HEADER SIGNALING PROTEIN 18-AUG-16 5T1A TITLE STRUCTURE OF CC CHEMOKINE RECEPTOR 2 WITH ORTHOSTERIC AND ALLOSTERIC TITLE 2 ANTAGONISTS COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF CC CHEMOKINE RECEPTOR TYPE 2 ISOFORM B COMPND 3 AND T4-LYSOZYME,LYSOZYME; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP P41597-2 RESIDUES 2-328 WITH UNP P00720 RESIDUES 2-161 COMPND 6 INSERTED AFTER RESIDUES 233; COMPND 7 SYNONYM: CCR2,MONOCYTE CHEMOATTRACTANT PROTEIN 1 RECEPTOR,MCP-1-R, COMPND 8 CCR2,MONOCYTE CHEMOATTRACTANT PROTEIN 1 RECEPTOR,MCP-1-R; COMPND 9 EC: 3.2.1.17; COMPND 10 ENGINEERED: YES; COMPND 11 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: CCR2, CMKBR2, E, T4TP126; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS C-C CHEMOKINE RECEPTOR TYPE 2, DUAL ANTAGONIST, INTRACELLULAR KEYWDS 2 ALLOSTERIC ANTAGONIST, COOPERATIVE BINDING, LIPIDIC CUBIC PHASE, KEYWDS 3 MEMBRANE PROTEIN, GPCR, STRUCTURAL GENOMICS, PSI-2, PROTEIN KEYWDS 4 STRUCTURE INITIATIVE, GPCR NETWORK, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.ZHENG,L.QIN,N.V.ORTIZ ZACARIAS,H.DE VRIES,G.W.HAN,M.GUSTAVSSON, AUTHOR 2 M.DABROS,C.ZHAO,R.J.CHERNEY,P.CARTER,D.STAMOS,R.ABAGYAN,V.CHEREZOV, AUTHOR 3 R.C.STEVENS,A.P.IJZERMAN,L.H.HEITMAN,A.TEBBEN,I.KUFAREVA,T.M.HANDEL REVDAT 6 11-DEC-19 5T1A 1 REMARK REVDAT 5 13-SEP-17 5T1A 1 REMARK REVDAT 4 04-JAN-17 5T1A 1 JRNL REVDAT 3 28-DEC-16 5T1A 1 AUTHOR REVDAT 2 21-DEC-16 5T1A 1 COMPND AUTHOR REVDAT 1 14-DEC-16 5T1A 0 JRNL AUTH Y.ZHENG,L.QIN,N.V.ZACARIAS,H.DE VRIES,G.W.HAN,M.GUSTAVSSON, JRNL AUTH 2 M.DABROS,C.ZHAO,R.J.CHERNEY,P.CARTER,D.STAMOS,R.ABAGYAN, JRNL AUTH 3 V.CHEREZOV,R.C.STEVENS,A.P.IJZERMAN,L.H.HEITMAN,A.TEBBEN, JRNL AUTH 4 I.KUFAREVA,T.M.HANDEL JRNL TITL STRUCTURE OF CC CHEMOKINE RECEPTOR 2 WITH ORTHOSTERIC AND JRNL TITL 2 ALLOSTERIC ANTAGONISTS. JRNL REF NATURE V. 540 458 2016 JRNL REFN ESSN 1476-4687 JRNL PMID 27926736 JRNL DOI 10.1038/NATURE20605 REMARK 2 REMARK 2 RESOLUTION. 2.81 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.32 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.2 REMARK 3 NUMBER OF REFLECTIONS : 14487 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.236 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 742 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 24.3215 - 4.7879 0.99 3260 178 0.2055 0.2141 REMARK 3 2 4.7879 - 3.8050 0.99 3140 153 0.2030 0.2581 REMARK 3 3 3.8050 - 3.3254 1.00 3126 169 0.2435 0.3032 REMARK 3 4 3.3254 - 3.0220 0.99 3062 155 0.3036 0.3343 REMARK 3 5 3.0220 - 2.8057 0.38 1157 87 0.3235 0.3926 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.600 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 40.35 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.21 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 3643 REMARK 3 ANGLE : 0.845 4961 REMARK 3 CHIRALITY : 0.032 577 REMARK 3 PLANARITY : 0.003 603 REMARK 3 DIHEDRAL : 12.851 1267 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 233 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.6724 23.8183 170.4808 REMARK 3 T TENSOR REMARK 3 T11: 0.3676 T22: 0.3114 REMARK 3 T33: 0.0923 T12: 0.0007 REMARK 3 T13: 0.0208 T23: 0.0216 REMARK 3 L TENSOR REMARK 3 L11: 1.1336 L22: 1.1581 REMARK 3 L33: 1.9287 L12: 0.1155 REMARK 3 L13: -0.3861 L23: -0.3647 REMARK 3 S TENSOR REMARK 3 S11: 0.0343 S12: 0.1441 S13: 0.1260 REMARK 3 S21: -0.1301 S22: 0.0035 S23: -0.0079 REMARK 3 S31: -0.1247 S32: -0.0548 S33: -0.0712 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1162 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.9811 12.4267 214.5599 REMARK 3 T TENSOR REMARK 3 T11: 0.4979 T22: 0.4515 REMARK 3 T33: -0.0008 T12: 0.0472 REMARK 3 T13: -0.0943 T23: -0.0229 REMARK 3 L TENSOR REMARK 3 L11: 0.6985 L22: 1.2603 REMARK 3 L33: 1.5096 L12: -0.4384 REMARK 3 L13: -0.7029 L23: -0.1469 REMARK 3 S TENSOR REMARK 3 S11: -0.0174 S12: -0.3179 S13: 0.1816 REMARK 3 S21: 0.3363 S22: 0.1725 S23: -0.4702 REMARK 3 S31: 0.0138 S32: 0.3401 S33: 0.1500 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 234 THROUGH 320 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3465 20.7634 171.3347 REMARK 3 T TENSOR REMARK 3 T11: 0.3414 T22: 0.4002 REMARK 3 T33: -0.0532 T12: -0.0021 REMARK 3 T13: 0.0222 T23: -0.0679 REMARK 3 L TENSOR REMARK 3 L11: 1.5216 L22: 1.3690 REMARK 3 L33: 3.2509 L12: 0.0271 REMARK 3 L13: 0.0571 L23: 0.1016 REMARK 3 S TENSOR REMARK 3 S11: -0.1300 S12: 0.3555 S13: -0.1375 REMARK 3 S21: -0.0037 S22: 0.0876 S23: -0.0406 REMARK 3 S31: -0.1402 S32: -0.1438 S33: -0.1384 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 5T1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-16. REMARK 100 THE DEPOSITION ID IS D_1000222819. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-AUG-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.1 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03321 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 X 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15550 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 23.321 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.24100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 66.6 REMARK 200 DATA REDUNDANCY IN SHELL : 1.80 REMARK 200 R MERGE FOR SHELL (I) : 1.13200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4MBS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN REMARK 280 AND CHOLESTEROL, 100 MM 2-(N-MORPHOLINO)ETHANESULFONIC ACID, PH REMARK 280 6.5, 30-32% (V/V) PEG 400, 75-85 MM LITHIUM SULFATE, PH 6.1, REMARK 280 TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 29.61500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.99000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.34500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.99000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.61500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.34500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A -9 REMARK 465 TYR A -8 REMARK 465 LYS A -7 REMARK 465 ASP A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 LYS A -2 REMARK 465 PRO A -1 REMARK 465 GLY A 0 REMARK 465 THR A 1 REMARK 465 LEU A 2 REMARK 465 SER A 3 REMARK 465 THR A 4 REMARK 465 SER A 5 REMARK 465 ARG A 6 REMARK 465 SER A 7 REMARK 465 ARG A 8 REMARK 465 PHE A 9 REMARK 465 ILE A 10 REMARK 465 ARG A 11 REMARK 465 ASN A 12 REMARK 465 THR A 13 REMARK 465 ASN A 14 REMARK 465 GLU A 15 REMARK 465 SER A 16 REMARK 465 GLY A 17 REMARK 465 GLU A 18 REMARK 465 GLU A 19 REMARK 465 VAL A 20 REMARK 465 THR A 21 REMARK 465 THR A 22 REMARK 465 PHE A 23 REMARK 465 PHE A 24 REMARK 465 ASP A 25 REMARK 465 TYR A 26 REMARK 465 ASP A 27 REMARK 465 TYR A 28 REMARK 465 GLY A 29 REMARK 465 ALA A 30 REMARK 465 PRO A 31 REMARK 465 CYS A 32 REMARK 465 HIS A 33 REMARK 465 LYS A 34 REMARK 465 PHE A 35 REMARK 465 ASP A 36 REMARK 465 ARG A 321 REMARK 465 LYS A 322 REMARK 465 HIS A 323 REMARK 465 ILE A 324 REMARK 465 THR A 325 REMARK 465 LYS A 326 REMARK 465 ARG A 327 REMARK 465 PHE A 328 REMARK 465 GLY A 329 REMARK 465 ARG A 330 REMARK 465 PRO A 331 REMARK 465 LEU A 332 REMARK 465 GLU A 333 REMARK 465 VAL A 334 REMARK 465 LEU A 335 REMARK 465 PHE A 336 REMARK 465 GLN A 337 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 GLN A 39 CG CD OE1 NE2 REMARK 470 LYS A 74 CG CD CE NZ REMARK 470 LYS A 150 CE NZ REMARK 470 LYS A 183 CG CD CE NZ REMARK 470 ASP A 185 CG OD1 OD2 REMARK 470 SER A 186 OG REMARK 470 ARG A 196 CG CD NE CZ NH1 NH2 REMARK 470 SER A 223 OG REMARK 470 LYS A 230 CG CD CE NZ REMARK 470 LYS A1016 CE NZ REMARK 470 THR A1021 OG1 CG2 REMARK 470 TYR A1024 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A1039 CG CD1 CD2 REMARK 470 GLU A1045 CG CD OE1 OE2 REMARK 470 LYS A1048 CE NZ REMARK 470 ASN A1053 CG OD1 ND2 REMARK 470 LYS A1060 CE NZ REMARK 470 LYS A1065 CG CD CE NZ REMARK 470 ARG A1080 CG CD NE CZ NH1 NH2 REMARK 470 GLU A1128 CG CD OE1 OE2 REMARK 470 PHE A 268 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A 271 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASN A 276 CG OD1 ND2 REMARK 470 GLU A 278 CG CD OE1 OE2 REMARK 470 GLN A 285 CD OE1 NE2 REMARK 470 PHE A 319 CG CD1 CD2 CE1 CE2 CZ 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 CYS A 70 -53.09 -124.95 REMARK 500 ASN A 104 -109.99 -124.61 REMARK 500 LEU A 211 -61.69 -147.52 REMARK 500 SER A 236 -63.77 -101.14 REMARK 500 THR A 267 -78.64 -112.78 REMARK 500 CYS A 298 1.75 -68.29 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1208 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 144 NE2 REMARK 620 2 GLU A1005 OE2 100.6 REMARK 620 3 GLU A 238 OE2 120.6 99.2 REMARK 620 4 HOH A1307 O 91.7 116.3 126.6 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 73R A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue VT5 A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1208 DBREF 5T1A A 2 233 UNP P41597 CCR2_HUMAN 2 233 DBREF 5T1A A 1002 1162 UNP D9IEF7 D9IEF7_BPT4 2 162 DBREF 5T1A A 234 328 UNP P41597 CCR2_HUMAN 234 328 SEQADV 5T1A ASP A -9 UNP P41597 EXPRESSION TAG SEQADV 5T1A TYR A -8 UNP P41597 EXPRESSION TAG SEQADV 5T1A LYS A -7 UNP P41597 EXPRESSION TAG SEQADV 5T1A ASP A -6 UNP P41597 EXPRESSION TAG SEQADV 5T1A ASP A -5 UNP P41597 EXPRESSION TAG SEQADV 5T1A ASP A -4 UNP P41597 EXPRESSION TAG SEQADV 5T1A ASP A -3 UNP P41597 EXPRESSION TAG SEQADV 5T1A LYS A -2 UNP P41597 EXPRESSION TAG SEQADV 5T1A PRO A -1 UNP P41597 EXPRESSION TAG SEQADV 5T1A GLY A 0 UNP P41597 EXPRESSION TAG SEQADV 5T1A THR A 1 UNP P41597 EXPRESSION TAG SEQADV 5T1A SER A 226 UNP P41597 LEU 226 ENGINEERED MUTATION SEQADV 5T1A ARG A 227 UNP P41597 LYS 227 ENGINEERED MUTATION SEQADV 5T1A ALA A 228 UNP P41597 THR 228 ENGINEERED MUTATION SEQADV 5T1A SER A 229 UNP P41597 LEU 229 ENGINEERED MUTATION SEQADV 5T1A LYS A 230 UNP P41597 LEU 230 ENGINEERED MUTATION SEQADV 5T1A SER A 231 UNP P41597 ARG 231 ENGINEERED MUTATION SEQADV 5T1A ARG A 232 UNP P41597 CYS 232 ENGINEERED MUTATION SEQADV 5T1A ILE A 233 UNP P41597 ARG 233 ENGINEERED MUTATION SEQADV 5T1A THR A 1054 UNP D9IEF7 CYS 54 ENGINEERED MUTATION SEQADV 5T1A ALA A 1097 UNP D9IEF7 CYS 97 ENGINEERED MUTATION SEQADV 5T1A PRO A 1162 UNP D9IEF7 LYS 162 ENGINEERED MUTATION SEQADV 5T1A PRO A 234 UNP P41597 ASN 234 ENGINEERED MUTATION SEQADV 5T1A PRO A 235 UNP P41597 GLU 235 ENGINEERED MUTATION SEQADV 5T1A SER A 236 UNP P41597 LYS 236 ENGINEERED MUTATION SEQADV 5T1A ARG A 237 UNP P41597 LYS 237 ENGINEERED MUTATION SEQADV 5T1A GLU A 238 UNP P41597 ARG 238 ENGINEERED MUTATION SEQADV 5T1A LYS A 239 UNP P41597 HIS 239 ENGINEERED MUTATION SEQADV 5T1A LYS A 240 UNP P41597 ARG 240 ENGINEERED MUTATION SEQADV 5T1A GLY A 329 UNP P41597 ENGINEERED MUTATION SEQADV 5T1A ARG A 330 UNP P41597 ENGINEERED MUTATION SEQADV 5T1A PRO A 331 UNP P41597 ENGINEERED MUTATION SEQADV 5T1A LEU A 332 UNP P41597 ENGINEERED MUTATION SEQADV 5T1A GLU A 333 UNP P41597 ENGINEERED MUTATION SEQADV 5T1A VAL A 334 UNP P41597 EXPRESSION TAG SEQADV 5T1A LEU A 335 UNP P41597 EXPRESSION TAG SEQADV 5T1A PHE A 336 UNP P41597 EXPRESSION TAG SEQADV 5T1A GLN A 337 UNP P41597 EXPRESSION TAG SEQRES 1 A 508 ASP TYR LYS ASP ASP ASP ASP LYS PRO GLY THR LEU SER SEQRES 2 A 508 THR SER ARG SER ARG PHE ILE ARG ASN THR ASN GLU SER SEQRES 3 A 508 GLY GLU GLU VAL THR THR PHE PHE ASP TYR ASP TYR GLY SEQRES 4 A 508 ALA PRO CYS HIS LYS PHE ASP VAL LYS GLN ILE GLY ALA SEQRES 5 A 508 GLN LEU LEU PRO PRO LEU TYR SER LEU VAL PHE ILE PHE SEQRES 6 A 508 GLY PHE VAL GLY ASN MET LEU VAL VAL LEU ILE LEU ILE SEQRES 7 A 508 ASN CYS LYS LYS LEU LYS CYS LEU THR ASP ILE TYR LEU SEQRES 8 A 508 LEU ASN LEU ALA ILE SER ASP LEU LEU PHE LEU ILE THR SEQRES 9 A 508 LEU PRO LEU TRP ALA HIS SER ALA ALA ASN GLU TRP VAL SEQRES 10 A 508 PHE GLY ASN ALA MET CYS LYS LEU PHE THR GLY LEU TYR SEQRES 11 A 508 HIS ILE GLY TYR PHE GLY GLY ILE PHE PHE ILE ILE LEU SEQRES 12 A 508 LEU THR ILE ASP ARG TYR LEU ALA ILE VAL HIS ALA VAL SEQRES 13 A 508 PHE ALA LEU LYS ALA ARG THR VAL THR PHE GLY VAL VAL SEQRES 14 A 508 THR SER VAL ILE THR TRP LEU VAL ALA VAL PHE ALA SER SEQRES 15 A 508 VAL PRO GLY ILE ILE PHE THR LYS YCM GLN LYS GLU ASP SEQRES 16 A 508 SER VAL TYR VAL CYS GLY PRO TYR PHE PRO ARG GLY TRP SEQRES 17 A 508 ASN ASN PHE HIS THR ILE MET ARG ASN ILE LEU GLY LEU SEQRES 18 A 508 VAL LEU PRO LEU LEU ILE MET VAL ILE CYS TYR SER GLY SEQRES 19 A 508 ILE SER ARG ALA SER LYS SER ARG ILE ASN ILE PHE GLU SEQRES 20 A 508 MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR SEQRES 21 A 508 LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS SEQRES 22 A 508 LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS SER SEQRES 23 A 508 GLU LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL SEQRES 24 A 508 ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP SEQRES 25 A 508 VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS SEQRES 26 A 508 LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG SEQRES 27 A 508 ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR SEQRES 28 A 508 GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN SEQRES 29 A 508 GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SEQRES 30 A 508 SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG SEQRES 31 A 508 VAL ILE THR THR PHE ARG THR GLY THR TRP ASP ALA TYR SEQRES 32 A 508 PRO PRO PRO SER ARG GLU LYS LYS ALA VAL ARG VAL ILE SEQRES 33 A 508 PHE THR ILE MET ILE VAL TYR PHE LEU PHE TRP THR PRO SEQRES 34 A 508 TYR ASN ILE VAL ILE LEU LEU ASN THR PHE GLN GLU PHE SEQRES 35 A 508 PHE GLY LEU SER ASN CYS GLU SER THR SER GLN LEU ASP SEQRES 36 A 508 GLN ALA THR GLN VAL THR GLU THR LEU GLY MET THR HIS SEQRES 37 A 508 CYS CYS ILE ASN PRO ILE ILE TYR ALA PHE VAL GLY GLU SEQRES 38 A 508 LYS PHE ARG ARG TYR LEU SER VAL PHE PHE ARG LYS HIS SEQRES 39 A 508 ILE THR LYS ARG PHE GLY ARG PRO LEU GLU VAL LEU PHE SEQRES 40 A 508 GLN MODRES 5T1A YCM A 181 CYS MODIFIED RESIDUE HET YCM A 181 10 HET 73R A1201 35 HET VT5 A1202 24 HET SO4 A1203 5 HET SO4 A1204 5 HET SO4 A1205 5 HET SO4 A1206 5 HET OLC A1207 25 HET ZN A1208 1 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM 73R (3S)-1-{(1S,2R,4R)-4-[METHYL(PROPAN-2-YL)AMINO]-2- HETNAM 2 73R PROPYLCYCLOHEXYL}-3-{[6-(TRIFLUOROMETHYL)QUINAZOLIN-4- HETNAM 3 73R YL]AMINO}PYRROLIDIN-2-ONE HETNAM VT5 (2~{R})-1-(4-CHLORANYL-2-FLUORANYL-PHENYL)-2- HETNAM 2 VT5 CYCLOHEXYL-3-ETHANOYL-4-OXIDANYL-2~{H}-PYRROL-5-ONE HETNAM SO4 SULFATE ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM ZN ZINC ION HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 2 73R C26 H36 F3 N5 O FORMUL 3 VT5 C18 H19 CL F N O3 FORMUL 4 SO4 4(O4 S 2-) FORMUL 8 OLC C21 H40 O4 FORMUL 9 ZN ZN 2+ FORMUL 10 HOH *17(H2 O) HELIX 1 AA1 VAL A 37 CYS A 70 1 34 HELIX 2 AA2 CYS A 75 ILE A 93 1 19 HELIX 3 AA3 THR A 94 ASN A 104 1 11 HELIX 4 AA4 GLY A 109 VAL A 143 1 35 HELIX 5 AA5 ALA A 145 ARG A 152 1 8 HELIX 6 AA6 THR A 153 ALA A 171 1 19 HELIX 7 AA7 SER A 172 PHE A 178 1 7 HELIX 8 AA8 PRO A 195 LEU A 211 1 17 HELIX 9 AA9 LEU A 211 SER A 229 1 19 HELIX 10 AB1 ASN A 1002 GLU A 1011 1 10 HELIX 11 AB2 SER A 1038 GLY A 1051 1 14 HELIX 12 AB3 THR A 1059 LEU A 1079 1 21 HELIX 13 AB4 LEU A 1084 SER A 1090 1 7 HELIX 14 AB5 ASP A 1092 ALA A 1112 1 21 HELIX 15 AB6 PHE A 1114 GLN A 1123 1 10 HELIX 16 AB7 ARG A 1125 ALA A 1134 1 10 HELIX 17 AB8 SER A 1136 THR A 1142 1 7 HELIX 18 AB9 THR A 1142 GLY A 1156 1 15 HELIX 19 AC1 SER A 236 ASN A 266 1 31 HELIX 20 AC2 PHE A 268 GLY A 273 1 6 HELIX 21 AC3 GLU A 278 THR A 296 1 19 HELIX 22 AC4 ILE A 300 GLY A 309 1 10 HELIX 23 AC5 GLY A 309 PHE A 320 1 12 SHEET 1 AA1 2 THR A 179 GLU A 184 0 SHEET 2 AA1 2 VAL A 187 PRO A 192 -1 O VAL A 187 N GLU A 184 SHEET 1 AA2 3 ARG A1014 LYS A1019 0 SHEET 2 AA2 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA2 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 113 CYS A 190 1555 1555 2.03 LINK NE2 HIS A 144 ZN ZN A1208 1555 1555 2.03 LINK C LYS A 180 N YCM A 181 1555 1555 1.33 LINK C YCM A 181 N GLN A 182 1555 1555 1.33 LINK OE2 GLU A1005 ZN ZN A1208 1555 1555 2.03 LINK OE2 GLU A 238 ZN ZN A1208 1555 1555 1.86 LINK ZN ZN A1208 O HOH A1307 1555 1555 1.98 SITE 1 AC1 14 VAL A 37 GLY A 41 LEU A 44 LEU A 45 SITE 2 AC1 14 TYR A 49 TRP A 98 THR A 117 TYR A 120 SITE 3 AC1 14 CYS A 190 GLN A 288 VAL A 289 GLU A 291 SITE 4 AC1 14 THR A 292 MET A 295 SITE 1 AC2 10 VAL A 63 THR A 77 ARG A 237 ALA A 241 SITE 2 AC2 10 VAL A 244 TYR A 305 GLY A 309 GLU A 310 SITE 3 AC2 10 LYS A 311 PHE A 312 SITE 1 AC3 5 LYS A 71 LYS A 311 ARG A 314 TYR A 315 SITE 2 AC3 5 LYS A1135 SITE 1 AC4 5 SER A 236 ARG A 237 ARG A1008 ARG A1119 SITE 2 AC4 5 ARG A1125 SITE 1 AC5 5 PHE A1114 THR A1115 ASN A1116 SER A1117 SITE 2 AC5 5 ASN A1132 SITE 1 AC6 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AC7 10 PHE A 170 LYS A 180 TRP A 198 MET A 205 SITE 2 AC7 10 TYR A 222 ARG A 232 LYS A 239 ARG A 243 SITE 3 AC7 10 PHE A 246 THR A 247 SITE 1 AC8 4 HIS A 144 GLU A 238 GLU A1005 HOH A1307 CRYST1 59.230 64.690 169.980 90.00 90.00 90.00 P 21 21 21 4 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 0.016883 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015458 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005883 0.00000 ATOM 1 N VAL A 37 -1.473 24.606 146.051 1.00 91.86 N ANISOU 1 N VAL A 37 12812 13763 8326 44 -1075 988 N ATOM 2 CA VAL A 37 -1.496 24.944 147.482 1.00 88.55 C ANISOU 2 CA VAL A 37 12308 13282 8055 81 -1026 1009 C ATOM 3 C VAL A 37 -0.941 26.368 147.707 1.00 83.45 C ANISOU 3 C VAL A 37 11697 12542 7468 181 -953 1130 C ATOM 4 O VAL A 37 -1.452 27.090 148.545 1.00 85.03 O ANISOU 4 O VAL A 37 11794 12751 7762 252 -955 1212 O ATOM 5 CB VAL A 37 -0.713 23.869 148.309 1.00 86.56 C ANISOU 5 CB VAL A 37 12098 12928 7861 16 -944 862 C ATOM 6 CG1 VAL A 37 0.416 24.497 149.122 1.00 85.04 C ANISOU 6 CG1 VAL A 37 11967 12578 7764 67 -819 876 C ATOM 7 CG2 VAL A 37 -1.661 23.075 149.230 1.00 85.78 C ANISOU 7 CG2 VAL A 37 11863 12906 7826 -44 -1001 811 C ATOM 8 N LYS A 38 0.055 26.767 146.909 1.00 78.90 N ANISOU 8 N LYS A 38 11263 11885 6830 187 -890 1145 N ATOM 9 CA LYS A 38 0.669 28.095 146.987 1.00 74.77 C ANISOU 9 CA LYS A 38 10785 11271 6354 255 -818 1260 C ATOM 10 C LYS A 38 -0.302 29.285 147.029 1.00 71.13 C ANISOU 10 C LYS A 38 10221 10877 5927 363 -875 1420 C ATOM 11 O LYS A 38 -0.014 30.305 147.660 1.00 70.09 O ANISOU 11 O LYS A 38 10078 10664 5889 438 -808 1503 O ATOM 12 CB LYS A 38 1.622 28.306 145.812 1.00 76.64 C ANISOU 12 CB LYS A 38 11175 11457 6486 229 -769 1269 C ATOM 13 N GLN A 39 -1.436 29.174 146.350 1.00 69.41 N ANISOU 13 N GLN A 39 9928 10808 5637 379 -993 1467 N ATOM 14 CA GLN A 39 -2.425 30.251 146.357 1.00 67.73 C ANISOU 14 CA GLN A 39 9607 10671 5457 500 -1049 1624 C ATOM 15 C GLN A 39 -2.993 30.451 147.760 1.00 64.99 C ANISOU 15 C GLN A 39 9122 10322 5249 567 -1030 1641 C ATOM 16 O GLN A 39 -3.089 31.577 148.248 1.00 65.24 O ANISOU 16 O GLN A 39 9124 10300 5364 689 -984 1752 O ATOM 17 CB GLN A 39 -3.562 29.960 145.367 1.00 69.26 C ANISOU 17 CB GLN A 39 9728 11046 5540 492 -1188 1662 C ATOM 18 N ILE A 40 -3.348 29.344 148.406 1.00 62.26 N ANISOU 18 N ILE A 40 8702 10027 4927 489 -1059 1528 N ATOM 19 CA ILE A 40 -3.898 29.366 149.757 1.00 59.91 C ANISOU 19 CA ILE A 40 8274 9741 4749 537 -1041 1530 C ATOM 20 C ILE A 40 -2.858 29.821 150.781 1.00 56.38 C ANISOU 20 C ILE A 40 7899 9119 4403 571 -910 1509 C ATOM 21 O ILE A 40 -3.182 30.502 151.755 1.00 55.41 O ANISOU 21 O ILE A 40 7703 8969 4380 675 -869 1570 O ATOM 22 CB ILE A 40 -4.434 27.974 150.152 1.00 58.80 C ANISOU 22 CB ILE A 40 8051 9692 4600 420 -1099 1407 C ATOM 23 CG1 ILE A 40 -5.455 27.493 149.119 1.00 60.02 C ANISOU 23 CG1 ILE A 40 8132 10024 4650 370 -1232 1422 C ATOM 24 CG2 ILE A 40 -5.049 28.000 151.544 1.00 58.24 C ANISOU 24 CG2 ILE A 40 7840 9645 4644 469 -1079 1417 C ATOM 25 CD1 ILE A 40 -5.183 26.105 148.588 1.00 59.92 C ANISOU 25 CD1 ILE A 40 8189 10029 4549 212 -1264 1272 C ATOM 26 N GLY A 41 -1.605 29.448 150.546 1.00 53.87 N ANISOU 26 N GLY A 41 7724 8688 4058 486 -841 1421 N ATOM 27 CA GLY A 41 -0.522 29.797 151.445 1.00 50.47 C ANISOU 27 CA GLY A 41 7360 8102 3715 495 -720 1392 C ATOM 28 C GLY A 41 -0.204 31.279 151.465 1.00 50.99 C ANISOU 28 C GLY A 41 7464 8080 3829 609 -655 1521 C ATOM 29 O GLY A 41 0.177 31.823 152.499 1.00 50.85 O ANISOU 29 O GLY A 41 7448 7963 3911 665 -572 1531 O ATOM 30 N ALA A 42 -0.360 31.939 150.323 1.00 52.35 N ANISOU 30 N ALA A 42 7676 8284 3929 646 -691 1620 N ATOM 31 CA ALA A 42 -0.032 33.356 150.218 1.00 51.97 C ANISOU 31 CA ALA A 42 7681 8142 3922 752 -626 1748 C ATOM 32 C ALA A 42 -1.060 34.227 150.929 1.00 52.78 C ANISOU 32 C ALA A 42 7681 8260 4112 912 -634 1856 C ATOM 33 O ALA A 42 -0.760 35.350 151.331 1.00 52.58 O ANISOU 33 O ALA A 42 7701 8114 4161 1014 -552 1937 O ATOM 34 CB ALA A 42 0.083 33.765 148.759 1.00 53.00 C ANISOU 34 CB ALA A 42 7889 8306 3944 742 -662 1825 C ATOM 35 N GLN A 43 -2.273 33.709 151.081 1.00 53.86 N ANISOU 35 N GLN A 43 7681 8543 4242 937 -727 1857 N ATOM 36 CA GLN A 43 -3.346 34.482 151.692 1.00 55.34 C ANISOU 36 CA GLN A 43 7751 8768 4506 1098 -735 1964 C ATOM 37 C GLN A 43 -3.472 34.198 153.182 1.00 52.43 C ANISOU 37 C GLN A 43 7317 8365 4240 1124 -681 1900 C ATOM 38 O GLN A 43 -3.973 35.026 153.941 1.00 52.50 O ANISOU 38 O GLN A 43 7278 8335 4334 1272 -635 1979 O ATOM 39 CB GLN A 43 -4.677 34.192 150.997 1.00 59.86 C ANISOU 39 CB GLN A 43 8188 9540 5016 1122 -867 2022 C ATOM 40 CG GLN A 43 -4.577 34.044 149.491 1.00 64.12 C ANISOU 40 CG GLN A 43 8792 10146 5424 1052 -943 2044 C ATOM 41 CD GLN A 43 -5.847 33.480 148.886 1.00 67.45 C ANISOU 41 CD GLN A 43 9074 10779 5775 1037 -1082 2067 C ATOM 42 OE1 GLN A 43 -6.791 33.148 149.603 1.00 67.84 O ANISOU 42 OE1 GLN A 43 8967 10932 5877 1067 -1120 2063 O ATOM 43 NE2 GLN A 43 -5.877 33.370 147.563 1.00 69.12 N ANISOU 43 NE2 GLN A 43 9339 11061 5862 986 -1157 2091 N ATOM 44 N LEU A 44 -3.004 33.026 153.596 1.00 49.46 N ANISOU 44 N LEU A 44 6948 7995 3849 984 -682 1758 N ATOM 45 CA LEU A 44 -3.189 32.566 154.967 1.00 46.36 C ANISOU 45 CA LEU A 44 6485 7595 3535 988 -645 1689 C ATOM 46 C LEU A 44 -1.934 32.699 155.830 1.00 43.46 C ANISOU 46 C LEU A 44 6236 7051 3227 960 -527 1616 C ATOM 47 O LEU A 44 -2.002 33.172 156.962 1.00 42.60 O ANISOU 47 O LEU A 44 6113 6871 3202 1050 -458 1629 O ATOM 48 CB LEU A 44 -3.657 31.110 154.966 1.00 45.48 C ANISOU 48 CB LEU A 44 6288 7618 3375 851 -730 1580 C ATOM 49 CG LEU A 44 -3.678 30.405 156.321 1.00 43.85 C ANISOU 49 CG LEU A 44 6027 7401 3232 816 -693 1488 C ATOM 50 CD1 LEU A 44 -4.732 31.019 157.231 1.00 44.40 C ANISOU 50 CD1 LEU A 44 5965 7529 3377 964 -682 1576 C ATOM 51 CD2 LEU A 44 -3.910 28.913 156.142 1.00 43.48 C ANISOU 51 CD2 LEU A 44 5937 7455 3131 653 -767 1370 C ATOM 52 N LEU A 45 -0.792 32.277 155.297 1.00 41.89 N ANISOU 52 N LEU A 45 6149 6784 2982 838 -501 1540 N ATOM 53 CA LEU A 45 0.445 32.234 156.077 1.00 39.94 C ANISOU 53 CA LEU A 45 5995 6392 2787 788 -398 1460 C ATOM 54 C LEU A 45 0.968 33.604 156.540 1.00 40.85 C ANISOU 54 C LEU A 45 6193 6353 2976 897 -296 1539 C ATOM 55 O LEU A 45 1.415 33.724 157.681 1.00 40.47 O ANISOU 55 O LEU A 45 6173 6207 2998 912 -220 1492 O ATOM 56 CB LEU A 45 1.541 31.505 155.290 1.00 38.04 C ANISOU 56 CB LEU A 45 5846 6127 2481 641 -390 1373 C ATOM 57 CG LEU A 45 1.727 30.013 155.580 1.00 36.65 C ANISOU 57 CG LEU A 45 5650 5993 2284 513 -416 1230 C ATOM 58 CD1 LEU A 45 0.404 29.273 155.513 1.00 37.39 C ANISOU 58 CD1 LEU A 45 5629 6234 2344 506 -521 1220 C ATOM 59 CD2 LEU A 45 2.734 29.397 154.620 1.00 36.15 C ANISOU 59 CD2 LEU A 45 5684 5903 2147 396 -402 1162 C ATOM 60 N PRO A 46 0.936 34.636 155.669 1.00 42.89 N ANISOU 60 N PRO A 46 6502 6580 3216 967 -291 1655 N ATOM 61 CA PRO A 46 1.438 35.919 156.185 1.00 43.02 C ANISOU 61 CA PRO A 46 6612 6425 3309 1063 -185 1721 C ATOM 62 C PRO A 46 0.646 36.500 157.375 1.00 43.82 C ANISOU 62 C PRO A 46 6671 6481 3497 1210 -147 1760 C ATOM 63 O PRO A 46 1.289 36.939 158.329 1.00 43.34 O ANISOU 63 O PRO A 46 6693 6271 3503 1227 -50 1727 O ATOM 64 CB PRO A 46 1.354 36.843 154.963 1.00 44.40 C ANISOU 64 CB PRO A 46 6837 6590 3442 1115 -199 1847 C ATOM 65 CG PRO A 46 1.465 35.928 153.801 1.00 44.63 C ANISOU 65 CG PRO A 46 6848 6747 3361 991 -283 1808 C ATOM 66 CD PRO A 46 0.735 34.681 154.208 1.00 43.88 C ANISOU 66 CD PRO A 46 6638 6788 3248 941 -362 1716 C ATOM 67 N PRO A 47 -0.702 36.504 157.339 1.00 45.18 N ANISOU 67 N PRO A 47 6719 6779 3669 1314 -216 1827 N ATOM 68 CA PRO A 47 -1.344 37.034 158.549 1.00 45.44 C ANISOU 68 CA PRO A 47 6718 6759 3787 1457 -159 1856 C ATOM 69 C PRO A 47 -1.274 36.082 159.744 1.00 44.58 C ANISOU 69 C PRO A 47 6563 6675 3699 1394 -145 1736 C ATOM 70 O PRO A 47 -1.215 36.544 160.884 1.00 43.74 O ANISOU 70 O PRO A 47 6501 6458 3659 1473 -60 1726 O ATOM 71 CB PRO A 47 -2.796 37.244 158.112 1.00 47.05 C ANISOU 71 CB PRO A 47 6778 7114 3983 1581 -238 1965 C ATOM 72 CG PRO A 47 -2.998 36.275 157.009 1.00 47.28 C ANISOU 72 CG PRO A 47 6736 7316 3914 1452 -359 1937 C ATOM 73 CD PRO A 47 -1.690 36.222 156.280 1.00 46.39 C ANISOU 73 CD PRO A 47 6766 7109 3752 1325 -332 1891 C ATOM 74 N LEU A 48 -1.280 34.777 159.488 1.00 44.37 N ANISOU 74 N LEU A 48 6462 6783 3613 1253 -224 1645 N ATOM 75 CA LEU A 48 -1.244 33.793 160.566 1.00 35.27 C ANISOU 75 CA LEU A 48 5262 5663 2476 1184 -217 1532 C ATOM 76 C LEU A 48 0.067 33.854 161.338 1.00 42.94 C ANISOU 76 C LEU A 48 6367 6465 3483 1120 -119 1443 C ATOM 77 O LEU A 48 0.071 33.963 162.564 1.00 42.12 O ANISOU 77 O LEU A 48 6257 6271 3473 1134 -56 1375 O ATOM 78 CB LEU A 48 -1.453 32.383 160.017 1.00 34.88 C ANISOU 78 CB LEU A 48 5128 5768 2358 1032 -318 1450 C ATOM 79 CG LEU A 48 -1.382 31.261 161.052 1.00 33.48 C ANISOU 79 CG LEU A 48 4906 5621 2193 942 -313 1330 C ATOM 80 CD1 LEU A 48 -2.480 31.428 162.086 1.00 33.84 C ANISOU 80 CD1 LEU A 48 4835 5718 2307 1041 -303 1357 C ATOM 81 CD2 LEU A 48 -1.472 29.901 160.381 1.00 33.27 C ANISOU 81 CD2 LEU A 48 4831 5709 2101 783 -403 1245 C ATOM 82 N TYR A 49 1.179 33.782 160.613 1.00 41.60 N ANISOU 82 N TYR A 49 6291 6233 3283 1016 -105 1408 N ATOM 83 CA TYR A 49 2.498 33.794 161.235 1.00 38.08 C ANISOU 83 CA TYR A 49 5956 5644 2869 940 -19 1325 C ATOM 84 C TYR A 49 2.777 35.127 161.918 1.00 39.00 C ANISOU 84 C TYR A 49 6167 5578 3075 1028 80 1365 C ATOM 85 O TYR A 49 3.472 35.179 162.931 1.00 38.73 O ANISOU 85 O TYR A 49 6179 5425 3113 974 146 1272 O ATOM 86 CB TYR A 49 3.585 33.496 160.201 1.00 35.68 C ANISOU 86 CB TYR A 49 5710 5326 2520 815 -23 1292 C ATOM 87 CG TYR A 49 3.559 32.079 159.675 1.00 34.26 C ANISOU 87 CG TYR A 49 5462 5275 2280 692 -99 1206 C ATOM 88 CD1 TYR A 49 2.850 31.083 160.336 1.00 30.84 C ANISOU 88 CD1 TYR A 49 4937 4933 1849 668 -147 1140 C ATOM 89 CD2 TYR A 49 4.247 31.735 158.520 1.00 33.90 C ANISOU 89 CD2 TYR A 49 5455 5251 2175 598 -116 1190 C ATOM 90 CE1 TYR A 49 2.825 29.786 159.857 1.00 34.32 C ANISOU 90 CE1 TYR A 49 5337 5465 2237 550 -210 1058 C ATOM 91 CE2 TYR A 49 4.228 30.440 158.035 1.00 33.34 C ANISOU 91 CE2 TYR A 49 5348 5272 2046 489 -175 1106 C ATOM 92 CZ TYR A 49 3.516 29.471 158.706 1.00 30.74 C ANISOU 92 CZ TYR A 49 4941 5015 1725 464 -222 1038 C ATOM 93 OH TYR A 49 3.495 28.184 158.225 1.00 30.56 O ANISOU 93 OH TYR A 49 4906 5058 1646 355 -275 951 O ATOM 94 N SER A 50 2.231 36.203 161.361 1.00 40.59 N ANISOU 94 N SER A 50 6400 5752 3272 1160 88 1500 N ATOM 95 CA SER A 50 2.386 37.524 161.959 1.00 42.61 C ANISOU 95 CA SER A 50 6757 5816 3616 1251 186 1540 C ATOM 96 C SER A 50 1.684 37.589 163.310 1.00 44.05 C ANISOU 96 C SER A 50 6882 5963 3891 1316 221 1480 C ATOM 97 O SER A 50 2.227 38.123 164.275 1.00 43.76 O ANISOU 97 O SER A 50 6932 5764 3931 1301 307 1414 O ATOM 98 CB SER A 50 1.837 38.606 161.030 1.00 44.20 C ANISOU 98 CB SER A 50 6999 6000 3795 1392 186 1707 C ATOM 99 OG SER A 50 2.501 38.583 159.779 1.00 44.74 O ANISOU 99 OG SER A 50 7098 6092 3811 1297 155 1729 O ATOM 100 N LEU A 51 0.477 37.034 163.371 1.00 46.29 N ANISOU 100 N LEU A 51 7019 6408 4162 1381 153 1502 N ATOM 101 CA LEU A 51 -0.306 37.027 164.600 1.00 47.23 C ANISOU 101 CA LEU A 51 7066 6521 4360 1449 187 1455 C ATOM 102 C LEU A 51 0.353 36.146 165.657 1.00 44.37 C ANISOU 102 C LEU A 51 6702 6132 4026 1307 207 1295 C ATOM 103 O LEU A 51 0.374 36.487 166.840 1.00 44.29 O ANISOU 103 O LEU A 51 6723 6016 4088 1331 281 1230 O ATOM 104 CB LEU A 51 -1.732 36.548 164.324 1.00 50.51 C ANISOU 104 CB LEU A 51 7303 7140 4746 1533 104 1523 C ATOM 105 CG LEU A 51 -2.788 36.962 165.349 1.00 55.18 C ANISOU 105 CG LEU A 51 7817 7729 5420 1673 155 1536 C ATOM 106 CD1 LEU A 51 -2.878 38.477 165.437 1.00 60.41 C ANISOU 106 CD1 LEU A 51 8592 8220 6142 1843 250 1627 C ATOM 107 CD2 LEU A 51 -4.140 36.365 164.994 1.00 57.05 C ANISOU 107 CD2 LEU A 51 7854 8198 5623 1730 62 1606 C ATOM 108 N VAL A 52 0.890 35.013 165.217 1.00 42.26 N ANISOU 108 N VAL A 52 6402 5959 3695 1165 144 1233 N ATOM 109 CA VAL A 52 1.634 34.121 166.098 1.00 39.91 C ANISOU 109 CA VAL A 52 6110 5637 3418 1030 158 1093 C ATOM 110 C VAL A 52 2.888 34.814 166.622 1.00 38.78 C ANISOU 110 C VAL A 52 6108 5308 3320 981 244 1041 C ATOM 111 O VAL A 52 3.231 34.696 167.798 1.00 38.66 O ANISOU 111 O VAL A 52 6111 5223 3355 938 288 946 O ATOM 112 CB VAL A 52 2.027 32.817 165.374 1.00 38.81 C ANISOU 112 CB VAL A 52 5927 5621 3199 900 81 1048 C ATOM 113 CG1 VAL A 52 3.007 32.010 166.206 1.00 28.17 C ANISOU 113 CG1 VAL A 52 4607 4223 1873 773 107 918 C ATOM 114 CG2 VAL A 52 0.787 31.997 165.056 1.00 30.06 C ANISOU 114 CG2 VAL A 52 4676 4698 2047 915 -7 1074 C ATOM 115 N PHE A 53 3.558 35.550 165.742 1.00 38.97 N ANISOU 115 N PHE A 53 6229 5257 3321 981 264 1106 N ATOM 116 CA PHE A 53 4.785 36.251 166.100 1.00 36.84 C ANISOU 116 CA PHE A 53 6090 4817 3089 916 342 1067 C ATOM 117 C PHE A 53 4.548 37.300 167.177 1.00 37.77 C ANISOU 117 C PHE A 53 6278 4783 3289 993 423 1052 C ATOM 118 O PHE A 53 5.326 37.410 168.122 1.00 37.67 O ANISOU 118 O PHE A 53 6327 4669 3318 913 472 957 O ATOM 119 CB PHE A 53 5.406 36.914 164.870 1.00 36.52 C ANISOU 119 CB PHE A 53 6138 4732 3006 910 354 1160 C ATOM 120 CG PHE A 53 6.635 37.721 165.175 1.00 36.21 C ANISOU 120 CG PHE A 53 6229 4520 3009 835 435 1131 C ATOM 121 CD1 PHE A 53 7.861 37.102 165.338 1.00 35.09 C ANISOU 121 CD1 PHE A 53 6094 4379 2859 686 441 1043 C ATOM 122 CD2 PHE A 53 6.565 39.099 165.298 1.00 37.33 C ANISOU 122 CD2 PHE A 53 6485 4497 3200 911 508 1194 C ATOM 123 CE1 PHE A 53 8.995 37.840 165.619 1.00 34.64 C ANISOU 123 CE1 PHE A 53 6142 4180 2840 602 510 1019 C ATOM 124 CE2 PHE A 53 7.696 39.842 165.579 1.00 37.02 C ANISOU 124 CE2 PHE A 53 6570 4297 3200 820 581 1164 C ATOM 125 CZ PHE A 53 8.912 39.210 165.740 1.00 35.36 C ANISOU 125 CZ PHE A 53 6350 4108 2979 660 578 1076 C ATOM 126 N ILE A 54 3.476 38.071 167.027 1.00 39.94 N ANISOU 126 N ILE A 54 6547 5045 3585 1151 439 1146 N ATOM 127 CA ILE A 54 3.171 39.147 167.962 1.00 42.41 C ANISOU 127 CA ILE A 54 6943 5200 3972 1246 529 1139 C ATOM 128 C ILE A 54 2.865 38.603 169.355 1.00 43.22 C ANISOU 128 C ILE A 54 6990 5321 4110 1227 547 1022 C ATOM 129 O ILE A 54 3.435 39.060 170.346 1.00 42.68 O ANISOU 129 O ILE A 54 7018 5115 4083 1183 615 937 O ATOM 130 CB ILE A 54 1.982 39.999 167.476 1.00 42.30 C ANISOU 130 CB ILE A 54 6916 5186 3972 1445 543 1276 C ATOM 131 CG1 ILE A 54 2.319 40.680 166.150 1.00 42.05 C ANISOU 131 CG1 ILE A 54 6964 5113 3902 1472 536 1402 C ATOM 132 CG2 ILE A 54 1.613 41.044 168.515 1.00 42.80 C ANISOU 132 CG2 ILE A 54 7069 5080 4112 1557 649 1257 C ATOM 133 CD1 ILE A 54 1.165 41.451 165.555 1.00 37.67 C ANISOU 133 CD1 ILE A 54 6386 4577 3350 1676 537 1556 C ATOM 134 N PHE A 55 1.971 37.622 169.424 1.00 44.68 N ANISOU 134 N PHE A 55 7022 5682 4273 1250 484 1019 N ATOM 135 CA PHE A 55 1.586 37.035 170.703 1.00 46.65 C ANISOU 135 CA PHE A 55 7209 5966 4548 1234 501 921 C ATOM 136 C PHE A 55 2.754 36.296 171.350 1.00 42.89 C ANISOU 136 C PHE A 55 6768 5467 4063 1061 494 797 C ATOM 137 O PHE A 55 2.976 36.402 172.556 1.00 42.20 O ANISOU 137 O PHE A 55 6724 5306 4005 1034 546 707 O ATOM 138 CB PHE A 55 0.402 36.079 170.531 1.00 52.38 C ANISOU 138 CB PHE A 55 7757 6895 5250 1275 430 954 C ATOM 139 CG PHE A 55 -0.906 36.766 170.246 1.00 60.73 C ANISOU 139 CG PHE A 55 8748 7997 6328 1461 444 1068 C ATOM 140 CD1 PHE A 55 -0.985 38.148 170.176 1.00 66.29 C ANISOU 140 CD1 PHE A 55 9563 8550 7073 1594 522 1136 C ATOM 141 CD2 PHE A 55 -2.061 36.025 170.054 1.00 64.93 C ANISOU 141 CD2 PHE A 55 9107 8724 6842 1503 379 1111 C ATOM 142 CE1 PHE A 55 -2.190 38.777 169.915 1.00 69.81 C ANISOU 142 CE1 PHE A 55 9943 9040 7542 1783 538 1251 C ATOM 143 CE2 PHE A 55 -3.268 36.647 169.793 1.00 68.55 C ANISOU 143 CE2 PHE A 55 9483 9243 7321 1680 388 1226 C ATOM 144 CZ PHE A 55 -3.332 38.024 169.723 1.00 70.20 C ANISOU 144 CZ PHE A 55 9799 9301 7571 1830 468 1299 C ATOM 145 N GLY A 56 3.498 35.549 170.542 1.00 41.20 N ANISOU 145 N GLY A 56 6533 5319 3801 951 431 793 N ATOM 146 CA GLY A 56 4.591 34.739 171.046 1.00 39.98 C ANISOU 146 CA GLY A 56 6391 5164 3635 801 418 690 C ATOM 147 C GLY A 56 5.781 35.544 171.523 1.00 39.42 C ANISOU 147 C GLY A 56 6451 4934 3593 732 479 641 C ATOM 148 O GLY A 56 6.421 35.193 172.516 1.00 27.08 O ANISOU 148 O GLY A 56 4904 3345 2041 644 491 545 O ATOM 149 N PHE A 57 6.083 36.624 170.813 1.00 39.23 N ANISOU 149 N PHE A 57 6523 4806 3579 765 515 710 N ATOM 150 CA PHE A 57 7.225 37.450 171.165 1.00 39.56 C ANISOU 150 CA PHE A 57 6692 4691 3646 682 573 670 C ATOM 151 C PHE A 57 6.994 38.137 172.504 1.00 40.97 C ANISOU 151 C PHE A 57 6945 4752 3870 712 639 600 C ATOM 152 O PHE A 57 7.802 37.999 173.417 1.00 43.84 O ANISOU 152 O PHE A 57 7343 5074 4239 603 651 502 O ATOM 153 CB PHE A 57 7.506 38.486 170.079 1.00 41.81 C ANISOU 153 CB PHE A 57 7072 4883 3932 712 604 771 C ATOM 154 CG PHE A 57 8.855 39.129 170.198 1.00 43.99 C ANISOU 154 CG PHE A 57 7461 5028 4226 586 650 735 C ATOM 155 CD1 PHE A 57 9.996 38.447 169.807 1.00 43.20 C ANISOU 155 CD1 PHE A 57 7326 4993 4096 448 618 707 C ATOM 156 CD2 PHE A 57 8.984 40.414 170.702 1.00 45.53 C ANISOU 156 CD2 PHE A 57 7797 5034 4467 601 729 729 C ATOM 157 CE1 PHE A 57 11.243 39.033 169.916 1.00 44.72 C ANISOU 157 CE1 PHE A 57 7602 5081 4307 324 659 679 C ATOM 158 CE2 PHE A 57 10.228 41.007 170.812 1.00 46.78 C ANISOU 158 CE2 PHE A 57 8057 5077 4642 464 768 695 C ATOM 159 CZ PHE A 57 11.359 40.317 170.417 1.00 46.36 C ANISOU 159 CZ PHE A 57 7948 5107 4560 322 730 673 C ATOM 160 N VAL A 58 5.885 38.860 172.625 1.00 37.80 N ANISOU 160 N VAL A 58 6565 4303 3496 864 683 651 N ATOM 161 CA VAL A 58 5.580 39.561 173.868 1.00 37.82 C ANISOU 161 CA VAL A 58 6650 4186 3535 910 760 583 C ATOM 162 C VAL A 58 5.314 38.575 175.005 1.00 37.89 C ANISOU 162 C VAL A 58 6570 4296 3529 873 739 486 C ATOM 163 O VAL A 58 5.516 38.896 176.174 1.00 37.92 O ANISOU 163 O VAL A 58 6649 4216 3542 843 789 395 O ATOM 164 CB VAL A 58 4.365 40.509 173.712 1.00 37.47 C ANISOU 164 CB VAL A 58 6637 4077 3525 1108 821 669 C ATOM 165 CG1 VAL A 58 4.597 41.481 172.566 1.00 38.76 C ANISOU 165 CG1 VAL A 58 6893 4136 3698 1153 842 780 C ATOM 166 CG2 VAL A 58 3.081 39.723 173.493 1.00 37.11 C ANISOU 166 CG2 VAL A 58 6420 4214 3466 1221 773 725 C ATOM 167 N GLY A 59 4.874 37.370 174.654 1.00 37.39 N ANISOU 167 N GLY A 59 6359 4411 3437 868 664 506 N ATOM 168 CA GLY A 59 4.588 36.347 175.642 1.00 35.45 C ANISOU 168 CA GLY A 59 6026 4267 3175 831 643 430 C ATOM 169 C GLY A 59 5.851 35.820 176.290 1.00 36.27 C ANISOU 169 C GLY A 59 6163 4357 3259 670 621 333 C ATOM 170 O GLY A 59 6.015 35.904 177.508 1.00 37.33 O ANISOU 170 O GLY A 59 6343 4448 3392 637 656 248 O ATOM 171 N ASN A 60 6.748 35.277 175.473 1.00 37.19 N ANISOU 171 N ASN A 60 6255 4520 3356 575 566 348 N ATOM 172 CA ASN A 60 8.005 34.730 175.971 1.00 36.85 C ANISOU 172 CA ASN A 60 6223 4481 3296 430 540 272 C ATOM 173 C ASN A 60 8.953 35.809 176.479 1.00 36.66 C ANISOU 173 C ASN A 60 6330 4310 3290 360 589 224 C ATOM 174 O ASN A 60 9.818 35.539 177.309 1.00 36.99 O ANISOU 174 O ASN A 60 6386 4349 3318 252 577 146 O ATOM 175 CB ASN A 60 8.698 33.907 174.886 1.00 37.79 C ANISOU 175 CB ASN A 60 6280 4687 3391 362 481 307 C ATOM 176 CG ASN A 60 8.035 32.566 174.666 1.00 40.44 C ANISOU 176 CG ASN A 60 6495 5170 3700 380 424 316 C ATOM 177 OD1 ASN A 60 8.285 31.609 175.401 1.00 40.38 O ANISOU 177 OD1 ASN A 60 6443 5221 3680 322 399 257 O ATOM 178 ND2 ASN A 60 7.188 32.484 173.646 1.00 40.87 N ANISOU 178 ND2 ASN A 60 6501 5285 3743 455 401 392 N ATOM 179 N MET A 61 8.796 37.029 175.976 1.00 36.51 N ANISOU 179 N MET A 61 6407 4167 3298 417 642 274 N ATOM 180 CA MET A 61 9.606 38.138 176.456 1.00 37.80 C ANISOU 180 CA MET A 61 6712 4171 3480 344 696 227 C ATOM 181 C MET A 61 9.185 38.496 177.875 1.00 38.85 C ANISOU 181 C MET A 61 6909 4239 3612 366 743 137 C ATOM 182 O MET A 61 10.025 38.799 178.722 1.00 38.59 O ANISOU 182 O MET A 61 6953 4141 3569 252 754 51 O ATOM 183 CB MET A 61 9.476 39.353 175.538 1.00 38.89 C ANISOU 183 CB MET A 61 6952 4178 3648 406 748 311 C ATOM 184 CG MET A 61 10.630 40.334 175.640 1.00 39.98 C ANISOU 184 CG MET A 61 7224 4164 3802 282 788 279 C ATOM 185 SD MET A 61 12.200 39.578 175.185 1.00 45.45 S ANISOU 185 SD MET A 61 7844 4953 4473 94 724 264 S ATOM 186 CE MET A 61 11.798 38.911 173.575 1.00 50.36 C ANISOU 186 CE MET A 61 8361 5699 5076 176 683 388 C ATOM 187 N LEU A 62 7.880 38.453 178.128 1.00 39.95 N ANISOU 187 N LEU A 62 7014 4407 3758 511 772 159 N ATOM 188 CA LEU A 62 7.351 38.727 179.459 1.00 40.31 C ANISOU 188 CA LEU A 62 7114 4406 3796 551 828 78 C ATOM 189 C LEU A 62 7.799 37.657 180.440 1.00 44.49 C ANISOU 189 C LEU A 62 7578 5045 4282 445 778 -7 C ATOM 190 O LEU A 62 8.102 37.951 181.595 1.00 46.72 O ANISOU 190 O LEU A 62 7943 5271 4539 390 808 -101 O ATOM 191 CB LEU A 62 5.825 38.812 179.433 1.00 37.51 C ANISOU 191 CB LEU A 62 6707 4086 3461 737 871 133 C ATOM 192 CG LEU A 62 5.239 40.213 179.621 1.00 38.56 C ANISOU 192 CG LEU A 62 6977 4046 3628 863 977 144 C ATOM 193 CD1 LEU A 62 5.743 41.169 178.546 1.00 40.33 C ANISOU 193 CD1 LEU A 62 7299 4141 3885 862 992 217 C ATOM 194 CD2 LEU A 62 3.722 40.157 179.629 1.00 39.18 C ANISOU 194 CD2 LEU A 62 6968 4193 3725 1054 1016 206 C ATOM 195 N VAL A 63 7.836 36.415 179.971 1.00 43.47 N ANISOU 195 N VAL A 63 7309 5070 4137 419 702 28 N ATOM 196 CA VAL A 63 8.333 35.303 180.770 1.00 42.51 C ANISOU 196 CA VAL A 63 7123 5054 3976 322 650 -34 C ATOM 197 C VAL A 63 9.777 35.551 181.200 1.00 43.02 C ANISOU 197 C VAL A 63 7257 5067 4023 171 629 -100 C ATOM 198 O VAL A 63 10.125 35.376 182.368 1.00 44.39 O ANISOU 198 O VAL A 63 7458 5250 4160 105 625 -180 O ATOM 199 CB VAL A 63 8.238 33.975 179.993 1.00 25.50 C ANISOU 199 CB VAL A 63 4826 3049 1815 316 577 21 C ATOM 200 CG1 VAL A 63 9.041 32.886 180.682 1.00 24.60 C ANISOU 200 CG1 VAL A 63 4663 3020 1665 207 523 -33 C ATOM 201 CG2 VAL A 63 6.782 33.562 179.835 1.00 25.54 C ANISOU 201 CG2 VAL A 63 4744 3133 1826 439 586 70 C ATOM 202 N VAL A 64 10.607 35.977 180.254 1.00 42.20 N ANISOU 202 N VAL A 64 7177 4916 3942 113 616 -61 N ATOM 203 CA VAL A 64 12.014 36.251 180.527 1.00 40.99 C ANISOU 203 CA VAL A 64 7071 4726 3778 -41 594 -111 C ATOM 204 C VAL A 64 12.187 37.429 181.484 1.00 42.28 C ANISOU 204 C VAL A 64 7385 4745 3934 -85 650 -191 C ATOM 205 O VAL A 64 12.969 37.355 182.434 1.00 44.36 O ANISOU 205 O VAL A 64 7674 5021 4161 -202 625 -271 O ATOM 206 CB VAL A 64 12.790 36.535 179.225 1.00 41.61 C ANISOU 206 CB VAL A 64 7143 4783 3884 -88 583 -43 C ATOM 207 CG1 VAL A 64 14.184 37.059 179.533 1.00 42.25 C ANISOU 207 CG1 VAL A 64 7280 4812 3962 -250 575 -91 C ATOM 208 CG2 VAL A 64 12.864 35.280 178.371 1.00 40.56 C ANISOU 208 CG2 VAL A 64 6873 4796 3743 -73 525 15 C ATOM 209 N LEU A 65 11.454 38.509 181.232 1.00 42.16 N ANISOU 209 N LEU A 65 7475 4595 3950 10 726 -169 N ATOM 210 CA LEU A 65 11.514 39.693 182.085 1.00 43.80 C ANISOU 210 CA LEU A 65 7851 4640 4152 -19 795 -249 C ATOM 211 C LEU A 65 11.176 39.345 183.530 1.00 41.63 C ANISOU 211 C LEU A 65 7590 4405 3822 -22 801 -346 C ATOM 212 O LEU A 65 11.818 39.827 184.461 1.00 42.62 O ANISOU 212 O LEU A 65 7818 4466 3909 -135 809 -443 O ATOM 213 CB LEU A 65 10.564 40.779 181.570 1.00 46.64 C ANISOU 213 CB LEU A 65 8312 4852 4556 127 885 -197 C ATOM 214 CG LEU A 65 10.944 41.454 180.250 1.00 47.85 C ANISOU 214 CG LEU A 65 8504 4921 4757 123 898 -105 C ATOM 215 CD1 LEU A 65 9.852 42.415 179.799 1.00 48.66 C ANISOU 215 CD1 LEU A 65 8694 4893 4901 299 984 -38 C ATOM 216 CD2 LEU A 65 12.280 42.173 180.375 1.00 48.77 C ANISOU 216 CD2 LEU A 65 8728 4928 4872 -63 899 -157 C ATOM 217 N ILE A 66 10.171 38.496 183.706 1.00 38.27 N ANISOU 217 N ILE A 66 7062 4093 3387 94 797 -319 N ATOM 218 CA ILE A 66 9.769 38.054 185.032 1.00 35.66 C ANISOU 218 CA ILE A 66 6731 3818 2999 100 808 -397 C ATOM 219 C ILE A 66 10.866 37.226 185.692 1.00 37.32 C ANISOU 219 C ILE A 66 6891 4134 3154 -55 722 -450 C ATOM 220 O ILE A 66 11.230 37.470 186.841 1.00 39.27 O ANISOU 220 O ILE A 66 7221 4358 3343 -134 728 -544 O ATOM 221 CB ILE A 66 8.471 37.233 184.974 1.00 33.54 C ANISOU 221 CB ILE A 66 6344 3663 2737 245 819 -342 C ATOM 222 CG1 ILE A 66 7.290 38.145 184.639 1.00 33.41 C ANISOU 222 CG1 ILE A 66 6381 3549 2764 414 914 -301 C ATOM 223 CG2 ILE A 66 8.227 36.521 186.293 1.00 31.63 C ANISOU 223 CG2 ILE A 66 6079 3510 2428 226 817 -410 C ATOM 224 CD1 ILE A 66 5.995 37.407 184.410 1.00 33.27 C ANISOU 224 CD1 ILE A 66 6226 3655 2762 553 921 -230 C ATOM 225 N LEU A 67 11.405 36.260 184.955 1.00 36.86 N ANISOU 225 N LEU A 67 6701 4192 3110 -96 644 -388 N ATOM 226 CA LEU A 67 12.425 35.364 185.494 1.00 36.11 C ANISOU 226 CA LEU A 67 6539 4212 2971 -220 561 -418 C ATOM 227 C LEU A 67 13.701 36.102 185.893 1.00 38.90 C ANISOU 227 C LEU A 67 6975 4502 3301 -379 539 -483 C ATOM 228 O LEU A 67 14.454 35.633 186.746 1.00 39.06 O ANISOU 228 O LEU A 67 6972 4602 3266 -481 481 -532 O ATOM 229 CB LEU A 67 12.756 34.266 184.482 1.00 31.63 C ANISOU 229 CB LEU A 67 5825 3761 2432 -217 497 -336 C ATOM 230 CG LEU A 67 11.668 33.213 184.267 1.00 29.48 C ANISOU 230 CG LEU A 67 5451 3585 2164 -104 494 -284 C ATOM 231 CD1 LEU A 67 12.056 32.264 183.150 1.00 29.66 C ANISOU 231 CD1 LEU A 67 5361 3696 2214 -110 438 -212 C ATOM 232 CD2 LEU A 67 11.401 32.446 185.550 1.00 25.25 C ANISOU 232 CD2 LEU A 67 4894 3129 1569 -111 480 -330 C ATOM 233 N ILE A 68 13.937 37.258 185.282 1.00 41.10 N ANISOU 233 N ILE A 68 7352 4642 3622 -403 583 -479 N ATOM 234 CA ILE A 68 15.143 38.030 185.557 1.00 42.83 C ANISOU 234 CA ILE A 68 7652 4794 3826 -571 565 -537 C ATOM 235 C ILE A 68 14.905 39.130 186.595 1.00 47.74 C ANISOU 235 C ILE A 68 8455 5275 4409 -604 627 -643 C ATOM 236 O ILE A 68 15.757 39.382 187.447 1.00 49.39 O ANISOU 236 O ILE A 68 8719 5486 4563 -754 591 -727 O ATOM 237 CB ILE A 68 15.706 38.662 184.264 1.00 40.48 C ANISOU 237 CB ILE A 68 7365 4421 3595 -609 579 -470 C ATOM 238 CG1 ILE A 68 16.037 37.571 183.243 1.00 37.41 C ANISOU 238 CG1 ILE A 68 6807 4174 3234 -586 522 -376 C ATOM 239 CG2 ILE A 68 16.944 39.492 184.560 1.00 41.22 C ANISOU 239 CG2 ILE A 68 7539 4445 3677 -801 563 -530 C ATOM 240 CD1 ILE A 68 16.715 38.086 181.995 1.00 35.85 C ANISOU 240 CD1 ILE A 68 6608 3926 3086 -637 533 -308 C ATOM 241 N ASN A 69 13.741 39.770 186.537 1.00 51.30 N ANISOU 241 N ASN A 69 9000 5609 4884 -461 721 -641 N ATOM 242 CA ASN A 69 13.474 40.927 187.387 1.00 55.60 C ANISOU 242 CA ASN A 69 9740 5987 5397 -474 802 -741 C ATOM 243 C ASN A 69 12.534 40.649 188.560 1.00 54.96 C ANISOU 243 C ASN A 69 9690 5939 5252 -382 844 -806 C ATOM 244 O ASN A 69 12.263 41.540 189.366 1.00 57.31 O ANISOU 244 O ASN A 69 10156 6106 5511 -384 919 -900 O ATOM 245 CB ASN A 69 12.912 42.072 186.544 1.00 60.45 C ANISOU 245 CB ASN A 69 10470 6412 6084 -375 898 -696 C ATOM 246 CG ASN A 69 13.931 42.627 185.564 1.00 65.41 C ANISOU 246 CG ASN A 69 11120 6970 6763 -495 876 -651 C ATOM 247 OD1 ASN A 69 15.136 42.579 185.812 1.00 67.87 O ANISOU 247 OD1 ASN A 69 11420 7320 7047 -684 810 -695 O ATOM 248 ND2 ASN A 69 13.451 43.158 184.445 1.00 68.98 N ANISOU 248 ND2 ASN A 69 11596 7326 7286 -387 930 -556 N ATOM 249 N CYS A 70 12.039 39.421 188.660 1.00 52.14 N ANISOU 249 N CYS A 70 9179 5752 4880 -306 803 -758 N ATOM 250 CA CYS A 70 11.200 39.039 189.792 1.00 52.40 C ANISOU 250 CA CYS A 70 9225 5839 4846 -233 841 -811 C ATOM 251 C CYS A 70 11.762 37.809 190.499 1.00 51.18 C ANISOU 251 C CYS A 70 8958 5867 4620 -322 743 -823 C ATOM 252 O CYS A 70 11.970 37.824 191.711 1.00 51.94 O ANISOU 252 O CYS A 70 9113 5987 4634 -390 735 -908 O ATOM 253 CB CYS A 70 9.761 38.781 189.340 1.00 51.93 C ANISOU 253 CB CYS A 70 9097 5799 4836 -28 909 -735 C ATOM 254 SG CYS A 70 8.898 40.256 188.744 1.00 87.30 S ANISOU 254 SG CYS A 70 13718 10066 9387 119 1040 -717 S ATOM 255 N LYS A 71 12.008 36.748 189.738 1.00 50.51 N ANISOU 255 N LYS A 71 8708 5911 4574 -317 668 -731 N ATOM 256 CA LYS A 71 12.586 35.527 190.290 1.00 50.53 C ANISOU 256 CA LYS A 71 8599 6078 4520 -388 577 -725 C ATOM 257 C LYS A 71 14.100 35.663 190.425 1.00 53.05 C ANISOU 257 C LYS A 71 8924 6422 4813 -567 491 -758 C ATOM 258 O LYS A 71 14.714 35.006 191.268 1.00 55.67 O ANISOU 258 O LYS A 71 9206 6866 5079 -646 419 -781 O ATOM 259 CB LYS A 71 12.239 34.321 189.414 1.00 48.82 C ANISOU 259 CB LYS A 71 8216 5977 4356 -309 538 -617 C ATOM 260 CG LYS A 71 11.158 33.405 189.986 1.00 48.28 C ANISOU 260 CG LYS A 71 8087 6001 4258 -209 562 -597 C ATOM 261 CD LYS A 71 11.732 32.468 191.040 1.00 48.97 C ANISOU 261 CD LYS A 71 8103 6211 4294 -283 487 -612 C ATOM 262 CE LYS A 71 10.738 31.380 191.434 1.00 48.55 C ANISOU 262 CE LYS A 71 7944 6257 4245 -193 497 -564 C ATOM 263 NZ LYS A 71 11.336 30.387 192.376 1.00 47.44 N1+ ANISOU 263 NZ LYS A 71 7720 6233 4073 -252 419 -557 N1+ ATOM 264 N LYS A 72 14.687 36.512 189.580 1.00 53.75 N ANISOU 264 N LYS A 72 9054 6409 4960 -624 498 -749 N ATOM 265 CA LYS A 72 16.120 36.835 189.604 1.00 54.74 C ANISOU 265 CA LYS A 72 9183 6544 5071 -804 429 -778 C ATOM 266 C LYS A 72 16.983 35.592 189.314 1.00 51.81 C ANISOU 266 C LYS A 72 8633 6351 4702 -849 327 -709 C ATOM 267 O LYS A 72 18.181 35.570 189.582 1.00 50.83 O ANISOU 267 O LYS A 72 8473 6290 4549 -993 253 -729 O ATOM 268 CB LYS A 72 16.487 37.497 190.954 1.00 57.82 C ANISOU 268 CB LYS A 72 9709 6895 5363 -925 424 -903 C ATOM 269 CG LYS A 72 17.911 38.077 191.063 1.00 61.22 C ANISOU 269 CG LYS A 72 10167 7320 5775 -1134 357 -949 C ATOM 270 CD LYS A 72 18.199 38.710 192.413 1.00 65.55 C ANISOU 270 CD LYS A 72 10826 7838 6241 -1247 345 -1063 C ATOM 271 CE LYS A 72 17.471 40.039 192.579 1.00 67.95 C ANISOU 271 CE LYS A 72 11330 7927 6562 -1210 460 -1135 C ATOM 272 NZ LYS A 72 17.998 41.059 191.624 1.00 68.72 N1+ ANISOU 272 NZ LYS A 72 11543 7867 6701 -1308 496 -1149 N1+ ATOM 273 N LEU A 73 16.360 34.572 188.730 1.00 49.23 N ANISOU 273 N LEU A 73 8192 6101 4412 -724 326 -627 N ATOM 274 CA LEU A 73 17.053 33.340 188.339 1.00 45.94 C ANISOU 274 CA LEU A 73 7617 5832 4007 -737 247 -556 C ATOM 275 C LEU A 73 17.793 32.685 189.503 1.00 47.86 C ANISOU 275 C LEU A 73 7819 6199 4166 -822 168 -589 C ATOM 276 O LEU A 73 18.992 32.419 189.418 1.00 48.28 O ANISOU 276 O LEU A 73 7792 6335 4216 -920 96 -570 O ATOM 277 CB LEU A 73 18.040 33.618 187.200 1.00 41.68 C ANISOU 277 CB LEU A 73 7024 5282 3531 -806 226 -508 C ATOM 278 CG LEU A 73 17.465 34.178 185.897 1.00 38.37 C ANISOU 278 CG LEU A 73 6631 4757 3189 -726 293 -455 C ATOM 279 CD1 LEU A 73 18.571 34.393 184.873 1.00 37.91 C ANISOU 279 CD1 LEU A 73 6518 4707 3179 -810 272 -408 C ATOM 280 CD2 LEU A 73 16.396 33.255 185.342 1.00 35.54 C ANISOU 280 CD2 LEU A 73 6202 4446 2856 -574 311 -391 C ATOM 281 N LYS A 74 17.078 32.441 190.593 1.00 50.57 N ANISOU 281 N LYS A 74 8213 6563 4438 -782 183 -632 N ATOM 282 CA LYS A 74 17.696 31.918 191.802 1.00 52.15 C ANISOU 282 CA LYS A 74 8355 6872 4588 -841 107 -649 C ATOM 283 C LYS A 74 17.496 30.412 191.933 1.00 47.95 C ANISOU 283 C LYS A 74 7686 6465 4070 -750 69 -569 C ATOM 284 O LYS A 74 18.298 29.725 192.567 1.00 47.45 O ANISOU 284 O LYS A 74 7544 6511 3974 -792 -9 -548 O ATOM 285 CB LYS A 74 17.136 32.634 193.035 1.00 55.59 C ANISOU 285 CB LYS A 74 8895 7248 4981 -843 145 -732 C ATOM 286 N CYS A 75 16.428 29.903 191.327 1.00 44.71 N ANISOU 286 N CYS A 75 7249 6032 3706 -626 123 -522 N ATOM 287 CA CYS A 75 16.111 28.481 191.402 1.00 40.67 C ANISOU 287 CA CYS A 75 6624 5615 3214 -544 98 -450 C ATOM 288 C CYS A 75 16.528 27.744 190.131 1.00 36.40 C ANISOU 288 C CYS A 75 6000 5108 2722 -523 76 -376 C ATOM 289 O CYS A 75 16.626 28.340 189.058 1.00 35.88 O ANISOU 289 O CYS A 75 5967 4982 2682 -537 103 -373 O ATOM 290 CB CYS A 75 14.615 28.282 191.657 1.00 39.98 C ANISOU 290 CB CYS A 75 6551 5499 3141 -434 169 -446 C ATOM 291 SG CYS A 75 14.094 26.549 191.755 1.00111.96 S ANISOU 291 SG CYS A 75 15546 14715 12280 -350 150 -363 S ATOM 292 N LEU A 76 16.777 26.445 190.266 1.00 33.96 N ANISOU 292 N LEU A 76 5594 4890 2420 -486 33 -317 N ATOM 293 CA LEU A 76 17.120 25.594 189.130 1.00 32.12 C ANISOU 293 CA LEU A 76 5285 4689 2231 -453 19 -248 C ATOM 294 C LEU A 76 16.032 25.627 188.067 1.00 32.57 C ANISOU 294 C LEU A 76 5354 4679 2341 -377 81 -229 C ATOM 295 O LEU A 76 16.315 25.673 186.869 1.00 33.00 O ANISOU 295 O LEU A 76 5395 4717 2425 -377 88 -201 O ATOM 296 CB LEU A 76 17.344 24.152 189.591 1.00 31.07 C ANISOU 296 CB LEU A 76 5071 4641 2092 -407 -22 -192 C ATOM 297 CG LEU A 76 17.165 23.056 188.534 1.00 28.85 C ANISOU 297 CG LEU A 76 4733 4369 1862 -338 -11 -127 C ATOM 298 CD1 LEU A 76 18.357 23.014 187.601 1.00 27.95 C ANISOU 298 CD1 LEU A 76 4578 4288 1752 -378 -39 -98 C ATOM 299 CD2 LEU A 76 16.934 21.695 189.174 1.00 29.06 C ANISOU 299 CD2 LEU A 76 4719 4442 1880 -281 -27 -80 C ATOM 300 N THR A 77 14.783 25.609 188.516 1.00 33.35 N ANISOU 300 N THR A 77 5474 4752 2444 -315 125 -241 N ATOM 301 CA THR A 77 13.649 25.563 187.608 1.00 33.25 C ANISOU 301 CA THR A 77 5461 4700 2475 -243 176 -217 C ATOM 302 C THR A 77 13.506 26.887 186.858 1.00 35.38 C ANISOU 302 C THR A 77 5814 4881 2748 -251 220 -243 C ATOM 303 O THR A 77 12.904 26.938 185.789 1.00 36.47 O ANISOU 303 O THR A 77 5939 4990 2927 -197 247 -208 O ATOM 304 CB THR A 77 12.341 25.225 188.363 1.00 34.86 C ANISOU 304 CB THR A 77 5659 4915 2671 -184 216 -220 C ATOM 305 OG1 THR A 77 11.427 24.571 187.476 1.00 37.26 O ANISOU 305 OG1 THR A 77 5916 5228 3014 -126 236 -173 O ATOM 306 CG2 THR A 77 11.687 26.476 188.932 1.00 36.41 C ANISOU 306 CG2 THR A 77 5949 5048 2838 -174 275 -278 C ATOM 307 N ASP A 78 14.082 27.952 187.407 1.00 36.25 N ANISOU 307 N ASP A 78 6006 4945 2823 -319 223 -300 N ATOM 308 CA ASP A 78 14.057 29.250 186.741 1.00 36.84 C ANISOU 308 CA ASP A 78 6145 4916 2938 -324 264 -319 C ATOM 309 C ASP A 78 14.983 29.240 185.530 1.00 34.68 C ANISOU 309 C ASP A 78 5817 4644 2715 -360 235 -274 C ATOM 310 O ASP A 78 14.730 29.916 184.534 1.00 34.39 O ANISOU 310 O ASP A 78 5804 4538 2726 -331 270 -250 O ATOM 311 CB ASP A 78 14.462 30.365 187.706 1.00 40.32 C ANISOU 311 CB ASP A 78 6693 5294 3332 -402 276 -400 C ATOM 312 CG ASP A 78 13.587 30.413 188.939 1.00 44.63 C ANISOU 312 CG ASP A 78 7303 5839 3815 -366 314 -451 C ATOM 313 OD1 ASP A 78 12.397 30.043 188.836 1.00 49.66 O ANISOU 313 OD1 ASP A 78 7918 6483 4467 -263 361 -423 O ATOM 314 OD2 ASP A 78 14.089 30.815 190.010 1.00 43.89 O1+ ANISOU 314 OD2 ASP A 78 7258 5746 3672 -440 295 -514 O1+ ATOM 315 N ILE A 79 16.055 28.462 185.626 1.00 32.94 N ANISOU 315 N ILE A 79 5524 4509 2482 -416 175 -255 N ATOM 316 CA ILE A 79 17.017 28.345 184.540 1.00 33.12 C ANISOU 316 CA ILE A 79 5484 4551 2548 -447 154 -211 C ATOM 317 C ILE A 79 16.401 27.645 183.334 1.00 32.03 C ANISOU 317 C ILE A 79 5298 4422 2452 -360 173 -152 C ATOM 318 O ILE A 79 16.534 28.110 182.201 1.00 32.35 O ANISOU 318 O ILE A 79 5338 4422 2530 -354 195 -122 O ATOM 319 CB ILE A 79 18.274 27.577 184.987 1.00 34.64 C ANISOU 319 CB ILE A 79 5597 4849 2718 -509 89 -199 C ATOM 320 CG1 ILE A 79 18.927 28.279 186.180 1.00 36.53 C ANISOU 320 CG1 ILE A 79 5879 