HEADER TRANSPORT PROTEIN/INHIBITOR 16-JAN-15 4XNV TITLE THE HUMAN P2Y1 RECEPTOR IN COMPLEX WITH BPTU COMPND MOL_ID: 1; COMPND 2 MOLECULE: P2Y PURINOCEPTOR 1, RUBREDOXIN, P2Y PURINOCEPTOR 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: P2Y1, ATP RECEPTOR, PURINERGIC RECEPTOR; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 OTHER_DETAILS: CHIMERA PROTEIN OF P2Y PURINOCEPTOR 1 (P2RY1_HUMA) COMPND 8 WITH RUBREDOXIN (RUBR_CLOPA) INSERTED INTO ICL3 DOMAIN BETWEEN COMPND 9 RESIDUES 247LYS AND 253PRO, AND REPLACED RESIDUES 248ASN TO 252SER. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, CLOSTRIDIUM PASTEURIANUM; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 1501; SOURCE 5 GENE: P2RY1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7106; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS HUMAN P2Y1 RECEPTOR, G PROTEIN COUPLED RECEPTOR, PLATELET ACTIVATION, KEYWDS 2 MEMBRANE PROTEIN, INHIBITOR COMPLEX, TRANSPORT PROTEIN-INHIBITOR KEYWDS 3 COMPLEX, PSI-BIOLOGY, STRUCTURAL GENOMICS, GPCR NETWORK, GPCR EXPDTA X-RAY DIFFRACTION AUTHOR D.ZHANG,Z.GAO,K.JACOBSON,G.W.HAN,R.STEVENS,Q.ZHAO,B.WU,GPCR NETWORK AUTHOR 2 (GPCR) REVDAT 4 05-FEB-20 4XNV 1 SOURCE KEYWDS AUTHOR JRNL REVDAT 4 2 1 REMARK REVDAT 3 29-APR-15 4XNV 1 KEYWDS REVDAT 2 22-APR-15 4XNV 1 JRNL REVDAT 1 01-APR-15 4XNV 0 JRNL AUTH D.ZHANG,Z.G.GAO,K.ZHANG,E.KISELEV,S.CRANE,J.WANG,S.PAOLETTA, JRNL AUTH 2 C.YI,L.MA,W.ZHANG,G.W.HAN,H.LIU,V.CHEREZOV,V.KATRITCH, JRNL AUTH 3 H.JIANG,R.C.STEVENS,K.A.JACOBSON,Q.ZHAO,B.WU JRNL TITL TWO DISPARATE LIGAND-BINDING SITES IN THE HUMAN P2Y1 JRNL TITL 2 RECEPTOR JRNL REF NATURE V. 520 317 2015 JRNL REFN ESSN 1476-4687 JRNL PMID 25822790 JRNL DOI 10.1038/NATURE14287 REMARK 2 REMARK 2 RESOLUTION. 2.20 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.40 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 19881 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) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.207 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 1017 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) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.32 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2887 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3667 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2754 REMARK 3 BIN R VALUE (WORKING SET) : 0.3661 REMARK 3 BIN FREE R VALUE : 0.3786 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.61 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133 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 : 2713 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 371 REMARK 3 SOLVENT ATOMS : 30 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 42.95 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.52040 REMARK 3 B22 (A**2) : -2.52040 REMARK 3 B33 (A**2) : 5.04090 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.369 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.265 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.190 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.293 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.200 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 : 0.941 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3164 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4262 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1126 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 38 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 440 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3164 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 406 ; 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 : 3716 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.04 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.19 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.56 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|39 - A|334 } REMARK 3 ORIGIN FOR THE GROUP (A): -11.1074 17.9445 9.7233 REMARK 3 T TENSOR REMARK 3 T11: -0.1738 T22: -0.1537 REMARK 3 T33: -0.0538 T12: 0.0229 REMARK 3 T13: 0.0008 T23: -0.0413 REMARK 3 L TENSOR REMARK 3 L11: 1.7026 L22: 2.2469 REMARK 3 L33: 1.0152 L12: 0.0833 REMARK 3 L13: 0.3764 L23: 0.0550 REMARK 3 S TENSOR REMARK 3 S11: 0.0034 S12: -0.2893 S13: 0.2711 REMARK 3 S21: 0.2173 S22: 0.0210 S23: 0.2022 REMARK 3 S31: -0.0437 S32: -0.0951 S33: -0.0244 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4XNV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000205835. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-JUN-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19881 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 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 (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG2000MME SODIUM CITRATE, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.13500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.13050 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 79.69000 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 33.13500 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 19.13050 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 79.69000 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 33.13500 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 19.13050 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 79.69000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 38.26100 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 159.38000 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 38.26100 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 159.38000 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 38.26100 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 159.38000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 330 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 THR A 2 REMARK 465 GLU A 3 REMARK 465 VAL A 4 REMARK 465 LEU A 5 REMARK 465 TRP A 6 REMARK 465 PRO A 7 REMARK 465 ALA A 8 REMARK 465 VAL A 9 REMARK 465 PRO A 10 REMARK 465 ASN A 11 REMARK 465 GLY A 12 REMARK 465 THR A 13 REMARK 465 ASP A 14 REMARK 465 ALA A 15 REMARK 465 ALA A 16 REMARK 465 PHE A 17 REMARK 465 LEU A 18 REMARK 465 ALA A 19 REMARK 465 GLY A 20 REMARK 465 PRO A 21 REMARK 465 GLY A 22 REMARK 465 SER A 23 REMARK 465 SER A 24 REMARK 465 TRP A 25 REMARK 465 GLY A 26 REMARK 465 ASN A 27 REMARK 465 SER A 28 REMARK 465 THR A 29 REMARK 465 VAL A 30 REMARK 465 ALA A 31 REMARK 465 SER A 32 REMARK 465 THR A 33 REMARK 465 ALA A 34 REMARK 465 ALA A 35 REMARK 465 VAL A 36 REMARK 465 SER A 37 REMARK 465 SER A 38 REMARK 465 LEU A 157 REMARK 465 PRO A 1034 REMARK 465 ASP A 1035 REMARK 465 ASP A 1036 REMARK 465 TRP A 1037 REMARK 465 LEU A 335 REMARK 465 SER A 336 REMARK 465 ARG A 337 REMARK 465 ALA A 338 REMARK 465 THR A 339 REMARK 465 ARG A 340 REMARK 465 LYS A 341 REMARK 465 ALA A 342 REMARK 465 SER A 343 REMARK 465 ARG A 344 REMARK 465 ARG A 345 REMARK 465 SER A 346 REMARK 465 GLU A 347 REMARK 465 ALA A 348 REMARK 465 ASN A 349 REMARK 465 LEU A 350 REMARK 465 GLN A 351 REMARK 465 SER A 352 REMARK 465 LYS A 353 REMARK 465 SER A 354 REMARK 465 GLU A 355 REMARK 465 ASP A 356 REMARK 465 MET A 357 REMARK 465 THR A 358 REMARK 465 LEU A 359 REMARK 465 ASN A 360 REMARK 465 ILE A 361 REMARK 465 LEU A 362 REMARK 465 PRO A 363 REMARK 465 GLU A 364 REMARK 465 PHE A 365 REMARK 465 LYS A 366 REMARK 465 GLN A 367 REMARK 465 ASN A 368 REMARK 465 GLY A 369 REMARK 465 ASP A 370 REMARK 465 THR A 371 REMARK 465 SER A 372 REMARK 465 LEU A 373 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 THR A 45 OG1 CG2 REMARK 470 LYS A 158 CG CD CE NZ REMARK 470 LEU A 160 CG CD1 CD2 REMARK 470 THR A 330 OG1 CG2 REMARK 470 ARG A 332 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 334 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 43 81.26 -67.33 REMARK 500 TYR A 155 68.17 -114.33 REMARK 500 LEU A 160 43.60 -100.99 REMARK 500 THR A 205 -95.87 -106.43 REMARK 500 PHE A 226 -62.25 -125.78 REMARK 500 LEU A1041 -75.93 -77.95 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 1106 REMARK 610 OLC A 1107 REMARK 610 OLC A 1112 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1115 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A1006 SG REMARK 620 2 CYS A1009 SG 104.5 REMARK 620 3 CYS A1039 SG 109.8 113.7 REMARK 620 4 CYS A1042 SG 98.5 119.5 109.3 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue BUR A 1101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1102 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1103 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1104 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 1105 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1106 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1107 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1108 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1109 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1110 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1111 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1112 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1113 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 1114 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1115 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4XNW RELATED DB: PDB REMARK 900 RELATED ID: GPCR-86 RELATED DB: TARGETTRACK DBREF 4XNV A 2 247 UNP P47900 P2RY1_HUMAN 2 247 DBREF 4XNV A 1001 1054 UNP P00268 RUBR_CLOPA 1 54 DBREF 4XNV A 253 373 UNP P47900 P2RY1_HUMAN 253 373 SEQADV 4XNV ASN A 320 UNP P47900 ASP 320 ENGINEERED MUTATION SEQRES 1 A 421 THR GLU VAL LEU TRP PRO ALA VAL PRO ASN GLY THR ASP SEQRES 2 A 421 ALA ALA PHE LEU ALA GLY PRO GLY SER SER TRP GLY ASN SEQRES 3 A 421 SER THR VAL ALA SER THR ALA ALA VAL SER SER SER PHE SEQRES 4 A 421 LYS CYS ALA LEU THR LYS THR GLY PHE GLN PHE TYR TYR SEQRES 5 A 421 LEU PRO ALA VAL TYR ILE LEU VAL PHE ILE ILE GLY PHE SEQRES 6 A 421 LEU GLY ASN SER VAL ALA ILE TRP MET PHE VAL PHE HIS SEQRES 7 A 421 MET LYS PRO TRP SER GLY ILE SER VAL TYR MET PHE ASN SEQRES 8 A 421 LEU ALA LEU ALA ASP PHE LEU TYR VAL LEU THR LEU PRO SEQRES 9 A 421 ALA LEU ILE PHE TYR TYR PHE ASN LYS THR ASP TRP ILE SEQRES 10 A 421 PHE GLY ASP ALA MET CYS LYS LEU GLN ARG PHE ILE PHE SEQRES 11 A 421 HIS VAL ASN LEU TYR GLY SER ILE LEU PHE LEU THR CYS SEQRES 12 A 421 ILE SER ALA HIS ARG TYR SER GLY VAL VAL TYR PRO LEU SEQRES 13 A 421 LYS SER LEU GLY ARG LEU LYS LYS LYS ASN ALA ILE CYS SEQRES 14 A 421 ILE SER VAL LEU VAL TRP LEU ILE VAL VAL VAL ALA ILE SEQRES 15 A 421 SER PRO ILE LEU PHE TYR SER GLY THR GLY VAL ARG LYS SEQRES 16 A 421 ASN LYS THR ILE THR CYS TYR ASP THR THR SER ASP GLU SEQRES 17 A 421 TYR LEU ARG SER TYR PHE ILE TYR SER MET CYS THR THR SEQRES 18 A 421 VAL ALA MET PHE CYS VAL PRO LEU VAL LEU ILE LEU GLY SEQRES 19 A 421 CYS TYR GLY LEU ILE VAL ARG ALA LEU ILE TYR LYS MET SEQRES 20 A 421 LYS LYS TYR THR CYS THR VAL CYS GLY TYR ILE TYR ASN SEQRES 21 A 421 PRO GLU ASP GLY ASP PRO ASP ASN GLY VAL ASN PRO GLY SEQRES 22 A 421 THR ASP PHE LYS ASP ILE PRO ASP ASP TRP VAL CYS PRO SEQRES 23 A 421 LEU CYS GLY VAL GLY LYS ASP GLN PHE GLU GLU VAL GLU SEQRES 24 A 421 GLU PRO LEU ARG ARG LYS SER ILE TYR LEU VAL ILE ILE SEQRES 25 A 421 VAL LEU THR VAL PHE ALA VAL SER TYR ILE PRO PHE HIS SEQRES 26 A 421 VAL MET LYS THR MET ASN LEU ARG ALA ARG LEU ASP PHE SEQRES 27 A 421 GLN THR PRO ALA MET CYS ALA PHE ASN ASP ARG VAL TYR SEQRES 28 A 421 ALA THR TYR GLN VAL THR ARG GLY LEU ALA SER LEU ASN SEQRES 29 A 421 SER CYS VAL ASN PRO ILE LEU TYR PHE LEU ALA GLY ASP SEQRES 30 A 421 THR PHE ARG ARG ARG LEU SER ARG ALA THR ARG LYS ALA SEQRES 31 A 421 SER ARG ARG SER GLU ALA ASN LEU GLN SER LYS SER GLU SEQRES 32 A 421 ASP MET THR LEU ASN ILE LEU PRO GLU PHE LYS GLN ASN SEQRES 33 A 421 GLY ASP THR SER LEU HET BUR A1101 32 HET CLR A1102 28 HET Y01 A1103 35 HET Y01 A1104 35 HET Y01 A1105 35 HET OLC A1106 21 HET OLC A1107 21 HET OLC A1108 25 HET OLC A1109 25 HET OLC A1110 25 HET OLC A1111 25 HET OLC A1112 22 HET OLC A1113 25 HET 1PE A1114 16 HET ZN A1115 1 HETNAM BUR 1-[2-(2-TERT-BUTYLPHENOXY)PYRIDIN-3-YL]-3-[4- HETNAM 2 BUR (TRIFLUOROMETHOXY)PHENYL]UREA HETNAM CLR CHOLESTEROL HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM 1PE PENTAETHYLENE GLYCOL HETNAM ZN ZINC ION HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN 1PE PEG400 FORMUL 2 BUR C23 H22 F3 N3 O3 FORMUL 3 CLR C27 H46 O FORMUL 4 Y01 3(C31 H50 O4) FORMUL 7 OLC 8(C21 H40 O4) FORMUL 15 1PE C10 H22 O6 FORMUL 16 ZN ZN 2+ FORMUL 17 HOH *30(H2 O) HELIX 1 AA1 PHE A 49 HIS A 79 1 31 HELIX 2 AA2 SER A 84 ASN A 113 1 30 HELIX 3 AA3 GLY A 120 TYR A 155 1 36 HELIX 4 AA4 LEU A 160 SER A 184 1 25 HELIX 5 AA5 PRO A 185 SER A 190 1 6 HELIX 6 AA6 TYR A 210 PHE A 226 1 17 HELIX 7 AA7 PHE A 226 TYR A 246 1 21 HELIX 8 AA8 ASP A 1029 ILE A 1033 5 5 HELIX 9 AA9 GLY A 1045 ASP A 1047 5 3 HELIX 10 AB1 GLU A 1054 SER A 272 1 21 HELIX 11 AB2 SER A 272 PHE A 290 1 19 HELIX 12 AB3 THR A 292 ALA A 294 5 3 HELIX 13 AB4 MET A 295 ASN A 320 1 26 HELIX 14 AB5 ASN A 320 ALA A 327 1 8 SHEET 1 AA1 2 GLY A 191 VAL A 194 0 SHEET 2 AA1 2 ILE A 200 TYR A 203 -1 O TYR A 203 N GLY A 191 SHEET 1 AA2 3 ILE A1012 TYR A1013 0 SHEET 2 AA2 3 TYR A1004 CYS A1006 -1 N TYR A1004 O TYR A1013 SHEET 3 AA2 3 PHE A1049 GLU A1051 -1 O GLU A1050 N THR A1005 SSBOND 1 CYS A 42 CYS A 296 1555 1555 2.04 SSBOND 2 CYS A 124 CYS A 202 1555 1555 2.03 LINK SG CYS A1006 ZN ZN A1115 1555 1555 2.88 LINK SG CYS A1009 ZN ZN A1115 1555 1555 2.18 LINK SG CYS A1039 ZN ZN A1115 1555 1555 2.60 LINK SG CYS A1042 ZN ZN A1115 1555 1555 2.35 CISPEP 1 LYS A 81 PRO A 82 0 -1.35 SITE 1 AC1 13 PHE A 62 PHE A 66 LEU A 102 THR A 103 SITE 2 AC1 13 PRO A 105 ALA A 106 MET A 123 GLN A 127 SITE 3 AC1 13 Y01 A1105 OLC A1107 OLC A1110 OLC A1113 SITE 4 AC1 13 1PE A1114 SITE 1 AC2 5 PRO A 185 TYR A 189 SER A 213 TYR A 217 SITE 2 AC2 5 Y01 A1103 SITE 1 AC3 8 ILE A 216 CYS A 220 ALA A 270 MET A 279 SITE 2 AC3 8 ARG A 301 THR A 305 CLR A1102 1PE A1114 SITE 1 AC4 7 TYR A 89 CYS A 144 HIS A 148 ALA A 224 SITE 2 AC4 7 LEU A 232 TYR A 246 LEU A 266 SITE 1 AC5 9 PHE A 62 ILE A 108 PHE A 109 PHE A 112 SITE 2 AC5 9 ASN A 113 ARG A 301 BUR A1101 OLC A1113 SITE 3 AC5 9 1PE A1114 SITE 1 AC6 5 ARG A 212 PHE A 215 ILE A 216 ASP A 289 SITE 2 AC6 5 OLC A1112 SITE 1 AC7 9 PHE A 109 SER A 184 PHE A 188 TYR A 189 SITE 2 AC7 9 TYR A 210 SER A 213 ARG A 301 BUR A1101 SITE 3 AC7 9 1PE A1114 SITE 1 AC8 4 ASP A 121 PHE A 129 OLC A1110 HOH A1206 SITE 1 AC9 6 LYS A 46 PHE A 49 TYR A 53 PHE A 112 SITE 2 AC9 6 CYS A 318 OLC A1111 SITE 1 AD1 10 ILE A 118 PHE A 119 ASP A 121 MET A 123 SITE 2 AD1 10 LYS A 125 SER A 184 LEU A 187 PHE A 188 SITE 3 AD1 10 BUR A1101 OLC A1108 SITE 1 AD2 6 PHE A 51 TYR A 52 PRO A 55 TYR A 111 SITE 2 AD2 6 PHE A 112 OLC A1109 SITE 1 AD3 5 PHE A 226 THR A 281 MET A 282 ARG A 285 SITE 2 AD3 5 OLC A1106 SITE 1 AD4 9 THR A 267 ALA A 270 ARG A 301 THR A 305 SITE 2 AD4 9 VAL A 308 BUR A1101 Y01 A1105 1PE A1114 SITE 3 AD4 9 HOH A1217 SITE 1 AD5 6 ARG A 301 BUR A1101 Y01 A1103 Y01 A1105 SITE 2 AD5 6 OLC A1107 OLC A1113 SITE 1 AD6 4 CYS A1006 CYS A1009 CYS A1039 CYS A1042 CRYST1 66.270 66.270 239.070 90.00 90.00 120.00 H 3 9 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 0.015090 0.008712 0.000000 0.00000 SCALE2 0.000000 0.017424 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004183 0.00000 ATOM 1 N SER A 39 -1.110 11.647 -24.095 1.00 81.03 N ANISOU 1 N SER A 39 12312 10565 7912 36 719 146 N ATOM 2 CA SER A 39 -1.527 11.293 -22.741 1.00 78.22 C ANISOU 2 CA SER A 39 11766 10121 7835 71 591 95 C ATOM 3 C SER A 39 -3.051 11.212 -22.626 1.00 79.84 C ANISOU 3 C SER A 39 12029 10250 8056 64 308 125 C ATOM 4 O SER A 39 -3.732 12.245 -22.573 1.00 79.32 O ANISOU 4 O SER A 39 11968 10146 8024 15 196 272 O ATOM 5 CB SER A 39 -0.955 12.276 -21.719 1.00 80.80 C ANISOU 5 CB SER A 39 11885 10419 8397 39 673 191 C ATOM 6 OG SER A 39 -1.426 12.013 -20.407 1.00 87.93 O ANISOU 6 OG SER A 39 12623 11242 9544 67 544 152 O ATOM 7 N PHE A 40 -3.578 9.972 -22.591 1.00 74.45 N ANISOU 7 N PHE A 40 11384 9539 7365 115 192 -17 N ATOM 8 CA PHE A 40 -5.008 9.695 -22.454 1.00 72.46 C ANISOU 8 CA PHE A 40 11167 9213 7152 111 -74 -12 C ATOM 9 C PHE A 40 -5.523 10.159 -21.083 1.00 71.64 C ANISOU 9 C PHE A 40 10857 9030 7333 102 -166 51 C ATOM 10 O PHE A 40 -4.848 9.962 -20.071 1.00 70.17 O ANISOU 10 O PHE A 40 10505 8833 7324 128 -64 5 O ATOM 11 CB PHE A 40 -5.301 8.188 -22.665 1.00 74.46 C ANISOU 11 CB PHE A 40 11495 9446 7352 162 -155 -190 C ATOM 12 CG PHE A 40 -6.721 7.786 -22.331 1.00 75.16 C ANISOU 12 CG PHE A 40 11573 9447 7536 155 -421 -196 C ATOM 13 CD1 PHE A 40 -7.742 7.937 -23.262 1.00 79.19 C ANISOU 13 CD1 PHE A 40 12250 9951 7889 123 -610 -153 C ATOM 14 CD2 PHE A 40 -7.048 7.310 -21.064 1.00 75.13 C ANISOU 14 CD2 PHE A 40 11389 9370 7787 174 -483 -233 C ATOM 15 CE1 PHE A 40 -9.061 7.609 -22.938 1.00 79.42 C ANISOU 15 CE1 PHE A 40 12246 9897 8034 112 -856 -154 C ATOM 16 CE2 PHE A 40 -8.369 7.004 -20.735 1.00 77.24 C ANISOU 16 CE2 PHE A 40 11630 9560 8157 158 -712 -226 C ATOM 17 CZ PHE A 40 -9.364 7.144 -21.676 1.00 76.74 C ANISOU 17 CZ PHE A 40 11715 9488 7956 127 -896 -190 C ATOM 18 N LYS A 41 -6.727 10.748 -21.059 1.00 65.62 N ANISOU 18 N LYS A 41 10108 8214 6611 70 -364 149 N ATOM 19 CA LYS A 41 -7.380 11.189 -19.831 1.00 62.60 C ANISOU 19 CA LYS A 41 9545 7757 6482 64 -461 202 C ATOM 20 C LYS A 41 -8.844 10.760 -19.842 1.00 65.32 C ANISOU 20 C LYS A 41 9913 8038 6866 62 -706 193 C ATOM 21 O LYS A 41 -9.502 10.846 -20.882 1.00 66.73 O ANISOU 21 O LYS A 41 10249 8222 6885 43 -835 228 O ATOM 22 CB LYS A 41 -7.251 12.708 -19.644 1.00 64.47 C ANISOU 22 CB LYS A 41 9726 7985 6785 23 -420 358 C ATOM 23 CG LYS A 41 -7.449 13.162 -18.199 1.00 73.30 C ANISOU 23 CG LYS A 41 10635 9045 8172 28 -434 380 C ATOM 24 CD LYS A 41 -7.043 14.610 -17.999 1.00 81.43 C ANISOU 24 CD LYS A 41 11608 10061 9273 -9 -361 509 C ATOM 25 CE LYS A 41 -7.219 15.055 -16.569 1.00 89.84 C ANISOU 25 CE LYS A 41 12478 11069 10589 0 -373 510 C ATOM 26 NZ LYS A 41 -6.663 16.413 -16.341 1.00 99.36 N ANISOU 26 NZ LYS A 41 13624 12253 11874 -35 -291 615 N ATOM 27 N CYS A 42 -9.345 10.282 -18.688 1.00 58.85 N ANISOU 27 N CYS A 42 8939 7162 6261 79 -771 147 N ATOM 28 CA CYS A 42 -10.738 9.866 -18.517 1.00 57.78 C ANISOU 28 CA CYS A 42 8781 6961 6213 72 -988 139 C ATOM 29 C CYS A 42 -11.632 11.111 -18.562 1.00 68.69 C ANISOU 29 C CYS A 42 10132 8306 7661 43 -1109 280 C ATOM 30 O CYS A 42 -11.497 11.994 -17.710 1.00 67.71 O ANISOU 30 O CYS A 42 9873 8163 7689 40 -1047 347 O ATOM 31 CB CYS A 42 -10.922 9.089 -17.213 1.00 53.94 C ANISOU 31 CB CYS A 42 8130 6430 5936 91 -989 67 C ATOM 32 SG CYS A 42 -10.229 7.414 -17.235 1.00 56.25 S ANISOU 32 SG CYS A 42 8469 6728 6177 130 -923 -102 S ATOM 33 N ALA A 43 -12.512 11.195 -19.578 1.00 71.35 N ANISOU 33 N ALA A 43 10600 8629 7881 24 -1288 321 N ATOM 34 CA ALA A 43 -13.432 12.318 -19.770 1.00 74.00 C ANISOU 34 CA ALA A 43 10921 8920 8275 3 -1434 456 C ATOM 35 C ALA A 43 -14.485 12.363 -18.651 1.00 82.58 C ANISOU 35 C ALA A 43 11810 9933 9634 10 -1541 461 C ATOM 36 O ALA A 43 -15.609 11.881 -18.825 1.00 83.39 O ANISOU 36 O ALA A 43 11904 9991 9787 4 -1732 441 O ATOM 37 CB ALA A 43 -14.091 12.233 -21.143 1.00 76.78 C ANISOU 37 CB ALA A 43 11469 9276 8426 -15 -1616 486 C ATOM 38 N LEU A 44 -14.093 12.934 -17.491 1.00 81.49 N ANISOU 38 N LEU A 44 11509 9783 9668 21 -1412 481 N ATOM 39 CA LEU A 44 -14.920 13.062 -16.287 1.00 81.91 C ANISOU 39 CA LEU A 44 11367 9781 9973 30 -1460 480 C ATOM 40 C LEU A 44 -16.199 13.858 -16.545 1.00 89.98 C ANISOU 40 C LEU A 44 12354 10740 11096 25 -1651 573 C ATOM 41 O LEU A 44 -16.144 14.988 -17.042 1.00 90.35 O ANISOU 41 O LEU A 44 12450 10772 11108 21 -1672 679 O ATOM 42 CB LEU A 44 -14.110 13.688 -15.138 1.00 80.66 C ANISOU 42 CB LEU A 44 11079 9632 9937 42 -1280 486 C ATOM 43 CG LEU A 44 -14.517 13.273 -13.726 1.00 84.11 C ANISOU 43 CG LEU A 44 11338 10045 10576 56 -1254 428 C ATOM 44 CD1 LEU A 44 -13.299 12.986 -12.875 1.00 83.10 C ANISOU 44 CD1 LEU A 44 11159 9958 10456 67 -1066 369 C ATOM 45 CD2 LEU A 44 -15.395 14.327 -13.071 1.00 86.37 C ANISOU 45 CD2 LEU A 44 11490 10275 11052 63 -1315 494 C ATOM 46 N THR A 45 -17.350 13.239 -16.227 1.00 89.06 N ANISOU 46 N THR A 45 12147 10580 11112 24 -1793 536 N ATOM 47 CA THR A 45 -18.680 13.821 -16.394 1.00 90.76 C ANISOU 47 CA THR A 45 12294 10730 11460 25 -1988 609 C ATOM 48 C THR A 45 -19.556 13.525 -15.174 1.00 95.60 C ANISOU 48 C THR A 45 12692 11302 12330 32 -2001 569 C ATOM 49 O THR A 45 -20.154 12.448 -15.072 1.00 95.30 O ANISOU 49 O THR A 45 12618 11251 12339 15 -2083 505 O ATOM 50 CB THR A 45 -19.303 13.396 -17.735 1.00100.34 C ANISOU 50 CB THR A 45 13664 11936 12527 6 -2199 622 C ATOM 51 N LYS A 46 -19.585 14.479 -14.229 1.00 92.57 N ANISOU 51 N LYS A 46 12167 10897 12107 55 -1908 605 N ATOM 52 CA LYS A 46 -20.380 14.418 -13.004 1.00 92.01 C ANISOU 52 CA LYS A 46 11890 10796 12275 66 -1889 574 C ATOM 53 C LYS A 46 -21.014 15.797 -12.742 1.00 97.51 C ANISOU 53 C LYS A 46 12476 11433 13139 99 -1931 651 C ATOM 54 O LYS A 46 -20.359 16.700 -12.211 1.00 96.35 O ANISOU 54 O LYS A 46 12305 11286 13019 119 -1802 670 O ATOM 55 CB LYS A 46 -19.547 13.910 -11.807 1.00 92.51 C ANISOU 55 CB LYS A 46 11888 10904 12356 67 -1685 499 C ATOM 56 CG LYS A 46 -20.374 13.774 -10.535 1.00103.14 C ANISOU 56 CG LYS A 46 13037 12230 13920 73 -1652 469 C ATOM 57 CD LYS A 46 -19.667 13.082 -9.394 1.00109.99 C ANISOU 57 CD LYS A 46 13860 13143 14787 67 -1483 399 C ATOM 58 CE LYS A 46 -20.421 13.279 -8.100 1.00119.88 C ANISOU 58 CE LYS A 46 14928 14383 16237 76 -1423 385 C ATOM 59 NZ LYS A 46 -21.640 12.432 -8.018 1.00130.27 N ANISOU 59 NZ LYS A 46 16150 15672 17675 47 -1525 376 N ATOM 60 N THR A 47 -22.283 15.954 -13.165 1.00 95.86 N ANISOU 60 N THR A 47 12205 11167 13051 104 -2124 692 N ATOM 61 CA THR A 47 -23.060 17.191 -13.029 1.00 96.69 C ANISOU 61 CA THR A 47 12197 11198 13342 144 -2200 762 C ATOM 62 C THR A 47 -24.490 16.922 -12.550 1.00101.49 C ANISOU 62 C THR A 47 12608 11761 14192 153 -2307 741 C ATOM 63 O THR A 47 -25.084 15.901 -12.907 1.00101.79 O ANISOU 63 O THR A 47 12646 11806 14226 120 -2422 712 O ATOM 64 CB THR A 47 -23.035 18.015 -14.332 1.00106.08 C ANISOU 64 CB THR A 47 13536 12350 14420 149 -2352 873 C ATOM 65 OG1 THR A 47 -23.179 17.149 -15.463 1.00106.84 O ANISOU 65 OG1 THR A 47 13784 12472 14340 114 -2500 874 O ATOM 66 CG2 THR A 47 -21.776 18.863 -14.470 1.00104.27 C ANISOU 66 CG2 THR A 47 13424 12138 14057 151 -2211 920 C ATOM 67 N GLY A 48 -25.019 17.851 -11.753 1.00 97.88 N ANISOU 67 N GLY A 48 11982 11256 13951 199 -2266 752 N ATOM 68 CA GLY A 48 -26.362 17.776 -11.184 1.00 98.06 C ANISOU 68 CA GLY A 48 11787 11236 14234 217 -2333 732 C ATOM 69 C GLY A 48 -26.427 17.133 -9.811 1.00 99.67 C ANISOU 69 C GLY A 48 11845 11487 14538 205 -2147 642 C ATOM 70 O GLY A 48 -27.495 17.117 -9.190 1.00 99.93 O ANISOU 70 O GLY A 48 11681 11494 14795 219 -2158 621 O ATOM 71 N PHE A 49 -25.285 16.599 -9.324 1.00 93.52 N ANISOU 71 N PHE A 49 11160 10779 13594 180 -1973 592 N ATOM 72 CA PHE A 49 -25.193 15.928 -8.026 1.00 91.47 C ANISOU 72 CA PHE A 49 10798 10570 13387 164 -1796 517 C ATOM 73 C PHE A 49 -24.238 16.648 -7.071 1.00 89.60 C ANISOU 73 C PHE A 49 10565 10363 13116 194 -1596 484 C ATOM 74 O PHE A 49 -24.693 17.205 -6.072 1.00 89.09 O ANISOU 74 O PHE A 49 10353 10288 13208 227 -1503 454 O ATOM 75 CB PHE A 49 -24.817 14.434 -8.176 1.00 93.37 C ANISOU 75 CB PHE A 49 11126 10859 13491 103 -1789 479 C ATOM 76 CG PHE A 49 -24.942 13.829 -9.556 1.00 96.53 C ANISOU 76 CG PHE A 49 11663 11240 13773 72 -1981 505 C ATOM 77 CD1 PHE A 49 -26.176 13.415 -10.045 1.00101.70 C ANISOU 77 CD1 PHE A 49 12238 11849 14555 50 -2166 521 C ATOM 78 CD2 PHE A 49 -23.822 13.649 -10.356 1.00 98.64 C ANISOU 78 CD2 PHE A 49 12137 11540 13803 64 -1974 507 C ATOM 79 CE1 PHE A 49 -26.289 12.853 -11.322 1.00103.86 C ANISOU 79 CE1 PHE A 49 12651 12106 14705 20 -2357 534 C ATOM 80 CE2 PHE A 49 -23.932 13.081 -11.629 1.00102.80 C ANISOU 80 CE2 PHE A 49 12804 12056 14198 37 -2143 519 C ATOM 81 CZ PHE A 49 -25.164 12.688 -12.105 1.00102.47 C ANISOU 81 CZ PHE A 49 12697 11967 14272 16 -2341 530 C ATOM 82 N GLN A 50 -22.925 16.648 -7.386 1.00 81.96 N ANISOU 82 N GLN A 50 9762 9431 11947 183 -1532 486 N ATOM 83 CA GLN A 50 -21.865 17.272 -6.579 1.00 79.14 C ANISOU 83 CA GLN A 50 9425 9102 11542 202 -1360 454 C ATOM 84 C GLN A 50 -21.957 18.799 -6.516 1.00 78.57 C ANISOU 84 C GLN A 50 9310 8966 11578 252 -1362 484 C ATOM 85 O GLN A 50 -21.503 19.398 -5.537 1.00 76.95 O ANISOU 85 O GLN A 50 9055 8768 11415 275 -1226 437 O ATOM 86 CB GLN A 50 -20.459 16.819 -7.033 1.00 79.82 C ANISOU 86 CB GLN A 50 9683 9239 11406 174 -1302 450 C ATOM 87 CG GLN A 50 -20.160 17.052 -8.522 1.00 99.06 C ANISOU 87 CG GLN A 50 12272 11655 13710 164 -1423 520 C ATOM 88 CD GLN A 50 -18.697 16.947 -8.895 1.00118.53 C ANISOU 88 CD GLN A 50 14885 14169 15981 147 -1328 517 C ATOM 89 OE1 GLN A 50 -17.790 17.078 -8.063 1.00113.81 O ANISOU 89 OE1 GLN A 50 14270 13604 15369 151 -1179 475 O ATOM 90 NE2 GLN A 50 -18.437 16.772 -10.182 1.00110.83 N ANISOU 90 NE2 GLN A 50 14057 13199 14854 128 -1414 562 N ATOM 91 N PHE A 51 -22.552 19.421 -7.551 1.00 73.15 N ANISOU 91 N PHE A 51 8646 8211 10938 268 -1526 562 N ATOM 92 CA PHE A 51 -22.712 20.875 -7.619 1.00 71.89 C ANISOU 92 CA PHE A 51 8449 7968 10898 317 -1555 604 C ATOM 93 C PHE A 51 -23.924 21.392 -6.835 1.00 70.49 C ANISOU 93 C PHE A 51 8068 7737 10978 370 -1561 569 C ATOM 94 O PHE A 51 -24.180 22.596 -6.808 1.00 71.63 O ANISOU 94 O PHE A 51 8161 7797 11257 422 -1591 593 O ATOM 95 CB PHE A 51 -22.651 21.378 -9.070 1.00 74.99 C ANISOU 95 CB PHE A 51 8977 8308 11208 312 -1722 716 C ATOM 96 CG PHE A 51 -21.311 21.099 -9.716 1.00 76.15 C ANISOU 96 CG PHE A 51 9319 8511 11105 266 -1666 742 C ATOM 97 CD1 PHE A 51 -20.213 21.916 -9.461 1.00 78.51 C ANISOU 97 CD1 PHE A 51 9672 8804 11356 265 -1543 750 C ATOM 98 CD2 PHE A 51 -21.139 20.003 -10.554 1.00 78.48 C ANISOU 98 CD2 PHE A 51 9734 8863 11224 223 -1729 750 C ATOM 99 CE1 PHE A 51 -18.971 21.646 -10.042 1.00 78.95 C ANISOU 99 CE1 PHE A 51 9885 8915 11198 222 -1476 772 C ATOM 100 CE2 PHE A 51 -19.897 19.737 -11.138 1.00 80.73 C ANISOU 100 CE2 PHE A 51 10187 9203 11284 188 -1658 763 C ATOM 101 CZ PHE A 51 -18.822 20.560 -10.878 1.00 78.27 C ANISOU 101 CZ PHE A 51 9913 8890 10935 187 -1527 777 C ATOM 102 N TYR A 52 -24.627 20.478 -6.151 1.00 61.16 N ANISOU 102 N TYR A 52 6767 6602 9870 357 -1519 510 N ATOM 103 CA TYR A 52 -25.757 20.768 -5.280 1.00 59.33 C ANISOU 103 CA TYR A 52 6326 6342 9874 401 -1484 462 C ATOM 104 C TYR A 52 -25.446 20.249 -3.867 1.00 53.66 C ANISOU 104 C TYR A 52 5548 5705 9136 387 -1270 366 C ATOM 105 O TYR A 52 -25.707 20.951 -2.891 1.00 51.98 O ANISOU 105 O TYR A 52 5223 5479 9049 435 -1157 305 O ATOM 106 CB TYR A 52 -27.046 20.137 -5.829 1.00 63.01 C ANISOU 106 CB TYR A 52 6689 6786 10466 388 -1642 495 C ATOM 107 CG TYR A 52 -27.590 20.826 -7.062 1.00 68.72 C ANISOU 107 CG TYR A 52 7437 7417 11258 417 -1869 587 C ATOM 108 CD1 TYR A 52 -27.127 20.492 -8.334 1.00 71.43 C ANISOU 108 CD1 TYR A 52 7968 7762 11412 377 -2014 662 C ATOM 109 CD2 TYR A 52 -28.593 21.786 -6.964 1.00 71.46 C ANISOU 109 CD2 TYR A 52 7621 7675 11857 487 -1941 599 C ATOM 110 CE1 TYR A 52 -27.630 21.119 -9.475 1.00 74.74 C ANISOU 110 CE1 TYR A 52 8426 8098 11871 401 -2233 757 C ATOM 111 CE2 TYR A 52 -29.109 22.413 -8.098 1.00 74.37 C ANISOU 111 CE2 TYR A 52 8013 7950 12293 516 -2169 694 C ATOM 112 CZ TYR A 52 -28.628 22.073 -9.353 1.00 84.04 C ANISOU 112 CZ TYR A 52 9441 9183 13309 470 -2319 778 C ATOM 113 OH TYR A 52 -29.139 22.685 -10.475 1.00 88.42 O ANISOU 113 OH TYR A 52 10037 9650 13910 496 -2554 882 O ATOM 114 N TYR A 53 -24.853 19.034 -3.768 1.00 44.50 N ANISOU 114 N TYR A 53 4473 4626 7809 325 -1218 353 N ATOM 115 CA TYR A 53 -24.510 18.376 -2.506 1.00 41.36 C ANISOU 115 CA TYR A 53 4045 4308 7363 302 -1037 282 C ATOM 116 C TYR A 53 -23.561 19.171 -1.602 1.00 42.84 C ANISOU 116 C TYR A 53 4267 4514 7495 332 -887 223 C ATOM 117 O TYR A 53 -23.940 19.505 -0.477 1.00 40.90 O ANISOU 117 O TYR A 53 3913 4285 7342 361 -763 157 O ATOM 118 CB TYR A 53 -24.015 16.945 -2.757 1.00 40.26 C ANISOU 118 CB TYR A 53 4007 4228 7062 234 -1046 293 C ATOM 119 CG TYR A 53 -23.421 16.257 -1.549 1.00 39.47 C ANISOU 119 CG TYR A 53 3914 4206 6877 209 -876 238 C ATOM 120 CD1 TYR A 53 -24.235 15.758 -0.532 1.00 41.80 C ANISOU 120 CD1 TYR A 53 4077 4534 7272 194 -783 208 C ATOM 121 CD2 TYR A 53 -22.047 16.066 -1.437 1.00 37.75 C ANISOU 121 CD2 TYR A 53 3836 4030 6479 197 -810 222 C ATOM 122 CE1 TYR A 53 -23.690 15.110 0.578 1.00 41.02 C ANISOU 122 CE1 TYR A 53 4001 4506 7079 167 -636 172 C ATOM 123 CE2 TYR A 53 -21.493 15.430 -0.329 1.00 37.18 C ANISOU 123 CE2 TYR A 53 3775 4024 6328 176 -675 178 C ATOM 124 CZ TYR A 53 -22.317 14.955 0.676 1.00 43.33 C ANISOU 124 CZ TYR A 53 4439 4834 7192 161 -592 157 C ATOM 125 OH TYR A 53 -21.762 14.339 1.767 1.00 42.12 O ANISOU 125 OH TYR A 53 4313 4746 6945 138 -467 127 O ATOM 126 N LEU A 54 -22.337 19.460 -2.084 1.00 39.76 N ANISOU 126 N LEU A 54 4028 4125 6955 323 -894 244 N ATOM 127 CA LEU A 54 -21.342 20.220 -1.326 1.00 39.19 C ANISOU 127 CA LEU A 54 3995 4063 6834 342 -773 190 C ATOM 128 C LEU A 54 -21.870 21.595 -0.902 1.00 42.64 C ANISOU 128 C LEU A 54 4333 4425 7445 407 -756 156 C ATOM 129 O LEU A 54 -21.868 21.848 0.304 1.00 42.22 O ANISOU 129 O LEU A 54 4216 4398 7427 429 -625 69 O ATOM 130 CB LEU A 54 -19.975 20.308 -2.042 1.00 38.64 C ANISOU 130 CB LEU A 54 4085 3999 6596 315 -790 227 C ATOM 131 CG LEU A 54 -19.162 19.004 -2.189 1.00 42.62 C ANISOU 131 CG LEU A 54 4689 4581 6922 263 -764 230 C ATOM 132 CD1 LEU A 54 -17.832 19.285 -2.845 1.00 42.02 C ANISOU 132 CD1 LEU A 54 4746 4507 6712 247 -761 258 C ATOM 133 CD2 LEU A 54 -18.901 18.331 -0.830 1.00 44.88 C ANISOU 133 CD2 LEU A 54 4939 4941 7173 252 -632 157 C ATOM 134 N PRO A 55 -22.446 22.445 -1.794 1.00 39.57 N ANISOU 134 N PRO A 55 3921 3939 7176 442 -885 216 N ATOM 135 CA PRO A 55 -22.987 23.732 -1.304 1.00 40.25 C ANISOU 135 CA PRO A 55 3900 3940 7452 513 -865 172 C ATOM 136 C PRO A 55 -24.094 23.588 -0.257 1.00 43.84 C ANISOU 136 C PRO A 55 4180 4417 8059 550 -774 89 C ATOM 137 O PRO A 55 -24.112 24.405 0.657 1.00 44.07 O ANISOU 137 O PRO A 55 4149 4423 8173 600 -671 1 O ATOM 138 CB PRO A 55 -23.482 24.444 -2.569 1.00 42.72 C ANISOU 138 CB PRO A 55 4224 4145 7862 538 -1049 273 C ATOM 139 CG PRO A 55 -23.559 23.411 -3.606 1.00 47.10 C ANISOU 139 CG PRO A 55 4857 4741 8299 484 -1164 356 C ATOM 140 CD PRO A 55 -22.579 22.335 -3.264 1.00 41.19 C ANISOU 140 CD PRO A 55 4206 4102 7343 422 -1059 324 C ATOM 141 N ALA A 56 -24.969 22.535 -0.347 1.00 38.90 N ANISOU 141 N ALA A 56 3476 3839 7465 522 -801 111 N ATOM 142 CA ALA A 56 -26.033 22.302 0.639 1.00 38.93 C ANISOU 142 CA ALA A 56 3304 3875 7612 545 -697 43 C ATOM 143 C ALA A 56 -25.439 21.904 1.993 1.00 41.71 C ANISOU 143 C ALA A 56 3680 4326 7842 525 -496 -47 C ATOM 144 O ALA A 56 -25.814 22.485 3.011 1.00 42.65 O ANISOU 144 O ALA A 56 3704 4449 8051 573 -368 -138 O ATOM 145 CB ALA A 56 -27.019 21.250 0.149 1.00 39.98 C ANISOU 145 CB ALA A 56 3355 4029 7808 504 -783 99 C ATOM 146 N VAL A 57 -24.476 20.958 1.996 1.00 36.07 N ANISOU 146 N VAL A 57 3101 3687 6918 458 -474 -23 N ATOM 147 CA VAL A 57 -23.770 20.520 3.196 1.00 34.57 C ANISOU 147 CA VAL A 57 2960 3588 6585 433 -313 -90 C ATOM 148 C VAL A 57 -23.036 21.718 3.800 1.00 38.13 C ANISOU 148 C VAL A 57 3452 4012 7022 481 -243 -171 C ATOM 149 O VAL A 57 -23.151 21.935 5.006 1.00 38.75 O ANISOU 149 O VAL A 57 3486 4134 7102 504 -102 -264 O ATOM 150 CB VAL A 57 -22.815 19.334 2.895 1.00 37.04 C ANISOU 150 CB VAL A 57 3413 3964 6697 362 -338 -40 C ATOM 151 CG1 VAL A 57 -21.790 19.143 4.007 1.00 36.07 C ANISOU 151 CG1 VAL A 57 3370 3916 6418 346 -207 -101 C ATOM 152 CG2 VAL A 57 -23.598 18.045 2.657 1.00 37.28 C ANISOU 152 CG2 VAL A 57 3392 4026 6746 310 -373 14 C ATOM 153 N TYR A 58 -22.344 22.528 2.964 1.00 33.78 N ANISOU 153 N TYR A 58 2985 3385 6466 495 -342 -136 N ATOM 154 CA TYR A 58 -21.623 23.717 3.444 1.00 34.91 C ANISOU 154 CA TYR A 58 3165 3480 6617 533 -296 -208 C ATOM 155 C TYR A 58 -22.518 24.765 4.105 1.00 41.56 C ANISOU 155 C TYR A 58 3879 4260 7652 612 -240 -297 C ATOM 156 O TYR A 58 -22.073 25.397 5.068 1.00 41.73 O ANISOU 156 O TYR A 58 3915 4285 7656 638 -141 -403 O ATOM 157 CB TYR A 58 -20.723 24.345 2.370 1.00 35.94 C ANISOU 157 CB TYR A 58 3406 3536 6714 520 -410 -136 C ATOM 158 CG TYR A 58 -19.599 23.461 1.877 1.00 37.38 C ANISOU 158 CG TYR A 58 3720 3782 6698 452 -430 -77 C ATOM 159 CD1 TYR A 58 -18.961 22.562 2.731 1.00 38.83 C ANISOU 159 CD1 TYR A 58 3946 4070 6738 416 -334 -123 C ATOM 160 CD2 TYR A 58 -19.150 23.541 0.562 1.00 37.84 C ANISOU 160 CD2 TYR A 58 3867 3798 6712 426 -544 24 C ATOM 161 CE1 TYR A 58 -17.941 21.730 2.275 1.00 39.10 C ANISOU 161 CE1 TYR A 58 4090 4156 6612 363 -354 -76 C ATOM 162 CE2 TYR A 58 -18.136 22.708 0.093 1.00 37.85 C ANISOU 162 CE2 TYR A 58 3983 3861 6539 371 -549 66 C ATOM 163 CZ TYR A 58 -17.525 21.813 0.956 1.00 45.50 C ANISOU 163 CZ TYR A 58 4976 4925 7389 343 -454 12 C ATOM 164 OH TYR A 58 -16.501 21.014 0.503 1.00 45.06 O ANISOU 164 OH TYR A 58 5021 4920 7181 298 -459 46 O ATOM 165 N ILE A 59 -23.772 24.941 3.604 1.00 38.74 N ANISOU 165 N ILE A 59 3393 3846 7482 651 -306 -263 N ATOM 166 CA ILE A 59 -24.764 25.871 4.168 1.00 40.61 C ANISOU 166 CA ILE A 59 3480 4017 7932 737 -253 -350 C ATOM 167 C ILE A 59 -25.187 25.327 5.547 1.00 46.76 C ANISOU 167 C ILE A 59 4184 4906 8675 737 -60 -454 C ATOM 168 O ILE A 59 -25.195 26.076 6.529 1.00 46.81 O ANISOU 168 O ILE A 59 4160 4906 8720 791 59 -579 O ATOM 169 CB ILE A 59 -25.998 26.065 3.217 1.00 44.62 C ANISOU 169 CB ILE A 59 3859 4439 8657 776 -391 -274 C ATOM 170 CG1 ILE A 59 -25.651 26.948 2.001 1.00 45.14 C ANISOU 170 CG1 ILE A 59 3999 4375 8777 794 -571 -184 C ATOM 171 CG2 ILE A 59 -27.212 26.635 3.961 1.00 46.78 C ANISOU 171 CG2 ILE A 59 3935 4678 9160 861 -301 -372 C ATOM 172 CD1 ILE A 59 -26.650 26.820 0.782 1.00 53.09 C ANISOU 172 CD1 ILE A 59 4936 5316 9922 805 -761 -66 C ATOM 173 N LEU A 60 -25.515 24.013 5.602 1.00 43.69 N ANISOU 173 N LEU A 60 3777 4617 8207 674 -32 -400 N ATOM 174 CA LEU A 60 -25.935 23.274 6.795 1.00 44.49 C ANISOU 174 CA LEU A 60 3820 4832 8253 653 145 -461 C ATOM 175 C LEU A 60 -24.857 23.348 7.881 1.00 45.03 C ANISOU 175 C LEU A 60 4016 4972 8121 639 267 -548 C ATOM 176 O LEU A 60 -25.171 23.685 9.030 1.00 44.86 O ANISOU 176 O LEU A 60 3946 4993 8105 676 424 -660 O ATOM 177 CB LEU A 60 -26.224 21.814 6.400 1.00 45.01 C ANISOU 177 CB LEU A 60 3883 4966 8254 570 108 -357 C ATOM 178 CG LEU A 60 -26.974 20.934 7.400 1.00 52.37 C ANISOU 178 CG LEU A 60 4719 5999 9180 536 270 -379 C ATOM 179 CD1 LEU A 60 -28.113 20.194 6.718 1.00 53.74 C ANISOU 179 CD1 LEU A 60 4754 6155 9508 504 194 -294 C ATOM 180 CD2 LEU A 60 -26.032 19.920 8.031 1.00 55.48 C ANISOU 180 CD2 LEU A 60 5258 6496 9325 461 341 -362 C ATOM 181 N VAL A 61 -23.581 23.089 7.494 1.00 39.33 N ANISOU 181 N VAL A 61 3455 4259 7228 591 192 -501 N ATOM 182 CA VAL A 61 -22.421 23.144 8.385 1.00 37.94 C ANISOU 182 CA VAL A 61 3406 4142 6867 573 268 -571 C ATOM 183 C VAL A 61 -22.201 24.572 8.847 1.00 42.59 C ANISOU 183 C VAL A 61 3992 4658 7531 643 299 -690 C ATOM 184 O VAL A 61 -21.974 24.771 10.036 1.00 43.13 O ANISOU 184 O VAL A 61 4088 4784 7514 657 422 -802 O ATOM 185 CB VAL A 61 -21.145 22.479 7.791 1.00 39.52 C ANISOU 185 CB VAL A 61 3754 4365 6896 508 176 -489 C ATOM 186 CG1 VAL A 61 -19.939 22.650 8.710 1.00 38.25 C ANISOU 186 CG1 VAL A 61 3707 4253 6574 496 235 -566 C ATOM 187 CG2 VAL A 61 -21.388 20.993 7.524 1.00 38.76 C ANISOU 187 CG2 VAL A 61 3665 4342 6721 443 162 -394 C ATOM 188 N PHE A 62 -22.327 25.568 7.941 1.00 39.15 N ANISOU 188 N PHE A 62 3524 4092 7257 687 187 -669 N ATOM 189 CA PHE A 62 -22.167 26.965 8.357 1.00 39.83 C ANISOU 189 CA PHE A 62 3604 4086 7443 755 208 -784 C ATOM 190 C PHE A 62 -23.170 27.375 9.419 1.00 45.41 C ANISOU 190 C PHE A 62 4193 4810 8252 826 355 -919 C ATOM 191 O PHE A 62 -22.751 27.906 10.442 1.00 45.88 O ANISOU 191 O PHE A 62 4298 4887 8247 850 451 -1054 O ATOM 192 CB PHE A 62 -22.133 27.976 7.191 1.00 41.27 C ANISOU 192 CB PHE A 62 3779 4112 7790 788 55 -722 C ATOM 193 CG PHE A 62 -21.885 29.397 7.671 1.00 43.84 C ANISOU 193 CG PHE A 62 4105 4327 8225 852 72 -843 C ATOM 194 CD1 PHE A 62 -20.611 29.815 8.032 1.00 45.48 C ANISOU 194 CD1 PHE A 62 4435 4524 8320 821 71 -894 C ATOM 195 CD2 PHE A 62 -22.936 30.303 7.795 1.00 47.71 C ANISOU 195 CD2 PHE A 62 4465 4716 8945 946 86 -914 C ATOM 196 CE1 PHE A 62 -20.389 31.113 8.503 1.00 47.37 C ANISOU 196 CE1 PHE A 62 4678 4651 8671 876 79 -1015 C ATOM 197 CE2 PHE A 62 -22.710 31.601 8.266 1.00 51.22 C ANISOU 197 CE2 PHE A 62 4915 5046 9501 1009 100 -1037 C ATOM 198 CZ PHE A 62 -21.437 31.999 8.605 1.00 48.33 C ANISOU 198 CZ PHE A 62 4680 4667 9016 970 93 -1087 C ATOM 199 N ILE A 63 -24.471 27.114 9.191 1.00 43.47 N ANISOU 199 N ILE A 63 3793 4559 8162 856 374 -889 N ATOM 200 CA ILE A 63 -25.557 27.490 10.106 1.00 45.34 C ANISOU 200 CA ILE A 63 3889 4811 8528 929 527 -1013 C ATOM 201 C ILE A 63 -25.429 26.795 11.468 1.00 50.41 C ANISOU 201 C ILE A 63 4574 5608 8971 895 719 -1096 C ATOM 202 O ILE A 63 -25.371 27.483 12.483 1.00 51.56 O ANISOU 202 O ILE A 63 4733 5765 9094 947 841 -1249 O ATOM 203 CB ILE A 63 -26.975 27.351 9.457 1.00 49.44 C ANISOU 203 CB ILE A 63 4214 5287 9285 965 491 -950 C ATOM 204 CG1 ILE A 63 -27.080 28.193 8.152 1.00 50.00 C ANISOU 204 CG1 ILE A 63 4258 5192 9547 1008 285 -871 C ATOM 205 CG2 ILE A 63 -28.099 27.736 10.450 1.00 53.05 C ANISOU 205 CG2 ILE A 63 4504 5765 9885 1044 675 -1088 C ATOM 206 CD1 ILE A 63 -28.327 27.898 7.252 1.00 56.01 C ANISOU 206 CD1 ILE A 63 4853 5909 10521 1026 184 -772 C ATOM 207 N ILE A 64 -25.348 25.451 11.480 1.00 46.08 N ANISOU 207 N ILE A 64 4062 5175 8273 809 738 -994 N ATOM 208 CA ILE A 64 -25.242 24.648 12.705 1.00 46.31 C ANISOU 208 CA ILE A 64 4143 5352 8100 764 907 -1037 C ATOM 209 C ILE A 64 -23.866 24.838 13.398 1.00 48.76 C ANISOU 209 C ILE A 64 4641 5701 8183 742 911 -1105 C ATOM 210 O ILE A 64 -23.823 25.025 14.619 1.00 48.89 O ANISOU 210 O ILE A 64 4696 5792 8087 760 1057 -1227 O ATOM 211 CB ILE A 64 -25.641 23.159 12.439 1.00 49.17 C ANISOU 211 CB ILE A 64 4476 5801 8404 677 911 -897 C ATOM 212 CG1 ILE A 64 -27.071 23.078 11.846 1.00 51.01 C ANISOU 212 CG1 ILE A 64 4503 5989 8890 702 904 -849 C ATOM 213 CG2 ILE A 64 -25.537 22.294 13.716 1.00 50.48 C ANISOU 213 CG2 ILE A 64 4703 6116 8360 625 1087 -922 C ATOM 214 CD1 ILE A 64 -27.423 21.777 11.125 1.00 61.00 C ANISOU 214 CD1 ILE A 64 5734 7283 10158 617 826 -694 C ATOM 215 N GLY A 65 -22.787 24.833 12.603 1.00 42.88 N ANISOU 215 N GLY A 65 4005 4905 7382 705 751 -1030 N ATOM 216 CA GLY A 65 -21.414 25.019 13.070 1.00 41.87 C ANISOU 216 CA GLY A 65 4038 4798 7074 679 721 -1079 C ATOM 217 C GLY A 65 -21.133 26.389 13.657 1.00 46.16 C ANISOU 217 C GLY A 65 4602 5272 7667 747 749 -1242 C ATOM 218 O GLY A 65 -20.464 26.485 14.689 1.00 45.02 O ANISOU 218 O GLY A 65 4558 5190 7357 739 811 -1343 O ATOM 219 N PHE A 66 -21.638 27.466 13.015 1.00 43.81 N ANISOU 219 N PHE A 66 4213 4835 7598 815 693 -1271 N ATOM 220 CA PHE A 66 -21.442 28.814 13.545 1.00 44.90 C ANISOU 220 CA PHE A 66 4362 4882 7814 885 714 -1434 C ATOM 221 C PHE A 66 -22.181 28.938 14.868 1.00 51.18 C ANISOU 221 C PHE A 66 5116 5759 8572 937 909 -1592 C ATOM 222 O PHE A 66 -21.586 29.418 15.824 1.00 51.14 O ANISOU 222 O PHE A 66 5205 5775 8450 950 962 -1734 O ATOM 223 CB PHE A 66 -21.871 29.907 12.548 1.00 47.15 C ANISOU 223 CB PHE A 66 4558 4989 8367 949 605 -1417 C ATOM 224 CG PHE A 66 -21.558 31.320 12.981 1.00 49.74 C ANISOU 224 CG PHE A 66 4908 5194 8796 1015 600 -1574 C ATOM 225 CD1 PHE A 66 -20.294 31.866 12.776 1.00 51.19 C ANISOU 225 CD1 PHE A 66 5211 5306 8934 977 490 -1576 C ATOM 226 CD2 PHE A 66 -22.531 32.111 13.586 1.00 54.18 C ANISOU 226 CD2 PHE A 66 5366 5705 9514 1115 706 -1724 C ATOM 227 CE1 PHE A 66 -20.007 33.170 13.177 1.00 53.51 C ANISOU 227 CE1 PHE A 66 5524 