 14.082 38.583 1.00 70.41 C ANISOU 3054 CA GLY A 258 15989 6121 4642 -499 1011 -126 C ATOM 3055 C GLY A 258 96.124 13.192 37.824 1.00 73.40 C ANISOU 3055 C GLY A 258 16187 6678 5023 -201 800 -81 C ATOM 3056 O GLY A 258 95.840 13.460 36.654 1.00 74.40 O ANISOU 3056 O GLY A 258 16593 6720 4957 -44 813 -25 O ATOM 3057 N ILE A 259 95.605 12.134 38.493 1.00 67.82 N ANISOU 3057 N ILE A 259 15038 6219 4511 -139 610 -113 N ATOM 3058 CA ILE A 259 94.632 11.178 37.939 1.00 66.94 C ANISOU 3058 CA ILE A 259 14702 6316 4414 75 409 -108 C ATOM 3059 C ILE A 259 93.306 11.906 37.650 1.00 72.88 C ANISOU 3059 C ILE A 259 15649 7068 4972 450 302 -38 C ATOM 3060 O ILE A 259 92.751 11.738 36.562 1.00 73.72 O ANISOU 3060 O ILE A 259 15826 7253 4933 640 207 -15 O ATOM 3061 CB ILE A 259 94.419 9.961 38.891 1.00 67.75 C ANISOU 3061 CB ILE A 259 14351 6640 4752 -1 282 -169 C ATOM 3062 CG1 ILE A 259 95.735 9.174 39.100 1.00 66.93 C ANISOU 3062 CG1 ILE A 259 14060 6559 4811 -285 369 -231 C ATOM 3063 CG2 ILE A 259 93.291 9.035 38.386 1.00 68.37 C ANISOU 3063 CG2 ILE A 259 14219 6935 4822 169 97 -191 C ATOM 3064 CD1 ILE A 259 95.683 8.090 40.187 1.00 72.14 C ANISOU 3064 CD1 ILE A 259 14370 7370 5668 -347 275 -273 C ATOM 3065 N SER A 260 92.823 12.721 38.620 1.00 69.91 N ANISOU 3065 N SER A 260 15364 6621 4577 574 316 -10 N ATOM 3066 CA SER A 260 91.579 13.496 38.548 1.00 71.59 C ANISOU 3066 CA SER A 260 15747 6848 4607 984 227 52 C ATOM 3067 C SER A 260 91.530 14.386 37.295 1.00 78.10 C ANISOU 3067 C SER A 260 17063 7478 5133 1210 284 141 C ATOM 3068 O SER A 260 90.534 14.338 36.572 1.00 79.08 O ANISOU 3068 O SER A 260 17174 7771 5100 1560 117 171 O ATOM 3069 CB SER A 260 91.413 14.355 39.796 1.00 75.20 C ANISOU 3069 CB SER A 260 16322 7171 5080 1027 311 64 C ATOM 3070 OG SER A 260 91.376 13.551 40.964 1.00 81.23 O ANISOU 3070 OG SER A 260 16665 8114 6084 849 252 -9 O ATOM 3071 N ILE A 261 92.609 15.158 37.023 1.00 75.71 N ANISOU 3071 N ILE A 261 17189 6843 4734 996 523 171 N ATOM 3072 CA ILE A 261 92.711 16.048 35.855 1.00 78.63 C ANISOU 3072 CA ILE A 261 18127 6956 4793 1157 634 262 C ATOM 3073 C ILE A 261 92.787 15.189 34.577 1.00 82.79 C ANISOU 3073 C ILE A 261 18537 7646 5275 1149 536 251 C ATOM 3074 O ILE A 261 92.099 15.492 33.600 1.00 84.68 O ANISOU 3074 O ILE A 261 19026 7893 5256 1495 440 324 O ATOM 3075 CB ILE A 261 93.918 17.037 35.964 1.00 83.01 C ANISOU 3075 CB ILE A 261 19167 7112 5260 824 962 265 C ATOM 3076 CG1 ILE A 261 93.885 17.837 37.294 1.00 83.52 C ANISOU 3076 CG1 ILE A 261 19349 7017 5367 778 1065 251 C ATOM 3077 CG2 ILE A 261 93.962 17.991 34.752 1.00 87.45 C ANISOU 3077 CG2 ILE A 261 20408 7360 5460 997 1109 370 C ATOM 3078 CD1 ILE A 261 95.192 18.611 37.661 1.00 90.79 C ANISOU 3078 CD1 ILE A 261 20610 7625 6261 303 1386 192 C ATOM 3079 N ASP A 262 93.590 14.103 34.611 1.00 77.23 N ANISOU 3079 N ASP A 262 17457 7082 4805 786 552 156 N ATOM 3080 CA ASP A 262 93.784 13.166 33.499 1.00 76.88 C ANISOU 3080 CA ASP A 262 17284 7181 4748 723 488 122 C ATOM 3081 C ASP A 262 92.474 12.459 33.116 1.00 81.32 C ANISOU 3081 C ASP A 262 17568 8064 5266 1035 195 110 C ATOM 3082 O ASP A 262 92.285 12.125 31.943 1.00 82.11 O ANISOU 3082 O ASP A 262 17754 8240 5205 1127 120 114 O ATOM 3083 CB ASP A 262 94.851 12.122 33.865 1.00 76.19 C ANISOU 3083 CB ASP A 262 16822 7186 4939 323 565 15 C ATOM 3084 CG ASP A 262 95.191 11.142 32.761 1.00 86.11 C ANISOU 3084 CG ASP A 262 17980 8551 6188 233 547 -32 C ATOM 3085 OD1 ASP A 262 95.477 11.595 31.627 1.00 88.64 O ANISOU 3085 OD1 ASP A 262 18675 8723 6282 256 655 9 O ATOM 3086 OD2 ASP A 262 95.222 9.925 33.040 1.00 89.89 O ANISOU 3086 OD2 ASP A 262 18049 9234 6872 129 451 -111 O ATOM 3087 N SER A 263 91.580 12.237 34.102 1.00 77.32 N ANISOU 3087 N SER A 263 16726 7763 4888 1169 39 81 N ATOM 3088 CA SER A 263 90.280 11.591 33.916 1.00 77.81 C ANISOU 3088 CA SER A 263 16457 8189 4920 1415 -225 34 C ATOM 3089 C SER A 263 89.362 12.434 33.033 1.00 85.45 C ANISOU 3089 C SER A 263 17720 9198 5548 1876 -348 114 C ATOM 3090 O SER A 263 88.658 11.874 32.194 1.00 86.28 O ANISOU 3090 O SER A 263 17669 9584 5530 2023 -544 70 O ATOM 3091 CB SER A 263 89.608 11.337 35.261 1.00 80.08 C ANISOU 3091 CB SER A 263 16366 8658 5405 1429 -304 -19 C ATOM 3092 OG SER A 263 90.397 10.484 36.072 1.00 86.50 O ANISOU 3092 OG SER A 263 16919 9449 6499 1048 -218 -86 O ATOM 3093 N PHE A 264 89.394 13.775 33.197 1.00 84.09 N ANISOU 3093 N PHE A 264 18009 8743 5199 2108 -228 228 N ATOM 3094 CA PHE A 264 88.569 14.705 32.425 1.00 87.90 C ANISOU 3094 CA PHE A 264 18865 9213 5321 2623 -327 330 C ATOM 3095 C PHE A 264 89.004 14.768 30.949 1.00 94.00 C ANISOU 3095 C PHE A 264 20025 9858 5833 2642 -298 385 C ATOM 3096 O PHE A 264 88.176 15.080 30.089 1.00 96.66 O ANISOU 3096 O PHE A 264 20526 10336 5864 3074 -476 440 O ATOM 3097 CB PHE A 264 88.596 16.115 33.035 1.00 91.50 C ANISOU 3097 CB PHE A 264 19806 9317 5645 2846 -156 440 C ATOM 3098 CG PHE A 264 88.126 16.213 34.468 1.00 91.83 C ANISOU 3098 CG PHE A 264 19546 9453 5891 2875 -166 394 C ATOM 3099 CD1 PHE A 264 86.859 15.771 34.835 1.00 95.35 C ANISOU 3099 CD1 PHE A 264 19508 10340 6381 3164 -412 327 C ATOM 3100 CD2 PHE A 264 88.912 16.831 35.432 1.00 93.05 C ANISOU 3100 CD2 PHE A 264 19930 9264 6159 2620 80 408 C ATOM 3101 CE1 PHE A 264 86.420 15.873 36.158 1.00 95.42 C ANISOU 3101 CE1 PHE A 264 19260 10432 6565 3185 -396 280 C ATOM 3102 CE2 PHE A 264 88.469 16.941 36.754 1.00 95.00 C ANISOU 3102 CE2 PHE A 264 19936 9590 6571 2652 75 365 C ATOM 3103 CZ PHE A 264 87.226 16.464 37.107 1.00 93.33 C ANISOU 3103 CZ PHE A 264 19251 9798 6411 2943 -155 308 C ATOM 3104 N ILE A 265 90.289 14.467 30.664 1.00 89.17 N ANISOU 3104 N ILE A 265 19545 9009 5326 2193 -77 365 N ATOM 3105 CA ILE A 265 90.851 14.429 29.307 1.00 90.50 C ANISOU 3105 CA ILE A 265 20067 9045 5275 2127 1 399 C ATOM 3106 C ILE A 265 90.250 13.214 28.576 1.00 94.51 C ANISOU 3106 C ILE A 265 20162 9961 5787 2156 -260 302 C ATOM 3107 O ILE A 265 89.891 13.318 27.400 1.00 96.78 O ANISOU 3107 O ILE A 265 20699 10304 5768 2390 -366 343 O ATOM 3108 CB ILE A 265 92.412 14.404 29.344 1.00 91.92 C ANISOU 3108 CB ILE A 265 20412 8914 5598 1609 333 370 C ATOM 3109 CG1 ILE A 265 92.964 15.672 30.048 1.00 93.16 C ANISOU 3109 CG1 ILE A 265 21007 8679 5711 1535 599 439 C ATOM 3110 CG2 ILE A 265 93.012 14.247 27.931 1.00 94.18 C ANISOU 3110 CG2 ILE A 265 21021 9090 5672 1505 437 384 C ATOM 3111 CD1 ILE A 265 94.458 15.677 30.361 1.00 98.67 C ANISOU 3111 CD1 ILE A 265 21746 9163 6583 986 916 369 C ATOM 3112 N LEU A 266 90.101 12.087 29.297 1.00 88.46 N ANISOU 3112 N LEU A 266 18800 9471 5341 1920 -360 171 N ATOM 3113 CA LEU A 266 89.537 10.842 28.774 1.00 88.13 C ANISOU 3113 CA LEU A 266 18352 9803 5330 1862 -576 47 C ATOM 3114 C LEU A 266 87.997 10.902 28.726 1.00 94.91 C ANISOU 3114 C LEU A 266 18966 11069 6026 2271 -889 16 C ATOM 3115 O LEU A 266 87.400 10.279 27.846 1.00 96.12 O ANISOU 3115 O LEU A 266 18974 11523 6023 2340 -1089 -63 O ATOM 3116 CB LEU A 266 89.998 9.641 29.621 1.00 84.64 C ANISOU 3116 CB LEU A 266 17445 9449 5267 1448 -522 -78 C ATOM 3117 CG LEU A 266 91.516 9.396 29.723 1.00 87.26 C ANISOU 3117 CG LEU A 266 17892 9484 5780 1061 -244 -80 C ATOM 3118 CD1 LEU A 266 91.836 8.414 30.828 1.00 84.56 C ANISOU 3118 CD1 LEU A 266 17118 9224 5786 777 -216 -173 C ATOM 3119 CD2 LEU A 266 92.110 8.924 28.399 1.00 90.44 C ANISOU 3119 CD2 LEU A 266 18491 9830 6041 938 -174 -106 C ATOM 3120 N LEU A 267 87.362 11.667 29.648 1.00 92.38 N ANISOU 3120 N LEU A 267 18597 10779 5724 2543 -926 65 N ATOM 3121 CA LEU A 267 85.901 11.828 29.714 1.00 94.99 C ANISOU 3121 CA LEU A 267 18654 11535 5903 2973 -1205 26 C ATOM 3122 C LEU A 267 85.402 12.945 28.761 1.00103.60 C ANISOU 3122 C LEU A 267 20218 12589 6558 3533 -1309 160 C ATOM 3123 O LEU A 267 84.204 13.244 28.746 1.00106.29 O ANISOU 3123 O LEU A 267 20369 13296 6720 3988 -1547 142 O ATOM 3124 CB LEU A 267 85.440 12.120 31.157 1.00 94.00 C ANISOU 3124 CB LEU A 267 18259 11468 5987 3036 -1179 9 C ATOM 3125 CG LEU A 267 85.465 10.943 32.145 1.00 95.59 C ANISOU 3125 CG LEU A 267 17914 11850 6556 2602 -1162 -140 C ATOM 3126 CD1 LEU A 267 85.417 11.433 33.576 1.00 94.46 C ANISOU 3126 CD1 LEU A 267 17692 11593 6604 2611 -1046 -115 C ATOM 3127 CD2 LEU A 267 84.337 9.948 31.875 1.00 99.54 C ANISOU 3127 CD2 LEU A 267 17884 12903 7034 2599 -1415 -315 C ATOM 3128 N GLU A 268 86.325 13.534 27.959 1.00100.94 N ANISOU 3128 N GLU A 268 20496 11823 6032 3505 -1122 288 N ATOM 3129 CA GLU A 268 86.120 14.567 26.926 1.00104.94 C ANISOU 3129 CA GLU A 268 21615 12169 6089 3977 -1156 441 C ATOM 3130 C GLU A 268 85.517 15.885 27.495 1.00111.02 C ANISOU 3130 C GLU A 268 22700 12801 6681 4512 -1146 574 C ATOM 3131 O GLU A 268 84.934 16.662 26.732 1.00114.87 O ANISOU 3131 O GLU A 268 23589 13297 6761 5064 -1269 688 O ATOM 3132 CB GLU A 268 85.223 14.043 25.782 1.00109.37 C ANISOU 3132 CB GLU A 268 21993 13196 6365 4249 -1490 375 C ATOM 3133 CG GLU A 268 85.819 12.876 25.011 1.00119.02 C ANISOU 3133 CG GLU A 268 23064 14488 7668 3779 -1478 260 C ATOM 3134 CD GLU A 268 84.924 12.305 23.930 1.00144.29 C ANISOU 3134 CD GLU A 268 26064 18175 10585 3988 -1812 164 C ATOM 3135 OE1 GLU A 268 84.443 11.163 24.103 1.00139.31 O ANISOU 3135 OE1 GLU A 268 24831 17966 10136 3729 -1973 -33 O ATOM 3136 OE2 GLU A 268 84.690 13.004 22.917 1.00142.18 O ANISOU 3136 OE2 GLU A 268 26264 17868 9891 4403 -1909 279 O ATOM 3137 N ILE A 269 85.709 16.164 28.801 1.00105.06 N ANISOU 3137 N ILE A 269 21828 11888 6202 4368 -985 566 N ATOM 3138 CA ILE A 269 85.232 17.410 29.423 1.00107.32 C ANISOU 3138 CA ILE A 269 22458 11983 6336 4836 -926 682 C ATOM 3139 C ILE A 269 86.339 18.468 29.187 1.00111.58 C ANISOU 3139 C ILE A 269 23846 11838 6710 4723 -570 837 C ATOM 3140 O ILE A 269 86.025 19.586 28.770 1.00115.23 O ANISOU 3140 O ILE A 269 24935 12050 6797 5222 -532 988 O ATOM 3141 CB ILE A 269 84.792 17.258 30.928 1.00108.33 C ANISOU 3141 CB ILE A 269 22085 12285 6791 4768 -926 589 C ATOM 3142 CG1 ILE A 269 85.166 18.453 31.852 1.00109.21 C ANISOU 3142 CG1 ILE A 269 22688 11910 6897 4851 -650 695 C ATOM 3143 CG2 ILE A 269 85.154 15.911 31.545 1.00104.55 C ANISOU 3143 CG2 ILE A 269 20952 12035 6738 4165 -933 419 C ATOM 3144 CD1 ILE A 269 84.240 19.692 31.762 1.00121.19 C ANISOU 3144 CD1 ILE A 269 24641 13363 8044 5615 -707 824 C ATOM 3145 N ILE A 270 87.618 18.101 29.418 1.00104.17 N ANISOU 3145 N ILE A 270 22936 10618 6027 4075 -306 790 N ATOM 3146 CA ILE A 270 88.773 18.968 29.167 1.00104.40 C ANISOU 3146 CA ILE A 270 23693 10053 5922 3829 60 887 C ATOM 3147 C ILE A 270 89.427 18.463 27.877 1.00107.55 C ANISOU 3147 C ILE A 270 24254 10415 6194 3595 99 885 C ATOM 3148 O ILE A 270 89.947 17.345 27.845 1.00103.72 O ANISOU 3148 O ILE A 270 23288 10134 5989 3153 81 758 O ATOM 3149 CB ILE A 270 89.756 19.041 30.376 1.00104.23 C ANISOU 3149 CB ILE A 270 23583 9781 6240 3286 340 818 C ATOM 3150 CG1 ILE A 270 89.058 19.675 31.610 1.00105.02 C ANISOU 3150 CG1 ILE A 270 23628 9872 6403 3563 320 831 C ATOM 3151 CG2 ILE A 270 91.038 19.815 29.998 1.00106.05 C ANISOU 3151 CG2 ILE A 270 24502 9464 6329 2920 734 872 C ATOM 3152 CD1 ILE A 270 89.850 19.667 32.947 1.00108.96 C ANISOU 3152 CD1 ILE A 270 23949 10215 7236 3063 533 743 C ATOM 3153 N LYS A 271 89.353 19.268 26.807 1.00107.71 N ANISOU 3153 N LYS A 271 24975 10178 5772 3927 152 1027 N ATOM 3154 CA LYS A 271 89.900 18.899 25.504 1.00108.10 C ANISOU 3154 CA LYS A 271 25267 10173 5634 3759 199 1037 C ATOM 3155 C LYS A 271 90.940 19.941 25.069 1.00113.51 C ANISOU 3155 C LYS A 271 26828 10231 6071 3556 620 1147 C ATOM 3156 O LYS A 271 90.590 20.984 24.504 1.00117.50 O ANISOU 3156 O LYS A 271 28069 10437 6138 3999 672 1310 O ATOM 3157 CB LYS A 271 88.762 18.760 24.474 1.00113.89 C ANISOU 3157 CB LYS A 271 26009 11252 6012 4348 -165 1090 C ATOM 3158 CG LYS A 271 89.110 17.903 23.266 1.00127.44 C ANISOU 3158 CG LYS A 271 27669 13119 7635 4130 -227 1034 C ATOM 3159 CD LYS A 271 87.913 17.773 22.326 1.00141.36 C ANISOU 3159 CD LYS A 271 29394 15287 9029 4718 -626 1065 C ATOM 3160 CE LYS A 271 88.131 16.790 21.198 1.00152.36 C ANISOU 3160 CE LYS A 271 30645 16900 10344 4489 -730 975 C ATOM 3161 NZ LYS A 271 88.191 15.381 21.679 1.00158.15 N ANISOU 3161 NZ LYS A 271 30543 18024 11524 4029 -837 761 N ATOM 3162 N GLN A 272 92.222 19.664 25.376 1.00106.65 N ANISOU 3162 N GLN A 272 25879 9172 5471 2883 931 1048 N ATOM 3163 CA GLN A 272 93.349 20.534 25.029 1.00108.09 C ANISOU 3163 CA GLN A 272 26794 8809 5466 2532 1378 1097 C ATOM 3164 C GLN A 272 94.414 19.742 24.243 1.00109.30 C ANISOU 3164 C GLN A 272 26815 9003 5711 2009 1545 995 C ATOM 3165 O GLN A 272 94.244 18.545 23.993 1.00106.39 O ANISOU 3165 O GLN A 272 25831 9049 5542 1956 1309 898 O ATOM 3166 CB GLN A 272 93.960 21.200 26.276 1.00108.46 C ANISOU 3166 CB GLN A 272 26923 8572 