5097 2904 -613 55 -259 C ATOM 321 CG2 ILE A 79 19.260 27.446 183.838 1.00 34.27 C ANISOU 321 CG2 ILE A 79 5476 4829 2717 -531 81 -150 C ATOM 322 CD1 ILE A 79 19.336 29.711 185.895 1.00 37.34 C ANISOU 322 CD1 ILE A 79 6052 5110 3025 -700 79 -297 C ATOM 323 N TYR A 80 15.721 26.531 183.586 1.00 30.84 N ANISOU 323 N TYR A 80 5110 4322 2287 -299 165 -134 N ATOM 324 CA TYR A 80 15.109 25.752 182.515 1.00 20.82 C ANISOU 324 CA TYR A 80 3798 3066 1045 -231 175 -87 C ATOM 325 C TYR A 80 13.999 26.529 181.808 1.00 25.97 C ANISOU 325 C TYR A 80 4491 3655 1722 -176 219 -78 C ATOM 326 O TYR A 80 13.912 26.519 180.581 1.00 26.59 O ANISOU 326 O TYR A 80 4550 3725 1826 -150 227 -39 O ATOM 327 CB TYR A 80 14.553 24.439 183.060 1.00 20.39 C ANISOU 327 CB TYR A 80 3709 3068 968 -193 160 -75 C ATOM 328 CG TYR A 80 15.598 23.455 183.540 1.00 20.85 C ANISOU 328 CG TYR A 80 3721 3192 1009 -221 117 -61 C ATOM 329 CD1 TYR A 80 16.932 23.581 183.172 1.00 20.77 C ANISOU 329 CD1 TYR A 80 3673 3206 1011 -263 94 -49 C ATOM 330 CD2 TYR A 80 15.242 22.392 184.360 1.00 20.53 C ANISOU 330 CD2 TYR A 80 3647 3190 964 -191 101 -50 C ATOM 331 CE1 TYR A 80 17.883 22.674 183.614 1.00 20.72 C ANISOU 331 CE1 TYR A 80 3612 3270 991 -272 56 -26 C ATOM 332 CE2 TYR A 80 16.182 21.483 184.804 1.00 20.39 C ANISOU 332 CE2 TYR A 80 3592 3228 927 -201 64 -26 C ATOM 333 CZ TYR A 80 17.498 21.626 184.430 1.00 20.60 C ANISOU 333 CZ TYR A 80 3594 3287 946 -239 40 -13 C ATOM 334 OH TYR A 80 18.424 20.712 184.880 1.00 20.86 O ANISOU 334 OH TYR A 80 3575 3385 965 -232 3 21 O ATOM 335 N LEU A 81 13.148 27.195 182.584 1.00 21.26 N ANISOU 335 N LEU A 81 3948 3017 1112 -151 251 -109 N ATOM 336 CA LEU A 81 12.074 28.008 182.018 1.00 23.22 C ANISOU 336 CA LEU A 81 4231 3207 1386 -83 296 -94 C ATOM 337 C LEU A 81 12.636 29.141 181.167 1.00 23.85 C ANISOU 337 C LEU A 81 4357 3210 1494 -104 315 -81 C ATOM 338 O LEU A 81 12.047 29.522 180.156 1.00 22.59 O ANISOU 338 O LEU A 81 4201 3023 1361 -47 336 -37 O ATOM 339 CB LEU A 81 11.186 28.580 183.126 1.00 22.07 C ANISOU 339 CB LEU A 81 4140 3027 1219 -47 339 -135 C ATOM 340 CG LEU A 81 10.321 27.593 183.910 1.00 21.80 C ANISOU 340 CG LEU A 81 4063 3064 1157 -14 340 -137 C ATOM 341 CD1 LEU A 81 9.704 28.281 185.116 1.00 24.79 C ANISOU 341 CD1 LEU A 81 4508 3408 1505 10 391 -188 C ATOM 342 CD2 LEU A 81 9.240 27.000 183.024 1.00 21.44 C ANISOU 342 CD2 LEU A 81 3948 3060 1137 55 343 -82 C ATOM 343 N LEU A 82 13.778 29.677 181.587 1.00 25.42 N ANISOU 343 N LEU A 82 4592 3380 1686 -192 305 -116 N ATOM 344 CA LEU A 82 14.455 30.727 180.837 1.00 25.44 C ANISOU 344 CA LEU A 82 4641 3308 1716 -236 324 -102 C ATOM 345 C LEU A 82 14.921 30.202 179.487 1.00 27.69 C ANISOU 345 C LEU A 82 4862 3639 2022 -232 308 -40 C ATOM 346 O LEU A 82 14.718 30.842 178.456 1.00 31.33 O ANISOU 346 O LEU A 82 5350 4049 2505 -204 336 2 O ATOM 347 CB LEU A 82 15.642 31.278 181.628 1.00 25.98 C ANISOU 347 CB LEU A 82 4745 3356 1768 -354 308 -155 C ATOM 348 CG LEU A 82 16.530 32.302 180.915 1.00 26.20 C ANISOU 348 CG LEU A 82 4816 3314 1825 -431 326 -141 C ATOM 349 CD1 LEU A 82 15.749 33.567 180.589 1.00 26.96 C ANISOU 349 CD1 LEU A 82 5024 3274 1946 -383 390 -138 C ATOM 350 CD2 LEU A 82 17.758 32.630 181.750 1.00 26.34 C ANISOU 350 CD2 LEU A 82 4841 3344 1821 -568 293 -194 C ATOM 351 N ASN A 83 15.544 29.028 179.499 1.00 25.44 N ANISOU 351 N ASN A 83 4496 3448 1724 -254 267 -34 N ATOM 352 CA ASN A 83 16.021 28.408 178.270 1.00 26.59 C ANISOU 352 CA ASN A 83 4584 3640 1880 -246 260 16 C ATOM 353 C ASN A 83 14.878 27.943 177.370 1.00 27.05 C ANISOU 353 C ASN A 83 4630 3711 1937 -159 267 54 C ATOM 354 O ASN A 83 15.009 27.932 176.145 1.00 21.06 O ANISOU 354 O ASN A 83 3862 2958 1181 -145 276 97 O ATOM 355 CB ASN A 83 16.943 27.237 178.600 1.00 25.52 C ANISOU 355 CB ASN A 83 4372 3594 1733 -277 222 12 C ATOM 356 CG ASN A 83 18.320 27.689 179.050 1.00 24.85 C ANISOU 356 CG ASN A 83 4269 3523 1651 -372 208 -4 C ATOM 357 OD1 ASN A 83 18.911 28.597 178.463 1.00 23.83 O ANISOU 357 OD1 ASN A 83 4160 3354 1540 -424 231 9 O ATOM 358 ND2 ASN A 83 18.831 27.069 180.107 1.00 24.21 N ANISOU 358 ND2 ASN A 83 4148 3504 1549 -400 168 -27 N ATOM 359 N LEU A 84 13.760 27.561 177.979 1.00 27.24 N ANISOU 359 N LEU A 84 4651 3747 1950 -107 263 40 N ATOM 360 CA LEU A 84 12.583 27.166 177.217 1.00 20.61 C ANISOU 360 CA LEU A 84 3792 2932 1109 -35 263 75 C ATOM 361 C LEU A 84 12.012 28.369 176.482 1.00 38.61 C ANISOU 361 C LEU A 84 6117 5149 3403 10 294 111 C ATOM 362 O LEU A 84 11.592 28.262 175.328 1.00 40.67 O ANISOU 362 O LEU A 84 6362 5433 3658 48 288 160 O ATOM 363 CB LEU A 84 11.525 26.546 178.131 1.00 20.41 C ANISOU 363 CB LEU A 84 3744 2940 1072 0 257 55 C ATOM 364 CG LEU A 84 10.206 26.139 177.472 1.00 20.36 C ANISOU 364 CG LEU A 84 3699 2974 1062 62 251 90 C ATOM 365 CD1 LEU A 84 10.461 25.182 176.328 1.00 20.00 C ANISOU 365 CD1 LEU A 84 3619 2979 1002 48 221 114 C ATOM 366 CD2 LEU A 84 9.275 25.507 178.491 1.00 20.27 C ANISOU 366 CD2 LEU A 84 3659 3002 1042 80 252 70 C ATOM 367 N ALA A 85 12.007 29.516 177.157 1.00 36.61 N ANISOU 367 N ALA A 85 5931 4815 3166 7 327 89 N ATOM 368 CA ALA A 85 11.531 30.759 176.562 1.00 34.59 C ANISOU 368 CA ALA A 85 5737 4477 2930 57 366 128 C ATOM 369 C ALA A 85 12.429 31.174 175.410 1.00 37.18 C ANISOU 369 C ALA A 85 6085 4781 3263 17 371 171 C ATOM 370 O ALA A 85 11.953 31.645 174.377 1.00 37.71 O ANISOU 370 O ALA A 85 6169 4829 3331 72 384 233 O ATOM 371 CB ALA A 85 11.467 31.860 177.602 1.00 31.57 C ANISOU 371 CB ALA A 85 5440 3994 2560 53 410 82 C ATOM 372 N ILE A 86 13.732 30.994 175.597 1.00 36.55 N ANISOU 372 N ILE A 86 5996 4710 3181 -78 362 144 N ATOM 373 CA ILE A 86 14.709 31.326 174.569 1.00 22.91 C ANISOU 373 CA ILE A 86 4275 2971 1457 -128 374 184 C ATOM 374 C ILE A 86 14.515 30.442 173.341 1.00 34.08 C ANISOU 374 C ILE A 86 5635 4468 2846 -88 356 232 C ATOM 375 O ILE A 86 14.629 30.905 172.206 1.00 33.51 O ANISOU 375 O ILE A 86 5588 4380 2766 -78 376 289 O ATOM 376 CB ILE A 86 16.149 31.184 175.101 1.00 25.35 C ANISOU 376 CB ILE A 86 4560 3301 1772 -239 364 146 C ATOM 377 CG1 ILE A 86 16.439 32.281 176.126 1.00 23.71 C ANISOU 377 CG1 ILE A 86 4427 3001 1580 -302 383 98 C ATOM 378 CG2 ILE A 86 17.159 31.257 173.969 1.00 25.56 C ANISOU 378 CG2 ILE A 86 4565 3348 1799 -286 381 193 C ATOM 379 CD1 ILE A 86 17.867 32.294 176.621 1.00 24.02 C ANISOU 379 CD1 ILE A 86 4436 3070 1622 -426 366 66 C ATOM 380 N SER A 87 14.199 29.173 173.576 1.00 21.74 N ANISOU 380 N SER A 87 4007 2987 1264 -68 320 209 N ATOM 381 CA SER A 87 13.951 28.235 172.490 1.00 27.72 C ANISOU 381 CA SER A 87 4725 3818 1989 -37 301 239 C ATOM 382 C SER A 87 12.821 28.723 171.592 1.00 29.69 C ANISOU 382 C SER A 87 4997 4061 2222 34 301 294 C ATOM 383 O SER A 87 12.948 28.725 170.369 1.00 30.25 O ANISOU 383 O SER A 87 5076 4156 2263 41 303 340 O ATOM 384 CB SER A 87 13.620 26.849 173.043 1.00 27.28 C ANISOU 384 CB SER A 87 4615 3830 1921 -29 266 201 C ATOM 385 OG SER A 87 14.734 26.291 173.716 1.00 27.87 O ANISOU 385 OG SER A 87 4661 3923 2004 -82 263 165 O ATOM 386 N ASP A 88 11.722 29.148 172.207 1.00 31.86 N ANISOU 386 N ASP A 88 5281 4311 2513 89 300 293 N ATOM 387 CA ASP A 88 10.570 29.630 171.457 1.00 34.49 C ANISOU 387 CA ASP A 88 5619 4651 2834 170 295 355 C ATOM 388 C ASP A 88 10.904 30.896 170.683 1.00 32.67 C ANISOU 388 C ASP A 88 5460 4344 2610 185 332 415 C ATOM 389 O ASP A 88 10.480 31.062 169.540 1.00 33.49 O ANISOU 389 O ASP A 88 5567 4476 2682 228 321 483 O ATOM 390 CB ASP A 88 9.388 29.880 172.391 1.00 39.79 C ANISOU 390 CB ASP A 88 6277 5312 3529 235 299 343 C ATOM 391 CG ASP A 88 8.813 28.596 172.952 1.00 46.41 C ANISOU 391 CG ASP A 88 7042 6238 4355 227 263 304 C ATOM 392 OD1 ASP A 88 9.557 27.595 173.024 1.00 48.65 O ANISOU 392 OD1 ASP A 88 7303 6557 4623 162 243 266 O ATOM 393 OD2 ASP A 88 7.617 28.587 173.319 1.00 50.76 O1+ ANISOU 393 OD2 ASP A 88 7554 6820 4912 286 259 315 O1+ ATOM 394 N LEU A 89 11.668 31.785 171.309 1.00 30.33 N ANISOU 394 N LEU A 89 5226 3949 2350 141 373 393 N ATOM 395 CA LEU A 89 12.082 33.024 170.661 1.00 29.74 C ANISOU 395 CA LEU A 89 5232 3781 2286 137 417 449 C ATOM 396 C LEU A 89 12.966 32.738 169.454 1.00 30.43 C ANISOU 396 C LEU A 89 5310 3913 2338 87 417 489 C ATOM 397 O LEU A 89 12.748 33.286 168.374 1.00 31.93 O ANISOU 397 O LEU A 89 5538 4090 2505 125 430 568 O ATOM 398 CB LEU A 89 12.817 33.929 171.648 1.00 24.93 C ANISOU 398 CB LEU A 89 4694 3058 1720 71 459 401 C ATOM 399 CG LEU A 89 11.964 34.486 172.785 1.00 26.56 C ANISOU 399 CG LEU A 89 4942 3194 1955 128 480 363 C ATOM 400 CD1 LEU A 89 12.827 35.259 173.764 1.00 27.39 C ANISOU 400 CD1 LEU A 89 5125 3195 2088 37 515 299 C ATOM 401 CD2 LEU A 89 10.859 35.369 172.227 1.00 27.77 C ANISOU 401 CD2 LEU A 89 5144 3289 2118 250 509 439 C ATOM 402 N LEU A 90 13.955 31.869 169.642 1.00 29.33 N ANISOU 402 N LEU A 90 5122 3831 2192 9 406 440 N ATOM 403 CA LEU A 90 14.842 31.463 168.556 1.00 29.52 C ANISOU 403 CA LEU A 90 5127 3908 2180 -33 416 470 C ATOM 404 C LEU A 90 14.047 30.906 167.385 1.00 31.90 C ANISOU 404 C LEU A 90 5414 4287 2421 32 389 517 C ATOM 405 O LEU A 90 14.478 30.980 166.236 1.00 35.21 O ANISOU 405 O LEU A 90 5851 4730 2796 21 408 567 O ATOM 406 CB LEU A 90 15.849 30.420 169.041 1.00 27.94 C ANISOU 406 CB LEU A 90 4861 3772 1984 -99 406 408 C ATOM 407 CG LEU A 90 16.956 30.895 169.982 1.00 26.97 C ANISOU 407 CG LEU A 90 4737 3604 1905 -187 427 370 C ATOM 408 CD1 LEU A 90 17.785 29.713 170.453 1.00 25.60 C ANISOU 408 CD1 LEU A 90 4481 3514 1731 -224 406 322 C ATOM 409 CD2 LEU A 90 17.831 31.927 169.292 1.00 27.32 C ANISOU 409 CD2 LEU A 90 4826 3595 1958 -249 478 420 C ATOM 410 N PHE A 91 12.880 30.353 167.688 1.00 30.60 N ANISOU 410 N PHE A 91 5214 4166 2247 92 343 501 N ATOM 411 CA PHE A 91 12.017 29.774 166.671 1.00 31.40 C ANISOU 411 CA PHE A 91 5292 4352 2285 141 303 538 C ATOM 412 C PHE A 91 11.186 30.843 165.972 1.00 33.21 C ANISOU 412 C PHE A 91 5564 4555 2500 215 304 629 C ATOM 413 O PHE A 91 11.157 30.911 164.744 1.00 33.41 O ANISOU 413 O PHE A 91 5609 4622 2463 229 297 690 O ATOM 414 CB PHE A 91 11.101 28.720 167.297 1.00 32.34 C ANISOU 414 CB PHE A 91 5348 4538 2403 160 252 488 C ATOM 415 CG PHE A 91 10.295 27.939 166.297 1.00 33.46 C ANISOU 415 CG PHE A 91 5460 4779 2475 181 202 509 C ATOM 416 CD1 PHE A 91 9.050 28.385 165.887 1.00 34.44 C ANISOU 416 CD1 PHE A 91 5568 4939 2579 250 167 570 C ATOM 417 CD2 PHE A 91 10.779 26.748 165.777 1.00 33.91 C ANISOU 417 CD2 PHE A 91 5472 4895 2519 124 183 460 C ATOM 418 CE1 PHE A 91 8.306 27.665 164.969 1.00 35.01 C ANISOU 418 CE1 PHE A 91 5597 5113 2590 249 107 584 C ATOM 419 CE2 PHE A 91 10.038 26.022 164.861 1.00 33.71 C ANISOU 419 CE2 PHE A 91 5407 4954 2446 119 132 464 C ATOM 420 CZ PHE A 91 8.799 26.482 164.457 1.00 34.06 C ANISOU 420 CZ PHE A 91 5446 5042 2454 171 89 524 C ATOM 421 N LEU A 92 10.517 31.685 166.753 1.00 34.42 N ANISOU 421 N LEU A 92 5735 4637 2705 270 317 640 N ATOM 422 CA LEU A 92 9.519 32.587 166.190 1.00 37.65 C ANISOU 422 CA LEU A 92 6171 5030 3105 368 313 732 C ATOM 423 C LEU A 92 10.117 33.822 165.512 1.00 38.10 C ANISOU 423 C LEU A 92 6323 4988 3164 371 367 809 C ATOM 424 O LEU A 92 9.426 34.502 164.755 1.00 39.29 O ANISOU 424 O LEU A 92 6502 5135 3291 454 363 904 O ATOM 425 CB LEU A 92 8.517 33.006 167.273 1.00 41.29 C ANISOU 425 CB LEU A 92 6615 5451 3622 443 318 718 C ATOM 426 CG LEU A 92 8.992 33.734 168.531 1.00 44.66 C ANISOU 426 CG LEU A 92 7101 5750 4119 420 376 662 C ATOM 427 CD1 LEU A 92 8.960 35.243 168.337 1.00 47.82 C ANISOU 427 CD1 LEU A 92 7605 6015 4550 476 435 730 C ATOM 428 CD2 LEU A 92 8.149 33.325 169.730 1.00 43.44 C ANISOU 428 CD2 LEU A 92 6892 5620 3995 458 366 603 C ATOM 429 N ILE A 93 11.393 34.111 165.755 1.00 36.87 N ANISOU 429 N ILE A 93 6214 4760 3036 279 416 775 N ATOM 430 CA ILE A 93 12.042 35.213 165.045 1.00 36.97 C ANISOU 430 CA ILE A 93 6318 4682 3047 260 472 851 C ATOM 431 C ILE A 93 12.276 34.843 163.584 1.00 37.37 C ANISOU 431 C ILE A 93 6363 4822 3012 254 459 917 C ATOM 432 O ILE A 93 12.593 35.699 162.757 1.00 39.20 O ANISOU 432 O ILE A 93 6670 5002 3224 256 499 1003 O ATOM 433 CB ILE A 93 13.390 35.614 165.678 1.00 37.03 C ANISOU 433 CB ILE A 93 6365 4601 3105 143 526 798 C ATOM 434 CG1 ILE A 93 14.362 34.432 165.656 1.00 36.00 C ANISOU 434 CG1 ILE A 93 6156 4572 2950 54 510 733 C ATOM 435 CG2 ILE A 93 13.184 36.153 167.089 1.00 37.65 C ANISOU 435 CG2 ILE A 93 6473 4578 3254 142 543 734 C ATOM 436 CD1 ILE A 93 15.762 34.789 166.094 1.00 36.45 C ANISOU 436 CD1 ILE A 93 6228 4574 3047 -66 557 698 C ATOM 437 N THR A 94 12.121 33.561 163.272 1.00 36.26 N ANISOU 437 N THR A 94 6147 4813 2818 243 407 874 N ATOM 438 CA THR A 94 12.295 33.076 161.911 1.00 34.69 C ANISOU 438 CA THR A 94 5928 4710 2542 229 388 911 C ATOM 439 C THR A 94 10.989 33.182 161.122 1.00 33.98 C ANISOU 439 C THR A 94 5812 4688 2410 316 325 981 C ATOM 440 O THR A 94 10.998 33.179 159.891 1.00 34.95 O ANISOU 440 O THR A 94 5926 4872 2482 309 306 1030 O ATOM 441 CB THR A 94 12.787 31.614 161.891 1.00 33.42 C ANISOU 441 CB THR A 94 5680 4649 2369 163 360 814 C ATOM 442 OG1 THR A 94 11.742 30.745 162.344 1.00 31.94 O ANISOU 442 OG1 THR A 94 5429 4528 2179 197 293 766 O ATOM 443 CG2 THR A 94 14.005 31.447 162.789 1.00 32.52 C ANISOU 443 CG2 THR A 94 5574 4484 2297 89 412 750 C ATOM 444 N LEU A 95 9.873 33.283 161.841 1.00 32.48 N ANISOU 444 N LEU A 95 5607 4497 2237 397 293 987 N ATOM 445 CA LEU A 95 8.546 33.376 161.227 1.00 33.93 C ANISOU 445 CA LEU A 95 5747 4760 2384 487 227 1059 C ATOM 446 C LEU A 95 8.380 34.483 160.170 1.00 36.60 C ANISOU 446 C LEU A 95 6139 5066 2700 543 238 1182 C ATOM 447 O LEU A 95 7.784 34.229 159.122 1.00 36.03 O ANISOU 447 O LEU A 95 6020 5099 2569 557 173 1227 O ATOM 448 CB LEU A 95 7.475 33.557 162.310 1.00 28.94 C ANISOU 448 CB LEU A 95 5086 4114 1795 578 214 1057 C ATOM 449 CG LEU A 95 7.171 32.364 163.219 1.00 27.82 C ANISOU 449 CG LEU A 95 4854 4039 1676 534 176 947 C ATOM 450 CD1 LEU A 95 6.058 32.712 164.193 1.00 28.01 C ANISOU 450 CD1 LEU A 95 4828 4048 1765 621 171 951 C ATOM 451 CD2 LEU A 95 6.803 31.136 162.402 1.00 27.67 C ANISOU 451 CD2 LEU A 95 4764 4168 1579 487 99 923 C ATOM 452 N PRO A 96 8.885 35.712 160.432 1.00 39.14 N ANISOU 452 N PRO A 96 6565 5239 3065 569 318 1239 N ATOM 453 CA PRO A 96 8.707 36.745 159.402 1.00 32.51 C ANISOU 453 CA PRO A 96 5779 4365 2209 623 329 1362 C ATOM 454 C PRO A 96 9.329 36.377 158.057 1.00 41.28 C ANISOU 454 C PRO A 96 6873 5560 3253 542 310 1376 C ATOM 455 O PRO A 96 8.842 36.816 157.015 1.00 43.59 O ANISOU 455 O PRO A 96 7169 5892 3500 587 278 1470 O ATOM 456 CB PRO A 96 9.415 37.962 160.002 1.00 32.96 C ANISOU 456 CB PRO A 96 5965 4228 2330 622 430 1392 C ATOM 457 CG PRO A 96 9.354 37.749 161.459 1.00 31.99 C ANISOU 457 CG PRO A 96 5840 4048 2268 619 451 1300 C ATOM 458 CD PRO A 96 9.502 36.273 161.649 1.00 38.83 C ANISOU 458 CD PRO A 96 6601 5054 3101 546 394 1193 C ATOM 459 N LEU A 97 10.387 35.575 158.083 1.00 38.77 N ANISOU 459 N LEU A 97 6534 5271 2925 429 332 1286 N ATOM 460 CA LEU A 97 11.046 35.156 156.854 1.00 37.35 C ANISOU 460 CA LEU A 97 6340 5173 2680 355 328 1291 C ATOM 461 C LEU A 97 10.242 34.085 156.126 1.00 38.15 C ANISOU 461 C LEU A 97 6361 5430 2704 351 233 1262 C ATOM 462 O LEU A 97 10.137 34.112 154.901 1.00 39.92 O ANISOU 462 O LEU A 97 6591 5722 2854 338 205 1315 O ATOM 463 CB LEU A 97 12.458 34.648 157.144 1.00 35.36 C ANISOU 463 CB LEU A 97 6085 4904 2447 250 392 1209 C ATOM 464 CG LEU A 97 13.559 35.712 157.162 1.00 36.16 C ANISOU 464 CG LEU A 97 6269 4884 2586 206 489 1259 C ATOM 465 CD1 LEU A 97 13.459 36.599 158.395 1.00 36.04 C ANISOU 465 CD1 LEU A 97 6326 4718 2649 234 531 1266 C ATOM 466 CD2 LEU A 97 14.934 35.069 157.066 1.00 35.63 C ANISOU 466 CD2 LEU A 97 6171 4852 2515 103 541 1194 C ATOM 467 N TRP A 98 9.674 33.145 156.875 1.00 37.59 N ANISOU 467 N TRP A 98 6224 5411 2648 350 184 1178 N ATOM 468 CA TRP A 98 8.883 32.084 156.261 1.00 38.13 C ANISOU 468 CA TRP A 98 6228 5614 2647 327 94 1142 C ATOM 469 C TRP A 98 7.593 32.653 155.684 1.00 40.70 C ANISOU 469 C TRP A 98 6542 5988 2932 412 23 1243 C ATOM 470 O TRP A 98 7.122 32.212 154.634 1.00 42.23 O ANISOU 470 O TRP A 98 6722 6282 3042 385 -45 1257 O ATOM 471 CB TRP A 98 8.565 30.972 157.267 1.00 35.25 C ANISOU 471 CB TRP A 98 5799 5282 2313 301 64 1034 C ATOM 472 CG TRP A 98 9.759 30.452 158.024 1.00 32.95 C ANISOU 472 CG TRP A 98 5509 4938 2074 238 130 941 C ATOM 473 CD1 TRP A 98 9.882 30.343 159.379 1.00 32.26 C ANISOU 473 CD1 TRP A 98 5411 4788 2057 247 155 885 C ATOM 474 CD2 TRP A 98 10.995 29.975 157.470 1.00 31.02 C ANISOU 474 CD2 TRP A 98 5272 4704 1809 163 180 897 C ATOM 475 NE1 TRP A 98 11.112 29.825 159.703 1.00 30.74 N ANISOU 475 NE1 TRP A 98 5218 4569 1893 180 209 813 N ATOM 476 CE2 TRP A 98 11.815 29.593 158.550 1.00 30.05 C ANISOU 476 CE2 TRP A 98 5137 4527 1755 135 228 821 C ATOM 477 CE3 TRP A 98 11.486 29.832 156.168 1.00 29.64 C ANISOU 477 CE3 TRP A 98 5112 4587 1563 124 190 918 C ATOM 478 CZ2 TRP A 98 13.097 29.081 158.368 1.00 29.66 C ANISOU 478 CZ2 TRP A 98 5082 4480 1709 79 285 771 C ATOM 479 CZ3 TRP A 98 12.758 29.324 155.991 1.00 31.17 C ANISOU 479 CZ3 TRP A 98 5302 4783 1759 72 256 864 C ATOM 480 CH2 TRP A 98 13.550 28.954 157.085 1.00 30.42 C ANISOU 480 CH2 TRP A 98 5187 4634 1739 54 302 794 C ATOM 481 N ALA A 99 7.031 33.640 156.375 1.00 41.07 N ANISOU 481 N ALA A 99 6602 5962 3040 519 40 1313 N ATOM 482 CA ALA A 99 5.786 34.265 155.947 1.00 42.51 C ANISOU 482 CA ALA A 99 6759 6191 3202 627 -20 1421 C ATOM 483 C ALA A 99 6.008 35.119 154.707 1.00 44.33 C ANISOU 483 C ALA A 99 7053 6408 3383 642 -13 1529 C ATOM 484 O ALA A 99 5.136 35.216 153.843 1.00 46.67 O ANISOU 484 O ALA A 99 7321 6794 3619 685 -89 1600 O ATOM 485 CB ALA A 99 5.202 35.104 157.071 1.00 43.61 C ANISOU 485 CB ALA A 99 6901 6243 3426 751 16 1466 C ATOM 486 N HIS A 100 7.179 35.739 154.627 1.00 43.19 N ANISOU 486 N HIS A 100 6993 6155 3264 603 78 1542 N ATOM 487 CA HIS A 100 7.520 36.566 153.479 1.00 44.58 C ANISOU 487 CA HIS A 100 7236 6309 3394 605 99 1646 C ATOM 488 C HIS A 100 7.759 35.709 152.241 1.00 43.58 C ANISOU 488 C HIS A 100 7094 6310 3155 509 49 1616 C ATOM 489 O HIS A 100 7.436 36.114 151.126 1.00 45.06 O ANISOU 489 O HIS A 100 7308 6543 3269 527 13 1705 O ATOM 490 CB HIS A 100 8.753 37.417 153.777 1.00 45.42 C ANISOU 490 CB HIS A 100 7434 6264 3559 572 215 1663 C ATOM 491 CG HIS A 100 9.187 38.269 152.624 1.00 46.69 C ANISOU 491 CG HIS A 100 7666 6397 3676 564 246 1771 C ATOM 492 ND1 HIS A 100 10.142 37.858 151.716 1.00 46.99 N ANISOU 492 ND1 HIS A 100 7715 6493 3646 458 270 1750 N ATOM 493 CD2 HIS A 100 8.794 39.498 152.229 1.00 47.96 C ANISOU 493 CD2 HIS A 100 7892 6481 3850 651 262 1902 C ATOM 494 CE1 HIS A 100 10.316 38.804 150.813 1.00 48.98 C ANISOU 494 CE1 HIS A 100 8036 6707 3866 473 297 1866 C ATOM 495 NE2 HIS A 100 9.514 39.812 151.097 1.00 49.78 N ANISOU 495 NE2 HIS A 100 8174 6723 4017 588 291 1960 N ATOM 496 N SER A 101 8.326 34.524 152.445 1.00 36.19 N ANISOU 496 N SER A 101 6123 5425 2204 410 52 1491 N ATOM 497 CA SER A 101 8.610 33.610 151.345 1.00 41.14 C ANISOU 497 CA SER A 101 6747 6158 2724 315 18 1444 C ATOM 498 C SER A 101 7.330 33.029 150.763 1.00 43.04 C ANISOU 498 C SER A 101 6956 6513 2885 329 -102 1447 C ATOM 499 O SER A 101 7.246 32.764 149.564 1.00 45.45 O ANISOU 499 O SER A 101 7297 6890 3081 284 -143 1463 O ATOM 500 CB SER A 101 9.527 32.480 151.809 1.00 40.33 C ANISOU 500 CB SER A 101 6614 6070 2640 222 61 1309 C ATOM 501 OG SER A 101 10.691 32.997 152.423 1.00 41.90 O ANISOU 501 OG SER A 101 6836 6169 2916 213 165 1304 O ATOM 502 N ALA A 102 6.335 32.827 151.619 1.00 41.58 N ANISOU 502 N ALA A 102 6706 6343 2749 389 -156 1430 N ATOM 503 CA ALA A 102 5.052 32.299 151.179 1.00 41.71 C ANISOU 503 CA ALA A 102 6676 6473 2701 409 -272 1434 C ATOM 504 C ALA A 102 4.318 33.324 150.320 1.00 44.13 C ANISOU 504 C ALA A 102 6993 6810 2963 501 -319 1579 C ATOM 505 O ALA A 102 3.590 32.966 149.394 1.00 44.55 O ANISOU 505 O ALA A 102 7039 6968 2920 492 -410 1597 O ATOM 506 CB ALA A 102 4.205 31.898 152.375 1.00 40.24 C ANISOU 506 CB ALA A 102 6397 6305 2586 456 -306 1391 C ATOM 507 N ALA A 103 4.517 34.601 150.633 1.00 45.02 N ANISOU 507 N ALA A 103 7134 6825 3146 592 -254 1681 N ATOM 508 CA ALA A 103 3.900 35.682 149.874 1.00 47.86 C ANISOU 508 CA ALA A 103 7514 7193 3478 693 -284 1830 C ATOM 509 C ALA A 103 4.649 35.929 148.568 1.00 49.81 C ANISOU 509 C ALA A 103 7854 7443 3629 626 -265 1874 C ATOM 510 O ALA A 103 4.045 36.246 147.543 1.00 51.63 O ANISOU 510 O ALA A 103 8098 7742 3775 661 -332 1962 O ATOM 511 CB ALA A 103 3.853 36.954 150.708 1.00 47.77 C ANISOU 511 CB ALA A 103 7521 7048 3581 818 -209 1919 C ATOM 512 N ASN A 104 5.969 35.780 148.614 1.00 50.25 N ANISOU 512 N ASN A 104 7966 7432 3695 531 -173 1815 N ATOM 513 CA ASN A 104 6.809 35.995 147.442 1.00 52.44 C ANISOU 513 CA ASN A 104 8324 7716 3885 461 -136 1852 C ATOM 514 C ASN A 104 7.668 34.772 147.138 1.00 52.58 C ANISOU 514 C ASN A 104 8349 7789 3842 323 -114 1721 C ATOM 515 O ASN A 104 7.162 33.733 146.709 1.00 52.52 O ANISOU 515 O ASN A 104 8329 7875 3750 273 -192 1646 O ATOM 516 CB ASN A 104 7.700 37.222 147.647 1.00 53.09 C ANISOU 516 CB ASN A 104 8470 7662 4041 490 -23 1936 C ATOM 517 CG ASN A 104 6.969 38.368 148.320 1.00 53.95 C ANISOU 517 CG ASN A 104 8581 7674 4245 631 -16 2038 C ATOM 518 OD1 ASN A 104 7.385 38.851 149.373 1.00 53.33 O ANISOU 518 OD1 ASN A 104 8517 7469 4277 659 62 2023 O ATOM 519 ND2 ASN A 104 5.871 38.807 147.716 1.00 55.49 N ANISOU 519 ND2 ASN A 104 8763 7925 4395 724 -97 2141 N ATOM 520 N GLU A 105 8.972 34.910 147.360 1.00 52.45 N ANISOU 520 N GLU A 105 8353 7708 3868 268 -3 1693 N ATOM 521 CA GLU A 105 9.919 33.812 147.205 1.00 52.53 C ANISOU 521 CA GLU A 105 8350 7768 3842 157 40 1573 C ATOM 522 C GLU A 105 11.160 34.109 148.035 1.00 50.03 C ANISOU 522 C GLU A 105 8021 7358 3631 143 159 1545 C ATOM 523 O GLU A 105 11.360 35.243 148.469 1.00 50.01 O ANISOU 523 O GLU A 105 8051 7247 3704 197 210 1627 O ATOM 524 CB GLU A 105 10.294 33.605 145.736 1.00 57.29 C ANISOU 524 CB GLU A 105 9010 8453 4306 89 40 1594 C ATOM 525 CG GLU A 105 11.137 34.725 145.147 1.00 61.66 C ANISOU 525 CG GLU A 105 9617 8957 4853 96 127 1706 C ATOM 526 CD GLU A 105 11.554 34.454 143.713 1.00 64.53 C ANISOU 526 CD GLU A 105 10033 9414 5071 24 135 1722 C ATOM 527 OE1 GLU A 105 11.111 33.432 143.145 1.00 65.29 O ANISOU 527 OE1 GLU A 105 10137 9605 5067 -27 68 1645 O ATOM 528 OE2 GLU A 105 12.326 35.262 143.153 1.00 65.90 O1+ ANISOU 528 OE2 GLU A 105 10250 9560 5228 16 213 1808 O1+ ATOM 529 N TRP A 106 11.993 33.097 148.256 1.00 47.54 N ANISOU 529 N TRP A 106 7665 7078 3319 74 204 1430 N ATOM 530 CA TRP A 106 13.188 33.277 149.074 1.00 44.24 C ANISOU 530 CA TRP A 106 7233 6577 2998 61 309 1396 C ATOM 531 C TRP A 106 14.216 34.153 148.366 1.00 44.27 C ANISOU 531 C TRP A 106 7290 6545 2983 38 401 1480 C ATOM 532 O TRP A 106 14.677 33.827 147.274 1.00 45.34 O ANISOU 532 O TRP A 106 7438 6766 3024 -8 422 1484 O ATOM 533 CB TRP A 106 13.811 31.930 149.437 1.00 41.34 C ANISOU 533 CB TRP A 106 6805 6264 2639 11 333 1257 C ATOM 534 CG TRP A 106 14.912 32.069 150.435 1.00 38.01 C ANISOU 534 CG TRP A 106 6367 5754 2321 3 424 1219 C ATOM 535 CD1 TRP A 106 16.250 32.116 150.179 1.00 36.42 C ANISOU 535 CD1 TRP A 106 6170 5544 2123 -38 523 1214 C ATOM 536 CD2 TRP A 106 14.769 32.206 151.854 1.00 36.05 C ANISOU 536 CD2 TRP A 106 6101 5416 2181 29 423 1184 C ATOM 537 NE1 TRP A 106 16.951 32.263 151.351 1.00 36.16 N ANISOU 537 NE1 TRP A 106 6122 5425 2195 -46 577 1179 N ATOM 538 CE2 TRP A 106 16.065 32.321 152.394 1.00 35.60 C ANISOU 538 CE2 TRP A 106 6041 5300 2186 -7 517 1157 C ATOM 539 CE3 TRP A 106 13.672 32.237 152.719 1.00 34.95 C ANISOU 539 CE3 TRP A 106 5947 5247 2087 78 353 1173 C ATOM 540 CZ2 TRP A 106 16.293 32.465 153.762 1.00 33.82 C ANISOU 540 CZ2 TRP A 106 5806 4984 2058 -5 538 1118 C ATOM 541 CZ3 TRP A 106 13.900 32.380 154.077 1.00 33.92 C ANISOU 541 CZ3 TRP A 106 5807 5025 2056 90 381 1133 C ATOM 542 CH2 TRP A 106 15.201 32.491 154.584 1.00 31.74 C ANISOU 542 CH2 TRP A 106 5538 4690 1833 44 470 1104 C ATOM 543 N VAL A 107 14.577 35.264 149.002 1.00 43.92 N ANISOU 543 N VAL A 107 7284 6374 3029 63 460 1546 N ATOM 544 CA VAL A 107 15.455 36.251 148.383 1.00 45.17 C ANISOU 544 CA VAL A 107 7503 6481 3180 35 547 1643 C ATOM 545 C VAL A 107 16.645 36.608 149.269 1.00 44.16 C ANISOU 545 C VAL A 107 7376 6250 3152 -8 651 1619 C ATOM 546 O VAL A 107 17.415 37.515 148.952 1.00 44.64 O ANISOU 546 O VAL A 107 7488 6247 3227 -43 731 1699 O ATOM 547 CB VAL A 107 14.685 37.545 148.053 1.00 46.06 C ANISOU 547 CB VAL A 107 7689 6518 3292 100 521 1783 C ATOM 548 CG1 VAL A 107 13.604 37.275 147.017 1.00 46.68 C ANISOU 548 CG1 VAL A 107 7772 6709 3257 133 419 1824 C ATOM 549 CG2 VAL A 107 14.080 38.136 149.319 1.00 44.77 C ANISOU 549 CG2 VAL A 107 7538 6230 3243 170 509 1788 C ATOM 550 N PHE A 108 16.799 35.888 150.374 1.00 42.93 N ANISOU 550 N PHE A 108 7167 6081 3064 -15 648 1510 N ATOM 551 CA PHE A 108 17.786 36.251 151.384 1.00 43.72 C ANISOU 551 CA PHE A 108 7272 6078 3260 -60 730 1485 C ATOM 552 C PHE A 108 19.134 35.559 151.180 1.00 43.68 C ANISOU 552 C PHE A 108 7216 6138 3243 -134 807 1428 C ATOM 553 O PHE A 108 20.106 35.868 151.867 1.00 43.01 O ANISOU 553 O PHE A 108 7128 5987 3228 -190 882 1417 O ATOM 554 CB PHE A 108 17.236 35.940 152.775 1.00 42.71 C ANISOU 554 CB PHE A 108 7121 5895 3211 -28 688 1408 C ATOM 555 CG PHE A 108 15.912 36.590 153.053 1.00 44.20 C ANISOU 555 CG PHE A 108 7352 6025 3418 58 621 1463 C ATOM 556 CD1 PHE A 108 15.850 37.884 153.544 1.00 45.19 C ANISOU 556 CD1 PHE A 108 7561 6000 3610 79 663 1539 C ATOM 557 CD2 PHE A 108 14.727 35.914 152.808 1.00 44.41 C ANISOU 557 CD2 PHE A 108 7336 6144 3394 116 522 1441 C ATOM 558 CE1 PHE A 108 14.632 38.489 153.793 1.00 45.81 C ANISOU 558 CE1 PHE A 108 7676 6023 3707 179 612 1594 C ATOM 559 CE2 PHE A 108 13.506 36.513 153.056 1.00 44.97 C ANISOU 559 CE2 PHE A 108 7431 6173 3481 205 464 1500 C ATOM 560 CZ PHE A 108 13.458 37.802 153.549 1.00 45.73 C ANISOU 560 CZ PHE A 108 7608 6121 3647 248 512 1579 C ATOM 561 N GLY A 109 19.191 34.631 150.232 1.00 43.94 N ANISOU 561 N GLY A 109 7210 6301 3185 -135 792 1392 N ATOM 562 CA GLY A 109 20.438 33.966 149.906 1.00 43.49 C ANISOU 562 CA GLY A 109 7107 6312 3107 -186 872 1345 C ATOM 563 C GLY A 109 20.559 32.581 150.506 1.00 42.25 C ANISOU 563 C GLY A 109 6878 6210 2964 -176 851 1213 C ATOM 564 O GLY A 109 19.703 32.150 151.278 1.00 40.84 O ANISOU 564 O GLY A 109 6684 6013 2821 -140 775 1156 O ATOM 565 N ASN A 110 21.632 31.884 150.148 1.00 43.10 N ANISOU 565 N ASN A 110 6944 6385 3046 -204 924 1169 N ATOM 566 CA ASN A 110 21.864 30.526 150.625 1.00 41.19 C ANISOU 566 CA ASN A 110 6643 6192 2817 -189 917 1049 C ATOM 567 C ASN A 110 22.359 30.502 152.068 1.00 40.64 C ANISOU 567 C ASN A 110 6534 6053 2854 -204 938 1009 C ATOM 568 O ASN A 110 21.927 29.671 152.868 1.00 38.67 O ANISOU 568 O ASN A 110 6255 5798 2639 -177 884 925 O ATOM 569 CB ASN A 110 22.865 29.812 149.713 1.00 41.64 C ANISOU 569 CB ASN A 110 6675 6341 2806 -205 999 1021 C ATOM 570 CG ASN A 110 23.106 28.375 150.125 1.00 41.87 C ANISOU 570 CG ASN A 110 6657 6408 2844 -180 999 899 C ATOM 571 OD1 ASN A 110 22.229 27.522 149.990 1.00 41.72 O ANISOU 571 OD1 ASN A 110 6647 6415 2789 -148 924 831 O ATOM 572 ND2 ASN A 110 24.305 28.096 150.625 1.00 42.53 N ANISOU 572 ND2 ASN A 110 6689 6496 2975 -199 1085 876 N ATOM 573 N ALA A 111 23.264 31.418 152.396 1.00 42.13 N ANISOU 573 N ALA A 111 6725 6189 3093 -257 1015 1072 N ATOM 574 CA ALA A 111 23.810 31.496 153.745 1.00 33.40 C ANISOU 574 CA ALA A 111 5587 5023 2081 -292 1038 1041 C ATOM 575 C ALA A 111 22.711 31.821 154.745 1.00 38.64 C ANISOU 575 C ALA A 111 6288 5598 2797 -267 951 1023 C ATOM 576 O ALA A 111 22.656 31.252 155.833 1.00 39.65 O ANISOU 576 O ALA A 111 6384 5710 2974 -262 922 951 O ATOM 577 CB ALA A 111 24.918 32.533 153.812 1.00 35.38 C ANISOU 577 CB ALA A 111 5839 5232 2370 -377 1136 1119 C ATOM 578 N MET A 112 21.830 32.737 154.362 1.00 38.90 N ANISOU 578 N MET A 112 6389 5576 2815 -246 912 1094 N ATOM 579 CA MET A 112 20.710 33.125 155.208 1.00 38.33 C ANISOU 579 CA MET A 112 6356 5422 2785 -209 837 1088 C ATOM 580 C MET A 112 19.719 31.973 155.356 1.00 36.14 C ANISOU 580 C MET A 112 6038 5210 2484 -146 746 1006 C ATOM 581 O MET A 112 19.063 31.834 156.389 1.00 35.36 O ANISOU 581 O MET A 112 5935 5068 2432 -123 694 963 O ATOM 582 CB MET A 112 20.013 34.357 154.631 1.00 39.01 C ANISOU 582 CB MET A 112 6525 5443 2856 -186 825 1195 C ATOM 583 CG MET A 112 19.434 35.294 155.673 1.00 39.56 C ANISOU 583 CG MET A 112 6658 5376 2996 -173 808 1219 C ATOM 584 SD MET A 112 20.706 35.980 156.746 1.00 55.02 S ANISOU 584 SD MET A 112 8641 7225 5039 -287 899 1210 S ATOM 585 CE MET A 112 19.758 37.209 157.641 1.00 52.79 C ANISOU 585 CE MET A 112 8471 6770 4816 -255 878 1249 C ATOM 586 N CYS A 113 19.620 31.148 154.319 1.00 34.97 N ANISOU 586 N CYS A 113 5863 5165 2260 -129 730 983 N ATOM 587 CA CYS A 113 18.739 29.986 154.340 1.00 35.22 C ANISOU 587 CA CYS A 113 5859 5259 2264 -91 650 903 C ATOM 588 C CYS A 113 19.208 28.944 155.349 1.00 34.97 C ANISOU 588 C CYS A 113 5773 5229 2286 -96 657 802 C ATOM 589 O CYS A 113 18.407 28.408 156.115 1.00 34.13 O ANISOU 589 O CYS A 113 5647 5112 2208 -72 591 746 O ATOM 590 CB CYS A 113 18.646 29.357 152.950 1.00 36.91 C ANISOU 590 CB CYS A 113 6073 5576 2377 -88 643 897 C ATOM 591 SG CYS A 113 17.811 27.755 152.916 1.00 40.09 S ANISOU 591 SG CYS A 113 6437 6054 2742 -67 565 782 S ATOM 592 N LYS A 114 20.507 28.660 155.344 1.00 35.21 N ANISOU 592 N LYS A 114 5776 5277 2325 -127 740 785 N ATOM 593 CA LYS A 114 21.077 27.680 156.260 1.00 33.75 C ANISOU 593 CA LYS A 114 5540 5099 2185 -128 755 702 C ATOM 594 C LYS A 114 21.097 28.223 157.686 1.00 33.14 C ANISOU 594 C LYS A 114 5462 4941 2189 -148 744 701 C ATOM 595 O LYS A 114 21.074 27.458 158.649 1.00 34.50 O ANISOU 595 O LYS A 114 5600 5110 2400 -138 718 633 O ATOM 596 CB LYS A 114 22.489 27.285 155.818 1.00 29.75 C ANISOU 596 CB LYS A 114 4999 4644 1659 -149 855 697 C ATOM 597 CG LYS A 114 22.553 26.732 154.398 1.00 35.17 C ANISOU 597 CG LYS A 114 5698 5408 2258 -133 877 690 C ATOM 598 CD LYS A 114 23.975 26.378 153.984 1.00 31.42 C ANISOU 598 CD LYS A 114 5187 4987 1765 -149 988 688 C ATOM 599 CE LYS A 114 24.256 24.894 154.159 1.00 35.04 C ANISOU 599 CE LYS A 114 5618 5478 2219 -111 1001 588 C ATOM 600 NZ LYS A 114 23.406 24.055 153.270 1.00 34.97 N1+ ANISOU 600 NZ LYS A 114 5652 5497 2138 -81 950 532 N1+ ATOM 601 N LEU A 115 21.128 29.545 157.815 1.00 33.58 N ANISOU 601 N LEU A 115 5565 4929 2266 -180 765 776 N ATOM 602 CA LEU A 115 21.147 30.183 159.128 1.00 33.95 C ANISOU 602 CA LEU A 115 5631 4888 2380 -215 760 774 C ATOM 603 C LEU A 115 19.804 30.059 159.845 1.00 34.36 C ANISOU 603 C LEU A 115 5699 4903 2452 -164 671 740 C ATOM 604 O LEU A 115 19.741 29.621 160.994 1.00 30.95 O ANISOU 604 O LEU A 115 5244 4454 2060 -168 645 680 O ATOM 605 CB LEU A 115 21.533 31.659 159.000 1.00 33.88 C ANISOU 605 CB LEU A 115 5687 4797 2387 -273 815 862 C ATOM 606 CG LEU A 115 21.455 32.486 160.285 1.00 34.65 C ANISOU 606 CG LEU A 115 5834 4786 2545 -323 812 859 C ATOM 607 CD1 LEU A 115 22.412 31.951 161.344 1.00 28.43 C ANISOU 607 CD1 LEU A 115 4962 4024 1815 -386 822 789 C ATOM 608 CD2 LEU A 115 21.737 33.949 159.994 1.00 37.09 C ANISOU 608 CD2 LEU A 115 6226 4996 2870 -382 868 949 C ATOM 609 N PHE A 116 18.731 30.448 159.164 1.00 35.76 N ANISOU 609 N PHE A 116 5911 5079 2597 -116 625 784 N ATOM 610 CA PHE A 116 17.407 30.431 159.773 1.00 36.48 C ANISOU 610 CA PHE A 116 6011 5146 2705 -64 548 767 C ATOM 611 C PHE A 116 16.846 29.019 159.883 1.00 37.06 C ANISOU 611 C PHE A 116 6019 5297 2765 -38 486 684 C ATOM 612 O PHE A 116 15.945 28.766 160.681 1.00 37.58 O ANISOU 612 O PHE A 116 6072 5350 2857 -11 431 651 O ATOM 613 CB PHE A 116 16.452 31.331 158.992 1.00 37.70 C ANISOU 613 CB PHE A 116 6217 5283 2825 -17 521 854 C ATOM 614 CG PHE A 116 16.536 32.775 159.391 1.00 41.33 C ANISOU 614 CG PHE A 116 6760 5622 3322 -21 564 928 C ATOM 615 CD1 PHE A 116 17.594 33.563 158.968 1.00 43.18 C ANISOU 615 CD1 PHE A 116 7038 5810 3560 -81 643 983 C ATOM 616 CD2 PHE A 116 15.569 33.341 160.205 1.00 42.45 C ANISOU 616 CD2 PHE A 116 6944 5690 3496 32 534 941 C ATOM 617 CE1 PHE A 116 17.681 34.890 159.343 1.00 43.34 C ANISOU 617 CE1 PHE A 116 7149 5699 3619 -99 688 1047 C ATOM 618 CE2 PHE A 116 15.650 34.668 160.582 1.00 42.73 C ANISOU 618 CE2 PHE A 116 7075 5595 3568 31 583 1004 C ATOM 619 CZ PHE A 116 16.707 35.443 160.150 1.00 42.87 C ANISOU 619 CZ PHE A 116 7143 5553 3591 -41 659 1055 C ATOM 620 N THR A 117 17.380 28.099 159.089 1.00 36.90 N ANISOU 620 N THR A 117 5964 5351 2705 -49 503 650 N ATOM 621 CA THR A 117 17.050 26.691 159.255 1.00 36.27 C ANISOU 621 CA THR A 117 5836 5324 2620 -37 462 565 C ATOM 622 C THR A 117 17.646 26.208 160.573 1.00 35.86 C ANISOU 622 C THR A 117 5755 5239 2633 -50 478 507 C ATOM 623 O THR A 117 17.033 25.422 161.297 1.00 36.64 O ANISOU 623 O THR A 117 5827 5339 2756 -36 429 450 O ATOM 624 CB THR A 117 17.569 25.839 158.085 1.00 36.50 C ANISOU 624 CB THR A 117 5855 5425 2587 -43 490 539 C ATOM 625 OG1 THR A 117 16.890 26.221 156.885 1.00 27.51 O ANISOU 625 OG1 THR A 117 4744 4331 1376 -36 462 590 O ATOM 626 CG2 THR A 117 17.321 24.363 158.340 1.00 26.14 C ANISOU 626 CG2 THR A 117 4513 4143 1276 -34 460 447 C ATOM 627 N GLY A 118 18.839 26.706 160.885 1.00 34.74 N ANISOU 627 N GLY A 118 5618 5070 2514 -84 547 528 N ATOM 628 CA GLY A 118 19.501 26.394 162.138 1.00 33.09 C ANISOU 628 CA GLY A 118 5381 4838 2353 -106 562 487 C ATOM 629 C GLY A 118 18.712 26.862 163.346 1.00 33.41 C ANISOU 629 C GLY A 118 5439 4817 2436 -106 513 476 C ATOM 630 O GLY A 118 18.500 26.099 164.285 1.00 33.02 O ANISOU 630 O GLY A 118 5360 4771 2415 -96 479 419 O ATOM 631 N LEU A 119 18.274 28.118 163.322 1.00 34.54 N ANISOU 631 N LEU A 119 5641 4901 2582 -112 514 533 N ATOM 632 CA LEU A 119 17.465 28.663 164.407 1.00 24.17 C ANISOU 632 CA LEU A 119 4360 3522 1300 -100 479 525 C ATOM 633 C LEU A 119 16.148 27.905 164.532 1.00 24.75 C ANISOU 633 C LEU A 119 4400 3632 1372 -42 407 491 C ATOM 634 O LEU A 119 15.665 27.656 165.637 1.00 23.07 O ANISOU 634 O LEU A 119 4175 3401 1189 -33 377 450 O ATOM 635 CB LEU A 119 17.190 30.151 164.183 1.00 24.90 C ANISOU 635 CB LEU A 119 4524 3535 1404 -100 501 598 C ATOM 636 CG LEU A 119 18.392 31.089 164.075 1.00 26.13 C ANISOU 636 CG LEU A 119 4699 3639 1591 -177 567 634 C ATOM 637 CD1 LEU A 119 17.913 32.518 163.914 1.00 26.43 C ANISOU 637 CD1 LEU A 119 4822 3574 1646 -166 585 703 C ATOM 638 CD2 LEU A 119 19.296 30.960 165.290 1.00 27.19 C ANISOU 638 CD2 LEU A 119 4776 3760 1794 -246 571 571 C ATOM 639 N TYR A 120 15.580 27.540 163.387 1.00 23.99 N ANISOU 639 N TYR A 120 4288 3593 1234 -13 380 510 N ATOM 640 CA TYR A 120 14.323 26.800 163.329 1.00 32.87 C ANISOU 640 CA TYR A 120 5378 4766 2344 20 312 484 C ATOM 641 C TYR A 120 14.427 25.458 164.048 1.00 30.42 C ANISOU 641 C TYR A 120 5016 4482 2061 5 293 401 C ATOM 642 O TYR A 120 13.569 25.108 164.860 1.00 28.60 O ANISOU 642 O TYR A 120 4766 4251 1851 18 251 373 O ATOM 643 CB TYR A 120 13.915 26.589 161.870 1.00 35.43 C ANISOU 643 CB TYR A 120 5700 5159 2604 28 290 514 C ATOM 644 CG TYR A 120 12.571 25.931 161.653 1.00 24.45 C ANISOU 644 CG TYR A 120 4279 3831 1181 44 216 499 C ATOM 645 CD1 TYR A 120 11.409 26.686 161.598 1.00 24.87 C ANISOU 645 CD1 TYR A 120 4345 3888 1216 85 173 559 C ATOM 646 CD2 TYR A 120 12.468 24.558 161.466 1.00 28.54 C ANISOU 646 CD2 TYR A 120 4759 4403 1681 20 192 429 C ATOM 647 CE1 TYR A 120 10.179 26.091 161.380 1.00 25.05 C ANISOU 647 CE1 TYR A 120 4334 3984 1202 89 102 552 C ATOM 648 CE2 TYR A 120 11.242 23.954 161.249 1.00 27.32 C ANISOU 648 CE2 TYR A 120 4580 4311 1489 19 125 415 C ATOM 649 CZ TYR A 120 10.101 24.726 161.207 1.00 24.82 C ANISOU 649 CZ TYR A 120 4267 4013 1150 44 76 478 C ATOM 650 OH TYR A 120 8.878 24.132 160.992 1.00 25.65 O ANISOU 650 OH TYR A 120 4343 4194 1209 30 4 472 O ATOM 651 N HIS A 121 15.484 24.712 163.748 1.00 29.68 N ANISOU 651 N HIS A 121 4905 4410 1963 -16 329 368 N ATOM 652 CA HIS A 121 15.671 23.392 164.335 1.00 28.62 C ANISOU 652 CA HIS A 121 4734 4289 1849 -20 319 299 C ATOM 653 C HIS A 121 16.159 23.470 165.783 1.00 28.31 C ANISOU 653 C HIS A 121 4684 4209 1862 -30 329 279 C ATOM 654 O HIS A 121 15.646 22.763 166.649 1.00 29.60 O ANISOU 654 O HIS A 121 4826 4369 2052 -25 296 239 O ATOM 655 CB HIS A 121 16.646 22.569 163.490 1.00 27.73 C ANISOU 655 CB HIS A 121 4619 4210 1708 -23 365 277 C ATOM 656 CG HIS A 121 16.062 22.078 162.203 1.00 28.93 C ANISOU 656 CG HIS A 121 4784 4410 1801 -18 345 270 C ATOM 657 ND1 HIS A 121 14.706 21.939 162.004 1.00 29.72 N ANISOU 657 ND1 HIS A 121 4881 4534 1878 -15 279 267 N ATOM 658 CD2 HIS A 121 16.652 21.693 161.044 1.00 29.35 C ANISOU 658 CD2 HIS A 121 4853 4498 1802 -18 385 264 C ATOM 659 CE1 HIS A 121 14.484 21.491 160.780 1.00 29.91 C ANISOU 659 CE1 HIS A 121 4921 4608 1836 -19 272 259 C ATOM 660 NE2 HIS A 121 15.650 21.334 160.178 1.00 29.53 N ANISOU 660 NE2 HIS A 121 4889 4562 1769 -19 337 254 N ATOM 661 N ILE A 122 17.144 24.325 166.042 1.00 27.85 N ANISOU 661 N ILE A 122 4645 4125 1813 -55 375 307 N ATOM 662 CA ILE A 122 17.695 24.469 167.388 1.00 26.71 C ANISOU 662 CA ILE A 122 4495 3952 1701 -81 382 288 C ATOM 663 C ILE A 122 16.620 24.943 168.359 1.00 26.28 C ANISOU 663 C ILE A 122 4457 3858 1670 -72 339 279 C ATOM 664 O ILE A 122 16.488 24.408 169.460 1.00 26.84 O ANISOU 664 O ILE A 122 4506 3927 1765 -73 315 240 O ATOM 665 CB ILE A 122 18.888 25.448 167.416 1.00 27.43 C ANISOU 665 CB ILE A 122 4585 4026 1812 -132 431 321 C ATOM 666 CG1 ILE A 122 20.086 24.845 166.678 1.00 26.95 C ANISOU 666 CG1 ILE A 122 4491 4019 1730 -138 486 327 C ATOM 667 CG2 ILE A 122 19.280 25.784 168.849 1.00 26.71 C ANISOU 667 CG2 ILE A 122 4457 3907 1783 -171 412 294 C ATOM 668 CD1 ILE A 122 21.276 25.769 166.586 1.00 26.68 C ANISOU 668 CD1 ILE A 122 4427 3985 1725 -198 535 365 C ATOM 669 N GLY A 123 15.845 25.936 167.939 1.00 26.38 N ANISOU 669 N GLY A 123 4513 3840 1671 -54 334 321 N ATOM 670 CA GLY A 123 14.740 26.431 168.739 1.00 26.21 C ANISOU 670 CA GLY A 123 4504 3784 1673 -27 304 318 C ATOM 671 C GLY A 123 13.715 25.351 169.035 1.00 26.36 C ANISOU 671 C GLY A 123 4480 3847 1687 1 256 283 C ATOM 672 O GLY A 123 13.151 25.303 170.127 1.00 26.56 O ANISOU 672 O GLY A 123 4501 3858 1732 9 240 259 O ATOM 673 N TYR A 124 13.481 24.476 168.062 1.00 27.06 N ANISOU 673 N TYR A 124 4535 3990 1755 6 236 279 N ATOM 674 CA TYR A 124 12.511 23.400 168.220 1.00 28.08 C ANISOU 674 CA TYR A 124 4625 4161 1883 11 192 246 C ATOM 675 C TYR A 124 12.983 22.337 169.205 1.00 30.12 C ANISOU 675 C TYR A 124 4856 4415 2175 -7 193 192 C ATOM 676 O TYR A 124 12.323 22.077 170.210 1.00 31.55 O ANISOU 676 O TYR A 124 5022 4591 2374 -5 173 173 O ATOM 677 CB TYR A 124 12.206 22.748 166.872 1.00 21.29 C ANISOU 677 CB TYR A 124 3755 3356 978 7 173 248 C ATOM 678 CG TYR A 124 11.468 21.431 166.995 1.00 27.66 C ANISOU 678 CG TYR A 124 4534 4199 1778 -7 136 203 C ATOM 679 CD1 TYR A 124 10.105 21.398 167.261 1.00 21.25 C ANISOU 679 CD1 TYR A 124 3705 3420 948 -3 91 212 C ATOM 680 CD2 TYR A 124 12.135 20.221 166.845 1.00 27.39 C ANISOU 680 CD2 TYR A 124 4499 4161 1747 -23 152 154 C ATOM 681 CE1 TYR A 124 9.429 20.198 167.377 1.00 21.25 C ANISOU 681 CE1 TYR A 124 3688 3450 936 -26 60 172 C ATOM 682 CE2 TYR A 124 11.467 19.017 166.961 1.00 21.08 C ANISOU 682 CE2 TYR A 124 3696 3374 937 -40 124 113 C ATOM 683 CZ TYR A 124 10.115 19.010 167.226 1.00 21.17 C ANISOU 683 CZ TYR A 124 3691 3418 933 -48 77 121 C ATOM 684 OH TYR A 124 9.449 17.810 167.339 1.00 21.31 O ANISOU 684 OH TYR A 124 3714 3444 938 -79 51 80 O ATOM 685 N PHE A 125 14.120 21.715 168.903 1.00 30.71 N ANISOU 685 N PHE A 125 4926 4492 2251 -19 221 175 N ATOM 686 CA PHE A 125 14.651 20.645 169.740 1.00 30.21 C ANISOU 686 CA PHE A 125 4845 4423 2210 -24 225 136 C ATOM 687 C PHE A 125 14.970 21.141 171.144 1.00 29.59 C ANISOU 687 C PHE A 125 4763 4320 2159 -33 226 134 C ATOM 688 O PHE A 125 14.748 20.432 172.122 1.00 29.34 O ANISOU 688 O PHE A 125 4716 4287 2146 -33 209 110 O ATOM 689 CB PHE A 125 15.898 20.031 169.103 1.00 31.73 C ANISOU 689 CB PHE A 125 5043 4627 2387 -20 268 129 C ATOM 690 CG PHE A 125 15.602 19.152 167.921 1.00 33.48 C ANISOU 690 CG PHE A 125 5278 4866 2576 -14 269 110 C ATOM 691 CD1 PHE A 125 14.957 17.940 168.091 1.00 33.87 C ANISOU 691 CD1 PHE A 125 5337 4909 2625 -16 246 71 C ATOM 692 CD2 PHE A 125 15.973 19.534 166.643 1.00 35.14 C ANISOU 692 CD2 PHE A 125 5503 5098 2748 -12 295 129 C ATOM 693 CE1 PHE A 125 14.683 17.126 167.007 1.00 35.13 C ANISOU 693 CE1 PHE A 125 5525 5078 2744 -21 248 44 C ATOM 694 CE2 PHE A 125 15.702 18.725 165.555 1.00 35.45 C ANISOU 694 CE2 PHE A 125 5566 5158 2748 -11 296 104 C ATOM 695 CZ PHE A 125 15.056 17.519 165.737 1.00 35.39 C ANISOU 695 CZ PHE A 125 5573 5139 2737 -17 271 58 C ATOM 696 N GLY A 126 15.484 22.363 171.236 1.00 29.53 N ANISOU 696 N GLY A 126 4780 4293 2149 -47 247 159 N ATOM 697 CA GLY A 126 15.736 22.983 172.523 1.00 29.67 C ANISOU 697 CA GLY A 126 4809 4285 2180 -70 245 149 C ATOM 698 C GLY A 126 14.451 23.114 173.316 1.00 30.37 C ANISOU 698 C GLY A 126 4900 4359 2280 -52 218 136 C ATOM 699 O GLY A 126 14.434 22.911 174.530 1.00 29.54 O ANISOU 699 O GLY A 126 4787 4250 2186 -61 207 112 O ATOM 700 N GLY A 127 13.369 23.445 172.619 1.00 31.02 N ANISOU 700 N GLY A 127 4992 4443 2351 -23 209 158 N ATOM 701 CA GLY A 127 12.064 23.568 173.239 1.00 31.02 C ANISOU 701 CA GLY A 127 4991 4444 2351 2 192 155 C ATOM 702 C GLY A 127 11.628 22.295 173.935 1.00 31.28 C ANISOU 702 C GLY A 127 4980 4508 2398 -7 169 124 C ATOM 703 O GLY A 127 11.370 22.298 175.134 1.00 32.39 O ANISOU 703 O GLY A 127 5119 4640 2547 -8 170 106 O ATOM 704 N ILE A 128 11.559 21.200 173.185 1.00 31.63 N ANISOU 704 N ILE A 128 4999 4583 2436 -15 154 117 N ATOM 705 CA ILE A 128 11.089 19.931 173.732 1.00 31.69 C ANISOU 705 CA ILE A 128 4985 4607 2450 -29 137 93 C ATOM 706 C ILE A 128 12.068 19.372 174.770 1.00 30.68 C ANISOU 706 C ILE A 128 4854 4459 2345 -37 148 74 C ATOM 707 O ILE A 128 11.651 18.770 175.761 1.00 31.50 O ANISOU 707 O ILE A 128 4949 4564 2455 -44 141 64 O ATOM 708 CB ILE A 128 10.842 18.886 172.603 1.00 20.75 C ANISOU 708 CB ILE A 128 3598 3242 1042 -41 123 84 C ATOM 709 CG1 ILE A 128 10.423 17.532 173.186 1.00 20.87 C ANISOU 709 CG1 ILE A 128 3615 3254 1060 -64 114 58 C ATOM 710 CG2 ILE A 128 12.066 18.732 171.716 1.00 19.47 C ANISOU 710 CG2 ILE A 128 3451 3069 877 -37 146 80 C ATOM 711 CD1 ILE A 128 9.196 17.592 174.076 1.00 20.13 C ANISOU 711 CD1 ILE A 128 3505 3182 961 -75 99 65 C ATOM 712 N PHE A 129 13.363 19.593 174.565 1.00 29.20 N ANISOU 712 N PHE A 129 4674 4262 2160 -37 166 77 N ATOM 713 CA PHE A 129 14.364 19.098 175.504 1.00 28.77 C ANISOU 713 CA PHE A 129 4615 4204 2110 -41 171 71 C ATOM 714 C PHE A 129 14.200 19.723 176.888 1.00 31.01 C ANISOU 714 C PHE A 129 4899 4485 2399 -53 161 64 C ATOM 715 O PHE A 129 14.231 19.020 177.899 1.00 34.94 O ANISOU 715 O PHE A 129 5388 4990 2898 -54 150 58 O ATOM 716 CB PHE A 129 15.779 19.357 174.983 1.00 26.65 C ANISOU 716 CB PHE A 129 4353 3944 1828 -43 195 83 C ATOM 717 CG PHE A 129 16.195 18.442 173.866 1.00 25.88 C ANISOU 717 CG PHE A 129 4262 3852 1718 -22 217 83 C ATOM 718 CD1 PHE A 129 15.416 17.351 173.516 1.00 24.62 C ANISOU 718 CD1 PHE A 129 4114 3681 1559 -15 209 65 C ATOM 719 CD2 PHE A 129 17.371 18.672 173.166 1.00 25.10 C ANISOU 719 CD2 PHE A 129 4169 3770 1600 -17 254 98 C ATOM 720 CE1 PHE A 129 15.798 16.510 172.487 1.00 24.26 C ANISOU 720 CE1 PHE A 129 4093 3630 1494 1 235 54 C ATOM 721 CE2 PHE A 129 17.760 17.834 172.135 1.00 23.42 C ANISOU 721 CE2 PHE A 129 3969 3560 1369 10 286 93 C ATOM 722 CZ PHE A 129 16.972 16.752 171.796 1.00 23.63 C ANISOU 722 CZ PHE A 129 4018 3566 1397 19 276 67 C ATOM 723 N PHE A 130 14.017 21.039 176.936 1.00 26.21 N ANISOU 723 N PHE A 130 4311 3860 1787 -61 168 65 N ATOM 724 CA PHE A 130 13.885 21.721 178.219 1.00 23.87 C ANISOU 724 CA PHE A 130 4031 3552 1485 -76 166 48 C ATOM 725 C PHE A 130 12.523 21.481 178.859 1.00 22.71 C ANISOU 725 C PHE A 130 3878 3410 1342 -56 164 40 C ATOM 726 O PHE A 130 12.360 21.679 180.062 1.00 23.03 O ANISOU 726 O PHE A 130 3926 3449 1373 -63 165 23 O ATOM 727 CB PHE A 130 14.147 23.219 178.062 1.00 23.97 C ANISOU 727 CB PHE A 130 4085 3527 1495 -93 184 47 C ATOM 728 CG PHE A 130 15.606 23.565 177.987 1.00 25.12 C ANISOU 728 CG PHE A 130 4218 3676 1650 -137 184 48 C ATOM 729 CD1 PHE A 130 16.402 23.499 179.119 1.00 24.80 C ANISOU 729 CD1 PHE A 130 4161 3658 1604 -175 164 29 C ATOM 730 CD2 PHE A 130 16.186 23.938 176.788 1.00 24.92 C ANISOU 730 CD2 PHE A 130 4189 3644 1634 -144 203 73 C ATOM 731 CE1 PHE A 130 17.747 23.804 179.056 1.00 24.22 C ANISOU 731 CE1 PHE A 130 4057 3605 1539 -223 158 35 C ATOM 732 CE2 PHE A 130 17.529 24.246 176.718 1.00 20.12 C ANISOU 732 CE2 PHE A 130 3555 3052 1037 -191 207 80 C ATOM 733 CZ PHE A 130 18.311 24.178 177.853 1.00 24.66 C ANISOU 733 CZ PHE A 130 4103 3655 1613 -232 183 61 C ATOM 734 N ILE A 131 11.549 21.049 178.064 1.00 21.41 N ANISOU 734 N ILE A 131 3698 3258 1178 -37 161 54 N ATOM 735 CA ILE A 131 10.264 20.632 178.617 1.00 20.19 C ANISOU 735 CA ILE A 131 3530 3126 1016 -29 162 54 C ATOM 736 C ILE A 131 10.436 19.300 179.347 1.00 21.85 C ANISOU 736 C ILE A 131 3721 3349 1233 -47 151 48 C ATOM 737 O ILE A 131 9.868 19.087 180.419 1.00 23.02 O ANISOU 737 O ILE A 131 3865 3508 1371 -51 159 44 O ATOM 738 CB ILE A 131 9.180 20.495 177.528 1.00 19.30 C ANISOU 738 CB ILE A 131 3407 3039 886 -17 154 74 C ATOM 739 CG1 ILE A 131 8.870 21.854 176.905 1.00 20.22 C ANISOU 739 CG1 ILE A 131 3547 3142 994 20 166 95 C ATOM 740 CG2 ILE A 131 7.904 19.919 178.112 1.00 20.36 C ANISOU 740 CG2 ILE A 131 3525 3211 1001 -21 155 78 C ATOM 741 CD1 ILE A 131 7.812 21.797 175.821 1.00 21.28 C ANISOU 741 CD1 ILE A 131 3651 3320 1116 39 147 126 C ATOM 742 N ILE A 132 11.237 18.415 178.761 1.00 22.07 N ANISOU 742 N ILE A 132 3746 3370 1269 -54 142 51 N ATOM 743 CA ILE A 132 11.541 17.122 179.365 1.00 21.34 C ANISOU 743 CA ILE A 132 3657 3274 1175 -62 138 53 C ATOM 744 C ILE A 132 12.310 17.293 180.676 1.00 22.36 C ANISOU 744 C ILE A 132 3786 3411 1299 -61 134 55 C ATOM 745 O ILE A 132 12.028 16.613 181.662 1.00 22.98 O ANISOU 745 O ILE A 132 3869 3495 1367 -65 133 62 O ATOM 746 CB ILE A 132 12.353 16.233 178.399 1.00 21.85 C ANISOU 746 CB ILE A 132 3738 3322 1240 -56 140 56 C ATOM 747 CG1 ILE A 132 11.519 15.897 177.161 1.00 21.56 C ANISOU 747 CG1 ILE A 132 3711 3285 1197 -68 138 48 C ATOM 748 CG2 ILE A 132 12.811 14.956 179.088 1.00 21.61 C ANISOU 748 CG2 ILE A 132 3735 3276 1202 -51 144 66 C ATOM 749 CD1 ILE A 132 12.240 15.029 176.152 1.00 21.92 C ANISOU 749 CD1 ILE A 132 3788 3307 1234 -62 150 39 C ATOM 750 N LEU A 133 13.275 18.209 180.682 1.00 22.81 N ANISOU 750 N LEU A 133 3844 3471 1353 -62 131 49 N ATOM 751 CA LEU A 133 14.066 18.492 181.878 1.00 23.11 C ANISOU 751 CA LEU A 133 3885 3527 1371 -74 117 47 C ATOM 752 C LEU A 133 13.181 18.962 183.026 1.00 23.38 C ANISOU 752 C LEU A 133 3925 3565 1394 -81 122 30 C ATOM 753 O LEU A 133 13.319 18.499 184.157 1.00 25.44 O ANISOU 753 O LEU A 133 4185 3846 1633 -85 111 35 O ATOM 754 CB LEU A 133 15.138 19.543 181.578 1.00 23.15 C ANISOU 754 CB LEU A 133 3897 3534 1364 -96 113 39 C ATOM 755 CG LEU A 133 16.372 19.061 180.814 1.00 19.28 C ANISOU 755 CG LEU A 133 3399 3062 863 -93 112 61 C ATOM 756 CD1 LEU A 133 17.255 20.230 180.419 1.00 19.53 C ANISOU 756 CD1 LEU A 133 3413 3098 908 -127 114 56 C ATOM 757 CD2 LEU A 133 17.151 18.063 181.650 1.00 20.48 C ANISOU 757 CD2 LEU A 133 3528 3251 1003 -78 91 85 C ATOM 758 N LEU A 134 12.273 19.885 182.726 1.00 23.12 N ANISOU 758 N LEU A 134 3904 3514 1367 -76 143 14 N ATOM 759 CA LEU A 134 11.321 20.382 183.712 1.00 21.66 C ANISOU 759 CA LEU A 134 3734 3333 1165 -72 164 -4 C ATOM 760 C LEU A 134 10.367 19.282 184.156 1.00 22.98 C ANISOU 760 C LEU A 134 3880 3524 1327 -66 172 15 C ATOM 761 O LEU A 134 9.963 19.230 185.317 1.00 24.78 O ANISOU 761 O LEU A 134 4114 3769 1531 -68 186 9 O ATOM 762 CB LEU A 134 10.531 21.557 183.146 1.00 19.85 C ANISOU 762 CB LEU A 134 3532 3076 933 -52 193 -15 C ATOM 763 CG LEU A 134 11.288 22.881 183.068 1.00 20.25 C ANISOU 763 CG LEU A 134 3633 3084 975 -66 200 -39 C ATOM 764 CD1 LEU A 134 10.704 23.768 181.984 1.00 21.46 C ANISOU 764 CD1 LEU A 134 3820 3203 1132 -34 227 -26 C ATOM 765 CD2 LEU A 134 11.245 23.582 184.413 1.00 20.39 C ANISOU 765 CD2 LEU A 134 3695 3090 961 -79 217 -79 C ATOM 766 N THR A 135 10.008 18.408 183.222 1.00 22.56 N ANISOU 766 N THR A 135 3812 3471 1290 -66 167 35 N ATOM 767 CA THR A 135 9.126 17.286 183.517 1.00 24.01 C ANISOU 767 CA THR A 135 3989 3670 1464 -78 176 54 C ATOM 768 C THR A 135 9.752 16.360 184.551 1.00 24.24 C ANISOU 768 C THR A 135 4029 3699 1481 -86 168 70 C ATOM 769 O THR A 135 9.105 15.972 185.523 1.00 24.66 O ANISOU 769 O THR A 135 4087 3770 1512 -95 185 81 O ATOM 770 CB THR A 135 8.796 16.480 182.247 1.00 25.57 C ANISOU 770 CB THR A 135 4186 3858 1672 -92 167 65 C ATOM 771 OG1 THR A 135 8.053 17.301 181.337 1.00 28.75 O ANISOU 771 OG1 THR A 135 4577 4276 2071 -83 170 61 O ATOM 772 CG2 THR A 135 7.976 15.250 182.594 1.00 23.41 C ANISOU 772 CG2 THR A 135 3923 3589 1382 -126 177 82 C ATOM 773 N ILE A 136 11.016 16.011 184.332 1.00 23.96 N ANISOU 773 N ILE A 136 4000 3651 1452 -80 144 78 N ATOM 774 CA ILE A 136 11.751 15.155 185.254 1.00 19.65 C ANISOU 774 CA ILE A 136 3469 3112 884 -76 132 105 C ATOM 775 C ILE A 136 11.925 15.833 186.604 1.00 28.49 C ANISOU 775 C ILE A 136 4584 4267 1974 -79 125 96 C ATOM 776 O ILE A 136 11.715 15.219 187.651 1.00 29.64 O ANISOU 776 O ILE A 136 4742 4430 2090 -81 129 119 O ATOM 777 CB ILE A 136 13.140 14.785 184.696 1.00 23.83 C ANISOU 777 CB ILE A 136 4005 3634 1414 -58 112 120 C ATOM 778 CG1 ILE A 136 12.998 13.985 183.402 1.00 23.12 C ANISOU 778 CG1 ILE A 136 3937 3504 1345 -52 126 123 C ATOM 779 CG2 ILE A 136 13.948 14.007 185.723 1.00 20.09 C ANISOU 779 CG2 ILE A 136 3548 3180 904 -44 95 160 C ATOM 780 CD1 ILE A 136 14.318 13.553 182.811 1.00 22.56 C ANISOU 780 CD1 ILE A 136 3882 3423 1266 -20 123 140 C ATOM 781 N ASP A 137 12.300 17.108 186.567 1.00 28.51 N ANISOU 781 N ASP A 137 4581 4276 1976 -83 118 62 N ATOM 782 CA ASP A 137 12.598 17.866 187.775 1.00 30.09 C ANISOU 782 CA ASP A 137 4792 4503 2139 -94 108 40 C ATOM 783 C ASP A 137 11.411 17.933 188.724 1.00 27.39 C ANISOU 783 C ASP A 137 4460 4172 1774 -93 143 31 C ATOM 784 O ASP A 137 11.550 17.694 189.921 1.00 26.39 O ANISOU 784 O ASP A 137 4345 4076 1606 -96 136 38 O ATOM 785 CB ASP A 137 13.047 19.282 187.417 1.00 34.74 C ANISOU 785 CB ASP A 137 5395 5075 2731 -112 105 -3 C ATOM 786 CG ASP A 137 13.323 20.130 188.640 1.00 39.94 C ANISOU 786 CG ASP A 137 6082 5750 3343 -137 96 -39 C ATOM 787 OD1 ASP A 137 13.886 19.593 189.619 1.00 44.06 O ANISOU 787 OD1 ASP A 137 6601 6314 3825 -144 66 -23 O ATOM 788 OD2 ASP A 137 12.974 21.329 188.625 1.00 38.69 O1+ ANISOU 788 OD2 ASP A 137 5960 5560 3182 -149 121 -83 O1+ ATOM 789 N ARG A 138 10.242 18.258 188.187 1.00 28.61 N ANISOU 789 N ARG A 138 4612 4310 1947 -85 181 20 N ATOM 790 CA ARG A 138 9.054 18.396 189.016 1.00 29.86 C ANISOU 790 CA ARG A 138 4778 4490 2078 -79 226 14 C ATOM 791 C ARG A 138 8.478 17.038 189.395 1.00 27.87 C ANISOU 791 C ARG A 138 4518 4257 1816 -88 237 60 C ATOM 792 O ARG A 138 7.765 16.917 190.388 1.00 29.50 O ANISOU 792 O ARG A 138 4731 4492 1986 -90 272 66 O ATOM 793 CB ARG A 138 8.005 19.256 188.312 1.00 32.82 C ANISOU 793 CB ARG A 138 5153 4853 2464 -61 266 -5 C ATOM 794 CG ARG A 138 8.133 