HEADER MEMBRANE PROTEIN 02-DEC-13 4NTJ TITLE STRUCTURE OF THE HUMAN P2Y12 RECEPTOR IN COMPLEX WITH AN TITLE 2 ANTITHROMBOTIC DRUG COMPND MOL_ID: 1; COMPND 2 MOLECULE: P2Y PURINOCEPTOR 12,SOLUBLE CYTOCHROME B562,P2Y COMPND 3 PURINOCEPTOR 12; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: P2Y12,ADP-GLUCOSE RECEPTOR,ADPG-R,P2T(AC),P2Y(AC),P2Y(CYC), COMPND 6 P2Y12 PLATELET ADP RECEPTOR,P2Y(ADP),SP1999; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 OTHER_DETAILS: CHIMERA PROTEIN OF N-TERMINAL RESIDUES 2-223 FROM COMPND 10 P2Y12R (P2Y12_HUMAN), SOLUBLE CYTOCHROME B562 (C562_ECOLX), AND C- COMPND 11 TERMINAL RESIDUES 224-342 FROM P2Y12R (P2Y12_HUMAN). SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: P2RY12, HORK3, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIROUS; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1 KEYWDS HUMAN P2Y12 RECEPTOR, GPCR NETWORK, MEMBRANE PROTEIN, LIPIDIC CUBIC KEYWDS 2 PHASE, ANTITHROMBOTIC DRUG, GPCR, PSI-BIOLOGY, STRUCTURAL GENOMICS, KEYWDS 3 SIGNALING PROTEIN, MEMBRANE EXPDTA X-RAY DIFFRACTION AUTHOR K.ZHANG,J.ZHANG,Z.-G.GAO,D.ZHANG,L.ZHU,G.W.HAN,S.M.MOSS,S.PAOLETTA, AUTHOR 2 E.KISELEV,W.LU,G.FENALTI,W.ZHANG,C.E.MULLER,H.YANG,H.JIANG, AUTHOR 3 V.CHEREZOV,V.KATRITCH,K.A.JACOBSON,R.C.STEVENS,B.WU,Q.ZHAO,GPCR AUTHOR 4 NETWORK (GPCR) REVDAT 4 22-NOV-17 4NTJ 1 REMARK REVDAT 3 21-JUN-17 4NTJ 1 COMPND SOURCE REVDAT 2 28-MAY-14 4NTJ 1 JRNL REVDAT 1 26-MAR-14 4NTJ 0 JRNL AUTH K.ZHANG,J.ZHANG,Z.-G.GAO,D.ZHANG,L.ZHU,G.W.HAN,S.M.MOSS, JRNL AUTH 2 S.PAOLETTA,E.KISELEV,W.LU,G.FENALTI,W.ZHANG,C.E.MULLER, JRNL AUTH 3 H.YANG,H.JIANG,V.CHEREZOV,V.KATRITCH,K.A.JACOBSON, JRNL AUTH 4 R.C.STEVENS,B.WU,Q.ZHAO JRNL TITL STRUCTURE OF THE HUMAN P2Y12 RECEPTOR IN COMPLEX WITH AN JRNL TITL 2 ANTITHROMBOTIC DRUG JRNL REF NATURE V. 509 115 2014 JRNL REFN ISSN 0028-0836 JRNL PMID 24670650 JRNL DOI 10.1038/NATURE13083 REMARK 2 REMARK 2 RESOLUTION. 2.62 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2 REMARK 3 NUMBER OF REFLECTIONS : 19094 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180 REMARK 3 FREE R VALUE TEST SET COUNT : 990 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.18 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2378 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2330 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2271 REMARK 3 BIN R VALUE (WORKING SET) : 0.2320 REMARK 3 BIN FREE R VALUE : 0.2567 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 107 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2886 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 127 REMARK 3 SOLVENT ATOMS : 12 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 84.46 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 106.1 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -14.03430 REMARK 3 B22 (A**2) : 14.16750 REMARK 3 B33 (A**2) : -0.13320 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.92040 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.549 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.385 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3080 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4190 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1414 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 435 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3080 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 434 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3584 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.05 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.16 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.16 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|16 - A|312 } REMARK 3 ORIGIN FOR THE GROUP (A): 13.0719 87.5364 46.9005 REMARK 3 T TENSOR REMARK 3 T11: -0.1235 T22: -0.3298 REMARK 3 T33: -0.1791 T12: 0.1110 REMARK 3 T13: -0.0508 T23: 0.0404 REMARK 3 L TENSOR REMARK 3 L11: 2.9964 L22: 5.3271 REMARK 3 L33: 1.9506 L12: -1.6291 REMARK 3 L13: -0.2778 L23: 0.5277 REMARK 3 S TENSOR REMARK 3 S11: -0.1818 S12: 0.0268 S13: -0.0774 REMARK 3 S21: 0.1630 S22: 0.2222 S23: 0.5350 REMARK 3 S31: 0.1073 S32: -0.0276 S33: -0.0405 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1001 - A|1106 } REMARK 3 ORIGIN FOR THE GROUP (A): 33.7948 48.4483 13.0903 REMARK 3 T TENSOR REMARK 3 T11: -0.1463 T22: -0.2704 REMARK 3 T33: -0.2015 T12: -0.0483 REMARK 3 T13: 0.0222 T23: -0.0579 REMARK 3 L TENSOR REMARK 3 L11: 6.3853 L22: 8.2964 REMARK 3 L33: 6.1819 L12: -0.9788 REMARK 3 L13: 1.5442 L23: 1.5059 REMARK 3 S TENSOR REMARK 3 S11: 0.0454 S12: 0.1219 S13: -0.3863 REMARK 3 S21: -0.2775 S22: -0.2232 S23: 0.1558 REMARK 3 S31: 0.2717 S32: -0.1292 S33: 0.1778 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THERE ARE SOME UNKNOWN DENSITIES. REMARK 3 LOCATED NEAR THE SIDE CHAIN OF TYR 32. THEY HAVE NOT BEEN REMARK 3 MODELLED. REMARK 4 REMARK 4 4NTJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-DEC-13. REMARK 100 THE DEPOSITION ID IS D_1000083637. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-MAR-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0-6.5 REMARK 200 NUMBER OF CRYSTALS USED : 15 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) : 1.033 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19116 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 79.5 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.95800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3VW7 (PAR1), PDB ENTRY 1M6T (BRIL) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05-0.15M AMMONIUM FORMATE, 0.1M REMARK 280 SODIUM CACODYLATE, PH 6.0-6.5, 25-35% PEG 400, 200M AZD1283, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.32500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.21500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.32500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 78.21500 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 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 -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 GLN A 2 REMARK 465 ALA A 3 REMARK 465 VAL A 4 REMARK 465 ASP A 5 REMARK 465 ASN A 6 REMARK 465 LEU A 7 REMARK 465 THR A 8 REMARK 465 SER A 9 REMARK 465 ALA A 10 REMARK 465 PRO A 11 REMARK 465 GLY A 12 REMARK 465 ASN A 13 REMARK 465 THR A 14 REMARK 465 SER A 15 REMARK 465 GLY A 88 REMARK 465 THR A 89 REMARK 465 GLY A 90 REMARK 465 PRO A 91 REMARK 465 SER A 133 REMARK 465 ASN A 134 REMARK 465 PRO A 135 REMARK 465 THR A 163 REMARK 465 ASN A 164 REMARK 465 ARG A 165 REMARK 465 GLN A 166 REMARK 465 PRO A 167 REMARK 465 ARG A 168 REMARK 465 ASP A 169 REMARK 465 LYS A 170 REMARK 465 ASN A 171 REMARK 465 VAL A 172 REMARK 465 LYS A 173 REMARK 465 LYS A 174 REMARK 465 CYS A 175 REMARK 465 SER A 176 REMARK 465 PHE A 177 REMARK 465 LEU A 178 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 LYS A 1059 REMARK 465 PRO A 230 REMARK 465 LEU A 313 REMARK 465 LYS A 314 REMARK 465 CYS A 315 REMARK 465 PRO A 316 REMARK 465 ASN A 317 REMARK 465 SER A 318 REMARK 465 ALA A 319 REMARK 465 THR A 320 REMARK 465 SER A 321 REMARK 465 LEU A 322 REMARK 465 SER A 323 REMARK 465 GLN A 324 REMARK 465 ASP A 325 REMARK 465 ASN A 326 REMARK 465 ARG A 327 REMARK 465 LYS A 328 REMARK 465 LYS A 329 REMARK 465 GLU A 330 REMARK 465 GLN A 331 REMARK 465 ASP A 332 REMARK 465 GLY A 333 REMARK 465 GLY A 334 REMARK 465 ASP A 335 REMARK 465 PRO A 336 REMARK 465 ASN A 337 REMARK 465 GLU A 338 REMARK 465 GLU A 339 REMARK 465 THR A 340 REMARK 465 PRO A 341 REMARK 465 MET A 342 REMARK 465 GLY A 343 REMARK 465 ARG A 344 REMARK 465 PRO A 345 REMARK 465 LEU A 346 REMARK 465 GLU A 347 REMARK 465 VAL A 348 REMARK 465 LEU A 349 REMARK 465 PHE A 350 REMARK 465 GLN A 351 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 ARG A 54 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 56 CG CD CE NZ REMARK 470 LYS A 86 CG CD CE NZ REMARK 470 ARG A 93 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 131 CG CD CE NZ REMARK 470 LEU A 138 CG CD1 CD2 REMARK 470 LEU A 139 CG CD1 CD2 REMARK 470 ILE A 161 CG1 CG2 CD1 REMARK 470 LYS A 179 CG CD CE NZ REMARK 470 GLU A 215 CG CD OE1 OE2 REMARK 470 LEU A1048 CG CD1 CD2 REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 GLU A1081 CG CD OE1 OE2 REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 LYS A1095 CE NZ REMARK 470 TYR A1101 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 228 CG CD CE NZ REMARK 470 ARG A 231 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 232 CG CD CE NZ REMARK 470 LYS A 233 CG CD CE NZ REMARK 470 VAL A 236 CG1 CG2 REMARK 470 LYS A 237 NZ REMARK 470 SER A 262 OG REMARK 470 GLN A 263 CG CD OE1 NE2 REMARK 470 THR A 264 OG1 CG2 REMARK 470 ARG A 265 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 267 CG1 CG2 REMARK 470 PHE A 268 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 303 CG CD CE NZ REMARK 470 LEU A 309 CG CD1 CD2 REMARK 470 ILE A 310 CG1 CG2 CD1 REMARK 470 MET A 312 CG SD CE REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 26 -66.20 -120.04 REMARK 500 LYS A 131 77.57 59.53 REMARK 500 MET A 160 -74.56 -69.04 REMARK 500 ASP A1021 -71.68 -113.65 REMARK 500 THR A1044 79.80 -118.11 REMARK 500 LYS A1083 106.36 -48.21 REMARK 500 LYS A 237 -60.06 -92.25 REMARK 500 PHE A 239 1.63 -63.56 REMARK 500 LEU A 261 54.89 -151.40 REMARK 500 SER A 262 -72.40 -142.69 REMARK 500 ARG A 265 -69.72 74.05 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1204 REMARK 610 OLC A 1205 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZJ A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1205 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-87 RELATED DB: TARGETTRACK DBREF 4NTJ A 2 223 UNP Q9H244 P2Y12_HUMAN 2 223 DBREF 4NTJ A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4NTJ A 224 342 UNP Q9H244 P2Y12_HUMAN 224 342 SEQADV 4NTJ ASP A -8 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ TYR A -7 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ LYS A -6 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ ASP A -5 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ ASP A -4 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ ASP A -3 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ ASP A -2 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ GLY A -1 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ ALA A 0 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ PRO A 1 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4NTJ ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4NTJ LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 4NTJ ASN A 294 UNP Q9H244 ASP 294 ENGINEERED MUTATION SEQADV 4NTJ GLY A 343 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ ARG A 344 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ PRO A 345 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ LEU A 346 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ GLU A 347 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ VAL A 348 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ LEU A 349 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ PHE A 350 UNP Q9H244 EXPRESSION TAG SEQADV 4NTJ GLN A 351 UNP Q9H244 EXPRESSION TAG SEQRES 1 A 466 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO GLN ALA VAL SEQRES 2 A 466 ASP ASN LEU THR SER ALA PRO GLY ASN THR SER LEU CYS SEQRES 3 A 466 THR ARG ASP TYR LYS ILE THR GLN VAL LEU PHE PRO LEU SEQRES 4 A 466 LEU TYR THR VAL LEU PHE PHE VAL GLY LEU ILE THR ASN SEQRES 5 A 466 GLY LEU ALA MET ARG ILE PHE PHE GLN ILE ARG SER LYS SEQRES 6 A 466 SER ASN PHE ILE ILE PHE LEU LYS ASN THR VAL ILE SER SEQRES 7 A 466 ASP LEU LEU MET ILE LEU THR PHE PRO PHE LYS ILE LEU SEQRES 8 A 466 SER ASP ALA LYS LEU GLY THR GLY PRO LEU ARG THR PHE SEQRES 9 A 466 VAL CYS GLN VAL THR SER VAL ILE PHE TYR PHE THR MET SEQRES 10 A 466 TYR ILE SER ILE SER PHE LEU GLY LEU ILE THR ILE ASP SEQRES 11 A 466 ARG TYR GLN LYS THR THR ARG PRO PHE LYS THR SER ASN SEQRES 12 A 466 PRO LYS ASN LEU LEU GLY ALA LYS ILE LEU SER VAL VAL SEQRES 13 A 466 ILE TRP ALA PHE MET PHE LEU LEU SER LEU PRO ASN MET SEQRES 14 A 466 ILE LEU THR ASN ARG GLN PRO ARG ASP LYS ASN VAL LYS SEQRES 15 A 466 LYS CYS SER PHE LEU LYS SER GLU PHE GLY LEU VAL TRP SEQRES 16 A 466 HIS GLU ILE VAL ASN TYR ILE CYS GLN VAL ILE PHE TRP SEQRES 17 A 466 ILE ASN PHE LEU ILE VAL ILE VAL CYS TYR THR LEU ILE SEQRES 18 A 466 THR LYS GLU LEU TYR ARG SER TYR VAL ARG THR ALA ASP SEQRES 19 A 466 LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS SEQRES 20 A 466 VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP SEQRES 21 A 466 ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN SEQRES 22 A 466 LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SEQRES 23 A 466 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 24 A 466 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 25 A 466 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 26 A 466 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 27 A 466 ARG GLY VAL GLY LYS VAL PRO ARG LYS LYS VAL ASN VAL SEQRES 28 A 466 LYS VAL PHE ILE ILE ILE ALA VAL PHE PHE ILE CYS PHE SEQRES 29 A 466 VAL PRO PHE HIS PHE ALA ARG ILE PRO TYR THR LEU SER SEQRES 30 A 466 GLN THR ARG ASP VAL PHE ASP CYS THR ALA GLU ASN THR SEQRES 31 A 466 LEU PHE TYR VAL LYS GLU SER THR LEU TRP LEU THR SER SEQRES 32 A 466 LEU ASN ALA CYS LEU ASN PRO PHE ILE TYR PHE PHE LEU SEQRES 33 A 466 CYS LYS SER PHE ARG ASN SER LEU ILE SER MET LEU LYS SEQRES 34 A 466 CYS PRO ASN SER ALA THR SER LEU SER GLN ASP ASN ARG SEQRES 35 A 466 LYS LYS GLU GLN ASP GLY GLY ASP PRO ASN GLU GLU THR SEQRES 36 A 466 PRO MET GLY ARG PRO LEU GLU VAL LEU PHE GLN HET AZJ A1201 33 HET CLR A1202 28 HET CLR A1203 28 HET OLC A1204 17 HET OLC A1205 21 HETNAM AZJ ETHYL 6-{4-[(BENZYLSULFONYL)CARBAMOYL]PIPERIDIN-1-YL}- HETNAM 2 AZJ 5-CYANO-2-METHYLPYRIDINE-3-CARBOXYLATE HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 AZJ C23 H26 N4 O5 S FORMUL 3 CLR 2(C27 H46 O) FORMUL 5 OLC 2(C21 H40 O4) FORMUL 7 HOH *12(H2 O) HELIX 1 1 ASP A 20 GLN A 25 1 6 HELIX 2 2 VAL A 26 PHE A 51 1 26 HELIX 3 3 SER A 57 LEU A 75 1 19 HELIX 4 4 THR A 76 ALA A 85 1 10 HELIX 5 5 ARG A 93 ARG A 128 1 36 HELIX 6 6 ASN A 137 ILE A 161 1 25 HELIX 7 7 SER A 180 ALA A 1020 1 64 HELIX 8 8 ASN A 1022 THR A 1044 1 23 HELIX 9 9 PHE A 1061 GLY A 1082 1 22 HELIX 10 10 LYS A 1083 GLN A 1093 1 11 HELIX 11 11 THR A 1096 GLY A 227 1 15 HELIX 12 12 VAL A 234 PHE A 239 1 6 HELIX 13 13 PHE A 239 PHE A 249 1 11 HELIX 14 14 PHE A 249 ILE A 257 1 9 HELIX 15 15 PRO A 258 LEU A 261 5 4 HELIX 16 16 ASP A 269 LEU A 289 1 21 HELIX 17 17 LEU A 289 CYS A 302 1 14 HELIX 18 18 CYS A 302 MET A 312 1 11 SSBOND 1 CYS A 17 CYS A 270 1555 1555 2.04 SITE 1 AC1 14 VAL A 102 TYR A 105 PHE A 106 TYR A 109 SITE 2 AC1 14 SER A 156 ASN A 159 VAL A 190 ASN A 191 SITE 3 AC1 14 CYS A 194 PHE A 252 ARG A 256 TYR A 259 SITE 4 AC1 14 LYS A 280 HOH A1311 SITE 1 AC2 3 LEU A 27 SER A 282 TRP A 285 SITE 1 AC3 7 GLN A 124 LEU A 203 ILE A 206 VAL A 207 SITE 2 AC3 7 THR A 210 LEU A 211 LYS A 214 SITE 1 AC4 2 PRO A 251 ALA A 255 SITE 1 AC5 4 ASN A 58 LEU A 117 ILE A 120 HOH A1312 CRYST1 98.650 156.430 47.770 90.00 111.08 90.00 C 1 2 1 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 0.010137 0.000000 0.003907 0.00000 SCALE2 0.000000 0.006393 0.000000 0.00000 SCALE3 0.000000 0.000000 0.022435 0.00000 ATOM 1 N LEU A 16 9.178 119.559 44.304 1.00136.21 N ANISOU 1 N LEU A 16 18727 11743 21285 1873 -511 1501 N ATOM 2 CA LEU A 16 9.853 120.517 43.427 1.00138.54 C ANISOU 2 CA LEU A 16 19153 11729 21756 1765 -412 1735 C ATOM 3 C LEU A 16 9.921 119.978 41.984 1.00140.43 C ANISOU 3 C LEU A 16 19491 12135 21732 1743 -406 2093 C ATOM 4 O LEU A 16 9.632 120.716 41.035 1.00142.40 O ANISOU 4 O LEU A 16 19896 12175 22036 1824 -378 2404 O ATOM 5 CB LEU A 16 11.263 120.896 43.967 1.00139.30 C ANISOU 5 CB LEU A 16 19218 11651 22058 1516 -305 1523 C ATOM 6 CG LEU A 16 12.374 119.821 44.047 1.00141.47 C ANISOU 6 CG LEU A 16 19399 12213 22140 1308 -282 1397 C ATOM 7 CD1 LEU A 16 13.746 120.456 43.915 1.00143.50 C ANISOU 7 CD1 LEU A 16 19642 12217 22663 1060 -144 1387 C ATOM 8 CD2 LEU A 16 12.288 118.993 45.333 1.00141.39 C ANISOU 8 CD2 LEU A 16 19273 12440 22008 1343 -387 1021 C ATOM 9 N CYS A 17 10.277 118.684 41.839 1.00132.59 N ANISOU 9 N CYS A 17 18429 11511 20436 1654 -436 2043 N ATOM 10 CA CYS A 17 10.381 117.966 40.571 1.00131.08 C ANISOU 10 CA CYS A 17 18334 11528 19940 1639 -445 2315 C ATOM 11 C CYS A 17 9.064 117.236 40.327 1.00127.68 C ANISOU 11 C CYS A 17 17858 11358 19298 1845 -647 2357 C ATOM 12 O CYS A 17 8.594 116.516 41.211 1.00125.62 O ANISOU 12 O CYS A 17 17432 11299 19000 1875 -720 2115 O ATOM 13 CB CYS A 17 11.568 117.008 40.602 1.00130.38 C ANISOU 13 CB CYS A 17 18187 11651 19698 1414 -350 2208 C ATOM 14 SG CYS A 17 12.345 116.734 38.990 1.00136.34 S ANISOU 14 SG CYS A 17 19132 12449 20222 1322 -206 2567 S ATOM 15 N THR A 18 8.446 117.455 39.153 1.00120.76 N ANISOU 15 N THR A 18 17126 10455 18302 1999 -740 2662 N ATOM 16 CA THR A 18 7.132 116.890 38.833 1.00117.58 C ANISOU 16 CA THR A 18 16661 10252 17763 2211 -974 2709 C ATOM 17 C THR A 18 7.215 115.737 37.818 1.00115.96 C ANISOU 17 C THR A 18 16528 10352 17180 2192 -1075 2832 C ATOM 18 O THR A 18 7.988 115.790 36.859 1.00116.15 O ANISOU 18 O THR A 18 16761 10346 17023 2126 -982 3045 O ATOM 19 CB THR A 18 6.185 118.001 38.331 1.00119.99 C ANISOU 19 CB THR A 18 17063 10297 18231 2453 -1081 2925 C ATOM 20 OG1 THR A 18 6.491 119.229 38.998 1.00115.74 O ANISOU 20 OG1 THR A 18 16545 9402 18030 2428 -929 2866 O ATOM 21 CG2 THR A 18 4.716 117.663 38.554 1.00116.72 C ANISOU 21 CG2 THR A 18 16466 10016 17868 2679 -1314 2853 C ATOM 22 N ARG A 19 6.385 114.701 38.045 1.00107.97 N ANISOU 22 N ARG A 19 15344 9615 16065 2258 -1251 2692 N ATOM 23 CA ARG A 19 6.256 113.515 37.193 1.00105.74 C ANISOU 23 CA ARG A 19 15099 9624 15455 2261 -1397 2750 C ATOM 24 C ARG A 19 4.798 113.289 36.818 1.00109.28 C ANISOU 24 C ARG A 19 15449 10158 15913 2490 -1695 2788 C ATOM 25 O ARG A 19 3.904 113.736 37.541 1.00108.95 O ANISOU 25 O ARG A 19 15225 10020 16151 2610 -1748 2694 O ATOM 26 CB ARG A 19 6.825 112.271 37.885 1.00101.27 C ANISOU 26 CB ARG A 19 14386 9310 14782 2075 -1319 2505 C ATOM 27 CG ARG A 19 8.334 112.307 38.026 1.00107.60 C ANISOU 27 CG ARG A 19 15276 10069 15538 1855 -1073 2477 C ATOM 28 CD ARG A 19 8.875 111.192 38.889 1.00107.95 C ANISOU 28 CD ARG A 19 15164 10329 15525 1700 -1009 2217 C ATOM 29 NE ARG A 19 8.443 111.293 40.286 1.00109.87 N ANISOU 29 NE ARG A 19 15219 10540 15988 1721 -994 1978 N ATOM 30 CZ ARG A 19 9.142 111.883 41.252 1.00119.62 C ANISOU 30 CZ ARG A 19 16422 11625 17404 1632 -853 1822 C ATOM 31 NH1 ARG A 19 10.313 112.451 40.983 1.00103.32 N ANISOU 31 NH1 ARG A 19 14457 9410 15390 1492 -714 1875 N ATOM 32 NH2 ARG A 19 8.675 111.910 42.493 1.00103.41 N ANISOU 32 NH2 ARG A 19 14240 9563 15489 1688 -846 1603 N ATOM 33 N ASP A 20 4.561 112.588 35.691 1.00106.18 N ANISOU 33 N ASP A 20 15173 9944 15226 2560 -1894 2911 N ATOM 34 CA ASP A 20 3.230 112.282 35.156 1.00107.36 C ANISOU 34 CA ASP A 20 15231 10189 15371 2777 -2239 2940 C ATOM 35 C ASP A 20 2.417 111.461 36.165 1.00109.16 C ANISOU 35 C ASP A 20 15091 10564 15820 2753 -2303 2668 C ATOM 36 O ASP A 20 2.914 110.448 36.673 1.00105.01 O ANISOU 36 O ASP A 20 14471 10220 15210 2574 -2195 2493 O ATOM 37 CB ASP A 20 3.371 111.538 33.811 1.00110.01 C ANISOU 37 CB ASP A 20 15791 10709 15299 2821 -2429 3068 C ATOM 38 CG ASP A 20 2.083 111.177 33.092 1.00121.59 C ANISOU 38 CG ASP A 20 17187 12283 16730 3049 -2849 3082 C ATOM 39 OD1 ASP A 20 1.067 111.876 33.298 1.00123.97 O ANISOU 39 OD1 ASP A 20 17336 12451 17317 3233 -3009 3103 O ATOM 40 OD2 ASP A 20 2.103 110.218 32.289 1.00128.34 O ANISOU 40 OD2 ASP A 20 18139 13343 17279 3054 -3032 3063 O ATOM 41 N TYR A 21 1.182 111.927 36.475 1.00108.19 N ANISOU 41 N TYR A 21 14762 10346 15999 2943 -2454 2645 N ATOM 42 CA TYR A 21 0.276 111.271 37.428 1.00107.68 C ANISOU 42 CA TYR A 21 14330 10380 16204 2950 -2476 2418 C ATOM 43 C TYR A 21 -0.236 109.927 36.884 1.00111.96 C ANISOU 43 C TYR A 21 14738 11171 16631 2935 -2725 2338 C ATOM 44 O TYR A 21 -0.545 109.031 37.670 1.00109.81 O ANISOU 44 O TYR A 21 14203 11018 16500 2844 -2655 2143 O ATOM 45 CB TYR A 21 -0.905 112.189 37.811 1.00111.99 C ANISOU 45 CB TYR A 21 14685 10736 17129 3175 -2556 2431 C ATOM 46 CG TYR A 21 -2.039 112.230 36.806 1.00118.05 C ANISOU 46 CG TYR A 21 15377 11518 17957 3411 -2950 2544 C ATOM 47 CD1 TYR A 21 -3.155 111.408 36.949 1.00120.62 C ANISOU 47 CD1 TYR A 21 15345 11974 18513 3474 -3141 2397 C ATOM 48 CD2 TYR A 21 -2.005 113.102 35.720 1.00122.16 C ANISOU 48 CD2 TYR A 21 16181 11907 18326 3582 -3138 2798 C ATOM 49 CE1 TYR A 21 -4.195 111.431 36.021 1.00125.20 C ANISOU 49 CE1 TYR A 21 15826 12564 19180 3697 -3554 2471 C ATOM 50 CE2 TYR A 21 -3.043 113.141 34.789 1.00126.72 C ANISOU 50 CE2 TYR A 21 16709 12503 18938 3830 -3549 2893 C ATOM 51 CZ TYR A 21 -4.138 112.304 34.945 1.00135.52 C ANISOU 51 CZ TYR A 21 17438 13758 20297 3887 -3778 2713 C ATOM 52 OH TYR A 21 -5.166 112.337 34.034 1.00140.84 O ANISOU 52 OH TYR A 21 18030 14444 21036 4137 -4229 2777 O ATOM 53 N LYS A 22 -0.328 109.799 35.544 1.00111.00 N ANISOU 53 N LYS A 22 14812 11111 16250 3035 -3010 2487 N ATOM 54 CA LYS A 22 -0.780 108.595 34.840 1.00111.33 C ANISOU 54 CA LYS A 22 14776 11368 16155 3040 -3305 2405 C ATOM 55 C LYS A 22 0.138 107.398 35.121 1.00112.24 C ANISOU 55 C LYS A 22 14915 11670 16063 2791 -3124 2260 C ATOM 56 O LYS A 22 -0.311 106.258 35.017 1.00111.72 O ANISOU 56 O LYS A 22 14674 11761 16013 2747 -3288 2112 O ATOM 57 CB LYS A 22 -0.865 108.853 33.324 1.00116.96 C ANISOU 57 CB LYS A 22 15795 12092 16552 3224 -3632 2605 C ATOM 58 CG LYS A 22 -1.994 109.801 32.932 1.00134.84 C ANISOU 58 CG LYS A 22 18000 14201 19033 3513 -3918 2731 C ATOM 59 CD LYS A 22 -1.887 110.253 31.481 1.00147.56 C ANISOU 59 CD LYS A 22 20003 15800 20265 3721 -4208 2967 C ATOM 60 CE LYS A 22 -2.841 111.379 31.148 1.00159.65 C ANISOU 60 CE LYS A 22 21528 17137 21995 4025 -4456 3131 C ATOM 61 NZ LYS A 22 -4.259 110.926 31.089 1.00169.51 N ANISOU 61 NZ LYS A 22 22387 18452 23566 4186 -4870 2969 N ATOM 62 N ILE A 23 1.408 107.657 35.490 1.00106.82 N ANISOU 62 N ILE A 23 14422 10948 15216 2632 -2795 2293 N ATOM 63 CA ILE A 23 2.392 106.611 35.803 1.00103.79 C ANISOU 63 CA ILE A 23 14067 10723 14645 2410 -2606 2164 C ATOM 64 C ILE A 23 2.527 106.464 37.332 1.00104.71 C ANISOU 64 C ILE A 23 13960 10814 15011 2284 -2325 1989 C ATOM 65 O ILE A 23 2.489 105.348 37.855 1.00101.79 O ANISOU 65 O ILE A 23 13430 10581 14664 2175 -2278 1825 O ATOM 66 CB ILE A 23 3.767 106.898 35.121 1.00106.66 C ANISOU 66 CB ILE A 23 14785 11081 14660 2326 -2446 2310 C ATOM 67 CG1 ILE A 23 3.607 107.133 33.593 1.00110.25 C ANISOU 67 CG1 ILE A 23 15525 11548 14819 2493 -2697 2513 C ATOM 68 CG2 ILE A 23 4.769 105.769 35.406 1.00104.68 C ANISOU 68 CG2 ILE A 23 14540 11000 14234 2118 -2276 2166 C ATOM 69 CD1 ILE A 23 4.759 107.912 32.915 1.00120.32 C ANISOU 69 CD1 ILE A 23 17163 12717 15835 2473 -2485 2744 C ATOM 70 N THR A 24 2.663 107.606 38.027 1.00102.09 N ANISOU 70 N THR A 24 13641 10292 14856 2317 -2146 2026 N ATOM 71 CA THR A 24 2.847 107.751 39.471 1.00100.02 C ANISOU 71 CA THR A 24 13241 9971 14790 2242 -1883 1869 C ATOM 72 C THR A 24 1.634 107.262 40.282 1.00103.07 C ANISOU 72 C THR A 24 13309 10391 15462 2315 -1900 1730 C ATOM 73 O THR A 24 1.800 106.439 41.178 1.00101.04 O ANISOU 73 O THR A 24 12941 10223 15224 2213 -1730 1576 O ATOM 74 CB THR A 24 3.144 109.237 39.796 1.00109.67 C ANISOU 74 CB THR A 24 14582 10947 16142 2297 -1748 1947 C ATOM 75 OG1 THR A 24 4.261 109.669 39.023 1.00109.92 O ANISOU 75 OG1 THR A 24 14888 10921 15955 2227 -1712 2105 O ATOM 76 CG2 THR A 24 3.421 109.484 41.270 1.00108.66 C ANISOU 76 CG2 THR A 24 14379 10751 16156 2225 -1492 1763 C ATOM 77 N GLN A 25 0.442 107.794 39.993 1.00101.50 N ANISOU 77 N GLN A 25 12964 10106 15496 2500 -2084 1792 N ATOM 78 CA GLN A 25 -0.773 107.529 40.760 1.00101.67 C ANISOU 78 CA GLN A 25 12650 10118 15863 2588 -2063 1678 C ATOM 79 C GLN A 25 -1.756 106.553 40.094 1.00105.18 C ANISOU 79 C GLN A 25 12863 10689 16412 2621 -2336 1648 C ATOM 80 O GLN A 25 -2.764 106.208 40.720 1.00105.03 O ANISOU 80 O GLN A 25 12523 10663 16721 2667 -2290 1549 O ATOM 81 CB GLN A 25 -1.490 108.862 41.039 1.00105.51 C ANISOU 81 CB GLN A 25 13071 10387 16630 2788 -2055 1737 C ATOM 82 CG GLN A 25 -0.619 109.867 41.791 1.00117.45 C ANISOU 82 CG GLN A 25 14774 11739 18113 2758 -1787 1719 C ATOM 83 CD GLN A 25 -1.299 111.188 42.004 1.00132.43 C ANISOU 83 CD GLN A 25 16631 13398 20287 2962 -1782 1772 C ATOM 84 OE1 GLN A 25 -1.825 111.802 41.073 1.00132.43 O ANISOU 84 OE1 GLN A 25 16663 13304 20351 3113 -2018 1934 O ATOM 85 NE2 GLN A 25 -1.255 111.677 43.231 1.00120.17 N ANISOU 85 NE2 GLN A 25 15043 11734 18883 2984 -1517 1636 N ATOM 86 N VAL A 26 -1.477 106.099 38.854 1.00101.65 N ANISOU 86 N VAL A 26 12571 10346 15707 2602 -2609 1721 N ATOM 87 CA VAL A 26 -2.383 105.185 38.153 1.00102.85 C ANISOU 87 CA VAL A 26 12517 10604 15958 2639 -2927 1662 C ATOM 88 C VAL A 26 -1.673 103.865 37.820 1.00105.15 C ANISOU 88 C VAL A 26 12906 11074 15970 2454 -2941 1577 C ATOM 89 O VAL A 26 -2.058 102.834 38.375 1.00104.74 O ANISOU 89 O VAL A 26 12612 11089 16097 2355 -2876 1432 O ATOM 90 CB VAL A 26 -3.034 105.820 36.888 1.00110.07 C ANISOU 90 CB VAL A 26 13496 11470 16854 2853 -3340 1795 C ATOM 91 CG1 VAL A 26 -3.993 104.843 36.202 1.00111.80 C ANISOU 91 CG1 VAL A 26 13472 11793 17213 2895 -3716 1686 C ATOM 92 CG2 VAL A 26 -3.751 107.129 37.224 1.00112.01 C ANISOU 92 CG2 VAL A 26 13643 11518 17396 3054 -3326 1884 C ATOM 93 N LEU A 27 -0.653 103.891 36.932 1.00100.67 N ANISOU 93 N LEU A 27 12693 10569 14987 2414 -2997 1671 N ATOM 94 CA LEU A 27 0.065 102.698 36.470 1.00 98.78 C ANISOU 94 CA LEU A 27 12583 10493 14457 2268 -3025 1596 C ATOM 95 C LEU A 27 0.675 101.865 37.612 1.00100.19 C ANISOU 95 C LEU A 27 12673 10728 14666 2074 -2696 1462 C ATOM 96 O LEU A 27 0.339 100.688 37.699 1.00100.01 O ANISOU 96 O LEU A 27 12485 10790 14724 1992 -2752 1330 O ATOM 97 CB LEU A 27 1.145 103.057 35.437 1.00 98.73 C ANISOU 97 CB LEU A 27 12986 10520 14009 2277 -3053 1743 C ATOM 98 CG LEU A 27 1.857 101.895 34.726 1.00102.05 C ANISOU 98 CG LEU A 27 13575 11105 14093 2170 -3109 1673 C ATOM 99 CD1 LEU A 27 0.904 101.114 33.822 1.00104.55 C ANISOU 99 CD1 LEU A 27 13818 11504 14402 2263 -3527 1588 C ATOM 100 CD2 LEU A 27 3.011 102.406 33.906 1.00104.12 C ANISOU 100 CD2 LEU A 27 14229 11373 13960 2170 -3001 1836 C ATOM 101 N PHE A 28 1.547 102.450 38.472 1.00 94.68 N ANISOU 101 N PHE A 28 12088 9973 13912 2008 -2377 1487 N ATOM 102 CA PHE A 28 2.191 101.719 39.576 1.00 91.50 C ANISOU 102 CA PHE A 28 11643 9626 13498 1856 -2088 1365 C ATOM 103 C PHE A 28 1.168 101.203 40.634 1.00 94.44 C ANISOU 103 C PHE A 28 11696 9975 14214 1862 -1980 1251 C ATOM 104 O PHE A 28 1.252 100.010 40.933 1.00 92.29 O ANISOU 104 O PHE A 28 11348 9788 13930 1754 -1915 1154 O ATOM 105 CB PHE A 28 3.321 102.527 40.222 1.00 91.90 C ANISOU 105 CB PHE A 28 11877 9608 13434 1808 -1829 1395 C ATOM 106 CG PHE A 28 4.622 102.393 39.462 1.00 92.49 C ANISOU 106 CG PHE A 28 12217 9750 13175 1713 -1812 1451 C ATOM 107 CD1 PHE A 28 5.480 101.326 39.703 1.00 93.15 C ANISOU 107 CD1 PHE A 28 12341 9956 13095 1577 -1699 1352 C ATOM 108 CD2 PHE A 28 4.976 103.321 38.487 1.00 96.20 C ANISOU 108 CD2 PHE A 28 12898 10150 13504 1772 -1889 1615 C ATOM 109 CE1 PHE A 28 6.675 101.195 38.990 1.00 93.56 C ANISOU 109 CE1 PHE A 28 12611 10067 12870 1499 -1659 1399 C ATOM 110 CE2 PHE A 28 6.172 103.188 37.773 1.00 98.40 C ANISOU 110 CE2 PHE A 28 13411 10482 13494 1687 -1821 1678 C ATOM 111 CZ PHE A 28 7.016 102.128 38.034 1.00 94.29 C ANISOU 111 CZ PHE A 28 12899 10092 12836 1550 -1704 1562 C ATOM 112 N PRO A 29 0.152 101.973 41.138 1.00 92.13 N ANISOU 112 N PRO A 29 11204 9562 14241 1991 -1954 1266 N ATOM 113 CA PRO A 29 -0.836 101.362 42.054 1.00 92.16 C ANISOU 113 CA PRO A 29 10893 9545 14580 1994 -1813 1170 C ATOM 114 C PRO A 29 -1.608 100.193 41.406 1.00 96.81 C ANISOU 114 C PRO A 29 11260 10199 15324 1947 -2040 1107 C ATOM 115 O PRO A 29 -1.908 99.225 42.099 1.00 96.13 O ANISOU 115 O PRO A 29 11001 10130 15393 1859 -1871 1023 O ATOM 116 CB PRO A 29 -1.767 102.526 42.398 1.00 95.69 C ANISOU 116 CB PRO A 29 11183 9844 15330 2169 -1788 1212 C ATOM 117 CG PRO A 29 -0.946 103.728 42.177 1.00 99.56 C ANISOU 117 CG PRO A 29 11957 10264 15607 2220 -1791 1306 C ATOM 118 CD PRO A 29 -0.140 103.408 40.960 1.00 94.62 C ANISOU 118 CD PRO A 29 11565 9737 14648 2145 -2012 1373 C ATOM 119 N LEU A 30 -1.881 100.247 40.085 1.00 94.37 N ANISOU 119 N LEU A 30 10977 9918 14959 2008 -2423 1144 N ATOM 120 CA LEU A 30 -2.552 99.152 39.373 1.00 95.56 C ANISOU 120 CA LEU A 30 10939 10125 15244 1967 -2704 1050 C ATOM 121 C LEU A 30 -1.598 97.965 39.168 1.00 96.84 C ANISOU 121 C LEU A 30 11283 10404 15106 1799 -2669 979 C ATOM 122 O LEU A 30 -2.025 96.809 39.228 1.00 96.87 O ANISOU 122 O LEU A 30 11096 10425 15285 1705 -2717 864 O ATOM 123 CB LEU A 30 -3.109 99.624 38.020 1.00 98.58 C ANISOU 123 CB LEU A 30 11340 10506 15609 2118 -3163 1095 C ATOM 124 CG LEU A 30 -4.449 100.360 38.052 1.00106.67 C ANISOU 124 CG LEU A 30 12037 11415 17078 2288 -3317 1107 C ATOM 125 CD1 LEU A 30 -4.718 101.051 36.731 1.00109.22 C ANISOU 125 CD1 LEU A 30 12504 11732 17264 2479 -3748 1199 C ATOM 126 CD2 LEU A 30 -5.597 99.413 38.382 1.00112.03 C ANISOU 126 CD2 LEU A 30 12266 12067 18232 2232 -3388 956 C ATOM 127 N LEU A 31 -0.306 98.262 38.928 1.00 91.14 N ANISOU 127 N LEU A 31 10917 9746 13968 1762 -2573 1047 N ATOM 128 CA LEU A 31 0.770 97.288 38.741 1.00 89.06 C ANISOU 128 CA LEU A 31 10854 9590 13395 1625 -2506 992 C ATOM 129 C LEU A 31 0.972 96.463 40.012 1.00 89.69 C ANISOU 129 C LEU A 31 10821 9664 13592 1505 -2177 914 C ATOM 130 O LEU A 31 1.245 95.270 39.928 1.00 89.05 O ANISOU 130 O LEU A 31 10752 9639 13442 1397 -2171 829 O ATOM 131 CB LEU A 31 2.071 98.018 38.359 1.00 88.12 C ANISOU 131 CB LEU A 31 11091 9510 12880 1629 -2430 1098 C ATOM 132 CG LEU A 31 2.678 97.726 36.981 1.00 94.06 C ANISOU 132 CG LEU A 31 12103 10361 13275 1632 -2650 1118 C ATOM 133 CD1 LEU A 31 1.724 98.066 35.859 1.00 97.28 C ANISOU 133 CD1 LEU A 31 12509 10754 13698 1785 -3033 1160 C ATOM 134 CD2 LEU A 31 3.965 98.503 36.787 1.00 96.02 C ANISOU 134 CD2 LEU A 31 12656 10623 13205 1614 -2469 1233 C ATOM 135 N TYR A 32 0.804 97.097 41.185 1.00 84.41 N ANISOU 135 N TYR A 32 10062 8916 13092 1544 -1905 944 N ATOM 136 CA TYR A 32 0.911 96.443 42.485 1.00 82.30 C ANISOU 136 CA TYR A 32 9722 8634 12915 1475 -1575 892 C ATOM 137 C TYR A 32 -0.395 95.739 42.855 1.00 89.21 C ANISOU 137 C TYR A 32 10249 9436 14210 1466 -1540 841 C ATOM 138 O TYR A 32 -0.361 94.786 43.634 1.00 88.93 O ANISOU 138 O TYR A 32 10157 9391 14242 1385 -1313 801 O ATOM 139 CB TYR A 32 1.302 97.450 43.570 1.00 81.64 C ANISOU 139 CB TYR A 32 9737 8497 12787 1543 -1302 929 C ATOM 140 CG TYR A 32 2.794 97.611 43.762 1.00 79.83 C ANISOU 140 CG TYR A 32 9803 8331 12198 1488 -1201 927 C ATOM 141 CD1 TYR A 32 3.466 98.718 43.255 1.00 81.27 C ANISOU 141 CD1 TYR A 32 10169 8495 12215 1523 -1276 988 C ATOM 142 CD2 TYR A 32 3.530 96.675 44.483 1.00 78.67 C ANISOU 142 CD2 TYR A 32 9740 8242 11909 1407 -1024 867 C ATOM 143 CE1 TYR A 32 4.834 98.893 43.461 1.00 80.07 C ANISOU 143 CE1 TYR A 32 10239 8382 11803 1462 -1175 974 C ATOM 144 CE2 TYR A 32 4.899 96.837 44.693 1.00 77.73 C ANISOU 144 CE2 TYR A 32 9853 8177 11504 1367 -952 848 C ATOM 145 CZ TYR A 32 5.546 97.949 44.181 1.00 85.82 C ANISOU 145 CZ TYR A 32 11020 9182 12407 1386 -1028 893 C ATOM 146 OH TYR A 32 6.894 98.119 44.381 1.00 87.30 O ANISOU 146 OH TYR A 32 11389 9405 12378 1335 -957 862 O ATOM 147 N THR A 33 -1.541 96.206 42.307 1.00 88.79 N ANISOU 147 N THR A 33 9956 9321 14460 1553 -1760 848 N ATOM 148 CA THR A 33 -2.863 95.604 42.529 1.00 91.22 C ANISOU 148 CA THR A 33 9868 9541 15251 1542 -1760 791 C ATOM 149 C THR A 33 -2.879 94.207 41.900 1.00 96.18 C ANISOU 149 C THR A 33 10430 10200 15913 1403 -1941 690 C ATOM 150 O THR A 33 -3.353 93.269 42.541 1.00 96.83 O ANISOU 150 O THR A 33 10294 10210 16286 1313 -1747 644 O ATOM 151 CB THR A 33 -3.978 96.515 41.994 1.00 98.42 C ANISOU 151 CB THR A 33 10543 10383 16471 1688 -2008 812 C ATOM 152 OG1 THR A 33 -3.937 97.742 42.717 1.00 96.16 O ANISOU 152 OG1 THR A 33 10323 10041 16170 1814 -1787 894 O ATOM 153 CG2 THR A 33 -5.365 95.906 42.151 1.00 99.52 C ANISOU 153 CG2 THR A 33 10214 10420 17178 1673 -2031 739 C ATOM 154 N VAL A 34 -2.318 94.069 40.670 1.00 92.64 N ANISOU 154 N VAL A 34 10194 9847 15158 1392 -2283 657 N ATOM 155 CA VAL A 34 -2.193 92.796 39.943 1.00 92.68 C ANISOU 155 CA VAL A 34 10205 9886 15125 1277 -2492 536 C ATOM 156 C VAL A 34 -1.429 91.819 40.837 1.00 95.58 C ANISOU 156 C VAL A 34 10677 10257 15384 1146 -2144 524 C ATOM 157 O VAL A 34 -1.986 90.789 41.201 1.00 96.89 O ANISOU 157 O VAL A 34 10621 10336 15856 1046 -2062 453 O ATOM 158 CB VAL A 34 -1.521 92.980 38.554 1.00 95.94 C ANISOU 158 CB VAL A 34 10917 10413 15123 1327 -2859 521 C ATOM 159 CG1 VAL A 34 -1.131 91.639 37.932 1.00 95.33 C ANISOU 159 CG1 VAL A 34 10928 10378 14915 1213 -3004 383 C ATOM 160 CG2 VAL A 34 -2.415 93.779 37.608 1.00 98.69 C ANISOU 160 CG2 VAL A 34 11154 10743 15600 1477 -3259 526 C ATOM 161 N LEU A 35 -0.209 92.198 41.276 1.00 89.85 N ANISOU 161 N LEU A 35 10263 9609 14268 1155 -1927 598 N ATOM 162 CA LEU A 35 0.643 91.401 42.162 1.00 87.98 C ANISOU 162 CA LEU A 35 10163 9386 13882 1069 -1618 597 C ATOM 163 C LEU A 35 -0.043 91.030 43.478 1.00 93.52 C ANISOU 163 C LEU A 35 10651 9972 14909 1053 -1269 626 C ATOM 164 O LEU A 35 0.235 89.956 44.015 1.00 92.59 O ANISOU 164 O LEU A 35 10557 9821 14801 970 -1080 608 O ATOM 165 CB LEU A 35 1.950 92.138 42.501 1.00 85.55 C ANISOU 165 CB LEU A 35 10172 9166 13167 1109 -1472 663 C ATOM 166 CG LEU A 35 2.972 92.439 41.404 1.00 89.83 C ANISOU 166 CG LEU A 35 10983 9818 13331 1112 -1680 664 C ATOM 167 CD1 LEU A 35 4.318 92.791 42.042 1.00 87.82 C ANISOU 167 CD1 LEU A 35 10969 9620 12779 1109 -1457 703 C ATOM 168 CD2 LEU A 35 3.158 91.262 40.441 1.00 92.61 C ANISOU 168 CD2 LEU A 35 11381 10215 13594 1034 -1881 563 C ATOM 169 N PHE A 36 -0.897 91.926 44.022 1.00 91.67 N ANISOU 169 N PHE A 36 10233 9669 14927 1148 -1157 681 N ATOM 170 CA PHE A 36 -1.581 91.676 45.288 1.00 92.52 C ANISOU 170 CA PHE A 36 10154 9666 15333 1159 -775 724 C ATOM 171 C PHE A 36 -2.535 90.491 45.161 1.00 99.85 C ANISOU 171 C PHE A 36 10766 10478 16696 1046 -781 670 C ATOM 172 O PHE A 36 -2.391 89.530 45.915 1.00 99.42 O ANISOU 172 O PHE A 36 10733 10362 16681 973 -498 692 O ATOM 173 CB PHE A 36 -2.320 92.928 45.799 1.00 95.37 C ANISOU 173 CB PHE A 36 10377 9972 15886 1301 -660 780 C ATOM 174 CG PHE A 36 -3.162 92.675 47.029 1.00 98.52 C ANISOU 174 CG PHE A 36 10561 10248 16623 1331 -245 825 C ATOM 175 CD1 PHE A 36 -2.576 92.577 48.285 1.00100.16 C ANISOU 175 CD1 PHE A 36 10992 10457 16608 1377 154 881 C ATOM 176 CD2 PHE A 36 -4.539 92.511 46.927 1.00103.96 C ANISOU 176 CD2 PHE A 36 10826 10816 17858 1322 -248 810 C ATOM 177 CE1 PHE A 36 -3.351 92.311 49.415 1.00103.27 C ANISOU 177 CE1 PHE A 36 11228 10734 17275 1423 579 942 C ATOM 178 CE2 PHE A 36 -5.315 92.256 48.059 1.00108.89 C ANISOU 178 CE2 PHE A 36 11245 11314 18813 1349 195 869 C ATOM 179 CZ PHE A 36 -4.716 92.164 49.297 1.00105.83 C ANISOU 179 CZ PHE A 36 11124 10932 18155 1404 624 944 C ATOM 180 N PHE A 37 -3.485 90.549 44.209 1.00 99.60 N ANISOU 180 N PHE A 37 10443 10402 16997 1036 -1113 597 N ATOM 181 CA PHE A 37 -4.463 89.483 44.014 1.00102.79 C ANISOU 181 CA PHE A 37 10488 10670 17896 918 -1170 514 C ATOM 182 C PHE A 37 -3.813 88.201 43.484 1.00106.18 C ANISOU 182 C PHE A 37 11060 11109 18175 775 -1304 422 C ATOM 183 O PHE A 37 -4.099 87.136 44.032 1.00107.20 O ANISOU 183 O PHE A 37 11043 11104 18584 662 -1074 415 O ATOM 184 CB PHE A 37 -5.609 89.946 43.112 1.00107.90 C ANISOU 184 CB PHE A 37 10793 11277 18927 965 -1562 430 C ATOM 185 CG PHE A 37 -6.477 90.975 43.797 1.00111.35 C ANISOU 185 CG PHE A 37 10983 11646 19678 1094 -1362 512 C ATOM 186 CD1 PHE A 37 -7.439 90.591 44.725 1.00117.30 C ANISOU 186 CD1 PHE A 37 11359 12236 20973 1056 -1017 537 C ATOM 187 CD2 PHE A 37 -6.309 92.330 43.541 1.00112.68 C ANISOU 187 CD2 PHE A 37 11301 11898 19612 1259 -1483 571 C ATOM 188 CE1 PHE A 37 -8.224 91.545 45.378 1.00120.05 C ANISOU 188 CE1 PHE A 37 11482 12521 21610 1193 -797 606 C ATOM 189 CE2 PHE A 37 -7.094 93.283 44.195 1.00117.28 C ANISOU 189 CE2 PHE A 37 11666 12406 20488 1394 -1288 635 C ATOM 190 CZ PHE A 37 -8.047 92.885 45.107 1.00118.10 C ANISOU 190 CZ PHE A 37 11394 12363 21116 1366 -946 646 C ATOM 191 N VAL A 38 -2.901 88.305 42.481 1.00100.89 N ANISOU 191 N VAL A 38 10689 10582 17063 789 -1630 362 N ATOM 192 CA VAL A 38 -2.167 87.167 41.902 1.00100.19 C ANISOU 192 CA VAL A 38 10777 10515 16774 681 -1767 261 C ATOM 193 C VAL A 38 -1.388 86.440 43.022 1.00103.21 C ANISOU 193 C VAL A 38 11336 10865 17015 626 -1336 343 C ATOM 194 O VAL A 38 -1.506 85.220 43.154 1.00104.07 O ANISOU 194 O VAL A 38 11364 10855 17324 510 -1258 290 O ATOM 195 CB VAL A 38 -1.241 87.597 40.723 1.00102.45 C ANISOU 195 CB VAL A 38 11391 10973 16561 742 -2114 212 C ATOM 196 CG1 VAL A 38 -0.212 86.517 40.381 1.00100.97 C ANISOU 196 CG1 VAL A 38 11458 10826 16081 659 -2129 134 C ATOM 197 CG2 VAL A 38 -2.056 87.967 39.487 1.00104.83 C ANISOU 197 CG2 VAL A 38 11545 11285 17000 797 -2597 107 C ATOM 198 N GLY A 39 -0.650 87.208 43.824 1.00 97.91 N ANISOU 198 N GLY A 39 10896 10282 16025 720 -1078 465 N ATOM 199 CA GLY A 39 0.141 86.711 44.943 1.00 96.45 C ANISOU 199 CA GLY A 39 10916 10086 15645 719 -702 548 C ATOM 200 C GLY A 39 -0.687 86.097 46.051 1.00103.95 C ANISOU 200 C GLY A 39 11658 10861 16977 687 -322 626 C ATOM 201 O GLY A 39 -0.321 85.043 46.579 1.00103.98 O ANISOU 201 O GLY A 39 11756 10788 16964 630 -110 656 O ATOM 202 N LEU A 40 -1.808 86.748 46.411 1.00103.12 N ANISOU 202 N LEU A 40 11271 10679 17229 733 -214 669 N ATOM 203 CA LEU A 40 -2.700 86.273 47.467 1.00105.77 C ANISOU 203 CA LEU A 40 11382 10838 17970 715 204 762 C ATOM 204 C LEU A 40 -3.364 84.940 47.097 1.00112.38 C ANISOU 204 C LEU A 40 11940 11491 19268 543 169 697 C ATOM 205 O LEU A 40 -3.528 84.099 47.977 1.00113.08 O ANISOU 205 O LEU A 40 11998 11427 19540 497 561 794 O ATOM 206 CB LEU A 40 -3.775 87.329 47.788 1.00107.99 C ANISOU 206 CB LEU A 40 11393 11082 18556 815 305 804 C ATOM 207 CG LEU A 40 -4.582 87.148 49.082 1.00115.60 C ANISOU 207 CG LEU A 40 12186 11887 19851 852 843 932 C ATOM 208 CD1 LEU A 40 -3.757 87.529 50.313 1.00114.25 C ANISOU 208 CD1 LEU A 40 12405 11786 19218 999 1220 1051 C ATOM 209 CD2 LEU A 40 -5.859 87.971 49.042 1.00121.12 C ANISOU 209 CD2 LEU A 40 12486 12515 21017 913 850 924 C ATOM 210 N ILE A 41 -3.735 84.741 45.814 1.00110.55 N ANISOU 210 N ILE A 41 11525 11260 19220 456 -296 533 N ATOM 211 CA ILE A 41 -4.415 83.508 45.397 1.00113.66 C ANISOU 211 CA ILE A 41 11627 11457 20099 285 -385 428 C ATOM 212 C ILE A 41 -3.411 82.348 45.200 1.00116.30 C ANISOU 212 C ILE A 41 12245 11777 20165 197 -410 382 C ATOM 213 O ILE A 41 -3.745 81.223 45.569 1.00117.81 O ANISOU 213 O ILE A 41 12302 11759 20701 74 -200 394 O ATOM 214 CB ILE A 41 -5.382 83.670 44.174 1.00119.55 C ANISOU 214 CB ILE A 41 12016 12174 21235 237 -889 239 C ATOM 215 CG1 ILE A 41 -4.661 84.052 42.857 1.00118.29 C ANISOU 215 CG1 ILE A 41 12117 12215 20611 295 -1422 104 C ATOM 216 CG2 ILE A 41 -6.531 84.643 44.493 1.00122.29 C ANISOU 216 CG2 ILE A 41 11996 12476 21991 318 -807 291 C ATOM 217 CD1 ILE A 41 -5.236 83.396 41.587 1.00127.73 C ANISOU 217 CD1 ILE A 41 13090 13348 22092 211 -1951 -133 C ATOM 218 N THR A 42 -2.199 82.608 44.656 1.00110.03 N ANISOU 218 N THR A 42 11830 11183 18791 263 -630 341 N ATOM 219 CA THR A 42 -1.207 81.544 44.429 1.00108.71 C ANISOU 219 CA THR A 42 11931 11012 18363 203 -661 287 C ATOM 220 C THR A 42 -0.583 81.078 45.748 1.00111.50 C ANISOU 220 C THR A 42 12500 11309 18555 240 -180 464 C ATOM 221 O THR A 42 -0.467 79.870 45.951 1.00112.29 O ANISOU 221 O THR A 42 12616 11244 18803 150 -46 464 O ATOM 222 CB THR A 42 -0.118 81.947 43.423 1.00115.01 C ANISOU 222 CB THR A 42 13042 12034 18625 269 -1012 190 C ATOM 223 OG1 THR A 42 0.545 83.133 43.868 1.00114.31 O ANISOU 223 OG1 THR A 42 13159 12122 18151 408 -900 310 O ATOM 224 CG2 THR A 42 -0.650 82.108 42.002 1.00113.94 C ANISOU 224 CG2 THR A 42 12768 11933 18592 242 -1517 0 C ATOM 225 N ASN A 43 -0.203 82.016 46.642 1.00106.16 N ANISOU 225 N ASN A 43 12002 10754 17579 383 63 608 N ATOM 226 CA ASN A 43 0.383 81.673 47.944 1.00105.30 C ANISOU 226 CA ASN A 43 12137 10610 17262 462 489 772 C ATOM 227 C ASN A 43 -0.685 81.201 48.921 1.00112.37 C ANISOU 227 C ASN A 43 12812 11276 18606 430 919 910 C ATOM 228 O ASN A 43 -0.368 80.468 49.864 1.00112.34 O ANISOU 228 O ASN A 43 12988 11169 18526 463 1271 1045 O ATOM 229 CB ASN A 43 1.168 82.832 48.540 1.00103.62 C ANISOU 229 CB ASN A 43 12192 10594 16584 634 565 842 C ATOM 230 CG ASN A 43 2.463 83.078 47.820 1.00115.53 C ANISOU 230 CG ASN A 43 13965 12296 17636 664 260 747 C ATOM 231 OD1 ASN A 43 3.473 82.403 48.050 1.00102.58 O ANISOU 231 OD1 ASN A 43 12573 10683 15720 688 306 754 O ATOM 232 ND2 ASN A 43 2.444 84.032 46.907 1.00105.45 N ANISOU 232 ND2 ASN A 43 12632 11145 16290 671 -50 662 N ATOM 233 N GLY A 44 -1.928 81.622 48.682 1.00111.43 N ANISOU 233 N GLY A 44 12308 11075 18956 378 895 882 N ATOM 234 CA GLY A 44 -3.083 81.238 49.482 1.00114.93 C ANISOU 234 CA GLY A 44 12459 11285 19924 332 1311 1003 C ATOM 235 C GLY A 44 -3.332 79.751 49.397 1.00121.19 C ANISOU 235 C GLY A 44 13130 11827 21090 161 1410 996 C ATOM 236 O GLY A 44 -3.420 79.084 50.430 1.00122.31 O ANISOU 236 O GLY A 44 13339 11796 21337 169 1888 1177 O ATOM 237 N LEU A 45 -3.379 79.214 48.159 1.00118.63 N ANISOU 237 N LEU A 45 12664 11474 20934 18 957 786 N ATOM 238 CA LEU A 45 -3.573 77.782 47.948 1.00121.41 C ANISOU 238 CA LEU A 45 12903 11571 21657 -157 981 733 C ATOM 239 C LEU A 45 -2.263 77.012 48.208 1.00123.13 C ANISOU 239 C LEU A 45 13569 11815 21398 -109 1067 790 C ATOM 240 O LEU A 45 -2.327 75.814 48.481 1.00124.78 O ANISOU 240 O LEU A 45 13772 11778 21861 -207 1282 842 O ATOM 241 CB LEU A 45 -4.178 77.444 46.562 1.00123.49 C ANISOU 241 CB LEU A 45 12854 11776 22291 -312 445 454 C ATOM 242 CG LEU A 45 -3.422 77.830 45.286 1.00125.79 C ANISOU 242 CG LEU A 45 13359 12318 22117 -260 -121 250 C ATOM 243 CD1 LEU A 45 -2.606 76.660 44.761 1.00125.46 C ANISOU 243 CD1 LEU A 45 13556 12218 21896 -330 -276 132 C ATOM 244 CD2 LEU A 45 -4.399 78.234 44.197 1.00130.81 C ANISOU 244 CD2 LEU A 45 13637 12962 23103 -317 -596 36 C ATOM 245 N ALA A 46 -1.094 77.697 48.158 1.00115.77 N ANISOU 245 N ALA A 46 13009 11163 19816 43 912 784 N ATOM 246 CA ALA A 46 0.212 77.085 48.437 1.00113.18 C ANISOU 246 CA ALA A 46 13093 10889 19021 120 971 831 C ATOM 247 C ALA A 46 0.317 76.699 49.912 1.00118.27 C ANISOU 247 C ALA A 46 13924 11411 19603 220 1514 1090 C ATOM 248 O ALA A 46 0.789 75.607 50.216 1.00118.56 O ANISOU 248 O ALA A 46 14137 11298 19612 208 1665 1156 O ATOM 249 CB ALA A 46 1.340 78.030 48.059 1.00109.93 C ANISOU 249 CB ALA A 46 12964 10793 18012 256 701 766 C ATOM 250 N MET A 47 -0.176 77.572 50.817 1.00115.86 N ANISOU 250 N MET A 47 13586 11150 19285 330 1813 1238 N ATOM 251 CA MET A 47 -0.202 77.344 52.265 1.00117.41 C ANISOU 251 CA MET A 47 13980 11241 19390 460 2355 1492 C ATOM 252 C MET A 47 -1.152 76.189 52.614 1.00125.03 C ANISOU 252 C MET A 47 14720 11850 20934 319 2722 1615 C ATOM 253 O MET A 47 -0.870 75.434 53.542 1.00125.70 O ANISOU 253 O MET A 47 15056 11790 20914 396 3105 1815 O ATOM 254 CB MET A 47 -0.619 78.623 53.009 1.00119.91 C ANISOU 254 CB MET A 47 14282 11684 19595 608 2559 1577 C ATOM 255 CG MET A 47 -0.134 78.670 54.440 1.00124.26 C ANISOU 255 CG MET A 47 15219 12250 19744 830 2989 1791 C ATOM 256 SD MET A 47 -0.823 80.071 55.345 1.00130.02 S ANISOU 256 SD MET A 47 15909 13072 20423 1004 3287 1876 S ATOM 257 CE MET A 47 -0.072 79.829 56.932 1.00127.66 C ANISOU 257 CE MET A 47 16152 12775 19576 1277 3732 2100 C ATOM 258 N ARG A 48 -2.265 76.059 51.862 1.00123.91 N ANISOU 258 N ARG A 48 14106 11559 21415 119 2592 1494 N ATOM 259 CA ARG A 48 -3.278 75.010 52.014 1.00128.15 C ANISOU 259 CA ARG A 48 14324 11730 22638 -63 2887 1564 C ATOM 260 C ARG A 48 -2.684 73.641 51.658 1.00132.80 C ANISOU 260 C ARG A 48 15059 12136 23264 -169 2793 1520 C ATOM 261 O ARG A 48 -2.992 72.647 52.321 1.00135.69 O ANISOU 261 O ARG A 48 15416 12193 23945 -231 3210 1696 O ATOM 262 CB ARG A 48 -4.492 75.322 51.121 1.00130.25 C ANISOU 262 CB ARG A 48 14029 11922 23540 -241 2627 1375 C ATOM 263 CG ARG A 48 -5.791 74.679 51.579 1.00146.60 C ANISOU 263 CG ARG A 48 15674 13629 26397 -398 3054 1487 C ATOM 264 CD ARG A 48 -6.959 75.134 