5471 9334 1032 475 -1724 C ATOM 228 CE2 PHE A 66 -22.241 33.418 13.988 1.00 57.97 C ANISOU 228 CE2 PHE A 66 5871 6057 10097 1180 694 -1882 C ATOM 229 CZ PHE A 66 -20.981 33.938 13.780 1.00 55.14 C ANISOU 229 CZ PHE A 66 5639 5622 9691 1135 573 -1879 C ATOM 230 N LEU A 67 -23.434 28.425 14.944 1.00 49.71 N ANISOU 230 N LEU A 67 4793 5626 8468 958 1017 -1565 N ATOM 231 CA LEU A 67 -24.269 28.462 16.150 1.00 51.89 C ANISOU 231 CA LEU A 67 5010 5991 8714 1005 1231 -1704 C ATOM 232 C LEU A 67 -23.627 27.709 17.325 1.00 55.22 C ANISOU 232 C LEU A 67 5579 6575 8826 943 1338 -1742 C ATOM 233 O LEU A 67 -23.322 28.330 18.342 1.00 55.96 O ANISOU 233 O LEU A 67 5751 6693 8817 979 1425 -1909 O ATOM 234 CB LEU A 67 -25.704 27.949 15.874 1.00 53.13 C ANISOU 234 CB LEU A 67 4975 6176 9037 1024 1319 -1640 C ATOM 235 CG LEU A 67 -26.656 28.875 15.096 1.00 59.27 C ANISOU 235 CG LEU A 67 5574 6800 10144 1118 1261 -1659 C ATOM 236 CD1 LEU A 67 -27.906 28.124 14.651 1.00 59.82 C ANISOU 236 CD1 LEU A 67 5460 6903 10365 1108 1298 -1552 C ATOM 237 CD2 LEU A 67 -27.038 30.112 15.903 1.00 64.75 C ANISOU 237 CD2 LEU A 67 6218 7433 10949 1232 1381 -1875 C ATOM 238 N GLY A 68 -23.384 26.409 17.144 1.00 50.12 N ANISOU 238 N GLY A 68 4979 6029 8035 850 1315 -1587 N ATOM 239 CA GLY A 68 -22.772 25.533 18.141 1.00 49.69 C ANISOU 239 CA GLY A 68 5067 6123 7690 782 1390 -1581 C ATOM 240 C GLY A 68 -21.412 25.985 18.637 1.00 51.94 C ANISOU 240 C GLY A 68 5527 6404 7803 771 1310 -1666 C ATOM 241 O GLY A 68 -21.168 25.992 19.850 1.00 52.04 O ANISOU 241 O GLY A 68 5640 6512 7620 772 1416 -1777 O ATOM 242 N ASN A 69 -20.524 26.397 17.706 1.00 46.72 N ANISOU 242 N ASN A 69 4903 5631 7216 760 1123 -1617 N ATOM 243 CA ASN A 69 -19.188 26.881 18.067 1.00 46.19 C ANISOU 243 CA ASN A 69 4981 5543 7026 744 1028 -1692 C ATOM 244 C ASN A 69 -19.183 28.281 18.645 1.00 52.68 C ANISOU 244 C ASN A 69 5811 6282 7922 821 1059 -1896 C ATOM 245 O ASN A 69 -18.297 28.591 19.442 1.00 52.72 O ANISOU 245 O ASN A 69 5943 6312 7776 810 1036 -2003 O ATOM 246 CB ASN A 69 -18.185 26.709 16.938 1.00 43.50 C ANISOU 246 CB ASN A 69 4676 5129 6722 693 840 -1560 C ATOM 247 CG ASN A 69 -17.915 25.257 16.673 1.00 52.40 C ANISOU 247 CG ASN A 69 5840 6355 7715 615 814 -1396 C ATOM 248 OD1 ASN A 69 -17.248 24.589 17.463 1.00 49.03 O ANISOU 248 OD1 ASN A 69 5523 6028 7076 571 825 -1395 O ATOM 249 ND2 ASN A 69 -18.489 24.717 15.601 1.00 36.16 N ANISOU 249 ND2 ASN A 69 3692 4267 5779 600 776 -1258 N ATOM 250 N SER A 70 -20.182 29.120 18.290 1.00 50.66 N ANISOU 250 N SER A 70 5420 5925 7903 902 1105 -1957 N ATOM 251 CA SER A 70 -20.307 30.460 18.874 1.00 52.14 C ANISOU 251 CA SER A 70 5605 6021 8184 987 1147 -2167 C ATOM 252 C SER A 70 -20.755 30.305 20.319 1.00 57.83 C ANISOU 252 C SER A 70 6372 6879 8722 1014 1345 -2320 C ATOM 253 O SER A 70 -20.213 30.974 21.190 1.00 58.08 O ANISOU 253 O SER A 70 6510 6906 8651 1038 1359 -2493 O ATOM 254 CB SER A 70 -21.301 31.321 18.102 1.00 55.76 C ANISOU 254 CB SER A 70 5899 6332 8956 1073 1141 -2181 C ATOM 255 OG SER A 70 -20.713 31.788 16.898 1.00 63.25 O ANISOU 255 OG SER A 70 6842 7133 10059 1055 949 -2075 O ATOM 256 N VAL A 71 -21.702 29.377 20.572 1.00 55.55 N ANISOU 256 N VAL A 71 6010 6714 8381 1001 1496 -2250 N ATOM 257 CA VAL A 71 -22.213 29.063 21.909 1.00 57.33 C ANISOU 257 CA VAL A 71 6276 7092 8413 1013 1712 -2362 C ATOM 258 C VAL A 71 -21.067 28.488 22.751 1.00 61.27 C ANISOU 258 C VAL A 71 6985 7710 8586 938 1675 -2365 C ATOM 259 O VAL A 71 -20.825 28.993 23.842 1.00 62.47 O ANISOU 259 O VAL A 71 7245 7908 8581 967 1750 -2544 O ATOM 260 CB VAL A 71 -23.462 28.132 21.866 1.00 61.52 C ANISOU 260 CB VAL A 71 6666 7720 8988 999 1871 -2253 C ATOM 261 CG1 VAL A 71 -23.813 27.591 23.251 1.00 63.19 C ANISOU 261 CG1 VAL A 71 6951 8115 8945 980 2095 -2323 C ATOM 262 CG2 VAL A 71 -24.664 28.852 21.262 1.00 62.33 C ANISOU 262 CG2 VAL A 71 6555 7710 9419 1092 1923 -2296 C ATOM 263 N ALA A 72 -20.323 27.492 22.209 1.00 56.14 N ANISOU 263 N ALA A 72 6392 7093 7844 846 1543 -2176 N ATOM 264 CA ALA A 72 -19.194 26.843 22.883 1.00 55.26 C ANISOU 264 CA ALA A 72 6464 7083 7448 774 1477 -2149 C ATOM 265 C ALA A 72 -18.089 27.834 23.271 1.00 59.52 C ANISOU 265 C ALA A 72 7125 7553 7937 793 1356 -2305 C ATOM 266 O ALA A 72 -17.705 27.864 24.439 1.00 59.93 O ANISOU 266 O ALA A 72 7316 7697 7757 788 1403 -2421 O ATOM 267 CB ALA A 72 -18.636 25.722 22.024 1.00 53.61 C ANISOU 267 CB ALA A 72 6263 6886 7221 691 1343 -1924 C ATOM 268 N ILE A 73 -17.625 28.677 22.316 1.00 55.85 N ANISOU 268 N ILE A 73 6607 6923 7692 813 1204 -2309 N ATOM 269 CA ILE A 73 -16.596 29.708 22.545 1.00 56.44 C ANISOU 269 CA ILE A 73 6771 6902 7773 825 1076 -2450 C ATOM 270 C ILE A 73 -17.048 30.750 23.595 1.00 64.95 C ANISOU 270 C ILE A 73 7882 7966 8832 906 1194 -2705 C ATOM 271 O ILE A 73 -16.238 31.163 24.423 1.00 65.40 O ANISOU 271 O ILE A 73 8075 8037 8736 898 1142 -2846 O ATOM 272 CB ILE A 73 -16.071 30.303 21.201 1.00 57.43 C ANISOU 272 CB ILE A 73 6823 6852 8147 817 901 -2367 C ATOM 273 CG1 ILE A 73 -15.190 29.265 20.477 1.00 55.52 C ANISOU 273 CG1 ILE A 73 6612 6650 7834 727 773 -2161 C ATOM 274 CG2 ILE A 73 -15.315 31.627 21.378 1.00 58.40 C ANISOU 274 CG2 ILE A 73 6996 6837 8356 842 796 -2533 C ATOM 275 CD1 ILE A 73 -15.042 29.467 19.009 1.00 59.60 C ANISOU 275 CD1 ILE A 73 7036 7038 8573 713 656 -2022 C ATOM 276 N TRP A 74 -18.351 31.112 23.589 1.00 64.56 N ANISOU 276 N TRP A 74 7706 7895 8930 985 1355 -2767 N ATOM 277 CA TRP A 74 -18.996 32.041 24.532 1.00 67.77 C ANISOU 277 CA TRP A 74 8118 8291 9341 1077 1504 -3013 C ATOM 278 C TRP A 74 -19.005 31.400 25.927 1.00 72.39 C ANISOU 278 C TRP A 74 8846 9076 9581 1054 1651 -3093 C ATOM 279 O TRP A 74 -18.600 32.041 26.896 1.00 73.44 O ANISOU 279 O TRP A 74 9108 9222 9575 1082 1665 -3298 O ATOM 280 CB TRP A 74 -20.441 32.337 24.053 1.00 67.89 C ANISOU 280 CB TRP A 74 7933 8250 9611 1161 1646 -3016 C ATOM 281 CG TRP A 74 -21.249 33.301 24.875 1.00 72.15 C ANISOU 281 CG TRP A 74 8440 8762 10211 1273 1816 -3267 C ATOM 282 CD1 TRP A 74 -21.803 33.069 26.100 1.00 77.28 C ANISOU 282 CD1 TRP A 74 9145 9567 10652 1300 2036 -3403 C ATOM 283 CD2 TRP A 74 -21.737 34.582 24.451 1.00 73.29 C ANISOU 283 CD2 TRP A 74 8469 8713 10666 1378 1796 -3398 C ATOM 284 NE1 TRP A 74 -22.532 34.164 26.504 1.00 79.20 N ANISOU 284 NE1 TRP A 74 9319 9725 11046 1420 2159 -3632 N ATOM 285 CE2 TRP A 74 -22.513 35.106 25.508 1.00 80.04 C ANISOU 285 CE2 TRP A 74 9317 9612 11483 1473 2009 -3634 C ATOM 286 CE3 TRP A 74 -21.563 35.360 23.291 1.00 73.66 C ANISOU 286 CE3 TRP A 74 8425 8548 11013 1403 1618 -3338 C ATOM 287 CZ2 TRP A 74 -23.117 36.369 25.441 1.00 81.24 C ANISOU 287 CZ2 TRP A 74 9368 9594 11906 1597 2043 -3820 C ATOM 288 CZ3 TRP A 74 -22.154 36.613 23.230 1.00 76.92 C ANISOU 288 CZ3 TRP A 74 8745 8790 11691 1520 1642 -3507 C ATOM 289 CH2 TRP A 74 -22.924 37.105 24.293 1.00 80.30 C ANISOU 289 CH2 TRP A 74 9160 9258 12094 1619 1849 -3749 C ATOM 290 N MET A 75 -19.453 30.129 26.013 1.00 68.25 N ANISOU 290 N MET A 75 8308 8705 8919 997 1752 -2925 N ATOM 291 CA MET A 75 -19.542 29.351 27.251 1.00 69.62 C ANISOU 291 CA MET A 75 8615 9077 8760 961 1899 -2948 C ATOM 292 C MET A 75 -18.181 29.099 27.909 1.00 72.64 C ANISOU 292 C MET A 75 9213 9521 8865 895 1749 -2964 C ATOM 293 O MET A 75 -18.100 29.172 29.131 1.00 74.28 O ANISOU 293 O MET A 75 9568 9842 8813 902 1841 -3103 O ATOM 294 CB MET A 75 -20.290 28.025 27.029 1.00 71.52 C ANISOU 294 CB MET A 75 8776 9437 8960 904 2016 -2733 C ATOM 295 CG MET A 75 -21.780 28.182 26.770 1.00 76.78 C ANISOU 295 CG MET A 75 9241 10092 9838 967 2216 -2748 C ATOM 296 SD MET A 75 -22.741 28.674 28.214 1.00 85.50 S ANISOU 296 SD MET A 75 10372 11315 10799 1044 2524 -2989 S ATOM 297 CE MET A 75 -22.851 27.107 29.075 1.00 82.76 C ANISOU 297 CE MET A 75 10145 11206 10096 934 2667 -2827 C ATOM 298 N PHE A 76 -17.120 28.798 27.125 1.00 65.39 N ANISOU 298 N PHE A 76 8314 8535 7998 833 1521 -2825 N ATOM 299 CA PHE A 76 -15.789 28.563 27.697 1.00 64.56 C ANISOU 299 CA PHE A 76 8389 8476 7663 773 1359 -2835 C ATOM 300 C PHE A 76 -15.130 29.848 28.220 1.00 71.02 C ANISOU 300 C PHE A 76 9295 9203 8485 816 1266 -3076 C ATOM 301 O PHE A 76 -14.514 29.821 29.283 1.00 71.20 O ANISOU 301 O PHE A 76 9493 9314 8247 796 1233 -3182 O ATOM 302 CB PHE A 76 -14.852 27.825 26.719 1.00 63.13 C ANISOU 302 CB PHE A 76 8187 8254 7547 697 1159 -2619 C ATOM 303 CG PHE A 76 -15.078 26.333 26.586 1.00 62.84 C ANISOU 303 CG PHE A 76 8148 8337 7389 633 1203 -2395 C ATOM 304 CD1 PHE A 76 -14.852 25.478 27.661 1.00 66.26 C ANISOU 304 CD1 PHE A 76 8735 8930 7510 587 1243 -2365 C ATOM 305 CD2 PHE A 76 -15.463 25.777 25.372 1.00 61.90 C ANISOU 305 CD2 PHE A 76 7884 8165 7469 613 1186 -2210 C ATOM 306 CE1 PHE A 76 -15.052 24.099 27.533 1.00 65.84 C ANISOU 306 CE1 PHE A 76 8682 8970 7363 525 1276 -2152 C ATOM 307 CE2 PHE A 76 -15.663 24.398 25.246 1.00 63.34 C ANISOU 307 CE2 PHE A 76 8068 8444 7554 552 1218 -2013 C ATOM 308 CZ PHE A 76 -15.455 23.569 26.326 1.00 62.41 C ANISOU 308 CZ PHE A 76 8096 8474 7143 508 1263 -1983 C ATOM 309 N VAL A 77 -15.278 30.966 27.483 1.00 69.04 N ANISOU 309 N VAL A 77 8930 8771 8531 872 1218 -3161 N ATOM 310 CA VAL A 77 -14.696 32.271 27.825 1.00 70.89 C ANISOU 310 CA VAL A 77 9225 8879 8830 912 1118 -3387 C ATOM 311 C VAL A 77 -15.405 32.975 29.003 1.00 79.45 C ANISOU 311 C VAL A 77 10380 10009 9800 994 1295 -3650 C ATOM 312 O VAL A 77 -14.739 33.371 29.965 1.00 80.33 O ANISOU 312 O VAL A 77 10655 10150 9716 990 1236 -3825 O ATOM 313 CB VAL A 77 -14.555 33.176 26.564 1.00 73.43 C ANISOU 313 CB VAL A 77 9405 8978 9516 934 992 -3359 C ATOM 314 CG1 VAL A 77 -14.246 34.628 26.925 1.00 74.86 C ANISOU 314 CG1 VAL A 77 9627 9007 9809 988 926 -3609 C ATOM 315 CG2 VAL A 77 -13.499 32.627 25.609 1.00 70.73 C ANISOU 315 CG2 VAL A 77 9045 8598 9229 845 795 -3148 C ATOM 316 N PHE A 78 -16.742 33.133 28.920 1.00 78.58 N ANISOU 316 N PHE A 78 10143 9902 9812 1070 1507 -3685 N ATOM 317 CA PHE A 78 -17.538 33.852 29.922 1.00 81.99 C ANISOU 317 CA PHE A 78 10610 10364 10177 1164 1704 -3943 C ATOM 318 C PHE A 78 -18.270 33.004 30.970 1.00 87.69 C ANISOU 318 C PHE A 78 11409 11316 10595 1159 1945 -3952 C ATOM 319 O PHE A 78 -18.780 33.575 31.936 1.00 90.27 O ANISOU 319 O PHE A 78 11802 11689 10806 1229 2107 -4184 O ATOM 320 CB PHE A 78 -18.522 34.825 29.241 1.00 84.66 C ANISOU 320 CB PHE A 78 10755 10534 10879 1270 1785 -4028 C ATOM 321 CG PHE A 78 -17.932 35.692 28.153 1.00 85.21 C ANISOU 321 CG PHE A 78 10744 10369 11264 1275 1565 -4002 C ATOM 322 CD1 PHE A 78 -17.117 36.774 28.467 1.00 89.76 C ANISOU 322 CD1 PHE A 78 11416 10810 11880 1293 1424 -4199 C ATOM 323 CD2 PHE A 78 -18.213 35.443 26.815 1.00 85.65 C ANISOU 323 CD2 PHE A 78 10632 10334 11577 1259 1499 -3781 C ATOM 324 CE1 PHE A 78 -16.570 37.576 27.459 1.00 89.76 C ANISOU 324 CE1 PHE A 78 11341 10588 12175 1288 1229 -4160 C ATOM 325 CE2 PHE A 78 -17.667 36.246 25.807 1.00 87.68 C ANISOU 325 CE2 PHE A 78 10827 10379 12108 1257 1304 -3743 C ATOM 326 CZ PHE A 78 -16.851 37.308 26.137 1.00 86.84 C ANISOU 326 CZ PHE A 78 10813 10140 12044 1270 1176 -3927 C ATOM 327 N HIS A 79 -18.353 31.670 30.791 1.00 82.58 N ANISOU 327 N HIS A 79 10751 10804 9820 1078 1978 -3706 N ATOM 328 CA HIS A 79 -19.074 30.807 31.738 1.00 84.10 C ANISOU 328 CA HIS A 79 11010 11210 9734 1061 2215 -3683 C ATOM 329 C HIS A 79 -18.246 29.603 32.239 1.00 85.85 C ANISOU 329 C HIS A 79 11409 11588 9623 950 2128 -3519 C ATOM 330 O HIS A 79 -18.816 28.569 32.600 1.00 85.69 O ANISOU 330 O HIS A 79 11402 11724 9431 905 2287 -3385 O ATOM 331 CB HIS A 79 -20.435 30.363 31.149 1.00 85.04 C ANISOU 331 CB HIS A 79 10911 11349 10051 1086 2419 -3560 C ATOM 332 CG HIS A 79 -21.292 31.496 30.671 1.00 89.74 C ANISOU 332 CG HIS A 79 11322 11791 10982 1202 2499 -3711 C ATOM 333 ND1 HIS A 79 -22.093 32.215 31.545 1.00 94.70 N ANISOU 333 ND1 HIS A 79 11949 12453 11580 1298 2724 -3956 N ATOM 334 CD2 HIS A 79 -21.433 32.009 29.426 1.00 90.06 C ANISOU 334 CD2 HIS A 79 11186 11645 11388 1236 2375 -3646 C ATOM 335 CE1 HIS A 79 -22.695 33.133 30.806 1.00 94.24 C ANISOU 335 CE1 HIS A 79 11702 12219 11885 1392 2724 -4033 C ATOM 336 NE2 HIS A 79 -22.331 33.048 29.525 1.00 91.83 N ANISOU 336 NE2 HIS A 79 11292 11777 11823 1356 2512 -3845 N ATOM 337 N MET A 80 -16.904 29.745 32.267 1.00 80.71 N ANISOU 337 N MET A 80 10887 10887 8891 904 1871 -3527 N ATOM 338 CA MET A 80 -15.979 28.701 32.727 1.00 79.67 C ANISOU 338 CA MET A 80 10924 10879 8470 809 1745 -3382 C ATOM 339 C MET A 80 -14.684 29.327 33.274 1.00 84.38 C ANISOU 339 C MET A 80 11692 11432 8935 797 1520 -3535 C ATOM 340 O MET A 80 -13.908 29.910 32.512 1.00 82.30 O ANISOU 340 O MET A 80 11366 11009 8895 794 1314 -3546 O ATOM 341 CB MET A 80 -15.696 27.675 31.606 1.00 78.82 C ANISOU 341 CB MET A 80 10705 10741 8502 737 1627 -3088 C ATOM 342 CG MET A 80 -14.834 26.506 32.042 1.00 81.82 C ANISOU 342 CG MET A 80 11238 11240 8609 646 1508 -2922 C ATOM 343 SD MET A 80 -15.750 25.180 32.848 1.00 87.20 S ANISOU 343 SD MET A 80 11988 12136 9008 598 1749 -2773 S ATOM 344 CE MET A 80 -16.066 24.116 31.447 1.00 80.82 C ANISOU 344 CE MET A 80 10985 11271 8452 547 1717 -2474 C ATOM 345 N LYS A 81 -14.476 29.219 34.605 1.00 83.49 N ANISOU 345 N LYS A 81 11797 11464 8461 786 1561 -3654 N ATOM 346 CA LYS A 81 -13.300 29.741 35.312 1.00 84.42 C ANISOU 346 CA LYS A 81 12101 11567 8407 771 1348 -3812 C ATOM 347 C LYS A 81 -13.059 28.976 36.635 1.00 90.94 C ANISOU 347 C LYS A 81 13173 12602 8778 724 1377 -3807 C ATOM 348 O LYS A 81 -13.897 29.053 37.534 1.00 93.05 O ANISOU 348 O LYS A 81 13529 12992 8833 761 1611 -3928 O ATOM 349 CB LYS A 81 -13.427 31.260 35.562 1.00 88.46 C ANISOU 349 CB LYS A 81 12615 11953 9044 858 1360 -4126 C ATOM 350 CG LYS A 81 -12.141 31.930 36.038 1.00 99.20 C ANISOU 350 CG LYS A 81 14126 13245 10319 836 1095 -4288 C ATOM 351 CD LYS A 81 -12.351 33.405 36.331 1.00109.64 C ANISOU 351 CD LYS A 81 15458 14438 11764 922 1121 -4607 C ATOM 352 CE LYS A 81 -11.070 34.081 36.748 1.00121.59 C ANISOU 352 CE LYS A 81 17107 15867 13224 892 841 -4767 C ATOM 353 NZ LYS A 81 -11.293 35.503 37.119 1.00133.28 N ANISOU 353 NZ LYS A 81 18614 17216 14809 976 868 -5094 N ATOM 354 N PRO A 82 -11.933 28.239 36.793 1.00 87.12 N ANISOU 354 N PRO A 82 12805 12161 8134 646 1146 -3667 N ATOM 355 CA PRO A 82 -10.843 28.019 35.826 1.00 83.96 C ANISOU 355 CA PRO A 82 12314 11638 7947 596 872 -3517 C ATOM 356 C PRO A 82 -11.137 26.881 34.846 1.00 83.87 C ANISOU 356 C PRO A 82 12154 11635 8079 553 910 -3216 C ATOM 357 O PRO A 82 -12.095 26.126 35.043 1.00 83.92 O ANISOU 357 O PRO A 82 12151 11757 7978 545 1125 -3105 O ATOM 358 CB PRO A 82 -9.650 27.711 36.736 1.00 87.15 C ANISOU 358 CB PRO A 82 12937 12120 8057 543 645 -3537 C ATOM 359 CG PRO A 82 -10.262 26.986 37.911 1.00 94.20 C ANISOU 359 CG PRO A 82 14016 13223 8551 530 826 -3516 C ATOM 360 CD PRO A 82 -11.679 27.514 38.057 1.00 91.07 C ANISOU 360 CD PRO A 82 13554 12855 8194 601 1151 -3649 C ATOM 361 N TRP A 83 -10.307 26.755 33.794 1.00 76.53 N ANISOU 361 N TRP A 83 11107 10581 7391 521 704 -3089 N ATOM 362 CA TRP A 83 -10.449 25.697 32.796 1.00 73.24 C ANISOU 362 CA TRP A 83 10555 10154 7117 480 708 -2819 C ATOM 363 C TRP A 83 -9.664 24.472 33.225 1.00 74.60 C ANISOU 363 C TRP A 83 10855 10432 7058 411 574 -2641 C ATOM 364 O TRP A 83 -8.502 24.590 33.611 1.00 74.36 O ANISOU 364 O TRP A 83 10929 10392 6934 387 352 -2687 O ATOM 365 CB TRP A 83 -9.941 26.153 31.413 1.00 69.67 C ANISOU 365 CB TRP A 83 9922 9521 7030 483 564 -2770 C ATOM 366 CG TRP A 83 -10.712 27.261 30.757 1.00 70.51 C ANISOU 366 CG TRP A 83 9880 9498 7413 548 673 -2893 C ATOM 367 CD1 TRP A 83 -11.721 28.002 31.299 1.00 75.39 C ANISOU 367 CD1 TRP A 83 10503 10132 8011 615 868 -3073 C ATOM 368 CD2 TRP A 83 -10.502 27.774 29.437 1.00 68.29 C ANISOU 368 CD2 TRP A 83 9427 9047 7474 555 584 -2844 C ATOM 369 NE1 TRP A 83 -12.158 28.940 30.396 1.00 74.24 N ANISOU 369 NE1 TRP A 83 10193 9827 8188 667 895 -3137 N ATOM 370 CE2 TRP A 83 -11.426 28.826 29.244 1.00 73.21 C ANISOU 370 CE2 TRP A 83 9959 9581 8276 629 720 -2992 C ATOM 371 CE3 TRP A 83 -9.625 27.443 28.392 1.00 67.00 C ANISOU 371 CE3 TRP A 83 9178 8798 7482 509 408 -2687 C ATOM 372 CZ2 TRP A 83 -11.497 29.549 28.048 1.00 71.06 C ANISOU 372 CZ2 TRP A 83 9524 9134 8339 652 671 -2975 C ATOM 373 CZ3 TRP A 83 -9.683 28.173 27.216 1.00 66.98 C ANISOU 373 CZ3 TRP A 83 9020 8633 7795 528 376 -2676 C ATOM 374 CH2 TRP A 83 -10.615 29.207 27.049 1.00 68.50 C ANISOU 374 CH2 TRP A 83 9135 8738 8154 597 499 -2811 C ATOM 375 N SER A 84 -10.282 23.291 33.118 1.00 69.32 N ANISOU 375 N SER A 84 10167 9852 6320 378 696 -2434 N ATOM 376 CA SER A 84 -9.637 22.013 33.419 1.00 68.34 C ANISOU 376 CA SER A 84 10148 9812 6008 314 577 -2235 C ATOM 377 C SER A 84 -8.736 21.614 32.228 1.00 68.22 C ANISOU 377 C SER A 84 10001 9675 6243 289 373 -2086 C ATOM 378 O SER A 84 -8.617 22.376 31.262 1.00 66.10 O ANISOU 378 O SER A 84 9581 9273 6260 316 333 -2143 O ATOM 379 CB SER A 84 -10.695 20.942 33.670 1.00 72.03 C ANISOU 379 CB SER A 84 10629 10397 6341 284 793 -2069 C ATOM 380 OG SER A 84 -11.498 20.711 32.522 1.00 76.36 O ANISOU 380 OG SER A 84 10971 10872 7169 290 910 -1958 O ATOM 381 N GLY A 85 -8.118 20.434 32.308 1.00 63.37 N ANISOU 381 N GLY A 85 9449 9108 5520 240 251 -1897 N ATOM 382 CA GLY A 85 -7.274 19.900 31.247 1.00 60.06 C ANISOU 382 CA GLY A 85 8917 8592 5312 219 75 -1749 C ATOM 383 C GLY A 85 -8.047 19.763 29.951 1.00 60.51 C ANISOU 383 C GLY A 85 8776 8567 5646 229 197 -1655 C ATOM 384 O GLY A 85 -7.700 20.413 28.962 1.00 58.28 O ANISOU 384 O GLY A 85 8359 8162 5622 248 127 -1695 O ATOM 385 N ILE A 86 -9.149 18.977 29.978 1.00 56.75 N ANISOU 385 N ILE A 86 8286 8160 5118 214 387 -1535 N ATOM 386 CA ILE A 86 -10.034 18.755 28.822 1.00 55.18 C ANISOU 386 CA ILE A 86 7907 7895 5163 219 509 -1440 C ATOM 387 C ILE A 86 -10.652 20.036 28.250 1.00 56.67 C ANISOU 387 C ILE A 86 7967 7997 5566 273 601 -1597 C ATOM 388 O ILE A 86 -10.878 20.096 27.043 1.00 54.35 O ANISOU 388 O ILE A 86 7519 7605 5526 282 595 -1537 O ATOM 389 CB ILE A 86 -11.116 17.657 29.041 1.00 59.31 C ANISOU 389 CB ILE A 86 8436 8507 5592 183 689 -1284 C ATOM 390 CG1 ILE A 86 -11.974 17.901 30.295 1.00 62.48 C ANISOU 390 CG1 ILE A 86 8949 9038 5753 187 889 -1378 C ATOM 391 CG2 ILE A 86 -10.544 16.253 28.980 1.00 60.16 C ANISOU 391 CG2 ILE A 86 8600 8634 5624 129 573 -1072 C ATOM 392 CD1 ILE A 86 -13.317 18.514 29.980 1.00 72.91 C ANISOU 392 CD1 ILE A 86 10132 10347 7224 223 1119 -1457 C ATOM 393 N SER A 87 -10.956 21.032 29.114 1.00 53.41 N ANISOU 393 N SER A 87 7624 7620 5049 311 685 -1798 N ATOM 394 CA SER A 87 -11.546 22.317 28.718 1.00 52.62 C ANISOU 394 CA SER A 87 7414 7429 5148 372 771 -1965 C ATOM 395 C SER A 87 -10.614 23.087 27.789 1.00 54.40 C ANISOU 395 C SER A 87 7557 7505 5610 384 583 -2009 C ATOM 396 O SER A 87 -11.086 23.708 26.832 1.00 53.26 O ANISOU 396 O SER A 87 7265 7251 5719 416 623 -2027 O ATOM 397 CB SER A 87 -11.900 23.157 29.940 1.00 57.66 C ANISOU 397 CB SER A 87 8168 8136 5604 411 881 -2183 C ATOM 398 OG SER A 87 -13.075 22.661 30.558 1.00 66.43 O ANISOU 398 OG SER A 87 9300 9368 6574 411 1119 -2154 O ATOM 399 N VAL A 88 -9.289 23.017 28.060 1.00 50.02 N ANISOU 399 N VAL A 88 7090 6941 4973 354 377 -2015 N ATOM 400 CA VAL A 88 -8.242 23.640 27.245 1.00 48.09 C ANISOU 400 CA VAL A 88 6771 6564 4939 350 192 -2040 C ATOM 401 C VAL A 88 -8.282 22.996 25.839 1.00 47.41 C ANISOU 401 C VAL A 88 6537 6410 5067 332 175 -1850 C ATOM 402 O VAL A 88 -8.395 23.722 24.853 1.00 45.58 O ANISOU 402 O VAL A 88 6182 6060 5076 352 171 -1870 O ATOM 403 CB VAL A 88 -6.837 23.545 27.914 1.00 52.60 C ANISOU 403 CB VAL A 88 7459 7156 5369 318 -23 -2076 C ATOM 404 CG1 VAL A 88 -5.725 23.964 26.953 1.00 50.79 C ANISOU 404 CG1 VAL A 88 7126 6796 5376 300 -204 -2060 C ATOM 405 CG2 VAL A 88 -6.778 24.368 29.197 1.00 54.94 C ANISOU 405 CG2 VAL A 88 7902 7500 5473 338 -25 -2294 C ATOM 406 N TYR A 89 -8.256 21.642 25.767 1.00 42.03 N ANISOU 406 N TYR A 89 5877 5801 4290 296 171 -1668 