20.729 188.666 1.00 36.87 C ANISOU 794 CG ARG A 138 5707 5344 2960 -49 288 -54 C ATOM 795 CD ARG A 138 8.113 20.894 190.180 1.00 42.76 C ANISOU 795 CD ARG A 138 6477 6113 3656 -56 305 -77 C ATOM 796 NE ARG A 138 8.712 22.147 190.632 1.00 47.84 N ANISOU 796 NE ARG A 138 7176 6724 4277 -64 307 -134 N ATOM 797 CZ ARG A 138 9.958 22.259 191.081 1.00 52.25 C ANISOU 797 CZ ARG A 138 7750 7285 4819 -101 255 -150 C ATOM 798 NH1 ARG A 138 10.745 21.192 191.133 1.00 50.49 N1+ ANISOU 798 NH1 ARG A 138 7488 7097 4599 -115 203 -109 N1+ ATOM 799 NH2 ARG A 138 10.420 23.438 191.477 1.00 57.01 N ANISOU 799 NH2 ARG A 138 8414 7854 5394 -124 259 -207 N ATOM 800 N TYR A 139 8.799 16.015 188.611 1.00 26.37 N ANISOU 800 N TYR A 139 4323 4045 1653 -97 215 91 N ATOM 801 CA TYR A 139 8.445 14.652 188.981 1.00 25.25 C ANISOU 801 CA TYR A 139 4196 3901 1497 -115 226 136 C ATOM 802 C TYR A 139 9.242 14.223 190.204 1.00 23.57 C ANISOU 802 C TYR A 139 4002 3707 1247 -109 208 162 C ATOM 803 O TYR A 139 8.670 13.789 191.203 1.00 21.98 O ANISOU 803 O TYR A 139 3814 3528 1009 -118 234 187 O ATOM 804 CB TYR A 139 8.691 13.683 187.825 1.00 28.18 C ANISOU 804 CB TYR A 139 4579 4229 1898 -128 210 156 C ATOM 805 CG TYR A 139 8.940 12.258 188.270 1.00 30.21 C ANISOU 805 CG TYR A 139 4880 4462 2138 -142 212 205 C ATOM 806 CD1 TYR A 139 7.924 11.495 188.831 1.00 31.81 C ANISOU 806 CD1 TYR A 139 5104 4664 2317 -179 248 235 C ATOM 807 CD2 TYR A 139 10.191 11.674 188.121 1.00 31.00 C ANISOU 807 CD2 TYR A 139 5004 4535 2238 -117 183 228 C ATOM 808 CE1 TYR A 139 8.149 10.194 189.238 1.00 33.02 C ANISOU 808 CE1 TYR A 139 5314 4780 2452 -194 256 287 C ATOM 809 CE2 TYR A 139 10.425 10.374 188.521 1.00 32.28 C ANISOU 809 CE2 TYR A 139 5223 4663 2379 -117 191 282 C ATOM 810 CZ TYR A 139 9.402 9.638 189.080 1.00 34.73 C ANISOU 810 CZ TYR A 139 5566 4961 2670 -157 227 311 C ATOM 811 OH TYR A 139 9.635 8.341 189.480 1.00 38.70 O ANISOU 811 OH TYR A 139 6140 5412 3151 -159 239 372 O ATOM 812 N LEU A 140 10.563 14.359 190.122 1.00 21.28 N ANISOU 812 N LEU A 140 3710 3418 957 -94 163 161 N ATOM 813 CA LEU A 140 11.447 13.975 191.217 1.00 21.80 C ANISOU 813 CA LEU A 140 3790 3519 976 -85 134 193 C ATOM 814 C LEU A 140 11.135 14.740 192.498 1.00 33.10 C ANISOU 814 C LEU A 140 5225 4994 2358 -89 144 168 C ATOM 815 O LEU A 140 11.333 14.227 193.598 1.00 22.93 O ANISOU 815 O LEU A 140 3955 3741 1018 -85 136 203 O ATOM 816 CB LEU A 140 12.908 14.196 190.824 1.00 21.72 C ANISOU 816 CB LEU A 140 3768 3519 964 -72 84 195 C ATOM 817 CG LEU A 140 13.444 13.275 189.728 1.00 25.71 C ANISOU 817 CG LEU A 140 4283 3985 1500 -56 78 228 C ATOM 818 CD1 LEU A 140 14.899 13.589 189.416 1.00 25.02 C ANISOU 818 CD1 LEU A 140 4180 3927 1401 -39 34 234 C ATOM 819 CD2 LEU A 140 13.286 11.823 190.136 1.00 26.53 C ANISOU 819 CD2 LEU A 140 4430 4063 1585 -45 91 293 C ATOM 820 N ALA A 141 10.631 15.961 192.342 1.00 31.01 N ANISOU 820 N ALA A 141 4954 4726 2104 -93 165 110 N ATOM 821 CA ALA A 141 10.345 16.840 193.473 1.00 29.08 C ANISOU 821 CA ALA A 141 4729 4512 1809 -96 183 71 C ATOM 822 C ALA A 141 9.123 16.397 194.280 1.00 28.82 C ANISOU 822 C ALA A 141 4705 4501 1744 -94 240 91 C ATOM 823 O ALA A 141 9.108 16.525 195.503 1.00 30.26 O ANISOU 823 O ALA A 141 4910 4722 1865 -94 248 88 O ATOM 824 CB ALA A 141 10.160 18.265 192.987 1.00 22.57 C ANISOU 824 CB ALA A 141 3911 3662 1003 -99 199 5 C ATOM 825 N ILE A 142 8.100 15.883 193.601 1.00 27.58 N ANISOU 825 N ILE A 142 4532 4326 1620 -98 280 114 N ATOM 826 CA ILE A 142 6.883 15.449 194.285 1.00 28.57 C ANISOU 826 CA ILE A 142 4662 4478 1714 -104 342 139 C ATOM 827 C ILE A 142 7.058 14.056 194.896 1.00 29.96 C ANISOU 827 C ILE A 142 4859 4660 1866 -120 335 209 C ATOM 828 O ILE A 142 6.270 13.634 195.742 1.00 31.43 O ANISOU 828 O ILE A 142 5056 4874 2011 -131 383 238 O ATOM 829 CB ILE A 142 5.661 15.448 193.333 1.00 27.58 C ANISOU 829 CB ILE A 142 4512 4345 1623 -112 389 140 C ATOM 830 CG1 ILE A 142 4.354 15.484 194.133 1.00 27.51 C ANISOU 830 CG1 ILE A 142 4498 4383 1570 -114 468 151 C ATOM 831 CG2 ILE A 142 5.708 14.255 192.388 1.00 27.77 C ANISOU 831 CG2 ILE A 142 4533 4331 1686 -142 367 184 C ATOM 832 CD1 ILE A 142 3.103 15.430 193.280 1.00 23.96 C ANISOU 832 CD1 ILE A 142 4015 3948 1141 -130 519 163 C ATOM 833 N VAL A 143 8.098 13.348 194.468 1.00 30.26 N ANISOU 833 N VAL A 143 4904 4669 1923 -120 281 239 N ATOM 834 CA VAL A 143 8.434 12.055 195.053 1.00 29.60 C ANISOU 834 CA VAL A 143 4852 4582 1811 -127 273 312 C ATOM 835 C VAL A 143 9.534 12.261 196.095 1.00 29.75 C ANISOU 835 C VAL A 143 4880 4650 1773 -103 226 322 C ATOM 836 O VAL A 143 9.927 11.334 196.804 1.00 30.71 O ANISOU 836 O VAL A 143 5029 4787 1854 -97 213 389 O ATOM 837 CB VAL A 143 8.885 11.042 193.977 1.00 30.86 C ANISOU 837 CB VAL A 143 5028 4679 2016 -134 251 348 C ATOM 838 CG1 VAL A 143 8.912 9.628 194.537 1.00 34.07 C ANISOU 838 CG1 VAL A 143 5487 5062 2395 -144 264 431 C ATOM 839 CG2 VAL A 143 7.952 11.098 192.787 1.00 30.36 C ANISOU 839 CG2 VAL A 143 4952 4579 2004 -161 282 320 C ATOM 840 N HIS A 144 10.010 13.501 196.183 1.00 29.15 N ANISOU 840 N HIS A 144 4789 4599 1689 -92 200 257 N ATOM 841 CA HIS A 144 11.045 13.896 197.137 1.00 29.41 C ANISOU 841 CA HIS A 144 4833 4683 1658 -79 150 251 C ATOM 842 C HIS A 144 12.311 13.054 196.999 1.00 29.70 C ANISOU 842 C HIS A 144 4868 4731 1686 -60 88 314 C ATOM 843 O HIS A 144 12.847 12.558 197.989 1.00 30.67 O ANISOU 843 O HIS A 144 5009 4900 1742 -43 60 365 O ATOM 844 CB HIS A 144 10.512 13.819 198.572 1.00 29.30 C ANISOU 844 CB HIS A 144 4850 4718 1566 -78 180 265 C ATOM 845 CG HIS A 144 9.372 14.751 198.840 1.00 30.76 C ANISOU 845 CG HIS A 144 5038 4906 1743 -87 244 203 C ATOM 846 ND1 HIS A 144 9.554 16.083 199.145 1.00 31.95 N ANISOU 846 ND1 HIS A 144 5202 5067 1868 -89 239 123 N ATOM 847 CD2 HIS A 144 8.033 14.545 198.846 1.00 26.21 C ANISOU 847 CD2 HIS A 144 4458 4325 1176 -94 320 213 C ATOM 848 CE1 HIS A 144 8.379 16.657 199.326 1.00 32.05 C ANISOU 848 CE1 HIS A 144 5220 5082 1875 -88 312 86 C ATOM 849 NE2 HIS A 144 7.439 15.745 199.150 1.00 26.46 N ANISOU 849 NE2 HIS A 144 4495 4372 1187 -88 361 142 N ATOM 850 N ALA A 145 12.780 12.899 195.764 1.00 24.49 N ANISOU 850 N ALA A 145 4187 4031 1087 -58 70 315 N ATOM 851 CA ALA A 145 14.040 12.217 195.493 1.00 30.68 C ANISOU 851 CA ALA A 145 4965 4829 1862 -34 17 372 C ATOM 852 C ALA A 145 15.198 12.979 196.121 1.00 32.98 C ANISOU 852 C ALA A 145 5253 5181 2098 -18 -49 353 C ATOM 853 O ALA A 145 15.446 14.133 195.775 1.00 33.16 O ANISOU 853 O ALA A 145 5265 5197 2138 -42 -63 280 O ATOM 854 CB ALA A 145 14.253 12.068 193.997 1.00 31.28 C ANISOU 854 CB ALA A 145 5028 4847 2009 -34 20 363 C ATOM 855 N VAL A 146 15.901 12.322 197.038 1.00 36.67 N ANISOU 855 N VAL A 146 5742 5693 2498 15 -90 420 N ATOM 856 CA VAL A 146 16.965 12.955 197.815 1.00 38.83 C ANISOU 856 CA VAL A 146 6042 6005 2707 8 -166 403 C ATOM 857 C VAL A 146 18.076 13.527 196.939 1.00 41.86 C ANISOU 857 C VAL A 146 6385 6396 3123 -18 -221 379 C ATOM 858 O VAL A 146 18.496 14.669 197.125 1.00 42.25 O ANISOU 858 O VAL A 146 6412 6483 3159 -72 -256 312 O ATOM 859 CB VAL A 146 17.588 11.963 198.816 1.00 37.84 C ANISOU 859 CB VAL A 146 5965 5900 2512 37 -214 495 C ATOM 860 CG1 VAL A 146 18.630 12.662 199.673 1.00 38.01 C ANISOU 860 CG1 VAL A 146 5972 6005 2465 -2 -303 477 C ATOM 861 CG2 VAL A 146 16.508 11.341 199.687 1.00 37.64 C ANISOU 861 CG2 VAL A 146 5961 5877 2462 58 -151 528 C ATOM 862 N PHE A 147 18.546 12.732 195.983 1.00 44.23 N ANISOU 862 N PHE A 147 6674 6669 3463 9 -225 437 N ATOM 863 CA PHE A 147 19.628 13.162 195.107 1.00 48.12 C ANISOU 863 CA PHE A 147 7094 7203 3985 -9 -268 432 C ATOM 864 C PHE A 147 19.204 14.328 194.220 1.00 46.03 C ANISOU 864 C PHE A 147 6813 6903 3772 -51 -233 337 C ATOM 865 O PHE A 147 20.018 15.185 193.880 1.00 47.65 O ANISOU 865 O PHE A 147 6967 7155 3982 -96 -271 304 O ATOM 866 CB PHE A 147 20.121 11.995 194.246 1.00 54.83 C ANISOU 866 CB PHE A 147 7914 8047 4870 52 -260 519 C ATOM 867 CG PHE A 147 19.050 11.361 193.399 1.00 59.17 C ANISOU 867 CG PHE A 147 8514 8498 5471 64 -180 516 C ATOM 868 CD1 PHE A 147 18.257 10.343 193.908 1.00 62.08 C ANISOU 868 CD1 PHE A 147 8929 8825 5833 74 -143 566 C ATOM 869 CD2 PHE A 147 18.848 11.769 192.090 1.00 60.06 C ANISOU 869 CD2 PHE A 147 8609 8572 5641 63 -142 465 C ATOM 870 CE1 PHE A 147 17.275 9.753 193.132 1.00 61.87 C ANISOU 870 CE1 PHE A 147 8937 8707 5865 87 -72 555 C ATOM 871 CE2 PHE A 147 17.868 11.183 191.309 1.00 60.66 C ANISOU 871 CE2 PHE A 147 8725 8553 5772 76 -75 453 C ATOM 872 CZ PHE A 147 17.081 10.173 191.831 1.00 60.95 C ANISOU 872 CZ PHE A 147 8811 8541 5807 84 -42 495 C ATOM 873 N ALA A 148 17.928 14.361 193.851 1.00 43.30 N ANISOU 873 N ALA A 148 6496 6490 3467 -40 -160 300 N ATOM 874 CA ALA A 148 17.405 15.437 193.015 1.00 40.53 C ANISOU 874 CA ALA A 148 6130 6099 3170 -77 -124 221 C ATOM 875 C ALA A 148 17.400 16.759 193.774 1.00 39.22 C ANISOU 875 C ALA A 148 5976 5953 2974 -131 -141 148 C ATOM 876 O ALA A 148 17.682 17.813 193.204 1.00 38.39 O ANISOU 876 O ALA A 148 5861 5835 2892 -176 -145 93 O ATOM 877 CB ALA A 148 16.006 15.100 192.528 1.00 39.53 C ANISOU 877 CB ALA A 148 6012 5913 3094 -65 -53 210 C ATOM 878 N LEU A 149 17.076 16.693 195.063 1.00 38.80 N ANISOU 878 N LEU A 149 5951 5927 2863 -130 -145 147 N ATOM 879 CA LEU A 149 17.063 17.872 195.922 1.00 37.91 C ANISOU 879 CA LEU A 149 5864 5833 2705 -182 -158 76 C ATOM 880 C LEU A 149 18.477 18.400 196.131 1.00 37.81 C ANISOU 880 C LEU A 149 5829 5882 2654 -240 -241 66 C ATOM 881 O LEU A 149 18.701 19.610 196.185 1.00 38.43 O ANISOU 881 O LEU A 149 5921 5957 2722 -308 -252 -7 O ATOM 882 CB LEU A 149 16.405 17.546 197.267 1.00 38.21 C ANISOU 882 CB LEU A 149 5942 5897 2679 -163 -140 85 C ATOM 883 CG LEU A 149 16.496 18.583 198.389 1.00 38.80 C ANISOU 883 CG LEU A 149 6057 6002 2682 -213 -158 16 C ATOM 884 CD1 LEU A 149 15.125 18.839 198.989 1.00 38.81 C ANISOU 884 CD1 LEU A 149 6097 5981 2667 -195 -79 -19 C ATOM 885 CD2 LEU A 149 17.468 18.121 199.467 1.00 39.58 C ANISOU 885 CD2 LEU A 149 6160 6181 2696 -222 -236 58 C ATOM 886 N LYS A 150 19.431 17.482 196.241 1.00 38.06 N ANISOU 886 N LYS A 150 5823 5976 2663 -219 -300 144 N ATOM 887 CA LYS A 150 20.834 17.849 196.388 1.00 39.18 C ANISOU 887 CA LYS A 150 5907 6207 2771 -276 -387 153 C ATOM 888 C LYS A 150 21.401 18.336 195.058 1.00 41.16 C ANISOU 888 C LYS A 150 6105 6455 3080 -310 -386 140 C ATOM 889 O LYS A 150 22.455 18.969 195.016 1.00 44.51 O ANISOU 889 O LYS A 150 6473 6954 3485 -383 -446 127 O ATOM 890 CB LYS A 150 21.649 16.664 196.912 1.00 39.72 C ANISOU 890 CB LYS A 150 5934 6357 2800 -229 -449 258 C ATOM 891 CG LYS A 150 21.190 16.147 198.270 1.00 40.98 C ANISOU 891 CG LYS A 150 6153 6526 2890 -200 -454 282 C ATOM 892 CD LYS A 150 21.868 14.833 198.627 1.00 42.00 C ANISOU 892 CD LYS A 150 6253 6712 2992 -136 -502 402 C ATOM 893 N ALA A 151 20.690 18.038 193.974 1.00 38.70 N ANISOU 893 N ALA A 151 5807 6063 2835 -263 -318 144 N ATOM 894 CA ALA A 151 21.112 18.442 192.639 1.00 38.77 C ANISOU 894 CA ALA A 151 5775 6062 2894 -286 -304 134 C ATOM 895 C ALA A 151 20.403 19.716 192.185 1.00 37.49 C ANISOU 895 C ALA A 151 5663 5818 2764 -336 -255 45 C ATOM 896 O ALA A 151 20.783 20.322 191.187 1.00 38.74 O ANISOU 896 O ALA A 151 5803 5965 2953 -375 -246 28 O ATOM 897 CB ALA A 151 20.860 17.317 191.644 1.00 24.41 C ANISOU 897 CB ALA A 151 3944 4209 1121 -204 -262 195 C ATOM 898 N ARG A 152 19.373 20.118 192.921 1.00 35.57 N ANISOU 898 N ARG A 152 5483 5523 2509 -330 -219 -3 N ATOM 899 CA ARG A 152 18.571 21.281 192.552 1.00 36.11 C ANISOU 899 CA ARG A 152 5603 5510 2606 -358 -165 -78 C ATOM 900 C ARG A 152 19.336 22.584 192.793 1.00 38.82 C ANISOU 900 C ARG A 152 5969 5866 2916 -463 -199 -141 C ATOM 901 O ARG A 152 19.012 23.351 193.699 1.00 39.14 O ANISOU 901 O ARG A 152 6068 5887 2916 -500 -192 -202 O ATOM 902 CB ARG A 152 17.253 21.281 193.330 1.00 37.17 C ANISOU 902 CB ARG A 152 5785 5606 2731 -316 -112 -103 C ATOM 903 CG ARG A 152 16.187 22.208 192.766 1.00 38.36 C ANISOU 903 CG ARG A 152 5979 5674 2923 -310 -41 -156 C ATOM 904 CD ARG A 152 14.874 21.472 192.543 1.00 38.87 C ANISOU 904 CD ARG A 152 6030 5713 3023 -237 17 -126 C ATOM 905 NE ARG A 152 14.457 20.721 193.724 1.00 40.49 N ANISOU 905 NE ARG A 152 6238 5963 3184 -212 19 -102 N ATOM 906 CZ ARG A 152 14.112 19.436 193.711 1.00 41.29 C ANISOU 906 CZ ARG A 152 6308 6084 3296 -168 25 -38 C ATOM 907 NH1 ARG A 152 14.128 18.751 192.573 1.00 39.93 N1+ ANISOU 907 NH1 ARG A 152 6102 5889 3180 -146 29 2 N1+ ATOM 908 NH2 ARG A 152 13.748 18.836 194.836 1.00 42.86 N ANISOU 908 NH2 ARG A 152 6519 6320 3445 -153 32 -15 N ATOM 909 N THR A 153 20.351 22.822 191.967 1.00 40.57 N ANISOU 909 N THR A 153 6146 6120 3150 -517 -231 -127 N ATOM 910 CA THR A 153 21.220 23.988 192.101 1.00 43.99 C ANISOU 910 CA THR A 153 6590 6574 3549 -640 -269 -180 C ATOM 911 C THR A 153 21.361 24.699 190.760 1.00 48.56 C ANISOU 911 C THR A 153 7180 7099 4171 -679 -232 -194 C ATOM 912 O THR A 153 21.276 24.062 189.710 1.00 51.48 O ANISOU 912 O THR A 153 7505 7460 4594 -613 -204 -141 O ATOM 913 CB THR A 153 22.621 23.587 192.610 1.00 44.66 C ANISOU 913 CB THR A 153 6585 6800 3585 -697 -365 -138 C ATOM 914 OG1 THR A 153 22.496 22.607 193.648 1.00 45.28 O ANISOU 914 OG1 THR A 153 6647 6930 3628 -630 -396 -95 O ATOM 915 CG2 THR A 153 23.380 24.798 193.141 1.00 46.24 C ANISOU 915 CG2 THR A 153 6806 7028 3737 -842 -415 -206 C ATOM 916 N VAL A 154 21.582 26.011 190.790 1.00 48.63 N ANISOU 916 N VAL A 154 7254 7062 4161 -784 -228 -264 N ATOM 917 CA VAL A 154 21.803 26.768 189.560 1.00 50.05 C ANISOU 917 CA VAL A 154 7431 7169 4416 -812 -188 -267 C ATOM 918 C VAL A 154 23.081 26.323 188.845 1.00 50.15 C ANISOU 918 C VAL A 154 7309 7271 4476 -832 -229 -202 C ATOM 919 O VAL A 154 23.204 26.479 187.632 1.00 50.87 O ANISOU 919 O VAL A 154 7369 7318 4641 -811 -187 -174 O ATOM 920 CB VAL A 154 21.877 28.283 189.829 1.00 52.39 C ANISOU 920 CB VAL A 154 7830 7383 4692 -927 -173 -354 C ATOM 921 CG1 VAL A 154 20.543 28.795 190.352 1.00 52.78 C ANISOU 921 CG1 VAL A 154 8017 7328 4708 -882 -109 -416 C ATOM 922 CG2 VAL A 154 23.001 28.600 190.807 1.00 53.47 C ANISOU 922 CG2 VAL A 154 7943 7616 4757 -1064 -259 -387 C ATOM 923 N THR A 155 24.026 25.771 189.600 1.00 50.06 N ANISOU 923 N THR A 155 7213 7391 4418 -868 -309 -173 N ATOM 924 CA THR A 155 25.241 25.212 189.020 1.00 49.42 C ANISOU 924 CA THR A 155 6985 7413 4380 -866 -344 -100 C ATOM 925 C THR A 155 24.895 23.997 188.167 1.00 45.92 C ANISOU 925 C THR A 155 6494 6960 3993 -719 -300 -28 C ATOM 926 O THR A 155 25.337 23.878 187.024 1.00 45.70 O ANISOU 926 O THR A 155 6403 6928 4033 -691 -266 10 O ATOM 927 CB THR A 155 26.258 24.806 190.105 1.00 54.18 C ANISOU 927 CB THR A 155 7499 8173 4913 -918 -445 -73 C ATOM 928 OG1 THR A 155 26.642 25.962 190.860 1.00 59.28 O ANISOU 928 OG1 THR A 155 8193 8833 5499 -1076 -492 -148 O ATOM 929 CG2 THR A 155 27.497 24.183 189.474 1.00 53.58 C ANISOU 929 CG2 THR A 155 7256 8212 4890 -894 -473 13 C ATOM 930 N PHE A 156 24.093 23.100 188.732 1.00 43.39 N ANISOU 930 N PHE A 156 6214 6634 3640 -631 -297 -13 N ATOM 931 CA PHE A 156 23.617 21.925 188.014 1.00 40.64 C ANISOU 931 CA PHE A 156 5847 6258 3338 -504 -253 43 C ATOM 932 C PHE A 156 22.769 22.344 186.817 1.00 38.31 C ANISOU 932 C PHE A 156 5608 5846 3101 -476 -175 19 C ATOM 933 O PHE A 156 22.746 21.668 185.789 1.00 36.57 O ANISOU 933 O PHE A 156 5356 5607 2933 -403 -137 59 O ATOM 934 CB PHE A 156 22.817 21.018 188.951 1.00 38.83 C ANISOU 934 CB PHE A 156 5668 6032 3056 -440 -261 58 C ATOM 935 CG PHE A 156 22.340 19.741 188.313 1.00 37.49 C ANISOU 935 CG PHE A 156 5489 5827 2927 -324 -219 113 C ATOM 936 CD1 PHE A 156 21.109 19.682 187.676 1.00 36.61 C ANISOU 936 CD1 PHE A 156 5448 5615 2846 -285 -154 90 C ATOM 937 CD2 PHE A 156 23.116 18.595 188.364 1.00 37.02 C ANISOU 937 CD2 PHE A 156 5354 5836 2876 -256 -244 189 C ATOM 938 CE1 PHE A 156 20.666 18.507 187.091 1.00 34.37 C ANISOU 938 CE1 PHE A 156 5165 5298 2596 -198 -119 132 C ATOM 939 CE2 PHE A 156 22.678 17.416 187.783 1.00 35.42 C ANISOU 939 CE2 PHE A 156 5164 5583 2710 -156 -199 232 C ATOM 940 CZ PHE A 156 21.452 17.373 187.146 1.00 33.59 C ANISOU 940 CZ PHE A 156 5010 5250 2505 -137 -139 198 C ATOM 941 N GLY A 157 22.075 23.468 186.961 1.00 37.28 N ANISOU 941 N GLY A 157 5569 5638 2959 -531 -150 -47 N ATOM 942 CA GLY A 157 21.246 23.996 185.895 1.00 35.14 C ANISOU 942 CA GLY A 157 5352 5262 2737 -503 -83 -64 C ATOM 943 C GLY A 157 22.059 24.471 184.710 1.00 36.15 C ANISOU 943 C GLY A 157 5430 5385 2920 -534 -64 -43 C ATOM 944 O GLY A 157 21.811 24.059 183.580 1.00 38.87 O ANISOU 944 O GLY A 157 5760 5701 3308 -470 -23 -11 O ATOM 945 N VAL A 158 23.032 25.338 184.975 1.00 35.59 N ANISOU 945 N VAL A 158 5336 5344 2842 -641 -94 -62 N ATOM 946 CA VAL A 158 23.879 25.899 183.929 1.00 34.33 C ANISOU 946 CA VAL A 158 5127 5186 2732 -690 -72 -40 C ATOM 947 C VAL A 158 24.594 24.807 183.139 1.00 34.28 C ANISOU 947 C VAL A 158 5007 5257 2760 -619 -66 30 C ATOM 948 O VAL A 158 24.634 24.850 181.910 1.00 33.61 O ANISOU 948 O VAL A 158 4911 5140 2718 -589 -14 56 O ATOM 949 CB VAL A 158 24.924 26.869 184.519 1.00 35.26 C ANISOU 949 CB VAL A 158 5221 5345 2831 -836 -117 -69 C ATOM 950 CG1 VAL A 158 25.940 27.277 183.460 1.00 35.45 C ANISOU 950 CG1 VAL A 158 5168 5395 2908 -891 -93 -31 C ATOM 951 CG2 VAL A 158 24.238 28.090 185.106 1.00 35.13 C ANISOU 951 CG2 VAL A 158 5341 5222 2785 -909 -104 -147 C ATOM 952 N VAL A 159 25.139 23.824 183.847 1.00 35.15 N ANISOU 952 N VAL A 159 5041 5467 2847 -584 -115 63 N ATOM 953 CA VAL A 159 25.878 22.743 183.205 1.00 24.58 C ANISOU 953 CA VAL A 159 3599 4200 1541 -503 -103 131 C ATOM 954 C VAL A 159 24.985 21.914 182.285 1.00 28.29 C ANISOU 954 C VAL A 159 4118 4596 2035 -389 -43 144 C ATOM 955 O VAL A 159 25.289 21.751 181.104 1.00 29.53 O ANISOU 955 O VAL A 159 4246 4746 2229 -354 7 170 O ATOM 956 CB VAL A 159 26.533 21.812 184.244 1.00 28.01 C ANISOU 956 CB VAL A 159 3953 4747 1943 -470 -168 171 C ATOM 957 CG1 VAL A 159 27.174 20.614 183.556 1.00 27.61 C ANISOU 957 CG1 VAL A 159 3812 4750 1930 -358 -141 243 C ATOM 958 CG2 VAL A 159 27.563 22.576 185.061 1.00 29.55 C ANISOU 958 CG2 VAL A 159 4077 5042 2108 -593 -239 164 C ATOM 959 N THR A 160 23.880 21.404 182.821 1.00 26.95 N ANISOU 959 N THR A 160 4025 4377 1839 -339 -46 126 N ATOM 960 CA THR A 160 22.987 20.549 182.044 1.00 26.03 C ANISOU 960 CA THR A 160 3953 4197 1738 -248 1 135 C ATOM 961 C THR A 160 22.251 21.335 180.963 1.00 24.42 C ANISOU 961 C THR A 160 3812 3912 1556 -261 50 109 C ATOM 962 O THR A 160 21.738 20.752 180.009 1.00 24.43 O ANISOU 962 O THR A 160 3836 3876 1570 -201 89 119 O ATOM 963 CB THR A 160 21.954 19.836 182.939 1.00 28.42 C ANISOU 963 CB THR A 160 4317 4474 2008 -207 -14 126 C ATOM 964 OG1 THR A 160 21.158 20.807 183.627 1.00 31.53 O ANISOU 964 OG1 THR A 160 4778 4828 2372 -265 -24 76 O ATOM 965 CG2 THR A 160 22.653 18.947 183.956 1.00 28.87 C ANISOU 965 CG2 THR A 160 4321 4609 2039 -180 -61 167 C ATOM 966 N SER A 161 22.200 22.656 181.110 1.00 23.69 N ANISOU 966 N SER A 161 3751 3789 1460 -341 48 76 N ATOM 967 CA SER A 161 21.612 23.507 180.080 1.00 24.82 C ANISOU 967 CA SER A 161 3951 3856 1624 -350 94 65 C ATOM 968 C SER A 161 22.557 23.657 178.895 1.00 25.19 C ANISOU 968 C SER A 161 3944 3927 1700 -361 127 100 C ATOM 969 O SER A 161 22.119 23.688 177.746 1.00 21.63 O ANISOU 969 O SER A 161 3524 3436 1259 -325 170 113 O ATOM 970 CB SER A 161 21.259 24.884 180.641 1.00 26.14 C ANISOU 970 CB SER A 161 4187 3965 1782 -424 90 22 C ATOM 971 OG SER A 161 20.231 24.789 181.610 1.00 26.95 O ANISOU 971 OG SER A 161 4347 4039 1854 -401 77 -12 O ATOM 972 N VAL A 162 23.853 23.755 179.185 1.00 25.74 N ANISOU 972 N VAL A 162 3930 4073 1778 -414 107 118 N ATOM 973 CA VAL A 162 24.876 23.849 178.148 1.00 23.19 C ANISOU 973 CA VAL A 162 3537 3793 1483 -426 145 157 C ATOM 974 C VAL A 162 24.908 22.566 177.322 1.00 23.32 C ANISOU 974 C VAL A 162 3524 3832 1504 -317 181 189 C ATOM 975 O VAL A 162 24.983 22.607 176.091 1.00 22.86 O ANISOU 975 O VAL A 162 3473 3758 1454 -295 237 207 O ATOM 976 CB VAL A 162 26.272 24.119 178.753 1.00 24.24 C ANISOU 976 CB VAL A 162 3561 4025 1623 -506 109 175 C ATOM 977 CG1 VAL A 162 27.362 23.918 177.713 1.00 24.83 C ANISOU 977 CG1 VAL A 162 3538 4168 1728 -496 157 226 C ATOM 978 CG2 VAL A 162 26.339 25.524 179.328 1.00 24.80 C ANISOU 978 CG2 VAL A 162 3675 4060 1688 -638 84 136 C ATOM 979 N ILE A 163 24.834 21.428 178.007 1.00 23.84 N ANISOU 979 N ILE A 163 3570 3929 1559 -250 154 195 N ATOM 980 CA ILE A 163 24.801 20.131 177.340 1.00 26.64 C ANISOU 980 CA ILE A 163 3920 4286 1918 -145 191 217 C ATOM 981 C ILE A 163 23.527 19.986 176.512 1.00 27.56 C ANISOU 981 C ILE A 163 4138 4315 2020 -112 223 191 C ATOM 982 O ILE A 163 23.549 19.432 175.412 1.00 28.67 O ANISOU 982 O ILE A 163 4292 4444 2158 -60 272 200 O ATOM 983 CB ILE A 163 24.894 18.969 178.353 1.00 26.62 C ANISOU 983 CB ILE A 163 3893 4316 1907 -83 154 234 C ATOM 984 CG1 ILE A 163 26.102 19.160 179.272 1.00 30.27 C ANISOU 984 CG1 ILE A 163 4245 4882 2373 -119 106 265 C ATOM 985 CG2 ILE A 163 24.975 17.630 177.635 1.00 22.59 C ANISOU 985 CG2 ILE A 163 3389 3792 1404 25 203 256 C ATOM 986 CD1 ILE A 163 27.418 19.307 178.532 1.00 30.64 C ANISOU 986 CD1 ILE A 163 4183 5009 2451 -121 141 306 C ATOM 987 N THR A 164 22.420 20.499 177.042 1.00 25.96 N ANISOU 987 N THR A 164 4004 4057 1802 -142 194 159 N ATOM 988 CA THR A 164 21.135 20.438 176.354 1.00 23.92 C ANISOU 988 CA THR A 164 3826 3733 1529 -117 213 140 C ATOM 989 C THR A 164 21.155 21.244 175.056 1.00 22.32 C ANISOU 989 C THR A 164 3644 3510 1327 -135 253 149 C ATOM 990 O THR A 164 20.603 20.816 174.043 1.00 21.94 O ANISOU 990 O THR A 164 3636 3442 1261 -97 279 150 O ATOM 991 CB THR A 164 19.992 20.955 177.250 1.00 24.27 C ANISOU 991 CB THR A 164 3923 3736 1562 -141 180 111 C ATOM 992 OG1 THR A 164 19.992 20.240 178.491 1.00 24.22 O ANISOU 992 OG1 THR A 164 3903 3754 1546 -129 146 107 O ATOM 993 CG2 THR A 164 18.652 20.762 176.568 1.00 24.22 C ANISOU 993 CG2 THR A 164 3977 3684 1543 -109 193 100 C ATOM 994 N TRP A 165 21.792 22.412 175.085 1.00 22.50 N ANISOU 994 N TRP A 165 3646 3538 1364 -201 257 158 N ATOM 995 CA TRP A 165 21.901 23.231 173.883 1.00 21.43 C ANISOU 995 CA TRP A 165 3534 3381 1228 -222 301 179 C ATOM 996 C TRP A 165 22.814 22.563 172.856 1.00 26.79 C ANISOU 996 C TRP A 165 4166 4111 1903 -189 349 207 C ATOM 997 O TRP A 165 22.603 22.702 171.652 1.00 26.97 O ANISOU 997 O TRP A 165 4225 4119 1903 -173 390 222 O ATOM 998 CB TRP A 165 22.404 24.639 174.221 1.00 21.97 C ANISOU 998 CB TRP A 165 3602 3430 1317 -313 299 182 C ATOM 999 CG TRP A 165 21.345 25.522 174.828 1.00 25.26 C ANISOU 999 CG TRP A 165 4096 3769 1731 -333 277 154 C ATOM 1000 CD1 TRP A 165 21.333 26.040 176.092 1.00 27.00 C ANISOU 1000 CD1 TRP A 165 4329 3973 1956 -383 243 121 C ATOM 1001 CD2 TRP A 165 20.140 25.978 174.199 1.00 21.48 C ANISOU 1001 CD2 TRP A 165 3695 3225 1240 -295 292 160 C ATOM 1002 NE1 TRP A 165 20.199 26.792 176.286 1.00 26.43 N ANISOU 1002 NE1 TRP A 165 4342 3821 1880 -372 246 101 N ATOM 1003 CE2 TRP A 165 19.449 26.770 175.138 1.00 24.94 C ANISOU 1003 CE2 TRP A 165 4187 3605 1686 -313 274 130 C ATOM 1004 CE3 TRP A 165 19.577 25.795 172.932 1.00 25.47 C ANISOU 1004 CE3 TRP A 165 4229 3723 1725 -244 318 188 C ATOM 1005 CZ2 TRP A 165 18.228 27.376 174.852 1.00 25.22 C ANISOU 1005 CZ2 TRP A 165 4291 3575 1716 -271 286 135 C ATOM 1006 CZ3 TRP A 165 18.364 26.398 172.649 1.00 25.70 C ANISOU 1006 CZ3 TRP A 165 4323 3697 1744 -212 317 196 C ATOM 1007 CH2 TRP A 165 17.704 27.178 173.604 1.00 26.00 C ANISOU 1007 CH2 TRP A 165 4402 3679 1799 -220 303 173 C ATOM 1008 N LEU A 166 23.816 21.829 173.333 1.00 26.06 N ANISOU 1008 N LEU A 166 3992 4083 1827 -171 347 217 N ATOM 1009 CA LEU A 166 24.705 21.084 172.445 1.00 24.94 C ANISOU 1009 CA LEU A 166 3800 3992 1683 -119 404 243 C ATOM 1010 C LEU A 166 23.946 20.015 171.668 1.00 25.47 C ANISOU 1010 C LEU A 166 3938 4023 1717 -39 430 225 C ATOM 1011 O LEU A 166 23.997 19.976 170.438 1.00 27.19 O ANISOU 1011 O LEU A 166 4185 4240 1907 -20 484 231 O ATOM 1012 CB LEU A 166 25.844 20.435 173.230 1.00 25.65 C ANISOU 1012 CB LEU A 166 3784 4162 1801 -97 393 265 C ATOM 1013 CG LEU A 166 27.078 21.290 173.515 1.00 27.18 C ANISOU 1013 CG LEU A 166 3872 4431 2023 -176 390 297 C ATOM 1014 CD1 LEU A 166 28.158 20.451 174.184 1.00 24.77 C ANISOU 1014 CD1 LEU A 166 3448 4223 1739 -129 377 329 C ATOM 1015 CD2 LEU A 166 27.596 21.917 172.233 1.00 27.66 C ANISOU 1015 CD2 LEU A 166 3922 4505 2082 -205 463 323 C ATOM 1016 N VAL A 167 23.245 19.149 172.395 1.00 21.82 N ANISOU 1016 N VAL A 167 3507 3533 1251 -1 393 200 N ATOM 1017 CA VAL A 167 22.462 18.081 171.785 1.00 21.58 C ANISOU 1017 CA VAL A 167 3549 3460 1189 56 410 175 C ATOM 1018 C VAL A 167 21.424 18.644 170.817 1.00 22.05 C ANISOU 1018 C VAL A 167 3684 3483 1209 30 412 161 C ATOM 1019 O VAL A 167 21.132 18.041 169.784 1.00 21.46 O ANISOU 1019 O VAL A 167 3662 3396 1094 60 444 146 O ATOM 1020 CB VAL A 167 21.754 17.230 172.850 1.00 21.16 C ANISOU 1020 CB VAL A 167 3521 3376 1141 78 364 156 C ATOM 1021 CG1 VAL A 167 21.024 16.064 172.205 1.00 21.11 C ANISOU 1021 CG1 VAL A 167 3594 3322 1104 121 385 128 C ATOM 1022 CG2 VAL A 167 22.758 16.730 173.871 1.00 22.57 C ANISOU 1022 CG2 VAL A 167 3626 3599 1352 108 353 182 C ATOM 1023 N ALA A 168 20.877 19.807 171.153 1.00 22.26 N ANISOU 1023 N ALA A 168 3721 3494 1245 -23 378 166 N ATOM 1024 CA ALA A 168 19.926 20.482 170.281 1.00 20.88 C ANISOU 1024 CA ALA A 168 3606 3291 1037 -38 377 168 C ATOM 1025 C ALA A 168 20.599 20.906 168.982 1.00 21.46 C ANISOU 1025 C ALA A 168 3684 3387 1084 -42 433 196 C ATOM 1026 O ALA A 168 19.997 20.838 167.911 1.00 22.32 O ANISOU 1026 O ALA A 168 3848 3490 1141 -29 444 197 O ATOM 1027 CB ALA A 168 19.317 21.684 170.983 1.00 20.64 C ANISOU 1027 CB ALA A 168 3585 3230 1029 -80 341 174 C ATOM 1028 N VAL A 169 21.852 21.340 169.083 1.00 27.36 N ANISOU 1028 N VAL A 169 4369 4168 1861 -66 466 222 N ATOM 1029 CA VAL A 169 22.615 21.755 167.911 1.00 28.89 C ANISOU 1029 CA VAL A 169 4557 4391 2031 -75 531 255 C ATOM 1030 C VAL A 169 22.981 20.556 167.034 1.00 30.27 C ANISOU 1030 C VAL A 169 4741 4594 2165 -10 585 241 C ATOM 1031 O VAL A 169 22.804 20.597 165.816 1.00 23.35 O ANISOU 1031 O VAL A 169 3918 3722 1230 0 625 248 O ATOM 1032 CB VAL A 169 23.897 22.515 168.315 1.00 23.20 C ANISOU 1032 CB VAL A 169 3750 3708 1357 -130 555 289 C ATOM 1033 CG1 VAL A 169 24.838 22.654 167.130 1.00 24.05 C ANISOU 1033 CG1 VAL A 169 3833 3862 1442 -131 637 326 C ATOM 1034 CG2 VAL A 169 23.543 23.882 168.880 1.00 23.11 C ANISOU 1034 CG2 VAL A 169 3760 3649 1372 -206 519 299 C ATOM 1035 N PHE A 170 23.476 19.488 167.656 1.00 30.64 N ANISOU 1035 N PHE A 170 4747 4658 2238 37 589 223 N ATOM 1036 CA PHE A 170 23.868 18.285 166.922 1.00 31.17 C ANISOU 1036 CA PHE A 170 4835 4736 2272 110 650 204 C ATOM 1037 C PHE A 170 22.681 17.618 166.231 1.00 35.58 C ANISOU 1037 C PHE A 170 5506 5246 2767 127 637 159 C ATOM 1038 O PHE A 170 22.847 16.954 165.208 1.00 42.32 O ANISOU 1038 O PHE A 170 6403 6102 3576 163 690 138 O ATOM 1039 CB PHE A 170 24.554 17.284 167.853 1.00 28.58 C ANISOU 1039 CB PHE A 170 4447 4422 1991 168 652 201 C ATOM 1040 CG PHE A 170 25.912 17.724 168.320 1.00 29.18 C ANISOU 1040 CG PHE A 170 4396 4572 2118 161 674 249 C ATOM 1041 CD1 PHE A 170 26.940 17.921 167.413 1.00 29.27 C ANISOU 1041 CD1 PHE A 170 4357 4643 2122 175 757 279 C ATOM 1042 CD2 PHE A 170 26.165 17.930 169.667 1.00 28.37 C ANISOU 1042 CD2 PHE A 170 4221 4491 2067 135 611 264 C ATOM 1043 CE1 PHE A 170 28.190 18.326 167.838 1.00 28.83 C ANISOU 1043 CE1 PHE A 170 4169 4671 2116 158 775 327 C ATOM 1044 CE2 PHE A 170 27.415 18.334 170.099 1.00 27.68 C ANISOU 1044 CE2 PHE A 170 4008 4488 2022 115 620 307 C ATOM 1045 CZ PHE A 170 28.428 18.531 169.183 1.00 28.50 C ANISOU 1045 CZ PHE A 170 4049 4654 2124 124 701 341 C ATOM 1046 N ALA A 171 21.487 17.796 166.789 1.00 33.93 N ANISOU 1046 N ALA A 171 5330 4999 2563 94 561 142 N ATOM 1047 CA ALA A 171 20.270 17.262 166.183 1.00 32.63 C ANISOU 1047 CA ALA A 171 5204 4802 2392 81 514 101 C ATOM 1048 C ALA A 171 19.762 18.184 165.080 1.00 33.08 C ANISOU 1048 C ALA A 171 5267 4878 2423 47 501 120 C ATOM 1049 O ALA A 171 18.817 17.851 164.363 1.00 34.13 O ANISOU 1049 O ALA A 171 5426 5007 2533 37 466 95 O ATOM 1050 CB ALA A 171 19.192 17.056 167.238 1.00 30.65 C ANISOU 1050 CB ALA A 171 4952 4519 2177 62 441 83 C ATOM 1051 N SER A 172 20.391 19.346 164.949 1.00 31.67 N ANISOU 1051 N SER A 172 5068 4722 2241 28 530 169 N ATOM 1052 CA SER A 172 19.995 20.315 163.937 1.00 32.12 C ANISOU 1052 CA SER A 172 5140 4792 2272 4 525 203 C ATOM 1053 C SER A 172 20.945 20.285 162.750 1.00 32.16 C ANISOU 1053 C SER A 172 5152 4836 2231 13 602 220 C ATOM 1054 O SER A 172 20.596 20.725 161.656 1.00 33.26 O ANISOU 1054 O SER A 172 5312 4993 2330 1 601 239 O ATOM 1055 CB SER A 172 19.945 21.722 164.532 1.00 34.88 C ANISOU 1055 CB SER A 172 5485 5124 2646 -30 511 253 C ATOM 1056 OG SER A 172 19.000 21.794 165.585 1.00 37.91 O ANISOU 1056 OG SER A 172 5865 5473 3066 -33 445 235 O ATOM 1057 N VAL A 173 22.145 19.761 162.978 1.00 30.91 N ANISOU 1057 N VAL A 173 4972 4698 2075 39 674 216 N ATOM 1058 CA VAL A 173 23.181 19.703 161.948 1.00 30.81 C ANISOU 1058 CA VAL A 173 4954 4729 2023 54 766 234 C ATOM 1059 C VAL A 173 22.729 19.031 160.641 1.00 32.72 C ANISOU 1059 C VAL A 173 5243 4976 2212 69 770 194 C ATOM 1060 O VAL A 173 22.966 19.585 159.568 1.00 34.72 O ANISOU 1060 O VAL A 173 5507 5265 2421 52 806 224 O ATOM 1061 CB VAL A 173 24.447 18.991 162.479 1.00 25.62 C ANISOU 1061 CB VAL A 173 4253 4101 1381 108 846 234 C ATOM 1062 CG1 VAL A 173 25.405 18.675 161.345 1.00 26.74 C ANISOU 1062 CG1 VAL A 173 4386 4289 1485 142 949 240 C ATOM 1063 CG2 VAL A 173 25.126 19.846 163.534 1.00 30.22 C ANISOU 1063 CG2 VAL A 173 4750 4707 2026 73 839 284 C ATOM 1064 N PRO A 174 22.074 17.852 160.713 1.00 25.67 N ANISOU 1064 N PRO A 174 4387 4050 1316 93 735 129 N ATOM 1065 CA PRO A 174 21.631 17.271 159.439 1.00 26.38 C ANISOU 1065 CA PRO A 174 4532 4150 1343 94 738 88 C ATOM 1066 C PRO A 174 20.675 18.186 158.674 1.00 34.50 C ANISOU 1066 C PRO A 174 5569 5206 2334 50 676 120 C ATOM 1067 O PRO A 174 20.800 18.328 157.458 1.00 35.76 O ANISOU 1067 O PRO A 174 5755 5405 2428 45 705 127 O ATOM 1068 CB PRO A 174 20.919 15.983 159.867 1.00 27.45 C ANISOU 1068 CB PRO A 174 4709 4232 1488 109 698 18 C ATOM 1069 CG PRO A 174 21.507 15.648 161.188 1.00 26.61 C ANISOU 1069 CG PRO A 174 4572 4095 1442 144 718 24 C ATOM 1070 CD PRO A 174 21.750 16.966 161.848 1.00 26.47 C ANISOU 1070 CD PRO A 174 4492 4105 1460 116 700 90 C ATOM 1071 N GLY A 175 19.742 18.807 159.389 1.00 33.30 N ANISOU 1071 N GLY A 175 5397 5037 2218 26 596 143 N ATOM 1072 CA GLY A 175 18.802 19.729 158.782 1.00 32.28 C ANISOU 1072 CA GLY A 175 5274 4933 2058 2 539 186 C ATOM 1073 C GLY A 175 19.490 20.912 158.129 1.00 31.31 C ANISOU 1073 C GLY A 175 5147 4837 1912 -9 589 259 C ATOM 1074 O GLY A 175 19.089 21.351 157.055 1.00 31.80 O ANISOU 1074 O GLY A 175 5234 4937 1913 -18 577 290 O ATOM 1075 N ILE A 176 20.531 21.425 158.778 1.00 30.62 N ANISOU 1075 N ILE A 176 5032 4735 1867 -13 645 291 N ATOM 1076 CA ILE A 176 21.276 22.568 158.259 1.00 31.28 C ANISOU 1076 CA ILE A 176 5113 4836 1934 -35 703 366 C ATOM 1077 C ILE A 176 22.071 22.208 157.006 1.00 32.95 C ANISOU 1077 C ILE A 176 5337 5102 2081 -28 781 364 C ATOM 1078 O ILE A 176 22.035 22.930 156.008 1.00 34.27 O ANISOU 1078 O ILE A 176 5527 5298 2197 -45 796 416 O ATOM 1079 CB ILE A 176 22.249 23.135 159.315 1.00 29.31 C ANISOU 1079 CB ILE A 176 4827 4567 1743 -53 751 397 C ATOM 1080 CG1 ILE A 176 21.483 23.610 160.549 1.00 29.40 C ANISOU 1080 CG1 ILE A 176 4839 4522 1810 -65 679 398 C ATOM 1081 CG2 ILE A 176 23.066 24.277 158.735 1.00 27.33 C ANISOU 1081 CG2 ILE A 176 4577 4333 1475 -91 822 477 C ATOM 1082 CD1 ILE A 176 22.376 24.150 161.642 1.00 29.38 C ANISOU 1082 CD1 ILE A 176 4811 4500 1852 -99 717 421 C ATOM 1083 N ILE A 177 22.781 21.085 157.067 1.00 32.47 N ANISOU 1083 N ILE A 177 5266 5051 2019 2 835 307 N ATOM 1084 CA ILE A 177 23.667 20.666 155.986 1.00 29.19 C ANISOU 1084 CA ILE A 177 4862 4683 1546 17 927 298 C ATOM 1085 C ILE A 177 22.940 20.500 154.653 1.00 37.17 C ANISOU 1085 C ILE A 177 5929 5724 2470 12 899 282 C ATOM 1086 O ILE A 177 23.362 21.051 153.635 1.00 38.98 O ANISOU 1086 O ILE A 177 6170 6000 2642 -3 949 326 O ATOM 1087 CB ILE A 177 24.373 19.342 156.329 1.00 29.33 C ANISOU 1087 CB ILE A 177 4872 4691 1581 71 987 231 C ATOM 1088 CG1 ILE A 177 25.361 19.542 157.478 1.00 28.99 C ANISOU 1088 CG1 ILE A 177 4759 4648 1606 83 1037 264 C ATOM 1089 CG2 ILE A 177 25.110 18.805 155.116 1.00 33.85 C ANISOU 1089 CG2 ILE A 177 5469 5305 2087 98 1082 210 C ATOM 1090 CD1 ILE A 177 26.529 20.429 157.126 1.00 29.80 C ANISOU 1090 CD1 ILE A 177 4811 4807 1705 58 1132 336 C ATOM 1091 N PHE A 178 21.842 19.750 154.664 1.00 35.97 N ANISOU 1091 N PHE A 178 5810 5552 2302 19 820 223 N ATOM 1092 CA PHE A 178 21.150 19.407 153.425 1.00 35.84 C ANISOU 1092 CA PHE A 178 5848 5576 2193 14 791 197 C ATOM 1093 C PHE A 178 20.027 20.380 153.072 1.00 36.51 C ANISOU 1093 C PHE A 178 5937 5688 2248 -14 704 257 C ATOM 1094 O PHE A 178 19.193 20.081 152.220 1.00 37.78 O ANISOU 1094 O PHE A 178 6134 5891 2332 -19 655 237 O ATOM 1095 CB PHE A 178 20.596 17.981 153.509 1.00 33.38 C ANISOU 1095 CB PHE A 178 5577 5236 1868 31 761 99 C ATOM 1096 CG PHE A 178 21.656 16.932 153.698 1.00 30.75 C ANISOU 1096 CG PHE A 178 5259 4870 1553 73 855 41 C ATOM 1097 CD1 PHE A 178 22.470 16.553 152.643 1.00 35.47 C ANISOU 1097 CD1 PHE A 178 5893 5501 2084 95 948 19 C ATOM 1098 CD2 PHE A 178 21.842 16.328 154.931 1.00 37.44 C ANISOU 1098 CD2 PHE A 178 6088 5657 2481 99 856 13 C ATOM 1099 CE1 PHE A 178 23.450 15.592 152.813 1.00 37.50 C ANISOU 1099 CE1 PHE A 178 6163 5725 2358 151 1045 -29 C ATOM 1100 CE2 PHE A 178 22.819 15.366 155.109 1.00 37.88 C ANISOU 1100 CE2 PHE A 178 6158 5683 2552 155 948 -30 C ATOM 1101 CZ PHE A 178 23.624 14.998 154.047 1.00 38.73 C ANISOU 1101 CZ PHE A 178 6298 5819 2598 186 1045 -51 C ATOM 1102 N THR A 179 20.007 21.543 153.717 1.00 36.30 N ANISOU 1102 N THR A 179 5877 5638 2278 -27 688 332 N ATOM 1103 CA THR A 179 19.047 22.584 153.354 1.00 38.42 C ANISOU 1103 CA THR A 179 6155 5924 2519 -41 621 404 C ATOM 1104 C THR A 179 19.748 23.693 152.579 1.00 41.63 C ANISOU 1104 C THR A 179 6574 6353 2890 -57 683 492 C ATOM 1105 O THR A 179 20.758 24.234 153.029 1.00 41.08 O ANISOU 1105 O THR A 179 6483 6254 2870 -68 752 528 O ATOM 1106 CB THR A 179 18.347 23.185 154.585 1.00 37.48 C ANISOU 1106 CB THR A 179 6009 5749 2483 -41 558 429 C ATOM 1107 OG1 THR A 179 17.630 22.157 155.278 1.00 37.62 O ANISOU 1107 OG1 THR A 179 6013 5751 2529 -31 501 353 O ATOM 1108 CG2 THR A 179 17.371 24.270 154.162 1.00 37.45 C ANISOU 1108 CG2 THR A 179 6022 5760 2448 -45 499 510 C ATOM 1109 N LYS A 180 19.207 24.023 151.409 1.00 46.09 N ANISOU 1109 N LYS A 180 7174 6975 3364 -63 657 532 N ATOM 1110 CA LYS A 180 19.838 24.980 150.506 1.00 48.85 C ANISOU 1110 CA LYS A 180 7545 7351 3663 -81 718 618 C ATOM 1111 C LYS A 180 18.825 25.928 149.871 1.00 49.50 C ANISOU 1111 C LYS A 180 7659 7458 3692 -86 651 705 C ATOM 1112 O LYS A 180 17.614 25.708 149.944 1.00 48.39 O ANISOU 1112 O LYS A 180 7516 7336 3533 -75 556 691 O ATOM 1113 CB LYS A 180 20.603 24.240 149.403 1.00 52.34 C ANISOU 1113 CB LYS A 180 8009 7859 4019 -82 792 578 C ATOM 1114 CG LYS A 180 21.758 23.388 149.904 1.00 56.08 C ANISOU 1114 CG LYS A 180 8456 8314 4540 -70 879 509 C ATOM 1115 CD LYS A 180 22.053 22.235 148.957 1.00 60.55 C ANISOU 1115 CD LYS A 180 9056 8931 5019 -53 923 430 C ATOM 1116 CE LYS A 180 22.950 21.200 149.621 1.00 63.23 C ANISOU 1116 CE LYS A 180 9373 9237 5415 -25 994 351 C ATOM 1117 NZ LYS A 180 22.572 19.806 149.255 1.00 62.79 N1+ ANISOU 1117 NZ LYS A 180 9365 9182 5309 2 981 244 N1+ HETATM 1118 N YCM A 181 19.334 26.988 149.251 1.00 51.33 N ANISOU 1118 N YCM A 181 7916 7691 3897 -105 702 801 N HETATM 1119 CA YCM A 181 18.529 27.840 148.412 1.00 53.52 C ANISOU 1119 CA YCM A 181 8234 7998 4103 -109 651 893 C HETATM 1120 CB YCM A 181 18.805 29.332 148.600 1.00 53.26 C ANISOU 1120 CB YCM A 181 8228 7891 4117 -119 684 1011 C HETATM 1121 SG YCM A 181 17.945 30.434 147.510 1.00 56.08 S ANISOU 1121 SG YCM A 181 8648 8273 4386 -118 633 1140 S HETATM 1122 CD YCM A 181 19.045 30.731 146.160 1.00 64.13 C ANISOU 1122 CD YCM A 181 9701 9352 5311 -155 734 1198 C HETATM 1123 CE YCM A 181 20.078 31.810 146.405 1.00 64.97 C ANISOU 1123 CE YCM A 181 9822 9382 5483 -180 830 1280 C HETATM 1124 OZ1 YCM A 181 21.301 31.570 146.277 1.00 65.55 O ANISOU 1124 OZ1 YCM A 181 9870 9475 5561 -209 931 1260 O HETATM 1125 NZ2 YCM A 181 19.651 33.058 146.768 1.00 65.36 N ANISOU 1125 NZ2 YCM A 181 9912 9336 5586 -171 811 1381 N HETATM 1126 C YCM A 181 18.707 27.449 146.950 1.00 56.43 C ANISOU 1126 C YCM A 181 8633 8468 4338 -121 675 893 C HETATM 1127 O YCM A 181 19.785 27.543 146.358 1.00 56.77 O ANISOU 1127 O YCM A 181 8688 8533 4350 -137 770 909 O ATOM 1128 N GLN A 182 17.617 26.987 146.348 1.00 59.11 N ANISOU 1128 N GLN A 182 8983 8883 4592 -114 588 874 N ATOM 1129 CA GLN A 182 17.667 26.526 144.966 1.00 63.79 C ANISOU 1129 CA GLN A 182 9609 9574 5055 -119 600 860 C ATOM 1130 C GLN A 182 16.478 27.016 144.153 1.00 67.38 C ANISOU 1130 C GLN A 182 10087 10086 5428 -123 502 928 C ATOM 1131 O GLN A 182 15.374 27.162 144.675 1.00 67.78 O ANISOU 1131 O GLN A 182 10117 10120 5515 -117 405 940 O ATOM 1132 CB GLN A 182 17.733 24.998 144.917 1.00 65.14 C ANISOU 1132 CB GLN A 182 9772 9783 5197 -99 606 722 C ATOM 1133 CG GLN A 182 19.118 24.450 144.613 1.00 67.22 C ANISOU 1133 CG GLN A 182 10047 10052 5441 -103 730 672 C ATOM 1134 CD GLN A 182 19.111 22.954 144.382 1.00 68.48 C ANISOU 1134 CD GLN A 182 10227 10239 5555 -81 737 539 C ATOM 1135 OE1 GLN A 182 19.779 22.201 145.091 1.00 67.96 O ANISOU 1135 OE1 GLN A 182 10145 10113 5563 -70 789 461 O ATOM 1136 NE2 GLN A 182 18.350 22.513 143.387 1.00 70.11 N ANISOU 1136 NE2 GLN A 182 10473 10528 5637 -72 683 514 N ATOM 1137 N LYS A 183 16.714 27.270 142.870 1.00 71.24 N ANISOU 1137 N LYS A 183 10618 10646 5803 -139 529 977 N ATOM 1138 CA LYS A 183 15.650 27.678 141.964 1.00 73.84 C ANISOU 1138 CA LYS A 183 10974 11046 6037 -151 436 1044 C ATOM 1139 C LYS A 183 14.891 26.457 141.457 1.00 75.19 C ANISOU 1139 C LYS A 183 11121 11324 6125 -114 373 946 C ATOM 1140 O LYS A 183 15.425 25.661 140.687 1.00 76.78 O ANISOU 1140 O LYS A 183 11349 11588 6238 -91 429 878 O ATOM 1141 CB LYS A 183 16.216 28.480 140.789 1.00 75.61 C ANISOU 1141 CB LYS A 183 11259 11306 6164 -180 492 1143 C ATOM 1142 N GLU A 184 13.648 26.308 141.906 1.00 75.53 N ANISOU 1142 N GLU A 184 11122 11382 6194 -94 263 939 N ATOM 1143 CA GLU A 184 12.793 25.214 141.455 1.00 78.00 C ANISOU 1143 CA GLU A 184 11430 11780 6425 12 204 851 C ATOM 1144 C GLU A 184 11.600 25.743 140.663 1.00 78.60 C ANISOU 1144 C GLU A 184 11520 11933 6412 110 114 934 C ATOM 1145 O GLU A 184 10.809 26.533 141.182 1.00 77.18 O ANISOU 1145 O GLU A 184 11261 11766 6296 19 29 1023 O ATOM 1146 CB GLU A 184 12.305 24.382 142.643 1.00 79.09 C ANISOU 1146 CB GLU A 184 11547 11845 6657 57 167 751 C ATOM 1147 CG GLU A 184 13.140 23.143 142.925 1.00 80.51 C ANISOU 1147 CG GLU A 184 11759 11983 6848 33 236 615 C ATOM 1148 CD GLU A 184 12.307 21.990 143.458 1.00 81.45 C ANISOU 1148 CD GLU A 184 11904 12070 6976 62 167 501 C ATOM 1149 OE1 GLU A 184 11.062 22.084 143.419 1.00 82.11 O ANISOU 1149 OE1 GLU A 184 12016 12152 7030 112 64 517 O ATOM 1150 OE2 GLU A 184 12.897 20.989 143.917 1.00 81.28 O1+ ANISOU 1150 OE2 GLU A 184 11893 12006 6984 28 216 396 O1+ ATOM 1151 N ASP A 185 11.481 25.295 139.414 1.00 80.31 N ANISOU 1151 N ASP A 185 11865 12176 6474 214 117 900 N ATOM 1152 CA ASP A 185 10.423 25.737 138.505 1.00 82.75 C ANISOU 1152 CA ASP A 185 12449 12333 6658 353 38 935 C ATOM 1153 C ASP A 185 10.408 27.259 138.377 1.00 83.56 C ANISOU 1153 C ASP A 185 12963 12010 6774 135 3 1023 C ATOM 1154 O ASP A 185 9.347 27.886 138.418 1.00 83.55 O ANISOU 1154 O ASP A 185 12951 12043 6752 -7 -139 1110 O ATOM 1155 CB ASP A 185 9.056 25.227 138.973 1.00 82.61 C ANISOU 1155 CB ASP A 185 12561 12196 6631 295 -114 867 C ATOM 1156 N SER A 186 11.602 27.831 138.231 1.00 84.55 N ANISOU 1156 N SER A 186 12479 12703 6943 -328 31 1180 N ATOM 1157 CA SER A 186 11.805 29.275 138.102 1.00 86.16 C ANISOU 1157 CA SER A 186 12890 12696 7149 -348 44 1302 C ATOM 1158 C SER A 186 11.346 30.050 139.339 1.00 85.92 C ANISOU 1158 C SER A 186 12868 12524 7252 -276 13 1357 C ATOM 1159 O SER A 186 11.050 31.242 139.255 1.00 86.98 O ANISOU 1159 O SER A 186 13058 12605 7385 -218 -6 1490 O ATOM 1160 CB SER A 186 11.093 29.810 136.856 1.00 88.59 C ANISOU 1160 CB SER A 186 13453 12908 7299 -337 -30 1366 C ATOM 1161 N VAL A 187 11.294 29.372 140.482 1.00 84.80 N ANISOU 1161 N VAL A 187 12628 12369 7224 -269 13 1265 N ATOM 1162 CA VAL A 187 10.977 30.011 141.759 1.00 84.55 C ANISOU 1162 CA VAL A 187 12563 12239 7323 -201 0 1308 C ATOM 1163 C VAL A 187 11.999 29.601 142.814 1.00 84.63 C ANISOU 1163 C VAL A 187 12440 12260 7455 -188 101 1241 C ATOM 1164 O VAL A 187 12.303 28.418 142.958 1.00 89.44 O ANISOU 1164 O VAL A 187 12962 12950 8071 -194 127 1124 O ATOM 1165 CB VAL A 187 9.559 29.644 142.261 1.00 85.28 C ANISOU 1165 CB VAL A 187 12718 12261 7425 -152 -125 1267 C ATOM 1166 CG1 VAL A 187 9.153 30.551 143.413 1.00 85.11 C ANISOU 1166 CG1 VAL A 187 12629 12192 7518 -74 -140 1353 C ATOM 1167 CG2 VAL A 187 8.542 29.742 141.134 1.00 87.66 C ANISOU 1167 CG2 VAL A 187 13155 12573 7580 -91 -224 1308 C ATOM 1168 N TYR A 188 12.531 30.573 143.551 1.00 80.81 N ANISOU 1168 N TYR A 188 11950 11690 7062 -143 164 1315 N ATOM 1169 CA TYR A 188 13.483 30.273 144.617 1.00 76.31 C ANISOU 1169 CA TYR A 188 11312 11079 6604 -126 253 1251 C ATOM 1170 C TYR A 188 12.793 29.652 145.824 1.00 69.61 C ANISOU 1170 C TYR A 188 10408 10197 5843 -109 195 1171 C ATOM 1171 O TYR A 188 11.735 30.111 146.252 1.00 69.22 O ANISOU 1171 O TYR A 188 10380 10103 5817 -84 112 1217 O ATOM 1172 CB TYR A 188 14.234 31.530 145.056 1.00 78.54 C ANISOU 1172 CB TYR A 188 11624 11266 6953 -103 335 1355 C ATOM 1173 CG TYR A 188 15.124 32.124 143.994 1.00 82.49 C ANISOU 1173 CG TYR A 188 12172 11789 7381 -127 415 1432 C ATOM 1174 CD1 TYR A 188 16.420 31.660 143.808 1.00 83.84 C ANISOU 1174 CD1 TYR A 188 12319 11987 7549 -152 525 1379 C ATOM 1175 CD2 TYR A 188 14.676 33.159 143.188 1.00 84.86 C ANISOU 1175 CD2 TYR A 188 12547 12081 7615 -120 385 1564 C ATOM 1176 CE1 TYR A 188 17.241 32.204 142.839 1.00 85.55 C ANISOU 1176 CE1 TYR A 188 12578 12229 7698 -178 604 1452 C ATOM 1177 CE2 TYR A 188 15.489 33.711 142.219 1.00 86.94 C ANISOU 1177 CE2 TYR A 188 12856 12367 7811 -147 462 1640 C ATOM 1178 CZ TYR A 188 16.770 33.230 142.046 1.00 87.27 C ANISOU 1178 CZ TYR A 188 12867 12442 7850 -180 573 1583 C ATOM 1179 OH TYR A 188 17.582 33.777 141.079 1.00 89.02 O ANISOU 1179 OH TYR A 188 13133 12690 8002 -211 655 1660 O ATOM 1180 N VAL A 189 13.399 28.605 146.371 1.00 63.37 N ANISOU 1180 N VAL A 189 9554 9425 5099 -108 242 1055 N ATOM 1181 CA VAL A 189 12.891 27.988 147.587 1.00 56.74 C ANISOU 1181 CA VAL A 189 8659 8551 4347 -92 201 978 C ATOM 1182 C VAL A 189 14.021 27.677 148.558 1.00 51.95 C ANISOU 1182 C VAL A 189 8023 7885 3832 -77 294 917 C ATOM 1183 O VAL A 189 15.101 27.237 148.160 1.00 51.48 O ANISOU 1183 O VAL A 189 7968 7845 3749 -84 377 877 O ATOM 1184 CB VAL A 189 12.107 26.689 147.291 1.00 56.28 C ANISOU 1184 CB VAL A 189 8553 8591 4241 -98 132 880 C ATOM 1185 CG1 VAL A 189 10.744 27.007 146.695 1.00 57.42 C ANISOU 1185 CG1 VAL A 189 8749 8751 4317 -150 10 933 C ATOM 1186 CG2 VAL A 189 12.903 25.776 146.372 1.00 57.00 C ANISOU 1186 CG2 VAL A 189 8644 8763 4251 -73 198 809 C ATOM 1187 N CYS A 190 13.769 27.936 149.834 1.00 47.96 N ANISOU 1187 N CYS A 190 7497 7301 3426 -59 278 914 N ATOM 1188 CA CYS A 190 14.651 27.477 150.893 1.00 42.81 C ANISOU 1188 CA CYS A 190 6812 6580 2872 -50 342 838 C ATOM 1189 C CYS A 190 14.089 26.167 151.415 1.00 38.63 C ANISOU 1189 C CYS A 190 6237 6087 2353 -47 292 730 C ATOM 1190 O CYS A 190 13.181 26.164 152.242 1.00 38.60 O ANISOU 1190 O CYS A 190 6209 6063 2396 -38 228 723 O ATOM 1191 CB CYS A 190 14.760 28.515 152.010 1.00 41.86 C ANISOU 1191 CB CYS A 190 6699 6346 2859 -28 361 889 C ATOM 1192 SG CYS A 190 15.854 28.049 153.369 1.00 46.02 S ANISOU 1192 SG CYS A 190 7190 6796 3498 -33 431 806 S ATOM 1193 N GLY A 191 14.611 25.055 150.910 1.00 37.27 N ANISOU 1193 N GLY A 191 6062 5963 2135 -51 326 646 N ATOM 1194 CA GLY A 191 14.077 23.754 151.265 1.00 37.17 C ANISOU 1194 CA GLY A 191 6026 5973 2124 -39 284 543 C ATOM 1195 C GLY A 191 15.137 22.706 151.530 1.00 36.47 C ANISOU 1195 C GLY A 191 5945 5844 2068 -40 358 447 C ATOM 1196 O GLY A 191 16.316 22.925 151.250 1.00 36.53 O ANISOU 1196 O GLY A 191 5968 5834 2079 -46 444 460 O ATOM 1197 N PRO A 192 14.717 21.557 152.081 1.00 35.06 N ANISOU 1197 N PRO A 192 5759 5650 1913 -34 326 356 N ATOM 1198 CA PRO A 192 15.593 20.419 152.375 1.00 36.04 C ANISOU 1198 CA PRO A 192 5899 5728 2067 -35 388 263 C ATOM 1199 C PRO A 192 15.865 19.558 151.145 1.00 39.70 C ANISOU 1199 C PRO A 192 6419 6239 2427 -36 420 205 C ATOM 1200 O PRO A 192 14.958 19.307 150.353 1.00 42.53 O ANISOU 1200 O PRO A 192 6805 6658 2696 -38 359 193 O ATOM 1201 CB PRO A 192 14.798 19.636 153.418 1.00 35.03 C ANISOU 1201 CB PRO A 192 5753 5559 1998 -36 328 202 C ATOM 1202 CG PRO A 192 13.376 19.912 153.066 1.00 35.19 C ANISOU 1202 CG PRO A 192 5766 5641 1963 -33 231 232 C ATOM 1203 CD PRO A 192 13.339 21.328 152.551 1.00 34.55 C ANISOU 1203 CD PRO A 192 5670 5604 1853 -25 229 344 C ATOM 1204 N TYR A 193 17.107 19.111 150.995 1.00 41.24 N ANISOU 1204 N TYR A 193 6634 6407 2628 -31 517 170 N ATOM 1205 CA TYR A 193 17.487 18.267 149.870 1.00 43.03 C ANISOU 1205 CA TYR A 193 6924 6667 2758 -28 565 108 C ATOM 1206 C TYR A 193 18.329 17.079 150.321 1.00 42.87 C ANISOU 1206 C TYR A 193 6930 6579 2779 -12 639 19 C ATOM 1207 O TYR A 193 19.448 16.883 149.847 1.00 43.27 O ANISOU 1207 O TYR A 193 7001 6633 2808 7 740 7 O ATOM 1208 CB TYR A 193 18.248 19.081 148.823 1.00 44.54 C ANISOU 1208 CB TYR A 193 7125 6918 2880 -28 632 174 C ATOM 1209 CG TYR A 193 17.385 20.077 148.085 1.00 45.95 C ANISOU 1209 CG TYR A 193 7300 7172 2985 -39 563 260 C ATOM 1210 CD1 TYR A 193 17.185 21.358 148.583 1.00 45.74 C ANISOU 1210 CD1 TYR A 193 7230 7134 3015 -46 536 362 C ATOM 1211 CD2 TYR A 193 16.763 19.732 146.892 1.00 47.47 C ANISOU 1211 CD2 TYR A 193 7543 7445 3049 -38 526 239 C ATOM 1212 CE1 TYR A 193 16.393 22.270 147.909 1.00 46.83 C ANISOU 1212 CE1 TYR A 193 7370 7337 3086 -50 477 450 C ATOM 1213 CE2 TYR A 193 15.969 20.637 146.213 1.00 48.41 C ANISOU 1213 CE2 TYR A 193 7657 7642 3093 -36 462 327 C ATOM 1214 CZ TYR A 193 15.788 21.904 146.725 1.00 48.19 C ANISOU 1214 CZ TYR A 193 7582 7598 3132 -42 438 435 C ATOM 1215 OH TYR A 193 15.000 22.806 146.050 1.00 49.35 O ANISOU 1215 OH TYR A 193 7726 7799 3225 -38 375 528 O ATOM 1216 N PHE A 194 17.782 16.291 151.240 1.00 42.66 N ANISOU 1216 N PHE A 194 6905 6491 2812 -15 593 -39 N ATOM 1217 CA PHE A 194 18.444 15.080 151.711 1.00 43.12 C ANISOU 1217 CA PHE A 194 7001 6474 2909 7 657 -120 C ATOM 1218 C PHE A 194 18.528 14.031 150.610 1.00 44.86 C ANISOU 1218 C PHE A 194 7316 6698 3031 8 696 -204 C ATOM 1219 O PHE A 194 17.626 13.926 149.781 1.00 45.67 O ANISOU 1219 O PHE A 194 7459 6849 3045 -24 632 -225 O ATOM 1220 CB PHE A 194 17.700 14.483 152.909 1.00 43.80 C ANISOU 1220 CB PHE A 194 7077 6492 3071 -5 593 -155 C ATOM 1221 CG PHE A 194 17.614 15.395 154.097 1.00 44.67 C ANISOU 1221 CG PHE A 194 7105 6590 3278 -4 559 -86 C ATOM 1222 CD1 PHE A 194 16.570 16.296 154.222 1.00 45.01 C ANISOU 1222 CD1 PHE A 194 7105 6673 3322 -27 470 -30 C ATOM 1223 CD2 PHE A 194 18.567 15.337 155.100 1.00 45.06 C ANISOU 1223 CD2 PHE A 194 7121 6587 3411 27 618 -77 C ATOM 1224 CE1 PHE A 194 16.486 17.131 155.320 1.00 44.45 C ANISOU 1224 CE1 PHE A 194 6970 6582 3337 -24 445 28 C ATOM 1225 CE2 PHE A 194 18.490 16.170 156.199 1.00 43.90 C ANISOU 1225 CE2 PHE A 194 6908 6429 3345 23 586 -20 C ATOM 1226 CZ PHE A 194 17.448 17.068 156.309 1.00 43.69 C ANISOU 1226 CZ PHE A 194 6848 6431 3320 -4 501 29 C ATOM 1227 N PRO A 195 19.615 13.247 150.597 1.00 44.68 N ANISOU 1227 N PRO A 195 7332 6625 3019 49 803 -253 N ATOM 1228 CA PRO A 195 19.618 12.020 149.794 1.00 48.56 C ANISOU 1228 CA PRO A 195 7932 7085 3432 54 842 -353 C ATOM 1229 C PRO A 195 18.559 11.042 150.305 1.00 50.70 C ANISOU 1229 C PRO A 195 8259 7287 3719 15 765 -425 C ATOM 1230 O PRO A 195 17.964 11.289 151.356 1.00 49.52 O ANISOU 1230 O PRO A 195 8054 7115 3649 -3 695 -394 O ATOM 1231 CB PRO A 195 21.032 11.471 149.994 1.00 48.42 C ANISOU 1231 CB PRO A 195 7928 7015 3454 125 979 -375 C ATOM 1232 CG PRO A 195 21.851 12.675 150.327 1.00 47.44 C ANISOU 1232 CG PRO A 195 7700 6944 3382 144 1017 -275 C ATOM 1233 CD PRO A 195 20.948 13.554 151.141 1.00 44.96 C ANISOU 1233 CD PRO A 195 7315 6643 3124 99 903 -213 C ATOM 1234 N ARG A 196 18.326 9.956 149.574 1.00 55.65 N ANISOU 1234 N ARG A 196 8998 7877 4269 -2 780 -519 N ATOM 1235 CA ARG A 196 17.267 9.013 149.926 1.00 55.65 C ANISOU 1235 CA ARG A 196 9063 7810 4271 -59 706 -589 C ATOM 1236 C ARG A 196 17.444 8.456 151.336 1.00 55.78 C ANISOU 1236 C ARG A 196 9069 7720 4406 -37 722 -596 C ATOM 1237 O ARG A 196 16.505 8.457 152.134 1.00 56.28 O ANISOU 1237 O ARG A 196 9103 7766 4515 -85 633 -586 O ATOM 1238 CB ARG A 196 17.216 7.866 148.914 1.00 56.35 C ANISOU 1238 CB ARG A 196 9294 7858 4260 -81 743 -697 C ATOM 1239 N GLY A 197 18.653 7.994 151.639 1.00 54.90 N ANISOU 1239 N GLY A 197 8979 7542 4338 41 838 -607 N ATOM 1240 CA GLY A 197 18.940 7.407 152.935 1.00 53.47 C ANISOU 1240 CA GLY A 197 8799 7260 4259 79 865 -609 C ATOM 1241 C GLY A 197 18.918 8.412 154.071 1.00 50.64 C ANISOU 1241 C GLY A 197 8311 6940 3991 86 817 -518 C ATOM 1242 O GLY A 197 18.503 8.093 155.185 1.00 48.80 O ANISOU 1242 O GLY A 197 8069 6648 3826 75 778 -515 O ATOM 1243 N TRP A 198 19.361 9.632 153.787 1.00 48.41 N ANISOU 1243 N TRP A 198 7936 6753 3705 100 822 -444 N ATOM 1244 CA TRP A 198 19.466 10.664 154.812 1.00 45.28 C ANISOU 1244 CA TRP A 198 7426 6388 3391 106 788 -358 C ATOM 1245 C TRP A 198 18.112 11.234 155.215 1.00 42.94 C ANISOU 1245 C TRP A 198 7085 6124 3108 37 661 -331 C ATOM 1246 O TRP A 198 17.938 11.687 156.346 1.00 42.87 O ANISOU 1246 O TRP A 198 7009 6103 3176 36 623 -287 O ATOM 1247 CB TRP A 198 20.383 11.787 154.334 1.00 45.87 C ANISOU 1247 CB TRP A 198 7430 6543 3455 131 841 -288 C ATOM 1248 CG TRP A 198 21.821 11.408 154.382 1.00 47.22 C ANISOU 1248 CG TRP A 198 7603 6692 3648 211 970 -290 C ATOM 1249 CD1 TRP A 198 22.584 10.945 153.352 1.00 49.23 C ANISOU 1249 CD1 TRP A 198 7910 6954 3839 252 1068 -325 C ATOM 1250 CD2 TRP A 198 22.673 11.444 155.531 1.00 46.08 C ANISOU 1250 CD2 TRP A 198 7398 6520 3591 269 1018 -251 C ATOM 1251 NE1 TRP A 198 23.863 10.696 153.787 1.00 48.84 N ANISOU 1251 NE1 TRP A 198 7829 6886 3840 339 1179 -307 N ATOM 1252 CE2 TRP A 198 23.943 10.995 155.120 1.00 47.38 C ANISOU 1252 CE2 TRP A 198 7573 6683 3745 351 1148 -260 C ATOM 1253 CE3 TRP A 198 22.485 11.816 156.865 1.00 45.43 C ANISOU 1253 CE3 TRP A 198 7252 6421 3590 263 965 -208 C ATOM 1254 CZ2 TRP A 198 25.020 10.909 155.998 1.00 48.63 C ANISOU 1254 CZ2 TRP A 198 7669 6835 3975 432 1223 -220 C ATOM 1255 CZ3 TRP A 198 23.555 11.729 157.734 1.00 46.66 C ANISOU 1255 CZ3 TRP A 198 7357 6567 3806 336 1035 -174 C ATOM 1256 CH2 TRP A 198 24.807 11.279 157.297 1.00 49.82 C ANISOU 1256 CH2 TRP A 198 7757 6975 4196 422 1162 -177 C ATOM 1257 N ASN A 199 