50.727 1.00161.33 C ANISOU 264 CD ARG A 48 16966 15457 28876 -540 2746 1280 C ATOM 265 NE ARG A 48 -8.202 74.451 51.091 1.00174.65 N ANISOU 265 NE ARG A 48 18180 16770 31409 -719 3132 1359 N ATOM 266 CZ ARG A 48 -9.385 74.694 50.535 1.00192.79 C ANISOU 266 CZ ARG A 48 19896 18960 34394 -855 2953 1203 C ATOM 267 NH1 ARG A 48 -9.504 75.611 49.582 1.00175.09 N ANISOU 267 NH1 ARG A 48 17508 16962 32055 -814 2379 968 N ATOM 268 NH2 ARG A 48 -10.460 74.024 50.929 1.00187.08 N ANISOU 268 NH2 ARG A 48 18730 17874 34479 -1026 3349 1285 N ATOM 269 N ILE A 49 -1.819 73.605 50.623 1.00126.35 N ANISOU 269 N ILE A 49 14388 11497 22121 -179 2270 1294 N ATOM 270 CA ILE A 49 -1.143 72.397 50.153 1.00126.37 C ANISOU 270 CA ILE A 49 14553 11361 22102 -255 2118 1208 C ATOM 271 C ILE A 49 -0.037 72.002 51.162 1.00130.93 C ANISOU 271 C ILE A 49 15624 11964 22161 -59 2422 1430 C ATOM 272 O ILE A 49 0.003 70.841 51.580 1.00133.31 O ANISOU 272 O ILE A 49 16016 11982 22655 -100 2688 1553 O ATOM 273 CB ILE A 49 -0.606 72.577 48.698 1.00126.55 C ANISOU 273 CB ILE A 49 14572 11581 21931 -304 1479 886 C ATOM 274 CG1 ILE A 49 -1.782 72.702 47.691 1.00128.78 C ANISOU 274 CG1 ILE A 49 14371 11776 22785 -495 1153 657 C ATOM 275 CG2 ILE A 49 0.339 71.422 48.298 1.00126.73 C ANISOU 275 CG2 ILE A 49 14847 11504 21799 -324 1343 797 C ATOM 276 CD1 ILE A 49 -1.454 73.321 46.319 1.00130.64 C ANISOU 276 CD1 ILE A 49 14607 12275 22756 -485 536 372 C ATOM 277 N PHE A 50 0.828 72.965 51.567 1.00125.19 N ANISOU 277 N PHE A 50 15204 11555 20806 158 2375 1478 N ATOM 278 CA PHE A 50 1.931 72.741 52.511 1.00124.25 C ANISOU 278 CA PHE A 50 15554 11504 20153 377 2581 1656 C ATOM 279 C PHE A 50 1.462 72.342 53.918 1.00133.16 C ANISOU 279 C PHE A 50 16810 12413 21373 475 3190 1977 C ATOM 280 O PHE A 50 2.181 71.607 54.597 1.00133.25 O ANISOU 280 O PHE A 50 17172 12338 21121 610 3381 2136 O ATOM 281 CB PHE A 50 2.843 73.971 52.608 1.00122.08 C ANISOU 281 CB PHE A 50 15514 11605 19265 569 2367 1602 C ATOM 282 CG PHE A 50 3.930 74.017 51.561 1.00120.50 C ANISOU 282 CG PHE A 50 15418 11607 18759 564 1881 1373 C ATOM 283 CD1 PHE A 50 4.925 73.045 51.523 1.00123.26 C ANISOU 283 CD1 PHE A 50 16032 11912 18887 628 1826 1369 C ATOM 284 CD2 PHE A 50 3.982 75.051 50.634 1.00120.47 C ANISOU 284 CD2 PHE A 50 15263 11834 18676 516 1505 1177 C ATOM 285 CE1 PHE A 50 5.933 73.090 50.555 1.00121.69 C ANISOU 285 CE1 PHE A 50 15918 11898 18421 633 1421 1160 C ATOM 286 CE2 PHE A 50 4.996 75.102 49.673 1.00120.88 C ANISOU 286 CE2 PHE A 50 15429 12066 18434 522 1113 987 C ATOM 287 CZ PHE A 50 5.963 74.119 49.637 1.00118.73 C ANISOU 287 CZ PHE A 50 15396 11750 17967 577 1084 975 C ATOM 288 N PHE A 51 0.267 72.803 54.349 1.00133.50 N ANISOU 288 N PHE A 51 16578 12358 21787 423 3503 2081 N ATOM 289 CA PHE A 51 -0.307 72.469 55.660 1.00137.51 C ANISOU 289 CA PHE A 51 17189 12644 22414 515 4144 2400 C ATOM 290 C PHE A 51 -0.674 70.980 55.752 1.00144.95 C ANISOU 290 C PHE A 51 18067 13176 23832 367 4424 2528 C ATOM 291 O PHE A 51 -0.765 70.442 56.859 1.00147.77 O ANISOU 291 O PHE A 51 18674 13338 24134 489 4944 2828 O ATOM 292 CB PHE A 51 -1.552 73.324 55.945 1.00141.72 C ANISOU 292 CB PHE A 51 17377 13162 23309 475 4403 2447 C ATOM 293 CG PHE A 51 -1.434 74.244 57.138 1.00143.71 C ANISOU 293 CG PHE A 51 17923 13581 23098 749 4743 2629 C ATOM 294 CD1 PHE A 51 -1.042 75.568 56.979 1.00143.81 C ANISOU 294 CD1 PHE A 51 18009 13935 22696 876 4435 2480 C ATOM 295 CD2 PHE A 51 -1.744 73.794 58.417 1.00149.97 C ANISOU 295 CD2 PHE A 51 18928 14173 23879 885 5383 2946 C ATOM 296 CE1 PHE A 51 -0.944 76.423 58.084 1.00145.03 C ANISOU 296 CE1 PHE A 51 18443 14229 22434 1133 4728 2614 C ATOM 297 CE2 PHE A 51 -1.645 74.650 59.521 1.00153.22 C ANISOU 297 CE2 PHE A 51 19647 14742 23829 1163 5688 3091 C ATOM 298 CZ PHE A 51 -1.247 75.958 59.347 1.00147.85 C ANISOU 298 CZ PHE A 51 19028 14401 22747 1283 5343 2908 C ATOM 299 N GLN A 52 -0.886 70.325 54.590 1.00140.94 N ANISOU 299 N GLN A 52 17244 12526 23782 115 4080 2298 N ATOM 300 CA GLN A 52 -1.255 68.914 54.481 1.00143.89 C ANISOU 300 CA GLN A 52 17497 12482 24693 -69 4264 2354 C ATOM 301 C GLN A 52 -0.034 67.991 54.396 1.00145.48 C ANISOU 301 C GLN A 52 18103 12642 24530 24 4123 2358 C ATOM 302 O GLN A 52 -0.101 66.874 54.914 1.00148.69 O ANISOU 302 O GLN A 52 18637 12707 25151 10 4491 2566 O ATOM 303 CB GLN A 52 -2.158 68.689 53.261 1.00146.60 C ANISOU 303 CB GLN A 52 17296 12680 25724 -376 3917 2062 C ATOM 304 CG GLN A 52 -3.598 69.146 53.472 1.00164.87 C ANISOU 304 CG GLN A 52 19124 14859 28659 -510 4189 2111 C ATOM 305 CD GLN A 52 -4.343 69.303 52.170 1.00184.87 C ANISOU 305 CD GLN A 52 21145 17381 31716 -748 3681 1762 C ATOM 306 OE1 GLN A 52 -4.557 68.340 51.424 1.00183.90 O ANISOU 306 OE1 GLN A 52 20818 17001 32055 -958 3466 1584 O ATOM 307 NE2 GLN A 52 -4.774 70.523 51.878 1.00173.21 N ANISOU 307 NE2 GLN A 52 19455 16170 30186 -708 3467 1650 N ATOM 308 N ILE A 53 1.066 68.434 53.746 1.00136.39 N ANISOU 308 N ILE A 53 17144 11817 22863 119 3616 2138 N ATOM 309 CA ILE A 53 2.263 67.597 53.590 1.00134.48 C ANISOU 309 CA ILE A 53 17251 11553 22292 217 3450 2111 C ATOM 310 C ILE A 53 3.305 67.881 54.698 1.00136.07 C ANISOU 310 C ILE A 53 17956 11941 21804 547 3636 2337 C ATOM 311 O ILE A 53 3.526 69.031 55.079 1.00133.45 O ANISOU 311 O ILE A 53 17720 11912 21074 699 3611 2356 O ATOM 312 CB ILE A 53 2.892 67.651 52.164 1.00134.38 C ANISOU 312 CB ILE A 53 17158 11729 22170 130 2827 1740 C ATOM 313 CG1 ILE A 53 3.504 69.013 51.808 1.00130.23 C ANISOU 313 CG1 ILE A 53 16690 11659 21133 250 2485 1596 C ATOM 314 CG2 ILE A 53 1.898 67.182 51.095 1.00137.75 C ANISOU 314 CG2 ILE A 53 17143 11925 23270 -170 2617 1503 C ATOM 315 CD1 ILE A 53 4.845 68.897 51.121 1.00133.42 C ANISOU 315 CD1 ILE A 53 17332 12276 21086 348 2088 1410 C ATOM 316 N ARG A 54 3.930 66.803 55.209 1.00133.78 N ANISOU 316 N ARG A 54 17988 11447 21395 662 3807 2499 N ATOM 317 CA ARG A 54 4.939 66.830 56.273 1.00132.23 C ANISOU 317 CA ARG A 54 18291 11376 20575 994 3954 2713 C ATOM 318 C ARG A 54 6.341 67.130 55.723 1.00129.47 C ANISOU 318 C ARG A 54 18131 11346 19715 1131 3449 2489 C ATOM 319 O ARG A 54 6.666 66.755 54.594 1.00127.27 O ANISOU 319 O ARG A 54 17695 11066 19594 985 3087 2233 O ATOM 320 CB ARG A 54 4.945 65.493 57.035 1.00136.34 C ANISOU 320 CB ARG A 54 19071 11502 21232 1072 4374 3011 C ATOM 321 N SER A 55 7.169 67.796 56.542 1.00122.95 N ANISOU 321 N SER A 55 17643 10781 18289 1419 3436 2579 N ATOM 322 CA SER A 55 8.536 68.175 56.200 1.00118.83 C ANISOU 322 CA SER A 55 17293 10563 17292 1572 3004 2391 C ATOM 323 C SER A 55 9.494 66.997 56.409 1.00122.67 C ANISOU 323 C SER A 55 18076 10889 17644 1728 2987 2468 C ATOM 324 O SER A 55 9.924 66.736 57.533 1.00124.59 O ANISOU 324 O SER A 55 18685 11078 17577 1993 3211 2711 O ATOM 325 CB SER A 55 8.971 69.384 57.023 1.00120.93 C ANISOU 325 CB SER A 55 17764 11148 17034 1807 2978 2431 C ATOM 326 OG SER A 55 8.231 70.549 56.691 1.00126.86 O ANISOU 326 OG SER A 55 18239 12069 17893 1674 2929 2322 O ATOM 327 N LYS A 56 9.814 66.280 55.323 1.00117.15 N ANISOU 327 N LYS A 56 17233 10105 17172 1582 2717 2256 N ATOM 328 CA LYS A 56 10.706 65.121 55.365 1.00117.56 C ANISOU 328 CA LYS A 56 17524 9984 17158 1716 2673 2292 C ATOM 329 C LYS A 56 12.103 65.453 54.795 1.00116.35 C ANISOU 329 C LYS A 56 17457 10144 16607 1861 2237 2062 C ATOM 330 O LYS A 56 12.958 64.564 54.716 1.00116.99 O ANISOU 330 O LYS A 56 17716 10121 16612 1995 2151 2055 O ATOM 331 CB LYS A 56 10.078 63.934 54.613 1.00122.52 C ANISOU 331 CB LYS A 56 17950 10240 18362 1465 2719 2217 C ATOM 332 N SER A 57 12.336 66.729 54.418 1.00108.03 N ANISOU 332 N SER A 57 16270 9453 15324 1840 1985 1883 N ATOM 333 CA SER A 57 13.613 67.217 53.874 1.00104.21 C ANISOU 333 CA SER A 57 15819 9275 14502 1954 1606 1668 C ATOM 334 C SER A 57 13.806 68.709 54.163 1.00103.02 C ANISOU 334 C SER A 57 15644 9471 14029 2021 1490 1620 C ATOM 335 O SER A 57 12.827 69.399 54.458 1.00103.25 O ANISOU 335 O SER A 57 15577 9512 14142 1934 1662 1703 O ATOM 336 CB SER A 57 13.700 66.957 52.370 1.00106.79 C ANISOU 336 CB SER A 57 15905 9615 15054 1747 1331 1377 C ATOM 337 OG SER A 57 12.716 67.669 51.637 1.00114.58 O ANISOU 337 OG SER A 57 16598 10659 16276 1496 1275 1256 O ATOM 338 N ASN A 58 15.067 69.204 54.084 1.00 95.23 N ANISOU 338 N ASN A 58 14730 8746 12707 2175 1207 1482 N ATOM 339 CA ASN A 58 15.424 70.618 54.302 1.00 92.03 C ANISOU 339 CA ASN A 58 14297 8656 12013 2239 1054 1401 C ATOM 340 C ASN A 58 14.672 71.526 53.341 1.00 91.90 C ANISOU 340 C ASN A 58 13977 8757 12183 1980 963 1251 C ATOM 341 O ASN A 58 14.183 72.584 53.738 1.00 90.25 O ANISOU 341 O ASN A 58 13726 8675 11891 1972 1010 1281 O ATOM 342 CB ASN A 58 16.929 70.836 54.109 1.00 90.89 C ANISOU 342 CB ASN A 58 14210 8724 11598 2402 750 1243 C ATOM 343 CG ASN A 58 17.822 70.033 55.005 1.00112.01 C ANISOU 343 CG ASN A 58 17174 11321 14064 2695 757 1360 C ATOM 344 OD1 ASN A 58 17.378 69.341 55.922 1.00108.73 O ANISOU 344 OD1 ASN A 58 16988 10705 13619 2822 1007 1596 O ATOM 345 ND2 ASN A 58 19.114 70.110 54.747 1.00104.11 N ANISOU 345 ND2 ASN A 58 16166 10471 12920 2820 488 1204 N ATOM 346 N PHE A 59 14.589 71.082 52.075 1.00 87.09 N ANISOU 346 N PHE A 59 13180 8096 11816 1791 825 1086 N ATOM 347 CA PHE A 59 13.939 71.721 50.945 1.00 85.40 C ANISOU 347 CA PHE A 59 12698 7969 11783 1559 687 923 C ATOM 348 C PHE A 59 12.501 72.120 51.274 1.00 90.47 C ANISOU 348 C PHE A 59 13201 8511 12661 1430 887 1038 C ATOM 349 O PHE A 59 12.163 73.291 51.105 1.00 88.91 O ANISOU 349 O PHE A 59 12879 8490 12412 1376 812 988 O ATOM 350 CB PHE A 59 13.978 70.781 49.727 1.00 87.74 C ANISOU 350 CB PHE A 59 12894 8141 12302 1422 550 755 C ATOM 351 CG PHE A 59 13.415 71.332 48.438 1.00 88.43 C ANISOU 351 CG PHE A 59 12749 8318 12533 1215 355 564 C ATOM 352 CD1 PHE A 59 13.881 72.531 47.912 1.00 89.11 C ANISOU 352 CD1 PHE A 59 12775 8687 12397 1215 170 457 C ATOM 353 CD2 PHE A 59 12.449 70.629 47.728 1.00 92.55 C ANISOU 353 CD2 PHE A 59 13121 8626 13416 1030 341 486 C ATOM 354 CE1 PHE A 59 13.356 73.039 46.726 1.00 89.66 C ANISOU 354 CE1 PHE A 59 12671 8834 12563 1054 -12 305 C ATOM 355 CE2 PHE A 59 11.942 71.127 46.527 1.00 94.76 C ANISOU 355 CE2 PHE A 59 13215 8996 13795 871 116 299 C ATOM 356 CZ PHE A 59 12.411 72.321 46.026 1.00 90.59 C ANISOU 356 CZ PHE A 59 12663 8758 12999 896 -56 220 C ATOM 357 N ILE A 60 11.679 71.177 51.790 1.00 89.30 N ANISOU 357 N ILE A 60 13071 8070 12789 1390 1162 1199 N ATOM 358 CA ILE A 60 10.278 71.447 52.146 1.00 90.74 C ANISOU 358 CA ILE A 60 13088 8122 13268 1266 1405 1320 C ATOM 359 C ILE A 60 10.212 72.524 53.250 1.00 93.77 C ANISOU 359 C ILE A 60 13594 8661 13372 1428 1568 1464 C ATOM 360 O ILE A 60 9.348 73.399 53.179 1.00 92.97 O ANISOU 360 O ILE A 60 13305 8616 13405 1335 1617 1459 O ATOM 361 CB ILE A 60 9.487 70.162 52.549 1.00 97.55 C ANISOU 361 CB ILE A 60 13943 8603 14519 1192 1716 1482 C ATOM 362 CG1 ILE A 60 9.732 68.994 51.553 1.00 98.88 C ANISOU 362 CG1 ILE A 60 14053 8594 14922 1073 1540 1321 C ATOM 363 CG2 ILE A 60 7.983 70.461 52.661 1.00 99.99 C ANISOU 363 CG2 ILE A 60 13976 8773 15242 1014 1934 1554 C ATOM 364 CD1 ILE A 60 9.411 67.552 52.083 1.00106.55 C ANISOU 364 CD1 ILE A 60 15126 9167 16191 1066 1836 1495 C ATOM 365 N ILE A 61 11.143 72.473 54.235 1.00 90.10 N ANISOU 365 N ILE A 61 13448 8267 12521 1683 1621 1570 N ATOM 366 CA ILE A 61 11.222 73.408 55.368 1.00 89.33 C ANISOU 366 CA ILE A 61 13534 8310 12096 1881 1746 1682 C ATOM 367 C ILE A 61 11.496 74.837 54.853 1.00 89.96 C ANISOU 367 C ILE A 61 13473 8682 12026 1841 1470 1490 C ATOM 368 O ILE A 61 10.790 75.772 55.254 1.00 90.38 O ANISOU 368 O ILE A 61 13469 8794 12079 1842 1590 1531 O ATOM 369 CB ILE A 61 12.268 72.938 56.438 1.00 93.05 C ANISOU 369 CB ILE A 61 14393 8789 12174 2184 1782 1801 C ATOM 370 CG1 ILE A 61 11.784 71.660 57.152 1.00 97.13 C ANISOU 370 CG1 ILE A 61 15090 8984 12833 2247 2141 2057 C ATOM 371 CG2 ILE A 61 12.591 74.037 57.464 1.00 92.78 C ANISOU 371 CG2 ILE A 61 14567 8952 11735 2410 1791 1834 C ATOM 372 CD1 ILE A 61 12.878 70.826 57.945 1.00107.66 C ANISOU 372 CD1 ILE A 61 16797 10264 13847 2534 2119 2167 C ATOM 373 N PHE A 62 12.492 74.998 53.960 1.00 82.56 N ANISOU 373 N PHE A 62 12479 7906 10983 1809 1131 1291 N ATOM 374 CA PHE A 62 12.851 76.311 53.425 1.00 79.35 C ANISOU 374 CA PHE A 62 11953 7750 10448 1769 884 1125 C ATOM 375 C PHE A 62 11.718 76.864 52.542 1.00 83.72 C ANISOU 375 C PHE A 62 12215 8293 11301 1543 865 1066 C ATOM 376 O PHE A 62 11.418 78.065 52.626 1.00 82.08 O ANISOU 376 O PHE A 62 11935 8213 11037 1540 834 1039 O ATOM 377 CB PHE A 62 14.197 76.265 52.679 1.00 78.91 C ANISOU 377 CB PHE A 62 11902 7838 10240 1790 585 950 C ATOM 378 CG PHE A 62 15.363 75.751 53.500 1.00 80.82 C ANISOU 378 CG PHE A 62 12392 8100 10216 2026 550 983 C ATOM 379 CD1 PHE A 62 15.495 76.087 54.846 1.00 84.82 C ANISOU 379 CD1 PHE A 62 13129 8628 10472 2246 657 1099 C ATOM 380 CD2 PHE A 62 16.336 74.942 52.926 1.00 82.28 C ANISOU 380 CD2 PHE A 62 12589 8283 10391 2053 394 886 C ATOM 381 CE1 PHE A 62 16.560 75.592 55.607 1.00 86.27 C ANISOU 381 CE1 PHE A 62 13551 8828 10402 2491 581 1123 C ATOM 382 CE2 PHE A 62 17.407 74.462 53.685 1.00 85.64 C ANISOU 382 CE2 PHE A 62 13223 8721 10596 2290 336 913 C ATOM 383 CZ PHE A 62 17.513 74.794 55.019 1.00 84.94 C ANISOU 383 CZ PHE A 62 13360 8654 10260 2510 411 1030 C ATOM 384 N LEU A 63 11.051 75.979 51.751 1.00 81.39 N ANISOU 384 N LEU A 63 11757 7827 11340 1369 876 1043 N ATOM 385 CA LEU A 63 9.898 76.344 50.920 1.00 81.34 C ANISOU 385 CA LEU A 63 11464 7782 11660 1168 827 980 C ATOM 386 C LEU A 63 8.716 76.762 51.798 1.00 88.61 C ANISOU 386 C LEU A 63 12306 8608 12755 1173 1119 1136 C ATOM 387 O LEU A 63 8.013 77.713 51.446 1.00 88.41 O ANISOU 387 O LEU A 63 12086 8657 12850 1096 1055 1088 O ATOM 388 CB LEU A 63 9.462 75.211 49.983 1.00 82.50 C ANISOU 388 CB LEU A 63 11469 7739 12139 999 760 900 C ATOM 389 CG LEU A 63 10.403 74.775 48.857 1.00 85.83 C ANISOU 389 CG LEU A 63 11924 8235 12452 966 470 709 C ATOM 390 CD1 LEU A 63 9.860 73.540 48.189 1.00 87.75 C ANISOU 390 CD1 LEU A 63 12056 8239 13044 820 446 635 C ATOM 391 CD2 LEU A 63 10.625 75.876 47.823 1.00 85.45 C ANISOU 391 CD2 LEU A 63 11781 8423 12263 916 190 553 C ATOM 392 N LYS A 64 8.516 76.080 52.953 1.00 87.84 N ANISOU 392 N LYS A 64 12374 8344 12659 1283 1455 1333 N ATOM 393 CA LYS A 64 7.445 76.408 53.901 1.00 90.29 C ANISOU 393 CA LYS A 64 12647 8550 13107 1319 1810 1506 C ATOM 394 C LYS A 64 7.605 77.842 54.448 1.00 94.11 C ANISOU 394 C LYS A 64 13214 9253 13292 1458 1787 1490 C ATOM 395 O LYS A 64 6.614 78.569 54.552 1.00 94.53 O ANISOU 395 O LYS A 64 13086 9295 13534 1413 1913 1516 O ATOM 396 CB LYS A 64 7.387 75.395 55.052 1.00 95.53 C ANISOU 396 CB LYS A 64 13551 9002 13743 1450 2190 1739 C ATOM 397 CG LYS A 64 6.455 74.219 54.778 1.00112.04 C ANISOU 397 CG LYS A 64 15450 10777 16342 1269 2403 1823 C ATOM 398 CD LYS A 64 6.346 73.302 55.990 1.00124.46 C ANISOU 398 CD LYS A 64 17292 12119 17878 1413 2831 2095 C ATOM 399 CE LYS A 64 5.219 72.297 55.892 1.00136.30 C ANISOU 399 CE LYS A 64 18566 13266 19955 1222 3138 2213 C ATOM 400 NZ LYS A 64 5.548 71.145 55.013 1.00139.59 N ANISOU 400 NZ LYS A 64 18910 13515 20613 1073 2936 2100 N ATOM 401 N ASN A 65 8.856 78.249 54.748 1.00 89.42 N ANISOU 401 N ASN A 65 12867 8843 12266 1623 1608 1428 N ATOM 402 CA ASN A 65 9.205 79.577 55.261 1.00 88.12 C ANISOU 402 CA ASN A 65 12804 8873 11804 1760 1537 1375 C ATOM 403 C ASN A 65 8.997 80.675 54.216 1.00 90.42 C ANISOU 403 C ASN A 65 12839 9301 12214 1612 1275 1212 C ATOM 404 O ASN A 65 8.634 81.800 54.574 1.00 89.62 O ANISOU 404 O ASN A 65 12715 9276 12062 1665 1312 1200 O ATOM 405 CB ASN A 65 10.652 79.593 55.724 1.00 86.07 C ANISOU 405 CB ASN A 65 12828 8748 11126 1950 1362 1319 C ATOM 406 CG ASN A 65 10.873 78.941 57.055 1.00 97.01 C ANISOU 406 CG ASN A 65 14545 10041 12275 2183 1610 1490 C ATOM 407 OD1 ASN A 65 10.494 79.478 58.099 1.00 93.77 O ANISOU 407 OD1 ASN A 65 14298 9630 11701 2342 1830 1583 O ATOM 408 ND2 ASN A 65 11.523 77.788 57.047 1.00 84.40 N ANISOU 408 ND2 ASN A 65 13077 8361 10628 2231 1578 1533 N ATOM 409 N THR A 66 9.239 80.339 52.931 1.00 85.98 N ANISOU 409 N THR A 66 12113 8759 11796 1446 1020 1092 N ATOM 410 CA THR A 66 9.103 81.222 51.769 1.00 84.27 C ANISOU 410 CA THR A 66 11687 8659 11673 1313 756 953 C ATOM 411 C THR A 66 7.627 81.652 51.625 1.00 90.29 C ANISOU 411 C THR A 66 12198 9331 12779 1217 871 998 C ATOM 412 O THR A 66 7.374 82.832 51.363 1.00 89.59 O ANISOU 412 O THR A 66 12017 9342 12681 1216 770 948 O ATOM 413 CB THR A 66 9.680 80.513 50.527 1.00 91.79 C ANISOU 413 CB THR A 66 12581 9627 12667 1193 507 831 C ATOM 414 OG1 THR A 66 11.100 80.416 50.678 1.00 91.04 O ANISOU 414 OG1 THR A 66 12691 9637 12266 1303 408 782 O ATOM 415 CG2 THR A 66 9.390 81.237 49.240 1.00 89.85 C ANISOU 415 CG2 THR A 66 12156 9483 12500 1070 250 710 C ATOM 416 N VAL A 67 6.667 80.715 51.855 1.00 88.79 N ANISOU 416 N VAL A 67 11888 8934 12913 1146 1096 1096 N ATOM 417 CA VAL A 67 5.213 80.954 51.806 1.00 90.27 C ANISOU 417 CA VAL A 67 11789 9001 13508 1055 1239 1142 C ATOM 418 C VAL A 67 4.841 82.069 52.804 1.00 94.86 C ANISOU 418 C VAL A 67 12424 9636 13981 1201 1460 1225 C ATOM 419 O VAL A 67 4.089 82.981 52.444 1.00 95.01 O ANISOU 419 O VAL A 67 12228 9685 14186 1163 1398 1184 O ATOM 420 CB VAL A 67 4.385 79.660 52.074 1.00 97.19 C ANISOU 420 CB VAL A 67 12541 9614 14773 959 1502 1247 C ATOM 421 CG1 VAL A 67 2.890 79.891 51.862 1.00 99.22 C ANISOU 421 CG1 VAL A 67 12428 9741 15530 843 1612 1265 C ATOM 422 CG2 VAL A 67 4.860 78.497 51.215 1.00 96.87 C ANISOU 422 CG2 VAL A 67 12491 9499 14815 837 1291 1148 C ATOM 423 N ILE A 68 5.391 82.005 54.038 1.00 91.87 N ANISOU 423 N ILE A 68 12352 9269 13284 1389 1694 1329 N ATOM 424 CA ILE A 68 5.141 82.981 55.108 1.00 92.70 C ANISOU 424 CA ILE A 68 12582 9421 13219 1566 1916 1391 C ATOM 425 C ILE A 68 5.701 84.360 54.699 1.00 94.60 C ANISOU 425 C ILE A 68 12836 9859 13250 1600 1612 1238 C ATOM 426 O ILE A 68 4.985 85.353 54.821 1.00 94.85 O ANISOU 426 O ILE A 68 12745 9900 13392 1626 1673 1227 O ATOM 427 CB ILE A 68 5.704 82.500 56.480 1.00 97.15 C ANISOU 427 CB ILE A 68 13528 9955 13430 1787 2188 1521 C ATOM 428 CG1 ILE A 68 5.072 81.155 56.908 1.00100.52 C ANISOU 428 CG1 ILE A 68 13953 10148 14092 1754 2541 1711 C ATOM 429 CG2 ILE A 68 5.506 83.558 57.572 1.00 98.77 C ANISOU 429 CG2 ILE A 68 13905 10218 13403 1996 2391 1551 C ATOM 430 CD1 ILE A 68 6.043 80.161 57.559 1.00108.48 C ANISOU 430 CD1 ILE A 68 15330 11122 14764 1907 2615 1807 C ATOM 431 N SER A 69 6.950 84.412 54.181 1.00 88.89 N ANISOU 431 N SER A 69 12240 9271 12263 1594 1301 1122 N ATOM 432 CA SER A 69 7.582 85.668 53.760 1.00 86.63 C ANISOU 432 CA SER A 69 11965 9144 11806 1607 1030 987 C ATOM 433 C SER A 69 6.899 86.251 52.526 1.00 89.97 C ANISOU 433 C SER A 69 12097 9577 12510 1448 840 928 C ATOM 434 O SER A 69 6.958 87.460 52.338 1.00 89.58 O ANISOU 434 O SER A 69 12022 9603 12411 1472 720 866 O ATOM 435 CB SER A 69 9.077 85.486 53.505 1.00 87.92 C ANISOU 435 CB SER A 69 12297 9426 11684 1628 785 890 C ATOM 436 OG SER A 69 9.349 84.690 52.365 1.00 94.74 O ANISOU 436 OG SER A 69 13047 10281 12667 1477 618 851 O ATOM 437 N ASP A 70 6.253 85.411 51.693 1.00 86.82 N ANISOU 437 N ASP A 70 11491 9089 12406 1297 797 941 N ATOM 438 CA ASP A 70 5.525 85.884 50.517 1.00 86.55 C ANISOU 438 CA ASP A 70 11191 9058 12634 1170 584 880 C ATOM 439 C ASP A 70 4.221 86.516 50.951 1.00 92.27 C ANISOU 439 C ASP A 70 11716 9697 13646 1200 767 942 C ATOM 440 O ASP A 70 3.909 87.617 50.505 1.00 92.13 O ANISOU 440 O ASP A 70 11591 9732 13683 1206 617 899 O ATOM 441 CB ASP A 70 5.258 84.753 49.518 1.00 89.22 C ANISOU 441 CB ASP A 70 11385 9322 13194 1015 444 839 C ATOM 442 CG ASP A 70 6.452 84.268 48.720 1.00 99.38 C ANISOU 442 CG ASP A 70 12817 10704 14240 973 205 744 C ATOM 443 OD1 ASP A 70 7.454 85.017 48.626 1.00 99.93 O ANISOU 443 OD1 ASP A 70 13039 10917 14014 1033 84 699 O ATOM 444 OD2 ASP A 70 6.375 83.154 48.167 1.00104.24 O ANISOU 444 OD2 ASP A 70 13381 11238 14988 878 144 706 O ATOM 445 N LEU A 71 3.483 85.842 51.857 1.00 91.10 N ANISOU 445 N LEU A 71 11524 9405 13684 1231 1114 1055 N ATOM 446 CA LEU A 71 2.207 86.316 52.400 1.00 93.64 C ANISOU 446 CA LEU A 71 11638 9624 14316 1271 1370 1127 C ATOM 447 C LEU A 71 2.377 87.636 53.158 1.00 96.67 C ANISOU 447 C LEU A 71 12172 10093 14464 1446 1455 1121 C ATOM 448 O LEU A 71 1.537 88.524 53.021 1.00 96.26 O ANISOU 448 O LEU A 71 11920 10019 14636 1467 1463 1110 O ATOM 449 CB LEU A 71 1.570 85.247 53.302 1.00 96.59 C ANISOU 449 CB LEU A 71 11986 9817 14895 1280 1790 1272 C ATOM 450 CG LEU A 71 0.842 84.117 52.561 1.00103.23 C ANISOU 450 CG LEU A 71 12541 10496 16185 1085 1758 1273 C ATOM 451 CD1 LEU A 71 0.827 82.834 53.383 1.00105.17 C ANISOU 451 CD1 LEU A 71 12907 10573 16480 1092 2131 1420 C ATOM 452 CD2 LEU A 71 -0.579 84.530 52.170 1.00107.65 C ANISOU 452 CD2 LEU A 71 12671 10956 17275 1003 1765 1255 C ATOM 453 N LEU A 72 3.491 87.781 53.902 1.00 92.97 N ANISOU 453 N LEU A 72 12050 9715 13558 1575 1485 1109 N ATOM 454 CA LEU A 72 3.837 88.990 54.647 1.00 93.01 C ANISOU 454 CA LEU A 72 12245 9796 13299 1745 1522 1063 C ATOM 455 C LEU A 72 4.164 90.150 53.695 1.00 93.80 C ANISOU 455 C LEU A 72 12264 9991 13385 1691 1171 944 C ATOM 456 O LEU A 72 3.874 91.303 54.013 1.00 93.99 O ANISOU 456 O LEU A 72 12299 10020 13394 1789 1197 907 O ATOM 457 CB LEU A 72 5.024 88.711 55.574 1.00 93.09 C ANISOU 457 CB LEU A 72 12631 9873 12865 1886 1566 1051 C ATOM 458 CG LEU A 72 4.719 88.791 57.068 1.00101.40 C ANISOU 458 CG LEU A 72 13915 10871 13741 2105 1947 1133 C ATOM 459 CD1 LEU A 72 4.346 87.421 57.632 1.00103.81 C ANISOU 459 CD1 LEU A 72 14224 11039 14178 2102 2295 1309 C ATOM 460 CD2 LEU A 72 5.900 89.365 57.831 1.00104.93 C ANISOU 460 CD2 LEU A 72 14734 11425 13710 2280 1838 1043 C ATOM 461 N MET A 73 4.740 89.830 52.522 1.00 87.29 N ANISOU 461 N MET A 73 11373 9227 12567 1543 863 892 N ATOM 462 CA MET A 73 5.097 90.766 51.454 1.00 85.11 C ANISOU 462 CA MET A 73 11037 9029 12273 1479 544 812 C ATOM 463 C MET A 73 3.826 91.352 50.809 1.00 89.87 C ANISOU 463 C MET A 73 11350 9565 13233 1442 491 835 C ATOM 464 O MET A 73 3.718 92.568 50.678 1.00 90.03 O ANISOU 464 O MET A 73 11353 9595 13259 1498 403 809 O ATOM 465 CB MET A 73 5.975 90.030 50.413 1.00 85.55 C ANISOU 465 CB MET A 73 11130 9159 12217 1354 295 766 C ATOM 466 CG MET A 73 6.185 90.765 49.109 1.00 87.80 C ANISOU 466 CG MET A 73 11343 9506 12510 1276 -5 718 C ATOM 467 SD MET A 73 7.896 90.863 48.548 1.00 89.68 S ANISOU 467 SD MET A 73 11791 9871 12413 1243 -196 643 S ATOM 468 CE MET A 73 8.349 89.141 48.437 1.00 86.87 C ANISOU 468 CE MET A 73 11463 9522 12020 1165 -205 631 C ATOM 469 N ILE A 74 2.885 90.476 50.404 1.00 86.99 N ANISOU 469 N ILE A 74 10750 9116 13188 1353 530 876 N ATOM 470 CA ILE A 74 1.605 90.788 49.761 1.00 88.36 C ANISOU 470 CA ILE A 74 10596 9212 13764 1314 451 884 C ATOM 471 C ILE A 74 0.782 91.754 50.635 1.00 94.07 C ANISOU 471 C ILE A 74 11236 9869 14636 1454 696 925 C ATOM 472 O ILE A 74 0.210 92.713 50.106 1.00 93.66 O ANISOU 472 O ILE A 74 11024 9804 14757 1486 543 907 O ATOM 473 CB ILE A 74 0.863 89.447 49.474 1.00 93.11 C ANISOU 473 CB ILE A 74 10971 9707 14698 1189 501 903 C ATOM 474 CG1 ILE A 74 1.535 88.690 48.308 1.00 92.11 C ANISOU 474 CG1 ILE A 74 10898 9642 14457 1059 181 825 C ATOM 475 CG2 ILE A 74 -0.642 89.625 49.229 1.00 96.48 C ANISOU 475 CG2 ILE A 74 11006 10018 15634 1169 512 913 C ATOM 476 CD1 ILE A 74 1.573 87.181 48.470 1.00100.90 C ANISOU 476 CD1 ILE A 74 11995 10661 15681 962 306 837 C ATOM 477 N LEU A 75 0.777 91.529 51.968 1.00 92.07 N ANISOU 477 N LEU A 75 11126 9573 14284 1561 1072 980 N ATOM 478 CA LEU A 75 0.057 92.342 52.954 1.00 94.05 C ANISOU 478 CA LEU A 75 11350 9757 14626 1722 1370 1012 C ATOM 479 C LEU A 75 0.565 93.807 53.029 1.00 96.34 C ANISOU 479 C LEU A 75 11805 10110 14692 1837 1231 935 C ATOM 480 O LEU A 75 -0.151 94.669 53.553 1.00 96.90 O ANISOU 480 O LEU A 75 11804 10116 14900 1967 1400 935 O ATOM 481 CB LEU A 75 0.134 91.680 54.340 1.00 95.60 C ANISOU 481 CB LEU A 75 11749 9906 14667 1830 1799 1091 C ATOM 482 CG LEU A 75 -0.816 90.500 54.561 1.00103.17 C ANISOU 482 CG LEU A 75 12489 10729 15984 1754 2092 1205 C ATOM 483 CD1 LEU A 75 -0.290 89.563 55.630 1.00103.91 C ANISOU 483 CD1 LEU A 75 12885 10797 15798 1829 2414 1299 C ATOM 484 CD2 LEU A 75 -2.214 90.976 54.924 1.00109.67 C ANISOU 484 CD2 LEU A 75 12998 11428 17244 1815 2370 1256 C ATOM 485 N THR A 76 1.775 94.084 52.483 1.00 90.35 N ANISOU 485 N THR A 76 11246 9456 13626 1788 940 865 N ATOM 486 CA THR A 76 2.396 95.417 52.439 1.00 88.86 C ANISOU 486 CA THR A 76 11208 9301 13254 1861 786 788 C ATOM 487 C THR A 76 1.854 96.245 51.259 1.00 91.09 C ANISOU 487 C THR A 76 11278 9557 13773 1814 520 794 C ATOM 488 O THR A 76 1.735 97.465 51.378 1.00 90.78 O ANISOU 488 O THR A 76 11265 9473 13756 1910 495 764 O ATOM 489 CB THR A 76 3.927 95.290 52.353 1.00 96.93 C ANISOU 489 CB THR A 76 12499 10426 13904 1817 618 721 C ATOM 490 OG1 THR A 76 4.392 94.523 53.457 1.00 99.53 O ANISOU 490 OG1 THR A 76 13031 10774 14011 1893 836 720 O ATOM 491 CG2 THR A 76 4.629 96.629 52.363 1.00 98.47 C ANISOU 491 CG2 THR A 76 12835 10625 13952 1873 478 632 C ATOM 492 N PHE A 77 1.533 95.574 50.133 1.00 86.50 N ANISOU 492 N PHE A 77 10511 8996 13361 1682 313 827 N ATOM 493 CA PHE A 77 1.062 96.183 48.888 1.00 86.16 C ANISOU 493 CA PHE A 77 10299 8941 13496 1650 11 840 C ATOM 494 C PHE A 77 -0.180 97.082 49.076 1.00 93.09 C ANISOU 494 C PHE A 77 10949 9710 14709 1772 80 864 C ATOM 495 O PHE A 77 -0.124 98.176 48.518 1.00 92.61 O ANISOU 495 O PHE A 77 10916 9632 14641 1825 -111 868 O ATOM 496 CB PHE A 77 0.812 95.136 47.784 1.00 87.68 C ANISOU 496 CB PHE A 77 10338 9167 13810 1513 -213 844 C ATOM 497 CG PHE A 77 1.967 94.211 47.441 1.00 87.04 C ANISOU 497 CG PHE A 77 10456 9183 13433 1400 -303 814 C ATOM 498 CD1 PHE A 77 3.283 94.559 47.747 1.00 87.70 C ANISOU 498 CD1 PHE A 77 10821 9339 13161 1412 -288 789 C ATOM 499 CD2 PHE A 77 1.744 93.012 46.776 1.00 89.39 C ANISOU 499 CD2 PHE A 77 10640 9487 13837 1286 -420 794 C ATOM 500 CE1 PHE A 77 4.343 93.702 47.430 1.00 86.53 C ANISOU 500 CE1 PHE A 77 10827 9276 12773 1322 -362 757 C ATOM 501 CE2 PHE A 77 2.808 92.160 46.454 1.00 90.04 C ANISOU 501 CE2 PHE A 77 10907 9649 13655 1199 -492 758 C ATOM 502 CZ PHE A 77 4.098 92.514 46.779 1.00 85.73 C ANISOU 502 CZ PHE A 77 10629 9183 12761 1222 -456 746 C ATOM 503 N PRO A 78 -1.257 96.751 49.864 1.00 92.54 N ANISOU 503 N PRO A 78 10664 9555 14943 1831 366 888 N ATOM 504 CA PRO A 78 -2.386 97.700 49.993 1.00 94.81 C ANISOU 504 CA PRO A 78 10718 9737 15569 1963 426 902 C ATOM 505 C PRO A 78 -1.966 99.077 50.501 1.00 97.45 C ANISOU 505 C PRO A 78 11260 10040 15725 2110 479 870 C ATOM 506 O PRO A 78 -2.505 100.075 50.032 1.00 98.44 O ANISOU 506 O PRO A 78 11263 10097 16042 2196 336 879 O ATOM 507 CB PRO A 78 -3.320 97.015 50.997 1.00 98.92 C ANISOU 507 CB PRO A 78 11042 10176 16369 2002 831 934 C ATOM 508 CG PRO A 78 -3.025 95.587 50.860 1.00102.48 C ANISOU 508 CG PRO A 78 11497 10665 16774 1844 845 952 C ATOM 509 CD PRO A 78 -1.545 95.509 50.612 1.00 94.99 C ANISOU 509 CD PRO A 78 10914 9839 15337 1785 662 917 C ATOM 510 N PHE A 79 -0.980 99.127 51.417 1.00 91.87 N ANISOU 510 N PHE A 79 10873 9372 14660 2144 652 822 N ATOM 511 CA PHE A 79 -0.434 100.358 51.990 1.00 91.43 C ANISOU 511 CA PHE A 79 11049 9276 14416 2270 692 751 C ATOM 512 C PHE A 79 0.327 101.148 50.923 1.00 93.43 C ANISOU 512 C PHE A 79 11402 9542 14555 2205 338 746 C ATOM 513 O PHE A 79 0.244 102.377 50.901 1.00 93.88 O ANISOU 513 O PHE A 79 11501 9504 14667 2303 292 722 O ATOM 514 CB PHE A 79 0.466 100.040 53.196 1.00 92.79 C ANISOU 514 CB PHE A 79 11532 9495 14228 2318 911 680 C ATOM 515 CG PHE A 79 -0.256 99.338 54.328 1.00 96.79 C ANISOU 515 CG PHE A 79 12007 9973 14795 2418 1316 710 C ATOM 516 CD1 PHE A 79 -0.306 97.950 54.390 1.00 99.62 C ANISOU 516 CD1 PHE A 79 12314 10378 15158 2319 1429 785 C ATOM 517 CD2 PHE A 79 -0.893 100.068 55.327 1.00101.63 C ANISOU 517 CD2 PHE A 79 12654 10495 15466 2619 1609 671 C ATOM 518 CE1 PHE A 79 -0.986 97.305 55.426 1.00102.90 C ANISOU 518 CE1 PHE A 79 12710 10742 15644 2411 1848 844 C ATOM 519 CE2 PHE A 79 -1.571 99.421 56.364 1.00106.57 C ANISOU 519 CE2 PHE A 79 13270 11087 16135 2725 2035 722 C ATOM 520 CZ PHE A 79 -1.614 98.045 56.405 1.00104.49 C ANISOU 520 CZ PHE A 79 12954 10863 15885 2616 2161 820 C ATOM 521 N LYS A 80 1.032 100.440 50.018 1.00 88.09 N ANISOU 521 N LYS A 80 10768 8967 13735 2045 111 776 N ATOM 522 CA LYS A 80 1.776 101.030 48.902 1.00 86.53 C ANISOU 522 CA LYS A 80 10675 8788 13415 1973 -186 801 C ATOM 523 C LYS A 80 0.799 101.580 47.851 1.00 93.17 C ANISOU 523 C LYS A 80 11310 9566 14523 2012 -403 885 C ATOM 524 O LYS A 80 0.908 102.747 47.474 1.00 93.35 O ANISOU 524 O LYS A 80 11408 9509 14552 2070 -526 917 O ATOM 525 CB LYS A 80 2.719 99.991 48.271 1.00 85.73 C ANISOU 525 CB LYS A 80 10678 8817 13078 1813 -316 805 C ATOM 526 CG LYS A 80 4.135 100.491 48.073 1.00 97.86 C ANISOU 526 CG LYS A 80 12455 10380 14348 1755 -415 775 C ATOM 527 CD LYS A 80 4.359 101.081 46.692 1.00109.88 C ANISOU 527 CD LYS A 80 13990 11893 15867 1706 -668 863 C ATOM 528 CE LYS A 80 5.689 101.788 46.607 1.00120.18 C ANISOU 528 CE LYS A 80 15503 13179 16979 1652 -702 844 C ATOM 529 NZ LYS A 80 5.937 102.323 45.245 1.00131.82 N ANISOU 529 NZ LYS A 80 17026 14640 18421 1611 -898 962 N ATOM 530 N ILE A 81 -0.169 100.736 47.413 1.00 91.48 N ANISOU 530 N ILE A 81 10836 9375 14549 1988 -459 917 N ATOM 531 CA ILE A 81 -1.220 101.030 46.433 1.00 93.66 C ANISOU 531 CA ILE A 81 10874 9603 15109 2039 -708 976 C ATOM 532 C ILE A 81 -1.954 102.322 46.819 1.00102.04 C ANISOU 532 C ILE A 81 11844 10524 16405 2219 -638 992 C ATOM 533 O ILE A 81 -2.050 103.232 45.993 1.00102.57 O ANISOU 533 O ILE A 81 11936 10533 16502 2288 -875 1055 O ATOM 534 CB ILE A 81 -2.206 99.824 46.310 1.00 97.72 C ANISOU 534 CB ILE A 81 11078 10139 15911 1980 -718 960 C ATOM 535 CG1 ILE A 81 -1.518 98.596 45.671 1.00 96.17 C ANISOU 535 CG1 ILE A 81 10978 10062 15500 1811 -862 939 C ATOM 536 CG2 ILE A 81 -3.493 100.201 45.547 1.00100.86 C ANISOU 536 CG2 ILE A 81 11162 10466 16695 2073 -962 988 C ATOM 537 CD1 ILE A 81 -2.152 97.215 46.001 1.00100.97 C ANISOU 537 CD1 ILE A 81 11356 10668 16341 1719 -738 900 C ATOM 538 N LEU A 82 -2.437 102.400 48.077 1.00101.32 N ANISOU 538 N LEU A 82 11672 10369 16458 2309 -298 941 N ATOM 539 CA LEU A 82 -3.193 103.528 48.621 1.00104.27 C ANISOU 539 CA LEU A 82 11946 10598 17072 2498 -166 932 C ATOM 540 C LEU A 82 -2.357 104.811 48.739 1.00107.60 C ANISOU 540 C LEU A 82 12657 10941 17285 2565 -201 913 C ATOM 541 O LEU A 82 -2.868 105.885 48.412 1.00108.82 O ANISOU 541 O LEU A 82 12748 10969 17631 2696 -303 949 O ATOM 542 CB LEU A 82 -3.794 103.152 49.984 1.00106.10 C ANISOU 542 CB LEU A 82 12074 10796 17444 2578 261 877 C ATOM 543 CG LEU A 82 -5.272 102.724 49.976 1.00114.50 C ANISOU 543 CG LEU A 82 12706 11801 18997 2634 355 907 C ATOM 544 CD1 LEU A 82 -5.458 101.300 49.452 1.00114.20 C ANISOU 544 CD1 LEU A 82 12484 11850 19056 2458 260 931 C ATOM 545 CD2 LEU A 82 -5.879 102.848 51.363 1.00120.21 C ANISOU 545 CD2 LEU A 82 13371 12443 19861 2779 832 869 C ATOM 546 N SER A 83 -1.089 104.705 49.189 1.00102.32 N ANISOU 546 N SER A 83 12289 10330 16259 2476 -129 852 N ATOM 547 CA SER A 83 -0.181 105.849 49.323 1.00101.90 C ANISOU 547 CA SER A 83 12497 10186 16035 2504 -166 810 C ATOM 548 C SER A 83 0.135 106.456 47.948 1.00106.68 C ANISOU 548 C SER A 83 13152 10753 16627 2455 -482 927 C ATOM 549 O SER A 83 -0.047 107.661 47.764 1.00107.68 O ANISOU 549 O SER A 83 13316 10720 16876 2562 -539 959 O ATOM 550 CB SER A 83 1.107 105.439 50.035 1.00103.09 C ANISOU 550 CB SER A 83 12908 10418 15843 2408 -62 706 C ATOM 551 OG SER A 83 2.088 106.465 50.040 1.00110.06 O ANISOU 551 OG SER A 83 14011 11205 16600 2399 -133 650 O ATOM 552 N ASP A 84 0.574 105.611 46.984 1.00102.39 N ANISOU 552 N ASP A 84 12626 10346 15932 2310 -672 997 N ATOM 553 CA ASP A 84 0.943 106.009 45.625 1.00102.68 C ANISOU 553 CA ASP A 84 12757 10373 15885 2268 -948 1124 C ATOM 554 C ASP A 84 -0.225 106.614 44.841 1.00109.88 C ANISOU 554 C ASP A 84 13495 11191 17062 2416 -1146 1231 C ATOM 555 O ASP A 84 -0.002 107.591 44.125 1.00111.49 O ANISOU 555 O ASP A 84 13830 11286 17244 2472 -1288 1338 O ATOM 556 CB ASP A 84 1.543 104.828 44.853 1.00103.10 C ANISOU 556 CB ASP A 84 12860 10603 15709 2108 -1078 1150 C ATOM 557 CG ASP A 84 2.950 104.438 45.284 1.00113.98 C ANISOU 557 CG ASP A 84 14446 12059 16802 1968 -955 1076 C ATOM 558 OD1 ASP A 84 3.418 104.941 46.338 1.00114.17 O ANISOU 558 OD1 ASP A 84 14556 12020 16804 1991 -766 975 O ATOM 559 OD2 ASP A 84 3.581 103.621 44.574 1.00120.01 O ANISOU 559 OD2 ASP A 84 15286 12945 17368 1849 -1058 1105 O ATOM 560 N ALA A 85 -1.460 106.078 44.996 1.00107.32 N ANISOU 560 N ALA A 85 12871 10892 17013 2487 -1149 1206 N ATOM 561 CA ALA A 85 -2.655 106.605 44.319 1.00109.92 C ANISOU 561 CA ALA A 85 12981 11134 17648 2648 -1362 1284 C ATOM 562 C ALA A 85 -3.239 107.830 45.074 1.00116.36 C ANISOU 562 C ALA A 85 13736 11756 18718 2837 -1201 1266 C ATOM 563 O ALA A 85 -4.301 108.339 44.692 1.00118.65 O ANISOU 563 O ALA A 85 13818 11952 19313 3002 -1347 1320 O ATOM 564 CB ALA A 85 -3.707 105.512 44.180 1.00111.61 C ANISOU 564 CB ALA A 85 12855 11435 18117 2635 -1432 1242 C ATOM 565 N LYS A 86 -2.516 108.304 46.127 1.00111.87 N ANISOU 565 N LYS A 86 13357 11124 18023 2823 -921 1176 N ATOM 566 CA LYS A 86 -2.832 109.433 47.014 1.00113.09 C ANISOU 566 CA LYS A 86 13527 11092 18352 2990 -724 1113 C ATOM 567 C LYS A 86 -4.244 109.271 47.610 1.00119.73 C ANISOU 567 C LYS A 86 14024 11898 19570 3147 -569 1067 C ATOM 568 O LYS A 86 -5.169 109.998 47.243 1.00122.14 O ANISOU 568 O LYS A 86 14149 12076 20184 3320 -681 1124 O ATOM 569 CB LYS A 86 -2.653 110.781 46.294 1.00116.53 C ANISOU 569 CB LYS A 86 14109 11339 18825 3086 -909 1221 C ATOM 570 N LEU A 87 -4.406 108.271 48.502 1.00115.68 N ANISOU 570 N LEU A 87 13414 11494 19047 3089 -303 977 N ATOM 571 CA LEU A 87 -5.679 107.955 49.161 1.00142.06 C ANISOU 571 CA LEU A 87 16420 14807 22751 3209 -69 938 C ATOM 572 C LEU A 87 -5.469 107.667 50.649 1.00168.34 C ANISOU 572 C LEU A 87 19869 18148 25944 3234 369 819 C ATOM 573 O LEU A 87 -6.375 107.872 51.456 1.00130.48 O ANISOU 573 O LEU A 87 14904 13269 21403 3397 663 772 O ATOM 574 CB LEU A 87 -6.369 106.756 48.480 1.00142.34 C ANISOU 574 CB LEU A 87 16139 14960 22985 3107 -218 990 C ATOM 575 CG LEU A 87 -6.991 107.009 47.104 1.00148.40 C ANISOU 575 CG LEU A 87 16719 15709 23956 3145 -662 1086 C ATOM 576 CD1 LEU A 87 -6.975 105.756 46.264 1.00147.60 C ANISOU 576 CD1 LEU A 87 16497 15760 23825 2971 -888 1102 C ATOM 577 CD2 LEU A 87 -8.407 107.553 47.224 1.00154.96 C ANISOU 577 CD2 LEU A 87 17176 16403 25298 3360 -655 1090 C ATOM 578 N LEU A 92 -0.966 107.824 62.251 1.00145.80 N ANISOU 578 N LEU A 92 19875 15381 20140 4273 2657 -498 N ATOM 579 CA LEU A 92 -0.835 108.715 61.099 1.00144.28 C ANISOU 579 CA LEU A 92 19472 15081 20268 4128 2302 -494 C ATOM 580 C LEU A 92 -0.694 107.925 59.784 1.00145.52 C ANISOU 580 C LEU A 92 19342 15343 20606 3840 2051 -280 C ATOM 581 O LEU A 92 -0.350 106.739 59.805 1.00143.19 O ANISOU 581 O LEU A 92 19075 15204 20125 3726 2071 -192 O ATOM 582 CB LEU A 92 0.370 109.663 61.279 1.00143.87 C ANISOU 582 CB LEU A 92 19716 14946 20004 4123 1992 -735 C ATOM 583 CG LEU A 92 0.189 110.839 62.246 1.00151.91 C ANISOU 583 CG LEU A 92 20981 15793 20944 4396 2127 -989 C ATOM 584 CD1 LEU A 92 1.500 111.199 62.914 1.00151.98 C ANISOU 584 CD1 LEU A 92 21365 15792 20590 4409 1879 -1262 C ATOM 585 CD2 LEU A 92 -0.383 112.060 61.538 1.00155.60 C ANISOU 585 CD2 LEU A 92 21240 16041 21839 4431 2056 -987 C ATOM 586 N ARG A 93 -0.969 108.596 58.642 1.00141.91 N ANISOU 586 N ARG A 93 18634 14791 20495 3743 1813 -199 N ATOM 587 CA ARG A 93 -0.876 108.031 57.291 1.00139.19 C ANISOU 587 CA ARG A 93 18044 14528 20314 3501 1541 -14 C ATOM 588 C ARG A 93 0.586 107.818 56.876 1.00140.39 C ANISOU 588 C ARG A 93 18394 14765 20182 3304 1235 -57 C ATOM 589 O ARG A 93 0.874 106.891 56.116 1.00137.74 O ANISOU 589 O ARG A 93 17957 14563 19816 3118 1100 69 O ATOM 590 CB ARG A 93 -1.580 108.946 56.279 1.00140.22 C ANISOU 590 CB ARG A 93 17917 14517 20844 3509 1369 74 C ATOM 591 N THR A 94 1.498 108.683 57.365 1.00137.23 N ANISOU 591 N THR A 94 18259 14275 19605 3347 1125 -250 N ATOM 592 CA THR A 94 2.937 108.614 57.088 1.00134.83 C ANISOU 592 CA THR A 94 18126 14023 19081 3176 851 -325 C ATOM 593 C THR A 94 3.599 107.532 57.950 1.00137.46 C ANISOU 593 C THR A 94 18657 14529 19042 3181 931 -397 C ATOM 594 O THR A 94 4.577 106.926 57.514 1.00134.64 O ANISOU 594 O THR A 94 18334 14280 18543 3008 736 -378 O ATOM 595 CB THR A 94 3.614 109.976 57.321 1.00145.65 C ANISOU 595 CB THR A 94 19673 15201 20467 3221 705 -527 C ATOM 596 OG1 THR A 94 3.461 110.354 58.690 1.00148.94 O ANISOU 596 OG1 THR A 94 20315 15560 20717 3458 901 -743 O ATOM 597 CG2 THR A 94 3.083 111.077 56.398 1.00145.34 C ANISOU 597 CG2 THR A 94 19469 14965 20788 3211 602 -434 C ATOM 598 N PHE A 95 3.076 107.309 59.175 1.00136.03 N ANISOU 598 N PHE A 95 18623 14363 18698 3398 1230 -475 N ATOM 599 CA PHE A 95 3.584 106.323 60.133 1.00135.81 C ANISOU 599 CA PHE A 95 18836 14480 18287 3466 1344 -530 C ATOM 600 C PHE A 95 3.323 104.884 59.664 1.00136.91 C ANISOU 600 C PHE A 95 18809 14773 18439 3332 1433 -304 C ATOM 601 O PHE A 95 4.199 104.035 59.835 1.00134.54 O ANISOU 601 O PHE A 95 18649 14597 17872 3264 1340 -313 O ATOM 602 CB PHE A 95 2.967 106.550 61.531 1.00141.21 C ANISOU 602 CB PHE A 95 19751 15116 18786 3769 1684 -652 C ATOM 603 CG PHE A 95 3.266 105.473 62.553 1.00143.65 C ANISOU 603 CG PHE A 95 20331 15564 18684 3888 1870 -657 C ATOM 604 CD1 PHE A 95 4.526 105.369 63.133 1.00146.65 C ANISOU 604 CD1 PHE A 95 21029 16010 18683 3925 1647 -846 C ATOM 605 CD2 PHE A 95 2.286 104.561 62.934 1.00147.17 C ANISOU 605 CD2 PHE A 95 20711 16060 19146 3974 2270 -471 C ATOM 606 CE1 PHE A 95 4.804 104.366 64.070 1.00148.57 C ANISOU 606 CE1 PHE A 95 21551 16376 18522 4066 1800 -836 C ATOM 607 CE2 PHE A 95 2.566 103.558 63.870 1.00151.00 C ANISOU 607 CE2 PHE A 95 21479 16654 19241 4098 2466 -444 C ATOM 608 CZ PHE A 95 3.821 103.470 64.433 1.00148.82 C ANISOU 608 CZ PHE A 95 21549 16450 18544 4155 2222 -622 C ATOM 609 N VAL A 96 2.118 104.603 59.117 1.00133.64 N ANISOU 609 N VAL A 96 18091 14336 18351 3305 1604 -119 N ATOM 610 CA VAL A 96 1.757 103.262 58.639 1.00131.99 C ANISOU 610 CA VAL A 96 17689 14237 18225 3172 1686 78 C ATOM 611 C VAL A 96 2.597 102.903 57.414 1.00132.04 C ANISOU 611 C VAL A 96 17598 14323 18248 2919 1322 136 C ATOM 612 O VAL A 96 3.083 101.778 57.349 1.00130.49 O ANISOU 612 O VAL A 96 17434 14242 17905 2819 1309 201 O ATOM 613 CB VAL A 96 0.243 103.022 58.383 1.00137.69 C ANISOU 613 CB VAL A 96 18072 14899 19344 3202 1938 234 C ATOM 614 CG1 VAL A 96 -0.510 102.825 59.693 1.00140.58 C ANISOU 614 CG1 VAL A 96 18545 15229 19641 3431 2409 231 C ATOM 615 CG2 VAL A 96 -0.392 104.130 57.540 1.00138.19 C ANISOU 615 CG2 VAL A 96 17894 14840 19772 3202 1782 239 C ATOM 616 N CYS A 97 2.834 103.865 56.490 1.00126.92 N ANISOU 616 N CYS A 97 16862 13603 17757 2830 1049 114 N ATOM 617 CA CYS A 97 3.649 103.619 55.299 1.00123.93 C ANISOU 617 CA CYS A 97 16420 13293 17376 2609 738 176 C ATOM 618 C CYS A 97 5.160 103.798 55.601 1.00123.34 C ANISOU 618 C CYS A 97 16597 13256 17010 2560 563 26 C ATOM 619 O CYS A 97 5.971 103.911 54.679 1.00121.59 O ANISOU 619 O CYS A 97 16346 13062 16792 2392 325 51 O ATOM 620 CB CYS A 97 3.193 104.470 54.115 1.00124.99 C ANISOU 620 CB CYS A 97 16357 13330 17804 2547 552 261 C ATOM 621 SG CYS A 97 3.561 106.235 54.270 1.00130.84 S ANISOU 621 SG CYS A 97 17228 13873 18612 2643 461 125 S ATOM 622 N GLN A 98 5.528 103.771 56.895 1.00118.23 N ANISOU 622 N GLN A 98 16196 12612 16112 2716 686 -130 N ATOM 623 CA GLN A 98 6.909 103.829 57.371 1.00116.41 C ANISOU 623 CA GLN A 98 16197 12422 15613 2704 511 -305 C ATOM 624 C GLN A 98 7.250 102.508 58.070 1.00116.54 C ANISOU 624 C GLN A 98 16359 12587 15334 2752 612 -288 C ATOM 625 O GLN A 98 8.378 102.027 57.947 1.00114.95 O ANISOU 625 O GLN A 98 16229 12472 14973 2660 421 -338 O ATOM 626 CB GLN A 98 7.143 105.035 58.296 1.00120.32 C ANISOU 626 CB GLN A 98 16893 12785 16040 2872 499 -537 C ATOM 627 CG GLN A 98 8.619 105.384 58.527 1.00144.30 C ANISOU 627 CG GLN A 98 20098 15818 18911 2825 228 -751 C ATOM 628 CD GLN A 98 9.402 105.569 57.244 1.00169.05 C ANISOU 628 CD GLN A 98 23060 18938 22232 2572 -18 -689 C ATOM 629 OE1 GLN A 98 9.211 106.540 56.499 1.00165.69 O ANISOU 629 OE1 GLN A 98 22517 18370 22070 2493 -85 -652 O ATOM 630 NE2 GLN A 98 10.294 104.627 56.953 1.00160.84 N ANISOU 630 NE2 GLN A 98 22016 18040 21057 2454 -136 -664 N ATOM 631 N VAL A 99 6.260 101.919 58.778 1.00111.29 N ANISOU 631 N VAL A 99 15727 11936 14621 2900 929 -205 N ATOM 632 CA VAL A 99 6.360 100.632 59.473 1.00109.64 C ANISOU 632 CA VAL A 99 15669 11836 14155 2970 1094 -141 C ATOM 633 C VAL A 99 6.263 99.497 58.427 1.00107.54 C ANISOU 633 C VAL A 99 15175 11648 14038 2758 1050 51 C ATOM 634 O VAL A 99 7.052 98.551 58.478 1.00105.38 O ANISOU 634 O VAL A 99 15004 11470 13564 2713 969 63 O ATOM 635 CB VAL A 99 5.276 100.497 60.590 1.00116.34 C ANISOU 635 CB VAL A 99 16632 12639 14932 3205 1508 -98 C ATOM 636 CG1 VAL A 99 5.258 99.093 61.197 1.00116.56 C ANISOU 636 CG1 VAL A 99 16803 12751 14733 3266 1728 29 C ATOM 637 CG2 VAL A 99 5.471 101.544 61.684 1.00118.55 C ANISOU 637 CG2 VAL A 99 17198 12850 14994 3443 1537 -321 C ATOM 638 N THR A 100 5.300 99.612 57.481 1.00101.35 N ANISOU 638 N THR A 100 14086 10815 13606 2644 1079 183 N ATOM 639 CA THR A 100 5.041 98.629 56.422 1.00 98.50 C ANISOU 639 CA THR A 100 13496 10508 13421 2454 1016 339 C ATOM 640 C THR A 100 6.206 98.541 55.427 1.00 98.13 C ANISOU 640 C THR A 100 13442 10535 13307 2274 680 306 C ATOM 641 O THR A 100 6.474 97.450 54.925 1.00 96.59 O ANISOU 641 O THR A 100 13199 10416 13084 2159 630 381 O ATOM 642 CB THR A 100 3.718 98.915 55.696 1.00104.53 C ANISOU 642 CB THR A 100 13942 11194 14580 2408 1076 449 C ATOM 643 OG1 THR A 100 3.714 100.254 55.210 1.00100.44 O ANISOU 643 OG1 THR A 100 13372 10602 14190 2417 907 387 O ATOM 644 CG2 THR A 100 2.498 98.664 56.573 1.00105.66 C ANISOU 644 CG2 THR A 100 14015 11269 14863 2551 1463 520 C ATOM 645 N SER A 101 6.915 99.661 55.164 1.00 92.80 N ANISOU 645 N SER A 101 12816 9822 12621 2252 474 196 N ATOM 646 CA SER A 101 8.081 99.667 54.269 1.00 89.88 C ANISOU 646 CA SER A 101 12441 9506 12205 2088 204 169 C ATOM 647 C SER A 101 9.242 98.915 54.913 1.00 90.89 C ANISOU 647 C SER A 101 12755 9729 12049 2108 153 75 C ATOM 648 O SER A 101 10.015 98.280 54.205 1.00 89.01 O ANISOU 648 O SER A 101 12478 9570 11773 1976 14 102 O ATOM 649 CB SER A 101 8.501 101.088 53.917 1.00 94.13 C ANISOU 649 CB SER A 101 12980 9942 12843 2063 48 86 C ATOM 650 OG SER A 101 8.985 101.777 55.057 1.00107.50 O ANISOU 650 OG SER A 101 14865 11576 14404 2201 66 -99 O ATOM 651 N VAL A 102 9.343 98.969 56.258 1.00 87.82 N ANISOU 651 N VAL A 102 12581 9332 11453 2294 265 -35 N ATOM 652 CA VAL A 102 10.355 98.250 57.041 1.00 86.98 C ANISOU 652 CA VAL A 102 12686 9313 11051 2371 207 -128 C ATOM 653 C VAL A 102 10.022 96.753 56.957 1.00 88.88 C ANISOU 653 C VAL A 102 12905 9628 11239 2347 350 35 C ATOM 654 O VAL A 102 10.918 95.957 56.680 1.00 88.42 O ANISOU 654 O VAL A 102 12872 9649 11074 2280 218 30 O ATOM 655 CB VAL A 102 10.475 98.775 58.507 1.00 92.58 C ANISOU 655 CB VAL A 102 13672 9987 11519 2616 273 -296 C ATOM 656 CG1 VAL A 102 11.285 97.824 59.389 1.00 92.87 C ANISOU 656 CG1 VAL A 102 13950 10119 11217 2745 238 -352 C ATOM 657 CG2 VAL A 102 11.088 100.173 58.538 1.00 92.76 C ANISOU 657 CG2 VAL A 102 13716 9921 11608 2612 64 -501 C ATOM 658 N ILE A 103 8.725 96.393 57.106 1.00 84.19 N ANISOU 658 N ILE A 103 12231 8988 10771 2386 620 178 N ATOM 659 CA ILE A 103 8.214 95.020 57.017 1.00 83.25 C ANISOU 659 CA ILE A 103 12055 8890 10688 2348 796 342 C ATOM 660 C ILE A 103 8.511 94.460 55.612 1.00 83.57 C ANISOU 660 C ILE A 103 11884 8975 10895 2120 597 403 C ATOM 661 O ILE A 103 8.919 93.303 55.495 1.00 83.01 O ANISOU 661 O ILE A 103 11845 8950 10747 2074 593 456 O ATOM 662 CB ILE A 103 6.701 94.954 57.392 1.00 88.21 C ANISOU 662 CB ILE A 103 12576 9426 11513 2419 1132 465 C ATOM 663 CG1 ILE A 103 6.504 95.220 58.908 1.00 91.22 C ANISOU 663 CG1 ILE A 103 13242 9777 11641 2680 1394 423 C ATOM 664 CG2 ILE A 103 6.054 93.611 56.985 1.00 88.35 C ANISOU 664 CG2 ILE A 103 12428 9424 11718 2309 1283 637 C ATOM 665 CD1 ILE A 103 5.118 