5713 2193 1658 1052 C ATOM 3167 CG GLN A 272 93.066 22.278 26.887 1.00126.21 C ANISOU 3167 CG GLN A 272 29578 10614 7761 2709 1613 1176 C ATOM 3168 CD GLN A 272 93.814 23.181 27.835 1.00145.85 C ANISOU 3168 CD GLN A 272 32431 12677 10308 2332 1983 1145 C ATOM 3169 OE1 GLN A 272 94.663 23.984 27.430 1.00143.62 O ANISOU 3169 OE1 GLN A 272 32861 11918 9792 2022 2374 1173 O ATOM 3170 NE2 GLN A 272 93.467 23.119 29.112 1.00136.16 N ANISOU 3170 NE2 GLN A 272 30769 11604 9361 2351 1880 1082 N ATOM 3171 N GLY A 273 95.482 20.436 23.846 1.00106.75 N ANISOU 3171 N GLY A 273 27099 8241 5220 1627 1972 1008 N ATOM 3172 CA GLY A 273 96.570 19.899 23.036 1.00105.60 C ANISOU 3172 CA GLY A 273 26949 8077 5099 1138 2209 914 C ATOM 3173 C GLY A 273 97.444 18.809 23.623 1.00103.07 C ANISOU 3173 C GLY A 273 25838 8063 5263 605 2254 712 C ATOM 3174 O GLY A 273 97.168 18.265 24.697 1.00 99.20 O ANISOU 3174 O GLY A 273 24708 7852 5131 601 2052 637 O ATOM 3175 N CYS A 274 98.520 18.496 22.883 1.00 98.61 N ANISOU 3175 N CYS A 274 25348 7439 4682 172 2536 625 N ATOM 3176 CA CYS A 274 99.536 17.486 23.170 1.00 94.73 C ANISOU 3176 CA CYS A 274 24206 7212 4575 -319 2640 433 C ATOM 3177 C CYS A 274 100.359 17.868 24.408 1.00 97.15 C ANISOU 3177 C CYS A 274 24297 7463 5153 -745 2863 324 C ATOM 3178 O CYS A 274 100.709 16.984 25.193 1.00 93.15 O ANISOU 3178 O CYS A 274 23074 7281 5038 -933 2759 193 O ATOM 3179 CB CYS A 274 100.435 17.305 21.948 1.00 96.75 C ANISOU 3179 CB CYS A 274 24742 7369 4650 -617 2935 382 C ATOM 3180 SG CYS A 274 101.785 16.116 22.173 1.00 97.65 S ANISOU 3180 SG CYS A 274 24105 7809 5188 -1171 3112 140 S ATOM 3181 N GLU A 275 100.680 19.170 24.565 1.00 96.92 N ANISOU 3181 N GLU A 275 24917 7019 4891 -902 3175 371 N ATOM 3182 CA GLU A 275 101.492 19.696 25.664 1.00 96.63 C ANISOU 3182 CA GLU A 275 24779 6897 5037 -1358 3423 251 C ATOM 3183 C GLU A 275 100.806 19.459 27.022 1.00 96.37 C ANISOU 3183 C GLU A 275 24236 7079 5301 -1141 3108 249 C ATOM 3184 O GLU A 275 101.452 18.927 27.923 1.00 93.13 O ANISOU 3184 O GLU A 275 23224 6926 5236 -1468 3110 98 O ATOM 3185 CB GLU A 275 101.783 21.195 25.457 1.00102.92 C ANISOU 3185 CB GLU A 275 26508 7146 5450 -1531 3820 314 C ATOM 3186 CG GLU A 275 102.843 21.772 26.388 1.00117.16 C ANISOU 3186 CG GLU A 275 28273 8856 7388 -2152 4162 143 C ATOM 3187 CD GLU A 275 104.243 21.199 26.248 1.00144.42 C ANISOU 3187 CD GLU A 275 31265 12566 11041 -2783 4426 -85 C ATOM 3188 OE1 GLU A 275 104.763 20.661 27.252 1.00140.85 O ANISOU 3188 OE1 GLU A 275 30099 12464 10954 -3040 4349 -246 O ATOM 3189 OE2 GLU A 275 104.807 21.261 25.131 1.00143.00 O ANISOU 3189 OE2 GLU A 275 31426 12264 10645 -2990 4701 -104 O ATOM 3190 N PHE A 276 99.506 19.820 27.151 1.00 93.01 N ANISOU 3190 N PHE A 276 24032 6578 4729 -572 2837 410 N ATOM 3191 CA PHE A 276 98.710 19.647 28.376 1.00 90.12 C ANISOU 3191 CA PHE A 276 23233 6406 4601 -317 2546 417 C ATOM 3192 C PHE A 276 98.534 18.160 28.706 1.00 88.92 C ANISOU 3192 C PHE A 276 22198 6760 4827 -292 2230 326 C ATOM 3193 O PHE A 276 98.506 17.790 29.881 1.00 85.73 O ANISOU 3193 O PHE A 276 21294 6554 4724 -373 2112 252 O ATOM 3194 CB PHE A 276 97.335 20.328 28.228 1.00 94.09 C ANISOU 3194 CB PHE A 276 24171 6759 4818 334 2338 602 C ATOM 3195 CG PHE A 276 96.480 20.342 29.476 1.00 93.97 C ANISOU 3195 CG PHE A 276 23805 6902 4997 608 2096 610 C ATOM 3196 CD1 PHE A 276 96.627 21.344 30.429 1.00 98.50 C ANISOU 3196 CD1 PHE A 276 24703 7183 5541 502 2290 609 C ATOM 3197 CD2 PHE A 276 95.500 19.377 29.679 1.00 93.71 C ANISOU 3197 CD2 PHE A 276 23154 7301 5150 958 1695 608 C ATOM 3198 CE1 PHE A 276 95.831 21.361 31.578 1.00 97.97 C ANISOU 3198 CE1 PHE A 276 24327 7258 5639 760 2084 612 C ATOM 3199 CE2 PHE A 276 94.705 19.394 30.830 1.00 95.14 C ANISOU 3199 CE2 PHE A 276 23016 7636 5498 1190 1502 606 C ATOM 3200 CZ PHE A 276 94.875 20.386 31.771 1.00 94.38 C ANISOU 3200 CZ PHE A 276 23235 7247 5377 1107 1696 613 C ATOM 3201 N GLU A 277 98.419 17.322 27.659 1.00 84.53 N ANISOU 3201 N GLU A 277 21506 6383 4227 -185 2111 329 N ATOM 3202 CA GLU A 277 98.262 15.869 27.729 1.00 80.60 C ANISOU 3202 CA GLU A 277 20293 6307 4023 -168 1850 242 C ATOM 3203 C GLU A 277 99.545 15.220 28.279 1.00 81.28 C ANISOU 3203 C GLU A 277 19912 6542 4430 -667 2027 76 C ATOM 3204 O GLU A 277 99.464 14.217 28.988 1.00 78.03 O ANISOU 3204 O GLU A 277 18892 6429 4325 -676 1833 2 O ATOM 3205 CB GLU A 277 97.921 15.335 26.327 1.00 83.18 C ANISOU 3205 CB GLU A 277 20757 6709 4138 29 1749 281 C ATOM 3206 CG GLU A 277 97.453 13.891 26.278 1.00 91.19 C ANISOU 3206 CG GLU A 277 21150 8122 5374 126 1450 206 C ATOM 3207 CD GLU A 277 96.846 13.468 24.954 1.00115.14 C ANISOU 3207 CD GLU A 277 24354 11246 8149 379 1293 245 C ATOM 3208 OE1 GLU A 277 97.312 12.455 24.384 1.00111.61 O ANISOU 3208 OE1 GLU A 277 23665 10948 7793 197 1312 148 O ATOM 3209 OE2 GLU A 277 95.910 14.152 24.481 1.00110.78 O ANISOU 3209 OE2 GLU A 277 24188 10622 7283 777 1149 368 O ATOM 3210 N ASN A 278 100.717 15.807 27.966 1.00 78.89 N ANISOU 3210 N ASN A 278 19901 6038 4034 -1075 2400 12 N ATOM 3211 CA ASN A 278 102.023 15.334 28.427 1.00 77.31 C ANISOU 3211 CA ASN A 278 19268 6014 4092 -1545 2595 -163 C ATOM 3212 C ASN A 278 102.411 15.970 29.770 1.00 79.67 C ANISOU 3212 C ASN A 278 19458 6282 4531 -1787 2680 -228 C ATOM 3213 O ASN A 278 103.228 15.392 30.489 1.00 77.89 O ANISOU 3213 O ASN A 278 18702 6318 4574 -2059 2703 -370 O ATOM 3214 CB ASN A 278 103.103 15.620 27.382 1.00 81.32 C ANISOU 3214 CB ASN A 278 20092 6388 4420 -1899 2971 -234 C ATOM 3215 CG ASN A 278 103.089 14.681 26.198 1.00105.26 C ANISOU 3215 CG ASN A 278 23044 9548 7402 -1777 2917 -236 C ATOM 3216 OD1 ASN A 278 103.046 13.452 26.336 1.00 97.25 O ANISOU 3216 OD1 ASN A 278 21475 8843 6634 -1685 2715 -297 O ATOM 3217 ND2 ASN A 278 103.221 15.236 25.004 1.00 99.96 N ANISOU 3217 ND2 ASN A 278 22963 8622 6394 -1812 3137 -182 N ATOM 3218 N THR A 279 101.830 17.145 30.111 1.00 76.82 N ANISOU 3218 N THR A 279 19610 5610 3969 -1666 2725 -129 N ATOM 3219 CA THR A 279 102.103 17.853 31.370 1.00 76.16 C ANISOU 3219 CA THR A 279 19516 5451 3971 -1891 2815 -190 C ATOM 3220 C THR A 279 101.511 17.046 32.541 1.00 74.75 C ANISOU 3220 C THR A 279 18715 5583 4105 -1678 2470 -200 C ATOM 3221 O THR A 279 102.208 16.847 33.537 1.00 73.04 O ANISOU 3221 O THR A 279 18102 5546 4105 -1973 2498 -327 O ATOM 3222 CB THR A 279 101.565 19.297 31.322 1.00 87.21 C ANISOU 3222 CB THR A 279 21714 6386 5035 -1764 2970 -71 C ATOM 3223 OG1 THR A 279 102.147 19.972 30.206 1.00 90.81 O ANISOU 3223 OG1 THR A 279 22787 6536 5182 -1982 3313 -61 O ATOM 3224 CG2 THR A 279 101.875 20.089 32.590 1.00 86.14 C ANISOU 3224 CG2 THR A 279 21643 6134 4954 -2036 3100 -151 C ATOM 3225 N VAL A 280 100.254 16.553 32.402 1.00 68.83 N ANISOU 3225 N VAL A 280 17868 4923 3362 -1187 2151 -79 N ATOM 3226 CA VAL A 280 99.574 15.746 33.430 1.00 65.02 C ANISOU 3226 CA VAL A 280 16836 4722 3147 -984 1841 -85 C ATOM 3227 C VAL A 280 100.325 14.418 33.622 1.00 66.07 C ANISOU 3227 C VAL A 280 16339 5194 3571 -1190 1775 -207 C ATOM 3228 O VAL A 280 100.368 13.914 34.742 1.00 63.32 O ANISOU 3228 O VAL A 280 15563 5039 3456 -1232 1648 -260 O ATOM 3229 CB VAL A 280 98.059 15.492 33.172 1.00 68.11 C ANISOU 3229 CB VAL A 280 17233 5183 3462 -457 1537 38 C ATOM 3230 CG1 VAL A 280 97.254 16.782 33.272 1.00 70.20 C ANISOU 3230 CG1 VAL A 280 18052 5156 3464 -166 1568 157 C ATOM 3231 CG2 VAL A 280 97.803 14.785 31.841 1.00 68.31 C ANISOU 3231 CG2 VAL A 280 17261 5309 3384 -297 1443 68 C ATOM 3232 N HIS A 281 100.936 13.879 32.543 1.00 63.41 N ANISOU 3232 N HIS A 281 15983 4912 3197 -1300 1877 -247 N ATOM 3233 CA HIS A 281 101.710 12.641 32.589 1.00 61.58 C ANISOU 3233 CA HIS A 281 15221 4973 3205 -1450 1851 -361 C ATOM 3234 C HIS A 281 102.993 12.855 33.393 1.00 66.00 C ANISOU 3234 C HIS A 281 15544 5634 3897 -1849 2043 -502 C ATOM 3235 O HIS A 281 103.289 12.046 34.271 1.00 63.63 O ANISOU 3235 O HIS A 281 14749 5591 3837 -1868 1912 -569 O ATOM 3236 CB HIS A 281 102.033 12.124 31.180 1.00 63.23 C ANISOU 3236 CB HIS A 281 15532 5189 3304 -1456 1946 -375 C ATOM 3237 CG HIS A 281 102.814 10.848 31.190 1.00 65.33 C ANISOU 3237 CG HIS A 281 15295 5732 3796 -1558 1938 -490 C ATOM 3238 ND1 HIS A 281 102.184 9.621 31.179 1.00 65.02 N ANISOU 3238 ND1 HIS A 281 14959 5859 3887 -1315 1692 -475 N ATOM 3239 CD2 HIS A 281 104.152 10.652 31.251 1.00 68.07 C ANISOU 3239 CD2 HIS A 281 15402 6220 4242 -1862 2153 -628 C ATOM 3240 CE1 HIS A 281 103.151 8.721 31.205 1.00 64.25 C ANISOU 3240 CE1 HIS A 281 14509 5950 3952 -1442 1771 -585 C ATOM 3241 NE2 HIS A 281 104.352 9.294 31.261 1.00 66.39 N ANISOU 3241 NE2 HIS A 281 14765 6243 4217 -1749 2034 -681 N ATOM 3242 N LYS A 282 103.741 13.946 33.104 1.00 65.47 N ANISOU 3242 N LYS A 282 15846 5376 3655 -2174 2353 -553 N ATOM 3243 CA LYS A 282 104.980 14.289 33.808 1.00 66.63 C ANISOU 3243 CA LYS A 282 15780 5651 3883 -2616 2559 -721 C ATOM 3244 C LYS A 282 104.701 14.470 35.303 1.00 69.89 C ANISOU 3244 C LYS A 282 15981 6139 4434 -2602 2394 -732 C ATOM 3245 O LYS A 282 105.515 14.052 36.125 1.00 69.14 O ANISOU 3245 O LYS A 282 15419 6335 4517 -2802 2374 -863 O ATOM 3246 CB LYS A 282 105.634 15.547 33.213 1.00 72.55 C ANISOU 3246 CB LYS A 282 17068 6127 4371 -2995 2944 -775 C ATOM 3247 CG LYS A 282 106.315 15.300 31.864 1.00 86.25 C ANISOU 3247 CG LYS A 282 18909 7868 5994 -3143 3176 -825 C ATOM 3248 CD LYS A 282 107.043 16.534 31.306 1.00 99.74 C ANISOU 3248 CD LYS A 282 21169 9301 7426 -3590 3608 -899 C ATOM 3249 CE LYS A 282 106.149 17.603 30.708 1.00111.22 C ANISOU 3249 CE LYS A 282 23458 10255 8548 -3409 3691 -720 C ATOM 3250 NZ LYS A 282 105.491 17.151 29.452 1.00119.12 N ANISOU 3250 NZ LYS A 282 24699 11157 9406 -3038 3594 -577 N ATOM 3251 N TRP A 283 103.515 15.026 35.643 1.00 66.36 N ANISOU 3251 N TRP A 283 15857 5459 3897 -2322 2258 -593 N ATOM 3252 CA TRP A 283 103.044 15.229 37.013 1.00 65.09 C ANISOU 3252 CA TRP A 283 15563 5329 3838 -2254 2101 -583 C ATOM 3253 C TRP A 283 102.804 13.868 37.687 1.00 65.90 C ANISOU 3253 C TRP A 283 15062 5765 4212 -2049 1807 -586 C ATOM 3254 O TRP A 283 103.353 13.634 38.758 1.00 65.04 O ANISOU 3254 O TRP A 283 14606 5857 4248 -2207 1758 -678 O ATOM 3255 CB TRP A 283 101.765 16.093 37.024 1.00 64.35 C ANISOU 3255 CB TRP A 283 15972 4917 3562 -1934 2043 -430 C ATOM 3256 CG TRP A 283 101.233 16.401 38.395 1.00 64.47 C ANISOU 3256 CG TRP A 283 15910 4933 3654 -1857 1918 -422 C ATOM 3257 CD1 TRP A 283 100.267 15.716 39.071 1.00 64.84 C ANISOU 3257 CD1 TRP A 283 15649 5137 3851 -1529 1635 -358 C ATOM 3258 CD2 TRP A 283 101.643 17.473 39.254 1.00 66.19 C ANISOU 3258 CD2 TRP A 283 16382 4982 3785 -2144 2097 -496 C ATOM 3259 NE1 TRP A 283 100.046 16.296 40.299 1.00 64.29 N ANISOU 3259 NE1 TRP A 283 15623 5007 3796 -1569 1625 -377 N ATOM 3260 CE2 TRP A 283 100.879 17.375 40.440 1.00 68.35 C ANISOU 3260 CE2 TRP A 283 16485 5319 4165 -1939 1897 -462 C ATOM 3261 CE3 TRP A 283 102.586 18.510 39.140 1.00 70.74 C ANISOU 3261 CE3 TRP A 283 17333 5355 4189 -2592 2426 -603 C ATOM 3262 CZ2 TRP A 283 101.031 18.271 41.505 1.00 68.91 C ANISOU 3262 CZ2 TRP A 283 16753 5254 4176 -2142 2003 -526 C ATOM 3263 CZ3 TRP A 283 102.736 19.396 40.196 1.00 73.57 C ANISOU 3263 CZ3 TRP A 283 17888 5579 4485 -2821 2533 -676 C ATOM 3264 CH2 TRP A 283 101.966 19.273 41.362 1.00 72.32 C ANISOU 3264 CH2 TRP A 283 17559 5484 4435 -2584 2316 -635 C ATOM 3265 N ILE A 284 102.034 12.966 37.038 1.00 60.89 N ANISOU 3265 N ILE A 284 14329 5188 3619 -1720 1625 -497 N ATOM 3266 CA ILE A 284 101.705 11.621 37.532 1.00 58.25 C ANISOU 3266 CA ILE A 284 13520 5109 3504 -1527 1377 -494 C ATOM 3267 C ILE A 284 102.997 10.777 37.691 1.00 62.45 C ANISOU 3267 C ILE A 284 13627 5908 4195 -1730 1433 -622 C ATOM 3268 O ILE A 284 103.164 10.138 38.728 1.00 60.74 O ANISOU 3268 O ILE A 284 13054 5884 4140 -1703 1296 -655 O ATOM 3269 CB ILE A 284 100.672 10.934 36.584 1.00 60.56 C ANISOU 3269 CB ILE A 284 13872 5387 3753 -1208 1224 -402 C ATOM 3270 CG1 ILE A 284 99.280 11.598 36.727 1.00 61.07 C ANISOU 3270 CG1 ILE A 284 14206 5305 3693 -928 1097 -289 C ATOM 3271 CG2 ILE A 284 100.569 9.414 36.835 1.00 59.40 C ANISOU 3271 CG2 ILE A 284 13290 5474 3807 -1094 1044 -428 C ATOM 3272 CD1 ILE A 284 98.273 11.304 35.583 1.00 69.58 C ANISOU 3272 CD1 ILE A 284 15434 6370 4633 -637 974 -213 C ATOM 3273 N SER A 285 103.901 10.802 36.689 1.00 61.22 N ANISOU 3273 N SER A 285 13520 5768 3971 -1911 1639 -693 N ATOM 3274 CA SER A 285 105.157 10.039 36.668 1.00 61.92 C ANISOU 3274 CA SER A 285 13202 6140 4183 -2063 1718 -827 C ATOM 3275 C SER A 285 106.085 10.364 37.849 1.00 66.78 C ANISOU 3275 C SER A 285 13526 6970 4879 -2317 1752 -953 C ATOM 3276 O SER A 285 106.732 9.447 38.359 1.00 65.95 O ANISOU 3276 O SER A 285 12974 7162 4923 -2265 1662 -1025 O ATOM 3277 CB SER A 285 105.919 