N ATOM 407 CA TYR A 89 -8.306 20.897 24.508 1.00 39.60 C ANISOU 407 CA TYR A 89 5451 5440 4155 278 155 -1493 C ATOM 408 C TYR A 89 -9.631 21.108 23.763 1.00 44.21 C ANISOU 408 C TYR A 89 5914 5987 4897 304 320 -1469 C ATOM 409 O TYR A 89 -9.632 21.237 22.533 1.00 42.47 O ANISOU 409 O TYR A 89 5576 5671 4888 307 289 -1406 O ATOM 410 CB TYR A 89 -8.066 19.389 24.734 1.00 39.95 C ANISOU 410 CB TYR A 89 5559 5565 4054 238 118 -1319 C ATOM 411 CG TYR A 89 -6.782 19.018 25.447 1.00 41.72 C ANISOU 411 CG TYR A 89 5896 5827 4128 216 -59 -1315 C ATOM 412 CD1 TYR A 89 -5.559 19.567 25.061 1.00 42.80 C ANISOU 412 CD1 TYR A 89 5997 5885 4382 216 -233 -1368 C ATOM 413 CD2 TYR A 89 -6.771 18.041 26.439 1.00 43.33 C ANISOU 413 CD2 TYR A 89 6235 6140 4089 191 -63 -1236 C ATOM 414 CE1 TYR A 89 -4.370 19.192 25.682 1.00 43.11 C ANISOU 414 CE1 TYR A 89 6121 5953 4307 198 -411 -1359 C ATOM 415 CE2 TYR A 89 -5.587 17.660 27.069 1.00 44.50 C ANISOU 415 CE2 TYR A 89 6484 6317 4108 175 -248 -1220 C ATOM 416 CZ TYR A 89 -4.390 18.241 26.690 1.00 50.40 C ANISOU 416 CZ TYR A 89 7181 6984 4984 181 -426 -1287 C ATOM 417 OH TYR A 89 -3.226 17.870 27.315 1.00 51.45 O ANISOU 417 OH TYR A 89 7398 7141 5007 167 -620 -1273 O ATOM 418 N MET A 90 -10.752 21.137 24.506 1.00 43.07 N ANISOU 418 N MET A 90 5798 5920 4647 321 495 -1519 N ATOM 419 CA MET A 90 -12.086 21.341 23.942 1.00 43.31 C ANISOU 419 CA MET A 90 5704 5923 4828 348 656 -1507 C ATOM 420 C MET A 90 -12.261 22.735 23.377 1.00 48.00 C ANISOU 420 C MET A 90 6204 6396 5637 401 653 -1641 C ATOM 421 O MET A 90 -12.892 22.882 22.328 1.00 46.54 O ANISOU 421 O MET A 90 5888 6133 5660 418 684 -1582 O ATOM 422 CB MET A 90 -13.187 20.985 24.946 1.00 47.41 C ANISOU 422 CB MET A 90 6268 6563 5182 350 854 -1526 C ATOM 423 CG MET A 90 -13.425 19.496 25.028 1.00 50.93 C ANISOU 423 CG MET A 90 6744 7093 5516 292 888 -1333 C ATOM 424 SD MET A 90 -14.625 19.034 26.287 1.00 58.01 S ANISOU 424 SD MET A 90 7702 8140 6200 278 1133 -1338 S ATOM 425 CE MET A 90 -14.775 17.296 25.914 1.00 53.80 C ANISOU 425 CE MET A 90 7165 7642 5634 200 1119 -1076 C ATOM 426 N PHE A 91 -11.668 23.752 24.036 1.00 46.58 N ANISOU 426 N PHE A 91 6096 6191 5413 426 599 -1816 N ATOM 427 CA PHE A 91 -11.718 25.130 23.546 1.00 47.01 C ANISOU 427 CA PHE A 91 6073 6111 5679 473 577 -1947 C ATOM 428 C PHE A 91 -10.905 25.245 22.251 1.00 48.08 C ANISOU 428 C PHE A 91 6128 6126 6013 449 424 -1848 C ATOM 429 O PHE A 91 -11.335 25.923 21.319 1.00 47.89 O ANISOU 429 O PHE A 91 5994 5990 6212 477 434 -1846 O ATOM 430 CB PHE A 91 -11.214 26.130 24.600 1.00 50.88 C ANISOU 430 CB PHE A 91 6670 6595 6068 498 543 -2163 C ATOM 431 CG PHE A 91 -11.163 27.559 24.107 1.00 53.18 C ANISOU 431 CG PHE A 91 6889 6726 6591 541 499 -2297 C ATOM 432 CD1 PHE A 91 -12.316 28.336 24.050 1.00 57.84 C ANISOU 432 CD1 PHE A 91 7401 7263 7313 610 640 -2398 C ATOM 433 CD2 PHE A 91 -9.962 28.128 23.694 1.00 55.43 C ANISOU 433 CD2 PHE A 91 7178 6907 6977 513 317 -2319 C ATOM 434 CE1 PHE A 91 -12.266 29.660 23.597 1.00 59.54 C ANISOU 434 CE1 PHE A 91 7553 7314 7754 652 590 -2516 C ATOM 435 CE2 PHE A 91 -9.914 29.452 23.240 1.00 58.95 C ANISOU 435 CE2 PHE A 91 7561 7193 7645 545 275 -2432 C ATOM 436 CZ PHE A 91 -11.067 30.208 23.192 1.00 57.99 C ANISOU 436 CZ PHE A 91 7372 7011 7648 616 407 -2527 C ATOM 437 N ASN A 92 -9.749 24.570 22.195 1.00 42.65 N ANISOU 437 N ASN A 92 5495 5464 5245 398 285 -1764 N ATOM 438 CA ASN A 92 -8.885 24.567 21.017 1.00 40.97 C ANISOU 438 CA ASN A 92 5213 5158 5197 369 154 -1666 C ATOM 439 C ASN A 92 -9.553 23.887 19.826 1.00 44.59 C ANISOU 439 C ASN A 92 5570 5596 5775 364 203 -1501 C ATOM 440 O ASN A 92 -9.441 24.389 18.709 1.00 44.24 O ANISOU 440 O ASN A 92 5441 5446 5922 366 159 -1462 O ATOM 441 CB ASN A 92 -7.516 23.981 21.334 1.00 37.24 C ANISOU 441 CB ASN A 92 4812 4725 4613 324 5 -1627 C ATOM 442 CG ASN A 92 -6.598 24.992 21.970 1.00 54.13 C ANISOU 442 CG ASN A 92 7002 6817 6746 321 -105 -1785 C ATOM 443 OD1 ASN A 92 -6.022 25.853 21.295 1.00 46.30 O ANISOU 443 OD1 ASN A 92 5945 5708 5939 313 -185 -1817 O ATOM 444 ND2 ASN A 92 -6.486 24.956 23.291 1.00 44.90 N ANISOU 444 ND2 ASN A 92 5957 5735 5366 325 -111 -1890 N ATOM 445 N LEU A 93 -10.287 22.780 20.076 1.00 40.98 N ANISOU 445 N LEU A 93 5128 5238 5204 355 294 -1407 N ATOM 446 CA LEU A 93 -11.062 22.050 19.070 1.00 40.08 C ANISOU 446 CA LEU A 93 4927 5114 5189 347 344 -1262 C ATOM 447 C LEU A 93 -12.187 22.962 18.509 1.00 44.96 C ANISOU 447 C LEU A 93 5437 5652 5994 394 429 -1311 C ATOM 448 O LEU A 93 -12.433 22.964 17.297 1.00 43.73 O ANISOU 448 O LEU A 93 5194 5421 5999 394 397 -1222 O ATOM 449 CB LEU A 93 -11.663 20.774 19.708 1.00 40.38 C ANISOU 449 CB LEU A 93 5011 5271 5062 322 432 -1175 C ATOM 450 CG LEU A 93 -12.476 19.846 18.812 1.00 43.89 C ANISOU 450 CG LEU A 93 5374 5712 5590 304 474 -1024 C ATOM 451 CD1 LEU A 93 -11.573 19.063 17.889 1.00 43.36 C ANISOU 451 CD1 LEU A 93 5310 5612 5554 270 345 -902 C ATOM 452 CD2 LEU A 93 -13.269 18.861 19.643 1.00 46.64 C ANISOU 452 CD2 LEU A 93 5759 6168 5793 279 592 -968 C ATOM 453 N ALA A 94 -12.851 23.725 19.396 1.00 42.79 N ANISOU 453 N ALA A 94 5171 5394 5694 437 533 -1455 N ATOM 454 CA ALA A 94 -13.918 24.671 19.052 1.00 44.02 C ANISOU 454 CA ALA A 94 5223 5471 6031 495 616 -1527 C ATOM 455 C ALA A 94 -13.365 25.838 18.232 1.00 49.23 C ANISOU 455 C ALA A 94 5842 5982 6883 514 506 -1570 C ATOM 456 O ALA A 94 -14.054 26.341 17.345 1.00 48.55 O ANISOU 456 O ALA A 94 5653 5801 6992 545 513 -1540 O ATOM 457 CB ALA A 94 -14.595 25.189 20.318 1.00 46.53 C ANISOU 457 CB ALA A 94 5576 5848 6256 540 757 -1691 C ATOM 458 N LEU A 95 -12.118 26.249 18.526 1.00 46.85 N ANISOU 458 N LEU A 95 5618 5654 6530 491 396 -1633 N ATOM 459 CA LEU A 95 -11.409 27.322 17.839 1.00 46.99 C ANISOU 459 CA LEU A 95 5607 5529 6718 491 286 -1667 C ATOM 460 C LEU A 95 -11.049 26.895 16.414 1.00 49.14 C ANISOU 460 C LEU A 95 5820 5749 7100 454 206 -1492 C ATOM 461 O LEU A 95 -11.161 27.701 15.490 1.00 48.91 O ANISOU 461 O LEU A 95 5727 5597 7258 467 169 -1471 O ATOM 462 CB LEU A 95 -10.146 27.678 18.629 1.00 48.15 C ANISOU 462 CB LEU A 95 5849 5681 6765 463 189 -1771 C ATOM 463 CG LEU A 95 -9.707 29.133 18.608 1.00 54.56 C ANISOU 463 CG LEU A 95 6652 6352 7728 479 122 -1905 C ATOM 464 CD1 LEU A 95 -10.619 29.997 19.475 1.00 56.96 C ANISOU 464 CD1 LEU A 95 6967 6636 8038 549 224 -2090 C ATOM 465 CD2 LEU A 95 -8.266 29.260 19.096 1.00 57.39 C ANISOU 465 CD2 LEU A 95 7082 6710 8014 429 -11 -1958 C ATOM 466 N ALA A 96 -10.641 25.618 16.240 1.00 44.41 N ANISOU 466 N ALA A 96 5251 5242 6381 409 183 -1368 N ATOM 467 CA ALA A 96 -10.305 25.021 14.949 1.00 42.22 C ANISOU 467 CA ALA A 96 4933 4936 6172 375 121 -1209 C ATOM 468 C ALA A 96 -11.562 24.893 14.071 1.00 44.76 C ANISOU 468 C ALA A 96 5172 5226 6610 401 178 -1128 C ATOM 469 O ALA A 96 -11.480 25.040 12.848 1.00 43.36 O ANISOU 469 O ALA A 96 4951 4973 6552 391 122 -1036 O ATOM 470 CB ALA A 96 -9.672 23.655 15.156 1.00 41.93 C ANISOU 470 CB ALA A 96 4952 5004 5977 334 92 -1120 C ATOM 471 N ASP A 97 -12.716 24.605 14.694 1.00 41.62 N ANISOU 471 N ASP A 97 4751 4889 6173 431 287 -1159 N ATOM 472 CA ASP A 97 -13.984 24.442 13.989 1.00 40.77 C ANISOU 472 CA ASP A 97 4550 4757 6184 455 338 -1090 C ATOM 473 C ASP A 97 -14.587 25.768 13.536 1.00 45.11 C ANISOU 473 C ASP A 97 5024 5181 6936 509 335 -1152 C ATOM 474 O ASP A 97 -14.930 25.896 12.362 1.00 44.26 O ANISOU 474 O ASP A 97 4856 4996 6963 513 280 -1058 O ATOM 475 CB ASP A 97 -14.962 23.575 14.794 1.00 42.91 C ANISOU 475 CB ASP A 97 4808 5139 6357 458 461 -1088 C ATOM 476 CG ASP A 97 -14.680 22.080 14.687 1.00 49.01 C ANISOU 476 CG ASP A 97 5625 6000 6998 401 444 -960 C ATOM 477 OD1 ASP A 97 -14.307 21.621 13.587 1.00 49.36 O ANISOU 477 OD1 ASP A 97 5660 6007 7090 373 354 -850 O ATOM 478 OD2 ASP A 97 -14.883 21.366 15.685 1.00 52.04 O ANISOU 478 OD2 ASP A 97 6055 6486 7233 384 522 -969 O ATOM 479 N PHE A 98 -14.663 26.759 14.445 1.00 42.41 N ANISOU 479 N PHE A 98 4693 4811 6612 553 382 -1312 N ATOM 480 CA PHE A 98 -15.180 28.108 14.197 1.00 43.28 C ANISOU 480 CA PHE A 98 4738 4787 6921 614 379 -1396 C ATOM 481 C PHE A 98 -14.401 28.815 13.077 1.00 47.55 C ANISOU 481 C PHE A 98 5279 5194 7594 592 246 -1329 C ATOM 482 O PHE A 98 -15.031 29.426 12.207 1.00 47.27 O ANISOU 482 O PHE A 98 5170 5050 7740 626 214 -1284 O ATOM 483 CB PHE A 98 -15.130 28.935 15.495 1.00 46.27 C ANISOU 483 CB PHE A 98 5158 5166 7256 657 446 -1597 C ATOM 484 CG PHE A 98 -15.758 30.303 15.441 1.00 49.19 C ANISOU 484 CG PHE A 98 5460 5396 7833 733 461 -1714 C ATOM 485 CD1 PHE A 98 -17.136 30.457 15.531 1.00 53.59 C ANISOU 485 CD1 PHE A 98 5914 5947 8500 803 568 -1751 C ATOM 486 CD2 PHE A 98 -14.970 31.443 15.364 1.00 51.55 C ANISOU 486 CD2 PHE A 98 5794 5565 8228 737 369 -1794 C ATOM 487 CE1 PHE A 98 -17.716 31.726 15.502 1.00 55.94 C ANISOU 487 CE1 PHE A 98 6143 6106 9005 884 578 -1866 C ATOM 488 CE2 PHE A 98 -15.551 32.713 15.342 1.00 55.80 C ANISOU 488 CE2 PHE A 98 6274 5958 8971 811 377 -1905 C ATOM 489 CZ PHE A 98 -16.920 32.846 15.409 1.00 55.19 C ANISOU 489 CZ PHE A 98 6094 5872 9002 890 480 -1943 C ATOM 490 N LEU A 99 -13.042 28.729 13.102 1.00 43.63 N ANISOU 490 N LEU A 99 4860 4706 7010 535 169 -1318 N ATOM 491 CA LEU A 99 -12.147 29.316 12.090 1.00 43.16 C ANISOU 491 CA LEU A 99 4805 4536 7057 499 59 -1245 C ATOM 492 C LEU A 99 -12.490 28.750 10.711 1.00 42.33 C ANISOU 492 C LEU A 99 4661 4419 7003 480 23 -1068 C ATOM 493 O LEU A 99 -12.687 29.523 9.771 1.00 41.54 O ANISOU 493 O LEU A 99 4526 4198 7058 490 -31 -1011 O ATOM 494 CB LEU A 99 -10.654 29.065 12.433 1.00 43.46 C ANISOU 494 CB LEU A 99 4917 4614 6980 436 -2 -1257 C ATOM 495 CG LEU A 99 -9.606 29.353 11.323 1.00 48.63 C ANISOU 495 CG LEU A 99 5571 5189 7718 380 -96 -1152 C ATOM 496 CD1 LEU A 99 -9.423 30.855 11.091 1.00 49.93 C ANISOU 496 CD1 LEU A 99 5714 5188 8069 388 -144 -1210 C ATOM 497 CD2 LEU A 99 -8.265 28.703 11.642 1.00 51.37 C ANISOU 497 CD2 LEU A 99 5966 5612 7939 321 -140 -1141 C ATOM 498 N TYR A 100 -12.586 27.406 10.608 1.00 34.54 N ANISOU 498 N TYR A 100 3689 3553 5883 453 48 -982 N ATOM 499 CA TYR A 100 -12.955 26.722 9.372 1.00 32.53 C ANISOU 499 CA TYR A 100 3408 3299 5653 435 13 -829 C ATOM 500 C TYR A 100 -14.368 27.099 8.929 1.00 35.16 C ANISOU 500 C TYR A 100 3657 3573 6131 488 28 -810 C ATOM 501 O TYR A 100 -14.589 27.294 7.733 1.00 33.88 O ANISOU 501 O TYR A 100 3474 3337 6061 484 -43 -705 O ATOM 502 CB TYR A 100 -12.819 25.189 9.510 1.00 32.32 C ANISOU 502 CB TYR A 100 3415 3404 5462 399 36 -762 C ATOM 503 CG TYR A 100 -13.493 24.423 8.390 1.00 33.63 C ANISOU 503 CG TYR A 100 3551 3575 5654 389 8 -631 C ATOM 504 CD1 TYR A 100 -12.984 24.452 7.093 1.00 34.46 C ANISOU 504 CD1 TYR A 100 3677 3626 5791 361 -71 -528 C ATOM 505 CD2 TYR A 100 -14.658 23.693 8.619 1.00 35.07 C ANISOU 505 CD2 TYR A 100 3684 3812 5829 404 61 -614 C ATOM 506 CE1 TYR A 100 -13.610 23.761 6.054 1.00 34.51 C ANISOU 506 CE1 TYR A 100 3669 3637 5808 352 -108 -418 C ATOM 507 CE2 TYR A 100 -15.292 22.995 7.588 1.00 35.53 C ANISOU 507 CE2 TYR A 100 3714 3867 5919 391 18 -502 C ATOM 508 CZ TYR A 100 -14.762 23.032 6.307 1.00 40.07 C ANISOU 508 CZ TYR A 100 4324 4390 6512 367 -73 -409 C ATOM 509 OH TYR A 100 -15.376 22.355 5.286 1.00 35.89 O ANISOU 509 OH TYR A 100 3781 3857 6000 355 -127 -310 O ATOM 510 N VAL A 101 -15.319 27.158 9.889 1.00 32.17 N ANISOU 510 N VAL A 101 3229 3229 5765 537 120 -909 N ATOM 511 CA VAL A 101 -16.722 27.537 9.661 1.00 33.72 C ANISOU 511 CA VAL A 101 3320 3372 6119 597 148 -914 C ATOM 512 C VAL A 101 -16.788 28.959 9.066 1.00 39.19 C ANISOU 512 C VAL A 101 3982 3900 7009 639 76 -932 C ATOM 513 O VAL A 101 -17.546 29.194 8.126 1.00 39.07 O ANISOU 513 O VAL A 101 3903 3809 7134 664 17 -848 O ATOM 514 CB VAL A 101 -17.592 27.341 10.940 1.00 38.83 C ANISOU 514 CB VAL A 101 3921 4102 6731 638 288 -1031 C ATOM 515 CG1 VAL A 101 -18.833 28.228 10.938 1.00 40.73 C ANISOU 515 CG1 VAL A 101 4042 4255 7177 721 326 -1096 C ATOM 516 CG2 VAL A 101 -17.980 25.877 11.124 1.00 37.79 C ANISOU 516 CG2 VAL A 101 3786 4104 6469 596 342 -954 C ATOM 517 N LEU A 102 -15.917 29.860 9.552 1.00 37.57 N ANISOU 517 N LEU A 102 3829 3633 6814 639 63 -1028 N ATOM 518 CA LEU A 102 -15.784 31.249 9.090 1.00 39.39 C ANISOU 518 CA LEU A 102 4045 3692 7229 667 -9 -1048 C ATOM 519 C LEU A 102 -15.486 31.364 7.584 1.00 41.53 C ANISOU 519 C LEU A 102 4331 3883 7565 628 -125 -873 C ATOM 520 O LEU A 102 -15.898 32.332 6.964 1.00 42.85 O ANISOU 520 O LEU A 102 4462 3908 7912 663 -189 -842 O ATOM 521 CB LEU A 102 -14.688 31.954 9.910 1.00 40.35 C ANISOU 521 CB LEU A 102 4235 3780 7314 648 -11 -1174 C ATOM 522 CG LEU A 102 -15.095 33.103 10.837 1.00 47.86 C ANISOU 522 CG LEU A 102 5160 4642 8384 721 32 -1360 C ATOM 523 CD1 LEU A 102 -16.287 32.750 11.725 1.00 48.93 C ANISOU 523 CD1 LEU A 102 5235 4864 8490 790 161 -1464 C ATOM 524 CD2 LEU A 102 -13.913 33.558 11.674 1.00 50.44 C ANISOU 524 CD2 LEU A 102 5570 4959 8637 685 15 -1481 C ATOM 525 N THR A 103 -14.818 30.363 6.999 1.00 36.24 N ANISOU 525 N THR A 103 3718 3303 6749 558 -150 -759 N ATOM 526 CA THR A 103 -14.435 30.345 5.581 1.00 35.55 C ANISOU 526 CA THR A 103 3664 3164 6678 513 -242 -596 C ATOM 527 C THR A 103 -15.525 29.802 4.658 1.00 39.59 C ANISOU 527 C THR A 103 4132 3684 7228 534 -284 -484 C ATOM 528 O THR A 103 -15.447 30.001 3.446 1.00 39.79 O ANISOU 528 O THR A 103 4185 3643 7289 513 -372 -355 O ATOM 529 CB THR A 103 -13.160 29.511 5.383 1.00 39.35 C ANISOU 529 CB THR A 103 4224 3739 6988 435 -242 -541 C ATOM 530 OG1 THR A 103 -13.480 28.118 5.531 1.00 38.04 O ANISOU 530 OG1 THR A 103 4060 3712 6683 426 -202 -515 O ATOM 531 CG2 THR A 103 -12.036 29.920 6.314 1.00 38.88 C ANISOU 531 CG2 THR A 103 4200 3683 6891 409 -217 -650 C ATOM 532 N LEU A 104 -16.495 29.066 5.212 1.00 36.75 N ANISOU 532 N LEU A 104 3709 3407 6846 567 -224 -526 N ATOM 533 CA LEU A 104 -17.562 28.436 4.428 1.00 37.06 C ANISOU 533 CA LEU A 104 3695 3462 6926 581 -269 -430 C ATOM 534 C LEU A 104 -18.360 29.336 3.486 1.00 43.57 C ANISOU 534 C LEU A 104 4466 4147 7941 627 -372 -360 C ATOM 535 O LEU A 104 -18.520 28.912 2.341 1.00 43.51 O ANISOU 535 O LEU A 104 4486 4137 7911 599 -465 -228 O ATOM 536 CB LEU A 104 -18.463 27.523 5.266 1.00 37.33 C ANISOU 536 CB LEU A 104 3655 3604 6922 600 -176 -489 C ATOM 537 CG LEU A 104 -17.763 26.299 5.866 1.00 40.63 C ANISOU 537 CG LEU A 104 4140 4165 7131 542 -108 -498 C ATOM 538 CD1 LEU A 104 -18.636 25.654 6.921 1.00 41.51 C ANISOU 538 CD1 LEU A 104 4182 4369 7220 563 5 -570 C ATOM 539 CD2 LEU A 104 -17.387 25.293 4.798 1.00 41.00 C ANISOU 539 CD2 LEU A 104 4246 4254 7078 485 -183 -365 C ATOM 540 N PRO A 105 -18.800 30.577 3.865 1.00 41.42 N ANISOU 540 N PRO A 105 4132 3753 7853 695 -373 -439 N ATOM 541 CA PRO A 105 -19.545 31.417 2.903 1.00 42.33 C ANISOU 541 CA PRO A 105 4200 3723 8159 740 -493 -354 C ATOM 542 C PRO A 105 -18.836 31.657 1.569 1.00 46.22 C ANISOU 542 C PRO A 105 4797 4151 8613 684 -614 -194 C ATOM 543 O PRO A 105 -19.504 31.631 0.536 1.00 46.41 O ANISOU 543 O PRO A 105 4808 4127 8697 695 -726 -74 O ATOM 544 CB PRO A 105 -19.791 32.711 3.682 1.00 45.28 C ANISOU 544 CB PRO A 105 4514 3974 8717 816 -459 -487 C ATOM 545 CG PRO A 105 -19.811 32.281 5.098 1.00 49.46 C ANISOU 545 CG PRO A 105 5013 4615 9163 831 -306 -650 C ATOM 546 CD PRO A 105 -18.711 31.258 5.176 1.00 43.46 C ANISOU 546 CD PRO A 105 4361 3993 8159 739 -273 -613 C ATOM 547 N ALA A 106 -17.491 31.826 1.584 1.00 42.61 N ANISOU 547 N ALA A 106 4442 3702 8047 619 -590 -187 N ATOM 548 CA ALA A 106 -16.651 31.981 0.385 1.00 42.70 C ANISOU 548 CA ALA A 106 4558 3673 7993 552 -670 -37 C ATOM 549 C ALA A 106 -16.812 30.748 -0.527 1.00 46.67 C ANISOU 549 C ALA A 106 5106 4285 8342 512 -710 78 C ATOM 550 O ALA A 106 -17.019 30.889 -1.736 1.00 46.21 O ANISOU 550 O ALA A 106 5095 4173 8288 498 -816 216 O ATOM 551 CB ALA A 106 -15.184 32.118 0.785 1.00 42.66 C ANISOU 551 CB ALA A 106 4626 3693 7892 487 -606 -76 C ATOM 552 N LEU A 107 -16.734 29.548 0.074 1.00 43.50 N ANISOU 552 N LEU A 107 4696 4029 7802 494 -629 17 N ATOM 553 CA LEU A 107 -16.875 28.280 -0.629 1.00 43.49 C ANISOU 553 CA LEU A 107 4735 4132 7659 457 -657 97 C ATOM 554 C LEU A 107 -18.275 28.092 -1.183 1.00 46.94 C ANISOU 554 C LEU A 107 5102 4540 8194 500 -749 149 C ATOM 555 O LEU A 107 -18.411 27.652 -2.322 1.00 47.17 O ANISOU 555 O LEU A 107 5190 4577 8157 472 -845 262 O ATOM 556 CB LEU A 107 -16.468 27.113 0.275 1.00 43.16 C ANISOU 556 CB LEU A 107 4694 4232 7473 431 -551 15 C ATOM 557 CG LEU A 107 -15.666 26.009 -0.383 1.00 47.74 C ANISOU 557 CG LEU A 107 5368 4905 7866 368 -554 83 C ATOM 558 CD1 LEU A 107 -14.422 26.556 -1.080 1.00 48.50 C ANISOU 558 CD1 LEU A 107 5556 4964 7906 321 -564 146 C ATOM 559 CD2 LEU A 107 -15.281 24.960 0.628 1.00 49.08 C ANISOU 559 CD2 LEU A 107 5532 5193 7922 352 -458 0 C ATOM 560 N ILE A 108 -19.307 28.466 -0.396 1.00 42.92 N ANISOU 560 N ILE A 108 4465 3994 7847 568 -723 62 N ATOM 561 CA ILE A 108 -20.720 28.415 -0.771 1.00 43.08 C ANISOU 561 CA ILE A 108 4382 3975 8012 619 -808 95 C ATOM 562 C ILE A 108 -20.953 29.347 -1.983 1.00 50.48 C ANISOU 562 C ILE A 108 5353 4774 9052 636 -967 219 C ATOM 563 O ILE A 108 -21.645 28.952 -2.927 1.00 50.10 O ANISOU 563 O ILE A 108 5304 4720 9013 634 -1091 317 O ATOM 564 CB ILE A 108 -21.642 28.761 0.440 1.00 46.12 C ANISOU 564 CB ILE A 108 4614 4348 8561 692 -716 -40 C ATOM 565 CG1 ILE A 108 -21.493 27.730 1.584 1.00 45.03 C ANISOU 565 CG1 ILE A 108 4457 4357 8295 666 -564 -140 C ATOM 566 CG2 ILE A 108 -23.111 28.894 0.012 1.00 47.01 C ANISOU 566 CG2 ILE A 108 4594 4399 8869 752 -811 -5 C ATOM 567 CD1 ILE A 108 -21.942 28.217 3.007 1.00 48.98 C ANISOU 567 CD1 ILE A 108 4857 4863 8891 727 -424 -299 C ATOM 568 N PHE A 109 -20.342 30.566 -1.957 1.00 48.72 N ANISOU 568 N PHE A 109 5170 4439 8903 648 -971 219 N ATOM 569 CA PHE A 109 -20.401 31.559 -3.038 1.00 50.30 C ANISOU 569 CA PHE A 109 5421 4496 9196 657 -1113 348 C ATOM 570 C PHE A 109 -19.809 30.987 -4.322 1.00 53.37 C ANISOU 570 C PHE A 109 5956 4934 9390 580 -1191 500 C ATOM 571 O PHE A 109 -20.426 31.121 -5.376 1.00 53.66 O ANISOU 571 O PHE A 109 6016 4912 9458 590 -1340 622 O ATOM 572 CB PHE A 109 -19.674 32.869 -2.643 1.00 53.17 C ANISOU 572 CB PHE A 109 5807 4734 9660 667 -1080 311 C ATOM 573 CG PHE A 109 -19.741 33.963 -3.686 1.00 56.56 C ANISOU 573 CG PHE A 109 6290 4998 10204 675 -1225 453 C ATOM 574 CD1 PHE A 109 -18.840 33.995 -4.747 1.00 59.52 C ANISOU 574 CD1 PHE A 109 6814 5370 10433 593 -1273 603 C ATOM 575 CD2 PHE A 109 -20.696 34.968 -3.604 1.00 60.98 C ANISOU 575 CD2 PHE A 109 6750 5400 11018 765 -1308 439 C ATOM 576 CE1 PHE A 109 -18.925 34.984 -5.728 1.00 62.13 C ANISOU 576 CE1 PHE A 109 7205 5548 10854 594 -1407 752 C ATOM 577 CE2 PHE A 109 -20.766 35.972 -4.577 1.00 65.46 C ANISOU 577 CE2 PHE A 109 7375 5804 11695 772 -1455 585 C ATOM 578 CZ PHE A 109 -19.877 35.975 -5.629 1.00 63.30 C ANISOU 578 CZ PHE A 109 7261 5533 11259 683 -1504 747 C ATOM 579 N TYR A 110 -18.612 30.364 -4.224 1.00 49.05 N ANISOU 579 N TYR A 110 5503 4491 8642 507 -1092 487 N ATOM 580 CA TYR A 110 -17.875 29.728 -5.315 1.00 48.78 C ANISOU 580 CA TYR A 110 5610 4524 8401 433 -1122 602 C ATOM 581 C TYR A 110 -18.757 28.706 -6.048 1.00 53.88 C ANISOU 581 C TYR A 110 6263 5235 8976 434 -1221 657 C ATOM 582 O TYR A 110 -18.807 28.743 -7.276 1.00 54.11 O ANISOU 582 O TYR A 110 6390 5237 8931 409 -1337 787 O ATOM 583 CB TYR A 110 -16.595 29.095 -4.753 1.00 48.71 C ANISOU 583 CB TYR A 110 5651 4627 8230 376 -977 534 C ATOM 584 CG TYR A 110 -15.781 28.227 -5.691 1.00 50.18 C ANISOU 584 CG TYR A 110 5965 4906 8196 306 -971 615 C ATOM 585 CD1 TYR A 110 -15.026 28.792 -6.715 1.00 52.45 C ANISOU 585 CD1 TYR A 110 6366 5148 8415 257 -997 736 C ATOM 586 CD2 TYR A 110 -15.651 26.856 -5.467 1.00 50.12 C ANISOU 586 CD2 TYR A 110 5964 5031 8048 288 -918 562 C ATOM 587 CE1 TYR A 110 -14.188 28.013 -7.513 1.00 52.74 C ANISOU 587 CE1 TYR A 110 6517 5279 8243 197 -962 794 C ATOM 588 CE2 TYR A 110 -14.839 26.062 -6.278 