95.720 59.321 1.00101.07 C ANISOU 665 CD1 ILE A 103 14391 10922 13088 2786 1703 475 C ATOM 666 N PHE A 104 8.373 95.299 54.571 1.00 77.21 N ANISOU 666 N PHE A 104 10898 8150 10290 1999 431 391 N ATOM 667 CA PHE A 104 8.651 94.932 53.184 1.00 74.16 C ANISOU 667 CA PHE A 104 10351 7807 10019 1810 236 438 C ATOM 668 C PHE A 104 10.116 94.552 52.975 1.00 75.56 C ANISOU 668 C PHE A 104 10641 8072 9998 1757 58 359 C ATOM 669 O PHE A 104 10.392 93.522 52.359 1.00 73.52 O ANISOU 669 O PHE A 104 10338 7865 9731 1662 7 406 O ATOM 670 CB PHE A 104 8.275 96.069 52.200 1.00 75.00 C ANISOU 670 CB PHE A 104 10306 7867 10326 1737 98 449 C ATOM 671 CG PHE A 104 8.675 95.741 50.779 1.00 74.66 C ANISOU 671 CG PHE A 104 10164 7878 10326 1574 -105 492 C ATOM 672 CD1 PHE A 104 7.916 94.865 50.010 1.00 77.91 C ANISOU 672 CD1 PHE A 104 10425 8299 10880 1494 -119 579 C ATOM 673 CD2 PHE A 104 9.864 96.227 50.244 1.00 75.42 C ANISOU 673 CD2 PHE A 104 10328 8010 10317 1506 -269 434 C ATOM 674 CE1 PHE A 104 8.323 94.507 48.722 1.00 78.00 C ANISOU 674 CE1 PHE A 104 10393 8367 10878 1371 -309 599 C ATOM 675 CE2 PHE A 104 10.272 95.863 48.959 1.00 77.46 C ANISOU 675 CE2 PHE A 104 10532 8323 10575 1377 -412 481 C ATOM 676 CZ PHE A 104 9.490 95.021 48.200 1.00 75.86 C ANISOU 676 CZ PHE A 104 10219 8141 10465 1322 -438 559 C ATOM 677 N TYR A 105 11.045 95.420 53.404 1.00 72.57 N ANISOU 677 N TYR A 105 10380 7697 9497 1810 -49 227 N ATOM 678 CA TYR A 105 12.469 95.166 53.214 1.00 71.90 C ANISOU 678 CA TYR A 105 10354 7684 9281 1761 -223 135 C ATOM 679 C TYR A 105 12.931 93.998 54.073 1.00 77.53 C ANISOU 679 C TYR A 105 11220 8456 9783 1867 -171 120 C ATOM 680 O TYR A 105 13.808 93.262 53.641 1.00 76.34 O ANISOU 680 O TYR A 105 11060 8371 9576 1806 -278 104 O ATOM 681 CB TYR A 105 13.302 96.421 53.472 1.00 73.15 C ANISOU 681 CB TYR A 105 10559 7803 9433 1779 -361 -19 C ATOM 682 CG TYR A 105 13.243 97.418 52.333 1.00 73.34 C ANISOU 682 CG TYR A 105 10438 7765 9662 1640 -442 19 C ATOM 683 CD1 TYR A 105 13.858 97.153 51.113 1.00 74.19 C ANISOU 683 CD1 TYR A 105 10446 7918 9823 1485 -536 76 C ATOM 684 CD2 TYR A 105 12.621 98.650 52.493 1.00 74.44 C ANISOU 684 CD2 TYR A 105 10565 7790 9927 1681 -414 2 C ATOM 685 CE1 TYR A 105 13.802 98.064 50.060 1.00 74.55 C ANISOU 685 CE1 TYR A 105 10403 7901 10021 1380 -587 140 C ATOM 686 CE2 TYR A 105 12.568 99.574 51.452 1.00 75.15 C ANISOU 686 CE2 TYR A 105 10549 7805 10197 1571 -483 62 C ATOM 687 CZ TYR A 105 13.165 99.280 50.238 1.00 82.04 C ANISOU 687 CZ TYR A 105 11346 8728 11099 1423 -567 140 C ATOM 688 OH TYR A 105 13.120 100.195 49.213 1.00 84.03 O ANISOU 688 OH TYR A 105 11535 8897 11494 1336 -613 225 O ATOM 689 N PHE A 106 12.296 93.791 55.248 1.00 76.96 N ANISOU 689 N PHE A 106 11295 8352 9596 2036 14 141 N ATOM 690 CA PHE A 106 12.544 92.669 56.165 1.00 77.93 C ANISOU 690 CA PHE A 106 11608 8507 9497 2173 110 170 C ATOM 691 C PHE A 106 12.220 91.353 55.448 1.00 81.79 C ANISOU 691 C PHE A 106 11989 9000 10088 2059 186 317 C ATOM 692 O PHE A 106 13.046 90.446 55.397 1.00 81.47 O ANISOU 692 O PHE A 106 12013 9008 9936 2063 105 309 O ATOM 693 CB PHE A 106 11.682 92.855 57.440 1.00 81.68 C ANISOU 693 CB PHE A 106 12265 8924 9846 2379 358 199 C ATOM 694 CG PHE A 106 11.267 91.629 58.231 1.00 84.31 C ANISOU 694 CG PHE A 106 12762 9238 10033 2506 605 338 C ATOM 695 CD1 PHE A 106 12.058 91.152 59.270 1.00 87.75 C ANISOU 695 CD1 PHE A 106 13491 9716 10136 2705 571 289 C ATOM 696 CD2 PHE A 106 10.037 91.015 58.002 1.00 86.52 C ANISOU 696 CD2 PHE A 106 12911 9441 10523 2444 880 518 C ATOM 697 CE1 PHE A 106 11.650 90.054 60.032 1.00 90.00 C ANISOU 697 CE1 PHE A 106 13965 9962 10270 2843 832 447 C ATOM 698 CE2 PHE A 106 9.638 89.909 58.754 1.00 90.36 C ANISOU 698 CE2 PHE A 106 13549 9876 10908 2555 1153 666 C ATOM 699 CZ PHE A 106 10.439 89.447 59.775 1.00 89.59 C ANISOU 699 CZ PHE A 106 13777 9816 10449 2759 1144 643 C ATOM 700 N THR A 107 11.032 91.310 54.839 1.00 78.56 N ANISOU 700 N THR A 107 11398 8530 9920 1957 315 431 N ATOM 701 CA THR A 107 10.446 90.188 54.136 1.00 78.26 C ANISOU 701 CA THR A 107 11227 8462 10044 1840 387 550 C ATOM 702 C THR A 107 11.207 89.878 52.812 1.00 82.35 C ANISOU 702 C THR A 107 11632 9046 10613 1674 149 508 C ATOM 703 O THR A 107 11.256 88.706 52.424 1.00 82.43 O ANISOU 703 O THR A 107 11618 9046 10654 1615 159 555 O ATOM 704 CB THR A 107 8.940 90.484 53.975 1.00 85.31 C ANISOU 704 CB THR A 107 11940 9262 11211 1803 567 646 C ATOM 705 OG1 THR A 107 8.154 89.369 54.378 1.00 90.81 O ANISOU 705 OG1 THR A 107 12598 9880 12026 1789 779 768 O ATOM 706 CG2 THR A 107 8.551 91.003 52.621 1.00 80.27 C ANISOU 706 CG2 THR A 107 11073 8629 10799 1656 389 632 C ATOM 707 N MET A 108 11.818 90.889 52.140 1.00 78.43 N ANISOU 707 N MET A 108 11079 8598 10122 1609 -41 422 N ATOM 708 CA MET A 108 12.522 90.616 50.886 1.00 76.80 C ANISOU 708 CA MET A 108 10790 8451 9941 1471 -215 398 C ATOM 709 C MET A 108 13.925 90.058 51.158 1.00 79.20 C ANISOU 709 C MET A 108 11203 8823 10066 1512 -300 316 C ATOM 710 O MET A 108 14.370 89.199 50.395 1.00 78.96 O ANISOU 710 O MET A 108 11138 8826 10036 1439 -355 320 O ATOM 711 CB MET A 108 12.533 91.823 49.920 1.00 78.93 C ANISOU 711 CB MET A 108 10957 8724 10307 1381 -339 381 C ATOM 712 CG MET A 108 13.734 92.743 50.022 1.00 82.85 C ANISOU 712 CG MET A 108 11505 9249 10723 1387 -447 278 C ATOM 713 SD MET A 108 14.478 93.108 48.405 1.00 86.37 S ANISOU 713 SD MET A 108 11866 9739 11214 1232 -580 288 S ATOM 714 CE MET A 108 14.445 94.843 48.428 1.00 83.34 C ANISOU 714 CE MET A 108 11463 9276 10927 1224 -616 264 C ATOM 715 N TYR A 109 14.586 90.473 52.265 1.00 74.86 N ANISOU 715 N TYR A 109 10788 8288 9368 1646 -318 229 N ATOM 716 CA TYR A 109 15.920 89.960 52.606 1.00 73.92 C ANISOU 716 CA TYR A 109 10753 8230 9102 1711 -433 136 C ATOM 717 C TYR A 109 15.817 88.600 53.318 1.00 79.02 C ANISOU 717 C TYR A 109 11539 8862 9624 1828 -328 205 C ATOM 718 O TYR A 109 16.834 87.918 53.452 1.00 80.10 O ANISOU 718 O TYR A 109 11733 9041 9659 1887 -423 152 O ATOM 719 CB TYR A 109 16.772 90.981 53.391 1.00 74.78 C ANISOU 719 CB TYR A 109 10931 8356 9128 1805 -562 -18 C ATOM 720 CG TYR A 109 17.223 92.117 52.499 1.00 75.16 C ANISOU 720 CG TYR A 109 10824 8399 9333 1662 -672 -82 C ATOM 721 CD1 TYR A 109 18.225 91.929 51.549 1.00 76.72 C ANISOU 721 CD1 TYR A 109 10905 8644 9603 1548 -767 -117 C ATOM 722 CD2 TYR A 109 16.574 93.349 52.525 1.00 75.57 C ANISOU 722 CD2 TYR A 109 10850 8383 9482 1640 -644 -85 C ATOM 723 CE1 TYR A 109 18.585 92.945 50.663 1.00 76.78 C ANISOU 723 CE1 TYR A 109 10784 8627 9762 1413 -812 -137 C ATOM 724 CE2 TYR A 109 16.917 94.368 51.638 1.00 76.06 C ANISOU 724 CE2 TYR A 109 10785 8411 9703 1506 -716 -107 C ATOM 725 CZ TYR A 109 17.935 94.167 50.717 1.00 83.54 C ANISOU 725 CZ TYR A 109 11631 9403 10709 1391 -790 -124 C ATOM 726 OH TYR A 109 18.297 95.177 49.854 1.00 85.11 O ANISOU 726 OH TYR A 109 11726 9550 11063 1265 -817 -120 O ATOM 727 N ILE A 110 14.590 88.177 53.702 1.00 74.93 N ANISOU 727 N ILE A 110 11055 8266 9148 1857 -120 334 N ATOM 728 CA ILE A 110 14.328 86.849 54.261 1.00 75.22 C ANISOU 728 CA ILE A 110 11213 8247 9120 1941 34 441 C ATOM 729 C ILE A 110 14.215 85.879 53.068 1.00 77.20 C ANISOU 729 C ILE A 110 11318 8474 9541 1777 11 485 C ATOM 730 O ILE A 110 14.848 84.819 53.077 1.00 76.28 O ANISOU 730 O ILE A 110 11273 8352 9359 1815 -12 491 O ATOM 731 CB ILE A 110 13.094 86.836 55.206 1.00 79.77 C ANISOU 731 CB ILE A 110 11878 8728 9703 2039 310 564 C ATOM 732 CG1 ILE A 110 13.533 87.274 56.606 1.00 81.67 C ANISOU 732 CG1 ILE A 110 12381 8995 9655 2277 332 513 C ATOM 733 CG2 ILE A 110 12.404 85.451 55.267 1.00 80.78 C ANISOU 733 CG2 ILE A 110 12020 8744 9929 2023 526 723 C ATOM 734 CD1 ILE A 110 12.475 87.676 57.477 1.00 91.22 C ANISOU 734 CD1 ILE A 110 13679 10136 10846 2384 588 591 C ATOM 735 N SER A 111 13.444 86.282 52.031 1.00 72.91 N ANISOU 735 N SER A 111 10581 7916 9206 1614 -8 500 N ATOM 736 CA SER A 111 13.250 85.544 50.783 1.00 72.29 C ANISOU 736 CA SER A 111 10369 7818 9278 1461 -71 507 C ATOM 737 C SER A 111 14.602 85.280 50.113 1.00 74.54 C ANISOU 737 C SER A 111 10673 8194 9456 1439 -241 408 C ATOM 738 O SER A 111 14.881 84.135 49.764 1.00 75.40 O ANISOU 738 O SER A 111 10798 8273 9576 1420 -245 407 O ATOM 739 CB SER A 111 12.331 86.318 49.839 1.00 76.85 C ANISOU 739 CB SER A 111 10768 8389 10042 1334 -126 514 C ATOM 740 OG SER A 111 11.010 86.427 50.345 1.00 88.53 O ANISOU 740 OG SER A 111 12177 9772 11687 1346 40 602 O ATOM 741 N ILE A 112 15.458 86.326 49.988 1.00 68.89 N ANISOU 741 N ILE A 112 9948 7569 8658 1446 -362 322 N ATOM 742 CA ILE A 112 16.817 86.244 49.421 1.00 67.30 C ANISOU 742 CA ILE A 112 9730 7450 8389 1429 -490 225 C ATOM 743 C ILE A 112 17.627 85.214 50.243 1.00 72.65 C ANISOU 743 C ILE A 112 10528 8126 8950 1568 -489 200 C ATOM 744 O ILE A 112 18.318 84.387 49.658 1.00 72.22 O ANISOU 744 O ILE A 112 10455 8090 8894 1553 -533 162 O ATOM 745 CB ILE A 112 17.502 87.664 49.368 1.00 68.92 C ANISOU 745 CB ILE A 112 9886 7713 8589 1412 -584 147 C ATOM 746 CG1 ILE A 112 16.859 88.559 48.282 1.00 67.62 C ANISOU 746 CG1 ILE A 112 9617 7542 8533 1277 -596 190 C ATOM 747 CG2 ILE A 112 19.032 87.585 49.172 1.00 68.38 C ANISOU 747 CG2 ILE A 112 9785 7713 8483 1428 -686 36 C ATOM 748 CD1 ILE A 112 17.149 90.005 48.363 1.00 69.62 C ANISOU 748 CD1 ILE A 112 9835 7794 8825 1260 -639 153 C ATOM 749 N SER A 113 17.487 85.234 51.584 1.00 70.76 N ANISOU 749 N SER A 113 10429 7856 8599 1723 -434 227 N ATOM 750 CA SER A 113 18.202 84.326 52.480 1.00 71.97 C ANISOU 750 CA SER A 113 10738 8000 8606 1897 -448 222 C ATOM 751 C SER A 113 17.777 82.861 52.288 1.00 77.02 C ANISOU 751 C SER A 113 11426 8543 9294 1893 -327 326 C ATOM 752 O SER A 113 18.652 81.994 52.212 1.00 77.01 O ANISOU 752 O SER A 113 11467 8545 9248 1961 -392 293 O ATOM 753 CB SER A 113 18.018 84.748 53.932 1.00 76.34 C ANISOU 753 CB SER A 113 11478 8541 8988 2085 -407 238 C ATOM 754 OG SER A 113 18.595 86.026 54.144 1.00 83.36 O ANISOU 754 OG SER A 113 12327 9502 9844 2101 -559 101 O ATOM 755 N PHE A 114 16.456 82.588 52.184 1.00 74.36 N ANISOU 755 N PHE A 114 11063 8104 9085 1810 -157 442 N ATOM 756 CA PHE A 114 15.940 81.226 51.996 1.00 75.19 C ANISOU 756 CA PHE A 114 11191 8077 9301 1778 -32 534 C ATOM 757 C PHE A 114 16.177 80.722 50.573 1.00 78.16 C ANISOU 757 C PHE A 114 11427 8461 9809 1624 -141 453 C ATOM 758 O PHE A 114 16.386 79.523 50.392 1.00 77.86 O ANISOU 758 O PHE A 114 11434 8336 9812 1638 -116 465 O ATOM 759 CB PHE A 114 14.451 81.119 52.360 1.00 78.29 C ANISOU 759 CB PHE A 114 11561 8339 9848 1731 192 671 C ATOM 760 CG PHE A 114 14.210 81.028 53.847 1.00 81.90 C ANISOU 760 CG PHE A 114 12231 8736 10152 1924 387 792 C ATOM 761 CD1 PHE A 114 14.534 79.874 54.551 1.00 87.05 C ANISOU 761 CD1 PHE A 114 13077 9285 10713 2061 497 892 C ATOM 762 CD2 PHE A 114 13.665 82.096 54.546 1.00 84.65 C ANISOU 762 CD2 PHE A 114 12613 9120 10429 1988 469 810 C ATOM 763 CE1 PHE A 114 14.340 79.803 55.933 1.00 90.09 C ANISOU 763 CE1 PHE A 114 13711 9618 10902 2271 688 1020 C ATOM 764 CE2 PHE A 114 13.469 82.022 55.928 1.00 89.47 C ANISOU 764 CE2 PHE A 114 13465 9682 10847 2196 662 916 C ATOM 765 CZ PHE A 114 13.818 80.882 56.614 1.00 89.27 C ANISOU 765 CZ PHE A 114 13654 9567 10696 2341 771 1026 C ATOM 766 N LEU A 115 16.158 81.625 49.573 1.00 74.61 N ANISOU 766 N LEU A 115 10834 8106 9409 1496 -256 374 N ATOM 767 CA LEU A 115 16.408 81.267 48.178 1.00 74.93 C ANISOU 767 CA LEU A 115 10783 8172 9515 1376 -359 291 C ATOM 768 C LEU A 115 17.842 80.766 48.018 1.00 78.83 C ANISOU 768 C LEU A 115 11326 8729 9898 1455 -435 202 C ATOM 769 O LEU A 115 18.063 79.796 47.287 1.00 78.86 O ANISOU 769 O LEU A 115 11330 8691 9943 1425 -451 154 O ATOM 770 CB LEU A 115 16.110 82.442 47.226 1.00 74.70 C ANISOU 770 CB LEU A 115 10637 8229 9517 1259 -449 254 C ATOM 771 CG LEU A 115 14.960 82.250 46.199 1.00 80.44 C ANISOU 771 CG LEU A 115 11268 8895 10400 1125 -484 260 C ATOM 772 CD1 LEU A 115 13.719 81.598 46.829 1.00 82.12 C ANISOU 772 CD1 LEU A 115 11446 8955 10799 1111 -360 348 C ATOM 773 CD2 LEU A 115 14.565 83.582 45.565 1.00 81.10 C ANISOU 773 CD2 LEU A 115 11271 9055 10488 1059 -568 262 C ATOM 774 N GLY A 116 18.775 81.382 48.757 1.00 74.89 N ANISOU 774 N GLY A 116 10860 8315 9280 1567 -484 168 N ATOM 775 CA GLY A 116 20.179 80.985 48.809 1.00 74.81 C ANISOU 775 CA GLY A 116 10861 8362 9200 1669 -566 78 C ATOM 776 C GLY A 116 20.336 79.596 49.408 1.00 79.63 C ANISOU 776 C GLY A 116 11602 8869 9786 1802 -520 122 C ATOM 777 O GLY A 116 21.131 78.798 48.911 1.00 79.35 O ANISOU 777 O GLY A 116 11555 8830 9766 1839 -558 55 O ATOM 778 N LEU A 117 19.541 79.289 50.466 1.00 77.16 N ANISOU 778 N LEU A 117 11423 8453 9440 1882 -412 248 N ATOM 779 CA LEU A 117 19.512 77.984 51.135 1.00 78.16 C ANISOU 779 CA LEU A 117 11709 8441 9546 2013 -324 339 C ATOM 780 C LEU A 117 18.899 76.921 50.221 1.00 82.47 C ANISOU 780 C LEU A 117 12212 8849 10274 1884 -245 355 C ATOM 781 O LEU A 117 19.398 75.796 50.193 1.00 83.83 O ANISOU 781 O LEU A 117 12458 8930 10463 1965 -241 350 O ATOM 782 CB LEU A 117 18.740 78.030 52.472 1.00 79.20 C ANISOU 782 CB LEU A 117 12015 8491 9588 2131 -175 494 C ATOM 783 CG LEU A 117 19.309 78.876 53.626 1.00 84.25 C ANISOU 783 CG LEU A 117 12776 9235 10000 2319 -261 473 C ATOM 784 CD1 LEU A 117 18.444 78.742 54.869 1.00 85.61 C ANISOU 784 CD1 LEU A 117 13164 9307 10057 2450 -60 642 C ATOM 785 CD2 LEU A 117 20.747 78.495 53.968 1.00 87.12 C ANISOU 785 CD2 LEU A 117 13206 9659 10236 2509 -448 384 C ATOM 786 N ILE A 118 17.826 77.275 49.483 1.00 77.95 N ANISOU 786 N ILE A 118 11519 8251 9848 1695 -206 358 N ATOM 787 CA ILE A 118 17.132 76.396 48.529 1.00 78.33 C ANISOU 787 CA ILE A 118 11501 8167 10092 1554 -182 332 C ATOM 788 C ILE A 118 18.109 76.021 47.396 1.00 82.49 C ANISOU 788 C ILE A 118 11993 8764 10585 1538 -314 173 C ATOM 789 O ILE A 118 18.162 74.848 47.007 1.00 84.57 O ANISOU 789 O ILE A 118 12296 8895 10941 1536 -300 134 O ATOM 790 CB ILE A 118 15.817 77.071 48.014 1.00 80.99 C ANISOU 790 CB ILE A 118 11696 8494 10584 1380 -170 346 C ATOM 791 CG1 ILE A 118 14.689 76.917 49.054 1.00 82.12 C ANISOU 791 CG1 ILE A 118 11860 8489 10852 1389 32 510 C ATOM 792 CG2 ILE A 118 15.365 76.527 46.645 1.00 82.84 C ANISOU 792 CG2 ILE A 118 11832 8667 10978 1228 -267 234 C ATOM 793 CD1 ILE A 118 13.602 77.946 48.989 1.00 87.75 C ANISOU 793 CD1 ILE A 118 12434 9235 11673 1289 55 541 C ATOM 794 N THR A 119 18.907 77.008 46.915 1.00 76.36 N ANISOU 794 N THR A 119 11149 8176 9688 1535 -418 85 N ATOM 795 CA THR A 119 19.927 76.832 45.877 1.00 75.40 C ANISOU 795 CA THR A 119 10990 8142 9518 1535 -496 -54 C ATOM 796 C THR A 119 20.949 75.767 46.340 1.00 80.76 C ANISOU 796 C THR A 119 11748 8765 10174 1702 -488 -82 C ATOM 797 O THR A 119 21.144 74.786 45.620 1.00 81.88 O ANISOU 797 O THR A 119 11911 8835 10366 1701 -487 -164 O ATOM 798 CB THR A 119 20.597 78.190 45.530 1.00 75.88 C ANISOU 798 CB THR A 119 10956 8389 9486 1508 -554 -101 C ATOM 799 OG1 THR A 119 19.612 79.108 45.052 1.00 72.44 O ANISOU 799 OG1 THR A 119 10467 7982 9075 1374 -567 -62 O ATOM 800 CG2 THR A 119 21.681 78.068 44.477 1.00 71.23 C ANISOU 800 CG2 THR A 119 10321 7886 8855 1511 -576 -224 C ATOM 801 N ILE A 120 21.563 75.946 47.542 1.00 76.42 N ANISOU 801 N ILE A 120 11252 8241 9544 1861 -499 -22 N ATOM 802 CA ILE A 120 22.565 75.030 48.110 1.00 77.17 C ANISOU 802 CA ILE A 120 11425 8289 9607 2057 -526 -37 C ATOM 803 C ILE A 120 21.981 73.620 48.216 1.00 83.72 C ANISOU 803 C ILE A 120 12383 8895 10530 2084 -431 34 C ATOM 804 O ILE A 120 22.630 72.668 47.775 1.00 85.08 O ANISOU 804 O ILE A 120 12574 9002 10751 2153 -445 -43 O ATOM 805 CB ILE A 120 23.128 75.523 49.481 1.00 80.29 C ANISOU 805 CB ILE A 120 11887 8747 9875 2240 -596 16 C ATOM 806 CG1 ILE A 120 23.864 76.878 49.338 1.00 79.08 C ANISOU 806 CG1 ILE A 120 11575 8785 9687 2210 -712 -93 C ATOM 807 CG2 ILE A 120 24.061 74.470 50.111 1.00 82.41 C ANISOU 807 CG2 ILE A 120 12265 8940 10106 2476 -646 23 C ATOM 808 CD1 ILE A 120 24.213 77.592 50.643 1.00 83.44 C ANISOU 808 CD1 ILE A 120 12184 9400 10119 2356 -816 -77 C ATOM 809 N ASP A 121 20.754 73.495 48.763 1.00 80.70 N ANISOU 809 N ASP A 121 12075 8382 10207 2022 -316 175 N ATOM 810 CA ASP A 121 20.050 72.219 48.924 1.00 82.38 C ANISOU 810 CA ASP A 121 12391 8342 10567 2015 -189 264 C ATOM 811 C ASP A 121 19.885 71.512 47.574 1.00 87.61 C ANISOU 811 C ASP A 121 12977 8922 11388 1877 -223 118 C ATOM 812 O ASP A 121 20.226 70.336 47.465 1.00 88.24 O ANISOU 812 O ASP A 121 13137 8841 11547 1951 -200 92 O ATOM 813 CB ASP A 121 18.685 72.433 49.595 1.00 84.52 C ANISOU 813 CB ASP A 121 12689 8502 10921 1931 -31 429 C ATOM 814 CG ASP A 121 17.861 71.174 49.739 1.00 95.93 C ANISOU 814 CG ASP A 121 14203 9656 12589 1887 134 531 C ATOM 815 OD1 ASP A 121 17.970 70.511 50.794 1.00 99.38 O ANISOU 815 OD1 ASP A 121 14825 9951 12983 2051 266 693 O ATOM 816 OD2 ASP A 121 17.107 70.853 48.801 1.00100.68 O ANISOU 816 OD2 ASP A 121 14682 10160 13414 1695 126 448 O ATOM 817 N ARG A 122 19.404 72.240 46.550 1.00 84.55 N ANISOU 817 N ARG A 122 12456 8640 11027 1700 -292 16 N ATOM 818 CA ARG A 122 19.199 71.700 45.209 1.00 85.64 C ANISOU 818 CA ARG A 122 12549 8725 11263 1582 -358 -147 C ATOM 819 C ARG A 122 20.522 71.271 44.550 1.00 92.56 C ANISOU 819 C ARG A 122 13451 9676 12041 1693 -415 -297 C ATOM 820 O ARG A 122 20.551 70.205 43.933 1.00 94.20 O ANISOU 820 O ARG A 122 13709 9740 12344 1691 -422 -405 O ATOM 821 CB ARG A 122 18.439 72.705 44.331 1.00 83.11 C ANISOU 821 CB ARG A 122 12113 8528 10938 1411 -441 -206 C ATOM 822 CG ARG A 122 17.025 72.248 43.992 1.00 87.23 C ANISOU 822 CG ARG A 122 12582 8866 11694 1251 -451 -218 C ATOM 823 CD ARG A 122 16.226 71.899 45.231 1.00 92.79 C ANISOU 823 CD ARG A 122 13287 9399 12570 1244 -293 -29 C ATOM 824 NE ARG A 122 15.368 70.733 45.032 1.00101.82 N ANISOU 824 NE ARG A 122 14415 10260 14011 1149 -246 -46 N ATOM 825 CZ ARG A 122 15.502 69.573 45.671 1.00113.32 C ANISOU 825 CZ ARG A 122 15982 11493 15582 1227 -111 31 C ATOM 826 NH1 ARG A 122 16.460 69.411 46.576 1.00 98.66 N ANISOU 826 NH1 ARG A 122 14272 9679 13537 1423 -33 135 N ATOM 827 NH2 ARG A 122 14.671 68.570 45.419 1.00 97.45 N ANISOU 827 NH2 ARG A 122 13933 9200 13892 1113 -67 5 N ATOM 828 N TYR A 123 21.615 72.058 44.727 1.00 89.03 N ANISOU 828 N TYR A 123 12959 9432 11436 1795 -447 -311 N ATOM 829 CA TYR A 123 22.949 71.752 44.196 1.00 89.87 C ANISOU 829 CA TYR A 123 13046 9616 11483 1913 -470 -443 C ATOM 830 C TYR A 123 23.492 70.470 44.831 1.00 96.69 C ANISOU 830 C TYR A 123 14012 10309 12418 2092 -441 -422 C ATOM 831 O TYR A 123 24.118 69.660 44.146 1.00 97.81 O ANISOU 831 O TYR A 123 14171 10397 12597 2159 -436 -552 O ATOM 832 CB TYR A 123 23.922 72.928 44.431 1.00 90.38 C ANISOU 832 CB TYR A 123 12996 9907 11437 1967 -505 -449 C ATOM 833 CG TYR A 123 25.388 72.553 44.318 1.00 93.99 C ANISOU 833 CG TYR A 123 13398 10420 11895 2131 -511 -551 C ATOM 834 CD1 TYR A 123 25.969 72.288 43.080 1.00 96.88 C ANISOU 834 CD1 TYR A 123 13726 10826 12258 2120 -463 -701 C ATOM 835 CD2 TYR A 123 26.186 72.436 45.452 1.00 95.63 C ANISOU 835 CD2 TYR A 123 13593 10634 12106 2317 -569 -506 C ATOM 836 CE1 TYR A 123 27.306 71.910 42.973 1.00 98.86 C ANISOU 836 CE1 TYR A 123 13897 11116 12548 2280 -440 -798 C ATOM 837 CE2 TYR A 123 27.527 72.066 45.358 1.00 98.10 C ANISOU 837 CE2 TYR A 123 13818 10990 12467 2479 -593 -610 C ATOM 838 CZ TYR A 123 28.083 71.803 44.116 1.00107.89 C ANISOU 838 CZ TYR A 123 14989 12264 13743 2454 -513 -754 C ATOM 839 OH TYR A 123 29.405 71.439 44.018 1.00113.44 O ANISOU 839 OH TYR A 123 15573 13001 14526 2621 -510 -859 O ATOM 840 N GLN A 124 23.255 70.297 46.143 1.00 94.24 N ANISOU 840 N GLN A 124 13787 9906 12113 2187 -413 -254 N ATOM 841 CA GLN A 124 23.689 69.134 46.910 1.00 95.89 C ANISOU 841 CA GLN A 124 14132 9934 12370 2382 -383 -184 C ATOM 842 C GLN A 124 22.978 67.870 46.430 1.00102.32 C ANISOU 842 C GLN A 124 15034 10475 13368 2310 -304 -203 C ATOM 843 O GLN A 124 23.561 66.792 46.487 1.00103.58 O ANISOU 843 O GLN A 124 15279 10480 13594 2456 -291 -230 O ATOM 844 CB GLN A 124 23.457 69.363 48.407 1.00 97.41 C ANISOU 844 CB GLN A 124 14440 10097 12474 2504 -356 22 C ATOM 845 CG GLN A 124 24.509 70.274 49.046 1.00108.45 C ANISOU 845 CG GLN A 124 15785 11712 13707 2665 -487 2 C ATOM 846 CD GLN A 124 24.494 70.270 50.561 1.00130.86 C ANISOU 846 CD GLN A 124 18803 14508 16411 2858 -492 179 C ATOM 847 OE1 GLN A 124 23.983 69.349 51.221 1.00130.55 O ANISOU 847 OE1 GLN A 124 18961 14253 16390 2943 -375 342 O ATOM 848 NE2 GLN A 124 25.114 71.282 51.151 1.00118.56 N ANISOU 848 NE2 GLN A 124 17194 13143 14709 2949 -627 148 N ATOM 849 N LYS A 125 21.744 68.009 45.919 1.00100.01 N ANISOU 849 N LYS A 125 14704 10112 13181 2090 -271 -208 N ATOM 850 CA LYS A 125 20.964 66.894 45.391 1.00102.29 C ANISOU 850 CA LYS A 125 15039 10130 13695 1984 -226 -262 C ATOM 851 C LYS A 125 21.416 66.521 43.971 1.00109.51 C ANISOU 851 C LYS A 125 15923 11072 14612 1951 -317 -520 C ATOM 852 O LYS A 125 21.228 65.371 43.575 1.00111.55 O ANISOU 852 O LYS A 125 16254 11091 15039 1947 -303 -610 O ATOM 853 CB LYS A 125 19.461 67.211 45.434 1.00104.39 C ANISOU 853 CB LYS A 125 15240 10310 14114 1768 -182 -187 C ATOM 854 CG LYS A 125 18.725 66.597 46.641 1.00122.70 C ANISOU 854 CG LYS A 125 17650 12371 16598 1787 -1 46 C ATOM 855 CD LYS A 125 19.153 67.169 48.017 1.00131.88 C ANISOU 855 CD LYS A 125 18911 13643 17554 1966 81 263 C ATOM 856 CE LYS A 125 18.164 66.902 49.132 1.00142.47 C ANISOU 856 CE LYS A 125 20345 14768 19018 1961 303 513 C ATOM 857 NZ LYS A 125 18.216 65.496 49.619 1.00152.25 N ANISOU 857 NZ LYS A 125 21756 15688 20404 2071 438 625 N ATOM 858 N THR A 126 22.031 67.466 43.217 1.00106.62 N ANISOU 858 N THR A 126 15469 10981 14060 1938 -391 -638 N ATOM 859 CA THR A 126 22.545 67.200 41.862 1.00107.93 C ANISOU 859 CA THR A 126 15638 11201 14168 1939 -440 -873 C ATOM 860 C THR A 126 23.888 66.460 41.949 1.00116.89 C ANISOU 860 C THR A 126 16813 12310 15289 2161 -397 -939 C ATOM 861 O THR A 126 24.211 65.676 41.053 1.00118.17 O ANISOU 861 O THR A 126 17035 12382 15481 2201 -396 -1124 O ATOM 862 CB THR A 126 22.666 68.477 41.001 1.00108.95 C ANISOU 862 CB THR A 126 15682 11612 14104 1853 -488 -942 C ATOM 863 OG1 THR A 126 23.744 69.294 41.462 1.00107.29 O ANISOU 863 OG1 THR A 126 15385 11607 13774 1959 -452 -870 O ATOM 864 CG2 THR A 126 21.358 69.265 40.891 1.00102.89 C ANISOU 864 CG2 THR A 126 14867 10869 13356 1656 -554 -887 C ATOM 865 N THR A 127 24.659 66.706 43.033 1.00115.97 N ANISOU 865 N THR A 127 16666 12267 15131 2319 -378 -803 N ATOM 866 CA THR A 127 25.955 66.062 43.303 1.00118.50 C ANISOU 866 CA THR A 127 16992 12565 15466 2559 -366 -846 C ATOM 867 C THR A 127 25.747 64.640 43.856 1.00127.47 C ANISOU 867 C THR A 127 18286 13379 16769 2666 -330 -787 C ATOM 868 O THR A 127 26.669 63.827 43.818 1.00129.13 O ANISOU 868 O THR A 127 18528 13501 17035 2855 -321 -867 O ATOM 869 CB THR A 127 26.799 66.907 44.274 1.00125.84 C ANISOU 869 CB THR A 127 17825 13684 16306 2694 -413 -739 C ATOM 870 OG1 THR A 127 26.091 67.068 45.503 1.00123.62 O ANISOU 870 OG1 THR A 127 17628 13332 16010 2693 -424 -528 O ATOM 871 CG2 THR A 127 27.179 68.270 43.699 1.00123.88 C ANISOU 871 CG2 THR A 127 17404 13722 15944 2599 -428 -809 C ATOM 872 N ARG A 128 24.540 64.361 44.379 1.00126.48 N ANISOU 872 N ARG A 128 18249 13064 16745 2550 -292 -638 N ATOM 873 CA ARG A 128 24.107 63.078 44.939 1.00129.81 C ANISOU 873 CA ARG A 128 18826 13136 17359 2608 -216 -539 C ATOM 874 C ARG A 128 23.475 62.202 43.825 1.00138.48 C ANISOU 874 C ARG A 128 19956 14014 18648 2461 -215 -735 C ATOM 875 O ARG A 128 22.932 62.778 42.874 1.00136.85 O ANISOU 875 O ARG A 128 19666 13931 18401 2275 -278 -881 O ATOM 876 CB ARG A 128 23.093 63.336 46.072 1.00129.64 C ANISOU 876 CB ARG A 128 18865 13020 17372 2538 -133 -276 C ATOM 877 CG ARG A 128 23.345 62.531 47.344 1.00142.12 C ANISOU 877 CG ARG A 128 20628 14396 18975 2764 -49 -51 C ATOM 878 CD ARG A 128 22.436 62.942 48.493 1.00152.51 C ANISOU 878 CD ARG A 128 22025 15661 20262 2724 72 219 C ATOM 879 NE ARG A 128 21.027 62.613 48.253 1.00160.01 N ANISOU 879 NE ARG A 128 22957 16372 21469 2477 206 263 N ATOM 880 CZ ARG A 128 20.054 62.782 49.144 1.00171.48 C ANISOU 880 CZ ARG A 128 24464 17714 22976 2413 374 497 C ATOM 881 NH1 ARG A 128 20.323 63.271 50.349 1.00159.38 N ANISOU 881 NH1 ARG A 128 23055 16293 21209 2592 428 708 N ATOM 882 NH2 ARG A 128 18.804 62.458 48.838 1.00154.93 N ANISOU 882 NH2 ARG A 128 22296 15389 21180 2176 492 510 N ATOM 883 N PRO A 129 23.506 60.835 43.907 1.00140.30 N ANISOU 883 N PRO A 129 20314 13908 19085 2547 -160 -753 N ATOM 884 CA PRO A 129 22.895 60.011 42.837 1.00142.88 C ANISOU 884 CA PRO A 129 20671 14008 19610 2403 -190 -979 C ATOM 885 C PRO A 129 21.414 60.325 42.589 1.00149.18 C ANISOU 885 C PRO A 129 21399 14727 20556 2115 -213 -974 C ATOM 886 O PRO A 129 20.709 60.725 43.520 1.00148.54 O ANISOU 886 O PRO A 129 21290 14619 20529 2042 -130 -734 O ATOM 887 CB PRO A 129 23.069 58.573 43.344 1.00147.48 C ANISOU 887 CB PRO A 129 21406 14202 20426 2547 -102 -922 C ATOM 888 CG PRO A 129 23.355 58.697 44.801 1.00151.40 C ANISOU 888 CG PRO A 129 21973 14690 20862 2712 -10 -599 C ATOM 889 CD PRO A 129 24.114 59.974 44.941 1.00143.97 C ANISOU 889 CD PRO A 129 20918 14171 19614 2790 -88 -580 C ATOM 890 N PHE A 130 20.955 60.161 41.325 1.00147.96 N ANISOU 890 N PHE A 130 21218 14542 20460 1968 -334 -1250 N ATOM 891 CA PHE A 130 19.583 60.465 40.893 1.00148.38 C ANISOU 891 CA PHE A 130 21173 14534 20672 1703 -420 -1307 C ATOM 892 C PHE A 130 18.543 59.566 41.569 1.00154.91 C ANISOU 892 C PHE A 130 22000 14949 21911 1580 -320 -1181 C ATOM 893 O PHE A 130 18.751 58.359 41.680 1.00157.03 O ANISOU 893 O PHE A 130 22380 14898 22388 1656 -253 -1210 O ATOM 894 CB PHE A 130 19.441 60.381 39.363 1.00151.36 C ANISOU 894 CB PHE A 130 21563 14958 20990 1626 -612 -1661 C ATOM 895 CG PHE A 130 18.272 61.179 38.833 1.00152.52 C ANISOU 895 CG PHE A 130 21586 15205 21162 1401 -765 -1725 C ATOM 896 CD1 PHE A 130 18.367 62.557 38.665 1.00153.10 C ANISOU 896 CD1 PHE A 130 21584 15647 20941 1385 -808 -1658 C ATOM 897 CD2 PHE A 130 17.070 60.556 38.520 1.00157.24 C ANISOU 897 CD2 PHE A 130 22127 15510 22109 1210 -876 -1855 C ATOM 898 CE1 PHE A 130 17.278 63.298 38.195 1.00153.77 C ANISOU 898 CE1 PHE A 130 21556 15814 21055 1201 -963 -1707 C ATOM 899 CE2 PHE A 130 15.982 61.298 38.047 1.00159.94 C ANISOU 899 CE2 PHE A 130 22328 15944 22499 1020 -1049 -1921 C ATOM 900 CZ PHE A 130 16.094 62.664 37.888 1.00155.37 C ANISOU 900 CZ PHE A 130 21694 15740 21599 1028 -1093 -1841 C ATOM 901 N LYS A 131 17.423 60.184 42.016 1.00151.02 N ANISOU 901 N LYS A 131 21373 14454 21555 1391 -289 -1033 N ATOM 902 CA LYS A 131 16.283 59.575 42.715 1.00153.07 C ANISOU 902 CA LYS A 131 21576 14349 22234 1238 -145 -874 C ATOM 903 C LYS A 131 16.741 58.909 44.032 1.00157.91 C ANISOU 903 C LYS A 131 22347 14762 22889 1417 115 -566 C ATOM 904 O LYS A 131 16.913 57.687 44.098 1.00160.25 O ANISOU 904 O LYS A 131 22762 14717 23410 1477 188 -585 O ATOM 905 CB LYS A 131 15.511 58.590 41.812 1.00158.93 C ANISOU 905 CB LYS A 131 22271 14747 23369 1063 -270 -1146 C ATOM 906 N THR A 132 16.974 59.746 45.066 1.00152.26 N ANISOU 906 N THR A 132 21655 14264 21933 1522 239 -291 N ATOM 907 CA THR A 132 17.403 59.356 46.417 1.00177.24 C ANISOU 907 CA THR A 132 25001 17307 25035 1730 462 27 C ATOM 908 C THR A 132 16.716 60.255 47.450 1.00199.02 C ANISOU 908 C THR A 132 27725 20174 27720 1694 628 310 C ATOM 909 O THR A 132 16.525 59.858 48.598 1.00159.32 O ANISOU 909 O THR A 132 22839 14936 22760 1785 874 602 O ATOM 910 CB THR A 132 18.937 59.416 46.567 1.00183.30 C ANISOU 910 CB THR A 132 25902 18297 25447 2026 374 5 C ATOM 911 OG1 THR A 132 19.440 60.610 45.966 1.00180.70 O ANISOU 911 OG1 THR A 132 25448 18385 24823 2013 189 -163 O ATOM 912 CG2 THR A 132 19.642 58.192 45.993 1.00183.27 C ANISOU 912 CG2 THR A 132 26010 18054 25571 2147 332 -157 C ATOM 913 N LYS A 136 18.806 63.806 58.677 1.00144.72 N ANISOU 913 N LYS A 136 22799 14092 18095 3768 1568 2468 N ATOM 914 CA LYS A 136 19.585 64.169 59.863 1.00145.65 C ANISOU 914 CA LYS A 136 23248 14368 17724 4158 1450 2579 C ATOM 915 C LYS A 136 19.661 65.699 60.046 1.00145.40 C ANISOU 915 C LYS A 136 23111 14712 17423 4149 1264 2421 C ATOM 916 O LYS A 136 19.913 66.170 61.159 1.00146.92 O ANISOU 916 O LYS A 136 23591 15019 17212 4434 1236 2530 O ATOM 917 CB LYS A 136 21.001 63.554 59.805 1.00149.21 C ANISOU 917 CB LYS A 136 23794 14843 18056 4429 1128 2483 C ATOM 918 CG LYS A 136 21.837 63.935 58.570 1.00159.28 C ANISOU 918 CG LYS A 136 24696 16347 19477 4281 768 2111 C ATOM 919 CD LYS A 136 23.123 63.109 58.458 1.00169.05 C ANISOU 919 CD LYS A 136 26004 17549 20679 4547 516 2036 C ATOM 920 CE LYS A 136 24.267 63.665 59.275 1.00177.66 C ANISOU 920 CE LYS A 136 27221 18901 21382 4893 189 1979 C ATOM 921 NZ LYS A 136 25.486 62.825 59.157 1.00185.34 N ANISOU 921 NZ LYS A 136 28234 19820 22367 5165 -54 1910 N ATOM 922 N ASN A 137 19.425 66.461 58.958 1.00136.13 N ANISOU 922 N ASN A 137 21546 13712 16465 3833 1136 2165 N ATOM 923 CA ASN A 137 19.478 67.922 58.939 1.00132.06 C ANISOU 923 CA ASN A 137 20884 13523 15771 3778 960 1995 C ATOM 924 C ASN A 137 18.101 68.587 59.192 1.00131.87 C ANISOU 924 C ASN A 137 20813 13472 15820 3598 1265 2111 C ATOM 925 O ASN A 137 18.019 69.818 59.139 1.00129.58 O ANISOU 925 O ASN A 137 20398 13423 15414 3536 1148 1977 O ATOM 926 CB ASN A 137 20.035 68.403 57.589 1.00131.44 C ANISOU 926 CB ASN A 137 20427 13638 15878 3557 665 1672 C ATOM 927 CG ASN A 137 21.455 67.996 57.283 1.00160.66 C ANISOU 927 CG ASN A 137 24107 17424 19512 3731 353 1513 C ATOM 928 OD1 ASN A 137 22.408 68.404 57.955 1.00158.66 O ANISOU 928 OD1 ASN A 137 23985 17328 18972 4001 132 1477 O ATOM 929 ND2 ASN A 137 21.633 67.252 56.202 1.00151.74 N ANISOU 929 ND2 ASN A 137 22785 16206 18662 3575 311 1382 N ATOM 930 N LEU A 138 17.038 67.797 59.465 1.00127.49 N ANISOU 930 N LEU A 138 20344 12613 15486 3515 1662 2357 N ATOM 931 CA LEU A 138 15.678 68.307 59.699 1.00126.43 C ANISOU 931 CA LEU A 138 20130 12411 15498 3343 2000 2482 C ATOM 932 C LEU A 138 15.593 69.247 60.915 1.00130.08 C ANISOU 932 C LEU A 138 20850 13037 15538 3579 2088 2586 C ATOM 933 O LEU A 138 14.874 70.247 60.843 1.00128.84 O ANISOU 933 O LEU A 138 20524 12996 15432 3435 2165 2529 O ATOM 934 CB LEU A 138 14.671 67.166 59.854 1.00129.36 C ANISOU 934 CB LEU A 138 20558 12387 16208 3246 2430 2745 C ATOM 935 N LEU A 139 16.321 68.945 62.011 1.00127.79 N ANISOU 935 N LEU A 139 20977 12754 14826 3956 2058 2725 N ATOM 936 CA LEU A 139 16.342 69.788 63.215 1.00128.39 C ANISOU 936 CA LEU A 139 21359 12986 14438 4229 2101 2799 C ATOM 937 C LEU A 139 17.218 71.023 62.981 1.00128.12 C ANISOU 937 C LEU A 139 21182 13306 14190 4261 1636 2475 C ATOM 938 O LEU A 139 16.859 72.116 63.414 1.00126.71 O ANISOU 938 O LEU A 139 21021 13283 13839 4281 1659 2418 O ATOM 939 CB LEU A 139 16.829 69.007 64.442 1.00132.58 C ANISOU 939 CB LEU A 139 22416 13392 14566 4646 2202 3056 C ATOM 940 N GLY A 140 18.335 70.830 62.276 1.00122.72 N ANISOU 940 N GLY A 140 20345 12725 13559 4257 1243 2264 N ATOM 941 CA GLY A 140 19.289 71.877 61.916 1.00119.85 C ANISOU 941 CA GLY A 140 19793 12662 13084 4258 802 1951 C ATOM 942 C GLY A 140 18.721 72.924 60.980 1.00119.83 C ANISOU 942 C GLY A 140 19401 12791 13337 3916 780 1767 C ATOM 943 O GLY A 140 18.987 74.116 61.158 1.00118.93 O ANISOU 943 O GLY A 140 19230 12892 13066 3939 580 1596 O ATOM 944 N ALA A 141 17.912 72.487 59.988 1.00113.80 N ANISOU 944 N ALA A 141 18379 11883 12977 3605 976 1800 N ATOM 945 CA ALA A 141 17.236 73.358 59.021 1.00109.83 C ANISOU 945 CA ALA A 141 17517 11472 12741 3282 968 1654 C ATOM 946 C ALA A 141 16.188 74.223 59.712 1.00112.47 C ANISOU 946 C ALA A 141 17908 11822 13002 3276 1216 1754 C ATOM 947 O ALA A 141 15.965 75.356 59.294 1.00110.31 O ANISOU 947 O ALA A 141 17419 11703 12791 3128 1115 1603 O ATOM 948 CB ALA A 141 16.582 72.525 57.933 1.00109.99 C ANISOU 948 CB ALA A 141 17298 11306 13186 3002 1095 1669 C ATOM 949 N LYS A 142 15.561 73.693 60.778 1.00111.03 N ANISOU 949 N LYS A 142 18029 11470 12686 3452 1560 2016 N ATOM 950 CA LYS A 142 14.556 74.382 61.592 1.00111.57 C ANISOU 950 CA LYS A 142 18204 11528 12659 3499 1867 2142 C ATOM 951 C LYS A 142 15.195 75.522 62.397 1.00114.28 C ANISOU 951 C LYS A 142 18745 12109 12566 3739 1644 2008 C ATOM 952 O LYS A 142 14.633 76.613 62.440 1.00112.78 O ANISOU 952 O LYS A 142 18439 12023 12390 3660 1679 1922 O ATOM 953 CB LYS A 142 13.849 73.390 62.536 1.00117.46 C ANISOU 953 CB LYS A 142 19255 12007 13366 3648 2333 2481 C ATOM 954 CG LYS A 142 12.351 73.239 62.275 1.00125.60 C ANISOU 954 CG LYS A 142 20055 12834 14833 3390 2759 2628 C ATOM 955 CD LYS A 142 12.001 71.977 61.481 1.00132.98 C ANISOU 955 CD LYS A 142 20790 13510 16225 3162 2858 2697 C ATOM 956 CE LYS A 142 11.750 70.768 62.355 1.00141.49 C ANISOU 956 CE LYS A 142 22189 14286 17287 3323 3256 3026 C ATOM 957 NZ LYS A 142 11.261 69.607 61.567 1.00147.33 N ANISOU 957 NZ LYS A 142 22706 14740 18534 3075 3356 3070 N ATOM 958 N ILE A 143 16.371 75.267 63.017 1.00111.74 N ANISOU 958 N ILE A 143 18712 11862 11883 4036 1393 1975 N ATOM 959 CA ILE A 143 17.131 76.232 63.827 1.00111.97 C ANISOU 959 CA ILE A 143 18948 12100 11494 4297 1107 1814 C ATOM 960 C ILE A 143 17.670 77.349 62.922 1.00111.45 C ANISOU 960 C ILE A 143 18512 12243 11589 4089 738 1494 C ATOM 961 O ILE A 143 17.570 78.528 63.277 1.00110.30 O ANISOU 961 O ILE A 143 18375 12227 11305 4123 658 1362 O ATOM 962 CB ILE A 143 18.283 75.529 64.629 1.00117.77 C ANISOU 962 CB ILE A 143 20039 12842 11866 4662 876 1845 C ATOM 963 CG1 ILE A 143 17.796 74.329 65.503 1.00122.12 C ANISOU 963 CG1 ILE A 143 21002 13156 12244 4889 1265 2204 C ATOM 964 CG2 ILE A 143 19.136 76.521 65.441 1.00119.45 C ANISOU 964 CG2 ILE A 143 20437 13272 11675 4933 496 1625 C ATOM 965 CD1 ILE A 143 16.612 74.573 66.521 1.00132.65 C ANISOU 965 CD1 ILE A 143 22645 14398 13359 5020 1740 2438 C ATOM 966 N LEU A 144 18.234 76.965 61.752 1.00105.10 N ANISOU 966 N LEU A 144 17400 11454 11079 3881 538 1378 N ATOM 967 CA LEU A 144 18.799 77.870 60.752 1.00101.44 C ANISOU 967 CA LEU A 144 16583 11160 10799 3671 233 1109 C ATOM 968 C LEU A 144 17.733 78.857 60.283 1.00102.66 C ANISOU 968 C LEU A 144 16521 11338 11148 3429 391 1084 C ATOM 969 O LEU A 144 18.013 80.054 60.196 1.00101.50 O ANISOU 969 O LEU A 144 16266 11336 10963 3394 197 899 O ATOM 970 CB LEU A 144 19.367 77.052 59.578 1.00 99.95 C ANISOU 970 CB LEU A 144 16149 10939 10887 3502 110 1049 C ATOM 971 CG LEU A 144 20.114 77.779 58.451 1.00102.21 C ANISOU 971 CG LEU A 144 16086 11382 11368 3294 -165 801 C ATOM 972 CD1 LEU A 144 21.297 78.591 58.975 1.00103.00 C ANISOU 972 CD1 LEU A 144 16204 11656 11277 3461 -506 596 C ATOM 973 CD2 LEU A 144 20.625 76.780 57.441 1.00104.24 C ANISOU 973 CD2 LEU A 144 16182 11582 11843 3185 -221 771 C ATOM 974 N SER A 145 16.495 78.359 60.063 1.00 97.86 N ANISOU 974 N SER A 145 15856 10567 10760 3280 744 1272 N ATOM 975 CA SER A 145 15.332 79.152 59.668 1.00 95.66 C ANISOU 975 CA SER A 145 15367 10280 10701 3072 922 1277 C ATOM 976 C SER A 145 14.935 80.131 60.785 1.00 99.48 C ANISOU 976 C SER A 145 16058 10820 10919 3256 1031 1286 C ATOM 977 O SER A 145 14.679 81.296 60.489 1.00 97.19 O ANISOU 977 O SER A 145 15598 10627 10701 3151 947 1151 O ATOM 978 CB SER A 145 14.162 78.242 59.305 1.00 99.07 C ANISOU 978 CB SER A 145 15694 10499 11450 2906 1265 1474 C ATOM 979 OG SER A 145 14.478 77.441 58.178 1.00102.69 O ANISOU 979 OG SER A 145 15947 10904 12166 2721 1136 1420 O ATOM 980 N VAL A 146 14.924 79.669 62.061 1.00 98.83 N ANISOU 980 N VAL A 146 16367 10673 10510 3550 1213 1441 N ATOM 981 CA VAL A 146 14.610 80.479 63.253 1.00100.82 C ANISOU 981 CA VAL A 146 16903 10973 10431 3788 1334 1451 C ATOM 982 C VAL A 146 15.614 81.645 63.347 1.00103.96 C ANISOU 982 C VAL A 146 17297 11573 10631 3871 902 1156 C ATOM 983 O VAL A 146 15.197 82.793 63.525 1.00103.49 O ANISOU 983 O VAL A 146 17200 11575 10547 3858 913 1049 O ATOM 984 CB VAL A 146 14.589 79.620 64.555 1.00108.56 C ANISOU 984 CB VAL A 146 18362 11846 11040 4127 1584 1681 C ATOM 985 CG1 VAL A 146 14.694 80.483 65.812 1.00110.80 C ANISOU 985 CG1 VAL A 146 19009 12223 10868 4439 1592 1624 C ATOM 986 CG2 VAL A 146 13.348 78.736 64.617 1.00109.97 C ANISOU 986 CG2 VAL A 146 18534 11790 11459 4032 2105 1986 C ATOM 987 N VAL A 147 16.924 81.340 63.177 1.00 99.76 N ANISOU 987 N VAL A 147 16772 11126 10009 3943 527 1021 N ATOM 988 CA VAL A 147 18.040 82.293 63.217 1.00 98.57 C ANISOU 988 CA VAL A 147 16571 11141 9739 4007 88 730 C ATOM 989 C VAL A 147 17.844 83.393 62.142 1.00 98.59 C ANISOU 989 C VAL A 147 16178 11209 10072 3696 -8 564 C ATOM 990 O VAL A 147 17.985 84.568 62.480 1.00 97.94 O ANISOU 990 O VAL A 147 16109 11204 9899 3743 -157 386 O ATOM 991 CB VAL A 147 19.411 81.566 63.101 1.00102.38 C ANISOU 991 CB VAL A 147 17062 11673 10167 4113 -249 644 C ATOM 992 CG1 VAL A 147 20.534 82.510 62.670 1.00100.91 C ANISOU 992 CG1 VAL A 147 16638 11635 10069 4048 -683 332 C ATOM 993 CG2 VAL A 147 19.768 80.881 64.415 1.00105.69 C ANISOU 993 CG2 VAL A 147 17942 12059 10156 4508 -260 751 C ATOM 994 N ILE A 148 17.470 83.023 60.891 1.00 92.50 N ANISOU 994 N ILE A 148 15087 10392 9667 3399 83 625 N ATOM 995 CA ILE A 148 17.220 83.995 59.811 1.00 89.64 C ANISOU 995 CA ILE A 148 14381 10079 9598 3121 11 506 C ATOM 996 C ILE A 148 16.131 84.998 60.252 1.00 94.25 C ANISOU 996 C ILE A 148 14997 10637 10176 3122 212 529 C ATOM 997 O ILE A 148 16.395 86.203 60.254 1.00 94.42 O ANISOU 997 O ILE A 148 14952 10730 10192 3105 39 353 O ATOM 998 CB ILE A 148 16.859 83.334 58.433 1.00 90.56 C ANISOU 998 CB ILE A 148 14210 10141 10058 2842 85 582 C ATOM 999 CG1 ILE A 148 17.966 82.382 57.884 1.00 90.34 C ANISOU 999 CG1 ILE A 148 14132 10135 10058 2838 -105 536 C ATOM 1000 CG2 ILE A 148 16.408 84.374 57.377 1.00 89.12 C ANISOU 1000 CG2 ILE A 148 13726 9998 10136 2588 43 498 C ATOM 1001 CD1 ILE A 148 19.404 82.979 57.650 1.00 98.38 C ANISOU 1001 CD1 ILE A 148 15046 11292 11044 2861 -465 305 C ATOM 1002 N TRP A 149 14.935 84.502 60.649 1.00 90.40 N ANISOU 1002 N TRP A 149 14600 10031 9716 3145 587 742 N ATOM 1003 CA TRP A 149 13.795 85.335 61.058 1.00 90.31 C ANISOU 1003 CA TRP A 149 14597 9977 9739 3156 840 786 C ATOM 1004 C TRP A 149 14.099 86.224 62.281 1.00 96.70 C ANISOU 1004 C TRP A 149 15711 10849 10184 3430 778 665 C ATOM 1005 O TRP A 149 13.776 87.415 62.254 1.00 95.38 O ANISOU 1005 O TRP A 149 15461 10706 10075 3395 757 548 O ATOM 1006 CB TRP A 149 12.568 84.463 61.348 1.00 90.00 C ANISOU 1006 CB TRP A 149 14602 9783 9812 3154 1281 1048 C ATOM 1007 CG TRP A 149 11.894 83.914 60.127 1.00 88.50 C ANISOU 1007 CG TRP A 149 14061 9509 10056 2858 1359 1129 C ATOM 1008 CD1 TRP A 149 12.075 82.681 59.575 1.00 90.82 C ANISOU 1008 CD1 TRP A 149 14288 9728 10493 2757 1358 1214 C ATOM 1009 CD2 TRP A 149 10.856 84.544 59.369 1.00 87.05 C ANISOU 1009 CD2 TRP A 149 13565 9292 10219 2651 1448 1125 C ATOM 1010 NE1 TRP A 149 11.236 82.515 58.500 1.00 88.75 N ANISOU 1010 NE1 TRP A 149 13694 9392 10636 2493 1418 1243 N ATOM 1011 CE2 TRP A 149 10.472 83.642 58.352 1.00 89.63 C ANISOU 1011 CE2 TRP A 149 13646 9533 10878 2428 1465 1194 C ATOM 1012 CE3 TRP A 149 10.203 85.785 59.453 1.00 88.11 C ANISOU 1012 CE3 TRP A 149 13606 9452 10421 2646 1500 1062 C ATOM 1013 CZ2 TRP A 149 9.484 83.951 57.412 1.00 88.00 C ANISOU 1013 CZ2 TRP A 149 13104 9279 11054 2208 1496 1193 C ATOM 1014 CZ3 TRP A 149 9.237 86.094 58.512 1.00 88.46 C ANISOU 1014 CZ3 TRP A 149 13309 9445 10855 2430 1547 1079 C ATOM 1015 CH2 TRP A 149 8.880 85.180 57.511 1.00 88.17 C ANISOU 1015 CH2 TRP A 149 13033 9336 11131 2218 1532 1143 C ATOM 1016 N ALA A 150 14.726 85.652 63.335 1.00 96.35 N ANISOU 1016 N ALA A 150 16030 10821 9759 3716 732 685 N ATOM 1017 CA ALA A 150 15.075 86.365 64.571 1.00 98.76 C ANISOU 1017 CA ALA A 150 16685 11184 9656 4023 636 553 C ATOM 1018 C ALA A 150 16.087 87.489 64.323 1.00102.81 C ANISOU 1018 C ALA A 150 17074 11811 10178 3988 180 232 C ATOM 1019 O ALA A 150 15.910 88.587 64.853 1.00104.09 O ANISOU 1019 O ALA A 150 17345 11993 10213 4093 136 77 O ATOM 1020 CB ALA A 150 15.621 85.395 65.604 1.00102.20 C ANISOU 1020 CB ALA A 150 17535 11611 9684 4342 641 654 C ATOM 1021 N PHE A 151 17.126 87.225 63.508 1.00 98.00 N ANISOU 1021 N PHE A 151 16231 11261 9746 3839 -136 128 N ATOM 1022 CA PHE A 151 18.170 88.197 63.180 1.00 97.58 C ANISOU 1022 CA PHE A 151 16007 11291 9778 3773 -546 -162 C ATOM 1023 C PHE A 151 17.606 89.369 62.377 1.00100.27 C ANISOU 1023 C PHE A 151 16060 11609 10428 3522 -503 -236 C ATOM 1024 O PHE A 151 17.977 90.514 62.640 1.00100.54 O ANISOU 1024 O PHE A 151 16096 11661 10442 3557 -705 -457 O ATOM 1025 CB PHE A 151 19.311 87.522 62.405 1.00 98.13 C ANISOU 1025 CB PHE A 151 15868 11412 10005 3665 -811 -216 C ATOM 1026 CG PHE A 151 20.445 88.433 62.000 1.00 99.38 C ANISOU 1026 CG PHE A 151 15805 11638 10318 3578 -1200 -499 C ATOM 1027 CD1 PHE A 151 20.580 88.858 60.681 1.00 99.48 C ANISOU 1027 CD1 PHE A 151 15438 11653 10707 3266 -1233 -534 C ATOM 1028 CD2 PHE A 151 21.383 88.861 62.934 1.00104.35 C ANISOU 1028 CD2 PHE A 151 16608 12316 10724 3814 -1532 -733 C ATOM 1029 CE1 PHE A 151 21.644 89.679 60.300 1.00100.37 C ANISOU 1029 CE1 PHE A 151 15333 11803 11000 3175 -1544 -773 C ATOM 1030 CE2 PHE A 151 22.437 89.697 62.556 1.00107.31 C ANISOU 1030 CE2 PHE A 151 16735 12727 11313 3712 -1884 -1004 C ATOM 1031 CZ PHE A 151 22.558 90.102 61.241 1.00102.69 C ANISOU 1031 CZ PHE A 151 15758 12129 11130 3385 -1862 -1011 C ATOM 1032 N MET A 152 16.721 89.082 61.404 1.00 94.90 N ANISOU 1032 N MET A 152 15141 10877 10039 3282 -259 -57 N ATOM 1033 CA MET A 152 16.099 90.096 60.555 1.00 92.95 C ANISOU 1033 CA MET A 152 14624 10600 10091 3056 -212 -86 C ATOM 1034 C MET A 152 15.166 90.982 61.350 1.00 98.86 C ANISOU 1034 C MET A 152 15519 11296 10746 3182 -22 -101 C ATOM 1035 O MET A 152 15.223 92.198 61.182 1.00 97.39 O ANISOU 1035 O MET A 152 15230 11099 10675 3118 -144 -255 O ATOM 1036 CB MET A 152 15.351 89.463 59.379 1.00 93.15 C ANISOU 1036 CB MET A 152 14393 10585 10415 2812 -29 102 C ATOM 1037 CG MET A 152 16.263 88.857 58.356 1.00 94.96 C ANISOU 1037 CG MET A 152 14435 10864 10780 2654 -225 77 C ATOM 1038 SD MET A 152 17.376 90.027 57.566 1.00 97.78 S ANISOU 1038 SD MET A 152 14570 11283 11297 2506 -555 -149 S ATOM 1039 CE MET A 152 18.175 88.921 56.432 1.00 93.21 C ANISOU 1039 CE MET A 152 13821 10751 10842 2365 -647 -109 C ATOM 1040 N PHE A 153 14.331 90.377 62.231 1.00 98.75 N ANISOU 1040 N PHE A 153 15753 11235 10533 3367 296 63 N ATOM 1041 CA PHE A 153 13.384 91.073 63.110 1.00100.91 C ANISOU 1041 CA PHE A 153 16205 11454 10683 3531 550 71 C ATOM 1042 C PHE A 153 14.121 92.034 64.037 1.00107.11 C ANISOU 1042 C PHE A 153 17241 12281 11173 3752 297 -195 C ATOM 1043 O PHE A 153 13.697 93.181 64.180 1.00107.02 O ANISOU 1043 O PHE A 153 17207 12231 11224 3762 313 -319 O ATOM 1044 CB PHE A 153 12.556 90.062 63.930 1.00104.94 C ANISOU 1044 CB PHE A 153 16959 11901 11011 3706 963 317 C ATOM 1045 CG PHE A 153 11.647 90.684 64.964 1.00109.32 C ANISOU 1045 CG PHE A 153 17752 12402 11381 3927 1281 338 C ATOM 1046 CD1 PHE A 153 10.452 91.291 64.591 1.00112.16 C ANISOU 1046 CD1 PHE A 153 17885 12685 12046 3807 1552 406 C ATOM 1047 CD2 PHE A 153 11.984 90.664 66.311 1.00114.54 C ANISOU 1047 CD2 PHE A 153 18877 13088 11554 4277 1313 290 C ATOM 1048 CE1 PHE A 153 9.613 91.872 65.548 1.00115.79 C ANISOU 1048 CE1 PHE A 153 18557 13090 12350 4025 1879 422 C ATOM 1049 CE2 PHE A 153 11.147 91.247 67.266 1.00120.29 C ANISOU 1049 CE2 PHE A 153 19856 13767 12083 4502 1639 306 C ATOM 1050 CZ PHE A 153 9.965 91.841 66.879 1.00117.92 C ANISOU 1050 CZ PHE A 153 19304 13386 12114 4371 1939 373 C ATOM 1051 N LEU A 154 15.227 91.563 64.646 1.00105.78 N ANISOU 1051 N LEU A 154 17302 12183 10707 3934 38 -297 N ATOM 1052 CA LEU A 154 16.053 92.341 65.559 1.00108.68 C ANISOU 1052 CA LEU A 154 17917 12591 10783 4164 -276 -582 C ATOM 1053 C LEU A 154 16.702 93.540 64.855 1.00111.43 C ANISOU 1053 C LEU A 154 17975 12937 11426 3964 -616 -845 C ATOM 1054 O LEU A 154 16.655 94.638 65.411 1.00112.70 O ANISOU 1054 O LEU A 154 18255 13063 11503 4074 -714 -1058 O ATOM 1055 CB LEU A 154 17.117 91.458 66.234 1.00110.85 C ANISOU 1055 CB LEU A 154 18452 12941 10726 4392 -520 -622 C ATOM 1056 CG LEU A 154 16.873 91.145 67.726 1.00120.75 C ANISOU 1056 CG LEU A 154 20241 14199 11438 4804 -386 -588 C ATOM 1057 CD1 LEU A 154 15.770 90.096 67.920 1.00121.81 C ANISOU 1057 CD1 LEU A 154 20522 14267 11494 4856 146 -217 C ATOM 1058 CD2 LEU A 154 18.150 90.664 68.401 1.00126.19 C ANISOU 