10.295 35.371 1.00 68.27 C ANISOU 3277 CB SER A 285 14177 6902 4859 -2256 1989 -894 C ATOM 3278 OG SER A 285 105.189 9.863 34.235 1.00 77.59 O ANISOU 3278 OG SER A 285 15590 7935 5955 -2024 1947 -796 O ATOM 3279 N ILE A 286 106.163 11.647 38.269 1.00 65.05 N ANISOU 3279 N ILE A 286 13576 6604 4538 -2580 1883 -985 N ATOM 3280 CA ILE A 286 107.048 12.064 39.360 1.00 66.59 C ANISOU 3280 CA ILE A 286 13519 7012 4769 -2881 1925 -1132 C ATOM 3281 C ILE A 286 106.321 11.924 40.726 1.00 68.38 C ANISOU 3281 C ILE A 286 13641 7256 5086 -2698 1670 -1063 C ATOM 3282 O ILE A 286 106.974 11.540 41.697 1.00 67.96 O ANISOU 3282 O ILE A 286 13191 7501 5129 -2768 1571 -1159 O ATOM 3283 CB ILE A 286 107.620 13.503 39.147 1.00 73.14 C ANISOU 3283 CB ILE A 286 14713 7675 5400 -3339 2239 -1239 C ATOM 3284 CG1 ILE A 286 108.868 13.757 40.029 1.00 76.05 C ANISOU 3284 CG1 ILE A 286 14702 8394 5801 -3744 2319 -1462 C ATOM 3285 CG2 ILE A 286 106.557 14.622 39.263 1.00 73.87 C ANISOU 3285 CG2 ILE A 286 15413 7330 5326 -3286 2273 -1112 C ATOM 3286 CD1 ILE A 286 109.764 14.947 39.612 1.00 88.14 C ANISOU 3286 CD1 ILE A 286 16493 9858 7140 -4308 2694 -1637 C ATOM 3287 N THR A 287 104.993 12.201 40.796 1.00 63.63 N ANISOU 3287 N THR A 287 13371 6367 4437 -2448 1562 -907 N ATOM 3288 CA THR A 287 104.221 12.105 42.044 1.00 61.93 C ANISOU 3288 CA THR A 287 13086 6152 4292 -2279 1352 -845 C ATOM 3289 C THR A 287 104.008 10.638 42.444 1.00 64.34 C ANISOU 3289 C THR A 287 12987 6680 4778 -1998 1114 -802 C ATOM 3290 O THR A 287 103.770 10.375 43.622 1.00 63.01 O ANISOU 3290 O THR A 287 12657 6603 4679 -1926 960 -792 O ATOM 3291 CB THR A 287 102.876 12.838 41.967 1.00 69.08 C ANISOU 3291 CB THR A 287 14433 6729 5085 -2076 1328 -709 C ATOM 3292 OG1 THR A 287 102.109 12.334 40.874 1.00 68.07 O ANISOU 3292 OG1 THR A 287 14411 6513 4938 -1796 1270 -602 O ATOM 3293 CG2 THR A 287 103.032 14.352 41.868 1.00 70.05 C ANISOU 3293 CG2 THR A 287 15037 6577 5003 -2324 1566 -741 C ATOM 3294 N GLU A 288 104.114 9.692 41.483 1.00 60.92 N ANISOU 3294 N GLU A 288 12435 6311 4399 -1851 1103 -782 N ATOM 3295 CA GLU A 288 104.008 8.254 41.750 1.00 59.47 C ANISOU 3295 CA GLU A 288 11940 6296 4361 -1603 924 -751 C ATOM 3296 C GLU A 288 105.243 7.802 42.527 1.00 64.68 C ANISOU 3296 C GLU A 288 12205 7271 5098 -1693 900 -865 C ATOM 3297 O GLU A 288 105.113 7.116 43.541 1.00 63.21 O ANISOU 3297 O GLU A 288 11829 7200 4990 -1539 727 -838 O ATOM 3298 CB GLU A 288 103.850 7.457 40.440 1.00 60.63 C ANISOU 3298 CB GLU A 288 12127 6398 4511 -1454 955 -719 C ATOM 3299 CG GLU A 288 103.505 5.989 40.641 1.00 71.12 C ANISOU 3299 CG GLU A 288 13259 7808 5955 -1195 793 -676 C ATOM 3300 CD GLU A 288 103.447 5.148 39.380 1.00 95.58 C ANISOU 3300 CD GLU A 288 16405 10866 9044 -1079 839 -670 C ATOM 3301 OE1 GLU A 288 102.391 4.521 39.136 1.00 91.80 O ANISOU 3301 OE1 GLU A 288 16029 10283 8566 -915 730 -601 O ATOM 3302 OE2 GLU A 288 104.456 5.110 38.638 1.00 91.75 O ANISOU 3302 OE2 GLU A 288 15849 10472 8541 -1172 994 -751 O ATOM 3303 N ALA A 289 106.437 8.230 42.057 1.00 63.91 N ANISOU 3303 N ALA A 289 11993 7331 4958 -1946 1081 -1000 N ATOM 3304 CA ALA A 289 107.745 7.940 42.644 1.00 65.78 C ANISOU 3304 CA ALA A 289 11805 7951 5239 -2053 1079 -1147 C ATOM 3305 C ALA A 289 107.869 8.517 44.054 1.00 70.07 C ANISOU 3305 C ALA A 289 12257 8607 5758 -2196 977 -1197 C ATOM 3306 O ALA A 289 108.426 7.856 44.927 1.00 70.16 O ANISOU 3306 O ALA A 289 11920 8916 5823 -2082 825 -1242 O ATOM 3307 CB ALA A 289 108.842 8.506 41.761 1.00 69.32 C ANISOU 3307 CB ALA A 289 12190 8531 5618 -2366 1339 -1302 C ATOM 3308 N LEU A 290 107.336 9.735 44.273 1.00 66.71 N ANISOU 3308 N LEU A 290 12177 7937 5232 -2416 1061 -1184 N ATOM 3309 CA LEU A 290 107.361 10.428 45.562 1.00 67.23 C ANISOU 3309 CA LEU A 290 12245 8052 5246 -2589 996 -1238 C ATOM 3310 C LEU A 290 106.286 9.882 46.516 1.00 69.32 C ANISOU 3310 C LEU A 290 12555 8212 5572 -2277 764 -1093 C ATOM 3311 O LEU A 290 106.460 9.985 47.731 1.00 69.13 O ANISOU 3311 O LEU A 290 12405 8330 5530 -2329 648 -1136 O ATOM 3312 CB LEU A 290 107.171 11.943 45.369 1.00 68.52 C ANISOU 3312 CB LEU A 290 12842 7936 5256 -2928 1213 -1280 C ATOM 3313 CG LEU A 290 108.306 12.697 44.661 1.00 76.50 C ANISOU 3313 CG LEU A 290 13859 9043 6163 -3363 1490 -1460 C ATOM 3314 CD1 LEU A 290 107.834 14.039 44.157 1.00 77.80 C ANISOU 3314 CD1 LEU A 290 14620 8785 6154 -3593 1732 -1437 C ATOM 3315 CD2 LEU A 290 109.524 12.864 45.562 1.00 81.64 C ANISOU 3315 CD2 LEU A 290 14105 10122 6793 -3689 1482 -1681 C ATOM 3316 N ALA A 291 105.195 9.287 45.977 1.00 64.39 N ANISOU 3316 N ALA A 291 12099 7363 5004 -1978 702 -938 N ATOM 3317 CA ALA A 291 104.103 8.703 46.772 1.00 62.35 C ANISOU 3317 CA ALA A 291 11883 7009 4798 -1712 518 -813 C ATOM 3318 C ALA A 291 104.542 7.422 47.495 1.00 66.44 C ANISOU 3318 C ALA A 291 12071 7773 5399 -1516 345 -809 C ATOM 3319 O ALA A 291 103.869 7.003 48.437 1.00 64.64 O ANISOU 3319 O ALA A 291 11866 7506 5190 -1366 208 -734 O ATOM 3320 CB ALA A 291 102.906 8.399 45.886 1.00 61.30 C ANISOU 3320 CB ALA A 291 11972 6635 4684 -1497 515 -689 C ATOM 3321 N PHE A 292 105.670 6.812 47.065 1.00 65.13 N ANISOU 3321 N PHE A 292 11622 7857 5266 -1500 364 -889 N ATOM 3322 CA PHE A 292 106.212 5.588 47.654 1.00 65.80 C ANISOU 3322 CA PHE A 292 11423 8178 5400 -1251 212 -884 C ATOM 3323 C PHE A 292 107.095 5.898 48.888 1.00 72.39 C ANISOU 3323 C PHE A 292 12006 9328 6173 -1359 110 -988 C ATOM 3324 O PHE A 292 107.730 4.989 49.431 1.00 73.15 O ANISOU 3324 O PHE A 292 11845 9677 6271 -1134 -27 -998 O ATOM 3325 CB PHE A 292 107.010 4.780 46.611 1.00 68.77 C ANISOU 3325 CB PHE A 292 11610 8696 5823 -1125 285 -927 C ATOM 3326 CG PHE A 292 106.266 4.389 45.349 1.00 68.89 C ANISOU 3326 CG PHE A 292 11857 8441 5875 -1029 378 -846 C ATOM 3327 CD1 PHE A 292 104.950 3.937 45.406 1.00 69.79 C ANISOU 3327 CD1 PHE A 292 12217 8287 6011 -876 303 -715 C ATOM 3328 CD2 PHE A 292 106.912 4.381 44.118 1.00 72.20 C ANISOU 3328 CD2 PHE A 292 12225 8914 6295 -1092 541 -917 C ATOM 3329 CE1 PHE A 292 104.274 3.550 44.243 1.00 69.62 C ANISOU 3329 CE1 PHE A 292 12381 8069 6002 -804 369 -664 C ATOM 3330 CE2 PHE A 292 106.238 3.986 42.957 1.00 73.77 C ANISOU 3330 CE2 PHE A 292 12647 8880 6502 -1001 612 -850 C ATOM 3331 CZ PHE A 292 104.926 3.570 43.028 1.00 69.67 C ANISOU 3331 CZ PHE A 292 12361 8114 5997 -858 514 -727 C ATOM 3332 N PHE A 293 107.080 7.162 49.365 1.00 70.11 N ANISOU 3332 N PHE A 293 11824 9011 5804 -1679 168 -1063 N ATOM 3333 CA PHE A 293 107.816 7.581 50.559 1.00 72.31 C ANISOU 3333 CA PHE A 293 11899 9580 5995 -1841 71 -1182 C ATOM 3334 C PHE A 293 107.081 7.096 51.826 1.00 75.23 C ANISOU 3334 C PHE A 293 12361 9878 6345 -1621 -125 -1067 C ATOM 3335 O PHE A 293 107.681 7.081 52.902 1.00 76.55 O ANISOU 3335 O PHE A 293 12337 10321 6429 -1642 -266 -1138 O ATOM 3336 CB PHE A 293 108.017 9.109 50.578 1.00 75.57 C ANISOU 3336 CB PHE A 293 12470 9936 6307 -2300 239 -1314 C ATOM 3337 CG PHE A 293 108.958 9.621 51.646 1.00 80.15 C ANISOU 3337 CG PHE A 293 12805 10873 6773 -2563 167 -1493 C ATOM 3338 CD1 PHE A 293 108.467 10.198 52.811 1.00 83.20 C ANISOU 3338 CD1 PHE A 293 13379 11164 7069 -2663 91 -1488 C ATOM 3339 CD2 PHE A 293 110.336 9.517 51.490 1.00 85.65 C ANISOU 3339 CD2 PHE A 293 13064 12038 7441 -2711 176 -1684 C ATOM 3340 CE1 PHE A 293 109.338 10.661 53.803 1.00 87.09 C ANISOU 3340 CE1 PHE A 293 13649 12008 7432 -2926 12 -1669 C ATOM 3341 CE2 PHE A 293 111.206 9.980 52.482 1.00 91.70 C ANISOU 3341 CE2 PHE A 293 13561 13199 8081 -2971 89 -1875 C ATOM 3342 CZ PHE A 293 110.700 10.551 53.631 1.00 89.51 C ANISOU 3342 CZ PHE A 293 13499 12805 7703 -3087 2 -1866 C ATOM 3343 N HIS A 294 105.808 6.634 51.684 1.00 69.47 N ANISOU 3343 N HIS A 294 11908 8812 5677 -1410 -135 -900 N ATOM 3344 CA HIS A 294 104.990 6.099 52.780 1.00 68.41 C ANISOU 3344 CA HIS A 294 11897 8573 5522 -1217 -276 -787 C ATOM 3345 C HIS A 294 105.633 4.813 53.363 1.00 74.70 C ANISOU 3345 C HIS A 294 12476 9604 6302 -919 -447 -756 C ATOM 3346 O HIS A 294 105.271 4.391 54.464 1.00 74.38 O ANISOU 3346 O HIS A 294 12518 9546 6198 -783 -573 -686 O ATOM 3347 CB HIS A 294 103.540 5.831 52.328 1.00 66.41 C ANISOU 3347 CB HIS A 294 11930 7966 5337 -1091 -219 -650 C ATOM 3348 CG HIS A 294 103.370 4.665 51.402 1.00 68.91 C ANISOU 3348 CG HIS A 294 12224 8218 5739 -863 -211 -578 C ATOM 3349 ND1 HIS A 294 103.401 4.822 50.029 1.00 70.22 N ANISOU 3349 ND1 HIS A 294 12414 8310 5957 -912 -86 -598 N ATOM 3350 CD2 HIS A 294 103.137 3.362 51.686 1.00 70.28 C ANISOU 3350 CD2 HIS A 294 12408 8364 5930 -606 -295 -493 C ATOM 3351 CE1 HIS A 294 103.206 3.616 49.524 1.00 69.04 C ANISOU 3351 CE1 HIS A 294 12264 8108 5861 -691 -106 -535 C ATOM 3352 NE2 HIS A 294 103.044 2.705 50.483 1.00 69.47 N ANISOU 3352 NE2 HIS A 294 12324 8174 5897 -508 -221 -471 N ATOM 3353 N CYS A 295 106.587 4.211 52.619 1.00 73.42 N ANISOU 3353 N CYS A 295 12065 9653 6177 -798 -439 -806 N ATOM 3354 CA CYS A 295 107.356 3.031 53.015 1.00 75.55 C ANISOU 3354 CA CYS A 295 12125 10168 6410 -457 -586 -787 C ATOM 3355 C CYS A 295 108.419 3.432 54.033 1.00 83.36 C ANISOU 3355 C CYS A 295 12815 11583 7274 -525 -732 -915 C ATOM 3356 O CYS A 295 108.689 2.685 54.973 1.00 84.65 O ANISOU 3356 O CYS A 295 12921 11901 7341 -242 -915 -865 O ATOM 3357 CB CYS A 295 107.987 2.369 51.795 1.00 76.65 C ANISOU 3357 CB CYS A 295 12105 10391 6626 -303 -497 -816 C ATOM 3358 SG CYS A 295 106.804 1.915 50.504 1.00 77.56 S ANISOU 3358 SG CYS A 295 12558 10052 6859 -260 -334 -697 S ATOM 3359 N CYS A 296 109.021 4.617 53.829 1.00 81.59 N ANISOU 3359 N CYS A 296 12422 11550 7027 -914 -645 -1088 N ATOM 3360 CA CYS A 296 110.063 5.204 54.672 1.00 84.80 C ANISOU 3360 CA CYS A 296 12512 12405 7302 -1102 -756 -1266 C ATOM 3361 C CYS A 296 109.439 5.954 55.855 1.00 88.29 C ANISOU 3361 C CYS A 296 13189 12718 7639 -1301 -822 -1256 C ATOM 3362 O CYS A 296 110.131 6.230 56.832 1.00 90.39 O ANISOU 3362 O CYS A 296 13247 13335 7761 -1391 -971 -1374 O ATOM 3363 CB CYS A 296 110.941 6.137 53.841 1.00 87.00 C ANISOU 3363 CB CYS A 296 12553 12912 7593 -1501 -579 -1477 C ATOM 3364 SG CYS A 296 111.507 5.431 52.272 1.00 91.25 S ANISOU 3364 SG CYS A 296 12893 13520 8260 -1330 -427 -1493 S ATOM 3365 N LEU A 297 108.141 6.295 55.749 1.00 82.02 N ANISOU 3365 N LEU A 297 12812 11448 6904 -1365 -710 -1129 N ATOM 3366 CA LEU A 297 107.352 7.073 56.708 1.00 81.16 C ANISOU 3366 CA LEU A 297 12990 11135 6711 -1544 -713 -1110 C ATOM 3367 C LEU A 297 107.282 6.436 58.108 1.00 86.48 C ANISOU 3367 C LEU A 297 13673 11925 7261 -1317 -934 -1044 C ATOM 3368 O LEU A 297 107.297 7.167 59.102 1.00 87.09 O ANISOU 3368 O LEU A 297 13817 12068 7204 -1525 -985 -1120 O ATOM 3369 CB LEU A 297 105.925 7.218 56.161 1.00 77.81 C ANISOU 3369 CB LEU A 297 12951 10221 6391 -1510 -563 -964 C ATOM 3370 CG LEU A 297 105.114 8.430 56.601 1.00 81.69 C ANISOU 3370 CG LEU A 297 13760 10454 6825 -1766 -452 -982 C ATOM 3371 CD1 LEU A 297 105.547 9.682 55.843 1.00 82.79 C ANISOU 3371 CD1 LEU A 297 13952 10559 6944 -2134 -260 -1122 C ATOM 3372 CD2 LEU A 297 103.645 8.195 56.342 1.00 81.28 C ANISOU 3372 CD2 LEU A 297 14006 10021 6857 -1587 -381 -821 C ATOM 3373 N ASN A 298 107.179 5.095 58.182 1.00 83.19 N ANISOU 3373 N ASN A 298 13245 11498 6865 -900 -1047 -903 N ATOM 3374 CA ASN A 298 107.061 4.357 59.442 1.00 84.04 C ANISOU 3374 CA ASN A 298 13442 11658 6830 -635 -1238 -809 C ATOM 3375 C ASN A 298 108.386 4.419 60.267 1.00 91.80 C ANISOU 3375 C ASN A 298 14072 13177 7631 -609 -1458 -950 C ATOM 3376 O ASN A 298 108.299 4.869 61.411 1.00 92.45 O ANISOU 3376 O ASN A 298 14244 13328 7555 -725 -1561 -983 O ATOM 3377 CB ASN A 298 106.643 2.901 59.184 1.00 84.53 C ANISOU 3377 CB ASN A 298 13649 11526 6941 -211 -1259 -627 C ATOM 3378 CG ASN A 298 106.277 2.102 60.414 1.00111.39 C ANISOU 3378 CG ASN A 298 17284 14854 10185 55 -1398 -496 C ATOM 3379 OD1 ASN A 298 106.012 2.639 61.497 1.00107.47 O ANISOU 3379 OD1 ASN A 298 16908 14368 9558 -81 -1461 -512 O ATOM 3380 ND2 ASN A 298 106.203 0.790 60.256 1.00104.35 N ANISOU 3380 ND2 ASN A 298 16519 13843 9285 432 -1422 -361 N ATOM 3381 N PRO A 299 109.598 4.034 59.764 1.00 90.95 N ANISOU 3381 N PRO A 299 13551 13483 7521 -471 -1536 -1051 N ATOM 3382 CA PRO A 299 110.800 4.109 60.620 1.00 95.01 C ANISOU 3382 CA PRO A 299 13687 14575 7837 -434 -1771 -1203 C ATOM 3383 C PRO A 299 111.271 5.541 60.914 1.00100.44 C ANISOU 3383 C PRO A 299 14206 15510 8447 -991 -1733 -1445 C ATOM 3384 O PRO A 299 111.912 5.750 61.944 1.00103.12 O ANISOU 3384 O PRO A 299 14352 16247 8580 -1036 -1938 -1563 O ATOM 3385 CB PRO A 299 111.867 3.369 59.806 1.00 99.09 C ANISOU 3385 CB PRO A 299 13790 15457 8401 -146 -1812 -1261 C ATOM 3386 CG PRO A 299 111.115 2.601 58.779 1.00100.39 C ANISOU 3386 CG PRO A 299 14224 15164 8753 75 -1639 -1082 C ATOM 3387 CD PRO A 299 109.940 