1.00 50.47 C ANISOU 588 CE2 TYR A 110 6123 5157 7897 233 -899 616 C ATOM 589 CZ TYR A 110 -14.113 26.645 -7.304 1.00 58.38 C ANISOU 589 CZ TYR A 110 7233 6120 8827 190 -916 727 C ATOM 590 OH TYR A 110 -13.308 25.877 -8.106 1.00 58.60 O ANISOU 590 OH TYR A 110 7372 6233 8659 140 -879 770 O ATOM 591 N TYR A 111 -19.498 27.848 -5.304 1.00 50.51 N ANISOU 591 N TYR A 111 5729 4882 8580 461 -1184 562 N ATOM 592 CA TYR A 111 -20.420 26.862 -5.899 1.00 50.32 C ANISOU 592 CA TYR A 111 5689 4908 8522 459 -1284 600 C ATOM 593 C TYR A 111 -21.645 27.502 -6.526 1.00 56.48 C ANISOU 593 C TYR A 111 6403 5578 9479 513 -1453 672 C ATOM 594 O TYR A 111 -22.131 27.013 -7.546 1.00 57.01 O ANISOU 594 O TYR A 111 6521 5654 9488 496 -1594 760 O ATOM 595 CB TYR A 111 -20.791 25.734 -4.920 1.00 49.74 C ANISOU 595 CB TYR A 111 5523 4942 8435 459 -1186 489 C ATOM 596 CG TYR A 111 -19.654 24.752 -4.725 1.00 48.63 C ANISOU 596 CG TYR A 111 5478 4916 8081 397 -1078 457 C ATOM 597 CD1 TYR A 111 -19.371 23.783 -5.684 1.00 49.90 C ANISOU 597 CD1 TYR A 111 5749 5139 8072 349 -1136 519 C ATOM 598 CD2 TYR A 111 -18.855 24.799 -3.588 1.00 47.95 C ANISOU 598 CD2 TYR A 111 5375 4874 7968 393 -927 361 C ATOM 599 CE1 TYR A 111 -18.315 22.891 -5.521 1.00 48.88 C ANISOU 599 CE1 TYR A 111 5700 5105 7766 302 -1038 485 C ATOM 600 CE2 TYR A 111 -17.789 23.917 -3.416 1.00 47.50 C ANISOU 600 CE2 TYR A 111 5399 4915 7734 343 -842 336 C ATOM 601 CZ TYR A 111 -17.516 22.971 -4.391 1.00 54.64 C ANISOU 601 CZ TYR A 111 6401 5872 8486 301 -894 399 C ATOM 602 OH TYR A 111 -16.467 22.096 -4.230 1.00 52.67 O ANISOU 602 OH TYR A 111 6222 5710 8080 261 -811 369 O ATOM 603 N PHE A 112 -22.114 28.620 -5.948 1.00 54.88 N ANISOU 603 N PHE A 112 6091 5265 9494 580 -1450 634 N ATOM 604 CA PHE A 112 -23.245 29.403 -6.454 1.00 56.53 C ANISOU 604 CA PHE A 112 6219 5346 9912 646 -1613 698 C ATOM 605 C PHE A 112 -22.812 30.333 -7.609 1.00 61.19 C ANISOU 605 C PHE A 112 6948 5827 10475 630 -1744 851 C ATOM 606 O PHE A 112 -23.667 30.948 -8.248 1.00 62.51 O ANISOU 606 O PHE A 112 7082 5884 10787 678 -1914 937 O ATOM 607 CB PHE A 112 -23.870 30.221 -5.313 1.00 59.34 C ANISOU 607 CB PHE A 112 6403 5624 10518 731 -1539 579 C ATOM 608 CG PHE A 112 -24.958 29.513 -4.542 1.00 61.52 C ANISOU 608 CG PHE A 112 6503 5964 10908 771 -1489 478 C ATOM 609 CD1 PHE A 112 -24.647 28.535 -3.603 1.00 63.03 C ANISOU 609 CD1 PHE A 112 6675 6294 10981 734 -1322 373 C ATOM 610 CD2 PHE A 112 -26.294 29.848 -4.728 1.00 66.16 C ANISOU 610 CD2 PHE A 112 6938 6467 11733 844 -1606 491 C ATOM 611 CE1 PHE A 112 -25.653 27.885 -2.884 1.00 64.41 C ANISOU 611 CE1 PHE A 112 6687 6526 11259 760 -1262 292 C ATOM 612 CE2 PHE A 112 -27.302 29.197 -4.008 1.00 69.36 C ANISOU 612 CE2 PHE A 112 7165 6933 12257 874 -1544 400 C ATOM 613 CZ PHE A 112 -26.972 28.220 -3.089 1.00 65.59 C ANISOU 613 CZ PHE A 112 6678 6598 11647 827 -1365 304 C ATOM 614 N ASN A 113 -21.491 30.429 -7.870 1.00 56.90 N ANISOU 614 N ASN A 113 6554 5314 9751 563 -1665 890 N ATOM 615 CA ASN A 113 -20.907 31.252 -8.933 1.00 57.83 C ANISOU 615 CA ASN A 113 6818 5343 9811 528 -1753 1043 C ATOM 616 C ASN A 113 -20.278 30.382 -10.041 1.00 62.09 C ANISOU 616 C ASN A 113 7533 5988 10068 447 -1781 1143 C ATOM 617 O ASN A 113 -19.238 30.741 -10.599 1.00 61.22 O ANISOU 617 O ASN A 113 7560 5873 9827 388 -1741 1227 O ATOM 618 CB ASN A 113 -19.891 32.254 -8.345 1.00 57.17 C ANISOU 618 CB ASN A 113 6753 5187 9781 514 -1635 1013 C ATOM 619 CG ASN A 113 -19.492 33.379 -9.276 1.00 72.79 C ANISOU 619 CG ASN A 113 8846 7031 11780 490 -1730 1175 C ATOM 620 OD1 ASN A 113 -20.324 33.978 -9.966 1.00 66.77 O ANISOU 620 OD1 ASN A 113 8083 6153 11135 532 -1901 1282 O ATOM 621 ND2 ASN A 113 -18.200 33.681 -9.323 1.00 60.10 N ANISOU 621 ND2 ASN A 113 7337 5433 10065 417 -1622 1203 N ATOM 622 N LYS A 114 -20.924 29.229 -10.359 1.00 59.11 N ANISOU 622 N LYS A 114 7147 5705 9605 443 -1845 1127 N ATOM 623 CA LYS A 114 -20.509 28.274 -11.398 1.00 58.40 C ANISOU 623 CA LYS A 114 7218 5717 9253 377 -1884 1196 C ATOM 624 C LYS A 114 -19.038 27.857 -11.277 1.00 59.17 C ANISOU 624 C LYS A 114 7422 5915 9147 309 -1704 1165 C ATOM 625 O LYS A 114 -18.337 27.753 -12.287 1.00 59.81 O ANISOU 625 O LYS A 114 7667 6030 9028 254 -1714 1260 O ATOM 626 CB LYS A 114 -20.826 28.832 -12.807 1.00 63.63 C ANISOU 626 CB LYS A 114 8010 6302 9864 369 -2082 1371 C ATOM 627 CG LYS A 114 -22.259 28.585 -13.281 1.00 85.42 C ANISOU 627 CG LYS A 114 10701 9023 12730 416 -2296 1402 C ATOM 628 CD LYS A 114 -22.405 27.252 -14.036 1.00 97.65 C ANISOU 628 CD LYS A 114 12355 10689 14059 370 -2369 1407 C ATOM 629 CE LYS A 114 -23.774 27.072 -14.651 1.00111.95 C ANISOU 629 CE LYS A 114 14114 12454 15967 405 -2613 1454 C ATOM 630 NZ LYS A 114 -24.819 26.779 -13.631 1.00121.43 N ANISOU 630 NZ LYS A 114 15077 13642 17421 461 -2607 1336 N ATOM 631 N THR A 115 -18.581 27.617 -10.031 1.00 52.29 N ANISOU 631 N THR A 115 6452 5090 8324 316 -1538 1030 N ATOM 632 CA THR A 115 -17.203 27.259 -9.673 1.00 50.12 C ANISOU 632 CA THR A 115 6236 4902 7906 263 -1365 978 C ATOM 633 C THR A 115 -16.141 28.240 -10.208 1.00 52.20 C ANISOU 633 C THR A 115 6603 5108 8121 218 -1323 1075 C ATOM 634 O THR A 115 -15.083 27.821 -10.684 1.00 51.87 O ANISOU 634 O THR A 115 6668 5143 7895 159 -1237 1102 O ATOM 635 CB THR A 115 -16.905 25.748 -9.796 1.00 57.16 C ANISOU 635 CB THR A 115 7175 5935 8609 231 -1315 923 C ATOM 636 OG1 THR A 115 -17.133 25.311 -11.137 1.00 60.34 O ANISOU 636 OG1 THR A 115 7710 6359 8858 205 -1433 1021 O ATOM 637 CG2 THR A 115 -17.705 24.913 -8.810 1.00 55.29 C ANISOU 637 CG2 THR A 115 6803 5744 8461 266 -1298 805 C ATOM 638 N ASP A 116 -16.419 29.551 -10.077 1.00 47.88 N ANISOU 638 N ASP A 116 6015 4421 7757 246 -1376 1123 N ATOM 639 CA ASP A 116 -15.523 30.629 -10.492 1.00 47.65 C ANISOU 639 CA ASP A 116 6065 4307 7733 201 -1346 1223 C ATOM 640 C ASP A 116 -15.041 31.396 -9.248 1.00 48.62 C ANISOU 640 C ASP A 116 6079 4365 8027 216 -1239 1115 C ATOM 641 O ASP A 116 -15.811 32.147 -8.647 1.00 48.74 O ANISOU 641 O ASP A 116 5992 4270 8256 280 -1294 1072 O ATOM 642 CB ASP A 116 -16.223 31.563 -11.510 1.00 51.07 C ANISOU 642 CB ASP A 116 6562 4606 8236 216 -1522 1387 C ATOM 643 CG ASP A 116 -15.331 32.515 -12.288 1.00 59.47 C ANISOU 643 CG ASP A 116 7753 5594 9251 150 -1509 1540 C ATOM 644 OD1 ASP A 116 -14.094 32.390 -12.190 1.00 59.75 O ANISOU 644 OD1 ASP A 116 7833 5693 9178 83 -1357 1526 O ATOM 645 OD2 ASP A 116 -15.872 33.361 -13.027 1.00 67.50 O ANISOU 645 OD2 ASP A 116 8822 6486 10338 163 -1655 1681 O ATOM 646 N TRP A 117 -13.778 31.162 -8.844 1.00 42.26 N ANISOU 646 N TRP A 117 5293 3631 7132 161 -1089 1062 N ATOM 647 CA TRP A 117 -13.162 31.788 -7.672 1.00 40.79 C ANISOU 647 CA TRP A 117 5020 3399 7079 162 -991 951 C ATOM 648 C TRP A 117 -12.789 33.238 -7.975 1.00 44.01 C ANISOU 648 C TRP A 117 5457 3644 7622 137 -1024 1046 C ATOM 649 O TRP A 117 -11.980 33.500 -8.866 1.00 44.47 O ANISOU 649 O TRP A 117 5620 3693 7584 63 -1005 1176 O ATOM 650 CB TRP A 117 -11.959 30.969 -7.174 1.00 38.19 C ANISOU 650 CB TRP A 117 4697 3200 6612 111 -843 868 C ATOM 651 CG TRP A 117 -11.415 31.427 -5.853 1.00 38.48 C ANISOU 651 CG TRP A 117 4642 3211 6769 118 -760 731 C ATOM 652 CD1 TRP A 117 -10.393 32.301 -5.650 1.00 41.68 C ANISOU 652 CD1 TRP A 117 5048 3544 7244 68 -707 737 C ATOM 653 CD2 TRP A 117 -11.856 31.016 -4.553 1.00 37.61 C ANISOU 653 CD2 TRP A 117 4431 3148 6713 174 -722 567 C ATOM 654 NE1 TRP A 117 -10.169 32.464 -4.305 1.00 40.50 N ANISOU 654 NE1 TRP A 117 4809 3392 7187 92 -653 578 N ATOM 655 CE2 TRP A 117 -11.047 31.680 -3.607 1.00 41.02 C ANISOU 655 CE2 TRP A 117 4818 3536 7233 158 -655 473 C ATOM 656 CE3 TRP A 117 -12.853 30.138 -4.092 1.00 38.53 C ANISOU 656 CE3 TRP A 117 4491 3339 6809 230 -736 494 C ATOM 657 CZ2 TRP A 117 -11.204 31.502 -2.226 1.00 39.78 C ANISOU 657 CZ2 TRP A 117 4578 3415 7122 200 -604 307 C ATOM 658 CZ3 TRP A 117 -13.005 29.961 -2.721 1.00 39.35 C ANISOU 658 CZ3 TRP A 117 4507 3480 6966 268 -670 339 C ATOM 659 CH2 TRP A 117 -12.190 30.642 -1.806 1.00 39.83 C ANISOU 659 CH2 TRP A 117 4540 3502 7092 256 -606 246 C ATOM 660 N ILE A 118 -13.422 34.177 -7.256 1.00 39.35 N ANISOU 660 N ILE A 118 4774 2919 7257 198 -1073 984 N ATOM 661 CA ILE A 118 -13.224 35.622 -7.443 1.00 40.19 C ANISOU 661 CA ILE A 118 4895 2840 7535 185 -1123 1063 C ATOM 662 C ILE A 118 -12.381 36.238 -6.324 1.00 44.54 C ANISOU 662 C ILE A 118 5381 3339 8203 166 -1024 934 C ATOM 663 O ILE A 118 -12.068 37.424 -6.382 1.00 46.38 O ANISOU 663 O ILE A 118 5623 3412 8587 144 -1054 985 O ATOM 664 CB ILE A 118 -14.591 36.349 -7.635 1.00 44.07 C ANISOU 664 CB ILE A 118 5341 3184 8219 273 -1278 1104 C ATOM 665 CG1 ILE A 118 -15.471 36.315 -6.346 1.00 43.42 C ANISOU 665 CG1 ILE A 118 5105 3093 8300 373 -1261 910 C ATOM 666 CG2 ILE A 118 -15.352 35.791 -8.856 1.00 44.70 C ANISOU 666 CG2 ILE A 118 5500 3305 8179 279 -1403 1251 C ATOM 667 CD1 ILE A 118 -16.483 37.509 -6.211 1.00 40.93 C ANISOU 667 CD1 ILE A 118 4713 2578 8262 463 -1378 910 C ATOM 668 N PHE A 119 -11.989 35.430 -5.321 1.00 39.40 N ANISOU 668 N PHE A 119 4671 2819 7481 171 -916 772 N ATOM 669 CA PHE A 119 -11.245 35.930 -4.166 1.00 38.93 C ANISOU 669 CA PHE A 119 4550 2724 7518 159 -838 630 C ATOM 670 C PHE A 119 -9.716 35.978 -4.281 1.00 43.01 C ANISOU 670 C PHE A 119 5109 3273 7961 55 -751 660 C ATOM 671 O PHE A 119 -9.049 36.463 -3.364 1.00 41.22 O ANISOU 671 O PHE A 119 4832 3005 7824 38 -706 545 O ATOM 672 CB PHE A 119 -11.737 35.267 -2.874 1.00 39.55 C ANISOU 672 CB PHE A 119 4537 2897 7592 228 -785 434 C ATOM 673 CG PHE A 119 -13.235 35.380 -2.705 1.00 41.86 C ANISOU 673 CG PHE A 119 4764 3142 7999 328 -856 398 C ATOM 674 CD1 PHE A 119 -13.830 36.604 -2.419 1.00 46.22 C ANISOU 674 CD1 PHE A 119 5264 3516 8781 388 -919 364 C ATOM 675 CD2 PHE A 119 -14.052 34.266 -2.847 1.00 42.98 C ANISOU 675 CD2 PHE A 119 4886 3409 8036 364 -864 397 C ATOM 676 CE1 PHE A 119 -15.218 36.711 -2.269 1.00 47.79 C ANISOU 676 CE1 PHE A 119 5383 3669 9106 488 -980 327 C ATOM 677 CE2 PHE A 119 -15.439 34.374 -2.699 1.00 46.53 C ANISOU 677 CE2 PHE A 119 5253 3812 8612 453 -928 366 C ATOM 678 CZ PHE A 119 -16.012 35.596 -2.414 1.00 45.43 C ANISOU 678 CZ PHE A 119 5054 3503 8704 517 -982 331 C ATOM 679 N GLY A 120 -9.184 35.522 -5.412 1.00 40.58 N ANISOU 679 N GLY A 120 4889 3032 7497 -13 -731 810 N ATOM 680 CA GLY A 120 -7.750 35.542 -5.655 1.00 41.01 C ANISOU 680 CA GLY A 120 4972 3121 7487 -113 -637 855 C ATOM 681 C GLY A 120 -7.028 34.287 -5.217 1.00 44.19 C ANISOU 681 C GLY A 120 5355 3710 7727 -130 -535 761 C ATOM 682 O GLY A 120 -7.574 33.453 -4.485 1.00 42.51 O ANISOU 682 O GLY A 120 5098 3591 7461 -66 -531 640 O ATOM 683 N ASP A 121 -5.779 34.164 -5.675 1.00 40.95 N ANISOU 683 N ASP A 121 4970 3346 7246 -218 -448 822 N ATOM 684 CA ASP A 121 -4.882 33.042 -5.423 1.00 38.92 C ANISOU 684 CA ASP A 121 4690 3249 6848 -242 -348 755 C ATOM 685 C ASP A 121 -4.613 32.799 -3.928 1.00 40.75 C ANISOU 685 C ASP A 121 4825 3516 7141 -209 -330 564 C ATOM 686 O ASP A 121 -4.771 31.673 -3.457 1.00 39.14 O ANISOU 686 O ASP A 121 4606 3441 6825 -167 -307 477 O ATOM 687 CB ASP A 121 -3.581 33.252 -6.212 1.00 41.43 C ANISOU 687 CB ASP A 121 5035 3577 7131 -344 -255 865 C ATOM 688 CG ASP A 121 -2.601 32.097 -6.165 1.00 49.01 C ANISOU 688 CG ASP A 121 5973 4698 7952 -367 -148 814 C ATOM 689 OD1 ASP A 121 -3.025 30.951 -6.419 1.00 46.72 O ANISOU 689 OD1 ASP A 121 5723 4527 7503 -320 -142 796 O ATOM 690 OD2 ASP A 121 -1.399 32.353 -5.939 1.00 56.79 O ANISOU 690 OD2 ASP A 121 6898 5682 8998 -433 -73 799 O ATOM 691 N ALA A 122 -4.231 33.856 -3.198 1.00 38.04 N ANISOU 691 N ALA A 122 4426 3054 6972 -231 -348 501 N ATOM 692 CA ALA A 122 -3.923 33.841 -1.763 1.00 36.77 C ANISOU 692 CA ALA A 122 4188 2907 6877 -208 -345 319 C ATOM 693 C ALA A 122 -5.085 33.361 -0.885 1.00 38.84 C ANISOU 693 C ALA A 122 4432 3214 7110 -108 -381 195 C ATOM 694 O ALA A 122 -4.848 32.617 0.058 1.00 37.10 O ANISOU 694 O ALA A 122 4179 3098 6821 -86 -353 73 O ATOM 695 CB ALA A 122 -3.460 35.223 -1.318 1.00 38.08 C ANISOU 695 CB ALA A 122 4316 2906 7248 -249 -380 286 C ATOM 696 N MET A 123 -6.335 33.791 -1.191 1.00 35.97 N ANISOU 696 N MET A 123 4087 2772 6806 -50 -444 233 N ATOM 697 CA MET A 123 -7.531 33.395 -0.446 1.00 35.18 C ANISOU 697 CA MET A 123 3958 2709 6702 43 -467 128 C ATOM 698 C MET A 123 -7.901 31.958 -0.718 1.00 38.53 C ANISOU 698 C MET A 123 4402 3292 6944 65 -440 149 C ATOM 699 O MET A 123 -8.432 31.279 0.169 1.00 36.94 O ANISOU 699 O MET A 123 4166 3171 6697 117 -422 39 O ATOM 700 CB MET A 123 -8.713 34.328 -0.723 1.00 38.49 C ANISOU 700 CB MET A 123 4370 2985 7271 101 -546 161 C ATOM 701 CG MET A 123 -8.587 35.676 -0.026 1.00 43.04 C ANISOU 701 CG MET A 123 4907 3398 8048 110 -575 73 C ATOM 702 SD MET A 123 -8.564 35.591 1.786 1.00 46.60 S ANISOU 702 SD MET A 123 5296 3897 8514 160 -530 -178 S ATOM 703 CE MET A 123 -10.322 35.324 2.124 1.00 43.41 C ANISOU 703 CE MET A 123 4847 3508 8138 279 -543 -239 C ATOM 704 N CYS A 124 -7.603 31.483 -1.938 1.00 35.99 N ANISOU 704 N CYS A 124 4143 3015 6514 22 -433 289 N ATOM 705 CA CYS A 124 -7.827 30.094 -2.305 1.00 35.38 C ANISOU 705 CA CYS A 124 4097 3081 6265 34 -412 308 C ATOM 706 C CYS A 124 -6.902 29.197 -1.488 1.00 36.78 C ANISOU 706 C CYS A 124 4247 3376 6353 18 -339 209 C ATOM 707 O CYS A 124 -7.352 28.180 -0.964 1.00 34.56 O ANISOU 707 O CYS A 124 3953 3191 5988 57 -329 145 O ATOM 708 CB CYS A 124 -7.624 29.870 -3.797 1.00 36.76 C ANISOU 708 CB CYS A 124 4358 3271 6338 -9 -418 467 C ATOM 709 SG CYS A 124 -7.595 28.122 -4.257 1.00 39.95 S ANISOU 709 SG CYS A 124 4808 3845 6525 -3 -382 471 S ATOM 710 N LYS A 125 -5.614 29.587 -1.395 1.00 33.36 N ANISOU 710 N LYS A 125 3799 2927 5948 -42 -296 205 N ATOM 711 CA LYS A 125 -4.568 28.885 -0.642 1.00 32.36 C ANISOU 711 CA LYS A 125 3637 2896 5765 -61 -243 118 C ATOM 712 C LYS A 125 -4.937 28.826 0.836 1.00 35.46 C ANISOU 712 C LYS A 125 3982 3304 6186 -12 -261 -33 C ATOM 713 O LYS A 125 -4.823 27.774 1.449 1.00 34.75 O ANISOU 713 O LYS A 125 3886 3323 5995 9 -240 -95 O ATOM 714 CB LYS A 125 -3.199 29.579 -0.822 1.00 34.17 C ANISOU 714 CB LYS A 125 3839 3076 6068 -138 -208 145 C ATOM 715 CG LYS A 125 -2.601 29.378 -2.200 1.00 38.27 C ANISOU 715 CG LYS A 125 4403 3619 6518 -193 -154 287 C ATOM 716 CD LYS A 125 -1.370 30.252 -2.431 1.00 40.62 C ANISOU 716 CD LYS A 125 4664 3851 6920 -278 -112 330 C ATOM 717 CE LYS A 125 -0.646 29.917 -3.716 1.00 35.94 C ANISOU 717 CE LYS A 125 4110 3309 6236 -334 -27 459 C ATOM 718 NZ LYS A 125 -0.035 28.552 -3.692 1.00 33.48 N ANISOU 718 NZ LYS A 125 3781 3143 5797 -318 37 411 N ATOM 719 N LEU A 126 -5.413 29.959 1.386 1.00 33.08 N ANISOU 719 N LEU A 126 3656 2890 6021 7 -299 -90 N ATOM 720 CA LEU A 126 -5.830 30.084 2.777 1.00 32.55 C ANISOU 720 CA LEU A 126 3556 2829 5982 56 -307 -243 C ATOM 721 C LEU A 126 -7.084 29.253 3.048 1.00 34.30 C ANISOU 721 C LEU A 126 3780 3126 6126 123 -300 -267 C ATOM 722 O LEU A 126 -7.182 28.636 4.106 1.00 32.12 O ANISOU 722 O LEU A 126 3493 2932 5778 149 -276 -368 O ATOM 723 CB LEU A 126 -6.058 31.562 3.122 1.00 33.89 C ANISOU 723 CB LEU A 126 3703 2843 6328 64 -346 -296 C ATOM 724 CG LEU A 126 -6.262 31.924 4.599 1.00 39.36 C ANISOU 724 CG LEU A 126 4370 3526 7059 106 -350 -476 C ATOM 725 CD1 LEU A 126 -5.049 31.544 5.460 1.00 38.64 C ANISOU 725 CD1 LEU A 126 4272 3507 6903 65 -343 -564 C ATOM 726 CD2 LEU A 126 -6.582 33.410 4.746 1.00 44.26 C ANISOU 726 CD2 LEU A 126 4974 3972 7871 122 -393 -523 C ATOM 727 N GLN A 127 -8.016 29.207 2.081 1.00 31.05 N ANISOU 727 N GLN A 127 3385 2687 5725 144 -324 -167 N ATOM 728 CA GLN A 127 -9.232 28.400 2.193 1.00 30.34 C ANISOU 728 CA GLN A 127 3284 2661 5582 198 -323 -174 C ATOM 729 C GLN A 127 -8.830 26.934 2.364 1.00 33.39 C ANISOU 729 C GLN A 127 3692 3190 5805 183 -286 -176 C ATOM 730 O GLN A 127 -9.298 26.272 3.288 1.00 32.86 O ANISOU 730 O GLN A 127 3605 3195 5685 214 -258 -252 O ATOM 731 CB GLN A 127 -10.118 28.582 0.942 1.00 31.66 C ANISOU 731 CB GLN A 127 3469 2770 5790 211 -380 -50 C ATOM 732 CG GLN A 127 -11.404 27.749 0.939 1.00 46.37 C ANISOU 732 CG GLN A 127 5308 4689 7622 258 -394 -47 C ATOM 733 CD GLN A 127 -12.549 28.440 1.637 1.00 65.19 C ANISOU 733 CD GLN A 127 7619 7007 10145 325 -402 -125 C ATOM 734 OE1 GLN A 127 -12.843 29.617 1.399 1.00 61.96 O ANISOU 734 OE1 GLN A 127 7191 6470 9882 347 -447 -111 O ATOM 735 NE2 GLN A 127 -13.271 27.700 2.460 1.00 57.84 N ANISOU 735 NE2 GLN A 127 6641 6157 9177 359 -356 -201 N ATOM 736 N ARG A 128 -7.924 26.447 1.505 1.00 30.55 N ANISOU 736 N ARG A 128 3374 2867 5368 136 -279 -95 N ATOM 737 CA ARG A 128 -7.497 25.048 1.531 1.00 28.64 C ANISOU 737 CA ARG A 128 3153 2743 4986 127 -250 -92 C ATOM 738 C ARG A 128 -6.645 24.702 2.741 1.00 32.49 C ANISOU 738 C ARG A 128 3618 3289 5437 121 -221 -191 C ATOM 739 O ARG A 128 -6.761 23.592 3.265 1.00 31.82 O ANISOU 739 O ARG A 128 3540 3292 5258 137 -207 -220 O ATOM 740 CB ARG A 128 -6.841 24.625 0.204 1.00 26.69 C ANISOU 740 CB ARG A 128 2956 2515 4670 87 -242 15 C ATOM 741 CG ARG A 128 -7.647 24.954 -1.073 1.00 34.06 C ANISOU 741 CG ARG A 128 3934 3395 5614 88 -286 125 C ATOM 742 CD ARG A 128 -9.080 24.449 -1.054 1.00 35.47 C ANISOU 742 CD ARG A 128 4105 3585 5788 134 -332 124 C ATOM 743 NE ARG A 128 -9.735 24.570 -2.360 1.00 37.16 N ANISOU 743 NE ARG A 128 4369 3760 5990 132 -394 234 N ATOM 744 CZ ARG A 128 -10.986 24.194 -2.618 1.00 51.27 C ANISOU 744 CZ ARG A 128 6148 5545 7787 164 -456 254 C ATOM 745 NH1 ARG A 128 -11.745 23.678 -1.658 1.00 36.71 N ANISOU 745 NH1 ARG A 128 4241 3736 5970 199 -446 177 N ATOM 746 NH2 ARG A 128 -11.483 24.319 -3.841 1.00 43.14 N ANISOU 746 NH2 ARG A 128 5174 4479 6737 159 -530 356 N ATOM 747 N PHE A 129 -5.796 25.646 3.180 1.00 29.53 N ANISOU 747 N PHE A 129 3221 2859 5141 95 -223 -240 N ATOM 748 CA PHE A 129 -4.920 25.497 4.343 1.00 29.76 C ANISOU 748 CA PHE A 129 3229 2930 5147 87 -220 -340 C ATOM 749 C PHE A 129 -5.735 25.334 5.617 1.00 33.81 C ANISOU 749 C PHE A 129 3740 3480 5627 133 -218 -442 C ATOM 750 O PHE A 129 -5.452 24.439 6.401 1.00 33.32 O ANISOU 750 O PHE A 129 3689 3506 5465 139 -212 -485 O ATOM 751 CB PHE A 129 -3.959 26.693 4.446 1.00 32.07 C ANISOU 751 CB PHE A 129 3492 3135 5557 44 -238 -370 C ATOM 752 CG PHE A 129 -3.080 26.762 5.674 1.00 33.49 C ANISOU 752 CG PHE A 129 3649 3342 5735 32 -261 -484 C ATOM 753 CD1 PHE A 129 -1.948 25.957 5.787 1.00 35.66 C ANISOU 753 CD1 PHE A 129 3907 3691 5951 7 -262 -480 C ATOM 754 CD2 PHE A 129 -3.344 27.676 6.688 1.00 35.51 C ANISOU 754 CD2 PHE A 129 3899 3540 6054 48 -289 -600 C ATOM 755 CE1 PHE A 129 -1.116 26.043 6.909 1.00 36.89 C ANISOU 755 CE1 PHE A 129 4041 3866 6110 -4 -306 -581 C ATOM 756 CE2 PHE A 129 -2.521 27.750 7.815 1.00 38.99 C ANISOU 756 CE2 PHE A 129 4330 4005 6479 35 -327 -710 C ATOM 757 CZ PHE A 129 -1.402 26.946 7.910 1.00 36.78 C ANISOU 757 CZ PHE A 129 4032 3800 6141 6 -343 -694 C ATOM 758 N ILE A 130 -6.749 26.188 5.803 1.00 31.37 N ANISOU 758 N ILE A 130 3417 3100 5401 166 -219 -477 N ATOM 759 CA ILE A 130 -7.647 26.167 6.960 1.00 30.99 C ANISOU 759 CA ILE A 130 3362 3082 5330 213 -194 -579 C ATOM 760 C ILE A 130 -8.427 24.847 7.044 1.00 33.51 C ANISOU 760 C ILE A 130 3690 3503 5537 234 -162 -542 C ATOM 761 O ILE A 130 -8.557 24.299 8.144 1.00 33.44 O ANISOU 761 O ILE A 130 3694 3571 5440 247 -133 -612 O ATOM 762 CB ILE A 130 -8.534 27.441 6.995 1.00 33.93 C ANISOU 762 CB ILE A 130 3703 3342 5846 250 -198 -625 C ATOM 763 CG1 ILE A 130 -7.662 28.671 7.379 1.00 34.58 C ANISOU 763 CG1 ILE A 130 3783 3330 6026 228 -230 -705 C ATOM 764 CG2 ILE A 130 -9.717 27.276 7.951 1.00 33.60 C ANISOU 764 CG2 ILE A 130 3642 3342 5782 308 -147 -711 C ATOM 765 CD1 ILE A 130 -8.303 30.082 7.176 1.00 37.57 C ANISOU 765 CD1 ILE A 130 4134 3558 6583 257 -252 -731 C ATOM 766 N PHE A 131 -8.905 24.318 5.897 1.00 28.95 N ANISOU 766 N PHE A 131 3115 2927 4959 230 -173 -432 N ATOM 767 CA PHE A 131 -9.615 23.030 5.896 1.00 28.86 C ANISOU 767 CA PHE A 131 3110 2998 4857 240 -153 -393 C ATOM 768 C PHE A 131 -8.703 