1058 CD2 LEU A 154 21177 14969 11799 5056 -793 -734 C ATOM 1059 N LEU A 155 17.250 93.363 63.629 1.00105.54 N ANISOU 1059 N LEU A 155 16861 12208 11029 3674 -762 -826 N ATOM 1060 CA LEU A 155 17.873 94.487 62.919 1.00104.42 C ANISOU 1060 CA LEU A 155 16445 12040 11190 3475 -1031 -1040 C ATOM 1061 C LEU A 155 16.800 95.426 62.287 1.00107.41 C ANISOU 1061 C LEU A 155 16644 12326 11839 3303 -809 -973 C ATOM 1062 O LEU A 155 17.102 96.597 62.058 1.00107.87 O ANISOU 1062 O LEU A 155 16590 12321 12075 3221 -978 -1161 O ATOM 1063 CB LEU A 155 18.961 94.041 61.910 1.00102.43 C ANISOU 1063 CB LEU A 155 15898 11837 11184 3264 -1260 -1061 C ATOM 1064 CG LEU A 155 18.585 93.646 60.488 1.00104.35 C ANISOU 1064 CG LEU A 155 15851 12080 11717 2988 -1076 -835 C ATOM 1065 CD1 LEU A 155 19.186 94.597 59.514 1.00103.10 C ANISOU 1065 CD1 LEU A 155 15382 11882 11910 2732 -1200 -924 C ATOM 1066 CD2 LEU A 155 19.168 92.316 60.138 1.00107.34 C ANISOU 1066 CD2 LEU A 155 16189 12532 12065 2980 -1151 -759 C ATOM 1067 N SER A 156 15.544 94.944 62.102 1.00102.68 N ANISOU 1067 N SER A 156 16027 11702 11283 3270 -440 -716 N ATOM 1068 CA SER A 156 14.412 95.746 61.607 1.00101.48 C ANISOU 1068 CA SER A 156 15713 11463 11382 3151 -224 -637 C ATOM 1069 C SER A 156 13.786 96.605 62.715 1.00108.79 C ANISOU 1069 C SER A 156 16888 12325 12123 3385 -86 -743 C ATOM 1070 O SER A 156 13.354 97.724 62.442 1.00108.45 O ANISOU 1070 O SER A 156 16727 12195 12285 3318 -65 -812 O ATOM 1071 CB SER A 156 13.324 94.851 61.026 1.00102.58 C ANISOU 1071 CB SER A 156 15711 11592 11671 3039 91 -350 C ATOM 1072 OG SER A 156 13.700 94.309 59.775 1.00109.05 O ANISOU 1072 OG SER A 156 16279 12453 12702 2805 -26 -267 O ATOM 1073 N LEU A 157 13.702 96.050 63.950 1.00108.02 N ANISOU 1073 N LEU A 157 17153 12261 11628 3674 31 -740 N ATOM 1074 CA LEU A 157 13.094 96.635 65.148 1.00111.12 C ANISOU 1074 CA LEU A 157 17863 12607 11750 3955 216 -823 C ATOM 1075 C LEU A 157 13.475 98.122 65.394 1.00116.37 C ANISOU 1075 C LEU A 157 18558 13205 12455 3995 -38 -1141 C ATOM 1076 O LEU A 157 12.539 98.912 65.511 1.00116.54 O ANISOU 1076 O LEU A 157 18574 13135 12570 4037 184 -1143 O ATOM 1077 CB LEU A 157 13.420 95.782 66.385 1.00114.11 C ANISOU 1077 CB LEU A 157 18677 13052 11627 4276 264 -808 C ATOM 1078 CG LEU A 157 12.540 95.977 67.622 1.00122.53 C ANISOU 1078 CG LEU A 157 20125 14077 12352 4597 609 -788 C ATOM 1079 CD1 LEU A 157 11.152 95.361 67.423 1.00122.53 C ANISOU 1079 CD1 LEU A 157 20021 14020 12516 4545 1152 -457 C ATOM 1080 CD2 LEU A 157 13.198 95.365 68.848 1.00127.85 C ANISOU 1080 CD2 LEU A 157 21286 14824 12468 4947 514 -851 C ATOM 1081 N PRO A 158 14.764 98.572 65.441 1.00113.70 N ANISOU 1081 N PRO A 158 18217 12883 12101 3976 -482 -1413 N ATOM 1082 CA PRO A 158 15.022 100.006 65.673 1.00115.19 C ANISOU 1082 CA PRO A 158 18419 12965 12383 4000 -696 -1717 C ATOM 1083 C PRO A 158 14.535 100.916 64.537 1.00117.67 C ANISOU 1083 C PRO A 158 18370 13162 13177 3719 -633 -1663 C ATOM 1084 O PRO A 158 14.170 102.051 64.816 1.00119.23 O ANISOU 1084 O PRO A 158 18611 13236 13455 3775 -631 -1826 O ATOM 1085 CB PRO A 158 16.546 100.073 65.829 1.00117.52 C ANISOU 1085 CB PRO A 158 18717 13298 12635 3998 -1184 -1988 C ATOM 1086 CG PRO A 158 16.954 98.680 66.186 1.00121.71 C ANISOU 1086 CG PRO A 158 19398 13971 12875 4118 -1196 -1851 C ATOM 1087 CD PRO A 158 16.041 97.837 65.354 1.00114.56 C ANISOU 1087 CD PRO A 158 18304 13088 12135 3946 -812 -1478 C ATOM 1088 N ASN A 159 14.482 100.420 63.284 1.00111.70 N ANISOU 1088 N ASN A 159 17285 12436 12719 3442 -577 -1435 N ATOM 1089 CA ASN A 159 14.003 101.186 62.122 1.00110.11 C ANISOU 1089 CA ASN A 159 16763 12134 12940 3193 -523 -1343 C ATOM 1090 C ASN A 159 12.483 101.454 62.192 1.00116.54 C ANISOU 1090 C ASN A 159 17571 12881 13826 3262 -154 -1181 C ATOM 1091 O ASN A 159 11.997 102.393 61.549 1.00115.00 O ANISOU 1091 O ASN A 159 17187 12571 13936 3144 -127 -1164 O ATOM 1092 CB ASN A 159 14.347 100.463 60.807 1.00106.12 C ANISOU 1092 CB ASN A 159 15962 11697 12661 2920 -571 -1149 C ATOM 1093 CG ASN A 159 15.695 100.802 60.202 1.00119.00 C ANISOU 1093 CG ASN A 159 17430 13317 14468 2744 -900 -1298 C ATOM 1094 OD1 ASN A 159 16.525 101.509 60.784 1.00110.90 O ANISOU 1094 OD1 ASN A 159 16486 12234 13419 2809 -1147 -1569 O ATOM 1095 ND2 ASN A 159 15.937 100.308 58.997 1.00108.54 N ANISOU 1095 ND2 ASN A 159 15860 12037 13343 2516 -903 -1130 N ATOM 1096 N MET A 160 11.749 100.635 62.978 1.00116.57 N ANISOU 1096 N MET A 160 17779 12946 13568 3461 138 -1056 N ATOM 1097 CA MET A 160 10.297 100.723 63.169 1.00118.42 C ANISOU 1097 CA MET A 160 17994 13122 13880 3547 535 -894 C ATOM 1098 C MET A 160 9.819 101.956 63.951 1.00126.16 C ANISOU 1098 C MET A 160 19133 13978 14823 3738 594 -1096 C ATOM 1099 O MET A 160 9.270 102.879 63.346 1.00125.81 O ANISOU 1099 O MET A 160 18878 13818 15107 3630 593 -1104 O ATOM 1100 CB MET A 160 9.754 99.480 63.900 1.00122.31 C ANISOU 1100 CB MET A 160 18682 13691 14100 3716 858 -709 C ATOM 1101 CG MET A 160 10.026 98.179 63.198 1.00124.26 C ANISOU 1101 CG MET A 160 18780 14029 14402 3544 843 -504 C ATOM 1102 SD MET A 160 8.645 97.708 62.149 1.00127.35 S ANISOU 1102 SD MET A 160 18781 14374 15231 3327 1130 -210 S ATOM 1103 CE MET A 160 8.977 95.966 61.972 1.00122.67 C ANISOU 1103 CE MET A 160 18195 13873 14541 3248 1172 -15 C ATOM 1104 N ILE A 161 10.019 101.968 65.284 1.00126.28 N ANISOU 1104 N ILE A 161 19542 14012 14428 4038 642 -1260 N ATOM 1105 CA ILE A 161 9.625 103.087 66.138 1.00129.88 C ANISOU 1105 CA ILE A 161 20208 14352 14790 4263 719 -1476 C ATOM 1106 C ILE A 161 10.773 104.072 66.348 1.00135.10 C ANISOU 1106 C ILE A 161 20977 14947 15407 4276 275 -1838 C ATOM 1107 O ILE A 161 10.600 105.266 66.094 1.00135.43 O ANISOU 1107 O ILE A 161 20924 14834 15701 4233 202 -1988 O ATOM 1108 CB ILE A 161 9.082 102.577 67.496 1.00136.65 C ANISOU 1108 CB ILE A 161 21466 15253 15202 4616 1070 -1448 C ATOM 1109 N LEU A 162 11.937 103.573 66.803 1.00131.97 N ANISOU 1109 N LEU A 162 20766 14652 14727 4336 -28 -1982 N ATOM 1110 CA LEU A 162 13.129 104.367 67.118 1.00161.90 C ANISOU 1110 CA LEU A 162 24653 18385 18476 4360 -487 -2354 C ATOM 1111 C LEU A 162 13.783 104.980 65.868 1.00172.99 C ANISOU 1111 C LEU A 162 25656 19695 20379 4008 -762 -2393 C ATOM 1112 O LEU A 162 13.238 104.924 64.766 1.00126.44 O ANISOU 1112 O LEU A 162 19442 13781 14818 3770 -603 -2135 O ATOM 1113 CB LEU A 162 14.162 103.510 67.875 1.00163.25 C ANISOU 1113 CB LEU A 162 25086 18704 18239 4522 -744 -2464 C ATOM 1114 CG LEU A 162 13.735 102.944 69.236 1.00171.44 C ANISOU 1114 CG LEU A 162 26616 19824 18699 4921 -530 -2463 C ATOM 1115 CD1 LEU A 162 13.237 101.507 69.106 1.00170.12 C ANISOU 1115 CD1 LEU A 162 26455 19785 18397 4923 -184 -2074 C ATOM 1116 CD2 LEU A 162 14.883 102.990 70.226 1.00177.14 C ANISOU 1116 CD2 LEU A 162 27673 20598 19033 5159 -967 -2801 C ATOM 1117 N LYS A 179 13.334 111.547 66.236 1.00140.21 N ANISOU 1117 N LYS A 179 21542 14463 17270 4081 -1198 -3545 N ATOM 1118 CA LYS A 179 14.287 112.270 65.398 1.00138.80 C ANISOU 1118 CA LYS A 179 21046 14124 17567 3754 -1478 -3595 C ATOM 1119 C LYS A 179 15.709 112.223 66.017 1.00143.86 C ANISOU 1119 C LYS A 179 21758 14766 18137 3741 -1939 -3955 C ATOM 1120 O LYS A 179 16.238 113.249 66.462 1.00146.27 O ANISOU 1120 O LYS A 179 22089 14839 18648 3730 -2209 -4307 O ATOM 1121 CB LYS A 179 13.811 113.720 65.177 1.00142.79 C ANISOU 1121 CB LYS A 179 21466 14317 18470 3705 -1424 -3678 C ATOM 1122 N SER A 180 16.316 111.015 66.041 1.00138.14 N ANISOU 1122 N SER A 180 21051 14290 17147 3746 -2038 -3873 N ATOM 1123 CA SER A 180 17.658 110.776 66.588 1.00139.09 C ANISOU 1123 CA SER A 180 21209 14448 17189 3755 -2487 -4187 C ATOM 1124 C SER A 180 18.693 110.543 65.485 1.00138.22 C ANISOU 1124 C SER A 180 20682 14333 17502 3392 -2654 -4073 C ATOM 1125 O SER A 180 18.376 109.904 64.480 1.00133.83 O ANISOU 1125 O SER A 180 19902 13873 17073 3203 -2404 -3689 O ATOM 1126 CB SER A 180 17.649 109.576 67.533 1.00143.32 C ANISOU 1126 CB SER A 180 22071 15250 17133 4046 -2506 -4190 C ATOM 1127 OG SER A 180 17.268 109.940 68.851 1.00156.38 O ANISOU 1127 OG SER A 180 24167 16893 18357 4419 -2425 -4390 O ATOM 1128 N GLU A 181 19.941 111.042 65.691 1.00135.70 N ANISOU 1128 N GLU A 181 20258 13896 17407 3304 -3080 -4423 N ATOM 1129 CA GLU A 181 21.081 110.864 64.777 1.00133.31 C ANISOU 1129 CA GLU A 181 19558 13572 17521 2982 -3257 -4374 C ATOM 1130 C GLU A 181 21.479 109.373 64.781 1.00133.47 C ANISOU 1130 C GLU A 181 19579 13900 17233 3032 -3278 -4200 C ATOM 1131 O GLU A 181 22.031 108.882 63.790 1.00130.53 O ANISOU 1131 O GLU A 181 18891 13586 17119 2781 -3246 -3994 O ATOM 1132 CB GLU A 181 22.254 111.807 65.155 1.00138.53 C ANISOU 1132 CB GLU A 181 20103 14000 18534 2901 -3704 -4836 C ATOM 1133 CG GLU A 181 23.668 111.240 65.036 1.00148.30 C ANISOU 1133 CG GLU A 181 21120 15333 19894 2803 -4062 -4987 C ATOM 1134 CD GLU A 181 24.489 111.525 63.794 1.00165.29 C ANISOU 1134 CD GLU A 181 22787 17334 22681 2411 -4099 -4916 C ATOM 1135 OE1 GLU A 181 23.936 112.053 62.801 1.00161.99 O ANISOU 1135 OE1 GLU A 181 22190 16754 22603 2179 -3799 -4659 O ATOM 1136 OE2 GLU A 181 25.699 111.202 63.815 1.00155.98 O ANISOU 1136 OE2 GLU A 181 21410 16200 21658 2349 -4421 -5110 O ATOM 1137 N PHE A 182 21.141 108.652 65.882 1.00129.64 N ANISOU 1137 N PHE A 182 19475 13601 16182 3375 -3301 -4269 N ATOM 1138 CA PHE A 182 21.344 107.211 66.022 1.00127.12 C ANISOU 1138 CA PHE A 182 19239 13556 15504 3486 -3283 -4088 C ATOM 1139 C PHE A 182 20.560 106.471 64.919 1.00125.93 C ANISOU 1139 C PHE A 182 18908 13516 15426 3303 -2855 -3597 C ATOM 1140 O PHE A 182 21.085 105.519 64.335 1.00123.00 O ANISOU 1140 O PHE A 182 18355 13285 15095 3180 -2870 -3422 O ATOM 1141 CB PHE A 182 20.917 106.721 67.425 1.00131.11 C ANISOU 1141 CB PHE A 182 20250 14195 15373 3912 -3295 -4206 C ATOM 1142 CG PHE A 182 20.843 105.214 67.533 1.00130.64 C ANISOU 1142 CG PHE A 182 20317 14392 14929 4039 -3162 -3932 C ATOM 1143 CD1 PHE A 182 21.989 104.459 67.751 1.00134.12 C ANISOU 1143 CD1 PHE A 182 20725 14955 15279 4088 -3514 -4047 C ATOM 1144 CD2 PHE A 182 19.635 104.546 67.355 1.00130.06 C ANISOU 1144 CD2 PHE A 182 20360 14416 14641 4096 -2683 -3552 C ATOM 1145 CE1 PHE A 182 21.928 103.065 67.796 1.00133.23 C ANISOU 1145 CE1 PHE A 182 20726 15052 14843 4201 -3381 -3778 C ATOM 1146 CE2 PHE A 182 19.576 103.152 67.400 1.00131.16 C ANISOU 1146 CE2 PHE A 182 20597 14755 14482 4188 -2547 -3291 C ATOM 1147 CZ PHE A 182 20.721 102.422 67.632 1.00129.98 C ANISOU 1147 CZ PHE A 182 20449 14719 14220 4247 -2893 -3401 C ATOM 1148 N GLY A 183 19.324 106.927 64.667 1.00120.94 N ANISOU 1148 N GLY A 183 18322 12807 14824 3300 -2501 -3407 N ATOM 1149 CA GLY A 183 18.419 106.396 63.651 1.00116.63 C ANISOU 1149 CA GLY A 183 17609 12331 14373 3145 -2118 -2980 C ATOM 1150 C GLY A 183 18.971 106.511 62.247 1.00117.02 C ANISOU 1150 C GLY A 183 17260 12324 14880 2790 -2138 -2823 C ATOM 1151 O GLY A 183 18.765 105.610 61.431 1.00113.95 O ANISOU 1151 O GLY A 183 16729 12066 14498 2667 -1955 -2515 O ATOM 1152 N LEU A 184 19.696 107.621 61.969 1.00113.95 N ANISOU 1152 N LEU A 184 16697 11724 14875 2628 -2352 -3040 N ATOM 1153 CA LEU A 184 20.359 107.902 60.691 1.00111.87 C ANISOU 1153 CA LEU A 184 16071 11367 15066 2297 -2363 -2917 C ATOM 1154 C LEU A 184 21.494 106.898 60.455 1.00113.18 C ANISOU 1154 C LEU A 184 16082 11698 15223 2215 -2533 -2917 C ATOM 1155 O LEU A 184 21.522 106.248 59.410 1.00110.13 O ANISOU 1155 O LEU A 184 15510 11409 14924 2045 -2366 -2631 O ATOM 1156 CB LEU A 184 20.910 109.347 60.662 1.00114.87 C ANISOU 1156 CB LEU A 184 16331 11445 15870 2169 -2542 -3178 C ATOM 1157 CG LEU A 184 19.952 110.483 60.260 1.00120.28 C ANISOU 1157 CG LEU A 184 17013 11902 16787 2110 -2327 -3069 C ATOM 1158 CD1 LEU A 184 19.068 110.918 61.420 1.00122.41 C ANISOU 1158 CD1 LEU A 184 17607 12133 16770 2405 -2276 -3226 C ATOM 1159 CD2 LEU A 184 20.729 111.700 59.803 1.00125.44 C ANISOU 1159 CD2 LEU A 184 17458 12245 17959 1892 -2477 -3243 C ATOM 1160 N VAL A 185 22.406 106.755 61.444 1.00110.91 N ANISOU 1160 N VAL A 185 15884 11444 14813 2360 -2877 -3250 N ATOM 1161 CA VAL A 185 23.557 105.846 61.405 1.00109.90 C ANISOU 1161 CA VAL A 185 15614 11459 14684 2333 -3099 -3314 C ATOM 1162 C VAL A 185 23.062 104.388 61.427 1.00110.25 C ANISOU 1162 C VAL A 185 15804 11765 14321 2464 -2914 -3036 C ATOM 1163 O VAL A 185 23.611 103.570 60.692 1.00108.26 O ANISOU 1163 O VAL A 185 15345 11620 14167 2329 -2886 -2880 O ATOM 1164 CB VAL A 185 24.587 106.134 62.534 1.00117.61 C ANISOU 1164 CB VAL A 185 16673 12394 15621 2501 -3562 -3769 C ATOM 1165 CG1 VAL A 185 25.839 105.273 62.379 1.00117.66 C ANISOU 1165 CG1 VAL A 185 16456 12520 15728 2451 -3810 -3840 C ATOM 1166 CG2 VAL A 185 24.972 107.611 62.565 1.00120.26 C ANISOU 1166 CG2 VAL A 185 16884 12434 16376 2376 -3739 -4066 C ATOM 1167 N TRP A 186 22.009 104.073 62.220 1.00106.17 N ANISOU 1167 N TRP A 186 15633 11332 13376 2720 -2756 -2967 N ATOM 1168 CA TRP A 186 21.440 102.722 62.267 1.00103.51 C ANISOU 1168 CA TRP A 186 15443 11201 12684 2840 -2539 -2690 C ATOM 1169 C TRP A 186 20.866 102.343 60.895 1.00105.11 C ANISOU 1169 C TRP A 186 15414 11430 13093 2594 -2219 -2323 C ATOM 1170 O TRP A 186 21.040 101.203 60.461 1.00103.43 O ANISOU 1170 O TRP A 186 15140 11361 12797 2558 -2145 -2133 O ATOM 1171 CB TRP A 186 20.369 102.573 63.363 1.00103.00 C ANISOU 1171 CB TRP A 186 15782 11181 12174 3150 -2375 -2678 C ATOM 1172 CG TRP A 186 19.848 101.171 63.485 1.00102.03 C ANISOU 1172 CG TRP A 186 15811 11236 11720 3273 -2142 -2398 C ATOM 1173 CD1 TRP A 186 18.694 100.678 62.952 1.00102.54 C ANISOU 1173 CD1 TRP A 186 15854 11333 11772 3214 -1752 -2069 C ATOM 1174 CD2 TRP A 186 20.518 100.056 64.089 1.00102.72 C ANISOU 1174 CD2 TRP A 186 16060 11471 11497 3455 -2298 -2419 C ATOM 1175 NE1 TRP A 186 18.586 99.333 63.214 1.00101.21 N ANISOU 1175 NE1 TRP A 186 15829 11309 11319 3337 -1635 -1887 N ATOM 1176 CE2 TRP A 186 19.698 98.920 63.899 1.00104.62 C ANISOU 1176 CE2 TRP A 186 16386 11813 11551 3492 -1957 -2082 C ATOM 1177 CE3 TRP A 186 21.734 99.906 64.783 1.00106.33 C ANISOU 1177 CE3 TRP A 186 16593 11974 11833 3602 -2711 -2696 C ATOM 1178 CZ2 TRP A 186 20.044 97.654 64.393 1.00104.34 C ANISOU 1178 CZ2 TRP A 186 16536 11908 11201 3671 -1987 -1995 C ATOM 1179 CZ3 TRP A 186 22.079 98.652 65.262 1.00108.15 C ANISOU 1179 CZ3 TRP A 186 17006 12353 11734 3798 -2765 -2610 C ATOM 1180 CH2 TRP A 186 21.240 97.543 65.067 1.00106.79 C ANISOU 1180 CH2 TRP A 186 16941 12265 11368 3832 -2392 -2253 C ATOM 1181 N HIS A 187 20.229 103.304 60.201 1.00101.59 N ANISOU 1181 N HIS A 187 14847 10835 12918 2437 -2056 -2236 N ATOM 1182 CA HIS A 187 19.662 103.094 58.870 1.00 99.11 C ANISOU 1182 CA HIS A 187 14330 10529 12797 2221 -1797 -1912 C ATOM 1183 C HIS A 187 20.744 102.709 57.878 1.00100.78 C ANISOU 1183 C HIS A 187 14268 10776 13247 1997 -1886 -1860 C ATOM 1184 O HIS A 187 20.533 101.787 57.102 1.00 98.24 O ANISOU 1184 O HIS A 187 13865 10570 12893 1912 -1728 -1614 O ATOM 1185 CB HIS A 187 18.914 104.339 58.377 1.00100.80 C ANISOU 1185 CB HIS A 187 14482 10552 13264 2126 -1666 -1863 C ATOM 1186 CG HIS A 187 17.451 104.111 58.197 1.00103.31 C ANISOU 1186 CG HIS A 187 14877 10905 13470 2191 -1369 -1612 C ATOM 1187 ND1 HIS A 187 16.531 104.572 59.123 1.00106.91 N ANISOU 1187 ND1 HIS A 187 15546 11307 13769 2403 -1261 -1685 N ATOM 1188 CD2 HIS A 187 16.793 103.456 57.210 1.00102.96 C ANISOU 1188 CD2 HIS A 187 14710 10941 13468 2078 -1172 -1313 C ATOM 1189 CE1 HIS A 187 15.346 104.198 58.665 1.00105.05 C ANISOU 1189 CE1 HIS A 187 15275 11114 13526 2400 -993 -1420 C ATOM 1190 NE2 HIS A 187 15.455 103.521 57.516 1.00102.95 N ANISOU 1190 NE2 HIS A 187 14811 10929 13378 2206 -954 -1199 N ATOM 1191 N GLU A 188 21.916 103.374 57.941 1.00 98.66 N ANISOU 1191 N GLU A 188 13855 10404 13228 1912 -2137 -2106 N ATOM 1192 CA GLU A 188 23.064 103.087 57.079 1.00 97.86 C ANISOU 1192 CA GLU A 188 13470 10320 13393 1710 -2209 -2088 C ATOM 1193 C GLU A 188 23.691 101.726 57.423 1.00 99.64 C ANISOU 1193 C GLU A 188 13724 10749 13386 1827 -2322 -2103 C ATOM 1194 O GLU A 188 24.198 101.061 56.516 1.00 97.91 O ANISOU 1194 O GLU A 188 13315 10606 13282 1688 -2249 -1961 O ATOM 1195 CB GLU A 188 24.115 104.204 57.160 1.00102.26 C ANISOU 1195 CB GLU A 188 13835 10678 14341 1587 -2434 -2364 C ATOM 1196 CG GLU A 188 23.746 105.428 56.339 1.00117.03 C ANISOU 1196 CG GLU A 188 15592 12322 16551 1391 -2271 -2267 C ATOM 1197 CD GLU A 188 24.797 106.521 56.279 1.00153.97 C ANISOU 1197 CD GLU A 188 20041 16764 21694 1224 -2445 -2504 C ATOM 1198 OE1 GLU A 188 25.329 106.767 55.173 1.00154.13 O ANISOU 1198 OE1 GLU A 188 19812 16697 22053 984 -2306 -2357 O ATOM 1199 OE2 GLU A 188 25.067 107.153 57.328 1.00155.03 O ANISOU 1199 OE2 GLU A 188 20253 16788 21863 1335 -2710 -2840 O ATOM 1200 N ILE A 189 23.642 101.308 58.718 1.00 95.91 N ANISOU 1200 N ILE A 189 13511 10358 12571 2099 -2486 -2266 N ATOM 1201 CA ILE A 189 24.168 100.016 59.190 1.00 95.07 C ANISOU 1201 CA ILE A 189 13492 10430 12202 2262 -2605 -2274 C ATOM 1202 C ILE A 189 23.305 98.885 58.604 1.00 95.34 C ANISOU 1202 C ILE A 189 13590 10591 12042 2252 -2295 -1929 C ATOM 1203 O ILE A 189 23.842 97.975 57.972 1.00 92.81 O ANISOU 1203 O ILE A 189 13129 10364 11768 2178 -2277 -1823 O ATOM 1204 CB ILE A 189 24.256 99.946 60.750 1.00100.58 C ANISOU 1204 CB ILE A 189 14511 11164 12541 2588 -2852 -2521 C ATOM 1205 CG1 ILE A 189 25.401 100.836 61.279 1.00104.04 C ANISOU 1205 CG1 ILE A 189 14832 11493 13205 2596 -3259 -2915 C ATOM 1206 CG2 ILE A 189 24.424 98.492 61.251 1.00100.41 C ANISOU 1206 CG2 ILE A 189 14676 11323 12151 2803 -2877 -2425 C ATOM 1207 CD1 ILE A 189 25.249 101.301 62.714 1.00110.09 C ANISOU 1207 CD1 ILE A 189 15933 12226 13668 2887 -3490 -3199 C ATOM 1208 N VAL A 190 21.969 98.980 58.799 1.00 90.89 N ANISOU 1208 N VAL A 190 13220 10016 11298 2323 -2052 -1771 N ATOM 1209 CA VAL A 190 20.952 98.032 58.337 1.00 88.06 C ANISOU 1209 CA VAL A 190 12920 9743 10797 2314 -1756 -1466 C ATOM 1210 C VAL A 190 21.046 97.851 56.815 1.00 89.84 C ANISOU 1210 C VAL A 190 12869 9972 11293 2046 -1633 -1277 C ATOM 1211 O VAL A 190 21.121 96.713 56.358 1.00 88.08 O ANISOU 1211 O VAL A 190 12616 9852 10999 2023 -1556 -1129 O ATOM 1212 CB VAL A 190 19.548 98.501 58.791 1.00 91.96 C ANISOU 1212 CB VAL A 190 13598 10179 11164 2415 -1533 -1379 C ATOM 1213 CG1 VAL A 190 18.431 97.835 57.995 1.00 89.63 C ANISOU 1213 CG1 VAL A 190 13244 9919 10891 2320 -1233 -1073 C ATOM 1214 CG2 VAL A 190 19.361 98.260 60.275 1.00 93.91 C ANISOU 1214 CG2 VAL A 190 14183 10463 11037 2723 -1571 -1495 C ATOM 1215 N ASN A 191 21.085 98.964 56.050 1.00 86.77 N ANISOU 1215 N ASN A 191 12305 9461 11201 1859 -1618 -1287 N ATOM 1216 CA ASN A 191 21.207 98.950 54.592 1.00 85.45 C ANISOU 1216 CA ASN A 191 11918 9285 11263 1626 -1497 -1110 C ATOM 1217 C ASN A 191 22.513 98.266 54.157 1.00 90.60 C ANISOU 1217 C ASN A 191 12405 10013 12005 1552 -1603 -1162 C ATOM 1218 O ASN A 191 22.502 97.533 53.167 1.00 89.29 O ANISOU 1218 O ASN A 191 12155 9920 11850 1453 -1473 -986 O ATOM 1219 CB ASN A 191 21.125 100.370 54.019 1.00 87.21 C ANISOU 1219 CB ASN A 191 12025 9334 11776 1474 -1470 -1122 C ATOM 1220 CG ASN A 191 19.789 101.072 54.184 1.00111.04 C ANISOU 1220 CG ASN A 191 15162 12266 14761 1528 -1336 -1033 C ATOM 1221 OD1 ASN A 191 18.907 100.664 54.960 1.00106.60 O ANISOU 1221 OD1 ASN A 191 14777 11758 13968 1698 -1265 -1009 O ATOM 1222 ND2 ASN A 191 19.637 102.196 53.499 1.00102.12 N ANISOU 1222 ND2 ASN A 191 13935 10982 13884 1395 -1287 -986 N ATOM 1223 N TYR A 192 23.616 98.470 54.918 1.00 89.12 N ANISOU 1223 N TYR A 192 12171 9808 11882 1618 -1851 -1417 N ATOM 1224 CA TYR A 192 24.909 97.843 54.646 1.00 89.85 C ANISOU 1224 CA TYR A 192 12078 9966 12096 1577 -1975 -1499 C ATOM 1225 C TYR A 192 24.805 96.329 54.873 1.00 89.84 C ANISOU 1225 C TYR A 192 12203 10125 11807 1723 -1949 -1398 C ATOM 1226 O TYR A 192 25.242 95.578 54.009 1.00 88.01 O ANISOU 1226 O TYR A 192 11836 9958 11646 1632 -1862 -1292 O ATOM 1227 CB TYR A 192 26.028 98.462 55.511 1.00 95.74 C ANISOU 1227 CB TYR A 192 12734 10641 13001 1636 -2292 -1826 C ATOM 1228 CG TYR A 192 27.437 98.080 55.098 1.00101.09 C ANISOU 1228 CG TYR A 192 13125 11346 13937 1554 -2414 -1928 C ATOM 1229 CD1 TYR A 192 28.180 98.895 54.245 1.00104.51 C ANISOU 1229 CD1 TYR A 192 13255 11653 14800 1316 -2356 -1956 C ATOM 1230 CD2 TYR A 192 28.047 96.932 55.599 1.00103.25 C ANISOU 1230 CD2 TYR A 192 13428 11756 14045 1725 -2574 -1996 C ATOM 1231 CE1 TYR A 192 29.484 98.557 53.874 1.00107.95 C ANISOU 1231 CE1 TYR A 192 13396 12105 15515 1241 -2432 -2051 C ATOM 1232 CE2 TYR A 192 29.347 96.580 55.231 1.00106.01 C ANISOU 1232 CE2 TYR A 192 13486 12126 14665 1665 -2684 -2099 C ATOM 1233 CZ TYR A 192 30.064 97.397 54.369 1.00116.06 C ANISOU 1233 CZ TYR A 192 14432 13279 16385 1419 -2604 -2132 C ATOM 1234 OH TYR A 192 31.345 97.049 54.006 1.00118.57 O ANISOU 1234 OH TYR A 192 14434 13611 17006 1361 -2676 -2233 O ATOM 1235 N ILE A 193 24.199 95.892 56.010 1.00 85.17 N ANISOU 1235 N ILE A 193 11888 9582 10891 1954 -1996 -1421 N ATOM 1236 CA ILE A 193 23.998 94.480 56.370 1.00 83.66 C ANISOU 1236 CA ILE A 193 11862 9508 10416 2116 -1951 -1308 C ATOM 1237 C ILE A 193 23.196 93.778 55.260 1.00 85.78 C ANISOU 1237 C ILE A 193 12092 9808 10693 1979 -1668 -1033 C ATOM 1238 O ILE A 193 23.617 92.714 54.789 1.00 84.86 O ANISOU 1238 O ILE A 193 11919 9762 10562 1968 -1640 -959 O ATOM 1239 CB ILE A 193 23.301 94.310 57.770 1.00 87.63 C ANISOU 1239 CB ILE A 193 12708 10025 10563 2388 -1980 -1343 C ATOM 1240 CG1 ILE A 193 24.055 94.991 58.964 1.00 90.94 C ANISOU 1240 CG1 ILE A 193 13222 10419 10914 2569 -2311 -1652 C ATOM 1241 CG2 ILE A 193 22.929 92.850 58.087 1.00 87.13 C ANISOU 1241 CG2 ILE A 193 12837 10046 10223 2542 -1860 -1168 C ATOM 1242 CD1 ILE A 193 25.477 94.530 59.318 1.00 96.18 C ANISOU 1242 CD1 ILE A 193 13793 11142 11611 2671 -2635 -1845 C ATOM 1243 N CYS A 194 22.061 94.393 54.839 1.00 80.66 N ANISOU 1243 N CYS A 194 11466 9099 10083 1884 -1482 -903 N ATOM 1244 CA CYS A 194 21.141 93.882 53.821 1.00 78.51 C ANISOU 1244 CA CYS A 194 11159 8842 9830 1764 -1257 -670 C ATOM 1245 C CYS A 194 21.808 93.749 52.452 1.00 82.18 C ANISOU 1245 C CYS A 194 11411 9328 10485 1573 -1230 -617 C ATOM 1246 O CYS A 194 21.535 92.766 51.767 1.00 81.37 O ANISOU 1246 O CYS A 194 11305 9280 10332 1536 -1124 -483 O ATOM 1247 CB CYS A 194 19.887 94.741 53.743 1.00 78.75 C ANISOU 1247 CB CYS A 194 11230 8793 9897 1726 -1120 -580 C ATOM 1248 SG CYS A 194 18.776 94.558 55.164 1.00 83.77 S ANISOU 1248 SG CYS A 194 12133 9415 10281 1958 -1019 -563 S ATOM 1249 N GLN A 195 22.692 94.693 52.059 1.00 79.71 N ANISOU 1249 N GLN A 195 10930 8962 10397 1458 -1311 -724 N ATOM 1250 CA GLN A 195 23.421 94.590 50.781 1.00 79.06 C ANISOU 1250 CA GLN A 195 10657 8893 10488 1292 -1241 -667 C ATOM 1251 C GLN A 195 24.381 93.404 50.833 1.00 83.54 C ANISOU 1251 C GLN A 195 11172 9557 11012 1361 -1307 -727 C ATOM 1252 O GLN A 195 24.451 92.638 49.872 1.00 83.22 O ANISOU 1252 O GLN A 195 11086 9570 10963 1296 -1189 -618 O ATOM 1253 CB GLN A 195 24.188 95.880 50.419 1.00 81.50 C ANISOU 1253 CB GLN A 195 10788 9092 11085 1153 -1272 -756 C ATOM 1254 CG GLN A 195 23.332 97.090 50.025 1.00 85.87 C ANISOU 1254 CG GLN A 195 11372 9526 11729 1059 -1174 -659 C ATOM 1255 CD GLN A 195 22.258 96.803 49.007 1.00 96.80 C ANISOU 1255 CD GLN A 195 12827 10942 13010 1004 -999 -423 C ATOM 1256 OE1 GLN A 195 21.063 96.872 49.317 1.00 90.09 O ANISOU 1256 OE1 GLN A 195 12104 10086 12041 1072 -968 -348 O ATOM 1257 NE2 GLN A 195 22.652 96.490 47.769 1.00 86.95 N ANISOU 1257 NE2 GLN A 195 11498 9726 11814 890 -885 -312 N ATOM 1258 N VAL A 196 25.071 93.216 51.981 1.00 80.74 N ANISOU 1258 N VAL A 196 10846 9222 10609 1517 -1510 -905 N ATOM 1259 CA VAL A 196 25.994 92.098 52.217 1.00 81.19 C ANISOU 1259 CA VAL A 196 10865 9359 10623 1628 -1613 -975 C ATOM 1260 C VAL A 196 25.194 90.768 52.147 1.00 83.65 C ANISOU 1260 C VAL A 196 11362 9733 10690 1715 -1487 -805 C ATOM 1261 O VAL A 196 25.713 89.789 51.616 1.00 83.61 O ANISOU 1261 O VAL A 196 11296 9778 10694 1721 -1455 -776 O ATOM 1262 CB VAL A 196 26.786 92.264 53.551 1.00 87.30 C ANISOU 1262 CB VAL A 196 11661 10134 11376 1809 -1906 -1210 C ATOM 1263 CG1 VAL A 196 27.639 91.039 53.863 1.00 87.90 C ANISOU 1263 CG1 VAL A 196 11725 10291 11382 1968 -2034 -1265 C ATOM 1264 CG2 VAL A 196 27.666 93.511 53.518 1.00 88.84 C ANISOU 1264 CG2 VAL A 196 11619 10243 11894 1693 -2041 -1402 C ATOM 1265 N ILE A 197 23.914 90.760 52.604 1.00 78.67 N ANISOU 1265 N ILE A 197 10933 9078 9880 1768 -1393 -694 N ATOM 1266 CA ILE A 197 23.043 89.578 52.527 1.00 76.90 C ANISOU 1266 CA ILE A 197 10856 8873 9489 1821 -1248 -528 C ATOM 1267 C ILE A 197 22.748 89.276 51.040 1.00 78.11 C ANISOU 1267 C ILE A 197 10893 9034 9751 1636 -1095 -404 C ATOM 1268 O ILE A 197 22.928 88.129 50.626 1.00 77.89 O ANISOU 1268 O ILE A 197 10875 9035 9684 1653 -1051 -356 O ATOM 1269 CB ILE A 197 21.753 89.705 53.395 1.00 79.88 C ANISOU 1269 CB ILE A 197 11442 9206 9701 1918 -1153 -442 C ATOM 1270 CG1 ILE A 197 22.111 89.635 54.888 1.00 81.86 C ANISOU 1270 CG1 ILE A 197 11884 9466 9753 2160 -1294 -553 C ATOM 1271 CG2 ILE A 197 20.721 88.609 53.066 1.00 79.73 C ANISOU 1271 CG2 ILE A 197 11506 9171 9617 1905 -961 -254 C ATOM 1272 CD1 ILE A 197 21.303 90.482 55.743 1.00 89.98 C ANISOU 1272 CD1 ILE A 197 13059 10447 10680 2241 -1261 -575 C ATOM 1273 N PHE A 198 22.368 90.289 50.235 1.00 72.23 N ANISOU 1273 N PHE A 198 10055 8257 9132 1478 -1030 -363 N ATOM 1274 CA PHE A 198 22.116 90.053 48.811 1.00 70.61 C ANISOU 1274 CA PHE A 198 9780 8065 8983 1332 -911 -254 C ATOM 1275 C PHE A 198 23.373 89.558 48.092 1.00 76.05 C ANISOU 1275 C PHE A 198 10344 8805 9746 1297 -913 -314 C ATOM 1276 O PHE A 198 23.301 88.558 47.370 1.00 75.71 O ANISOU 1276 O PHE A 198 10325 8795 9648 1283 -841 -258 O ATOM 1277 CB PHE A 198 21.569 91.303 48.076 1.00 71.37 C ANISOU 1277 CB PHE A 198 9825 8110 9183 1199 -854 -186 C ATOM 1278 CG PHE A 198 21.687 91.173 46.567 1.00 72.00 C ANISOU 1278 CG PHE A 198 9850 8214 9292 1076 -759 -98 C ATOM 1279 CD1 PHE A 198 20.767 90.422 45.842 1.00 73.89 C ANISOU 1279 CD1 PHE A 198 10164 8472 9439 1056 -707 7 C ATOM 1280 CD2 PHE A 198 22.766 91.734 45.884 1.00 74.41 C ANISOU 1280 CD2 PHE A 198 10034 8519 9719 992 -719 -131 C ATOM 1281 CE1 PHE A 198 20.898 90.270 44.456 1.00 74.80 C ANISOU 1281 CE1 PHE A 198 10273 8618 9531 975 -643 68 C ATOM 1282 CE2 PHE A 198 22.908 91.561 44.502 1.00 77.21 C ANISOU 1282 CE2 PHE A 198 10385 8902 10050 909 -602 -42 C ATOM 1283 CZ PHE A 198 21.966 90.841 43.794 1.00 74.51 C ANISOU 1283 CZ PHE A 198 10158 8591 9563 912 -578 51 C ATOM 1284 N TRP A 199 24.503 90.282 48.257 1.00 73.29 N ANISOU 1284 N TRP A 199 9850 8448 9549 1278 -988 -437 N ATOM 1285 CA TRP A 199 25.743 89.994 47.554 1.00 73.82 C ANISOU 1285 CA TRP A 199 9750 8550 9750 1235 -956 -498 C ATOM 1286 C TRP A 199 26.355 88.663 47.946 1.00 77.37 C ANISOU 1286 C TRP A 199 10211 9056 10132 1376 -1022 -563 C ATOM 1287 O TRP A 199 26.997 88.057 47.095 1.00 76.82 O ANISOU 1287 O TRP A 199 10049 9021 10119 1348 -932 -565 O ATOM 1288 CB TRP A 199 26.749 91.138 47.699 1.00 74.48 C ANISOU 1288 CB TRP A 199 9635 8581 10083 1168 -1016 -621 C ATOM 1289 CG TRP A 199 26.360 92.347 46.895 1.00 75.64 C ANISOU 1289 CG TRP A 199 9750 8652 10338 1004 -886 -524 C ATOM 1290 CD1 TRP A 199 25.904 93.536 47.379 1.00 78.73 C ANISOU 1290 CD1 TRP A 199 10160 8951 10802 967 -941 -541 C ATOM 1291 CD2 TRP A 199 26.287 92.442 45.461 1.00 75.72 C ANISOU 1291 CD2 TRP A 199 9749 8663 10356 882 -675 -378 C ATOM 1292 NE1 TRP A 199 25.564 94.373 46.342 1.00 78.50 N ANISOU 1292 NE1 TRP A 199 10121 8855 10849 826 -781 -403 N ATOM 1293 CE2 TRP A 199 25.806 93.735 45.152 1.00 79.94 C ANISOU 1293 CE2 TRP A 199 10295 9099 10979 777 -617 -296 C ATOM 1294 CE3 TRP A 199 26.626 91.573 44.402 1.00 77.17 C ANISOU 1294 CE3 TRP A 199 9934 8916 10471 868 -529 -315 C ATOM 1295 CZ2 TRP A 199 25.660 94.188 43.830 1.00 79.56 C ANISOU 1295 CZ2 TRP A 199 10272 9021 10936 667 -422 -134 C ATOM 1296 CZ3 TRP A 199 26.460 92.016 43.092 1.00 79.09 C ANISOU 1296 CZ3 TRP A 199 10214 9142 10696 763 -334 -171 C ATOM 1297 CH2 TRP A 199 25.985 93.309 42.817 1.00 80.03 C ANISOU 1297 CH2 TRP A 199 10357 9164 10887 668 -284 -72 C ATOM 1298 N ILE A 200 26.114 88.170 49.178 1.00 75.03 N ANISOU 1298 N ILE A 200 10049 8761 9698 1541 -1156 -600 N ATOM 1299 CA ILE A 200 26.619 86.855 49.594 1.00 76.43 C ANISOU 1299 CA ILE A 200 10276 8971 9794 1702 -1221 -634 C ATOM 1300 C ILE A 200 25.769 85.763 48.910 1.00 79.63 C ANISOU 1300 C ILE A 200 10810 9368 10076 1679 -1066 -493 C ATOM 1301 O ILE A 200 26.330 84.795 48.382 1.00 79.24 O ANISOU 1301 O ILE A 200 10724 9337 10047 1712 -1028 -509 O ATOM 1302 CB ILE A 200 26.674 86.710 51.141 1.00 80.99 C ANISOU 1302 CB ILE A 200 10993 9541 10237 1911 -1413 -707 C ATOM 1303 CG1 ILE A 200 27.984 87.311 51.675 1.00 83.62 C ANISOU 1303 CG1 ILE A 200 11146 9892 10734 1973 -1634 -913 C ATOM 1304 CG2 ILE A 200 26.504 85.250 51.608 1.00 82.17 C ANISOU 1304 CG2 ILE A 200 11324 9687 10209 2086 -1409 -636 C ATOM 1305 CD1 ILE A 200 28.005 87.552 53.165 1.00 94.84 C ANISOU 1305 CD1 ILE A 200 12720 11307 12009 2172 -1863 -1018 C ATOM 1306 N ASN A 201 24.427 85.952 48.886 1.00 75.13 N ANISOU 1306 N ASN A 201 10372 8761 9414 1621 -982 -372 N ATOM 1307 CA ASN A 201 23.491 85.015 48.272 1.00 73.67 C ANISOU 1307 CA ASN A 201 10288 8544 9159 1582 -864 -258 C ATOM 1308 C ASN A 201 23.565 85.069 46.757 1.00 77.94 C ANISOU 1308 C ASN A 201 10745 9112 9758 1437 -772 -241 C ATOM 1309 O ASN A 201 23.323 84.051 46.119 1.00 78.43 O ANISOU 1309 O ASN A 201 10860 9158 9781 1433 -717 -216 O ATOM 1310 CB ASN A 201 22.076 85.254 48.756 1.00 70.48 C ANISOU 1310 CB ASN A 201 10001 8085 8695 1567 -813 -151 C ATOM 1311 CG ASN A 201 21.880 84.735 50.153 1.00 81.85 C ANISOU 1311 CG ASN A 201 11596 9485 10019 1741 -836 -130 C ATOM 1312 OD1 ASN A 201 21.889 83.524 50.395 1.00 77.77 O ANISOU 1312 OD1 ASN A 201 11174 8928 9449 1830 -802 -87 O ATOM 1313 ND2 ASN A 201 21.742 85.636 51.113 1.00 67.66 N ANISOU 1313 ND2 ASN A 201 9849 7689 8171 1810 -890 -160 N ATOM 1314 N PHE A 202 23.940 86.221 46.177 1.00 74.33 N ANISOU 1314 N PHE A 202 10176 8681 9386 1331 -749 -256 N ATOM 1315 CA PHE A 202 24.110 86.344 44.729 1.00 74.06 C ANISOU 1315 CA PHE A 202 10098 8674 9367 1219 -638 -225 C ATOM 1316 C PHE A 202 25.283 85.464 44.298 1.00 77.85 C ANISOU 1316 C PHE A 202 10504 9193 9881 1273 -594 -310 C ATOM 1317 O PHE A 202 25.182 84.742 43.307 1.00 76.70 O ANISOU 1317 O PHE A 202 10416 9062 9665 1256 -508 -296 O ATOM 1318 CB PHE A 202 24.325 87.816 44.321 1.00 76.43 C ANISOU 1318 CB PHE A 202 10310 8967 9765 1109 -595 -197 C ATOM 1319 CG PHE A 202 24.734 88.037 42.885 1.00 79.16 C ANISOU 1319 CG PHE A 202 10626 9337 10113 1019 -448 -153 C ATOM 1320 CD1 PHE A 202 23.825 87.854 41.848 1.00 82.31 C ANISOU 1320 CD1 PHE A 202 11160 9745 10370 977 -398 -59 C ATOM 1321 CD2 PHE A 202 26.034 88.414 42.566 1.00 83.06 C ANISOU 1321 CD2 PHE A 202 10961 9841 10757 989 -356 -208 C ATOM 1322 CE1 PHE A 202 24.209 88.049 40.515 1.00 84.53 C ANISOU 1322 CE1 PHE A 202 11468 10054 10595 927 -253 -11 C ATOM 1323 CE2 PHE A 202 26.419 88.604 41.231 1.00 87.10 C ANISOU 1323 CE2 PHE A 202 11473 10370 11251 922 -164 -145 C ATOM 1324 CZ PHE A 202 25.503 88.424 40.215 1.00 84.81 C ANISOU 1324 CZ PHE A 202 11370 10098 10757 901 -112 -41 C ATOM 1325 N LEU A 203 26.366 85.481 45.093 1.00 76.07 N ANISOU 1325 N LEU A 203 10158 8981 9766 1358 -672 -414 N ATOM 1326 CA LEU A 203 27.566 84.688 44.866 1.00 77.52 C ANISOU 1326 CA LEU A 203 10229 9195 10030 1437 -650 -510 C ATOM 1327 C LEU A 203 27.307 83.193 45.047 1.00 80.54 C ANISOU 1327 C LEU A 203 10746 9556 10299 1561 -675 -510 C ATOM 1328 O LEU A 203 27.835 82.406 44.273 1.00 80.65 O ANISOU 1328 O LEU A 203 10736 9583 10325 1589 -586 -551 O ATOM 1329 CB LEU A 203 28.708 85.143 45.782 1.00 79.30 C ANISOU 1329 CB LEU A 203 10268 9427 10434 1508 -784 -637 C ATOM 1330 CG LEU A 203 30.004 85.583 45.082 1.00 86.79 C ANISOU 1330 CG LEU A 203 10960 10396 11620 1446 -680 -717 C ATOM 1331 CD1 LEU A 203 30.410 84.600 43.958 1.00 87.96 C ANISOU 1331 CD1 LEU A 203 11102 10575 11742 1467 -497 -711 C ATOM 1332 CD2 LEU A 203 29.897 87.025 44.551 1.00 89.08 C ANISOU 1332 CD2 LEU A 203 11174 10656 12017 1265 -569 -659 C ATOM 1333 N ILE A 204 26.482 82.805 46.037 1.00 75.89 N ANISOU 1333 N ILE A 204 10307 8919 9608 1636 -769 -460 N ATOM 1334 CA ILE A 204 26.106 81.413 46.282 1.00 75.64 C ANISOU 1334 CA ILE A 204 10421 8826 9492 1741 -771 -430 C ATOM 1335 C ILE A 204 25.364 80.871 45.034 1.00 80.18 C ANISOU 1335 C ILE A 204 11071 9373 10020 1633 -652 -388 C ATOM 1336 O ILE A 204 25.651 79.761 44.581 1.00 80.74 O ANISOU 1336 O ILE A 204 11181 9410 10087 1691 -614 -431 O ATOM 1337 CB ILE A 204 25.261 81.322 47.585 1.00 78.24 C ANISOU 1337 CB ILE A 204 10905 9095 9728 1825 -841 -351 C ATOM 1338 CG1 ILE A 204 26.170 81.415 48.838 1.00 79.79 C ANISOU 1338 CG1 ILE A 204 11088 9312 9915 2009 -999 -423 C ATOM 1339 CG2 ILE A 204 24.391 80.057 47.621 1.00 78.56 C ANISOU 1339 CG2 ILE A 204 11110 9031 9711 1858 -772 -263 C ATOM 1340 CD1 ILE A 204 25.463 81.705 50.178 1.00 82.09 C ANISOU 1340 CD1 ILE A 204 11546 9570 10075 2107 -1062 -359 C ATOM 1341 N VAL A 205 24.460 81.690 44.462 1.00 75.58 N ANISOU 1341 N VAL A 205 10509 8803 9406 1491 -614 -322 N ATOM 1342 CA VAL A 205 23.654 81.388 43.281 1.00 75.17 C ANISOU 1342 CA VAL A 205 10533 8733 9294 1394 -557 -296 C ATOM 1343 C VAL A 205 24.563 81.279 42.028 1.00 82.80 C ANISOU 1343 C VAL A 205 11460 9761 10237 1381 -461 -370 C ATOM 1344 O VAL A 205 24.397 80.337 41.252 1.00 83.46 O ANISOU 1344 O VAL A 205 11634 9815 10260 1395 -432 -416 O ATOM 1345 CB VAL A 205 22.530 82.457 43.136 1.00 77.31 C ANISOU 1345 CB VAL A 205 10820 9005 9548 1278 -575 -205 C ATOM 1346 CG1 VAL A 205 22.030 82.606 41.700 1.00 77.05 C ANISOU 1346 CG1 VAL A 205 10840 8995 9440 1187 -548 -194 C ATOM 1347 CG2 VAL A 205 21.375 82.165 44.089 1.00 76.31 C ANISOU 1347 CG2 VAL A 205 10758 8792 9444 1293 -617 -134 C ATOM 1348 N ILE A 206 25.522 82.212 41.845 1.00 81.30 N ANISOU 1348 N ILE A 206 11139 9642 10109 1358 -397 -387 N ATOM 1349 CA ILE A 206 26.437 82.207 40.693 1.00 82.85 C ANISOU 1349 CA ILE A 206 11290 9893 10297 1351 -244 -436 C ATOM 1350 C ILE A 206 27.324 80.963 40.745 1.00 88.27 C ANISOU 1350 C ILE A 206 11944 10567 11027 1482 -218 -546 C ATOM 1351 O ILE A 206 27.413 80.265 39.741 1.00 90.37 O ANISOU 1351 O ILE A 206 12298 10835 11203 1506 -120 -594 O ATOM 1352 CB ILE A 206 27.279 83.527 40.601 1.00 87.15 C ANISOU 1352 CB ILE A 206 11664 10482 10968 1284 -151 -415 C ATOM 1353 CG1 ILE A 206 26.429 84.758 40.187 1.00 86.78 C ANISOU 1353 CG1 ILE A 206 11680 10431 10860 1159 -135 -294 C ATOM 1354 CG2 ILE A 206 28.524 83.383 39.711 1.00 90.95 C ANISOU 1354 CG2 ILE A 206 12041 11006 11511 1308 51 -473 C ATOM 1355 CD1 ILE A 206 25.692 84.693 38.806 1.00 93.47 C ANISOU 1355 CD1 ILE A 206 12722 11296 11497 1118 -63 -227 C ATOM 1356 N VAL A 207 27.938 80.670 41.912 1.00 83.90 N ANISOU 1356 N VAL A 207 11288 9995 10597 1587 -318 -592 N ATOM 1357 CA VAL A 207 28.839 79.524 42.121 1.00 84.54 C ANISOU 1357 CA VAL A 207 11322 10052 10748 1742 -321 -690 C ATOM 1358 C VAL A 207 28.091 78.191 41.940 1.00 88.99 C ANISOU 1358 C VAL A 207 12084 10523 11204 1796 -341 -693 C ATOM 1359 O VAL A 207 28.597 77.331 41.220 1.00 90.78 O ANISOU 1359 O VAL A 207 12331 10732 11428 1865 -253 -778 O ATOM 1360 CB VAL A 207 29.583 79.593 43.487 1.00 88.07 C ANISOU 1360 CB VAL A 207 11634 10496 11331 1866 -478 -733 C ATOM 1361 CG1 VAL A 207 30.314 78.289 43.806 1.00 89.02 C ANISOU 1361 CG1 VAL A 207 11745 10571 11506 2057 -519 -813 C ATOM 1362 CG2 VAL A 207 30.563 80.759 43.508 1.00 88.61 C ANISOU 1362 CG2 VAL A 207 11455 10632 11579 1813 -457 -783 C ATOM 1363 N CYS A 208 26.911 78.020 42.572 1.00 84.03 N ANISOU 1363 N CYS A 208 11590 9821 10515 1764 -439 -609 N ATOM 1364 CA CYS A 208 26.127 76.781 42.476 1.00 83.79 C ANISOU 1364 CA CYS A 208 11724 9665 10446 1791 -454 -607 C ATOM 1365 C CYS A 208 25.674 76.515 41.036 1.00 87.18 C ANISOU 1365 C CYS A 208 12243 10092 10789 1705 -384 -667 C ATOM 1366 O CYS A 208 25.728 75.367 40.599 1.00 88.16 O ANISOU 1366 O CYS A 208 12452 10131 10914 1769 -363 -752 O ATOM 1367 CB CYS A 208 24.935 76.798 43.430 1.00 83.19 C ANISOU 1367 CB CYS A 208 11739 9505 10365 1754 -529 -490 C ATOM 1368 SG CYS A 208 25.368 76.650 45.189 1.00 87.28 S ANISOU 1368 SG CYS A 208 12266 9984 10910 1926 -614 -427 S ATOM 1369 N TYR A 209 25.262 77.556 40.294 1.00 82.27 N ANISOU 1369 N TYR A 209 11620 9555 10083 1581 -357 -630 N ATOM 1370 CA TYR A 209 24.800 77.353 38.923 1.00 82.98 C ANISOU 1370 CA TYR A 209 11834 9652 10041 1526 -325 -689 C ATOM 1371 C TYR A 209 25.951 77.307 37.908 1.00 87.83 C ANISOU 1371 C TYR A 209 12439 10350 10583 1590 -162 -778 C ATOM 1372 O TYR A 209 25.725 76.872 36.778 1.00 88.27 O ANISOU 1372 O TYR A 209 12643 10403 10492 1596 -129 -858 O ATOM 1373 CB TYR A 209 23.714 78.358 38.530 1.00 83.55 C ANISOU 1373 CB TYR A 209 11950 9762 10033 1396 -388 -601 C ATOM 1374 CG TYR A 209 22.372 77.919 39.076 1.00 85.12 C ANISOU 1374 CG TYR A 209 12195 9844 10305 1342 -524 -565 C ATOM 1375 CD1 TYR A 209 21.578 77.012 38.377 1.00 88.17 C ANISOU 1375 CD1 TYR A 209 12693 10135 10672 1318 -605 -652 C ATOM 1376 CD2 TYR A 209 21.951 78.307 40.347 1.00 84.53 C ANISOU 1376 CD2 TYR A 209 12044 9733 10340 1325 -561 -457 C ATOM 1377 CE1 TYR A 209 20.377 76.544 38.906 1.00 89.16 C ANISOU 1377 CE1 TYR A 209 12816 10125 10935 1256 -707 -622 C ATOM 1378 CE2 TYR A 209 20.748 77.853 40.883 1.00 85.20 C ANISOU 1378 CE2 TYR A 209 12154 9695 10522 1279 -630 -410 C ATOM 1379 CZ TYR A 209 19.969 76.962 40.163 1.00 95.21 C ANISOU 1379 CZ TYR A 209 13495 10859 11821 1236 -695 -488 C ATOM 1380 OH TYR A 209 18.787 76.496 40.685 1.00 97.38 O ANISOU 1380 OH TYR A 209 13755 10989 12257 1175 -742 -444 O ATOM 1381 N THR A 210 27.187 77.667 38.321 1.00 84.17 N ANISOU 1381 N THR A 210 11802 9948 10231 1649 -63 -781 N ATOM 1382 CA THR A 210 28.372 77.519 37.475 1.00 85.56 C ANISOU 1382 CA THR A 210 11926 10184 10398 1724 135 -866 C ATOM 1383 C THR A 210 28.778 76.040 37.549 1.00 90.15 C ANISOU 1383 C THR A 210 12550 10678 11027 1870 129 -994 C ATOM 1384 O THR A 210 29.021 75.415 36.517 1.00 92.05 O ANISOU 1384 O THR A 210 12901 10913 11159 1930 246 -1098 O ATOM 1385 CB THR A 210 29.493 78.491 37.893 1.00 91.02 C ANISOU 1385 CB THR A 210 12368 10953 11264 1717 236 -831 C ATOM 1386 OG1 THR A 210 29.098 79.818 37.542 1.00 87.52 O ANISOU 1386 OG1 THR A 210 11926 10564 10764 1579 276 -716 O ATOM 1387 CG2 THR A 210 30.837 78.176 37.222 1.00 90.58 C ANISOU 1387 CG2 THR A 210 12196 10937 11282 1812 468 -924 C ATOM 1388 N LEU A 211 28.794 75.480 38.769 1.00 84.92 N ANISOU 1388 N LEU A 211 11829 9933 10506 1939 -10 -982 N ATOM 1389 CA LEU A 211 29.134 74.087 39.028 1.00 86.01 C ANISOU 1389 CA LEU A 211 12013 9953 10715 2089 -36 -1073 C ATOM 1390 C LEU A 211 28.108 73.125 38.409 1.00 90.07 C ANISOU 1390 C LEU A 211 12756 10342 11126 2059 -82 -1131 C ATOM 1391 O LEU A 211 28.495 72.049 37.956 1.00 91.74 O ANISOU 1391 O LEU A 211 13040 10468 11351 2170 -32 -1256 O ATOM 1392 CB LEU A 211 29.253 73.832 40.537 1.00 85.66 C ANISOU 1392 CB LEU A 211 11899 9843 10806 2176 -184 -1005 C ATOM 1393 CG LEU A 211 30.409 74.540 41.273 1.00 91.31 C ANISOU 1393 CG LEU A 211 12375 10653 11664 2254 -205 -1004 C ATOM 1394 CD1 LEU A 211 30.143 74.609 42.763 1.00 90.77 C ANISOU 1394 CD1 LEU A 211 12313 10542 11633 2314 -393 -915 C ATOM 1395 CD2 LEU A 211 31.728 73.849 41.034 1.00 96.48 C ANISOU 1395 CD2 LEU A 211 12900 11305 12452 2426 -123 -1129 C ATOM 1396 N ILE A 212 26.817 73.522 38.362 1.00 85.00 N ANISOU 1396 N ILE A 212 12211 9678 10408 1913 -184 -1058 N ATOM 1397 CA ILE A 212 25.724 72.725 37.788 1.00 84.96 C ANISOU 1397 CA ILE A 212 12384 9543 10352 1858 -269 -1127 C ATOM 1398 C ILE A 212 25.847 72.711 36.245 1.00 90.15 C ANISOU 1398 C ILE A 212 13170 10268 10813 1861 -195 -1263 C ATOM 1399 O ILE A 212 25.796 71.626 35.655 1.00 91.76 O ANISOU 1399 O ILE A 212 13508 10362 10996 1924 -207 -1417 O ATOM 1400 CB ILE A 212 24.334 73.218 38.300 1.00 86.40 C ANISOU 1400 CB ILE A 212 12578 9681 10567 1710 -404 -1006 C ATOM 1401 CG1 ILE A 212 24.027 72.591 39.684 1.00 85.98 C ANISOU 1401 CG1 ILE A 212 12499 9479 10690 1748 -451 -911 C ATOM 1402 CG2 ILE A 212 23.198 72.931 37.301 1.00 88.10 C ANISOU 1402 CG2 ILE A 212 12931 9829 10713 1612 -509 -1095 C ATOM 1403 CD1 ILE A 212 23.016 73.329 40.535 1.00 88.21 C ANISOU 1403 CD1 ILE A 212 12737 9757 11021 1644 -511 -752 C ATOM 1404 N THR A 213 26.044 73.897 35.610 1.00 85.54 N ANISOU 1404 N THR A 213 12567 9853 10082 1809 -108 -1207 N ATOM 1405 CA THR A 213 26.209 74.055 34.157 1.00 86.99 C ANISOU 1405 CA THR A 213 12909 10119 10023 1838 -4 -1301 C ATOM 1406 C THR A 213 27.402 73.215 33.685 1.00 93.10 C ANISOU 1406 C THR A 213 13696 10884 10794 2001 184 -1444 C ATOM 1407 O THR A 213 27.274 72.490 32.701 1.00 94.97 O ANISOU 1407 O THR A 213 14135 11083 10868 2070 200 -1603 O ATOM 1408 CB THR A 213 26.366 75.544 33.787 1.00 96.91 C ANISOU 1408 CB THR A 213 14127 11535 11158 1765 99 -1162 C ATOM 1409 OG1 THR A 213 25.283 76.291 34.341 1.00 96.20 O ANISOU 1409 OG1 THR A 213 14007 11438 11109 1633 -78 -1034 O ATOM 1410 CG2 THR A 213 26.412 75.781 32.284 1.00 97.81 C ANISOU 1410 CG2 THR A 213 14464 11731 10968 1808 211 -1221 C ATOM 1411 N LYS A 214 28.532 73.279 34.424 1.00 89.49 N ANISOU 1411 N LYS A 214 13019 10453 10530 2074 303 -1405 N ATOM 1412 CA LYS A 214 29.767 72.525 34.177 1.00 91.27 C ANISOU 1412 CA LYS A 214 13184 10665 10830 2245 485 -1529 C ATOM 1413 C LYS A 214 29.494 71.018 34.145 1.00 95.39 C ANISOU 1413 C LYS A 214 13852 11007 11384 2346 390 -1687 C ATOM 1414 O LYS A 214 29.969 70.347 33.227 1.00 98.59 O ANISOU 1414 O LYS A 214 14372 11393 11694 2468 527 -1848 O ATOM 1415 CB LYS A 214 30.808 72.861 35.261 1.00 93.82 C ANISOU 1415 CB LYS A 214 13207 11023 11418 2296 525 -1456 C ATOM 1416 CG LYS A 214 32.159 72.153 35.136 1.00112.71 C ANISOU 1416 CG LYS A 214 15467 13405 13954 2484 704 -1577 C ATOM 1417 CD LYS A 214 33.082 72.461 36.327 1.00125.93 C ANISOU 1417 CD LYS A 214 16827 15102 15917 2543 659 -1522 C ATOM 1418 CE LYS A 214 32.769 71.663 37.581 1.00137.79 C ANISOU 1418 CE LYS A 214 18338 16472 17546 2621 412 -1501 C ATOM 1419 NZ LYS A 214 33.652 72.040 38.718 1.00145.69 N ANISOU 1419 NZ LYS A 214 19065 17512 18780 2699 322 -1458 N ATOM 1420 N GLU A 215 28.731 70.493 35.128 1.00 88.90 N ANISOU 1420 N GLU A 215 13038 10039 10701 2299 178 -1639 N ATOM 1421 CA GLU A 215 28.395 69.067 35.221 1.00 89.46 C ANISOU 1421 CA GLU A 215 13239 9894 10860 2373 88 -1764 C ATOM 1422 C GLU A 215 27.456 68.641 34.081 1.00 94.17 C ANISOU 1422 C GLU A 215 14080 10421 11278 2313 6 -1918 C ATOM 1423 O GLU A 215 27.636 67.559 33.522 1.00 95.71 O ANISOU 1423 O GLU A 215 14412 10485 11469 2419 23 -2108 O ATOM 1424 CB GLU A 215 27.770 68.734 36.584 1.00 89.19 C ANISOU 1424 CB GLU A 215 13150 9711 11025 2331 -73 -1632 C ATOM 1425 N LEU A 216 26.494 69.514 33.715 1.00 89.51 N ANISOU 1425 N LEU A 216 13547 9919 10545 2159 -99 -1852 N ATOM 1426 CA LEU A 216 25.526 69.292 32.642 1.00 90.71 C ANISOU 1426 CA LEU A 216 13920 10030 10518 2102 -238 -1997 C ATOM 1427 C LEU A 216 26.202 69.340 31.269 1.00 95.53 C ANISOU 1427 C LEU A 216 14711 10758 10829 2226 -82 -2150 C ATOM 1428 O LEU A 216 25.835 68.562 30.381 1.00 97.84 O ANISOU 1428 O LEU A 216 15225 10958 10989 2277 -174 -2367 O ATOM 1429 CB LEU A 216 24.398 70.332 32.724 1.00 89.68 C ANISOU 1429 CB LEU A 216 13765 9974 10337 1930 -398 -1859 C ATOM 1430 CG LEU A 216 23.070 69.884 33.366 1.00 95.10 C ANISOU 1430 CG LEU A 216 14420 10472 11240 1796 -631 -1844 C ATOM 1431 CD1 LEU A 216 23.228 69.557 34.865 1.00 93.99 C ANISOU 1431 CD1 LEU A 216 14104 10223 11385 1785 -590 -1685 C ATOM 1432 CD2 LEU A 216 22.025 70.974 33.237 1.00 97.83 C ANISOU 1432 CD2 LEU A 216 14749 10910 11511 1655 -780 -1744 C ATOM 1433 N TYR A 217 27.202 70.231 31.102 1.00 90.27 N ANISOU 1433 N TYR A 217 13953 10280 10064 2278 164 -2044 N ATOM 1434 CA TYR A 217 27.964 70.357 29.862 1.00 91.90 C ANISOU 1434 CA TYR A 217 14322 10604 9991 2409 398 -2147 C ATOM 1435 C TYR A 217 28.764 69.075 29.614 1.00 97.21 C ANISOU 1435 C TYR A 217 15048 11163 10725 2594 525 -2357 C ATOM 1436 O TYR A 217 28.646 68.494 28.536 1.00 99.27 O ANISOU 1436 O TYR A 217 15576 11395 10748 2697 542 -2563 O ATOM 1437 CB TYR A 217 28.892 71.596 29.895 1.00 92.18 C ANISOU 1437 CB TYR A 217 14190 10830 10003 2400 669 -1958 C ATOM 1438 CG TYR A 217 29.871 71.667 28.738 1.00 96.43 C ANISOU 1438 CG TYR A 217 14851 