3.445 58.455 1.00 92.13 C ANISOU 3387 CD PRO A 299 13543 13636 7827 -307 -1428 -1039 C ATOM 3388 N ILE A 300 110.961 6.514 60.030 1.00 95.33 N ANISOU 3388 N ILE A 300 13662 14624 7934 -1412 -1472 -1523 N ATOM 3389 CA ILE A 300 111.341 7.926 60.194 1.00 96.89 C ANISOU 3389 CA ILE A 300 13807 14958 8050 -1989 -1369 -1755 C ATOM 3390 C ILE A 300 110.500 8.563 61.338 1.00100.08 C ANISOU 3390 C ILE A 300 14604 15093 8327 -2155 -1391 -1716 C ATOM 3391 O ILE A 300 110.998 9.464 62.019 1.00102.16 O ANISOU 3391 O ILE A 300 14795 15596 8426 -2537 -1421 -1916 O ATOM 3392 CB ILE A 300 111.198 8.697 58.834 1.00 98.48 C ANISOU 3392 CB ILE A 300 14105 14902 8409 -2328 -1054 -1816 C ATOM 3393 CG1 ILE A 300 112.317 8.298 57.820 1.00101.06 C ANISOU 3393 CG1 ILE A 300 13968 15621 8809 -2288 -1016 -1937 C ATOM 3394 CG2 ILE A 300 111.108 10.230 58.981 1.00 99.90 C ANISOU 3394 CG2 ILE A 300 14506 14948 8502 -2921 -864 -1985 C ATOM 3395 CD1 ILE A 300 113.840 8.588 58.211 1.00113.87 C ANISOU 3395 CD1 ILE A 300 15008 17980 10276 -2520 -1135 -2235 C ATOM 3396 N LEU A 301 109.273 8.048 61.588 1.00 93.68 N ANISOU 3396 N LEU A 301 14190 13827 7577 -1877 -1375 -1480 N ATOM 3397 CA LEU A 301 108.350 8.534 62.625 1.00 92.60 C ANISOU 3397 CA LEU A 301 14443 13406 7335 -1975 -1368 -1423 C ATOM 3398 C LEU A 301 108.922 8.346 64.060 1.00 99.90 C ANISOU 3398 C LEU A 301 15251 14701 8004 -1913 -1637 -1488 C ATOM 3399 O LEU A 301 108.419 8.967 65.000 1.00 99.65 O ANISOU 3399 O LEU A 301 15496 14528 7839 -2096 -1630 -1509 O ATOM 3400 CB LEU A 301 107.002 7.805 62.506 1.00 89.03 C ANISOU 3400 CB LEU A 301 14348 12476 7005 -1656 -1295 -1170 C ATOM 3401 CG LEU A 301 105.785 8.575 63.006 1.00 91.85 C ANISOU 3401 CG LEU A 301 15132 12425 7343 -1824 -1146 -1122 C ATOM 3402 CD1 LEU A 301 104.902 8.998 61.850 1.00 89.06 C ANISOU 3402 CD1 LEU A 301 14974 11682 7181 -1890 -899 -1061 C ATOM 3403 CD2 LEU A 301 104.995 7.756 64.006 1.00 93.69 C ANISOU 3403 CD2 LEU A 301 15594 12506 7497 -1536 -1242 -956 C ATOM 3404 N TYR A 302 109.981 7.522 64.213 1.00 99.35 N ANISOU 3404 N TYR A 302 14780 15119 7850 -1639 -1874 -1526 N ATOM 3405 CA TYR A 302 110.653 7.259 65.491 1.00102.77 C ANISOU 3405 CA TYR A 302 15051 15986 8010 -1512 -2172 -1591 C ATOM 3406 C TYR A 302 111.537 8.443 65.926 1.00109.54 C ANISOU 3406 C TYR A 302 15652 17271 8699 -2033 -2213 -1900 C ATOM 3407 O TYR A 302 111.838 8.564 67.115 1.00111.74 O ANISOU 3407 O TYR A 302 15909 17824 8722 -2062 -2424 -1977 O ATOM 3408 CB TYR A 302 111.502 5.981 65.399 1.00106.47 C ANISOU 3408 CB TYR A 302 15170 16849 8434 -982 -2408 -1530 C ATOM 3409 CG TYR A 302 110.680 4.711 65.403 1.00106.12 C ANISOU 3409 CG TYR A 302 15467 16406 8447 -457 -2415 -1232 C ATOM 3410 CD1 TYR A 302 110.107 4.223 64.232 1.00104.87 C ANISOU 3410 CD1 TYR A 302 15434 15869 8542 -330 -2208 -1099 C ATOM 3411 CD2 TYR A 302 110.486 3.986 66.575 1.00108.37 C ANISOU 3411 CD2 TYR A 302 15977 16690 8508 -107 -2619 -1093 C ATOM 3412 CE1 TYR A 302 109.344 3.057 64.230 1.00104.11 C ANISOU 3412 CE1 TYR A 302 15674 15403 8482 87 -2190 -852 C ATOM 3413 CE2 TYR A 302 109.733 2.813 66.585 1.00107.60 C ANISOU 3413 CE2 TYR A 302 16247 16196 8439 326 -2588 -832 C ATOM 3414 CZ TYR A 302 109.164 2.352 65.409 1.00111.97 C ANISOU 3414 CZ TYR A 302 16912 16379 9254 402 -2367 -721 C ATOM 3415 OH TYR A 302 108.415 1.202 65.408 1.00111.77 O ANISOU 3415 OH TYR A 302 17267 15959 9241 765 -2311 -490 O ATOM 3416 N ALA A 303 111.938 9.312 64.974 1.00106.04 N ANISOU 3416 N ALA A 303 15048 16870 8373 -2466 -1998 -2083 N ATOM 3417 CA ALA A 303 112.768 10.490 65.238 1.00135.30 C ANISOU 3417 CA ALA A 303 18545 20940 11922 -3056 -1969 -2405 C ATOM 3418 C ALA A 303 111.965 11.607 65.920 1.00154.57 C ANISOU 3418 C ALA A 303 21492 22978 14261 -3463 -1815 -2445 C ATOM 3419 O ALA A 303 110.742 11.531 66.040 1.00108.85 O ANISOU 3419 O ALA A 303 16176 16628 8553 -3290 -1703 -2227 O ATOM 3420 CB ALA A 303 113.370 11.006 63.941 1.00136.57 C ANISOU 3420 CB ALA A 303 18460 21197 12235 -3391 -1735 -2569 C TER 3421 ALA A 303 ATOM 3422 N LEU C 1 104.801 -0.342 34.341 1.00127.89 N ANISOU 3422 N LEU C 1 37943 7364 3285 307 -1323 894 N ATOM 3423 CA LEU C 1 104.308 -0.297 35.714 1.00128.01 C ANISOU 3423 CA LEU C 1 37969 7474 3196 66 -957 974 C ATOM 3424 C LEU C 1 103.776 1.096 36.058 1.00130.58 C ANISOU 3424 C LEU C 1 37984 8006 3625 -315 -508 912 C ATOM 3425 O LEU C 1 104.550 2.053 36.159 1.00130.79 O ANISOU 3425 O LEU C 1 37960 8105 3630 19 -1099 774 O ATOM 3426 CB LEU C 1 105.412 -0.702 36.711 1.00129.31 C ANISOU 3426 CB LEU C 1 37884 7860 3388 720 -1824 931 C ATOM 3427 CG LEU C 1 105.978 -2.120 36.616 1.00133.04 C ANISOU 3427 CG LEU C 1 37815 8566 4168 1104 -2202 988 C ATOM 3428 CD1 LEU C 1 107.265 -2.234 37.399 1.00134.69 C ANISOU 3428 CD1 LEU C 1 37607 9084 4484 1766 -3115 861 C ATOM 3429 CD2 LEU C 1 104.970 -3.161 37.079 1.00134.09 C ANISOU 3429 CD2 LEU C 1 37922 8691 4336 630 -1449 1201 C ATOM 3430 N GLY C 2 102.458 1.183 36.220 1.00127.99 N ANISOU 3430 N GLY C 2 37954 7514 3163 -1027 528 976 N ATOM 3431 CA GLY C 2 101.742 2.403 36.576 1.00127.81 C ANISOU 3431 CA GLY C 2 37891 7549 3123 -1464 1133 902 C ATOM 3432 C GLY C 2 101.820 3.533 35.569 1.00130.17 C ANISOU 3432 C GLY C 2 37781 7996 3680 -1536 1151 792 C ATOM 3433 O GLY C 2 101.014 3.591 34.635 1.00125.24 O ANISOU 3433 O GLY C 2 36180 7773 3631 -1930 1772 772 O ATOM 3434 N ALA C 3 102.791 4.448 35.771 1.00125.80 N ANISOU 3434 N ALA C 3 36803 7706 3288 -1079 402 698 N ATOM 3435 CA ALA C 3 103.015 5.645 34.955 1.00119.03 C ANISOU 3435 CA ALA C 3 34402 7578 3247 -1037 297 585 C ATOM 3436 C ALA C 3 103.475 5.322 33.526 1.00117.78 C ANISOU 3436 C ALA C 3 33076 7903 3772 -837 -6 567 C ATOM 3437 O ALA C 3 103.015 5.983 32.598 1.00111.76 O ANISOU 3437 O ALA C 3 31159 7650 3655 -1077 377 538 O ATOM 3438 CB ALA C 3 104.047 6.540 35.617 1.00121.11 C ANISOU 3438 CB ALA C 3 34705 7904 3409 -632 -462 452 C ATOM 3439 N SER C 4 104.376 4.332 33.344 1.00116.82 N ANISOU 3439 N SER C 4 33289 7606 3492 -370 -700 565 N ATOM 3440 CA SER C 4 104.903 3.954 32.025 1.00112.72 C ANISOU 3440 CA SER C 4 31747 7507 3573 -148 -1001 518 C ATOM 3441 C SER C 4 103.818 3.329 31.125 1.00114.46 C ANISOU 3441 C SER C 4 31655 7795 4039 -612 -231 646 C ATOM 3442 O SER C 4 103.950 3.353 29.900 1.00109.30 O ANISOU 3442 O SER C 4 29946 7593 3989 -591 -253 613 O ATOM 3443 CB SER C 4 106.067 2.981 32.175 1.00120.26 C ANISOU 3443 CB SER C 4 33258 8198 4239 506 -1909 441 C ATOM 3444 OG SER C 4 105.671 1.796 32.843 1.00134.38 O ANISOU 3444 OG SER C 4 36493 9278 5285 496 -1785 595 O ATOM 3445 N CYS C 5 102.746 2.801 31.739 1.00114.94 N ANISOU 3445 N CYS C 5 32638 7408 3626 -1065 468 754 N ATOM 3446 CA CYS C 5 101.613 2.151 31.080 1.00113.92 C ANISOU 3446 CA CYS C 5 32346 7284 3652 -1591 1254 809 C ATOM 3447 C CYS C 5 100.576 3.174 30.582 1.00112.02 C ANISOU 3447 C CYS C 5 31035 7549 3977 -2055 1954 727 C ATOM 3448 O CYS C 5 99.765 2.835 29.716 1.00108.88 O ANISOU 3448 O CYS C 5 30062 7368 3938 -2400 2447 701 O ATOM 3449 CB CYS C 5 100.965 1.161 32.042 1.00121.52 C ANISOU 3449 CB CYS C 5 34828 7517 3828 -1925 1732 890 C ATOM 3450 SG CYS C 5 102.058 -0.185 32.562 1.00132.02 S ANISOU 3450 SG CYS C 5 37616 8138 4407 -1326 902 992 S ATOM 3451 N HIS C 6 100.585 4.400 31.150 1.00107.46 N ANISOU 3451 N HIS C 6 30245 7131 3453 -2040 1968 660 N ATOM 3452 CA HIS C 6 99.633 5.476 30.871 1.00104.05 C ANISOU 3452 CA HIS C 6 28959 7103 3473 -2379 2568 555 C ATOM 3453 C HIS C 6 99.646 5.986 29.409 1.00101.65 C ANISOU 3453 C HIS C 6 27282 7404 3935 -2280 2433 519 C ATOM 3454 O HIS C 6 98.678 5.727 28.691 1.00100.19 O ANISOU 3454 O HIS C 6 26628 7393 4046 -2584 2909 475 O ATOM 3455 CB HIS C 6 99.890 6.665 31.813 1.00105.64 C ANISOU 3455 CB HIS C 6 29356 7280 3504 -2269 2451 502 C ATOM 3456 CG HIS C 6 98.956 7.819 31.632 1.00106.78 C ANISOU 3456 CG HIS C 6 28739 7777 4056 -2531 3019 375 C ATOM 3457 ND1 HIS C 6 99.428 9.112 31.527 1.00105.68 N ANISOU 3457 ND1 HIS C 6 28016 7934 4203 -2302 2706 325 N ATOM 3458 CD2 HIS C 6 97.608 7.834 31.519 1.00109.39 C ANISOU 3458 CD2 HIS C 6 28807 8202 4555 -2972 3847 250 C ATOM 3459 CE1 HIS C 6 98.358 9.873 31.380 1.00104.31 C ANISOU 3459 CE1 HIS C 6 27330 7981 4321 -2551 3318 203 C ATOM 3460 NE2 HIS C 6 97.242 9.146 31.353 1.00106.89 N ANISOU 3460 NE2 HIS C 6 27756 8233 4624 -2936 3996 129 N ATOM 3461 N ARG C 7 100.700 6.705 28.972 1.00 94.65 N ANISOU 3461 N ARG C 7 25797 6818 3349 -1899 1823 506 N ATOM 3462 CA ARG C 7 100.802 7.162 27.582 1.00 89.23 C ANISOU 3462 CA ARG C 7 23969 6632 3303 -1828 1722 476 C ATOM 3463 C ARG C 7 102.234 6.894 27.047 1.00 92.92 C ANISOU 3463 C ARG C 7 24201 7209 3896 -1409 969 473 C ATOM 3464 O ARG C 7 103.081 7.793 27.066 1.00 91.77 O ANISOU 3464 O ARG C 7 23711 7252 3904 -1203 575 388 O ATOM 3465 CB ARG C 7 100.406 8.650 27.447 1.00 85.42 C ANISOU 3465 CB ARG C 7 22853 6456 3146 -1896 1929 392 C ATOM 3466 CG ARG C 7 98.902 8.903 27.574 1.00 89.76 C ANISOU 3466 CG ARG C 7 23284 7046 3775 -2256 2680 309 C ATOM 3467 CD ARG C 7 98.524 10.341 27.268 1.00 87.73 C ANISOU 3467 CD ARG C 7 22373 7089 3871 -2215 2807 211 C ATOM 3468 NE ARG C 7 97.075 10.503 27.120 1.00 90.04 N ANISOU 3468 NE ARG C 7 22326 7517 4369 -2471 3452 56 N ATOM 3469 CZ ARG C 7 96.270 11.049 28.027 1.00105.27 C ANISOU 3469 CZ ARG C 7 24497 9346 6154 -2636 3937 -87 C ATOM 3470 NH1 ARG C 7 96.769 11.545 29.154 1.00 95.91 N ANISOU 3470 NH1 ARG C 7 23969 7894 4578 -2579 3845 -51 N ATOM 3471 NH2 ARG C 7 94.969 11.149 27.795 1.00 91.79 N ANISOU 3471 NH2 ARG C 7 22333 7827 4715 -2840 4500 -311 N ATOM 3472 N PRO C 8 102.519 5.659 26.557 1.00 90.45 N ANISOU 3472 N PRO C 8 24051 6783 3532 -1296 789 522 N ATOM 3473 CA PRO C 8 103.886 5.350 26.101 1.00 90.26 C ANISOU 3473 CA PRO C 8 23787 6870 3639 -861 89 450 C ATOM 3474 C PRO C 8 104.101 5.436 24.579 1.00 91.21 C ANISOU 3474 C PRO C 8 22915 7414 4325 -850 73 411 C ATOM 3475 O PRO C 8 105.250 5.342 24.140 1.00 90.92 O ANISOU 3475 O PRO C 8 22538 7536 4471 -531 -429 287 O ATOM 3476 CB PRO C 8 104.069 3.900 26.558 1.00 96.08 C ANISOU 3476 CB PRO C 8 25455 7146 3904 -689 -108 516 C ATOM 3477 CG PRO C 8 102.659 3.324 26.625 1.00101.03 C ANISOU 3477 CG PRO C 8 26490 7548 4350 -1180 642 636 C ATOM 3478 CD PRO C 8 101.665 4.453 26.509 1.00 93.84 C ANISOU 3478 CD PRO C 8 24980 6936 3740 -1560 1210 604 C ATOM 3479 N ASP C 9 103.023 5.584 23.778 1.00 85.71 N ANISOU 3479 N ASP C 9 21774 6897 3897 -1181 603 474 N ATOM 3480 CA ASP C 9 103.109 5.612 22.316 1.00 82.32 C ANISOU 3480 CA ASP C 9 20550 6805 3923 -1188 611 452 C ATOM 3481 C ASP C 9 102.546 6.905 21.715 1.00 84.29 C ANISOU 3481 C ASP C 9 20144 7365 4516 -1363 886 428 C ATOM 3482 O ASP C 9 101.670 7.538 22.309 1.00 84.46 O ANISOU 3482 O ASP C 9 20282 7347 4462 -1545 1224 434 O ATOM 3483 CB ASP C 9 102.347 4.409 21.726 1.00 84.28 C ANISOU 3483 CB ASP C 9 20930 6945 4147 -1362 891 526 C ATOM 3484 CG ASP C 9 102.881 3.038 22.116 1.00 97.19 C ANISOU 3484 CG ASP C 9 23282 8219 5428 -1166 624 561 C ATOM 3485 OD1 ASP C 9 102.147 2.045 21.935 1.00 98.75 O ANISOU 3485 OD1 ASP C 9 23817 8217 5487 -1388 927 622 O ATOM 3486 OD2 ASP C 9 104.039 2.958 22.588 1.00105.04 O ANISOU 3486 OD2 ASP C 9 24507 9122 6283 -778 89 495 O ATOM 3487 N LYS C 10 103.047 7.272 20.515 1.00 79.09 N ANISOU 3487 N LYS C 10 18856 6987 4210 -1296 753 382 N ATOM 3488 CA LYS C 10 102.637 8.453 19.743 1.00 76.86 C ANISOU 3488 CA LYS C 10 18050 6942 4212 -1404 942 363 C ATOM 3489 C LYS C 10 101.204 8.294 19.238 1.00 81.08 C ANISOU 3489 C LYS C 10 18433 7529 4846 -1591 1336 405 C ATOM 3490 O LYS C 10 100.857 7.231 18.713 1.00 80.66 O ANISOU 3490 O LYS C 10 18380 7455 4811 -1656 1405 431 O ATOM 3491 CB LYS C 10 103.588 8.689 18.553 1.00 77.72 C ANISOU 3491 CB LYS C 10 17681 7259 4588 -1321 735 294 C ATOM 3492 CG LYS C 10 105.042 8.975 18.934 1.00 92.12 C ANISOU 3492 CG LYS C 10 19460 9123 6419 -1171 364 138 C ATOM 3493 CD LYS C 10 105.974 9.059 17.711 1.00 98.66 C ANISOU 3493 CD LYS C 10 19796 10164 7528 -1160 268 4 C ATOM 3494 CE LYS C 10 106.273 7.737 17.028 1.00106.33 C ANISOU 3494 CE LYS C 10 20702 11144 8554 -1026 160 -9 C ATOM 3495 NZ LYS C 10 107.041 6.806 17.898 1.00117.46 N ANISOU 3495 NZ LYS C 10 22397 12429 9802 -741 -226 -110 N ATOM 3496 N CYS C 11 100.377 9.345 19.395 1.00 78.43 N ANISOU 3496 N CYS C 11 17954 7264 4583 -1660 1572 369 N ATOM 3497 CA CYS C 11 98.974 9.330 18.971 1.00 78.99 C ANISOU 3497 CA CYS C 11 17773 7438 4802 -1786 1902 311 C ATOM 3498 C CYS C 11 98.647 10.553 18.099 1.00 81.28 C ANISOU 3498 C CYS C 11 17651 7907 5325 -1666 1874 265 C ATOM 3499 O CYS C 11 99.343 11.570 18.158 1.00 80.19 O ANISOU 3499 O CYS C 11 17549 7749 5169 -1564 1726 284 O ATOM 3500 CB CYS C 11 98.047 9.263 20.184 1.00 82.39 C ANISOU 3500 CB CYS C 11 18509 7740 5058 -1956 2270 237 C ATOM 3501 SG CYS C 11 98.230 7.762 21.185 1.00 89.21 S ANISOU 