17.156 11.216 154.294 1.00 42.31 N ANISOU 1257 N ASN A 199 7040 6088 2947 -16 597 -356 N ATOM 1258 CA ASN A 199 15.811 11.676 154.608 1.00 41.56 C ANISOU 1258 CA ASN A 199 6903 6031 2858 -71 481 -330 C ATOM 1259 C ASN A 199 15.099 10.676 155.509 1.00 41.47 C ANISOU 1259 C ASN A 199 6929 5939 2889 -107 441 -382 C ATOM 1260 O ASN A 199 14.309 11.056 156.374 1.00 39.77 O ANISOU 1260 O ASN A 199 6654 5733 2725 -132 371 -348 O ATOM 1261 CB ASN A 199 15.001 11.910 153.334 1.00 42.95 C ANISOU 1261 CB ASN A 199 7105 6288 2926 -110 423 -337 C ATOM 1262 CG ASN A 199 13.608 12.434 153.621 1.00 42.90 C ANISOU 1262 CG ASN A 199 7048 6331 2921 -153 306 -301 C ATOM 1263 OD1 ASN A 199 13.425 13.616 153.912 1.00 42.50 O ANISOU 1263 OD1 ASN A 199 6915 6332 2901 -132 275 -217 O ATOM 1264 ND2 ASN A 199 12.615 11.555 153.541 1.00 43.62 N ANISOU 1264 ND2 ASN A 199 7191 6403 2978 -214 245 -364 N ATOM 1265 N ASN A 200 15.386 9.395 155.297 1.00 42.32 N ANISOU 1265 N ASN A 200 7141 5964 2973 -109 494 -464 N ATOM 1266 CA ASN A 200 14.840 8.340 156.138 1.00 39.68 C ANISOU 1266 CA ASN A 200 6864 5536 2678 -147 474 -514 C ATOM 1267 C ASN A 200 15.397 8.434 157.546 1.00 37.37 C ANISOU 1267 C ASN A 200 6520 5192 2486 -96 504 -471 C ATOM 1268 O ASN A 200 14.657 8.340 158.525 1.00 36.49 O ANISOU 1268 O ASN A 200 6384 5058 2423 -133 447 -460 O ATOM 1269 CB ASN A 200 15.144 6.963 155.550 1.00 41.06 C ANISOU 1269 CB ASN A 200 7182 5617 2804 -152 539 -610 C ATOM 1270 CG ASN A 200 14.652 6.816 154.127 1.00 43.70 C ANISOU 1270 CG ASN A 200 7577 6002 3025 -206 512 -660 C ATOM 1271 OD1 ASN A 200 13.744 7.526 153.695 1.00 44.24 O ANISOU 1271 OD1 ASN A 200 7590 6169 3051 -257 420 -631 O ATOM 1272 ND2 ASN A 200 15.250 5.890 153.388 1.00 45.72 N ANISOU 1272 ND2 ASN A 200 7951 6193 3229 -187 594 -735 N ATOM 1273 N PHE A 201 16.709 8.622 157.639 1.00 36.01 N ANISOU 1273 N PHE A 201 6331 5009 2341 -12 594 -446 N ATOM 1274 CA PHE A 201 17.365 8.741 158.931 1.00 33.83 C ANISOU 1274 CA PHE A 201 6005 4698 2152 44 626 -402 C ATOM 1275 C PHE A 201 16.856 9.954 159.693 1.00 31.89 C ANISOU 1275 C PHE A 201 5643 4519 1955 18 548 -328 C ATOM 1276 O PHE A 201 16.590 9.877 160.891 1.00 31.96 O ANISOU 1276 O PHE A 201 5625 4495 2022 15 520 -309 O ATOM 1277 CB PHE A 201 18.881 8.834 158.772 1.00 33.34 C ANISOU 1277 CB PHE A 201 5931 4637 2100 138 736 -380 C ATOM 1278 CG PHE A 201 19.581 9.307 160.011 1.00 31.45 C ANISOU 1278 CG PHE A 201 5611 4400 1938 192 755 -316 C ATOM 1279 CD1 PHE A 201 19.743 8.458 161.094 1.00 31.00 C ANISOU 1279 CD1 PHE A 201 5590 4262 1927 234 776 -324 C ATOM 1280 CD2 PHE A 201 20.062 10.603 160.102 1.00 29.85 C ANISOU 1280 CD2 PHE A 201 5305 4282 1757 197 751 -245 C ATOM 1281 CE1 PHE A 201 20.377 8.890 162.243 1.00 30.08 C ANISOU 1281 CE1 PHE A 201 5397 4161 1869 284 787 -262 C ATOM 1282 CE2 PHE A 201 20.698 11.041 161.247 1.00 30.19 C ANISOU 1282 CE2 PHE A 201 5276 4332 1861 236 763 -190 C ATOM 1283 CZ PHE A 201 20.856 10.183 162.320 1.00 30.02 C ANISOU 1283 CZ PHE A 201 5283 4244 1880 282 779 -198 C ATOM 1284 N HIS A 202 16.728 11.076 158.994 1.00 27.56 N ANISOU 1284 N HIS A 202 5034 4060 1378 3 519 -286 N ATOM 1285 CA HIS A 202 16.278 12.311 159.621 1.00 35.08 C ANISOU 1285 CA HIS A 202 5888 5066 2373 -12 457 -215 C ATOM 1286 C HIS A 202 14.860 12.169 160.160 1.00 31.47 C ANISOU 1286 C HIS A 202 5421 4608 1928 -67 364 -223 C ATOM 1287 O HIS A 202 14.533 12.704 161.218 1.00 28.97 O ANISOU 1287 O HIS A 202 5044 4294 1671 -69 328 -183 O ATOM 1288 CB HIS A 202 16.350 13.474 158.631 1.00 37.87 C ANISOU 1288 CB HIS A 202 6203 5504 2683 -15 450 -166 C ATOM 1289 CG HIS A 202 15.843 14.769 159.183 1.00 39.58 C ANISOU 1289 CG HIS A 202 6339 5762 2938 -26 393 -94 C ATOM 1290 ND1 HIS A 202 14.713 15.393 158.700 1.00 40.13 N ANISOU 1290 ND1 HIS A 202 6390 5888 2970 -53 319 -67 N ATOM 1291 CD2 HIS A 202 16.307 15.555 160.184 1.00 39.43 C ANISOU 1291 CD2 HIS A 202 6262 5733 2988 -8 403 -43 C ATOM 1292 CE1 HIS A 202 14.507 16.510 159.374 1.00 39.24 C ANISOU 1292 CE1 HIS A 202 6215 5789 2904 -46 292 -2 C ATOM 1293 NE2 HIS A 202 15.460 16.632 160.281 1.00 38.69 N ANISOU 1293 NE2 HIS A 202 6125 5676 2900 -25 341 9 N ATOM 1294 N THR A 203 14.027 11.435 159.431 1.00 31.78 N ANISOU 1294 N THR A 203 5523 4646 1907 -116 329 -277 N ATOM 1295 CA THR A 203 12.640 11.237 159.826 1.00 30.51 C ANISOU 1295 CA THR A 203 5353 4494 1745 -180 243 -287 C ATOM 1296 C THR A 203 12.535 10.446 161.127 1.00 30.46 C ANISOU 1296 C THR A 203 5366 4407 1801 -192 249 -305 C ATOM 1297 O THR A 203 11.846 10.864 162.056 1.00 30.43 O ANISOU 1297 O THR A 203 5302 4420 1840 -209 200 -270 O ATOM 1298 CB THR A 203 11.838 10.517 158.727 1.00 32.21 C ANISOU 1298 CB THR A 203 5641 4725 1873 -244 205 -347 C ATOM 1299 OG1 THR A 203 11.837 11.314 157.537 1.00 33.61 O ANISOU 1299 OG1 THR A 203 5799 4989 1983 -230 191 -320 O ATOM 1300 CG2 THR A 203 10.404 10.292 159.176 1.00 32.22 C ANISOU 1300 CG2 THR A 203 5626 4744 1873 -322 116 -353 C ATOM 1301 N ILE A 204 13.224 9.310 161.200 1.00 31.55 N ANISOU 1301 N ILE A 204 5594 4455 1938 -177 316 -358 N ATOM 1302 CA ILE A 204 13.152 8.466 162.389 1.00 30.87 C ANISOU 1302 CA ILE A 204 5547 4283 1900 -185 328 -372 C ATOM 1303 C ILE A 204 13.867 9.112 163.572 1.00 30.72 C ANISOU 1303 C ILE A 204 5452 4266 1953 -120 350 -309 C ATOM 1304 O ILE A 204 13.493 8.889 164.720 1.00 31.39 O ANISOU 1304 O ILE A 204 5527 4321 2079 -133 329 -294 O ATOM 1305 CB ILE A 204 13.744 7.059 162.136 1.00 31.85 C ANISOU 1305 CB ILE A 204 5808 4295 2000 -170 404 -440 C ATOM 1306 CG1 ILE A 204 15.247 7.134 161.872 1.00 34.27 C ANISOU 1306 CG1 ILE A 204 6121 4585 2314 -65 501 -429 C ATOM 1307 CG2 ILE A 204 13.034 6.381 160.974 1.00 32.93 C ANISOU 1307 CG2 ILE A 204 6031 4421 2059 -249 381 -512 C ATOM 1308 CD1 ILE A 204 15.936 5.790 161.898 1.00 37.97 C ANISOU 1308 CD1 ILE A 204 6721 4931 2776 -16 591 -481 C ATOM 1309 N MET A 205 14.884 9.922 163.294 1.00 30.34 N ANISOU 1309 N MET A 205 5352 4259 1914 -57 391 -272 N ATOM 1310 CA MET A 205 15.605 10.614 164.355 1.00 29.70 C ANISOU 1310 CA MET A 205 5199 4190 1894 -7 407 -214 C ATOM 1311 C MET A 205 14.719 11.677 164.985 1.00 30.77 C ANISOU 1311 C MET A 205 5247 4382 2063 -42 332 -169 C ATOM 1312 O MET A 205 14.675 11.821 166.204 1.00 31.86 O ANISOU 1312 O MET A 205 5350 4507 2248 -35 318 -142 O ATOM 1313 CB MET A 205 16.888 11.256 163.824 1.00 29.83 C ANISOU 1313 CB MET A 205 5184 4243 1906 52 471 -185 C ATOM 1314 CG MET A 205 17.695 11.981 164.894 1.00 28.55 C ANISOU 1314 CG MET A 205 4950 4100 1797 92 486 -128 C ATOM 1315 SD MET A 205 18.692 13.346 164.257 1.00 84.40 S ANISOU 1315 SD MET A 205 11957 11249 8864 111 524 -75 S ATOM 1316 CE MET A 205 17.421 14.446 163.637 1.00 29.77 C ANISOU 1316 CE MET A 205 5004 4381 1928 45 442 -56 C ATOM 1317 N ARG A 206 14.018 12.424 164.140 1.00 32.43 N ANISOU 1317 N ARG A 206 5426 4656 2241 -73 287 -157 N ATOM 1318 CA ARG A 206 13.105 13.459 164.604 1.00 35.54 C ANISOU 1318 CA ARG A 206 5747 5100 2657 -92 224 -112 C ATOM 1319 C ARG A 206 11.978 12.851 165.435 1.00 37.65 C ANISOU 1319 C ARG A 206 6020 5349 2938 -137 177 -129 C ATOM 1320 O ARG A 206 11.584 13.402 166.464 1.00 37.47 O ANISOU 1320 O ARG A 206 5943 5335 2957 -134 152 -96 O ATOM 1321 CB ARG A 206 12.537 14.240 163.417 1.00 38.11 C ANISOU 1321 CB ARG A 206 6055 5495 2929 -104 190 -92 C ATOM 1322 CG ARG A 206 11.319 15.086 163.745 1.00 39.26 C ANISOU 1322 CG ARG A 206 6147 5691 3079 -118 122 -51 C ATOM 1323 CD ARG A 206 11.585 16.566 163.532 1.00 40.01 C ANISOU 1323 CD ARG A 206 6196 5825 3179 -84 127 15 C ATOM 1324 NE ARG A 206 10.388 17.365 163.774 1.00 41.70 N ANISOU 1324 NE ARG A 206 6373 6084 3388 -84 69 58 N ATOM 1325 CZ ARG A 206 10.353 18.694 163.737 1.00 43.55 C ANISOU 1325 CZ ARG A 206 6580 6341 3626 -56 67 121 C ATOM 1326 NH1 ARG A 206 11.455 19.383 163.470 1.00 45.58 N1+ ANISOU 1326 NH1 ARG A 206 6844 6578 3895 -40 117 147 N1+ ATOM 1327 NH2 ARG A 206 9.216 19.334 163.971 1.00 43.15 N ANISOU 1327 NH2 ARG A 206 6503 6331 3562 -47 20 162 N ATOM 1328 N ASN A 207 11.474 11.704 164.990 1.00 40.09 N ANISOU 1328 N ASN A 207 6399 5626 3207 -185 168 -183 N ATOM 1329 CA ASN A 207 10.404 11.011 165.698 1.00 42.60 C ANISOU 1329 CA ASN A 207 6733 5924 3528 -248 128 -201 C ATOM 1330 C ASN A 207 10.834 10.486 167.060 1.00 40.31 C ANISOU 1330 C ASN A 207 6458 5568 3290 -230 161 -195 C ATOM 1331 O ASN A 207 10.038 10.444 167.994 1.00 40.61 O ANISOU 1331 O ASN A 207 6471 5612 3349 -266 130 -180 O ATOM 1332 CB ASN A 207 9.871 9.856 164.855 1.00 48.20 C ANISOU 1332 CB ASN A 207 7532 6605 4177 -321 117 -267 C ATOM 1333 CG ASN A 207 8.972 10.325 163.739 1.00 53.83 C ANISOU 1333 CG ASN A 207 8220 7404 4830 -362 55 -268 C ATOM 1334 OD1 ASN A 207 7.813 10.667 163.969 1.00 53.14 O ANISOU 1334 OD1 ASN A 207 8079 7378 4734 -410 -10 -245 O ATOM 1335 ND2 ASN A 207 9.498 10.348 162.520 1.00 58.31 N ANISOU 1335 ND2 ASN A 207 8823 7984 5348 -342 76 -289 N ATOM 1336 N ILE A 208 12.091 10.076 167.170 1.00 37.60 N ANISOU 1336 N ILE A 208 6157 5168 2961 -173 226 -202 N ATOM 1337 CA ILE A 208 12.611 9.598 168.444 1.00 34.58 C ANISOU 1337 CA ILE A 208 5792 4729 2617 -141 257 -186 C ATOM 1338 C ILE A 208 12.756 10.748 169.434 1.00 34.38 C ANISOU 1338 C ILE A 208 5667 4755 2641 -110 236 -129 C ATOM 1339 O ILE A 208 12.224 10.692 170.540 1.00 38.74 O ANISOU 1339 O ILE A 208 6201 5303 3217 -129 214 -111 O ATOM 1340 CB ILE A 208 13.972 8.897 168.276 1.00 31.61 C ANISOU 1340 CB ILE A 208 5486 4290 2235 -68 336 -199 C ATOM 1341 CG1 ILE A 208 13.796 7.575 167.528 1.00 30.65 C ANISOU 1341 CG1 ILE A 208 5492 4086 2066 -97 368 -265 C ATOM 1342 CG2 ILE A 208 14.613 8.653 169.630 1.00 29.72 C ANISOU 1342 CG2 ILE A 208 5246 4017 2031 -15 361 -162 C ATOM 1343 CD1 ILE A 208 15.096 6.895 167.182 1.00 27.79 C ANISOU 1343 CD1 ILE A 208 5206 3660 1692 -8 459 -282 C ATOM 1344 N LEU A 209 13.464 11.795 169.022 1.00 30.47 N ANISOU 1344 N LEU A 209 5116 4306 2155 -70 247 -103 N ATOM 1345 CA LEU A 209 13.767 12.911 169.910 1.00 28.20 C ANISOU 1345 CA LEU A 209 4753 4054 1909 -47 235 -57 C ATOM 1346 C LEU A 209 12.538 13.760 170.229 1.00 27.51 C ANISOU 1346 C LEU A 209 4611 4009 1832 -80 181 -38 C ATOM 1347 O LEU A 209 12.463 14.377 171.293 1.00 27.10 O ANISOU 1347 O LEU A 209 4518 3966 1812 -72 170 -13 O ATOM 1348 CB LEU A 209 14.857 13.792 169.296 1.00 26.42 C ANISOU 1348 CB LEU A 209 4499 3858 1681 -11 267 -35 C ATOM 1349 CG LEU A 209 16.195 13.112 168.996 1.00 23.75 C ANISOU 1349 CG LEU A 209 4203 3494 1329 39 334 -43 C ATOM 1350 CD1 LEU A 209 17.231 14.135 168.560 1.00 21.38 C ANISOU 1350 CD1 LEU A 209 3860 3237 1025 63 367 -11 C ATOM 1351 CD2 LEU A 209 16.687 12.324 170.202 1.00 22.72 C ANISOU 1351 CD2 LEU A 209 4093 3324 1214 75 352 -35 C ATOM 1352 N GLY A 210 11.576 13.790 169.312 1.00 26.75 N ANISOU 1352 N GLY A 210 4520 3943 1701 -113 150 -50 N ATOM 1353 CA GLY A 210 10.423 14.660 169.458 1.00 26.21 C ANISOU 1353 CA GLY A 210 4402 3927 1630 -129 104 -24 C ATOM 1354 C GLY A 210 9.121 13.968 169.817 1.00 26.24 C ANISOU 1354 C GLY A 210 4412 3942 1615 -184 68 -38 C ATOM 1355 O GLY A 210 8.085 14.621 169.954 1.00 25.35 O ANISOU 1355 O GLY A 210 4257 3883 1491 -195 32 -12 O ATOM 1356 N LEU A 211 9.164 12.649 169.975 1.00 26.13 N ANISOU 1356 N LEU A 211 4459 3878 1593 -223 81 -75 N ATOM 1357 CA LEU A 211 7.954 11.890 170.264 1.00 26.69 C ANISOU 1357 CA LEU A 211 4545 3957 1640 -301 50 -91 C ATOM 1358 C LEU A 211 8.230 10.676 171.145 1.00 28.54 C ANISOU 1358 C LEU A 211 4845 4112 1885 -328 82 -110 C ATOM 1359 O LEU A 211 7.711 10.585 172.254 1.00 30.65 O ANISOU 1359 O LEU A 211 5094 4384 2168 -350 79 -89 O ATOM 1360 CB LEU A 211 7.280 11.453 168.963 1.00 26.65 C ANISOU 1360 CB LEU A 211 4570 3981 1575 -364 14 -124 C ATOM 1361 CG LEU A 211 6.049 10.553 169.074 1.00 23.33 C ANISOU 1361 CG LEU A 211 4170 3575 1118 -476 -24 -148 C ATOM 1362 CD1 LEU A 211 4.985 11.184 169.960 1.00 23.40 C ANISOU 1362 CD1 LEU A 211 4093 3661 1137 -497 -55 -102 C ATOM 1363 CD2 LEU A 211 5.490 10.261 167.691 1.00 24.29 C ANISOU 1363 CD2 LEU A 211 4314 3737 1176 -539 -68 -183 C ATOM 1364 N VAL A 212 9.046 9.748 170.655 1.00 29.89 N ANISOU 1364 N VAL A 212 5104 4211 2043 -320 119 -146 N ATOM 1365 CA VAL A 212 9.337 8.522 171.396 1.00 30.25 C ANISOU 1365 CA VAL A 212 5239 4166 2088 -336 157 -160 C ATOM 1366 C VAL A 212 10.027 8.809 172.728 1.00 31.65 C ANISOU 1366 C VAL A 212 5384 4331 2309 -270 181 -114 C ATOM 1367 O VAL A 212 9.657 8.244 173.758 1.00 32.57 O ANISOU 1367 O VAL A 212 5529 4419 2428 -299 187 -98 O ATOM 1368 CB VAL A 212 10.210 7.559 170.568 1.00 31.02 C ANISOU 1368 CB VAL A 212 5448 4180 2158 -315 207 -206 C ATOM 1369 CG1 VAL A 212 10.751 6.437 171.445 1.00 30.80 C ANISOU 1369 CG1 VAL A 212 5522 4048 2132 -293 260 -204 C ATOM 1370 CG2 VAL A 212 9.413 6.995 169.400 1.00 31.33 C ANISOU 1370 CG2 VAL A 212 5543 4216 2143 -404 181 -264 C ATOM 1371 N LEU A 213 11.019 9.694 172.712 1.00 31.84 N ANISOU 1371 N LEU A 213 5353 4384 2362 -191 193 -91 N ATOM 1372 CA LEU A 213 11.730 10.056 173.937 1.00 20.87 C ANISOU 1372 CA LEU A 213 3927 2996 1006 -137 206 -49 C ATOM 1373 C LEU A 213 10.836 10.787 174.951 1.00 20.43 C ANISOU 1373 C LEU A 213 3801 2992 971 -163 172 -22 C ATOM 1374 O LEU A 213 10.792 10.385 176.111 1.00 20.41 O ANISOU 1374 O LEU A 213 3810 2971 974 -164 180 0 O ATOM 1375 CB LEU A 213 12.973 10.898 173.618 1.00 24.60 C ANISOU 1375 CB LEU A 213 4355 3496 1494 -70 223 -34 C ATOM 1376 CG LEU A 213 13.722 11.482 174.821 1.00 25.00 C ANISOU 1376 CG LEU A 213 4358 3570 1571 -28 223 5 C ATOM 1377 CD1 LEU A 213 14.239 10.373 175.723 1.00 24.78 C ANISOU 1377 CD1 LEU A 213 4391 3492 1532 4 248 25 C ATOM 1378 CD2 LEU A 213 14.863 12.384 174.371 1.00 23.99 C ANISOU 1378 CD2 LEU A 213 4188 3477 1448 13 238 18 C ATOM 1379 N PRO A 214 10.119 11.854 174.532 1.00 28.63 N ANISOU 1379 N PRO A 214 4772 4094 2013 -176 142 -20 N ATOM 1380 CA PRO A 214 9.259 12.511 175.526 1.00 28.19 C ANISOU 1380 CA PRO A 214 4662 4081 1969 -189 125 4 C ATOM 1381 C PRO A 214 8.146 11.611 176.053 1.00 28.83 C ANISOU 1381 C PRO A 214 4770 4158 2028 -258 120 3 C ATOM 1382 O PRO A 214 7.815 11.678 177.237 1.00 20.26 O ANISOU 1382 O PRO A 214 3665 3083 949 -261 129 25 O ATOM 1383 CB PRO A 214 8.659 13.691 174.753 1.00 19.88 C ANISOU 1383 CB PRO A 214 3557 3087 910 -182 100 10 C ATOM 1384 CG PRO A 214 9.586 13.926 173.631 1.00 19.88 C ANISOU 1384 CG PRO A 214 3569 3076 908 -152 108 0 C ATOM 1385 CD PRO A 214 10.094 12.576 173.247 1.00 28.55 C ANISOU 1385 CD PRO A 214 4737 4119 1991 -169 128 -29 C ATOM 1386 N LEU A 215 7.577 10.788 175.177 1.00 29.47 N ANISOU 1386 N LEU A 215 4896 4226 2073 -323 109 -24 N ATOM 1387 CA LEU A 215 6.480 9.904 175.553 1.00 30.00 C ANISOU 1387 CA LEU A 215 4989 4296 2115 -416 103 -27 C ATOM 1388 C LEU A 215 6.927 8.913 176.612 1.00 31.88 C ANISOU 1388 C LEU A 215 5283 4456 2374 -413 140 -13 C ATOM 1389 O LEU A 215 6.219 8.667 177.586 1.00 36.33 O ANISOU 1389 O LEU A 215 5822 5032 2950 -450 146 12 O ATOM 1390 CB LEU A 215 5.943 9.157 174.332 1.00 31.50 C ANISOU 1390 CB LEU A 215 5225 4478 2264 -497 80 -69 C ATOM 1391 CG LEU A 215 4.618 8.415 174.507 1.00 33.16 C ANISOU 1391 CG LEU A 215 5420 4710 2468 -612 60 -73 C ATOM 1392 CD1 LEU A 215 3.485 9.405 174.713 1.00 33.56 C ANISOU 1392 CD1 LEU A 215 5344 4883 2525 -623 25 -38 C ATOM 1393 CD2 LEU A 215 4.336 7.514 173.313 1.00 34.04 C ANISOU 1393 CD2 LEU A 215 5608 4794 2533 -703 38 -128 C ATOM 1394 N LEU A 216 8.112 8.348 176.417 1.00 30.46 N ANISOU 1394 N LEU A 216 5176 4200 2197 -362 168 -23 N ATOM 1395 CA LEU A 216 8.658 7.383 177.359 1.00 30.04 C ANISOU 1395 CA LEU A 216 5182 4069 2163 -340 203 1 C ATOM 1396 C LEU A 216 8.973 8.047 178.697 1.00 29.03 C ANISOU 1396 C LEU A 216 4996 3982 2053 -288 204 49 C ATOM 1397 O LEU A 216 8.638 7.514 179.756 1.00 29.16 O ANISOU 1397 O LEU A 216 5025 3981 2075 -308 217 81 O ATOM 1398 CB LEU A 216 9.908 6.723 176.777 1.00 30.05 C ANISOU 1398 CB LEU A 216 5263 3990 2166 -276 236 -14 C ATOM 1399 CG LEU A 216 10.701 5.822 177.720 1.00 30.75 C ANISOU 1399 CG LEU A 216 5405 4001 2276 -219 273 26 C ATOM 1400 CD1 LEU A 216 9.910 4.565 178.027 1.00 31.34 C ANISOU 1400 CD1 LEU A 216 5564 3993 2351 -296 292 26 C ATOM 1401 CD2 LEU A 216 12.048 5.476 177.115 1.00 31.59 C ANISOU 1401 CD2 LEU A 216 5558 4057 2390 -125 309 19 C ATOM 1402 N ILE A 217 9.612 9.213 178.640 1.00 28.20 N ANISOU 1402 N ILE A 217 4834 3929 1951 -228 191 52 N ATOM 1403 CA ILE A 217 9.923 9.992 179.837 1.00 27.69 C ANISOU 1403 CA ILE A 217 4712 3908 1902 -187 186 83 C ATOM 1404 C ILE A 217 8.670 10.258 180.665 1.00 28.18 C ANISOU 1404 C ILE A 217 4735 4014 1956 -236 183 96 C ATOM 1405 O ILE A 217 8.677 10.112 181.886 1.00 29.61 O ANISOU 1405 O ILE A 217 4917 4200 2132 -229 194 126 O ATOM 1406 CB ILE A 217 10.581 11.347 179.482 1.00 24.76 C ANISOU 1406 CB ILE A 217 4267 3584 1556 -138 169 74 C ATOM 1407 CG1 ILE A 217 12.003 11.140 178.955 1.00 24.28 C ANISOU 1407 CG1 ILE A 217 4233 3497 1498 -85 180 74 C ATOM 1408 CG2 ILE A 217 10.611 12.266 180.694 1.00 23.02 C ANISOU 1408 CG2 ILE A 217 3991 3408 1346 -120 160 91 C ATOM 1409 CD1 ILE A 217 13.003 10.765 180.021 1.00 23.22 C ANISOU 1409 CD1 ILE A 217 4114 3353 1353 -39 187 111 C ATOM 1410 N MET A 218 7.589 10.631 179.990 1.00 28.83 N ANISOU 1410 N MET A 218 4785 4138 2030 -283 170 78 N ATOM 1411 CA MET A 218 6.350 10.974 180.673 1.00 30.47 C ANISOU 1411 CA MET A 218 4938 4404 2234 -321 174 93 C ATOM 1412 C MET A 218 5.698 9.753 181.315 1.00 34.86 C ANISOU 1412 C MET A 218 5525 4932 2787 -388 195 112 C ATOM 1413 O MET A 218 5.097 9.852 182.385 1.00 39.96 O ANISOU 1413 O MET A 218 6142 5613 3428 -401 216 139 O ATOM 1414 CB MET A 218 5.375 11.637 179.703 1.00 31.19 C ANISOU 1414 CB MET A 218 4968 4557 2324 -345 150 78 C ATOM 1415 CG MET A 218 4.597 12.788 180.312 1.00 32.00 C ANISOU 1415 CG MET A 218 4994 4734 2433 -317 159 95 C ATOM 1416 SD MET A 218 3.334 13.427 179.200 1.00111.59 S ANISOU 1416 SD MET A 218 14989 14898 12512 -336 128 97 S ATOM 1417 CE MET A 218 2.392 11.939 178.870 1.00 57.76 C ANISOU 1417 CE MET A 218 8172 8089 5685 -457 113 94 C ATOM 1418 N VAL A 219 5.816 8.604 180.659 1.00 33.51 N ANISOU 1418 N VAL A 219 5423 4694 2617 -433 195 99 N ATOM 1419 CA VAL A 219 5.265 7.364 181.197 1.00 32.33 C ANISOU 1419 CA VAL A 219 5322 4494 2467 -507 219 118 C ATOM 1420 C VAL A 219 5.997 6.958 182.474 1.00 32.47 C ANISOU 1420 C VAL A 219 5385 4468 2482 -458 248 163 C ATOM 1421 O VAL A 219 5.369 6.568 183.462 1.00 31.70 O ANISOU 1421 O VAL A 219 5287 4380 2378 -499 273 200 O ATOM 1422 CB VAL A 219 5.339 6.224 180.165 1.00 31.90 C ANISOU 1422 CB VAL A 219 5356 4355 2412 -565 218 85 C ATOM 1423 CG1 VAL A 219 5.074 4.880 180.825 1.00 32.35 C ANISOU 1423 CG1 VAL A 219 5494 4326 2473 -629 253 111 C ATOM 1424 CG2 VAL A 219 4.349 6.473 179.039 1.00 31.87 C ANISOU 1424 CG2 VAL A 219 5303 4410 2394 -644 182 46 C ATOM 1425 N ILE A 220 7.323 7.059 182.447 1.00 33.37 N ANISOU 1425 N ILE A 220 5533 4547 2600 -371 245 166 N ATOM 1426 CA ILE A 220 8.142 6.792 183.625 1.00 34.02 C ANISOU 1426 CA ILE A 220 5645 4608 2672 -312 259 215 C ATOM 1427 C ILE A 220 7.689 7.660 184.791 1.00 32.26 C ANISOU 1427 C ILE A 220 5361 4471 2427 -310 260 237 C ATOM 1428 O ILE A 220 7.477 7.170 185.901 1.00 34.78 O ANISOU 1428 O ILE A 220 5704 4786 2724 -323 282 282 O ATOM 1429 CB ILE A 220 9.636 7.056 183.351 1.00 21.90 C ANISOU 1429 CB ILE A 220 4117 3059 1144 -216 246 215 C ATOM 1430 CG1 ILE A 220 10.142 6.155 182.226 1.00 22.25 C ANISOU 1430 CG1 ILE A 220 4232 3016 1208 -204 261 192 C ATOM 1431 CG2 ILE A 220 10.457 6.843 184.608 1.00 22.12 C ANISOU 1431 CG2 ILE A 220 4159 3090 1156 -157 248 273 C ATOM 1432 CD1 ILE A 220 11.571 6.436 181.820 1.00 22.03 C ANISOU 1432 CD1 ILE A 220 4195 2987 1189 -108 258 192 C ATOM 1433 N CYS A 221 7.527 8.951 184.520 1.00 28.15 N ANISOU 1433 N CYS A 221 4770 4021 1906 -292 241 205 N ATOM 1434 CA CYS A 221 7.129 9.911 185.541 1.00 27.32 C ANISOU 1434 CA CYS A 221 4601 3987 1794 -274 247 211 C ATOM 1435 C CYS A 221 5.727 9.631 186.073 1.00 30.35 C ANISOU 1435 C CYS A 221 4975 4407 2152 -345 282 230 C ATOM 1436 O CYS A 221 5.509 9.658 187.282 1.00 33.21 O ANISOU 1436 O CYS A 221 5329 4796 2494 -339 306 258 O ATOM 1437 CB CYS A 221 7.212 11.333 184.989 1.00 20.76 C ANISOU 1437 CB CYS A 221 3702 3201 985 -234 226 171 C ATOM 1438 SG CYS A 221 8.895 11.854 184.586 1.00 39.33 S ANISOU 1438 SG CYS A 221 6048 5532 3362 -165 193 156 S ATOM 1439 N TYR A 222 4.782 9.362 185.177 1.00 31.78 N ANISOU 1439 N TYR A 222 5126 4593 2355 -406 280 214 N ATOM 1440 CA TYR A 222 3.417 9.053 185.593 1.00 35.45 C ANISOU 1440 CA TYR A 222 5548 5104 2817 -479 311 235 C ATOM 1441 C TYR A 222 3.368 7.797 186.454 1.00 34.28 C ANISOU 1441 C TYR A 222 5467 4903 2654 -529 344 281 C ATOM 1442 O TYR A 222 2.631 7.740 187.439 1.00 34.52 O ANISOU 1442 O TYR A 222 5474 4979 2664 -559 384 315 O ATOM 1443 CB TYR A 222 2.500 8.887 184.381 1.00 40.32 C ANISOU 1443 CB TYR A 222 6117 5745 3459 -548 289 211 C ATOM 1444 CG TYR A 222 1.794 10.159 183.975 1.00 43.15 C ANISOU 1444 CG TYR A 222 6372 6197 3824 -516 278 196 C ATOM 1445 CD1 TYR A 222 0.831 10.732 184.796 1.00 44.78 C ANISOU 1445 CD1 TYR A 222 6502 6486 4025 -511 316 218 C ATOM 1446 CD2 TYR A 222 2.083 10.782 182.768 1.00 44.19 C ANISOU 1446 CD2 TYR A 222 6488 6335 3968 -484 236 164 C ATOM 1447 CE1 TYR A 222 0.181 11.896 184.429 1.00 46.94 C ANISOU 1447 CE1 TYR A 222 6685 6840 4311 -464 313 211 C ATOM 1448 CE2 TYR A 222 1.437 11.946 182.391 1.00 45.65 C ANISOU 1448 CE2 TYR A 222 6584 6599 4160 -444 227 161 C ATOM 1449 CZ TYR A 222 0.488 12.499 183.225 1.00 48.32 C ANISOU 1449 CZ TYR A 222 6849 7013 4500 -430 266 185 C ATOM 1450 OH TYR A 222 -0.155 13.657 182.851 1.00 50.82 O ANISOU 1450 OH TYR A 222 7080 7400 4827 -373 264 189 O ATOM 1451 N SER A 223 4.156 6.794 186.078 1.00 33.50 N ANISOU 1451 N SER A 223 5457 4705 2565 -532 334 286 N ATOM 1452 CA SER A 223 4.226 5.555 186.842 1.00 33.45 C ANISOU 1452 CA SER A 223 5534 4627 2547 -567 367 339 C ATOM 1453 C SER A 223 4.794 5.815 188.233 1.00 34.13 C ANISOU 1453 C SER A 223 5636 4740 2592 -502 383 386 C ATOM 1454 O SER A 223 4.188 5.438 189.236 1.00 35.47 O ANISOU 1454 O SER A 223 5815 4927 2733 -542 422 433 O ATOM 1455 CB SER A 223 5.073 4.512 186.109 1.00 33.27 C ANISOU 1455 CB SER A 223 5612 4482 2546 -557 359 333 C ATOM 1456 N GLY A 224 5.950 6.472 188.282 1.00 32.30 N ANISOU 1456 N GLY A 224 5405 4518 2351 -409 351 374 N ATOM 1457 CA GLY A 224 6.617 6.782 189.536 1.00 23.74 C ANISOU 1457 CA GLY A 224 4315 3468 1235 -344 346 408 C ATOM 1458 C GLY A 224 5.791 7.633 190.484 1.00 34.84 C ANISOU 1458 C GLY A 224 5650 4965 2622 -351 368 403 C ATOM 1459 O GLY A 224 5.935 7.534 191.703 1.00 34.43 O ANISOU 1459 O GLY A 224 5604 4938 2537 -329 380 441 O ATOM 1460 N ILE A 225 4.928 8.474 189.924 1.00 35.36 N ANISOU 1460 N ILE A 225 5652 5083 2700 -375 377 358 N ATOM 1461 CA ILE A 225 4.025 9.296 190.722 1.00 35.03 C ANISOU 1461 CA ILE A 225 5550 5124 2636 -374 414 351 C ATOM 1462 C ILE A 225 2.890 8.449 191.297 1.00 36.69 C ANISOU 1462 C ILE A 225 5771 5351 2819 -458 474 401 C ATOM 1463 O ILE A 225 2.572 8.541 192.482 1.00 37.04 O ANISOU 1463 O ILE A 225 5807 5437 2831 -447 513 428 O ATOM 1464 CB ILE A 225 3.431 10.459 189.892 1.00 33.01 C ANISOU 1464 CB ILE A 225 5225 4919 2398 -364 412 299 C ATOM 1465 CG1 ILE A 225 4.485 11.541 189.654 1.00 30.69 C ANISOU 1465 CG1 ILE A 225 4919 4617 2126 -281 368 254 C ATOM 1466 CG2 ILE A 225 2.230 11.068 190.597 1.00 33.04 C ANISOU 1466 CG2 ILE A 225 5174 5006 2372 -375 473 303 C ATOM 1467 CD1 ILE A 225 4.002 12.679 188.779 1.00 29.53 C ANISOU 1467 CD1 ILE A 225 4721 4503 1995 -263 366 212 C ATOM 1468 N SER A 226 2.289 7.617 190.452 1.00 39.37 N ANISOU 1468 N SER A 226 6122 5660 3179 -547 481 410 N ATOM 1469 CA SER A 226 1.141 6.814 190.860 1.00 45.08 C ANISOU 1469 CA SER A 226 6830 6398 3899 -644 534 454 C ATOM 1470 C SER A 226 1.533 5.675 191.796 1.00 48.27 C ANISOU 1470 C SER A 226 7337 6736 4268 -667 562 523 C ATOM 1471 O SER A 226 0.689 5.130 192.509 1.00 47.76 O ANISOU 1471 O SER A 226 7270 6693 4182 -738 619 573 O ATOM 1472 CB SER A 226 0.419 6.256 189.629 1.00 48.04 C ANISOU 1472 CB SER A 226 7170 6752 4330 -734 516 434 C ATOM 1473 OG SER A 226 -0.713 5.492 190.007 1.00 51.75 O ANISOU 1473 OG SER A 226 7617 7245 4802 -846 565 476 O ATOM 1474 N ARG A 227 2.816 5.327 191.786 1.00 50.32 N ANISOU 1474 N ARG A 227 7678 6917 4523 -602 523 533 N ATOM 1475 CA ARG A 227 3.328 4.235 192.611 1.00 52.44 C ANISOU 1475 CA ARG A 227 8038 7113 4774 -596 539 605 C ATOM 1476 C ARG A 227 3.784 4.742 193.983 1.00 50.58 C ANISOU 1476 C ARG A 227 7775 6940 4503 -511 536 631 C ATOM 1477 O ARG A 227 3.731 4.006 194.977 1.00 50.98 O ANISOU 1477 O ARG A 227 7872 6975 4523 -521 567 701 O ATOM 1478 CB ARG A 227 4.472 3.515 191.891 1.00 56.11 C ANISOU 1478 CB ARG A 227 8596 7464 5257 -556 503 611 C ATOM 1479 CG ARG A 227 5.343 2.623 192.762 1.00 61.34 C ANISOU 1479 CG ARG A 227 9345 8061 5902 -499 505 690 C ATOM 1480 CD ARG A 227 5.970 1.480 191.967 1.00 65.88 C ANISOU 1480 CD ARG A 227 10032 8491 6508 -494 505 710 C ATOM 1481 NE ARG A 227 6.009 1.747 190.533 1.00 69.40 N ANISOU 1481 NE ARG A 227 10445 8912 7013 -503 477 625 N ATOM 1482 CZ ARG A 227 5.660 0.869 189.596 1.00 73.21 C ANISOU 1482 CZ ARG A 227 10986 9291 7542 -572 493 602 C ATOM 1483 NH1 ARG A 227 5.243 -0.345 189.941 1.00 75.81 N1+ ANISOU 1483 NH1 ARG A 227 11411 9519 7874 -641 540 657 N1+ ATOM 1484 NH2 ARG A 227 5.727 1.204 188.313 1.00 72.82 N ANISOU 1484 NH2 ARG A 227 10906 9234 7528 -577 463 523 N ATOM 1485 N ALA A 228 4.200 6.005 194.043 1.00 49.66 N ANISOU 1485 N ALA A 228 7589 6894 4386 -436 501 575 N ATOM 1486 CA ALA A 228 4.629 6.614 195.298 1.00 48.98 C ANISOU 1486 CA ALA A 228 7480 6875 4256 -368 493 583 C ATOM 1487 C ALA A 228 3.475 6.702 196.296 1.00 49.30 C ANISOU 1487 C ALA A 228 7497 6980 4256 -405 563 607 C ATOM 1488 O ALA A 228 3.539 6.117 197.376 1.00 49.46 O ANISOU 1488 O ALA A 228 7554 7007 4231 -403 585 669 O ATOM 1489 CB ALA A 228 5.219 7.991 195.038 1.00 47.17 C ANISOU 1489 CB ALA A 228 7191 6694 4037 -302 447 508 C ATOM 1490 N SER A 229 2.435 7.451 195.939 1.00 49.74 N ANISOU 1490 N SER A 229 7488 7089 4324 -432 602 562 N ATOM 1491 CA SER A 229 1.242 7.560 196.773 1.00 51.12 C ANISOU 1491 CA SER A 229 7629 7333 4463 -466 682 585 C ATOM 1492 C SER A 229 0.039 8.040 195.967 1.00 53.53 C ANISOU 1492 C SER A 229 7857 7688 4795 -520 724 552 C ATOM 1493 O SER A 229 0.187 8.777 194.991 1.00 54.32 O ANISOU 1493 O SER A 229 7921 7792 4927 -496 687 495 O ATOM 1494 CB SER A 229 1.486 8.509 197.946 1.00 51.62 C ANISOU 1494 CB SER A 229 7682 7462 4471 -385 692 562 C ATOM 1495 OG SER A 229 2.448 7.979 198.839 1.00 54.18 O ANISOU 1495 OG SER A 229 8062 7769 4754 -352 657 607 O ATOM 1496 N LYS A 230 -1.153 7.619 196.379 1.00 55.21 N ANISOU 1496 N LYS A 230 8034 7950 4992 -595 802 595 N ATOM 1497 CA LYS A 230 -2.383 8.056 195.727 1.00 55.82 C ANISOU 1497 CA LYS A 230 8009 8111 5089 -650 847 578 C ATOM 1498 C LYS A 230 -2.806 9.426 196.252 1.00 55.98 C ANISOU 1498 C LYS A 230 7969 8219 5084 -560 893 535 C ATOM 1499 O LYS A 230 -3.526 10.166 195.581 1.00 55.47 O ANISOU 1499 O LYS A 230 7812 8227 5037 -558 913 505 O ATOM 1500 CB LYS A 230 -3.502 7.032 195.943 1.00 56.80 C ANISOU 1500 CB LYS A 230 8101 8266 5213 -779 914 645 C ATOM 1501 N SER A 231 -2.345 9.756 197.455 1.00 56.42 N ANISOU 1501 N SER A 231 8077 8270 5091 -483 911 533 N ATOM 1502 CA SER A 231 -2.644 11.041 198.076 1.00 55.86 C ANISOU 1502 CA SER A 231 7982 8258 4984 -394 962 485 C ATOM 1503 C SER A 231 -1.476 12.007 197.920 1.00 53.76 C ANISOU 1503 C SER A 231 7762 7947 4716 -303 888 417 C ATOM 1504 O SER A 231 -1.539 13.149 198.377 1.00 55.11 O ANISOU 1504 O SER A 231 7935 8148 4856 -228 920 366 O ATOM 1505 CB SER A 231 -2.973 10.853 199.556 1.00 57.24 C ANISOU 1505 CB SER A 231 8187 8468 5092 -377 1036 522 C ATOM 1506 OG SER A 231 -1.905 10.210 200.229 1.00 57.77 O ANISOU 1506 OG SER A 231 8339 8483 5129 -365 977 552 O ATOM 1507 N ARG A 232 -0.418 11.530 197.267 1.00 51.41 N ANISOU 1507 N ARG A 232 7501 7579 4454 -314 795 416 N ATOM 1508 CA ARG A 232 0.811 12.294 197.029 1.00 50.40 C ANISOU 1508 CA ARG A 232 7402 7413 4336 -247 716 360 C ATOM 1509 C ARG A 232 1.465 12.780 198.328 1.00 47.14 C ANISOU 1509 C ARG A 232 7027 7024 3861 -193 708 343 C ATOM 1510 O ARG A 232 2.222 13.753 198.322 1.00 45.11 O ANISOU 1510 O ARG A 232 6776 6763 3600 -148 663 282 O ATOM 1511 CB ARG A 232 0.544 13.497 196.110 1.00 54.06 C ANISOU 1511 CB ARG A 232 7824 7887 4830 -211 718 297 C ATOM 1512 CG ARG A 232 -0.525 13.292 195.036 1.00 56.82 C ANISOU 1512 CG ARG A 232 8105 8267 5216 -266 750 312 C ATOM 1513 CD ARG A 232 -0.176 12.200 194.039 1.00 57.93 C ANISOU 1513 CD ARG A 232 8253 8357 5400 -338 688 341 C ATOM 1514 NE ARG A 232 -1.160 12.141 192.960 1.00 59.94 N ANISOU 1514 NE ARG A 232 8426 8665 5683 -397 702 347 N ATOM 1515 CZ ARG A 232 -1.289 11.124 192.114 1.00 62.58 C ANISOU 1515 CZ ARG A 232 8748 8964 6065 -474 663 372 C ATOM 1516 NH1 ARG A 232 -0.499 10.065 192.221 1.00 62.97 N1+ ANISOU 1516 NH1 ARG A 232 8889 8935 6104 -515 632 398 N1+ ATOM 1517 NH2 ARG A 232 -2.213 11.163 191.164 1.00 64.92 N ANISOU 1517 NH2 ARG A 232 8945 9304 6418 -508 656 370 N ATOM 1518 N ILE A 233 1.181 12.100 199.435 1.00 44.37 N ANISOU 1518 N ILE A 233 6702 6702 3457 -209 749 396 N ATOM 1519 CA ILE A 233 1.710 12.508 200.733 1.00 41.25 C ANISOU 1519 CA ILE A 233 6340 6346 2985 -168 742 383 C ATOM 1520 C ILE A 233 2.931 11.682 201.130 1.00 41.85 C ANISOU 1520 C ILE A 233 6461 6397 3043 -174 663 428 C ATOM 1521 O ILE A 233 2.899 10.452 201.107 1.00 42.59 O ANISOU 1521 O ILE A 233 6574 6461 3146 -212 664 504 O ATOM 1522 CB ILE A 233 0.642 12.394 201.841 1.00 39.63 C ANISOU 1522 CB ILE A 233 6137 6206 2714 -170 843 415 C ATOM 1523 CG1 ILE A 233 -0.550 13.301 201.531 1.00 38.49 C ANISOU 1523 CG1 ILE A 233 5943 6100 2580 -148 933 373 C ATOM 1524 CG2 ILE A 233 1.232 12.752 203.197 1.00 40.10 C ANISOU 1524 CG2 ILE A 233 6239 6314 2682 -136 829 401 C ATOM 1525 CD1 ILE A 233 -1.574 13.366 202.644 1.00 38.73 C ANISOU 1525 CD1 ILE A 233 5969 6203 2544 -135 1046 397 C ATOM 1526 N ASN A1002 4.006 12.375 201.493 1.00 33.75 N ANISOU 1526 N ASN A1002 5142 5008 2676 26 78 229 N ATOM 1527 CA ASN A1002 5.235 11.732 201.934 1.00 35.14 C ANISOU 1527 CA ASN A1002 5320 5198 2832 29 45 207 C ATOM 1528 C ASN A1002 5.452 11.996 203.421 1.00 33.06 C ANISOU 1528 C ASN A1002 5054 4969 2537 23 -3 180 C ATOM 1529 O ASN A1002 4.689 12.743 204.034 1.00 31.13 O ANISOU 1529 O ASN A1002 4808 4730 2289 19 -1 179 O ATOM 1530 CB ASN A1002 6.420 12.238 201.106 1.00 41.23 C ANISOU 1530 CB ASN A1002 6085 5974 3607 26 85 191 C ATOM 1531 CG ASN A1002 7.657 11.372 201.254 1.00 48.21 C ANISOU 1531 CG ASN A1002 6974 6873 4469 30 57 177 C ATOM 1532 OD1 ASN A1002 8.675 11.813 201.789 1.00 51.16 O ANISOU 1532 OD1 ASN A1002 7334 7291 4815 13 41 141 O ATOM 1533 ND2 ASN A1002 7.574 10.134 200.781 1.00 53.17 N ANISOU 1533 ND2 ASN A1002 7627 7470 5106 51 50 201 N ATOM 1534 N ILE A1003 6.481 11.385 204.002 1.00 32.69 N ANISOU 1534 N ILE A1003 5012 4945 2464 24 -47 160 N ATOM 1535 CA ILE A1003 6.806 11.602 205.408 1.00 31.15 C ANISOU 1535 CA ILE A1003 4819 4786 2231 17 -103 129 C ATOM 1536 C ILE A1003 7.170 13.068 205.650 1.00 29.32 C ANISOU 1536 C ILE A1003 4565 4587 1987 -5 -87 85 C ATOM 1537 O ILE A1003 7.022 13.583 206.758 1.00 28.02 O ANISOU 1537 O ILE A1003 4405 4443 1798 -10 -120 57 O ATOM 1538 CB ILE A1003 7.967 10.683 205.873 1.00 20.90 C ANISOU 1538 CB ILE A1003 3534 3505 902 24 -159 115 C ATOM 1539 CG1 ILE A1003 8.122 10.726 207.396 1.00 21.48 C ANISOU 1539 CG1 ILE A1003 3620 3606 934 24 -228 89 C ATOM 1540 CG2 ILE A1003 9.273 11.058 205.186 1.00 20.91 C ANISOU 1540 CG2 ILE A1003 3519 3530 895 1 -146 87 C ATOM 1541 CD1 ILE A1003 9.264 9.886 207.916 1.00 22.04 C ANISOU 1541 CD1 ILE A1003 3709 3694 973 41 -294 78 C ATOM 1542 N PHE A1004 7.631 13.739 204.597 1.00 28.33 N ANISOU 1542 N PHE A1004 4422 4460 1883 -13 -31 76 N ATOM 1543 CA PHE A1004 7.982 15.151 204.673 1.00 26.31 C ANISOU 1543 CA PHE A1004 4151 4227 1619 -21 3 30 C ATOM 1544 C PHE A1004 6.768 15.991 205.049 1.00 24.86 C ANISOU 1544 C PHE A1004 3980 4027 1439 -11 26 45 C ATOM 1545 O PHE A1004 6.836 16.818 205.955 1.00 24.40 O ANISOU 1545 O PHE A1004 3925 3992 1354 -13 11 0 O ATOM 1546 CB PHE A1004 8.567 15.630 203.343 1.00 26.04 C ANISOU 1546 CB PHE A1004 4158 4168 1569 -3 84 31 C ATOM 1547 CG PHE A1004 8.825 17.110 203.292 1.00 26.40 C ANISOU 1547 CG PHE A1004 4263 4185 1583 14 149 -13 C ATOM 1548 CD1 PHE A1004 9.954 17.651 203.884 1.00 26.80 C ANISOU 1548 CD1 PHE A1004 4398 4233 1553 22 135 -100 C ATOM 1549 CD2 PHE A1004 7.941 17.960 202.647 1.00 25.35 C ANISOU 1549 CD2 PHE A1004 4112 4017 1501 13 222 24 C ATOM 1550 CE1 PHE A1004 10.194 19.009 203.839 1.00 27.75 C ANISOU 1550 CE1 PHE A1004 4599 4294 1649 6 214 -155 C ATOM 1551 CE2 PHE A1004 8.174 19.318 202.599 1.00 26.06 C ANISOU 1551 CE2 PHE A1004 4277 4052 1571 17 301 -12 C ATOM 1552 CZ PHE A1004 9.303 19.844 203.195 1.00 27.81 C ANISOU 1552 CZ PHE A1004 4597 4250 1718 5 310 -103 C ATOM 1553 N GLU A1005 5.659 15.770 204.351 1.00 26.82 N ANISOU 1553 N GLU A1005 4243 4232 1714 0 60 102 N ATOM 1554 CA GLU A1005 4.427 16.497 204.631 1.00 29.81 C ANISOU 1554 CA GLU A1005 4641 4583 2103 8 84 124 C ATOM 1555 C GLU A1005 3.907 16.197 206.032 1.00 28.10 C ANISOU 1555 C GLU A1005 4439 4379 1858 11 28 117 C ATOM 1556 O GLU A1005 3.381 17.080 206.709 1.00 27.58 O ANISOU 1556 O GLU A1005 4393 4308 1776 15 39 107 O ATOM 1557 CB GLU A1005 3.349 16.162 203.595 1.00 32.72 C ANISOU 1557 CB GLU A1005 5012 4909 2509 15 117 178 C ATOM 1558 CG GLU A1005 3.469 16.929 202.284 1.00 36.00 C ANISOU 1558 CG GLU A1005 5430 5297 2951 17 187 191 C ATOM 1559 CD GLU A1005 4.587 16.417 201.400 1.00 40.82 C ANISOU 1559 CD GLU A1005 6029 5908 3571 15 200 183 C ATOM 1560 OE1 GLU A1005 5.123 15.326 201.688 1.00 44.17 O ANISOU 1560 OE1 GLU A1005 6446 6353 3984 12 152 175 O ATOM 1561 OE2 GLU A1005 4.927 17.105 200.414 1.00 43.81 O1+ ANISOU 1561 OE2 GLU A1005 6413 6263 3968 19 265 186 O1+ ATOM 1562 N MET A1006 4.057 14.949 206.464 1.00 27.05 N ANISOU 1562 N MET A1006 4307 4254 1718 13 -24 125 N ATOM 1563 CA MET A1006 3.553 14.529 207.766 1.00 27.97 C ANISOU 1563 CA MET A1006 4445 4374 1809 22 -70 125 C ATOM 1564 C MET A1006 4.245 15.263 208.906 1.00 29.97 C ANISOU 1564 C MET A1006 4708 4664 2014 15 -106 70 C ATOM 1565 O MET A1006 3.592 15.850 209.769 1.00 31.95 O ANISOU 1565 O MET A1006 4985 4907 2245 23 -107 64 O ATOM 1566 CB MET A1006 3.723 13.020 207.951 1.00 27.71 C ANISOU 1566 CB MET A1006 4418 4335 1774 31 -112 144 C ATOM 1567 CG MET A1006 3.255 12.529 209.308 1.00 28.66 C ANISOU 1567 CG MET A1006 4570 4454 1865 47 -154 146 C ATOM 1568 SD MET A1006 3.454 10.759 209.569 1.00 26.39 S ANISOU 1568 SD MET A1006 4304 4151 1571 69 -192 169 S ATOM 1569 CE MET A1006 5.239 10.659 209.652 1.00 63.21 C ANISOU 1569 CE MET A1006 8959 8850 6209 65 -242 128 C ATOM 1570 N LEU A1007 5.573 15.228 208.905 1.00 29.66 N ANISOU 1570 N LEU A1007 4649 4666 1955 -2 -138 23 N ATOM 1571 CA LEU A1007 6.344 15.832 209.981 1.00 28.75 C ANISOU 1571 CA LEU A1007 4534 4592 1796 -16 -187 -46 C ATOM 1572 C LEU A1007 6.426 17.348 209.834 1.00 29.92 C ANISOU 1572 C LEU A1007 4678 4752 1940 -19 -141 -97 C ATOM 1573 O LEU A1007 6.834 18.043 210.761 1.00 32.32 O ANISOU 1573 O LEU A1007 4996 5085 2201 -26 -175 -167 O ATOM 1574 CB LEU A1007 7.744 15.217 210.038 1.00 29.85 C ANISOU 1574 CB LEU A1007 4652 4765 1925 -42 -245 -84 C ATOM 1575 CG LEU A1007 7.764 13.805 210.632 1.00 30.02 C ANISOU 1575 CG LEU A1007 4704 4777 1925 -25 -306 -46 C ATOM 1576 CD1 LEU A1007 9.132 13.160 210.500 1.00 30.35 C ANISOU 1576 CD1 LEU A1007 4740 4837 1956 -43 -362 -66 C ATOM 1577 CD2 LEU A1007 7.335 13.847 212.089 1.00 31.24 C ANISOU 1577 CD2 LEU A1007 4895 4944 2029 -10 -357 -58 C ATOM 1578 N ARG A1008 6.030 17.861 208.675 1.00 28.50 N ANISOU 1578 N ARG A1008 4494 4540 1794 -9 -63 -64 N ATOM 1579 CA ARG A1008 5.912 19.304 208.501 1.00 27.70 C ANISOU 1579 CA ARG A1008 4413 4430 1684 -2 -2 -97 C ATOM 1580 C ARG A1008 4.665 19.817 209.220 1.00 27.64 C ANISOU 1580 C ARG A1008 4456 4380 1667 8 14 -67 C ATOM 1581 O ARG A1008 4.655 20.922 209.761 1.00 28.92 O ANISOU 1581 O ARG A1008 4653 4533 1801 9 34 -113 O ATOM 1582 CB ARG A1008 5.863 19.676 207.017 1.00 25.84 C ANISOU 1582 CB ARG A1008 4180 4152 1486 4 85 -59 C ATOM 1583 CG ARG A1008 5.773 21.172 206.762 1.00 26.78 C ANISOU 1583 CG ARG A1008 4385 4197 1595 10 169 -83 C ATOM 1584 CD ARG A1008 5.813 21.483 205.279 1.00 26.13 C ANISOU 1584 CD ARG A1008 4304 4065 1559 11 262 -40 C ATOM 1585 NE ARG A1008 4.674 20.917 204.565 1.00 22.96 N ANISOU 1585 NE ARG A1008 3837 3669 1218 13 265 47 N ATOM 1586 CZ ARG A1008 4.508 21.005 203.250 1.00 24.16 C ANISOU 1586 CZ ARG A1008 3987 3781 1413 17 327 90 C ATOM 1587 NH1 ARG A1008 5.410 21.632 202.509 1.00 24.43 N1+ ANISOU 1587 NH1 ARG A1008 4034 3793 1455 15 398 67 N1+ ATOM 1588 NH2 ARG A1008 3.444 20.464 202.673 1.00 26.58 N ANISOU 1588 NH2 ARG A1008 4291 4061 1746 26 321 149 N ATOM 1589 N ILE A1009 3.615 19.006 209.227 1.00 27.03 N ANISOU 1589 N ILE A1009 4385 4271 1615 18 7 4 N ATOM 1590 CA ILE A1009 2.388 19.356 209.930 1.00 28.85 C ANISOU 1590 CA ILE A1009 4657 4466 1839 32 20 35 C ATOM 1591 C ILE A1009 2.561 19.181 211.434 1.00 30.31 C ANISOU 1591 C ILE A1009 4870 4675 1972 36 -43 -4 C ATOM 1592 O ILE A1009 2.227 20.073 212.215 1.00 31.99 O ANISOU 1592 O ILE A1009 5129 4874 2152 42 -32 -28 O ATOM 1593 CB ILE A1009 1.197 18.498 209.457 1.00 31.20 C ANISOU 1593 CB ILE A1009 4944 4736 2174 43 32 109 C ATOM 1594 CG1 ILE A1009 0.963 18.684 207.956 1.00 32.41 C ANISOU 1594 CG1 ILE A1009 5073 4869 2374 39 88 144 C ATOM 1595 CG2 ILE A1009 -0.057 18.849 210.235 1.00 32.14 C ANISOU 1595 CG2 ILE A1009 5100 4830 2281 60 46 136 C ATOM 1596 CD1 ILE A1009 0.749 20.122 207.542 1.00 32.14 C ANISOU 1596 CD1 ILE A1009 5064 4804 2344 44 157 141 C ATOM 1597 N ASP A1010 3.099 18.030 211.828 1.00 30.01 N ANISOU 1597 N ASP A1010 4813 4668 1922 32 -108 -8 N ATOM 1598 CA ASP A1010 3.218 17.664 213.237 1.00 31.87 C ANISOU 1598 CA ASP A1010 5081 4921 2109 39 -173 -34 C ATOM 1599 C ASP A1010 4.324 18.414 213.982 1.00 34.55 C ANISOU 1599 C ASP A1010 5423 5313 2391 18 -219 -128 C ATOM 1600 O ASP A1010 4.117 18.884 215.102 1.00 37.44 O ANISOU 1600 O ASP A1010 5835 5679 2711 25 -243 -160 O ATOM 1601 CB ASP A1010 3.456 16.158 213.369 1.00 30.92 C ANISOU 1601 CB ASP A1010 4948 4806 1995 47 -222 -4 C ATOM 1602 CG ASP A1010 2.231 15.340 213.017 1.00 30.12 C ANISOU 1602 CG ASP A1010 4853 4659 1932 68 -189 69 C ATOM 1603 OD1 ASP A1010 1.115 15.904 213.025 1.00 30.14 O ANISOU 1603 OD1 ASP A1010 4873 4632 1945 77 -143 97 O ATOM 1604 OD2 ASP A1010 2.381 14.130 212.747 1.00 29.70 O1+ ANISOU 1604 OD2 ASP A1010 4789 4601 1895 74 -208 95 O1+ ATOM 1605 N GLU A1011 5.497 18.515 213.367 1.00 34.08 N ANISOU 1605 N GLU A1011 5314 5304 2331 -11 -234 -181 N ATOM 1606 CA GLU A1011 6.649 19.113 214.033 1.00 36.17 C ANISOU 1606 CA GLU A1011 5571 5620 2552 -37 -292 -291 C ATOM 1607 C GLU A1011 6.818 20.584 213.664 1.00 35.47 C ANISOU 1607 C GLU A1011 5559 5489 2428 -24 -247 -366 C ATOM 1608 O GLU A1011 7.425 21.351 214.409 1.00 36.39 O ANISOU 1608 O GLU A1011 5744 5598 2484 -37 -297 -475 O ATOM 1609 CB GLU A1011 7.922 18.338 213.688 1.00 40.59 C ANISOU 1609 CB GLU A1011 6123 6200 3099 -55 -359 -321 C ATOM 1610 CG GLU A1011 9.072 18.561 214.656 1.00 45.74 C ANISOU 1610 CG GLU A1011 6819 6887 3672 -81 -473 -432 C ATOM 1611 CD GLU A1011 8.873 17.842 215.977 1.00 48.84 C ANISOU 1611 CD GLU A1011 7212 7303 4040 -88 -538 -403 C ATOM 1612 OE1 GLU A1011 8.232 16.768 215.984 1.00 46.71 O ANISOU 1612 OE1 GLU A1011 6912 7021 3814 -74 -514 -301 O ATOM 1613 OE2 GLU A1011 9.354 18.354 217.010 1.00 52.39 O1+ ANISOU 1613 OE2 GLU A1011 7701 7779 4424 -105 -615 -489 O1+ ATOM 1614 N GLY A1012 6.280 20.975 212.513 1.00 34.20 N ANISOU 1614 N GLY A1012 5397 5278 2319 -10 -152 -309 N ATOM 1615 CA GLY A1012 6.389 22.347 212.049 1.00 33.52 C ANISOU 1615 CA GLY A1012 5411 5106 2219 -13 -79 -356 C ATOM 1616 C GLY A1012 7.601 22.576 211.165 1.00 33.47 C ANISOU 1616 C GLY A1012 5459 5059 2197 -40 -67 -424 C ATOM 1617 O GLY A1012 8.402 21.669 210.944 1.00 34.99 O ANISOU 1617 O GLY A1012 5608 5304 2383 -38 -131 -439 O ATOM 1618 N LEU A1013 7.737 23.797 210.659 1.00 32.82 N ANISOU 1618 N LEU A1013 5482 4878 2111 -82 30 -465 N ATOM 1619 CA LEU A1013 8.854 24.146 209.787 1.00 33.54 C ANISOU 1619 CA LEU A1013 5637 4911 2196 -155 82 -538 C ATOM 1620 C LEU A1013 9.476 25.479 210.203 1.00 35.27 C ANISOU 1620 C LEU A1013 5973 5044 2383 -274 127 -686 C ATOM 1621 O LEU A1013 8.831 26.525 210.127 1.00 37.49 O ANISOU 1621 O LEU A1013 6324 5241 2679 -285 243 -669 O ATOM 1622 CB LEU A1013 8.392 24.205 208.329 1.00 33.44 C ANISOU 1622 CB LEU A1013 5604 4854 2248 -131 222 -428 C ATOM 1623 CG LEU A1013 9.445 24.456 207.248 1.00 33.17 C ANISOU 1623 CG LEU A1013 5617 4764 2223 -207 324 -478 C ATOM 1624 CD1 LEU A1013 10.421 23.297 207.164 1.00 32.35 C ANISOU 1624 CD1 LEU A1013 5463 4736 2091 -214 222 -510 C ATOM 1625 CD2 LEU A1013 8.776 24.697 205.902 1.00 31.81 C ANISOU 1625 CD2 LEU A1013 5417 4541 2128 -160 466 -356 C ATOM 1626 N ARG A1014 10.731 25.435 210.641 1.00 35.19 N ANISOU 1626 N ARG A1014 5965 5061 2344 -379 31 -840 N ATOM 1627 CA ARG A1014 11.419 26.634 211.109 1.00 37.09 C ANISOU 1627 CA ARG A1014 6229 5233 2632 -514 53 -1003 C ATOM 1628 C ARG A1014 12.396 27.165 210.068 1.00 35.14 C ANISOU 1628 C ARG A1014 5856 4911 2586 -599 169 -1041 C ATOM 1629 O ARG A1014 13.346 26.479 209.694 1.00 34.32 O ANISOU 1629 O ARG A1014 5599 4862 2578 -607 106 -1053 O ATOM 1630 CB ARG A1014 12.164 26.351 212.415 1.00 41.57 C ANISOU 1630 CB ARG A1014 6743 5884 3168 -548 -158 -1133 C ATOM 1631 CG ARG A1014 11.353 25.585 213.441 1.00 43.17 C ANISOU 1631 CG ARG A1014 6962 6165 3278 -401 -282 -1051 C ATOM 1632 CD ARG A1014 10.138 26.372 213.896 1.00 44.28 C ANISOU 1632 CD ARG A1014 7180 6241 3404 -347 -191 -989 C ATOM 1633 NE ARG A1014 9.236 25.546 214.693 1.00 45.64 N ANISOU 1633 NE ARG A1014 7281 6505 3556 -216 -256 -882 N ATOM 1634 CZ ARG A1014 8.163 26.006 215.325 1.00 48.17 C ANISOU 1634 CZ ARG A1014 7636 6805 3863 -175 -206 -827 C ATOM 1635 NH1 ARG A1014 7.855 27.295 215.260 1.00 51.28 N1+ ANISOU 1635 NH1 ARG A1014 8147 7085 4253 -224 -100 -863 N1+ ATOM 1636 NH2 ARG A1014 7.398 25.177 216.024 1.00 46.54 N ANISOU 1636 NH2 ARG A1014 7347 6684 3651 -104 -246 -737 N ATOM 1637 N LEU A1015 12.162 28.389 209.606 1.00 34.58 N ANISOU 1637 N LEU A1015 5850 4710 2578 -656 349 -1054 N ATOM 1638 CA LEU A1015 13.064 29.029 208.656 1.00 33.42 C ANISOU 1638 CA LEU A1015 5599 4472 2626 -744 484 -1093 C ATOM 1639 C LEU A1015 14.028 29.958 209.387 1.00 35.86 C ANISOU 1639 C LEU A1015 5849 4730 3047 -893 446 -1276 C ATOM 1640 O LEU A1015 15.108 30.265 208.885 1.00 37.15 O ANISOU 1640 O LEU A1015 5872 4854 3390 -987 493 -1344 O ATOM 1641 CB LEU A1015 12.278 29.797 207.594 1.00 32.11 C ANISOU 1641 CB LEU A1015 5543 4189 2471 -711 723 -990 C ATOM 1642 CG LEU A1015 11.369 28.943 206.707 1.00 31.36 C ANISOU 1642 CG LEU A1015 5492 4144 2279 -576 770 -814 C ATOM 1643 CD1 LEU A1015 10.689 29.798 205.651 1.00 31.13 C ANISOU 1643 CD1 LEU A1015 5560 4004 2263 -542 1003 -720 C ATOM 1644 CD2 LEU A1015 12.154 27.808 206.063 1.00 30.91 C ANISOU 1644 CD2 LEU A1015 5287 4165 2292 -551 700 -780 C ATOM 1645 N LYS A1016 13.627 30.403 210.574 1.00 36.56 N ANISOU 1645 N LYS A1016 6046 4817 3026 -917 365 -1357 N ATOM 1646 CA LYS A1016 14.510 31.165 211.449 1.00 39.62 C ANISOU 1646 CA LYS A1016 6385 5176 3491 -1061 287 -1547 C ATOM 1647 C LYS A1016 14.734 30.380 212.734 1.00 41.40 C ANISOU 1647 C LYS A1016 6582 5549 3601 -1036 29 -1618 C ATOM 1648 O LYS A1016 13.850 29.640 213.166 1.00 40.63 O ANISOU 1648 O LYS A1016 6582 5525 3329 -912 -46 -1527 O ATOM 1649 CB LYS A1016 13.929 32.550 211.753 1.00 39.33 C ANISOU 1649 CB LYS A1016 6522 4990 3430 -1124 432 -1603 C ATOM 1650 CG LYS A1016 14.923 33.517 212.386 1.00 40.69 C ANISOU 1650 CG LYS A1016 6644 5097 3721 -1304 400 -1807 C ATOM 1651 CD LYS A1016 14.227 34.730 212.984 1.00 41.46 C ANISOU 1651 CD LYS A1016 6952 5060 3743 -1347 506 -1869 C ATOM 1652 N ILE A1017 15.917 30.527 213.326 1.00 44.90 N ANISOU 1652 N ILE A1017 6884 6035 4140 -1150 -106 -1779 N ATOM 1653 CA ILE A1017 16.267 29.793 214.541 1.00 47.51 C ANISOU 1653 CA ILE A1017 7172 6514 4365 -1123 -362 -1855 C ATOM 1654 C ILE A1017 15.216 29.993 215.623 1.00 50.87 C ANISOU 1654 C ILE A1017 7812 6936 4581 -1065 -413 -1859 C ATOM 1655 O ILE A1017 15.049 31.090 216.155 1.00 52.30 O ANISOU 1655 O ILE A1017 8105 7020 4747 -1154 -363 -1964 O ATOM 1656 CB ILE A1017 17.646 30.208 215.089 1.00 46.86 C ANISOU 1656 CB ILE A1017 6920 6470 4415 -1275 -490 -2050 C ATOM 1657 CG1 ILE A1017 18.748 29.820 214.102 1.00 47.07 C ANISOU 1657 CG1 ILE A1017 6710 6528 4645 -1314 -461 -2036 C ATOM 1658 CG2 ILE A1017 17.901 29.553 216.435 1.00 45.47 C ANISOU 1658 CG2 ILE A1017 6729 6449 4100 -1235 -756 -2131 C ATOM 1659 CD1 ILE A1017 20.148 30.029 214.638 1.00 48.83 C ANISOU 1659 CD1 ILE A1017 6727 6825 5002 -1450 -612 -2215 C ATOM 1660 N TYR A1018 14.500 28.918 215.927 1.00 53.89 N ANISOU 1660 N TYR A1018 8257 7418 4801 -916 -501 -1742 N ATOM 1661 CA TYR A1018 13.387 28.964 216.862 1.00 58.03 C ANISOU 1661 CA TYR A1018 8942 7933 5174 -798 -526 -1680 C ATOM 1662 C TYR A1018 13.794 28.458 218.238 1.00 61.28 C ANISOU 1662 C TYR A1018 9296 8452 5536 -727 -757 -1744 C ATOM 1663 O TYR A1018 14.379 27.383 218.369 1.00 60.82 O ANISOU 1663 O TYR A1018 9125 8511 5471 -666 -906 -1727 O ATOM 1664 CB TYR A1018 12.216 28.142 216.320 1.00 59.70 C ANISOU 1664 CB TYR A1018 9184 8165 5336 -620 -444 -1457 C ATOM 1665 CG TYR A1018 11.021 28.067 217.242 1.00 62.91 C ANISOU 1665 CG TYR A1018 9637 8591 5674 -472 -446 -1356 C ATOM 1666 CD1 TYR A1018 10.155 29.144 217.378 1.00 64.68 C ANISOU 1666 CD1 TYR A1018 9983 8707 5887 -480 -309 -1334 C ATOM 1667 CD2 TYR A1018 10.751 26.913 217.965 1.00 64.17 C ANISOU 1667 CD2 TYR A1018 9701 8887 5793 -344 -559 -1282 C ATOM 1668 CE1 TYR A1018 9.060 29.077 218.217 1.00 65.15 C ANISOU 1668 CE1 TYR A1018 10064 8796 5895 -370 -301 -1243 C ATOM 1669 CE2 TYR A1018 9.658 26.837 218.805 1.00 64.85 C ANISOU 1669 CE2 TYR A1018 9799 9004 5836 -262 -528 -1194 C ATOM 1670 CZ TYR A1018 8.817 27.921 218.928 1.00 66.27 C ANISOU 1670 CZ TYR A1018 10100 9076 6006 -272 -409 -1176 C ATOM 1671 OH TYR A1018 7.728 27.849 219.765 1.00 69.33 O ANISOU 1671 OH TYR A1018 10500 9487 6355 -200 -381 -1088 O ATOM 1672 N LYS A1019 13.488 29.244 219.264 1.00 64.79 N ANISOU 1672 N LYS A1019 9823 8853 5942 -725 -778 -1814 N ATOM 1673 CA LYS A1019 13.754 28.840 220.637 1.00 68.58 C ANISOU 1673 CA LYS A1019 10257 9439 6361 -639 -973 -1878 C ATOM 1674 C LYS A1019 12.620 27.973 221.171 1.00 71.64 C ANISOU 1674 C LYS A1019 10624 9936 6659 -464 -939 -1718 C ATOM 1675 O LYS A1019 11.471 28.411 221.237 1.00 71.30 O ANISOU 1675 O LYS A1019 10678 9827 6585 -424 -800 -1622 O ATOM 1676 CB LYS A1019 13.948 30.064 221.527 1.00 68.30 C ANISOU 1676 CB LYS A1019 10301 9327 6322 -735 -996 -2035 C ATOM 1677 CG LYS A1019 13.913 29.749 223.005 1.00 67.97 C ANISOU 1677 CG LYS A1019 10227 9408 6191 -631 -1146 -2088 C ATOM 1678 CD LYS A1019 14.462 30.899 223.818 1.00 68.96 C ANISOU 1678 CD LYS A1019 10416 9457 6330 -744 -1217 -2276 C ATOM 1679 CE LYS A1019 15.933 31.121 223.529 1.00 68.45 C ANISOU 1679 CE LYS A1019 10272 9357 6378 -914 -1354 -2414 C ATOM 1680 NZ LYS A1019 16.514 32.133 224.448 1.00 69.15 N ANISOU 1680 NZ LYS A1019 10399 9391 6483 -1028 -1446 -2596 N ATOM 1681 N ASP A1020 12.954 26.742 221.551 1.00 75.62 N ANISOU 1681 N ASP A1020 10986 10609 7136 -413 -1037 -1672 N ATOM 1682 CA ASP A1020 11.964 25.774 222.013 1.00 77.97 C ANISOU 1682 CA ASP A1020 11263 10991 7370 -350 -971 -1485 C ATOM 1683 C ASP A1020 11.243 26.272 223.263 1.00 79.49 C ANISOU 1683 C ASP A1020 11539 11179 7486 -333 -956 -1495 C ATOM 1684 O ASP A1020 11.734 27.162 223.959 1.00 81.15 O ANISOU 1684 O ASP A1020 11789 11373 7672 -389 -1022 -1657 O ATOM 1685 CB ASP A1020 12.631 24.422 222.286 1.00 81.02 C ANISOU 1685 CB ASP A1020 11564 11475 7746 -392 -1065 -1397 C ATOM 1686 CG ASP A1020 11.632 23.286 222.385 1.00 82.04 C ANISOU 1686 CG ASP A1020 11693 11627 7852 -306 -999 -1197 C ATOM 1687 OD1 ASP A1020 10.546 23.394 221.779 1.00 80.92 O1+ ANISOU 1687 OD1 ASP A1020 11568 11440 7738 -238 -869 -1108 O1+ ATOM 1688 OD2 ASP A1020 11.934 22.285 223.068 1.00 84.98 O ANISOU 1688 OD2 ASP A1020 12055 12047 8188 -304 -1085 -1130 O ATOM 1689 N THR A1021 10.076 25.694 223.537 1.00 78.65 N ANISOU 1689 N THR A1021 11454 11072 7356 -257 -872 -1323 N ATOM 1690 CA THR A1021 9.254 26.095 224.676 1.00 79.67 C ANISOU 1690 CA THR A1021 11669 11178 7422 -224 -846 -1306 C ATOM 1691 C THR A1021 9.995 25.926 225.997 1.00 81.40 C ANISOU 1691 C THR A1021 11884 11485 7560 -273 -981 -1400 C ATOM 1692 O THR A1021 9.726 26.636 226.966 1.00 83.11 O ANISOU 1692 O THR A1021 12184 11679 7715 -273 -989 -1468 O ATOM 1693 CB THR A1021 7.944 25.287 224.733 1.00 78.24 C ANISOU 1693 CB THR A1021 11485 10989 7253 -141 -752 -1104 C ATOM 1694 N GLU A1022 10.932 24.984 226.025 1.00 80.71 N ANISOU 1694 N GLU A1022 11714 11483 7467 -319 -1087 -1393 N ATOM 1695 CA GLU A1022 11.723 24.725 227.221 1.00 81.48 C ANISOU 1695 CA GLU A1022 11821 11653 7486 -370 -1230 -1456 C ATOM 1696 C GLU A1022 12.936 25.648 227.299 1.00 79.65 C ANISOU 1696 C GLU A1022 11573 11426 7264 -494 -1334 -1655 C ATOM 1697 O GLU A1022 13.279 26.146 228.371 1.00 81.01 O ANISOU 1697 O GLU A1022 11789 11625 7367 -543 -1414 -1762 O ATOM 1698 CB GLU A1022 12.173 23.266 227.254 1.00 83.30 C ANISOU 1698 CB GLU A1022 12001 11931 7720 -341 -1309 -1330 C ATOM 1699 CG GLU A1022 11.170 22.306 226.645 1.00 83.86 C ANISOU 1699 CG GLU A1022 12048 11971 7844 -246 -1193 -1145 C ATOM 1700 CD GLU A1022 11.685 20.884 226.612 1.00 86.57 C ANISOU 1700 CD GLU A1022 12345 12346 8203 -207 -1267 -1042 C ATOM 1701 OE1 GLU A1022 12.554 20.550 227.445 1.00 89.07 O ANISOU 1701 OE1 GLU A1022 12664 12712 8466 -209 -1406 -1084 O ATOM 1702 OE2 GLU A1022 11.226 20.104 225.752 1.00 85.81 O1+ ANISOU 1702 OE2 GLU A1022 12209 12222 8174 -165 -1188 -923 O1+ ATOM 1703 N GLY A1023 13.580 25.872 226.159 1.00 76.08 N ANISOU 1703 N GLY A1023 11061 10937 6910 -551 -1331 -1704 N ATOM 1704 CA GLY A1023 14.739 26.744 226.098 1.00 74.57 C ANISOU 1704 CA GLY A1023 10851 10717 6767 -695 -1422 -1883 C ATOM 1705 C GLY A1023 15.764 26.270 225.088 1.00 71.04 C ANISOU 1705 C GLY A1023 10391 10201 6400 -771 -1516 -1846 C ATOM 1706 O GLY A1023 16.815 26.889 224.918 1.00 71.73 O ANISOU 1706 O GLY A1023 10536 10163 6555 -855 -1669 -1960 O ATOM 1707 N TYR A1024 15.453 25.165 224.416 1.00 66.66 N ANISOU 1707 N TYR A1024 9791 9678 5858 -671 -1479 -1694 N ATOM 1708 CA TYR A1024 16.335 24.601 223.401 1.00 63.42 C ANISOU 1708 CA TYR A1024 9334 9232 5530 -660 -1578 -1676 C ATOM 1709 C TYR A1024 16.265 25.398 222.100 1.00 60.43 C ANISOU 1709 C TYR A1024 9002 8706 5254 -672 -1495 -1731 C ATOM 1710 O TYR A1024 15.329 26.165 221.883 1.00 59.59 O ANISOU 1710 O TYR A1024 9031 8465 5147 -652 -1354 -1704 O ATOM 1711 CB TYR A1024 15.976 23.136 223.141 1.00 61.21 C ANISOU 1711 CB TYR A1024 8998 9033 5227 -542 -1551 -1500 C ATOM 1712 N TYR A1025 17.261 25.215 221.237 1.00 59.14 N ANISOU 1712 N TYR A1025 8679 8595 5199 -671 -1575 -1822 N ATOM 1713 CA TYR A1025 17.284 25.881 219.937 1.00 56.78 C ANISOU 1713 CA TYR A1025 8302 8261 5011 -722 -1434 -1904 C ATOM 1714 C TYR A1025 17.055 24.889 218.805 1.00 54.97 C ANISOU 1714 C TYR A1025 8009 8081 4794 -641 -1349 -1768 C ATOM 1715 O TYR A1025 17.758 23.885 218.700 1.00 54.06 O ANISOU 1715 O TYR A1025 7756 8078 4707 -593 -1445 -1729 O ATOM 1716 CB TYR A1025 18.610 26.610 219.726 1.00 58.32 C ANISOU 1716 CB TYR A1025 8288 8514 5357 -906 -1483 -2113 C ATOM 1717 CG TYR A1025 18.727 27.901 220.500 1.00 61.10 C ANISOU 1717 CG TYR A1025 8713 8775 5725 -1028 -1499 -2266 C ATOM 1718 CD1 TYR A1025 19.176 27.907 221.813 1.00 63.14 C ANISOU 1718 CD1 TYR A1025 8995 9065 5930 -1020 -1690 -2317 C ATOM 1719 CD2 TYR A1025 18.389 29.114 219.916 1.00 61.48 C ANISOU 1719 CD2 TYR A1025 8827 8694 5838 -1163 -1307 -2346 C ATOM 1720 CE1 TYR A1025 19.284 29.086 222.523 1.00 64.63 C ANISOU 1720 CE1 TYR A1025 9260 9169 6129 -1125 -1709 -2461 C ATOM 1721 CE2 TYR A1025 18.494 30.297 220.617 1.00 62.96 C ANISOU 1721 CE2 TYR A1025 9091 8785 6046 -1271 -1309 -2481 C ATOM 1722 CZ TYR A1025 18.942 30.277 221.920 1.00 64.60 C ANISOU 1722 CZ TYR A1025 9307 9037 6199 -1245 -1519 -2548 C ATOM 1723 OH TYR A1025 19.048 31.455 222.621 1.00 66.93 O ANISOU 1723 OH TYR A1025 9684 9236 6510 -1350 -1526 -2688 O ATOM 1724 N THR A1026 16.073 25.176 217.957 1.00 54.57 N ANISOU 1724 N THR A1026 8059 7949 4727 -619 -1160 -1690 N ATOM 1725 CA THR A1026 15.739 24.284 216.853 1.00 37.59 C ANISOU 1725 CA THR A1026 5879 5827 2576 -546 -1066 -1548 C ATOM 1726 C THR A1026 15.736 25.005 215.508 1.00 37.03 C ANISOU 1726 C THR A1026 5771 5662 2637 -645 -855 -1538 C ATOM 1727 O THR A1026 15.850 26.229 215.444 1.00 37.93 O ANISOU 1727 O THR A1026 5906 5673 2834 -765 -761 -1631 O ATOM 1728 CB THR A1026 14.360 23.623 217.059 1.00 35.80 C ANISOU 1728 CB THR A1026 5780 5549 2272 -338 -1010 -1358 C ATOM 1729 OG1 THR A1026 13.365 24.635 217.252 1.00 40.24 O ANISOU 1729 OG1 THR A1026 6412 6065 2812 -354 -871 -1367 O ATOM 1730 CG2 THR A1026 14.382 22.706 218.270 1.00 36.81 C ANISOU 1730 CG2 THR A1026 5880 5769 2337 -422 -1074 -1254 C ATOM 1731 N ILE A1027 15.607 24.226 214.438 1.00 40.47 N ANISOU 1731 N ILE A1027 6161 6101 3116 -572 -770 -1402 N ATOM 1732 CA ILE A1027 15.511 24.763 213.085 1.00 39.57 C ANISOU 1732 CA ILE A1027 6025 5873 3135 -617 -558 -1342 C ATOM 1733 C ILE A1027 14.864 23.717 212.182 1.00 38.74 C ANISOU 1733 C ILE A1027 5953 5786 2979 -497 -489 -1167 C ATOM 1734 O ILE A1027 14.878 22.526 212.497 1.00 38.75 O ANISOU 1734 O ILE A1027 5940 5888 2895 -400 -611 -1112 O ATOM 1735 CB ILE A1027 16.897 25.163 212.523 1.00 40.10 C ANISOU 1735 CB ILE A1027 5887 5927 3423 -728 -536 -1435 C ATOM 1736 CG1 ILE A1027 16.754 26.127 211.341 1.00 39.84 C ANISOU 1736 CG1 ILE A1027 5870 5745 3524 -799 -297 -1405 C ATOM 1737 CG2 ILE A1027 17.697 23.930 212.124 1.00 39.55 C ANISOU 1737 CG2 ILE A1027 5656 5964 3406 -654 -621 -1381 C ATOM 1738 CD1 ILE A1027 15.976 27.380 211.660 1.00 36.32 C ANISOU 1738 CD1 ILE A1027 5588 5180 3031 -863 -189 -1449 C ATOM 1739 N GLY A1028 14.285 24.168 211.072 1.00 38.55 N ANISOU 1739 N GLY A1028 5984 5662 3002 -502 -293 -1082 N ATOM 1740 CA GLY A1028 13.674 23.275 210.104 1.00 37.36 C ANISOU 1740 CA GLY A1028 5865 5520 2809 -403 -218 -926 C ATOM 1741 C GLY A1028 12.588 22.409 210.707 1.00 36.67 C ANISOU 1741 C GLY A1028 5909 5498 2525 -297 -297 -838 C ATOM 1742 O GLY A1028 11.765 22.882 211.490 1.00 37.37 O ANISOU 1742 O GLY A1028 6058 5563 2577 -259 -301 -829 O ATOM 1743 N ILE A1029 12.592 21.132 210.345 1.00 36.10 N ANISOU 1743 N ILE A1029 5800 5490 2425 -206 -344 -745 N ATOM 1744 CA ILE A1029 11.617 20.193 210.880 1.00 35.84 C ANISOU 1744 CA ILE A1029 5689 5522 2406 -83 -373 -624 C ATOM 1745 C ILE A1029 12.199 19.451 212.081 1.00 38.27 C ANISOU 1745 C ILE A1029 5937 5920 2685 -111 -526 -662 C ATOM 1746 O ILE A1029 12.754 18.359 211.945 1.00 40.38 O ANISOU 1746 O ILE A1029 6196 6194 2952 -113 -590 -610 O ATOM 1747 CB ILE A1029 11.160 19.187 209.806 1.00 34.25 C ANISOU 1747 CB ILE A1029 5431 5330 2254 -44 -294 -483 C ATOM 1748 CG1 ILE A1029 10.689 19.935 208.557 1.00 32.82 C ANISOU 1748 CG1 ILE A1029 5303 5054 2113 -45 -139 -435 C ATOM 1749 CG2 ILE A1029 10.054 18.292 210.342 1.00 34.34 C ANISOU 1749 CG2 ILE A1029 5363 5370 2314 -39 -294 -367 C ATOM 1750 CD1 ILE A1029 10.214 19.036 207.441 1.00 32.21 C ANISOU 1750 CD1 ILE A1029 5158 4983 2097 -10 -71 -310 C ATOM 1751 N GLY A1030 12.083 20.072 213.252 1.00 38.53 N ANISOU 1751 N GLY A1030 5982 5967 2691 -133 -583 -735 N ATOM 1752 CA GLY A1030 12.533 19.480 214.500 1.00 39.91 C ANISOU 1752 CA GLY A1030 6153 6174 2835 -177 -716 -743 C ATOM 1753 C GLY A1030 13.994 19.075 214.536 1.00 41.42 C ANISOU 1753 C GLY A1030 6341 6378 3018 -172 -881 -824 C ATOM 1754 O GLY A1030 14.311 17.905 214.754 1.00 42.76 O ANISOU 1754 O GLY A1030 6461 6585 3199 -109 -946 -753 O ATOM 1755 N HIS A1031 14.887 20.036 214.325 1.00 41.37 N ANISOU 1755 N HIS A1031 6298 6390 3031 -201 -938 -998 N ATOM 1756 CA HIS A1031 16.318 19.759 214.373 1.00 43.35 C ANISOU 1756 CA HIS A1031 6358 6779 3333 -198 -1076 -1123 C ATOM 1757 C HIS A1031 16.993 20.520 215.507 1.00 45.74 C ANISOU 1757 C HIS A1031 6610 7118 3651 -277 -1212 -1280 C ATOM 1758 O HIS A1031 17.124 21.742 215.455 1.00 47.07 O ANISOU 1758 O HIS A1031 6767 7238 3879 -400 -1158 -1400 O ATOM 1759 CB HIS A1031 16.988 20.111 213.044 1.00 43.02 C ANISOU 1759 CB HIS A1031 6179 6691 3475 -264 -943 -1127 C ATOM 1760 CG HIS A1031 18.475 19.932 213.055 1.00 44.36 C ANISOU 1760 CG HIS A1031 6129 6939 3788 -294 -1038 -1209 C ATOM 1761 ND1 HIS A1031 19.076 18.723 213.333 1.00 44.52 N ANISOU 1761 ND1 HIS A1031 6066 7077 3774 -186 -1169 -1174 N ATOM 1762 CD2 HIS A1031 19.481 20.811 212.834 1.00 45.08 C ANISOU 1762 CD2 HIS A1031 6060 7009 4058 -419 -1016 -1324 C ATOM 1763 CE1 HIS A1031 20.389 18.863 213.276 1.00 45.48 C ANISOU 1763 CE1 HIS A1031 5976 7256 4046 -236 -1230 -1259 C ATOM 1764 NE2 HIS A1031 20.661 20.120 212.976 1.00 45.87 N ANISOU 1764 NE2 HIS A1031 5971 7224 4231 -384 -1140 -1354 N ATOM 1765 N LEU A1032 17.428 19.786 216.525 1.00 47.15 N ANISOU 1765 N LEU A1032 6761 7344 3811 -225 -1355 -1248 N ATOM 1766 CA LEU A1032 18.075 20.388 217.684 1.00 50.07 C ANISOU 1766 CA LEU A1032 7089 7750 4184 -290 -1495 -1377 C ATOM 1767 C LEU A1032 19.461 20.931 217.338 1.00 52.91 C ANISOU 1767 C LEU A1032 7214 8225 4663 -381 -1582 -1576 C ATOM 1768 O LEU A1032 20.311 20.211 216.814 1.00 51.90 O ANISOU 1768 O LEU A1032 6913 8210 4597 -336 -1635 -1580 O ATOM 1769 CB LEU A1032 18.178 19.368 218.821 1.00 51.33 C ANISOU 1769 CB LEU A1032 7266 7953 4284 -211 -1601 -1279 C ATOM 1770 CG LEU A1032 18.782 19.863 220.135 1.00 54.27 C ANISOU 1770 CG LEU A1032 7615 8371 4633 -264 -1748 -1388 C ATOM 1771 CD1 LEU A1032 17.960 21.008 220.708 1.00 54.79 C ANISOU 1771 CD1 LEU A1032 7841 8335 4640 -361 -1685 -1433 C ATOM 1772 CD2 LEU A1032 18.887 18.722 221.131 1.00 55.33 C ANISOU 1772 CD2 LEU A1032 7754 8567 4704 -169 -1828 -1282 C ATOM 1773 N LEU A1033 19.680 22.208 217.635 1.00 55.68 N ANISOU 1773 N LEU A1033 7553 8543 5061 -527 -1584 -1739 N ATOM 1774 CA LEU A1033 20.966 22.847 217.385 1.00 43.76 C ANISOU 1774 CA LEU A1033 5816 7074 3735 -666 -1621 -1893 C ATOM 1775 C LEU A1033 21.859 22.760 218.618 1.00 55.21 C ANISOU 1775 C LEU A1033 7168 8644 5165 -675 -1851 -2002 C ATOM 1776 O LEU A1033 22.994 22.289 218.541 1.00 57.45 O ANISOU 1776 O LEU A1033 7230 9058 5541 -669 -1963 -2049 O ATOM 1777 CB LEU A1033 20.767 24.306 216.976 1.00 44.07 C ANISOU 1777 CB LEU A1033 5902 6956 3887 -835 -1456 -1975 C ATOM 1778 CG LEU A1033 19.889 24.533 215.746 1.00 42.03 C ANISOU 1778 CG LEU A1033 5752 6547 3671 -823 -1204 -1839 C ATOM 1779 CD1 LEU A1033 19.746 26.016 215.444 1.00 42.62 C ANISOU 1779 CD1 LEU A1033 5880 6467 3849 -981 -1044 -1926 C ATOM 1780 CD2 LEU A1033 20.463 23.793 214.551 1.00 48.22 C ANISOU 1780 CD2 LEU A1033 6381 7348 4591 -775 -1124 -1736 C ATOM 1781 N THR A1034 21.336 23.218 219.752 1.00 54.56 N ANISOU 1781 N THR A1034 7263 8484 4984 -683 -1895 -1998 N ATOM 1782 CA THR A1034 22.053 23.155 221.022 1.00 55.02 C ANISOU 1782 CA THR A1034 7277 8611 5017 -688 -2080 -2048 C ATOM 1783 C THR A1034 21.078 23.306 222.192 1.00 54.10 C ANISOU 1783 C THR A1034 7416 8404 4737 -655 -2082 -1971 C ATOM 1784 O THR A1034 19.911 23.645 221.992 1.00 51.14 O ANISOU 1784 O THR A1034 7233 7905 4292 -648 -1940 -1903 O ATOM 1785 CB THR A1034 23.139 24.239 221.110 1.00 56.63 C ANISOU 1785 CB THR A1034 7304 8846 5367 -871 -2149 -2265 C ATOM 1786 OG1 THR A1034 23.929 24.033 222.288 1.00 58.90 O ANISOU 1786 OG1 THR A1034 7527 9228 5625 -862 -2344 -2302 O ATOM 1787 CG2 THR A1034 22.511 25.623 221.152 1.00 56.64 C ANISOU 1787 CG2 THR A1034 7456 8692 5371 -1010 -2036 -2367 C ATOM 1788 N LYS A1035 21.553 23.051 223.408 1.00 56.61 N ANISOU 1788 N LYS A1035 7726 8793 4991 -640 -2232 -1981 N ATOM 1789 CA LYS A1035 20.694 23.095 224.591 1.00 58.12 C ANISOU 1789 CA LYS A1035 8129 8933 5022 -621 -2223 -1909 C ATOM 1790 C LYS A1035 21.087 24.217 225.547 1.00 62.73 C ANISOU 1790 C LYS A1035 8751 9497 5585 -751 -2319 -2070 C ATOM 1791 O LYS A1035 20.676 24.232 226.704 1.00 64.71 O ANISOU 1791 O LYS A1035 9132 9754 5702 -747 -2347 -2040 O ATOM 1792 CB LYS A1035 20.736 21.756 225.329 1.00 56.77 C ANISOU 1792 CB LYS A1035 7945 8861 4764 -485 -2289 -1770 C ATOM 1793 CG LYS A1035 20.161 20.589 224.547 1.00 48.16 C ANISOU 1793 CG LYS A1035 6861 7762 3676 -358 -2178 -1595 C ATOM 1794 CD LYS A1035 20.128 19.336 225.403 1.00 51.49 C ANISOU 1794 CD LYS A1035 7293 8255 4016 -231 -2227 -1469 C ATOM 1795 CE LYS A1035 19.452 18.182 224.680 1.00 49.46 C ANISOU 1795 CE LYS A1035 7062 7963 3765 -120 -2101 -1297 C ATOM 1796 NZ LYS A1035 19.369 16.956 225.525 1.00 49.69 N1+ ANISOU 1796 NZ LYS A1035 7112 8042 3727 1 -2132 -1182 N1+ ATOM 1797 N SER A1036 21.877 25.161 225.056 1.00 65.37 N ANISOU 1797 N SER A1036 8960 9817 6060 -877 -2354 -2246 N ATOM 1798 CA SER A1036 22.422 26.211 225.908 1.00 70.83 C ANISOU 1798 CA SER A1036 9663 10491 6759 -1013 -2458 -2413 C ATOM 1799 C SER A1036 22.120 27.620 225.371 1.00 71.83 C ANISOU 1799 C SER A1036 9861 10460 6972 -1149 -2339 -2549 C ATOM 1800 O SER A1036 22.175 27.850 224.159 1.00 70.58 O ANISOU 1800 O SER A1036 9598 10271 6949 -1190 -2216 -2582 O ATOM 1801 CB SER A1036 23.932 26.000 226.069 1.00 76.19 C ANISOU 1801 CB SER A1036 10070 11326 7552 -1059 -2636 -2518 C ATOM 1802 OG SER A1036 24.236 24.631 226.253 1.00 80.32 O ANISOU 1802 OG SER A1036 10503 11987 8026 -906 -2715 -2386 O ATOM 1803 N PRO A1037 21.798 28.564 226.283 1.00 73.27 N ANISOU 1803 N PRO A1037 10223 10543 7073 -1220 -2361 -2630 N ATOM 1804 CA PRO A1037 21.247 29.904 226.023 1.00 72.15 C ANISOU 1804 CA PRO A1037 10220 10220 6974 -1304 -2234 -2740 C ATOM 1805 C PRO A1037 21.784 30.679 224.819 1.00 72.55 C ANISOU 1805 C PRO A1037 10090 10233 7243 -1450 -2109 -2872 C ATOM 1806 O PRO A1037 20.983 31.286 224.108 1.00 74.38 O ANISOU 1806 O PRO A1037 10423 10338 7499 -1462 -1908 -2865 O ATOM 1807 CB PRO A1037 21.584 30.669 227.310 1.00 74.75 C ANISOU 1807 CB PRO A1037 10648 10519 7233 -1391 -2370 -2863 C ATOM 1808 CG PRO A1037 22.439 29.747 228.143 1.00 76.74 C ANISOU 1808 CG PRO A1037 10774 10961 7422 -1377 -2564 -2829 C ATOM 1809 CD PRO A1037 22.047 28.380 227.722 1.00 74.89 C ANISOU 1809 CD PRO A1037 10497 10822 7137 -1222 -2517 -2632 C ATOM 1810 N SER A1038 23.095 30.678 224.608 1.00 71.78 N ANISOU 1810 N SER A1038 9730 10241 7300 -1572 -2202 -2981 N ATOM 1811 CA SER A1038 23.702 31.523 223.582 1.00 71.27 C ANISOU 1811 CA SER A1038 9498 10124 7457 -1763 -2067 -3113 C ATOM 1812 C SER A1038 23.141 31.266 222.185 1.00 67.28 C ANISOU 1812 C SER A1038 8973 9578 7012 -1737 -1849 -3025 C ATOM 1813 O SER A1038 23.232 30.155 221.662 1.00 65.55 O ANISOU 1813 O SER A1038 8645 9475 6786 -1625 -1874 -2916 O ATOM 1814 CB SER A1038 25.218 31.328 223.567 1.00 73.43 C ANISOU 1814 CB SER A1038 9466 10543 7893 -1869 -2214 -3213 C ATOM 1815 OG SER A1038 25.851 32.362 222.833 1.00 74.87 O ANISOU 1815 OG SER A1038 9512 10641 8295 -2088 -2087 -3358 O ATOM 1816 N LEU A1039 22.555 32.302 221.590 1.00 65.50 N ANISOU 1816 N LEU A1039 8868 9180 6839 -1842 -1627 -3067 N ATOM 1817 CA LEU A1039 22.071 32.224 220.217 1.00 61.48 C ANISOU 1817 CA LEU A1039 8355 8611 6392 -1854 -1396 -2994 C ATOM 1818 C LEU A1039 23.251 32.220 219.256 1.00 62.06 C ANISOU 1818 C LEU A1039 8144 8735 6701 -2004 -1357 -3082 C ATOM 1819 O LEU A1039 23.144 31.740 218.128 1.00 59.84 O ANISOU 1819 O LEU A1039 7801 8430 6506 -1933 -1213 -2933 O ATOM 1820 CB LEU A1039 21.132 33.388 219.898 1.00 59.92 C ANISOU 1820 CB LEU A1039 8386 8199 6181 -1922 -1155 -3000 C ATOM 1821 N ASN A1040 24.373 32.767 219.713 1.00 64.65 N ANISOU 1821 N ASN A1040 8309 9088 7169 -2150 -1466 -3231 N ATOM 1822 CA ASN A1040 25.615 32.715 218.956 1.00 65.47 C ANISOU 1822 CA ASN A1040 8108 9256 7513 -2282 -1457 -3310 C ATOM 1823 C ASN A1040 26.122 31.282 218.869 1.00 64.59 C ANISOU 1823 C ASN A1040 7801 9364 7377 -2131 -1625 -3223 C ATOM 1824 O ASN A1040 26.664 30.863 217.846 1.00 63.66 O ANISOU 1824 O ASN A1040 7504 9259 7427 -2111 -1530 -3131 O ATOM 1825 CB ASN A1040 26.674 33.614 219.592 1.00 69.33 C ANISOU 1825 CB ASN A1040 8473 9728 8140 -2463 -1551 -3476 C ATOM 1826 CG ASN A1040 26.231 35.059 219.679 1.00 71.44 C ANISOU 1826 CG ASN A1040 8936 9770 8439 -2611 -1379 -3563 C ATOM 1827 OD1 ASN A1040 25.409 35.517 218.884 1.00 70.32 O ANISOU 1827 OD1 ASN A1040 8950 9465 8303 -2627 -1132 -3514 O ATOM 1828 ND2 ASN A1040 26.776 35.788 220.647 1.00 74.61 N ANISOU 1828 ND2 ASN A1040 9338 10155 8855 -2715 -1505 -3689 N ATOM 1829 N ALA A1041 25.939 30.537 219.954 1.00 64.45 N ANISOU 1829 N ALA A1041 7858 9461 7170 -1963 -1837 -3153 N ATOM 1830 CA ALA A1041 26.267 29.119 219.975 1.00 58.98 C ANISOU 1830 CA ALA A1041 7034 8957 6420 -1784 -1984 -3039 C ATOM 1831 C ALA A1041 25.323 28.352 219.058 1.00 59.84 C ANISOU 1831 C ALA A1041 7243 9045 6448 -1641 -1840 -2878 C ATOM 1832 O ALA A1041 25.722 27.392 218.399 1.00 59.26 O ANISOU 1832 O ALA A1041 7024 9053 6439 -1533 -1837 -2757 O ATOM 1833 CB ALA A1041 26.193 28.574 221.390 1.00 59.84 C ANISOU 1833 CB ALA A1041 7247 9150 6339 -1644 -2206 -2984 C ATOM 1834 N ALA A1042 24.067 28.788 219.022 1.00 57.77 N ANISOU 1834 N ALA A1042 7252 8634 6063 -1610 -1695 -2812 N ATOM 1835 CA ALA A1042 23.061 28.168 218.169 1.00 54.15 C ANISOU 1835 CA ALA A1042 6927 8105 5541 -1455 -1527 -2596 C ATOM 1836 C ALA A1042 23.384 28.398 216.698 1.00 53.14 C ANISOU 1836 C ALA A1042 6686 7871 5634 -1509 -1301 -2520 C ATOM 1837 O ALA A1042 23.313 27.475 215.889 1.00 52.03 O ANISOU 1837 O ALA A1042 6496 7762 5512 -1383 -1243 -2363 O ATOM 1838 CB ALA A1042 21.681 28.706 218.502 1.00 52.92 C ANISOU 1838 CB ALA A1042 7071 7822 5215 -1423 -1424 -2557 C ATOM 1839 N LYS A1043 23.739 29.633 216.360 1.00 55.03 N ANISOU 1839 N LYS A1043 6896 7977 6036 -1696 -1167 -2632 N ATOM 1840 CA LYS A1043 24.127 29.973 214.996 1.00 55.16 C ANISOU 1840 CA LYS A1043 6805 7881 6271 -1760 -941 -2573 C ATOM 1841 C LYS A1043 25.404 29.239 214.599 1.00 56.50 C ANISOU 1841 C LYS A1043 6678 8188 6603 -1756 -1028 -2575 C ATOM 1842 O LYS A1043 25.544 28.793 213.462 1.00 57.34 O ANISOU 1842 O LYS A1043 6709 8264 6813 -1694 -886 -2444 O ATOM 1843 CB LYS A1043 24.314 31.486 214.848 1.00 56.72 C ANISOU 1843 CB LYS A1043 7034 7906 6610 -1970 -786 -2710 C ATOM 1844 CG LYS A1043 23.021 32.276 214.962 1.00 56.13 C ANISOU 1844 CG LYS A1043 7258 7667 6403 -1960 -637 -2679 C ATOM 1845 CD LYS A1043 23.264 33.774 214.912 1.00 58.84 C ANISOU 1845 CD LYS A1043 7644 7834 6880 -2169 -487 -2825 C ATOM 1846 CE LYS A1043 21.957 34.542 215.062 1.00 57.57 C ANISOU 1846 CE LYS A1043 7788 7511 6574 -2139 -336 -2785 C ATOM 1847 NZ LYS A1043 22.163 36.016 215.084 1.00 58.84 N1+ ANISOU 1847 NZ LYS A1043 8018 7488 6853 -2338 -184 -2931 N1+ ATOM 1848 N SER A1044 26.326 29.112 215.548 1.00 57.51 N ANISOU 1848 N SER A1044 6639 8469 6743 -1816 -1262 -2721 N ATOM 1849 CA SER A1044 27.578 28.402 215.316 1.00 59.26 C ANISOU 1849 CA SER A1044 6563 8845 7107 -1804 -1370 -2728 C ATOM 1850 C SER A1044 27.330 26.956 214.901 1.00 57.74 C ANISOU 1850 C SER A1044 6367 8750 6821 -1574 -1397 -2534 C ATOM 1851 O SER A1044 27.906 26.473 213.926 1.00 57.29 O ANISOU 1851 O SER A1044 6154 8705 6909 -1535 -1303 -2444 O ATOM 1852 CB SER A1044 28.454 28.441 216.570 1.00 62.06 C ANISOU 1852 CB SER A1044 6765 9374 7441 -1880 -1650 -2913 C ATOM 1853 OG SER A1044 29.621 27.654 216.402 1.00 62.22 O ANISOU 1853 OG SER A1044 6494 9567 7581 -1839 -1767 -2905 O ATOM 1854 N GLU A1045 26.465 26.272 215.643 1.00 57.04 N ANISOU 1854 N GLU A1045 6460 8723 6489 -1424 -1516 -2470 N ATOM 1855 CA GLU A1045 26.159 24.874 215.367 1.00 55.51 C ANISOU 1855 CA GLU A1045 6290 8615 6187 -1209 -1549 -2293 C ATOM 1856 C GLU A1045 25.417 24.716 214.043 1.00 55.54 C ANISOU 1856 C GLU A1045 6406 8473 6223 -1146 -1296 -2121 C ATOM 1857 O GLU A1045 25.604 23.728 213.333 1.00 55.66 O ANISOU 1857 O GLU A1045 6353 8532 6263 -1022 -1260 -1989 O ATOM 1858 CB GLU A1045 25.335 24.272 216.507 1.00 53.90 C ANISOU 1858 CB GLU A1045 6274 8491 5714 -1076 -1717 -2269 C ATOM 1859 N LEU A1046 24.579 25.695 213.714 1.00 55.49 N ANISOU 1859 N LEU A1046 6576 8295 6212 -1227 -1120 -2123 N ATOM 1860 CA LEU A1046 23.791 25.644 212.486 1.00 54.67 C ANISOU 1860 CA LEU A1046 6593 8056 6123 -1167 -884 -1965 C ATOM 1861 C LEU A1046 24.640 25.928 211.253 1.00 57.58 C ANISOU 1861 C LEU A1046 6787 8358 6733 -1240 -712 -1947 C ATOM 1862 O LEU A1046 24.544 25.222 210.249 1.00 56.20 O ANISOU 1862 O LEU A1046 6603 8168 6584 -1135 -603 -1803 O ATOM 1863 CB LEU A1046 22.628 26.636 212.545 1.00 52.44 C ANISOU 1863 CB LEU A1046 6552 7619 5754 -1218 -748 -1968 C ATOM 1864 CG LEU A1046 21.784 26.705 211.267 1.00 48.71 C ANISOU 1864 CG LEU A1046 6204 7010 5293 -1160 -502 -1810 C ATOM 1865 CD1 LEU A1046 20.945 25.449 211.126 1.00 45.43 C ANISOU 1865 CD1 LEU A1046 5896 6661 4706 -972 -540 -1646 C ATOM 1866 CD2 LEU A1046 20.901 27.943 211.238 1.00 42.56 C ANISOU 1866 CD2 LEU A1046 5617 6069 4483 -1238 -344 -1836 C ATOM 1867 N ASP A1047 25.470 26.965 211.333 1.00 61.86 N ANISOU 1867 N ASP A1047 7197 8856 7450 -1422 -685 -2097 N ATOM 1868 CA ASP A1047 26.309 27.358 210.205 1.00 64.97 C ANISOU 1868 CA ASP A1047 7423 9175 8088 -1508 -506 -2090 C ATOM 1869 C ASP A1047 27.285 26.245 209.827 1.00 64.67 C ANISOU 1869 C ASP A1047 7159 9277 8137 -1415 -581 -2029 C ATOM 1870 O ASP A1047 27.789 26.205 208.705 1.00 65.00 O ANISOU 1870 O ASP A1047 7093 9263 8342 -1418 -414 -1961 O ATOM 1871 CB ASP A1047 27.071 28.651 210.519 1.00 71.42 C ANISOU 1871 CB ASP A1047 8129 9930 9078 -1736 -483 -2280 C ATOM 1872 CG ASP A1047 26.174 29.882 210.497 1.00 75.83 C ANISOU 1872 CG ASP A1047 8914 10296 9600 -1832 -318 -2318 C ATOM 1873 OD1 ASP A1047 25.810 30.341 209.394 1.00 75.08 O ANISOU 1873 OD1 ASP A1047 8899 10045 9583 -1836 -67 -2227 O ATOM 1874 OD2 ASP A1047 25.840 30.402 211.582 1.00 80.13 O1+ ANISOU 1874 OD2 ASP A1047 9563 10846 10035 -1898 -436 -2436 O1+ ATOM 1875 N LYS A1048 27.539 25.340 210.767 1.00 64.41 N ANISOU 1875 N LYS A1048 7062 9424 7986 -1322 -825 -2047 N ATOM 1876 CA LYS A1048 28.388 24.183 210.512 1.00 64.90 C ANISOU 1876 CA LYS A1048 6931 9629 8100 -1203 -909 -1976 C ATOM 1877 C LYS A1048 27.598 23.078 209.813 1.00 62.48 C ANISOU 1877 C LYS A1048 6773 9303 7664 -1006 -829 -1778 C ATOM 1878 O LYS A1048 28.121 22.383 208.939 1.00 62.11 O ANISOU 1878 O LYS A1048 6616 9273 7709 -925 -751 -1679 O ATOM 1879 CB LYS A1048 28.989 23.660 211.820 1.00 66.84 C ANISOU 1879 CB LYS A1048 7054 10079 8263 -1170 -1202 -2073 C ATOM 1880 CG LYS A1048 29.837 22.407 211.669 1.00 67.57 C ANISOU 1880 CG LYS A1048 6956 10332 8386 -1023 -1300 -1992 C ATOM 1881 CD LYS A1048 30.470 22.005 212.991 1.00 54.44 C ANISOU 1881 CD LYS A1048 5166 8877 6644 -993 -1592 -2096 C ATOM 1882 N ALA A1049 26.333 22.930 210.196 1.00 61.10 N ANISOU 1882 N ALA A1049 6850 9087 7278 -935 -845 -1722 N ATOM 1883 CA ALA A1049 25.474 21.880 209.655 1.00 58.57 C ANISOU 1883 CA ALA A1049 6687 8752 6816 -761 -788 -1546 C ATOM 1884 C ALA A1049 25.013 22.185 208.230 1.00 57.29 C ANISOU 1884 C ALA A1049 6607 8431 6731 -766 -524 -1439 C ATOM 1885 O ALA A1049 24.488 21.311 207.540 1.00 55.52 O ANISOU 1885 O ALA A1049 6476 8190 6427 -636 -455 -1295 O ATOM 1886 CB ALA A1049 24.269 21.671 210.562 1.00 57.04 C ANISOU 1886 CB ALA A1049 6722 8570 6380 -694 -887 -1527 C ATOM 1887 N ILE A1050 25.210 23.426 207.796 1.00 57.54 N ANISOU 1887 N ILE A1050 6609 8342 6910 -917 -376 -1512 N ATOM 1888 CA ILE A1050 24.804 23.846 206.458 1.00 55.47 C ANISOU 1888 CA ILE A1050 6429 7925 6722 -924 -119 -1417 C ATOM 1889 C ILE A1050 26.008 24.064 205.546 1.00 59.59 C ANISOU 1889 C ILE A1050 6738 8418 7487 -986 7 -1429 C ATOM 1890 O ILE A1050 26.034 23.588 204.410 1.00 62.45 O ANISOU 1890 O ILE A1050 7104 8732 7891 -903 154 -1307 O ATOM 1891 CB ILE A1050 23.973 25.145 206.504 1.00 51.48 C ANISOU 1891 CB ILE A1050 6092 7274 6193 -1030 5 -1465 C ATOM 1892 CG1 ILE A1050 22.708 24.939 207.340 1.00 48.04 C ANISOU 1892 CG1 ILE A1050 5874 6861 5517 -959 -96 -1438 C ATOM 1893 CG2 ILE A1050 23.620 25.609 205.098 1.00 50.05 C ANISOU 1893 CG2 ILE A1050 5988 6939 6091 -1027 275 -1364 C ATOM 1894 CD1 ILE A1050 21.782 23.877 206.794 1.00 45.19 C ANISOU 1894 CD1 ILE A1050 5651 6514 5003 -793 -67 -1268 C ATOM 1895 N GLY A1051 27.007 24.781 206.051 1.00 63.33 N ANISOU 1895 N GLY A1051 7024 8921 8118 -1133 -50 -1578 N ATOM 1896 CA GLY A1051 28.177 25.120 205.263 1.00 65.36 C ANISOU 1896 CA GLY A1051 7063 9146 8625 -1216 77 -1603 C ATOM 1897 C GLY A1051 28.002 26.470 204.596 1.00 66.58 C ANISOU 1897 C GLY A1051 7283 9110 8904 -1357 313 -1639 C ATOM 1898 O GLY A1051 28.545 26.724 203.520 1.00 67.47 O ANISOU 1898 O GLY A1051 7309 9136 9189 -1384 510 -1594 O ATOM 1899 N ARG A1052 27.239 27.340 205.249 1.00 66.12 N ANISOU 1899 N ARG A1052 7386 8981 8755 -1441 300 -1716 N ATOM 1900 CA ARG A1052 26.906 28.648 204.703 1.00 65.80 C ANISOU 1900 CA ARG A1052 7453 8747 8801 -1560 529 -1744 C ATOM 1901 C ARG A1052 26.771 29.671 205.828 1.00 66.57 C ANISOU 1901 C ARG A1052 7600 8815 8876 -1715 440 -1913 C ATOM 1902 O ARG A1052 26.537 29.302 206.977 1.00 66.24 O ANISOU 1902 O ARG A1052 7587 8892 8688 -1690 213 -1975 O ATOM 1903 CB ARG A1052 25.606 28.567 203.898 1.00 62.71 C ANISOU 1903 CB ARG A1052 7318 8248 8263 -1433 692 -1585 C ATOM 1904 CG ARG A1052 25.350 29.741 202.972 1.00 61.76 C ANISOU 1904 CG ARG A1052 7296 7924 8245 -1510 974 -1565 C ATOM 1905 CD ARG A1052 23.879 29.826 202.599 1.00 58.50 C ANISOU 1905 CD ARG A1052 7157 7430 7639 -1397 1076 -1442 C ATOM 1906 NE ARG A1052 23.080 30.401 203.677 1.00 58.43 N ANISOU 1906 NE ARG A1052 7299 7410 7492 -1441 983 -1520 N ATOM 1907 CZ ARG A1052 21.751 30.425 203.694 1.00 55.67 C ANISOU 1907 CZ ARG A1052 7176 7025 6950 -1344 1016 -1431 C ATOM 1908 NH1 ARG A1052 21.065 29.897 202.690 1.00 53.01 N1+ ANISOU 1908 NH1 ARG A1052 6938 6668 6535 -1203 1128 -1267 N1+ ATOM 1909 NH2 ARG A1052 21.107 30.973 204.716 1.00 55.07 N ANISOU 1909 NH2 ARG A1052 7228 6937 6758 -1386 937 -1507 N ATOM 1910 N ASN A1053 26.928 30.951 205.503 1.00 67.37 N ANISOU 1910 N ASN A1053 7723 8755 9121 -1872 626 -1989 N ATOM 1911 CA ASN A1053 26.659 32.018 206.461 1.00 66.87 C ANISOU 1911 CA ASN A1053 7756 8627 9024 -2018 583 -2143 C ATOM 1912 C ASN A1053 25.167 32.338 206.479 1.00 63.50 C ANISOU 1912 C ASN A1053 7636 8097 8393 -1930 670 -2059 C ATOM 1913 O ASN A1053 24.674 33.092 205.639 1.00 62.94 O ANISOU 1913 O ASN A1053 7699 7854 8360 -1940 917 -1995 O ATOM 1914 CB ASN A1053 27.471 33.270 206.126 1.00 68.73 C ANISOU 1914 CB ASN A1053 7891 8720 9504 -2231 756 -2265 C ATOM 1915 N THR A1054 24.455 31.760 207.441 1.00 61.17 N ANISOU 1915 N THR A1054 7450 7910 7881 -1838 470 -2054 N ATOM 1916 CA THR A1054 22.995 31.800 207.450 1.00 58.38 C ANISOU 1916 CA THR A1054 7368 7495 7318 -1721 532 -1947 C ATOM 1917 C THR A1054 22.404 32.981 208.218 1.00 59.43 C ANISOU 1917 C THR A1054 7677 7516 7387 -1824 566 -2055 C ATOM 1918 O THR A1054 21.281 33.402 207.936 1.00 58.10 O ANISOU 1918 O THR A1054 7728 7241 7107 -1757 707 -1966 O ATOM 1919 CB THR A1054 22.415 30.506 208.051 1.00 54.63 C ANISOU 1919 CB THR A1054 6940 7186 6632 -1554 321 -1866 C ATOM 1920 OG1 THR A1054 22.957 30.303 209.362 1.00 55.61 O ANISOU 1920 OG1 THR A1054 6972 7442 6716 -1609 68 -2008 O ATOM 1921 CG2 THR A1054 22.762 29.313 207.177 1.00 53.18 C ANISOU 1921 CG2 THR A1054 6639 7085 6481 -1427 323 -1732 C ATOM 1922 N ASN A1055 23.158 33.497 209.188 1.00 61.85 N ANISOU 1922 N ASN A1055 7888 7852 7759 -1981 432 -2245 N ATOM 1923 CA ASN A1055 22.685 34.552 210.088 1.00 62.01 C ANISOU 1923 CA ASN A1055 8076 7779 7705 -2085 431 -2371 C ATOM 1924 C ASN A1055 21.436 34.140 210.862 1.00 60.65 C ANISOU 1924 C ASN A1055 8120 7660 7265 -1942 324 -2306 C ATOM 1925 O ASN A1055 20.692 34.990 211.353 1.00 62.95 O ANISOU 1925 O ASN A1055 8612 7845 7463 -1975 388 -2349 O ATOM 1926 CB ASN A1055 22.410 35.847 209.316 1.00 62.69 C ANISOU 1926 CB ASN A1055 8287 7633 7899 -2175 730 -2367 C ATOM 1927 CG ASN A1055 23.667 36.457 208.734 1.00 66.37 C ANISOU 1927 CG ASN A1055 8554 8025 8640 -2351 844 -2464 C ATOM 1928 OD1 ASN A1055 24.084 36.113 207.628 1.00 67.00 O ANISOU 1928 OD1 ASN A1055 8518 8092 8847 -2310 971 -2361 O ATOM 1929 ND2 ASN A1055 24.279 37.370 209.479 1.00 69.28 N ANISOU 1929 ND2 ASN A1055 8883 8340 9100 -2554 804 -2665 N ATOM 1930 N GLY A1056 21.213 32.833 210.971 1.00 58.16 N ANISOU 1930 N GLY A1056 7766 7505 6828 -1783 170 -2200 N ATOM 1931 CA GLY A1056 20.069 32.307 211.691 1.00 56.07 C ANISOU 1931 CA GLY A1056 7686 7302 6315 -1643 65 -2128 C ATOM 1932 C GLY A1056 18.838 32.110 210.826 1.00 52.62 C ANISOU 1932 C GLY A1056 7420 6796 5778 -1496 240 -1932 C ATOM 1933 O GLY A1056 17.738 31.914 211.342 1.00 41.88 O ANISOU 1933 O GLY A1056 6237 5452 4223 -1394 204 -1869 O ATOM 1934 N VAL A1057 19.019 32.163 209.510 1.00 50.53 N ANISOU 1934 N VAL A1057 7100 6456 5644 -1483 429 -1837 N ATOM 1935 CA VAL A1057 17.911 31.983 208.575 1.00 46.89 C ANISOU 1935 CA VAL A1057 6784 5936 5094 -1346 596 -1653 C ATOM 1936 C VAL A1057 18.200 30.848 207.592 1.00 46.19 C ANISOU 1936 C VAL A1057 6576 5928 5046 -1243 599 -1524 C ATOM 1937 O VAL A1057 19.285 30.774 207.014 1.00 48.60 O ANISOU 1937 O VAL A1057 6703 6233 5531 -1304 632 -1556 O ATOM 1938 CB VAL A1057 17.620 33.278 207.789 1.00 46.07 C ANISOU 1938 CB VAL A1057 6788 5635 5080 -1408 870 -1639 C ATOM 1939 CG1 VAL A1057 16.488 33.058 206.797 1.00 38.86 C ANISOU 1939 CG1 VAL A1057 6013 4683 4067 -1254 1029 -1444 C ATOM 1940 CG2 VAL A1057 17.283 34.416 208.741 1.00 42.10 C ANISOU 1940 CG2 VAL A1057 6428 5037 4529 -1505 886 -1762 C ATOM 1941 N ILE A1058 17.222 29.965 207.408 1.00 43.17 N ANISOU 1941 N ILE A1058 6294 5609 4498 -1087 569 -1380 N ATOM 1942 CA ILE A1058 17.373 28.820 206.518 1.00 40.06 C ANISOU 1942 CA ILE A1058 5818 5288 4114 -981 567 -1256 C ATOM 1943 C ILE A1058 16.381 28.909 205.356 1.00 38.56 C ANISOU 1943 C ILE A1058 5763 5019 3871 -886 765 -1098 C ATOM 1944 O ILE A1058 15.414 29.670 205.414 1.00 38.71 O ANISOU 1944 O ILE A1058 5945 4957 3805 -873 868 -1068 O ATOM 1945 CB ILE A1058 17.180 27.486 207.287 1.00 39.59 C ANISOU 1945 CB ILE A1058 5744 5392 3907 -879 340 -1224 C ATOM 1946 CG1 ILE A1058 18.192 26.443 206.818 1.00 40.00 C ANISOU 1946 CG1 ILE A1058 5611 5535 4053 -844 270 -1200 C ATOM 1947 CG2 ILE A1058 15.748 26.973 207.173 1.00 38.18 C ANISOU 1947 CG2 ILE A1058 5746 5230 3532 -747 360 -1084 C ATOM 1948 CD1 ILE A1058 19.624 26.839 207.092 1.00 42.40 C ANISOU 1948 CD1 ILE A1058 5711 5855 4544 -970 216 -1343 C ATOM 1949 N THR A1059 16.630 28.149 204.294 1.00 37.71 N ANISOU 1949 N THR A1059 5587 4934 3808 -814 820 -996 N ATOM 1950 CA THR A1059 15.697 28.096 203.175 1.00 37.67 C ANISOU 1950 CA THR A1059 5703 4875 3734 -714 984 -845 C ATOM 1951 C THR A1059 14.908 26.791 203.193 1.00 37.64 C ANISOU 1951 C THR A1059 5755 4987 3558 -582 867 -734 C ATOM 1952 O THR A1059 15.317 25.816 203.825 1.00 37.44 O ANISOU 1952 O THR A1059 5651 5074 3501 -561 687 -761 O ATOM 1953 CB THR A1059 16.413 28.237 201.820 1.00 37.44 C ANISOU 1953 CB THR A1059 5592 4770 3864 -721 1161 -799 C ATOM 1954 OG1 THR A1059 17.465 27.270 201.726 1.00 37.86 O ANISOU 1954 OG1 THR A1059 5472 4910 4003 -716 1056 -817 O ATOM 1955 CG2 THR A1059 17.002 29.632 201.673 1.00 39.50 C ANISOU 1955 CG2 THR A1059 5828 4889 4290 -849 1322 -890 C ATOM 1956 N LYS A1060 13.777 26.788 202.494 1.00 38.27 N ANISOU 1956 N LYS A1060 5973 5041 3528 -494 975 -609 N ATOM 1957 CA LYS A1060 12.855 25.656 202.485 1.00 37.30 C ANISOU 1957 CA LYS A1060 5921 5016 3236 -382 883 -502 C ATOM 1958 C LYS A1060 13.530 24.345 202.082 1.00 38.51 C ANISOU 1958 C LYS A1060 5969 5248 3415 -335 796 -469 C ATOM 1959 O LYS A1060 13.293 23.305 202.698 1.00 38.63 O ANISOU 1959 O LYS A1060 5989 5363 3324 -285 640 -452 O ATOM 1960 CB LYS A1060 11.683 25.951 201.547 1.00 36.46 C ANISOU 1960 CB LYS A1060 5949 4865 3037 -305 1036 -375 C ATOM 1961 CG LYS A1060 10.658 24.838 201.445 1.00 36.24 C ANISOU 1961 CG LYS A1060 5951 4934 2885 -194 928 -258 C ATOM 1962 CD LYS A1060 9.560 25.198 200.453 1.00 36.21 C ANISOU 1962 CD LYS A1060 5899 4897 2963 -108 968 -127 C ATOM 1963 N ASP A1061 14.373 24.397 201.056 1.00 39.70 N ANISOU 1963 N ASP A1061 6030 5347 3705 -347 909 -457 N ATOM 1964 CA ASP A1061 15.062 23.202 200.582 1.00 40.21 C ANISOU 1964 CA ASP A1061 6001 5473 3803 -296 853 -421 C ATOM 1965 C ASP A1061 16.185 22.786 201.526 1.00 39.89 C ANISOU 1965 C ASP A1061 5808 5507 3843 -342 690 -526 C ATOM 1966 O ASP A1061 16.503 21.602 201.635 1.00 40.51 O ANISOU 1966 O ASP A1061 5836 5670 3885 -279 577 -499 O ATOM 1967 CB ASP A1061 15.612 23.422 199.172 1.00 44.77 C ANISOU 1967 CB ASP A1061 6537 5969 4503 -286 1038 -370 C ATOM 1968 CG ASP A1061 14.535 23.332 198.106 1.00 48.37 C ANISOU 1968 CG ASP A1061 7139 6394 4847 -199 1161 -242 C ATOM 1969 OD1 ASP A1061 13.349 23.552 198.435 1.00 47.28 O ANISOU 1969 OD1 ASP A1061 7125 6270 4567 -173 1144 -204 O ATOM 1970 OD2 ASP A1061 14.875 23.043 196.938 1.00 50.70 O1+ ANISOU 1970 OD2 ASP A1061 7420 6653 5190 -154 1274 -178 O1+ ATOM 1971 N GLU A1062 16.783 23.759 202.208 1.00 39.51 N ANISOU 1971 N GLU A1062 5688 5426 3897 -451 677 -648 N ATOM 1972 CA GLU A1062 17.816 23.466 203.197 1.00 40.15 C ANISOU 1972 CA GLU A1062 5619 5591 4045 -501 506 -759 C ATOM 1973 C GLU A1062 17.212 22.774 204.410 1.00 38.84 C ANISOU 1973 C GLU A1062 5523 5531 3706 -450 307 -769 C ATOM 1974 O GLU A1062 17.891 22.031 205.119 1.00 38.66 O ANISOU 1974 O GLU A1062 5398 5609 3681 -432 143 -814 O ATOM 1975 CB GLU A1062 18.538 24.743 203.625 1.00 42.96 C ANISOU 1975 CB GLU A1062 5891 5883 4549 -645 542 -897 C ATOM 1976 CG GLU A1062 19.650 25.177 202.687 1.00 45.27 C ANISOU 1976 CG GLU A1062 6036 6105 5057 -709 687 -919 C ATOM 1977 CD GLU A1062 20.246 26.516 203.075 1.00 47.89 C ANISOU 1977 CD GLU A1062 6304 6356 5535 -867 743 -1057 C ATOM 1978 OE1 GLU A1062 19.607 27.247 203.862 1.00 47.24 O ANISOU 1978 OE1 GLU A1062 6335 6242 5373 -917 715 -1117 O ATOM 1979 OE2 GLU A1062 21.353 26.838 202.597 1.00 50.21 O1+ ANISOU 1979 OE2 GLU A1062 6438 6615 6025 -943 822 -1105 O1+ ATOM 1980 N ALA A1063 15.928 23.027 204.641 1.00 37.40 N ANISOU 1980 N ALA A1063 5512 5324 3374 -420 330 -720 N ATOM 1981 CA ALA A1063 15.207 22.387 205.730 1.00 34.76 C ANISOU 1981 CA ALA A1063 5264 5077 2864 -365 168 -712 C ATOM 1982 C ALA A1063 14.993 20.911 205.429 1.00 32.75 C ANISOU 1982 C ALA A1063 5023 4900 2520 -252 103 -609 C ATOM 1983 O ALA A1063 15.199 20.061 206.293 1.00 32.15 O ANISOU 1983 O ALA A1063 4923 4917 2373 -209 -61 -627 O ATOM 1984 CB ALA A1063 13.877 23.081 205.969 1.00 28.47 C ANISOU 1984 CB ALA A1063 4642 4230 1944 -360 234 -678 C ATOM 1985 N GLU A1064 14.585 20.610 204.198 1.00 32.20 N ANISOU 1985 N GLU A1064 4999 4787 2448 -203 234 -501 N ATOM 1986 CA GLU A1064 14.325 19.229 203.805 1.00 32.77 C ANISOU 1986 CA GLU A1064 5103 4915 2433 -105 190 -404 C ATOM 1987 C GLU A1064 15.624 18.438 203.705 1.00 32.46 C ANISOU 1987 C GLU A1064 4914 4923 2495 -83 125 -429 C ATOM 1988 O GLU A1064 15.647 17.236 203.965 1.00 26.77 O ANISOU 1988 O GLU A1064 4203 4272 1696 -5 25 -387 O ATOM 1989 CB GLU A1064 13.569 19.167 202.476 1.00 34.00 C ANISOU 1989 CB GLU A1064 5348 5013 2556 -65 346 -292 C ATOM 1990 CG GLU A1064 13.180 17.752 202.070 1.00 35.46 C ANISOU 1990 CG GLU A1064 5588 5248 2638 24 304 -197 C ATOM 1991 CD GLU A1064 12.327 17.706 200.817 1.00 36.12 C ANISOU 1991 CD GLU A1064 5703 5286 2735 52 421 -93 C ATOM 1992 OE1 GLU A1064 11.922 18.782 200.327 1.00 36.46 O ANISOU 1992 OE1 GLU A1064 5759 5267 2827 25 532 -83 O ATOM 1993 OE2 GLU A1064 12.063 16.589 200.322 1.00 35.82 O1+ ANISOU 1993 OE2 GLU A1064 5608 5268 2732 84 378 -25 O1+ ATOM 1994 N LYS A1065 16.703 19.117 203.328 1.00 33.83 N ANISOU 1994 N LYS A1065 4950 5057 2845 -148 192 -494 N ATOM 1995 CA LYS A1065 18.021 18.491 203.293 1.00 35.26 C ANISOU 1995 CA LYS A1065 4965 5291 3141 -130 133 -524 C ATOM 1996 C LYS A1065 18.439 18.077 204.701 1.00 38.49 C ANISOU 1996 C LYS A1065 5311 5810 3504 -122 -77 -602 C ATOM 1997 O LYS A1065 18.946 16.975 204.908 1.00 42.31 O ANISOU 1997 O LYS A1065 5739 6372 3964 -41 -175 -576 O ATOM 1998 CB LYS A1065 19.057 19.436 202.682 1.00 35.50 C ANISOU 1998 CB LYS A1065 4852 5256 3381 -218 253 -586 C ATOM 1999 N LEU A1066 18.219 18.966 205.664 1.00 37.05 N ANISOU 1999 N LEU A1066 5148 5631 3299 -199 -141 -696 N ATOM 2000 CA LEU A1066 18.459 18.654 207.069 1.00 37.41 C ANISOU 2000 CA LEU A1066 5164 5780 3270 -188 -344 -771 C ATOM 2001 C LEU A1066 17.494 17.577 207.539 1.00 36.07 C ANISOU 2001 C LEU A1066 5142 5663 2901 -77 -428 -683 C ATOM 2002 O LEU A1066 17.865 16.682 208.298 1.00 36.45 O ANISOU 2002 O LEU A1066 5157 5807 2886 -6 -578 -689 O ATOM 2003 CB LEU A1066 18.310 19.905 207.938 1.00 38.61 C ANISOU 2003 CB LEU A1066 5336 5907 3426 -297 -376 -890 C ATOM 2004 CG LEU A1066 19.596 20.605 208.377 1.00 40.61 C ANISOU 2004 CG LEU A1066 5402 6188 3839 -403 -438 -1034 C ATOM 2005 CD1 LEU A1066 19.275 21.890 209.124 1.00 40.99 C ANISOU 2005 CD1 LEU A1066 5513 6184 3878 -518 -442 -1147 C ATOM 2006 CD2 LEU A1066 20.441 19.675 209.235 1.00 41.76 C ANISOU 2006 CD2 LEU A1066 5426 6480 3962 -341 -644 -1073 C ATOM 2007 N PHE A1067 16.251 17.679 207.077 1.00 34.42 N ANISOU 2007 N PHE A1067 5094 5390 2594 -62 -326 -601 N ATOM 2008 CA PHE A1067 15.196 16.747 207.454 1.00 34.13 C ANISOU 2008 CA PHE A1067 5204 5389 2374 25 -383 -515 C ATOM 2009 C PHE A1067 15.535 15.321 207.046 1.00 34.32 C ANISOU 2009 C PHE A1067 5208 5456 2375 124 -414 -435 C ATOM 2010 O PHE A1067 15.313 14.384 207.809 1.00 27.17 O ANISOU 2010 O PHE A1067 4357 4616 1350 199 -530 -409 O ATOM 2011 CB PHE A1067 13.867 17.170 206.826 1.00 34.14 C ANISOU 2011 CB PHE A1067 5353 5317 2301 15 -250 -437 C ATOM 2012 CG PHE A1067 12.752 16.194 207.051 1.00 25.01 C ANISOU 2012 CG PHE A1067 4224 4156 1122 26 -259 -316 C ATOM 2013 CD1 PHE A1067 12.145 16.091 208.289 1.00 25.00 C ANISOU 2013 CD1 PHE A1067 4198 4173 1127 -9 -329 -310 C ATOM 2014 CD2 PHE A1067 12.306 15.383 206.021 1.00 27.50 C ANISOU 2014 CD2 PHE A1067 4515 4438 1496 41 -178 -210 C ATOM 2015 CE1 PHE A1067 11.118 15.196 208.499 1.00 24.01 C ANISOU 2015 CE1 PHE A1067 4022 4041 1061 -22 -311 -207 C ATOM 2016 CE2 PHE A1067 11.277 14.485 206.224 1.00 26.83 C ANISOU 2016 CE2 PHE A1067 4375 4345 1476 16 -182 -122 C ATOM 2017 CZ PHE A1067 10.681 14.392 207.466 1.00 26.51 C ANISOU 2017 CZ PHE A1067 4308 4327 1438 -13 -244 -122 C ATOM 2018 N ASN A1068 16.073 15.161 205.841 1.00 35.91 N ANISOU 2018 N ASN A1068 5343 5614 2686 129 -302 -395 N ATOM 2019 CA ASN A1068 16.466 13.844 205.353 1.00 36.02 C ANISOU 2019 CA ASN A1068 5344 5655 2688 224 -312 -321 C ATOM 2020 C ASN A1068 17.597 13.254 206.190 1.00 39.74 C ANISOU 2020 C ASN A1068 5686 6219 3192 274 -458 -373 C ATOM 2021 O ASN A1068 17.645 12.045 206.419 1.00 38.90 O ANISOU 2021 O ASN A1068 5618 6160 3004 375 -525 -317 O ATOM 2022 CB ASN A1068 16.880 13.916 203.882 1.00 34.06 C ANISOU 2022 CB ASN A1068 5050 5335 2557 219 -150 -275 C ATOM 2023 CG ASN A1068 15.715 14.237 202.962 1.00 31.90 C ANISOU 2023 CG ASN A1068 4916 4983 2221 200 -14 -204 C ATOM 2024 OD1 ASN A1068 14.553 14.079 203.334 1.00 31.10 O ANISOU 2024 OD1 ASN A1068 4950 4891 1978 209 -43 -166 O ATOM 2025 ND2 ASN A1068 16.024 14.683 201.750 1.00 32.05 N ANISOU 2025 ND2 ASN A1068 4902 4931 2345 179 137 -180 N ATOM 2026 N GLN A1069 18.499 14.115 206.651 1.00 43.83 N ANISOU 2026 N GLN A1069 6056 6767 3830 205 -507 -481 N ATOM 2027 CA GLN A1069 19.600 13.687 207.506 1.00 48.65 C ANISOU 2027 CA GLN A1069 6524 7486 4476 247 -661 -542 C ATOM 2028 C GLN A1069 19.095 13.241 208.876 1.00 48.83 C ANISOU 2028 C GLN A1069 6639 7587 4328 301 -826 -557 C ATOM 2029 O GLN A1069 19.716 12.408 209.534 1.00 50.44 O ANISOU 2029 O GLN A1069 6785 7884 4494 391 -954 -558 O ATOM 2030 CB GLN A1069 20.624 14.813 207.674 1.00 53.58 C ANISOU 2030 CB GLN A1069 6962 8124 5271 137 -675 -665 C ATOM 2031 CG GLN A1069 21.322 15.230 206.391 1.00 56.08 C ANISOU 2031 CG GLN A1069 7163 8370 5774 89 -511 -654 C ATOM 2032 CD GLN A1069 22.297 16.373 206.606 1.00 59.90 C ANISOU 2032 CD GLN A1069 7464 8861 6433 -36 -519 -782 C ATOM 2033 OE1 GLN A1069 22.808 16.956 205.649 1.00 62.07 O ANISOU 2033 OE1 GLN A1069 7650 9064 6869 -99 -372 -786 O ATOM 2034 NE2 GLN A1069 22.557 16.701 207.868 1.00 61.29 N ANISOU 2034 NE2 GLN A1069 7588 9123 6578 -76 -688 -890 N ATOM 2035 N ASP A1070 17.969 13.804 209.302 1.00 47.72 N ANISOU 2035 N ASP A1070 6643 7407 4082 255 -817 -564 N ATOM 2036 CA ASP A1070 17.397 13.477 210.604 1.00 48.59 C ANISOU 2036 CA ASP A1070 6856 7570 4035 299 -951 -573 C ATOM 2037 C ASP A1070 16.509 12.237 210.538 1.00 48.04 C ANISOU 2037 C ASP A1070 6898 7379 3976 326 -873 -405 C ATOM 2038 O ASP A1070 16.360 11.521 211.529 1.00 51.95 O ANISOU 2038 O ASP A1070 7412 7860 4468 343 -932 -361 O ATOM 2039 CB ASP A1070 16.598 14.664 211.154 1.00 48.71 C ANISOU 2039 CB ASP A1070 6951 7511 4044 189 -922 -619 C ATOM 2040 CG ASP A1070 17.488 15.768 211.700 1.00 50.33 C ANISOU 2040 CG ASP A1070 7031 7784 4308 111 -1010 -786 C ATOM 2041 OD1 ASP A1070 18.005 16.572 210.897 1.00 50.69 O1+ ANISOU 2041 OD1 ASP A1070 6975 7772 4515 20 -906 -826 O1+ ATOM 2042 OD2 ASP A1070 17.668 15.833 212.934 1.00 51.80 O ANISOU 2042 OD2 ASP A1070 7217 8025 4440 114 -1152 -848 O ATOM 2043 N VAL A1071 15.921 11.987 209.372 1.00 43.46 N ANISOU 2043 N VAL A1071 6375 6722 3415 317 -735 -323 N ATOM 2044 CA VAL A1071 15.047 10.832 209.196 1.00 41.88 C ANISOU 2044 CA VAL A1071 6235 6425 3251 305 -659 -195 C ATOM 2045 C VAL A1071 15.841 9.531 209.193 1.00 44.23 C ANISOU 2045 C VAL A1071 6503 6763 3539 418 -710 -160 C ATOM 2046 O VAL A1071 15.526 8.606 209.942 1.00 45.08 O ANISOU 2046 O VAL A1071 6633 6843 3654 429 -735 -108 O ATOM 2047 CB VAL A1071 14.229 10.922 207.890 1.00 37.62 C ANISOU 2047 CB VAL A1071 5736 5805 2754 250 -510 -131 C ATOM 2048 CG1 VAL A1071 13.539 9.599 207.600 1.00 35.20 C ANISOU 2048 CG1 VAL A1071 5441 5437 2497 241 -458 -33 C ATOM 2049 CG2 VAL A1071 13.207 12.037 207.980 1.00 36.17 C ANISOU 2049 CG2 VAL A1071 5570 5584 2590 144 -448 -141 C ATOM 2050 N ASP A1072 16.874 9.458 208.358 1.00 45.40 N ANISOU 2050 N ASP A1072 6594 6991 3664 511 -715 -187 N ATOM 2051 CA ASP A1072 17.666 8.236 208.271 1.00 47.12 C ANISOU 2051 CA ASP A1072 6781 7256 3868 636 -752 -145 C ATOM 2052 C ASP A1072 18.485 8.018 209.543 1.00 43.93 C ANISOU 2052 C ASP A1072 6292 6958 3440 704 -913 -197 C ATOM 2053 O ASP A1072 18.864 6.893 209.858 1.00 43.53 O ANISOU 2053 O ASP A1072 6241 6918 3378 799 -945 -145 O ATOM 2054 CB ASP A1072 18.568 8.251 207.024 1.00 53.64 C ANISOU 2054 CB ASP A1072 7543 8154 4686 718 -697 -150 C ATOM 2055 CG ASP A1072 19.578 9.389 207.025 1.00 64.16 C ANISOU 2055 CG ASP A1072 8674 9517 6188 639 -710 -250 C ATOM 2056 OD1 ASP A1072 19.741 10.069 208.058 1.00 72.01 O ANISOU 2056 OD1 ASP A1072 9609 10575 7178 594 -827 -340 O ATOM 2057 OD2 ASP A1072 20.222 9.598 205.974 1.00 66.33 O1+ ANISOU 2057 OD2 ASP A1072 8852 9748 6601 619 -597 -241 O1+ ATOM 2058 N ALA A1073 18.739 9.100 210.273 1.00 41.48 N ANISOU 2058 N ALA A1073 5914 6721 3126 651 -1009 -303 N ATOM 2059 CA ALA A1073 19.413 9.017 211.564 1.00 40.30 C ANISOU 2059 CA ALA A1073 5685 6660 2966 689 -1164 -359 C ATOM 2060 C ALA A1073 18.488 8.405 212.607 1.00 38.91 C ANISOU 2060 C ALA A1073 5628 6375 2781 656 -1146 -283 C ATOM 2061 O ALA A1073 18.926 7.651 213.477 1.00 39.66 O ANISOU 2061 O ALA A1073 5703 6510 2856 732 -1226 -266 O ATOM 2062 CB ALA A1073 19.880 10.389 212.013 1.00 41.69 C ANISOU 2062 CB ALA A1073 5754 6931 3155 612 -1264 -508 C ATOM 2063 N ALA A1074 17.206 8.741 212.517 1.00 38.93 N ANISOU 2063 N ALA A1074 5735 6256 2801 542 -1038 -239 N ATOM 2064 CA ALA A1074 16.202 8.164 213.399 1.00 39.72 C ANISOU 2064 CA ALA A1074 5913 6277 2901 498 -1002 -169 C ATOM 2065 C ALA A1074 16.019 6.686 213.075 1.00 39.28 C ANISOU 2065 C ALA A1074 5894 6173 2857 562 -942 -76 C ATOM 2066 O ALA A1074 15.958 5.846 213.972 1.00 40.05 O ANISOU 2066 O ALA A1074 6013 6269 2933 608 -973 -43 O ATOM 2067 CB ALA A1074 14.883 8.911 213.272 1.00 28.84 C ANISOU 2067 CB ALA A1074 4590 4817 1552 365 -900 -150 C ATOM 2068 N VAL A1075 15.939 6.378 211.783 1.00 37.69 N ANISOU 2068 N VAL A1075 5706 5931 2683 566 -853 -39 N ATOM 2069 CA VAL A1075 15.820 5.000 211.321 1.00 39.17 C ANISOU 2069 CA VAL A1075 5933 6067 2882 623 -792 38 C ATOM 2070 C VAL A1075 17.056 4.204 211.720 1.00 43.85 C ANISOU 2070 C VAL A1075 6490 6741 3429 781 -882 35 C ATOM 2071 O VAL A1075 16.967 3.031 212.085 1.00 46.20 O ANISOU 2071 O VAL A1075 6832 7007 3716 841 -868 88 O ATOM 2072 CB VAL A1075 15.631 4.931 209.794 1.00 40.14 C ANISOU 2072 CB VAL A1075 6074 6138 3039 600 -685 68 C ATOM 2073 CG1 VAL A1075 15.619 3.485 209.318 1.00 27.51 C ANISOU 2073 CG1 VAL A1075 4519 4485 1446 663 -629 135 C ATOM 2074 CG2 VAL A1075 14.348 5.639 209.387 1.00 26.19 C ANISOU 2074 CG2 VAL A1075 4324 4304 1325 451 -597 77 C ATOM 2075 N ARG A1076 18.209 4.860 211.653 1.00 46.78 N ANISOU 2075 N ARG A1076 6766 7232 3776 852 -976 -33 N ATOM 2076 CA ARG A1076 19.462 4.254 212.076 1.00 48.66 C ANISOU 2076 CA ARG A1076 6924 7587 3979 1007 -1082 -44 C ATOM 2077 C ARG A1076 19.383 3.880 213.552 1.00 49.80 C ANISOU 2077 C ARG A1076 7084 7741 4096 1025 -1161 -44 C ATOM 2078 O ARG A1076 19.820 2.803 213.956 1.00 52.52 O ANISOU 2078 O ARG A1076 7439 8105 4412 1143 -1184 0 O ATOM 2079 CB ARG A1076 20.631 5.209 211.821 1.00 52.94 C ANISOU 2079 CB ARG A1076 7305 8289 4521 1049 -1188 -139 C ATOM 2080 CG ARG A1076 21.967 4.525 211.588 1.00 58.02 C ANISOU 2080 CG ARG A1076 7824 9069 5151 1221 -1259 -129 C ATOM 2081 CD ARG A1076 23.040 5.520 211.158 1.00 60.80 C ANISOU 2081 CD ARG A1076 7965 9602 5533 1235 -1356 -231 C ATOM 2082 NE ARG A1076 23.003 5.783 209.721 1.00 61.98 N ANISOU 2082 NE ARG A1076 8099 9641 5807 1161 -1175 -199 N ATOM 2083 CZ ARG A1076 22.566 6.914 209.174 1.00 63.92 C ANISOU 2083 CZ ARG A1076 8339 9816 6133 1006 -1091 -251 C ATOM 2084 NH1 ARG A1076 22.129 7.903 209.943 1.00 65.54 N1+ ANISOU 2084 NH1 ARG A1076 8551 10042 6310 904 -1169 -342 N1+ ATOM 2085 NH2 ARG A1076 22.569 7.057 207.856 1.00 63.53 N ANISOU 2085 NH2 ARG A1076 8284 9669 6187 961 -924 -211 N ATOM 2086 N GLY A1077 18.805 4.772 214.349 1.00 48.16 N ANISOU 2086 N GLY A1077 6889 7518 3890 915 -1193 -90 N ATOM 2087 CA GLY A1077 18.670 4.545 215.776 1.00 47.99 C ANISOU 2087 CA GLY A1077 6891 7508 3833 926 -1260 -92 C ATOM 2088 C GLY A1077 17.669 3.455 216.099 1.00 45.52 C ANISOU 2088 C GLY A1077 6690 7088 3517 919 -1164 -4 C ATOM 2089 O GLY A1077 17.909 2.620 216.969 1.00 46.42 O ANISOU 2089 O GLY A1077 6825 7221 3589 1009 -1204 22 O ATOM 2090 N ILE A1078 16.542 3.470 215.395 1.00 42.92 N ANISOU 2090 N ILE A1078 6421 6654 3233 811 -1039 37 N ATOM 2091 CA ILE A1078 15.503 2.458 215.561 1.00 39.76 C ANISOU 2091 CA ILE A1078 6098 6162 2847 785 -946 108 C ATOM 2092 C ILE A1078 16.033 1.059 215.257 1.00 43.29 C ANISOU 2092 C ILE A1078 6577 6596 3274 913 -926 159 C ATOM 2093 O ILE A1078 15.811 0.119 216.022 1.00 47.22 O ANISOU 2093 O ILE A1078 7127 7072 3743 969 -921 194 O ATOM 2094 CB ILE A1078 14.294 2.750 214.656 1.00 35.39 C ANISOU 2094 CB ILE A1078 5564 5526 2359 647 -827 133 C ATOM 2095 CG1 ILE A1078 13.571 4.011 215.128 1.00 33.98 C ANISOU 2095 CG1 ILE A1078 5365 5352 2192 530 -828 97 C ATOM 2096 CG2 ILE A1078 13.338 1.573 214.643 1.00 34.92 C ANISOU 2096 CG2 ILE A1078 5572 5389 2309 664 -745 189 C ATOM 2097 CD1 ILE A1078 12.360 4.360 214.298 1.00 33.31 C ANISOU 2097 CD1 ILE A1078 5297 5205 2156 454 -725 112 C ATOM 2098 N LEU A1079 16.750 0.935 214.144 1.00 42.74 N ANISOU 2098 N LEU A1079 6482 6543 3214 970 -911 161 N ATOM 2099 CA LEU A1079 17.324 -0.342 213.729 1.00 42.28 C ANISOU 2099 CA LEU A1079 6458 6473 3134 1103 -882 211 C ATOM 2100 C LEU A1079 18.518 -0.750 214.591 1.00 46.00 C ANISOU 2100 C LEU A1079 6885 7050 3543 1269 -992 203 C ATOM 2101 O LEU A1079 19.139 -1.785 214.351 1.00 49.10 O ANISOU 2101 O LEU A1079 7298 7449 3907 1406 -975 246 O ATOM 2102 CB LEU A1079 17.741 -0.280 212.258 1.00 40.48 C ANISOU 2102 CB LEU A1079 6214 6236 2930 1120 -824 220 C ATOM 2103 CG LEU A1079 16.611 -0.485 211.248 1.00 38.84 C ANISOU 2103 CG LEU A1079 6069 5909 2778 996 -695 252 C ATOM 2104 CD1 LEU A1079 17.029 -0.027 209.862 1.00 39.10 C ANISOU 2104 CD1 LEU A1079 6079 5946 2831 996 -648 247 C ATOM 2105 CD2 LEU A1079 16.188 -1.945 211.223 1.00 39.32 C ANISOU 2105 CD2 LEU A1079 6217 5887 2837 1034 -625 309 C ATOM 2106 N ARG A1080 18.839 0.065 215.590 1.00 45.41 N ANISOU 2106 N ARG A1080 6747 7061 3447 1259 -1104 146 N ATOM 2107 CA ARG A1080 19.915 -0.252 216.520 1.00 47.49 C ANISOU 2107 CA ARG A1080 6952 7439 3655 1405 -1224 130 C ATOM 2108 C ARG A1080 19.364 -0.450 217.929 1.00 48.37 C ANISOU 2108 C ARG A1080 7122 7531 3727 1390 -1254 134 C ATOM 2109 O ARG A1080 20.115 -0.700 218.872 1.00 48.89 O ANISOU 2109 O ARG A1080 7151 7685 3739 1501 -1354 120 O ATOM 2110 CB ARG A1080 20.979 0.848 216.514 1.00 48.56 C ANISOU 2110 CB ARG A1080 6934 7719 3796 1420 -1355 47 C ATOM 2111 N ASN A1081 18.045 -0.332 218.065 1.00 49.40 N ANISOU 2111 N ASN A1081 7333 7554 3883 1258 -1166 152 N ATOM 2112 CA ASN A1081 17.383 -0.552 219.346 1.00 50.46 C ANISOU 2112 CA ASN A1081 7528 7664 3981 1244 -1174 163 C ATOM 2113 C ASN A1081 16.712 -1.922 219.386 1.00 51.70 C ANISOU 2113 C ASN A1081 7787 7726 4129 1288 -1073 236 C ATOM 2114 O ASN A1081 15.992 -2.300 218.461 1.00 50.50 O ANISOU 2114 O ASN A1081 7674 7485 4028 1219 -966 269 O ATOM 2115 CB ASN A1081 16.359 0.551 219.619 1.00 50.54 C ANISOU 2115 CB ASN A1081 7543 7638 4023 1079 -1150 133 C ATOM 2116 CG ASN A1081 15.868 0.549 221.054 1.00 52.99 C ANISOU 2116 CG ASN A1081 7898 7953 4284 1080 -1180 132 C ATOM 2117 OD1 ASN A1081 16.365 -0.204 221.892 1.00 55.22 O ANISOU 2117 OD1 ASN A1081 8206 8271 4504 1205 -1232 147 O ATOM 2118 ND2 ASN A1081 14.894 1.400 221.347 1.00 53.73 N ANISOU 2118 ND2 ASN A1081 8016 8013 4384 995 -1151 104 N ATOM 2119 N ALA A1082 16.950 -2.657 220.467 1.00 53.97 N ANISOU 2119 N ALA A1082 8118 8036 4350 1402 -1111 255 N ATOM 2120 CA ALA A1082 16.525 -4.050 220.570 1.00 55.09 C ANISOU 2120 CA ALA A1082 8361 8099 4471 1476 -1026 318 C ATOM 2121 C ALA A1082 15.009 -4.209 220.630 1.00 55.07 C ANISOU 2121 C ALA A1082 8450 7987 4487 1403 -925 330 C ATOM 2122 O ALA A1082 14.479 -5.280 220.332 1.00 54.68 O ANISOU 2122 O ALA A1082 8489 7851 4436 1443 -835 373 O ATOM 2123 CB ALA A1082 17.164 -4.696 221.789 1.00 56.83 C ANISOU 2123 CB ALA A1082 8612 8378 4603 1638 -1096 329 C ATOM 2124 N LYS A1083 14.311 -3.146 221.012 1.00 55.62 N ANISOU 2124 N LYS A1083 8501 8061 4570 1308 -941 290 N ATOM 2125 CA LYS A1083 12.867 -3.224 221.184 1.00 55.73 C ANISOU 2125 CA LYS A1083 8594 7986 4597 1258 -857 300 C ATOM 2126 C LYS A1083 12.116 -2.542 220.039 1.00 52.42 C ANISOU 2126 C LYS A1083 8138 7523 4258 1118 -793 289 C ATOM 2127 O LYS A1083 10.925 -2.782 219.836 1.00 51.38 O ANISOU 2127 O LYS A1083 8059 7311 4150 1072 -713 307 O ATOM 2128 CB LYS A1083 12.463 -2.608 222.525 1.00 58.94 C ANISOU 2128 CB LYS A1083 9022 8420 4952 1270 -907 272 C ATOM 2129 CG LYS A1083 11.041 -2.933 222.944 1.00 62.36 C ANISOU 2129 CG LYS A1083 9549 8763 5381 1257 -825 294 C ATOM 2130 CD LYS A1083 10.796 -2.611 224.405 1.00 66.59 C ANISOU 2130 CD LYS A1083 10129 9324 5847 1311 -872 277 C ATOM 2131 CE LYS A1083 9.690 -3.490 224.966 1.00 70.04 C ANISOU 2131 CE LYS A1083 10684 9671 6257 1359 -791 318 C ATOM 2132 NZ LYS A1083 8.516 -3.549 224.048 1.00 68.46 N1+ ANISOU 2132 NZ LYS A1083 10496 9387 6129 1255 -692 338 N1+ ATOM 2133 N LEU A1084 12.817 -1.703 219.284 1.00 50.07 N ANISOU 2133 N LEU A1084 7746 7279 3999 1052 -831 261 N ATOM 2134 CA LEU A1084 12.196 -0.972 218.185 1.00 45.68 C ANISOU 2134 CA LEU A1084 7153 6690 3513 928 -773 250 C ATOM 2135 C LEU A1084 12.437 -1.634 216.833 1.00 45.21 C ANISOU 2135 C LEU A1084 7091 6591 3495 920 -712 279 C ATOM 2136 O LEU A1084 11.695 -1.391 215.881 1.00 45.30 O ANISOU 2136 O LEU A1084 7098 6555 3560 835 -643 282 O ATOM 2137 CB LEU A1084 12.706 0.468 218.150 1.00 43.46 C ANISOU 2137 CB LEU A1084 6784 6483 3248 850 -839 198 C ATOM 2138 CG LEU A1084 12.271 1.339 219.327 1.00 43.29 C ANISOU 2138 CG LEU A1084 6768 6488 3191 830 -885 162 C ATOM 2139 CD1 LEU A1084 12.745 2.769 219.143 1.00 42.80 C ANISOU 2139 CD1 LEU A1084 6627 6487 3146 738 -940 106 C ATOM 2140 CD2 LEU A1084 10.762 1.287 219.490 1.00 42.83 C ANISOU 2140 CD2 LEU A1084 6772 6353 3147 796 -802 182 C ATOM 2141 N LYS A1085 13.468 -2.471 216.752 1.00 44.91 N ANISOU 2141 N LYS A1085 7057 6575 3431 1016 -736 302 N ATOM 2142 CA LYS A1085 13.835 -3.105 215.486 1.00 42.90 C ANISOU 2142 CA LYS A1085 6805 6286 3208 1022 -679 330 C ATOM 2143 C LYS A1085 12.819 -4.141 214.976 1.00 40.19 C ANISOU 2143 C LYS A1085 6556 5834 2879 1017 -575 364 C ATOM 2144 O LYS A1085 12.440 -4.087 213.806 1.00 39.19 O ANISOU 2144 O LYS A1085 6424 5664 2801 946 -514 367 O ATOM 2145 CB LYS A1085 15.218 -3.756 215.593 1.00 44.57 C ANISOU 2145 CB LYS A1085 7005 6552 3378 1155 -731 349 C ATOM 2146 CG LYS A1085 15.730 -4.311 214.272 1.00 44.80 C ANISOU 2146 CG LYS A1085 7051 6549 3422 1207 -674 373 C ATOM 2147 CD LYS A1085 17.107 -4.937 214.419 1.00 46.52 C ANISOU 2147 CD LYS A1085 7269 6831 3577 1407 -723 389 C ATOM 2148 CE LYS A1085 17.648 -5.384 213.071 1.00 46.02 C ANISOU 2148 CE LYS A1085 7220 6739 3525 1465 -658 415 C ATOM 2149 NZ LYS A1085 16.724 -6.337 212.395 1.00 45.25 N1+ ANISOU 2149 NZ LYS A1085 7224 6511 3458 1403 -538 451 N1+ ATOM 2150 N PRO A1086 12.379 -5.090 215.830 1.00 39.87 N ANISOU 2150 N PRO A1086 6606 5750 2794 1092 -556 389 N ATOM 2151 CA PRO A1086 11.420 -6.058 215.279 1.00 39.00 C ANISOU 2151 CA PRO A1086 6586 5534 2699 1073 -461 416 C ATOM 2152 C PRO A1086 10.083 -5.422 214.894 1.00 37.79 C ANISOU 2152 C PRO A1086 6421 5343 2595 946 -420 400 C ATOM 2153 O PRO A1086 9.439 -5.879 213.948 1.00 36.54 O ANISOU 2153 O PRO A1086 6295 5117 2469 893 -352 411 O ATOM 2154 CB PRO A1086 11.237 -7.063 216.421 1.00 40.16 C ANISOU 2154 CB PRO A1086 6831 5647 2782 1179 -454 443 C ATOM 2155 CG PRO A1086 11.593 -6.311 217.648 1.00 40.71 C ANISOU 2155 CG PRO A1086 6857 5798 2813 1215 -542 420 C ATOM 2156 CD PRO A1086 12.695 -5.385 217.241 1.00 40.37 C ANISOU 2156 CD PRO A1086 6701 5849 2789 1195 -614 393 C ATOM 2157 N VAL A1087 9.684 -4.379 215.616 1.00 38.10 N ANISOU 2157 N VAL A1087 6415 5427 2636 903 -461 373 N ATOM 2158 CA VAL A1087 8.449 -3.660 215.315 1.00 37.39 C ANISOU 2158 CA VAL A1087 6302 5314 2589 793 -426 361 C ATOM 2159 C VAL A1087 8.558 -2.943 213.977 1.00 37.63 C ANISOU 2159 C VAL A1087 6260 5359 2679 708 -407 345 C ATOM 2160 O VAL A1087 7.662 -3.025 213.137 1.00 36.80 O ANISOU 2160 O VAL A1087 6161 5209 2613 639 -350 352 O ATOM 2161 CB VAL A1087 8.111 -2.631 216.410 1.00 36.51 C ANISOU 2161 CB VAL A1087 6162 5249 2461 777 -474 337 C ATOM 2162 CG1 VAL A1087 6.763 -1.988 216.135 1.00 28.50 C ANISOU 2162 CG1 VAL A1087 5132 4209 1487 680 -429 333 C ATOM 2163 CG2 VAL A1087 8.121 -3.291 217.778 1.00 38.23 C ANISOU 2163 CG2 VAL A1087 6454 5460 2612 874 -497 351 C ATOM 2164 N TYR A1088 9.673 -2.245 213.793 1.00 39.77 N ANISOU 2164 N TYR A1088 6463 5696 2953 715 -458 324 N ATOM 2165 CA TYR A1088 9.922 -1.460 212.591 1.00 40.10 C ANISOU 2165 CA TYR A1088 6436 5756 3042 642 -443 