21.934 6.484 1.00 33.16 C ANISOU 768 C PHE A 131 3691 3635 5275 219 -145 -406 C ATOM 769 O PHE A 131 -9.124 21.201 7.369 1.00 33.02 O ANISOU 769 O PHE A 131 3680 3686 5182 230 -116 -437 O ATOM 770 CB PHE A 131 -10.105 22.633 4.483 1.00 29.93 C ANISOU 770 CB PHE A 131 3253 3113 5007 233 -187 -279 C ATOM 771 CG PHE A 131 -10.566 21.196 4.410 1.00 30.43 C ANISOU 771 CG PHE A 131 3330 3253 4978 230 -181 -240 C ATOM 772 CD1 PHE A 131 -11.849 20.840 4.805 1.00 33.00 C ANISOU 772 CD1 PHE A 131 3617 3598 5325 253 -162 -248 C ATOM 773 CD2 PHE A 131 -9.684 20.183 4.037 1.00 32.07 C ANISOU 773 CD2 PHE A 131 3583 3512 5090 204 -189 -201 C ATOM 774 CE1 PHE A 131 -12.262 19.514 4.774 1.00 34.38 C ANISOU 774 CE1 PHE A 131 3801 3832 5429 240 -160 -209 C ATOM 775 CE2 PHE A 131 -10.095 18.849 4.025 1.00 34.16 C ANISOU 775 CE2 PHE A 131 3864 3833 5282 201 -190 -170 C ATOM 776 CZ PHE A 131 -11.382 18.523 4.388 1.00 32.49 C ANISOU 776 CZ PHE A 131 3618 3633 5095 214 -179 -171 C ATOM 777 N HIS A 132 -7.454 21.844 6.008 1.00 30.78 N ANISOU 777 N HIS A 132 3407 3332 4957 188 -169 -378 N ATOM 778 CA HIS A 132 -6.520 20.825 6.486 1.00 29.97 C ANISOU 778 CA HIS A 132 3327 3304 4758 175 -175 -386 C ATOM 779 C HIS A 132 -6.050 21.073 7.916 1.00 32.05 C ANISOU 779 C HIS A 132 3595 3598 4986 179 -180 -485 C ATOM 780 O HIS A 132 -5.910 20.117 8.674 1.00 30.45 O ANISOU 780 O HIS A 132 3419 3467 4684 184 -183 -495 O ATOM 781 CB HIS A 132 -5.375 20.638 5.504 1.00 30.93 C ANISOU 781 CB HIS A 132 3450 3415 4888 148 -189 -330 C ATOM 782 CG HIS A 132 -5.800 19.969 4.235 1.00 34.18 C ANISOU 782 CG HIS A 132 3884 3828 5274 147 -184 -240 C ATOM 783 ND1 HIS A 132 -6.038 20.696 3.076 1.00 36.08 N ANISOU 783 ND1 HIS A 132 4130 4008 5572 135 -186 -180 N ATOM 784 CD2 HIS A 132 -6.012 18.657 3.983 1.00 34.94 C ANISOU 784 CD2 HIS A 132 4009 3976 5292 155 -185 -204 C ATOM 785 CE1 HIS A 132 -6.388 19.803 2.165 1.00 35.02 C ANISOU 785 CE1 HIS A 132 4030 3897 5378 137 -191 -117 C ATOM 786 NE2 HIS A 132 -6.378 18.563 2.662 1.00 34.93 N ANISOU 786 NE2 HIS A 132 4031 3949 5292 149 -190 -134 N ATOM 787 N VAL A 133 -5.891 22.348 8.309 1.00 29.12 N ANISOU 787 N VAL A 133 3205 3166 4693 178 -188 -558 N ATOM 788 CA VAL A 133 -5.527 22.732 9.683 1.00 29.60 C ANISOU 788 CA VAL A 133 3281 3249 4718 183 -203 -671 C ATOM 789 C VAL A 133 -6.661 22.315 10.635 1.00 33.84 C ANISOU 789 C VAL A 133 3843 3846 5168 215 -153 -713 C ATOM 790 O VAL A 133 -6.399 21.733 11.682 1.00 33.05 O ANISOU 790 O VAL A 133 3785 3821 4953 216 -158 -754 O ATOM 791 CB VAL A 133 -5.144 24.237 9.797 1.00 33.63 C ANISOU 791 CB VAL A 133 3767 3663 5347 173 -228 -747 C ATOM 792 CG1 VAL A 133 -5.218 24.737 11.237 1.00 34.05 C ANISOU 792 CG1 VAL A 133 3847 3732 5357 191 -234 -886 C ATOM 793 CG2 VAL A 133 -3.750 24.484 9.223 1.00 33.25 C ANISOU 793 CG2 VAL A 133 3691 3579 5361 127 -274 -716 C ATOM 794 N ASN A 134 -7.915 22.549 10.232 1.00 32.15 N ANISOU 794 N ASN A 134 3603 3603 5010 240 -106 -692 N ATOM 795 CA ASN A 134 -9.072 22.145 11.020 1.00 32.41 C ANISOU 795 CA ASN A 134 3639 3693 4982 267 -39 -721 C ATOM 796 C ASN A 134 -9.133 20.615 11.129 1.00 35.55 C ANISOU 796 C ASN A 134 4067 4179 5260 251 -30 -643 C ATOM 797 O ASN A 134 -9.347 20.092 12.221 1.00 35.96 O ANISOU 797 O ASN A 134 4157 4306 5201 252 5 -677 O ATOM 798 CB ASN A 134 -10.368 22.688 10.422 1.00 30.75 C ANISOU 798 CB ASN A 134 3371 3424 4889 297 -1 -704 C ATOM 799 CG ASN A 134 -11.590 22.021 11.008 1.00 41.23 C ANISOU 799 CG ASN A 134 4680 4817 6168 316 77 -705 C ATOM 800 OD1 ASN A 134 -12.071 21.019 10.510 1.00 33.12 O ANISOU 800 OD1 ASN A 134 3642 3823 5120 302 81 -614 O ATOM 801 ND2 ASN A 134 -12.013 22.452 12.164 1.00 39.83 N ANISOU 801 ND2 ASN A 134 4506 4668 5959 342 144 -811 N ATOM 802 N LEU A 135 -8.947 19.915 10.004 1.00 30.67 N ANISOU 802 N LEU A 135 3441 3549 4662 234 -63 -541 N ATOM 803 CA LEU A 135 -8.982 18.456 9.943 1.00 31.03 C ANISOU 803 CA LEU A 135 3514 3655 4620 219 -66 -466 C ATOM 804 C LEU A 135 -7.984 17.807 10.902 1.00 32.68 C ANISOU 804 C LEU A 135 3777 3925 4715 208 -95 -487 C ATOM 805 O LEU A 135 -8.391 17.053 11.792 1.00 31.47 O ANISOU 805 O LEU A 135 3658 3835 4464 205 -68 -479 O ATOM 806 CB LEU A 135 -8.789 17.962 8.488 1.00 31.10 C ANISOU 806 CB LEU A 135 3515 3629 4674 207 -104 -375 C ATOM 807 CG LEU A 135 -8.667 16.452 8.244 1.00 37.21 C ANISOU 807 CG LEU A 135 4320 4443 5375 194 -122 -304 C ATOM 808 CD1 LEU A 135 -9.909 15.718 8.668 1.00 38.75 C ANISOU 808 CD1 LEU A 135 4510 4670 5544 190 -83 -275 C ATOM 809 CD2 LEU A 135 -8.386 16.164 6.795 1.00 39.82 C ANISOU 809 CD2 LEU A 135 4652 4735 5743 187 -156 -242 C ATOM 810 N TYR A 136 -6.703 18.145 10.752 1.00 28.38 N ANISOU 810 N TYR A 136 3235 3361 4189 200 -153 -509 N ATOM 811 CA TYR A 136 -5.635 17.582 11.572 1.00 27.36 C ANISOU 811 CA TYR A 136 3144 3278 3973 193 -206 -527 C ATOM 812 C TYR A 136 -5.548 18.112 12.979 1.00 32.18 C ANISOU 812 C TYR A 136 3793 3926 4507 198 -211 -622 C ATOM 813 O TYR A 136 -5.207 17.357 13.880 1.00 31.75 O ANISOU 813 O TYR A 136 3793 3933 4337 195 -242 -617 O ATOM 814 CB TYR A 136 -4.314 17.576 10.811 1.00 27.23 C ANISOU 814 CB TYR A 136 3099 3231 4017 183 -264 -506 C ATOM 815 CG TYR A 136 -4.443 16.684 9.595 1.00 27.43 C ANISOU 815 CG TYR A 136 3114 3244 4065 183 -253 -414 C ATOM 816 CD1 TYR A 136 -4.597 15.302 9.732 1.00 28.77 C ANISOU 816 CD1 TYR A 136 3317 3452 4161 189 -263 -358 C ATOM 817 CD2 TYR A 136 -4.535 17.225 8.317 1.00 27.53 C ANISOU 817 CD2 TYR A 136 3093 3203 4165 176 -232 -382 C ATOM 818 CE1 TYR A 136 -4.755 14.477 8.623 1.00 27.87 C ANISOU 818 CE1 TYR A 136 3202 3320 4068 191 -257 -289 C ATOM 819 CE2 TYR A 136 -4.681 16.410 7.196 1.00 27.80 C ANISOU 819 CE2 TYR A 136 3133 3230 4200 177 -225 -309 C ATOM 820 CZ TYR A 136 -4.791 15.036 7.356 1.00 31.59 C ANISOU 820 CZ TYR A 136 3645 3746 4612 186 -238 -271 C ATOM 821 OH TYR A 136 -4.979 14.234 6.263 1.00 30.42 O ANISOU 821 OH TYR A 136 3509 3583 4464 189 -236 -214 O ATOM 822 N GLY A 137 -5.924 19.375 13.170 1.00 30.06 N ANISOU 822 N GLY A 137 3506 3618 4297 207 -182 -707 N ATOM 823 CA GLY A 137 -5.984 19.992 14.491 1.00 31.10 C ANISOU 823 CA GLY A 137 3684 3782 4353 216 -176 -819 C ATOM 824 C GLY A 137 -7.053 19.297 15.312 1.00 35.55 C ANISOU 824 C GLY A 137 4292 4423 4791 225 -97 -808 C ATOM 825 O GLY A 137 -6.808 18.937 16.463 1.00 36.33 O ANISOU 825 O GLY A 137 4465 4593 4746 221 -110 -841 O ATOM 826 N SER A 138 -8.230 19.035 14.685 1.00 30.95 N ANISOU 826 N SER A 138 3665 3830 4263 233 -18 -749 N ATOM 827 CA SER A 138 -9.348 18.323 15.299 1.00 30.69 C ANISOU 827 CA SER A 138 3651 3865 4144 233 73 -719 C ATOM 828 C SER A 138 -8.938 16.930 15.714 1.00 33.08 C ANISOU 828 C SER A 138 4018 4233 4317 207 40 -631 C ATOM 829 O SER A 138 -9.165 16.552 16.865 1.00 33.44 O ANISOU 829 O SER A 138 4131 4354 4220 200 79 -646 O ATOM 830 CB SER A 138 -10.538 18.233 14.349 1.00 33.61 C ANISOU 830 CB SER A 138 3943 4197 4631 240 133 -657 C ATOM 831 OG SER A 138 -11.090 19.520 14.139 1.00 44.33 O ANISOU 831 OG SER A 138 5242 5492 6108 272 168 -737 O ATOM 832 N ILE A 139 -8.309 16.175 14.785 1.00 27.61 N ANISOU 832 N ILE A 139 3309 3509 3671 195 -32 -543 N ATOM 833 CA ILE A 139 -7.836 14.817 15.063 1.00 27.10 C ANISOU 833 CA ILE A 139 3299 3484 3513 177 -80 -456 C ATOM 834 C ILE A 139 -6.887 14.821 16.255 1.00 32.47 C ANISOU 834 C ILE A 139 4056 4213 4066 176 -144 -503 C ATOM 835 O ILE A 139 -7.076 14.020 17.176 1.00 33.40 O ANISOU 835 O ILE A 139 4247 4394 4048 163 -135 -461 O ATOM 836 CB ILE A 139 -7.213 14.127 13.821 1.00 28.51 C ANISOU 836 CB ILE A 139 3445 3610 3778 175 -146 -380 C ATOM 837 CG1 ILE A 139 -8.276 13.900 12.715 1.00 27.96 C ANISOU 837 CG1 ILE A 139 3321 3501 3804 170 -95 -323 C ATOM 838 CG2 ILE A 139 -6.573 12.800 14.228 1.00 29.12 C ANISOU 838 CG2 ILE A 139 3578 3714 3771 167 -210 -307 C ATOM 839 CD1 ILE A 139 -7.687 13.635 11.289 1.00 33.32 C ANISOU 839 CD1 ILE A 139 3967 4120 4574 175 -150 -280 C ATOM 840 N LEU A 140 -5.877 15.726 16.239 1.00 28.40 N ANISOU 840 N LEU A 140 3527 3668 3595 187 -216 -585 N ATOM 841 CA LEU A 140 -4.897 15.805 17.315 1.00 29.70 C ANISOU 841 CA LEU A 140 3758 3873 3655 185 -305 -639 C ATOM 842 C LEU A 140 -5.507 16.230 18.650 1.00 35.19 C ANISOU 842 C LEU A 140 4533 4635 4201 186 -249 -718 C ATOM 843 O LEU A 140 -5.103 15.695 19.681 1.00 36.13 O ANISOU 843 O LEU A 140 4745 4818 4166 178 -303 -709 O ATOM 844 CB LEU A 140 -3.647 16.642 16.941 1.00 29.48 C ANISOU 844 CB LEU A 140 3680 3789 3733 188 -401 -706 C ATOM 845 CG LEU A 140 -2.753 16.172 15.768 1.00 32.45 C ANISOU 845 CG LEU A 140 3983 4112 4232 187 -459 -636 C ATOM 846 CD1 LEU A 140 -1.359 16.776 15.875 1.00 32.12 C ANISOU 846 CD1 LEU A 140 3905 4042 4258 182 -565 -699 C ATOM 847 CD2 LEU A 140 -2.607 14.670 15.723 1.00 33.03 C ANISOU 847 CD2 LEU A 140 4087 4214 4249 191 -491 -529 C ATOM 848 N PHE A 141 -6.497 17.154 18.635 1.00 31.71 N ANISOU 848 N PHE A 141 4062 4182 3802 198 -141 -792 N ATOM 849 CA PHE A 141 -7.175 17.574 19.869 1.00 33.12 C ANISOU 849 CA PHE A 141 4315 4430 3840 205 -60 -880 C ATOM 850 C PHE A 141 -8.100 16.488 20.398 1.00 36.76 C ANISOU 850 C PHE A 141 4825 4971 4172 187 36 -786 C ATOM 851 O PHE A 141 -8.212 16.332 21.614 1.00 36.25 O ANISOU 851 O PHE A 141 4862 4989 3921 179 65 -816 O ATOM 852 CB PHE A 141 -7.838 18.966 19.765 1.00 35.45 C ANISOU 852 CB PHE A 141 4558 4678 4233 233 20 -1009 C ATOM 853 CG PHE A 141 -6.815 20.082 19.816 1.00 37.73 C ANISOU 853 CG PHE A 141 4845 4906 4586 241 -84 -1127 C ATOM 854 CD1 PHE A 141 -6.022 20.273 20.945 1.00 42.09 C ANISOU 854 CD1 PHE A 141 5493 5504 4996 234 -167 -1214 C ATOM 855 CD2 PHE A 141 -6.629 20.928 18.730 1.00 38.91 C ANISOU 855 CD2 PHE A 141 4898 4947 4937 248 -107 -1144 C ATOM 856 CE1 PHE A 141 -5.057 21.279 20.978 1.00 43.43 C ANISOU 856 CE1 PHE A 141 5650 5607 5242 233 -275 -1324 C ATOM 857 CE2 PHE A 141 -5.657 21.934 18.764 1.00 42.01 C ANISOU 857 CE2 PHE A 141 5282 5274 5405 244 -203 -1242 C ATOM 858 CZ PHE A 141 -4.878 22.101 19.885 1.00 41.59 C ANISOU 858 CZ PHE A 141 5313 5263 5226 235 -288 -1335 C ATOM 859 N LEU A 142 -8.659 15.657 19.490 1.00 33.27 N ANISOU 859 N LEU A 142 4319 4501 3819 174 71 -665 N ATOM 860 CA LEU A 142 -9.476 14.499 19.872 1.00 33.48 C ANISOU 860 CA LEU A 142 4381 4587 3752 145 150 -554 C ATOM 861 C LEU A 142 -8.572 13.454 20.530 1.00 38.29 C ANISOU 861 C LEU A 142 5095 5237 4217 123 46 -473 C ATOM 862 O LEU A 142 -8.993 12.809 21.496 1.00 39.46 O ANISOU 862 O LEU A 142 5330 5460 4203 97 100 -421 O ATOM 863 CB LEU A 142 -10.238 13.888 18.672 1.00 31.85 C ANISOU 863 CB LEU A 142 4079 4327 3697 133 189 -453 C ATOM 864 CG LEU A 142 -11.417 14.705 18.123 1.00 36.37 C ANISOU 864 CG LEU A 142 4548 4868 4404 151 300 -503 C ATOM 865 CD1 LEU A 142 -11.942 14.108 16.834 1.00 35.53 C ANISOU 865 CD1 LEU A 142 4355 4698 4447 139 289 -406 C ATOM 866 CD2 LEU A 142 -12.530 14.873 19.151 1.00 37.65 C ANISOU 866 CD2 LEU A 142 4723 5107 4476 146 455 -540 C ATOM 867 N THR A 143 -7.306 13.342 20.045 1.00 33.74 N ANISOU 867 N THR A 143 4509 4610 3699 135 -102 -465 N ATOM 868 CA THR A 143 -6.303 12.430 20.593 1.00 33.78 C ANISOU 868 CA THR A 143 4597 4637 3602 126 -230 -397 C ATOM 869 C THR A 143 -5.907 12.902 22.000 1.00 41.25 C ANISOU 869 C THR A 143 5656 5658 4357 126 -267 -478 C ATOM 870 O THR A 143 -5.789 12.070 22.904 1.00 42.62 O ANISOU 870 O THR A 143 5938 5890 4364 107 -301 -404 O ATOM 871 CB THR A 143 -5.105 12.267 19.648 1.00 35.40 C ANISOU 871 CB THR A 143 4735 4766 3947 145 -362 -382 C ATOM 872 OG1 THR A 143 -5.570 11.982 18.327 1.00 32.31 O ANISOU 872 OG1 THR A 143 4252 4313 3713 147 -313 -329 O ATOM 873 CG2 THR A 143 -4.156 11.164 20.096 1.00 32.58 C ANISOU 873 CG2 THR A 143 4442 4417 3519 146 -495 -296 C ATOM 874 N CYS A 144 -5.738 14.234 22.181 1.00 37.79 N ANISOU 874 N CYS A 144 5201 5214 3943 145 -263 -629 N ATOM 875 CA CYS A 144 -5.403 14.870 23.463 1.00 39.09 C ANISOU 875 CA CYS A 144 5475 5444 3934 148 -299 -740 C ATOM 876 C CYS A 144 -6.466 14.555 24.504 1.00 44.15 C ANISOU 876 C CYS A 144 6219 6185 4371 130 -160 -723 C ATOM 877 O CYS A 144 -6.122 14.126 25.608 1.00 45.75 O ANISOU 877 O CYS A 144 6557 6462 4363 116 -216 -704 O ATOM 878 CB CYS A 144 -5.229 16.376 23.295 1.00 39.16 C ANISOU 878 CB CYS A 144 5430 5406 4044 171 -299 -909 C ATOM 879 SG CYS A 144 -3.690 16.861 22.480 1.00 42.03 S ANISOU 879 SG CYS A 144 5704 5671 4593 177 -483 -944 S ATOM 880 N ILE A 145 -7.760 14.757 24.143 1.00 40.10 N ANISOU 880 N ILE A 145 5639 5673 3923 131 20 -724 N ATOM 881 CA ILE A 145 -8.923 14.488 25.004 1.00 40.52 C ANISOU 881 CA ILE A 145 5759 5821 3817 111 191 -705 C ATOM 882 C ILE A 145 -8.964 12.999 25.378 1.00 44.92 C ANISOU 882 C ILE A 145 6395 6423 4249 66 175 -523 C ATOM 883 O ILE A 145 -9.150 12.668 26.547 1.00 46.15 O ANISOU 883 O ILE A 145 6684 6675 4175 42 219 -501 O ATOM 884 CB ILE A 145 -10.251 14.998 24.372 1.00 42.19 C ANISOU 884 CB ILE A 145 5845 6007 4178 125 372 -740 C ATOM 885 CG1 ILE A 145 -10.217 16.527 24.171 1.00 41.52 C ANISOU 885 CG1 ILE A 145 5702 5873 4203 173 383 -924 C ATOM 886 CG2 ILE A 145 -11.462 14.603 25.231 1.00 43.96 C ANISOU 886 CG2 ILE A 145 6117 6332 4256 99 565 -706 C ATOM 887 CD1 ILE A 145 -11.133 17.080 23.066 1.00 40.87 C ANISOU 887 CD1 ILE A 145 5460 5710 4358 197 475 -940 C ATOM 888 N SER A 146 -8.735 12.121 24.388 1.00 41.15 N ANISOU 888 N SER A 146 5844 5871 3919 55 106 -396 N ATOM 889 CA SER A 146 -8.699 10.666 24.556 1.00 41.60 C ANISOU 889 CA SER A 146 5961 5937 3906 16 69 -218 C ATOM 890 C SER A 146 -7.574 10.232 25.505 1.00 46.61 C ANISOU 890 C SER A 146 6739 6610 4360 14 -93 -185 C ATOM 891 O SER A 146 -7.838 9.471 26.436 1.00 47.15 O ANISOU 891 O SER A 146 6930 6746 4239 -24 -66 -85 O ATOM 892 CB SER A 146 -8.572 9.978 23.199 1.00 42.84 C ANISOU 892 CB SER A 146 6006 5991 4280 18 10 -126 C ATOM 893 OG SER A 146 -9.677 10.325 22.382 1.00 47.18 O ANISOU 893 OG SER A 146 6435 6510 4982 16 145 -145 O ATOM 894 N ALA A 147 -6.338 10.757 25.300 1.00 43.49 N ANISOU 894 N ALA A 147 6329 6173 4023 50 -260 -269 N ATOM 895 CA ALA A 147 -5.170 10.473 26.146 1.00 44.54 C ANISOU 895 CA ALA A 147 6577 6332 4014 55 -444 -256 C ATOM 896 C ALA A 147 -5.352 11.026 27.566 1.00 50.06 C ANISOU 896 C ALA A 147 7429 7143 4447 43 -411 -338 C ATOM 897 O ALA A 147 -4.913 10.391 28.531 1.00 50.51 O ANISOU 897 O ALA A 147 7630 7254 4305 26 -510 -264 O ATOM 898 CB ALA A 147 -3.910 11.043 25.515 1.00 44.45 C ANISOU 898 CB ALA A 147 6480 6247 4164 93 -610 -340 C ATOM 899 N HIS A 148 -6.036 12.185 27.692 1.00 47.07 N ANISOU 899 N HIS A 148 7027 6796 4062 55 -272 -490 N ATOM 900 CA HIS A 148 -6.324 12.821 28.977 1.00 49.17 C ANISOU 900 CA HIS A 148 7435 7169 4081 51 -210 -600 C ATOM 901 C HIS A 148 -7.316 11.978 29.794 1.00 55.26 C ANISOU 901 C HIS A 148 8317 8039 4638 6 -54 -480 C ATOM 902 O HIS A 148 -7.059 11.730 30.972 1.00 56.48 O ANISOU 902 O HIS A 148 8649 8285 4526 -13 -96 -463 O ATOM 903 CB HIS A 148 -6.828 14.260 28.783 1.00 49.63 C ANISOU 903 CB HIS A 148 7418 7213 4225 84 -96 -799 C ATOM 904 CG HIS A 148 -6.905 15.041 30.054 1.00 55.22 C ANISOU 904 CG HIS A 148 8272 8015 4693 91 -60 -951 C ATOM 905 ND1 HIS A 148 -5.845 15.825 30.485 1.00 57.75 N ANISOU 905 ND1 HIS A 148 8650 8321 4971 111 -234 -1093 N ATOM 906 CD2 HIS A 148 -7.902 15.116 30.965 1.00 58.49 C ANISOU 906 CD2 HIS A 148 8785 8538 4900 79 130 -982 C ATOM 907 CE1 HIS A 148 -6.237 16.361 31.628 1.00 59.01 C ANISOU 907 CE1 HIS A 148 8951 8579 4892 113 -153 -1215 C ATOM 908 NE2 HIS A 148 -7.469 15.966 31.957 1.00 60.08 N ANISOU 908 NE2 HIS A 148 9118 8795 4916 97 75 -1155 N ATOM 909 N ARG A 149 -8.426 11.517 29.166 1.00 51.85 N ANISOU 909 N ARG A 149 7785 7589 4325 -15 120 -390 N ATOM 910 CA ARG A 149 -9.429 10.669 29.821 1.00 53.62 C ANISOU 910 CA ARG A 149 8086 7897 4390 -69 287 -258 C ATOM 911 C ARG A 149 -8.853 9.319 30.226 1.00 59.64 C ANISOU 911 C ARG A 149 8967 8663 5031 -110 154 -60 C ATOM 912 O ARG A 149 -9.237 8.799 31.264 1.00 61.61 O ANISOU 912 O ARG A 149 9363 9008 5036 -154 228 25 O ATOM 913 CB ARG A 149 -10.687 10.494 28.958 1.00 53.22 C ANISOU 913 CB ARG A 149 7875 7809 4537 -85 477 -210 C ATOM 914 CG ARG A 149 -11.684 11.640 29.088 1.00 61.99 C ANISOU 914 CG ARG A 149 8920 8964 5669 -59 682 -373 C ATOM 915 CD ARG A 149 -12.505 11.572 30.366 1.00 68.95 C ANISOU 915 CD ARG A 149 9926 9986 6288 -94 877 -372 C ATOM 916 NE ARG A 149 -13.572 12.574 30.369 1.00 73.67 N ANISOU 916 NE ARG A 149 10428 10614 6949 -63 1093 -523 N ATOM 917 CZ ARG A 149 -13.525 13.727 31.026 1.00 84.34 C ANISOU 917 CZ ARG A 149 11838 12017 8192 -15 1141 -725 C ATOM 918 NH1 ARG A 149 -12.470 14.034 31.770 1.00 74.05 N ANISOU 918 NH1 ARG A 149 10693 10745 6696 -1 982 -803 N ATOM 919 NH2 ARG A 149 -14.541 14.577 30.957 1.00 66.01 N ANISOU 919 NH2 ARG A 149 9412 9708 5960 20 1341 -857 N ATOM 920 N TYR A 150 -7.904 8.775 29.438 1.00 56.32 N ANISOU 920 N TYR A 150 8485 8137 4776 -91 -42 10 N ATOM 921 CA TYR A 150 -7.215 7.524 29.756 1.00 57.54 C ANISOU 921 CA TYR A 150 8740 8271 4853 -115 -201 188 C ATOM 922 C TYR A 150 -6.392 7.710 31.044 1.00 64.19 C ANISOU 922 C TYR A 150 9772 9196 5421 -111 -340 156 C ATOM 923 O TYR A 150 -6.431 6.844 31.918 1.00 65.58 O ANISOU 923 O TYR A 150 10103 9425 5388 -152 -364 301 O ATOM 924 CB TYR A 150 -6.348 7.044 28.569 1.00 57.21 C ANISOU 924 CB TYR A 150 8572 8094 5071 -80 -372 232 C ATOM 925 CG TYR A 150 -5.219 6.103 28.945 1.00 60.66 C ANISOU 925 CG TYR A 150 9102 8496 5449 -73 -600 351 C ATOM 926 CD1 TYR A 150 -5.473 4.776 29.285 1.00 63.59 C ANISOU 926 CD1 TYR A 150 9559 8854 5748 -116 -611 555 C ATOM 927 CD2 TYR A 150 -3.895 6.531 28.934 1.00 61.76 C ANISOU 927 CD2 TYR A 150 9232 8605 5628 -23 -811 265 C ATOM 928 CE1 TYR A 150 -4.441 3.912 29.654 1.00 65.13 C ANISOU 928 CE1 TYR A 150 9840 9007 5899 -103 -832 668 C ATOM 929 CE2 TYR A 150 -2.851 5.669 29.276 1.00 63.91 C ANISOU 929 CE2 TYR A 150 9575 8841 5869 -9 -1031 373 C ATOM 930 CZ TYR A 150 -3.129 4.359 29.635 1.00 73.23 C ANISOU 930 CZ TYR A 150 10848 10006 6970 -45 -1044 575 C ATOM 931 OH TYR A 150 -2.103 3.506 29.975 1.00 76.14 O ANISOU 931 OH TYR A 150 11284 10326 7321 -23 -1272 685 O ATOM 932 N SER A 151 -5.696 8.861 31.172 1.00 60.90 N ANISOU 932 N SER A 151 9349 8789 5004 -66 -431 -33 N ATOM 933 CA SER A 151 -4.901 9.215 32.348 1.00 62.63 C ANISOU 933 CA SER A 151 9738 9082 4974 -58 -579 -101 C ATOM 934 C SER A 151 -5.786 9.398 33.588 1.00 68.45 C ANISOU 934 C SER A 151 10652 9964 5393 -96 -406 -121 C ATOM 935 O SER A 151 -5.388 9.003 34.677 1.00 69.46 O ANISOU 935 O SER A 151 10974 10168 5250 -117 -507 -61 O ATOM 936 CB SER A 151 -4.079 10.471 32.088 1.00 65.89 C ANISOU 936 CB SER A 151 10079 9458 5500 -9 -696 -312 C ATOM 937 OG SER A 151 -2.966 10.185 31.258 1.00 75.66 O ANISOU 937 OG SER A 151 11200 10584 6964 20 -899 -278 O ATOM 938 N GLY A 152 -6.977 9.962 33.400 1.00 65.01 N ANISOU 938 N GLY A 152 10145 9565 4992 -103 -148 -199 N ATOM 939 CA GLY A 152 -7.944 10.173 34.472 1.00 67.11 C ANISOU 939 CA GLY A 152 10548 9969 4982 -135 65 -229 C ATOM 940 C GLY A 152 -8.604 8.889 34.937 1.00 72.44 C ANISOU 940 C GLY A 152 11317 10697 5508 -205 170 4 C ATOM 941 O GLY A 152 -8.718 8.660 36.140 1.00 74.03 O ANISOU 941 O GLY A 152 11723 11018 5386 -241 209 48 O ATOM 942 N VAL A 153 -9.044 8.044 33.980 1.00 68.32 N ANISOU 942 N VAL A 153 10653 10085 5219 -229 216 158 N ATOM 943 CA VAL A 153 -9.706 6.756 34.236 1.00 69.35 C ANISOU 943 CA VAL A 153 10841 10233 5274 -304 313 394 C ATOM 944 C VAL A 153 -8.734 5.704 34.811 1.00 76.19 C ANISOU 944 C VAL A 153 11875 11084 5988 -327 81 573 C ATOM 945 O VAL A 153 -9.022 5.121 35.859 1.00 78.45 O ANISOU 945 O VAL A 153 12346 11465 5998 -385 138 703 O ATOM 946 CB VAL A 153 -10.484 6.253 32.978 1.00 70.55 C ANISOU 946 CB VAL A 153 10781 10281 5745 -322 420 479 C ATOM 947 CG1 VAL A 153 -10.846 4.771 33.069 1.00 71.06 C ANISOU 947 CG1 VAL A 153 10895 10317 5789 -399 439 739 C ATOM 948 CG2 VAL A 153 -11.732 7.093 32.729 1.00 69.93 C ANISOU 948 CG2 VAL A 153 10572 10245 5752 -319 689 350 C ATOM 949 N VAL A 154 -7.598 5.472 34.131 1.00 72.42 N ANISOU 