3501 SG CYS C 11 20083 8278 5535 -2136 2370 296 S ATOM 3502 N CYS C 12 97.575 10.441 17.293 1.00 77.91 N ANISOU 3502 N CYS C 12 16880 7629 5094 -1678 1998 176 N ATOM 3503 CA CYS C 12 97.086 11.514 16.432 1.00 77.46 C ANISOU 3503 CA CYS C 12 16526 7695 5211 -1491 1922 110 C ATOM 3504 C CYS C 12 95.901 12.199 17.106 1.00 84.09 C ANISOU 3504 C CYS C 12 17255 8583 6113 -1442 2168 -70 C ATOM 3505 O CYS C 12 94.933 11.533 17.485 1.00 85.93 O ANISOU 3505 O CYS C 12 17340 8894 6417 -1600 2442 -230 O ATOM 3506 CB CYS C 12 96.714 10.991 15.045 1.00 77.17 C ANISOU 3506 CB CYS C 12 16190 7792 5339 -1453 1795 82 C ATOM 3507 SG CYS C 12 98.123 10.424 14.054 1.00 78.43 S ANISOU 3507 SG CYS C 12 16450 7902 5447 -1469 1542 248 S ATOM 3508 N LEU C 13 95.993 13.525 17.278 1.00 80.93 N ANISOU 3508 N LEU C 13 16941 8125 5685 -1247 2107 -79 N ATOM 3509 CA LEU C 13 94.941 14.343 17.889 1.00 83.38 C ANISOU 3509 CA LEU C 13 17152 8470 6061 -1117 2315 -279 C ATOM 3510 C LEU C 13 94.147 15.071 16.796 1.00 88.11 C ANISOU 3510 C LEU C 13 17431 9189 6858 -782 2126 -423 C ATOM 3511 O LEU C 13 93.027 15.528 17.035 1.00 90.75 O ANISOU 3511 O LEU C 13 17502 9635 7345 -603 2253 -685 O ATOM 3512 CB LEU C 13 95.545 15.337 18.899 1.00 83.53 C ANISOU 3512 CB LEU C 13 17573 8292 5871 -1087 2356 -212 C ATOM 3513 CG LEU C 13 96.211 14.715 20.138 1.00 87.97 C ANISOU 3513 CG LEU C 13 18525 8710 6191 -1345 2487 -121 C ATOM 3514 CD1 LEU C 13 97.125 15.699 20.818 1.00 87.85 C ANISOU 3514 CD1 LEU C 13 18893 8514 5974 -1306 2369 -41 C ATOM 3515 CD2 LEU C 13 95.183 14.162 21.118 1.00 93.26 C ANISOU 3515 CD2 LEU C 13 19221 9387 6827 -1522 2915 -290 C ATOM 3516 N GLY C 14 94.738 15.127 15.605 1.00 82.62 N ANISOU 3516 N GLY C 14 16784 8461 6146 -686 1819 -282 N ATOM 3517 CA GLY C 14 94.175 15.721 14.400 1.00 83.76 C ANISOU 3517 CA GLY C 14 16801 8643 6382 -347 1541 -371 C ATOM 3518 C GLY C 14 94.794 15.099 13.165 1.00 85.55 C ANISOU 3518 C GLY C 14 17071 8862 6573 -419 1320 -221 C ATOM 3519 O GLY C 14 95.801 14.392 13.268 1.00 82.54 O ANISOU 3519 O GLY C 14 16818 8435 6106 -700 1380 -49 O ATOM 3520 N TYR C 15 94.202 15.354 11.987 1.00 83.67 N ANISOU 3520 N TYR C 15 16751 8654 6385 -131 1038 -311 N ATOM 3521 CA TYR C 15 94.685 14.787 10.726 1.00 82.05 C ANISOU 3521 CA TYR C 15 16640 8421 6115 -187 838 -192 C ATOM 3522 C TYR C 15 94.996 15.879 9.704 1.00 86.76 C ANISOU 3522 C TYR C 15 17712 8763 6488 81 580 -107 C ATOM 3523 O TYR C 15 94.429 16.972 9.778 1.00 89.20 O ANISOU 3523 O TYR C 15 18185 8961 6745 430 450 -205 O ATOM 3524 CB TYR C 15 93.645 13.812 10.145 1.00 84.94 C ANISOU 3524 CB TYR C 15 16540 9038 6696 -151 725 -401 C ATOM 3525 CG TYR C 15 93.113 12.803 11.141 1.00 87.15 C ANISOU 3525 CG TYR C 15 16417 9526 7170 -448 1043 -546 C ATOM 3526 CD1 TYR C 15 93.887 11.720 11.548 1.00 86.54 C ANISOU 3526 CD1 TYR C 15 16443 9412 7025 -833 1254 -380 C ATOM 3527 CD2 TYR C 15 91.823 12.911 11.651 1.00 91.61 C ANISOU 3527 CD2 TYR C 15 16533 10304 7971 -344 1147 -889 C ATOM 3528 CE1 TYR C 15 93.399 10.782 12.456 1.00 88.29 C ANISOU 3528 CE1 TYR C 15 16473 9734 7337 -1131 1573 -501 C ATOM 3529 CE2 TYR C 15 91.322 11.976 12.556 1.00 93.57 C ANISOU 3529 CE2 TYR C 15 16494 10701 8356 -708 1537 -1050 C ATOM 3530 CZ TYR C 15 92.114 10.912 12.956 1.00 98.45 C ANISOU 3530 CZ TYR C 15 17363 11210 8833 -1115 1754 -831 C ATOM 3531 OH TYR C 15 91.625 9.987 13.845 1.00101.65 O ANISOU 3531 OH TYR C 15 17659 11675 9290 -1497 2162 -977 O ATOM 3532 N GLN C 16 95.892 15.572 8.742 1.00 81.38 N ANISOU 3532 N GLN C 16 17313 7958 5651 -83 528 58 N ATOM 3533 CA GLN C 16 96.295 16.482 7.665 1.00 82.48 C ANISOU 3533 CA GLN C 16 18047 7790 5500 66 362 150 C ATOM 3534 C GLN C 16 95.123 16.671 6.692 1.00 89.15 C ANISOU 3534 C GLN C 16 18918 8631 6322 525 -46 -3 C ATOM 3535 O GLN C 16 94.595 15.690 6.162 1.00 88.96 O ANISOU 3535 O GLN C 16 18535 8820 6445 534 -192 -102 O ATOM 3536 CB GLN C 16 97.551 15.943 6.946 1.00 81.81 C ANISOU 3536 CB GLN C 16 18189 7613 5284 -298 507 305 C ATOM 3537 CG GLN C 16 98.138 16.843 5.847 1.00 99.25 C ANISOU 3537 CG GLN C 16 21123 9451 7136 -290 477 395 C ATOM 3538 CD GLN C 16 98.879 18.080 6.313 1.00120.13 C ANISOU 3538 CD GLN C 16 24240 11817 9586 -425 684 448 C ATOM 3539 OE1 GLN C 16 98.641 18.640 7.391 1.00115.87 O ANISOU 3539 OE1 GLN C 16 23592 11304 9129 -345 730 410 O ATOM 3540 NE2 GLN C 16 99.770 18.570 5.464 1.00113.32 N ANISOU 3540 NE2 GLN C 16 23973 10651 8431 -661 845 512 N ATOM 3541 N LYS C 17 94.702 17.932 6.494 1.00 88.35 N ANISOU 3541 N LYS C 17 19261 8277 6030 932 -263 -50 N ATOM 3542 CA LYS C 17 93.577 18.288 5.632 1.00 92.34 C ANISOU 3542 CA LYS C 17 19858 8743 6484 1501 -760 -243 C ATOM 3543 C LYS C 17 93.971 18.237 4.146 1.00 96.94 C ANISOU 3543 C LYS C 17 21074 9045 6715 1534 -992 -116 C ATOM 3544 O LYS C 17 93.281 17.578 3.364 1.00 98.11 O ANISOU 3544 O LYS C 17 20994 9349 6935 1733 -1331 -259 O ATOM 3545 CB LYS C 17 93.046 19.683 5.993 1.00 98.55 C ANISOU 3545 CB LYS C 17 21004 9296 7144 1991 -936 -344 C ATOM 3546 N ARG C 18 95.065 18.928 3.762 1.00 92.92 N ANISOU 3546 N ARG C 18 21372 8117 5816 1303 -782 118 N ATOM 3547 CA ARG C 18 95.543 18.989 2.377 1.00 94.32 C ANISOU 3547 CA ARG C 18 22311 7946 5579 1260 -887 241 C ATOM 3548 C ARG C 18 96.310 17.709 1.998 1.00 93.81 C ANISOU 3548 C ARG C 18 21928 8086 5629 752 -613 325 C ATOM 3549 O ARG C 18 97.183 17.289 2.762 1.00 89.54 O ANISOU 3549 O ARG C 18 21028 7710 5282 293 -186 396 O ATOM 3550 CB ARG C 18 96.432 20.224 2.160 1.00 96.36 C ANISOU 3550 CB ARG C 18 23580 7660 5372 1107 -650 407 C ATOM 3551 N PRO C 19 96.017 17.088 0.824 1.00 91.46 N ANISOU 3551 N PRO C 19 21794 7762 5195 861 -885 298 N ATOM 3552 CA PRO C 19 96.733 15.858 0.435 1.00 88.05 C ANISOU 3552 CA PRO C 19 21096 7499 4860 411 -621 360 C ATOM 3553 C PRO C 19 98.230 16.090 0.213 1.00 90.33 C ANISOU 3553 C PRO C 19 21870 7533 4918 -102 -101 516 C ATOM 3554 O PRO C 19 98.630 17.136 -0.297 1.00 93.08 O ANISOU 3554 O PRO C 19 23068 7443 4854 -116 -15 588 O ATOM 3555 CB PRO C 19 96.046 15.442 -0.869 1.00 93.03 C ANISOU 3555 CB PRO C 19 22008 8051 5288 700 -1071 284 C ATOM 3556 CG PRO C 19 94.725 16.140 -0.851 1.00101.66 C ANISOU 3556 CG PRO C 19 23103 9140 6384 1348 -1644 98 C ATOM 3557 CD PRO C 19 95.003 17.446 -0.187 1.00 98.08 C ANISOU 3557 CD PRO C 19 23070 8414 5780 1440 -1491 179 C ATOM 3558 N LEU C 20 99.050 15.105 0.616 1.00 82.75 N ANISOU 3558 N LEU C 20 20374 6841 4227 -523 252 527 N ATOM 3559 CA LEU C 20 100.515 15.151 0.545 1.00 81.51 C ANISOU 3559 CA LEU C 20 20408 6572 3990 -1025 762 566 C ATOM 3560 C LEU C 20 101.069 14.561 -0.770 1.00 86.29 C ANISOU 3560 C LEU C 20 21394 7030 4364 -1236 906 569 C ATOM 3561 O LEU C 20 100.524 13.569 -1.265 1.00 85.21 O ANISOU 3561 O LEU C 20 21021 7050 4305 -1096 668 547 O ATOM 3562 CB LEU C 20 101.117 14.372 1.732 1.00 77.65 C ANISOU 3562 CB LEU C 20 19120 6458 3925 -1272 991 522 C ATOM 3563 CG LEU C 20 100.776 14.846 3.148 1.00 80.92 C ANISOU 3563 CG LEU C 20 19173 7017 4556 -1161 947 511 C ATOM 3564 CD1 LEU C 20 101.013 13.744 4.150 1.00 77.77 C ANISOU 3564 CD1 LEU C 20 18067 6969 4515 -1285 1022 473 C ATOM 3565 CD2 LEU C 20 101.547 16.107 3.527 1.00 84.88 C ANISOU 3565 CD2 LEU C 20 20081 7276 4893 -1359 1204 515 C ATOM 3566 N PRO C 21 102.181 15.114 -1.324 1.00 84.62 N ANISOU 3566 N PRO C 21 21754 6523 3874 -1627 1350 560 N ATOM 3567 CA PRO C 21 102.752 14.533 -2.552 1.00 85.82 C ANISOU 3567 CA PRO C 21 22274 6532 3800 -1869 1576 528 C ATOM 3568 C PRO C 21 103.602 13.301 -2.237 1.00 85.97 C ANISOU 3568 C PRO C 21 21523 6929 4214 -2151 1858 414 C ATOM 3569 O PRO C 21 104.430 13.332 -1.324 1.00 83.63 O ANISOU 3569 O PRO C 21 20737 6833 4206 -2390 2133 316 O ATOM 3570 CB PRO C 21 103.599 15.673 -3.141 1.00 91.76 C ANISOU 3570 CB PRO C 21 23934 6816 4114 -2236 2030 509 C ATOM 3571 CG PRO C 21 103.515 16.818 -2.155 1.00 96.55 C ANISOU 3571 CG PRO C 21 24600 7337 4746 -2192 2024 536 C ATOM 3572 CD PRO C 21 102.971 16.278 -0.874 1.00 87.69 C ANISOU 3572 CD PRO C 21 22490 6689 4137 -1922 1719 537 C ATOM 3573 N GLN C 22 103.391 12.217 -3.008 1.00 82.23 N ANISOU 3573 N GLN C 22 20982 6531 3732 -2088 1746 404 N ATOM 3574 CA GLN C 22 104.059 10.913 -2.886 1.00 79.75 C ANISOU 3574 CA GLN C 22 20049 6516 3735 -2253 1934 294 C ATOM 3575 C GLN C 22 105.599 11.018 -2.990 1.00 84.66 C ANISOU 3575 C GLN C 22 20627 7131 4408 -2711 2541 100 C ATOM 3576 O GLN C 22 106.305 10.206 -2.386 1.00 82.43 O ANISOU 3576 O GLN C 22 19671 7155 4495 -2788 2669 -42 O ATOM 3577 CB GLN C 22 103.538 9.971 -3.986 1.00 81.92 C ANISOU 3577 CB GLN C 22 20543 6736 3847 -2130 1735 314 C ATOM 3578 CG GLN C 22 103.969 8.512 -3.841 1.00 93.30 C ANISOU 3578 CG GLN C 22 21392 8459 5599 -2197 1825 219 C ATOM 3579 CD GLN C 22 103.589 7.658 -5.023 1.00111.88 C ANISOU 3579 CD GLN C 22 24063 10704 7740 -2143 1699 217 C ATOM 3580 OE1 GLN C 22 102.540 7.837 -5.654 1.00108.53 O ANISOU 3580 OE1 GLN C 22 24041 10133 7064 -1917 1302 296 O ATOM 3581 NE2 GLN C 22 104.406 6.656 -5.301 1.00103.93 N ANISOU 3581 NE2 GLN C 22 22847 9788 6852 -2308 1983 93 N ATOM 3582 N VAL C 23 106.104 12.010 -3.750 1.00 84.67 N ANISOU 3582 N VAL C 23 21365 6772 4032 -3007 2910 57 N ATOM 3583 CA VAL C 23 107.533 12.254 -3.992 1.00 86.89 C ANISOU 3583 CA VAL C 23 21660 7022 4334 -3534 3579 -208 C ATOM 3584 C VAL C 23 108.274 12.684 -2.695 1.00 88.99 C ANISOU 3584 C VAL C 23 21270 7554 4988 -3704 3732 -373 C ATOM 3585 O VAL C 23 109.488 12.481 -2.606 1.00 90.45 O ANISOU 3585 O VAL C 23 21035 7919 5411 -4058 4175 -690 O ATOM 3586 CB VAL C 23 107.758 13.305 -5.113 1.00 95.91 C ANISOU 3586 CB VAL C 23 23920 7630 4894 -3867 3976 -210 C ATOM 3587 CG1 VAL C 23 107.394 12.734 -6.480 1.00 97.90 C ANISOU 3587 CG1 VAL C 23 24814 7628 4756 -3793 3937 -140 C ATOM 3588 CG2 VAL C 23 107.000 14.608 -4.844 1.00 96.70 C ANISOU 3588 CG2 VAL C 23 24673 7394 4674 -3695 3717 -5 C ATOM 3589 N LEU C 24 107.558 13.261 -1.709 1.00 82.40 N ANISOU 3589 N LEU C 24 20329 6754 4223 -3444 3360 -204 N ATOM 3590 CA LEU C 24 108.145 13.725 -0.449 1.00 81.18 C ANISOU 3590 CA LEU C 24 19654 6813 4378 -3572 3435 -338 C ATOM 3591 C LEU C 24 108.060 12.661 0.667 1.00 80.57 C ANISOU 3591 C LEU C 24 18692 7168 4755 -3271 3087 -352 C ATOM 3592 O LEU C 24 108.849 12.710 1.613 1.00 80.09 O ANISOU 3592 O LEU C 24 18108 7337 4986 -3388 3161 -550 O ATOM 3593 CB LEU C 24 107.435 15.006 0.011 1.00 81.60 C ANISOU 3593 CB LEU C 24 20198 6606 4200 -3463 3264 -157 C ATOM 3594 N LEU C 25 107.111 11.713 0.553 1.00 73.74 N ANISOU 3594 N LEU C 25 17720 6382 3916 -2902 2705 -166 N ATOM 3595 CA LEU C 25 106.858 10.650 1.534 1.00 69.81 C ANISOU 3595 CA LEU C 25 16588 6191 3744 -2629 2390 -142 C ATOM 3596 C LEU C 25 107.746 9.421 1.286 1.00 73.63 C ANISOU 3596 C LEU C 25 16670 6867 4440 -2671 2516 -344 C ATOM 3597 O LEU C 25 108.029 9.089 0.133 1.00 74.93 O ANISOU 3597 O LEU C 25 17074 6928 4469 -2799 2738 -414 O ATOM 3598 CB LEU C 25 105.378 10.243 1.479 1.00 67.66 C ANISOU 3598 CB LEU C 25 16428 5891 3389 -2290 1986 97 C ATOM 3599 CG LEU C 25 104.339 11.354 1.676 1.00 72.23 C ANISOU 3599 CG LEU C 25 17352 6304 3787 -2125 1783 251 C ATOM 3600 CD1 LEU C 25 103.008 10.954 1.111 1.00 72.06 C ANISOU 3600 CD1 LEU C 25 17469 6248 3662 -1833 1431 366 C ATOM 3601 CD2 LEU C 25 104.216 11.766 3.133 1.00 72.78 C ANISOU 3601 CD2 LEU C 25 17092 6511 4050 -2049 1690 262 C ATOM 3602 N SER C 26 108.164 8.736 2.372 1.00 68.66 N ANISOU 3602 N SER C 26 15493 6485 4110 -2523 2353 -445 N ATOM 3603 CA SER C 26 109.048 7.567 2.302 1.00 69.21 C ANISOU 3603 CA SER C 26 15168 6729 4397 -2456 2393 -675 C ATOM 3604 C SER C 26 108.368 6.277 2.808 1.00 70.27 C ANISOU 3604 C SER C 26 15184 6920 4597 -2116 2027 -522 C ATOM 3605 O SER C 26 108.519 5.236 2.168 1.00 70.48 O ANISOU 3605 O SER C 26 15204 6943 4634 -2035 2045 -579 O ATOM 3606 CB SER C 26 110.318 7.819 3.110 1.00 74.69 C ANISOU 3606 CB SER C 26 15374 7636 5368 -2539 2481 -1014 C ATOM 3607 OG SER C 26 111.260 6.769 2.966 1.00 85.18 O ANISOU 3607 OG SER C 26 16299 9141 6925 -2417 2504 -1315 O ATOM 3608 N SER C 27 107.664 6.333 3.960 1.00 64.33 N ANISOU 3608 N SER C 27 14384 6191 3868 -1952 1746 -355 N ATOM 3609 CA SER C 27 107.003 5.171 4.570 1.00 62.45 C ANISOU 3609 CA SER C 27 14124 5955 3649 -1715 1473 -228 C ATOM 3610 C SER C 27 105.687 5.556 5.274 1.00 63.84 C ANISOU 3610 C SER C 27 14439 6080 3736 -1677 1316 3 C ATOM 3611 O SER C 27 105.290 6.722 5.242 1.00 63.37 O ANISOU 3611 O SER C 27 14486 5984 3606 -1763 1370 68 O ATOM 3612 CB SER C 27 107.940 4.506 5.579 1.00 67.07 C ANISOU 3612 CB SER C 27 14439 6643 4400 -1521 1316 -406 C ATOM 3613 OG SER C 27 109.141 4.041 4.988 1.00 78.80 O ANISOU 3613 OG SER C 27 15693 8220 6026 -1490 1432 -698 O ATOM 3614 N TRP C 28 105.012 4.563 5.898 1.00 58.90 N ANISOU 3614 N TRP C 28 13845 5431 3105 -1558 1155 94 N ATOM 3615 CA TRP C 28 103.777 4.747 6.665 1.00 57.57 C ANISOU 