11473 10317 2553 1009 -2034 C ATOM 1439 CD1 TYR A 217 31.178 71.205 28.874 1.00 99.50 C ANISOU 1439 CD1 TYR A 217 15064 11856 10885 2691 1276 -2088 C ATOM 1440 CD2 TYR A 217 29.488 72.185 27.504 1.00 98.89 C ANISOU 1440 CD2 TYR A 217 15456 11883 10234 2578 1074 -2045 C ATOM 1441 CE1 TYR A 217 32.077 71.248 27.811 1.00103.36 C ANISOU 1441 CE1 TYR A 217 15652 12432 11189 2838 1637 -2154 C ATOM 1442 CE2 TYR A 217 30.381 72.241 26.434 1.00103.10 C ANISOU 1442 CE2 TYR A 217 16135 12507 10531 2736 1434 -2097 C ATOM 1443 CZ TYR A 217 31.678 71.778 26.595 1.00111.74 C ANISOU 1443 CZ TYR A 217 17031 13590 11833 2859 1737 -2150 C ATOM 1444 OH TYR A 217 32.569 71.826 25.548 1.00115.00 O ANISOU 1444 OH TYR A 217 17572 14085 12039 3021 2141 -2197 O ATOM 1445 N ARG A 218 29.552 68.630 30.621 1.00 92.47 N ANISOU 1445 N ARG A 218 14207 10492 10437 2652 592 -2313 N ATOM 1446 CA ARG A 218 30.400 67.439 30.547 1.00 94.21 C ANISOU 1446 CA ARG A 218 14429 10590 10776 2845 714 -2487 C ATOM 1447 C ARG A 218 29.581 66.153 30.390 1.00 98.09 C ANISOU 1447 C ARG A 218 15131 10842 11299 2864 496 -2685 C ATOM 1448 O ARG A 218 30.064 65.205 29.769 1.00 99.70 O ANISOU 1448 O ARG A 218 15468 10947 11467 3031 596 -2899 O ATOM 1449 CB ARG A 218 31.322 67.354 31.766 1.00 94.73 C ANISOU 1449 CB ARG A 218 14180 10637 11177 2905 774 -2369 C ATOM 1450 CG ARG A 218 32.651 68.058 31.527 1.00110.57 C ANISOU 1450 CG ARG A 218 15984 12821 13207 2994 1085 -2321 C ATOM 1451 CD ARG A 218 33.258 68.644 32.791 1.00123.49 C ANISOU 1451 CD ARG A 218 17271 14503 15145 2976 1059 -2156 C ATOM 1452 NE ARG A 218 34.548 69.289 32.523 1.00138.37 N ANISOU 1452 NE ARG A 218 18922 16531 17123 3054 1358 -2141 N ATOM 1453 CZ ARG A 218 34.706 70.570 32.196 1.00155.10 C ANISOU 1453 CZ ARG A 218 20943 18811 19178 2937 1510 -2013 C ATOM 1454 NH1 ARG A 218 33.652 71.372 32.090 1.00140.00 N ANISOU 1454 NH1 ARG A 218 19160 16952 17083 2751 1373 -1888 N ATOM 1455 NH2 ARG A 218 35.918 71.059 31.972 1.00145.92 N ANISOU 1455 NH2 ARG A 218 19537 17741 18164 3005 1808 -2007 N ATOM 1456 N SER A 219 28.336 66.134 30.905 1.00 93.20 N ANISOU 1456 N SER A 219 14537 10114 10760 2692 215 -2625 N ATOM 1457 CA SER A 219 27.445 64.978 30.756 1.00 94.26 C ANISOU 1457 CA SER A 219 14842 9993 10980 2670 -2 -2811 C ATOM 1458 C SER A 219 26.901 64.915 29.320 1.00 98.91 C ANISOU 1458 C SER A 219 15728 10611 11242 2687 -84 -3044 C ATOM 1459 O SER A 219 26.866 63.833 28.734 1.00100.88 O ANISOU 1459 O SER A 219 16163 10685 11480 2787 -134 -3305 O ATOM 1460 CB SER A 219 26.303 65.031 31.766 1.00 95.89 C ANISOU 1460 CB SER A 219 14946 10070 11417 2476 -237 -2660 C ATOM 1461 OG SER A 219 25.543 63.834 31.715 1.00108.67 O ANISOU 1461 OG SER A 219 16683 11399 13207 2448 -413 -2832 O ATOM 1462 N TYR A 220 26.510 66.081 28.752 1.00 93.42 N ANISOU 1462 N TYR A 220 15093 10131 10270 2608 -102 -2954 N ATOM 1463 CA TYR A 220 25.997 66.198 27.386 1.00 95.02 C ANISOU 1463 CA TYR A 220 15606 10401 10097 2649 -199 -3143 C ATOM 1464 C TYR A 220 27.089 65.885 26.354 1.00 99.37 C ANISOU 1464 C TYR A 220 16356 11032 10367 2883 90 -3313 C ATOM 1465 O TYR A 220 26.802 65.232 25.351 1.00102.44 O ANISOU 1465 O TYR A 220 17047 11351 10526 2987 -9 -3589 O ATOM 1466 CB TYR A 220 25.399 67.604 27.134 1.00 95.19 C ANISOU 1466 CB TYR A 220 15635 10631 9901 2530 -269 -2952 C ATOM 1467 CG TYR A 220 25.146 67.894 25.670 1.00100.89 C ANISOU 1467 CG TYR A 220 16708 11472 10155 2629 -313 -3103 C ATOM 1468 CD1 TYR A 220 24.110 67.265 24.984 1.00105.41 C ANISOU 1468 CD1 TYR A 220 17510 11921 10620 2621 -664 -3357 C ATOM 1469 CD2 TYR A 220 25.987 68.738 24.951 1.00103.27 C ANISOU 1469 CD2 TYR A 220 17123 11993 10121 2746 0 -3003 C ATOM 1470 CE1 TYR A 220 23.909 67.481 23.620 1.00110.31 C ANISOU 1470 CE1 TYR A 220 18496 12653 10763 2752 -737 -3516 C ATOM 1471 CE2 TYR A 220 25.796 68.962 23.586 1.00107.66 C ANISOU 1471 CE2 TYR A 220 18057 12655 10193 2875 -17 -3128 C ATOM 1472 CZ TYR A 220 24.749 68.338 22.927 1.00118.55 C ANISOU 1472 CZ TYR A 220 19693 13927 11424 2888 -405 -3388 C ATOM 1473 OH TYR A 220 24.554 68.562 21.584 1.00125.18 O ANISOU 1473 OH TYR A 220 20941 14878 11744 3045 -459 -3522 O ATOM 1474 N VAL A 221 28.318 66.377 26.583 1.00 93.59 N ANISOU 1474 N VAL A 221 15455 10445 9659 2969 444 -3159 N ATOM 1475 CA VAL A 221 29.457 66.186 25.682 1.00 96.00 C ANISOU 1475 CA VAL A 221 15894 10837 9744 3194 798 -3282 C ATOM 1476 C VAL A 221 29.803 64.688 25.592 1.00101.62 C ANISOU 1476 C VAL A 221 16692 11324 10594 3355 795 -3562 C ATOM 1477 O VAL A 221 29.991 64.185 24.490 1.00104.80 O ANISOU 1477 O VAL A 221 17395 11715 10707 3527 885 -3808 O ATOM 1478 CB VAL A 221 30.674 67.065 26.098 1.00 98.46 C ANISOU 1478 CB VAL A 221 15916 11322 10170 3219 1169 -3046 C ATOM 1479 CG1 VAL A 221 31.953 66.660 25.362 1.00101.69 C ANISOU 1479 CG1 VAL A 221 16385 11775 10478 3460 1573 -3180 C ATOM 1480 CG2 VAL A 221 30.378 68.543 25.858 1.00 96.73 C ANISOU 1480 CG2 VAL A 221 15695 11308 9748 3090 1216 -2809 C ATOM 1481 N ARG A 222 29.821 63.981 26.736 1.00 96.21 N ANISOU 1481 N ARG A 222 15778 10448 10330 3309 679 -3524 N ATOM 1482 CA ARG A 222 30.126 62.552 26.843 1.00 97.73 C ANISOU 1482 CA ARG A 222 16021 10384 10727 3451 662 -3749 C ATOM 1483 C ARG A 222 29.122 61.695 26.041 1.00103.34 C ANISOU 1483 C ARG A 222 17063 10903 11300 3443 381 -4054 C ATOM 1484 O ARG A 222 29.544 60.773 25.334 1.00106.99 O ANISOU 1484 O ARG A 222 17732 11245 11676 3634 464 -4335 O ATOM 1485 CB ARG A 222 30.143 62.137 28.328 1.00 96.87 C ANISOU 1485 CB ARG A 222 15621 10109 11074 3379 558 -3580 C ATOM 1486 CG ARG A 222 30.635 60.717 28.592 1.00117.06 C ANISOU 1486 CG ARG A 222 18197 12391 13891 3548 579 -3754 C ATOM 1487 CD ARG A 222 29.708 59.958 29.522 1.00130.93 C ANISOU 1487 CD ARG A 222 19914 13862 15973 3415 299 -3705 C ATOM 1488 NE ARG A 222 28.451 59.590 28.865 1.00141.25 N ANISOU 1488 NE ARG A 222 21453 15021 17195 3278 30 -3893 N ATOM 1489 CZ ARG A 222 28.135 58.359 28.479 1.00157.29 C ANISOU 1489 CZ ARG A 222 23680 16764 19320 3341 -83 -4177 C ATOM 1490 NH1 ARG A 222 28.975 57.352 28.689 1.00144.36 N ANISOU 1490 NH1 ARG A 222 22052 14946 17851 3548 66 -4291 N ATOM 1491 NH2 ARG A 222 26.970 58.122 27.891 1.00146.68 N ANISOU 1491 NH2 ARG A 222 22511 15292 17928 3201 -364 -4360 N ATOM 1492 N THR A 223 27.814 62.018 26.132 1.00 97.75 N ANISOU 1492 N THR A 223 16394 10161 10585 3231 49 -4015 N ATOM 1493 CA THR A 223 26.729 61.309 25.441 1.00 99.99 C ANISOU 1493 CA THR A 223 16939 10256 10798 3188 -284 -4308 C ATOM 1494 C THR A 223 26.781 61.560 23.920 1.00108.04 C ANISOU 1494 C THR A 223 18331 11436 11284 3341 -257 -4537 C ATOM 1495 O THR A 223 26.654 60.610 23.142 1.00110.74 O ANISOU 1495 O THR A 223 18946 11614 11516 3463 -372 -4885 O ATOM 1496 CB THR A 223 25.349 61.714 26.010 1.00103.67 C ANISOU 1496 CB THR A 223 17280 10657 11452 2919 -630 -4180 C ATOM 1497 OG1 THR A 223 25.427 61.905 27.422 1.00 98.39 O ANISOU 1497 OG1 THR A 223 16284 9937 11164 2798 -570 -3883 O ATOM 1498 CG2 THR A 223 24.270 60.689 25.706 1.00105.14 C ANISOU 1498 CG2 THR A 223 17612 10544 11794 2846 -987 -4480 C ATOM 1499 N ALA A1001 26.942 62.839 23.513 1.00 79.73 N ANISOU 1499 N ALA A1001 10432 9830 10032 1585 -226 -3435 N ATOM 1500 CA ALA A1001 27.003 63.289 22.116 1.00 78.34 C ANISOU 1500 CA ALA A1001 10261 9282 10222 1593 -548 -3238 C ATOM 1501 C ALA A1001 28.206 62.700 21.388 1.00 78.79 C ANISOU 1501 C ALA A1001 10491 9192 10255 1230 -650 -2787 C ATOM 1502 O ALA A1001 28.041 62.226 20.263 1.00 75.70 O ANISOU 1502 O ALA A1001 10006 8765 9993 1139 -687 -2529 O ATOM 1503 CB ALA A1001 27.048 64.815 22.048 1.00 82.18 C ANISOU 1503 CB ALA A1001 10951 9320 10952 1875 -912 -3497 C ATOM 1504 N ASP A1002 29.403 62.709 22.035 1.00 76.39 N ANISOU 1504 N ASP A1002 10417 8827 9781 1044 -704 -2724 N ATOM 1505 CA ASP A1002 30.639 62.156 21.472 1.00 74.01 C ANISOU 1505 CA ASP A1002 10215 8419 9485 723 -774 -2344 C ATOM 1506 C ASP A1002 30.494 60.661 21.231 1.00 77.00 C ANISOU 1506 C ASP A1002 10427 9114 9718 552 -500 -2090 C ATOM 1507 O ASP A1002 30.891 60.176 20.177 1.00 74.19 O ANISOU 1507 O ASP A1002 10053 8674 9463 395 -527 -1804 O ATOM 1508 CB ASP A1002 31.853 62.430 22.388 1.00 77.34 C ANISOU 1508 CB ASP A1002 10833 8762 9790 597 -917 -2403 C ATOM 1509 CG ASP A1002 32.313 63.880 22.527 1.00100.65 C ANISOU 1509 CG ASP A1002 13985 11299 12961 666 -1253 -2623 C ATOM 1510 OD1 ASP A1002 31.749 64.762 21.825 1.00104.81 O ANISOU 1510 OD1 ASP A1002 14547 11532 13745 828 -1390 -2690 O ATOM 1511 OD2 ASP A1002 33.214 64.142 23.368 1.00110.08 O ANISOU 1511 OD2 ASP A1002 15312 12437 14079 571 -1419 -2746 O ATOM 1512 N LEU A1003 29.899 59.939 22.197 1.00 76.93 N ANISOU 1512 N LEU A1003 10315 9450 9463 581 -224 -2198 N ATOM 1513 CA LEU A1003 29.673 58.496 22.131 1.00 76.08 C ANISOU 1513 CA LEU A1003 10075 9597 9237 402 46 -1968 C ATOM 1514 C LEU A1003 28.646 58.157 21.051 1.00 81.12 C ANISOU 1514 C LEU A1003 10456 10257 10109 422 100 -1931 C ATOM 1515 O LEU A1003 28.859 57.192 20.315 1.00 78.71 O ANISOU 1515 O LEU A1003 10108 9953 9846 241 139 -1687 O ATOM 1516 CB LEU A1003 29.240 57.960 23.512 1.00 78.76 C ANISOU 1516 CB LEU A1003 10421 10269 9236 413 348 -2075 C ATOM 1517 CG LEU A1003 29.151 56.438 23.747 1.00 82.58 C ANISOU 1517 CG LEU A1003 10853 10967 9556 189 640 -1800 C ATOM 1518 CD1 LEU A1003 30.270 55.671 23.066 1.00 79.25 C ANISOU 1518 CD1 LEU A1003 10541 10370 9200 -4 485 -1472 C ATOM 1519 CD2 LEU A1003 29.151 56.130 25.229 1.00 87.79 C ANISOU 1519 CD2 LEU A1003 11683 11896 9779 194 877 -1842 C ATOM 1520 N GLU A1004 27.569 58.962 20.917 1.00 81.70 N ANISOU 1520 N GLU A1004 10361 10329 10354 669 55 -2201 N ATOM 1521 CA GLU A1004 26.568 58.746 19.869 1.00 82.92 C ANISOU 1521 CA GLU A1004 10248 10498 10759 731 5 -2208 C ATOM 1522 C GLU A1004 27.210 59.020 18.495 1.00 87.08 C ANISOU 1522 C GLU A1004 10963 10715 11408 694 -313 -1980 C ATOM 1523 O GLU A1004 26.907 58.320 17.524 1.00 86.19 O ANISOU 1523 O GLU A1004 10750 10628 11370 613 -353 -1850 O ATOM 1524 CB GLU A1004 25.310 59.606 20.102 1.00 88.44 C ANISOU 1524 CB GLU A1004 10691 11271 11643 1063 -10 -2581 C ATOM 1525 CG GLU A1004 24.205 59.454 19.055 1.00104.70 C ANISOU 1525 CG GLU A1004 12418 13363 14002 1173 -141 -2640 C ATOM 1526 CD GLU A1004 23.682 58.054 18.769 1.00131.57 C ANISOU 1526 CD GLU A1004 15533 17013 17447 908 75 -2517 C ATOM 1527 OE1 GLU A1004 22.820 57.571 19.539 1.00134.41 O ANISOU 1527 OE1 GLU A1004 15547 17684 17839 864 419 -2678 O ATOM 1528 OE2 GLU A1004 24.099 57.461 17.746 1.00119.56 O ANISOU 1528 OE2 GLU A1004 14128 15362 15938 741 -92 -2276 O ATOM 1529 N ASP A1005 28.134 60.002 18.437 1.00 84.37 N ANISOU 1529 N ASP A1005 10908 10083 11066 726 -521 -1932 N ATOM 1530 CA ASP A1005 28.886 60.344 17.233 1.00 83.12 C ANISOU 1530 CA ASP A1005 10970 9636 10976 646 -745 -1671 C ATOM 1531 C ASP A1005 29.803 59.169 16.842 1.00 81.83 C ANISOU 1531 C ASP A1005 10846 9568 10676 361 -596 -1388 C ATOM 1532 O ASP A1005 29.874 58.840 15.657 1.00 80.01 O ANISOU 1532 O ASP A1005 10670 9279 10450 309 -660 -1206 O ATOM 1533 CB ASP A1005 29.683 61.651 17.437 1.00 87.26 C ANISOU 1533 CB ASP A1005 11760 9811 11585 682 -954 -1685 C ATOM 1534 CG ASP A1005 30.560 62.079 16.270 1.00106.42 C ANISOU 1534 CG ASP A1005 14428 11932 14074 543 -1112 -1364 C ATOM 1535 OD1 ASP A1005 30.134 61.896 15.099 1.00109.10 O ANISOU 1535 OD1 ASP A1005 14794 12253 14405 593 -1186 -1211 O ATOM 1536 OD2 ASP A1005 31.660 62.620 16.524 1.00115.04 O ANISOU 1536 OD2 ASP A1005 15682 12811 15218 377 -1162 -1272 O ATOM 1537 N ASN A1006 30.445 58.507 17.839 1.00 76.38 N ANISOU 1537 N ASN A1006 10144 9032 9846 216 -413 -1371 N ATOM 1538 CA ASN A1006 31.325 57.340 17.648 1.00 73.50 C ANISOU 1538 CA ASN A1006 9798 8744 9386 1 -288 -1141 C ATOM 1539 C ASN A1006 30.595 56.174 16.981 1.00 76.42 C ANISOU 1539 C ASN A1006 10028 9250 9759 -49 -174 -1086 C ATOM 1540 O ASN A1006 31.126 55.597 16.038 1.00 74.63 O ANISOU 1540 O ASN A1006 9863 8968 9526 -139 -184 -922 O ATOM 1541 CB ASN A1006 31.926 56.864 18.979 1.00 72.62 C ANISOU 1541 CB ASN A1006 9714 8764 9115 -76 -178 -1155 C ATOM 1542 CG ASN A1006 32.999 57.763 19.559 1.00 91.06 C ANISOU 1542 CG ASN A1006 12189 10953 11457 -91 -348 -1192 C ATOM 1543 OD1 ASN A1006 33.777 58.401 18.836 1.00 79.92 O ANISOU 1543 OD1 ASN A1006 10839 9326 10199 -163 -484 -1086 O ATOM 1544 ND2 ASN A1006 33.099 57.791 20.887 1.00 81.80 N ANISOU 1544 ND2 ASN A1006 11075 9899 10107 -48 -341 -1339 N ATOM 1545 N TRP A1007 29.381 55.841 17.446 1.00 75.04 N ANISOU 1545 N TRP A1007 9650 9249 9612 4 -61 -1247 N ATOM 1546 CA TRP A1007 28.620 54.733 16.879 1.00 75.41 C ANISOU 1546 CA TRP A1007 9522 9397 9732 -87 18 -1232 C ATOM 1547 C TRP A1007 28.037 55.077 15.504 1.00 80.10 C ANISOU 1547 C TRP A1007 10083 9902 10450 27 -224 -1278 C ATOM 1548 O TRP A1007 27.954 54.178 14.663 1.00 79.41 O ANISOU 1548 O TRP A1007 9982 9814 10376 -67 -254 -1222 O ATOM 1549 CB TRP A1007 27.523 54.247 17.831 1.00 76.50 C ANISOU 1549 CB TRP A1007 9400 9761 9904 -124 255 -1375 C ATOM 1550 CG TRP A1007 28.049 53.514 19.034 1.00 77.76 C ANISOU 1550 CG TRP A1007 9661 10019 9864 -280 506 -1248 C ATOM 1551 CD1 TRP A1007 28.067 53.964 20.323 1.00 82.31 C ANISOU 1551 CD1 TRP A1007 10293 10733 10249 -221 656 -1330 C ATOM 1552 CD2 TRP A1007 28.629 52.196 19.060 1.00 76.78 C ANISOU 1552 CD2 TRP A1007 9646 9846 9682 -487 602 -1017 C ATOM 1553 NE1 TRP A1007 28.622 53.012 21.151 1.00 81.98 N ANISOU 1553 NE1 TRP A1007 10409 10746 9994 -384 826 -1128 N ATOM 1554 CE2 TRP A1007 28.979 51.918 20.401 1.00 81.88 C ANISOU 1554 CE2 TRP A1007 10425 10595 10090 -543 787 -925 C ATOM 1555 CE3 TRP A1007 28.873 51.214 18.082 1.00 76.88 C ANISOU 1555 CE3 TRP A1007 9683 9720 9806 -602 531 -900 C ATOM 1556 CZ2 TRP A1007 29.570 50.705 20.789 1.00 81.17 C ANISOU 1556 CZ2 TRP A1007 10498 10443 9899 -704 875 -678 C ATOM 1557 CZ3 TRP A1007 29.478 50.021 18.465 1.00 78.11 C ANISOU 1557 CZ3 TRP A1007 9978 9801 9898 -752 634 -700 C ATOM 1558 CH2 TRP A1007 29.797 49.767 19.806 1.00 79.87 C ANISOU 1558 CH2 TRP A1007 10331 10099 9915 -802 795 -571 C ATOM 1559 N GLU A1008 27.663 56.354 15.253 1.00 78.16 N ANISOU 1559 N GLU A1008 9866 9553 10278 249 -432 -1386 N ATOM 1560 CA GLU A1008 27.126 56.720 13.935 1.00 79.61 C ANISOU 1560 CA GLU A1008 10086 9636 10528 395 -724 -1393 C ATOM 1561 C GLU A1008 28.267 56.839 12.898 1.00 80.50 C ANISOU 1561 C GLU A1008 10553 9568 10467 324 -812 -1128 C ATOM 1562 O GLU A1008 28.019 56.571 11.729 1.00 80.64 O ANISOU 1562 O GLU A1008 10659 9568 10414 364 -976 -1082 O ATOM 1563 CB GLU A1008 26.224 57.976 13.965 1.00 84.48 C ANISOU 1563 CB GLU A1008 10617 10171 11309 700 -957 -1589 C ATOM 1564 CG GLU A1008 26.924 59.311 14.176 1.00102.57 C ANISOU 1564 CG GLU A1008 13192 12194 13585 814 -1073 -1531 C ATOM 1565 CD GLU A1008 26.034 60.532 14.343 1.00143.81 C ANISOU 1565 CD GLU A1008 18351 17281 19011 1160 -1319 -1760 C ATOM 1566 OE1 GLU A1008 26.558 61.663 14.204 1.00146.77 O ANISOU 1566 OE1 GLU A1008 19027 17327 19411 1257 -1509 -1677 O ATOM 1567 OE2 GLU A1008 24.826 60.368 14.636 1.00146.30 O ANISOU 1567 OE2 GLU A1008 18295 17796 19495 1331 -1317 -2033 O ATOM 1568 N THR A1009 29.510 57.181 13.331 1.00 74.89 N ANISOU 1568 N THR A1009 10022 8754 9681 208 -690 -973 N ATOM 1569 CA THR A1009 30.699 57.246 12.463 1.00 73.71 C ANISOU 1569 CA THR A1009 10128 8480 9397 93 -668 -720 C ATOM 1570 C THR A1009 31.017 55.829 11.962 1.00 78.43 C ANISOU 1570 C THR A1009 10693 9224 9885 -31 -518 -671 C ATOM 1571 O THR A1009 31.281 55.643 10.766 1.00 79.00 O ANISOU 1571 O THR A1009 10939 9273 9803 -26 -553 -565 O ATOM 1572 CB THR A1009 31.885 57.877 13.212 1.00 73.30 C ANISOU 1572 CB THR A1009 10153 8310 9389 -25 -581 -626 C ATOM 1573 OG1 THR A1009 31.658 59.279 13.328 1.00 75.81 O ANISOU 1573 OG1 THR A1009 10592 8396 9817 91 -774 -658 O ATOM 1574 CG2 THR A1009 33.224 57.639 12.523 1.00 68.80 C ANISOU 1574 CG2 THR A1009 9706 7699 8736 -201 -444 -386 C ATOM 1575 N LEU A1010 30.968 54.838 12.890 1.00 73.96 N ANISOU 1575 N LEU A1010 9940 8787 9373 -127 -353 -753 N ATOM 1576 CA LEU A1010 31.200 53.424 12.629 1.00 73.55 C ANISOU 1576 CA LEU A1010 9854 8807 9283 -234 -230 -737 C ATOM 1577 C LEU A1010 30.196 52.901 11.576 1.00 79.29 C ANISOU 1577 C LEU A1010 10558 9566 10002 -182 -380 -859 C ATOM 1578 O LEU A1010 30.617 52.270 10.610 1.00 79.58 O ANISOU 1578 O LEU A1010 10733 9586 9916 -196 -379 -832 O ATOM 1579 CB LEU A1010 31.080 52.633 13.950 1.00 73.49 C ANISOU 1579 CB LEU A1010 9692 8880 9350 -335 -69 -774 C ATOM 1580 CG LEU A1010 31.513 51.167 13.922 1.00 78.89 C ANISOU 1580 CG LEU A1010 10386 9551 10040 -449 49 -721 C ATOM 1581 CD1 LEU A1010 32.875 50.996 14.545 1.00 78.38 C ANISOU 1581 CD1 LEU A1010 10402 9448 9930 -475 138 -576 C ATOM 1582 CD2 LEU A1010 30.510 50.292 14.648 1.00 83.88 C ANISOU 1582 CD2 LEU A1010 10859 10237 10774 -560 145 -783 C ATOM 1583 N ASN A1011 28.890 53.211 11.738 1.00 77.35 N ANISOU 1583 N ASN A1011 10124 9375 9892 -100 -526 -1027 N ATOM 1584 CA ASN A1011 27.828 52.774 10.832 1.00 79.37 C ANISOU 1584 CA ASN A1011 10286 9671 10200 -47 -747 -1191 C ATOM 1585 C ASN A1011 27.844 53.495 9.483 1.00 86.43 C ANISOU 1585 C ASN A1011 11448 10497 10895 133 -1027 -1145 C ATOM 1586 O ASN A1011 27.568 52.852 8.468 1.00 88.47 O ANISOU 1586 O ASN A1011 11795 10776 11043 151 -1187 -1228 O ATOM 1587 CB ASN A1011 26.460 52.924 11.481 1.00 81.24 C ANISOU 1587 CB ASN A1011 10149 10017 10701 -12 -803 -1402 C ATOM 1588 CG ASN A1011 26.212 51.968 12.630 1.00108.06 C ANISOU 1588 CG ASN A1011 13302 13506 14250 -232 -501 -1431 C ATOM 1589 OD1 ASN A1011 25.563 52.312 13.622 1.00110.26 O ANISOU 1589 OD1 ASN A1011 13322 13906 14668 -222 -370 -1529 O ATOM 1590 ND2 ASN A1011 26.707 50.741 12.532 1.00 97.17 N ANISOU 1590 ND2 ASN A1011 12021 12064 12836 -424 -369 -1342 N ATOM 1591 N ASP A1012 28.154 54.806 9.461 1.00 83.66 N ANISOU 1591 N ASP A1012 11266 10041 10479 262 -1102 -1011 N ATOM 1592 CA ASP A1012 28.204 55.592 8.223 1.00 86.09 C ANISOU 1592 CA ASP A1012 11907 10245 10560 426 -1356 -884 C ATOM 1593 C ASP A1012 29.359 55.152 7.315 1.00 89.87 C ANISOU 1593 C ASP A1012 12713 10723 10711 326 -1188 -689 C ATOM 1594 O ASP A1012 29.185 55.078 6.093 1.00 91.67 O ANISOU 1594 O ASP A1012 13203 10968 10660 431 -1373 -665 O ATOM 1595 CB ASP A1012 28.315 57.097 8.519 1.00 89.07 C ANISOU 1595 CB ASP A1012 12412 10431 10999 552 -1456 -756 C ATOM 1596 CG ASP A1012 27.039 57.758 9.022 1.00105.84 C ANISOU 1596 CG ASP A1012 14272 12541 13400 776 -1706 -985 C ATOM 1597 OD1 ASP A1012 25.964 57.109 8.970 1.00107.90 O ANISOU 1597 OD1 ASP A1012 14223 12969 13806 833 -1832 -1230 O ATOM 1598 OD2 ASP A1012 27.114 58.923 9.477 1.00114.99 O ANISOU 1598 OD2 ASP A1012 15507 13514 14669 893 -1771 -946 O ATOM 1599 N ASN A1013 30.526 54.847 7.911 1.00 83.97 N ANISOU 1599 N ASN A1013 11942 9978 9984 147 -845 -572 N ATOM 1600 CA ASN A1013 31.698 54.421 7.154 1.00 83.35 C ANISOU 1600 CA ASN A1013 12082 9934 9654 64 -615 -422 C ATOM 1601 C ASN A1013 31.543 52.987 6.654 1.00 85.53 C ANISOU 1601 C ASN A1013 12333 10326 9839 62 -590 -616 C ATOM 1602 O ASN A1013 32.225 52.626 5.701 1.00 86.89 O ANISOU 1602 O ASN A1013 12733 10554 9726 81 -464 -569 O ATOM 1603 CB ASN A1013 32.975 54.608 7.949 1.00 81.76 C ANISOU 1603 CB ASN A1013 11791 9699 9576 -96 -314 -272 C ATOM 1604 CG ASN A1013 33.412 56.045 7.987 1.00 95.60 C ANISOU 1604 CG ASN A1013 13685 11288 11351 -131 -329 -50 C ATOM 1605 OD1 ASN A1013 33.863 56.611 6.989 1.00 89.25 O ANISOU 1605 OD1 ASN A1013 13158 10430 10325 -150 -270 168 O ATOM 1606 ND2 ASN A1013 33.266 56.675 9.136 1.00 87.96 N ANISOU 1606 ND2 ASN A1013 12560 10221 10641 -146 -403 -102 N ATOM 1607 N LEU A1014 30.607 52.199 7.226 1.00 80.68 N ANISOU 1607 N LEU A1014 11458 9736 9462 38 -705 -845 N ATOM 1608 CA LEU A1014 30.318 50.857 6.714 1.00 81.70 C ANISOU 1608 CA LEU A1014 11575 9897 9571 16 -754 -1061 C ATOM 1609 C LEU A1014 29.635 51.004 5.346 1.00 89.23 C ANISOU 1609 C LEU A1014 12761 10893 10249 176 -1083 -1178 C ATOM 1610 O LEU A1014 29.953 50.257 4.415 1.00 91.05 O ANISOU 1610 O LEU A1014 13209 11158 10229 218 -1083 -1291 O ATOM 1611 CB LEU A1014 29.440 50.026 7.676 1.00 80.99 C ANISOU 1611 CB LEU A1014 11141 9785 9845 -113 -784 -1234 C ATOM 1612 CG LEU A1014 29.831 48.539 7.932 1.00 85.34 C ANISOU 1612 CG LEU A1014 11653 10258 10515 -244 -635 -1330 C ATOM 1613 CD1 LEU A1014 28.797 47.847 8.798 1.00 85.60 C ANISOU 1613 CD1 LEU A1014 11375 10247 10902 -423 -628 -1415 C ATOM 1614 CD2 LEU A1014 29.976 47.733 6.650 1.00 89.38 C ANISOU 1614 CD2 LEU A1014 12368 10739 10852 -175 -797 -1544 C ATOM 1615 N LYS A1015 28.742 52.013 5.225 1.00 86.15 N ANISOU 1615 N LYS A1015 12354 10496 9882 302 -1382 -1162 N ATOM 1616 CA LYS A1015 27.992 52.337 4.005 1.00 89.55 C ANISOU 1616 CA LYS A1015 13020 10958 10047 504 -1798 -1245 C ATOM 1617 C LYS A1015 28.941 52.789 2.880 1.00 95.10 C ANISOU 1617 C LYS A1015 14241 11678 10215 592 -1696 -1004 C ATOM 1618 O LYS A1015 28.736 52.409 1.722 1.00 98.43 O ANISOU 1618 O LYS A1015 14966 12176 10258 721 -1914 -1110 O ATOM 1619 CB LYS A1015 26.923 53.405 4.291 1.00 93.01 C ANISOU 1619 CB LYS A1015 13289 11354 10697 661 -2137 -1259 C ATOM 1620 CG LYS A1015 25.856 52.932 5.276 1.00105.66 C ANISOU 1620 CG LYS A1015 14341 13003 12804 580 -2200 -1527 C ATOM 1621 CD LYS A1015 24.941 54.062 5.733 1.00117.78 C ANISOU 1621 CD LYS A1015 15655 14515 14583 778 -2461 -1568 C ATOM 1622 CE LYS A1015 23.888 53.592 6.710 1.00130.51 C ANISOU 1622 CE LYS A1015 16673 16231 16684 687 -2428 -1837 C ATOM 1623 NZ LYS A1015 22.839 52.757 6.056 1.00143.81 N ANISOU 1623 NZ LYS A1015 18103 18007 18531 662 -2758 -2147 N ATOM 1624 N VAL A1016 29.995 53.561 3.236 1.00 88.92 N ANISOU 1624 N VAL A1016 13553 10835 9399 502 -1349 -689 N ATOM 1625 CA VAL A1016 31.041 54.049 2.330 1.00 89.76 C ANISOU 1625 CA VAL A1016 14081 10961 9063 500 -1109 -397 C ATOM 1626 C VAL A1016 31.769 52.828 1.733 1.00 93.49 C ANISOU 1626 C VAL A1016 14649 11592 9282 471 -836 -547 C ATOM 1627 O VAL A1016 31.906 52.751 0.515 1.00 96.69 O ANISOU 1627 O VAL A1016 15458 12104 9177 585 -846 -521 O ATOM 1628 CB VAL A1016 32.002 55.032 3.067 1.00 91.25 C ANISOU 1628 CB VAL A1016 14205 11024 9440 339 -797 -82 C ATOM 1629 CG1 VAL A1016 33.294 55.269 2.286 1.00 93.54 C ANISOU 1629 CG1 VAL A1016 14806 11365 9371 241 -409 212 C ATOM 1630 CG2 VAL A1016 31.310 56.357 3.358 1.00 91.41 C ANISOU 1630 CG2 VAL A1016 14252 10840 9637 427 -1104 45 C ATOM 1631 N ILE A1017 32.161 51.855 2.591 1.00 86.83 N ANISOU 1631 N ILE A1017 13463 10751 8776 351 -622 -721 N ATOM 1632 CA ILE A1017 32.829 50.599 2.221 1.00 86.99 C ANISOU 1632 CA ILE A1017 13514 10858 8681 359 -390 -921 C ATOM 1633 C ILE A1017 31.945 49.798 1.255 1.00 95.09 C ANISOU 1633 C ILE A1017 14743 11928 9460 506 -741 -1255 C ATOM 1634 O ILE A1017 32.457 49.320 0.241 1.00 99.00 O ANISOU 1634 O ILE A1017 15551 12541 9526 619 -620 -1359 O ATOM 1635 CB ILE A1017 33.211 49.776 3.487 1.00 86.07 C ANISOU 1635 CB ILE A1017 13002 10657 9045 226 -208 -1013 C ATOM 1636 CG1 ILE A1017 34.398 50.436 4.204 1.00 84.01 C ANISOU 1636 CG1 ILE A1017 12601 10399 8921 115 153 -733 C ATOM 1637 CG2 ILE A1017 33.522 48.294 3.156 1.00 87.78 C ANISOU 1637 CG2 ILE A1017 13234 10863 9257 282 -139 -1317 C ATOM 1638 CD1 ILE A1017 34.539 50.110 5.631 1.00 82.00 C ANISOU 1638 CD1 ILE A1017 11998 10048 9110 0 193 -731 C ATOM 1639 N GLU A1018 30.628 49.682 1.548 1.00 91.10 N ANISOU 1639 N GLU A1018 14045 11345 9222 508 -1173 -1447 N ATOM 1640 CA GLU A1018 29.656 48.963 0.706 1.00 93.95 C ANISOU 1640 CA GLU A1018 14518 11724 9456 615 -1610 -1807 C ATOM 1641 C GLU A1018 29.562 49.553 -0.703 1.00102.50 C ANISOU 1641 C GLU A1018 16118 12940 9888 840 -1837 -1763 C ATOM 1642 O GLU A1018 29.395 48.802 -1.665 1.00106.16 O ANISOU 1642 O GLU A1018 16845 13471 10018 959 -2025 -2063 O ATOM 1643 CB GLU A1018 28.254 48.983 1.335 1.00 94.51 C ANISOU 1643 CB GLU A1018 14196 11716 9995 554 -2013 -1965 C ATOM 1644 CG GLU A1018 28.093 48.170 2.606 1.00 99.12 C ANISOU 1644 CG GLU A1018 14327 12180 11155 318 -1845 -2069 C ATOM 1645 CD GLU A1018 26.948 48.611 3.500 1.00118.91 C ANISOU 1645 CD GLU A1018 16391 14668 14121 230 -2020 -2083 C ATOM 1646 OE1 GLU A1018 26.220 49.561 3.127 1.00120.02 O ANISOU 1646 OE1 GLU A1018 16529 14873 14199 389 -2347 -2070 O ATOM 1647 OE2 GLU A1018 26.785 48.009 4.585 1.00108.56 O ANISOU 1647 OE2 GLU A1018 14743 13280 13224 17 -1818 -2102 O ATOM 1648 N LYS A1019 29.672 50.892 -0.818 1.00 99.14 N ANISOU 1648 N LYS A1019 15878 12526 9264 900 -1833 -1388 N ATOM 1649 CA LYS A1019 29.545 51.615 -2.082 1.00104.04 C ANISOU 1649 CA LYS A1019 17055 13239 9238 1110 -2061 -1237 C ATOM 1650 C LYS A1019 30.906 52.028 -2.709 1.00110.53 C ANISOU 1650 C LYS A1019 18289 14172 9535 1084 -1514 -894 C ATOM 1651 O LYS A1019 30.917 52.623 -3.791 1.00115.00 O ANISOU 1651 O LYS A1019 19390 14821 9482 1231 -1613 -692 O ATOM 1652 CB LYS A1019 28.646 52.846 -1.875 1.00107.06 C ANISOU 1652 CB LYS A1019 17415 13501 9763 1215 -2480 -1032 C ATOM 1653 CG LYS A1019 27.178 52.489 -1.586 1.00124.99 C ANISOU 1653 CG LYS A1019 19294 15734 12463 1297 -3064 -1404 C ATOM 1654 CD LYS A1019 26.258 52.556 -2.831 1.00143.92 C ANISOU 1654 CD LYS A1019 22043 18206 14435 1584 -3731 -1576 C ATOM 1655 CE LYS A1019 26.232 51.314 -3.706 1.00158.74 C ANISOU 1655 CE LYS A1019 24107 20216 15991 1621 -3894 -1989 C ATOM 1656 NZ LYS A1019 25.472 50.197 -3.087 1.00166.00 N ANISOU 1656 NZ LYS A1019 24445 21081 17546 1457 -4066 -2447 N ATOM 1657 N ALA A1020 32.035 51.668 -2.067 1.00104.71 N ANISOU 1657 N ALA A1020 17301 13450 9035 903 -946 -834 N ATOM 1658 CA ALA A1020 33.390 51.990 -2.530 1.00106.70 C ANISOU 1658 CA ALA A1020 17782 13833 8926 834 -355 -543 C ATOM 1659 C ALA A1020 33.805 51.172 -3.766 1.00116.89 C ANISOU 1659 C ALA A1020 19474 15365 9574 1001 -183 -770 C ATOM 1660 O ALA A1020 33.193 50.142 -4.059 1.00117.48 O ANISOU 1660 O ALA A1020 19567 15459 9609 1140 -496 -1220 O ATOM 1661 CB ALA A1020 34.389 51.758 -1.405 1.00102.91 C ANISOU 1661 CB ALA A1020 16818 13304 8978 626 106 -490 C ATOM 1662 N ASP A1021 34.861 51.641 -4.477 1.00118.21 N ANISOU 1662 N ASP A1021 19954 15712 9249 972 339 -469 N ATOM 1663 CA ASP A1021 35.455 51.012 -5.668 1.00124.13 C ANISOU 1663 CA ASP A1021 21114 16751 9298 1137 655 -642 C ATOM 1664 C ASP A1021 36.890 50.524 -5.362 1.00127.70 C ANISOU 1664 C ASP A1021 21242 17349 9929 1035 1395 -663 C ATOM 1665 O ASP A1021 37.121 49.318 -5.253 1.00127.65 O ANISOU 1665 O ASP A1021 21065 17399 10037 1166 1485 -1114 O ATOM 1666 CB ASP A1021 35.475 51.984 -6.874 1.00132.53 C ANISOU 1666 CB ASP A1021 22867 17961 9526 1207 699 -247 C ATOM 1667 CG ASP A1021 34.138 52.579 -7.263 1.00144.98 C ANISOU 1667 CG ASP A1021 24803 19399 10885 1365 -69 -187 C ATOM 1668 OD1 ASP A1021 33.433 51.962 -8.091 1.00149.23 O ANISOU 1668 OD1 ASP A1021 25691 20054 10954 1622 -500 -549 O ATOM 1669 OD2 ASP A1021 33.826 53.697 -6.793 1.00149.29 O ANISOU 1669 OD2 ASP A1021 25298 19713 11712 1255 -260 209 O ATOM 1670 N ASN A1022 37.839 51.476 -5.215 1.00123.68 N ANISOU 1670 N ASN A1022 20628 16871 9491 803 1892 -186 N ATOM 1671 CA ASN A1022 39.267 51.253 -4.956 1.00123.25 C ANISOU 1671 CA ASN A1022 20202 16981 9648 678 2607 -139 C ATOM 1672 C ASN A1022 39.561 50.953 -3.465 1.00118.49 C ANISOU 1672 C ASN A1022 18901 16168 9950 535 2570 -229 C ATOM 1673 O ASN A1022 38.648 50.975 -2.640 1.00112.70 O ANISOU 1673 O ASN A1022 18010 15178 9633 508 2053 -291 O ATOM 1674 CB ASN A1022 40.079 52.474 -5.424 1.00126.90 C ANISOU 1674 CB ASN A1022 20858 17555 9803 439 3127 432 C ATOM 1675 CG ASN A1022 39.607 53.785 -4.841 1.00142.60 C ANISOU 1675 CG ASN A1022 22871 19224 12086 202 2818 897 C ATOM 1676 OD1 ASN A1022 39.921 54.136 -3.702 1.00133.43 O ANISOU 1676 OD1 ASN A1022 21211 17863 11623 -14 2831 1001 O ATOM 1677 ND2 ASN A1022 38.826 54.530 -5.604 1.00136.31 N ANISOU 1677 ND2 ASN A1022 22680 18354 10758 273 2489 1159 N ATOM 1678 N ALA A1023 40.847 50.681 -3.140 1.00114.32 N ANISOU 1678 N ALA A1023 17956 15778 9702 458 3128 -238 N ATOM 1679 CA ALA A1023 41.345 50.375 -1.801 1.00108.44 C ANISOU 1679 CA ALA A1023 16579 14882 9741 355 3129 -312 C ATOM 1680 C ALA A1023 41.452 51.607 -0.916 1.00108.10 C ANISOU 1680 C ALA A1023 16314 14644 10116 39 3053 105 C ATOM 1681 O ALA A1023 41.185 51.495 0.280 1.00103.15 O ANISOU 1681 O ALA A1023 15355 13803 10036 -12 2735 33 O ATOM 1682 CB ALA A1023 42.702 49.698 -1.891 1.00112.25 C ANISOU 1682 CB ALA A1023 16694 15602 10355 428 3712 -481 C ATOM 1683 N ALA A1024 41.858 52.769 -1.480 1.00106.63 N ANISOU 1683 N ALA A1024 16334 14511 9669 -178 3348 537 N ATOM 1684 CA ALA A1024 42.022 54.025 -0.740 1.00104.20 C ANISOU 1684 CA ALA A1024 15868 13967 9758 -496 3283 929 C ATOM 1685 C ALA A1024 40.739 54.421 -0.010 1.00102.19 C ANISOU 1685 C ALA A1024 15720 13395 9712 -457 2615 915 C ATOM 1686 O ALA A1024 40.812 54.826 1.150 1.00 98.46 O ANISOU 1686 O ALA A1024 14902 12720 9789 -604 2444 956 O ATOM 1687 CB ALA A1024 42.460 55.139 -1.675 1.00110.85 C ANISOU 1687 CB ALA A1024 17069 14859 10191 -721 3662 1408 C ATOM 1688 N GLN A1025 39.572 54.255 -0.670 1.00 98.18 N ANISOU 1688 N GLN A1025 15661 12868 8773 -237 2232 812 N ATOM 1689 CA GLN A1025 38.242 54.524 -0.110 1.00 93.85 C ANISOU 1689 CA GLN A1025 15177 12077 8407 -148 1607 736 C ATOM 1690 C GLN A1025 37.955 53.578 1.059 1.00 91.92 C ANISOU 1690 C GLN A1025 14471 11771 8681 -92 1397 373 C ATOM 1691 O GLN A1025 37.473 54.015 2.110 1.00 86.79 O ANISOU 1691 O GLN A1025 13607 10923 8445 -162 1119 392 O ATOM 1692 CB GLN A1025 37.152 54.361 -1.188 1.00 97.79 C ANISOU 1692 CB GLN A1025 16191 12630 8335 100 1245 639 C ATOM 1693 CG GLN A1025 37.173 55.419 -2.282 1.00119.20 C ANISOU 1693 CG GLN A1025 19474 15339 10479 76 1314 1062 C ATOM 1694 CD GLN A1025 36.403 55.030 -3.529 1.00145.01 C ANISOU 1694 CD GLN A1025 23291 18756 13052 358 1021 929 C ATOM 1695 OE1 GLN A1025 36.232 53.851 -3.857 1.00139.63 O ANISOU 1695 OE1 GLN A1025 22589 18252 12211 545 945 497 O ATOM 1696 NE2 GLN A1025 35.998 56.020 -4.308 1.00142.81 N ANISOU 1696 NE2 GLN A1025 23560 18389 12313 398 842 1303 N ATOM 1697 N VAL A1026 38.279 52.280 0.864 1.00 89.55 N ANISOU 1697 N VAL A1026 14055 11632 8338 43 1550 48 N ATOM 1698 CA VAL A1026 38.085 51.191 1.827 1.00 85.82 C ANISOU 1698 CA VAL A1026 13229 11082 8297 103 1390 -270 C ATOM 1699 C VAL A1026 39.032 51.378 3.034 1.00 87.93 C ANISOU 1699 C VAL A1026 13041 11290 9079 -62 1583 -157 C ATOM 1700 O VAL A1026 38.544 51.349 4.163 1.00 84.21 O ANISOU 1700 O VAL A1026 12355 10662 8979 -106 1318 -206 O ATOM 1701 CB VAL A1026 38.232 49.795 1.146 1.00 91.72 C ANISOU 1701 CB VAL A1026 14058 11954 8838 315 1485 -643 C ATOM 1702 CG1 VAL A1026 38.127 48.656 2.159 1.00 88.38 C ANISOU 1702 CG1 VAL A1026 13305 11380 8895 354 1341 -910 C ATOM 1703 CG2 VAL A1026 37.186 49.614 0.044 1.00 93.94 C ANISOU 1703 CG2 VAL A1026 14789 12275 8627 477 1173 -812 C ATOM 1704 N LYS A1027 40.353 51.605 2.800 1.00 87.32 N ANISOU 1704 N LYS A1027 12810 11352 9014 -156 2035 -11 N ATOM 1705 CA LYS A1027 41.366 51.824 3.850 1.00 86.01 C ANISOU 1705 CA LYS A1027 12183 11154 9343 -310 2185 76 C ATOM 1706 C LYS A1027 41.009 53.024 4.747 1.00 89.20 C ANISOU 1706 C LYS A1027 12535 11344 10013 -517 1927 302 C ATOM 1707 O LYS A1027 41.061 52.902 5.977 1.00 86.12 O ANISOU 1707 O LYS A1027 11856 10850 10016 -551 1739 227 O ATOM 1708 CB LYS A1027 42.765 52.045 3.246 1.00 92.80 C ANISOU 1708 CB LYS A1027 12865 12229 10165 -408 2732 204 C ATOM 1709 CG LYS A1027 43.411 50.808 2.624 1.00108.88 C ANISOU 1709 CG LYS A1027 14787 14489 12092 -167 3046 -92 C ATOM 1710 CD LYS A1027 44.798 51.103 2.043 1.00122.64 C ANISOU 1710 CD LYS A1027 16265 16494 13838 -275 3654 28 C ATOM 1711 CE LYS A1027 44.760 51.694 0.650 1.00138.80 C ANISOU 1711 CE LYS A1027 18752 18741 15245 -317 4030 210 C ATOM 1712 NZ LYS A1027 46.115 52.067 0.164 1.00152.91 N ANISOU 1712 NZ LYS A1027 20233 20796 17072 -494 4697 377 N ATOM 1713 N ASP A1028 40.625 54.167 4.136 1.00 88.23 N ANISOU 1713 N ASP A1028 12732 11138 9651 -630 1898 568 N ATOM 1714 CA ASP A1028 40.266 55.380 4.875 1.00 87.28 C ANISOU 1714 CA ASP A1028 12617 10765 9778 -792 1643 754 C ATOM 1715 C ASP A1028 39.021 55.186 5.750 1.00 86.06 C ANISOU 1715 C ASP A1028 12456 10477 9767 -653 1184 552 C ATOM 1716 O ASP A1028 39.030 55.625 6.898 1.00 83.70 O ANISOU 1716 O ASP A1028 11946 10044 9814 -736 1024 532 O ATOM 1717 CB ASP A1028 40.051 56.577 3.932 1.00 93.72 C ANISOU 1717 CB ASP A1028 13851 11463 10295 -898 1678 1095 C ATOM 1718 CG ASP A1028 39.604 57.835 4.661 1.00109.04 C ANISOU 1718 CG ASP A1028 15843 13072 12513 -1014 1361 1244 C ATOM 1719 OD1 ASP A1028 38.441 58.252 4.464 1.00110.03 O ANISOU 1719 OD1 ASP A1028 16262 13054 12490 -851 995 1237 O ATOM 1720 OD2 ASP A1028 40.383 58.344 5.505 1.00116.30 O ANISOU 1720 OD2 ASP A1028 16475 13873 13839 -1238 1434 1308 O ATOM 1721 N ALA A1029 37.958 54.562 5.212 1.00 81.43 N ANISOU 1721 N ALA A1029 12087 9938 8915 -452 979 389 N ATOM 1722 CA ALA A1029 36.714 54.335 5.950 1.00 78.10 C ANISOU 1722 CA ALA A1029 11605 9426 8643 -344 599 192 C ATOM 1723 C ALA A1029 36.949 53.433 7.174 1.00 79.24 C ANISOU 1723 C ALA A1029 11399 9590 9118 -362 612 8 C ATOM 1724 O ALA A1029 36.409 53.720 8.249 1.00 77.59 O ANISOU 1724 O ALA A1029 11056 9289 9136 -383 423 -41 O ATOM 1725 CB ALA A1029 35.660 53.734 5.037 1.00 79.72 C ANISOU 1725 CB ALA A1029 12045 9700 8545 -161 392 25 C ATOM 1726 N LEU A1030 37.801 52.390 7.022 1.00 74.44 N ANISOU 1726 N LEU A1030 10668 9096 8520 -332 842 -85 N ATOM 1727 CA LEU A1030 38.164 51.459 8.090 1.00 71.58 C ANISOU 1727 CA LEU A1030 10034 8722 8442 -318 841 -214 C ATOM 1728 C LEU A1030 39.010 52.126 9.172 1.00 77.11 C ANISOU 1728 C LEU A1030 10491 9381 9425 -447 866 -93 C ATOM 1729 O LEU A1030 38.917 51.736 10.330 1.00 76.46 O ANISOU 1729 O LEU A1030 10265 9252 9534 -439 728 -158 O ATOM 1730 CB LEU A1030 38.914 50.251 7.528 1.00 72.60 C ANISOU 1730 CB LEU A1030 10118 8943 8525 -199 1052 -354 C ATOM 1731 CG LEU A1030 38.070 49.250 6.752 1.00 76.82 C ANISOU 1731 CG LEU A1030 10859 9465 8863 -59 947 -579 C ATOM 1732 CD1 LEU A1030 38.938 48.375 5.868 1.00 79.18 C ANISOU 1732 CD1 LEU A1030 11191 9868 9026 92 1206 -731 C ATOM 1733 CD2 LEU A1030 37.206 48.424 7.677 1.00 76.26 C ANISOU 1733 CD2 LEU A1030 10706 9246 9024 -65 707 -706 C ATOM 1734 N THR A1031 39.821 53.127 8.807 1.00 76.09 N ANISOU 1734 N THR A1031 10336 9262 9314 -580 1028 86 N ATOM 1735 CA THR A1031 40.666 53.868 9.745 1.00 76.29 C ANISOU 1735 CA THR A1031 10119 9225 9644 -737 1006 171 C ATOM 1736 C THR A1031 39.754 54.704 10.673 1.00 79.58 C ANISOU 1736 C THR A1031 10627 9478 10130 -768 697 158 C ATOM 1737 O THR A1031 39.972 54.701 11.886 1.00 78.90 O ANISOU 1737 O THR A1031 10378 9363 10238 -784 548 80 O ATOM 1738 CB THR A1031 41.704 54.681 8.965 1.00 87.49 C ANISOU 1738 CB THR A1031 11479 10671 11091 -924 1293 371 C ATOM 1739 OG1 THR A1031 42.446 53.782 8.136 1.00 88.91 O ANISOU 1739 OG1 THR A1031 11553 11057 11174 -839 1622 321 O ATOM 1740 CG2 THR A1031 42.666 55.431 9.865 1.00 87.74 C ANISOU 1740 CG2 THR A1031 11208 10622 11510 -1128 1244 426 C ATOM 1741 N LYS A1032 38.712 55.363 10.107 1.00 76.19 N ANISOU 1741 N LYS A1032 10472 8958 9520 -733 585 206 N ATOM 1742 CA LYS A1032 37.693 56.130 10.842 1.00 74.44 C ANISOU 1742 CA LYS A1032 10333 8593 9357 -691 308 141 C ATOM 1743 C LYS A1032 36.911 55.203 11.782 1.00 76.81 C ANISOU 1743 C LYS A1032 10524 8982 9677 -573 194 -65 C ATOM 1744 O LYS A1032 36.686 55.552 12.936 1.00 75.84 O ANISOU 1744 O LYS A1032 10329 8819 9668 -571 64 -154 O ATOM 1745 CB LYS A1032 36.707 56.821 9.870 1.00 77.17 C ANISOU 1745 CB LYS A1032 10975 8840 9508 -606 187 219 C ATOM 1746 CG LYS A1032 37.036 58.257 9.492 1.00 81.33 C ANISOU 1746 CG LYS A1032 11688 9132 10080 -725 157 444 C ATOM 1747 CD LYS A1032 37.934 58.329 8.270 1.00 90.90 C ANISOU 1747 CD LYS A1032 13035 10389 11116 -864 452 703 C ATOM 1748 CE LYS A1032 37.964 59.688 7.628 1.00100.84 C ANISOU 1748 CE LYS A1032 14600 11377 12338 -978 415 997 C ATOM 1749 NZ LYS A1032 36.817 59.876 6.704 1.00111.42 N ANISOU 1749 NZ LYS A1032 16317 12661 13355 -761 198 1058 N ATOM 1750 N MET A1033 36.518 54.014 11.278 1.00 73.61 N ANISOU 1750 N MET A1033 10128 8688 9153 -490 258 -142 N ATOM 1751 CA MET A1033 35.771 52.979 11.997 1.00 71.75 C ANISOU 1751 CA MET A1033 9808 8504 8950 -434 200 -290 C ATOM 1752 C MET A1033 36.535 52.465 13.217 1.00 73.70 C ANISOU 1752 C MET A1033 9906 8770 9327 -471 231 -286 C ATOM 1753 O MET A1033 35.960 52.430 14.306 1.00 73.20 O ANISOU 1753 O MET A1033 9810 8717 9286 -470 153 -343 O ATOM 1754 CB MET A1033 35.437 51.813 11.059 1.00 74.59 C ANISOU 1754 CB MET A1033 10232 8908 9199 -373 248 -372 C ATOM 1755 CG MET A1033 34.252 52.087 10.167 1.00 79.21 C ANISOU 1755 CG MET A1033 10949 9495 9654 -304 93 -449 C ATOM 1756 SD MET A1033 33.919 50.730 9.014 1.00 84.98 S ANISOU 1756 SD MET A1033 11786 10261 10243 -236 83 -614 S ATOM 1757 CE MET A1033 32.846 49.765 9.959 1.00 80.56 C ANISOU 1757 CE MET A1033 11037 9656 9915 -306 -12 -767 C ATOM 1758 N ARG A1034 37.828 52.097 13.040 1.00 69.35 N ANISOU 1758 N ARG A1034 9261 8240 8848 -485 344 -223 N ATOM 1759 CA ARG A1034 38.712 51.585 14.097 1.00 68.93 C ANISOU 1759 CA ARG A1034 9062 8200 8929 -475 305 -215 C ATOM 1760 C ARG A1034 38.876 52.607 15.226 1.00 73.25 C ANISOU 1760 C ARG A1034 9569 8725 9538 -540 145 -215 C ATOM 1761 O ARG A1034 38.769 52.235 16.393 1.00 73.69 O ANISOU 1761 O ARG A1034 9633 8800 9565 -503 31 -244 O ATOM 1762 CB ARG A1034 40.083 51.212 13.519 1.00 69.68 C ANISOU 1762 CB ARG A1034 8990 8339 9145 -449 446 -183 C ATOM 1763 CG ARG A1034 40.938 50.357 14.443 1.00 78.15 C ANISOU 1763 CG ARG A1034 9903 9413 10376 -360 349 -195 C ATOM 1764 CD ARG A1034 42.361 50.335 13.936 1.00 87.74 C ANISOU 1764 CD ARG A1034 10848 10703 11787 -328 486 -198 C ATOM 1765 NE ARG A1034 43.288 49.701 14.876 1.00 90.09 N ANISOU 1765 NE ARG A1034 10941 11000 12290 -210 310 -220 N ATOM 1766 CZ ARG A1034 44.138 50.365 15.652 1.00 98.48 C ANISOU 1766 CZ ARG A1034 11778 12098 13543 -279 138 -213 C ATOM 1767 NH1 ARG A1034 44.175 51.692 15.626 1.00 81.29 N ANISOU 1767 NH1 ARG A1034 9562 9921 11404 -494 143 -186 N ATOM 1768 NH2 ARG A1034 44.963 49.707 16.456 1.00 87.05 N ANISOU 1768 NH2 ARG A1034 10153 10654 12266 -126 -85 -244 N ATOM 1769 N ALA A1035 39.113 53.884 14.875 1.00 69.28 N ANISOU 1769 N ALA A1035 9066 8158 9097 -637 128 -182 N ATOM 1770 CA ALA A1035 39.247 54.983 15.826 1.00 69.12 C ANISOU 1770 CA ALA A1035 9039 8060 9162 -701 -58 -234 C ATOM 1771 C ALA A1035 37.929 55.228 16.576 1.00 72.00 C ANISOU 1771 C ALA A1035 9552 8426 9381 -612 -162 -359 C ATOM 1772 O ALA A1035 37.957 55.462 17.782 1.00 72.96 O ANISOU 1772 O ALA A1035 9684 8567 9470 -588 -301 -462 O ATOM 1773 CB ALA A1035 39.685 56.249 15.104 1.00 71.16 C ANISOU 1773 CB ALA A1035 9309 8174 9556 -847 -38 -148 C ATOM 1774 N ALA A1036 36.781 55.139 15.876 1.00 66.73 N ANISOU 1774 N ALA A1036 8978 7763 8615 -549 -97 -373 N ATOM 1775 CA ALA A1036 35.465 55.344 16.482 1.00 65.79 C ANISOU 1775 CA ALA A1036 8906 7680 8410 -454 -148 -516 C ATOM 1776 C ALA A1036 35.129 54.206 17.431 1.00 69.64 C ANISOU 1776 C ALA A1036 9358 8313 8788 -437 -70 -546 C ATOM 1777 O ALA A1036 34.603 54.460 18.513 1.00 69.46 O ANISOU 1777 O ALA A1036 9357 8363 8670 -393 -87 -658 O ATOM 1778 CB ALA A1036 34.398 55.477 15.411 1.00 66.06 C ANISOU 1778 CB ALA A1036 8986 7692 8424 -386 -145 -532 C ATOM 1779 N ALA A1037 35.464 52.954 17.043 1.00 66.51 N ANISOU 1779 N ALA A1037 8936 7943 8391 -468 25 -444 N ATOM 1780 CA ALA A1037 35.228 51.762 17.874 1.00 66.27 C ANISOU 1780 CA ALA A1037 8926 7975 8279 -479 94 -402 C ATOM 1781 C ALA A1037 36.065 51.815 19.148 1.00 69.28 C ANISOU 1781 C ALA A1037 9357 8390 8574 -458 -8 -366 C ATOM 1782 O ALA A1037 35.545 51.529 20.220 1.00 70.80 O ANISOU 1782 O ALA A1037 9641 8668 8591 -454 28 -362 O ATOM 1783 CB ALA A1037 35.544 50.498 17.094 1.00 66.80 C ANISOU 1783 CB ALA A1037 8989 7976 8417 -491 164 -322 C ATOM 1784 N LEU A1038 37.333 52.239 19.041 1.00 64.32 N ANISOU 1784 N LEU A1038 8664 7715 8061 -453 -138 -346 N ATOM 1785 CA LEU A1038 38.231 52.349 20.188 1.00 65.30 C ANISOU 1785 CA LEU A1038 8806 7870 8136 -418 -332 -348 C ATOM 1786 C LEU A1038 37.826 53.513 21.098 1.00 71.07 C ANISOU 1786 C LEU A1038 9629 8640 8732 -407 -447 -513 C ATOM 1787 O LEU A1038 37.957 53.387 22.317 1.00 71.47 O ANISOU 1787 O LEU A1038 9809 8779 8568 -349 -566 -544 O ATOM 1788 CB LEU A1038 39.699 52.465 19.745 1.00 65.48 C ANISOU 1788 CB LEU A1038 8633 7840 8405 -434 -444 -318 C ATOM 1789 CG LEU A1038 40.300 51.181 19.150 1.00 68.74 C ANISOU 1789 CG LEU A1038 8953 8233 8931 -363 -364 -207 C ATOM 1790 CD1 LEU A1038 41.584 51.463 18.403 1.00 69.15 C ANISOU 1790 CD1 LEU A1038 8730 8278 9263 -389 -352 -214 C ATOM 1791 CD2 LEU A1038 40.487 50.101 20.211 1.00 71.28 C ANISOU 1791 CD2 LEU A1038 9392 8558 9135 -244 -512 -122 C ATOM 1792 N ASP A1039 37.282 54.612 20.516 1.00 68.27 N ANISOU 1792 N ASP A1039 9253 8211 8474 -434 -424 -625 N ATOM 1793 CA ASP A1039 36.776 55.768 21.269 1.00 69.65 C ANISOU 1793 CA ASP A1039 9525 8375 8564 -380 -532 -838 C ATOM 1794 C ASP A1039 35.517 55.377 22.063 1.00 74.03 C ANISOU 1794 C ASP A1039 10179 9109 8839 -287 -366 -921 C ATOM 1795 O ASP A1039 35.402 55.743 23.238 1.00 76.48 O ANISOU 1795 O ASP A1039 10621 9517 8922 -208 -433 -1078 O ATOM 1796 CB ASP A1039 36.487 56.955 20.339 1.00 71.84 C ANISOU 1796 CB ASP A1039 9779 8466 9051 -400 -562 -902 C ATOM 1797 CG ASP A1039 37.645 57.933 20.172 1.00 94.92 C ANISOU 1797 CG ASP A1039 12664 11184 12215 -519 -764 -912 C ATOM 1798 OD1 ASP A1039 38.538 57.965 21.059 1.00 98.34 O ANISOU 1798 OD1 ASP A1039 13080 11637 12648 -548 -958 -994 O ATOM 1799 OD2 ASP A1039 37.633 58.706 19.184 1.00105.54 O ANISOU 1799 OD2 ASP A1039 14011 12340 13750 -591 -749 -837 O ATOM 1800 N ALA A1040 34.605 54.590 21.436 1.00 68.16 N ANISOU 1800 N ALA A1040 9366 8424 8108 -311 -139 -826 N ATOM 1801 CA ALA A1040 33.398 54.068 22.073 1.00 68.38 C ANISOU 1801 CA ALA A1040 9404 8632 7945 -291 91 -866 C ATOM 1802 C ALA A1040 33.784 53.150 23.229 1.00 72.39 C ANISOU 1802 C ALA A1040 10079 9256 8168 -320 140 -723 C ATOM 1803 O ALA A1040 33.186 53.252 24.292 1.00 73.68 O ANISOU 1803 O ALA A1040 10350 9598 8046 -278 275 -803 O ATOM 1804 CB ALA A1040 32.546 53.318 21.062 1.00 67.87 C ANISOU 1804 CB ALA A1040 9188 8558 8043 -361 256 -792 C ATOM 1805 N GLN A1041 34.828 52.299 23.036 1.00 67.85 N ANISOU 1805 N GLN A1041 9544 8580 7654 -365 25 -514 N ATOM 1806 CA GLN A1041 35.347 51.386 24.059 1.00 69.37 C ANISOU 1806 CA GLN A1041 9941 8821 7595 -355 -19 -332 C ATOM 1807 C GLN A1041 35.882 52.190 25.238 1.00 76.07 C ANISOU 1807 C GLN A1041 10960 9774 8169 -246 -241 -471 C ATOM 1808 O GLN A1041 35.475 51.942 26.373 1.00 78.91 O ANISOU 1808 O GLN A1041 11558 10294 8132 -211 -160 -429 O ATOM 1809 CB GLN A1041 36.433 50.461 23.484 1.00 69.39 C ANISOU 1809 CB GLN A1041 9903 8657 7805 -354 -163 -143 C ATOM 1810 CG GLN A1041 36.851 49.332 24.430 1.00 72.85 C ANISOU 1810 CG GLN A1041 10581 9078 8022 -310 -241 93 C ATOM 1811 CD GLN A1041 37.929 48.432 23.869 1.00 87.78 C ANISOU 1811 CD GLN A1041 12403 10781 10168 -242 -408 232 C ATOM 1812 OE1 GLN A1041 38.329 48.529 22.705 1.00 87.24 O ANISOU 1812 OE1 GLN A1041 12101 10625 10423 -247 -391 156 O ATOM 1813 NE2 GLN A1041 38.453 47.544 24.698 1.00 76.19 N ANISOU 1813 NE2 GLN A1041 11155 9252 8542 -145 -578 435 N ATOM 1814 N LYS A1042 36.741 53.191 24.956 1.00 71.73 N ANISOU 1814 N LYS A1042 10303 9132 7820 -210 -511 -646 N ATOM 1815 CA LYS A1042 37.318 54.093 25.952 1.00 74.02 C ANISOU 1815 CA LYS A1042 10722 9468 7934 -123 -805 -857 C ATOM 1816 C LYS A1042 36.200 54.691 26.826 1.00 80.37 C ANISOU 1816 C LYS A1042 11705 10448 8383 -37 -636 -1077 C ATOM 1817 O LYS A1042 36.302 54.638 28.047 1.00 82.27 O ANISOU 1817 O LYS A1042 12211 10848 8201 59 -732 -1142 O ATOM 1818 CB LYS A1042 38.140 55.191 25.257 1.00 75.24 C ANISOU 1818 CB LYS A1042 10673 9430 8485 -177 -1049 -1012 C ATOM 1819 CG LYS A1042 39.196 55.843 26.154 1.00 90.27 C ANISOU 1819 CG LYS A1042 12637 11314 10348 -138 -1474 -1196 C ATOM 1820 CD LYS A1042 40.211 56.666 25.355 1.00 93.62 C ANISOU 1820 CD LYS A1042 12788 11513 11268 -279 -1681 -1266 C ATOM 1821 CE LYS A1042 39.856 58.129 25.275 1.00 98.78 C ANISOU 1821 CE LYS A1042 13484 11996 12054 -314 -1745 -1533 C ATOM 1822 NZ LYS A1042 40.328 58.741 24.005 1.00107.47 N ANISOU 1822 NZ LYS A1042 14341 12841 13650 -511 -1756 -1461 N ATOM 1823 N ALA A1043 35.098 55.163 26.186 1.00 76.71 N ANISOU 1823 N ALA A1043 11097 9978 8070 -45 -375 -1191 N ATOM 1824 CA ALA A1043 33.912 55.766 26.818 1.00 78.52 C ANISOU 1824 CA ALA A1043 11387 10384 8062 71 -153 -1446 C ATOM 1825 C ALA A1043 32.955 54.726 27.430 1.00 85.94 C ANISOU 1825 C ALA A1043 12398 11585 8669 27 256 -1280 C ATOM 1826 O ALA A1043 32.036 55.115 28.158 1.00 88.38 O ANISOU 1826 O ALA