308 C ATOM 2166 C TYR A1088 10.013 -2.331 211.342 1.00 39.86 C ANISOU 2166 C TYR A1088 6437 5672 3035 646 -381 331 C ATOM 2167 O TYR A1088 9.639 -1.904 210.248 1.00 38.69 O ANISOU 2167 O TYR A1088 6260 5510 2932 575 -340 325 O ATOM 2168 CB TYR A1088 11.209 -0.653 212.762 1.00 42.53 C ANISOU 2168 CB TYR A1088 6675 6147 3338 656 -515 282 C ATOM 2169 CG TYR A1088 11.507 0.296 211.628 1.00 44.46 C ANISOU 2169 CG TYR A1088 6853 6414 3627 580 -499 262 C ATOM 2170 CD1 TYR A1088 10.897 1.542 211.565 1.00 44.74 C ANISOU 2170 CD1 TYR A1088 6845 6466 3689 494 -494 234 C ATOM 2171 CD2 TYR A1088 12.409 -0.045 210.630 1.00 45.10 C ANISOU 2171 CD2 TYR A1088 6920 6499 3719 602 -484 274 C ATOM 2172 CE1 TYR A1088 11.168 2.417 210.533 1.00 44.02 C ANISOU 2172 CE1 TYR A1088 6702 6391 3632 429 -473 217 C ATOM 2173 CE2 TYR A1088 12.687 0.824 209.593 1.00 45.08 C ANISOU 2173 CE2 TYR A1088 6864 6512 3750 537 -463 258 C ATOM 2174 CZ TYR A1088 12.063 2.055 209.551 1.00 44.92 C ANISOU 2174 CZ TYR A1088 6805 6506 3755 450 -457 228 C ATOM 2175 OH TYR A1088 12.335 2.927 208.522 1.00 46.79 O ANISOU 2175 OH TYR A1088 6999 6756 4021 390 -428 213 O ATOM 2176 N ASP A1089 10.511 -3.552 211.511 1.00 41.06 N ANISOU 2176 N ASP A1089 6654 5794 3153 734 -373 358 N ATOM 2177 CA ASP A1089 10.704 -4.460 210.386 1.00 41.63 C ANISOU 2177 CA ASP A1089 6771 5808 3237 750 -313 379 C ATOM 2178 C ASP A1089 9.396 -5.076 209.908 1.00 43.04 C ANISOU 2178 C ASP A1089 7015 5903 3434 695 -246 389 C ATOM 2179 O ASP A1089 9.304 -5.539 208.772 1.00 47.85 O ANISOU 2179 O ASP A1089 7652 6463 4065 673 -194 395 O ATOM 2180 CB ASP A1089 11.690 -5.567 210.759 1.00 43.37 C ANISOU 2180 CB ASP A1089 7047 6021 3409 873 -321 408 C ATOM 2181 CG ASP A1089 13.113 -5.062 210.875 1.00 46.15 C ANISOU 2181 CG ASP A1089 7326 6462 3747 928 -386 404 C ATOM 2182 OD1 ASP A1089 13.461 -4.103 210.155 1.00 45.87 O ANISOU 2182 OD1 ASP A1089 7215 6469 3747 866 -397 384 O ATOM 2183 OD2 ASP A1089 13.883 -5.622 211.685 1.00 49.66 O1+ ANISOU 2183 OD2 ASP A1089 7788 6938 4143 1035 -428 422 O1+ ATOM 2184 N SER A1090 8.386 -5.079 210.772 1.00 38.76 N ANISOU 2184 N SER A1090 6499 5347 2882 673 -249 389 N ATOM 2185 CA SER A1090 7.104 -5.686 210.435 1.00 36.30 C ANISOU 2185 CA SER A1090 6247 4964 2582 618 -193 399 C ATOM 2186 C SER A1090 6.107 -4.654 209.924 1.00 34.93 C ANISOU 2186 C SER A1090 6005 4814 2455 513 -185 381 C ATOM 2187 O SER A1090 4.947 -4.977 209.666 1.00 34.72 O ANISOU 2187 O SER A1090 6008 4747 2438 457 -149 387 O ATOM 2188 CB SER A1090 6.517 -6.405 211.648 1.00 37.13 C ANISOU 2188 CB SER A1090 6429 5035 2644 659 -190 417 C ATOM 2189 OG SER A1090 6.062 -5.469 212.607 1.00 37.59 O ANISOU 2189 OG SER A1090 6439 5144 2700 638 -229 405 O ATOM 2190 N LEU A1091 6.560 -3.412 209.785 1.00 34.05 N ANISOU 2190 N LEU A1091 5802 4768 2367 488 -218 359 N ATOM 2191 CA LEU A1091 5.689 -2.326 209.346 1.00 32.02 C ANISOU 2191 CA LEU A1091 5478 4537 2150 404 -209 344 C ATOM 2192 C LEU A1091 5.976 -1.909 207.909 1.00 31.95 C ANISOU 2192 C LEU A1091 5426 4532 2180 365 -183 335 C ATOM 2193 O LEU A1091 7.112 -1.988 207.444 1.00 31.23 O ANISOU 2193 O LEU A1091 5328 4451 2087 400 -189 332 O ATOM 2194 CB LEU A1091 5.834 -1.115 210.271 1.00 31.39 C ANISOU 2194 CB LEU A1091 5338 4521 2066 399 -256 326 C ATOM 2195 CG LEU A1091 5.355 -1.262 211.717 1.00 25.46 C ANISOU 2195 CG LEU A1091 4626 3771 1279 430 -279 332 C ATOM 2196 CD1 LEU A1091 5.772 -0.052 212.533 1.00 25.52 C ANISOU 2196 CD1 LEU A1091 4581 3840 1276 431 -331 306 C ATOM 2197 CD2 LEU A1091 3.847 -1.451 211.773 1.00 25.29 C ANISOU 2197 CD2 LEU A1091 4626 3716 1265 382 -239 347 C ATOM 2198 N ASP A1092 4.934 -1.468 207.210 1.00 32.93 N ANISOU 2198 N ASP A1092 5524 4654 2336 297 -154 332 N ATOM 2199 CA ASP A1092 5.081 -0.940 205.861 1.00 34.49 C ANISOU 2199 CA ASP A1092 5680 4857 2568 263 -129 323 C ATOM 2200 C ASP A1092 5.589 0.496 205.913 1.00 33.30 C ANISOU 2200 C ASP A1092 5449 4768 2436 247 -151 304 C ATOM 2201 O ASP A1092 5.700 1.079 206.988 1.00 36.40 O ANISOU 2201 O ASP A1092 5820 5197 2815 255 -187 295 O ATOM 2202 CB ASP A1092 3.755 -1.006 205.107 1.00 38.69 C ANISOU 2202 CB ASP A1092 6213 5368 3118 204 -95 328 C ATOM 2203 CG ASP A1092 2.651 -0.231 205.800 1.00 42.28 C ANISOU 2203 CG ASP A1092 6625 5861 3578 169 -105 329 C ATOM 2204 OD1 ASP A1092 2.551 -0.321 207.043 1.00 40.41 O ANISOU 2204 OD1 ASP A1092 6405 5632 3319 191 -128 334 O ATOM 2205 OD2 ASP A1092 1.892 0.477 205.104 1.00 44.62 O1+ ANISOU 2205 OD2 ASP A1092 6874 6180 3897 127 -89 328 O1+ ATOM 2206 N ALA A1093 5.877 1.067 204.748 1.00 32.60 N ANISOU 2206 N ALA A1093 5325 4686 2374 225 -126 296 N ATOM 2207 CA ALA A1093 6.499 2.387 204.663 1.00 34.19 C ANISOU 2207 CA ALA A1093 5463 4939 2591 209 -137 277 C ATOM 2208 C ALA A1093 5.661 3.498 205.296 1.00 32.24 C ANISOU 2208 C ALA A1093 5172 4725 2351 173 -148 268 C ATOM 2209 O ALA A1093 6.204 4.494 205.774 1.00 31.80 O ANISOU 2209 O ALA A1093 5081 4711 2291 165 -171 248 O ATOM 2210 CB ALA A1093 6.796 2.727 203.209 1.00 37.71 C ANISOU 2210 CB ALA A1093 5890 5374 3062 193 -95 276 C ATOM 2211 N VAL A1094 4.343 3.331 205.298 1.00 31.08 N ANISOU 2211 N VAL A1094 5032 4563 2212 150 -130 282 N ATOM 2212 CA VAL A1094 3.462 4.338 205.881 1.00 32.64 C ANISOU 2212 CA VAL A1094 5194 4791 2415 124 -133 279 C ATOM 2213 C VAL A1094 3.486 4.279 207.408 1.00 31.75 C ANISOU 2213 C VAL A1094 5102 4689 2272 145 -172 275 C ATOM 2214 O VAL A1094 3.718 5.291 208.070 1.00 31.74 O ANISOU 2214 O VAL A1094 5075 4720 2263 141 -193 257 O ATOM 2215 CB VAL A1094 2.011 4.179 205.383 1.00 34.78 C ANISOU 2215 CB VAL A1094 5462 5055 2699 96 -104 299 C ATOM 2216 CG1 VAL A1094 1.088 5.132 206.124 1.00 21.17 C ANISOU 2216 CG1 VAL A1094 3707 3362 974 80 -106 302 C ATOM 2217 CG2 VAL A1094 1.936 4.430 203.887 1.00 20.89 C ANISOU 2217 CG2 VAL A1094 3681 3291 964 78 -70 300 C ATOM 2218 N ARG A1095 3.258 3.093 207.963 1.00 29.96 N ANISOU 2218 N ARG A1095 4929 4433 2022 170 -180 290 N ATOM 2219 CA ARG A1095 3.244 2.918 209.412 1.00 28.11 C ANISOU 2219 CA ARG A1095 4726 4203 1752 201 -214 290 C ATOM 2220 C ARG A1095 4.632 3.082 210.027 1.00 29.11 C ANISOU 2220 C ARG A1095 4853 4354 1854 240 -262 270 C ATOM 2221 O ARG A1095 4.759 3.432 211.201 1.00 28.50 O ANISOU 2221 O ARG A1095 4785 4298 1747 261 -299 258 O ATOM 2222 CB ARG A1095 2.665 1.552 209.779 1.00 28.91 C ANISOU 2222 CB ARG A1095 4894 4260 1831 221 -202 315 C ATOM 2223 CG ARG A1095 1.175 1.430 209.505 1.00 29.27 C ANISOU 2223 CG ARG A1095 4938 4297 1888 178 -167 334 C ATOM 2224 CD ARG A1095 0.612 0.134 210.059 1.00 29.18 C ANISOU 2224 CD ARG A1095 5001 4243 1845 193 -155 357 C ATOM 2225 NE ARG A1095 -0.840 0.061 209.921 1.00 28.77 N ANISOU 2225 NE ARG A1095 4941 4195 1794 148 -126 376 N ATOM 2226 CZ ARG A1095 -1.466 -0.493 208.887 1.00 29.53 C ANISOU 2226 CZ ARG A1095 5042 4278 1901 110 -97 386 C ATOM 2227 NH1 ARG A1095 -0.766 -1.022 207.893 1.00 29.78 N1+ ANISOU 2227 NH1 ARG A1095 5093 4278 1944 112 -90 376 N1+ ATOM 2228 NH2 ARG A1095 -2.790 -0.517 208.844 1.00 30.38 N ANISOU 2228 NH2 ARG A1095 5136 4404 2002 71 -76 405 N ATOM 2229 N ARG A1096 5.670 2.825 209.235 1.00 29.72 N ANISOU 2229 N ARG A1096 4922 4433 1938 252 -263 265 N ATOM 2230 CA ARG A1096 7.036 3.075 209.677 1.00 29.31 C ANISOU 2230 CA ARG A1096 4857 4419 1861 284 -313 244 C ATOM 2231 C ARG A1096 7.247 4.564 209.901 1.00 31.46 C ANISOU 2231 C ARG A1096 5076 4741 2137 242 -334 212 C ATOM 2232 O ARG A1096 7.931 4.967 210.839 1.00 34.97 O ANISOU 2232 O ARG A1096 5516 5224 2547 258 -390 188 O ATOM 2233 CB ARG A1096 8.052 2.548 208.662 1.00 27.83 C ANISOU 2233 CB ARG A1096 4670 4225 1681 303 -301 250 C ATOM 2234 CG ARG A1096 8.328 1.063 208.773 1.00 29.35 C ANISOU 2234 CG ARG A1096 4925 4376 1849 368 -299 275 C ATOM 2235 CD ARG A1096 9.361 0.618 207.754 1.00 30.43 C ANISOU 2235 CD ARG A1096 5064 4507 1992 394 -282 282 C ATOM 2236 NE ARG A1096 9.627 -0.815 207.837 1.00 31.95 N ANISOU 2236 NE ARG A1096 5327 4654 2157 463 -271 308 N ATOM 2237 CZ ARG A1096 10.471 -1.462 207.041 1.00 33.78 C ANISOU 2237 CZ ARG A1096 5580 4868 2386 505 -248 322 C ATOM 2238 NH1 ARG A1096 11.133 -0.802 206.101 1.00 35.60 N1+ ANISOU 2238 NH1 ARG A1096 5764 5124 2638 483 -235 313 N1+ ATOM 2239 NH2 ARG A1096 10.653 -2.768 207.183 1.00 33.71 N ANISOU 2239 NH2 ARG A1096 5646 4812 2349 574 -233 347 N ATOM 2240 N ALA A1097 6.648 5.378 209.036 1.00 29.76 N ANISOU 2240 N ALA A1097 4826 4524 1959 192 -289 210 N ATOM 2241 CA ALA A1097 6.766 6.826 209.143 1.00 29.69 C ANISOU 2241 CA ALA A1097 4775 4553 1951 153 -294 180 C ATOM 2242 C ALA A1097 6.166 7.321 210.454 1.00 29.02 C ANISOU 2242 C ALA A1097 4704 4481 1840 156 -321 169 C ATOM 2243 O ALA A1097 6.731 8.190 211.116 1.00 30.27 O ANISOU 2243 O ALA A1097 4851 4679 1973 143 -359 133 O ATOM 2244 CB ALA A1097 6.095 7.503 207.960 1.00 21.71 C ANISOU 2244 CB ALA A1097 3733 3531 983 116 -233 188 C ATOM 2245 N ALA A1098 5.025 6.753 210.828 1.00 26.63 N ANISOU 2245 N ALA A1098 4432 4146 1541 170 -301 197 N ATOM 2246 CA ALA A1098 4.362 7.116 212.073 1.00 23.22 C ANISOU 2246 CA ALA A1098 4023 3718 1081 180 -319 193 C ATOM 2247 C ALA A1098 5.235 6.778 213.279 1.00 29.19 C ANISOU 2247 C ALA A1098 4811 4494 1787 223 -385 174 C ATOM 2248 O ALA A1098 5.200 7.473 214.292 1.00 29.84 O ANISOU 2248 O ALA A1098 4904 4598 1837 228 -416 151 O ATOM 2249 CB ALA A1098 3.017 6.418 212.180 1.00 23.17 C ANISOU 2249 CB ALA A1098 4045 3674 1083 185 -283 230 C ATOM 2250 N LEU A1099 6.017 5.709 213.165 1.00 29.66 N ANISOU 2250 N LEU A1099 4889 4547 1834 262 -407 184 N ATOM 2251 CA LEU A1099 6.933 5.320 214.232 1.00 25.32 C ANISOU 2251 CA LEU A1099 4366 4023 1234 316 -476 169 C ATOM 2252 C LEU A1099 8.102 6.297 214.309 1.00 25.56 C ANISOU 2252 C LEU A1099 4352 4113 1247 292 -533 123 C ATOM 2253 O LEU A1099 8.561 6.647 215.395 1.00 26.36 O ANISOU 2253 O LEU A1099 4462 4252 1302 311 -598 93 O ATOM 2254 CB LEU A1099 7.444 3.895 214.017 1.00 25.91 C ANISOU 2254 CB LEU A1099 4473 4073 1299 375 -480 197 C ATOM 2255 CG LEU A1099 8.312 3.320 215.138 1.00 26.76 C ANISOU 2255 CG LEU A1099 4613 4207 1349 453 -550 191 C ATOM 2256 CD1 LEU A1099 7.542 3.303 216.445 1.00 27.35 C ANISOU 2256 CD1 LEU A1099 4737 4270 1386 484 -561 193 C ATOM 2257 CD2 LEU A1099 8.793 1.925 214.784 1.00 27.07 C ANISOU 2257 CD2 LEU A1099 4687 4216 1380 517 -539 223 C ATOM 2258 N ILE A1100 8.579 6.733 213.149 1.00 24.94 N ANISOU 2258 N ILE A1100 4230 4046 1202 247 -509 114 N ATOM 2259 CA ILE A1100 9.621 7.750 213.077 1.00 28.19 C ANISOU 2259 CA ILE A1100 4600 4510 1599 205 -554 65 C ATOM 2260 C ILE A1100 9.089 9.077 213.607 1.00 28.75 C ANISOU 2260 C ILE A1100 4664 4601 1660 155 -551 29 C ATOM 2261 O ILE A1100 9.825 9.863 214.206 1.00 30.29 O ANISOU 2261 O ILE A1100 4847 4843 1819 128 -612 -24 O ATOM 2262 CB ILE A1100 10.129 7.927 211.638 1.00 27.23 C ANISOU 2262 CB ILE A1100 4445 4385 1515 168 -513 68 C ATOM 2263 CG1 ILE A1100 10.610 6.585 211.088 1.00 27.72 C ANISOU 2263 CG1 ILE A1100 4523 4424 1585 225 -507 105 C ATOM 2264 CG2 ILE A1100 11.253 8.949 211.583 1.00 24.69 C ANISOU 2264 CG2 ILE A1100 4093 4115 1174 119 -561 11 C ATOM 2265 CD1 ILE A1100 10.774 6.566 209.591 1.00 27.45 C ANISOU 2265 CD1 ILE A1100 4471 4369 1589 200 -444 120 C ATOM 2266 N ASN A1101 7.800 9.314 213.389 1.00 27.54 N ANISOU 2266 N ASN A1101 4518 4411 1535 146 -483 55 N ATOM 2267 CA ASN A1101 7.128 10.486 213.934 1.00 26.94 C ANISOU 2267 CA ASN A1101 4444 4345 1448 118 -469 30 C ATOM 2268 C ASN A1101 7.228 10.502 215.456 1.00 28.17 C ANISOU 2268 C ASN A1101 4638 4519 1545 150 -534 6 C ATOM 2269 O ASN A1101 7.569 11.522 216.053 1.00 29.97 O ANISOU 2269 O ASN A1101 4863 4786 1738 120 -568 -47 O ATOM 2270 CB ASN A1101 5.661 10.511 213.490 1.00 27.28 C ANISOU 2270 CB ASN A1101 4494 4341 1531 121 -393 74 C ATOM 2271 CG ASN A1101 4.993 11.856 213.722 1.00 28.28 C ANISOU 2271 CG ASN A1101 4618 4474 1654 97 -362 54 C ATOM 2272 OD1 ASN A1101 5.309 12.570 214.672 1.00 30.93 O ANISOU 2272 OD1 ASN A1101 4969 4838 1946 92 -400 11 O ATOM 2273 ND2 ASN A1101 4.059 12.205 212.846 1.00 27.15 N ANISOU 2273 ND2 ASN A1101 4459 4304 1555 85 -295 85 N ATOM 2274 N MET A1102 6.942 9.362 216.079 1.00 28.33 N ANISOU 2274 N MET A1102 4701 4514 1551 211 -549 41 N ATOM 2275 CA MET A1102 6.986 9.257 217.534 1.00 30.06 C ANISOU 2275 CA MET A1102 4964 4746 1710 257 -607 25 C ATOM 2276 C MET A1102 8.407 9.427 218.061 1.00 32.80 C ANISOU 2276 C MET A1102 5295 5156 2011 260 -704 -26 C ATOM 2277 O MET A1102 8.618 10.035 219.110 1.00 34.99 O ANISOU 2277 O MET A1102 5591 5467 2237 261 -759 -69 O ATOM 2278 CB MET A1102 6.411 7.917 217.995 1.00 29.72 C ANISOU 2278 CB MET A1102 4975 4659 1659 327 -594 76 C ATOM 2279 CG MET A1102 4.958 7.707 217.612 1.00 26.49 C ANISOU 2279 CG MET A1102 4583 4193 1288 317 -512 121 C ATOM 2280 SD MET A1102 4.246 6.235 218.370 1.00 33.31 S ANISOU 2280 SD MET A1102 5521 5008 2128 388 -498 168 S ATOM 2281 CE MET A1102 4.207 6.720 220.092 1.00 28.16 C ANISOU 2281 CE MET A1102 4925 4373 1401 437 -549 142 C ATOM 2282 N VAL A1103 9.379 8.890 217.330 1.00 32.38 N ANISOU 2282 N VAL A1103 5208 5119 1975 261 -727 -22 N ATOM 2283 CA VAL A1103 10.783 9.054 217.690 1.00 28.71 C ANISOU 2283 CA VAL A1103 4716 4718 1475 260 -828 -70 C ATOM 2284 C VAL A1103 11.192 10.522 217.571 1.00 31.56 C ANISOU 2284 C VAL A1103 5044 5117 1830 166 -850 -140 C ATOM 2285 O VAL A1103 11.965 11.031 218.382 1.00 33.60 O ANISOU 2285 O VAL A1103 5295 5427 2043 150 -943 -200 O ATOM 2286 CB VAL A1103 11.699 8.183 216.806 1.00 28.56 C ANISOU 2286 CB VAL A1103 4666 4702 1481 287 -841 -46 C ATOM 2287 CG1 VAL A1103 13.164 8.441 217.128 1.00 29.76 C ANISOU 2287 CG1 VAL A1103 4784 4926 1598 312 -961 -104 C ATOM 2288 CG2 VAL A1103 11.366 6.713 216.989 1.00 28.71 C ANISOU 2288 CG2 VAL A1103 4728 4683 1496 381 -818 14 C ATOM 2289 N PHE A1104 10.652 11.201 216.565 1.00 30.89 N ANISOU 2289 N PHE A1104 4940 5007 1788 104 -765 -137 N ATOM 2290 CA PHE A1104 10.926 12.621 216.355 1.00 30.66 C ANISOU 2290 CA PHE A1104 4897 5004 1749 25 -766 -209 C ATOM 2291 C PHE A1104 10.443 13.463 217.529 1.00 31.41 C ANISOU 2291 C PHE A1104 5013 5121 1799 2 -781 -251 C ATOM 2292 O PHE A1104 10.950 14.558 217.768 1.00 32.69 O ANISOU 2292 O PHE A1104 5190 5308 1922 -29 -827 -343 O ATOM 2293 CB PHE A1104 10.264 13.110 215.066 1.00 28.79 C ANISOU 2293 CB PHE A1104 4635 4739 1567 -18 -653 -185 C ATOM 2294 CG PHE A1104 11.215 13.289 213.917 1.00 28.47 C ANISOU 2294 CG PHE A1104 4598 4689 1529 -4 -664 -220 C ATOM 2295 CD1 PHE A1104 11.649 12.201 213.181 1.00 28.73 C ANISOU 2295 CD1 PHE A1104 4624 4705 1589 44 -663 -171 C ATOM 2296 CD2 PHE A1104 11.660 14.552 213.560 1.00 29.82 C ANISOU 2296 CD2 PHE A1104 4785 4870 1674 -30 -668 -308 C ATOM 2297 CE1 PHE A1104 12.520 12.365 212.116 1.00 30.05 C ANISOU 2297 CE1 PHE A1104 4791 4872 1753 76 -667 -204 C ATOM 2298 CE2 PHE A1104 12.530 14.724 212.496 1.00 30.65 C ANISOU 2298 CE2 PHE A1104 4895 4970 1780 -6 -673 -348 C ATOM 2299 CZ PHE A1104 12.960 13.629 211.773 1.00 30.27 C ANISOU 2299 CZ PHE A1104 4830 4914 1756 55 -672 -292 C ATOM 2300 N GLN A1105 9.462 12.946 218.261 1.00 32.06 N ANISOU 2300 N GLN A1105 5140 5172 1870 72 -759 -204 N ATOM 2301 CA GLN A1105 8.847 13.695 219.349 1.00 33.88 C ANISOU 2301 CA GLN A1105 5412 5407 2053 77 -764 -236 C ATOM 2302 C GLN A1105 9.424 13.333 220.713 1.00 36.48 C ANISOU 2302 C GLN A1105 5776 5771 2314 120 -868 -266 C ATOM 2303 O GLN A1105 9.790 14.214 221.490 1.00 37.67 O ANISOU 2303 O GLN A1105 5938 5962 2413 83 -923 -340 O ATOM 2304 CB GLN A1105 7.332 13.472 219.357 1.00 32.66 C ANISOU 2304 CB GLN A1105 5296 5187 1926 126 -676 -168 C ATOM 2305 CG GLN A1105 6.601 14.236 220.450 1.00 32.06 C ANISOU 2305 CG GLN A1105 5276 5102 1803 142 -672 -191 C ATOM 2306 CD GLN A1105 5.101 14.022 220.412 1.00 31.74 C ANISOU 2306 CD GLN A1105 5274 4992 1793 184 -588 -120 C ATOM 2307 OE1 GLN A1105 4.606 13.132 219.724 1.00 32.56 O ANISOU 2307 OE1 GLN A1105 5366 5059 1948 203 -546 -58 O ATOM 2308 NE2 GLN A1105 4.367 14.846 221.150 1.00 32.46 N ANISOU 2308 NE2 GLN A1105 5415 5065 1853 194 -567 -134 N ATOM 2309 N MET A1106 9.509 12.037 220.999 1.00 36.71 N ANISOU 2309 N MET A1106 5823 5784 2339 202 -895 -212 N ATOM 2310 CA MET A1106 9.847 11.577 222.341 1.00 32.13 C ANISOU 2310 CA MET A1106 5285 5233 1691 270 -981 -226 C ATOM 2311 C MET A1106 11.217 10.910 222.453 1.00 33.05 C ANISOU 2311 C MET A1106 5365 5405 1789 299 -1085 -243 C ATOM 2312 O MET A1106 11.727 10.713 223.556 1.00 38.47 O ANISOU 2312 O MET A1106 6072 6135 2411 350 -1177 -270 O ATOM 2313 CB MET A1106 8.771 10.612 222.836 1.00 32.01 C ANISOU 2313 CB MET A1106 5334 5156 1670 360 -927 -155 C ATOM 2314 CG MET A1106 7.434 11.276 223.109 1.00 32.58 C ANISOU 2314 CG MET A1106 5453 5180 1746 350 -850 -141 C ATOM 2315 SD MET A1106 6.088 10.091 223.246 1.00 60.55 S ANISOU 2315 SD MET A1106 9057 8640 5311 428 -770 -51 S ATOM 2316 CE MET A1106 6.003 9.498 221.561 1.00 34.94 C ANISOU 2316 CE MET A1106 5750 5367 2159 388 -702 -5 C ATOM 2317 N GLY A1107 11.811 10.563 221.317 1.00 36.43 N ANISOU 2317 N GLY A1107 5738 5833 2270 277 -1075 -225 N ATOM 2318 CA GLY A1107 13.080 9.857 221.316 1.00 37.19 C ANISOU 2318 CA GLY A1107 5794 5979 2358 320 -1169 -230 C ATOM 2319 C GLY A1107 12.883 8.358 221.450 1.00 39.62 C ANISOU 2319 C GLY A1107 6134 6258 2663 437 -1147 -156 C ATOM 2320 O GLY A1107 11.825 7.903 221.885 1.00 38.62 O ANISOU 2320 O GLY A1107 6071 6078 2523 484 -1084 -115 O ATOM 2321 N GLU A1108 13.905 7.591 221.080 1.00 44.01 N ANISOU 2321 N GLU A1108 6647 6846 3227 485 -1199 -141 N ATOM 2322 CA GLU A1108 13.825 6.132 221.078 1.00 46.43 C ANISOU 2322 CA GLU A1108 6989 7124 3530 596 -1170 -74 C ATOM 2323 C GLU A1108 13.552 5.551 222.462 1.00 47.46 C ANISOU 2323 C GLU A1108 7184 7260 3588 694 -1205 -64 C ATOM 2324 O GLU A1108 12.876 4.531 222.592 1.00 46.41 O ANISOU 2324 O GLU A1108 7116 7070 3449 766 -1140 -8 O ATOM 2325 CB GLU A1108 15.114 5.539 220.513 1.00 50.98 C ANISOU 2325 CB GLU A1108 7507 7750 4113 663 -1234 -74 C ATOM 2326 CG GLU A1108 15.819 6.454 219.535 1.00 55.98 C ANISOU 2326 CG GLU A1108 8074 8420 4777 629 -1268 -136 C ATOM 2327 CD GLU A1108 16.983 5.781 218.843 1.00 62.16 C ANISOU 2327 CD GLU A1108 8796 9258 5565 743 -1319 -137 C ATOM 2328 OE1 GLU A1108 17.455 4.737 219.346 1.00 61.90 O ANISOU 2328 OE1 GLU A1108 8768 9253 5497 858 -1358 -103 O ATOM 2329 OE2 GLU A1108 17.424 6.296 217.794 1.00 66.67 O1+ ANISOU 2329 OE2 GLU A1108 9313 9848 6170 726 -1316 -172 O1+ ATOM 2330 N THR A1109 14.083 6.203 223.491 1.00 49.02 N ANISOU 2330 N THR A1109 7370 7526 3728 694 -1308 -121 N ATOM 2331 CA THR A1109 13.860 5.773 224.866 1.00 51.92 C ANISOU 2331 CA THR A1109 7806 7906 4017 789 -1347 -118 C ATOM 2332 C THR A1109 12.383 5.875 225.243 1.00 50.41 C ANISOU 2332 C THR A1109 7701 7633 3820 784 -1249 -92 C ATOM 2333 O THR A1109 11.838 4.993 225.908 1.00 50.21 O ANISOU 2333 O THR A1109 7752 7568 3757 878 -1219 -50 O ATOM 2334 CB THR A1109 14.697 6.603 225.856 1.00 57.11 C ANISOU 2334 CB THR A1109 8430 8657 4612 774 -1482 -195 C ATOM 2335 OG1 THR A1109 14.514 7.998 225.583 1.00 60.98 O ANISOU 2335 OG1 THR A1109 8895 9151 5126 641 -1479 -256 O ATOM 2336 CG2 THR A1109 16.172 6.262 225.718 1.00 57.29 C ANISOU 2336 CG2 THR A1109 8365 8770 4634 812 -1597 -213 C ATOM 2337 N GLY A1110 11.740 6.954 224.807 1.00 49.13 N ANISOU 2337 N GLY A1110 7528 7446 3695 678 -1198 -116 N ATOM 2338 CA GLY A1110 10.331 7.165 225.081 1.00 47.68 C ANISOU 2338 CA GLY A1110 7411 7190 3515 670 -1108 -91 C ATOM 2339 C GLY A1110 9.435 6.217 224.306 1.00 45.42 C ANISOU 2339 C GLY A1110 7150 6821 3285 690 -999 -18 C ATOM 2340 O GLY A1110 8.462 5.693 224.847 1.00 45.64 O ANISOU 2340 O GLY A1110 7251 6793 3297 740 -946 20 O ATOM 2341 N VAL A1111 9.762 6.002 223.034 1.00 42.76 N ANISOU 2341 N VAL A1111 6757 6477 3013 646 -967 -2 N ATOM 2342 CA VAL A1111 8.996 5.098 222.184 1.00 39.85 C ANISOU 2342 CA VAL A1111 6408 6036 2698 654 -871 59 C ATOM 2343 C VAL A1111 9.095 3.665 222.701 1.00 40.87 C ANISOU 2343 C VAL A1111 6598 6141 2790 764 -873 101 C ATOM 2344 O VAL A1111 8.124 2.908 222.656 1.00 42.24 O ANISOU 2344 O VAL A1111 6828 6245 2977 787 -798 146 O ATOM 2345 CB VAL A1111 9.478 5.154 220.718 1.00 38.77 C ANISOU 2345 CB VAL A1111 6203 5902 2627 592 -844 63 C ATOM 2346 CG1 VAL A1111 8.663 4.211 219.850 1.00 37.90 C ANISOU 2346 CG1 VAL A1111 6117 5718 2566 595 -751 120 C ATOM 2347 CG2 VAL A1111 9.384 6.574 220.184 1.00 37.58 C ANISOU 2347 CG2 VAL A1111 5999 5771 2508 488 -834 22 C ATOM 2348 N ALA A1112 10.269 3.307 223.214 1.00 39.70 N ANISOU 2348 N ALA A1112 6438 6054 2593 834 -961 85 N ATOM 2349 CA ALA A1112 10.490 1.977 223.772 1.00 39.75 C ANISOU 2349 CA ALA A1112 6505 6046 2553 955 -967 123 C ATOM 2350 C ALA A1112 9.688 1.765 225.055 1.00 40.75 C ANISOU 2350 C ALA A1112 6723 6142 2619 1019 -957 133 C ATOM 2351 O ALA A1112 9.561 0.640 225.539 1.00 36.44 O ANISOU 2351 O ALA A1112 6249 5562 2034 1117 -936 172 O ATOM 2352 CB ALA A1112 11.970 1.754 224.033 1.00 40.30 C ANISOU 2352 CB ALA A1112 6528 6201 2582 1020 -1072 102 C ATOM 2353 N GLY A1113 9.152 2.852 225.603 1.00 40.39 N ANISOU 2353 N GLY A1113 6681 6105 2560 967 -967 100 N ATOM 2354 CA GLY A1113 8.325 2.783 226.793 1.00 41.01 C ANISOU 2354 CA GLY A1113 6850 6152 2582 1023 -952 109 C ATOM 2355 C GLY A1113 6.955 2.189 226.521 1.00 39.92 C ANISOU 2355 C GLY A1113 6771 5918 2480 1014 -839 163 C ATOM 2356 O GLY A1113 6.350 1.576 227.400 1.00 40.36 O ANISOU 2356 O GLY A1113 6915 5932 2488 1089 -812 191 O ATOM 2357 N PHE A1114 6.465 2.369 225.298 1.00 39.15 N ANISOU 2357 N PHE A1114 6624 5788 2465 922 -774 177 N ATOM 2358 CA PHE A1114 5.167 1.830 224.904 1.00 40.08 C ANISOU 2358 CA PHE A1114 6781 5825 2622 897 -674 224 C ATOM 2359 C PHE A1114 5.250 0.333 224.635 1.00 44.17 C ANISOU 2359 C PHE A1114 7347 6298 3137 957 -639 268 C ATOM 2360 O PHE A1114 4.935 -0.118 223.536 1.00 43.99 O ANISOU 2360 O PHE A1114 7302 6239 3173 904 -583 292 O ATOM 2361 CB PHE A1114 4.639 2.542 223.657 1.00 37.61 C ANISOU 2361 CB PHE A1114 6397 5502 2393 781 -625 222 C ATOM 2362 CG PHE A1114 4.356 4.001 223.860 1.00 36.88 C ANISOU 2362 CG PHE A1114 6269 5438 2304 722 -638 185 C ATOM 2363 CD1 PHE A1114 5.344 4.948 223.645 1.00 36.82 C ANISOU 2363 CD1 PHE A1114 6198 5495 2297 684 -701 135 C ATOM 2364 CD2 PHE A1114 3.099 4.428 224.254 1.00 36.56 C ANISOU 2364 CD2 PHE A1114 6264 5361 2265 704 -585 201 C ATOM 2365 CE1 PHE A1114 5.087 6.294 223.827 1.00 36.45 C ANISOU 2365 CE1 PHE A1114 6131 5470 2250 628 -707 99 C ATOM 2366 CE2 PHE A1114 2.834 5.772 224.438 1.00 36.62 C ANISOU 2366 CE2 PHE A1114 6250 5391 2274 657 -591 169 C ATOM 2367 CZ PHE A1114 3.830 6.706 224.224 1.00 36.67 C ANISOU 2367 CZ PHE A1114 6199 5455 2277 619 -650 117 C ATOM 2368 N THR A1115 5.663 -0.432 225.641 1.00 45.60 N ANISOU 2368 N THR A1115 7599 6481 3245 1069 -669 279 N ATOM 2369 CA THR A1115 5.899 -1.863 225.474 1.00 46.49 C ANISOU 2369 CA THR A1115 7767 6553 3343 1143 -638 319 C ATOM 2370 C THR A1115 4.663 -2.596 224.957 1.00 44.67 C ANISOU 2370 C THR A1115 7587 6235 3152 1100 -536 363 C ATOM 2371 O THR A1115 4.748 -3.373 224.007 1.00 34.15 O ANISOU 2371 O THR A1115 6252 4868 1855 1080 -496 385 O ATOM 2372 CB THR A1115 6.356 -2.513 226.794 1.00 48.22 C ANISOU 2372 CB THR A1115 8070 6784 3468 1283 -678 328 C ATOM 2373 OG1 THR A1115 5.287 -2.474 227.747 1.00 48.16 O ANISOU 2373 OG1 THR A1115 8144 6732 3424 1305 -638 342 O ATOM 2374 CG2 THR A1115 7.562 -1.778 227.356 1.00 50.20 C ANISOU 2374 CG2 THR A1115 8268 7135 3673 1321 -792 280 C ATOM 2375 N ASN A1116 3.518 -2.336 225.577 1.00 44.56 N ANISOU 2375 N ASN A1116 7618 6187 3127 1083 -495 375 N ATOM 2376 CA ASN A1116 2.272 -2.974 225.173 1.00 42.85 C ANISOU 2376 CA ASN A1116 7442 5897 2941 1033 -404 415 C ATOM 2377 C ASN A1116 1.910 -2.667 223.724 1.00 39.37 C ANISOU 2377 C ASN A1116 6918 5454 2585 913 -372 412 C ATOM 2378 O ASN A1116 1.757 -3.577 222.912 1.00 38.38 O ANISOU 2378 O ASN A1116 6809 5287 2486 890 -327 436 O ATOM 2379 CB ASN A1116 1.127 -2.544 226.093 1.00 43.67 C ANISOU 2379 CB ASN A1116 7593 5981 3020 1031 -373 426 C ATOM 2380 CG ASN A1116 1.075 -3.351 227.375 1.00 46.79 C ANISOU 2380 CG ASN A1116 8105 6341 3331 1151 -363 450 C ATOM 2381 OD1 ASN A1116 1.369 -4.546 227.382 1.00 48.71 O ANISOU 2381 OD1 ASN A1116 8413 6546 3549 1214 -339 477 O ATOM 2382 ND2 ASN A1116 0.701 -2.699 228.469 1.00 49.04 N ANISOU 2382 ND2 ASN A1116 8426 6637 3569 1188 -377 441 N ATOM 2383 N SER A1117 1.788 -1.381 223.410 1.00 37.09 N ANISOU 2383 N SER A1117 6549 5211 2335 841 -394 382 N ATOM 2384 CA SER A1117 1.357 -0.945 222.086 1.00 33.74 C ANISOU 2384 CA SER A1117 6045 4790 1985 733 -362 380 C ATOM 2385 C SER A1117 2.281 -1.446 220.983 1.00 33.20 C ANISOU 2385 C SER A1117 5940 4726 1949 723 -372 375 C ATOM 2386 O SER A1117 1.819 -1.827 219.909 1.00 33.92 O ANISOU 2386 O SER A1117 6012 4790 2085 660 -326 390 O ATOM 2387 CB SER A1117 1.264 0.581 222.035 1.00 30.19 C ANISOU 2387 CB SER A1117 5522 4388 1559 678 -387 347 C ATOM 2388 OG SER A1117 0.275 1.058 222.931 1.00 35.31 O ANISOU 2388 OG SER A1117 6207 5026 2183 683 -366 355 O ATOM 2389 N LEU A1118 3.583 -1.451 221.256 1.00 30.87 N ANISOU 2389 N LEU A1118 5636 4469 1625 787 -434 354 N ATOM 2390 CA LEU A1118 4.572 -1.900 220.281 1.00 30.61 C ANISOU 2390 CA LEU A1118 5569 4445 1615 790 -446 351 C ATOM 2391 C LEU A1118 4.384 -3.368 219.908 1.00 31.97 C ANISOU 2391 C LEU A1118 5815 4551 1782 823 -392 389 C ATOM 2392 O LEU A1118 4.481 -3.736 218.736 1.00 31.09 O ANISOU 2392 O LEU A1118 5683 4419 1712 779 -362 396 O ATOM 2393 CB LEU A1118 5.987 -1.676 220.814 1.00 31.39 C ANISOU 2393 CB LEU A1118 5647 4608 1673 863 -529 325 C ATOM 2394 CG LEU A1118 6.487 -0.232 220.803 1.00 31.09 C ANISOU 2394 CG LEU A1118 5523 4641 1648 811 -587 279 C ATOM 2395 CD1 LEU A1118 7.899 -0.152 221.360 1.00 32.55 C ANISOU 2395 CD1 LEU A1118 5686 4897 1785 882 -677 254 C ATOM 2396 CD2 LEU A1118 6.423 0.343 219.399 1.00 29.83 C ANISOU 2396 CD2 LEU A1118 5287 4484 1561 713 -556 271 C ATOM 2397 N ARG A1119 4.118 -4.201 220.908 1.00 33.18 N ANISOU 2397 N ARG A1119 6063 4667 1878 901 -378 414 N ATOM 2398 CA ARG A1119 3.883 -5.620 220.675 1.00 32.22 C ANISOU 2398 CA ARG A1119 6029 4471 1742 935 -319 451 C ATOM 2399 C ARG A1119 2.651 -5.826 219.805 1.00 31.39 C ANISOU 2399 C ARG A1119 5925 4318 1685 828 -250 466 C ATOM 2400 O ARG A1119 2.659 -6.638 218.883 1.00 33.35 O ANISOU 2400 O ARG A1119 6197 4521 1952 805 -210 479 O ATOM 2401 CB ARG A1119 3.721 -6.366 222.000 1.00 33.51 C ANISOU 2401 CB ARG A1119 6299 4601 1830 1040 -310 475 C ATOM 2402 CG ARG A1119 3.341 -7.828 221.838 1.00 34.01 C ANISOU 2402 CG ARG A1119 6471 4577 1874 1070 -236 515 C ATOM 2403 CD ARG A1119 3.145 -8.519 223.181 1.00 38.03 C ANISOU 2403 CD ARG A1119 7093 5050 2307 1179 -218 541 C ATOM 2404 NE ARG A1119 2.082 -7.905 223.973 1.00 35.37 N ANISOU 2404 NE ARG A1119 6763 4714 1960 1145 -206 543 N ATOM 2405 CZ ARG A1119 2.294 -7.090 225.002 1.00 39.59 C ANISOU 2405 CZ ARG A1119 7283 5302 2458 1196 -261 523 C ATOM 2406 NH1 ARG A1119 3.533 -6.794 225.371 1.00 40.08 N1+ ANISOU 2406 NH1 ARG A1119 7315 5425 2487 1277 -338 499 N1+ ATOM 2407 NH2 ARG A1119 1.269 -6.573 225.666 1.00 39.90 N ANISOU 2407 NH2 ARG A1119 7338 5333 2488 1167 -240 528 N ATOM 2408 N MET A1120 1.596 -5.075 220.098 1.00 31.02 N ANISOU 2408 N MET A1120 5851 4282 1652 766 -237 464 N ATOM 2409 CA MET A1120 0.350 -5.180 219.352 1.00 35.24 C ANISOU 2409 CA MET A1120 6373 4789 2226 664 -180 480 C ATOM 2410 C MET A1120 0.522 -4.694 217.916 1.00 35.57 C ANISOU 2410 C MET A1120 6327 4858 2332 583 -183 461 C ATOM 2411 O MET A1120 -0.093 -5.231 216.996 1.00 35.84 O ANISOU 2411 O MET A1120 6366 4861 2390 519 -139 473 O ATOM 2412 CB MET A1120 -0.753 -4.391 220.056 1.00 34.80 C ANISOU 2412 CB MET A1120 6302 4754 2167 630 -169 485 C ATOM 2413 CG MET A1120 -0.893 -4.753 221.523 1.00 36.62 C ANISOU 2413 CG MET A1120 6623 4961 2331 718 -167 502 C ATOM 2414 SD MET A1120 -1.882 -3.582 222.464 1.00 44.61 S ANISOU 2414 SD MET A1120 7613 6005 3331 700 -167 500 S ATOM 2415 CE MET A1120 -3.514 -3.975 221.861 1.00 40.07 C ANISOU 2415 CE MET A1120 7034 5407 2784 597 -89 538 C ATOM 2416 N LEU A1121 1.358 -3.676 217.728 1.00 36.32 N ANISOU 2416 N LEU A1121 6344 5010 2448 585 -233 430 N ATOM 2417 CA LEU A1121 1.692 -3.210 216.387 1.00 27.94 C ANISOU 2417 CA LEU A1121 5204 3971 1441 523 -234 412 C ATOM 2418 C LEU A1121 2.503 -4.271 215.662 1.00 39.45 C ANISOU 2418 C LEU A1121 6702 5392 2896 556 -223 419 C ATOM 2419 O LEU A1121 2.306 -4.523 214.474 1.00 40.15 O ANISOU 2419 O LEU A1121 6774 5460 3019 501 -191 420 O ATOM 2420 CB LEU A1121 2.474 -1.897 216.435 1.00 27.59 C ANISOU 2420 CB LEU A1121 5078 3992 1412 520 -287 378 C ATOM 2421 CG LEU A1121 1.706 -0.617 216.757 1.00 27.18 C ANISOU 2421 CG LEU A1121 4975 3976 1376 471 -290 365 C ATOM 2422 CD1 LEU A1121 2.664 0.559 216.819 1.00 27.01 C ANISOU 2422 CD1 LEU A1121 4890 4011 1361 472 -342 328 C ATOM 2423 CD2 LEU A1121 0.617 -0.369 215.725 1.00 26.36 C ANISOU 2423 CD2 LEU A1121 4828 3869 1320 384 -242 376 C ATOM 2424 N GLN A1122 3.416 -4.895 216.397 1.00 39.92 N ANISOU 2424 N GLN A1122 6816 5442 2909 653 -247 425 N ATOM 2425 CA GLN A1122 4.262 -5.942 215.850 1.00 40.74 C ANISOU 2425 CA GLN A1122 6968 5511 3001 706 -234 436 C ATOM 2426 C GLN A1122 3.414 -7.140 215.419 1.00 39.85 C ANISOU 2426 C GLN A1122 6943 5313 2884 679 -165 463 C ATOM 2427 O GLN A1122 3.812 -7.914 214.550 1.00 38.92 O ANISOU 2427 O GLN A1122 6862 5153 2773 685 -136 469 O ATOM 2428 CB GLN A1122 5.315 -6.357 216.883 1.00 43.79 C ANISOU 2428 CB GLN A1122 7397 5913 3329 831 -276 442 C ATOM 2429 CG GLN A1122 6.634 -6.826 216.294 1.00 45.95 C ANISOU 2429 CG GLN A1122 7665 6197 3596 894 -291 444 C ATOM 2430 CD GLN A1122 6.570 -8.247 215.783 1.00 49.24 C ANISOU 2430 CD GLN A1122 8183 6528 3999 927 -226 473 C ATOM 2431 OE1 GLN A1122 5.881 -9.092 216.355 1.00 51.65 O ANISOU 2431 OE1 GLN A1122 8584 6770 4271 951 -184 497 O ATOM 2432 NE2 GLN A1122 7.283 -8.519 214.694 1.00 50.95 N ANISOU 2432 NE2 GLN A1122 8385 6736 4237 928 -212 473 N ATOM 2433 N GLN A1123 2.233 -7.271 216.016 1.00 39.27 N ANISOU 2433 N GLN A1123 6908 5215 2797 647 -136 478 N ATOM 2434 CA GLN A1123 1.350 -8.399 215.740 1.00 38.73 C ANISOU 2434 CA GLN A1123 6928 5069 2717 612 -71 502 C ATOM 2435 C GLN A1123 0.212 -8.044 214.785 1.00 38.23 C ANISOU 2435 C GLN A1123 6814 5014 2698 488 -44 497 C ATOM 2436 O GLN A1123 -0.715 -8.833 214.602 1.00 39.79 O ANISOU 2436 O GLN A1123 7074 5161 2885 439 6 515 O ATOM 2437 CB GLN A1123 0.775 -8.946 217.047 1.00 38.83 C ANISOU 2437 CB GLN A1123 7029 5047 2676 662 -48 529 C ATOM 2438 CG GLN A1123 1.813 -9.561 217.969 1.00 39.02 C ANISOU 2438 CG GLN A1123 7128 5054 2644 799 -65 540 C ATOM 2439 CD GLN A1123 1.226 -9.983 219.297 1.00 38.93 C ANISOU 2439 CD GLN A1123 7203 5011 2577 855 -42 566 C ATOM 2440 OE1 GLN A1123 0.034 -9.803 219.546 1.00 38.55 O ANISOU 2440 OE1 GLN A1123 7159 4956 2534 788 -11 577 O ATOM 2441 NE2 GLN A1123 2.062 -10.547 220.160 1.00 39.58 N ANISOU 2441 NE2 GLN A1123 7356 5080 2602 986 -54 578 N ATOM 2442 N LYS A1124 0.288 -6.856 214.190 1.00 38.62 N ANISOU 2442 N LYS A1124 6751 5129 2793 440 -76 474 N ATOM 2443 CA LYS A1124 -0.697 -6.396 213.208 1.00 40.02 C ANISOU 2443 CA LYS A1124 6866 5328 3011 337 -56 468 C ATOM 2444 C LYS A1124 -2.118 -6.295 213.771 1.00 40.61 C ANISOU 2444 C LYS A1124 6943 5414 3074 287 -32 489 C ATOM 2445 O LYS A1124 -3.094 -6.508 213.050 1.00 40.37 O ANISOU 2445 O LYS A1124 6902 5381 3054 210 -2 496 O ATOM 2446 CB LYS A1124 -0.697 -7.316 211.983 1.00 43.34 C ANISOU 2446 CB LYS A1124 7332 5693 3440 299 -21 467 C ATOM 2447 CG LYS A1124 0.599 -7.317 211.188 1.00 45.39 C ANISOU 2447 CG LYS A1124 7579 5949 3718 338 -37 449 C ATOM 2448 CD LYS A1124 0.825 -8.666 210.517 1.00 50.37 C ANISOU 2448 CD LYS A1124 8314 6493 4330 345 5 456 C ATOM 2449 CE LYS A1124 -0.445 -9.182 209.855 1.00 54.83 C ANISOU 2449 CE LYS A1124 8914 7021 4896 248 46 459 C ATOM 2450 NZ LYS A1124 -0.298 -9.310 208.379 1.00 52.96 N1+ ANISOU 2450 NZ LYS A1124 8675 6764 4685 200 60 440 N1+ ATOM 2451 N ARG A1125 -2.234 -5.974 215.056 1.00 40.96 N ANISOU 2451 N ARG A1125 7001 5473 3090 334 -45 498 N ATOM 2452 CA ARG A1125 -3.538 -5.724 215.663 1.00 41.93 C ANISOU 2452 CA ARG A1125 7117 5615 3199 294 -21 520 C ATOM 2453 C ARG A1125 -3.776 -4.223 215.761 1.00 41.40 C ANISOU 2453 C ARG A1125 6946 5623 3160 273 -51 506 C ATOM 2454 O ARG A1125 -3.741 -3.648 216.848 1.00 43.79 O ANISOU 2454 O ARG A1125 7253 5942 3442 317 -69 505 O ATOM 2455 CB ARG A1125 -3.632 -6.377 217.041 1.00 29.28 C ANISOU 2455 CB ARG A1125 5613 3970 1541 362 -6 544 C ATOM 2456 CG ARG A1125 -3.620 -7.896 217.003 1.00 31.62 C ANISOU 2456 CG ARG A1125 6026 4183 1804 379 40 565 C ATOM 2457 CD ARG A1125 -2.925 -8.466 218.221 1.00 31.03 C ANISOU 2457 CD ARG A1125 6048 4066 1676 494 37 577 C ATOM 2458 NE ARG A1125 -3.593 -8.075 219.456 1.00 33.22 N ANISOU 2458 NE ARG A1125 6341 4359 1921 521 42 594 N ATOM 2459 CZ ARG A1125 -3.039 -8.160 220.659 1.00 32.31 C ANISOU 2459 CZ ARG A1125 6287 4230 1758 629 26 599 C ATOM 2460 NH1 ARG A1125 -1.801 -8.613 220.788 1.00 32.74 N1+ ANISOU 2460 NH1 ARG A1125 6382 4266 1791 721 -1 589 N1+ ATOM 2461 NH2 ARG A1125 -3.719 -7.784 221.731 1.00 32.76 N ANISOU 2461 NH2 ARG A1125 6364 4297 1785 650 36 614 N ATOM 2462 N TRP A1126 -4.023 -3.601 214.612 1.00 38.33 N ANISOU 2462 N TRP A1126 6473 5275 2816 211 -52 493 N ATOM 2463 CA TRP A1126 -4.062 -2.147 214.497 1.00 34.99 C ANISOU 2463 CA TRP A1126 5956 4916 2424 195 -76 476 C ATOM 2464 C TRP A1126 -5.157 -1.504 215.342 1.00 36.61 C ANISOU 2464 C TRP A1126 6143 5156 2613 183 -62 496 C ATOM 2465 O TRP A1126 -4.912 -0.513 216.030 1.00 36.40 O ANISOU 2465 O TRP A1126 6094 5152 2585 212 -86 482 O ATOM 2466 CB TRP A1126 -4.247 -1.738 213.033 1.00 32.89 C ANISOU 2466 CB TRP A1126 5614 4681 2202 138 -69 466 C ATOM 2467 CG TRP A1126 -3.406 -2.519 212.062 1.00 31.65 C ANISOU 2467 CG TRP A1126 5485 4483 2058 140 -69 452 C ATOM 2468 CD1 TRP A1126 -3.854 -3.280 211.021 1.00 31.08 C ANISOU 2468 CD1 TRP A1126 5431 4387 1991 94 -42 457 C ATOM 2469 CD2 TRP A1126 -1.976 -2.619 212.045 1.00 31.39 C ANISOU 2469 CD2 TRP A1126 5471 4427 2027 193 -96 430 C ATOM 2470 NE1 TRP A1126 -2.793 -3.842 210.355 1.00 31.08 N ANISOU 2470 NE1 TRP A1126 5466 4343 1998 116 -47 440 N ATOM 2471 CE2 TRP A1126 -1.630 -3.454 210.963 1.00 31.13 C ANISOU 2471 CE2 TRP A1126 5469 4355 2004 179 -79 427 C ATOM 2472 CE3 TRP A1126 -0.956 -2.084 212.837 1.00 32.20 C ANISOU 2472 CE3 TRP A1126 5569 4545 2122 251 -135 414 C ATOM 2473 CZ2 TRP A1126 -0.307 -3.766 210.655 1.00 30.96 C ANISOU 2473 CZ2 TRP A1126 5469 4309 1984 226 -95 413 C ATOM 2474 CZ3 TRP A1126 0.356 -2.396 212.529 1.00 32.41 C ANISOU 2474 CZ3 TRP A1126 5610 4557 2149 295 -156 400 C ATOM 2475 CH2 TRP A1126 0.669 -3.229 211.448 1.00 31.54 C ANISOU 2475 CH2 TRP A1126 5526 4408 2049 285 -133 401 C ATOM 2476 N ASP A1127 -6.360 -2.064 215.279 1.00 38.44 N ANISOU 2476 N ASP A1127 6385 5391 2828 141 -23 529 N ATOM 2477 CA ASP A1127 -7.501 -1.504 215.995 1.00 41.25 C ANISOU 2477 CA ASP A1127 6719 5788 3166 127 -3 556 C ATOM 2478 C ASP A1127 -7.269 -1.482 217.502 1.00 38.91 C ANISOU 2478 C ASP A1127 6495 5460 2830 193 -9 560 C ATOM 2479 O ASP A1127 -7.476 -0.460 218.156 1.00 38.96 O ANISOU 2479 O ASP A1127 6478 5493 2832 210 -19 556 O ATOM 2480 CB ASP A1127 -8.770 -2.294 215.671 1.00 48.79 C ANISOU 2480 CB ASP A1127 7680 6756 4104 72 43 596 C ATOM 2481 CG ASP A1127 -9.203 -2.133 214.227 1.00 54.27 C ANISOU 2481 CG ASP A1127 8296 7495 4829 17 48 594 C ATOM 2482 OD1 ASP A1127 -8.633 -2.820 213.352 1.00 59.58 O1+ ANISOU 2482 OD1 ASP A1127 8995 8127 5515 3 44 574 O1+ ATOM 2483 OD2 ASP A1127 -10.115 -1.319 213.967 1.00 52.35 O ANISOU 2483 OD2 ASP A1127 7973 7326 4592 -6 58 612 O ATOM 2484 N GLU A1128 -6.829 -2.612 218.043 1.00 36.02 N ANISOU 2484 N GLU A1128 6224 5031 2430 236 -2 567 N ATOM 2485 CA GLU A1128 -6.604 -2.743 219.476 1.00 33.39 C ANISOU 2485 CA GLU A1128 5972 4664 2050 314 -6 573 C ATOM 2486 C GLU A1128 -5.434 -1.878 219.938 1.00 30.50 C ANISOU 2486 C GLU A1128 5595 4308 1686 378 -62 533 C ATOM 2487 O GLU A1128 -5.478 -1.285 221.016 1.00 29.33 O ANISOU 2487 O GLU A1128 5472 4164 1508 427 -74 530 O ATOM 2488 CB GLU A1128 -6.362 -4.209 219.841 1.00 33.03 C ANISOU 2488 CB GLU A1128 6036 4547 1965 354 19 592 C ATOM 2489 N ALA A1129 -4.390 -1.807 219.118 1.00 30.40 N ANISOU 2489 N ALA A1129 5546 4301 1704 377 -96 504 N ATOM 2490 CA ALA A1129 -3.228 -0.973 219.423 1.00 31.90 C ANISOU 2490 CA ALA A1129 5712 4512 1895 425 -151 466 C ATOM 2491 C ALA A1129 -3.584 0.510 219.362 1.00 31.83 C ANISOU 2491 C ALA A1129 5629 4553 1913 388 -161 449 C ATOM 2492 O ALA A1129 -2.972 1.336 220.039 1.00 32.15 O ANISOU 2492 O ALA A1129 5669 4610 1937 428 -200 421 O ATOM 2493 CB ALA A1129 -2.087 -1.281 218.468 1.00 27.93 C ANISOU 2493 CB ALA A1129 5184 4009 1421 426 -176 445 C ATOM 2494 N ALA A1130 -4.577 0.838 218.542 1.00 30.71 N ANISOU 2494 N ALA A1130 5427 4436 1805 315 -127 464 N ATOM 2495 CA ALA A1130 -5.040 2.212 218.409 1.00 30.88 C ANISOU 2495 CA ALA A1130 5383 4500 1849 284 -125 455 C ATOM 2496 C ALA A1130 -5.753 2.662 219.675 1.00 33.21 C ANISOU 2496 C ALA A1130 5722 4793 2104 316 -113 468 C ATOM 2497 O ALA A1130 -5.536 3.772 220.164 1.00 33.78 O ANISOU 2497 O ALA A1130 5785 4878 2170 336 -132 445 O ATOM 2498 CB ALA A1130 -5.960 2.346 217.206 1.00 31.64 C ANISOU 2498 CB ALA A1130 5407 4632 1984 209 -92 475 C ATOM 2499 N VAL A1131 -6.606 1.787 220.198 1.00 34.60 N ANISOU 2499 N VAL A1131 5950 4948 2249 321 -77 506 N ATOM 2500 CA VAL A1131 -7.372 2.076 221.404 1.00 35.26 C ANISOU 2500 CA VAL A1131 6084 5024 2290 357 -55 526 C ATOM 2501 C VAL A1131 -6.459 2.218 222.614 1.00 35.90 C ANISOU 2501 C VAL A1131 6240 5076 2326 447 -93 499 C ATOM 2502 O VAL A1131 -6.610 3.142 223.416 1.00 29.54 O ANISOU 2502 O VAL A1131 5451 4276 1497 480 -99 488 O ATOM 2503 CB VAL A1131 -8.414 0.978 221.679 1.00 29.09 C ANISOU 2503 CB VAL A1131 5347 4225 1480 342 -3 577 C ATOM 2504 CG1 VAL A1131 -9.110 1.221 223.008 1.00 29.91 C ANISOU 2504 CG1 VAL A1131 5515 4314 1534 392 24 599 C ATOM 2505 CG2 VAL A1131 -9.426 0.918 220.545 1.00 28.54 C ANISOU 2505 CG2 VAL A1131 5195 4205 1443 251 30 606 C ATOM 2506 N ASN A1132 -5.503 1.303 222.734 1.00 35.22 N ANISOU 2506 N ASN A1132 6198 4960 2222 492 -120 489 N ATOM 2507 CA ASN A1132 -4.575 1.309 223.856 1.00 34.05 C ANISOU 2507 CA ASN A1132 6119 4797 2022 585 -164 466 C ATOM 2508 C ASN A1132 -3.703 2.557 223.882 1.00 34.20 C ANISOU 2508 C ASN A1132 6092 4854 2049 590 -220 417 C ATOM 2509 O ASN A1132 -3.366 3.065 224.952 1.00 35.16 O ANISOU 2509 O ASN A1132 6258 4979 2121 651 -252 397 O ATOM 2510 CB ASN A1132 -3.694 0.063 223.822 1.00 33.16 C ANISOU 2510 CB ASN A1132 6055 4655 1890 632 -181 469 C ATOM 2511 CG ASN A1132 -2.686 0.037 224.947 1.00 34.90 C ANISOU 2511 CG ASN A1132 6337 4875 2050 736 -234 446 C ATOM 2512 OD1 ASN A1132 -3.026 -0.257 226.093 1.00 37.22 O ANISOU 2512 OD1 ASN A1132 6715 5143 2285 805 -221 463 O ATOM 2513 ND2 ASN A1132 -1.435 0.346 224.628 1.00 34.63 N ANISOU 2513 ND2 ASN A1132 6261 4873 2023 750 -296 409 N ATOM 2514 N LEU A1133 -3.343 3.050 222.702 1.00 34.46 N ANISOU 2514 N LEU A1133 6039 4916 2139 526 -231 399 N ATOM 2515 CA LEU A1133 -2.514 4.246 222.593 1.00 34.31 C ANISOU 2515 CA LEU A1133 5973 4933 2129 518 -277 353 C ATOM 2516 C LEU A1133 -3.292 5.508 222.964 1.00 33.36 C ANISOU 2516 C LEU A1133 5844 4825 2006 501 -257 348 C ATOM 2517 O LEU A1133 -2.705 6.514 223.366 1.00 31.52 O ANISOU 2517 O LEU A1133 5608 4613 1755 513 -295 309 O ATOM 2518 CB LEU A1133 -1.943 4.370 221.180 1.00 33.16 C ANISOU 2518 CB LEU A1133 5746 4810 2044 458 -284 339 C ATOM 2519 CG LEU A1133 -0.603 3.676 220.923 1.00 33.36 C ANISOU 2519 CG LEU A1133 5772 4840 2064 488 -329 322 C ATOM 2520 CD1 LEU A1133 -0.305 3.593 219.437 1.00 27.27 C ANISOU 2520 CD1 LEU A1133 4931 4079 1353 429 -316 320 C ATOM 2521 CD2 LEU A1133 0.511 4.416 221.643 1.00 34.33 C ANISOU 2521 CD2 LEU A1133 5896 5000 2149 527 -398 277 C ATOM 2522 N ALA A1134 -4.615 5.444 222.842 1.00 33.86 N ANISOU 2522 N ALA A1134 5905 4877 2082 471 -198 387 N ATOM 2523 CA ALA A1134 -5.478 6.567 223.194 1.00 34.36 C ANISOU 2523 CA ALA A1134 5966 4949 2141 463 -169 390 C ATOM 2524 C ALA A1134 -5.691 6.671 224.704 1.00 38.46 C ANISOU 2524 C ALA A1134 6578 5444 2592 538 -172 391 C ATOM 2525 O ALA A1134 -6.484 7.487 225.173 1.00 41.08 O ANISOU 2525 O ALA A1134 6927 5773 2908 546 -141 399 O ATOM 2526 CB ALA A1134 -6.815 6.444 222.485 1.00 33.36 C ANISOU 2526 CB ALA A1134 5795 4833 2048 406 -108 436 C ATOM 2527 N LYS A1135 -4.984 5.839 225.460 1.00 37.09 N ANISOU 2527 N LYS A1135 6467 5252 2372 602 -207 384 N ATOM 2528 CA LYS A1135 -5.090 5.847 226.914 1.00 36.80 C ANISOU 2528 CA LYS A1135 6528 5193 2262 685 -213 383 C ATOM 2529 C LYS A1135 -3.779 6.295 227.545 1.00 37.54 C ANISOU 2529 C LYS A1135 6646 5308 2311 734 -293 330 C ATOM 2530 O LYS A1135 -3.689 6.475 228.759 1.00 39.46 O ANISOU 2530 O LYS A1135 6968 5542 2484 806 -314 318 O ATOM 2531 CB LYS A1135 -5.477 4.460 227.430 1.00 37.82 C ANISOU 2531 CB LYS A1135 6725 5284 2358 732 -183 425 C ATOM 2532 CG LYS A1135 -6.767 3.914 226.836 1.00 38.53 C ANISOU 2532 CG LYS A1135 6791 5365 2484 674 -109 478 C ATOM 2533 CD LYS A1135 -6.993 2.464 227.235 1.00 32.55 C ANISOU 2533 CD LYS A1135 6105 4569 1696 711 -79 516 C ATOM 2534 CE LYS A1135 -8.253 1.912 226.596 1.00 32.20 C ANISOU 2534 CE LYS A1135 6029 4524 1680 638 -10 567 C ATOM 2535 NZ LYS A1135 -8.417 0.456 226.856 1.00 32.84 N1+ ANISOU 2535 NZ LYS A1135 6181 4563 1733 662 23 603 N1+ ATOM 2536 N SER A1136 -2.765 6.478 226.708 1.00 37.06 N ANISOU 2536 N SER A1136 6516 5281 2285 693 -339 297 N ATOM 2537 CA SER A1136 -1.428 6.813 227.180 1.00 38.79 C ANISOU 2537 CA SER A1136 6740 5537 2461 727 -423 245 C ATOM 2538 C SER A1136 -1.326 8.252 227.665 1.00 41.13 C ANISOU 2538 C SER A1136 7042 5856 2729 715 -448 201 C ATOM 2539 O SER A1136 -2.181 9.088 227.370 1.00 40.96 O ANISOU 2539 O SER A1136 7005 5821 2736 674 -397 210 O ATOM 2540 CB SER A1136 -0.401 6.573 226.072 1.00 37.16 C ANISOU 2540 CB SER A1136 6454 5363 2303 682 -457 227 C ATOM 2541 OG SER A1136 -0.648 7.418 224.960 1.00 35.70 O ANISOU 2541 OG SER A1136 6190 5191 2183 597 -428 220 O ATOM 2542 N ARG A1137 -0.266 8.527 228.416 1.00 45.31 N ANISOU 2542 N ARG A1137 7597 6422 3196 753 -528 153 N ATOM 2543 CA ARG A1137 0.031 9.877 228.871 1.00 47.80 C ANISOU 2543 CA ARG A1137 7920 6767 3475 734 -564 98 C ATOM 2544 C ARG A1137 0.397 10.753 227.680 1.00 46.36 C ANISOU 2544 C ARG A1137 7644 6614 3355 640 -561 70 C ATOM 2545 O ARG A1137 0.074 11.940 227.642 1.00 45.84 O ANISOU 2545 O ARG A1137 7579 6549 3290 603 -540 47 O ATOM 2546 CB ARG A1137 1.168 9.853 229.893 1.00 53.47 C ANISOU 2546 CB ARG A1137 8678 7533 4107 789 -664 47 C ATOM 2547 CG ARG A1137 1.400 11.168 230.616 1.00 58.29 C ANISOU 2547 CG ARG A1137 9321 8171 4657 775 -706 -15 C ATOM 2548 CD ARG A1137 2.626 11.084 231.514 1.00 64.03 C ANISOU 2548 CD ARG A1137 10070 8961 5297 817 -820 -72 C ATOM 2549 NE ARG A1137 3.553 10.043 231.073 1.00 67.38 N ANISOU 2549 NE ARG A1137 10441 9421 5740 834 -867 -63 N ATOM 2550 CZ ARG A1137 4.320 9.326 231.889 1.00 70.70 C ANISOU 2550 CZ ARG A1137 10896 9877 6091 914 -945 -75 C ATOM 2551 NH1 ARG A1137 4.278 9.532 233.199 1.00 74.01 N1+ ANISOU 2551 NH1 ARG A1137 11404 10304 6414 983 -987 -99 N1+ ATOM 2552 NH2 ARG A1137 5.132 8.400 231.394 1.00 70.70 N ANISOU 2552 NH2 ARG A1137 10846 9905 6113 933 -979 -61 N ATOM 2553 N TRP A1138 1.069 10.150 226.705 1.00 44.98 N ANISOU 2553 N TRP A1138 7399 6461 3230 608 -575 75 N ATOM 2554 CA TRP A1138 1.464 10.850 225.489 1.00 42.77 C ANISOU 2554 CA TRP A1138 7033 6208 3012 525 -567 53 C ATOM 2555 C TRP A1138 0.248 11.342 224.709 1.00 41.93 C ANISOU 2555 C TRP A1138 6903 6062 2965 482 -477 90 C ATOM 2556 O TRP A1138 0.274 12.426 224.131 1.00 41.04 O ANISOU 2556 O TRP A1138 6753 5964 2878 429 -460 65 O ATOM 2557 CB TRP A1138 2.331 9.941 224.611 1.00 41.12 C ANISOU 2557 CB TRP A1138 6763 6019 2840 511 -592 61 C ATOM 2558 CG TRP A1138 2.383 10.349 223.167 1.00 39.64 C ANISOU 2558 CG TRP A1138 6494 5838 2728 435 -553 63 C ATOM 2559 CD1 TRP A1138 3.012 11.442 222.643 1.00 39.33 C ANISOU 2559 CD1 TRP A1138 6404 5839 2701 375 -570 15 C ATOM 2560 CD2 TRP A1138 1.788 9.661 222.060 1.00 39.11 C ANISOU 2560 CD2 TRP A1138 6390 5739 2729 412 -492 113 C ATOM 2561 NE1 TRP A1138 2.840 11.479 221.280 1.00 38.05 N ANISOU 2561 NE1 TRP A1138 6180 5668 2610 325 -518 36 N ATOM 2562 CE2 TRP A1138 2.092 10.395 220.897 1.00 37.62 C ANISOU 2562 CE2 TRP A1138 6132 5571 2591 346 -474 95 C ATOM 2563 CE3 TRP A1138 1.024 8.495 221.941 1.00 38.97 C ANISOU 2563 CE3 TRP A1138 6397 5680 2730 438 -450 166 C ATOM 2564 CZ2 TRP A1138 1.660 10.003 219.632 1.00 36.36 C ANISOU 2564 CZ2 TRP A1138 5926 5392 2497 312 -420 131 C ATOM 2565 CZ3 TRP A1138 0.597 8.107 220.684 1.00 37.01 C ANISOU 2565 CZ3 TRP A1138 6100 5416 2547 393 -400 197 C ATOM 2566 CH2 TRP A1138 0.915 8.859 219.548 1.00 35.91 C ANISOU 2566 CH2 TRP A1138 5890 5298 2454 334 -388 180 C ATOM 2567 N TYR A1139 -0.819 10.550 224.703 1.00 42.97 N ANISOU 2567 N TYR A1139 7059 6151 3117 506 -420 148 N ATOM 2568 CA TYR A1139 -2.026 10.918 223.971 1.00 44.04 C ANISOU 2568 CA TYR A1139 7166 6262 3306 467 -342 187 C ATOM 2569 C TYR A1139 -2.723 12.131 224.583 1.00 48.28 C ANISOU 2569 C TYR A1139 7745 6786 3815 475 -313 177 C ATOM 2570 O TYR A1139 -3.047 13.086 223.880 1.00 47.57 O ANISOU 2570 O TYR A1139 7617 6698 3760 433 -277 173 O ATOM 2571 CB TYR A1139 -2.999 9.739 223.910 1.00 42.33 C ANISOU 2571 CB TYR A1139 6964 6014 3106 483 -295 246 C ATOM 2572 CG TYR A1139 -4.299 10.062 223.207 1.00 39.89 C ANISOU 2572 CG TYR A1139 6620 5695 2843 441 -223 286 C ATOM 2573 CD1 TYR A1139 -4.384 10.052 221.820 1.00 37.31 C ANISOU 2573 CD1 TYR A1139 6211 5384 2580 380 -201 298 C ATOM 2574 CD2 TYR A1139 -5.441 10.380 223.930 1.00 28.78 C ANISOU 2574 CD2 TYR A1139 5259 4267 1409 468 -178 314 C ATOM 2575 CE1 TYR A1139 -5.570 10.350 221.174 1.00 35.36 C ANISOU 2575 CE1 TYR A1139 5928 5141 2368 344 -143 334 C ATOM 2576 CE2 TYR A1139 -6.629 10.680 223.292 1.00 35.75 C ANISOU 2576 CE2 TYR A1139 6101 5153 2328 431 -116 353 C ATOM 2577 CZ TYR A1139 -6.688 10.662 221.915 1.00 34.82 C ANISOU 2577 CZ TYR A1139 5899 5060 2271 368 -103 362 C ATOM 2578 OH TYR A1139 -7.871 10.958 221.277 1.00 34.39 O ANISOU 2578 OH TYR A1139 5801 5021 2245 333 -49 402 O ATOM 2579 N ASN A1140 -2.948 12.088 225.893 1.00 53.57 N ANISOU 2579 N ASN A1140 8501 7438 4417 537 -326 174 N ATOM 2580 CA ASN A1140 -3.716 13.123 226.585 1.00 57.35 C ANISOU 2580 CA ASN A1140 9036 7893 4860 558 -291 172 C ATOM 2581 C ASN A1140 -2.985 14.459 226.651 1.00 57.88 C ANISOU 2581 C ASN A1140 9106 7983 4903 531 -323 108 C ATOM 2582 O ASN A1140 -3.612 15.517 226.741 1.00 60.37 O ANISOU 2582 O ASN A1140 9448 8277 5212 527 -279 106 O ATOM 2583 CB ASN A1140 -4.065 12.657 228.000 1.00 62.98 C ANISOU 2583 CB ASN A1140 9851 8580 5501 639 -298 183 C ATOM 2584 CG ASN A1140 -5.176 13.476 228.633 1.00 69.11 C ANISOU 2584 CG ASN A1140 10690 9320 6249 669 -238 202 C ATOM 2585 OD1 ASN A1140 -6.309 13.490 228.149 1.00 74.38 O ANISOU 2585 OD1 ASN A1140 11333 9970 6959 654 -165 251 O ATOM 2586 ND2 ASN A1140 -4.855 14.161 229.724 1.00 70.15 N ANISOU 2586 ND2 ASN A1140 10905 9445 6304 712 -270 161 N ATOM 2587 N GLN A1141 -1.658 14.407 226.605 1.00 56.77 N ANISOU 2587 N GLN A1141 8939 7888 4745 511 -399 55 N ATOM 2588 CA GLN A1141 -0.858 15.621 226.691 1.00 57.14 C ANISOU 2588 CA GLN A1141 8984 7967 4760 474 -437 -17 C ATOM 2589 C GLN A1141 -0.820 16.357 225.353 1.00 52.72 C ANISOU 2589 C GLN A1141 8347 7416 4268 404 -395 -22 C ATOM 2590 O GLN A1141 -0.835 17.587 225.311 1.00 52.63 O ANISOU 2590 O GLN A1141 8351 7402 4243 378 -374 -60 O ATOM 2591 CB GLN A1141 0.556 15.293 227.162 1.00 60.68 C ANISOU 2591 CB GLN A1141 9423 8474 5157 473 -540 -77 C ATOM 2592 CG GLN A1141 1.354 16.514 227.578 1.00 62.71 C ANISOU 2592 CG GLN A1141 9694 8775 5358 434 -591 -167 C ATOM 2593 CD GLN A1141 2.723 16.159 228.118 1.00 63.87 C ANISOU 2593 CD GLN A1141 9827 8993 5449 431 -703 -230 C ATOM 2594 OE1 GLN A1141 3.477 15.414 227.491 1.00 63.22 O ANISOU 2594 OE1 GLN A1141 9675 8945 5401 414 -738 -224 O ATOM 2595 NE2 GLN A1141 3.050 16.686 229.293 1.00 65.16 N ANISOU 2595 NE2 GLN A1141 10058 9180 5521 450 -762 -292 N ATOM 2596 N THR A1142 -0.769 15.599 224.261 1.00 48.31 N ANISOU 2596 N THR A1142 7713 6864 3779 378 -378 14 N ATOM 2597 CA THR A1142 -0.821 16.181 222.920 1.00 43.98 C ANISOU 2597 CA THR A1142 7095 6320 3297 322 -333 19 C ATOM 2598 C THR A1142 -1.828 15.438 222.045 1.00 42.11 C ANISOU 2598 C THR A1142 6818 6055 3126 320 -272 92 C ATOM 2599 O THR A1142 -1.442 14.667 221.166 1.00 40.40 O ANISOU 2599 O THR A1142 6542 5853 2954 296 -280 107 O ATOM 2600 CB THR A1142 0.562 16.163 222.232 1.00 42.35 C ANISOU 2600 CB THR A1142 6821 6167 3103 274 -384 -31 C ATOM 2601 OG1 THR A1142 1.039 14.815 222.140 1.00 41.92 O ANISOU 2601 OG1 THR A1142 6742 6125 3060 290 -424 -8 O ATOM 2602 CG2 THR A1142 1.564 17.000 223.014 1.00 43.25 C ANISOU 2602 CG2 THR A1142 6961 6324 3148 257 -448 -118 C ATOM 2603 N PRO A1143 -3.127 15.683 222.276 1.00 42.07 N ANISOU 2603 N PRO A1143 6845 6014 3124 343 -212 136 N ATOM 2604 CA PRO A1143 -4.208 14.908 221.655 1.00 41.73 C ANISOU 2604 CA PRO A1143 6767 5958 3129 339 -162 201 C ATOM 2605 C PRO A1143 -4.296 15.021 220.132 1.00 41.80 C ANISOU 2605 C PRO A1143 6693 5981 3206 288 -131 218 C ATOM 2606 O PRO A1143 -4.461 13.993 219.478 1.00 42.07 O ANISOU 2606 O PRO A1143 6685 6025 3275 271 -129 248 O ATOM 2607 CB PRO A1143 -5.469 15.481 222.315 1.00 42.50 C ANISOU 2607 CB PRO A1143 6918 6027 3203 373 -108 231 C ATOM 2608 CG PRO A1143 -5.083 16.837 222.768 1.00 43.95 C ANISOU 2608 CG PRO A1143 7148 6201 3350 381 -110 185 C ATOM 2609 CD PRO A1143 -3.644 16.742 223.159 1.00 44.01 C ANISOU 2609 CD PRO A1143 7165 6236 3322 372 -188 122 C ATOM 2610 N ASN A1144 -4.191 16.224 219.574 1.00 43.34 N ANISOU 2610 N ASN A1144 6873 6178 3416 267 -105 198 N ATOM 2611 CA ASN A1144 -4.398 16.396 218.135 1.00 41.31 C ANISOU 2611 CA ASN A1144 6546 5932 3220 229 -69 220 C ATOM 2612 C ASN A1144 -3.315 15.739 217.286 1.00 36.00 C ANISOU 2612 C ASN A1144 5819 5283 2577 197 -105 201 C ATOM 2613 O ASN A1144 -3.618 15.110 216.274 1.00 34.40 O ANISOU 2613 O ASN A1144 5564 5088 2418 175 -88 233 O ATOM 2614 CB ASN A1144 -4.506 17.880 217.778 1.00 45.44 C ANISOU 2614 CB ASN A1144 7078 6442 3746 224 -26 205 C ATOM 2615 CG ASN A1144 -5.788 18.506 218.285 1.00 49.33 C ANISOU 2615 CG ASN A1144 7614 6908 4221 257 28 239 C ATOM 2616 OD1 ASN A1144 -6.866 17.924 218.163 1.00 48.74 O ANISOU 2616 OD1 ASN A1144 7520 6839 4161 264 53 291 O ATOM 2617 ND2 ASN A1144 -5.679 19.696 218.862 1.00 53.97 N ANISOU 2617 ND2 ASN A1144 8263 7471 4773 277 47 209 N ATOM 2618 N ARG A1145 -2.057 15.880 217.693 1.00 34.20 N ANISOU 2618 N ARG A1145 5602 5072 2320 195 -156 148 N ATOM 2619 CA ARG A1145 -0.965 15.227 216.977 1.00 33.50 C ANISOU 2619 CA ARG A1145 5465 5010 2254 171 -192 130 C ATOM 2620 C ARG A1145 -1.041 13.713 217.137 1.00 33.38 C ANISOU 2620 C ARG A1145 5451 4990 2243 187 -217 161 C ATOM 2621 O ARG A1145 -0.865 12.971 216.172 1.00 32.97 O ANISOU 2621 O ARG A1145 5355 4941 2230 169 -211 179 O ATOM 2622 CB ARG A1145 0.394 15.733 217.462 1.00 25.01 C ANISOU 2622 CB ARG A1145 4396 3969 1137 161 -247 61 C ATOM 2623 CG ARG A1145 1.566 14.960 216.876 1.00 25.82 C ANISOU 2623 CG ARG A1145 4452 4104 1254 142 -290 44 C ATOM 2624 CD ARG A1145 2.900 15.617 217.186 1.00 29.28 C ANISOU 2624 CD ARG A1145 4880 4594 1651 116 -344 -32 C ATOM 2625 NE ARG A1145 4.014 14.822 216.676 1.00 31.35 N ANISOU 2625 NE ARG A1145 5100 4890 1924 100 -387 -44 N ATOM 2626 CZ ARG A1145 5.290 15.182 216.757 1.00 32.60 C ANISOU 2626 CZ ARG A1145 5231 5103 2051 65 -441 -110 C ATOM 2627 NH1 ARG A1145 5.622 16.331 217.326 1.00 33.17 N1+ ANISOU 2627 NH1 ARG A1145 5315 5209 2080 39 -458 -181 