3615 CA TRP C 28 13744 5241 2890 -1558 1076 235 C ATOM 3616 C TRP C 28 103.649 3.641 7.724 1.00 63.08 C ANISOU 3616 C TRP C 28 14521 5878 3567 -1479 982 255 C ATOM 3617 O TRP C 28 104.157 2.541 7.516 1.00 63.82 O ANISOU 3617 O TRP C 28 14690 5910 3648 -1397 933 204 O ATOM 3618 CB TRP C 28 102.531 4.780 5.750 1.00 55.80 C ANISOU 3618 CB TRP C 28 13599 4999 2603 -1616 1064 305 C ATOM 3619 CG TRP C 28 102.094 3.451 5.202 1.00 57.00 C ANISOU 3619 CG TRP C 28 13816 5111 2730 -1644 1028 299 C ATOM 3620 CD1 TRP C 28 102.465 2.890 4.016 1.00 60.45 C ANISOU 3620 CD1 TRP C 28 14347 5502 3117 -1659 1050 256 C ATOM 3621 CD2 TRP C 28 101.164 2.540 5.804 1.00 57.14 C ANISOU 3621 CD2 TRP C 28 13858 5104 2748 -1709 1006 313 C ATOM 3622 NE1 TRP C 28 101.847 1.670 3.855 1.00 60.28 N ANISOU 3622 NE1 TRP C 28 14406 5430 3069 -1706 1003 254 N ATOM 3623 CE2 TRP C 28 101.045 1.429 4.940 1.00 61.73 C ANISOU 3623 CE2 TRP C 28 14552 5621 3283 -1764 992 281 C ATOM 3624 CE3 TRP C 28 100.443 2.537 7.011 1.00 58.53 C ANISOU 3624 CE3 TRP C 28 14019 5284 2938 -1770 1050 328 C ATOM 3625 CZ2 TRP C 28 100.217 0.339 5.234 1.00 62.12 C ANISOU 3625 CZ2 TRP C 28 14695 5602 3304 -1906 1017 258 C ATOM 3626 CZ3 TRP C 28 99.632 1.453 7.305 1.00 61.19 C ANISOU 3626 CZ3 TRP C 28 14453 5553 3241 -1931 1119 296 C ATOM 3627 CH2 TRP C 28 99.528 0.369 6.425 1.00 62.65 C ANISOU 3627 CH2 TRP C 28 14750 5669 3386 -2011 1101 259 C ATOM 3628 N TYR C 29 102.963 3.929 8.846 1.00 60.11 N ANISOU 3628 N TYR C 29 14208 5480 3152 -1501 977 321 N ATOM 3629 CA TYR C 29 102.706 2.963 9.921 1.00 61.30 C ANISOU 3629 CA TYR C 29 14598 5497 3196 -1483 946 353 C ATOM 3630 C TYR C 29 101.456 3.402 10.713 1.00 66.16 C ANISOU 3630 C TYR C 29 15253 6110 3774 -1629 1081 401 C ATOM 3631 O TYR C 29 101.226 4.608 10.845 1.00 65.03 O ANISOU 3631 O TYR C 29 14952 6065 3691 -1626 1112 401 O ATOM 3632 CB TYR C 29 103.928 2.764 10.846 1.00 63.82 C ANISOU 3632 CB TYR C 29 15032 5750 3466 -1276 769 289 C ATOM 3633 CG TYR C 29 104.404 3.993 11.588 1.00 65.75 C ANISOU 3633 CG TYR C 29 15153 6080 3750 -1242 720 248 C ATOM 3634 CD1 TYR C 29 105.301 4.882 11.000 1.00 67.68 C ANISOU 3634 CD1 TYR C 29 15100 6474 4141 -1242 719 127 C ATOM 3635 CD2 TYR C 29 104.043 4.214 12.914 1.00 67.03 C ANISOU 3635 CD2 TYR C 29 15552 6142 3774 -1241 701 300 C ATOM 3636 CE1 TYR C 29 105.775 5.996 11.692 1.00 68.86 C ANISOU 3636 CE1 TYR C 29 15163 6684 4318 -1258 685 59 C ATOM 3637 CE2 TYR C 29 104.512 5.323 13.617 1.00 67.94 C ANISOU 3637 CE2 TYR C 29 15591 6318 3905 -1212 638 248 C ATOM 3638 CZ TYR C 29 105.380 6.210 13.002 1.00 75.06 C ANISOU 3638 CZ TYR C 29 16167 7379 4972 -1224 617 125 C ATOM 3639 OH TYR C 29 105.849 7.304 13.685 1.00 76.65 O ANISOU 3639 OH TYR C 29 16314 7626 5185 -1248 571 47 O ATOM 3640 N PRO C 30 100.608 2.465 11.208 1.00 64.83 N ANISOU 3640 N PRO C 30 15305 5822 3506 -1781 1205 409 N ATOM 3641 CA PRO C 30 99.395 2.895 11.921 1.00 65.91 C ANISOU 3641 CA PRO C 30 15402 5994 3649 -1963 1414 375 C ATOM 3642 C PRO C 30 99.659 3.234 13.386 1.00 72.24 C ANISOU 3642 C PRO C 30 16485 6669 4295 -1932 1459 411 C ATOM 3643 O PRO C 30 100.698 2.867 13.941 1.00 72.24 O ANISOU 3643 O PRO C 30 16784 6516 4147 -1769 1285 457 O ATOM 3644 CB PRO C 30 98.453 1.686 11.803 1.00 69.44 C ANISOU 3644 CB PRO C 30 15984 6352 4047 -2230 1602 310 C ATOM 3645 CG PRO C 30 99.255 0.583 11.175 1.00 73.61 C ANISOU 3645 CG PRO C 30 16746 6736 4488 -2146 1458 358 C ATOM 3646 CD PRO C 30 100.687 0.994 11.140 1.00 67.73 C ANISOU 3646 CD PRO C 30 15996 5995 3743 -1827 1209 414 C ATOM 3647 N THR C 31 98.699 3.944 14.007 1.00 70.95 N ANISOU 3647 N THR C 31 16223 6570 4163 -2059 1671 354 N ATOM 3648 CA THR C 31 98.743 4.338 15.419 1.00 72.63 C ANISOU 3648 CA THR C 31 16744 6650 4201 -2075 1776 371 C ATOM 3649 C THR C 31 98.441 3.123 16.302 1.00 80.18 C ANISOU 3649 C THR C 31 18261 7322 4883 -2284 1981 377 C ATOM 3650 O THR C 31 97.758 2.196 15.859 1.00 80.97 O ANISOU 3650 O THR C 31 18383 7385 4996 -2517 2164 316 O ATOM 3651 CB THR C 31 97.759 5.491 15.703 1.00 82.45 C ANISOU 3651 CB THR C 31 17693 8054 5579 -2132 1978 270 C ATOM 3652 OG1 THR C 31 96.429 5.076 15.380 1.00 85.06 O ANISOU 3652 OG1 THR C 31 17777 8495 6046 -2368 2247 104 O ATOM 3653 CG2 THR C 31 98.112 6.772 14.950 1.00 78.82 C ANISOU 3653 CG2 THR C 31 16884 7770 5294 -1905 1768 284 C ATOM 3654 N SER C 32 98.945 3.138 17.549 1.00 79.07 N ANISOU 3654 N SER C 32 18642 6945 4457 -2218 1948 436 N ATOM 3655 CA SER C 32 98.752 2.071 18.535 1.00 82.92 C ANISOU 3655 CA SER C 32 19888 7053 4563 -2395 2135 462 C ATOM 3656 C SER C 32 97.273 1.935 18.933 1.00 90.60 C ANISOU 3656 C SER C 32 20885 8012 5526 -2860 2713 321 C ATOM 3657 O SER C 32 96.524 2.914 18.858 1.00 89.54 O ANISOU 3657 O SER C 32 20223 8152 5646 -2935 2904 196 O ATOM 3658 CB SER C 32 99.599 2.347 19.774 1.00 87.87 C ANISOU 3658 CB SER C 32 21079 7440 4868 -2171 1912 535 C ATOM 3659 OG SER C 32 99.489 1.315 20.741 1.00100.79 O ANISOU 3659 OG SER C 32 23631 8625 6040 -2298 2048 577 O ATOM 3660 N GLN C 33 96.864 0.720 19.368 1.00 91.64 N ANISOU 3660 N GLN C 33 21653 7809 5359 -3175 3007 303 N ATOM 3661 CA GLN C 33 95.499 0.407 19.822 1.00 95.70 C ANISOU 3661 CA GLN C 33 22259 8269 5834 -3727 3656 100 C ATOM 3662 C GLN C 33 95.156 1.181 21.105 1.00102.04 C ANISOU 3662 C GLN C 33 23333 8981 6456 -3833 3964 45 C ATOM 3663 O GLN C 33 93.981 1.325 21.450 1.00104.72 O ANISOU 3663 O GLN C 33 23491 9410 6887 -4255 4536 -201 O ATOM 3664 CB GLN C 33 95.319 -1.107 20.063 1.00101.31 C ANISOU 3664 CB GLN C 33 23788 8536 6168 -4078 3921 108 C ATOM 3665 CG GLN C 33 95.415 -1.993 18.815 1.00120.33 C ANISOU 3665 CG GLN C 33 25972 11007 8741 -4082 3741 109 C ATOM 3666 CD GLN C 33 96.817 -2.445 18.457 1.00141.45 C ANISOU 3666 CD GLN C 33 28980 13501 11262 -3559 3135 340 C ATOM 3667 OE1 GLN C 33 97.814 -1.730 18.630 1.00135.11 O ANISOU 3667 OE1 GLN C 33 28071 12781 10482 -3084 2692 459 O ATOM 3668 NE2 GLN C 33 96.915 -3.645 17.901 1.00135.75 N ANISOU 3668 NE2 GLN C 33 28615 12551 10414 -3644 3112 359 N ATOM 3669 N LEU C 34 96.198 1.676 21.797 1.00 97.60 N ANISOU 3669 N LEU C 34 23177 8256 5651 -3451 3582 229 N ATOM 3670 CA LEU C 34 96.128 2.446 23.035 1.00 99.34 C ANISOU 3670 CA LEU C 34 23767 8343 5635 -3465 3754 216 C ATOM 3671 C LEU C 34 95.613 3.874 22.786 1.00100.99 C ANISOU 3671 C LEU C 34 23114 8989 6267 -3386 3833 79 C ATOM 3672 O LEU C 34 95.057 4.481 23.702 1.00103.09 O ANISOU 3672 O LEU C 34 23535 9207 6426 -3542 4200 -33 O ATOM 3673 CB LEU C 34 97.528 2.498 23.684 1.00 99.07 C ANISOU 3673 CB LEU C 34 24363 8035 5245 -3016 3174 422 C ATOM 3674 CG LEU C 34 98.191 1.151 24.027 1.00106.81 C ANISOU 3674 CG LEU C 34 26316 8523 5744 -2925 2948 552 C ATOM 3675 CD1 LEU C 34 99.686 1.300 24.189 1.00105.86 C ANISOU 3675 CD1 LEU C 34 26383 8335 5505 -2329 2182 664 C ATOM 3676 CD2 LEU C 34 97.568 0.509 25.262 1.00115.37 C ANISOU 3676 CD2 LEU C 34 28512 9078 6245 -3319 3457 536 C ATOM 3677 N CYS C 35 95.797 4.401 21.554 1.00 93.40 N ANISOU 3677 N CYS C 35 21333 8410 5745 -3132 3499 81 N ATOM 3678 CA CYS C 35 95.389 5.751 21.148 1.00 91.19 C ANISOU 3678 CA CYS C 35 20321 8493 5835 -2971 3475 -32 C ATOM 3679 C CYS C 35 93.868 5.862 21.039 1.00 97.44 C ANISOU 3679 C CYS C 35 20625 9506 6890 -3279 3995 -346 C ATOM 3680 O CYS C 35 93.203 4.920 20.602 1.00 99.10 O ANISOU 3680 O CYS C 35 20715 9751 7186 -3587 4238 -486 O ATOM 3681 CB CYS C 35 96.051 6.137 19.830 1.00 87.37 C ANISOU 3681 CB CYS C 35 19296 8257 5645 -2643 2988 63 C ATOM 3682 SG CYS C 35 97.856 6.220 19.909 1.00 88.78 S ANISOU 3682 SG CYS C 35 19812 8285 5634 -2285 2410 298 S ATOM 3683 N SER C 36 93.334 7.042 21.409 1.00 94.09 N ANISOU 3683 N SER C 36 19883 9248 6618 -3179 4145 -499 N ATOM 3684 CA SER C 36 91.907 7.367 21.377 1.00 97.06 C ANISOU 3684 CA SER C 36 19681 9893 7306 -3368 4596 -886 C ATOM 3685 C SER C 36 91.396 7.504 19.940 1.00 98.98 C ANISOU 3685 C SER C 36 19095 10512 7999 -3190 4330 -1041 C ATOM 3686 O SER C 36 90.284 7.059 19.650 1.00101.98 O ANISOU 3686 O SER C 36 19009 11104 8634 -3456 4645 -1389 O ATOM 3687 CB SER C 36 91.638 8.656 22.146 1.00101.91 C ANISOU 3687 CB SER C 36 20236 10549 7936 -3190 4739 -996 C ATOM 3688 OG SER C 36 92.026 8.535 23.504 1.00113.20 O ANISOU 3688 OG SER C 36 22477 11617 8915 -3371 4997 -885 O ATOM 3689 N LYS C 37 92.202 8.118 19.047 1.00 90.75 N ANISOU 3689 N LYS C 37 17900 9542 7039 -2767 3763 -818 N ATOM 3690 CA LYS C 37 91.852 8.324 17.639 1.00 89.12 C ANISOU 3690 CA LYS C 37 17080 9617 7164 -2538 3432 -917 C ATOM 3691 C LYS C 37 92.666 7.401 16.716 1.00 89.11 C ANISOU 3691 C LYS C 37 17234 9537 7087 -2554 3117 -683 C ATOM 3692 O LYS C 37 93.899 7.393 16.802 1.00 85.59 O ANISOU 3692 O LYS C 37 17205 8894 6420 -2426 2870 -383 O ATOM 3693 CB LYS C 37 92.060 9.790 17.215 1.00 89.95 C ANISOU 3693 CB LYS C 37 16985 9813 7377 -2062 3081 -874 C ATOM 3694 CG LYS C 37 91.028 10.770 17.754 1.00106.90 C ANISOU 3694 CG LYS C 37 18806 12109 9702 -1924 3308 -1192 C ATOM 3695 CD LYS C 37 91.246 12.157 17.163 1.00114.81 C ANISOU 3695 CD LYS C 37 19722 13134 10765 -1417 2902 -1134 C ATOM 3696 CE LYS C 37 90.199 13.144 17.609 1.00129.07 C ANISOU 3696 CE LYS C 37 21199 15081 12761 -1179 3067 -1482 C ATOM 3697 NZ LYS C 37 90.412 14.481 16.997 1.00137.08 N ANISOU 3697 NZ LYS C 37 22273 16038 13774 -657 2646 -1414 N ATOM 3698 N PRO C 38 92.004 6.636 15.809 1.00 86.23 N ANISOU 3698 N PRO C 38 16505 9338 6920 -2699 3110 -859 N ATOM 3699 CA PRO C 38 92.768 5.772 14.892 1.00 83.07 C ANISOU 3699 CA PRO C 38 16276 8849 6438 -2698 2826 -650 C ATOM 3700 C PRO C 38 93.295 6.551 13.685 1.00 82.73 C ANISOU 3700 C PRO C 38 16027 8912 6495 -2292 2343 -527 C ATOM 3701 O PRO C 38 92.726 7.577 13.307 1.00 83.01 O ANISOU 3701 O PRO C 38 15711 9123 6708 -2032 2202 -671 O ATOM 3702 CB PRO C 38 91.747 4.714 14.471 1.00 88.12 C ANISOU 3702 CB PRO C 38 16637 9612 7233 -3060 3052 -932 C ATOM 3703 CG PRO C 38 90.422 5.393 14.584 1.00 96.49 C ANISOU 3703 CG PRO C 38 17071 10981 8611 -3066 3238 -1347 C ATOM 3704 CD PRO C 38 90.548 6.531 15.566 1.00 92.00 C ANISOU 3704 CD PRO C 38 16617 10363 7974 -2865 3346 -1305 C ATOM 3705 N GLY C 39 94.373 6.049 13.091 1.00 75.78 N ANISOU 3705 N GLY C 39 15418 7897 5478 -2235 2109 -285 N ATOM 3706 CA GLY C 39 94.991 6.667 11.923 1.00 72.88 C ANISOU 3706 CA GLY C 39 14976 7572 5144 -1941 1741 -168 C ATOM 3707 C GLY C 39 96.359 6.122 11.576 1.00 72.80 C ANISOU 3707 C GLY C 39 15286 7400 4974 -1919 1593 59 C ATOM 3708 O GLY C 39 96.820 5.146 12.177 1.00 72.48 O ANISOU 3708 O GLY C 39 15532 7209 4798 -2070 1698 128 O ATOM 3709 N VAL C 40 97.011 6.757 10.589 1.00 66.43 N ANISOU 3709 N VAL C 40 14466 6605 4169 -1719 1358 143 N ATOM 3710 CA VAL C 40 98.346 6.380 10.119 1.00 63.83 C ANISOU 3710 CA VAL C 40 14336 6172 3744 -1690 1248 279 C ATOM 3711 C VAL C 40 99.287 7.588 10.204 1.00 65.10 C ANISOU 3711 C VAL C 40 14583 6294 3859 -1561 1181 346 C ATOM 3712 O VAL C 40 98.850 8.737 10.091 1.00 64.84 O ANISOU 3712 O VAL C 40 14513 6283 3842 -1455 1156 321 O ATOM 3713 CB VAL C 40 98.357 5.768 8.691 1.00 67.55 C ANISOU 3713 CB VAL C 40 14765 6668 4235 -1690 1126 266 C ATOM 3714 CG1 VAL C 40 97.800 4.350 8.695 1.00 68.44 C ANISOU 3714 CG1 VAL C 40 14883 6766 4356 -1880 1209 205 C ATOM 3715 CG2 VAL C 40 97.628 6.649 7.675 1.00 68.16 C ANISOU 3715 CG2 VAL C 40 14716 6826 4356 -1546 973 199 C ATOM 3716 N ILE C 41 100.579 7.309 10.413 1.00 60.10 N ANISOU 3716 N ILE C 41 14066 5595 3172 -1567 1147 389 N ATOM 3717 CA ILE C 41 101.624 8.320 10.521 1.00 59.31 C ANISOU 3717 CA ILE C 41 14007 5476 3053 -1532 1120 384 C ATOM 3718 C ILE C 41 102.572 8.150 9.320 1.00 62.99 C ANISOU 3718 C ILE C 41 14446 5948 3539 -1559 1103 348 C ATOM 3719 O ILE C 41 103.306 7.160 9.244 1.00 62.69 O ANISOU 3719 O ILE C 41 14371 5919 3528 -1550 1064 303 O ATOM 3720 CB ILE C 41 102.352 8.223 11.898 1.00 62.67 C ANISOU 3720 CB ILE C 41 14524 5859 3429 -1518 1083 364 C ATOM 3721 CG1 ILE C 41 101.347 8.390 13.075 1.00 63.75 C ANISOU 3721 CG1 ILE C 41 14775 5952 3497 -1535 1179 392 C ATOM 3722 CG2 ILE C 41 103.487 9.245 11.989 1.00 63.41 C ANISOU 3722 CG2 ILE C 41 14586 5966 3539 -1534 1049 287 C ATOM 3723 CD1 ILE C 41 101.856 8.008 14.491 1.00 71.08 C ANISOU 3723 CD1 ILE C 41 15955 6770 4283 -1516 1126 390 C ATOM 3724 N PHE C 42 102.519 9.105 8.370 1.00 59.70 N ANISOU 3724 N PHE C 42 14111 5494 3079 -1581 1146 351 N ATOM 3725 CA PHE C 42 103.353 9.103 7.170 1.00 60.11 C ANISOU 3725 CA PHE C 42 14229 5511 3099 -1670 1223 298 C ATOM 3726 C PHE C 42 104.742 9.659 7.466 1.00 65.01 C ANISOU 3726 C PHE C 42 14791 6147 3764 -1803 1343 164 C ATOM 3727 O PHE C 42 104.875 10.814 7.874 1.00 65.09 O ANISOU 3727 O PHE C 42 14905 6101 3727 -1873 1404 149 O ATOM 3728 CB PHE C 42 102.706 9.906 6.024 1.00 62.85 C ANISOU 3728 CB PHE C 42 14844 5737 3298 -1649 1224 349 C ATOM 3729 CG PHE C 42 101.529 9.254 5.338 1.00 64.53 C