949 N VAL A 154 11333 10490 5694 -280 -175 583 N ATOM 950 CA VAL A 154 -6.608 4.463 34.519 1.00 73.82 C ANISOU 950 CA VAL A 154 11632 10624 5792 -286 -421 749 C ATOM 951 C VAL A 154 -5.682 4.895 35.669 1.00 81.46 C ANISOU 951 C VAL A 154 12795 11677 6481 -265 -605 682 C ATOM 952 O VAL A 154 -5.503 4.117 36.611 1.00 83.68 O ANISOU 952 O VAL A 154 13269 12006 6519 -305 -684 843 O ATOM 953 CB VAL A 154 -5.860 3.858 33.295 1.00 75.54 C ANISOU 953 CB VAL A 154 11688 10676 6338 -245 -599 808 C ATOM 954 CG1 VAL A 154 -4.878 2.764 33.712 1.00 76.61 C ANISOU 954 CG1 VAL A 154 11941 10757 6412 -243 -851 984 C ATOM 955 CG2 VAL A 154 -6.852 3.307 32.272 1.00 73.81 C ANISOU 955 CG2 VAL A 154 11313 10381 6352 -276 -425 890 C ATOM 956 N TYR A 155 -5.117 6.121 35.613 1.00 78.26 N ANISOU 956 N TYR A 155 12346 11286 6104 -209 -678 453 N ATOM 957 CA TYR A 155 -4.189 6.612 36.645 1.00 80.59 C ANISOU 957 CA TYR A 155 12813 11652 6155 -189 -875 364 C ATOM 958 C TYR A 155 -4.717 7.826 37.479 1.00 85.79 C ANISOU 958 C TYR A 155 13574 12446 6577 -190 -720 156 C ATOM 959 O TYR A 155 -4.153 8.918 37.356 1.00 84.78 O ANISOU 959 O TYR A 155 13393 12303 6518 -142 -808 -56 O ATOM 960 CB TYR A 155 -2.808 6.919 36.021 1.00 80.88 C ANISOU 960 CB TYR A 155 12735 11580 6417 -124 -1158 277 C ATOM 961 CG TYR A 155 -2.122 5.730 35.381 1.00 82.55 C ANISOU 961 CG TYR A 155 12871 11666 6829 -111 -1337 463 C ATOM 962 CD1 TYR A 155 -1.299 4.890 36.127 1.00 86.79 C ANISOU 962 CD1 TYR A 155 13559 12200 7219 -114 -1575 611 C ATOM 963 CD2 TYR A 155 -2.253 5.474 34.018 1.00 80.75 C ANISOU 963 CD2 TYR A 155 12423 11318 6941 -90 -1280 483 C ATOM 964 CE1 TYR A 155 -0.649 3.804 35.539 1.00 87.69 C ANISOU 964 CE1 TYR A 155 13596 12187 7535 -91 -1743 772 C ATOM 965 CE2 TYR A 155 -1.609 4.392 33.419 1.00 81.01 C ANISOU 965 CE2 TYR A 155 12388 11232 7161 -70 -1438 634 C ATOM 966 CZ TYR A 155 -0.809 3.558 34.184 1.00 91.50 C ANISOU 966 CZ TYR A 155 13858 12551 8356 -67 -1667 776 C ATOM 967 OH TYR A 155 -0.173 2.490 33.598 1.00 92.65 O ANISOU 967 OH TYR A 155 13931 12568 8703 -38 -1823 917 O ATOM 968 N PRO A 156 -5.759 7.689 38.344 1.00 84.43 N ANISOU 968 N PRO A 156 13549 12403 6129 -243 -489 203 N ATOM 969 CA PRO A 156 -6.217 8.863 39.111 1.00 88.49 C ANISOU 969 CA PRO A 156 14156 13040 6426 -232 -339 -17 C ATOM 970 C PRO A 156 -5.431 9.116 40.398 1.00116.98 C ANISOU 970 C PRO A 156 18018 16747 9683 -230 -530 -82 C ATOM 971 O PRO A 156 -4.364 8.546 40.619 1.00 77.25 O ANISOU 971 O PRO A 156 13072 11677 4601 -228 -813 30 O ATOM 972 CB PRO A 156 -7.696 8.560 39.391 1.00 90.84 C ANISOU 972 CB PRO A 156 14480 13433 6603 -288 7 64 C ATOM 973 CG PRO A 156 -7.892 7.094 39.067 1.00 94.03 C ANISOU 973 CG PRO A 156 14863 13776 7086 -345 -2 357 C ATOM 974 CD PRO A 156 -6.574 6.503 38.673 1.00 87.98 C ANISOU 974 CD PRO A 156 14083 12891 6454 -316 -343 449 C ATOM 975 N LYS A 158 -4.999 12.731 45.378 1.00111.95 N ANISOU 975 N LYS A 158 18326 16662 7547 -194 -567 -911 N ATOM 976 CA LYS A 158 -4.386 13.207 44.142 1.00108.50 C ANISOU 976 CA LYS A 158 17611 16049 7567 -145 -710 -997 C ATOM 977 C LYS A 158 -5.166 14.385 43.555 1.00111.01 C ANISOU 977 C LYS A 158 17752 16332 8094 -100 -465 -1237 C ATOM 978 O LYS A 158 -6.356 14.249 43.262 1.00110.41 O ANISOU 978 O LYS A 158 17589 16288 8074 -111 -147 -1194 O ATOM 979 CB LYS A 158 -4.269 12.066 43.114 1.00108.34 C ANISOU 979 CB LYS A 158 17407 15911 7846 -163 -757 -729 C ATOM 980 N SER A 159 -4.494 15.544 43.400 1.00106.66 N ANISOU 980 N SER A 159 17145 15710 7669 -51 -620 -1488 N ATOM 981 CA SER A 159 -5.083 16.763 42.839 1.00105.12 C ANISOU 981 CA SER A 159 16787 15458 7696 -2 -436 -1730 C ATOM 982 C SER A 159 -4.048 17.559 42.031 1.00105.68 C ANISOU 982 C SER A 159 16686 15366 8102 36 -687 -1869 C ATOM 983 O SER A 159 -3.433 18.501 42.544 1.00106.36 O ANISOU 983 O SER A 159 16860 15445 8108 58 -844 -2091 O ATOM 984 CB SER A 159 -5.728 17.615 43.930 1.00112.65 C ANISOU 984 CB SER A 159 17935 16545 8323 15 -255 -1961 C ATOM 985 OG SER A 159 -6.416 18.723 43.371 1.00122.02 O ANISOU 985 OG SER A 159 18954 17667 9742 68 -56 -2181 O ATOM 986 N LEU A 160 -3.854 17.157 40.761 1.00 98.21 N ANISOU 986 N LEU A 160 15497 14288 7532 40 -725 -1733 N ATOM 987 CA LEU A 160 -2.921 17.797 39.833 1.00 95.47 C ANISOU 987 CA LEU A 160 14957 13782 7535 67 -931 -1825 C ATOM 988 C LEU A 160 -3.677 18.724 38.863 1.00 96.35 C ANISOU 988 C LEU A 160 14855 13801 7954 104 -720 -1957 C ATOM 989 O LEU A 160 -3.388 18.742 37.663 1.00 93.47 O ANISOU 989 O LEU A 160 14270 13304 7939 114 -768 -1902 O ATOM 990 CB LEU A 160 -2.107 16.729 39.081 1.00 93.56 C ANISOU 990 CB LEU A 160 14600 13456 7491 49 -1126 -1588 C ATOM 991 N GLY A 161 -4.622 19.495 39.414 1.00 93.14 N ANISOU 991 N GLY A 161 14521 13464 7405 127 -491 -2134 N ATOM 992 CA GLY A 161 -5.477 20.436 38.693 1.00 90.99 C ANISOU 992 CA GLY A 161 14073 13116 7383 171 -275 -2276 C ATOM 993 C GLY A 161 -4.735 21.439 37.836 1.00 91.30 C ANISOU 993 C GLY A 161 13945 12987 7759 199 -437 -2416 C ATOM 994 O GLY A 161 -4.914 21.446 36.614 1.00 87.91 O ANISOU 994 O GLY A 161 13297 12445 7661 208 -389 -2340 O ATOM 995 N ARG A 162 -3.889 22.285 38.469 1.00 88.40 N ANISOU 995 N ARG A 162 13684 12600 7305 206 -635 -2617 N ATOM 996 CA ARG A 162 -3.074 23.293 37.778 1.00 86.49 C ANISOU 996 CA ARG A 162 13299 12196 7369 220 -811 -2758 C ATOM 997 C ARG A 162 -2.025 22.640 36.871 1.00 86.38 C ANISOU 997 C ARG A 162 13136 12088 7596 190 -1029 -2572 C ATOM 998 O ARG A 162 -1.773 23.146 35.776 1.00 83.43 O ANISOU 998 O ARG A 162 12560 11574 7566 199 -1053 -2585 O ATOM 999 CB ARG A 162 -2.397 24.240 38.773 1.00 89.67 C ANISOU 999 CB ARG A 162 13864 12603 7601 225 -988 -3010 C ATOM 1000 CG ARG A 162 -3.097 25.584 38.915 1.00101.45 C ANISOU 1000 CG ARG A 162 15347 14043 9156 274 -831 -3282 C ATOM 1001 CD ARG A 162 -2.152 26.634 39.469 1.00110.60 C ANISOU 1001 CD ARG A 162 16590 15133 10301 272 -1074 -3527 C ATOM 1002 NE ARG A 162 -2.810 27.506 40.443 1.00119.78 N ANISOU 1002 NE ARG A 162 17924 16355 11234 313 -942 -3794 N ATOM 1003 CZ ARG A 162 -2.786 27.316 41.759 1.00135.27 C ANISOU 1003 CZ ARG A 162 20151 18469 12777 306 -972 -3875 C ATOM 1004 NH1 ARG A 162 -2.138 26.278 42.276 1.00123.69 N ANISOU 1004 NH1 ARG A 162 18812 17107 11078 258 -1144 -3699 N ATOM 1005 NH2 ARG A 162 -3.410 28.161 42.568 1.00121.18 N ANISOU 1005 NH2 ARG A 162 18512 16732 10799 350 -833 -4135 N ATOM 1006 N LEU A 163 -1.432 21.510 37.327 1.00 82.32 N ANISOU 1006 N LEU A 163 12725 11651 6901 157 -1179 -2396 N ATOM 1007 CA LEU A 163 -0.429 20.731 36.593 1.00 79.67 C ANISOU 1007 CA LEU A 163 12264 11242 6763 136 -1384 -2213 C ATOM 1008 C LEU A 163 -1.009 20.183 35.285 1.00 78.15 C ANISOU 1008 C LEU A 163 11867 10985 6842 141 -1216 -2041 C ATOM 1009 O LEU A 163 -0.313 20.203 34.273 1.00 76.13 O ANISOU 1009 O LEU A 163 11432 10613 6882 140 -1324 -1991 O ATOM 1010 CB LEU A 163 0.134 19.592 37.471 1.00 81.38 C ANISOU 1010 CB LEU A 163 12656 11563 6702 109 -1555 -2058 C ATOM 1011 CG LEU A 163 1.265 18.729 36.880 1.00 85.03 C ANISOU 1011 CG LEU A 163 13007 11954 7347 95 -1792 -1878 C ATOM 1012 CD1 LEU A 163 2.601 19.464 36.892 1.00 85.90 C ANISOU 1012 CD1 LEU A 163 13061 11977 7602 92 -2084 -2013 C ATOM 1013 CD2 LEU A 163 1.397 17.425 37.635 1.00 89.13 C ANISOU 1013 CD2 LEU A 163 13692 12575 7598 76 -1877 -1678 C ATOM 1014 N LYS A 164 -2.279 19.720 35.302 1.00 72.13 N ANISOU 1014 N LYS A 164 11130 10297 5977 146 -952 -1957 N ATOM 1015 CA LYS A 164 -2.970 19.209 34.117 1.00 68.14 C ANISOU 1015 CA LYS A 164 10445 9737 5709 149 -785 -1806 C ATOM 1016 C LYS A 164 -3.372 20.348 33.182 1.00 68.37 C ANISOU 1016 C LYS A 164 10297 9652 6027 180 -678 -1942 C ATOM 1017 O LYS A 164 -3.299 20.169 31.969 1.00 65.44 O ANISOU 1017 O LYS A 164 9747 9184 5933 182 -674 -1845 O ATOM 1018 CB LYS A 164 -4.185 18.347 34.491 1.00 70.83 C ANISOU 1018 CB LYS A 164 10863 10191 5859 135 -550 -1675 C ATOM 1019 CG LYS A 164 -3.819 16.916 34.875 1.00 80.68 C ANISOU 1019 CG LYS A 164 12211 11501 6942 98 -651 -1446 C ATOM 1020 CD LYS A 164 -5.036 16.096 35.291 1.00 90.25 C ANISOU 1020 CD LYS A 164 13503 12821 7967 72 -411 -1311 C ATOM 1021 CE LYS A 164 -5.254 16.079 36.787 1.00103.44 C ANISOU 1021 CE LYS A 164 15426 14642 9233 54 -372 -1362 C ATOM 1022 NZ LYS A 164 -6.455 15.289 37.162 1.00112.63 N ANISOU 1022 NZ LYS A 164 16654 15911 10230 19 -116 -1222 N ATOM 1023 N LYS A 165 -3.767 21.517 33.738 1.00 64.97 N ANISOU 1023 N LYS A 165 9927 9228 5533 207 -601 -2168 N ATOM 1024 CA LYS A 165 -4.154 22.708 32.973 1.00 63.57 C ANISOU 1024 CA LYS A 165 9601 8932 5622 241 -512 -2314 C ATOM 1025 C LYS A 165 -2.939 23.317 32.257 1.00 66.65 C ANISOU 1025 C LYS A 165 9872 9179 6272 231 -736 -2358 C ATOM 1026 O LYS A 165 -3.015 23.568 31.053 1.00 64.57 O ANISOU 1026 O LYS A 165 9427 8804 6301 237 -699 -2308 O ATOM 1027 CB LYS A 165 -4.844 23.753 33.875 1.00 67.79 C ANISOU 1027 CB LYS A 165 10247 9506 6006 278 -385 -2556 C ATOM 1028 CG LYS A 165 -5.288 25.023 33.146 1.00 78.30 C ANISOU 1028 CG LYS A 165 11431 10701 7618 321 -295 -2711 C ATOM 1029 CD LYS A 165 -5.607 26.153 34.116 1.00 93.93 C ANISOU 1029 CD LYS A 165 13532 12695 9461 360 -238 -2985 C ATOM 1030 CE LYS A 165 -6.170 27.365 33.412 1.00106.20 C ANISOU 1030 CE LYS A 165 14942 14107 11303 410 -135 -3128 C ATOM 1031 NZ LYS A 165 -6.653 28.392 34.374 1.00116.93 N ANISOU 1031 NZ LYS A 165 16419 15483 12527 460 -43 -3401 N ATOM 1032 N LYS A 166 -1.831 23.551 32.996 1.00 64.24 N ANISOU 1032 N LYS A 166 9669 8881 5859 211 -968 -2448 N ATOM 1033 CA LYS A 166 -0.593 24.118 32.455 1.00 63.25 C ANISOU 1033 CA LYS A 166 9433 8629 5970 190 -1193 -2495 C ATOM 1034 C LYS A 166 -0.009 23.239 31.356 1.00 64.24 C ANISOU 1034 C LYS A 166 9401 8703 6303 170 -1261 -2278 C ATOM 1035 O LYS A 166 0.439 23.765 30.336 1.00 62.65 O ANISOU 1035 O LYS A 166 9032 8377 6395 163 -1300 -2280 O ATOM 1036 CB LYS A 166 0.443 24.370 33.563 1.00 68.08 C ANISOU 1036 CB LYS A 166 10192 9273 6400 169 -1439 -2618 C ATOM 1037 CG LYS A 166 0.191 25.650 34.357 1.00 91.71 C ANISOU 1037 CG LYS A 166 13293 12251 9300 188 -1426 -2892 C ATOM 1038 CD LYS A 166 0.945 26.858 33.791 1.00105.26 C ANISOU 1038 CD LYS A 166 14878 13797 11320 175 -1561 -3038 C ATOM 1039 CE LYS A 166 2.218 27.156 34.550 1.00119.56 C ANISOU 1039 CE LYS A 166 16765 15592 13069 138 -1863 -3145 C ATOM 1040 NZ LYS A 166 2.900 28.371 34.030 1.00128.07 N ANISOU 1040 NZ LYS A 166 17709 16496 14454 115 -1984 -3288 N ATOM 1041 N ASN A 167 -0.036 21.904 31.560 1.00 60.01 N ANISOU 1041 N ASN A 167 8926 8262 5614 161 -1266 -2091 N ATOM 1042 CA ASN A 167 0.437 20.920 30.591 1.00 57.72 C ANISOU 1042 CA ASN A 167 8505 7933 5494 150 -1316 -1885 C ATOM 1043 C ASN A 167 -0.467 20.913 29.356 1.00 59.10 C ANISOU 1043 C ASN A 167 8527 8047 5881 164 -1109 -1808 C ATOM 1044 O ASN A 167 0.050 20.888 28.243 1.00 56.73 O ANISOU 1044 O ASN A 167 8068 7653 5834 158 -1154 -1740 O ATOM 1045 CB ASN A 167 0.543 19.524 31.214 1.00 58.04 C ANISOU 1045 CB ASN A 167 8665 8079 5311 140 -1372 -1715 C ATOM 1046 CG ASN A 167 1.807 19.268 32.009 1.00 77.58 C ANISOU 1046 CG ASN A 167 11226 10575 7675 124 -1650 -1724 C ATOM 1047 OD1 ASN A 167 2.569 20.176 32.362 1.00 74.86 O ANISOU 1047 OD1 ASN A 167 10889 10190 7362 117 -1807 -1884 O ATOM 1048 ND2 ASN A 167 2.053 18.010 32.324 1.00 66.92 N ANISOU 1048 ND2 ASN A 167 9944 9283 6200 119 -1728 -1548 N ATOM 1049 N ALA A 168 -1.806 20.997 29.551 1.00 55.98 N ANISOU 1049 N ALA A 168 8177 7706 5386 183 -884 -1828 N ATOM 1050 CA ALA A 168 -2.788 21.048 28.463 1.00 54.14 C ANISOU 1050 CA ALA A 168 7808 7421 5343 199 -691 -1767 C ATOM 1051 C ALA A 168 -2.578 22.267 27.574 1.00 57.60 C ANISOU 1051 C ALA A 168 8105 7721 6057 210 -704 -1875 C ATOM 1052 O ALA A 168 -2.661 22.128 26.356 1.00 55.35 O ANISOU 1052 O ALA A 168 7677 7361 5990 209 -666 -1775 O ATOM 1053 CB ALA A 168 -4.206 21.029 29.008 1.00 55.65 C ANISOU 1053 CB ALA A 168 8071 7697 5378 217 -462 -1794 C ATOM 1054 N ILE A 169 -2.265 23.445 28.173 1.00 56.12 N ANISOU 1054 N ILE A 169 7966 7497 5858 217 -768 -2076 N ATOM 1055 CA ILE A 169 -1.991 24.685 27.430 1.00 55.50 C ANISOU 1055 CA ILE A 169 7768 7275 6044 220 -798 -2186 C ATOM 1056 C ILE A 169 -0.715 24.518 26.598 1.00 59.55 C ANISOU 1056 C ILE A 169 8163 7706 6756 184 -971 -2097 C ATOM 1057 O ILE A 169 -0.718 24.849 25.409 1.00 57.11 O ANISOU 1057 O ILE A 169 7711 7298 6691 180 -930 -2041 O ATOM 1058 CB ILE A 169 -1.959 25.946 28.340 1.00 60.19 C ANISOU 1058 CB ILE A 169 8453 7841 6576 234 -834 -2431 C ATOM 1059 CG1 ILE A 169 -3.333 26.200 28.986 1.00 61.28 C ANISOU 1059 CG1 ILE A 169 8676 8048 6560 281 -620 -2527 C ATOM 1060 CG2 ILE A 169 -1.487 27.194 27.564 1.00 60.46 C ANISOU 1060 CG2 ILE A 169 8362 7706 6905 226 -902 -2528 C ATOM 1061 CD1 ILE A 169 -3.284 26.984 30.303 1.00 67.09 C ANISOU 1061 CD1 ILE A 169 9573 8821 7096 297 -654 -2759 C ATOM 1062 N CYS A 170 0.354 23.976 27.220 1.00 57.99 N ANISOU 1062 N CYS A 170 8027 7557 6451 159 -1158 -2076 N ATOM 1063 CA CYS A 170 1.634 23.734 26.562 1.00 57.83 C ANISOU 1063 CA CYS A 170 7891 7473 6609 127 -1325 -1997 C ATOM 1064 C CYS A 170 1.470 22.747 25.397 1.00 56.01 C ANISOU 1064 C CYS A 170 7548 7236 6497 131 -1241 -1795 C ATOM 1065 O CYS A 170 1.911 23.042 24.288 1.00 53.72 O ANISOU 1065 O CYS A 170 7113 6852 6448 117 -1247 -1753 O ATOM 1066 CB CYS A 170 2.684 23.265 27.566 1.00 61.20 C ANISOU 1066 CB CYS A 170 8412 7963 6879 110 -1541 -2012 C ATOM 1067 SG CYS A 170 4.230 22.694 26.809 1.00 65.38 S ANISOU 1067 SG CYS A 170 8784 8433 7623 82 -1737 -1891 S ATOM 1068 N ILE A 171 0.792 21.607 25.645 1.00 50.16 N ANISOU 1068 N ILE A 171 6882 6593 5585 148 -1155 -1674 N ATOM 1069 CA ILE A 171 0.518 20.573 24.648 1.00 46.92 C ANISOU 1069 CA ILE A 171 6389 6182 5258 153 -1075 -1492 C ATOM 1070 C ILE A 171 -0.287 21.162 23.479 1.00 47.36 C ANISOU 1070 C ILE A 171 6331 6160 5505 162 -916 -1484 C ATOM 1071 O ILE A 171 0.088 20.941 22.322 1.00 44.76 O ANISOU 1071 O ILE A 171 5880 5767 5359 155 -919 -1393 O ATOM 1072 CB ILE A 171 -0.101 19.297 25.305 1.00 50.07 C ANISOU 1072 CB ILE A 171 6906 6693 5426 161 -1022 -1376 C ATOM 1073 CG1 ILE A 171 0.981 18.530 26.113 1.00 51.28 C ANISOU 1073 CG1 ILE A 171 7137 6895 5452 151 -1223 -1330 C ATOM 1074 CG2 ILE A 171 -0.773 18.374 24.279 1.00 48.13 C ANISOU 1074 CG2 ILE A 171 6584 6437 5267 167 -896 -1213 C ATOM 1075 CD1 ILE A 171 0.458 17.640 27.244 1.00 56.89 C ANISOU 1075 CD1 ILE A 171 8024 7724 5869 151 -1204 -1269 C ATOM 1076 N SER A 172 -1.325 21.982 23.791 1.00 43.31 N ANISOU 1076 N SER A 172 5856 5646 4954 181 -787 -1591 N ATOM 1077 CA SER A 172 -2.171 22.667 22.809 1.00 41.69 C ANISOU 1077 CA SER A 172 5553 5361 4926 196 -650 -1597 C ATOM 1078 C SER A 172 -1.354 23.538 21.863 1.00 46.71 C ANISOU 1078 C SER A 172 6069 5871 5809 177 -727 -1622 C ATOM 1079 O SER A 172 -1.584 23.498 20.650 1.00 46.26 O ANISOU 1079 O SER A 172 5910 5754 5913 175 -665 -1528 O ATOM 1080 CB SER A 172 -3.237 23.517 23.500 1.00 43.68 C ANISOU 1080 CB SER A 172 5867 5626 5104 227 -528 -1738 C ATOM 1081 OG SER A 172 -4.147 22.699 24.213 1.00 49.36 O ANISOU 1081 OG SER A 172 6678 6463 5612 240 -416 -1696 O ATOM 1082 N VAL A 173 -0.404 24.317 22.416 1.00 44.36 N ANISOU 1082 N VAL A 173 5787 5531 5536 156 -863 -1747 N ATOM 1083 CA VAL A 173 0.483 25.192 21.649 1.00 44.58 C ANISOU 1083 CA VAL A 173 5703 5437 5800 124 -946 -1775 C ATOM 1084 C VAL A 173 1.321 24.331 20.688 1.00 47.30 C ANISOU 1084 C VAL A 173 5947 5777 6250 101 -994 -1617 C ATOM 1085 O VAL A 173 1.325 24.601 19.484 1.00 45.16 O ANISOU 1085 O VAL A 173 5570 5428 6161 89 -938 -1547 O ATOM 1086 CB VAL A 173 1.332 26.121 22.563 1.00 50.14 C ANISOU 1086 CB VAL A 173 6448 6102 6501 100 -1098 -1945 C ATOM 1087 CG1 VAL A 173 2.438 26.826 21.782 1.00 49.91 C ANISOU 1087 CG1 VAL A 173 6288 5951 6724 51 -1199 -1946 C ATOM 1088 CG2 VAL A 173 0.446 27.146 23.262 1.00 51.31 C ANISOU 1088 CG2 VAL A 173 6678 6226 6590 129 -1028 -2118 C ATOM 1089 N LEU A 174 1.957 23.262 21.217 1.00 44.47 N ANISOU 1089 N LEU A 174 5629 5502 5767 100 -1089 -1557 N ATOM 1090 CA LEU A 174 2.765 22.323 20.432 1.00 43.81 C ANISOU 1090 CA LEU A 174 5456 5420 5770 91 -1136 -1419 C ATOM 1091 C LEU A 174 1.941 21.711 19.299 1.00 44.44 C ANISOU 1091 C LEU A 174 5491 5499 5897 109 -985 -1288 C ATOM 1092 O LEU A 174 2.408 21.700 18.163 1.00 42.80 O ANISOU 1092 O LEU A 174 5174 5234 5854 95 -970 -1216 O ATOM 1093 CB LEU A 174 3.387 21.224 21.318 1.00 45.12 C ANISOU 1093 CB LEU A 174 5692 5674 5777 99 -1262 -1378 C ATOM 1094 CG LEU A 174 4.321 21.694 22.455 1.00 53.45 C ANISOU 1094 CG LEU A 174 6797 6738 6774 81 -1449 -1498 C ATOM 1095 CD1 LEU A 174 4.703 20.533 23.368 1.00 54.91 C ANISOU 1095 CD1 LEU A 174 7078 7017 6769 97 -1565 -1438 C ATOM 1096 CD2 LEU A 174 5.577 22.418 21.922 1.00 56.77 C ANISOU 1096 CD2 LEU A 174 7073 7064 7432 42 -1564 -1539 C ATOM 1097 N VAL A 175 0.689 21.280 19.598 1.00 39.52 N ANISOU 1097 N VAL A 175 4949 4934 5132 136 -870 -1262 N ATOM 1098 CA VAL A 175 -0.235 20.708 18.619 1.00 36.99 C ANISOU 1098 CA VAL A 175 4594 4613 4847 151 -737 -1149 C ATOM 1099 C VAL A 175 -0.473 21.701 17.471 1.00 39.33 C ANISOU 1099 C VAL A 175 4797 4810 5338 143 -670 -1157 C ATOM 1100 O VAL A 175 -0.315 21.324 16.311 1.00 36.65 O ANISOU 1100 O VAL A 175 4384 4438 5103 137 -641 -1056 O ATOM 1101 CB VAL A 175 -1.556 20.169 19.255 1.00 40.45 C ANISOU 1101 CB VAL A 175 5126 5129 5112 173 -627 -1132 C ATOM 1102 CG1 VAL A 175 -2.584 19.811 18.184 1.00 38.62 C ANISOU 1102 CG1 VAL A 175 4841 4877 4955 184 -498 -1036 C ATOM 1103 CG2 VAL A 175 -1.285 18.961 20.152 1.00 40.58 C ANISOU 1103 CG2 VAL A 175 5234 5239 4946 174 -689 -1070 C ATOM 1104 N TRP A 176 -0.787 22.967 17.795 1.00 38.71 N ANISOU 1104 N TRP A 176 4726 4677 5306 142 -654 -1278 N ATOM 1105 CA TRP A 176 -0.989 24.008 16.789 1.00 39.86 C ANISOU 1105 CA TRP A 176 4792 4713 5641 133 -607 -1285 C ATOM 1106 C TRP A 176 0.272 24.213 15.962 1.00 42.03 C ANISOU 1106 C TRP A 176 4973 4922 6073 92 -682 -1240 C ATOM 1107 O TRP A 176 0.173 24.303 14.742 1.00 40.84 O ANISOU 1107 O TRP A 176 4757 4720 6042 82 -625 -1152 O ATOM 1108 CB TRP A 176 -1.452 25.336 17.413 1.00 41.17 C ANISOU 1108 CB TRP A 176 4987 4818 5838 144 -596 -1438 C ATOM 1109 CG TRP A 176 -2.908 25.382 17.778 1.00 43.39 C ANISOU 1109 CG TRP A 176 5317 5132 6038 190 -473 -1471 C ATOM 1110 CD1 TRP A 176 -3.435 25.469 19.033 1.00 47.40 C ANISOU 1110 CD1 TRP A 176 5917 5705 6389 216 -444 -1584 C ATOM 1111 CD2 TRP A 176 -4.023 25.369 16.874 1.00 42.94 C ANISOU 1111 CD2 TRP A 176 5211 5045 6060 214 -361 -1394 C ATOM 1112 NE1 TRP A 176 -4.808 25.488 18.969 1.00 46.89 N ANISOU 1112 NE1 TRP A 176 5851 5655 6310 256 -306 -1581 N ATOM 1113 CE2 TRP A 176 -5.197 25.434 17.657 1.00 47.41 C ANISOU 1113 CE2 TRP A 176 5827 5660 6528 256 -263 -1465 C ATOM 1114 CE3 TRP A 176 -4.146 25.282 15.474 1.00 43.74 C ANISOU 1114 CE3 TRP A 176 5234 5087 6297 204 -335 -1270 C ATOM 1115 CZ2 TRP A 176 -6.475 25.447 17.089 1.00 46.96 C ANISOU 1115 CZ2 TRP A 176 5725 5585 6532 289 -150 -1419 C ATOM 1116 CZ3 TRP A 176 -5.416 25.277 14.913 1.00 45.19 C ANISOU 1116 CZ3 TRP A 176 5392 5256 6523 236 -238 -1222 C ATOM 1117 CH2 TRP A 176 -6.561 25.367 15.715 1.00 46.65 C ANISOU 1117 CH2 TRP A 176 5608 5481 6634 278 -151 -1296 C ATOM 1118 N LEU A 177 1.453 24.207 16.609 1.00 38.87 N ANISOU 1118 N LEU A 177 4568 4534 5669 67 -807 -1293 N ATOM 1119 CA LEU A 177 2.741 24.340 15.916 1.00 38.66 C ANISOU 1119 CA LEU A 177 4435 4454 5801 25 -876 -1253 C ATOM 1120 C LEU A 177 3.006 23.185 14.963 1.00 41.23 C ANISOU 1120 C LEU A 177 4709 4819 6137 33 -835 -1110 C ATOM 1121 O LEU A 177 3.308 23.436 13.796 1.00 40.09 O ANISOU 1121 O LEU A 177 4483 4619 6132 9 -787 -1043 O ATOM 1122 CB LEU A 177 3.918 24.581 16.881 1.00 40.10 C ANISOU 1122 CB LEU A 177 4611 4638 5989 -2 -1034 -1349 C ATOM 1123 CG LEU A 177 3.919 25.934 17.622 1.00 46.50 C ANISOU 1123 CG LEU A 177 5451 5376 6840 -24 -1093 -1507 C ATOM 1124 CD1 LEU A 177 5.008 25.987 18.678 1.00 47.74 C ANISOU 1124 CD1 LEU A 177 5621 5553 6965 -47 -1270 -1602 C ATOM 1125 CD2 LEU A 177 4.051 27.113 