A1043 12754 12117 8709 125 505 -1487 O ATOM 1827 CB ALA A1043 33.158 56.612 25.803 1.00 77.12 C ANISOU 1827 CB ALA A1043 10978 10073 8250 108 -92 -1618 C ATOM 1828 N THR A1044 33.166 53.420 27.152 1.00 83.26 N ANISOU 1828 N THR A1044 12066 11205 8362 -123 344 -918 N ATOM 1829 CA THR A1044 32.311 52.347 27.680 1.00 86.35 C ANISOU 1829 CA THR A1044 12540 11769 8500 -239 736 -692 C ATOM 1830 C THR A1044 33.153 51.390 28.583 1.00 97.37 C ANISOU 1830 C THR A1044 14301 13168 9527 -255 611 -380 C ATOM 1831 O THR A1044 33.540 50.300 28.134 1.00 95.63 O ANISOU 1831 O THR A1044 14091 12762 9483 -360 562 -75 O ATOM 1832 CB THR A1044 31.576 51.624 26.520 1.00 83.01 C ANISOU 1832 CB THR A1044 11820 11234 8486 -413 953 -555 C ATOM 1833 OG1 THR A1044 31.012 52.605 25.644 1.00 75.89 O ANISOU 1833 OG1 THR A1044 10627 10297 7909 -338 925 -838 O ATOM 1834 CG2 THR A1044 30.481 50.685 27.001 1.00 80.98 C ANISOU 1834 CG2 THR A1044 11556 11137 8075 -592 1404 -376 C ATOM 1835 N PRO A1045 33.425 51.771 29.864 1.00102.23 N ANISOU 1835 N PRO A1045 15250 13981 9611 -120 528 -467 N ATOM 1836 CA PRO A1045 34.173 50.869 30.765 1.00106.81 C ANISOU 1836 CA PRO A1045 16233 14568 9782 -98 358 -148 C ATOM 1837 C PRO A1045 33.348 49.624 31.145 1.00117.61 C ANISOU 1837 C PRO A1045 17775 16000 10913 -286 811 249 C ATOM 1838 O PRO A1045 32.120 49.669 30.994 1.00117.72 O ANISOU 1838 O PRO A1045 17592 16162 10976 -420 1290 183 O ATOM 1839 CB PRO A1045 34.463 51.753 31.994 1.00112.50 C ANISOU 1839 CB PRO A1045 17276 15521 9950 108 161 -419 C ATOM 1840 CG PRO A1045 34.172 53.167 31.555 1.00114.67 C ANISOU 1840 CG PRO A1045 17274 15807 10487 196 133 -906 C ATOM 1841 CD PRO A1045 33.059 53.015 30.569 1.00107.06 C ANISOU 1841 CD PRO A1045 15932 14808 9937 50 556 -875 C ATOM 1842 N PRO A1046 33.971 48.499 31.607 1.00119.71 N ANISOU 1842 N PRO A1046 18383 16129 10971 -310 665 666 N ATOM 1843 CA PRO A1046 33.172 47.297 31.938 1.00123.98 C ANISOU 1843 CA PRO A1046 19123 16653 11333 -544 1108 1092 C ATOM 1844 C PRO A1046 32.100 47.558 33.001 1.00135.62 C ANISOU 1844 C PRO A1046 20795 18516 12217 -614 1629 1077 C ATOM 1845 O PRO A1046 32.347 48.296 33.962 1.00137.68 O ANISOU 1845 O PRO A1046 21338 19045 11929 -403 1515 877 O ATOM 1846 CB PRO A1046 34.217 46.296 32.442 1.00128.33 C ANISOU 1846 CB PRO A1046 20112 16976 11672 -456 731 1502 C ATOM 1847 CG PRO A1046 35.506 46.767 31.882 1.00128.68 C ANISOU 1847 CG PRO A1046 19962 16857 12074 -229 133 1278 C ATOM 1848 CD PRO A1046 35.412 48.256 31.830 1.00121.91 C ANISOU 1848 CD PRO A1046 18862 16233 11225 -125 76 774 C ATOM 1849 N LYS A1047 30.895 46.968 32.799 1.00136.18 N ANISOU 1849 N LYS A1047 20688 18631 12425 -913 2210 1251 N ATOM 1850 CA LYS A1047 29.728 47.111 33.681 1.00142.56 C ANISOU 1850 CA LYS A1047 21565 19838 12765 -1036 2846 1248 C ATOM 1851 C LYS A1047 29.961 46.417 35.035 1.00155.68 C ANISOU 1851 C LYS A1047 23915 21615 13620 -1056 2965 1694 C ATOM 1852 O LYS A1047 30.755 45.476 35.122 1.00156.06 O ANISOU 1852 O LYS A1047 24329 21340 13627 -1080 2646 2126 O ATOM 1853 CB LYS A1047 28.436 46.589 32.989 1.00145.15 C ANISOU 1853 CB LYS A1047 21414 20150 13586 -1396 3402 1319 C ATOM 1854 CG LYS A1047 27.979 45.160 33.326 1.00162.44 C ANISOU 1854 CG LYS A1047 23836 22169 15713 -1788 3780 1911 C ATOM 1855 CD LYS A1047 28.675 44.083 32.495 1.00167.55 C ANISOU 1855 CD LYS A1047 24554 22259 16850 -1886 3362 2217 C ATOM 1856 CE LYS A1047 28.346 42.684 32.965 1.00179.71 C ANISOU 1856 CE LYS A1047 26472 23546 18264 -2236 3647 2838 C ATOM 1857 NZ LYS A1047 26.956 42.280 32.617 1.00188.34 N ANISOU 1857 NZ LYS A1047 27141 24661 19760 -2694 4255 2902 N ATOM 1858 N LEU A1048 29.262 46.894 36.082 1.00159.56 N ANISOU 1858 N LEU A1048 24601 22570 13453 -1015 3420 1576 N ATOM 1859 CA LEU A1048 29.351 46.342 37.431 1.00167.94 C ANISOU 1859 CA LEU A1048 26372 23831 13607 -1028 3619 1984 C ATOM 1860 C LEU A1048 28.142 45.442 37.712 1.00179.05 C ANISOU 1860 C LEU A1048 27760 25352 14918 -1469 4456 2412 C ATOM 1861 O LEU A1048 27.033 45.938 37.928 1.00181.95 O ANISOU 1861 O LEU A1048 27812 26134 15187 -1560 5101 2154 O ATOM 1862 CB LEU A1048 29.460 47.465 38.472 1.00171.78 C ANISOU 1862 CB LEU A1048 27153 24783 13333 -678 3585 1551 C ATOM 1863 N GLU A1049 28.364 44.111 37.664 1.00178.23 N ANISOU 1863 N GLU A1049 27952 24847 14921 -1749 4438 3051 N ATOM 1864 CA GLU A1049 27.356 43.074 37.913 1.00218.10 C ANISOU 1864 CA GLU A1049 30931 30975 20961 -1445 4202 3798 C ATOM 1865 C GLU A1049 28.039 41.776 38.353 1.00218.79 C ANISOU 1865 C GLU A1049 29741 29484 23904 -866 2217 2571 C ATOM 1866 O GLU A1049 27.582 41.123 39.290 1.00197.10 O ANISOU 1866 O GLU A1049 27488 27129 20274 -1127 2805 3287 O ATOM 1867 CB GLU A1049 26.477 42.842 36.661 1.00218.77 C ANISOU 1867 CB GLU A1049 31021 30432 21670 -1959 4757 3606 C ATOM 1868 CG GLU A1049 25.316 41.867 36.847 1.00223.06 C ANISOU 1868 CG GLU A1049 30413 31017 23322 -1821 4454 3777 C ATOM 1869 CD GLU A1049 24.345 42.141 37.982 1.00225.79 C ANISOU 1869 CD GLU A1049 30039 30745 25006 -1238 3308 2497 C ATOM 1870 OE1 GLU A1049 23.817 43.274 38.063 1.00219.47 O ANISOU 1870 OE1 GLU A1049 29062 30088 24239 -1066 3325 2090 O ATOM 1871 OE2 GLU A1049 24.090 41.208 38.776 1.00208.82 O ANISOU 1871 OE2 GLU A1049 27870 28380 23093 -1251 3108 2539 O ATOM 1872 N ASP A1060 30.817 40.497 29.126 1.00151.27 N ANISOU 1872 N ASP A1060 22492 18279 16705 -2068 2122 2821 N ATOM 1873 CA ASP A1060 31.186 40.353 27.719 1.00145.96 C ANISOU 1873 CA ASP A1060 21491 17317 16651 -1978 1804 2547 C ATOM 1874 C ASP A1060 31.376 41.733 27.037 1.00143.03 C ANISOU 1874 C ASP A1060 20700 17266 16378 -1728 1640 2031 C ATOM 1875 O ASP A1060 31.642 41.788 25.833 1.00138.58 O ANISOU 1875 O ASP A1060 19865 16542 16247 -1639 1415 1782 O ATOM 1876 CB ASP A1060 30.132 39.512 26.972 1.00149.30 C ANISOU 1876 CB ASP A1060 21665 17474 17588 -2378 2073 2571 C ATOM 1877 CG ASP A1060 30.649 38.849 25.708 1.00157.15 C ANISOU 1877 CG ASP A1060 22559 18024 19127 -2294 1716 2426 C ATOM 1878 OD1 ASP A1060 31.324 37.798 25.820 1.00159.83 O ANISOU 1878 OD1 ASP A1060 23275 17917 19536 -2234 1489 2715 O ATOM 1879 OD2 ASP A1060 30.375 39.378 24.606 1.00158.91 O ANISOU 1879 OD2 ASP A1060 22354 18341 19684 -2262 1653 2015 O ATOM 1880 N PHE A1061 31.272 42.842 27.817 1.00138.84 N ANISOU 1880 N PHE A1061 20164 17166 15423 -1606 1745 1877 N ATOM 1881 CA PHE A1061 31.463 44.221 27.335 1.00133.37 C ANISOU 1881 CA PHE A1061 19150 16731 14793 -1378 1582 1425 C ATOM 1882 C PHE A1061 32.932 44.448 26.917 1.00132.13 C ANISOU 1882 C PHE A1061 19049 16420 14736 -1075 1062 1338 C ATOM 1883 O PHE A1061 33.202 45.202 25.977 1.00127.24 O ANISOU 1883 O PHE A1061 18120 15827 14400 -961 900 1027 O ATOM 1884 CB PHE A1061 31.037 45.237 28.407 1.00137.37 C ANISOU 1884 CB PHE A1061 19724 17668 14801 -1302 1796 1285 C ATOM 1885 N ARG A1062 33.869 43.763 27.608 1.00129.94 N ANISOU 1885 N ARG A1062 19157 15975 14240 -950 807 1632 N ATOM 1886 CA ARG A1062 35.305 43.803 27.331 1.00127.01 C ANISOU 1886 CA ARG A1062 18795 15460 14004 -662 316 1574 C ATOM 1887 C ARG A1062 35.606 43.031 26.039 1.00125.29 C ANISOU 1887 C ARG A1062 18375 14898 14332 -664 220 1550 C ATOM 1888 O ARG A1062 36.275 43.571 25.153 1.00121.35 O ANISOU 1888 O ARG A1062 17588 14405 14114 -513 26 1289 O ATOM 1889 CB ARG A1062 36.101 43.225 28.517 1.00131.67 C ANISOU 1889 CB ARG A1062 19859 15985 14183 -495 37 1895 C ATOM 1890 N HIS A1063 35.077 41.779 25.934 1.00121.18 N ANISOU 1890 N HIS A1063 18019 14070 13953 -852 382 1813 N ATOM 1891 CA HIS A1063 35.228 40.864 24.795 1.00118.21 C ANISOU 1891 CA HIS A1063 17531 13317 14065 -860 302 1774 C ATOM 1892 C HIS A1063 34.552 41.384 23.527 1.00112.41 C ANISOU 1892 C HIS A1063 16381 12676 13652 -980 465 1419 C ATOM 1893 O HIS A1063 35.110 41.231 22.441 1.00110.27 O ANISOU 1893 O HIS A1063 15946 12257 13694 -844 307 1225 O ATOM 1894 CB HIS A1063 34.646 39.480 25.124 1.00124.05 C ANISOU 1894 CB HIS A1063 18595 13666 14871 -1084 435 2142 C ATOM 1895 CG HIS A1063 35.329 38.770 26.248 1.00132.64 C ANISOU 1895 CG HIS A1063 20175 14564 15658 -942 223 2555 C ATOM 1896 ND1 HIS A1063 36.541 38.127 26.064 1.00135.68 N ANISOU 1896 ND1 HIS A1063 20692 14624 16236 -613 -200 2613 N ATOM 1897 CD2 HIS A1063 34.923 38.585 27.526 1.00139.22 C ANISOU 1897 CD2 HIS A1063 21406 15491 16001 -1069 380 2926 C ATOM 1898 CE1 HIS A1063 36.843 37.591 27.236 1.00140.31 C ANISOU 1898 CE1 HIS A1063 21762 15091 16457 -534 -351 3027 C ATOM 1899 NE2 HIS A1063 35.900 37.841 28.147 1.00142.96 N ANISOU 1899 NE2 HIS A1063 22307 15677 16335 -813 -1 3244 N ATOM 1900 N GLY A1064 33.351 41.948 23.674 1.00103.99 N ANISOU 1900 N GLY A1064 15160 11858 12492 -1210 775 1336 N ATOM 1901 CA GLY A1064 32.541 42.473 22.580 1.00 98.85 C ANISOU 1901 CA GLY A1064 14135 11313 12111 -1315 892 1018 C ATOM 1902 C GLY A1064 33.253 43.464 21.682 1.00 94.03 C ANISOU 1902 C GLY A1064 13304 10834 11589 -1077 685 719 C ATOM 1903 O GLY A1064 33.181 43.356 20.454 1.00 90.88 O ANISOU 1903 O GLY A1064 12734 10337 11460 -1068 630 525 O ATOM 1904 N PHE A1065 33.956 44.429 22.295 1.00 86.79 N ANISOU 1904 N PHE A1065 12415 10131 10430 -899 565 682 N ATOM 1905 CA PHE A1065 34.705 45.440 21.563 1.00 82.03 C ANISOU 1905 CA PHE A1065 11618 9630 9919 -723 391 450 C ATOM 1906 C PHE A1065 35.892 44.812 20.820 1.00 84.27 C ANISOU 1906 C PHE A1065 11891 9705 10425 -563 193 455 C ATOM 1907 O PHE A1065 36.140 45.192 19.673 1.00 82.31 O ANISOU 1907 O PHE A1065 11455 9468 10352 -509 177 270 O ATOM 1908 CB PHE A1065 35.167 46.575 22.490 1.00 83.34 C ANISOU 1908 CB PHE A1065 11821 10022 9821 -612 284 395 C ATOM 1909 CG PHE A1065 34.144 47.673 22.692 1.00 83.35 C ANISOU 1909 CG PHE A1065 11712 10255 9702 -673 451 212 C ATOM 1910 CD1 PHE A1065 33.868 48.588 21.677 1.00 82.70 C ANISOU 1910 CD1 PHE A1065 11399 10209 9812 -651 438 -15 C ATOM 1911 CD2 PHE A1065 33.479 47.811 23.904 1.00 86.68 C ANISOU 1911 CD2 PHE A1065 12281 10857 9796 -722 619 264 C ATOM 1912 CE1 PHE A1065 32.923 49.602 21.864 1.00 82.85 C ANISOU 1912 CE1 PHE A1065 11313 10402 9766 -650 547 -203 C ATOM 1913 CE2 PHE A1065 32.534 48.825 24.087 1.00 89.09 C ANISOU 1913 CE2 PHE A1065 12449 11383 10021 -724 786 39 C ATOM 1914 CZ PHE A1065 32.257 49.708 23.063 1.00 84.30 C ANISOU 1914 CZ PHE A1065 11588 10769 9674 -674 726 -201 C ATOM 1915 N ASP A1066 36.579 43.819 21.438 1.00 81.71 N ANISOU 1915 N ASP A1066 11776 9186 10083 -470 58 667 N ATOM 1916 CA ASP A1066 37.714 43.092 20.840 1.00 81.63 C ANISOU 1916 CA ASP A1066 11736 8962 10318 -262 -130 653 C ATOM 1917 C ASP A1066 37.295 42.361 19.550 1.00 83.43 C ANISOU 1917 C ASP A1066 11898 8987 10815 -312 -19 514 C ATOM 1918 O ASP A1066 38.082 42.282 18.602 1.00 82.13 O ANISOU 1918 O ASP A1066 11586 8786 10833 -139 -75 344 O ATOM 1919 CB ASP A1066 38.319 42.082 21.834 1.00 87.53 C ANISOU 1919 CB ASP A1066 12770 9487 11000 -132 -331 929 C ATOM 1920 CG ASP A1066 38.704 42.630 23.200 1.00105.08 C ANISOU 1920 CG ASP A1066 15152 11897 12878 -63 -499 1076 C ATOM 1921 OD1 ASP A1066 38.942 43.860 23.310 1.00104.72 O ANISOU 1921 OD1 ASP A1066 14925 12137 12729 -49 -536 898 O ATOM 1922 OD2 ASP A1066 38.799 41.824 24.157 1.00116.44 O ANISOU 1922 OD2 ASP A1066 16932 13173 14137 -15 -622 1369 O ATOM 1923 N ILE A1067 36.048 41.846 19.523 1.00 79.55 N ANISOU 1923 N ILE A1067 11499 8383 10343 -555 145 563 N ATOM 1924 CA ILE A1067 35.458 41.152 18.383 1.00 79.31 C ANISOU 1924 CA ILE A1067 11427 8151 10558 -644 200 395 C ATOM 1925 C ILE A1067 35.230 42.155 17.258 1.00 81.74 C ANISOU 1925 C ILE A1067 11491 8706 10861 -622 248 108 C ATOM 1926 O ILE A1067 35.658 41.906 16.130 1.00 81.98 O ANISOU 1926 O ILE A1067 11477 8665 11006 -486 202 -86 O ATOM 1927 CB ILE A1067 34.150 40.401 18.787 1.00 84.39 C ANISOU 1927 CB ILE A1067 12178 8620 11268 -970 347 530 C ATOM 1928 CG1 ILE A1067 34.472 39.146 19.626 1.00 88.12 C ANISOU 1928 CG1 ILE A1067 12982 8719 11779 -991 285 856 C ATOM 1929 CG2 ILE A1067 33.307 40.032 17.557 1.00 85.04 C ANISOU 1929 CG2 ILE A1067 12135 8572 11604 -1105 362 265 C ATOM 1930 CD1 ILE A1067 33.390 38.712 20.566 1.00 97.26 C ANISOU 1930 CD1 ILE A1067 14278 9813 12864 -1346 508 1134 C ATOM 1931 N LEU A1068 34.575 43.287 17.568 1.00 77.32 N ANISOU 1931 N LEU A1068 10806 8428 10144 -728 337 83 N ATOM 1932 CA LEU A1068 34.278 44.326 16.585 1.00 74.89 C ANISOU 1932 CA LEU A1068 10322 8320 9813 -701 346 -135 C ATOM 1933 C LEU A1068 35.558 45.008 16.104 1.00 76.10 C ANISOU 1933 C LEU A1068 10418 8570 9928 -499 282 -186 C ATOM 1934 O LEU A1068 35.718 45.166 14.888 1.00 74.71 O ANISOU 1934 O LEU A1068 10197 8415 9774 -432 291 -339 O ATOM 1935 CB LEU A1068 33.264 45.351 17.122 1.00 74.38 C ANISOU 1935 CB LEU A1068 10143 8484 9633 -815 429 -155 C ATOM 1936 CG LEU A1068 31.908 44.794 17.627 1.00 81.34 C ANISOU 1936 CG LEU A1068 10978 9349 10579 -1049 571 -120 C ATOM 1937 CD1 LEU A1068 31.001 45.920 18.099 1.00 81.51 C ANISOU 1937 CD1 LEU A1068 10830 9642 10498 -1082 672 -203 C ATOM 1938 CD2 LEU A1068 31.191 43.946 16.562 1.00 84.09 C ANISOU 1938 CD2 LEU A1068 11256 9527 11169 -1169 529 -271 C ATOM 1939 N VAL A1069 36.503 45.327 17.026 1.00 72.02 N ANISOU 1939 N VAL A1069 9904 8110 9352 -411 216 -60 N ATOM 1940 CA VAL A1069 37.787 45.944 16.647 1.00 71.44 C ANISOU 1940 CA VAL A1069 9697 8125 9322 -266 164 -105 C ATOM 1941 C VAL A1069 38.605 44.931 15.820 1.00 77.37 C ANISOU 1941 C VAL A1069 10427 8731 10237 -103 173 -173 C ATOM 1942 O VAL A1069 39.207 45.311 14.812 1.00 77.25 O ANISOU 1942 O VAL A1069 10287 8809 10257 -28 261 -290 O ATOM 1943 CB VAL A1069 38.577 46.522 17.852 1.00 75.48 C ANISOU 1943 CB VAL A1069 10176 8728 9776 -219 22 -4 C ATOM 1944 CG1 VAL A1069 40.008 46.874 17.474 1.00 75.67 C ANISOU 1944 CG1 VAL A1069 9984 8807 9958 -96 -42 -55 C ATOM 1945 CG2 VAL A1069 37.873 47.752 18.420 1.00 74.16 C ANISOU 1945 CG2 VAL A1069 10018 8716 9442 -335 29 -32 C ATOM 1946 N GLY A1070 38.541 43.654 16.212 1.00 75.77 N ANISOU 1946 N GLY A1070 10374 8290 10124 -56 106 -104 N ATOM 1947 CA GLY A1070 39.196 42.550 15.520 1.00 76.65 C ANISOU 1947 CA GLY A1070 10507 8195 10421 138 87 -208 C ATOM 1948 C GLY A1070 38.817 42.483 14.056 1.00 78.73 C ANISOU 1948 C GLY A1070 10761 8479 10673 139 220 -450 C ATOM 1949 O GLY A1070 39.702 42.444 13.202 1.00 80.47 O ANISOU 1949 O GLY A1070 10873 8764 10937 326 303 -604 O ATOM 1950 N GLN A1071 37.502 42.522 13.755 1.00 72.61 N ANISOU 1950 N GLN A1071 10082 7686 9820 -64 241 -499 N ATOM 1951 CA GLN A1071 36.978 42.487 12.388 1.00 72.81 C ANISOU 1951 CA GLN A1071 10145 7740 9780 -65 286 -742 C ATOM 1952 C GLN A1071 37.439 43.693 11.558 1.00 77.89 C ANISOU 1952 C GLN A1071 10684 8681 10228 -4 401 -795 C ATOM 1953 O GLN A1071 37.794 43.515 10.393 1.00 79.54 O ANISOU 1953 O GLN A1071 10941 8935 10345 127 486 -977 O ATOM 1954 CB GLN A1071 35.444 42.414 12.381 1.00 73.70 C ANISOU 1954 CB GLN A1071 10307 7799 9895 -303 223 -779 C ATOM 1955 CG GLN A1071 34.888 41.015 12.620 1.00 91.72 C ANISOU 1955 CG GLN A1071 12722 9725 12403 -408 140 -803 C ATOM 1956 CD GLN A1071 34.922 40.099 11.412 1.00107.91 C ANISOU 1956 CD GLN A1071 14899 11569 14533 -296 60 -1107 C ATOM 1957 OE1 GLN A1071 35.459 40.421 10.340 1.00 98.54 O ANISOU 1957 OE1 GLN A1071 13725 10541 13177 -102 98 -1312 O ATOM 1958 NE2 GLN A1071 34.329 38.926 11.569 1.00103.35 N ANISOU 1958 NE2 GLN A1071 14444 10621 14204 -431 -44 -1146 N ATOM 1959 N ILE A1072 37.429 44.911 12.158 1.00 73.43 N ANISOU 1959 N ILE A1072 10015 8299 9588 -103 413 -637 N ATOM 1960 CA ILE A1072 37.862 46.156 11.515 1.00 72.63 C ANISOU 1960 CA ILE A1072 9842 8410 9343 -98 514 -620 C ATOM 1961 C ILE A1072 39.353 46.018 11.187 1.00 80.28 C ANISOU 1961 C ILE A1072 10675 9443 10386 53 661 -634 C ATOM 1962 O ILE A1072 39.735 46.292 10.049 1.00 82.04 O ANISOU 1962 O ILE A1072 10911 9789 10471 110 836 -710 O ATOM 1963 CB ILE A1072 37.533 47.431 12.360 1.00 73.27 C ANISOU 1963 CB ILE A1072 9857 8589 9394 -230 454 -476 C ATOM 1964 CG1 ILE A1072 36.016 47.558 12.617 1.00 71.90 C ANISOU 1964 CG1 ILE A1072 9748 8391 9179 -341 350 -508 C ATOM 1965 CG2 ILE A1072 38.052 48.691 11.659 1.00 74.23 C ANISOU 1965 CG2 ILE A1072 9951 8842 9413 -251 546 -428 C ATOM 1966 CD1 ILE A1072 35.642 48.371 13.807 1.00 76.32 C ANISOU 1966 CD1 ILE A1072 10247 9009 9743 -419 299 -417 C ATOM 1967 N ASP A1073 40.169 45.523 12.148 1.00 78.60 N ANISOU 1967 N ASP A1073 10330 9155 10379 136 592 -569 N ATOM 1968 CA ASP A1073 41.604 45.259 11.950 1.00 81.81 C ANISOU 1968 CA ASP A1073 10512 9620 10950 318 695 -618 C ATOM 1969 C ASP A1073 41.826 44.182 10.874 1.00 89.46 C ANISOU 1969 C ASP A1073 11552 10522 11917 528 829 -845 C ATOM 1970 O ASP A1073 42.800 44.255 10.130 1.00 91.64 O ANISOU 1970 O ASP A1073 11653 10957 12208 657 1059 -948 O ATOM 1971 CB ASP A1073 42.278 44.816 13.264 1.00 84.82 C ANISOU 1971 CB ASP A1073 10775 9897 11554 413 482 -518 C ATOM 1972 CG ASP A1073 42.482 45.893 14.318 1.00 96.25 C ANISOU 1972 CG ASP A1073 12102 11456 13013 272 344 -365 C ATOM 1973 OD1 ASP A1073 42.785 47.048 13.942 1.00 96.59 O ANISOU 1973 OD1 ASP A1073 11992 11666 13042 146 460 -355 O ATOM 1974 OD2 ASP A1073 42.423 45.560 15.523 1.00103.45 O ANISOU 1974 OD2 ASP A1073 13092 12270 13944 295 112 -258 O ATOM 1975 N ASP A1074 40.926 43.186 10.805 1.00 87.40 N ANISOU 1975 N ASP A1074 11538 10021 11649 550 700 -941 N ATOM 1976 CA ASP A1074 40.983 42.107 9.824 1.00 91.03 C ANISOU 1976 CA ASP A1074 12131 10348 12108 751 760 -1216 C ATOM 1977 C ASP A1074 40.672 42.648 8.426 1.00 95.51 C ANISOU 1977 C ASP A1074 12810 11133 12347 732 951 -1374 C ATOM 1978 O ASP A1074 41.387 42.320 7.480 1.00 98.73 O ANISOU 1978 O ASP A1074 13208 11634 12671 946 1157 -1590 O ATOM 1979 CB ASP A1074 40.023 40.960 10.203 1.00 94.05 C ANISOU 1979 CB ASP A1074 12759 10360 12614 701 529 -1260 C ATOM 1980 CG ASP A1074 40.657 39.815 10.986 1.00111.09 C ANISOU 1980 CG ASP A1074 14929 12198 15082 892 382 -1227 C ATOM 1981 OD1 ASP A1074 41.592 40.080 11.786 1.00111.61 O ANISOU 1981 OD1 ASP A1074 14793 12340 15273 1000 351 -1068 O ATOM 1982 OD2 ASP A1074 40.200 38.659 10.822 1.00121.47 O ANISOU 1982 OD2 ASP A1074 16468 13154 16532 932 254 -1357 O ATOM 1983 N ALA A1075 39.633 43.497 8.299 1.00 88.86 N ANISOU 1983 N ALA A1075 12084 10382 11296 507 881 -1270 N ATOM 1984 CA ALA A1075 39.267 44.120 7.028 1.00 89.04 C ANISOU 1984 CA ALA A1075 12275 10600 10955 495 990 -1359 C ATOM 1985 C ALA A1075 40.364 45.092 6.579 1.00 93.75 C ANISOU 1985 C ALA A1075 12726 11477 11418 510 1307 -1231 C ATOM 1986 O ALA A1075 40.670 45.133 5.393 1.00 95.46 O ANISOU 1986 O ALA A1075 13076 11864 11332 612 1530 -1349 O ATOM 1987 CB ALA A1075 37.932 44.836 7.157 1.00 87.31 C ANISOU 1987 CB ALA A1075 12172 10378 10624 290 775 -1263 C ATOM 1988 N LEU A1076 40.993 45.818 7.539 1.00 90.08 N ANISOU 1988 N LEU A1076 11992 11057 11179 398 1333 -1000 N ATOM 1989 CA LEU A1076 42.072 46.788 7.305 1.00 91.68 C ANISOU 1989 CA LEU A1076 11977 11480 11379 332 1616 -851 C ATOM 1990 C LEU A1076 43.334 46.128 6.785 1.00101.60 C ANISOU 1990 C LEU A1076 13013 12866 12724 547 1924 -1018 C ATOM 1991 O LEU A1076 43.928 46.658 5.844 1.00105.11 O ANISOU 1991 O LEU A1076 13436 13544 12958 530 2284 -998 O ATOM 1992 CB LEU A1076 42.410 47.576 8.579 1.00 89.38 C ANISOU 1992 CB LEU A1076 11435 11153 11372 164 1477 -638 C ATOM 1993 CG LEU A1076 42.515 49.095 8.439 1.00 93.63 C ANISOU 1993 CG LEU A1076 11955 11788 11834 -75 1569 -414 C ATOM 1994 CD1 LEU A1076 42.285 49.767 9.769 1.00 91.52 C ANISOU 1994 CD1 LEU A1076 11606 11402 11765 -221 1285 -291 C ATOM 1995 CD2 LEU A1076 43.860 49.525 7.881 1.00 99.05 C ANISOU 1995 CD2 LEU A1076 12355 12662 12616 -125 1932 -353 C ATOM 1996 N LYS A1077 43.751 44.986 7.388 1.00 99.58 N ANISOU 1996 N LYS A1077 12602 12458 12777 761 1800 -1174 N ATOM 1997 CA LYS A1077 44.959 44.250 6.987 1.00104.18 C ANISOU 1997 CA LYS A1077 12921 13136 13525 1046 2052 -1391 C ATOM 1998 C LYS A1077 44.780 43.612 5.596 1.00111.69 C ANISOU 1998 C LYS A1077 14149 14163 14126 1245 2286 -1685 C ATOM 1999 O LYS A1077 45.769 43.368 4.906 1.00115.42 O ANISOU 1999 O LYS A1077 14427 14848 14579 1446 2660 -1864 O ATOM 2000 CB LYS A1077 45.370 43.201 8.044 1.00107.52 C ANISOU 2000 CB LYS A1077 13175 13307 14371 1269 1767 -1468 C ATOM 2001 CG LYS A1077 44.444 41.990 8.174 1.00129.83 C ANISOU 2001 CG LYS A1077 16367 15771 17193 1382 1471 -1603 C ATOM 2002 CD LYS A1077 44.926 40.977 9.205 1.00144.81 C ANISOU 2002 CD LYS A1077 18153 17377 19491 1616 1199 -1621 C ATOM 2003 CE LYS A1077 44.001 39.786 9.292 1.00155.16 C ANISOU 2003 CE LYS A1077 19853 18271 20830 1673 939 -1721 C ATOM 2004 NZ LYS A1077 44.422 38.833 10.352 1.00165.77 N ANISOU 2004 NZ LYS A1077 21172 19272 22541 1886 646 -1658 N ATOM 2005 N LEU A1078 43.516 43.363 5.196 1.00107.40 N ANISOU 2005 N LEU A1078 14037 13465 13307 1191 2064 -1759 N ATOM 2006 CA LEU A1078 43.119 42.805 3.900 1.00110.55 C ANISOU 2006 CA LEU A1078 14785 13911 13310 1356 2167 -2066 C ATOM 2007 C LEU A1078 43.142 43.901 2.840 1.00114.94 C ANISOU 2007 C LEU A1078 15491 14812 13370 1231 2485 -1933 C ATOM 2008 O LEU A1078 43.533 43.650 1.697 1.00119.00 O ANISOU 2008 O LEU A1078 16147 15540 13527 1419 2810 -2152 O ATOM 2009 CB LEU A1078 41.708 42.204 4.013 1.00108.80 C ANISOU 2009 CB LEU A1078 14906 13380 13052 1287 1732 -2175 C ATOM 2010 CG LEU A1078 41.566 40.684 4.094 1.00116.21 C ANISOU 2010 CG LEU A1078 15969 13974 14213 1520 1531 -2525 C ATOM 2011 CD1 LEU A1078 42.378 40.085 5.252 1.00116.84 C ANISOU 2011 CD1 LEU A1078 15751 13836 14808 1653 1470 -2460 C ATOM 2012 CD2 LEU A1078 40.113 40.310 4.266 1.00116.47 C ANISOU 2012 CD2 LEU A1078 16267 13717 14268 1331 1121 -2567 C ATOM 2013 N ALA A1079 42.724 45.120 3.236 1.00107.44 N ANISOU 2013 N ALA A1079 14539 13900 12382 926 2396 -1568 N ATOM 2014 CA ALA A1079 42.698 46.320 2.402 1.00108.55 C ANISOU 2014 CA ALA A1079 14859 14283 12100 760 2638 -1332 C ATOM 2015 C ALA A1079 44.117 46.840 2.159 1.00115.87 C ANISOU 2015 C ALA A1079 15450 15485 13090 717 3171 -1201 C ATOM 2016 O ALA A1079 44.365 47.454 1.119 1.00119.53 O ANISOU 2016 O ALA A1079 16103 16194 13117 657 3538 -1083 O ATOM 2017 CB ALA A1079 41.848 47.394 3.059 1.00105.06 C ANISOU 2017 CB ALA A1079 14487 13713 11718 483 2330 -1014 C ATOM 2018 N ASN A1080 45.043 46.587 3.112 1.00111.38 N ANISOU 2018 N ASN A1080 14378 14880 13062 742 3208 -1212 N ATOM 2019 CA ASN A1080 46.454 46.975 3.023 1.00115.03 C ANISOU 2019 CA ASN A1080 14373 15600 13734 697 3679 -1137 C ATOM 2020 C ASN A1080 47.236 46.000 2.119 1.00125.08 C ANISOU 2020 C ASN A1080 15549 17098 14878 1045 4102 -1500 C ATOM 2021 O ASN A1080 48.161 46.417 1.414 1.00129.54 O ANISOU 2021 O ASN A1080 15888 17993 15338 1003 4664 -1453 O ATOM 2022 CB ASN A1080 47.082 47.044 4.416 1.00112.46 C ANISOU 2022 CB ASN A1080 13536 15148 14047 628 3452 -1056 C ATOM 2023 CG ASN A1080 46.721 48.278 5.220 1.00131.62 C ANISOU 2023 CG ASN A1080 15953 17450 16608 262 3201 -709 C ATOM 2024 OD1 ASN A1080 46.361 49.337 4.684 1.00127.22 O ANISOU 2024 OD1 ASN A1080 15650 16932 15756 12 3314 -462 O ATOM 2025 ND2 ASN A1080 46.862 48.185 6.534 1.00118.74 N ANISOU 2025 ND2 ASN A1080 14046 15653 15417 246 2843 -690 N ATOM 2026 N GLU A1081 46.849 44.704 2.138 1.00121.43 N ANISOU 2026 N GLU A1081 15262 16442 14434 1382 3846 -1869 N ATOM 2027 CA GLU A1081 47.443 43.643 1.324 1.00126.39 C ANISOU 2027 CA GLU A1081 15869 17203 14952 1786 4156 -2306 C ATOM 2028 C GLU A1081 47.022 43.799 -0.138 1.00134.09 C ANISOU 2028 C GLU A1081 17350 18428 15169 1830 4473 -2415 C ATOM 2029 O GLU A1081 47.757 43.382 -1.033 1.00140.05 O ANISOU 2029 O GLU A1081 18049 19468 15696 2093 4962 -2701 O ATOM 2030 CB GLU A1081 47.045 42.259 1.859 1.00126.33 C ANISOU 2030 CB GLU A1081 15964 16800 15237 2097 3698 -2643 C ATOM 2031 N GLY A1082 45.855 44.403 -0.360 1.00127.51 N ANISOU 2031 N GLY A1082 17002 17504 13941 1603 4184 -2204 N ATOM 2032 CA GLY A1082 45.329 44.669 -1.692 1.00130.91 C ANISOU 2032 CA GLY A1082 17991 18154 13597 1633 4363 -2251 C ATOM 2033 C GLY A1082 43.870 44.328 -1.898 1.00132.30 C ANISOU 2033 C GLY A1082 18707 18080 13480 1670 3787 -2401 C ATOM 2034 O GLY A1082 43.098 45.185 -2.336 1.00131.74 O ANISOU 2034 O GLY A1082 19031 18076 12949 1500 3665 -2164 O ATOM 2035 N LYS A1083 43.493 43.064 -1.599 1.00127.64 N ANISOU 2035 N LYS A1083 18131 17182 13186 1893 3414 -2798 N ATOM 2036 CA LYS A1083 42.153 42.486 -1.775 1.00125.97 C ANISOU 2036 CA LYS A1083 18342 16694 12827 1924 2850 -3034 C ATOM 2037 C LYS A1083 41.042 43.394 -1.209 1.00123.72 C ANISOU 2037 C LYS A1083 18132 16271 12604 1583 2431 -2651 C ATOM 2038 O LYS A1083 40.896 43.510 0.006 1.00118.76 O ANISOU 2038 O LYS A1083 17183 15431 12509 1403 2236 -2430 O ATOM 2039 CB LYS A1083 42.086 41.082 -1.149 1.00128.02 C ANISOU 2039 CB LYS A1083 18479 16554 13608 2121 2547 -3411 C ATOM 2040 CG LYS A1083 41.545 40.035 -2.112 1.00145.91 C ANISOU 2040 CG LYS A1083 21185 18696 15558 2385 2337 -3963 C ATOM 2041 CD LYS A1083 41.800 38.614 -1.624 1.00157.04 C ANISOU 2041 CD LYS A1083 22470 19692 17506 2630 2162 -4347 C ATOM 2042 CE LYS A1083 41.303 37.572 -2.600 1.00172.22 C ANISOU 2042 CE LYS A1083 24835 21453 19149 2907 1958 -4961 C ATOM 2043 NZ LYS A1083 42.209 37.420 -3.772 1.00187.22 N ANISOU 2043 NZ LYS A1083 26879 23749 20508 3280 2480 -5310 N ATOM 2044 N VAL A1084 40.282 44.048 -2.113 1.00120.98 N ANISOU 2044 N VAL A1084 18224 16065 11680 1532 2295 -2584 N ATOM 2045 CA VAL A1084 39.205 44.993 -1.783 1.00116.40 C ANISOU 2045 CA VAL A1084 17743 15386 11097 1280 1899 -2262 C ATOM 2046 C VAL A1084 37.876 44.275 -1.538 1.00117.34 C ANISOU 2046 C VAL A1084 17957 15205 11422 1274 1285 -2533 C ATOM 2047 O VAL A1084 37.199 44.612 -0.570 1.00113.01 O ANISOU 2047 O VAL A1084 17191 14468 11280 1066 997 -2334 O ATOM 2048 CB VAL A1084 39.031 46.145 -2.815 1.00123.21 C ANISOU 2048 CB VAL A1084 19022 16516 11275 1238 2008 -1992 C ATOM 2049 CG1 VAL A1084 40.207 47.101 -2.758 1.00123.52 C ANISOU 2049 CG1 VAL A1084 18869 16760 11302 1075 2567 -1562 C ATOM 2050 CG2 VAL A1084 38.825 45.631 -4.241 1.00129.55 C ANISOU 2050 CG2 VAL A1084 20346 17524 11354 1509 2039 -2344 C ATOM 2051 N LYS A1085 37.504 43.307 -2.399 1.00116.52 N ANISOU 2051 N LYS A1085 18163 15062 11047 1487 1098 -3004 N ATOM 2052 CA LYS A1085 36.265 42.537 -2.281 1.00115.64 C ANISOU 2052 CA LYS A1085 18127 14652 11159 1452 515 -3320 C ATOM 2053 C LYS A1085 36.257 41.730 -0.982 1.00115.26 C ANISOU 2053 C LYS A1085 17686 14238 11870 1326 417 -3337 C ATOM 2054 O LYS A1085 35.215 41.632 -0.334 1.00111.55 O ANISOU 2054 O LYS A1085 17086 13542 11755 1118 29 -3302 O ATOM 2055 CB LYS A1085 36.086 41.613 -3.494 1.00124.44 C ANISOU 2055 CB LYS A1085 19661 15784 11836 1721 369 -3874 C ATOM 2056 N GLU A1086 37.433 41.185 -0.592 1.00112.42 N ANISOU 2056 N GLU A1086 17129 13835 11751 1460 780 -3372 N ATOM 2057 CA GLU A1086 37.624 40.409 0.635 1.00109.54 C ANISOU 2057 CA GLU A1086 16451 13119 12048 1391 710 -3336 C ATOM 2058 C GLU A1086 37.540 41.311 1.854 1.00107.41 C ANISOU 2058 C GLU A1086 15861 12865 12084 1120 720 -2847 C ATOM 2059 O GLU A1086 37.024 40.880 2.883 1.00105.32 O ANISOU 2059 O GLU A1086 15441 12314 12263 954 492 -2762 O ATOM 2060 CB GLU A1086 38.972 39.673 0.614 1.00113.87 C ANISOU 2060 CB GLU A1086 16881 13651 12734 1683 1063 -3515 C ATOM 2061 CG GLU A1086 38.851 38.161 0.744 1.00127.97 C ANISOU 2061 CG GLU A1086 18761 14991 14873 1845 823 -3923 C ATOM 2062 CD GLU A1086 38.834 37.606 2.159 1.00146.40 C ANISOU 2062 CD GLU A1086 20847 16919 17859 1714 648 -3712 C ATOM 2063 OE1 GLU A1086 39.687 36.739 2.457 1.00141.60 O ANISOU 2063 OE1 GLU A1086 20148 16097 17556 1968 739 -3852 O ATOM 2064 OE2 GLU A1086 37.961 38.015 2.961 1.00133.07 O ANISOU 2064 OE2 GLU A1086 19070 15128 16362 1382 419 -3414 O ATOM 2065 N ALA A1087 38.044 42.562 1.735 1.00101.25 N ANISOU 2065 N ALA A1087 15012 12407 11050 1065 994 -2528 N ATOM 2066 CA ALA A1087 38.017 43.576 2.790 1.00 95.61 C ANISOU 2066 CA ALA A1087 14037 11726 10566 829 1002 -2104 C ATOM 2067 C ALA A1087 36.601 44.106 2.989 1.00 95.85 C ANISOU 2067 C ALA A1087 14145 11684 10590 636 622 -2019 C ATOM 2068 O ALA A1087 36.210 44.371 4.125 1.00 92.88 O ANISOU 2068 O ALA A1087 13547 11189 10555 458 500 -1823 O ATOM 2069 CB ALA A1087 38.959 44.719 2.445 1.00 96.91 C ANISOU 2069 CB ALA A1087 14148 12199 10476 812 1384 -1835 C ATOM 2070 N GLN A1088 35.838 44.269 1.885 1.00 93.10 N ANISOU 2070 N GLN A1088 14106 11428 9840 696 425 -2185 N ATOM 2071 CA GLN A1088 34.448 44.744 1.891 1.00 91.06 C ANISOU 2071 CA GLN A1088 13891 11125 9584 571 12 -2172 C ATOM 2072 C GLN A1088 33.547 43.725 2.565 1.00 93.13 C ANISOU 2072 C GLN A1088 13986 11099 10301 447 -283 -2383 C ATOM 2073 O GLN A1088 32.616 44.108 3.271 1.00 90.22 O ANISOU 2073 O GLN A1088 13411 10668 10199 266 -481 -2264 O ATOM 2074 CB GLN A1088 33.949 45.018 0.462 1.00 96.14 C ANISOU 2074 CB GLN A1088 14932 11935 9663 718 -184 -2339 C ATOM 2075 CG GLN A1088 34.486 46.297 -0.163 1.00101.39 C ANISOU 2075 CG GLN A1088 15807 12855 9861 763 41 -2009 C ATOM 2076 CD GLN A1088 33.981 46.477 -1.567 1.00121.38 C ANISOU 2076 CD GLN A1088 18812 15546 11759 936 -181 -2151 C ATOM 2077 OE1 GLN A1088 34.277 45.688 -2.472 1.00122.59 O ANISOU 2077 OE1 GLN A1088 19242 15786 11549 1118 -114 -2469 O ATOM 2078 NE2 GLN A1088 33.209 47.531 -1.783 1.00112.31 N ANISOU 2078 NE2 GLN A1088 17799 14436 10437 917 -471 -1929 N ATOM 2079 N ALA A1089 33.834 42.428 2.333 1.00 92.26 N ANISOU 2079 N ALA A1089 13963 10799 10294 542 -287 -2699 N ATOM 2080 CA ALA A1089 33.129 41.277 2.891 1.00 92.50 C ANISOU 2080 CA ALA A1089 13887 10474 10784 400 -532 -2896 C ATOM 2081 C ALA A1089 33.511 41.081 4.351 1.00 93.36 C ANISOU 2081 C ALA A1089 13718 10413 11339 251 -361 -2599 C ATOM 2082 O ALA A1089 32.638 40.754 5.154 1.00 93.11 O ANISOU 2082 O ALA A1089 13525 10186 11668 11 -525 -2543 O ATOM 2083 CB ALA A1089 33.444 40.024 2.088 1.00 97.50 C ANISOU 2083 CB ALA A1089 14768 10911 11368 589 -590 -3332 C ATOM 2084 N ALA A1090 34.802 41.296 4.703 1.00 88.23 N ANISOU 2084 N ALA A1090 13004 9859 10660 385 -32 -2407 N ATOM 2085 CA ALA A1090 35.288 41.197 6.086 1.00 85.72 C ANISOU 2085 CA ALA A1090 12461 9416 10692 292 86 -2117 C ATOM 2086 C ALA A1090 34.641 42.286 6.959 1.00 86.71 C ANISOU 2086 C ALA A1090 12401 9683 10861 70 55 -1811 C ATOM 2087 O ALA A1090 34.315 42.025 8.113 1.00 85.29 O ANISOU 2087 O ALA A1090 12090 9354 10962 -94 23 -1643 O ATOM 2088 CB ALA A1090 36.801 41.311 6.128 1.00 86.65 C ANISOU 2088 CB ALA A1090 12505 9652 10768 510 384 -2036 C ATOM 2089 N ALA A1091 34.419 43.486 6.383 1.00 82.66 N ANISOU 2089 N ALA A1091 11918 9441 10049 81 61 -1745 N ATOM 2090 CA ALA A1091 33.740 44.612 7.023 1.00 80.28 C ANISOU 2090 CA ALA A1091 11471 9260 9772 -68 -3 -1527 C ATOM 2091 C ALA A1091 32.246 44.323 7.139 1.00 83.81 C ANISOU 2091 C ALA A1091 11838 9611 10396 -226 -276 -1662 C ATOM 2092 O ALA A1091 31.640 44.656 8.156 1.00 81.79 O ANISOU 2092 O ALA A1091 11378 9353 10348 -383 -281 -1520 O ATOM 2093 CB ALA A1091 33.971 45.890 6.225 1.00 81.40 C ANISOU 2093 CB ALA A1091 11730 9638 9562 19 45 -1428 C ATOM 2094 N GLU A1092 31.666 43.656 6.114 1.00 82.90 N ANISOU 2094 N GLU A1092 11863 9423 10210 -187 -497 -1967 N ATOM 2095 CA GLU A1092 30.253 43.263 6.069 1.00 84.22 C ANISOU 2095 CA GLU A1092 11902 9491 10606 -354 -799 -2163 C ATOM 2096 C GLU A1092 29.914 42.255 7.173 1.00 86.56 C ANISOU 2096 C GLU A1092 12016 9519 11353 -601 -742 -2117 C ATOM 2097 O GLU A1092 28.745 42.149 7.538 1.00 87.72 O ANISOU 2097 O GLU A1092 11930 9627 11771 -820 -880 -2171 O ATOM 2098 CB GLU A1092 29.880 42.694 4.694 1.00 89.72 C ANISOU 2098 CB GLU A1092 12826 10147 11116 -243 -1089 -2544 C ATOM 2099 CG GLU A1092 29.371 43.740 3.714 1.00105.61 C ANISOU 2099 CG GLU A1092 14966 12416 12745 -90 -1322 -2597 C ATOM 2100 CD GLU A1092 27.895 44.073 3.827 1.00134.00 C ANISOU 2100 CD GLU A1092 18293 16049 16573 -211 -1682 -2695 C ATOM 2101 OE1 GLU A1092 27.575 45.169 4.340 1.00127.12 O ANISOU 2101 OE1 GLU A1092 17246 15323 15731 -209 -1646 -2467 O ATOM 2102 OE2 GLU A1092 27.058 43.248 3.391 1.00132.44 O ANISOU 2102 OE2 GLU A1092 18038 15727 16557 -299 -2015 -3030 O ATOM 2103 N GLN A1093 30.931 41.560 7.737 1.00 80.84 N ANISOU 2103 N GLN A1093 11383 8614 10716 -567 -532 -1993 N ATOM 2104 CA GLN A1093 30.771 40.608 8.840 1.00 81.26 C ANISOU 2104 CA GLN A1093 11361 8375 11139 -783 -462 -1858 C ATOM 2105 C GLN A1093 30.254 41.280 10.125 1.00 83.07 C ANISOU 2105 C GLN A1093 11352 8743 11470 -980 -319 -1562 C ATOM 2106 O GLN A1093 29.674 40.599 10.971 1.00 82.92 O ANISOU 2106 O GLN A1093 11242 8534 11731 -1239 -268 -1455 O ATOM 2107 CB GLN A1093 32.086 39.873 9.127 1.00 82.85 C ANISOU 2107 CB GLN A1093 11739 8377 11365 -612 -318 -1766 C ATOM 2108 CG GLN A1093 32.313 38.647 8.240 1.00 94.35 C ANISOU 2108 CG GLN A1093 13417 9517 12913 -491 -456 -2094 C ATOM 2109 CD GLN A1093 31.297 37.563 8.496 1.00104.39 C ANISOU 2109 CD GLN A1093 14692 10393 14578 -786 -639 -2198 C ATOM 2110 OE1 GLN A1093 31.283 36.923 9.557 1.00101.64 O ANISOU 2110 OE1 GLN A1093 14344 9760 14515 -967 -565 -1948 O ATOM 2111 NE2 GLN A1093 30.405 37.366 7.539 1.00 89.36 N ANISOU 2111 NE2 GLN A1093 12796 8462 12694 -860 -895 -2553 N ATOM 2112 N LEU A1094 30.419 42.624 10.246 1.00 78.34 N ANISOU 2112 N LEU A1094 10669 8462 10635 -867 -245 -1440 N ATOM 2113 CA LEU A1094 29.908 43.419 11.366 1.00 76.63 C ANISOU 2113 CA LEU A1094 10243 8415 10457 -989 -122 -1241 C ATOM 2114 C LEU A1094 28.375 43.477 11.319 1.00 82.57 C ANISOU 2114 C LEU A1094 10728 9228 11419 -1181 -237 -1393 C ATOM 2115 O LEU A1094 27.747 43.838 12.316 1.00 82.67 O ANISOU 2115 O LEU A1094 10523 9356 11531 -1319 -90 -1276 O ATOM 2116 CB LEU A1094 30.488 44.837 11.345 1.00 74.20 C ANISOU 2116 CB LEU A1094 9947 8361 9885 -799 -73 -1138 C ATOM 2117 CG LEU A1094 31.998 44.994 11.549 1.00 77.28 C ANISOU 2117 CG LEU A1094 10480 8750 10132 -647 61 -977 C ATOM 2118 CD1 LEU A1094 32.456 46.342 11.053 1.00 75.23 C ANISOU 2118 CD1 LEU A1094 10245 8687 9652 -506 64 -940 C ATOM 2119 CD2 LEU A1094 32.394 44.815 13.016 1.00 79.04 C ANISOU 2119 CD2 LEU A1094 10670 8934 10427 -726 195 -747 C ATOM 2120 N LYS A1095 27.781 43.091 10.157 1.00 80.94 N ANISOU 2120 N LYS A1095 10521 8954 11278 -1177 -507 -1686 N ATOM 2121 CA LYS A1095 26.341 43.040 9.902 1.00 82.92 C ANISOU 2121 CA LYS A1095 10465 9250 11790 -1346 -708 -1904 C ATOM 2122 C LYS A1095 25.733 41.623 10.163 1.00 90.87 C ANISOU 2122 C LYS A1095 11365 9950 13211 -1689 -715 -1986 C ATOM 2123 O LYS A1095 24.532 41.439 9.928 1.00 94.54 O ANISOU 2123 O LYS A1095 11508 10428 13983 -1888 -885 -2192 O ATOM 2124 CB LYS A1095 26.021 43.515 8.474 1.00 85.58 C ANISOU 2124 CB LYS A1095 10880 9699 11939 -1131 -1083 -2189 C ATOM 2125 CG LYS A1095 26.057 45.024 8.307 1.00 88.67 C ANISOU 2125 CG LYS A1095 11275 10366 12051 -881 -1125 -2096 C ATOM 2126 CD LYS A1095 25.413 45.448 7.003 1.00 99.02 C ANISOU 2126 CD LYS A1095 12651 11773 13200 -694 -1552 -2349 C ATOM 2127 N THR A1096 26.529 40.644 10.686 1.00 86.20 N ANISOU 2127 N THR A1096 11018 9059 12674 -1769 -546 -1816 N ATOM 2128 CA THR A1096 25.987 39.320 11.050 1.00 89.45 C ANISOU 2128 CA THR A1096 11386 9098 13505 -2127 -530 -1818 C ATOM 2129 C THR A1096 25.128 39.492 12.307 1.00 94.02 C ANISOU 2129 C THR A1096 11640 9792 14290 -2448 -229 -1567 C ATOM 2130 O THR A1096 25.417 40.378 13.111 1.00 91.02 O ANISOU 2130 O THR A1096 11231 9689 13661 -2330 8 -1337 O ATOM 2131 CB THR A1096 27.085 38.248 11.256 1.00 96.78 C ANISOU 2131 CB THR A1096 12708 9627 14439 -2070 -469 -1687 C ATOM 2132 OG1 THR A1096 27.938 38.604 12.346 1.00 94.46 O ANISOU 2132 OG1 THR A1096 12534 9427 13929 -1959 -190 -1307 O ATOM 2133 CG2 THR A1096 27.895 37.957 9.993 1.00 93.65 C ANISOU 2133 CG2 THR A1096 12601 9121 13859 -1749 -712 -1998 C ATOM 2134 N THR A1097 24.087 38.664 12.484 1.00 95.57 N ANISOU 2134 N THR A1097 11590 9786 14938 -2862 -222 -1626 N ATOM 2135 CA THR A1097 23.165 38.756 13.629 1.00 97.91 C ANISOU 2135 CA THR A1097 11528 10222 15453 -3218 135 -1405 C ATOM 2136 C THR A1097 23.909 38.798 14.975 1.00101.19 C ANISOU 2136 C THR A1097 12203 10659 15584 -3210 541 -937 C ATOM 2137 O THR A1097 23.514 39.584 15.837 1.00101.10 O ANISOU 2137 O THR A1097 11973 11006 15433 -3226 832 -802 O ATOM 2138 CB THR A1097 22.136 37.635 13.615 1.00108.85 C ANISOU 2138 CB THR A1097 12669 11279 17408 -3730 120 -1484 C ATOM 2139 OG1 THR A1097 22.820 36.387 13.648 1.00112.97 O ANISOU 2139 OG1 THR A1097 13637 11254 18033 -3833 62 -1356 O ATOM 2140 CG2 THR A1097 21.209 37.705 12.408 1.00108.30 C ANISOU 2140 CG2 THR A1097 12222 11274 17653 -3770 -307 -1981 C ATOM 2141 N ARG A1098 25.003 38.009 15.132 1.00 96.89 N ANISOU 2141 N ARG A1098 12131 9749 14935 -3132 522 -727 N ATOM 2142 CA ARG A1098 25.820 37.986 16.349 1.00 95.46 C ANISOU 2142 CA ARG A1098 12254 9558 14458 -3073 798 -291 C ATOM 2143 C ARG A1098 26.533 39.326 16.546 1.00 94.01 C ANISOU 2143 C ARG A1098 12098 9801 13822 -2671 818 -284 C ATOM 2144 O ARG A1098 26.396 39.917 17.613 1.00 93.83 O ANISOU 2144 O ARG A1098 12031 10044 13575 -2698 1093 -68 O ATOM 2145 CB ARG A1098 26.840 36.832 16.327 1.00 97.29 C ANISOU 2145 CB ARG A1098 12957 9272 14738 -3007 668 -125 C ATOM 2146 CG ARG A1098 27.431 36.520 17.705 1.00109.02 C ANISOU 2146 CG ARG A1098 14767 10666 15991 -3027 907 373 C ATOM 2147 CD ARG A1098 28.908 36.172 17.645 1.00119.81 C ANISOU 2147 CD ARG A1098 16544 11768 17210 -2646 688 458 C ATOM 2148 NE ARG A1098 29.481 36.026 18.988 1.00132.13 N ANISOU 2148 NE ARG A1098 18412 13304 18489 -2602 835 920 N ATOM 2149 CZ ARG A1098 30.764 35.779 19.244 1.00144.65 C ANISOU 2149 CZ ARG A1098 20320 14715 19927 -2254 648 1058 C ATOM 2150 NH1 ARG A1098 31.634 35.641 18.250 1.00131.46 N ANISOU 2150 NH1 ARG A1098 18679 12892 18379 -1924 375 764 N ATOM 2151 NH2 ARG A1098 31.187 35.669 20.496 1.00129.27 N ANISOU 2151 NH2 ARG A1098 18659 12766 17694 -2215 729 1477 N ATOM 2152 N ASN A1099 27.264 39.814 15.513 1.00 86.83 N ANISOU 2152 N ASN A1099 11268 8951 12773 -2320 543 -530 N ATOM 2153 CA ASN A1099 28.024 41.072 15.542 1.00 81.91 C ANISOU 2153 CA ASN A1099 10678 8660 11786 -1975 531 -532 C ATOM 2154 C ASN A1099 27.122 42.306 15.664 1.00 85.76 C ANISOU 2154 C ASN A1099 10825 9544 12217 -1969 603 -655 C ATOM 2155 O ASN A1099 27.550 43.306 16.246 1.00 83.19 O ANISOU 2155 O ASN A1099 10524 9461 11622 -1790 695 -566 O ATOM 2156 CB ASN A1099 28.932 41.190 14.320 1.00 77.93 C ANISOU 2156 CB ASN A1099 10330 8101 11178 -1668 279 -743 C ATOM 2157 CG ASN A1099 30.228 40.422 14.468 1.00 93.97 C ANISOU 2157 CG ASN A1099 12677 9873 13155 -1504 257 -601 C ATOM 2158 OD1 ASN A1099 30.716 40.178 15.574 1.00 87.51 O ANISOU 2158 OD1 ASN A1099 11996 8978 12276 -1528 381 -304 O ATOM 2159 ND2 ASN A1099 30.830 40.030 13.357 1.00 84.18 N ANISOU 2159 ND2 ASN A1099 11563 8508 11915 -1298 90 -824 N ATOM 2160 N ALA A1100 25.878 42.233 15.142 1.00 84.86 N ANISOU 2160 N ALA A1100 10379 9476 12389 -2149 531 -886 N ATOM 2161 CA ALA A1100 24.891 43.307 15.263 1.00 84.56 C ANISOU 2161 CA ALA A1100 9955 9790 12384 -2119 576 -1039 C ATOM 2162 C ALA A1100 24.362 43.348 16.697 1.00 90.09 C ANISOU 2162 C ALA A1100 10499 10656 13076 -2330 995 -827 C ATOM 2163 O ALA A1100 24.197 44.438 17.252 1.00 88.80 O ANISOU 2163 O ALA A1100 10202 10804 12735 -2165 1122 -859 O ATOM 2164 CB ALA A1100 23.752 43.095 14.280 1.00 88.21 C ANISOU 2164 CB ALA A1100 10072 10241 13201 -2239 325 -1366 C ATOM 2165 N TYR A1101 24.135 42.149 17.307 1.00 89.33 N ANISOU 2165 N TYR A1101 10467 10328 13145 -2687 1218 -603 N ATOM 2166 CA TYR A1101 23.666 41.984 18.692 1.00 91.92 C ANISOU 2166 CA TYR A1101 10732 10792 13403 -2941 1680 -331 C ATOM 2167 C TYR A1101 24.707 42.534 19.670 1.00 91.99 C ANISOU 2167 C TYR A1101 11118 10932 12903 -2693 1808 -86 C ATOM 2168 O TYR A1101 24.333 43.195 20.638 1.00 91.74 O ANISOU 2168 O TYR A1101 10981 11224 12654 -2680 2110 -39 O ATOM 2169 CB TYR A1101 23.343 40.510 19.011 1.00 97.46 C ANISOU 2169 CB TYR A1101 11524 11121 14384 -3395 1851 -82 C ATOM 2170 N ILE A1102 26.010 42.290 19.391 1.00 85.86 N ANISOU 2170 N ILE A1102 10752 9919 11950 -2476 1559 23 N ATOM 2171 CA ILE A1102 27.135 42.795 20.185 1.00 83.71 C ANISOU 2171 CA ILE A1102 10814 9739 11251 -2220 1562 211 C ATOM 2172 C ILE A1102 27.098 44.342 20.149 1.00 86.56 C ANISOU 2172 C ILE A1102 10994 10467 11427 -1945 1517 -27 C ATOM 2173 O ILE A1102 27.085 44.962 21.210 1.00 87.45 O ANISOU 2173 O ILE A1102 11160 10821 11246 -1886 1714 44 O ATOM 2174 CB ILE A1102 28.501 42.204 19.705 1.00 84.30 C ANISOU 2174 CB ILE A1102 11236 9493 11300 -2028 1267 300 C ATOM 2175 CG1 ILE A1102 28.617 40.692 20.048 1.00 87.93 C ANISOU 2175 CG1 ILE A1102 11966 9537 11906 -2256 1312 588 C ATOM 2176 CG2 ILE A1102 29.686 42.990 20.288 1.00 82.08 C ANISOU 2176 CG2 ILE A1102 11166 9361 10658 -1721 1170 381 C ATOM 2177 CD1 ILE A1102 29.765 39.909 19.313 1.00 89.24 C ANISOU 2177 CD1 ILE A1102 12393 9320 12196 -2054 1001 573 C ATOM 2178 N GLN A1103 27.002 44.943 18.944 1.00 81.54 N ANISOU 2178 N GLN A1103 10175 9853 10955 -1783 1256 -313 N ATOM 2179 CA GLN A1103 26.927 46.394 18.747 1.00 80.15 C ANISOU 2179 CA GLN A1103 9859 9926 10671 -1523 1156 -529 C ATOM 2180 C GLN A1103 25.718 47.002 19.486 1.00 87.99 C ANISOU 2180 C GLN A1103 10527 11217 11689 -1576 1420 -653 C ATOM 2181 O GLN A1103 25.871 48.028 20.151 1.00 87.74 O ANISOU 2181 O GLN A1103 10526 11382 11429 -1381 1478 -718 O ATOM 2182 CB GLN A1103 26.869 46.742 17.246 1.00 79.99 C ANISOU 2182 CB GLN A1103 9739 9833 10820 -1384 832 -759 C ATOM 2183 CG GLN A1103 26.947 48.246 16.969 1.00 97.02 C ANISOU 2183 CG GLN A1103 11855 12147 12862 -1101 679 -914 C ATOM 2184 CD GLN A1103 26.780 48.652 15.526 1.00117.52 C ANISOU 2184 CD GLN A1103 14402 14690 15562 -963 368 -1094 C ATOM 2185 OE1 GLN A1103 26.027 49.580 15.216 1.00111.22 O ANISOU 2185 OE1 GLN A1103 13416 14012 14832 -814 241 -1271 O ATOM 2186 NE2 GLN A1103 27.514 48.015 14.615 1.00110.86 N ANISOU 2186 NE2 GLN A1103 13757 13664 14698 -970 225 -1061 N ATOM 2187 N LYS A1104 24.540 46.361 19.383 1.00 88.72 N ANISOU 2187 N LYS A1104 10287 11337 12085 -1840 1580 -716 N ATOM 2188 CA LYS A1104 23.300 46.800 20.027 1.00 92.87 C ANISOU 2188 CA LYS A1104 10397 12175 12713 -1914 1890 -861 C ATOM 2189 C LYS A1104 23.422 46.725 21.562 1.00100.56 C ANISOU 2189 C LYS A1104 11557 13326 13325 -2002 2327 -632 C ATOM 2190 O LYS A1104 22.871 47.585 22.258 1.00101.85 O ANISOU 2190 O LYS A1104 11537 13810 13351 -1864 2556 -793 O ATOM 2191 CB LYS A1104 22.107 45.964 19.528 1.00 99.48 C ANISOU 2191 CB LYS A1104 10799 12972 14027 -2244 1956 -961 C ATOM 2192 CG LYS A1104 20.777 46.710 19.593 1.00119.96 C ANISOU 2192 CG LYS A1104 12792 15899 16887 -2184 2068 -1286 C ATOM 2193 CD LYS A1104 19.691 46.036 18.763 1.00134.05 C ANISOU 2193 CD LYS A1104 14085 17621 19228 -2458 1949 -1472 C ATOM 2194 CE LYS A1104 18.385 46.791 18.825 1.00148.28 C ANISOU 2194 CE LYS A1104 15219 19773 21349 -2346 2012 -1828 C ATOM 2195 NZ LYS A1104 17.329 46.139 18.007 1.00161.33 N ANISOU 2195 NZ LYS A1104 16327 21376 23594 -2627 1842 -2042 N ATOM 2196 N TYR A1105 24.170 45.719 22.079 1.00 98.38 N ANISOU 2196 N TYR A1105 11683 12832 12865 -2190 2416 -268 N ATOM 2197 CA TYR A1105 24.420 45.529 23.512 1.00101.24 C ANISOU 2197 CA TYR A1105 12351 13324 12793 -2267 2770 18 C ATOM 2198 C TYR A1105 25.383 46.602 24.024 1.00101.80 C ANISOU 2198 C TYR A1105 12729 13525 12427 -1892 2596 -45 C ATOM 2199 O TYR A1105 25.093 47.254 25.031 1.00104.09 O ANISOU 2199 O TYR A1105 13051 14121 12377 -1804 2865 -98 O ATOM 2200 CB TYR A1105 24.972 44.112 23.800 1.00104.49 C ANISOU 2200 CB TYR A1105 13143 13384 13173 -2539 2808 443 C ATOM 2201 CG TYR A1105 25.584 43.952 25.176 1.00109.27 C ANISOU 2201 CG TYR A1105 14225 14064 13229 -2527 3017 791 C ATOM 2202 CD1 TYR A1105 24.786 43.742 26.297 1.00117.31 C ANISOU 2202 CD1 TYR A1105 15235 15330 14007 -2772 3555 977 C ATOM 2203 CD2 TYR A1105 26.964 44.006 25.358 1.00107.35 C ANISOU 2203 CD2 TYR A1105 14435 13662 12691 -2265 2674 929 C ATOM 2204 CE1 TYR A1105 25.343 43.613 27.568 1.00121.49 C ANISOU 2204 CE1 TYR A1105 16278 15950 13934 -2736 3725 1307 C ATOM 2205 CE2 TYR A1105 27.532 43.883 26.625 1.00111.21 C ANISOU 2205 CE2 TYR A1105 15383 14230 12644 -2215 2779 1229 C ATOM 2206 CZ TYR A1105 26.718 43.677 27.727 1.00125.46 C ANISOU 2206 CZ TYR A1105 17255 16276 14136 -2444 3294 1429 C ATOM 2207 OH TYR A1105 27.275 43.552 28.977 1.00131.05 O ANISOU 2207 OH TYR A1105 18492 17074 14227 -2377 3375 1741 O ATOM 2208 N LEU A1106 26.530 46.768 23.329 1.00 93.19 N ANISOU 2208 N LEU A1106 11851 12204 11353 -1686 2161 -59 N ATOM 2209 CA LEU A1106 27.578 47.733 23.668 1.00 90.07 C ANISOU 2209 CA LEU A1106 11708 11867 10647 -1379 1930 -126 C ATOM 2210 C LEU A1106 27.046 49.164 23.632 1.00 93.44 C ANISOU 2210 C LEU A1106 11892 12535 11075 -1151 1920 -489 C ATOM 2211 O LEU A1106 27.497 49.983 24.428 1.00 93.46 O ANISOU 2211 O LEU A1106 12084 12670 10757 -960 1889 -572 O ATOM 2212 CB LEU A1106 28.813 