N1+ ATOM 2628 NH2 ARG A1145 6.234 14.393 216.266 1.00 32.88 N ANISOU 2628 NH2 ARG A1145 5233 5161 2097 54 -478 -110 N ATOM 2629 N ALA A1146 -1.306 13.262 218.360 1.00 32.66 N ANISOU 2629 N ALA A1146 5416 4887 2108 226 -240 165 N ATOM 2630 CA ALA A1146 -1.407 11.836 218.643 1.00 30.68 C ANISOU 2630 CA ALA A1146 5181 4625 1852 250 -257 194 C ATOM 2631 C ALA A1146 -2.542 11.198 217.851 1.00 31.71 C ANISOU 2631 C ALA A1146 5283 4740 2024 231 -205 247 C ATOM 2632 O ALA A1146 -2.360 10.149 217.240 1.00 32.60 O ANISOU 2632 O ALA A1146 5374 4852 2159 221 -209 264 O ATOM 2633 CB ALA A1146 -1.601 11.603 220.129 1.00 26.42 C ANISOU 2633 CB ALA A1146 4716 4071 1250 303 -282 191 C ATOM 2634 N LYS A1147 -3.702 11.850 217.854 1.00 33.11 N ANISOU 2634 N LYS A1147 5461 4911 2207 225 -158 272 N ATOM 2635 CA LYS A1147 -4.893 11.345 217.173 1.00 34.65 C ANISOU 2635 CA LYS A1147 5624 5112 2431 200 -114 321 C ATOM 2636 C LYS A1147 -4.644 10.999 215.707 1.00 35.31 C ANISOU 2636 C LYS A1147 5642 5212 2563 158 -107 328 C ATOM 2637 O LYS A1147 -5.101 9.964 215.222 1.00 36.12 O ANISOU 2637 O LYS A1147 5725 5321 2677 140 -98 357 O ATOM 2638 CB LYS A1147 -6.026 12.370 217.270 1.00 37.34 C ANISOU 2638 CB LYS A1147 5965 5454 2769 198 -67 343 C ATOM 2639 CG LYS A1147 -7.275 12.017 216.472 1.00 39.20 C ANISOU 2639 CG LYS A1147 6152 5713 3027 163 -27 393 C ATOM 2640 CD LYS A1147 -8.068 10.902 217.134 1.00 41.21 C ANISOU 2640 CD LYS A1147 6432 5970 3255 169 -21 429 C ATOM 2641 CE LYS A1147 -9.376 10.644 216.399 1.00 41.60 C ANISOU 2641 CE LYS A1147 6429 6061 3314 123 15 479 C ATOM 2642 NZ LYS A1147 -9.152 10.200 214.996 1.00 41.09 N1+ ANISOU 2642 NZ LYS A1147 6299 6027 3286 75 8 482 N1+ ATOM 2643 N ARG A1148 -3.915 11.860 215.004 1.00 34.85 N ANISOU 2643 N ARG A1148 5552 5160 2527 143 -108 300 N ATOM 2644 CA ARG A1148 -3.682 11.656 213.578 1.00 34.85 C ANISOU 2644 CA ARG A1148 5496 5173 2570 111 -96 305 C ATOM 2645 C ARG A1148 -2.510 10.709 213.334 1.00 30.61 C ANISOU 2645 C ARG A1148 4959 4634 2039 115 -133 286 C ATOM 2646 O ARG A1148 -2.336 10.199 212.229 1.00 29.54 O ANISOU 2646 O ARG A1148 4789 4503 1934 95 -124 295 O ATOM 2647 CB ARG A1148 -3.446 12.994 212.870 1.00 33.68 C ANISOU 2647 CB ARG A1148 5323 5032 2443 97 -72 288 C ATOM 2648 CG ARG A1148 -2.190 13.728 213.291 1.00 34.29 C ANISOU 2648 CG ARG A1148 5418 5107 2503 107 -99 238 C ATOM 2649 CD ARG A1148 -2.016 15.004 212.485 1.00 33.68 C ANISOU 2649 CD ARG A1148 5320 5032 2446 93 -64 224 C ATOM 2650 NE ARG A1148 -2.967 16.041 212.875 1.00 34.28 N ANISOU 2650 NE ARG A1148 5422 5094 2509 104 -26 237 N ATOM 2651 CZ ARG A1148 -2.647 17.116 213.589 1.00 34.82 C ANISOU 2651 CZ ARG A1148 5530 5153 2546 117 -22 202 C ATOM 2652 NH1 ARG A1148 -1.395 17.303 213.987 1.00 34.28 N1+ ANISOU 2652 NH1 ARG A1148 5472 5099 2453 112 -62 149 N1+ ATOM 2653 NH2 ARG A1148 -3.578 18.008 213.899 1.00 35.70 N ANISOU 2653 NH2 ARG A1148 5673 5245 2648 134 20 219 N ATOM 2654 N VAL A1149 -1.706 10.477 214.367 1.00 29.04 N ANISOU 2654 N VAL A1149 4801 4428 1805 144 -175 260 N ATOM 2655 CA VAL A1149 -0.670 9.455 214.295 1.00 28.41 C ANISOU 2655 CA VAL A1149 4728 4345 1721 157 -212 249 C ATOM 2656 C VAL A1149 -1.305 8.090 214.541 1.00 27.52 C ANISOU 2656 C VAL A1149 4646 4211 1599 171 -206 284 C ATOM 2657 O VAL A1149 -1.003 7.120 213.848 1.00 23.41 O ANISOU 2657 O VAL A1149 4119 3681 1094 167 -205 294 O ATOM 2658 CB VAL A1149 0.464 9.706 215.311 1.00 23.92 C ANISOU 2658 CB VAL A1149 4189 3790 1110 185 -268 209 C ATOM 2659 CG1 VAL A1149 1.379 8.495 215.404 1.00 24.23 C ANISOU 2659 CG1 VAL A1149 4245 3827 1136 211 -307 207 C ATOM 2660 CG2 VAL A1149 1.258 10.940 214.925 1.00 23.71 C ANISOU 2660 CG2 VAL A1149 4129 3793 1088 159 -276 168 C ATOM 2661 N ILE A1150 -2.199 8.031 215.526 1.00 27.31 N ANISOU 2661 N ILE A1150 4658 4175 1543 189 -196 302 N ATOM 2662 CA ILE A1150 -2.938 6.810 215.830 1.00 28.92 C ANISOU 2662 CA ILE A1150 4897 4361 1733 198 -182 337 C ATOM 2663 C ILE A1150 -3.739 6.350 214.616 1.00 29.93 C ANISOU 2663 C ILE A1150 4978 4499 1894 152 -145 367 C ATOM 2664 O ILE A1150 -3.851 5.154 214.346 1.00 30.93 O ANISOU 2664 O ILE A1150 5124 4612 2018 150 -139 385 O ATOM 2665 CB ILE A1150 -3.904 7.002 217.023 1.00 29.39 C ANISOU 2665 CB ILE A1150 5000 4411 1753 221 -167 356 C ATOM 2666 CG1 ILE A1150 -3.155 7.467 218.274 1.00 29.71 C ANISOU 2666 CG1 ILE A1150 5093 4444 1751 273 -207 324 C ATOM 2667 CG2 ILE A1150 -4.663 5.720 217.313 1.00 30.13 C ANISOU 2667 CG2 ILE A1150 5132 4489 1829 226 -147 394 C ATOM 2668 CD1 ILE A1150 -1.889 6.713 218.549 1.00 30.62 C ANISOU 2668 CD1 ILE A1150 5236 4554 1846 309 -257 303 C ATOM 2669 N THR A1151 -4.292 7.313 213.886 1.00 30.91 N ANISOU 2669 N THR A1151 5049 4651 2045 120 -120 371 N ATOM 2670 CA THR A1151 -5.056 7.022 212.680 1.00 31.04 C ANISOU 2670 CA THR A1151 5015 4694 2086 80 -90 397 C ATOM 2671 C THR A1151 -4.153 6.415 211.610 1.00 30.14 C ANISOU 2671 C THR A1151 4886 4568 1998 75 -100 382 C ATOM 2672 O THR A1151 -4.523 5.438 210.953 1.00 29.19 O ANISOU 2672 O THR A1151 4763 4449 1880 60 -88 400 O ATOM 2673 CB THR A1151 -5.739 8.289 212.130 1.00 32.54 C ANISOU 2673 CB THR A1151 5153 4918 2293 56 -65 406 C ATOM 2674 OG1 THR A1151 -6.783 8.693 213.024 1.00 31.53 O ANISOU 2674 OG1 THR A1151 5041 4801 2138 58 -48 429 O ATOM 2675 CG2 THR A1151 -6.334 8.030 210.751 1.00 34.81 C ANISOU 2675 CG2 THR A1151 5383 5244 2602 23 -43 429 C ATOM 2676 N THR A1152 -2.965 6.992 211.450 1.00 28.86 N ANISOU 2676 N THR A1152 4720 4397 1850 87 -121 349 N ATOM 2677 CA THR A1152 -1.988 6.483 210.491 1.00 28.78 C ANISOU 2677 CA THR A1152 4701 4375 1861 86 -128 335 C ATOM 2678 C THR A1152 -1.642 5.024 210.793 1.00 28.46 C ANISOU 2678 C THR A1152 4711 4302 1800 107 -143 342 C ATOM 2679 O THR A1152 -1.627 4.183 209.895 1.00 26.91 O ANISOU 2679 O THR A1152 4518 4091 1614 97 -130 350 O ATOM 2680 CB THR A1152 -0.707 7.332 210.492 1.00 28.45 C ANISOU 2680 CB THR A1152 4648 4336 1825 97 -151 299 C ATOM 2681 OG1 THR A1152 -1.007 8.658 210.041 1.00 21.65 O ANISOU 2681 OG1 THR A1152 3748 3495 983 77 -128 293 O ATOM 2682 CG2 THR A1152 0.342 6.729 209.580 1.00 21.82 C ANISOU 2682 CG2 THR A1152 3804 3486 1002 100 -158 288 C ATOM 2683 N PHE A1153 -1.382 4.734 212.065 1.00 30.53 N ANISOU 2683 N PHE A1153 5022 4550 2028 141 -168 338 N ATOM 2684 CA PHE A1153 -1.059 3.381 212.505 1.00 23.60 C ANISOU 2684 CA PHE A1153 4206 3637 1124 172 -179 348 C ATOM 2685 C PHE A1153 -2.235 2.416 212.335 1.00 23.77 C ANISOU 2685 C PHE A1153 4251 3642 1137 150 -146 381 C ATOM 2686 O PHE A1153 -2.039 1.239 212.022 1.00 23.99 O ANISOU 2686 O PHE A1153 4323 3636 1157 157 -139 390 O ATOM 2687 CB PHE A1153 -0.613 3.392 213.970 1.00 24.26 C ANISOU 2687 CB PHE A1153 4339 3714 1165 223 -214 338 C ATOM 2688 CG PHE A1153 0.878 3.352 214.159 1.00 36.26 C ANISOU 2688 CG PHE A1153 5866 5239 2672 262 -259 311 C ATOM 2689 CD1 PHE A1153 1.648 2.430 213.476 1.00 35.97 C ANISOU 2689 CD1 PHE A1153 5842 5184 2641 277 -261 314 C ATOM 2690 CD2 PHE A1153 1.502 4.213 215.044 1.00 24.82 C ANISOU 2690 CD2 PHE A1153 4415 3818 1198 286 -300 284 C ATOM 2691 CE1 PHE A1153 3.017 2.375 213.652 1.00 35.30 C ANISOU 2691 CE1 PHE A1153 5758 5114 2540 317 -304 294 C ATOM 2692 CE2 PHE A1153 2.877 4.165 215.228 1.00 25.16 C ANISOU 2692 CE2 PHE A1153 4457 3881 1222 319 -350 259 C ATOM 2693 CZ PHE A1153 3.635 3.246 214.532 1.00 34.35 C ANISOU 2693 CZ PHE A1153 5626 5033 2394 337 -352 266 C ATOM 2694 N ARG A1154 -3.450 2.918 212.543 1.00 25.74 N ANISOU 2694 N ARG A1154 4476 3920 1385 124 -123 400 N ATOM 2695 CA ARG A1154 -4.646 2.088 212.466 1.00 27.28 C ANISOU 2695 CA ARG A1154 4687 4116 1564 98 -93 434 C ATOM 2696 C ARG A1154 -5.043 1.779 211.022 1.00 30.40 C ANISOU 2696 C ARG A1154 5042 4526 1983 59 -72 441 C ATOM 2697 O ARG A1154 -5.394 0.643 210.700 1.00 31.60 O ANISOU 2697 O ARG A1154 5234 4652 2121 44 -56 455 O ATOM 2698 CB ARG A1154 -5.809 2.765 213.196 1.00 27.46 C ANISOU 2698 CB ARG A1154 4689 4174 1569 87 -76 457 C ATOM 2699 CG ARG A1154 -7.107 1.958 213.205 1.00 29.05 C ANISOU 2699 CG ARG A1154 4899 4392 1747 60 -43 498 C ATOM 2700 CD ARG A1154 -8.221 2.671 212.447 1.00 30.29 C ANISOU 2700 CD ARG A1154 4972 4620 1915 25 -20 521 C ATOM 2701 NE ARG A1154 -8.469 4.009 212.980 1.00 31.77 N ANISOU 2701 NE ARG A1154 5127 4840 2105 29 -21 520 N ATOM 2702 CZ ARG A1154 -9.295 4.898 212.433 1.00 32.45 C ANISOU 2702 CZ ARG A1154 5141 4990 2199 7 -4 540 C ATOM 2703 NH1 ARG A1154 -9.961 4.601 211.326 1.00 31.40 N1+ ANISOU 2703 NH1 ARG A1154 4953 4897 2082 -5 14 557 N1+ ATOM 2704 NH2 ARG A1154 -9.451 6.090 212.994 1.00 33.29 N ANISOU 2704 NH2 ARG A1154 5242 5104 2305 8 -3 536 N ATOM 2705 N THR A1155 -4.983 2.788 210.156 1.00 30.65 N ANISOU 2705 N THR A1155 5007 4593 2046 45 -70 429 N ATOM 2706 CA THR A1155 -5.434 2.632 208.774 1.00 30.30 C ANISOU 2706 CA THR A1155 4926 4569 2018 19 -51 436 C ATOM 2707 C THR A1155 -4.300 2.325 207.798 1.00 29.07 C ANISOU 2707 C THR A1155 4783 4376 1885 23 -59 410 C ATOM 2708 O THR A1155 -4.528 1.738 206.741 1.00 30.01 O ANISOU 2708 O THR A1155 4909 4485 2008 5 -46 412 O ATOM 2709 CB THR A1155 -6.165 3.892 208.273 1.00 29.44 C ANISOU 2709 CB THR A1155 4738 4524 1923 9 -37 446 C ATOM 2710 OG1 THR A1155 -5.254 4.997 208.242 1.00 22.06 O ANISOU 2710 OG1 THR A1155 3782 3588 1014 17 -50 420 O ATOM 2711 CG2 THR A1155 -7.343 4.227 209.177 1.00 22.78 C ANISOU 2711 CG2 THR A1155 3877 3725 1052 6 -24 477 C ATOM 2712 N GLY A1156 -3.083 2.729 208.143 1.00 28.54 N ANISOU 2712 N GLY A1156 4723 4291 1829 48 -81 386 N ATOM 2713 CA GLY A1156 -1.947 2.518 207.264 1.00 29.79 C ANISOU 2713 CA GLY A1156 4889 4423 2007 57 -86 366 C ATOM 2714 C GLY A1156 -1.981 3.421 206.044 1.00 32.66 C ANISOU 2714 C GLY A1156 5195 4815 2400 40 -70 360 C ATOM 2715 O GLY A1156 -1.413 3.092 205.002 1.00 33.27 O ANISOU 2715 O GLY A1156 5281 4871 2490 38 -62 351 O ATOM 2716 N THR A1157 -2.650 4.563 206.175 1.00 31.32 N ANISOU 2716 N THR A1157 4973 4689 2237 30 -63 366 N ATOM 2717 CA THR A1157 -2.773 5.523 205.083 1.00 30.24 C ANISOU 2717 CA THR A1157 4786 4582 2124 18 -44 365 C ATOM 2718 C THR A1157 -2.483 6.940 205.562 1.00 30.72 C ANISOU 2718 C THR A1157 4818 4660 2195 21 -45 354 C ATOM 2719 O THR A1157 -2.297 7.174 206.755 1.00 30.95 O ANISOU 2719 O THR A1157 4865 4684 2211 31 -64 346 O ATOM 2720 CB THR A1157 -4.176 5.489 204.454 1.00 30.22 C ANISOU 2720 CB THR A1157 4751 4623 2110 5 -23 393 C ATOM 2721 OG1 THR A1157 -5.165 5.629 205.481 1.00 21.41 O ANISOU 2721 OG1 THR A1157 3624 3538 972 4 -23 415 O ATOM 2722 CG2 THR A1157 -4.401 4.179 203.718 1.00 30.71 C ANISOU 2722 CG2 THR A1157 4852 4657 2159 -3 -18 397 C ATOM 2723 N TRP A1158 -2.454 7.885 204.628 1.00 31.03 N ANISOU 2723 N TRP A1158 4822 4715 2253 11 -25 352 N ATOM 2724 CA TRP A1158 -2.150 9.272 204.959 1.00 31.20 C ANISOU 2724 CA TRP A1158 4829 4741 2283 11 -19 339 C ATOM 2725 C TRP A1158 -3.416 10.104 205.116 1.00 32.99 C ANISOU 2725 C TRP A1158 5030 4998 2507 -4 0 362 C ATOM 2726 O TRP A1158 -3.380 11.329 204.988 1.00 33.45 O ANISOU 2726 O TRP A1158 5082 5053 2575 -8 19 356 O ATOM 2727 CB TRP A1158 -1.256 9.894 203.888 1.00 20.05 C ANISOU 2727 CB TRP A1158 3408 3315 895 10 0 323 C ATOM 2728 CG TRP A1158 0.040 9.178 203.680 1.00 20.02 C ANISOU 2728 CG TRP A1158 3426 3284 896 24 -15 302 C ATOM 2729 CD1 TRP A1158 0.328 8.279 202.698 1.00 20.00 C ANISOU 2729 CD1 TRP A1158 3436 3264 899 26 -7 307 C ATOM 2730 CD2 TRP A1158 1.230 9.307 204.468 1.00 22.26 C ANISOU 2730 CD2 TRP A1158 3725 3562 1171 36 -40 275 C ATOM 2731 NE1 TRP A1158 1.622 7.838 202.825 1.00 26.19 N ANISOU 2731 NE1 TRP A1158 4243 4027 1682 41 -22 288 N ATOM 2732 CE2 TRP A1158 2.198 8.454 203.905 1.00 23.68 C ANISOU 2732 CE2 TRP A1158 3921 3722 1353 47 -45 269 C ATOM 2733 CE3 TRP A1158 1.570 10.059 205.597 1.00 22.25 C ANISOU 2733 CE3 TRP A1158 3726 3573 1152 40 -60 254 C ATOM 2734 CZ2 TRP A1158 3.481 8.332 204.431 1.00 20.27 C ANISOU 2734 CZ2 TRP A1158 3499 3295 906 60 -73 246 C ATOM 2735 CZ3 TRP A1158 2.845 9.937 206.116 1.00 20.42 C ANISOU 2735 CZ3 TRP A1158 3506 3350 904 50 -92 227 C ATOM 2736 CH2 TRP A1158 3.785 9.081 205.534 1.00 20.44 C ANISOU 2736 CH2 TRP A1158 3515 3341 908 59 -100 224 C ATOM 2737 N ASP A1159 -4.529 9.436 205.402 1.00 34.98 N ANISOU 2737 N ASP A1159 5272 5271 2748 -10 -2 387 N ATOM 2738 CA ASP A1159 -5.833 10.092 205.455 1.00 36.13 C ANISOU 2738 CA ASP A1159 5386 5447 2895 -28 16 413 C ATOM 2739 C ASP A1159 -5.930 11.103 206.592 1.00 32.85 C ANISOU 2739 C ASP A1159 4996 5020 2465 -27 18 408 C ATOM 2740 O ASP A1159 -6.812 11.960 206.598 1.00 32.85 O ANISOU 2740 O ASP A1159 4988 5029 2463 -45 38 426 O ATOM 2741 CB ASP A1159 -6.947 9.051 205.593 1.00 42.50 C ANISOU 2741 CB ASP A1159 6172 6289 3687 -27 15 442 C ATOM 2742 CG ASP A1159 -6.990 8.082 204.425 1.00 51.01 C ANISOU 2742 CG ASP A1159 7239 7376 4767 -9 19 446 C ATOM 2743 OD1 ASP A1159 -6.589 8.473 203.307 1.00 49.67 O ANISOU 2743 OD1 ASP A1159 7054 7203 4616 -12 27 437 O ATOM 2744 OD2 ASP A1159 -7.425 6.927 204.624 1.00 59.42 O1+ ANISOU 2744 OD2 ASP A1159 8329 8441 5808 9 16 457 O1+ ATOM 2745 N ALA A1160 -5.017 11.002 207.550 1.00 31.07 N ANISOU 2745 N ALA A1160 4811 4774 2220 -5 -3 384 N ATOM 2746 CA ALA A1160 -5.021 11.889 208.704 1.00 30.18 C ANISOU 2746 CA ALA A1160 4731 4649 2088 10 -3 373 C ATOM 2747 C ALA A1160 -4.327 13.212 208.400 1.00 29.06 C ANISOU 2747 C ALA A1160 4594 4488 1961 18 13 347 C ATOM 2748 O ALA A1160 -4.293 14.112 209.238 1.00 29.23 O ANISOU 2748 O ALA A1160 4644 4495 1967 35 19 333 O ATOM 2749 CB ALA A1160 -4.358 11.209 209.884 1.00 31.09 C ANISOU 2749 CB ALA A1160 4888 4741 2183 34 -37 353 C ATOM 2750 N TYR A1161 -3.779 13.330 207.197 1.00 27.99 N ANISOU 2750 N TYR A1161 4435 4350 1851 9 26 341 N ATOM 2751 CA TYR A1161 -2.996 14.504 206.841 1.00 27.63 C ANISOU 2751 CA TYR A1161 4395 4285 1817 18 47 316 C ATOM 2752 C TYR A1161 -3.474 15.144 205.543 1.00 28.71 C ANISOU 2752 C TYR A1161 4514 4422 1974 7 88 336 C ATOM 2753 O TYR A1161 -3.999 14.462 204.662 1.00 31.15 O ANISOU 2753 O TYR A1161 4798 4750 2288 -13 88 361 O ATOM 2754 CB TYR A1161 -1.515 14.131 206.731 1.00 26.65 C ANISOU 2754 CB TYR A1161 4274 4152 1699 24 24 281 C ATOM 2755 CG TYR A1161 -0.897 13.731 208.051 1.00 25.45 C ANISOU 2755 CG TYR A1161 4148 4003 1520 37 -20 254 C ATOM 2756 CD1 TYR A1161 -0.966 12.422 208.505 1.00 23.61 C ANISOU 2756 CD1 TYR A1161 3924 3769 1276 42 -53 264 C ATOM 2757 CD2 TYR A1161 -0.251 14.668 208.846 1.00 24.35 C ANISOU 2757 CD2 TYR A1161 4029 3865 1357 44 -29 218 C ATOM 2758 CE1 TYR A1161 -0.403 12.057 209.712 1.00 21.23 C ANISOU 2758 CE1 TYR A1161 3654 3468 945 59 -94 243 C ATOM 2759 CE2 TYR A1161 0.313 14.312 210.050 1.00 22.23 C ANISOU 2759 CE2 TYR A1161 3786 3605 1054 55 -77 192 C ATOM 2760 CZ TYR A1161 0.229 13.008 210.482 1.00 21.48 C ANISOU 2760 CZ TYR A1161 3703 3508 952 65 -110 207 C ATOM 2761 OH TYR A1161 0.793 12.654 211.685 1.00 23.46 O ANISOU 2761 OH TYR A1161 3984 3765 1163 82 -159 183 O ATOM 2762 N PRO A1162 -3.303 16.469 205.430 1.00 28.11 N ANISOU 2762 N PRO A1162 4455 4325 1902 20 125 326 N ATOM 2763 CA PRO A1162 -3.634 17.190 204.198 1.00 27.25 C ANISOU 2763 CA PRO A1162 4340 4203 1809 21 170 344 C ATOM 2764 C PRO A1162 -2.575 16.990 203.116 1.00 27.88 C ANISOU 2764 C PRO A1162 4410 4272 1911 19 179 329 C ATOM 2765 O PRO A1162 -1.379 17.062 203.405 1.00 28.41 O ANISOU 2765 O PRO A1162 4484 4330 1981 25 172 296 O ATOM 2766 CB PRO A1162 -3.686 18.649 204.654 1.00 27.11 C ANISOU 2766 CB PRO A1162 4357 4158 1785 48 212 335 C ATOM 2767 CG PRO A1162 -2.755 18.704 205.810 1.00 27.09 C ANISOU 2767 CG PRO A1162 4373 4153 1766 51 185 295 C ATOM 2768 CD PRO A1162 -2.889 17.382 206.509 1.00 27.74 C ANISOU 2768 CD PRO A1162 4441 4261 1836 39 129 298 C ATOM 2769 N PRO A 234 -3.013 16.734 201.875 1.00 39.61 N ANISOU 2769 N PRO A 234 6795 5830 2426 357 458 237 N ATOM 2770 CA PRO A 234 -2.105 16.525 200.743 1.00 38.61 C ANISOU 2770 CA PRO A 234 6636 5607 2428 361 387 217 C ATOM 2771 C PRO A 234 -1.399 17.813 200.332 1.00 36.97 C ANISOU 2771 C PRO A 234 6425 5332 2292 429 312 144 C ATOM 2772 O PRO A 234 -1.885 18.896 200.655 1.00 39.06 O ANISOU 2772 O PRO A 234 6696 5625 2521 473 329 101 O ATOM 2773 CB PRO A 234 -3.040 16.032 199.635 1.00 38.64 C ANISOU 2773 CB PRO A 234 6527 5684 2472 286 454 211 C ATOM 2774 CG PRO A 234 -4.362 16.617 199.981 1.00 39.51 C ANISOU 2774 CG PRO A 234 6586 5925 2501 267 540 190 C ATOM 2775 CD PRO A 234 -4.427 16.625 201.479 1.00 39.98 C ANISOU 2775 CD PRO A 234 6741 6011 2439 290 561 231 C ATOM 2776 N PRO A 235 -0.258 17.699 199.634 1.00 35.13 N ANISOU 2776 N PRO A 235 6185 5012 2148 439 234 131 N ATOM 2777 CA PRO A 235 0.451 18.888 199.153 1.00 33.90 C ANISOU 2777 CA PRO A 235 6020 4804 2057 482 167 71 C ATOM 2778 C PRO A 235 -0.307 19.569 198.022 1.00 33.22 C ANISOU 2778 C PRO A 235 5844 4745 2033 475 202 26 C ATOM 2779 O PRO A 235 -0.941 18.892 197.218 1.00 33.81 O ANISOU 2779 O PRO A 235 5842 4865 2139 424 250 35 O ATOM 2780 CB PRO A 235 1.784 18.325 198.658 1.00 33.82 C ANISOU 2780 CB PRO A 235 6009 4730 2112 475 90 79 C ATOM 2781 CG PRO A 235 1.473 16.926 198.279 1.00 34.37 C ANISOU 2781 CG PRO A 235 6058 4811 2192 430 133 127 C ATOM 2782 CD PRO A 235 0.445 16.457 199.272 1.00 35.74 C ANISOU 2782 CD PRO A 235 6273 5042 2263 411 207 175 C ATOM 2783 N SER A 236 -0.244 20.894 197.967 1.00 32.34 N ANISOU 2783 N SER A 236 5752 4606 1931 527 175 -21 N ATOM 2784 CA SER A 236 -0.949 21.641 196.937 1.00 31.49 C ANISOU 2784 CA SER A 236 5577 4517 1872 538 201 -57 C ATOM 2785 C SER A 236 -0.010 22.077 195.816 1.00 31.94 C ANISOU 2785 C SER A 236 5603 4510 2024 527 137 -81 C ATOM 2786 O SER A 236 -0.157 21.648 194.672 1.00 31.43 O ANISOU 2786 O SER A 236 5453 4467 2022 484 150 -82 O ATOM 2787 CB SER A 236 -1.641 22.859 197.545 1.00 32.57 C ANISOU 2787 CB SER A 236 5769 4661 1945 615 224 -87 C ATOM 2788 OG SER A 236 -2.333 23.598 196.554 1.00 33.51 O ANISOU 2788 OG SER A 236 5834 4796 2104 645 245 -115 O ATOM 2789 N ARG A 237 0.957 22.925 196.155 1.00 34.87 N ANISOU 2789 N ARG A 237 6042 4813 2392 554 68 -102 N ATOM 2790 CA ARG A 237 1.864 23.502 195.167 1.00 36.36 C ANISOU 2790 CA ARG A 237 6207 4955 2651 531 11 -125 C ATOM 2791 C ARG A 237 2.676 22.446 194.423 1.00 35.95 C ANISOU 2791 C ARG A 237 6084 4916 2660 472 -12 -109 C ATOM 2792 O ARG A 237 3.018 22.631 193.254 1.00 35.17 O ANISOU 2792 O ARG A 237 5924 4816 2623 441 -26 -124 O ATOM 2793 CB ARG A 237 2.807 24.507 195.832 1.00 40.19 C ANISOU 2793 CB ARG A 237 6787 5383 3100 546 -59 -150 C ATOM 2794 CG ARG A 237 2.137 25.814 196.219 1.00 46.23 C ANISOU 2794 CG ARG A 237 7638 6112 3817 611 -47 -180 C ATOM 2795 CD ARG A 237 3.147 26.819 196.740 1.00 52.26 C ANISOU 2795 CD ARG A 237 8505 6811 4542 603 -123 -211 C ATOM 2796 NE ARG A 237 3.734 26.395 198.007 1.00 57.57 N ANISOU 2796 NE ARG A 237 9231 7499 5144 596 -157 -205 N ATOM 2797 CZ ARG A 237 4.755 27.007 198.598 1.00 62.03 C ANISOU 2797 CZ ARG A 237 9872 8037 5661 568 -234 -231 C ATOM 2798 NH1 ARG A 237 5.311 28.071 198.035 1.00 64.15 N1+ ANISOU 2798 NH1 ARG A 237 10175 8252 5945 535 -281 -265 N1+ ATOM 2799 NH2 ARG A 237 5.223 26.550 199.752 1.00 62.42 N ANISOU 2799 NH2 ARG A 237 9963 8118 5636 565 -268 -222 N ATOM 2800 N GLU A 238 2.983 21.344 195.098 1.00 36.33 N ANISOU 2800 N GLU A 238 6148 4976 2680 462 -14 -77 N ATOM 2801 CA GLU A 238 3.737 20.264 194.474 1.00 35.93 C ANISOU 2801 CA GLU A 238 6048 4930 2674 426 -34 -61 C ATOM 2802 C GLU A 238 2.912 19.594 193.378 1.00 33.28 C ANISOU 2802 C GLU A 238 5632 4628 2386 392 26 -61 C ATOM 2803 O GLU A 238 3.431 19.279 192.307 1.00 32.06 O ANISOU 2803 O GLU A 238 5417 4477 2287 361 12 -75 O ATOM 2804 CB GLU A 238 4.176 19.239 195.522 1.00 40.91 C ANISOU 2804 CB GLU A 238 6738 5555 3249 440 -51 -19 C ATOM 2805 CG GLU A 238 5.084 19.819 196.600 1.00 45.26 C ANISOU 2805 CG GLU A 238 7362 6093 3741 466 -123 -22 C ATOM 2806 CD GLU A 238 5.647 18.761 197.531 1.00 48.57 C ANISOU 2806 CD GLU A 238 7837 6514 4102 485 -154 27 C ATOM 2807 OE1 GLU A 238 6.591 19.077 198.287 1.00 52.20 O ANISOU 2807 OE1 GLU A 238 8340 6982 4513 500 -229 26 O ATOM 2808 OE2 GLU A 238 5.149 17.616 197.509 1.00 48.79 O1+ ANISOU 2808 OE2 GLU A 238 7872 6539 4127 482 -107 69 O1+ ATOM 2809 N LYS A 239 1.625 19.392 193.647 1.00 32.99 N ANISOU 2809 N LYS A 239 5589 4631 2313 389 95 -48 N ATOM 2810 CA LYS A 239 0.718 18.813 192.660 1.00 31.70 C ANISOU 2810 CA LYS A 239 5344 4524 2175 341 152 -53 C ATOM 2811 C LYS A 239 0.411 19.802 191.541 1.00 30.05 C ANISOU 2811 C LYS A 239 5071 4332 2013 340 150 -91 C ATOM 2812 O LYS A 239 0.361 19.428 190.370 1.00 27.50 O ANISOU 2812 O LYS A 239 4676 4038 1735 296 159 -107 O ATOM 2813 CB LYS A 239 -0.584 18.354 193.323 1.00 34.07 C ANISOU 2813 CB LYS A 239 5645 4895 2404 322 227 -29 C ATOM 2814 CG LYS A 239 -0.587 16.887 193.716 1.00 36.23 C ANISOU 2814 CG LYS A 239 5946 5177 2645 282 255 15 C ATOM 2815 CD LYS A 239 -1.990 16.381 194.008 1.00 38.24 C ANISOU 2815 CD LYS A 239 6166 5537 2827 229 343 37 C ATOM 2816 CE LYS A 239 -2.546 16.975 195.287 1.00 41.68 C ANISOU 2816 CE LYS A 239 6652 6007 3177 261 371 53 C ATOM 2817 NZ LYS A 239 -3.797 16.288 195.715 1.00 46.24 N1+ ANISOU 2817 NZ LYS A 239 7197 6707 3664 194 464 86 N1+ ATOM 2818 N LYS A 240 0.204 21.063 191.911 1.00 31.21 N ANISOU 2818 N LYS A 240 5257 4460 2140 393 138 -105 N ATOM 2819 CA LYS A 240 -0.092 22.114 190.942 1.00 22.73 C ANISOU 2819 CA LYS A 240 4151 3387 1098 409 132 -131 C ATOM 2820 C LYS A 240 1.082 22.343 189.997 1.00 26.05 C ANISOU 2820 C LYS A 240 4549 3769 1579 379 77 -145 C ATOM 2821 O LYS A 240 0.899 22.770 188.858 1.00 25.66 O ANISOU 2821 O LYS A 240 4451 3738 1562 363 79 -159 O ATOM 2822 CB LYS A 240 -0.448 23.420 191.654 1.00 23.52 C ANISOU 2822 CB LYS A 240 4330 3454 1154 489 126 -142 C ATOM 2823 CG LYS A 240 -1.808 23.423 192.327 1.00 40.23 C ANISOU 2823 CG LYS A 240 6448 5635 3202 529 192 -138 C ATOM 2824 CD LYS A 240 -2.057 24.735 193.054 1.00 42.47 C ANISOU 2824 CD LYS A 240 6825 5875 3435 628 184 -155 C ATOM 2825 CE LYS A 240 -3.428 24.756 193.712 1.00 43.77 C ANISOU 2825 CE LYS A 240 6983 6125 3522 678 258 -155 C ATOM 2826 NZ LYS A 240 -4.524 24.879 192.710 1.00 43.07 N ANISOU 2826 NZ LYS A 240 6807 6117 3443 690 301 -163 N ATOM 2827 N ALA A 241 2.288 22.057 190.480 1.00 21.92 N ANISOU 2827 N ALA A 241 4061 3208 1060 369 30 -139 N ATOM 2828 CA ALA A 241 3.492 22.222 189.680 1.00 23.00 C ANISOU 2828 CA ALA A 241 4168 3335 1236 331 -18 -154 C ATOM 2829 C ALA A 241 3.537 21.219 188.533 1.00 24.92 C ANISOU 2829 C ALA A 241 4323 3624 1523 283 4 -160 C ATOM 2830 O ALA A 241 3.791 21.593 187.388 1.00 24.87 O ANISOU 2830 O ALA A 241 4263 3639 1546 251 -2 -179 O ATOM 2831 CB ALA A 241 4.726 22.085 190.550 1.00 21.75 C ANISOU 2831 CB ALA A 241 4058 3154 1054 331 -75 -149 C ATOM 2832 N VAL A 242 3.286 19.948 188.838 1.00 26.15 N ANISOU 2832 N VAL A 242 4472 3792 1670 276 32 -145 N ATOM 2833 CA VAL A 242 3.318 18.913 187.808 1.00 25.26 C ANISOU 2833 CA VAL A 242 4295 3715 1588 233 55 -159 C ATOM 2834 C VAL A 242 2.092 19.008 186.914 1.00 27.04 C ANISOU 2834 C VAL A 242 4458 3998 1819 201 104 -175 C ATOM 2835 O VAL A 242 2.080 18.474 185.810 1.00 28.77 O ANISOU 2835 O VAL A 242 4614 4256 2061 157 119 -200 O ATOM 2836 CB VAL A 242 3.403 17.487 188.402 1.00 24.06 C ANISOU 2836 CB VAL A 242 4181 3548 1414 238 71 -138 C ATOM 2837 CG1 VAL A 242 4.654 17.338 189.251 1.00 20.84 C ANISOU 2837 CG1 VAL A 242 3833 3095 988 276 13 -120 C ATOM 2838 CG2 VAL A 242 2.158 17.154 189.200 1.00 25.14 C ANISOU 2838 CG2 VAL A 242 4346 3702 1504 237 123 -111 C ATOM 2839 N ARG A 243 1.058 19.690 187.391 1.00 28.55 N ANISOU 2839 N ARG A 243 4664 4203 1980 223 129 -165 N ATOM 2840 CA ARG A 243 -0.111 19.934 186.563 1.00 30.69 C ANISOU 2840 CA ARG A 243 4876 4542 2243 195 168 -181 C ATOM 2841 C ARG A 243 0.268 20.880 185.435 1.00 31.35 C ANISOU 2841 C ARG A 243 4933 4618 2359 193 138 -199 C ATOM 2842 O ARG A 243 -0.143 20.693 184.292 1.00 35.17 O ANISOU 2842 O ARG A 243 5357 5155 2851 144 156 -218 O ATOM 2843 CB ARG A 243 -1.259 20.514 187.386 1.00 33.69 C ANISOU 2843 CB ARG A 243 5285 4945 2571 235 202 -169 C ATOM 2844 CG ARG A 243 -2.272 19.479 187.837 1.00 36.10 C ANISOU 2844 CG ARG A 243 5565 5326 2824 184 265 -162 C ATOM 2845 CD ARG A 243 -3.417 20.130 188.582 1.00 39.71 C ANISOU 2845 CD ARG A 243 6044 5824 3220 223 306 -155 C ATOM 2846 NE ARG A 243 -4.171 19.169 189.380 1.00 43.43 N ANISOU 2846 NE ARG A 243 6510 6366 3624 167 368 -139 N ATOM 2847 CZ ARG A 243 -4.116 19.105 190.705 1.00 45.03 C ANISOU 2847 CZ ARG A 243 6776 6554 3780 205 379 -111 C ATOM 2848 NH1 ARG A 243 -3.335 19.940 191.375 1.00 45.05 N1+ ANISOU 2848 NH1 ARG A 243 6855 6466 3796 295 328 -104 N1+ ATOM 2849 NH2 ARG A 243 -4.834 18.206 191.362 1.00 47.29 N ANISOU 2849 NH2 ARG A 243 7052 6921 3993 142 442 -89 N ATOM 2850 N VAL A 244 1.069 21.890 185.761 1.00 28.74 N ANISOU 2850 N VAL A 244 4657 4227 2037 236 93 -192 N ATOM 2851 CA VAL A 244 1.493 22.874 184.774 1.00 26.75 C ANISOU 2851 CA VAL A 244 4395 3968 1801 230 66 -201 C ATOM 2852 C VAL A 244 2.391 22.254 183.711 1.00 27.44 C ANISOU 2852 C VAL A 244 4418 4091 1918 163 56 -219 C ATOM 2853 O VAL A 244 2.129 22.386 182.516 1.00 27.94 O ANISOU 2853 O VAL A 244 4431 4198 1985 126 67 -232 O ATOM 2854 CB VAL A 244 2.239 24.054 185.427 1.00 24.99 C ANISOU 2854 CB VAL A 244 4258 3673 1565 270 20 -194 C ATOM 2855 CG1 VAL A 244 2.850 24.948 184.360 1.00 23.50 C ANISOU 2855 CG1 VAL A 244 4063 3483 1381 240 -7 -201 C ATOM 2856 CG2 VAL A 244 1.298 24.853 186.313 1.00 25.65 C ANISOU 2856 CG2 VAL A 244 4416 3719 1609 350 33 -186 C ATOM 2857 N ILE A 245 3.439 21.565 184.150 1.00 28.14 N ANISOU 2857 N ILE A 245 4510 4164 2017 151 36 -222 N ATOM 2858 CA ILE A 245 4.454 21.064 183.230 1.00 29.12 C ANISOU 2858 CA ILE A 245 4578 4327 2158 102 25 -246 C ATOM 2859 C ILE A 245 3.965 19.872 182.402 1.00 30.41 C ANISOU 2859 C ILE A 245 4684 4538 2333 63 67 -272 C ATOM 2860 O ILE A 245 4.397 19.686 181.266 1.00 30.65 O ANISOU 2860 O ILE A 245 4662 4613 2370 15 73 -302 O ATOM 2861 CB ILE A 245 5.749 20.677 183.984 1.00 18.98 C ANISOU 2861 CB ILE A 245 3318 3024 867 110 -13 -245 C ATOM 2862 CG1 ILE A 245 6.891 20.442 182.993 1.00 27.44 C ANISOU 2862 CG1 ILE A 245 4329 4156 1941 58 -24 -276 C ATOM 2863 CG2 ILE A 245 5.528 19.467 184.884 1.00 19.12 C ANISOU 2863 CG2 ILE A 245 3372 3012 881 143 1 -233 C ATOM 2864 CD1 ILE A 245 7.093 21.592 182.023 1.00 18.81 C ANISOU 2864 CD1 ILE A 245 3200 3110 837 18 -32 -285 C ATOM 2865 N PHE A 246 3.059 19.071 182.952 1.00 32.01 N ANISOU 2865 N PHE A 246 4898 4738 2526 74 99 -266 N ATOM 2866 CA PHE A 246 2.497 17.969 182.183 1.00 33.76 C ANISOU 2866 CA PHE A 246 5068 5013 2745 29 139 -299 C ATOM 2867 C PHE A 246 1.570 18.517 181.112 1.00 32.10 C ANISOU 2867 C PHE A 246 4809 4841 2547 -16 158 -309 C ATOM 2868 O PHE A 246 1.531 18.005 179.996 1.00 35.17 O ANISOU 2868 O PHE A 246 5147 5252 2965 -65 173 -340 O ATOM 2869 CB PHE A 246 1.749 16.983 183.081 1.00 39.81 C ANISOU 2869 CB PHE A 246 5860 5779 3486 43 170 -286 C ATOM 2870 CG PHE A 246 2.637 15.962 183.740 1.00 46.67 C ANISOU 2870 CG PHE A 246 6787 6587 4357 76 158 -279 C ATOM 2871 CD1 PHE A 246 3.946 15.789 183.326 1.00 50.17 C ANISOU 2871 CD1 PHE A 246 7232 7007 4822 85 128 -300 C ATOM 2872 CD2 PHE A 246 2.156 15.169 184.769 1.00 51.63 C ANISOU 2872 CD2 PHE A 246 7476 7188 4954 95 181 -248 C ATOM 2873 CE1 PHE A 246 4.760 14.847 183.929 1.00 50.88 C ANISOU 2873 CE1 PHE A 246 7386 7042 4903 123 114 -294 C ATOM 2874 CE2 PHE A 246 2.967 14.226 185.376 1.00 51.19 C ANISOU 2874 CE2 PHE A 246 7499 7061 4890 128 167 -233 C ATOM 2875 CZ PHE A 246 4.270 14.066 184.955 1.00 50.30 C ANISOU 2875 CZ PHE A 246 7389 6922 4800 149 131 -257 C ATOM 2876 N THR A 247 0.828 19.565 181.455 1.00 29.00 N ANISOU 2876 N THR A 247 4449 4446 2125 4 157 -284 N ATOM 2877 CA THR A 247 -0.036 20.231 180.488 1.00 28.21 C ANISOU 2877 CA THR A 247 4343 4356 2020 -23 169 -285 C ATOM 2878 C THR A 247 0.791 20.809 179.344 1.00 27.78 C ANISOU 2878 C THR A 247 4275 4294 1987 -44 143 -290 C ATOM 2879 O THR A 247 0.427 20.672 178.176 1.00 27.13 O ANISOU 2879 O THR A 247 4203 4193 1913 -92 158 -300 O ATOM 2880 CB THR A 247 -0.859 21.349 181.144 1.00 29.14 C ANISOU 2880 CB THR A 247 4507 4471 2092 46 167 -258 C ATOM 2881 OG1 THR A 247 -1.755 20.777 182.103 1.00 31.77 O ANISOU 2881 OG1 THR A 247 4851 4822 2398 51 204 -253 O ATOM 2882 CG2 THR A 247 -1.663 22.105 180.103 1.00 19.75 C ANISOU 2882 CG2 THR A 247 3325 3299 881 54 169 -255 C ATOM 2883 N ILE A 248 1.908 21.441 179.693 1.00 27.36 N ANISOU 2883 N ILE A 248 4230 4233 1931 -13 107 -282 N ATOM 2884 CA ILE A 248 2.840 21.991 178.711 1.00 25.34 C ANISOU 2884 CA ILE A 248 3950 3989 1688 -44 86 -286 C ATOM 2885 C ILE A 248 3.255 20.940 177.685 1.00 27.83 C ANISOU 2885 C ILE A 248 4228 4302 2043 -115 109 -317 C ATOM 2886 O ILE A 248 3.267 21.202 176.480 1.00 28.55 O ANISOU 2886 O ILE A 248 4359 4354 2134 -169 119 -315 O ATOM 2887 CB ILE A 248 4.102 22.559 179.401 1.00 22.04 C ANISOU 2887 CB ILE A 248 3552 3563 1258 -16 47 -278 C ATOM 2888 CG1 ILE A 248 3.770 23.861 180.130 1.00 20.89 C ANISOU 2888 CG1 ILE A 248 3484 3369 1083 42 22 -248 C ATOM 2889 CG2 ILE A 248 5.218 22.791 178.394 1.00 21.61 C ANISOU 2889 CG2 ILE A 248 3441 3551 1218 -58 34 -290 C ATOM 2890 CD1 ILE A 248 3.385 24.990 179.209 1.00 19.30 C ANISOU 2890 CD1 ILE A 248 3300 3180 852 44 16 -233 C ATOM 2891 N MET A 249 3.572 19.745 178.171 1.00 30.32 N ANISOU 2891 N MET A 249 4528 4615 2378 -111 122 -340 N ATOM 2892 CA MET A 249 4.039 18.667 177.310 1.00 33.30 C ANISOU 2892 CA MET A 249 4922 4950 2779 -170 151 -376 C ATOM 2893 C MET A 249 2.905 18.026 176.512 1.00 37.29 C ANISOU 2893 C MET A 249 5601 5286 3281 -158 191 -364 C ATOM 2894 O MET A 249 3.080 17.689 175.341 1.00 39.59 O ANISOU 2894 O MET A 249 5972 5516 3555 20 176 -367 O ATOM 2895 CB MET A 249 4.758 17.607 178.141 1.00 18.37 C ANISOU 2895 CB MET A 249 2994 3095 891 -121 146 -403 C ATOM 2896 CG MET A 249 5.104 16.352 177.370 1.00 19.55 C ANISOU 2896 CG MET A 249 3154 3220 1054 -159 182 -456 C ATOM 2897 SD MET A 249 6.500 15.467 178.073 1.00 69.78 S ANISOU 2897 SD MET A 249 9537 9576 7399 -99 168 -486 S ATOM 2898 CE MET A 249 7.856 16.384 177.355 1.00 21.42 C ANISOU 2898 CE MET A 249 3495 3377 1266 -135 156 -466 C ATOM 2899 N ILE A 250 1.747 17.858 177.142 1.00 38.87 N ANISOU 2899 N ILE A 250 5757 5541 3472 -182 207 -363 N ATOM 2900 CA ILE A 250 0.592 17.289 176.454 1.00 19.02 C ANISOU 2900 CA ILE A 250 3381 2921 925 24 211 -344 C ATOM 2901 C ILE A 250 0.175 18.180 175.290 1.00 21.38 C ANISOU 2901 C ILE A 250 3632 3301 1190 27 196 -349 C ATOM 2902 O ILE A 250 -0.106 17.692 174.195 1.00 22.48 O ANISOU 2902 O ILE A 250 3727 3515 1300 51 198 -385 O ATOM 2903 CB ILE A 250 -0.605 17.095 177.403 1.00 21.38 C ANISOU 2903 CB ILE A 250 3693 3226 1204 9 239 -328 C ATOM 2904 CG1 ILE A 250 -0.307 15.995 178.419 1.00 21.52 C ANISOU 2904 CG1 ILE A 250 3510 3434 1232 316 184 -337 C ATOM 2905 CG2 ILE A 250 -1.853 16.727 176.620 1.00 19.78 C ANISOU 2905 CG2 ILE A 250 3431 3139 947 77 249 -351 C ATOM 2906 CD1 ILE A 250 -0.057 14.650 177.792 1.00 24.70 C ANISOU 2906 CD1 ILE A 250 3894 3869 1622 259 201 -400 C ATOM 2907 N VAL A 251 0.150 19.487 175.526 1.00 21.50 N ANISOU 2907 N VAL A 251 3636 3334 1200 -39 183 -322 N ATOM 2908 CA VAL A 251 -0.208 20.441 174.482 1.00 23.07 C ANISOU 2908 CA VAL A 251 3817 3591 1356 -21 164 -313 C ATOM 2909 C VAL A 251 0.837 20.428 173.367 1.00 23.93 C ANISOU 2909 C VAL A 251 3931 3694 1467 4 149 -325 C ATOM 2910 O VAL A 251 0.495 20.518 172.186 1.00 26.13 O ANISOU 2910 O VAL A 251 4181 4045 1701 19 145 -339 O ATOM 2911 CB VAL A 251 -0.369 21.866 175.050 1.00 19.53 C ANISOU 2911 CB VAL A 251 3342 3191 889 -62 145 -284 C ATOM 2912 CG1 VAL A 251 -0.612 22.866 173.934 1.00 19.98 C ANISOU 2912 CG1 VAL A 251 3409 3288 895 -44 122 -267 C ATOM 2913 CG2 VAL A 251 -1.520 21.904 176.040 1.00 19.75 C ANISOU 2913 CG2 VAL A 251 3349 3268 889 -31 160 -279 C ATOM 2914 N TYR A 252 2.107 20.298 173.743 1.00 21.70 N ANISOU 2914 N TYR A 252 3672 3352 1221 1 143 -324 N ATOM 2915 CA TYR A 252 3.177 20.126 172.767 1.00 19.52 C ANISOU 2915 CA TYR A 252 3375 3109 934 36 136 -347 C ATOM 2916 C TYR A 252 2.894 18.931 171.867 1.00 21.78 C ANISOU 2916 C TYR A 252 3611 3466 1199 40 160 -404 C ATOM 2917 O TYR A 252 3.040 19.013 170.649 1.00 26.34 O ANISOU 2917 O TYR A 252 4153 4116 1740 24 163 -427 O ATOM 2918 CB TYR A 252 4.529 19.940 173.458 1.00 19.52 C ANISOU 2918 CB TYR A 252 3393 3061 964 42 128 -348 C ATOM 2919 CG TYR A 252 5.552 19.241 172.586 1.00 20.90 C ANISOU 2919 CG TYR A 252 3524 3297 1120 50 141 -396 C ATOM 2920 CD1 TYR A 252 6.337 19.958 171.693 1.00 19.58 C ANISOU 2920 CD1 TYR A 252 3334 3193 912 40 137 -397 C ATOM 2921 CD2 TYR A 252 5.724 17.861 172.650 1.00 19.32 C ANISOU 2921 CD2 TYR A 252 3316 3091 933 55 167 -444 C ATOM 2922 CE1 TYR A 252 7.266 19.323 170.889 1.00 24.04 C ANISOU 2922 CE1 TYR A 252 3853 3824 1456 21 163 -447 C ATOM 2923 CE2 TYR A 252 6.642 17.219 171.847 1.00 25.66 C ANISOU 2923 CE2 TYR A 252 4093 3944 1713 50 191 -498 C ATOM 2924 CZ TYR A 252 7.416 17.953 170.972 1.00 25.25 C ANISOU 2924 CZ TYR A 252 3998 3967 1630 29 190 -501 C ATOM 2925 OH TYR A 252 8.338 17.312 170.174 1.00 25.21 O ANISOU 2925 OH TYR A 252 3938 4023 1617 17 222 -556 O ATOM 2926 N PHE A 253 2.510 17.816 172.484 1.00 21.16 N ANISOU 2926 N PHE A 253 3535 3362 1142 51 176 -427 N ATOM 2927 CA PHE A 253 2.155 16.608 171.748 1.00 22.08 C ANISOU 2927 CA PHE A 253 3624 3532 1235 43 198 -491 C ATOM 2928 C PHE A 253 1.047 16.899 170.746 1.00 24.08 C ANISOU 2928 C PHE A 253 3809 3877 1461 2 194 -499 C ATOM 2929 O PHE A 253 1.139 16.522 169.583 1.00 23.23 O ANISOU 2929 O PHE A 253 3649 3835 1341 -33 199 -544 O ATOM 2930 CB PHE A 253 1.716 15.495 172.705 1.00 22.03 C ANISOU 2930 CB PHE A 253 3640 3483 1249 68 211 -504 C ATOM 2931 CG PHE A 253 2.856 14.725 173.312 1.00 21.84 C ANISOU 2931 CG PHE A 253 3649 3390 1260 111 212 -518 C ATOM 2932 CD1 PHE A 253 4.003 14.462 172.582 1.00 22.04 C ANISOU 2932 CD1 PHE A 253 3676 3416 1282 102 221 -557 C ATOM 2933 CD2 PHE A 253 2.778 14.264 174.615 1.00 19.58 C ANISOU 2933 CD2 PHE A 253 3380 3062 998 176 201 -494 C ATOM 2934 CE1 PHE A 253 5.050 13.752 173.141 1.00 20.05 C ANISOU 2934 CE1 PHE A 253 3471 3094 1052 131 228 -571 C ATOM 2935 CE2 PHE A 253 3.822 13.554 175.180 1.00 19.62 C ANISOU 2935 CE2 PHE A 253 3370 3058 1025 256 182 -514 C ATOM 2936 CZ PHE A 253 4.959 13.298 174.443 1.00 19.86 C ANISOU 2936 CZ PHE A 253 3487 3005 1053 192 212 -540 C ATOM 2937 N LEU A 254 0.006 17.584 171.206 1.00 24.75 N ANISOU 2937 N LEU A 254 3898 3975 1532 6 186 -459 N ATOM 2938 CA LEU A 254 -1.122 17.935 170.353 1.00 25.13 C ANISOU 2938 CA LEU A 254 3876 4125 1545 -21 175 -463 C ATOM 2939 C LEU A 254 -0.688 18.690 169.097 1.00 26.07 C ANISOU 2939 C LEU A 254 3972 4296 1637 -31 157 -458 C ATOM 2940 O LEU A 254 -1.208 18.447 168.008 1.00 28.23 O ANISOU 2940 O LEU A 254 4178 4667 1880 -65 151 -490 O ATOM 2941 CB LEU A 254 -2.134 18.768 171.142 1.00 20.91 C ANISOU 2941 CB LEU A 254 3356 3597 992 2 169 -416 C ATOM 2942 CG LEU A 254 -3.266 19.433 170.358 1.00 21.62 C ANISOU 2942 CG LEU A 254 3374 3806 1034 1 148 -407 C ATOM 2943 CD1 LEU A 254 -4.208 18.393 169.774 1.00 22.28 C ANISOU 2943 CD1 LEU A 254 3359 4006 1102 -47 155 -461 C ATOM 2944 CD2 LEU A 254 -4.021 20.405 171.247 1.00 21.66 C ANISOU 2944 CD2 LEU A 254 3401 3811 1019 41 144 -360 C ATOM 2945 N PHE A 255 0.278 19.591 169.247 1.00 25.05 N ANISOU 2945 N PHE A 255 3903 4107 1509 -9 148 -419 N ATOM 2946 CA PHE A 255 0.674 20.474 168.154 1.00 24.82 C ANISOU 2946 CA PHE A 255 3874 4120 1438 -17 133 -401 C ATOM 2947 C PHE A 255 1.701 19.866 167.201 1.00 27.54 C ANISOU 2947 C PHE A 255 4174 4506 1785 -47 150 -446 C ATOM 2948 O PHE A 255 1.743 20.221 166.024 1.00 30.16 O ANISOU 2948 O PHE A 255 4480 4911 2070 -69 147 -449 O ATOM 2949 CB PHE A 255 1.224 21.789 168.716 1.00 24.34 C ANISOU 2949 CB PHE A 255 3912 3977 1359 6 116 -341 C ATOM 2950 CG PHE A 255 0.162 22.798 169.056 1.00 25.51 C ANISOU 2950 CG PHE A 255 4109 4116 1468 12 97 -297 C ATOM 2951 CD1 PHE A 255 -0.748 22.553 170.070 1.00 25.66 C ANISOU 2951 CD1 PHE A 255 4110 4129 1508 16 103 -297 C ATOM 2952 CD2 PHE A 255 0.081 23.998 168.368 1.00 27.16 C ANISOU 2952 CD2 PHE A 255 4373 4334 1614 6 74 -256 C ATOM 2953 CE1 PHE A 255 -1.723 23.482 170.387 1.00 25.63 C ANISOU 2953 CE1 PHE A 255 4109 4161 1468 26 87 -264 C ATOM 2954 CE2 PHE A 255 -0.892 24.931 168.681 1.00 26.86 C ANISOU 2954 CE2 PHE A 255 4354 4316 1536 -1 53 -219 C ATOM 2955 CZ PHE A 255 -1.794 24.672 169.692 1.00 25.42 C ANISOU 2955 CZ PHE A 255 4120 4160 1379 23 60 -227 C ATOM 2956 N TRP A 256 2.527 18.952 167.700 1.00 27.06 N ANISOU 2956 N TRP A 256 4111 4402 1767 -47 171 -482 N ATOM 2957 CA TRP A 256 3.642 18.450 166.901 1.00 28.14 C ANISOU 2957 CA TRP A 256 4214 4578 1901 -71 194 -527 C ATOM 2958 C TRP A 256 3.573 16.961 166.548 1.00 28.83 C ANISOU 2958 C TRP A 256 4272 4682 2000 -89 221 -608 C ATOM 2959 O TRP A 256 4.365 16.483 165.734 1.00 29.36 O ANISOU 2959 O TRP A 256 4313 4790 2052 -106 246 -659 O ATOM 2960 CB TRP A 256 4.963 18.731 167.619 1.00 21.28 C ANISOU 2960 CB TRP A 256 3376 3656 1053 -50 198 -510 C ATOM 2961 CG TRP A 256 5.553 20.074 167.300 1.00 25.51 C ANISOU 2961 CG TRP A 256 3928 4212 1553 -59 184 -459 C ATOM 2962 CD1 TRP A 256 5.814 21.088 168.177 1.00 24.72 C ANISOU 2962 CD1 TRP A 256 3892 4050 1450 -33 158 -403 C ATOM 2963 CD2 TRP A 256 5.954 20.548 166.009 1.00 26.31 C ANISOU 2963 CD2 TRP A 256 3994 4400 1603 -99 196 -460 C ATOM 2964 NE1 TRP A 256 6.358 22.161 167.512 1.00 24.45 N ANISOU 2964 NE1 TRP A 256 3869 4056 1366 -53 153 -370 N ATOM 2965 CE2 TRP A 256 6.453 21.854 166.177 1.00 22.26 C ANISOU 2965 CE2 TRP A 256 3530 3870 1056 -98 178 -400 C ATOM 2966 CE3 TRP A 256 5.942 19.993 164.724 1.00 23.00 C ANISOU 2966 CE3 TRP A 256 3516 4071 1151 -136 221 -508 C ATOM 2967 CZ2 TRP A 256 6.934 22.613 165.115 1.00 23.07 C ANISOU 2967 CZ2 TRP A 256 3626 4044 1094 -139 188 -378 C ATOM 2968 CZ3 TRP A 256 6.417 20.749 163.671 1.00 23.78 C ANISOU 2968 CZ3 TRP A 256 3603 4244 1186 -173 230 -489 C ATOM 2969 CH2 TRP A 256 6.907 22.044 163.872 1.00 23.81 C ANISOU 2969 CH2 TRP A 256 3659 4229 1157 -177 216 -420 C ATOM 2970 N THR A 257 2.643 16.227 167.148 1.00 27.42 N ANISOU 2970 N THR A 257 4106 4473 1838 -86 219 -625 N ATOM 2971 CA THR A 257 2.525 14.800 166.851 1.00 25.98 C ANISOU 2971 CA THR A 257 3925 4291 1657 -106 243 -708 C ATOM 2972 C THR A 257 1.929 14.509 165.467 1.00 28.78 C ANISOU 2972 C THR A 257 4224 4745 1967 -165 245 -762 C ATOM 2973 O THR A 257 2.418 13.613 164.775 1.00 30.02 O ANISOU 2973 O THR A 257 4387 4911 2109 -180 270 -839 O ATOM 2974 CB THR A 257 1.687 14.061 167.910 1.00 24.86 C ANISOU 2974 CB THR A 257 3821 4093 1533 -97 243 -712 C ATOM 2975 OG1 THR A 257 2.176 14.386 169.217 1.00 23.63 O ANISOU 2975 OG1 THR A 257 3723 3851 1405 -38 238 -658 O ATOM 2976 CG2 THR A 257 1.771 12.558 167.705 1.00 25.68 C ANISOU 2976 CG2 THR A 257 3958 4167 1631 -109 267 -803 C ATOM 2977 N PRO A 258 0.872 15.244 165.053 1.00 30.36 N ANISOU 2977 N PRO A 258 4377 5022 2137 -192 218 -729 N ATOM 2978 CA PRO A 258 0.375 14.954 163.702 1.00 31.89 C ANISOU 2978 CA PRO A 258 4519 5321 2276 -249 215 -784 C ATOM 2979 C PRO A 258 1.430 15.165 162.617 1.00 33.31 C ANISOU 2979 C PRO A 258 4691 5542 2423 -252 232 -804 C ATOM 2980 O PRO A 258 1.402 14.464 161.609 1.00 26.30 O ANISOU 2980 O PRO A 258 3785 4712 1494 -293 246 -880 O ATOM 2981 CB PRO A 258 -0.793 15.940 163.531 1.00 31.03 C ANISOU 2981 CB PRO A 258 4367 5293 2132 -252 178 -727 C ATOM 2982 CG PRO A 258 -0.609 16.962 164.596 1.00 32.09 C ANISOU 2982 CG PRO A 258 4543 5352 2297 -189 167 -641 C ATOM 2983 CD PRO A 258 0.013 16.227 165.735 1.00 31.11 C ANISOU 2983 CD PRO A 258 4469 5118 2233 -168 191 -654 C ATOM 2984 N TYR A 259 2.356 16.097 162.825 1.00 31.62 N ANISOU 2984 N TYR A 259 4493 5303 2218 -217 234 -744 N ATOM 2985 CA TYR A 259 3.435 16.297 161.864 1.00 29.15 C ANISOU 2985 CA TYR A 259 4166 5042 1868 -228 259 -763 C ATOM 2986 C TYR A 259 4.418 15.131 161.874 1.00 28.96 C ANISOU 2986 C TYR A 259 4156 4984 1863 -216 302 -844 C ATOM 2987 O TYR A 259 4.801 14.628 160.822 1.00 30.11 O ANISOU 2987 O TYR A 259 4285 5192 1964 -237 331 -912 O ATOM 2988 CB TYR A 259 4.187 17.599 162.140 1.00 27.23 C ANISOU 2988 CB TYR A 259 3941 4785 1622 -207 252 -681 C ATOM 2989 CG TYR A 259 5.451 17.729 161.320 1.00 25.62 C ANISOU 2989 CG TYR A 259 3713 4639 1380 -227 288 -701 C ATOM 2990 CD1 TYR A 259 5.400 18.102 159.984 1.00 26.69 C ANISOU 2990 CD1 TYR A 259 3826 4877 1436 -266 294 -707 C ATOM 2991 CD2 TYR A 259 6.696 17.465 161.879 1.00 25.68 C ANISOU 2991 CD2 TYR A 259 3720 4615 1424 -208 317 -717 C ATOM 2992 CE1 TYR A 259 6.553 18.215 159.229 1.00 27.47 C ANISOU 2992 CE1 TYR A 259 3900 5045 1491 -290 335 -726 C ATOM 2993 CE2 TYR A 259 7.854 17.575 161.131 1.00 26.13 C ANISOU 2993 CE2 TYR A 259 3739 4749 1440 -230 356 -741 C ATOM 2994 CZ TYR A 259 7.777 17.951 159.808 1.00 27.19 C ANISOU 2994 CZ TYR A 259 3851 4986 1496 -274 368 -745 C ATOM 2995 OH TYR A 259 8.928 18.063 159.062 1.00 28.13 O ANISOU 2995 OH TYR A 259 3928 5195 1565 -301 416 -769 O ATOM 2996 N ASN A 260 4.832 14.713 163.066 1.00 29.37 N ANISOU 2996 N ASN A 260 4249 4937 1972 -172 309 -839 N ATOM 2997 CA ASN A 260 5.800 13.629 163.202 1.00 30.40 C ANISOU 2997 CA ASN A 260 4414 5022 2116 -136 349 -912 C ATOM 2998 C ASN A 260 5.315 12.330 162.570 1.00 32.27 C ANISOU 2998 C ASN A 260 4680 5255 2327 -151 368 -1015 C ATOM 2999 O ASN A 260 6.100 11.586 161.986 1.00 34.48 O ANISOU 2999 O ASN A 260 4980 5540 2582 -128 409 -1095 O ATOM 3000 CB ASN A 260 6.128 13.393 164.677 1.00 30.27 C ANISOU 3000 CB ASN A 260 4454 4893 2152 -81 344 -883 C ATOM 3001 CG ASN A 260 6.941 14.521 165.282 1.00 31.33 C ANISOU 3001 CG ASN A 260 4571 5030 2305 -67 331 -806 C ATOM 3002 OD1 ASN A 260 7.792 15.116 164.619 1.00 31.73 O ANISOU 3002 OD1 ASN A 260 4571 5156 2329 -84 347 -801 O ATOM 3003 ND2 ASN A 260 6.679 14.826 166.547 1.00 33.00 N ANISOU 3003 ND2 ASN A 260 4824 5162 2551 -40 304 -748 N ATOM 3004 N ILE A 261 4.019 12.066 162.676 1.00 32.34 N ANISOU 3004 N ILE A 261 4693 5259 2335 -190 340 -1019 N ATOM 3005 CA ILE A 261 3.460 10.827 162.155 1.00 33.63 C ANISOU 3005 CA ILE A 261 4893 5414 2472 -222 351 -1123 C ATOM 3006 C ILE A 261 3.318 10.851 160.632 1.00 35.71 C ANISOU 3006 C ILE A 261 5111 5791 2665 -276 358 -1179 C ATOM 3007 O ILE A 261 3.686 9.885 159.963 1.00 38.20 O ANISOU 3007 O ILE A 261 5471 6096 2946 -273 388 -1282 O ATOM 3008 CB ILE A 261 2.095 10.518 162.800 1.00 27.13 C ANISOU 3008 CB ILE A 261 4075 4568 1664 -268 321 -1114 C ATOM 3009 CG1 ILE A 261 2.292 10.112 164.262 1.00 26.95 C ANISOU 3009 CG1 ILE A 261 4122 4423 1693 -209 323 -1087 C ATOM 3010 CG2 ILE A 261 1.381 9.410 162.048 1.00 28.49 C ANISOU 3010 CG2 ILE A 261 4269 4760 1795 -337 324 -1225 C ATOM 3011 CD1 ILE A 261 1.069 9.499 164.901 1.00 28.54 C ANISOU 3011 CD1 ILE A 261 4341 4600 1902 -261 309 -1103 C ATOM 3012 N VAL A 262 2.807 11.950 160.080 1.00 35.39 N ANISOU 3012 N VAL A 262 4998 5854 2595 -316 329 -1115 N ATOM 3013 CA VAL A 262 2.571 12.014 158.637 1.00 35.85 C ANISOU 3013 CA VAL A 262 5019 6030 2572 -366 330 -1161 C ATOM 3014 C VAL A 262 3.869 11.980 157.838 1.00 35.38 C ANISOU 3014 C VAL A 262 4963 6005 2474 -339 376 -1201 C ATOM 3015 O VAL A 262 3.877 11.529 156.696 1.00 36.72 O ANISOU 3015 O VAL A 262 5133 6246 2573 -369 394 -1280 O ATOM 3016 CB VAL A 262 1.772 13.272 158.220 1.00 37.08 C ANISOU 3016 CB VAL A 262 5112 6289 2690 -395 286 -1076 C ATOM 3017 CG1 VAL A 262 0.378 13.248 158.829 1.00 38.32 C ANISOU 3017 CG1 VAL A 262 5247 6448 2865 -424 245 -1053 C ATOM 3018 CG2 VAL A 262 2.514 14.541 158.594 1.00 38.56 C ANISOU 3018 CG2 VAL A 262 5292 6464 2896 -350 284 -972 C ATOM 3019 N ILE A 263 4.965 12.444 158.428 1.00 34.85 N ANISOU 3019 N ILE A 263 4897 5899 2447 -286 399 -1151 N ATOM 3020 CA ILE A 263 6.246 12.378 157.735 1.00 37.47 C ANISOU 3020 CA ILE A 263 5216 6280 2739 -262 452 -1193 C ATOM 3021 C ILE A 263 6.843 10.986 157.896 1.00 31.39 C ANISOU 3021 C ILE A 263 4515 5432 1982 -206 498 -1304 C ATOM 3022 O ILE A 263 7.659 10.558 157.086 1.00 38.93 O ANISOU 3022 O ILE A 263 5472 6434 2886 -183 550 -1380 O ATOM 3023 CB ILE A 263 7.246 13.441 158.241 1.00 29.85 C ANISOU 3023 CB ILE A 263 4214 5328 1801 -239 459 -1105 C ATOM 3024 CG1 ILE A 263 7.720 13.120 159.659 1.00 31.92 C ANISOU 3024 CG1 ILE A 263 4512 5472 2145 -179 461 -1086 C ATOM 3025 CG2 ILE A 263 6.628 14.827 158.170 1.00 29.39 C ANISOU 3025 CG2 ILE A 263 4126 5314 1727 -280 413 -996 C ATOM 3026 CD1 ILE A 263 8.769 14.072 160.176 1.00 28.16 C ANISOU 3026 CD1 ILE A 263 3996 5014 1688 -165 467 -1015 C ATOM 3027 N LEU A 264 6.424 10.279 158.940 1.00 33.94 N ANISOU 3027 N LEU A 264 4904 5630 2361 -176 482 -1314 N ATOM 3028 CA LEU A 264 6.865 8.908 159.149 1.00 36.67 C ANISOU 3028 CA LEU A 264 5350 5872 2711 -111 520 -1419 C ATOM 3029 C LEU A 264 6.168 7.995 158.147 1.00 40.45 C ANISOU 3029 C LEU A 264 5876 6366 3128 -153 522 -1533 C ATOM 3030 O LEU A 264 6.764 7.052 157.628 1.00 41.71 O ANISOU 3030 O LEU A 264 6108 6491 3250 -102 569 -1644 O ATOM 3031 CB LEU A 264 6.583 8.461 160.584 1.00 35.80 C ANISOU 3031 CB LEU A 264 5314 5621 2668 -68 498 -1390 C ATOM 3032 CG LEU A 264 7.259 7.178 161.068 1.00 36.83 C ANISOU 3032 CG LEU A 264 5573 5616 2805 32 537 -1476 C ATOM 3033 CD1 LEU A 264 8.770 7.259 160.893 1.00 36.92 C ANISOU 3033 CD1 LEU A 264 5566 5654 2809 106 604 -1496 C ATOM 3034 CD2 LEU A 264 6.902 6.926 162.524 1.00 35.22 C ANISOU 3034 CD2 LEU A 264 5430 5297 2655 65 506 -1433 C ATOM 3035 N LEU A 265 4.900 8.292 157.877 1.00 42.66 N ANISOU 3035 N LEU A 265 6115 6700 3393 -245 472 -1510 N ATOM 3036 CA LEU A 265 4.143 7.593 156.845 1.00 45.49 C ANISOU 3036 CA LEU A 265 6498 7103 3684 -313 464 -1614 C ATOM 3037 C LEU A 265 4.693 7.929 155.462 1.00 50.86 C ANISOU 3037 C LEU A 265 7137 7911 4278 -323 495 -1651 C ATOM 3038 O LEU A 265 4.783 7.066 154.591 1.00 55.56 O ANISOU 3038 O LEU A 265 7791 8512 4806 -326 520 -1774 O ATOM 3039 CB LEU A 265 2.658 7.959 156.921 1.00 43.66 C ANISOU 3039 CB LEU A 265 6211 6927 3452 -414 404 -1571 C ATOM 3040 CG LEU A 265 1.721 7.110 157.787 1.00 42.66 C ANISOU 3040 CG LEU A 265 6139 6702 3368 -453 378 -1605 C ATOM 3041 CD1 LEU A 265 2.163 7.083 159.242 1.00 40.97 C ANISOU 3041 CD1 LEU A 265 5967 6362 3236 -375 384 -1541 C ATOM 3042 CD2 LEU A 265 0.291 7.624 157.674 1.00 42.05 C ANISOU 3042 CD2 LEU A 265 5974 6729 3274 -560 328 -1561 C ATOM 3043 N ASN A 266 5.066 9.191 155.275 1.00 52.48 N ANISOU 3043 N ASN A 266 7250 8213 4476 -328 493 -1548 N ATOM 3044 CA ASN A 266 5.568 9.680 153.994 1.00 56.19 C ANISOU 3044 CA ASN A 266 7674 8819 4855 -346 521 -1564 C ATOM 3045 C ASN A 266 6.995 9.210 153.717 1.00 58.08 C ANISOU 3045 C ASN A 266 7940 9054 5076 -269 599 -1632 C ATOM 3046 O ASN A 266 7.527 9.408 152.625 1.00 58.75 O ANISOU 3046 O ASN A 266 7996 9252 5075 -278 638 -1668 O ATOM 3047 CB ASN A 266 5.501 11.211 153.960 1.00 56.52 C ANISOU 3047 CB ASN A 266 7630 8951 4893 -375 490 -1427 C ATOM 3048 CG ASN A 266 5.716 11.782 152.572 1.00 57.54 C ANISOU 3048 CG ASN A 266 7722 9230 4910 -412 506 -1431 C ATOM 3049 OD1 ASN A 266 5.552 11.091 151.568 1.00 59.05 O ANISOU 3049 OD1 ASN A 266 7941 9477 5019 -435 523 -1534 O ATOM 3050 ND2 ASN A 266 6.082 13.057 152.511 1.00 56.84 N ANISOU 3050 ND2 ASN A 266 7586 9204 4808 -420 500 -1321 N ATOM 3051 N THR A 267 7.612 8.585 154.714 1.00 59.51 N ANISOU 3051 N THR A 267 8176 9108 5327 -189 625 -1651 N ATOM 3052 CA THR A 267 8.989 8.128 154.586 1.00 62.84 C ANISOU 3052 CA THR A 267 8615 9525 5736 -99 704 -1715 C ATOM 3053 C THR A 267 9.076 6.603 154.591 1.00 68.38 C ANISOU 3053 C THR A 267 9456 10099 6427 -26 741 -1856 C ATOM 3054 O THR A 267 9.208 5.978 153.539 1.00 69.77 O ANISOU 3054 O THR A 267 9677 10312 6520 -17 781 -1969 O ATOM 3055 CB THR A 267 9.878 8.697 155.719 1.00 59.00 C ANISOU 3055 CB THR A 267 8082 9005 5330 -46 715 -1625 C ATOM 3056 OG1 THR A 267 9.868 10.130 155.665 1.00 56.50 O ANISOU 3056 OG1 THR A 267 7659 8795 5014 -112 682 -1504 O ATOM 3057 CG2 THR A 267 11.306 8.210 155.582 1.00 59.08 C ANISOU 3057 CG2 THR A 267 8089 9032 5326 49 803 -1696 C ATOM 3058 N PHE A 268 8.988 6.010 155.777 1.00 72.21 N ANISOU 3058 N PHE A 268 10024 10426 6986 30 727 -1850 N ATOM 3059 CA PHE A 268 9.248 4.585 155.939 1.00 79.06 C ANISOU 3059 CA PHE A 268 11046 11147 7845 122 766 -1981 C ATOM 3060 C PHE A 268 8.084 3.711 155.477 1.00 85.26 C ANISOU 3060 C PHE A 268 11930 11876 8589 64 719 -2081 C ATOM 3061 O PHE A 268 8.269 2.782 154.689 1.00 86.97 O ANISOU 3061 O PHE A 268 12240 12066 8739 97 757 -2226 O ATOM 3062 CB PHE A 268 9.578 4.276 157.401 1.00 78.44 C ANISOU 3062 CB PHE A 268 11016 10937 7850 193 768 -1952 C ATOM 3063 N GLN A 269 6.887 4.015 155.967 1.00 89.80 N ANISOU 3063 N GLN A 269 12477 12441 9204 -29 638 -2012 N ATOM 3064 CA GLN A 269 5.727 3.160 155.737 1.00 92.53 C ANISOU 3064 CA GLN A 269 12891 12740 9527 -112 590 -2112 C ATOM 3065 C GLN A 269 5.075 3.377 154.374 1.00 92.37 C ANISOU 3065 C GLN A 269 12824 12854 9419 -214 572 -2152 C ATOM 3066 O GLN A 269 4.083 2.722 154.047 1.00 95.39 O ANISOU 3066 O GLN A 269 13249 13223 9773 -308 532 -2241 O ATOM 3067 CB GLN A 269 4.696 3.367 156.848 1.00 91.25 C ANISOU 3067 CB GLN A 269 12695 12536 9440 -186 528 -2032 C ATOM 3068 CG GLN A 269 5.186 2.912 158.210 1.00 93.06 C ANISOU 3068 CG GLN A 269 12996 12623 9742 -95 538 -2024 C ATOM 3069 CD GLN A 269 4.167 3.148 159.303 1.00 94.27 C ANISOU 3069 CD GLN A 269 13110 12750 9960 -176 487 -1945 C ATOM 3070 OE1 GLN A 269 3.292 4.004 159.178 1.00 95.32 O ANISOU 3070 OE1 GLN A 269 13138 12985 10095 -274 450 -1852 O ATOM 3071 NE2 GLN A 269 4.277 2.388 160.385 1.00 95.64 N ANISOU 3071 NE2 GLN A 269 13368 12787 10182 -132 488 -1987 N ATOM 3072 N GLU A 270 5.626 4.292 153.582 1.00 88.13 N ANISOU 3072 N GLU A 270 12185 12467 8833 -218 605 -2104 N ATOM 3073 CA GLU A 270 5.175 4.457 152.206 1.00 86.10 C ANISOU 3073 CA GLU A 270 11890 12353 8473 -303 597 -2159 C ATOM 3074 C GLU A 270 5.822 3.368 151.359 1.00 87.73 C ANISOU 3074 C GLU A 270 12220 12516 8596 -236 655 -2325 C ATOM 3075 O GLU A 270 5.397 3.093 150.237 1.00 89.57 O ANISOU 3075 O GLU A 270 12474 12828 8731 -298 647 -2418 O ATOM 3076 CB GLU A 270 5.517 5.850 151.674 1.00 83.28 C ANISOU 3076 CB GLU A 270 11391 12167 8084 -328 607 -2045 C ATOM 3077 CG GLU A 270 4.835 6.193 150.354 1.00 82.30 C ANISOU 3077 CG GLU A 270 11221 12201 7848 -423 581 -2073 C ATOM 3078 CD GLU A 270 5.128 7.607 149.886 1.00 78.47 C ANISOU 3078 CD GLU A 270 10617 11871 7329 -443 581 -1950 C ATOM 3079 OE1 GLU A 270 5.697 8.391 150.674 1.00 75.15 O ANISOU 3079 OE1 GLU A 270 10141 11430 6982 -403 590 -1837 O ATOM 3080 OE2 GLU A 270 4.787 7.935 148.729 1.00 78.55 O1+ ANISOU 3080 OE2 GLU A 270 10599 12017 7228 -500 570 -1969 O1+ ATOM 3081 N PHE A 271 6.859 2.750 151.915 1.00 87.94 N ANISOU 3081 N PHE A 271 12338 12417 8659 -100 714 -2366 N ATOM 3082 CA PHE A 271 7.508 1.612 151.282 1.00 90.46 C ANISOU 3082 CA PHE A 271 12800 12664 8908 -8 777 -2534 C ATOM 3083 C PHE A 271 6.788 0.328 151.675 1.00 93.10 C ANISOU 3083 C PHE A 271 13286 12830 9259 -21 732 -2669 C ATOM 3084 O PHE A 271 6.714 -0.621 150.894 1.00 94.79 O ANISOU 3084 O PHE A 271 13621 12999 9394 -11 743 -2835 O ATOM 3085 CB PHE A 271 8.984 1.541 151.675 1.00 89.70 C ANISOU 3085 CB PHE A 271 12713 12532 8838 140 877 -2535 C ATOM 3086 N PHE A 272 6.259 0.310 152.896 1.00 93.53 N ANISOU 3086 N PHE A 272 13333 12790 9413 -48 680 -2603 N ATOM 3087 CA PHE A 272 5.471 -0.818 153.379 1.00 97.39 C ANISOU 3087 CA PHE A 272 13941 13128 9935 -95 629 -2722 C ATOM 3088 C PHE A 272 4.191 -0.959 152.561 1.00106.88 C ANISOU 3088 C PHE A 272 15121 14407 11082 -278 569 -2783 C ATOM 3089 O PHE A 272 3.894 -2.029 152.027 1.00108.43 O ANISOU 3089 O PHE A 272 15442 14525 11231 -313 559 -2957 O ATOM 3090 