ANISOU 3729 CG PHE C 42 15059 5969 3490 -1525 1063 389 C ATOM 3730 CD1 PHE C 42 101.714 8.177 4.478 1.00 67.62 C ANISOU 3730 CD1 PHE C 42 15445 6373 3875 -1574 1059 369 C ATOM 3731 CD2 PHE C 42 100.247 9.769 5.483 1.00 67.34 C ANISOU 3731 CD2 PHE C 42 15409 6336 3840 -1351 905 396 C ATOM 3732 CE1 PHE C 42 100.626 7.581 3.835 1.00 69.08 C ANISOU 3732 CE1 PHE C 42 15622 6583 4043 -1492 888 366 C ATOM 3733 CE2 PHE C 42 99.162 9.184 4.823 1.00 71.02 C ANISOU 3733 CE2 PHE C 42 15793 6864 4327 -1245 720 350 C ATOM 3734 CZ PHE C 42 99.358 8.091 4.009 1.00 69.02 C ANISOU 3734 CZ PHE C 42 15545 6621 4058 -1337 708 340 C ATOM 3735 N LEU C 43 105.773 8.832 7.251 1.00 62.49 N ANISOU 3735 N LEU C 43 14286 5911 3548 -1836 1373 21 N ATOM 3736 CA LEU C 43 107.170 9.209 7.440 1.00 64.27 C ANISOU 3736 CA LEU C 43 14314 6219 3885 -1969 1481 -221 C ATOM 3737 C LEU C 43 107.720 9.745 6.118 1.00 69.91 C ANISOU 3737 C LEU C 43 15153 6867 4542 -2222 1788 -333 C ATOM 3738 O LEU C 43 107.798 9.004 5.136 1.00 69.88 O ANISOU 3738 O LEU C 43 15177 6852 4520 -2223 1868 -354 O ATOM 3739 CB LEU C 43 107.989 8.002 7.955 1.00 65.20 C ANISOU 3739 CB LEU C 43 14136 6472 4164 -1797 1312 -388 C ATOM 3740 CG LEU C 43 109.500 8.195 8.173 1.00 72.92 C ANISOU 3740 CG LEU C 43 14752 7614 5339 -1866 1347 -755 C ATOM 3741 CD1 LEU C 43 109.786 9.063 9.390 1.00 73.80 C ANISOU 3741 CD1 LEU C 43 14796 7767 5477 -1894 1221 -833 C ATOM 3742 CD2 LEU C 43 110.190 6.858 8.352 1.00 77.06 C ANISOU 3742 CD2 LEU C 43 15033 8243 6004 -1584 1131 -937 C ATOM 3743 N THR C 44 108.064 11.040 6.086 1.00 68.00 N ANISOU 3743 N THR C 44 15072 6538 4226 -2463 1989 -404 N ATOM 3744 CA THR C 44 108.601 11.702 4.892 1.00 70.43 C ANISOU 3744 CA THR C 44 15653 6704 4402 -2788 2365 -522 C ATOM 3745 C THR C 44 110.092 11.380 4.718 1.00 77.70 C ANISOU 3745 C THR C 44 16152 7817 5555 -3024 2619 -921 C ATOM 3746 O THR C 44 110.746 10.961 5.677 1.00 77.56 O ANISOU 3746 O THR C 44 15641 8033 5794 -2908 2436 -1121 O ATOM 3747 CB THR C 44 108.392 13.231 4.975 1.00 77.83 C ANISOU 3747 CB THR C 44 17032 7412 5129 -2986 2513 -463 C ATOM 3748 OG1 THR C 44 109.108 13.748 6.095 1.00 77.08 O ANISOU 3748 OG1 THR C 44 16640 7445 5201 -3111 2513 -652 O ATOM 3749 CG2 THR C 44 106.923 13.633 5.053 1.00 74.02 C ANISOU 3749 CG2 THR C 44 16938 6748 4437 -2695 2253 -143 C ATOM 3750 N LYS C 45 110.632 11.611 3.499 1.00 77.50 N ANISOU 3750 N LYS C 45 16341 7682 5424 -3348 3042 -1076 N ATOM 3751 CA LYS C 45 112.057 11.433 3.177 1.00 81.41 C ANISOU 3751 CA LYS C 45 16408 8367 6155 -3650 3406 -1546 C ATOM 3752 C LYS C 45 112.900 12.446 3.970 1.00 88.39 C ANISOU 3752 C LYS C 45 17036 9354 7192 -3966 3557 -1852 C ATOM 3753 O LYS C 45 114.070 12.193 4.265 1.00 91.20 O ANISOU 3753 O LYS C 45 16760 10006 7886 -4088 3655 -2319 O ATOM 3754 CB LYS C 45 112.308 11.585 1.665 1.00 86.81 C ANISOU 3754 CB LYS C 45 17528 8841 6613 -4001 3919 -1628 C ATOM 3755 CG LYS C 45 111.706 10.481 0.800 1.00 98.90 C ANISOU 3755 CG LYS C 45 19245 10307 8025 -3730 3794 -1429 C ATOM 3756 CD LYS C 45 112.030 10.703 -0.677 1.00113.14 C ANISOU 3756 CD LYS C 45 21570 11867 9551 -4108 4331 -1536 C ATOM 3757 CE LYS C 45 111.565 9.588 -1.588 1.00124.17 C ANISOU 3757 CE LYS C 45 23150 13202 10828 -3876 4231 -1399 C ATOM 3758 NZ LYS C 45 110.083 9.510 -1.691 1.00130.52 N ANISOU 3758 NZ LYS C 45 24430 13807 11356 -3533 3760 -937 N ATOM 3759 N ARG C 46 112.268 13.583 4.329 1.00 84.26 N ANISOU 3759 N ARG C 46 16996 8592 6428 -4067 3537 -1617 N ATOM 3760 CA ARG C 46 112.793 14.703 5.117 1.00 86.31 C ANISOU 3760 CA ARG C 46 17200 8855 6737 -4372 3649 -1817 C ATOM 3761 C ARG C 46 113.109 14.279 6.556 1.00 88.73 C ANISOU 3761 C ARG C 46 16870 9483 7360 -4076 3191 -1955 C ATOM 3762 O ARG C 46 113.992 14.865 7.187 1.00 91.32 O ANISOU 3762 O ARG C 46 16868 9960 7870 -4343 3266 -2320 O ATOM 3763 CB ARG C 46 111.757 15.843 5.134 1.00 85.89 C ANISOU 3763 CB ARG C 46 17934 8408 6291 -4382 3634 -1441 C ATOM 3764 CG ARG C 46 111.445 16.434 3.759 1.00100.30 C ANISOU 3764 CG ARG C 46 20578 9824 7707 -4642 4025 -1307 C ATOM 3765 CD ARG C 46 110.033 16.993 3.659 1.00109.52 C ANISOU 3765 CD ARG C 46 22464 10643 8503 -4299 3739 -854 C ATOM 3766 NE ARG C 46 109.810 18.162 4.513 1.00118.62 N ANISOU 3766 NE ARG C 46 23891 11630 9548 -4346 3684 -800 N ATOM 3767 CZ ARG C 46 109.990 19.422 4.126 1.00136.43 C ANISOU 3767 CZ ARG C 46 26882 13487 11470 -4717 4034 -835 C ATOM 3768 NH1 ARG C 46 110.406 19.695 2.895 1.00124.87 N ANISOU 3768 NH1 ARG C 46 25996 11729 9719 -5107 4496 -924 N ATOM 3769 NH2 ARG C 46 109.760 20.420 4.970 1.00124.98 N ANISOU 3769 NH2 ARG C 46 25674 11884 9929 -4719 3952 -786 N ATOM 3770 N GLY C 47 112.364 13.290 7.056 1.00 81.20 N ANISOU 3770 N GLY C 47 15821 8600 6431 -3554 2726 -1677 N ATOM 3771 CA GLY C 47 112.501 12.750 8.404 1.00 79.92 C ANISOU 3771 CA GLY C 47 15260 8648 6456 -3205 2250 -1734 C ATOM 3772 C GLY C 47 111.280 12.963 9.276 1.00 79.86 C ANISOU 3772 C GLY C 47 15622 8477 6243 -2930 1947 -1319 C ATOM 3773 O GLY C 47 111.009 12.152 10.165 1.00 77.77 O ANISOU 3773 O GLY C 47 15229 8295 6024 -2568 1566 -1229 O ATOM 3774 N ARG C 48 110.538 14.063 9.028 1.00 75.76 N ANISOU 3774 N ARG C 48 15611 7698 5475 -3097 2134 -1092 N ATOM 3775 CA ARG C 48 109.340 14.459 9.778 1.00 73.02 C ANISOU 3775 CA ARG C 48 15602 7196 4948 -2862 1923 -761 C ATOM 3776 C ARG C 48 108.171 13.495 9.518 1.00 74.12 C ANISOU 3776 C ARG C 48 15835 7307 5021 -2517 1739 -459 C ATOM 3777 O ARG C 48 108.100 12.860 8.467 1.00 73.30 O ANISOU 3777 O ARG C 48 15739 7201 4912 -2509 1826 -428 O ATOM 3778 CB ARG C 48 108.923 15.914 9.473 1.00 73.83 C ANISOU 3778 CB ARG C 48 16239 7009 4804 -3081 2159 -659 C ATOM 3779 CG ARG C 48 109.152 16.407 8.040 1.00 84.37 C ANISOU 3779 CG ARG C 48 17948 8138 5972 -3386 2539 -696 C ATOM 3780 CD ARG C 48 109.296 17.922 7.986 1.00 93.68 C ANISOU 3780 CD ARG C 48 19659 9017 6919 -3716 2811 -739 C ATOM 3781 NE ARG C 48 110.474 18.387 8.728 1.00101.98 N ANISOU 3781 NE ARG C 48 20381 10216 8153 -4083 2946 -1101 N ATOM 3782 CZ ARG C 48 111.625 18.760 8.177 1.00118.29 C ANISOU 3782 CZ ARG C 48 22367 12296 10282 -4613 3366 -1466 C ATOM 3783 NH1 ARG C 48 111.763 18.777 6.858 1.00106.20 N ANISOU 3783 NH1 ARG C 48 21178 10584 8587 -4861 3747 -1481 N ATOM 3784 NH2 ARG C 48 112.636 19.155 8.940 1.00107.45 N ANISOU 3784 NH2 ARG C 48 20596 11109 9122 -4928 3428 -1854 N ATOM 3785 N GLN C 49 107.282 13.374 10.522 1.00 69.54 N ANISOU 3785 N GLN C 49 15322 6710 4392 -2269 1511 -276 N ATOM 3786 CA GLN C 49 106.125 12.473 10.556 1.00 67.46 C ANISOU 3786 CA GLN C 49 15096 6444 4093 -2004 1363 -56 C ATOM 3787 C GLN C 49 104.806 13.263 10.515 1.00 71.56 C ANISOU 3787 C GLN C 49 15909 6815 4467 -1904 1384 131 C ATOM 3788 O GLN C 49 104.686 14.284 11.192 1.00 71.73 O ANISOU 3788 O GLN C 49 16093 6746 4415 -1927 1410 130 O ATOM 3789 CB GLN C 49 106.197 11.608 11.826 1.00 68.41 C ANISOU 3789 CB GLN C 49 15073 6652 4266 -1831 1136 -69 C ATOM 3790 CG GLN C 49 107.434 10.698 11.875 1.00 81.11 C ANISOU 3790 CG GLN C 49 16397 8403 6019 -1791 1005 -287 C ATOM 3791 CD GLN C 49 107.675 10.022 13.205 1.00 94.83 C ANISOU 3791 CD GLN C 49 18143 10157 7733 -1578 711 -329 C ATOM 3792 OE1 GLN C 49 106.763 9.793 14.006 1.00 88.85 O ANISOU 3792 OE1 GLN C 49 17644 9288 6828 -1475 655 -147 O ATOM 3793 NE2 GLN C 49 108.921 9.652 13.452 1.00 87.09 N ANISOU 3793 NE2 GLN C 49 16901 9305 6884 -1497 516 -608 N ATOM 3794 N VAL C 50 103.826 12.799 9.707 1.00 68.44 N ANISOU 3794 N VAL C 50 15568 6399 4039 -1771 1348 250 N ATOM 3795 CA VAL C 50 102.542 13.490 9.515 1.00 69.18 C ANISOU 3795 CA VAL C 50 15861 6389 4035 -1598 1300 347 C ATOM 3796 C VAL C 50 101.353 12.525 9.737 1.00 73.52 C ANISOU 3796 C VAL C 50 16198 7061 4676 -1428 1189 388 C ATOM 3797 O VAL C 50 101.324 11.441 9.155 1.00 72.77 O ANISOU 3797 O VAL C 50 15973 7041 4635 -1448 1152 392 O ATOM 3798 CB VAL C 50 102.463 14.143 8.093 1.00 74.64 C ANISOU 3798 CB VAL C 50 16900 6900 4559 -1603 1336 373 C ATOM 3799 CG1 VAL C 50 101.096 14.775 7.826 1.00 75.57 C ANISOU 3799 CG1 VAL C 50 17217 6917 4581 -1302 1168 426 C ATOM 3800 CG2 VAL C 50 103.568 15.178 7.885 1.00 76.19 C ANISOU 3800 CG2 VAL C 50 17392 6926 4629 -1869 1549 300 C ATOM 3801 N CYS C 51 100.357 12.959 10.540 1.00 71.39 N ANISOU 3801 N CYS C 51 15902 6802 4422 -1291 1175 380 N ATOM 3802 CA CYS C 51 99.120 12.216 10.815 1.00 72.00 C ANISOU 3802 CA CYS C 51 15744 7005 4606 -1200 1155 336 C ATOM 3803 C CYS C 51 98.168 12.310 9.627 1.00 76.08 C ANISOU 3803 C CYS C 51 16214 7548 5144 -1020 1002 285 C ATOM 3804 O CYS C 51 98.203 13.297 8.890 1.00 76.60 O ANISOU 3804 O CYS C 51 16542 7473 5088 -876 899 302 O ATOM 3805 CB CYS C 51 98.446 12.730 12.083 1.00 73.88 C ANISOU 3805 CB CYS C 51 15952 7254 4863 -1141 1258 278 C ATOM 3806 SG CYS C 51 99.174 12.115 13.620 1.00 77.48 S ANISOU 3806 SG CYS C 51 16492 7688 5260 -1329 1385 310 S ATOM 3807 N ALA C 52 97.286 11.298 9.472 1.00 72.41 N ANISOU 3807 N ALA C 52 15465 7237 4811 -1031 975 196 N ATOM 3808 CA ALA C 52 96.280 11.224 8.407 1.00 73.71 C ANISOU 3808 CA ALA C 52 15499 7476 5030 -850 762 78 C ATOM 3809 C ALA C 52 95.166 10.233 8.750 1.00 78.17 C ANISOU 3809 C ALA C 52 15645 8257 5800 -941 824 -113 C ATOM 3810 O ALA C 52 95.423 9.219 9.405 1.00 76.63 O ANISOU 3810 O ALA C 52 15401 8084 5630 -1213 1034 -80 O ATOM 3811 CB ALA C 52 96.934 10.822 7.096 1.00 73.77 C ANISOU 3811 CB ALA C 52 15720 7394 4914 -892 643 170 C ATOM 3812 N ASP C 53 93.928 10.533 8.307 1.00 77.31 N ANISOU 3812 N ASP C 53 15257 8290 5827 -713 634 -350 N ATOM 3813 CA ASP C 53 92.760 9.676 8.527 1.00 79.46 C ANISOU 3813 CA ASP C 53 15041 8810 6342 -845 715 -637 C ATOM 3814 C ASP C 53 92.753 8.544 7.500 1.00 83.72 C ANISOU 3814 C ASP C 53 15538 9390 6882 -998 585 -652 C ATOM 3815 O ASP C 53 92.844 8.811 6.301 1.00 83.61 O ANISOU 3815 O ASP C 53 15687 9315 6765 -777 252 -621 O ATOM 3816 CB ASP C 53 91.452 10.494 8.458 1.00 85.23 C ANISOU 3816 CB ASP C 53 15386 9726 7272 -496 522 -982 C ATOM 3817 CG ASP C 53 90.173 9.703 8.696 1.00 96.67 C ANISOU 3817 CG ASP C 53 16203 11490 9037 -670 648 -1398 C ATOM 3818 OD1 ASP C 53 90.199 8.754 9.515 1.00 96.30 O ANISOU 3818 OD1 ASP C 53 16085 11471 9033 -1125 1069 -1407 O ATOM 3819 OD2 ASP C 53 89.134 10.069 8.109 1.00105.75 O ANISOU 3819 OD2 ASP C 53 16951 12845 10383 -351 330 -1751 O ATOM 3820 N LYS C 54 92.639 7.285 7.971 1.00 80.74 N ANISOU 3820 N LYS C 54 15034 9070 6576 -1384 858 -702 N ATOM 3821 CA LYS C 54 92.633 6.078 7.128 1.00 80.84 C ANISOU 3821 CA LYS C 54 15045 9092 6578 -1588 791 -726 C ATOM 3822 C LYS C 54 91.387 5.999 6.223 1.00 88.62 C ANISOU 3822 C LYS C 54 15604 10311 7757 -1474 501 -1081 C ATOM 3823 O LYS C 54 91.447 5.347 5.180 1.00 88.39 O ANISOU 3823 O LYS C 54 15655 10262 7666 -1513 295 -1085 O ATOM 3824 CB LYS C 54 92.715 4.805 7.989 1.00 83.34 C ANISOU 3824 CB LYS C 54 15426 9353 6885 -2031 1180 -720 C ATOM 3825 CG LYS C 54 94.086 4.592 8.628 1.00 95.71 C ANISOU 3825 CG LYS C 54 17473 10666 8225 -2082 1323 -389 C ATOM 3826 CD LYS C 54 94.217 3.284 9.424 1.00106.76 C ANISOU 3826 CD LYS C 54 19119 11919 9526 -2443 1631 -365 C ATOM 3827 CE LYS C 54 93.572 3.313 10.791 1.00119.09 C ANISOU 3827 CE LYS C 54 20667 13477 11104 -2668 1997 -492 C ATOM 3828 NZ LYS C 54 93.842 2.064 11.549 1.00128.87 N ANISOU 3828 NZ LYS C 54 22374 14460 12132 -2999 2282 -423 N ATOM 3829 N SER C 55 90.280 6.665 6.612 1.00 88.72 N ANISOU 3829 N SER C 55 15153 10551 8005 -1309 459 -1416 N ATOM 3830 CA SER C 55 89.018 6.682 5.866 1.00 93.36 C ANISOU 3830 CA SER C 55 15213 11420 8838 -1132 121 -1862 C ATOM 3831 C SER C 55 89.102 7.546 4.590 1.00 97.52 C ANISOU 3831 C SER C 55 15990 11859 9205 -585 -488 -1808 C ATOM 3832 O SER C 55 88.320 7.318 3.663 1.00100.93 O ANISOU 3832 O SER C 55 16156 12455 9739 -426 -892 -2113 O ATOM 3833 CB SER C 55 87.886 7.192 6.752 1.00101.23 C ANISOU 3833 CB SER C 55 15605 12698 10160 -1074 283 -2290 C ATOM 3834 OG SER C 55 87.685 6.334 7.863 1.00110.98 O ANISOU 3834 OG SER C 55 16682 13985 11501 -1640 889 -2391 O ATOM 3835 N LYS C 56 90.038 8.524 4.543 1.00 90.61 N ANISOU 3835 N LYS C 56 15676 10701 8052 -323 -552 -1449 N ATOM 3836 CA LYS C 56 90.235 9.429 3.402 1.00 91.15 C ANISOU 3836 CA LYS C 56 16204 10568 7859 150 -1044 -1351 C ATOM 3837 C LYS C 56 90.725 8.665 2.166 1.00 93.67 C ANISOU 3837 C LYS C 56 16882 10751 7958 34 -1225 -1212 C ATOM 3838 O LYS C 56 91.554 7.760 2.281 1.00 89.77 O ANISOU 3838 O LYS C 56 16537 10175 7396 -374 -891 -992 O ATOM 3839 CB LYS C 56 91.224 10.546 3.754 1.00 90.75 C ANISOU 3839 CB LYS C 56 16725 10210 7546 288 -916 -1008 C ATOM 3840 N ASP C 57 90.198 9.045 0.989 1.00 93.64 N ANISOU 3840 N ASP C 57 17057 10703 7820 438 -1783 -1364 N ATOM 3841 CA ASP C 57 90.477 8.431 -0.312 1.00 93.83 C ANISOU 3841 CA ASP C 57 17472 10584 7595 400 -2035 -1293 C ATOM 3842 C ASP C 57 91.934 8.627 -0.760 1.00 93.09 C