47.589 22.752 1.00 85.73 C ANISOU 2212 CB LEU A1106 11322 11032 10220 -1254 1522 -80 C ATOM 2213 CG LEU A1106 29.607 46.267 22.839 1.00 90.13 C ANISOU 2213 CG LEU A1106 12169 11311 10768 -1363 1451 241 C ATOM 2214 CD1 LEU A1106 30.756 46.265 21.878 1.00 86.53 C ANISOU 2214 CD1 LEU A1106 11772 10643 10463 -1196 1105 200 C ATOM 2215 CD2 LEU A1106 30.133 46.007 24.231 1.00 95.35 C ANISOU 2215 CD2 LEU A1106 13188 12034 11006 -1346 1530 499 C ATOM 2216 N ARG A 224 26.067 49.454 22.752 1.00153.23 N ANISOU 2216 N ARG A 224 25202 13861 19157 4014 -1233 -7380 N ATOM 2217 CA ARG A 224 25.434 50.770 22.680 1.00150.27 C ANISOU 2217 CA ARG A 224 24737 13854 18505 3828 -1361 -7158 C ATOM 2218 C ARG A 224 24.612 51.034 23.948 1.00152.06 C ANISOU 2218 C ARG A 224 24605 13967 19205 3509 -1489 -6790 C ATOM 2219 O ARG A 224 24.603 52.161 24.450 1.00147.88 O ANISOU 2219 O ARG A 224 23874 13757 18556 3403 -1399 -6422 O ATOM 2220 CB ARG A 224 24.555 50.890 21.431 1.00153.69 C ANISOU 2220 CB ARG A 224 25481 14332 18582 3807 -1733 -7554 C ATOM 2221 CG ARG A 224 25.203 51.698 20.320 1.00164.26 C ANISOU 2221 CG ARG A 224 27115 16085 19209 4060 -1551 -7648 C ATOM 2222 CD ARG A 224 24.178 52.297 19.376 1.00175.90 C ANISOU 2222 CD ARG A 224 28820 17727 20287 3988 -1939 -7845 C ATOM 2223 NE ARG A 224 23.624 51.298 18.462 1.00186.10 N ANISOU 2223 NE ARG A 224 29633 19128 21950 3023 -1275 -7812 N ATOM 2224 CZ ARG A 224 24.111 51.031 17.253 1.00194.87 C ANISOU 2224 CZ ARG A 224 29800 20925 23318 1620 306 -7304 C ATOM 2225 NH1 ARG A 224 25.168 51.691 16.795 1.00187.04 N ANISOU 2225 NH1 ARG A 224 29038 20153 21875 2104 289 -7428 N ATOM 2226 NH2 ARG A 224 23.548 50.100 16.495 1.00184.90 N ANISOU 2226 NH2 ARG A 224 28745 19471 22037 1473 236 -7646 N ATOM 2227 N GLY A 225 23.976 49.979 24.465 1.00151.57 N ANISOU 2227 N GLY A 225 24472 13435 19682 3369 -1664 -6888 N ATOM 2228 CA GLY A 225 23.150 50.014 25.667 1.00149.42 C ANISOU 2228 CA GLY A 225 23889 12975 19907 3079 -1751 -6565 C ATOM 2229 C GLY A 225 23.918 50.237 26.955 1.00151.32 C ANISOU 2229 C GLY A 225 23885 13277 20332 3119 -1416 -6093 C ATOM 2230 O GLY A 225 23.479 51.021 27.801 1.00147.42 O ANISOU 2230 O GLY A 225 23150 12909 19953 2929 -1409 -5726 O ATOM 2231 N VAL A 226 25.072 49.549 27.108 1.00150.17 N ANISOU 2231 N VAL A 226 23805 13039 20213 3386 -1150 -6115 N ATOM 2232 CA VAL A 226 25.968 49.615 28.276 1.00147.95 C ANISOU 2232 CA VAL A 226 23322 12796 20098 3493 -858 -5719 C ATOM 2233 C VAL A 226 26.462 51.066 28.497 1.00149.43 C ANISOU 2233 C VAL A 226 23344 13508 19925 3501 -700 -5401 C ATOM 2234 O VAL A 226 26.477 51.541 29.635 1.00146.02 O ANISOU 2234 O VAL A 226 22682 13146 19654 3413 -624 -5011 O ATOM 2235 CB VAL A 226 27.154 48.612 28.134 1.00154.94 C ANISOU 2235 CB VAL A 226 24327 13488 21057 3817 -641 -5883 C ATOM 2236 CG1 VAL A 226 28.117 48.690 29.318 1.00152.39 C ANISOU 2236 CG1 VAL A 226 23790 13231 20881 3964 -380 -5491 C ATOM 2237 CG2 VAL A 226 26.648 47.186 27.971 1.00159.05 C ANISOU 2237 CG2 VAL A 226 25001 13446 21984 3795 -793 -6174 C ATOM 2238 N GLY A 227 26.823 51.749 27.411 1.00147.55 N ANISOU 2238 N GLY A 227 23244 13610 19209 3606 -655 -5574 N ATOM 2239 CA GLY A 227 27.313 53.122 27.453 1.00144.50 C ANISOU 2239 CA GLY A 227 22724 13696 18483 3615 -490 -5310 C ATOM 2240 C GLY A 227 26.251 54.205 27.480 1.00146.72 C ANISOU 2240 C GLY A 227 22930 14184 18633 3348 -697 -5160 C ATOM 2241 O GLY A 227 26.592 55.384 27.614 1.00142.97 O ANISOU 2241 O GLY A 227 22335 14073 17914 3333 -570 -4919 O ATOM 2242 N LYS A 228 24.960 53.822 27.359 1.00145.75 N ANISOU 2242 N LYS A 228 22857 13814 18708 3137 -1019 -5307 N ATOM 2243 CA LYS A 228 23.824 54.756 27.349 1.00144.20 C ANISOU 2243 CA LYS A 228 22577 13767 18446 2885 -1258 -5203 C ATOM 2244 C LYS A 228 23.441 55.251 28.767 1.00145.54 C ANISOU 2244 C LYS A 228 22435 13936 18927 2691 -1213 -4770 C ATOM 2245 O LYS A 228 22.587 56.136 28.886 1.00143.60 O ANISOU 2245 O LYS A 228 22080 13837 18643 2494 -1366 -4636 O ATOM 2246 CB LYS A 228 22.603 54.113 26.666 1.00150.11 C ANISOU 2246 CB LYS A 228 23465 14230 19341 2745 -1636 -5560 C ATOM 2247 N VAL A 229 24.091 54.704 29.825 1.00141.57 N ANISOU 2247 N VAL A 229 21807 13276 18707 2770 -1006 -4555 N ATOM 2248 CA VAL A 229 23.856 55.050 31.239 1.00166.93 C ANISOU 2248 CA VAL A 229 24776 16467 22184 2642 -933 -4148 C ATOM 2249 C VAL A 229 24.274 56.503 31.527 1.00193.14 C ANISOU 2249 C VAL A 229 27951 20232 25202 2638 -818 -3870 C ATOM 2250 O VAL A 229 23.616 57.198 32.301 1.00153.83 O ANISOU 2250 O VAL A 229 22804 15319 20327 2467 -854 -3597 O ATOM 2251 CB VAL A 229 24.544 54.062 32.227 1.00171.40 C ANISOU 2251 CB VAL A 229 25303 16751 23070 2786 -756 -4005 C ATOM 2252 CG1 VAL A 229 23.893 52.682 32.181 1.00174.73 C ANISOU 2252 CG1 VAL A 229 25830 16666 23892 2726 -871 -4206 C ATOM 2253 CG2 VAL A 229 26.052 53.964 31.989 1.00171.74 C ANISOU 2253 CG2 VAL A 229 25391 16953 22911 3090 -534 -4054 C ATOM 2254 N ARG A 231 21.671 58.947 34.353 1.00165.25 N ANISOU 2254 N ARG A 231 23846 16879 22064 2009 -960 -2957 N ATOM 2255 CA ARG A 231 20.626 59.925 34.654 1.00162.87 C ANISOU 2255 CA ARG A 231 23400 16707 21777 1801 -1059 -2791 C ATOM 2256 C ARG A 231 21.223 61.212 35.235 1.00162.56 C ANISOU 2256 C ARG A 231 23251 17023 21492 1851 -923 -2518 C ATOM 2257 O ARG A 231 22.081 61.152 36.120 1.00161.14 O ANISOU 2257 O ARG A 231 23033 16867 21327 1988 -751 -2338 O ATOM 2258 CB ARG A 231 19.590 59.333 35.621 1.00163.96 C ANISOU 2258 CB ARG A 231 23428 16512 22359 1631 -1068 -2642 C ATOM 2259 N LYS A 232 20.760 62.371 34.730 1.00156.93 N ANISOU 2259 N LYS A 232 22489 16571 20568 1748 -1021 -2497 N ATOM 2260 CA LYS A 232 21.215 63.701 35.148 1.00153.33 C ANISOU 2260 CA LYS A 232 21927 16439 19895 1767 -917 -2266 C ATOM 2261 C LYS A 232 20.037 64.605 35.543 1.00154.50 C ANISOU 2261 C LYS A 232 21940 16648 20114 1570 -1023 -2108 C ATOM 2262 O LYS A 232 18.887 64.288 35.224 1.00155.43 O ANISOU 2262 O LYS A 232 22043 16598 20416 1424 -1196 -2214 O ATOM 2263 CB LYS A 232 22.030 64.357 34.021 1.00156.06 C ANISOU 2263 CB LYS A 232 22368 17068 19858 1880 -877 -2394 C ATOM 2264 N LYS A 233 20.332 65.730 36.237 1.00147.47 N ANISOU 2264 N LYS A 233 20939 15988 19107 1572 -924 -1869 N ATOM 2265 CA LYS A 233 19.342 66.718 36.681 1.00145.12 C ANISOU 2265 CA LYS A 233 20510 15771 18858 1416 -989 -1701 C ATOM 2266 C LYS A 233 18.690 67.420 35.487 1.00148.13 C ANISOU 2266 C LYS A 233 20926 16296 19060 1333 -1179 -1840 C ATOM 2267 O LYS A 233 19.363 67.659 34.478 1.00148.36 O ANISOU 2267 O LYS A 233 21082 16493 18795 1430 -1182 -1970 O ATOM 2268 CB LYS A 233 19.993 67.753 37.607 1.00144.98 C ANISOU 2268 CB LYS A 233 20397 15964 18726 1470 -845 -1456 C ATOM 2269 N VAL A 234 17.380 67.739 35.600 1.00143.43 N ANISOU 2269 N VAL A 234 20221 15630 18645 1170 -1327 -1804 N ATOM 2270 CA VAL A 234 16.598 68.401 34.540 1.00143.28 C ANISOU 2270 CA VAL A 234 20224 15725 18493 1100 -1560 -1925 C ATOM 2271 C VAL A 234 17.024 69.877 34.437 1.00142.16 C ANISOU 2271 C VAL A 234 20072 15893 18049 1138 -1494 -1762 C ATOM 2272 O VAL A 234 17.016 70.594 35.439 1.00139.13 O ANISOU 2272 O VAL A 234 19551 15572 17739 1102 -1371 -1530 O ATOM 2273 CB VAL A 234 15.057 68.256 34.728 1.00148.43 C ANISOU 2273 CB VAL A 234 20713 16184 19499 920 -1749 -1944 C ATOM 2274 CG1 VAL A 234 14.300 68.783 33.508 1.00149.75 C ANISOU 2274 CG1 VAL A 234 20923 16450 19525 884 -2055 -2123 C ATOM 2275 CG2 VAL A 234 14.661 66.806 35.006 1.00150.62 C ANISOU 2275 CG2 VAL A 234 20966 16109 20155 860 -1759 -2065 C ATOM 2276 N ASN A 235 17.398 70.310 33.215 1.00137.92 N ANISOU 2276 N ASN A 235 19702 15533 17170 1218 -1565 -1886 N ATOM 2277 CA ASN A 235 17.852 71.665 32.897 1.00135.56 C ANISOU 2277 CA ASN A 235 19430 15503 16573 1261 -1489 -1747 C ATOM 2278 C ASN A 235 16.737 72.689 33.164 1.00136.25 C ANISOU 2278 C ASN A 235 19384 15640 16747 1142 -1629 -1607 C ATOM 2279 O ASN A 235 16.849 73.483 34.104 1.00133.00 O ANISOU 2279 O ASN A 235 18834 15303 16399 1108 -1494 -1388 O ATOM 2280 CB ASN A 235 18.331 71.737 31.431 1.00139.07 C ANISOU 2280 CB ASN A 235 20128 16079 16634 1383 -1528 -1920 C ATOM 2281 CG ASN A 235 19.099 72.988 31.055 1.00168.77 C ANISOU 2281 CG ASN A 235 23947 20090 20087 1450 -1358 -1766 C ATOM 2282 OD1 ASN A 235 18.545 74.089 30.939 1.00166.32 O ANISOU 2282 OD1 ASN A 235 23614 19887 19693 1399 -1441 -1638 O ATOM 2283 ND2 ASN A 235 20.385 72.834 30.779 1.00161.13 N ANISOU 2283 ND2 ASN A 235 23059 19204 18959 1572 -1110 -1782 N ATOM 2284 N VAL A 236 15.640 72.617 32.376 1.00133.32 N ANISOU 2284 N VAL A 236 19045 15212 16401 1090 -1918 -1753 N ATOM 2285 CA VAL A 236 14.474 73.512 32.419 1.00131.96 C ANISOU 2285 CA VAL A 236 18742 15073 16324 998 -2102 -1662 C ATOM 2286 C VAL A 236 13.835 73.628 33.825 1.00131.12 C ANISOU 2286 C VAL A 236 18366 14848 16608 873 -2008 -1478 C ATOM 2287 O VAL A 236 13.135 74.618 34.086 1.00130.77 O ANISOU 2287 O VAL A 236 18193 14865 16628 819 -2068 -1345 O ATOM 2288 CB VAL A 236 13.413 73.067 31.388 1.00139.04 C ANISOU 2288 CB VAL A 236 19699 15882 17247 977 -2474 -1907 C ATOM 2289 N LYS A 237 14.084 72.643 34.719 1.00123.06 N ANISOU 2289 N LYS A 237 17277 13651 15828 848 -1847 -1461 N ATOM 2290 CA LYS A 237 13.503 72.632 36.052 1.00119.72 C ANISOU 2290 CA LYS A 237 16648 13099 15742 756 -1719 -1281 C ATOM 2291 C LYS A 237 14.403 73.305 37.095 1.00115.90 C ANISOU 2291 C LYS A 237 16152 12742 15142 822 -1453 -1053 C ATOM 2292 O LYS A 237 13.966 74.286 37.685 1.00114.29 O ANISOU 2292 O LYS A 237 15835 12613 14977 785 -1412 -889 O ATOM 2293 CB LYS A 237 13.137 71.202 36.480 1.00124.18 C ANISOU 2293 CB LYS A 237 17164 13367 16654 694 -1694 -1368 C ATOM 2294 CG LYS A 237 11.644 70.883 36.363 1.00139.86 C ANISOU 2294 CG LYS A 237 18966 15152 19025 542 -1891 -1459 C ATOM 2295 CD LYS A 237 11.219 70.439 34.967 1.00152.75 C ANISOU 2295 CD LYS A 237 20680 16756 20603 534 -2233 -1763 C ATOM 2296 CE LYS A 237 9.741 70.146 34.900 1.00166.43 C ANISOU 2296 CE LYS A 237 22179 18274 22784 377 -2457 -1871 C ATOM 2297 N VAL A 238 15.640 72.809 37.314 1.00107.98 N ANISOU 2297 N VAL A 238 15258 11761 14007 930 -1296 -1060 N ATOM 2298 CA VAL A 238 16.583 73.325 38.329 1.00103.92 C ANISOU 2298 CA VAL A 238 14727 11352 13407 1010 -1086 -884 C ATOM 2299 C VAL A 238 16.832 74.847 38.170 1.00101.96 C ANISOU 2299 C VAL A 238 14453 11338 12949 1018 -1076 -780 C ATOM 2300 O VAL A 238 16.735 75.581 39.155 1.00 99.54 O ANISOU 2300 O VAL A 238 14055 11072 12694 1009 -989 -616 O ATOM 2301 CB VAL A 238 17.923 72.529 38.346 1.00108.06 C ANISOU 2301 CB VAL A 238 15359 11868 13831 1143 -971 -955 C ATOM 2302 CG1 VAL A 238 18.908 73.100 39.362 1.00105.78 C ANISOU 2302 CG1 VAL A 238 15031 11700 13459 1238 -812 -805 C ATOM 2303 CG2 VAL A 238 17.678 71.049 38.635 1.00109.81 C ANISOU 2303 CG2 VAL A 238 15610 11824 14290 1143 -957 -1023 C ATOM 2304 N PHE A 239 17.093 75.307 36.933 1.00 96.31 N ANISOU 2304 N PHE A 239 13834 10757 12000 1039 -1161 -873 N ATOM 2305 CA PHE A 239 17.389 76.698 36.577 1.00 93.59 C ANISOU 2305 CA PHE A 239 13496 10608 11455 1050 -1136 -776 C ATOM 2306 C PHE A 239 16.226 77.698 36.844 1.00 95.22 C ANISOU 2306 C PHE A 239 13594 10827 11760 963 -1240 -659 C ATOM 2307 O PHE A 239 16.397 78.894 36.595 1.00 94.35 O ANISOU 2307 O PHE A 239 13495 10850 11503 970 -1228 -570 O ATOM 2308 CB PHE A 239 17.819 76.768 35.103 1.00 96.51 C ANISOU 2308 CB PHE A 239 14045 11085 11541 1112 -1183 -898 C ATOM 2309 CG PHE A 239 19.260 76.363 34.893 1.00 98.05 C ANISOU 2309 CG PHE A 239 14316 11339 11598 1218 -994 -952 C ATOM 2310 CD1 PHE A 239 20.263 77.321 34.802 1.00100.17 C ANISOU 2310 CD1 PHE A 239 14572 11760 11729 1259 -820 -851 C ATOM 2311 CD2 PHE A 239 19.619 75.022 34.805 1.00101.15 C ANISOU 2311 CD2 PHE A 239 14774 11618 12039 1277 -980 -1108 C ATOM 2312 CE1 PHE A 239 21.599 76.946 34.622 1.00101.55 C ANISOU 2312 CE1 PHE A 239 14771 11982 11831 1358 -631 -907 C ATOM 2313 CE2 PHE A 239 20.955 74.648 34.631 1.00104.25 C ANISOU 2313 CE2 PHE A 239 15213 12062 12333 1392 -797 -1162 C ATOM 2314 CZ PHE A 239 21.936 75.612 34.544 1.00101.59 C ANISOU 2314 CZ PHE A 239 14836 11888 11876 1432 -621 -1062 C ATOM 2315 N ILE A 240 15.082 77.237 37.396 1.00 90.67 N ANISOU 2315 N ILE A 240 12899 10097 11454 885 -1314 -649 N ATOM 2316 CA ILE A 240 13.949 78.113 37.705 1.00 89.52 C ANISOU 2316 CA ILE A 240 12619 9947 11447 814 -1394 -547 C ATOM 2317 C ILE A 240 14.327 79.058 38.869 1.00 90.47 C ANISOU 2317 C ILE A 240 12666 10133 11574 834 -1213 -364 C ATOM 2318 O ILE A 240 13.906 80.216 38.860 1.00 89.82 O ANISOU 2318 O ILE A 240 12527 10120 11482 816 -1249 -273 O ATOM 2319 CB ILE A 240 12.636 77.308 37.964 1.00 93.99 C ANISOU 2319 CB ILE A 240 13047 10311 12353 720 -1500 -602 C ATOM 2320 CG1 ILE A 240 11.366 77.994 37.406 1.00 95.61 C ANISOU 2320 CG1 ILE A 240 13144 10522 12662 663 -1727 -622 C ATOM 2321 CG2 ILE A 240 12.482 76.737 39.382 1.00 94.57 C ANISOU 2321 CG2 ILE A 240 13017 10234 12680 695 -1295 -488 C ATOM 2322 CD1 ILE A 240 10.777 79.235 38.161 1.00101.40 C ANISOU 2322 CD1 ILE A 240 13730 11303 13493 647 -1665 -441 C ATOM 2323 N ILE A 241 15.167 78.581 39.820 1.00 85.09 N ANISOU 2323 N ILE A 241 12004 9430 10897 889 -1042 -323 N ATOM 2324 CA ILE A 241 15.614 79.355 40.983 1.00 82.70 C ANISOU 2324 CA ILE A 241 11660 9182 10582 933 -902 -188 C ATOM 2325 C ILE A 241 16.453 80.559 40.517 1.00 84.27 C ANISOU 2325 C ILE A 241 11886 9550 10582 958 -895 -165 C ATOM 2326 O ILE A 241 16.071 81.700 40.814 1.00 83.09 O ANISOU 2326 O ILE A 241 11679 9445 10448 935 -898 -74 O ATOM 2327 CB ILE A 241 16.366 78.493 42.041 1.00 85.16 C ANISOU 2327 CB ILE A 241 12010 9425 10920 1017 -768 -167 C ATOM 2328 CG1 ILE A 241 15.527 77.279 42.482 1.00 86.45 C ANISOU 2328 CG1 ILE A 241 12162 9383 11301 986 -737 -165 C ATOM 2329 CG2 ILE A 241 16.759 79.347 43.253 1.00 84.49 C ANISOU 2329 CG2 ILE A 241 11903 9400 10797 1081 -671 -52 C ATOM 2330 CD1 ILE A 241 16.349 76.090 42.956 1.00 93.27 C ANISOU 2330 CD1 ILE A 241 13119 10156 12164 1083 -646 -181 C ATOM 2331 N ILE A 242 17.548 80.310 39.749 1.00 79.64 N ANISOU 2331 N ILE A 242 11384 9042 9835 1005 -868 -245 N ATOM 2332 CA ILE A 242 18.437 81.364 39.239 1.00 78.38 C ANISOU 2332 CA ILE A 242 11243 9018 9520 1021 -811 -217 C ATOM 2333 C ILE A 242 17.632 82.376 38.396 1.00 83.89 C ANISOU 2333 C ILE A 242 11966 9759 10149 969 -907 -162 C ATOM 2334 O ILE A 242 17.887 83.574 38.516 1.00 83.31 O ANISOU 2334 O ILE A 242 11861 9745 10049 958 -857 -69 O ATOM 2335 CB ILE A 242 19.696 80.825 38.494 1.00 81.56 C ANISOU 2335 CB ILE A 242 11721 9479 9789 1085 -726 -314 C ATOM 2336 CG1 ILE A 242 20.708 81.959 38.236 1.00 81.49 C ANISOU 2336 CG1 ILE A 242 11684 9583 9694 1093 -605 -260 C ATOM 2337 CG2 ILE A 242 19.352 80.057 37.214 1.00 83.47 C ANISOU 2337 CG2 ILE A 242 12099 9702 9916 1092 -810 -431 C ATOM 2338 CD1 ILE A 242 22.145 81.593 38.053 1.00 86.01 C ANISOU 2338 CD1 ILE A 242 12234 10204 10243 1163 -462 -328 C ATOM 2339 N ALA A 243 16.631 81.904 37.610 1.00 82.00 N ANISOU 2339 N ALA A 243 11777 9473 9907 943 -1065 -224 N ATOM 2340 CA ALA A 243 15.765 82.760 36.791 1.00 82.25 C ANISOU 2340 CA ALA A 243 11841 9536 9873 922 -1209 -182 C ATOM 2341 C ALA A 243 14.954 83.709 37.684 1.00 85.21 C ANISOU 2341 C ALA A 243 12074 9876 10424 882 -1220 -58 C ATOM 2342 O ALA A 243 15.008 84.917 37.463 1.00 84.59 O ANISOU 2342 O ALA A 243 12011 9856 10276 889 -1208 41 O ATOM 2343 CB ALA A 243 14.843 81.915 35.925 1.00 84.56 C ANISOU 2343 CB ALA A 243 12188 9769 10171 914 -1422 -312 C ATOM 2344 N VAL A 244 14.283 83.172 38.739 1.00 81.30 N ANISOU 2344 N VAL A 244 11453 9277 10160 851 -1206 -54 N ATOM 2345 CA VAL A 244 13.488 83.943 39.713 1.00 80.35 C ANISOU 2345 CA VAL A 244 11199 9110 10218 831 -1173 52 C ATOM 2346 C VAL A 244 14.403 84.953 40.444 1.00 82.98 C ANISOU 2346 C VAL A 244 11541 9510 10476 866 -1028 135 C ATOM 2347 O VAL A 244 14.056 86.133 40.526 1.00 81.94 O ANISOU 2347 O VAL A 244 11372 9394 10369 864 -1038 217 O ATOM 2348 CB VAL A 244 12.722 83.013 40.703 1.00 84.23 C ANISOU 2348 CB VAL A 244 11584 9465 10954 804 -1119 47 C ATOM 2349 CG1 VAL A 244 12.322 83.738 41.990 1.00 83.21 C ANISOU 2349 CG1 VAL A 244 11366 9304 10947 824 -984 163 C ATOM 2350 CG2 VAL A 244 11.497 82.394 40.037 1.00 85.61 C ANISOU 2350 CG2 VAL A 244 11673 9543 11310 744 -1292 -27 C ATOM 2351 N PHE A 245 15.579 84.497 40.931 1.00 78.75 N ANISOU 2351 N PHE A 245 11047 9005 9868 903 -914 100 N ATOM 2352 CA PHE A 245 16.529 85.360 41.631 1.00 77.09 C ANISOU 2352 CA PHE A 245 10823 8846 9620 935 -814 138 C ATOM 2353 C PHE A 245 16.942 86.534 40.763 1.00 82.07 C ANISOU 2353 C PHE A 245 11482 9546 10158 911 -817 181 C ATOM 2354 O PHE A 245 16.901 87.664 41.235 1.00 81.91 O ANISOU 2354 O PHE A 245 11416 9517 10188 905 -791 243 O ATOM 2355 CB PHE A 245 17.773 84.573 42.080 1.00 78.05 C ANISOU 2355 CB PHE A 245 10969 8991 9697 993 -737 69 C ATOM 2356 CG PHE A 245 18.637 85.288 43.095 1.00 78.27 C ANISOU 2356 CG PHE A 245 10954 9047 9739 1039 -681 76 C ATOM 2357 CD1 PHE A 245 18.412 85.131 44.461 1.00 80.85 C ANISOU 2357 CD1 PHE A 245 11278 9325 10117 1104 -662 94 C ATOM 2358 CD2 PHE A 245 19.691 86.100 42.688 1.00 79.42 C ANISOU 2358 CD2 PHE A 245 11065 9257 9852 1025 -645 57 C ATOM 2359 CE1 PHE A 245 19.216 85.788 45.401 1.00 81.14 C ANISOU 2359 CE1 PHE A 245 11295 9388 10148 1167 -657 67 C ATOM 2360 CE2 PHE A 245 20.491 86.760 43.628 1.00 81.91 C ANISOU 2360 CE2 PHE A 245 11316 9583 10224 1061 -633 29 C ATOM 2361 CZ PHE A 245 20.248 86.599 44.977 1.00 79.76 C ANISOU 2361 CZ PHE A 245 11056 9272 9977 1138 -663 21 C ATOM 2362 N PHE A 246 17.308 86.274 39.496 1.00 80.43 N ANISOU 2362 N PHE A 246 11365 9389 9809 906 -834 151 N ATOM 2363 CA PHE A 246 17.774 87.300 38.567 1.00 81.42 C ANISOU 2363 CA PHE A 246 11553 9566 9816 895 -790 217 C ATOM 2364 C PHE A 246 16.687 88.265 38.145 1.00 85.59 C ANISOU 2364 C PHE A 246 12103 10068 10349 883 -896 316 C ATOM 2365 O PHE A 246 16.964 89.457 38.097 1.00 86.01 O ANISOU 2365 O PHE A 246 12159 10116 10404 871 -832 410 O ATOM 2366 CB PHE A 246 18.422 86.672 37.334 1.00 84.97 C ANISOU 2366 CB PHE A 246 12134 10076 10075 924 -749 161 C ATOM 2367 CG PHE A 246 19.918 86.554 37.471 1.00 87.23 C ANISOU 2367 CG PHE A 246 12384 10404 10356 938 -567 125 C ATOM 2368 CD1 PHE A 246 20.762 87.467 36.851 1.00 92.35 C ANISOU 2368 CD1 PHE A 246 13056 11086 10947 924 -413 199 C ATOM 2369 CD2 PHE A 246 20.485 85.552 38.253 1.00 88.53 C ANISOU 2369 CD2 PHE A 246 12476 10558 10603 970 -540 24 C ATOM 2370 CE1 PHE A 246 22.149 87.366 36.994 1.00 93.93 C ANISOU 2370 CE1 PHE A 246 13170 11312 11207 930 -237 155 C ATOM 2371 CE2 PHE A 246 21.869 85.454 38.397 1.00 91.77 C ANISOU 2371 CE2 PHE A 246 12817 11005 11046 997 -397 -23 C ATOM 2372 CZ PHE A 246 22.692 86.357 37.764 1.00 91.46 C ANISOU 2372 CZ PHE A 246 12764 11002 10985 971 -246 34 C ATOM 2373 N ILE A 247 15.471 87.778 37.835 1.00 82.20 N ANISOU 2373 N ILE A 247 11676 9606 9949 888 -1064 292 N ATOM 2374 CA ILE A 247 14.354 88.637 37.418 1.00 82.93 C ANISOU 2374 CA ILE A 247 11767 9671 10074 897 -1204 375 C ATOM 2375 C ILE A 247 13.968 89.621 38.554 1.00 85.93 C ANISOU 2375 C ILE A 247 12014 9989 10647 885 -1150 454 C ATOM 2376 O ILE A 247 13.769 90.813 38.291 1.00 85.90 O ANISOU 2376 O ILE A 247 12031 9967 10642 900 -1162 556 O ATOM 2377 CB ILE A 247 13.123 87.780 36.961 1.00 86.94 C ANISOU 2377 CB ILE A 247 12251 10144 10639 903 -1424 294 C ATOM 2378 CG1 ILE A 247 13.408 87.057 35.625 1.00 89.20 C ANISOU 2378 CG1 ILE A 247 12719 10488 10686 940 -1523 205 C ATOM 2379 CG2 ILE A 247 11.835 88.625 36.849 1.00 87.99 C ANISOU 2379 CG2 ILE A 247 12303 10229 10899 922 -1588 368 C ATOM 2380 CD1 ILE A 247 12.561 85.757 35.366 1.00 97.48 C ANISOU 2380 CD1 ILE A 247 13728 11480 11829 926 -1721 48 C ATOM 2381 N CYS A 248 13.908 89.119 39.805 1.00 80.89 N ANISOU 2381 N CYS A 248 11267 9311 10156 874 -1078 407 N ATOM 2382 CA CYS A 248 13.424 89.855 40.973 1.00 80.09 C ANISOU 2382 CA CYS A 248 11063 9149 10219 887 -1021 453 C ATOM 2383 C CYS A 248 14.444 90.733 41.700 1.00 79.69 C ANISOU 2383 C CYS A 248 11021 9103 10153 895 -898 466 C ATOM 2384 O CYS A 248 14.161 91.918 41.900 1.00 79.63 O ANISOU 2384 O CYS A 248 10992 9050 10215 904 -893 528 O ATOM 2385 CB CYS A 248 12.758 88.899 41.961 1.00 80.77 C ANISOU 2385 CB CYS A 248 11062 9178 10448 894 -985 412 C ATOM 2386 SG CYS A 248 11.375 87.962 41.261 1.00 86.56 S ANISOU 2386 SG CYS A 248 11712 9855 11321 861 -1140 378 S ATOM 2387 N PHE A 249 15.557 90.157 42.181 1.00 72.69 N ANISOU 2387 N PHE A 249 10152 8254 9212 899 -817 394 N ATOM 2388 CA PHE A 249 16.461 90.872 43.075 1.00 71.24 C ANISOU 2388 CA PHE A 249 9944 8062 9061 915 -743 366 C ATOM 2389 C PHE A 249 17.689 91.504 42.445 1.00 74.95 C ANISOU 2389 C PHE A 249 10423 8560 9495 872 -689 364 C ATOM 2390 O PHE A 249 18.170 92.514 42.970 1.00 73.97 O ANISOU 2390 O PHE A 249 10256 8393 9459 862 -658 354 O ATOM 2391 CB PHE A 249 16.905 89.934 44.206 1.00 72.08 C ANISOU 2391 CB PHE A 249 10047 8179 9161 973 -708 282 C ATOM 2392 CG PHE A 249 15.753 89.286 44.936 1.00 72.81 C ANISOU 2392 CG PHE A 249 10137 8221 9308 1015 -698 305 C ATOM 2393 CD1 PHE A 249 14.775 90.059 45.557 1.00 75.09 C ANISOU 2393 CD1 PHE A 249 10393 8449 9689 1042 -676 353 C ATOM 2394 CD2 PHE A 249 15.636 87.903 44.994 1.00 74.64 C ANISOU 2394 CD2 PHE A 249 10391 8445 9522 1029 -684 282 C ATOM 2395 CE1 PHE A 249 13.701 89.459 46.222 1.00 75.86 C ANISOU 2395 CE1 PHE A 249 10469 8487 9867 1080 -616 386 C ATOM 2396 CE2 PHE A 249 14.572 87.304 45.678 1.00 77.35 C ANISOU 2396 CE2 PHE A 249 10719 8714 9958 1056 -632 320 C ATOM 2397 CZ PHE A 249 13.621 88.088 46.298 1.00 75.27 C ANISOU 2397 CZ PHE A 249 10410 8397 9790 1080 -585 376 C ATOM 2398 N VAL A 250 18.215 90.913 41.369 1.00 72.66 N ANISOU 2398 N VAL A 250 10185 8329 9095 851 -662 365 N ATOM 2399 CA VAL A 250 19.424 91.384 40.684 1.00 73.23 C ANISOU 2399 CA VAL A 250 10258 8422 9144 812 -552 377 C ATOM 2400 C VAL A 250 19.241 92.834 40.152 1.00 77.44 C ANISOU 2400 C VAL A 250 10816 8889 9721 770 -514 500 C ATOM 2401 O VAL A 250 20.138 93.630 40.435 1.00 77.81 O ANISOU 2401 O VAL A 250 10786 8887 9890 727 -424 491 O ATOM 2402 CB VAL A 250 19.890 90.373 39.582 1.00 77.77 C ANISOU 2402 CB VAL A 250 10915 9073 9561 823 -503 353 C ATOM 2403 CG1 VAL A 250 20.768 91.020 38.513 1.00 78.84 C ANISOU 2403 CG1 VAL A 250 11098 9220 9639 790 -349 427 C ATOM 2404 CG2 VAL A 250 20.603 89.175 40.208 1.00 77.14 C ANISOU 2404 CG2 VAL A 250 10779 9030 9499 863 -489 226 C ATOM 2405 N PRO A 251 18.136 93.239 39.451 1.00 74.21 N ANISOU 2405 N PRO A 251 10497 8456 9245 785 -590 609 N ATOM 2406 CA PRO A 251 18.079 94.616 38.923 1.00 75.35 C ANISOU 2406 CA PRO A 251 10686 8518 9427 763 -541 744 C ATOM 2407 C PRO A 251 18.169 95.706 39.992 1.00 80.02 C ANISOU 2407 C PRO A 251 11171 9000 10234 738 -525 728 C ATOM 2408 O PRO A 251 18.919 96.661 39.795 1.00 80.51 O ANISOU 2408 O PRO A 251 11218 8981 10393 684 -412 782 O ATOM 2409 CB PRO A 251 16.733 94.664 38.191 1.00 77.56 C ANISOU 2409 CB PRO A 251 11068 8797 9603 821 -688 836 C ATOM 2410 CG PRO A 251 16.447 93.257 37.837 1.00 81.41 C ANISOU 2410 CG PRO A 251 11593 9381 9958 849 -777 747 C ATOM 2411 CD PRO A 251 16.958 92.467 39.000 1.00 75.43 C ANISOU 2411 CD PRO A 251 10713 8643 9303 828 -734 612 C ATOM 2412 N PHE A 252 17.447 95.543 41.122 1.00 76.00 N ANISOU 2412 N PHE A 252 10594 8476 9805 779 -619 650 N ATOM 2413 CA PHE A 252 17.406 96.497 42.232 1.00 76.05 C ANISOU 2413 CA PHE A 252 10531 8383 9983 786 -622 603 C ATOM 2414 C PHE A 252 18.794 96.777 42.827 1.00 80.53 C ANISOU 2414 C PHE A 252 11016 8924 10657 737 -557 491 C ATOM 2415 O PHE A 252 19.183 97.942 42.953 1.00 81.73 O ANISOU 2415 O PHE A 252 11132 8959 10964 691 -518 499 O ATOM 2416 CB PHE A 252 16.449 95.989 43.333 1.00 76.83 C ANISOU 2416 CB PHE A 252 10601 8495 10097 862 -694 532 C ATOM 2417 CG PHE A 252 16.335 96.868 44.559 1.00 78.34 C ANISOU 2417 CG PHE A 252 10757 8592 10415 904 -695 461 C ATOM 2418 CD1 PHE A 252 15.483 97.969 44.571 1.00 82.25 C ANISOU 2418 CD1 PHE A 252 11257 8978 11015 930 -707 531 C ATOM 2419 CD2 PHE A 252 17.050 96.575 45.714 1.00 79.92 C ANISOU 2419 CD2 PHE A 252 10940 8812 10615 942 -698 314 C ATOM 2420 CE1 PHE A 252 15.363 98.770 45.711 1.00 83.82 C ANISOU 2420 CE1 PHE A 252 11444 9083 11321 984 -702 442 C ATOM 2421 CE2 PHE A 252 16.934 97.378 46.852 1.00 83.69 C ANISOU 2421 CE2 PHE A 252 11422 9205 11170 1005 -716 223 C ATOM 2422 CZ PHE A 252 16.099 98.478 46.841 1.00 82.75 C ANISOU 2422 CZ PHE A 252 11309 8972 11158 1021 -708 282 C ATOM 2423 N HIS A 253 19.521 95.717 43.197 1.00 75.40 N ANISOU 2423 N HIS A 253 10327 8369 9953 751 -560 379 N ATOM 2424 CA HIS A 253 20.824 95.830 43.841 1.00 75.46 C ANISOU 2424 CA HIS A 253 10226 8363 10081 727 -546 244 C ATOM 2425 C HIS A 253 21.946 96.224 42.869 1.00 84.99 C ANISOU 2425 C HIS A 253 11369 9545 11379 628 -408 290 C ATOM 2426 O HIS A 253 22.947 96.791 43.314 1.00 86.71 O ANISOU 2426 O HIS A 253 11454 9693 11798 578 -391 193 O ATOM 2427 CB HIS A 253 21.158 94.538 44.567 1.00 73.94 C ANISOU 2427 CB HIS A 253 10022 8273 9800 805 -609 123 C ATOM 2428 CG HIS A 253 20.150 94.200 45.616 1.00 75.12 C ANISOU 2428 CG HIS A 253 10242 8426 9876 905 -691 94 C ATOM 2429 ND1 HIS A 253 19.018 93.467 45.314 1.00 75.52 N ANISOU 2429 ND1 HIS A 253 10367 8511 9817 935 -686 182 N ATOM 2430 CD2 HIS A 253 20.101 94.564 46.917 1.00 75.84 C ANISOU 2430 CD2 HIS A 253 10343 8475 9998 983 -762 -10 C ATOM 2431 CE1 HIS A 253 18.337 93.378 46.445 1.00 74.14 C ANISOU 2431 CE1 HIS A 253 10229 8311 9628 1022 -714 148 C ATOM 2432 NE2 HIS A 253 18.946 94.032 47.434 1.00 74.84 N ANISOU 2432 NE2 HIS A 253 10305 8361 9770 1066 -757 36 N ATOM 2433 N PHE A 254 21.784 95.958 41.560 1.00 83.78 N ANISOU 2433 N PHE A 254 11308 9434 11089 607 -306 430 N ATOM 2434 CA PHE A 254 22.770 96.381 40.566 1.00 86.20 C ANISOU 2434 CA PHE A 254 11587 9707 11459 527 -115 508 C ATOM 2435 C PHE A 254 22.594 97.882 40.276 1.00 90.49 C ANISOU 2435 C PHE A 254 12149 10086 12147 461 -38 638 C ATOM 2436 O PHE A 254 23.583 98.610 40.231 1.00 91.90 O ANISOU 2436 O PHE A 254 12213 10160 12546 369 102 639 O ATOM 2437 CB PHE A 254 22.676 95.540 39.283 1.00 89.17 C ANISOU 2437 CB PHE A 254 12105 10190 11587 559 -25 604 C ATOM 2438 CG PHE A 254 23.639 94.378 39.272 1.00 92.16 C ANISOU 2438 CG PHE A 254 12406 10670 11940 577 35 485 C ATOM 2439 CD1 PHE A 254 23.333 93.193 39.933 1.00 94.62 C ANISOU 2439 CD1 PHE A 254 12715 11072 12164 653 -109 362 C ATOM 2440 CD2 PHE A 254 24.872 94.481 38.640 1.00 97.22 C ANISOU 2440 CD2 PHE A 254 12967 11300 12674 525 257 502 C ATOM 2441 CE1 PHE A 254 24.233 92.122 39.938 1.00 95.94 C ANISOU 2441 CE1 PHE A 254 12814 11316 12322 688 -60 254 C ATOM 2442 CE2 PHE A 254 25.775 93.412 38.653 1.00100.45 C ANISOU 2442 CE2 PHE A 254 13282 11796 13086 559 315 384 C ATOM 2443 CZ PHE A 254 25.446 92.238 39.296 1.00 96.95 C ANISOU 2443 CZ PHE A 254 12852 11442 12542 646 143 258 C ATOM 2444 N ALA A 255 21.335 98.343 40.138 1.00 85.78 N ANISOU 2444 N ALA A 255 11678 9449 11466 508 -130 742 N ATOM 2445 CA ALA A 255 20.987 99.742 39.889 1.00 86.99 C ANISOU 2445 CA ALA A 255 11877 9431 11745 474 -79 878 C ATOM 2446 C ALA A 255 21.410 100.652 41.045 1.00 92.09 C ANISOU 2446 C ALA A 255 12374 9928 12688 422 -117 745 C ATOM 2447 O ALA A 255 21.707 101.824 40.818 1.00 93.65 O ANISOU 2447 O ALA A 255 12556 9944 13082 351 -16 827 O ATOM 2448 CB ALA A 255 19.494 99.874 39.655 1.00 86.99 C ANISOU 2448 CB ALA A 255 12018 9435 11600 567 -211 987 C ATOM 2449 N ARG A 256 21.441 100.109 42.274 1.00 87.68 N ANISOU 2449 N ARG A 256 11726 9432 12155 467 -265 540 N ATOM 2450 CA ARG A 256 21.807 100.839 43.486 1.00 88.02 C ANISOU 2450 CA ARG A 256 11659 9356 12429 452 -354 364 C ATOM 2451 C ARG A 256 23.288 101.257 43.481 1.00 95.00 C ANISOU 2451 C ARG A 256 12362 10147 13585 332 -269 271 C ATOM 2452 O ARG A 256 23.594 102.329 44.002 1.00 95.92 O ANISOU 2452 O ARG A 256 12398 10083 13965 275 -295 189 O ATOM 2453 CB ARG A 256 21.491 99.998 44.735 1.00 85.09 C ANISOU 2453 CB ARG A 256 11289 9099 11943 566 -524 184 C ATOM 2454 CG ARG A 256 21.496 100.798 46.031 1.00 91.15 C ANISOU 2454 CG ARG A 256 12022 9751 12858 606 -649 3 C ATOM 2455 CD ARG A 256 21.250 99.931 47.245 1.00 91.57 C ANISOU 2455 CD ARG A 256 12123 9923 12746 744 -786 -152 C ATOM 2456 NE ARG A 256 21.393 100.699 48.480 1.00102.10 N ANISOU 2456 NE ARG A 256 13456 11154 14184 804 -915 -353 N ATOM 2457 CZ ARG A 256 22.538 100.865 49.138 1.00121.68 C ANISOU 2457 CZ ARG A 256 15829 13601 16801 794 -1036 -565 C ATOM 2458 NH1 ARG A 256 23.660 100.314 48.687 1.00107.19 N ANISOU 2458 NH1 ARG A 256 13852 11828 15048 720 -1021 -593 N ATOM 2459 NH2 ARG A 256 22.569 101.583 50.253 1.00114.49 N ANISOU 2459 NH2 ARG A 256 14951 12593 15957 868 -1182 -767 N ATOM 2460 N ILE A 257 24.192 100.425 42.893 1.00 92.88 N ANISOU 2460 N ILE A 257 12018 9987 13286 296 -165 273 N ATOM 2461 CA ILE A 257 25.646 100.665 42.820 1.00 95.10 C ANISOU 2461 CA ILE A 257 12079 10196 13860 184 -60 183 C ATOM 2462 C ILE A 257 25.962 102.077 42.241 1.00102.88 C ANISOU 2462 C ILE A 257 13013 10939 15138 45 123 305 C ATOM 2463 O ILE A 257 26.581 102.843 42.979 1.00103.74 O ANISOU 2463 O ILE A 257 12944 10891 15580 -29 51 140 O ATOM 2464 CB ILE A 257 26.428 99.553 42.055 1.00 98.24 C ANISOU 2464 CB ILE A 257 12427 10744 14157 184 84 214 C ATOM 2465 CG1 ILE A 257 26.073 98.134 42.560 1.00 96.49 C ANISOU 2465 CG1 ILE A 257 12276 10729 13656 321 -82 115 C ATOM 2466 CG2 ILE A 257 27.943 99.813 42.119 1.00101.26 C ANISOU 2466 CG2 ILE A 257 12523 11043 14909 75 187 93 C ATOM 2467 CD1 ILE A 257 26.349 97.001 41.555 1.00103.43 C ANISOU 2467 CD1 ILE A 257 13211 11754 14335 351 65 196 C ATOM 2468 N PRO A 258 25.547 102.475 40.997 1.00101.71 N ANISOU 2468 N PRO A 258 13025 10737 14884 18 339 581 N ATOM 2469 CA PRO A 258 25.880 103.831 40.513 1.00104.88 C ANISOU 2469 CA PRO A 258 13391 10877 15583 -108 534 716 C ATOM 2470 C PRO A 258 25.343 104.967 41.388 1.00111.32 C ANISOU 2470 C PRO A 258 14207 11494 16598 -115 374 635 C ATOM 2471 O PRO A 258 26.014 105.989 41.523 1.00113.49 O ANISOU 2471 O PRO A 258 14341 11525 17256 -243 461 605 O ATOM 2472 CB PRO A 258 25.227 103.881 39.127 1.00107.05 C ANISOU 2472 CB PRO A 258 13924 11172 15578 -66 737 1036 C ATOM 2473 CG PRO A 258 25.107 102.467 38.708 1.00109.42 C ANISOU 2473 CG PRO A 258 14312 11742 15520 34 708 1027 C ATOM 2474 CD PRO A 258 24.807 101.722 39.960 1.00102.26 C ANISOU 2474 CD PRO A 258 13325 10964 14564 108 410 779 C ATOM 2475 N TYR A 259 24.154 104.783 41.991 1.00107.78 N ANISOU 2475 N TYR A 259 13902 11133 15917 21 155 591 N ATOM 2476 CA TYR A 259 23.499 105.778 42.838 1.00109.07 C ANISOU 2476 CA TYR A 259 14095 11126 16221 52 9 507 C ATOM 2477 C TYR A 259 24.036 105.803 44.278 1.00116.53 C ANISOU 2477 C TYR A 259 14878 12046 17352 56 -207 168 C ATOM 2478 O TYR A 259 23.565 106.624 45.068 1.00116.93 O ANISOU 2478 O TYR A 259 14961 11953 17514 95 -333 56 O ATOM 2479 CB TYR A 259 21.973 105.546 42.866 1.00108.29 C ANISOU 2479 CB TYR A 259 14202 11131 15813 210 -106 604 C ATOM 2480 CG TYR A 259 21.278 105.825 41.551 1.00110.84 C ANISOU 2480 CG TYR A 259 14707 11426 15981 237 30 917 C ATOM 2481 CD1 TYR A 259 21.161 107.126 41.062 1.00115.12 C ANISOU 2481 CD1 TYR A 259 15311 11711 16718 191 149 1085 C ATOM 2482 CD2 TYR A 259 20.701 104.796 40.812 1.00110.02 C ANISOU 2482 CD2 TYR A 259 14731 11539 15534 326 14 1036 C ATOM 2483 CE1 TYR A 259 20.517 107.389 39.853 1.00116.69 C ANISOU 2483 CE1 TYR A 259 15712 11884 16740 250 249 1383 C ATOM 2484 CE2 TYR A 259 20.054 105.047 39.603 1.00111.94 C ANISOU 2484 CE2 TYR A 259 15165 11764 15605 379 88 1303 C ATOM 2485 CZ TYR A 259 19.965 106.346 39.127 1.00122.36 C ANISOU 2485 CZ TYR A 259 16561 12840 17089 352 203 1484 C ATOM 2486 OH TYR A 259 19.328 106.602 37.937 1.00125.03 O ANISOU 2486 OH TYR A 259 17119 13161 17227 435 255 1757 O ATOM 2487 N THR A 260 25.009 104.942 44.630 1.00115.74 N ANISOU 2487 N THR A 260 14617 12077 17281 36 -263 -4 N ATOM 2488 CA THR A 260 25.507 104.931 46.005 1.00117.36 C ANISOU 2488 CA THR A 260 14700 12272 17621 75 -513 -333 C ATOM 2489 C THR A 260 27.019 105.325 46.090 1.00127.33 C ANISOU 2489 C THR A 260 15667 13395 19318 -78 -501 -504 C ATOM 2490 O THR A 260 27.541 105.397 47.206 1.00127.71 O ANISOU 2490 O THR A 260 15597 13424 19503 -42 -751 -805 O ATOM 2491 CB THR A 260 25.132 103.603 46.710 1.00123.53 C ANISOU 2491 CB THR A 260 15570 13320 18044 246 -684 -438 C ATOM 2492 OG1 THR A 260 25.083 103.795 48.124 1.00125.46 O ANISOU 2492 OG1 THR A 260 15822 13540 18308 349 -939 -714 O ATOM 2493 CG2 THR A 260 26.029 102.430 46.344 1.00121.27 C ANISOU 2493 CG2 THR A 260 15172 13213 17693 235 -637 -445 C ATOM 2494 N LEU A 261 27.690 105.646 44.946 1.00128.59 N ANISOU 2494 N LEU A 261 15709 13439 19709 -241 -215 -318 N ATOM 2495 CA LEU A 261 29.089 106.112 44.954 1.00133.17 C ANISOU 2495 CA LEU A 261 15965 13847 20785 -410 -156 -460 C ATOM 2496 C LEU A 261 29.421 107.052 43.755 1.00143.85 C ANISOU 2496 C LEU A 261 17269 14954 22433 -594 218 -193 C ATOM 2497 O LEU A 261 30.403 106.818 43.041 1.00145.43 O ANISOU 2497 O LEU A 261 17265 15130 22860 -712 454 -132 O ATOM 2498 CB LEU A 261 30.150 104.971 45.072 1.00133.10 C ANISOU 2498 CB LEU A 261 15740 14031 20802 -394 -200 -606 C ATOM 2499 CG LEU A 261 30.077 103.623 44.298 1.00135.30 C ANISOU 2499 CG LEU A 261 16116 14582 20710 -311 -47 -433 C ATOM 2500 CD1 LEU A 261 29.337 102.567 45.059 1.00132.26 C ANISOU 2500 CD1 LEU A 261 15916 14443 19895 -109 -303 -527 C ATOM 2501 CD2 LEU A 261 29.700 103.747 42.821 1.00137.41 C ANISOU 2501 CD2 LEU A 261 16548 14829 20833 -368 323 -72 C ATOM 2502 N SER A 262 28.649 108.148 43.576 1.00144.02 N ANISOU 2502 N SER A 262 17469 14773 22478 -611 285 -36 N ATOM 2503 CA SER A 262 28.911 109.068 42.462 1.00148.13 C ANISOU 2503 CA SER A 262 17992 15041 23249 -762 651 251 C ATOM 2504 C SER A 262 28.691 110.565 42.806 1.00157.60 C ANISOU 2504 C SER A 262 19182 15868 24829 -854 633 224 C ATOM 2505 O SER A 262 29.674 111.310 42.894 1.00160.71 O ANISOU 2505 O SER A 262 19310 15993 25758 -1042 731 126 O ATOM 2506 CB SER A 262 28.073 108.687 41.244 1.00150.41 C ANISOU 2506 CB SER A 262 18595 15469 23085 -664 868 623 C ATOM 2507 N GLN A 263 27.415 111.003 42.958 1.00154.71 N ANISOU 2507 N GLN A 263 19089 15470 24222 -726 524 313 N ATOM 2508 CA GLN A 263 27.028 112.398 43.210 1.00157.61 C ANISOU 2508 CA GLN A 263 19505 15484 24896 -776 516 317 C ATOM 2509 C GLN A 263 27.548 112.937 44.544 1.00164.96 C ANISOU 2509 C GLN A 263 20220 16241 26217 -834 230 -104 C ATOM 2510 O GLN A 263 27.484 112.243 45.563 1.00162.77 O ANISOU 2510 O GLN A 263 19909 16178 25759 -720 -77 -400 O ATOM 2511 CB GLN A 263 25.501 112.555 43.158 1.00156.83 C ANISOU 2511 CB GLN A 263 19731 15441 24418 -584 428 475 C ATOM 2512 N THR A 264 28.052 114.192 44.523 1.00166.58 N ANISOU 2512 N THR A 264 20300 16040 26953 -1004 330 -128 N ATOM 2513 CA THR A 264 28.558 114.907 45.697 1.00169.35 C ANISOU 2513 CA THR A 264 20454 16153 27739 -1075 56 -538 C ATOM 2514 C THR A 264 27.346 115.371 46.516 1.00172.74 C ANISOU 2514 C THR A 264 21142 16565 27927 -880 -198 -664 C ATOM 2515 O THR A 264 26.776 116.436 46.249 1.00173.85 O ANISOU 2515 O THR A 264 21423 16420 28212 -887 -94 -521 O ATOM 2516 CB THR A 264 29.490 116.053 45.272 1.00182.81 C ANISOU 2516 CB THR A 264 21930 17404 30126 -1338 290 -494 C ATOM 2517 N ARG A 265 26.936 114.518 47.484 1.00167.09 N ANISOU 2517 N ARG A 265 20504 16161 26823 -687 -502 -907 N ATOM 2518 CA ARG A 265 25.777 114.639 48.378 1.00165.41 C ANISOU 2518 CA ARG A 265 20537 16023 26288 -460 -731 -1047 C ATOM 2519 C ARG A 265 24.477 114.352 47.595 1.00166.89 C ANISOU 2519 C ARG A 265 20998 16360 26052 -319 -554 -670 C ATOM 2520 O ARG A 265 23.876 113.299 47.817 1.00163.36 O ANISOU 2520 O ARG A 265 20677 16240 25153 -147 -647 -663 O ATOM 2521 CB ARG A 265 25.717 115.990 49.122 1.00168.87 C ANISOU 2521 CB ARG A 265 20975 16087 27100 -480 -883 -1309 C ATOM 2522 N ASP A 266 24.067 115.254 46.665 1.00165.00 N ANISOU 2522 N ASP A 266 20844 15875 25973 -388 -305 -353 N ATOM 2523 CA ASP A 266 22.850 115.111 45.846 1.00162.78 C ANISOU 2523 CA ASP A 266 20810 15698 25339 -249 -169 6 C ATOM 2524 C ASP A 266 22.943 115.833 44.482 1.00167.59 C ANISOU 2524 C ASP A 266 21476 16073 26128 -365 152 401 C ATOM 2525 O ASP A 266 23.682 116.813 44.342 1.00170.72 O ANISOU 2525 O ASP A 266 21754 16117 26994 -541 278 394 O ATOM 2526 CB ASP A 266 21.614 115.645 46.607 1.00164.35 C ANISOU 2526 CB ASP A 266 21186 15821 25438 -55 -326 -92 C ATOM 2527 CG ASP A 266 21.060 114.731 47.689 1.00172.45 C ANISOU 2527 CG ASP A 266 22287 17172 26064 147 -541 -292 C ATOM 2528 OD1 ASP A 266 20.882 113.520 47.415 1.00170.55 O ANISOU 2528 OD1 ASP A 266 22062 17260 25480 193 -522 -182 O ATOM 2529 OD2 ASP A 266 20.756 115.235 48.792 1.00178.78 O ANISOU 2529 OD2 ASP A 266 23152 17885 26890 269 -705 -544 O ATOM 2530 N VAL A 267 22.154 115.351 43.491 1.00161.00 N ANISOU 2530 N VAL A 267 20837 15422 24912 -254 274 744 N ATOM 2531 CA VAL A 267 22.043 115.916 42.138 1.00161.89 C ANISOU 2531 CA VAL A 267 21095 15364 25050 -290 560 1162 C ATOM 2532 C VAL A 267 20.938 116.988 42.116 1.00163.92 C ANISOU 2532 C VAL A 267 21552 15397 25333 -146 516 1297 C ATOM 2533 O VAL A 267 19.985 116.896 42.895 1.00161.56 O ANISOU 2533 O VAL A 267 21314 15222 24848 28 291 1147 O ATOM 2534 CB VAL A 267 21.778 114.815 41.087 1.00163.88 C ANISOU 2534 CB VAL A 267 21471 15946 24851 -222 673 1427 C ATOM 2535 N PHE A 268 21.062 117.997 41.228 1.00161.50 N ANISOU 2535 N PHE A 268 21347 14749 25267 -209 749 1588 N ATOM 2536 CA PHE A 268 20.102 119.109 41.149 1.00161.76 C ANISOU 2536 CA PHE A 268 21563 14515 25383 -70 718 1729 C ATOM 2537 C PHE A 268 19.211 119.099 39.885 1.00162.36 C ANISOU 2537 C PHE A 268 21918 14645 25125 97 824 2174 C ATOM 2538 O PHE A 268 18.125 119.689 39.926 1.00162.27 O ANISOU 2538 O PHE A 268 22053 14528 25075 282 711 2258 O ATOM 2539 CB PHE A 268 20.835 120.457 41.237 1.00167.83 C ANISOU 2539 CB PHE A 268 22258 14776 26733 -239 863 1705 C ATOM 2540 N ASP A 269 19.663 118.469 38.772 1.00155.81 N ANISOU 2540 N ASP A 269 21173 13965 24061 52 1032 2448 N ATOM 2541 CA ASP A 269 18.887 118.438 37.523 1.00154.48 C ANISOU 2541 CA ASP A 269 21305 13851 23537 231 1106 2859 C ATOM 2542 C ASP A 269 17.704 117.470 37.646 1.00149.43 C ANISOU 2542 C ASP A 269 20735 13596 22446 455 810 2797 C ATOM 2543 O ASP A 269 17.867 116.337 38.099 1.00145.64 O ANISOU 2543 O ASP A 269 20122 13448 21765 430 695 2580 O ATOM 2544 CB ASP A 269 19.761 118.121 36.288 1.00158.21 C ANISOU 2544 CB ASP A 269 21886 14349 23877 136 1440 3165 C ATOM 2545 CG ASP A 269 20.590 116.850 36.337 1.00166.16 C ANISOU 2545 CG ASP A 269 22733 15698 24701 29 1476 3004 C ATOM 2546 OD1 ASP A 269 21.190 116.568 37.400 1.00165.20 O ANISOU 2546 OD1 ASP A 269 22321 15613 24833 -117 1389 2649 O ATOM 2547 OD2 ASP A 269 20.709 116.181 35.287 1.00172.02 O ANISOU 2547 OD2 ASP A 269 23651 16649 25057 98 1600 3234 O ATOM 2548 N CYS A 270 16.507 117.959 37.270 1.00142.81 N ANISOU 2548 N CYS A 270 20085 12682 21494 674 685 2983 N ATOM 2549 CA CYS A 270 15.218 117.268 37.345 1.00137.90 C ANISOU 2549 CA CYS A 270 19507 12347 20543 900 398 2945 C ATOM 2550 C CYS A 270 15.164 116.006 36.478 1.00136.81 C ANISOU 2550 C CYS A 270 19459 12581 19941 951 364 3055 C ATOM 2551 O CYS A 270 14.448 115.070 36.834 1.00132.81 O ANISOU 2551 O CYS A 270 18867 12371 19223 1040 139 2884 O ATOM 2552 CB CYS A 270 14.082 118.222 36.987 1.00139.73 C ANISOU 2552 CB CYS A 270 19914 12362 20814 1121 300 3162 C ATOM 2553 SG CYS A 270 12.951 118.575 38.359 1.00141.68 S ANISOU 2553 SG CYS A 270 19993 12563 21275 1264 41 2854 S ATOM 2554 N THR A 271 15.897 115.986 35.349 1.00133.78 N ANISOU 2554 N THR A 271 19256 12167 19409 901 601 3335 N ATOM 2555 CA THR A 271 15.951 114.853 34.417 1.00131.83 C ANISOU 2555 CA THR A 271 19138 12244 18707 957 597 3444 C ATOM 2556 C THR A 271 16.708 113.653 35.048 1.00130.17 C ANISOU 2556 C THR A 271 18691 12310 18458 798 598 3140 C ATOM 2557 O THR A 271 16.432 112.507 34.685 1.00127.80 O ANISOU 2557 O THR A 271 18428 12326 17803 871 474 3100 O ATOM 2558 CB THR A 271 16.534 115.287 33.051 1.00143.91 C ANISOU 2558 CB THR A 271 20961 13635 20082 968 898 3835 C ATOM 2559 OG1 THR A 271 16.592 114.161 32.173 1.00141.91 O ANISOU 2559 OG1 THR A 271 20853 13705 19361 1040 884 3903 O ATOM 2560 CG2 THR A 271 17.912 115.960 33.156 1.00145.14 C ANISOU 2560 CG2 THR A 271 21020 13508 20620 720 1285 3877 C ATOM 2561 N ALA A 272 17.630 113.921 36.001 1.00124.47 N ANISOU 2561 N ALA A 272 17729 11456 18109 595 711 2914 N ATOM 2562 CA ALA A 272 18.408 112.904 36.719 1.00120.44 C ANISOU 2562 CA ALA A 272 16981 11168 17611 457 692 2615 C ATOM 2563 C ALA A 272 17.658 112.394 37.963 1.00118.51 C ANISOU 2563 C ALA A 272 16577 11086 17365 526 392 2296 C ATOM 2564 O ALA A 272 17.775 111.217 38.311 1.00115.30 O ANISOU 2564 O ALA A 272 16071 10963 16774 516 295 2116 O ATOM 2565 CB ALA A 272 19.761 113.466 37.121 1.00122.75 C ANISOU 2565 CB ALA A 272 17086 11233 18320 225 923 2518 C ATOM 2566 N GLU A 273 16.910 113.287 38.636 1.00113.68 N ANISOU 2566 N GLU A 273 15952 10280 16963 602 271 2233 N ATOM 2567 CA GLU A 273 16.109 112.990 39.825 1.00110.32 C ANISOU 2567 CA GLU A 273 15405 9963 16548 694 36 1959 C ATOM 2568 C GLU A 273 14.937 112.076 39.451 1.00109.88 C ANISOU 2568 C GLU A 273 15419 10185 16145 870 -143 2023 C ATOM 2569 O GLU A 273 14.591 111.170 40.218 1.00106.89 O ANISOU 2569 O GLU A 273 14924 10024 15664 902 -276 1808 O ATOM 2570 CB GLU A 273 15.601 114.302 40.446 1.00113.64 C ANISOU 2570 CB GLU A 273 15828 10069 17282 752 -3 1914 C ATOM 2571 CG GLU A 273 15.170 114.210 41.900 1.00125.22 C ANISOU 2571 CG GLU A 273 17157 11578 18842 806 -165 1574 C ATOM 2572 CD GLU A 273 14.351 115.388 42.399 1.00157.56 C ANISOU 2572 CD GLU A 273 21290 15403 23174 929 -221 1542 C ATOM 2573 OE1 GLU A 273 14.809 116.547 42.260 1.00157.71 O ANISOU 2573 OE1 GLU A 273 21346 15082 23496 856 -114 1604 O ATOM 2574 OE2 GLU A 273 13.250 115.149 42.946 1.00154.36 O ANISOU 2574 OE2 GLU A 273 20866 15110 22676 1099 -355 1450 O ATOM 2575 N ASN A 274 14.347 112.312 38.260 1.00106.26 N ANISOU 2575 N ASN A 274 15154 9706 15513 987 -149 2321 N ATOM 2576 CA ASN A 274 13.221 111.546 37.736 1.00104.73 C ANISOU 2576 CA ASN A 274 15027 9740 15027 1159 -351 2393 C ATOM 2577 C ASN A 274 13.679 110.215 37.155 1.00106.59 C ANISOU 2577 C ASN A 274 15285 10268 14945 1110 -347 2379 C ATOM 2578 O ASN A 274 12.912 109.252 37.211 1.00104.39 O ANISOU 2578 O ASN A 274 14957 10215 14493 1195 -534 2290 O ATOM 2579 CB ASN A 274 12.431 112.346 36.698 1.00108.47 C ANISOU 2579 CB ASN A 274 15713 10068 15432 1331 -407 2698 C ATOM 2580 CG ASN A 274 11.627 113.497 37.267 1.00124.06 C ANISOU 2580 CG ASN A 274 17655 11787 17694 1443 -479 2700 C ATOM 2581 OD1 ASN A 274 11.299 113.561 38.461 1.00115.08 O ANISOU 2581 OD1 ASN A 274 16336 10631 16758 1441 -538 2454 O ATOM 2582 ND2 ASN A 274 11.262 114.420 36.408 1.00116.60 N ANISOU 2582 ND2 ASN A 274 16910 10637 16754 1568 -473 2984 N ATOM 2583 N THR A 275 14.923 110.133 36.626 1.00103.58 N ANISOU 2583 N THR A 275 14964 9873 14519 972 -122 2457 N ATOM 2584 CA THR A 275 15.420 108.850 36.125 1.00101.72 C ANISOU 2584 CA THR A 275 14749 9905 13996 932 -96 2421 C ATOM 2585 C THR A 275 15.735 107.953 37.343 1.00100.75 C ANISOU 2585 C THR A 275 14384 9941 13954 840 -160 2099 C ATOM 2586 O THR A 275 15.510 106.749 37.271 1.00 98.91 O ANISOU 2586 O THR A 275 14131 9953 13499 869 -262 2009 O ATOM 2587 CB THR A 275 16.572 108.997 35.109 1.00114.51 C ANISOU 2587 CB THR A 275 16512 11462 15532 843 193 2619 C ATOM 2588 OG1 THR A 275 16.672 107.777 34.375 1.00115.21 O ANISOU 2588 OG1 THR A 275 16709 11814 15252 890 169 2638 O ATOM 2589 CG2 THR A 275 17.920 109.319 35.748 1.00113.49 C ANISOU 2589 CG2 THR A 275 16192 11208 15720 631 425 2491 C ATOM 2590 N LEU A 276 16.162 108.555 38.477 1.00 95.13 N ANISOU 2590 N LEU A 276 13510 9080 13556 751 -124 1922 N ATOM 2591 CA LEU A 276 16.428 107.844 39.731 1.00 91.46 C ANISOU 2591 CA LEU A 276 12854 8739 13159 700 -202 1622 C ATOM 2592 C LEU A 276 15.113 107.288 40.294 1.00 91.58 C ANISOU 2592 C LEU A 276 12839 8890 13066 843 -409 1530 C ATOM 2593 O LEU A 276 15.091 106.134 40.725 1.00 88.72 O ANISOU 2593 O LEU A 276 12403 8736 12570 844 -475 1384 O ATOM 2594 CB LEU A 276 17.134 108.778 40.753 1.00 92.10 C ANISOU 2594 CB LEU A 276 12809 8595 13590 600 -146 1454 C ATOM 2595 CG LEU A 276 17.070 108.437 42.260 1.00 94.18 C ANISOU 2595 CG LEU A 276 12933 8921 13931 621 -283 1141 C ATOM 2596 CD1 LEU A 276 17.811 107.139 42.595 1.00 92.37 C ANISOU 2596 CD1 LEU A 276 12607 8923 13565 564 -301 977 C ATOM 2597 CD2 LEU A 276 17.625 109.567 43.083 1.00 96.51 C ANISOU 2597 CD2 LEU A 