CB PHE A 272 5.132 -0.647 154.863 1.00 88.36 C ANISOU 3090 CB PHE A 272 12766 11900 8907 -108 592 -2621 C ATOM 3091 CG PHE A 272 6.261 -0.996 155.793 1.00 81.39 C ANISOU 3091 CG PHE A 272 11962 10887 8077 74 638 -2621 C ATOM 3092 CD1 PHE A 272 7.512 -1.331 155.299 1.00 79.37 C ANISOU 3092 CD1 PHE A 272 11784 10604 7769 232 722 -2690 C ATOM 3093 CD2 PHE A 272 6.066 -1.001 157.166 1.00 76.76 C ANISOU 3093 CD2 PHE A 272 11371 10210 7586 83 606 -2555 C ATOM 3094 CE1 PHE A 272 8.549 -1.655 156.156 1.00 77.30 C ANISOU 3094 CE1 PHE A 272 11597 10224 7550 397 778 -2688 C ATOM 3095 CE2 PHE A 272 7.098 -1.326 158.027 1.00 74.61 C ANISOU 3095 CE2 PHE A 272 11171 9824 7355 258 643 -2559 C ATOM 3096 CZ PHE A 272 8.341 -1.653 157.522 1.00 75.22 C ANISOU 3096 CZ PHE A 272 11332 9869 7379 417 731 -2622 C ATOM 3097 N GLY A 273 3.440 0.135 152.471 1.00115.11 N ANISOU 3097 N GLY A 273 16005 15602 12127 -392 530 -2644 N ATOM 3098 CA GLY A 273 2.204 0.174 151.710 1.00117.18 C ANISOU 3098 CA GLY A 273 16220 15973 12332 -566 475 -2681 C ATOM 3099 C GLY A 273 1.891 1.601 151.309 1.00116.71 C ANISOU 3099 C GLY A 273 15991 16106 12248 -606 453 -2520 C ATOM 3100 O GLY A 273 2.807 2.384 151.059 1.00121.63 O ANISOU 3100 O GLY A 273 16560 16797 12858 -514 496 -2440 O ATOM 3101 N LEU A 274 0.604 1.935 151.238 1.00105.88 N ANISOU 3101 N LEU A 274 14530 14830 10868 -756 392 -2483 N ATOM 3102 CA LEU A 274 0.164 3.306 150.965 1.00 95.02 C ANISOU 3102 CA LEU A 274 12996 13633 9475 -793 364 -2336 C ATOM 3103 C LEU A 274 0.694 3.868 149.645 1.00 90.08 C ANISOU 3103 C LEU A 274 12330 13157 8737 -771 389 -2347 C ATOM 3104 O LEU A 274 0.758 5.085 149.471 1.00 89.08 O ANISOU 3104 O LEU A 274 12089 13158 8601 -763 384 -2221 O ATOM 3105 CB LEU A 274 0.588 4.235 152.106 1.00 88.48 C ANISOU 3105 CB LEU A 274 12094 12775 8750 -717 377 -2172 C ATOM 3106 CG LEU A 274 -0.465 4.656 153.128 1.00 83.80 C ANISOU 3106 CG LEU A 274 11426 12184 8232 -785 330 -2071 C ATOM 3107 CD1 LEU A 274 -0.994 3.449 153.882 1.00 83.52 C ANISOU 3107 CD1 LEU A 274 11477 12017 8241 -856 325 -2169 C ATOM 3108 CD2 LEU A 274 0.121 5.677 154.085 1.00 80.39 C ANISOU 3108 CD2 LEU A 274 10932 11732 7882 -695 345 -1918 C ATOM 3109 N SER A 275 1.067 2.990 148.720 1.00 87.42 N ANISOU 3109 N SER A 275 12101 12803 8312 -759 415 -2501 N ATOM 3110 CA SER A 275 1.737 3.417 147.494 1.00 84.91 C ANISOU 3110 CA SER A 275 11764 12619 7880 -725 455 -2524 C ATOM 3111 C SER A 275 0.768 3.858 146.397 1.00 84.71 C ANISOU 3111 C SER A 275 11667 12781 7737 -843 399 -2532 C ATOM 3112 O SER A 275 -0.220 3.179 146.111 1.00 84.74 O ANISOU 3112 O SER A 275 11706 12789 7701 -948 345 -2628 O ATOM 3113 CB SER A 275 2.634 2.296 146.966 1.00 85.51 C ANISOU 3113 CB SER A 275 11994 12598 7897 -639 517 -2692 C ATOM 3114 OG SER A 275 3.697 2.028 147.864 1.00 83.31 O ANISOU 3114 OG SER A 275 11773 12174 7707 -502 576 -2673 O ATOM 3115 N ASN A 276 1.072 5.001 145.788 1.00 84.14 N ANISOU 3115 N ASN A 276 11499 12865 7607 -826 409 -2431 N ATOM 3116 CA ASN A 276 0.306 5.534 144.664 1.00 85.84 C ANISOU 3116 CA ASN A 276 11652 13270 7691 -910 358 -2426 C ATOM 3117 C ASN A 276 1.064 6.678 143.990 1.00 85.95 C ANISOU 3117 C ASN A 276 11604 13417 7636 -858 393 -2327 C ATOM 3118 O ASN A 276 2.062 7.165 144.522 1.00 84.71 O ANISOU 3118 O ASN A 276 11427 13210 7548 -774 450 -2246 O ATOM 3119 CB ASN A 276 -1.074 6.012 145.122 1.00 84.79 C ANISOU 3119 CB ASN A 276 11423 13199 7595 -1002 270 -2341 C ATOM 3120 N CYS A 277 0.594 7.098 142.819 1.00 87.66 N ANISOU 3120 N CYS A 277 11794 13806 7708 -913 359 -2334 N ATOM 3121 CA CYS A 277 1.235 8.189 142.090 1.00 86.86 C ANISOU 3121 CA CYS A 277 11649 13836 7519 -876 388 -2239 C ATOM 3122 C CYS A 277 0.877 9.538 142.701 1.00 85.10 C ANISOU 3122 C CYS A 277 11326 13647 7359 -867 343 -2047 C ATOM 3123 O CYS A 277 1.722 10.427 142.809 1.00 84.60 O ANISOU 3123 O CYS A 277 11238 13595 7311 -813 384 -1941 O ATOM 3124 CB CYS A 277 0.837 8.162 140.612 1.00 89.22 C ANISOU 3124 CB CYS A 277 11970 14305 7624 -933 362 -2313 C ATOM 3125 SG CYS A 277 1.435 6.722 139.697 1.00 99.33 S ANISOU 3125 SG CYS A 277 13388 15558 8795 -926 427 -2546 S ATOM 3126 N GLU A 278 -0.382 9.681 143.100 1.00 84.45 N ANISOU 3126 N GLU A 278 11195 13584 7309 -921 258 -2007 N ATOM 3127 CA GLU A 278 -0.846 10.904 143.740 1.00 83.26 C ANISOU 3127 CA GLU A 278 10965 13454 7215 -899 211 -1836 C ATOM 3128 C GLU A 278 -0.628 10.839 145.248 1.00 80.14 C ANISOU 3128 C GLU A 278 10556 12893 7001 -857 230 -1782 C ATOM 3129 O GLU A 278 -0.994 11.760 145.976 1.00 78.48 O ANISOU 3129 O GLU A 278 10292 12670 6855 -831 196 -1650 O ATOM 3130 CB GLU A 278 -2.324 11.146 143.426 1.00 84.81 C ANISOU 3130 CB GLU A 278 11105 13775 7346 -962 113 -1817 C ATOM 3131 N SER A 279 -0.026 9.745 145.707 1.00 79.93 N ANISOU 3131 N SER A 279 10591 12735 7044 -843 284 -1886 N ATOM 3132 CA SER A 279 0.213 9.529 147.131 1.00 77.83 C ANISOU 3132 CA SER A 279 10329 12306 6936 -802 302 -1848 C ATOM 3133 C SER A 279 1.229 10.513 147.700 1.00 76.48 C ANISOU 3133 C SER A 279 10132 12096 6830 -722 341 -1722 C ATOM 3134 O SER A 279 0.940 11.231 148.659 1.00 74.96 O ANISOU 3134 O SER A 279 9897 11858 6726 -702 312 -1607 O ATOM 3135 CB SER A 279 0.689 8.096 147.381 1.00 77.96 C ANISOU 3135 CB SER A 279 10443 12187 6990 -791 349 -1995 C ATOM 3136 OG SER A 279 1.003 7.890 148.747 1.00 76.13 O ANISOU 3136 OG SER A 279 10228 11799 6898 -740 366 -1953 O ATOM 3137 N THR A 280 2.419 10.536 147.105 1.00 77.63 N ANISOU 3137 N THR A 280 10305 12265 6926 -681 408 -1750 N ATOM 3138 CA THR A 280 3.502 11.397 147.571 1.00 76.84 C ANISOU 3138 CA THR A 280 10178 12140 6877 -622 451 -1647 C ATOM 3139 C THR A 280 3.091 12.868 147.548 1.00 76.66 C ANISOU 3139 C THR A 280 10105 12191 6833 -633 402 -1493 C ATOM 3140 O THR A 280 3.429 13.630 148.454 1.00 78.04 O ANISOU 3140 O THR A 280 10259 12299 7093 -598 400 -1386 O ATOM 3141 CB THR A 280 4.775 11.205 146.719 1.00 78.61 C ANISOU 3141 CB THR A 280 10424 12423 7021 -591 535 -1711 C ATOM 3142 OG1 THR A 280 5.194 9.836 146.784 1.00 79.25 O ANISOU 3142 OG1 THR A 280 10574 12419 7120 -555 583 -1859 O ATOM 3143 CG2 THR A 280 5.901 12.093 147.223 1.00 77.70 C ANISOU 3143 CG2 THR A 280 10269 12298 6957 -547 579 -1607 C ATOM 3144 N SER A 281 2.345 13.255 146.517 1.00 75.98 N ANISOU 3144 N SER A 281 10011 12235 6623 -676 359 -1484 N ATOM 3145 CA SER A 281 1.886 14.633 146.376 1.00 74.55 C ANISOU 3145 CA SER A 281 9809 12120 6397 -673 309 -1342 C ATOM 3146 C SER A 281 0.938 15.029 147.508 1.00 70.50 C ANISOU 3146 C SER A 281 9266 11534 5987 -656 246 -1262 C ATOM 3147 O SER A 281 1.043 16.125 148.060 1.00 69.50 O ANISOU 3147 O SER A 281 9141 11370 5895 -616 231 -1137 O ATOM 3148 CB SER A 281 1.200 14.831 145.023 1.00 77.18 C ANISOU 3148 CB SER A 281 10150 12612 6563 -713 268 -1360 C ATOM 3149 OG SER A 281 0.686 16.146 144.897 1.00 77.42 O ANISOU 3149 OG SER A 281 10181 12696 6540 -693 213 -1220 O ATOM 3150 N GLN A 282 0.017 14.132 147.849 1.00 68.51 N ANISOU 3150 N GLN A 282 8994 11262 5775 -689 213 -1338 N ATOM 3151 CA GLN A 282 -0.948 14.388 148.914 1.00 64.64 C ANISOU 3151 CA GLN A 282 8466 10722 5374 -678 161 -1275 C ATOM 3152 C GLN A 282 -0.295 14.298 150.291 1.00 58.70 C ANISOU 3152 C GLN A 282 7726 9808 4768 -634 197 -1242 C ATOM 3153 O GLN A 282 -0.657 15.036 151.209 1.00 55.85 O ANISOU 3153 O GLN A 282 7349 9398 4474 -597 169 -1144 O ATOM 3154 CB GLN A 282 -2.122 13.410 148.825 1.00 67.32 C ANISOU 3154 CB GLN A 282 8774 11106 5699 -747 120 -1373 C ATOM 3155 CG GLN A 282 -3.061 13.666 147.658 1.00 71.53 C ANISOU 3155 CG GLN A 282 9275 11815 6088 -789 59 -1386 C ATOM 3156 CD GLN A 282 -4.188 12.654 147.583 1.00 76.29 C ANISOU 3156 CD GLN A 282 9840 12473 6675 -876 18 -1493 C ATOM 3157 OE1 GLN A 282 -4.171 11.635 148.274 1.00 79.04 O ANISOU 3157 OE1 GLN A 282 10208 12715 7109 -913 45 -1573 O ATOM 3158 NE2 GLN A 282 -5.176 12.930 146.740 1.00 78.65 N ANISOU 3158 NE2 GLN A 282 10090 12938 6854 -913 -50 -1494 N ATOM 3159 N LEU A 283 0.665 13.389 150.429 1.00 55.33 N ANISOU 3159 N LEU A 283 7336 9304 4383 -628 259 -1327 N ATOM 3160 CA LEU A 283 1.406 13.251 151.676 1.00 51.52 C ANISOU 3160 CA LEU A 283 6872 8677 4025 -578 293 -1300 C ATOM 3161 C LEU A 283 2.252 14.493 151.933 1.00 50.75 C ANISOU 3161 C LEU A 283 6770 8571 3944 -532 307 -1182 C ATOM 3162 O LEU A 283 2.504 14.856 153.082 1.00 49.58 O ANISOU 3162 O LEU A 283 6624 8324 3891 -493 306 -1116 O ATOM 3163 CB LEU A 283 2.284 11.998 151.647 1.00 50.60 C ANISOU 3163 CB LEU A 283 6807 8491 3929 -565 354 -1422 C ATOM 3164 CG LEU A 283 1.577 10.675 151.948 1.00 50.11 C ANISOU 3164 CG LEU A 283 6786 8360 3894 -600 344 -1532 C ATOM 3165 CD1 LEU A 283 2.449 9.486 151.574 1.00 39.17 C ANISOU 3165 CD1 LEU A 283 5480 6915 2488 -573 404 -1666 C ATOM 3166 CD2 LEU A 283 1.197 10.611 153.418 1.00 36.27 C ANISOU 3166 CD2 LEU A 283 5035 6488 2259 -581 325 -1477 C ATOM 3167 N ASP A 284 2.683 15.144 150.857 1.00 52.09 N ANISOU 3167 N ASP A 284 6940 8843 4009 -543 320 -1158 N ATOM 3168 CA ASP A 284 3.421 16.397 150.966 1.00 51.07 C ANISOU 3168 CA ASP A 284 6818 8713 3871 -518 332 -1045 C ATOM 3169 C ASP A 284 2.509 17.512 151.449 1.00 48.55 C ANISOU 3169 C ASP A 284 6509 8377 3560 -498 267 -927 C ATOM 3170 O ASP A 284 2.899 18.325 152.285 1.00 47.75 O ANISOU 3170 O ASP A 284 6430 8197 3517 -464 265 -840 O ATOM 3171 CB ASP A 284 4.049 16.777 149.626 1.00 54.52 C ANISOU 3171 CB ASP A 284 7266 9273 4176 -545 367 -1050 C ATOM 3172 CG ASP A 284 5.360 16.066 149.379 1.00 58.38 C ANISOU 3172 CG ASP A 284 7746 9769 4665 -542 449 -1135 C ATOM 3173 OD1 ASP A 284 5.545 14.956 149.922 1.00 59.17 O ANISOU 3173 OD1 ASP A 284 7846 9795 4842 -520 472 -1226 O ATOM 3174 OD2 ASP A 284 6.207 16.618 148.646 1.00 61.58 O1+ ANISOU 3174 OD2 ASP A 284 8151 10258 4988 -558 494 -1109 O1+ ATOM 3175 N GLN A 285 1.294 17.545 150.913 1.00 47.57 N ANISOU 3175 N GLN A 285 6373 8332 3371 -513 212 -931 N ATOM 3176 CA GLN A 285 0.304 18.527 151.329 1.00 45.33 C ANISOU 3176 CA GLN A 285 6098 8044 3081 -477 148 -830 C ATOM 3177 C GLN A 285 0.014 18.389 152.821 1.00 42.23 C ANISOU 3177 C GLN A 285 5693 7530 2822 -444 138 -810 C ATOM 3178 O GLN A 285 -0.016 19.381 153.548 1.00 41.23 O ANISOU 3178 O GLN A 285 5604 7336 2727 -394 119 -713 O ATOM 3179 CB GLN A 285 -0.981 18.371 150.512 1.00 47.46 C ANISOU 3179 CB GLN A 285 6335 8442 3255 -499 89 -857 C ATOM 3180 CG GLN A 285 -0.798 18.610 149.019 1.00 49.25 C ANISOU 3180 CG GLN A 285 6586 8797 3329 -526 88 -867 C ATOM 3181 N ALA A 286 -0.180 17.153 153.273 1.00 40.33 N ANISOU 3181 N ALA A 286 5416 7256 2651 -472 153 -903 N ATOM 3182 CA ALA A 286 -0.426 16.884 154.685 1.00 37.32 C ANISOU 3182 CA ALA A 286 5029 6762 2387 -448 151 -890 C ATOM 3183 C ALA A 286 0.778 17.284 155.533 1.00 35.60 C ANISOU 3183 C ALA A 286 4853 6429 2246 -406 188 -840 C ATOM 3184 O ALA A 286 0.622 17.757 156.658 1.00 34.62 O ANISOU 3184 O ALA A 286 4746 6219 2190 -366 173 -777 O ATOM 3185 CB ALA A 286 -0.762 15.416 154.898 1.00 36.11 C ANISOU 3185 CB ALA A 286 4856 6589 2275 -496 166 -1003 C ATOM 3186 N THR A 287 1.975 17.093 154.988 1.00 35.67 N ANISOU 3186 N THR A 287 4874 6446 2233 -417 236 -874 N ATOM 3187 CA THR A 287 3.202 17.484 155.674 1.00 34.74 C ANISOU 3187 CA THR A 287 4778 6249 2171 -388 271 -833 C ATOM 3188 C THR A 287 3.254 18.998 155.868 1.00 36.80 C ANISOU 3188 C THR A 287 5078 6496 2408 -364 246 -713 C ATOM 3189 O THR A 287 3.618 19.486 156.938 1.00 35.84 O ANISOU 3189 O THR A 287 4984 6281 2353 -332 244 -659 O ATOM 3190 CB THR A 287 4.455 17.028 154.901 1.00 34.97 C ANISOU 3190 CB THR A 287 4798 6327 2163 -406 333 -897 C ATOM 3191 OG1 THR A 287 4.477 15.598 154.817 1.00 35.25 O ANISOU 3191 OG1 THR A 287 4828 6347 2219 -411 359 -1015 O ATOM 3192 CG2 THR A 287 5.714 17.504 155.599 1.00 34.62 C ANISOU 3192 CG2 THR A 287 4757 6229 2167 -384 365 -853 C ATOM 3193 N GLN A 288 2.877 19.735 154.829 1.00 40.45 N ANISOU 3193 N GLN A 288 5560 7046 2763 -377 226 -674 N ATOM 3194 CA GLN A 288 2.878 21.191 154.885 1.00 43.69 C ANISOU 3194 CA GLN A 288 6043 7433 3125 -349 201 -560 C ATOM 3195 C GLN A 288 1.888 21.713 155.919 1.00 43.99 C ANISOU 3195 C GLN A 288 6114 7389 3210 -293 150 -502 C ATOM 3196 O GLN A 288 2.222 22.586 156.721 1.00 42.59 O ANISOU 3196 O GLN A 288 6004 7119 3061 -258 145 -432 O ATOM 3197 CB GLN A 288 2.552 21.780 153.513 1.00 47.06 C ANISOU 3197 CB GLN A 288 6501 7969 3410 -366 185 -530 C ATOM 3198 CG GLN A 288 3.563 21.444 152.437 1.00 49.56 C ANISOU 3198 CG GLN A 288 6797 8377 3658 -421 241 -577 C ATOM 3199 CD GLN A 288 3.087 21.841 151.057 1.00 55.47 C ANISOU 3199 CD GLN A 288 7576 9245 4256 -438 222 -558 C ATOM 3200 OE1 GLN A 288 2.450 21.052 150.357 1.00 59.98 O ANISOU 3200 OE1 GLN A 288 8102 9904 4784 -458 207 -633 O ATOM 3201 NE2 GLN A 288 3.389 23.070 150.658 1.00 58.05 N ANISOU 3201 NE2 GLN A 288 7991 9574 4491 -432 219 -456 N ATOM 3202 N VAL A 289 0.673 21.177 155.896 1.00 44.21 N ANISOU 3202 N VAL A 289 6095 7463 3240 -288 115 -537 N ATOM 3203 CA VAL A 289 -0.380 21.631 156.797 1.00 30.16 C ANISOU 3203 CA VAL A 289 4331 5637 1492 -235 71 -489 C ATOM 3204 C VAL A 289 -0.029 21.347 158.253 1.00 28.63 C ANISOU 3204 C VAL A 289 4141 5320 1417 -215 90 -492 C ATOM 3205 O VAL A 289 -0.133 22.225 159.108 1.00 27.98 O ANISOU 3205 O VAL A 289 4126 5152 1354 -165 73 -423 O ATOM 3206 CB VAL A 289 -1.735 20.968 156.467 1.00 31.69 C ANISOU 3206 CB VAL A 289 4442 5938 1661 -248 34 -539 C ATOM 3207 CG1 VAL A 289 -2.781 21.350 157.502 1.00 30.19 C ANISOU 3207 CG1 VAL A 289 4245 5718 1508 -194 -1 -497 C ATOM 3208 CG2 VAL A 289 -2.195 21.363 155.075 1.00 32.47 C ANISOU 3208 CG2 VAL A 289 4542 6168 1627 -258 2 -528 C ATOM 3209 N THR A 290 0.396 20.118 158.526 1.00 33.22 N ANISOU 3209 N THR A 290 4668 5887 2068 -250 125 -572 N ATOM 3210 CA THR A 290 0.711 19.704 159.887 1.00 26.93 C ANISOU 3210 CA THR A 290 3880 4979 1374 -230 141 -577 C ATOM 3211 C THR A 290 1.898 20.467 160.459 1.00 40.39 C ANISOU 3211 C THR A 290 5645 6596 3104 -206 158 -523 C ATOM 3212 O THR A 290 1.920 20.785 161.649 1.00 40.57 O ANISOU 3212 O THR A 290 5707 6524 3182 -169 150 -486 O ATOM 3213 CB THR A 290 1.009 18.203 159.958 1.00 26.90 C ANISOU 3213 CB THR A 290 3833 4968 1419 -267 174 -674 C ATOM 3214 OG1 THR A 290 1.946 17.859 158.932 1.00 27.72 O ANISOU 3214 OG1 THR A 290 3926 5124 1483 -300 208 -724 O ATOM 3215 CG2 THR A 290 -0.264 17.400 159.765 1.00 27.42 C ANISOU 3215 CG2 THR A 290 3850 5097 1472 -301 155 -729 C ATOM 3216 N GLU A 291 2.885 20.758 159.617 1.00 41.17 N ANISOU 3216 N GLU A 291 5750 6739 3156 -234 183 -523 N ATOM 3217 CA GLU A 291 4.046 21.518 160.064 1.00 26.53 C ANISOU 3217 CA GLU A 291 3940 4829 1312 -228 200 -475 C ATOM 3218 C GLU A 291 3.641 22.954 160.371 1.00 33.38 C ANISOU 3218 C GLU A 291 4905 5641 2136 -188 163 -380 C ATOM 3219 O GLU A 291 4.160 23.570 161.299 1.00 25.84 O ANISOU 3219 O GLU A 291 4006 4600 1211 -164 160 -338 O ATOM 3220 CB GLU A 291 5.162 21.488 159.020 1.00 27.48 C ANISOU 3220 CB GLU A 291 4030 5033 1378 -280 242 -498 C ATOM 3221 CG GLU A 291 6.466 22.103 159.507 1.00 40.70 C ANISOU 3221 CG GLU A 291 5722 6677 3066 -294 266 -462 C ATOM 3222 CD GLU A 291 7.661 21.702 158.664 1.00 41.20 C ANISOU 3222 CD GLU A 291 5722 6838 3093 -350 322 -510 C ATOM 3223 OE1 GLU A 291 7.460 21.142 157.565 1.00 42.50 O ANISOU 3223 OE1 GLU A 291 5853 7091 3205 -372 342 -562 O ATOM 3224 OE2 GLU A 291 8.804 21.946 159.105 1.00 40.56 O1+ ANISOU 3224 OE2 GLU A 291 5624 6756 3030 -372 347 -501 O1+ ATOM 3225 N THR A 292 2.705 23.480 159.589 1.00 35.46 N ANISOU 3225 N THR A 292 5201 5954 2317 -175 133 -348 N ATOM 3226 CA THR A 292 2.142 24.799 159.848 1.00 35.82 C ANISOU 3226 CA THR A 292 5369 5937 2306 -121 94 -262 C ATOM 3227 C THR A 292 1.485 24.821 161.224 1.00 38.58 C ANISOU 3227 C THR A 292 5744 6189 2726 -74 72 -253 C ATOM 3228 O THR A 292 1.650 25.773 161.987 1.00 42.95 O ANISOU 3228 O THR A 292 6411 6638 3271 -36 58 -197 O ATOM 3229 CB THR A 292 1.112 25.198 158.776 1.00 33.89 C ANISOU 3229 CB THR A 292 5148 5774 1955 -109 57 -237 C ATOM 3230 OG1 THR A 292 1.754 25.264 157.496 1.00 34.17 O ANISOU 3230 OG1 THR A 292 5178 5897 1908 -153 80 -238 O ATOM 3231 CG2 THR A 292 0.496 26.549 159.100 1.00 32.44 C ANISOU 3231 CG2 THR A 292 5115 5507 1703 -50 12 -148 C ATOM 3232 N LEU A 293 0.752 23.756 161.535 1.00 35.36 N ANISOU 3232 N LEU A 293 5237 5820 2379 -82 73 -310 N ATOM 3233 CA LEU A 293 0.115 23.610 162.839 1.00 34.61 C ANISOU 3233 CA LEU A 293 5146 5656 2350 -50 63 -308 C ATOM 3234 C LEU A 293 1.143 23.639 163.962 1.00 33.41 C ANISOU 3234 C LEU A 293 5040 5390 2265 -42 83 -301 C ATOM 3235 O LEU A 293 0.975 24.345 164.955 1.00 33.79 O ANISOU 3235 O LEU A 293 5174 5344 2320 -11 68 -260 O ATOM 3236 CB LEU A 293 -0.685 22.309 162.901 1.00 34.13 C ANISOU 3236 CB LEU A 293 4965 5668 2334 -71 69 -376 C ATOM 3237 CG LEU A 293 -1.232 21.936 164.278 1.00 24.21 C ANISOU 3237 CG LEU A 293 3701 4352 1147 -48 72 -380 C ATOM 3238 CD1 LEU A 293 -2.233 22.975 164.744 1.00 24.42 C ANISOU 3238 CD1 LEU A 293 3769 4375 1134 1 41 -323 C ATOM 3239 CD2 LEU A 293 -1.861 20.555 164.245 1.00 29.52 C ANISOU 3239 CD2 LEU A 293 4272 5093 1851 -85 85 -452 C ATOM 3240 N GLY A 294 2.211 22.866 163.794 1.00 33.41 N ANISOU 3240 N GLY A 294 4981 5408 2305 -75 115 -346 N ATOM 3241 CA GLY A 294 3.273 22.802 164.777 1.00 31.83 C ANISOU 3241 CA GLY A 294 4802 5131 2162 -68 130 -346 C ATOM 3242 C GLY A 294 4.006 24.119 164.948 1.00 34.26 C ANISOU 3242 C GLY A 294 5201 5389 2425 -48 117 -284 C ATOM 3243 O GLY A 294 4.495 24.426 166.034 1.00 34.13 O ANISOU 3243 O GLY A 294 5229 5298 2442 -18 109 -267 O ATOM 3244 N MET A 295 4.086 24.902 163.878 1.00 34.32 N ANISOU 3244 N MET A 295 5242 5447 2349 -59 114 -250 N ATOM 3245 CA MET A 295 4.797 26.174 163.927 1.00 33.12 C ANISOU 3245 CA MET A 295 5175 5268 2140 -37 104 -189 C ATOM 3246 C MET A 295 4.052 27.211 164.762 1.00 32.61 C ANISOU 3246 C MET A 295 5212 5099 2079 52 62 -133 C ATOM 3247 O MET A 295 4.639 28.203 165.196 1.00 33.68 O ANISOU 3247 O MET A 295 5356 5236 2205 102 49 -90 O ATOM 3248 CB MET A 295 5.034 26.708 162.514 1.00 34.56 C ANISOU 3248 CB MET A 295 5369 5536 2227 -75 116 -160 C ATOM 3249 CG MET A 295 6.113 25.963 161.743 1.00 36.84 C ANISOU 3249 CG MET A 295 5545 5925 2527 -173 164 -208 C ATOM 3250 SD MET A 295 6.240 26.495 160.026 1.00 27.92 S ANISOU 3250 SD MET A 295 4433 4905 1270 -225 183 -176 S ATOM 3251 CE MET A 295 6.734 28.203 160.235 1.00 28.58 C ANISOU 3251 CE MET A 295 4640 4945 1274 -211 168 -70 C ATOM 3252 N THR A 296 2.764 26.980 164.994 1.00 31.53 N ANISOU 3252 N THR A 296 5106 4910 1963 47 45 -138 N ATOM 3253 CA THR A 296 1.962 27.901 165.793 1.00 32.09 C ANISOU 3253 CA THR A 296 5286 4856 2052 26 14 -93 C ATOM 3254 C THR A 296 2.025 27.554 167.277 1.00 34.07 C ANISOU 3254 C THR A 296 5518 5032 2396 -26 20 -113 C ATOM 3255 O THR A 296 1.262 28.093 168.078 1.00 36.36 O ANISOU 3255 O THR A 296 5686 5445 2686 -208 7 -98 O ATOM 3256 CB THR A 296 0.486 27.901 165.359 1.00 31.07 C ANISOU 3256 CB THR A 296 5119 4822 1863 -51 -6 -88 C ATOM 3257 OG1 THR A 296 -0.107 26.635 165.674 1.00 30.38 O ANISOU 3257 OG1 THR A 296 4924 4806 1812 -14 12 -148 O ATOM 3258 CG2 THR A 296 0.366 28.161 163.866 1.00 32.41 C ANISOU 3258 CG2 THR A 296 5320 5063 1931 -23 -18 -68 C ATOM 3259 N HIS A 297 2.933 26.653 167.640 1.00 33.84 N ANISOU 3259 N HIS A 297 5405 5032 2418 69 39 -154 N ATOM 3260 CA HIS A 297 3.058 26.216 169.026 1.00 32.95 C ANISOU 3260 CA HIS A 297 5288 4845 2387 56 42 -170 C ATOM 3261 C HIS A 297 4.023 27.091 169.823 1.00 33.04 C ANISOU 3261 C HIS A 297 5124 5018 2412 277 9 -156 C ATOM 3262 O HIS A 297 3.957 27.141 171.053 1.00 34.51 O ANISOU 3262 O HIS A 297 4974 5502 2637 65 11 -182 O ATOM 3263 CB HIS A 297 3.510 24.755 169.090 1.00 31.72 C ANISOU 3263 CB HIS A 297 5023 4760 2269 53 69 -228 C ATOM 3264 CG HIS A 297 3.803 24.279 170.478 1.00 30.62 C ANISOU 3264 CG HIS A 297 4884 4550 2202 59 69 -238 C ATOM 3265 ND1 HIS A 297 5.085 24.153 170.967 1.00 30.28 N ANISOU 3265 ND1 HIS A 297 4803 4522 2179 100 62 -249 N ATOM 3266 CD2 HIS A 297 2.977 23.922 171.491 1.00 29.28 C ANISOU 3266 CD2 HIS A 297 4724 4331 2072 -9 80 -240 C ATOM 3267 CE1 HIS A 297 5.037 23.728 172.217 1.00 29.78 C ANISOU 3267 CE1 HIS A 297 4760 4386 2172 108 57 -252 C ATOM 3268 NE2 HIS A 297 3.770 23.580 172.558 1.00 29.29 N ANISOU 3268 NE2 HIS A 297 4734 4273 2122 -8 78 -245 N ATOM 3269 N CYS A 298 4.903 27.797 169.123 1.00 33.19 N ANISOU 3269 N CYS A 298 5109 5139 2362 214 11 -137 N ATOM 3270 CA CYS A 298 5.925 28.611 169.777 1.00 36.18 C ANISOU 3270 CA CYS A 298 5458 5579 2708 123 -1 -122 C ATOM 3271 C CYS A 298 5.352 29.822 170.517 1.00 38.66 C ANISOU 3271 C CYS A 298 5775 5935 2980 43 -25 -82 C ATOM 3272 O CYS A 298 6.101 30.614 171.086 1.00 41.76 O ANISOU 3272 O CYS A 298 6277 6265 3327 -4 -43 -62 O ATOM 3273 CB CYS A 298 6.957 29.085 168.751 1.00 38.27 C ANISOU 3273 CB CYS A 298 5818 5839 2885 48 14 -98 C ATOM 3274 SG CYS A 298 6.285 30.155 167.458 1.00 51.97 S ANISOU 3274 SG CYS A 298 7593 7635 4517 54 12 -31 S ATOM 3275 N CYS A 299 4.030 29.966 170.509 1.00 37.01 N ANISOU 3275 N CYS A 299 5534 5760 2766 5 -28 -68 N ATOM 3276 CA CYS A 299 3.383 31.078 171.196 1.00 36.91 C ANISOU 3276 CA CYS A 299 5677 5659 2688 1 -55 -27 C ATOM 3277 C CYS A 299 2.394 30.589 172.250 1.00 35.47 C ANISOU 3277 C CYS A 299 5503 5411 2564 24 -50 -55 C ATOM 3278 O CYS A 299 1.621 31.374 172.799 1.00 35.84 O ANISOU 3278 O CYS A 299 5667 5350 2602 107 -67 -30 O ATOM 3279 CB CYS A 299 2.659 31.976 170.193 1.00 38.57 C ANISOU 3279 CB CYS A 299 5962 5876 2817 14 -71 33 C ATOM 3280 SG CYS A 299 1.111 31.290 169.572 1.00 48.10 S ANISOU 3280 SG CYS A 299 7118 7143 4016 -10 -66 21 S ATOM 3281 N ILE A 300 2.426 29.292 172.537 1.00 33.59 N ANISOU 3281 N ILE A 300 5154 5212 2398 -22 -24 -105 N ATOM 3282 CA ILE A 300 1.418 28.680 173.394 1.00 32.40 C ANISOU 3282 CA ILE A 300 5023 5012 2274 2 -10 -127 C ATOM 3283 C ILE A 300 1.823 28.634 174.866 1.00 31.71 C ANISOU 3283 C ILE A 300 4965 4845 2239 53 -15 -140 C ATOM 3284 O ILE A 300 0.998 28.897 175.745 1.00 32.27 O ANISOU 3284 O ILE A 300 5098 4843 2322 140 -16 -134 O ATOM 3285 CB ILE A 300 1.093 27.254 172.917 1.00 31.60 C ANISOU 3285 CB ILE A 300 4860 4909 2239 -75 23 -165 C ATOM 3286 CG1 ILE A 300 0.595 27.293 171.473 1.00 31.65 C ANISOU 3286 CG1 ILE A 300 4909 4914 2204 -111 23 -152 C ATOM 3287 CG2 ILE A 300 0.049 26.611 173.807 1.00 32.09 C ANISOU 3287 CG2 ILE A 300 4943 4938 2312 -20 40 -182 C ATOM 3288 CD1 ILE A 300 -0.606 28.191 171.274 1.00 31.96 C ANISOU 3288 CD1 ILE A 300 4997 4995 2150 -16 0 -117 C ATOM 3289 N ASN A 301 3.089 28.313 175.130 1.00 30.57 N ANISOU 3289 N ASN A 301 4776 4722 2117 12 -19 -159 N ATOM 3290 CA ASN A 301 3.571 28.138 176.503 1.00 29.55 C ANISOU 3290 CA ASN A 301 4681 4517 2029 39 -29 -172 C ATOM 3291 C ASN A 301 3.253 29.301 177.461 1.00 28.56 C ANISOU 3291 C ASN A 301 4705 4257 1891 114 -53 -148 C ATOM 3292 O ASN A 301 2.752 29.060 178.560 1.00 27.19 O ANISOU 3292 O ASN A 301 4561 4029 1742 166 -48 -156 O ATOM 3293 CB ASN A 301 5.082 27.869 176.501 1.00 29.83 C ANISOU 3293 CB ASN A 301 4667 4596 2070 4 -41 -191 C ATOM 3294 CG ASN A 301 5.431 26.503 175.946 1.00 31.50 C ANISOU 3294 CG ASN A 301 4738 4887 2343 -18 -16 -225 C ATOM 3295 OD1 ASN A 301 4.617 25.579 175.985 1.00 32.85 O ANISOU 3295 OD1 ASN A 301 4873 5053 2554 -51 12 -240 O ATOM 3296 ND2 ASN A 301 6.649 26.365 175.433 1.00 31.52 N ANISOU 3296 ND2 ASN A 301 4701 4925 2350 27 -27 -238 N ATOM 3297 N PRO A 302 3.531 30.560 177.061 1.00 28.28 N ANISOU 3297 N PRO A 302 4775 4162 1808 121 -79 -119 N ATOM 3298 CA PRO A 302 3.162 31.641 177.985 1.00 28.49 C ANISOU 3298 CA PRO A 302 4966 4044 1814 197 -101 -106 C ATOM 3299 C PRO A 302 1.659 31.729 178.254 1.00 28.67 C ANISOU 3299 C PRO A 302 5012 4049 1831 316 -84 -101 C ATOM 3300 O PRO A 302 1.261 32.171 179.332 1.00 23.29 O ANISOU 3300 O PRO A 302 4427 3276 1146 401 -89 -108 O ATOM 3301 CB PRO A 302 3.654 32.900 177.265 1.00 29.19 C ANISOU 3301 CB PRO A 302 5178 4067 1844 168 -129 -72 C ATOM 3302 CG PRO A 302 4.741 32.418 176.370 1.00 28.31 C ANISOU 3302 CG PRO A 302 4961 4065 1731 63 -124 -73 C ATOM 3303 CD PRO A 302 4.281 31.076 175.900 1.00 27.70 C ANISOU 3303 CD PRO A 302 4703 4133 1690 63 -89 -97 C ATOM 3304 N ILE A 303 0.839 31.313 177.294 1.00 30.08 N ANISOU 3304 N ILE A 303 5104 4325 2000 325 -64 -93 N ATOM 3305 CA ILE A 303 -0.608 31.330 177.483 1.00 31.39 C ANISOU 3305 CA ILE A 303 5270 4505 2152 442 -48 -91 C ATOM 3306 C ILE A 303 -1.020 30.256 178.482 1.00 34.56 C ANISOU 3306 C ILE A 303 5594 4938 2598 451 -18 -121 C ATOM 3307 O ILE A 303 -1.887 30.479 179.329 1.00 38.20 O ANISOU 3307 O ILE A 303 6092 5374 3047 562 -6 -124 O ATOM 3308 CB ILE A 303 -1.362 31.118 176.157 1.00 28.87 C ANISOU 3308 CB ILE A 303 4877 4291 1801 436 -42 -76 C ATOM 3309 CG1 ILE A 303 -0.980 32.207 175.152 1.00 29.03 C ANISOU 3309 CG1 ILE A 303 4984 4284 1762 429 -72 -36 C ATOM 3310 CG2 ILE A 303 -2.864 31.111 176.392 1.00 27.37 C ANISOU 3310 CG2 ILE A 303 4670 4139 1589 570 -27 -77 C ATOM 3311 CD1 ILE A 303 -1.674 32.078 173.812 1.00 29.67 C ANISOU 3311 CD1 ILE A 303 5007 4471 1798 423 -74 -15 C ATOM 3312 N ILE A 304 -0.386 29.092 178.384 1.00 31.74 N ANISOU 3312 N ILE A 304 5135 4639 2285 338 -4 -142 N ATOM 3313 CA ILE A 304 -0.649 28.001 179.311 1.00 31.01 C ANISOU 3313 CA ILE A 304 4987 4566 2229 330 23 -163 C ATOM 3314 C ILE A 304 -0.270 28.412 180.732 1.00 32.60 C ANISOU 3314 C ILE A 304 5274 4675 2436 384 11 -164 C ATOM 3315 O ILE A 304 -0.958 28.063 181.692 1.00 32.57 O ANISOU 3315 O ILE A 304 5272 4672 2431 439 33 -170 O ATOM 3316 CB ILE A 304 0.115 26.724 178.906 1.00 20.48 C ANISOU 3316 CB ILE A 304 3558 3290 934 208 36 -186 C ATOM 3317 CG1 ILE A 304 -0.292 26.295 177.495 1.00 25.05 C ANISOU 3317 CG1 ILE A 304 4076 3943 1497 144 51 -193 C ATOM 3318 CG2 ILE A 304 -0.144 25.598 179.896 1.00 20.16 C ANISOU 3318 CG2 ILE A 304 3485 3254 920 201 63 -202 C ATOM 3319 CD1 ILE A 304 0.324 24.990 177.050 1.00 24.62 C ANISOU 3319 CD1 ILE A 304 3959 3924 1471 31 72 -225 C ATOM 3320 N TYR A 305 0.818 29.167 180.855 1.00 34.39 N ANISOU 3320 N TYR A 305 5579 4829 2658 360 -24 -160 N ATOM 3321 CA TYR A 305 1.247 29.688 182.147 1.00 21.98 C ANISOU 3321 CA TYR A 305 4114 3158 1078 398 -45 -165 C ATOM 3322 C TYR A 305 0.148 30.533 182.778 1.00 32.86 C ANISOU 3322 C TYR A 305 5593 4477 2416 532 -37 -161 C ATOM 3323 O TYR A 305 -0.187 30.362 183.947 1.00 23.09 O ANISOU 3323 O TYR A 305 4384 3217 1172 587 -25 -171 O ATOM 3324 CB TYR A 305 2.519 30.526 182.005 1.00 24.43 C ANISOU 3324 CB TYR A 305 4508 3402 1373 336 -88 -162 C ATOM 3325 CG TYR A 305 3.750 29.754 181.586 1.00 23.40 C ANISOU 3325 CG TYR A 305 4278 3345 1270 223 -97 -172 C ATOM 3326 CD1 TYR A 305 3.836 28.383 181.772 1.00 22.38 C ANISOU 3326 CD1 TYR A 305 4030 3293 1179 195 -75 -187 C ATOM 3327 CD2 TYR A 305 4.834 30.406 181.013 1.00 24.47 C ANISOU 3327 CD2 TYR A 305 4444 3472 1380 150 -128 -168 C ATOM 3328 CE1 TYR A 305 4.966 27.682 181.392 1.00 23.80 C ANISOU 3328 CE1 TYR A 305 4123 3545 1374 119 -83 -201 C ATOM 3329 CE2 TYR A 305 5.965 29.717 180.632 1.00 24.60 C ANISOU 3329 CE2 TYR A 305 4358 3580 1409 71 -133 -182 C ATOM 3330 CZ TYR A 305 6.027 28.356 180.823 1.00 25.65 C ANISOU 3330 CZ TYR A 305 4371 3794 1582 66 -111 -201 C ATOM 3331 OH TYR A 305 7.158 27.672 180.440 1.00 27.97 O ANISOU 3331 OH TYR A 305 4566 4183 1878 15 -118 -221 O ATOM 3332 N ALA A 306 -0.414 31.440 181.986 1.00 35.05 N ANISOU 3332 N ALA A 306 5925 4737 2657 595 -43 -145 N ATOM 3333 CA ALA A 306 -1.423 32.375 182.474 1.00 35.85 C ANISOU 3333 CA ALA A 306 6133 4780 2708 750 -39 -143 C ATOM 3334 C ALA A 306 -2.731 31.686 182.861 1.00 36.51 C ANISOU 3334 C ALA A 306 6118 4968 2786 834 7 -149 C ATOM 3335 O ALA A 306 -3.459 32.173 183.721 1.00 37.14 O ANISOU 3335 O ALA A 306 6264 5021 2825 962 21 -156 O ATOM 3336 CB ALA A 306 -1.689 33.449 181.426 1.00 34.76 C ANISOU 3336 CB ALA A 306 6079 4603 2524 805 -59 -120 C ATOM 3337 N PHE A 307 -3.029 30.556 182.229 1.00 37.90 N ANISOU 3337 N PHE A 307 6142 5267 2993 758 32 -149 N ATOM 3338 CA PHE A 307 -4.288 29.863 182.487 1.00 40.85 C ANISOU 3338 CA PHE A 307 6418 5752 3351 810 77 -155 C ATOM 3339 C PHE A 307 -4.173 28.796 183.571 1.00 40.80 C ANISOU 3339 C PHE A 307 6366 5768 3368 749 106 -168 C ATOM 3340 O PHE A 307 -5.121 28.563 184.319 1.00 40.62 O ANISOU 3340 O PHE A 307 6319 5803 3313 813 145 -173 O ATOM 3341 CB PHE A 307 -4.822 29.231 181.200 1.00 44.73 C ANISOU 3341 CB PHE A 307 6790 6359 3846 755 87 -151 C ATOM 3342 CG PHE A 307 -5.686 30.151 180.386 1.00 51.09 C ANISOU 3342 CG PHE A 307 7611 7200 4599 878 75 -134 C ATOM 3343 CD1 PHE A 307 -6.067 31.387 180.883 1.00 56.27 C ANISOU 3343 CD1 PHE A 307 8385 7788 5207 1043 63 -125 C ATOM 3344 CD2 PHE A 307 -6.126 29.776 179.126 1.00 52.23 C ANISOU 3344 CD2 PHE A 307 7666 7444 4733 839 73 -128 C ATOM 3345 CE1 PHE A 307 -6.864 32.236 180.137 1.00 57.84 C ANISOU 3345 CE1 PHE A 307 8608 8020 5348 1178 49 -107 C ATOM 3346 CE2 PHE A 307 -6.923 30.619 178.376 1.00 53.95 C ANISOU 3346 CE2 PHE A 307 7896 7708 4894 966 55 -107 C ATOM 3347 CZ PHE A 307 -7.293 31.850 178.882 1.00 55.95 C ANISOU 3347 CZ PHE A 307 8263 7894 5099 1141 43 -94 C ATOM 3348 N VAL A 308 -3.016 28.150 183.656 1.00 40.92 N ANISOU 3348 N VAL A 308 6369 5748 3429 630 90 -173 N ATOM 3349 CA VAL A 308 -2.836 27.049 184.595 1.00 22.48 C ANISOU 3349 CA VAL A 308 3998 3433 1111 572 114 -180 C ATOM 3350 C VAL A 308 -2.027 27.459 185.821 1.00 34.37 C ANISOU 3350 C VAL A 308 5605 4842 2611 597 89 -181 C ATOM 3351 O VAL A 308 -2.343 27.070 186.944 1.00 35.85 O ANISOU 3351 O VAL A 308 5808 5039 2775 621 113 -183 O ATOM 3352 CB VAL A 308 -2.142 25.853 183.921 1.00 21.54 C ANISOU 3352 CB VAL A 308 3793 3353 1039 439 114 -186 C ATOM 3353 CG1 VAL A 308 -2.088 24.667 184.868 1.00 25.65 C ANISOU 3353 CG1 VAL A 308 4290 3892 1564 392 140 -189 C ATOM 3354 CG2 VAL A 308 -2.867 25.476 182.642 1.00 24.45 C ANISOU 3354 CG2 VAL A 308 4080 3805 1404 398 134 -192 C ATOM 3355 N GLY A 309 -0.986 28.255 185.600 1.00 33.97 N ANISOU 3355 N GLY A 309 5630 4706 2572 580 41 -182 N ATOM 3356 CA GLY A 309 -0.049 28.596 186.655 1.00 34.13 C ANISOU 3356 CA GLY A 309 5746 4640 2582 575 8 -189 C ATOM 3357 C GLY A 309 -0.441 29.790 187.502 1.00 35.46 C ANISOU 3357 C GLY A 309 6055 4723 2694 683 -1 -197 C ATOM 3358 O GLY A 309 -0.592 30.902 186.996 1.00 34.66 O ANISOU 3358 O GLY A 309 6038 4562 2569 737 -19 -197 O ATOM 3359 N GLU A 310 -0.589 29.559 188.803 1.00 38.44 N ANISOU 3359 N GLU A 310 6472 5092 3040 718 11 -204 N ATOM 3360 CA GLU A 310 -1.002 30.610 189.724 1.00 41.29 C ANISOU 3360 CA GLU A 310 6972 5379 3336 827 7 -219 C ATOM 3361 C GLU A 310 0.161 31.522 190.108 1.00 40.05 C ANISOU 3361 C GLU A 310 6958 5099 3160 791 -55 -235 C ATOM 3362 O GLU A 310 -0.031 32.717 190.338 1.00 40.35 O ANISOU 3362 O GLU A 310 7142 5041 3147 869 -73 -249 O ATOM 3363 CB GLU A 310 -1.628 30.002 190.981 1.00 45.08 C ANISOU 3363 CB GLU A 310 7440 5914 3774 870 50 -222 C ATOM 3364 CG GLU A 310 -0.732 29.017 191.709 1.00 48.48 C ANISOU 3364 CG GLU A 310 7843 6356 4220 775 34 -217 C ATOM 3365 CD GLU A 310 -1.345 28.523 193.001 1.00 54.47 C ANISOU 3365 CD GLU A 310 8615 7163 4920 816 76 -217 C ATOM 3366 OE1 GLU A 310 -2.561 28.729 193.198 1.00 56.55 O ANISOU 3366 OE1 GLU A 310 8868 7481 5137 903 130 -220 O ATOM 3367 OE2 GLU A 310 -0.610 27.930 193.820 1.00 59.09 O1+ ANISOU 3367 OE2 GLU A 310 9218 7740 5494 764 56 -212 O1+ ATOM 3368 N LYS A 311 1.365 30.961 190.178 1.00 37.69 N ANISOU 3368 N LYS A 311 6622 4805 2893 674 -91 -234 N ATOM 3369 CA LYS A 311 2.541 31.753 190.524 1.00 38.59 C ANISOU 3369 CA LYS A 311 6853 4829 2981 612 -155 -252 C ATOM 3370 C LYS A 311 2.871 32.749 189.419 1.00 39.13 C ANISOU 3370 C LYS A 311 6984 4832 3053 580 -183 -250 C ATOM 3371 O LYS A 311 3.340 33.855 189.688 1.00 39.55 O ANISOU 3371 O LYS A 311 7193 4775 3058 568 -227 -266 O ATOM 3372 CB LYS A 311 3.749 30.852 190.798 1.00 36.37 C ANISOU 3372 CB LYS A 311 6492 4602 2724 502 -188 -252 C ATOM 3373 CG LYS A 311 3.742 30.208 192.174 1.00 34.91 C ANISOU 3373 CG LYS A 311 6318 4443 2505 526 -185 -257 C ATOM 3374 CD LYS A 311 5.103 29.632 192.533 1.00 31.40 C ANISOU 3374 CD LYS A 311 5834 4037 2062 431 -239 -260 C ATOM 3375 CE LYS A 311 5.151 29.242 194.004 1.00 31.37 C ANISOU 3375 CE LYS A 311 5878 4042 2000 460 -250 -265 C ATOM 3376 NZ LYS A 311 6.506 28.800 194.434 1.00 31.83 N1+ ANISOU 3376 NZ LYS A 311 5908 4146 2040 382 -316 -270 N1+ ATOM 3377 N PHE A 312 2.619 32.353 188.176 1.00 38.72 N ANISOU 3377 N PHE A 312 6819 4845 3047 559 -159 -229 N ATOM 3378 CA PHE A 312 2.908 33.207 187.032 1.00 37.20 C ANISOU 3378 CA PHE A 312 6678 4605 2850 523 -180 -219 C ATOM 3379 C PHE A 312 1.987 34.418 187.019 1.00 41.15 C ANISOU 3379 C PHE A 312 7334 5003 3298 648 -176 -219 C ATOM 3380 O PHE A 312 2.423 35.538 186.752 1.00 42.69 O ANISOU 3380 O PHE A 312 7683 5083 3453 626 -215 -220 O ATOM 3381 CB PHE A 312 2.774 32.424 185.727 1.00 33.46 C ANISOU 3381 CB PHE A 312 6043 4243 2427 479 -152 -199 C ATOM 3382 CG PHE A 312 3.151 33.213 184.508 1.00 33.03 C ANISOU 3382 CG PHE A 312 6031 4159 2359 429 -172 -183 C ATOM 3383 CD1 PHE A 312 4.481 33.470 184.219 1.00 32.46 C ANISOU 3383 CD1 PHE A 312 5978 4075 2281 301 -212 -185 C ATOM 3384 CD2 PHE A 312 2.178 33.689 183.644 1.00 32.80 C ANISOU 3384 CD2 PHE A 312 6021 4128 2313 508 -152 -165 C ATOM 3385 CE1 PHE A 312 4.834 34.194 183.096 1.00 32.26 C ANISOU 3385 CE1 PHE A 312 5999 4028 2232 244 -226 -165 C ATOM 3386 CE2 PHE A 312 2.524 34.413 182.517 1.00 32.44 C ANISOU 3386 CE2 PHE A 312 6027 4054 2244 461 -171 -143 C ATOM 3387 CZ PHE A 312 3.855 34.665 182.243 1.00 32.24 C ANISOU 3387 CZ PHE A 312 6029 4010 2212 323 -206 -142 C ATOM 3388 N ARG A 313 0.712 34.185 187.312 1.00 41.18 N ANISOU 3388 N ARG A 313 7304 5052 3293 780 -130 -218 N ATOM 3389 CA ARG A 313 -0.261 35.267 187.393 1.00 42.30 C ANISOU 3389 CA ARG A 313 7582 5115 3373 936 -123 -221 C ATOM 3390 C ARG A 313 0.061 36.195 188.558 1.00 45.57 C ANISOU 3390 C ARG A 313 8198 5391 3724 975 -155 -248 C ATOM 3391 O ARG A 313 -0.190 37.399 188.492 1.00 46.92 O ANISOU 3391 O ARG A 313 8552 5436 3837 1061 -176 -253 O ATOM 3392 CB ARG A 313 -1.676 34.711 187.537 1.00 40.75 C ANISOU 3392 CB ARG A 313 7275 5036 3171 1066 -63 -216 C ATOM 3393 CG ARG A 313 -2.245 34.123 186.260 1.00 38.70 C ANISOU 3393 CG ARG A 313 6859 4897 2949 1055 -38 -193 C ATOM 3394 CD ARG A 313 -3.720 33.798 186.422 1.00 37.98 C ANISOU 3394 CD ARG A 313 6677 4923 2830 1189 15 -191 C ATOM 3395 NE ARG A 313 -3.947 32.795 187.457 1.00 36.53 N ANISOU 3395 NE ARG A 313 6405 4820 2655 1162 53 -202 N ATOM 3396 CZ ARG A 313 -3.870 31.484 187.253 1.00 34.43 C ANISOU 3396 CZ ARG A 313 5983 4661 2438 1047 77 -195 C ATOM 3397 NH1 ARG A 313 -3.569 31.018 186.049 1.00 33.18 N1+ ANISOU 3397 NH1 ARG A 313 5732 4548 2328 953 66 -182 N1+ ATOM 3398 NH2 ARG A 313 -4.091 30.639 188.252 1.00 33.91 N ANISOU 3398 NH2 ARG A 313 5867 4653 2365 1024 111 -201 N ATOM 3399 N ARG A 314 0.615 35.629 189.624 1.00 47.58 N ANISOU 3399 N ARG A 314 8428 5668 3981 913 -163 -267 N ATOM 3400 CA ARG A 314 1.044 36.421 190.770 1.00 51.02 C ANISOU 3400 CA ARG A 314 9047 5987 4350 924 -201 -298 C ATOM 3401 C ARG A 314 2.214 37.315 190.371 1.00 54.57 C ANISOU 3401 C ARG A 314 9636 6316 4784 800 -268 -304 C ATOM 3402 O ARG A 314 2.289 38.474 190.778 1.00 56.16 O ANISOU 3402 O ARG A 314 10051 6371 4915 834 -303 -324 O ATOM 3403 CB ARG A 314 1.435 35.516 191.943 1.00 48.39 C ANISOU 3403 CB ARG A 314 8641 5726 4017 875 -198 -314 C ATOM 3404 CG ARG A 314 1.673 36.253 193.256 1.00 46.64 C ANISOU 3404 CG ARG A 314 8600 5412 3711 905 -231 -352 C ATOM 3405 CD ARG A 314 2.051 35.283 194.367 1.00 44.13 C ANISOU 3405 CD ARG A 314 8201 5180 3385 857 -229 -362 C ATOM 3406 NE ARG A 314 3.366 34.685 194.151 1.00 41.79 N ANISOU 3406 NE ARG A 314 7820 4926 3133 696 -278 -356 N ATOM 3407 CZ ARG A 314 3.783 33.560 194.727 1.00 39.52 C ANISOU 3407 CZ ARG A 314 7417 4738 2860 646 -277 -349 C ATOM 3408 NH1 ARG A 314 2.984 32.897 195.552 1.00 38.54 N1+ ANISOU 3408 NH1 ARG A 314 7255 4675 2712 726 -227 -344 N1+ ATOM 3409 NH2 ARG A 314 4.998 33.093 194.471 1.00 38.36 N ANISOU 3409 NH2 ARG A 314 7194 4637 2744 518 -326 -345 N ATOM 3410 N TYR A 315 3.120 36.771 189.565 1.00 56.63 N ANISOU 3410 N TYR A 315 9776 6639 5100 652 -286 -286 N ATOM 3411 CA TYR A 315 4.262 37.532 189.073 1.00 59.49 C ANISOU 3411 CA TYR A 315 10241 6918 5443 510 -344 -287 C ATOM 3412 C TYR A 315 3.800 38.654 188.149 1.00 60.10 C ANISOU 3412 C TYR A 315 10471 6876 5488 562 -348 -268 C ATOM 3413 O TYR A 315 4.445 39.697 188.052 1.00 61.61 O ANISOU 3413 O TYR A 315 10903 6894 5611 495 -404 -270 O ATOM 3414 CB TYR A 315 5.248 36.617 188.344 1.00 61.55 C ANISOU 3414 CB TYR A 315 10313 7308 5765 361 -351 -272 C ATOM 3415 CG TYR A 315 5.889 35.560 189.220 1.00 63.51 C ANISOU 3415 CG TYR A 315 10433 7664 6035 308 -361 -289 C ATOM 3416 CD1 TYR A 315 5.981 35.729 190.595 1.00 65.32 C ANISOU 3416 CD1 TYR A 315 10753 7851 6214 334 -386 -319 C ATOM 3417 CD2 TYR A 315 6.405 34.394 188.668 1.00 63.19 C ANISOU 3417 CD2 TYR A 315 10189 7766 6052 240 -346 -274 C ATOM 3418 CE1 TYR A 315 6.568 34.764 191.398 1.00 65.86 C ANISOU 3418 CE1 TYR A 315 10712 8020 6290 293 -400 -330 C ATOM 3419 CE2 TYR A 315 6.993 33.425 189.460 1.00 63.56 C ANISOU 3419 CE2 TYR A 315 10136 7905 6110 208 -359 -286 C ATOM 3420 CZ TYR A 315 7.072 33.615 190.823 1.00 65.09 C ANISOU 3420 CZ TYR A 315 10421 8056 6252 234 -387 -311 C ATOM 3421 OH TYR A 315 7.657 32.651 191.612 1.00 65.86 O ANISOU 3421 OH TYR A 315 10427 8247 6349 209 -405 -318 O ATOM 3422 N LEU A 316 2.680 38.430 187.470 1.00 59.63 N ANISOU 3422 N LEU A 316 10337 6869 5450 690 -298 -246 N ATOM 3423 CA LEU A 316 2.094 39.441 186.598 1.00 61.52 C ANISOU 3423 CA LEU A 316 10761 6978 5635 791 -304 -223 C ATOM 3424 C LEU A 316 1.423 40.538 187.415 1.00 63.61 C ANISOU 3424 C LEU A 316 11314 7054 5802 970 -320 -241 C ATOM 3425 O LEU A 316 1.393 41.700 187.011 1.00 65.12 O ANISOU 3425 O LEU A 316 11793 7039 5911 1028 -357 -229 O ATOM 3426 CB LEU A 316 1.082 38.807 185.642 1.00 60.61 C ANISOU 3426 CB LEU A 316 10449 7013 5567 878 -249 -197 C ATOM 3427 CG LEU A 316 1.643 37.871 184.571 1.00 59.35 C ANISOU 3427 CG LEU A 316 10067 7007 5478 729 -237 -173 C ATOM 3428 CD1 LEU A 316 0.517 37.215 183.783 1.00 58.50 C ANISOU 3428 CD1 LEU A 316 9794 7035 5396 827 -189 -153 C ATOM 3429 CD2 LEU A 316 2.582 38.628 183.644 1.00 59.71 C ANISOU 3429 CD2 LEU A 316 10236 6959 5491 604 -279 -150 C ATOM 3430 N SER A 317 0.883 40.157 188.568 1.00 64.25 N ANISOU 3430 N SER A 317 11330 7200 5881 1061 -292 -269 N ATOM 3431 CA SER A 317 0.195 41.098 189.441 1.00 66.76 C ANISOU 3431 CA SER A 317 11896 7372 6098 1250 -299 -290 C ATOM 3432 C SER A 317 1.169 42.096 190.050 1.00 70.00 C ANISOU 3432 C SER A 317 12598 7570 6429 1159 -372 -312 C ATOM 3433 O SER A 317 0.832 43.261 190.249 1.00 72.08 O ANISOU 3433 O SER A 317 13172 7627 6586 1289 -402 -314 O ATOM 3434 CB SER A 317 -0.549 40.356 190.550 1.00 65.82 C ANISOU 3434 CB SER A 317 11615 7404 5990 1339 -246 -316 C ATOM 3435 OG SER A 317 0.359 39.698 191.416 1.00 65.20 O ANISOU 3435 OG SER A 317 11431 7396 5946 1171 -260 -341 O ATOM 3436 N VAL A 318 2.378 41.635 190.349 1.00 71.03 N ANISOU 3436 N VAL A 318 12634 7754 6601 937 -405 -327 N ATOM 3437 CA VAL A 318 3.387 42.514 190.924 1.00 73.86 C ANISOU 3437 CA VAL A 318 13245 7937 6881 812 -481 -350 C ATOM 3438 C VAL A 318 4.145 43.252 189.822 1.00 74.21 C ANISOU 3438 C VAL A 318 13469 7829 6897 671 -533 -316 C ATOM 3439 O VAL A 318 4.857 44.219 190.089 1.00 76.56 O ANISOU 3439 O VAL A 318 14047 7934 7107 563 -601 -324 O ATOM 3440 CB VAL A 318 4.381 41.739 191.815 1.00 74.81 C ANISOU 3440 CB VAL A 318 13193 8195 7038 645 -503 -385 C ATOM 3441 CG1 VAL A 318 3.656 41.116 193.004 1.00 75.17 C ANISOU 3441 CG1 VAL A 318 13116 8361 7085 772 -456 -417 C ATOM 3442 CG2 VAL A 318 5.115 40.679 191.010 1.00 74.49 C ANISOU 3442 CG2 VAL A 318 12867 8337 7100 490 -491 -361 C ATOM 3443 N PHE A 319 3.983 42.799 188.582 1.00 72.33 N ANISOU 3443 N PHE A 319 13078 7681 6725 656 -499 -277 N ATOM 3444 CA PHE A 319 4.612 43.466 187.448 1.00 72.42 C ANISOU 3444 CA PHE A 319 13255 7560 6701 522 -538 -240 C ATOM 3445 C PHE A 319 3.796 44.683 187.033 1.00 72.99 C ANISOU 3445 C PHE A 319 13677 7384 6673 695 -552 -215 C ATOM 3446 O PHE A 319 4.332 45.651 186.494 1.00 74.46 O ANISOU 3446 O PHE A 319 14160 7353 6777 588 -606 -187 O ATOM 3447 CB PHE A 319 4.765 42.502 186.268 1.00 70.52 C ANISOU 3447 CB PHE A 319 12712 7526 6557 443 -497 -210 C ATOM 3448 N PHE A 320 2.494 44.621 187.295 1.00 71.65 N ANISOU 3448 N PHE A 320 13479 7248 6498 966 -505 -222 N ATOM 3449 CA PHE A 320 1.574 45.692 186.934 1.00 72.15 C ANISOU 3449 CA PHE A 320 13853 7102 6457 1198 -514 -200 C ATOM 3450 C PHE A 320 0.818 46.203 188.157 1.00 72.82 C ANISOU 3450 C PHE A 320 14102 7108 6459 1420 -514 -225 C ATOM 3451 O PHE A 320 1.183 47.218 188.749 1.00 74.79 O ANISOU 3451 O PHE A 320 14690 7132 6595 1404 -573 -228 O ATOM 3452 CB PHE A 320 0.586 45.209 185.870 1.00 71.07 C ANISOU 3452 CB PHE A 320 13522 7112 6369 1358 -456 -178 C ATOM 3453 CG PHE A 320 1.244 44.677 184.627 1.00 69.69 C ANISOU 3453 CG PHE A 320 13164 7051 6265 1152 -450 -151 C ATOM 3454 CD1 PHE A 320 2.335 45.327 184.073 1.00 70.81 C ANISOU 3454 CD1 PHE A 320 13518 7025 6361 933 -506 -130 C ATOM 3455 CD2 PHE A 320 0.773 43.526 184.014 1.00 67.54 C ANISOU 3455 CD2 PHE A 320 12511 7060 6092 1164 -391 -142 C ATOM 3456 CE1 PHE A 320 2.943 44.841 182.931 1.00 69.65 C ANISOU 3456 CE1 PHE A 320 13190 7008 6265 746 -497 -99 C ATOM 3457 CE2 PHE A 320 1.378 43.035 182.871 1.00 66.28 C ANISOU 3457 CE2 PHE A 320 12179 7020 5984 983 -386 -110 C ATOM 3458 CZ PHE A 320 2.465 43.694 182.330 1.00 67.36 C ANISOU 3458 CZ PHE A 320 12513 7007 6074 783 -436 -88 C TER 3459 PHE A 320 HETATM 3460 C1 73R A1201 2.612 26.418 152.427 1.00 42.33 C HETATM 3461 C2 73R A1201 2.580 25.930 153.784 1.00 40.78 C HETATM 3462 C3 73R A1201 3.864 25.693 154.379 1.00 38.08 C HETATM 3463 C5 73R A1201 4.977 26.356 152.480 1.00 38.42 C HETATM 3464 C8 73R A1201 1.437 26.676 151.767 1.00 42.24 C HETATM 3465 C9 73R A1201 0.200 26.476 152.385 1.00 39.60 C HETATM 3466 C12 73R A1201 0.140 26.002 153.708 1.00 39.74 C HETATM 3467 C13 73R A1201 1.316 25.729 154.406 1.00 40.23 C HETATM 3468 C14 73R A1201 5.124 25.117 156.581 1.00 30.15 C HETATM 3469 C15 73R A1201 5.961 26.310 156.584 1.00 28.02 C HETATM 3470 C17 73R A1201 7.513 24.396 156.556 1.00 26.05 C HETATM 3471 C18 73R A1201 6.059 24.119 156.055 1.00 29.96 C HETATM 3472 CAP 73R A1201 -1.227 25.788 154.361 1.00 40.37 C HETATM 3473 N4 73R A1201 4.971 25.914 153.710 1.00 38.86 N HETATM 3474 N6 73R A1201 3.841 26.613 151.823 1.00 40.29 N HETATM 3475 N7 73R A1201 3.907 25.196 155.767 1.00 32.85 N HETATM 3476 N16 73R A1201 7.367 25.918 156.574 1.00 26.99 N HETATM 3477 O24 73R A1201 5.574 27.465 156.612 1.00 27.82 O HETATM 3478 C26 73R A1201 8.417 26.939 156.610 1.00 28.52 C HETATM 3479 C27 73R A1201 9.230 26.882 157.875 1.00 28.65 C HETATM 3480 C28 73R A1201 10.317 25.768 157.765 1.00 35.30 C HETATM 3481 C29 73R A1201 11.169 25.737 156.503 1.00 35.87 C HETATM 3482 C30 73R A1201 10.279 25.867 155.287 1.00 34.22 C HETATM 3483 C31 73R A1201 9.291 27.020 155.377 1.00 31.25 C HETATM 3484 C35 73R A1201 8.415 27.098 154.135 1.00 30.14 C HETATM 3485 C36 73R A1201 8.582 28.552 153.526 1.00 36.25 C HETATM 3486 C37 73R A1201 7.281 29.002 152.872 1.00 37.43 C HETATM 3487 N38 73R A1201 11.917 24.504 156.374 1.00 39.24 N HETATM 3488 C39 73R A1201 11.477 23.448 157.260 1.00 42.45 C HETATM 3489 C40 73R A1201 13.365 24.683 156.482 1.00 37.74 C HETATM 3490 C41 73R A1201 13.755 25.213 157.809 1.00 37.73 C HETATM 3491 C42 73R A1201 13.876 25.608 155.372 1.00 37.34 C HETATM 3492 F32 73R A1201 -2.184 25.880 153.403 1.00 41.03 F HETATM 3493 F33 73R A1201 -1.277 24.556 154.929 1.00 40.34 F HETATM 3494 F34 73R A1201 -1.446 26.724 155.297 1.00 40.60 F HETATM 3495 C VT5 A1202 3.528 25.441 191.332 1.00 34.52 C HETATM 3496 C1 VT5 A1202 4.672 26.130 190.644 1.00 33.69 C HETATM 3497 O VT5 A1202 5.826 25.881 190.956 1.00 36.66 O HETATM 3498 C2 VT5 A1202 4.403 27.155 189.576 1.00 28.84 C HETATM 3499 C3 VT5 A1202 3.337 27.697 189.319 1.00 29.52 C HETATM 3500 C4 VT5 A1202 3.637 28.654 188.211 1.00 27.41 C HETATM 3501 O1 VT5 A1202 2.754 29.403 187.659 1.00 29.12 O HETATM 3502 N VT5 A1202 4.945 28.590 187.922 1.00 25.08 N HETATM 3503 C5 VT5 A1202 5.605 27.593 188.794 1.00 25.74 C HETATM 3504 C6 VT5 A1202 6.164 26.578 187.788 1.00 22.50 C HETATM 3505 C11 VT5 A1202 7.550 26.071 188.176 1.00 20.59 C HETATM 3506 C10 VT5 A1202 8.143 25.277 187.021 1.00 17.00 C HETATM 3507 C9 VT5 A1202 7.251 24.085 186.702 1.00 16.61 C HETATM 3508 C8 VT5 A1202 5.836 24.539 186.368 1.00 18.20 C HETATM 3509 C7 VT5 A1202 5.245 25.397 187.483 1.00 20.93 C HETATM 3510 C12 VT5 A1202 5.566 29.315 186.990 1.00 24.90 C HETATM 3511 C13 VT5 A1202 6.648 30.123 187.333 1.00 25.07 C HETATM 3512 C14 VT5 A1202 7.330 30.907 186.418 1.00 24.49 C HETATM 3513 C15 VT5 A1202 6.935 30.909 185.094 1.00 23.56 C HETATM 3514 C16 VT5 A1202 5.860 30.122 184.711 1.00 23.95 C HETATM 3515 C17 VT5 A1202 5.192 29.342 185.652 1.00 25.10 C HETATM 3516 F VT5 A1202 4.152 28.588 185.252 1.00 26.00 F HETATM 3517 CL VT5 A1202 7.821 31.924 183.912 1.00 57.42 CL HETATM 3518 O2 VT5 A1202 1.991 27.493 189.905 1.00 32.75 O HETATM 3519 S SO4 A1203 8.466 31.905 194.925 1.00 80.56 S HETATM 3520 O1 SO4 A1203 8.915 30.908 193.957 1.00 80.01 O1+ HETATM 3521 O2 SO4 A1203 9.028 33.207 194.579 1.00 80.71 O HETATM 3522 O3 SO4 A1203 7.008 31.979 194.903 1.00 80.89 O HETATM 3523 O4 SO4 A1203 8.912 31.517 196.260 1.00 80.20 O HETATM 3524 S SO4 A1204 1.835 23.086 200.132 1.00 29.30 S HETATM 3525 O1 SO4 A1204 2.275 22.470 198.883 1.00 33.85 O1+ HETATM 3526 O2 SO4 A1204 0.845 24.119 199.847 1.00 30.33 O HETATM 3527 O3 SO4 A1204 1.232 22.073 200.993 1.00 31.49 O HETATM 3528 O4 SO4 A1204 2.992 23.676 200.800 1.00 31.37 O HETATM 3529 S SO4 A1205 1.876 0.926 226.776 1.00 53.50 S HETATM 3530 O1 SO4 A1205 0.555 0.403 227.119 1.00 53.51 O1+ HETATM 3531 O2 SO4 A1205 2.054 0.879 225.328 1.00 53.43 O HETATM 3532 O3 SO4 A1205 2.911 0.121 227.421 1.00 53.34 O HETATM 3533 O4 SO4 A1205 1.982 2.309 227.232 1.00 53.40 O HETATM 3534 S SO4 A1206 -1.326 19.123 220.340 1.00 67.24 S HETATM 3535 O1 SO4 A1206 -0.051 18.563 219.899 1.00 66.88 O HETATM 3536 O2 SO4 A1206 -1.500 20.452 219.763 1.00 66.21 O HETATM 3537 O3 SO4 A1206 -1.347 19.221 221.796 1.00 67.97 O HETATM 3538 O4 SO4 A1206 -2.410 18.251 219.911 1.00 66.86 O HETATM 3539 C18 OLC A1207 -8.074 19.986 170.669 1.00 38.84 C HETATM 3540 C10 OLC A1207 -3.942 19.169 178.660 1.00 44.41 C HETATM 3541 C9 OLC A1207 -3.649 18.680 179.883 1.00 44.82 C HETATM 3542 C17 OLC A1207 -8.590 19.085 171.771 1.00 40.16 C HETATM 3543 C11 OLC A1207 -4.931 18.468 177.753 1.00 45.15 C HETATM 3544 C8 OLC A1207 -4.298 17.411 180.390 1.00 44.71 C HETATM 3545 C24 OLC A1207 -5.042 14.965 191.446 1.00 51.44 C HETATM 3546 C16 OLC A1207 -7.477 18.758 172.745 1.00 41.51 C HETATM 3547 C12 OLC A1207 -5.478 19.469 176.756 1.00 45.15 C HETATM 3548 C7 OLC A1207 -4.306 17.423 181.903 1.00 44.13 C HETATM 3549 C15 OLC A1207 -7.310 19.887 173.739 1.00 42.32 C HETATM 3550 C13 OLC A1207 -5.990 18.760 175.520 1.00 43.31 C HETATM 3551 C6 OLC A1207 -2.892 17.285 182.424 1.00 44.34 C HETATM 3552 C14 OLC A1207 -7.340 19.335 175.148 1.00 42.63 C HETATM 3553 C5 OLC A1207 -2.936 16.825 183.866 1.00 44.97 C HETATM 3554 C4 OLC A1207 -1.531 16.777 184.426 1.00 44.60 C HETATM 3555 C3 OLC A1207 -1.428 15.702 185.487 1.00 46.07 C HETATM 3556 C2 OLC A1207 -2.284 16.071 186.679 1.00 48.69 C HETATM 3557 C21 OLC A1207 -3.531 15.258 189.498 1.00 52.39 C HETATM 3558 C1 OLC A1207 -1.785 15.337 187.906 1.00 50.13 C HETATM 3559 C22 OLC A1207 -3.610 14.913 190.970 1.00 52.22 C HETATM 3560 O19 OLC A1207 -0.998 14.417 187.780 1.00 49.33 O HETATM 3561 O25 OLC A1207 -5.086 14.470 192.765 1.00 52.38 O HETATM 3562 O23 OLC A1207 -3.123 13.609 191.181 1.00 54.19 O HETATM 3563 O20 OLC A1207 -2.233 15.712 189.186 1.00 51.58 O HETATM 3564 ZN ZN A1208 5.518 16.229 198.687 1.00 40.29 ZN HETATM 3565 O HOH A1301 11.818 21.252 200.180 1.00 18.42 O HETATM 3566 O HOH A1302 6.606 -4.565 222.790 1.00 34.52 O HETATM 3567 O HOH A1303 18.314 17.829 161.880 1.00 17.14 O HETATM 3568 O HOH A1304 -7.517 -0.764 210.205 1.00 21.38 O HETATM 3569 O HOH A1305 17.006 17.070 216.161 1.00 35.79 O HETATM 3570 O HOH A1306 11.832 14.415 202.181 1.00 24.34 O HETATM 3571 O HOH A1307 5.032 14.327 198.459 1.00 7.78 O HETATM 3572 O HOH A1308 6.529 26.228 167.188 1.00 40.81 O HETATM 3573 O HOH A1309 -3.803 8.572 201.851 1.00 24.03 O HETATM 3574 O HOH A1310 5.941 30.975 198.858 1.00 8.65 O HETATM 3575 O HOH A1311 -2.553 7.066 200.763 1.00 3.08 O HETATM 3576 O HOH A1312 10.421 24.909 194.409 1.00 26.91 O HETATM 3577 O HOH A1313 10.355 22.239 154.323 1.00 28.84 O HETATM 3578 O HOH A1314 0.508 4.148 161.185 1.00 25.79 O HETATM 3579 O HOH A1315 15.034 14.598 215.822 1.00 30.01 O HETATM 3580 O HOH A1316 17.079 12.508 215.054 1.00 14.32 O HETATM 3581 O HOH A1317 1.182 4.687 163.526 1.00 14.53 O CONECT 591 1192 CONECT 849 3564 CONECT 1111 1118 CONECT 1118 1111 1119 CONECT 1119 1118 1120 1126 CONECT 1120 1119 1121 CONECT 1121 1120 1122 CONECT 1122 1121 1123 CONECT 1123 1122 1124 1125 CONECT 1124 1123 CONECT 1125 1123 CONECT 1126 1119 1127 1128 CONECT 1127 1126 CONECT 1128 1126 CONECT 1192 591 CONECT 1561 3564 CONECT 2808 3564 CONECT 3460 3461 3464 3474 CONECT 3461 3460 3462 3467 CONECT 3462 3461 3473 3475 CONECT 3463 3473 3474 CONECT 3464 3460 3465 CONECT 3465 3464 3466 CONECT 3466 3465 3467 3472 CONECT 3467 3461 3466 CONECT 3468 3469 3471 3475 CONECT 3469 3468 3476 3477 CONECT 3470 3471 3476 CONECT 3471 3468 3470 CONECT 3472 3466 3492 3493 3494 CONECT 3473 3462 3463 CONECT 3474 3460 3463 CONECT 3475 3462 3468 CONECT 3476 3469 3470 3478 CONECT 3477 3469 CONECT 3478 3476 3479 3483 CONECT 3479 3478 3480 CONECT 3480 3479 3481 CONECT 3481 3480 3482 3487 CONECT 3482 3481 3483 CONECT 3483 3478 3482 3484 CONECT 3484 3483 3485 CONECT 3485 3484 3486 CONECT 3486 3485 CONECT 3487 3481 3488 3489 CONECT 3488 3487 CONECT 3489 3487 3490 3491 CONECT 3490 3489 CONECT 3491 3489 CONECT 3492 3472 CONECT 3493 3472 CONECT 3494 3472 CONECT 3495 3496 CONECT 3496 3495 3497 3498 CONECT 3497 3496 CONECT 3498 3496 3499 3503 CONECT 3499 3498 3500 3518 CONECT 3500 3499 3501 3502 CONECT 3501 3500 CONECT 3502 3500 3503 3510 CONECT 3503 3498 3502 3504 CONECT 3504 3503 3505 3509 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 CONECT 3508 3507 3509 CONECT 3509 3504 3508 CONECT 3510 3502 3511 3515 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 3514 3517 CONECT 3514 3513 3515 CONECT 3515 3510 3514 3516 CONECT 3516 3515 CONECT 3517 3513 CONECT 3518 3499 CONECT 3519 3520 3521 3522 3523 CONECT 3520 3519 CONECT 3521 3519 CONECT 3522 3519 CONECT 3523 3519 CONECT 3524 3525 3526 3527 3528 CONECT 3525 3524 CONECT 3526 3524 CONECT 3527 3524 CONECT 3528 3524 CONECT 3529 3530 3531 3532 3533 CONECT 3530 3529 CONECT 3531 3529 CONECT 3532 3529 CONECT 3533 3529 CONECT 3534 3535 3536 3537 3538 CONECT 3535 3534 CONECT 3536 3534 CONECT 3537 3534 CONECT 3538 3534 CONECT 3539 3542 CONECT 3540 3541 3543 CONECT 3541 3540 3544 CONECT 3542 3539 3546 CONECT 3543 3540 3547 CONECT 3544 3541 3548 CONECT 3545 3559 3561 CONECT 3546 3542 3549 CONECT 3547 3543 3550 CONECT 3548 3544 3551 CONECT 3549 3546 3552 CONECT 3550 3547 3552 CONECT 3551 3548 3553 CONECT 3552 3549 3550 CONECT 3553 3551 3554 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3558 CONECT 3557 3559 3563 CONECT 3558 3556 3560 3563 CONECT 3559 3545 3557 3562 CONECT 3560 3558 CONECT 3561 3545 CONECT 3562 3559 CONECT 3563 3557 3558 CONECT 3564 849 1561 2808 3571 CONECT 3571 3564 MASTER 415 0 9 23 5 0 18 6 3580 1 123 40 END