ANISOU 3842 C ASP C 57 18174 10097 7098 258 -1792 -847 C ATOM 3843 O ASP C 57 92.524 7.683 -1.290 1.00 90.83 O ANISOU 3843 O ASP C 57 18064 9740 6705 -46 -1641 -728 O ATOM 3844 CB ASP C 57 89.537 9.005 -1.388 1.00101.67 C ANISOU 3844 CB ASP C 57 18576 11576 8480 964 -2764 -1580 C ATOM 3845 CG ASP C 57 88.056 8.777 -1.128 1.00117.64 C ANISOU 3845 CG ASP C 57 19704 14046 10949 1135 -3078 -2146 C ATOM 3846 OD1 ASP C 57 87.593 9.082 -0.003 1.00118.76 O ANISOU 3846 OD1 ASP C 57 19284 14418 11422 1119 -2828 -2326 O ATOM 3847 OD2 ASP C 57 87.346 8.365 -2.071 1.00127.52 O ANISOU 3847 OD2 ASP C 57 20823 15417 12213 1306 -3590 -2453 O ATOM 3848 N TRP C 58 92.506 9.834 -0.561 1.00 88.42 N ANISOU 3848 N TRP C 58 18051 9253 6291 454 -1727 -645 N ATOM 3849 CA TRP C 58 93.882 10.142 -0.971 1.00 85.41 C ANISOU 3849 CA TRP C 58 18382 8517 5554 268 -1439 -305 C ATOM 3850 C TRP C 58 94.911 9.442 -0.065 1.00 83.14 C ANISOU 3850 C TRP C 58 17853 8307 5428 -208 -871 -132 C ATOM 3851 O TRP C 58 96.026 9.179 -0.516 1.00 80.98 O ANISOU 3851 O TRP C 58 17950 7853 4965 -447 -615 45 O ATOM 3852 CB TRP C 58 94.140 11.659 -0.993 1.00 85.78 C ANISOU 3852 CB TRP C 58 19028 8250 5317 560 -1509 -190 C ATOM 3853 CG TRP C 58 93.960 12.367 0.320 1.00 85.81 C ANISOU 3853 CG TRP C 58 18690 8366 5547 628 -1343 -216 C ATOM 3854 CD1 TRP C 58 92.812 12.926 0.799 1.00 91.66 C ANISOU 3854 CD1 TRP C 58 19071 9272 6486 1030 -1645 -463 C ATOM 3855 CD2 TRP C 58 94.985 12.675 1.275 1.00 82.09 C ANISOU 3855 CD2 TRP C 58 18258 7831 5102 315 -855 -19 C ATOM 3856 NE1 TRP C 58 93.049 13.531 2.011 1.00 89.29 N ANISOU 3856 NE1 TRP C 58 18618 8995 6314 962 -1332 -405 N ATOM 3857 CE2 TRP C 58 94.375 13.392 2.328 1.00 86.67 C ANISOU 3857 CE2 TRP C 58 18541 8520 5869 523 -871 -126 C ATOM 3858 CE3 TRP C 58 96.359 12.387 1.358 1.00 80.15 C ANISOU 3858 CE3 TRP C 58 18217 7472 4765 -110 -421 186 C ATOM 3859 CZ2 TRP C 58 95.092 13.831 3.449 1.00 83.34 C ANISOU 3859 CZ2 TRP C 58 18098 8067 5501 305 -488 0 C ATOM 3860 CZ3 TRP C 58 97.068 12.824 2.468 1.00 79.30 C ANISOU 3860 CZ3 TRP C 58 18015 7368 4748 -304 -83 273 C ATOM 3861 CH2 TRP C 58 96.437 13.537 3.496 1.00 80.44 C ANISOU 3861 CH2 TRP C 58 17937 7592 5035 -106 -126 198 C ATOM 3862 N VAL C 59 94.533 9.128 1.187 1.00 77.20 N ANISOU 3862 N VAL C 59 16511 7812 5010 -327 -686 -219 N ATOM 3863 CA VAL C 59 95.396 8.452 2.162 1.00 72.77 C ANISOU 3863 CA VAL C 59 15771 7303 4575 -695 -243 -84 C ATOM 3864 C VAL C 59 95.495 6.962 1.789 1.00 74.90 C ANISOU 3864 C VAL C 59 15907 7647 4903 -962 -168 -113 C ATOM 3865 O VAL C 59 96.600 6.414 1.795 1.00 72.26 O ANISOU 3865 O VAL C 59 15750 7211 4495 -1169 81 39 O ATOM 3866 CB VAL C 59 94.884 8.667 3.613 1.00 76.03 C ANISOU 3866 CB VAL C 59 15757 7893 5237 -719 -78 -172 C ATOM 3867 CG1 VAL C 59 95.680 7.846 4.626 1.00 72.80 C ANISOU 3867 CG1 VAL C 59 15253 7502 4904 -1055 297 -52 C ATOM 3868 CG2 VAL C 59 94.919 10.145 3.986 1.00 76.45 C ANISOU 3868 CG2 VAL C 59 16016 7828 5204 -457 -126 -130 C ATOM 3869 N LYS C 60 94.353 6.330 1.428 1.00 73.11 N ANISOU 3869 N LYS C 60 15370 7596 4812 -943 -398 -347 N ATOM 3870 CA LYS C 60 94.268 4.919 1.023 1.00 72.60 C ANISOU 3870 CA LYS C 60 15215 7581 4787 -1211 -350 -415 C ATOM 3871 C LYS C 60 95.128 4.648 -0.219 1.00 75.37 C ANISOU 3871 C LYS C 60 16073 7711 4855 -1214 -407 -268 C ATOM 3872 O LYS C 60 95.685 3.556 -0.341 1.00 73.48 O ANISOU 3872 O LYS C 60 15905 7419 4595 -1452 -214 -213 O ATOM 3873 CB LYS C 60 92.812 4.506 0.759 1.00 78.75 C ANISOU 3873 CB LYS C 60 15550 8603 5768 -1195 -626 -770 C ATOM 3874 CG LYS C 60 91.989 4.347 2.038 1.00 91.82 C ANISOU 3874 CG LYS C 60 16651 10496 7739 -1368 -396 -983 C ATOM 3875 CD LYS C 60 90.524 3.967 1.801 1.00105.63 C ANISOU 3875 CD LYS C 60 17833 12544 9756 -1406 -617 -1445 C ATOM 3876 CE LYS C 60 89.650 5.124 1.373 1.00119.64 C ANISOU 3876 CE LYS C 60 19375 14469 11616 -905 -1099 -1702 C ATOM 3877 NZ LYS C 60 88.229 4.721 1.226 1.00134.70 N ANISOU 3877 NZ LYS C 60 20585 16736 13859 -942 -1320 -2253 N ATOM 3878 N LYS C 61 95.259 5.653 -1.111 1.00 73.17 N ANISOU 3878 N LYS C 61 16215 7262 4325 -947 -639 -214 N ATOM 3879 CA LYS C 61 96.077 5.594 -2.324 1.00 73.07 C ANISOU 3879 CA LYS C 61 16791 6991 3981 -966 -629 -92 C ATOM 3880 C LYS C 61 97.571 5.623 -1.960 1.00 73.25 C ANISOU 3880 C LYS C 61 16996 6884 3951 -1181 -163 103 C ATOM 3881 O LYS C 61 98.348 4.863 -2.539 1.00 72.39 O ANISOU 3881 O LYS C 61 17081 6682 3744 -1351 26 139 O ATOM 3882 CB LYS C 61 95.727 6.762 -3.265 1.00 78.88 C ANISOU 3882 CB LYS C 61 18050 7519 4401 -625 -991 -101 C ATOM 3883 CG LYS C 61 96.389 6.677 -4.645 1.00 96.67 C ANISOU 3883 CG LYS C 61 21029 9461 6239 -668 -983 -12 C ATOM 3884 CD LYS C 61 96.373 8.009 -5.412 1.00110.65 C ANISOU 3884 CD LYS C 61 23565 10891 7585 -380 -1206 49 C ATOM 3885 CE LYS C 61 97.575 8.907 -5.162 1.00119.49 C ANISOU 3885 CE LYS C 61 25106 11765 8530 -562 -732 236 C ATOM 3886 NZ LYS C 61 97.632 9.451 -3.776 1.00125.13 N ANISOU 3886 NZ LYS C 61 25327 12660 9557 -569 -564 263 N ATOM 3887 N LEU C 62 97.963 6.499 -1.002 1.00 67.55 N ANISOU 3887 N LEU C 62 16182 6173 3310 -1160 10 180 N ATOM 3888 CA LEU C 62 99.349 6.664 -0.545 1.00 64.73 C ANISOU 3888 CA LEU C 62 15897 5743 2953 -1347 401 285 C ATOM 3889 C LEU C 62 99.851 5.431 0.200 1.00 65.26 C ANISOU 3889 C LEU C 62 15609 5948 3239 -1519 595 273 C ATOM 3890 O LEU C 62 101.035 5.119 0.107 1.00 63.84 O ANISOU 3890 O LEU C 62 15496 5714 3045 -1640 843 282 O ATOM 3891 CB LEU C 62 99.509 7.900 0.353 1.00 64.17 C ANISOU 3891 CB LEU C 62 15808 5656 2917 -1282 477 335 C ATOM 3892 CG LEU C 62 99.351 9.278 -0.299 1.00 71.38 C ANISOU 3892 CG LEU C 62 17250 6328 3543 -1118 361 371 C ATOM 3893 CD1 LEU C 62 99.299 10.361 0.750 1.00 71.02 C ANISOU 3893 CD1 LEU C 62 17129 6285 3571 -1039 406 398 C ATOM 3894 CD2 LEU C 62 100.461 9.565 -1.315 1.00 75.18 C ANISOU 3894 CD2 LEU C 62 18298 6541 3726 -1317 631 413 C ATOM 3895 N MET C 63 98.964 4.726 0.922 1.00 61.14 N ANISOU 3895 N MET C 63 14744 5583 2905 -1528 493 217 N ATOM 3896 CA MET C 63 99.334 3.505 1.642 1.00 59.75 C ANISOU 3896 CA MET C 63 14396 5450 2855 -1673 651 214 C ATOM 3897 C MET C 63 99.678 2.391 0.644 1.00 64.49 C ANISOU 3897 C MET C 63 15181 5961 3359 -1752 668 183 C ATOM 3898 O MET C 63 100.576 1.592 0.907 1.00 63.62 O ANISOU 3898 O MET C 63 15099 5800 3274 -1798 827 193 O ATOM 3899 CB MET C 63 98.224 3.052 2.603 1.00 62.40 C ANISOU 3899 CB MET C 63 14442 5915 3353 -1745 617 139 C ATOM 3900 CG MET C 63 98.011 3.998 3.771 1.00 65.31 C ANISOU 3900 CG MET C 63 14643 6356 3816 -1682 674 158 C ATOM 3901 SD MET C 63 96.971 3.317 5.087 1.00 70.41 S ANISOU 3901 SD MET C 63 15026 7107 4619 -1866 810 47 S ATOM 3902 CE MET C 63 95.380 3.251 4.272 1.00 70.21 C ANISOU 3902 CE MET C 63 14700 7263 4715 -1877 599 -209 C ATOM 3903 N GLN C 64 98.996 2.373 -0.515 1.00 62.51 N ANISOU 3903 N GLN C 64 15091 5679 2983 -1726 470 125 N ATOM 3904 CA GLN C 64 99.241 1.406 -1.583 1.00 63.15 C ANISOU 3904 CA GLN C 64 15415 5650 2928 -1801 471 85 C ATOM 3905 C GLN C 64 100.604 1.661 -2.236 1.00 66.51 C ANISOU 3905 C GLN C 64 16138 5931 3204 -1802 712 129 C ATOM 3906 O GLN C 64 101.374 0.722 -2.432 1.00 66.63 O ANISOU 3906 O GLN C 64 16209 5888 3221 -1861 885 93 O ATOM 3907 CB GLN C 64 98.122 1.458 -2.638 1.00 67.01 C ANISOU 3907 CB GLN C 64 16029 6139 3292 -1748 135 -18 C ATOM 3908 CG GLN C 64 96.779 0.919 -2.145 1.00 85.36 C ANISOU 3908 CG GLN C 64 17965 8651 5816 -1825 -58 -181 C ATOM 3909 CD GLN C 64 95.668 1.056 -3.159 1.00110.58 C ANISOU 3909 CD GLN C 64 21185 11898 8932 -1720 -476 -365 C ATOM 3910 OE1 GLN C 64 95.540 2.067 -3.861 1.00108.42 O ANISOU 3910 OE1 GLN C 64 21167 11550 8475 -1467 -730 -354 O ATOM 3911 NE2 GLN C 64 94.788 0.066 -3.204 1.00105.29 N ANISOU 3911 NE2 GLN C 64 20268 11348 8389 -1908 -582 -572 N ATOM 3912 N GLN C 65 100.915 2.935 -2.517 1.00 62.57 N ANISOU 3912 N GLN C 65 15832 5363 2579 -1750 756 173 N ATOM 3913 CA GLN C 65 102.145 3.370 -3.182 1.00 62.98 C ANISOU 3913 CA GLN C 65 16184 5270 2474 -1841 1068 157 C ATOM 3914 C GLN C 65 103.391 3.294 -2.280 1.00 65.16 C ANISOU 3914 C GLN C 65 16142 5645 2970 -1907 1370 101 C ATOM 3915 O GLN C 65 104.497 3.139 -2.803 1.00 65.38 O ANISOU 3915 O GLN C 65 16254 5620 2966 -2012 1672 -15 O ATOM 3916 CB GLN C 65 101.993 4.820 -3.681 1.00 65.91 C ANISOU 3916 CB GLN C 65 16964 5481 2599 -1808 1039 210 C ATOM 3917 CG GLN C 65 100.873 5.059 -4.703 1.00 83.06 C ANISOU 3917 CG GLN C 65 19559 7510 4489 -1651 659 226 C ATOM 3918 CD GLN C 65 101.090 4.364 -6.026 1.00105.65 C ANISOU 3918 CD GLN C 65 22865 10196 7083 -1732 703 179 C ATOM 3919 OE1 GLN C 65 102.063 4.620 -6.747 1.00103.18 O ANISOU 3919 OE1 GLN C 65 22984 9680 6540 -1900 1064 161 O ATOM 3920 NE2 GLN C 65 100.151 3.508 -6.398 1.00 99.17 N ANISOU 3920 NE2 GLN C 65 21972 9440 6270 -1646 358 123 N ATOM 3921 N LEU C 66 103.225 3.432 -0.950 1.00 60.60 N ANISOU 3921 N LEU C 66 15205 5211 2608 -1841 1287 140 N ATOM 3922 CA LEU C 66 104.342 3.460 0.003 1.00 60.11 C ANISOU 3922 CA LEU C 66 14851 5247 2740 -1847 1462 60 C ATOM 3923 C LEU C 66 104.463 2.173 0.851 1.00 64.48 C ANISOU 3923 C LEU C 66 15179 5866 3454 -1736 1367 33 C ATOM 3924 O LEU C 66 103.448 1.533 1.133 1.00 63.66 O ANISOU 3924 O LEU C 66 15098 5749 3339 -1717 1193 115 O ATOM 3925 CB LEU C 66 104.178 4.662 0.956 1.00 59.13 C ANISOU 3925 CB LEU C 66 14614 5178 2674 -1838 1426 120 C ATOM 3926 CG LEU C 66 104.303 6.063 0.346 1.00 64.79 C ANISOU 3926 CG LEU C 66 15636 5770 3210 -1942 1556 134 C ATOM 3927 CD1 LEU C 66 103.577 7.080 1.187 1.00 64.13 C ANISOU 3927 CD1 LEU C 66 15528 5700 3137 -1856 1404 233 C ATOM 3928 CD2 LEU C 66 105.759 6.458 0.128 1.00 68.34 C ANISOU 3928 CD2 LEU C 66 16065 6211 3689 -2146 1923 -46 C ATOM 3929 N PRO C 67 105.689 1.805 1.307 1.00 62.53 N ANISOU 3929 N PRO C 67 14736 5676 3348 -1660 1471 -118 N ATOM 3930 CA PRO C 67 105.823 0.609 2.157 1.00 62.91 C ANISOU 3930 CA PRO C 67 14717 5710 3477 -1481 1320 -139 C ATOM 3931 C PRO C 67 105.654 0.919 3.649 1.00 66.96 C ANISOU 3931 C PRO C 67 15114 6269 4059 -1400 1171 -72 C ATOM 3932 O PRO C 67 105.612 2.087 4.037 1.00 66.14 O ANISOU 3932 O PRO C 67 14900 6244 3988 -1472 1202 -42 O ATOM 3933 CB PRO C 67 107.250 0.142 1.868 1.00 66.80 C ANISOU 3933 CB PRO C 67 15052 6244 4085 -1352 1439 -394 C ATOM 3934 CG PRO C 67 107.996 1.391 1.498 1.00 71.80 C ANISOU 3934 CG PRO C 67 15507 6989 4784 -1520 1683 -533 C ATOM 3935 CD PRO C 67 107.005 2.439 1.068 1.00 65.74 C ANISOU 3935 CD PRO C 67 14982 6153 3842 -1727 1720 -326 C ATOM 3936 N VAL C 68 105.588 -0.129 4.488 1.00 64.63 N ANISOU 3936 N VAL C 68 14935 5879 3743 -1252 1021 -53 N ATOM 3937 CA VAL C 68 105.493 0.018 5.944 1.00 64.63 C ANISOU 3937 CA VAL C 68 14958 5860 3738 -1164 885 2 C ATOM 3938 C VAL C 68 106.923 0.242 6.479 1.00 71.44 C ANISOU 3938 C VAL C 68 15599 6815 4730 -932 782 -205 C ATOM 3939 O VAL C 68 107.868 -0.372 5.972 1.00 73.29 O ANISOU 3939 O VAL C 68 15736 7067 5045 -759 766 -403 O ATOM 3940 CB VAL C 68 104.769 -1.184 6.623 1.00 69.09 C ANISOU 3940 CB VAL C 68 15895 6211 4146 -1147 802 102 C ATOM 3941 CG1 VAL C 68 104.772 -1.067 8.146 1.00 69.50 C ANISOU 3941 CG1 VAL C 68 16105 6181 4119 -1056 686 149 C ATOM 3942 CG2 VAL C 68 103.339 -1.317 6.116 1.00 68.03 C ANISOU 3942 CG2 VAL C 68 15845 6054 3950 -1435 920 210 C ATOM 3943 N THR C 69 107.074 1.143 7.475 1.00 68.23 N ANISOU 3943 N THR C 69 15078 6485 4360 -925 709 -204 N ATOM 3944 CA THR C 69 108.346 1.501 8.118 1.00 70.23 C ANISOU 3944 CA THR C 69 15067 6862 4755 -732 559 -447 C ATOM 3945 C THR C 69 109.002 0.249 8.746 1.00 77.23 C ANISOU 3945 C THR C 69 16115 7628 5600 -333 246 -577 C ATOM 3946 O THR C 69 108.306 -0.573 9.351 1.00 76.91 O ANISOU 3946 O THR C 69 16538 7345 5339 -255 130 -394 O ATOM 3947 CB THR C 69 108.108 2.595 9.181 1.00 77.84 C ANISOU 3947 CB THR C 69 16012 7868 5695 -818 507 -376 C ATOM 3948 OG1 THR C 69 107.198 3.576 8.678 1.00 75.51 O ANISOU 3948 OG1 THR C 69 15727 7596 5367 -1112 746 -205 O ATOM 3949 CG2 THR C 69 109.398 3.271 9.637 1.00 79.04 C ANISOU 3949 CG2 THR C 69 15800 8203 6028 -726 392 -677 C ATOM 3950 N ALA C 70 110.335 0.110 8.581 1.00 76.83 N ANISOU 3950 N ALA C 70 15704 7732 5754 -85 123 -931 N ATOM 3951 CA ALA C 70 111.121 -1.011 9.107 1.00110.63 C ANISOU 3951 CA ALA C 70 20100 11913 10022 413 -256 -1138 C ATOM 3952 C ALA C 70 111.270 -0.924 10.631 1.00138.33 C ANISOU 3952 C ALA C 70 23841 15323 13395 675 -659 -1135 C ATOM 3953 O ALA C 70 111.506 0.152 11.181 1.00 97.48 O ANISOU 3953 O ALA C 70 18398 10321 8317 553 -684 -1208 O ATOM 3954 CB ALA C 70 112.493 -1.040 8.452 1.00114.78 C ANISOU 3954 CB ALA C 70 20039 12701 10871 605 -256 -1609 C TER 3955 ALA C 70 CONECT 45 3180 CONECT 662 1278 CONECT 1278 662 CONECT 1284 3450 CONECT 3180 45 CONECT 3450 1284 CONECT 3501 3682 CONECT 3507 3806 CONECT 3682 3501 CONECT 3806 3507 MASTER 411 0 0 26 8 0 0 6 3953 2 10 46 END