276 13156 8951 14564 555 -265 991 C ATOM 2598 N PHE A 277 14.025 108.106 40.266 1.00 88.03 N ANISOU 2598 N PHE A 277 12439 8309 12700 966 -493 1625 N ATOM 2599 CA PHE A 277 12.697 107.731 40.760 1.00 86.01 C ANISOU 2599 CA PHE A 277 12124 8144 12413 1107 -657 1558 C ATOM 2600 C PHE A 277 12.153 106.493 40.034 1.00 88.67 C ANISOU 2600 C PHE A 277 12481 8721 12488 1157 -771 1611 C ATOM 2601 O PHE A 277 11.713 105.558 40.701 1.00 86.56 O ANISOU 2601 O PHE A 277 12103 8603 12182 1179 -839 1462 O ATOM 2602 CB PHE A 277 11.686 108.900 40.640 1.00 89.31 C ANISOU 2602 CB PHE A 277 12585 8358 12991 1242 -718 1682 C ATOM 2603 CG PHE A 277 10.292 108.549 41.129 1.00 89.92 C ANISOU 2603 CG PHE A 277 12557 8513 13094 1391 -862 1612 C ATOM 2604 CD1 PHE A 277 9.955 108.678 42.472 1.00 92.15 C ANISOU 2604 CD1 PHE A 277 12724 8754 13535 1428 -836 1408 C ATOM 2605 CD2 PHE A 277 9.337 108.032 40.257 1.00 92.00 C ANISOU 2605 CD2 PHE A 277 12833 8897 13228 1498 -1019 1736 C ATOM 2606 CE1 PHE A 277 8.684 108.310 42.930 1.00 92.61 C ANISOU 2606 CE1 PHE A 277 12667 8880 13641 1563 -914 1354 C ATOM 2607 CE2 PHE A 277 8.068 107.668 40.714 1.00 94.35 C ANISOU 2607 CE2 PHE A 277 12981 9254 13613 1619 -1136 1662 C ATOM 2608 CZ PHE A 277 7.751 107.806 42.048 1.00 91.81 C ANISOU 2608 CZ PHE A 277 12532 8883 13468 1647 -1057 1483 C ATOM 2609 N TYR A 278 12.153 106.504 38.689 1.00 86.54 N ANISOU 2609 N TYR A 278 12368 8471 12042 1187 -790 1820 N ATOM 2610 CA TYR A 278 11.610 105.408 37.896 1.00 86.18 C ANISOU 2610 CA TYR A 278 12368 8630 11744 1248 -935 1855 C ATOM 2611 C TYR A 278 12.485 104.165 37.947 1.00 88.31 C ANISOU 2611 C TYR A 278 12610 9088 11855 1138 -865 1729 C ATOM 2612 O TYR A 278 11.935 103.066 37.966 1.00 87.26 O ANISOU 2612 O TYR A 278 12425 9121 11610 1169 -994 1643 O ATOM 2613 CB TYR A 278 11.343 105.837 36.451 1.00 90.27 C ANISOU 2613 CB TYR A 278 13110 9110 12079 1349 -996 2105 C ATOM 2614 CG TYR A 278 10.167 106.782 36.331 1.00 94.37 C ANISOU 2614 CG TYR A 278 13645 9484 12728 1511 -1151 2224 C ATOM 2615 CD1 TYR A 278 8.896 106.409 36.764 1.00 96.00 C ANISOU 2615 CD1 TYR A 278 13691 9757 13026 1618 -1368 2127 C ATOM 2616 CD2 TYR A 278 10.316 108.042 35.756 1.00 97.98 C ANISOU 2616 CD2 TYR A 278 14269 9721 13237 1563 -1070 2443 C ATOM 2617 CE1 TYR A 278 7.812 107.279 36.662 1.00 99.41 C ANISOU 2617 CE1 TYR A 278 14108 10054 13612 1783 -1515 2228 C ATOM 2618 CE2 TYR A 278 9.237 108.918 35.642 1.00100.82 C ANISOU 2618 CE2 TYR A 278 14647 9935 13725 1734 -1224 2556 C ATOM 2619 CZ TYR A 278 7.986 108.531 36.095 1.00109.44 C ANISOU 2619 CZ TYR A 278 15557 11110 14914 1849 -1455 2441 C ATOM 2620 OH TYR A 278 6.919 109.388 35.976 1.00116.32 O ANISOU 2620 OH TYR A 278 16419 11836 15942 2033 -1612 2546 O ATOM 2621 N VAL A 279 13.822 104.317 38.028 1.00 84.47 N ANISOU 2621 N VAL A 279 12134 8563 11398 1010 -667 1707 N ATOM 2622 CA VAL A 279 14.720 103.161 38.153 1.00 82.72 C ANISOU 2622 CA VAL A 279 11864 8508 11059 918 -596 1576 C ATOM 2623 C VAL A 279 14.416 102.453 39.492 1.00 82.91 C ANISOU 2623 C VAL A 279 11713 8613 11178 913 -672 1349 C ATOM 2624 O VAL A 279 14.122 101.257 39.483 1.00 81.48 O ANISOU 2624 O VAL A 279 11504 8594 10862 929 -747 1269 O ATOM 2625 CB VAL A 279 16.221 103.545 38.001 1.00 87.99 C ANISOU 2625 CB VAL A 279 12539 9098 11795 788 -363 1601 C ATOM 2626 CG1 VAL A 279 17.144 102.472 38.574 1.00 85.93 C ANISOU 2626 CG1 VAL A 279 12146 8972 11531 702 -312 1401 C ATOM 2627 CG2 VAL A 279 16.571 103.826 36.540 1.00 90.07 C ANISOU 2627 CG2 VAL A 279 13012 9347 11862 806 -240 1834 C ATOM 2628 N LYS A 280 14.404 103.206 40.613 1.00 78.20 N ANISOU 2628 N LYS A 280 11023 7888 10803 909 -652 1253 N ATOM 2629 CA LYS A 280 14.127 102.658 41.943 1.00 76.16 C ANISOU 2629 CA LYS A 280 10647 7689 10602 934 -696 1055 C ATOM 2630 C LYS A 280 12.720 102.039 42.028 1.00 79.62 C ANISOU 2630 C LYS A 280 11047 8210 10996 1039 -816 1062 C ATOM 2631 O LYS A 280 12.589 100.927 42.538 1.00 76.95 O ANISOU 2631 O LYS A 280 10651 7999 10588 1042 -833 957 O ATOM 2632 CB LYS A 280 14.307 103.728 43.043 1.00 78.48 C ANISOU 2632 CB LYS A 280 10893 7812 11114 939 -661 947 C ATOM 2633 CG LYS A 280 14.321 103.130 44.453 1.00 88.52 C ANISOU 2633 CG LYS A 280 12095 9152 12386 977 -679 732 C ATOM 2634 CD LYS A 280 14.352 104.167 45.559 1.00 97.37 C ANISOU 2634 CD LYS A 280 13205 10108 13685 1016 -671 600 C ATOM 2635 CE LYS A 280 14.203 103.519 46.916 1.00105.58 C ANISOU 2635 CE LYS A 280 14230 11229 14656 1101 -688 409 C ATOM 2636 NZ LYS A 280 14.265 104.519 48.014 1.00116.52 N ANISOU 2636 NZ LYS A 280 15640 12457 16177 1160 -695 248 N ATOM 2637 N GLU A 281 11.687 102.746 41.526 1.00 78.39 N ANISOU 2637 N GLU A 281 10911 7968 10906 1127 -897 1190 N ATOM 2638 CA GLU A 281 10.301 102.291 41.597 1.00 79.03 C ANISOU 2638 CA GLU A 281 10905 8098 11026 1227 -1019 1192 C ATOM 2639 C GLU A 281 10.040 101.049 40.765 1.00 83.54 C ANISOU 2639 C GLU A 281 11483 8829 11430 1215 -1129 1208 C ATOM 2640 O GLU A 281 9.295 100.171 41.214 1.00 82.71 O ANISOU 2640 O GLU A 281 11259 8795 11373 1237 -1175 1125 O ATOM 2641 CB GLU A 281 9.330 103.401 41.186 1.00 82.61 C ANISOU 2641 CB GLU A 281 11364 8410 11615 1339 -1105 1322 C ATOM 2642 CG GLU A 281 8.177 103.567 42.161 1.00 97.14 C ANISOU 2642 CG GLU A 281 13046 10205 13658 1441 -1122 1249 C ATOM 2643 CD GLU A 281 8.584 103.743 43.612 1.00123.37 C ANISOU 2643 CD GLU A 281 16326 13479 17071 1433 -965 1089 C ATOM 2644 OE1 GLU A 281 9.059 104.845 43.971 1.00120.30 O ANISOU 2644 OE1 GLU A 281 15993 12935 16780 1443 -900 1074 O ATOM 2645 OE2 GLU A 281 8.473 102.760 44.379 1.00123.51 O ANISOU 2645 OE2 GLU A 281 16275 13604 17048 1420 -908 975 O ATOM 2646 N SER A 282 10.645 100.977 39.564 1.00 81.05 N ANISOU 2646 N SER A 282 11313 8556 10926 1185 -1155 1310 N ATOM 2647 CA SER A 282 10.506 99.851 38.641 1.00 80.90 C ANISOU 2647 CA SER A 282 11346 8679 10712 1186 -1273 1308 C ATOM 2648 C SER A 282 11.197 98.594 39.158 1.00 82.61 C ANISOU 2648 C SER A 282 11513 9015 10861 1099 -1192 1158 C ATOM 2649 O SER A 282 10.632 97.511 39.039 1.00 82.34 O ANISOU 2649 O SER A 282 11418 9063 10804 1107 -1295 1086 O ATOM 2650 CB SER A 282 11.072 100.214 37.277 1.00 85.86 C ANISOU 2650 CB SER A 282 12190 9312 11119 1200 -1277 1459 C ATOM 2651 OG SER A 282 10.342 101.300 36.738 1.00 95.66 O ANISOU 2651 OG SER A 282 13502 10440 12404 1310 -1381 1615 O ATOM 2652 N THR A 283 12.412 98.732 39.718 1.00 77.62 N ANISOU 2652 N THR A 283 10896 8375 10223 1021 -1020 1107 N ATOM 2653 CA THR A 283 13.175 97.609 40.261 1.00 75.80 C ANISOU 2653 CA THR A 283 10623 8244 9935 960 -948 970 C ATOM 2654 C THR A 283 12.561 97.114 41.588 1.00 80.19 C ANISOU 2654 C THR A 283 11050 8800 10619 989 -948 857 C ATOM 2655 O THR A 283 12.628 95.911 41.854 1.00 79.76 O ANISOU 2655 O THR A 283 10967 8828 10511 975 -949 775 O ATOM 2656 CB THR A 283 14.652 97.957 40.407 1.00 80.37 C ANISOU 2656 CB THR A 283 11225 8804 10508 884 -795 942 C ATOM 2657 OG1 THR A 283 14.791 99.108 41.231 1.00 82.18 O ANISOU 2657 OG1 THR A 283 11406 8900 10918 881 -744 928 O ATOM 2658 CG2 THR A 283 15.345 98.168 39.062 1.00 78.66 C ANISOU 2658 CG2 THR A 283 11140 8602 10147 852 -726 1059 C ATOM 2659 N LEU A 284 11.942 98.019 42.396 1.00 77.57 N ANISOU 2659 N LEU A 284 10658 8363 10451 1041 -929 859 N ATOM 2660 CA LEU A 284 11.245 97.660 43.645 1.00 77.20 C ANISOU 2660 CA LEU A 284 10515 8303 10512 1095 -886 775 C ATOM 2661 C LEU A 284 10.023 96.812 43.350 1.00 82.70 C ANISOU 2661 C LEU A 284 11120 9035 11268 1123 -968 797 C ATOM 2662 O LEU A 284 9.674 95.940 44.143 1.00 82.63 O ANISOU 2662 O LEU A 284 11045 9048 11301 1135 -901 734 O ATOM 2663 CB LEU A 284 10.804 98.892 44.436 1.00 78.05 C ANISOU 2663 CB LEU A 284 10597 8283 10776 1165 -839 772 C ATOM 2664 CG LEU A 284 11.702 99.360 45.563 1.00 82.80 C ANISOU 2664 CG LEU A 284 11241 8840 11378 1168 -745 653 C ATOM 2665 CD1 LEU A 284 11.312 100.762 45.997 1.00 84.22 C ANISOU 2665 CD1 LEU A 284 11423 8866 11712 1231 -726 654 C ATOM 2666 CD2 LEU A 284 11.658 98.405 46.750 1.00 84.33 C ANISOU 2666 CD2 LEU A 284 11428 9099 11513 1218 -671 544 C ATOM 2667 N TRP A 285 9.355 97.092 42.218 1.00 80.84 N ANISOU 2667 N TRP A 285 10880 8790 11045 1142 -1118 888 N ATOM 2668 CA TRP A 285 8.197 96.339 41.761 1.00 81.60 C ANISOU 2668 CA TRP A 285 10864 8908 11232 1163 -1255 888 C ATOM 2669 C TRP A 285 8.636 94.923 41.330 1.00 85.08 C ANISOU 2669 C TRP A 285 11341 9448 11537 1092 -1290 817 C ATOM 2670 O TRP A 285 7.929 93.961 41.632 1.00 85.13 O ANISOU 2670 O TRP A 285 11225 9453 11668 1079 -1305 759 O ATOM 2671 CB TRP A 285 7.476 97.075 40.631 1.00 82.00 C ANISOU 2671 CB TRP A 285 10928 8924 11304 1228 -1455 989 C ATOM 2672 CG TRP A 285 6.287 96.327 40.118 1.00 84.50 C ANISOU 2672 CG TRP A 285 11101 9256 11748 1254 -1651 958 C ATOM 2673 CD1 TRP A 285 5.027 96.334 40.639 1.00 88.42 C ANISOU 2673 CD1 TRP A 285 11371 9684 12542 1302 -1677 938 C ATOM 2674 CD2 TRP A 285 6.260 95.418 39.009 1.00 85.15 C ANISOU 2674 CD2 TRP A 285 11242 9418 11693 1231 -1849 919 C ATOM 2675 NE1 TRP A 285 4.210 95.500 39.910 1.00 89.49 N ANISOU 2675 NE1 TRP A 285 11389 9842 12771 1298 -1898 887 N ATOM 2676 CE2 TRP A 285 4.941 94.925 38.903 1.00 90.84 C ANISOU 2676 CE2 TRP A 285 11747 10104 12663 1259 -2024 865 C ATOM 2677 CE3 TRP A 285 7.226 94.977 38.084 1.00 86.17 C ANISOU 2677 CE3 TRP A 285 11584 9638 11521 1199 -1890 913 C ATOM 2678 CZ2 TRP A 285 4.558 94.016 37.906 1.00 91.62 C ANISOU 2678 CZ2 TRP A 285 11842 10250 12718 1250 -2280 785 C ATOM 2679 CZ3 TRP A 285 6.843 94.085 37.092 1.00 89.00 C ANISOU 2679 CZ3 TRP A 285 11971 10052 11794 1208 -2120 843 C ATOM 2680 CH2 TRP A 285 5.525 93.616 37.007 1.00 91.21 C ANISOU 2680 CH2 TRP A 285 12040 10290 12324 1232 -2332 770 C ATOM 2681 N LEU A 286 9.811 94.799 40.661 1.00 80.86 N ANISOU 2681 N LEU A 286 10967 8982 10775 1048 -1277 819 N ATOM 2682 CA LEU A 286 10.379 93.516 40.231 1.00 80.52 C ANISOU 2682 CA LEU A 286 10980 9025 10587 996 -1291 742 C ATOM 2683 C LEU A 286 10.709 92.645 41.443 1.00 84.16 C ANISOU 2683 C LEU A 286 11378 9490 11107 969 -1145 654 C ATOM 2684 O LEU A 286 10.535 91.433 41.408 1.00 84.50 O ANISOU 2684 O LEU A 286 11395 9555 11158 942 -1168 588 O ATOM 2685 CB LEU A 286 11.641 93.730 39.378 1.00 80.52 C ANISOU 2685 CB LEU A 286 11154 9086 10354 972 -1247 772 C ATOM 2686 CG LEU A 286 11.438 94.127 37.914 1.00 86.81 C ANISOU 2686 CG LEU A 286 12091 9902 10990 1015 -1382 863 C ATOM 2687 CD1 LEU A 286 12.742 94.595 37.304 1.00 87.04 C ANISOU 2687 CD1 LEU A 286 12280 9960 10830 991 -1237 925 C ATOM 2688 CD2 LEU A 286 10.859 92.977 37.094 1.00 89.59 C ANISOU 2688 CD2 LEU A 286 12470 10312 11257 1034 -1577 787 C ATOM 2689 N THR A 287 11.168 93.290 42.512 1.00 79.73 N ANISOU 2689 N THR A 287 10813 8896 10585 988 -1005 651 N ATOM 2690 CA THR A 287 11.516 92.731 43.810 1.00 78.25 C ANISOU 2690 CA THR A 287 10610 8705 10414 1004 -869 584 C ATOM 2691 C THR A 287 10.242 92.153 44.470 1.00 81.80 C ANISOU 2691 C THR A 287 10943 9096 11040 1035 -826 589 C ATOM 2692 O THR A 287 10.288 91.078 45.062 1.00 80.61 O ANISOU 2692 O THR A 287 10791 8946 10891 1033 -743 553 O ATOM 2693 CB THR A 287 12.179 93.872 44.602 1.00 86.39 C ANISOU 2693 CB THR A 287 11682 9703 11441 1037 -789 569 C ATOM 2694 OG1 THR A 287 13.583 93.872 44.354 1.00 86.44 O ANISOU 2694 OG1 THR A 287 11759 9761 11324 993 -778 529 O ATOM 2695 CG2 THR A 287 11.882 93.842 46.069 1.00 85.23 C ANISOU 2695 CG2 THR A 287 11525 9518 11341 1112 -674 521 C ATOM 2696 N SER A 288 9.115 92.878 44.345 1.00 79.55 N ANISOU 2696 N SER A 288 10553 8749 10925 1067 -870 643 N ATOM 2697 CA SER A 288 7.800 92.518 44.878 1.00 79.89 C ANISOU 2697 CA SER A 288 10433 8717 11203 1094 -812 658 C ATOM 2698 C SER A 288 7.189 91.325 44.129 1.00 83.43 C ANISOU 2698 C SER A 288 10782 9162 11754 1028 -929 632 C ATOM 2699 O SER A 288 6.408 90.571 44.710 1.00 83.30 O ANISOU 2699 O SER A 288 10634 9076 11942 1018 -828 629 O ATOM 2700 CB SER A 288 6.862 93.716 44.779 1.00 83.83 C ANISOU 2700 CB SER A 288 10830 9150 11872 1156 -858 714 C ATOM 2701 OG SER A 288 7.344 94.802 45.552 1.00 90.46 O ANISOU 2701 OG SER A 288 11756 9961 12654 1220 -745 716 O ATOM 2702 N LEU A 289 7.548 91.171 42.833 1.00 79.50 N ANISOU 2702 N LEU A 289 10356 8728 11123 986 -1131 610 N ATOM 2703 CA LEU A 289 7.096 90.122 41.920 1.00 80.02 C ANISOU 2703 CA LEU A 289 10367 8794 11242 932 -1304 548 C ATOM 2704 C LEU A 289 7.620 88.734 42.393 1.00 83.34 C ANISOU 2704 C LEU A 289 10824 9206 11637 878 -1184 483 C ATOM 2705 O LEU A 289 7.110 87.701 41.952 1.00 84.60 O ANISOU 2705 O LEU A 289 10903 9318 11921 824 -1282 415 O ATOM 2706 CB LEU A 289 7.552 90.491 40.477 1.00 80.40 C ANISOU 2706 CB LEU A 289 10563 8924 11061 941 -1520 546 C ATOM 2707 CG LEU A 289 7.418 89.487 39.303 1.00 86.05 C ANISOU 2707 CG LEU A 289 11321 9670 11704 910 -1738 449 C ATOM 2708 CD1 LEU A 289 5.968 89.051 39.072 1.00 88.03 C ANISOU 2708 CD1 LEU A 289 11354 9838 12256 900 -1934 392 C ATOM 2709 CD2 LEU A 289 8.001 90.071 38.028 1.00 88.34 C ANISOU 2709 CD2 LEU A 289 11823 10048 11693 958 -1878 480 C ATOM 2710 N ASN A 290 8.576 88.716 43.347 1.00 77.79 N ANISOU 2710 N ASN A 290 10230 8527 10798 903 -986 498 N ATOM 2711 CA ASN A 290 9.110 87.489 43.940 1.00 77.07 C ANISOU 2711 CA ASN A 290 10195 8416 10672 886 -860 460 C ATOM 2712 C ASN A 290 8.007 86.721 44.676 1.00 83.02 C ANISOU 2712 C ASN A 290 10798 9040 11705 869 -734 486 C ATOM 2713 O ASN A 290 8.009 85.487 44.656 1.00 82.97 O ANISOU 2713 O ASN A 290 10787 8971 11765 823 -707 449 O ATOM 2714 CB ASN A 290 10.267 87.808 44.885 1.00 75.55 C ANISOU 2714 CB ASN A 290 10142 8275 10288 949 -712 472 C ATOM 2715 CG ASN A 290 10.762 86.615 45.668 1.00 90.47 C ANISOU 2715 CG ASN A 290 12106 10136 12132 971 -585 452 C ATOM 2716 OD1 ASN A 290 10.557 86.510 46.886 1.00 86.01 O ANISOU 2716 OD1 ASN A 290 11569 9520 11590 1040 -411 498 O ATOM 2717 ND2 ASN A 290 11.405 85.683 44.981 1.00 74.92 N ANISOU 2717 ND2 ASN A 290 10194 8193 10081 932 -663 388 N ATOM 2718 N ALA A 291 7.056 87.453 45.300 1.00 81.21 N ANISOU 2718 N ALA A 291 10439 8754 11664 907 -641 551 N ATOM 2719 CA ALA A 291 5.904 86.882 46.000 1.00 83.32 C ANISOU 2719 CA ALA A 291 10528 8884 12247 892 -473 594 C ATOM 2720 C ALA A 291 4.982 86.108 45.030 1.00 90.54 C ANISOU 2720 C ALA A 291 11242 9717 13441 787 -659 527 C ATOM 2721 O ALA A 291 4.377 85.125 45.446 1.00 91.85 O ANISOU 2721 O ALA A 291 11286 9750 13864 733 -523 537 O ATOM 2722 CB ALA A 291 5.124 87.975 46.712 1.00 84.58 C ANISOU 2722 CB ALA A 291 10583 9011 12544 970 -347 662 C ATOM 2723 N CYS A 292 4.922 86.520 43.741 1.00 88.29 N ANISOU 2723 N CYS A 292 10944 9504 13100 766 -969 457 N ATOM 2724 CA CYS A 292 4.116 85.887 42.688 1.00 91.17 C ANISOU 2724 CA CYS A 292 11149 9809 13682 689 -1231 355 C ATOM 2725 C CYS A 292 4.912 84.828 41.888 1.00 93.91 C ANISOU 2725 C CYS A 292 11658 10188 13835 637 -1370 242 C ATOM 2726 O CYS A 292 4.304 83.996 41.211 1.00 94.69 O ANISOU 2726 O CYS A 292 11642 10205 14131 565 -1556 128 O ATOM 2727 CB CYS A 292 3.542 86.946 41.752 1.00 93.54 C ANISOU 2727 CB CYS A 292 11374 10165 14004 736 -1510 343 C ATOM 2728 SG CYS A 292 2.420 88.115 42.559 1.00 99.10 S ANISOU 2728 SG CYS A 292 11850 10805 14998 812 -1373 451 S ATOM 2729 N LEU A 293 6.252 84.871 41.948 1.00 88.52 N ANISOU 2729 N LEU A 293 11226 9615 12792 676 -1292 258 N ATOM 2730 CA LEU A 293 7.107 83.954 41.200 1.00 87.89 C ANISOU 2730 CA LEU A 293 11310 9573 12510 651 -1392 152 C ATOM 2731 C LEU A 293 7.596 82.764 42.035 1.00 92.96 C ANISOU 2731 C LEU A 293 12001 10127 13193 627 -1178 151 C ATOM 2732 O LEU A 293 7.970 81.753 41.444 1.00 93.12 O ANISOU 2732 O LEU A 293 12095 10117 13168 593 -1265 43 O ATOM 2733 CB LEU A 293 8.306 84.701 40.588 1.00 85.94 C ANISOU 2733 CB LEU A 293 11285 9491 11876 713 -1439 164 C ATOM 2734 CG LEU A 293 8.018 85.619 39.393 1.00 90.09 C ANISOU 2734 CG LEU A 293 11849 10099 12284 749 -1684 158 C ATOM 2735 CD1 LEU A 293 9.298 86.110 38.784 1.00 88.60 C ANISOU 2735 CD1 LEU A 293 11892 10041 11733 795 -1665 177 C ATOM 2736 CD2 LEU A 293 7.204 84.911 38.317 1.00 93.91 C ANISOU 2736 CD2 LEU A 293 12275 10536 12870 720 -1974 24 C ATOM 2737 N ASN A 294 7.587 82.857 43.386 1.00 90.22 N ANISOU 2737 N ASN A 294 11635 9728 12916 662 -902 269 N ATOM 2738 CA ASN A 294 8.008 81.731 44.238 1.00 90.66 C ANISOU 2738 CA ASN A 294 11766 9685 12998 667 -692 298 C ATOM 2739 C ASN A 294 7.031 80.538 44.142 1.00 98.32 C ANISOU 2739 C ASN A 294 12572 10450 14337 564 -681 256 C ATOM 2740 O ASN A 294 7.536 79.414 44.127 1.00 98.32 O ANISOU 2740 O ASN A 294 12666 10371 14322 546 -646 211 O ATOM 2741 CB ASN A 294 8.217 82.135 45.694 1.00 89.14 C ANISOU 2741 CB ASN A 294 11640 9489 12739 761 -412 435 C ATOM 2742 CG ASN A 294 9.521 82.853 45.955 1.00 97.50 C ANISOU 2742 CG ASN A 294 12892 10708 13446 860 -411 440 C ATOM 2743 OD1 ASN A 294 10.527 82.660 45.260 1.00 86.65 O ANISOU 2743 OD1 ASN A 294 11626 9421 11874 862 -534 361 O ATOM 2744 ND2 ASN A 294 9.532 83.701 46.976 1.00 85.55 N ANISOU 2744 ND2 ASN A 294 11415 9225 11866 947 -267 521 N ATOM 2745 N PRO A 295 5.680 80.709 43.979 1.00 97.78 N ANISOU 2745 N PRO A 295 12244 10279 14629 491 -734 250 N ATOM 2746 CA PRO A 295 4.810 79.526 43.817 1.00100.46 C ANISOU 2746 CA PRO A 295 12398 10399 15375 371 -742 184 C ATOM 2747 C PRO A 295 5.181 78.657 42.603 1.00105.60 C ANISOU 2747 C PRO A 295 13114 11034 15975 311 -1033 -13 C ATOM 2748 O PRO A 295 4.850 77.472 42.599 1.00107.55 O ANISOU 2748 O PRO A 295 13280 11081 16503 220 -1011 -80 O ATOM 2749 CB PRO A 295 3.414 80.130 43.661 1.00104.20 C ANISOU 2749 CB PRO A 295 12557 10808 16224 321 -816 184 C ATOM 2750 CG PRO A 295 3.503 81.451 44.324 1.00107.05 C ANISOU 2750 CG PRO A 295 12964 11304 16405 432 -676 319 C ATOM 2751 CD PRO A 295 4.869 81.944 43.972 1.00 99.76 C ANISOU 2751 CD PRO A 295 12337 10584 14985 516 -783 298 C ATOM 2752 N PHE A 296 5.897 79.227 41.603 1.00100.98 N ANISOU 2752 N PHE A 296 12694 10643 15029 370 -1278 -103 N ATOM 2753 CA PHE A 296 6.391 78.497 40.431 1.00101.57 C ANISOU 2753 CA PHE A 296 12896 10733 14961 352 -1530 -294 C ATOM 2754 C PHE A 296 7.510 77.549 40.842 1.00104.03 C ANISOU 2754 C PHE A 296 13407 11008 15109 383 -1349 -290 C ATOM 2755 O PHE A 296 7.614 76.461 40.269 1.00105.97 O ANISOU 2755 O PHE A 296 13693 11141 15429 338 -1456 -441 O ATOM 2756 CB PHE A 296 6.886 79.441 39.321 1.00102.83 C ANISOU 2756 CB PHE A 296 13208 11112 14751 430 -1774 -351 C ATOM 2757 CG PHE A 296 5.806 80.177 38.562 1.00106.46 C ANISOU 2757 CG PHE A 296 13506 11592 15350 422 -2053 -399 C ATOM 2758 CD1 PHE A 296 5.198 79.602 37.452 1.00112.80 C ANISOU 2758 CD1 PHE A 296 14251 12330 16278 382 -2394 -602 C ATOM 2759 CD2 PHE A 296 5.416 81.455 38.941 1.00108.17 C ANISOU 2759 CD2 PHE A 296 13636 11888 15575 469 -1999 -255 C ATOM 2760 CE1 PHE A 296 4.203 80.285 36.748 1.00116.03 C ANISOU 2760 CE1 PHE A 296 14509 12760 16817 399 -2695 -653 C ATOM 2761 CE2 PHE A 296 4.424 82.140 38.234 1.00113.16 C ANISOU 2761 CE2 PHE A 296 14116 12531 16348 484 -2272 -293 C ATOM 2762 CZ PHE A 296 3.828 81.554 37.139 1.00114.23 C ANISOU 2762 CZ PHE A 296 14190 12612 16601 454 -2629 -488 C ATOM 2763 N ILE A 297 8.343 77.951 41.837 1.00 96.66 N ANISOU 2763 N ILE A 297 12599 10160 13966 471 -1095 -133 N ATOM 2764 CA ILE A 297 9.432 77.111 42.350 1.00 94.72 C ANISOU 2764 CA ILE A 297 12535 9886 13567 532 -929 -111 C ATOM 2765 C ILE A 297 8.794 75.872 43.002 1.00 99.43 C ANISOU 2765 C ILE A 297 13048 10215 14516 466 -764 -77 C ATOM 2766 O ILE A 297 9.215 74.762 42.685 1.00 99.58 O ANISOU 2766 O ILE A 297 13158 10123 14553 458 -783 -169 O ATOM 2767 CB ILE A 297 10.420 77.865 43.301 1.00 95.04 C ANISOU 2767 CB ILE A 297 12712 10078 13322 655 -746 29 C ATOM 2768 CG1 ILE A 297 11.139 79.020 42.567 1.00 93.61 C ANISOU 2768 CG1 ILE A 297 12602 10124 12841 700 -892 -10 C ATOM 2769 CG2 ILE A 297 11.451 76.904 43.926 1.00 95.16 C ANISOU 2769 CG2 ILE A 297 12893 10044 13220 740 -600 51 C ATOM 2770 CD1 ILE A 297 11.826 80.076 43.483 1.00 96.49 C ANISOU 2770 CD1 ILE A 297 13030 10620 13010 792 -758 108 C ATOM 2771 N TYR A 298 7.740 76.054 43.844 1.00 96.46 N ANISOU 2771 N TYR A 298 12493 9715 14443 416 -591 52 N ATOM 2772 CA TYR A 298 7.050 74.928 44.493 1.00 98.58 C ANISOU 2772 CA TYR A 298 12666 9698 15090 341 -381 116 C ATOM 2773 C TYR A 298 6.444 73.968 43.460 1.00106.46 C ANISOU 2773 C TYR A 298 13521 10513 16415 198 -606 -88 C ATOM 2774 O TYR A 298 6.511 72.753 43.640 1.00107.23 O ANISOU 2774 O TYR A 298 13644 10381 16716 151 -498 -101 O ATOM 2775 CB TYR A 298 5.921 75.365 45.458 1.00100.49 C ANISOU 2775 CB TYR A 298 12717 9837 15627 313 -122 291 C ATOM 2776 CG TYR A 298 6.085 76.631 46.280 1.00100.09 C ANISOU 2776 CG TYR A 298 12729 9972 15327 435 20 438 C ATOM 2777 CD1 TYR A 298 7.322 76.992 46.808 1.00 99.88 C ANISOU 2777 CD1 TYR A 298 12972 10111 14866 587 85 501 C ATOM 2778 CD2 TYR A 298 4.973 77.376 46.668 1.00101.37 C ANISOU 2778 CD2 TYR A 298 12673 10110 15733 407 121 516 C ATOM 2779 CE1 TYR A 298 7.465 78.125 47.610 1.00 99.20 C ANISOU 2779 CE1 TYR A 298 12949 10169 14573 699 202 610 C ATOM 2780 CE2 TYR A 298 5.102 78.509 47.469 1.00100.57 C ANISOU 2780 CE2 TYR A 298 12646 10154 15414 529 264 635 C ATOM 2781 CZ TYR A 298 6.350 78.882 47.935 1.00105.09 C ANISOU 2781 CZ TYR A 298 13502 10890 15537 672 295 675 C ATOM 2782 OH TYR A 298 6.473 79.996 48.729 1.00103.04 O ANISOU 2782 OH TYR A 298 13319 10756 15077 792 411 762 O ATOM 2783 N PHE A 299 5.851 74.523 42.383 1.00105.08 N ANISOU 2783 N PHE A 299 13207 10426 16292 139 -932 -251 N ATOM 2784 CA PHE A 299 5.187 73.758 41.330 1.00108.08 C ANISOU 2784 CA PHE A 299 13445 10650 16970 16 -1222 -486 C ATOM 2785 C PHE A 299 6.160 72.887 40.509 1.00112.81 C ANISOU 2785 C PHE A 299 14282 11253 17329 51 -1385 -672 C ATOM 2786 O PHE A 299 5.888 71.703 40.332 1.00114.31 O ANISOU 2786 O PHE A 299 14424 11194 17814 -38 -1413 -793 O ATOM 2787 CB PHE A 299 4.386 74.692 40.399 1.00110.53 C ANISOU 2787 CB PHE A 299 13582 11082 17331 -8 -1562 -605 C ATOM 2788 CG PHE A 299 3.583 73.963 39.344 1.00115.54 C ANISOU 2788 CG PHE A 299 14056 11557 18289 -121 -1919 -875 C ATOM 2789 CD1 PHE A 299 4.037 73.883 38.033 1.00119.13 C ANISOU 2789 CD1 PHE A 299 14694 12135 18436 -66 -2287 -1105 C ATOM 2790 CD2 PHE A 299 2.386 73.330 39.669 1.00120.90 C ANISOU 2790 CD2 PHE A 299 14403 11949 19586 -276 -1880 -909 C ATOM 2791 CE1 PHE A 299 3.306 73.191 37.062 1.00123.59 C ANISOU 2791 CE1 PHE A 299 15136 12549 19274 -151 -2657 -1388 C ATOM 2792 CE2 PHE A 299 1.656 72.636 38.698 1.00127.19 C ANISOU 2792 CE2 PHE A 299 15031 12580 20717 -385 -2250 -1194 C ATOM 2793 CZ PHE A 299 2.119 72.574 37.401 1.00125.67 C ANISOU 2793 CZ PHE A 299 15047 12523 20180 -315 -2658 -1443 C ATOM 2794 N PHE A 300 7.262 73.465 40.008 1.00108.60 N ANISOU 2794 N PHE A 300 13990 10979 16295 179 -1476 -700 N ATOM 2795 CA PHE A 300 8.218 72.768 39.145 1.00109.46 C ANISOU 2795 CA PHE A 300 14327 11122 16142 237 -1615 -881 C ATOM 2796 C PHE A 300 9.320 71.984 39.881 1.00113.62 C ANISOU 2796 C PHE A 300 15036 11584 16550 316 -1348 -794 C ATOM 2797 O PHE A 300 10.022 71.208 39.227 1.00114.58 O ANISOU 2797 O PHE A 300 15315 11669 16554 356 -1434 -957 O ATOM 2798 CB PHE A 300 8.877 73.764 38.173 1.00110.12 C ANISOU 2798 CB PHE A 300 14575 11502 15762 342 -1802 -942 C ATOM 2799 CG PHE A 300 7.972 74.185 37.041 1.00114.20 C ANISOU 2799 CG PHE A 300 15009 12063 16320 305 -2165 -1108 C ATOM 2800 CD1 PHE A 300 7.215 75.347 37.129 1.00117.63 C ANISOU 2800 CD1 PHE A 300 15284 12592 16819 293 -2235 -1004 C ATOM 2801 CD2 PHE A 300 7.866 73.414 35.889 1.00119.19 C ANISOU 2801 CD2 PHE A 300 15734 12635 16918 302 -2456 -1381 C ATOM 2802 CE1 PHE A 300 6.374 75.735 36.081 1.00120.80 C ANISOU 2802 CE1 PHE A 300 15614 13031 17254 286 -2604 -1155 C ATOM 2803 CE2 PHE A 300 7.021 73.800 34.844 1.00124.37 C ANISOU 2803 CE2 PHE A 300 16337 13335 17584 296 -2836 -1547 C ATOM 2804 CZ PHE A 300 6.279 74.956 34.949 1.00122.20 C ANISOU 2804 CZ PHE A 300 15896 13157 17378 291 -2915 -1426 C ATOM 2805 N LEU A 301 9.478 72.156 41.209 1.00109.00 N ANISOU 2805 N LEU A 301 14447 10981 15988 358 -1040 -551 N ATOM 2806 CA LEU A 301 10.552 71.475 41.942 1.00107.97 C ANISOU 2806 CA LEU A 301 14504 10803 15718 469 -821 -458 C ATOM 2807 C LEU A 301 10.065 70.528 43.048 1.00113.52 C ANISOU 2807 C LEU A 301 15163 11209 16762 430 -555 -308 C ATOM 2808 O LEU A 301 10.851 69.704 43.522 1.00113.53 O ANISOU 2808 O LEU A 301 15329 11107 16702 520 -421 -265 O ATOM 2809 CB LEU A 301 11.507 72.513 42.528 1.00105.24 C ANISOU 2809 CB LEU A 301 14273 10713 15000 609 -707 -308 C ATOM 2810 CG LEU A 301 12.880 72.624 41.879 1.00108.82 C ANISOU 2810 CG LEU A 301 14902 11358 15086 726 -793 -411 C ATOM 2811 CD1 LEU A 301 12.790 72.875 40.379 1.00109.30 C ANISOU 2811 CD1 LEU A 301 14967 11542 15020 684 -1056 -610 C ATOM 2812 CD2 LEU A 301 13.675 73.721 42.525 1.00109.49 C ANISOU 2812 CD2 LEU A 301 15046 11656 14901 840 -684 -268 C ATOM 2813 N CYS A 302 8.794 70.630 43.450 1.00111.45 N ANISOU 2813 N CYS A 302 14683 10798 16864 309 -461 -220 N ATOM 2814 CA CYS A 302 8.214 69.742 44.450 1.00113.60 C ANISOU 2814 CA CYS A 302 14905 10761 17498 260 -162 -57 C ATOM 2815 C CYS A 302 7.124 68.892 43.775 1.00120.13 C ANISOU 2815 C CYS A 302 15499 11297 18848 59 -286 -225 C ATOM 2816 O CYS A 302 6.141 69.430 43.252 1.00120.42 O ANISOU 2816 O CYS A 302 15286 11351 19118 -60 -452 -315 O ATOM 2817 CB CYS A 302 7.682 70.529 45.646 1.00113.82 C ANISOU 2817 CB CYS A 302 14871 10823 17550 297 129 205 C ATOM 2818 SG CYS A 302 7.008 69.502 46.980 1.00121.13 S ANISOU 2818 SG CYS A 302 15773 11366 18884 262 582 460 S ATOM 2819 N LYS A 303 7.348 67.563 43.735 1.00118.26 N ANISOU 2819 N LYS A 303 15344 10786 18805 29 -234 -285 N ATOM 2820 CA LYS A 303 6.452 66.585 43.114 1.00121.21 C ANISOU 2820 CA LYS A 303 15518 10832 19704 -162 -359 -475 C ATOM 2821 C LYS A 303 5.107 66.501 43.851 1.00126.63 C ANISOU 2821 C LYS A 303 15904 11260 20948 -320 -112 -318 C ATOM 2822 O LYS A 303 4.064 66.554 43.197 1.00128.41 O ANISOU 2822 O LYS A 303 15832 11380 21580 -490 -326 -496 O ATOM 2823 CB LYS A 303 7.117 65.202 43.056 1.00125.29 C ANISOU 2823 CB LYS A 303 16225 11092 20287 -132 -302 -541 C ATOM 2824 N SER A 304 5.129 66.392 45.201 1.00122.43 N ANISOU 2824 N SER A 304 15453 10630 20434 -251 334 11 N ATOM 2825 CA SER A 304 3.921 66.300 46.031 1.00124.76 C ANISOU 2825 CA SER A 304 15493 10673 21236 -376 672 210 C ATOM 2826 C SER A 304 3.073 67.578 45.953 1.00126.94 C ANISOU 2826 C SER A 304 15500 11155 21576 -423 587 206 C ATOM 2827 O SER A 304 1.848 67.487 46.066 1.00129.13 O ANISOU 2827 O SER A 304 15434 11216 22414 -589 689 219 O ATOM 2828 CB SER A 304 4.267 65.973 47.481 1.00129.02 C ANISOU 2828 CB SER A 304 16268 11108 21644 -233 1173 575 C ATOM 2829 OG SER A 304 5.296 66.803 47.994 1.00136.89 O ANISOU 2829 OG SER A 304 17542 12460 22011 -3 1192 695 O ATOM 2830 N PHE A 305 3.714 68.753 45.725 1.00119.40 N ANISOU 2830 N PHE A 305 14682 10597 20087 -279 399 181 N ATOM 2831 CA PHE A 305 3.018 70.033 45.555 1.00118.01 C ANISOU 2831 CA PHE A 305 14290 10633 19916 -293 281 167 C ATOM 2832 C PHE A 305 2.290 70.047 44.203 1.00124.24 C ANISOU 2832 C PHE A 305 14803 11400 21003 -445 -173 -144 C ATOM 2833 O PHE A 305 1.111 70.405 44.158 1.00126.15 O ANISOU 2833 O PHE A 305 14699 11566 21667 -555 -197 -161 O ATOM 2834 CB PHE A 305 3.995 71.227 45.661 1.00115.20 C ANISOU 2834 CB PHE A 305 14186 10671 18915 -98 204 221 C ATOM 2835 CG PHE A 305 3.347 72.595 45.647 1.00115.21 C ANISOU 2835 CG PHE A 305 14008 10872 18895 -84 143 252 C ATOM 2836 CD1 PHE A 305 3.022 73.239 46.832 1.00117.66 C ANISOU 2836 CD1 PHE A 305 14308 11202 19195 -6 505 497 C ATOM 2837 CD2 PHE A 305 3.085 73.249 44.447 1.00116.55 C ANISOU 2837 CD2 PHE A 305 14049 11205 19028 -124 -278 37 C ATOM 2838 CE1 PHE A 305 2.413 74.498 46.819 1.00117.56 C ANISOU 2838 CE1 PHE A 305 14130 11355 19183 19 454 516 C ATOM 2839 CE2 PHE A 305 2.477 74.508 44.435 1.00118.46 C ANISOU 2839 CE2 PHE A 305 14133 11612 19265 -95 -337 76 C ATOM 2840 CZ PHE A 305 2.147 75.124 45.622 1.00116.16 C ANISOU 2840 CZ PHE A 305 13807 11325 19003 -28 30 310 C ATOM 2841 N ARG A 306 2.998 69.660 43.115 1.00120.37 N ANISOU 2841 N ARG A 306 14474 10982 20280 -430 -535 -395 N ATOM 2842 CA ARG A 306 2.492 69.622 41.740 1.00122.34 C ANISOU 2842 CA ARG A 306 14560 11237 20688 -526 -1022 -723 C ATOM 2843 C ARG A 306 1.278 68.687 41.603 1.00133.05 C ANISOU 2843 C ARG A 306 15560 12205 22788 -744 -1057 -850 C ATOM 2844 O ARG A 306 0.314 69.050 40.928 1.00135.15 O ANISOU 2844 O ARG A 306 15522 12460 23370 -839 -1362 -1025 O ATOM 2845 CB ARG A 306 3.614 69.202 40.775 1.00120.96 C ANISOU 2845 CB ARG A 306 14700 11182 20076 -436 -1299 -937 C ATOM 2846 CG ARG A 306 3.243 69.258 39.288 1.00132.58 C ANISOU 2846 CG ARG A 306 16103 12711 21561 -479 -1827 -1286 C ATOM 2847 CD ARG A 306 4.440 69.496 38.379 1.00142.61 C ANISOU 2847 CD ARG A 306 17730 14256 22199 -318 -2047 -1421 C ATOM 2848 NE ARG A 306 5.532 68.545 38.609 1.00152.67 N ANISOU 2848 NE ARG A 306 19273 15442 23294 -253 -1867 -1416 N ATOM 2849 CZ ARG A 306 6.786 68.728 38.205 1.00167.63 C ANISOU 2849 CZ ARG A 306 21479 17560 24653 -95 -1909 -1460 C ATOM 2850 NH1 ARG A 306 7.126 69.830 37.546 1.00155.09 N ANISOU 2850 NH1 ARG A 306 19995 16290 22641 5 -2100 -1497 N ATOM 2851 NH2 ARG A 306 7.711 67.813 38.461 1.00155.35 N ANISOU 2851 NH2 ARG A 306 20127 15897 23000 -30 -1742 -1458 N ATOM 2852 N ASN A 307 1.320 67.506 42.253 1.00132.52 N ANISOU 2852 N ASN A 307 15522 11808 23022 -818 -751 -760 N ATOM 2853 CA ASN A 307 0.241 66.513 42.211 1.00137.35 C ANISOU 2853 CA ASN A 307 15798 11992 24396 -1043 -721 -862 C ATOM 2854 C ASN A 307 -1.003 66.990 42.979 1.00143.87 C ANISOU 2854 C ASN A 307 16226 12696 25744 -1152 -442 -675 C ATOM 2855 O ASN A 307 -2.120 66.742 42.520 1.00147.49 O ANISOU 2855 O ASN A 307 16277 12934 26829 -1337 -628 -857 O ATOM 2856 CB ASN A 307 0.724 65.162 42.755 1.00138.58 C ANISOU 2856 CB ASN A 307 16138 11819 24697 -1070 -410 -765 C ATOM 2857 CG ASN A 307 1.865 64.539 41.978 1.00156.14 C ANISOU 2857 CG ASN A 307 18710 14103 26512 -971 -669 -977 C ATOM 2858 OD1 ASN A 307 2.074 64.799 40.784 1.00146.54 O ANISOU 2858 OD1 ASN A 307 17545 13078 25054 -940 -1139 -1283 O ATOM 2859 ND2 ASN A 307 2.627 63.684 42.644 1.00148.80 N ANISOU 2859 ND2 ASN A 307 18043 13005 25489 -899 -354 -811 N ATOM 2860 N SER A 308 -0.810 67.676 44.129 1.00138.36 N ANISOU 2860 N SER A 308 15639 12138 24794 -1026 -8 -330 N ATOM 2861 CA SER A 308 -1.892 68.213 44.963 1.00140.14 C ANISOU 2861 CA SER A 308 15537 12276 25434 -1086 332 -120 C ATOM 2862 C SER A 308 -2.645 69.340 44.243 1.00144.58 C ANISOU 2862 C SER A 308 15801 13059 26074 -1097 -41 -285 C ATOM 2863 O SER A 308 -3.876 69.383 44.301 1.00147.35 O ANISOU 2863 O SER A 308 15704 13224 27058 -1238 9 -305 O ATOM 2864 CB SER A 308 -1.345 68.723 46.292 1.00141.12 C ANISOU 2864 CB SER A 308 15943 12530 25145 -902 845 255 C ATOM 2865 OG SER A 308 -0.689 67.702 47.023 1.00150.12 O ANISOU 2865 OG SER A 308 17368 13458 26213 -863 1193 435 O ATOM 2866 N LEU A 309 -1.900 70.244 43.567 1.00138.33 N ANISOU 2866 N LEU A 309 15251 12649 24659 -942 -403 -395 N ATOM 2867 CA LEU A 309 -2.448 71.369 42.807 1.00138.32 C ANISOU 2867 CA LEU A 309 15050 12879 24624 -910 -791 -538 C ATOM 2868 C LEU A 309 -3.199 70.871 41.562 1.00146.96 C ANISOU 2868 C LEU A 309 15849 13828 26160 -1058 -1318 -902 C ATOM 2869 O LEU A 309 -4.245 71.430 41.225 1.00149.10 O ANISOU 2869 O LEU A 309 15750 14102 26800 -1106 -1536 -996 O ATOM 2870 CB LEU A 309 -1.334 72.355 42.412 1.00133.81 C ANISOU 2870 CB LEU A 309 14865 12716 23258 -704 -992 -535 C ATOM 2871 N ILE A 310 -2.679 69.810 40.899 1.00145.23 N ANISOU 2871 N ILE A 310 15792 13472 25916 -1117 -1535 -1117 N ATOM 2872 CA ILE A 310 -3.294 69.198 39.714 1.00149.15 C ANISOU 2872 CA ILE A 310 16064 13806 26799 -1246 -2061 -1504 C ATOM 2873 C ILE A 310 -4.604 68.487 40.091 1.00159.52 C ANISOU 2873 C ILE A 310 16856 14699 29055 -1485 -1920 -1537 C ATOM 2874 O ILE A 310 -5.555 68.522 39.307 1.00162.34 O ANISOU 2874 O ILE A 310 16848 14963 29871 -1587 -2355 -1816 O ATOM 2875 CB ILE A 310 -2.320 68.225 39.013 1.00151.74 C ANISOU 2875 CB ILE A 310 16750 14091 26812 -1223 -2276 -1721 C ATOM 2876 N SER A 311 -4.651 67.863 41.293 1.00157.06 N ANISOU 2876 N SER A 311 16511 14127 29036 -1564 -1311 -1249 N ATOM 2877 CA SER A 311 -5.815 67.143 41.823 1.00161.95 C ANISOU 2877 CA SER A 311 16653 14311 30571 -1796 -1033 -1210 C ATOM 2878 C SER A 311 -6.963 68.095 42.218 1.00167.73 C ANISOU 2878 C SER A 311 16930 15084 31714 -1822 -916 -1098 C ATOM 2879 O SER A 311 -8.124 67.673 42.207 1.00172.76 O ANISOU 2879 O SER A 311 17046 15403 33191 -2025 -921 -1203 O ATOM 2880 CB SER A 311 -5.412 66.293 43.024 1.00165.41 C ANISOU 2880 CB SER A 311 17279 14489 31082 -1825 -369 -882 C ATOM 2881 OG SER A 311 -6.486 65.486 43.476 1.00177.33 O ANISOU 2881 OG SER A 311 18347 15531 33501 -2064 -71 -842 O ATOM 2882 N MET A 312 -6.641 69.361 42.569 1.00158.68 N ANISOU 2882 N MET A 312 15966 14309 30018 -1618 -806 -896 N ATOM 2883 CA MET A 312 -7.619 70.378 42.968 1.00183.06 C ANISOU 2883 CA MET A 312 18681 17472 33400 -1594 -679 -777 C ATOM 2884 C MET A 312 -8.396 70.909 41.758 1.00207.05 C ANISOU 2884 C MET A 312 22067 21305 35296 -1629 -1181 -989 C ATOM 2885 O MET A 312 -7.816 71.188 40.710 1.00158.72 O ANISOU 2885 O MET A 312 15507 14718 30080 -1517 -1896 -1347 O ATOM 2886 CB MET A 312 -6.929 71.539 43.703 1.00180.50 C ANISOU 2886 CB MET A 312 18712 17506 32362 -1354 -394 -488 C TER 2887 MET A 312 HETATM 2888 CAA AZJ A1201 15.921 94.175 57.389 1.00 85.43 C HETATM 2889 CAB AZJ A1201 13.771 100.339 55.769 1.00 84.96 C HETATM 2890 NAC AZJ A1201 18.732 97.525 52.124 1.00 87.26 N HETATM 2891 OAD AZJ A1201 19.314 103.057 48.946 1.00103.04 O HETATM 2892 OAE AZJ A1201 13.955 97.948 57.289 1.00 87.05 O HETATM 2893 OAF AZJ A1201 17.219 106.038 46.455 1.00112.02 O HETATM 2894 OAG AZJ A1201 19.154 105.981 48.045 1.00111.85 O HETATM 2895 CAH AZJ A1201 17.880 97.980 52.757 1.00 86.65 C HETATM 2896 CAI AZJ A1201 17.564 101.563 43.169 1.00102.56 C HETATM 2897 CAJ AZJ A1201 18.081 102.779 42.715 1.00102.93 C HETATM 2898 CAK AZJ A1201 17.619 101.249 44.531 1.00102.88 C HETATM 2899 CAL AZJ A1201 18.656 103.676 43.624 1.00104.09 C HETATM 2900 CAM AZJ A1201 18.188 102.148 45.439 1.00104.19 C HETATM 2901 CAN AZJ A1201 16.367 97.888 54.670 1.00 85.15 C HETATM 2902 CAO AZJ A1201 15.031 95.287 56.826 1.00 86.46 C HETATM 2903 CAP AZJ A1201 17.038 102.905 51.108 1.00 93.81 C HETATM 2904 CAQ AZJ A1201 17.577 100.787 49.712 1.00 96.16 C HETATM 2905 CAR AZJ A1201 16.174 102.007 51.996 1.00 92.57 C HETATM 2906 CAS AZJ A1201 16.673 99.984 50.671 1.00 93.23 C HETATM 2907 CAT AZJ A1201 19.319 104.282 45.881 1.00109.52 C HETATM 2908 NAU AZJ A1201 15.254 100.295 53.982 1.00 85.89 N HETATM 2909 NAV AZJ A1201 17.427 104.047 48.091 1.00107.99 N HETATM 2910 OAW AZJ A1201 15.714 96.552 56.895 1.00 87.84 O HETATM 2911 CAX AZJ A1201 18.087 103.156 48.854 1.00102.97 C HETATM 2912 CAY AZJ A1201 14.935 97.644 56.605 1.00 87.30 C HETATM 2913 CAZ AZJ A1201 14.798 99.668 55.091 1.00 86.56 C HETATM 2914 CBA AZJ A1201 18.684 103.383 44.996 1.00106.06 C HETATM 2915 CBB AZJ A1201 16.814 98.566 53.536 1.00 85.79 C HETATM 2916 CBC AZJ A1201 15.350 98.411 55.485 1.00 86.79 C HETATM 2917 CBD AZJ A1201 16.213 99.786 53.177 1.00 87.10 C HETATM 2918 CBE AZJ A1201 17.143 102.292 49.698 1.00 97.63 C HETATM 2919 NBF AZJ A1201 16.703 100.604 52.028 1.00 90.82 N HETATM 2920 SBG AZJ A1201 18.251 105.128 47.141 1.00111.75 S HETATM 2921 C1 CLR A1202 9.688 103.536 31.531 1.00126.16 C HETATM 2922 C2 CLR A1202 9.622 105.067 31.386 1.00125.97 C HETATM 2923 C3 CLR A1202 8.223 105.640 31.630 1.00125.77 C HETATM 2924 C4 CLR A1202 7.673 105.179 32.985 1.00126.25 C HETATM 2925 C5 CLR A1202 7.833 103.675 33.191 1.00126.50 C HETATM 2926 C6 CLR A1202 6.772 103.021 33.709 1.00126.78 C HETATM 2927 C7 CLR A1202 6.497 101.574 33.363 1.00126.64 C HETATM 2928 C8 CLR A1202 7.783 100.760 33.502 1.00126.61 C HETATM 2929 C9 CLR A1202 8.909 101.405 32.647 1.00126.54 C HETATM 2930 C10 CLR A1202 9.140 102.939 32.848 1.00126.25 C HETATM 2931 C11 CLR A1202 10.179 100.517 32.529 1.00126.88 C HETATM 2932 C12 CLR A1202 9.950 98.994 32.374 1.00127.07 C HETATM 2933 C13 CLR A1202 8.851 98.394 33.278 1.00127.26 C HETATM 2934 C14 CLR A1202 7.607 99.275 33.102 1.00126.87 C HETATM 2935 C15 CLR A1202 6.391 98.460 33.540 1.00126.54 C HETATM 2936 C16 CLR A1202 6.768 97.037 33.123 1.00127.23 C HETATM 2937 C17 CLR A1202 8.273 97.050 32.786 1.00128.18 C HETATM 2938 C18 CLR A1202 9.351 98.269 34.734 1.00126.65 C HETATM 2939 C19 CLR A1202 10.136 103.210 33.986 1.00126.06 C HETATM 2940 C20 CLR A1202 9.106 95.761 33.004 1.00129.65 C HETATM 2941 C21 CLR A1202 9.842 95.307 31.738 1.00130.11 C HETATM 2942 C22 CLR A1202 8.516 94.628 33.861 1.00129.97 C HETATM 2943 C23 CLR A1202 7.915 93.457 33.082 1.00130.92 C HETATM 2944 C24 CLR A1202 7.613 92.264 33.995 1.00131.71 C HETATM 2945 C25 CLR A1202 8.009 90.877 33.470 1.00131.57 C HETATM 2946 C26 CLR A1202 7.547 90.537 32.052 1.00131.48 C HETATM 2947 C27 CLR A1202 9.463 90.501 33.744 1.00131.27 C HETATM 2948 O1 CLR A1202 8.276 107.075 31.594 1.00124.67 O HETATM 2949 C1 CLR A1203 28.215 76.122 50.652 1.00140.66 C HETATM 2950 C2 CLR A1203 27.915 74.615 50.521 1.00140.52 C HETATM 2951 C3 CLR A1203 27.720 74.111 49.082 1.00139.67 C HETATM 2952 C4 CLR A1203 28.791 74.633 48.118 1.00139.34 C HETATM 2953 C5 CLR A1203 29.127 76.102 48.348 1.00139.34 C HETATM 2954 C6 CLR A1203 29.219 76.871 47.241 1.00138.45 C HETATM 2955 C7 CLR A1203 29.132 78.382 47.296 1.00138.23 C HETATM 2956 C8 CLR A1203 29.909 78.895 48.508 1.00138.54 C HETATM 2957 C9 CLR A1203 29.354 78.219 49.790 1.00139.84 C HETATM 2958 C10 CLR A1203 29.362 76.659 49.766 1.00140.41 C HETATM 2959 C11 CLR A1203 29.794 78.883 51.125 1.00140.07 C HETATM 2960 C12 CLR A1203 30.085 80.402 51.132 1.00139.35 C HETATM 2961 C13 CLR A1203 30.669 80.989 49.837 1.00138.13 C HETATM 2962 C14 CLR A1203 29.849 80.426 48.675 1.00138.27 C HETATM 2963 C15 CLR A1203 30.005 81.367 47.485 1.00138.64 C HETATM 2964 C16 CLR A1203 30.143 82.736 48.155 1.00138.75 C HETATM 2965 C17 CLR A1203 30.359 82.481 49.657 1.00138.37 C HETATM 2966 C18 CLR A1203 32.184 80.730 49.727 1.00137.45 C HETATM 2967 C19 CLR A1203 30.713 76.132 50.284 1.00140.99 C HETATM 2968 C20 CLR A1203 31.120 83.527 50.503 1.00138.26 C HETATM 2969 C21 CLR A1203 30.166 84.159 51.516 1.00138.41 C HETATM 2970 C22 CLR A1203 31.911 84.574 49.706 1.00137.91 C HETATM 2971 C23 CLR A1203 32.885 85.410 50.538 1.00137.53 C HETATM 2972 C24 CLR A1203 33.445 86.565 49.700 1.00136.89 C HETATM 2973 C25 CLR A1203 33.373 87.961 50.330 1.00136.40 C HETATM 2974 C26 CLR A1203 31.963 88.496 50.589 1.00136.02 C HETATM 2975 C27 CLR A1203 34.342 88.189 51.489 1.00136.37 C HETATM 2976 O1 CLR A1203 27.766 72.678 49.077 1.00139.18 O HETATM 2977 C10 OLC A1204 15.520 91.489 34.081 1.00120.19 C HETATM 2978 C9 OLC A1204 16.508 90.796 34.647 1.00120.64 C HETATM 2979 C8 OLC A1204 17.898 90.811 34.049 1.00120.64 C HETATM 2980 C24 OLC A1204 20.249 102.866 35.969 1.00130.94 C HETATM 2981 C7 OLC A1204 18.899 91.374 35.056 1.00120.59 C HETATM 2982 C6 OLC A1204 19.733 92.503 34.453 1.00120.66 C HETATM 2983 C5 OLC A1204 20.452 93.306 35.533 1.00120.89 C HETATM 2984 C4 OLC A1204 20.985 94.630 34.999 1.00121.07 C HETATM 2985 C3 OLC A1204 20.533 95.798 35.868 1.00121.81 C HETATM 2986 C2 OLC A1204 19.541 96.676 35.110 1.00123.86 C HETATM 2987 C21 OLC A1204 19.410 100.566 35.423 1.00129.19 C HETATM 2988 C1 OLC A1204 19.395 98.034 35.761 1.00126.30 C HETATM 2989 C22 OLC A1204 20.653 101.445 35.573 1.00130.78 C HETATM 2990 O19 OLC A1204 18.939 98.116 36.893 1.00126.73 O HETATM 2991 O25 OLC A1204 21.377 103.612 36.452 1.00130.40 O HETATM 2992 O23 OLC A1204 21.526 100.891 36.568 1.00131.68 O HETATM 2993 O20 OLC A1204 19.787 99.240 35.027 1.00128.04 O HETATM 2994 C10 OLC A1205 32.680 81.915 54.464 1.00130.64 C HETATM 2995 C9 OLC A1205 31.498 81.319 54.692 1.00132.03 C HETATM 2996 C11 OLC A1205 32.884 83.362 54.063 1.00128.88 C HETATM 2997 C8 OLC A1205 30.131 81.974 54.594 1.00132.60 C HETATM 2998 C24 OLC A1205 22.003 72.736 54.852 1.00130.73 C HETATM 2999 C12 OLC A1205 34.345 83.570 53.679 1.00127.51 C HETATM 3000 C7 OLC A1205 29.057 80.890 54.669 1.00132.65 C HETATM 3001 C13 OLC A1205 34.769 85.024 53.851 1.00126.70 C HETATM 3002 C6 OLC A1205 27.649 81.449 54.490 1.00132.40 C HETATM 3003 C14 OLC A1205 36.137 85.285 53.229 1.00126.02 C HETATM 3004 C5 OLC A1205 26.662 80.342 54.119 1.00132.53 C HETATM 3005 C4 OLC A1205 25.720 79.991 55.269 1.00132.22 C HETATM 3006 C3 OLC A1205 24.626 79.023 54.824 1.00131.90 C HETATM 3007 C2 OLC A1205 24.658 77.730 55.640 1.00132.33 C HETATM 3008 C21 OLC A1205 22.340 75.206 54.500 1.00132.27 C HETATM 3009 C1 OLC A1205 24.488 76.499 54.769 1.00133.45 C HETATM 3010 C22 OLC A1205 22.262 73.836 53.824 1.00131.34 C HETATM 3011 O19 OLC A1205 25.122 76.372 53.730 1.00135.01 O HETATM 3012 O25 OLC A1205 20.628 72.730 55.256 1.00130.39 O HETATM 3013 O23 OLC A1205 21.218 73.839 52.837 1.00130.60 O HETATM 3014 O20 OLC A1205 23.589 75.419 55.169 1.00132.76 O HETATM 3015 O HOH A1301 31.472 37.436 15.554 1.00 74.75 O HETATM 3016 O HOH A1302 30.019 36.647 13.370 1.00 76.02 O HETATM 3017 O HOH A1303 21.809 81.992 53.098 1.00 86.09 O HETATM 3018 O HOH A1304 22.273 84.334 54.251 1.00103.98 O HETATM 3019 O HOH A1305 20.482 50.029 21.830 1.00 99.78 O HETATM 3020 O HOH A1306 28.887 52.230 24.078 1.00 66.64 O HETATM 3021 O HOH A1307 13.715 78.226 33.605 1.00100.79 O HETATM 3022 O HOH A1308 19.662 109.642 48.337 1.00106.64 O HETATM 3023 O HOH A1309 31.288 62.258 12.396 1.00 81.50 O HETATM 3024 O HOH A1310 7.485 111.202 33.845 1.00 79.11 O HETATM 3025 O HOH A1311 21.214 105.540 50.317 1.00 99.50 O HETATM 3026 O HOH A1312 20.953 73.120 58.097 1.00102.90 O CONECT 14 2553 CONECT 2553 14 CONECT 2888 2902 CONECT 2889 2913 CONECT 2890 2895 CONECT 2891 2911 CONECT 2892 2912 CONECT 2893 2920 CONECT 2894 2920 CONECT 2895 2890 2915 CONECT 2896 2897 2898 CONECT 2897 2896 2899 CONECT 2898 2896 2900 CONECT 2899 2897 2914 CONECT 2900 2898 2914 CONECT 2901 2915 2916 CONECT 2902 2888 2910 CONECT 2903 2905 2918 CONECT 2904 2906 2918 CONECT 2905 2903 2919 CONECT 2906 2904 2919 CONECT 2907 2914 2920 CONECT 2908 2913 2917 CONECT 2909 2911 2920 CONECT 2910 2902 2912 CONECT 2911 2891 2909 2918 CONECT 2912 2892 2910 2916 CONECT 2913 2889 2908 2916 CONECT 2914 2899 2900 2907 CONECT 2915 2895 2901 2917 CONECT 2916 2901 2912 2913 CONECT 2917 2908 2915 2919 CONECT 2918 2903 2904 2911 CONECT 2919 2905 2906 2917 CONECT 2920 2893 2894 2907 2909 CONECT 2921 2922 2930 CONECT 2922 2921 2923 CONECT 2923 2922 2924 2948 CONECT 2924 2923 2925 CONECT 2925 2924 2926 2930 CONECT 2926 2925 2927 CONECT 2927 2926 2928 CONECT 2928 2927 2929 2934 CONECT 2929 2928 2930 2931 CONECT 2930 2921 2925 2929 2939 CONECT 2931 2929 2932 CONECT 2932 2931 2933 CONECT 2933 2932 2934 2937 2938 CONECT 2934 2928 2933 2935 CONECT 2935 2934 2936 CONECT 2936 2935 2937 CONECT 2937 2933 2936 2940 CONECT 2938 2933 CONECT 2939 2930 CONECT 2940 2937 2941 2942 CONECT 2941 2940 CONECT 2942 2940 2943 CONECT 2943 2942 2944 CONECT 2944 2943 2945 CONECT 2945 2944 2946 2947 CONECT 2946 2945 CONECT 2947 2945 CONECT 2948 2923 CONECT 2949 2950 2958 CONECT 2950 2949 2951 CONECT 2951 2950 2952 2976 CONECT 2952 2951 2953 CONECT 2953 2952 2954 2958 CONECT 2954 2953 2955 CONECT 2955 2954 2956 CONECT 2956 2955 2957 2962 CONECT 2957 2956 2958 2959 CONECT 2958 2949 2953 2957 2967 CONECT 2959 2957 2960 CONECT 2960 2959 2961 CONECT 2961 2960 2962 2965 2966 CONECT 2962 2956 2961 2963 CONECT 2963 2962 2964 CONECT 2964 2963 2965 CONECT 2965 2961 2964 2968 CONECT 2966 2961 CONECT 2967 2958 CONECT 2968 2965 2969 2970 CONECT 2969 2968 CONECT 2970 2968 2971 CONECT 2971 2970 2972 CONECT 2972 2971 2973 CONECT 2973 2972 2974 2975 CONECT 2974 2973 CONECT 2975 2973 CONECT 2976 2951 CONECT 2977 2978 CONECT 2978 2977 2979 CONECT 2979 2978 2981 CONECT 2980 2989 2991 CONECT 2981 2979 2982 CONECT 2982 2981 2983 CONECT 2983 2982 2984 CONECT 2984 2983 2985 CONECT 2985 2984 2986 CONECT 2986 2985 2988 CONECT 2987 2989 2993 CONECT 2988 2986 2990 2993 CONECT 2989 2980 2987 2992 CONECT 2990 2988 CONECT 2991 2980 CONECT 2992 2989 CONECT 2993 2987 2988 CONECT 2994 2995 2996 CONECT 2995 2994 2997 CONECT 2996 2994 2999 CONECT 2997 2995 3000 CONECT 2998 3010 3012 CONECT 2999 2996 3001 CONECT 3000 2997 3002 CONECT 3001 2999 3003 CONECT 3002 3000 3004 CONECT 3003 3001 CONECT 3004 3002 3005 CONECT 3005 3004 3006 CONECT 3006 3005 3007 CONECT 3007 3006 3009 CONECT 3008 3010 3014 CONECT 3009 3007 3011 3014 CONECT 3010 2998 3008 3013 CONECT 3011 3009 CONECT 3012 2998 CONECT 3013 3010 CONECT 3014 3008 3009 MASTER 451 0 5 18 0 0 9 6 3025 1 129 36 END