16.658 1.00 49.69 C ANISOU 1125 CD2 LEU A 177 5763 5647 7468 -65 -1055 -1507 C ATOM 1126 N ILE A 178 2.805 21.929 15.428 1.00 37.90 N ANISOU 1126 N ILE A 178 4346 4490 5563 66 -846 -1062 N ATOM 1127 CA ILE A 178 2.956 20.714 14.623 1.00 37.17 C ANISOU 1127 CA ILE A 178 4222 4432 5468 83 -811 -938 C ATOM 1128 C ILE A 178 2.023 20.764 13.389 1.00 37.98 C ANISOU 1128 C ILE A 178 4310 4504 5618 89 -678 -861 C ATOM 1129 O ILE A 178 2.491 20.567 12.262 1.00 36.40 O ANISOU 1129 O ILE A 178 4040 4277 5515 79 -643 -789 O ATOM 1130 CB ILE A 178 2.732 19.429 15.485 1.00 41.38 C ANISOU 1130 CB ILE A 178 4842 5056 5826 117 -851 -904 C ATOM 1131 CG1 ILE A 178 3.882 19.215 16.504 1.00 43.75 C ANISOU 1131 CG1 ILE A 178 5145 5384 6095 113 -1009 -952 C ATOM 1132 CG2 ILE A 178 2.532 18.181 14.611 1.00 41.04 C ANISOU 1132 CG2 ILE A 178 4783 5034 5776 141 -793 -782 C ATOM 1133 CD1 ILE A 178 3.481 18.451 17.792 1.00 52.06 C ANISOU 1133 CD1 ILE A 178 6325 6519 6936 136 -1064 -955 C ATOM 1134 N VAL A 179 0.723 21.063 13.609 1.00 33.12 N ANISOU 1134 N VAL A 179 3756 3891 4935 106 -606 -881 N ATOM 1135 CA VAL A 179 -0.274 21.137 12.539 1.00 32.04 C ANISOU 1135 CA VAL A 179 3609 3724 4840 115 -501 -813 C ATOM 1136 C VAL A 179 0.102 22.202 11.490 1.00 37.26 C ANISOU 1136 C VAL A 179 4199 4292 5666 83 -481 -801 C ATOM 1137 O VAL A 179 0.239 21.859 10.324 1.00 36.22 O ANISOU 1137 O VAL A 179 4032 4147 5585 76 -438 -710 O ATOM 1138 CB VAL A 179 -1.727 21.252 13.086 1.00 36.01 C ANISOU 1138 CB VAL A 179 4175 4250 5257 142 -434 -842 C ATOM 1139 CG1 VAL A 179 -2.735 21.519 11.970 1.00 34.80 C ANISOU 1139 CG1 VAL A 179 3995 4049 5178 150 -350 -781 C ATOM 1140 CG2 VAL A 179 -2.113 19.991 13.857 1.00 35.75 C ANISOU 1140 CG2 VAL A 179 4209 4311 5063 162 -431 -810 C ATOM 1141 N VAL A 180 0.334 23.457 11.916 1.00 36.98 N ANISOU 1141 N VAL A 180 4149 4191 5712 62 -516 -892 N ATOM 1142 CA VAL A 180 0.721 24.581 11.043 1.00 37.01 C ANISOU 1142 CA VAL A 180 4089 4090 5882 23 -504 -879 C ATOM 1143 C VAL A 180 1.943 24.235 10.168 1.00 38.89 C ANISOU 1143 C VAL A 180 4250 4325 6202 -14 -512 -803 C ATOM 1144 O VAL A 180 1.876 24.377 8.946 1.00 37.62 O ANISOU 1144 O VAL A 180 4060 4125 6108 -32 -447 -714 O ATOM 1145 CB VAL A 180 0.839 25.917 11.825 1.00 41.87 C ANISOU 1145 CB VAL A 180 4707 4628 6575 4 -557 -1005 C ATOM 1146 CG1 VAL A 180 1.598 26.983 11.038 1.00 42.28 C ANISOU 1146 CG1 VAL A 180 4682 4567 6814 -53 -569 -985 C ATOM 1147 CG2 VAL A 180 -0.544 26.429 12.221 1.00 41.90 C ANISOU 1147 CG2 VAL A 180 4767 4610 6541 47 -506 -1063 C ATOM 1148 N VAL A 181 2.995 23.685 10.778 1.00 35.66 N ANISOU 1148 N VAL A 181 3811 3962 5775 -21 -586 -832 N ATOM 1149 CA VAL A 181 4.200 23.260 10.068 1.00 35.11 C ANISOU 1149 CA VAL A 181 3652 3898 5790 -47 -589 -773 C ATOM 1150 C VAL A 181 3.901 22.134 9.076 1.00 38.45 C ANISOU 1150 C VAL A 181 4086 4372 6153 -17 -508 -667 C ATOM 1151 O VAL A 181 4.185 22.293 7.888 1.00 38.25 O ANISOU 1151 O VAL A 181 4014 4317 6202 -42 -437 -596 O ATOM 1152 CB VAL A 181 5.370 22.929 11.033 1.00 39.51 C ANISOU 1152 CB VAL A 181 4165 4489 6360 -54 -707 -837 C ATOM 1153 CG1 VAL A 181 6.527 22.250 10.304 1.00 39.35 C ANISOU 1153 CG1 VAL A 181 4041 4486 6424 -63 -697 -773 C ATOM 1154 CG2 VAL A 181 5.851 24.182 11.756 1.00 40.21 C ANISOU 1154 CG2 VAL A 181 4226 4507 6544 -99 -792 -942 C ATOM 1155 N ALA A 182 3.289 21.027 9.547 1.00 34.38 N ANISOU 1155 N ALA A 182 3638 3927 5497 31 -516 -656 N ATOM 1156 CA ALA A 182 2.985 19.875 8.693 1.00 33.18 C ANISOU 1156 CA ALA A 182 3504 3816 5287 61 -455 -569 C ATOM 1157 C ALA A 182 1.987 20.162 7.567 1.00 35.10 C ANISOU 1157 C ALA A 182 3778 4028 5530 58 -363 -505 C ATOM 1158 O ALA A 182 2.062 19.524 6.514 1.00 33.63 O ANISOU 1158 O ALA A 182 3587 3853 5336 65 -309 -435 O ATOM 1159 CB ALA A 182 2.531 18.692 9.530 1.00 33.48 C ANISOU 1159 CB ALA A 182 3609 3921 5191 105 -494 -569 C ATOM 1160 N ILE A 183 1.081 21.132 7.780 1.00 31.34 N ANISOU 1160 N ILE A 183 3334 3507 5065 51 -352 -533 N ATOM 1161 CA ILE A 183 0.054 21.520 6.816 1.00 30.35 C ANISOU 1161 CA ILE A 183 3237 3343 4952 51 -290 -474 C ATOM 1162 C ILE A 183 0.447 22.727 5.929 1.00 33.92 C ANISOU 1162 C ILE A 183 3648 3710 5529 6 -263 -443 C ATOM 1163 O ILE A 183 -0.180 22.946 4.890 1.00 33.24 O ANISOU 1163 O ILE A 183 3586 3593 5453 3 -217 -370 O ATOM 1164 CB ILE A 183 -1.360 21.585 7.495 1.00 33.68 C ANISOU 1164 CB ILE A 183 3715 3773 5309 84 -286 -508 C ATOM 1165 CG1 ILE A 183 -1.756 20.207 8.116 1.00 33.35 C ANISOU 1165 CG1 ILE A 183 3717 3817 5139 118 -293 -501 C ATOM 1166 CG2 ILE A 183 -2.478 22.128 6.568 1.00 34.09 C ANISOU 1166 CG2 ILE A 183 3781 3770 5400 89 -242 -455 C ATOM 1167 CD1 ILE A 183 -1.615 18.970 7.212 1.00 37.10 C ANISOU 1167 CD1 ILE A 183 4199 4326 5572 127 -273 -418 C ATOM 1168 N SER A 184 1.550 23.431 6.271 1.00 30.54 N ANISOU 1168 N SER A 184 3158 3246 5199 -34 -296 -487 N ATOM 1169 CA SER A 184 2.059 24.559 5.488 1.00 31.29 C ANISOU 1169 CA SER A 184 3208 3255 5427 -90 -270 -449 C ATOM 1170 C SER A 184 2.277 24.245 3.978 1.00 35.29 C ANISOU 1170 C SER A 184 3710 3768 5930 -110 -186 -331 C ATOM 1171 O SER A 184 1.987 25.134 3.180 1.00 34.67 O ANISOU 1171 O SER A 184 3644 3616 5912 -142 -154 -269 O ATOM 1172 CB SER A 184 3.300 25.174 6.132 1.00 34.94 C ANISOU 1172 CB SER A 184 3591 3683 6001 -136 -325 -516 C ATOM 1173 OG SER A 184 4.434 24.325 6.100 1.00 43.46 O ANISOU 1173 OG SER A 184 4607 4826 7080 -140 -330 -509 O ATOM 1174 N PRO A 185 2.705 23.017 3.536 1.00 30.92 N ANISOU 1174 N PRO A 185 3153 3295 5302 -88 -150 -296 N ATOM 1175 CA PRO A 185 2.837 22.770 2.085 1.00 30.77 C ANISOU 1175 CA PRO A 185 3147 3284 5260 -104 -63 -197 C ATOM 1176 C PRO A 185 1.554 22.961 1.276 1.00 33.72 C ANISOU 1176 C PRO A 185 3609 3632 5571 -92 -43 -128 C ATOM 1177 O PRO A 185 1.654 23.193 0.073 1.00 34.74 O ANISOU 1177 O PRO A 185 3761 3746 5694 -121 19 -41 O ATOM 1178 CB PRO A 185 3.341 21.325 2.015 1.00 32.16 C ANISOU 1178 CB PRO A 185 3312 3547 5359 -64 -45 -206 C ATOM 1179 CG PRO A 185 4.059 21.132 3.311 1.00 36.54 C ANISOU 1179 CG PRO A 185 3806 4122 5957 -53 -121 -292 C ATOM 1180 CD PRO A 185 3.168 21.836 4.296 1.00 31.71 C ANISOU 1180 CD PRO A 185 3236 3473 5339 -48 -189 -346 C ATOM 1181 N ILE A 186 0.359 22.898 1.923 1.00 29.38 N ANISOU 1181 N ILE A 186 3107 3078 4976 -51 -94 -164 N ATOM 1182 CA ILE A 186 -0.949 23.154 1.283 1.00 28.91 C ANISOU 1182 CA ILE A 186 3114 2986 4884 -35 -96 -107 C ATOM 1183 C ILE A 186 -0.940 24.570 0.675 1.00 32.09 C ANISOU 1183 C ILE A 186 3512 3288 5391 -80 -89 -52 C ATOM 1184 O ILE A 186 -1.458 24.765 -0.422 1.00 31.78 O ANISOU 1184 O ILE A 186 3525 3223 5328 -88 -72 41 O ATOM 1185 CB ILE A 186 -2.160 22.903 2.251 1.00 30.92 C ANISOU 1185 CB ILE A 186 3392 3254 5104 15 -143 -167 C ATOM 1186 CG1 ILE A 186 -2.291 21.407 2.683 1.00 29.09 C ANISOU 1186 CG1 ILE A 186 3178 3113 4760 52 -148 -192 C ATOM 1187 CG2 ILE A 186 -3.495 23.479 1.724 1.00 30.41 C ANISOU 1187 CG2 ILE A 186 3364 3131 5058 30 -158 -120 C ATOM 1188 CD1 ILE A 186 -2.620 20.352 1.612 1.00 29.28 C ANISOU 1188 CD1 ILE A 186 3251 3177 4696 66 -126 -123 C ATOM 1189 N LEU A 187 -0.233 25.517 1.339 1.00 29.50 N ANISOU 1189 N LEU A 187 3127 2901 5180 -114 -108 -104 N ATOM 1190 CA LEU A 187 -0.040 26.895 0.887 1.00 28.96 C ANISOU 1190 CA LEU A 187 3045 2720 5239 -167 -106 -56 C ATOM 1191 C LEU A 187 0.772 26.955 -0.407 1.00 34.36 C ANISOU 1191 C LEU A 187 3730 3405 5923 -225 -31 59 C ATOM 1192 O LEU A 187 0.602 27.903 -1.172 1.00 34.89 O ANISOU 1192 O LEU A 187 3821 3384 6050 -265 -21 148 O ATOM 1193 CB LEU A 187 0.570 27.782 1.989 1.00 28.96 C ANISOU 1193 CB LEU A 187 2981 2655 5366 -193 -153 -155 C ATOM 1194 CG LEU A 187 -0.316 27.991 3.235 1.00 32.63 C ANISOU 1194 CG LEU A 187 3461 3106 5832 -139 -217 -274 C ATOM 1195 CD1 LEU A 187 0.509 28.448 4.430 1.00 32.13 C ANISOU 1195 CD1 LEU A 187 3344 3021 5842 -160 -267 -394 C ATOM 1196 CD2 LEU A 187 -1.496 28.960 2.950 1.00 32.65 C ANISOU 1196 CD2 LEU A 187 3499 3002 5905 -119 -238 -250 C ATOM 1197 N PHE A 188 1.627 25.932 -0.673 1.00 30.76 N ANISOU 1197 N PHE A 188 3249 3045 5396 -227 26 62 N ATOM 1198 CA PHE A 188 2.359 25.844 -1.932 1.00 31.48 C ANISOU 1198 CA PHE A 188 3344 3157 5462 -274 121 163 C ATOM 1199 C PHE A 188 1.491 25.165 -3.007 1.00 35.51 C ANISOU 1199 C PHE A 188 3961 3711 5819 -241 146 239 C ATOM 1200 O PHE A 188 1.298 25.739 -4.076 1.00 36.62 O ANISOU 1200 O PHE A 188 4160 3812 5941 -278 178 348 O ATOM 1201 CB PHE A 188 3.720 25.126 -1.785 1.00 33.89 C ANISOU 1201 CB PHE A 188 3561 3535 5781 -286 180 122 C ATOM 1202 CG PHE A 188 4.285 24.696 -3.127 1.00 36.43 C ANISOU 1202 CG PHE A 188 3902 3910 6032 -312 300 211 C ATOM 1203 CD1 PHE A 188 4.959 25.603 -3.941 1.00 40.98 C ANISOU 1203 CD1 PHE A 188 4453 4438 6680 -393 383 303 C ATOM 1204 CD2 PHE A 188 4.088 23.403 -3.603 1.00 37.42 C ANISOU 1204 CD2 PHE A 188 4079 4126 6012 -256 335 203 C ATOM 1205 CE1 PHE A 188 5.443 25.218 -5.197 1.00 42.36 C ANISOU 1205 CE1 PHE A 188 4658 4671 6768 -417 511 386 C ATOM 1206 CE2 PHE A 188 4.559 23.025 -4.866 1.00 40.90 C ANISOU 1206 CE2 PHE A 188 4552 4617 6371 -275 454 272 C ATOM 1207 CZ PHE A 188 5.240 23.930 -5.649 1.00 40.15 C ANISOU 1207 CZ PHE A 188 4434 4487 6333 -354 547 362 C ATOM 1208 N TYR A 189 0.999 23.938 -2.728 1.00 31.93 N ANISOU 1208 N TYR A 189 3536 3338 5258 -177 122 185 N ATOM 1209 CA TYR A 189 0.211 23.099 -3.646 1.00 31.01 C ANISOU 1209 CA TYR A 189 3515 3269 4997 -143 129 233 C ATOM 1210 C TYR A 189 -1.093 23.706 -4.133 1.00 35.83 C ANISOU 1210 C TYR A 189 4203 3818 5592 -136 68 300 C ATOM 1211 O TYR A 189 -1.376 23.681 -5.334 1.00 34.86 O ANISOU 1211 O TYR A 189 4162 3698 5384 -151 88 392 O ATOM 1212 CB TYR A 189 -0.076 21.717 -3.027 1.00 29.98 C ANISOU 1212 CB TYR A 189 3387 3215 4789 -80 99 153 C ATOM 1213 CG TYR A 189 1.144 20.841 -2.831 1.00 29.39 C ANISOU 1213 CG TYR A 189 3252 3206 4707 -72 154 102 C ATOM 1214 CD1 TYR A 189 1.839 20.323 -3.922 1.00 30.73 C ANISOU 1214 CD1 TYR A 189 3442 3423 4813 -81 247 140 C ATOM 1215 CD2 TYR A 189 1.540 20.443 -1.558 1.00 29.53 C ANISOU 1215 CD2 TYR A 189 3201 3244 4775 -47 109 13 C ATOM 1216 CE1 TYR A 189 2.950 19.495 -3.746 1.00 30.51 C ANISOU 1216 CE1 TYR A 189 3345 3449 4797 -63 298 86 C ATOM 1217 CE2 TYR A 189 2.634 19.603 -1.370 1.00 31.02 C ANISOU 1217 CE2 TYR A 189 3330 3486 4972 -30 142 -30 C ATOM 1218 CZ TYR A 189 3.338 19.135 -2.465 1.00 33.71 C ANISOU 1218 CZ TYR A 189 3671 3863 5273 -36 238 3 C ATOM 1219 OH TYR A 189 4.411 18.324 -2.258 1.00 35.03 O ANISOU 1219 OH TYR A 189 3764 4076 5471 -10 270 -46 O ATOM 1220 N SER A 190 -1.908 24.203 -3.207 1.00 34.12 N ANISOU 1220 N SER A 190 3963 3548 5452 -110 -9 251 N ATOM 1221 CA SER A 190 -3.204 24.777 -3.559 1.00 35.33 C ANISOU 1221 CA SER A 190 4168 3636 5621 -92 -76 303 C ATOM 1222 C SER A 190 -3.055 26.149 -4.232 1.00 41.59 C ANISOU 1222 C SER A 190 4977 4325 6499 -143 -76 399 C ATOM 1223 O SER A 190 -1.984 26.755 -4.203 1.00 41.95 O ANISOU 1223 O SER A 190 4980 4341 6617 -197 -24 410 O ATOM 1224 CB SER A 190 -4.111 24.845 -2.337 1.00 39.15 C ANISOU 1224 CB SER A 190 4610 4099 6166 -43 -140 211 C ATOM 1225 OG SER A 190 -3.674 25.842 -1.427 1.00 50.76 O ANISOU 1225 OG SER A 190 6017 5506 7763 -58 -146 149 O ATOM 1226 N GLY A 191 -4.114 26.590 -4.882 1.00 39.46 N ANISOU 1226 N GLY A 191 4768 3997 6226 -130 -138 477 N ATOM 1227 CA GLY A 191 -4.121 27.865 -5.580 1.00 40.55 C ANISOU 1227 CA GLY A 191 4938 4025 6444 -174 -156 587 C ATOM 1228 C GLY A 191 -5.123 27.884 -6.709 1.00 44.58 C ANISOU 1228 C GLY A 191 5546 4513 6878 -159 -221 700 C ATOM 1229 O GLY A 191 -5.832 26.898 -6.950 1.00 41.78 O ANISOU 1229 O GLY A 191 5230 4229 6415 -117 -256 684 O ATOM 1230 N THR A 192 -5.187 29.023 -7.393 1.00 43.66 N ANISOU 1230 N THR A 192 5472 4289 6827 -197 -250 818 N ATOM 1231 CA THR A 192 -6.105 29.259 -8.503 1.00 44.43 C ANISOU 1231 CA THR A 192 5670 4346 6866 -189 -335 946 C ATOM 1232 C THR A 192 -5.513 28.849 -9.846 1.00 50.77 C ANISOU 1232 C THR A 192 6588 5219 7482 -243 -272 1062 C ATOM 1233 O THR A 192 -4.300 28.937 -10.054 1.00 50.09 O ANISOU 1233 O THR A 192 6497 5165 7371 -305 -153 1085 O ATOM 1234 CB THR A 192 -6.566 30.720 -8.529 1.00 49.25 C ANISOU 1234 CB THR A 192 6275 4791 7649 -195 -415 1021 C ATOM 1235 OG1 THR A 192 -5.425 31.570 -8.567 1.00 52.36 O ANISOU 1235 OG1 THR A 192 6651 5122 8120 -272 -339 1068 O ATOM 1236 CG2 THR A 192 -7.467 31.078 -7.360 1.00 46.18 C ANISOU 1236 CG2 THR A 192 5790 4332 7426 -123 -491 904 C ATOM 1237 N GLY A 193 -6.396 28.431 -10.746 1.00 49.95 N ANISOU 1237 N GLY A 193 6585 5139 7254 -218 -353 1131 N ATOM 1238 CA GLY A 193 -6.067 28.045 -12.111 1.00 51.77 C ANISOU 1238 CA GLY A 193 6954 5436 7280 -259 -315 1241 C ATOM 1239 C GLY A 193 -7.102 28.557 -13.090 1.00 59.28 C ANISOU 1239 C GLY A 193 8017 6318 8187 -252 -455 1377 C ATOM 1240 O GLY A 193 -8.299 28.552 -12.787 1.00 58.96 O ANISOU 1240 O GLY A 193 7947 6230 8224 -191 -593 1349 O ATOM 1241 N VAL A 194 -6.650 29.013 -14.265 1.00 58.97 N ANISOU 1241 N VAL A 194 8106 6272 8029 -316 -422 1531 N ATOM 1242 CA VAL A 194 -7.541 29.528 -15.304 1.00 61.01 C ANISOU 1242 CA VAL A 194 8493 6464 8222 -317 -564 1684 C ATOM 1243 C VAL A 194 -7.945 28.383 -16.231 1.00 67.53 C ANISOU 1243 C VAL A 194 9449 7408 8801 -299 -604 1683 C ATOM 1244 O VAL A 194 -7.083 27.744 -16.833 1.00 68.03 O ANISOU 1244 O VAL A 194 9590 7584 8676 -338 -472 1681 O ATOM 1245 CB VAL A 194 -6.943 30.732 -16.084 1.00 66.81 C ANISOU 1245 CB VAL A 194 9314 7114 8958 -400 -526 1872 C ATOM 1246 CG1 VAL A 194 -7.972 31.329 -17.040 1.00 68.18 C ANISOU 1246 CG1 VAL A 194 9620 7202 9085 -392 -704 2037 C ATOM 1247 CG2 VAL A 194 -6.421 31.807 -15.133 1.00 66.62 C ANISOU 1247 CG2 VAL A 194 9157 6966 9189 -425 -482 1855 C ATOM 1248 N ARG A 195 -9.255 28.123 -16.334 1.00 65.43 N ANISOU 1248 N ARG A 195 9199 7115 8546 -239 -785 1676 N ATOM 1249 CA ARG A 195 -9.820 27.082 -17.197 1.00 66.28 C ANISOU 1249 CA ARG A 195 9428 7314 8441 -220 -865 1669 C ATOM 1250 C ARG A 195 -9.810 27.554 -18.665 1.00 75.17 C ANISOU 1250 C ARG A 195 10757 8432 9372 -271 -918 1854 C ATOM 1251 O ARG A 195 -9.519 28.728 -18.929 1.00 76.23 O ANISOU 1251 O ARG A 195 10922 8474 9569 -315 -911 1996 O ATOM 1252 CB ARG A 195 -11.255 26.726 -16.756 1.00 63.91 C ANISOU 1252 CB ARG A 195 9055 6974 8255 -145 -1053 1603 C ATOM 1253 CG ARG A 195 -11.344 26.030 -15.407 1.00 68.92 C ANISOU 1253 CG ARG A 195 9517 7641 9029 -99 -999 1423 C ATOM 1254 CD ARG A 195 -12.755 25.548 -15.125 1.00 74.62 C ANISOU 1254 CD ARG A 195 10175 8339 9836 -36 -1167 1368 C ATOM 1255 NE ARG A 195 -12.957 25.183 -13.720 1.00 75.89 N ANISOU 1255 NE ARG A 195 10162 8506 10166 6 -1118 1221 N ATOM 1256 CZ ARG A 195 -13.533 25.968 -12.813 1.00 84.86 C ANISOU 1256 CZ ARG A 195 11165 9549 11530 45 -1154 1196 C ATOM 1257 NH1 ARG A 195 -13.953 27.183 -13.145 1.00 69.33 N ANISOU 1257 NH1 ARG A 195 9208 7462 9674 51 -1247 1306 N ATOM 1258 NH2 ARG A 195 -13.679 25.551 -11.563 1.00 67.13 N ANISOU 1258 NH2 ARG A 195 8780 7326 9400 78 -1095 1061 N ATOM 1259 N LYS A 196 -10.133 26.642 -19.616 1.00 73.88 N ANISOU 1259 N LYS A 196 10740 8362 8969 -266 -976 1854 N ATOM 1260 CA LYS A 196 -10.197 26.956 -21.049 1.00 76.47 C ANISOU 1260 CA LYS A 196 11286 8700 9068 -311 -1039 2021 C ATOM 1261 C LYS A 196 -11.338 27.949 -21.328 1.00 82.43 C ANISOU 1261 C LYS A 196 12066 9314 9939 -291 -1273 2163 C ATOM 1262 O LYS A 196 -11.170 28.853 -22.151 1.00 84.70 O ANISOU 1262 O LYS A 196 12485 9547 10149 -342 -1300 2348 O ATOM 1263 CB LYS A 196 -10.334 25.675 -21.893 1.00 79.51 C ANISOU 1263 CB LYS A 196 11817 9215 9178 -302 -1064 1954 C ATOM 1264 CG LYS A 196 -10.200 25.899 -23.400 1.00 98.13 C ANISOU 1264 CG LYS A 196 14427 11613 11243 -355 -1092 2111 C ATOM 1265 CD LYS A 196 -9.108 25.040 -24.020 1.00107.96 C ANISOU 1265 CD LYS A 196 15787 13010 12222 -391 -880 2049 C ATOM 1266 CE LYS A 196 -9.033 25.229 -25.515 1.00116.85 C ANISOU 1266 CE LYS A 196 17179 14188 13032 -442 -904 2199 C ATOM 1267 NZ LYS A 196 -7.985 24.373 -26.129 1.00124.69 N ANISOU 1267 NZ LYS A 196 18283 15332 13760 -469 -682 2122 N ATOM 1268 N ASN A 197 -12.465 27.816 -20.596 1.00 77.79 N ANISOU 1268 N ASN A 197 11342 8662 9554 -218 -1434 2081 N ATOM 1269 CA ASN A 197 -13.630 28.706 -20.707 1.00 78.64 C ANISOU 1269 CA ASN A 197 11429 8627 9824 -180 -1664 2188 C ATOM 1270 C ASN A 197 -13.431 30.041 -19.948 1.00 81.80 C ANISOU 1270 C ASN A 197 11704 8881 10496 -179 -1629 2243 C ATOM 1271 O ASN A 197 -14.394 30.779 -19.721 1.00 81.85 O ANISOU 1271 O ASN A 197 11637 8753 10708 -129 -1799 2290 O ATOM 1272 CB ASN A 197 -14.924 27.983 -20.283 1.00 80.03 C ANISOU 1272 CB ASN A 197 11500 8799 10107 -104 -1839 2074 C ATOM 1273 CG ASN A 197 -14.846 27.235 -18.973 1.00103.76 C ANISOU 1273 CG ASN A 197 14313 11852 13259 -66 -1724 1872 C ATOM 1274 OD1 ASN A 197 -14.109 26.252 -18.830 1.00 99.34 O ANISOU 1274 OD1 ASN A 197 13766 11412 12565 -86 -1574 1763 O ATOM 1275 ND2 ASN A 197 -15.657 27.643 -18.008 1.00 94.42 N ANISOU 1275 ND2 ASN A 197 12949 10575 12350 -7 -1798 1818 N ATOM 1276 N LYS A 198 -12.162 30.347 -19.588 1.00 77.32 N ANISOU 1276 N LYS A 198 11112 8334 9931 -236 -1410 2233 N ATOM 1277 CA LYS A 198 -11.685 31.538 -18.872 1.00 76.43 C ANISOU 1277 CA LYS A 198 10894 8095 10050 -255 -1338 2269 C ATOM 1278 C LYS A 198 -12.085 31.686 -17.393 1.00 75.98 C ANISOU 1278 C LYS A 198 10614 7972 10283 -187 -1340 2107 C ATOM 1279 O LYS A 198 -11.694 32.671 -16.753 1.00 75.64 O ANISOU 1279 O LYS A 198 10485 7818 10436 -200 -1287 2117 O ATOM 1280 CB LYS A 198 -11.856 32.838 -19.688 1.00 81.40 C ANISOU 1280 CB LYS A 198 11636 8582 10710 -292 -1447 2496 C ATOM 1281 CG LYS A 198 -10.642 33.200 -20.557 1.00 97.52 C ANISOU 1281 CG LYS A 198 13830 10662 12561 -401 -1291 2646 C ATOM 1282 CD LYS A 198 -9.349 33.547 -19.775 1.00106.12 C ANISOU 1282 CD LYS A 198 14806 11748 13766 -459 -1061 2587 C ATOM 1283 CE LYS A 198 -9.387 34.850 -19.000 1.00115.74 C ANISOU 1283 CE LYS A 198 15902 12774 15297 -456 -1097 2618 C ATOM 1284 NZ LYS A 198 -9.811 34.642 -17.588 1.00120.02 N ANISOU 1284 NZ LYS A 198 16239 13291 16071 -373 -1114 2407 N ATOM 1285 N THR A 199 -12.814 30.693 -16.837 1.00 68.79 N ANISOU 1285 N THR A 199 9615 7130 9393 -120 -1389 1956 N ATOM 1286 CA THR A 199 -13.230 30.701 -15.428 1.00 65.65 C ANISOU 1286 CA THR A 199 9015 6692 9234 -56 -1376 1796 C ATOM 1287 C THR A 199 -12.057 30.346 -14.507 1.00 63.60 C ANISOU 1287 C THR A 199 8675 6510 8978 -86 -1164 1666 C ATOM 1288 O THR A 199 -11.055 29.792 -14.970 1.00 63.11 O ANISOU 1288 O THR A 199 8696 6556 8726 -142 -1036 1673 O ATOM 1289 CB THR A 199 -14.477 29.838 -15.191 1.00 73.99 C ANISOU 1289 CB THR A 199 10005 7787 10320 16 -1504 1703 C ATOM 1290 OG1 THR A 199 -14.215 28.503 -15.615 1.00 74.81 O ANISOU 1290 OG1 THR A 199 10188 8042 10192 -6 -1457 1649 O ATOM 1291 CG2 THR A 199 -15.717 30.391 -15.879 1.00 73.35 C ANISOU 1291 CG2 THR A 199 9955 7599 10316 57 -1736 1820 C ATOM 1292 N ILE A 200 -12.172 30.684 -13.212 1.00 55.40 N ANISOU 1292 N ILE A 200 7476 5418 8157 -45 -1129 1544 N ATOM 1293 CA ILE A 200 -11.107 30.449 -12.240 1.00 52.12 C ANISOU 1293 CA ILE A 200 6976 5059 7767 -69 -955 1420 C ATOM 1294 C ILE A 200 -11.440 29.344 -11.242 1.00 53.27 C ANISOU 1294 C ILE A 200 7016 5301 7922 -16 -922 1243 C ATOM 1295 O ILE A 200 -12.385 29.467 -10.465 1.00 53.05 O ANISOU 1295 O ILE A 200 6883 5225 8049 48 -991 1167 O ATOM 1296 CB ILE A 200 -10.656 31.777 -11.555 1.00 54.85 C ANISOU 1296 CB ILE A 200 7246 5268 8327 -84 -921 1424 C ATOM 1297 CG1 ILE A 200 -10.119 32.800 -12.595 1.00 56.15 C ANISOU 1297 CG1 ILE A 200 7526 5340 8468 -156 -930 1617 C ATOM 1298 CG2 ILE A 200 -9.630 31.519 -10.445 1.00 53.41 C ANISOU 1298 CG2 ILE A 200 6967 5143 8185 -103 -768 1280 C ATOM 1299 CD1 ILE A 200 -10.144 34.236 -12.137 1.00 56.62 C ANISOU 1299 CD1 ILE A 200 7527 5215 8772 -157 -971 1653 C ATOM 1300 N THR A 201 -10.635 28.277 -11.250 1.00 47.32 N ANISOU 1300 N THR A 201 6289 4682 7007 -44 -809 1180 N ATOM 1301 CA THR A 201 -10.779 27.178 -10.302 1.00 44.93 C ANISOU 1301 CA THR A 201 5900 4472 6700 -6 -766 1026 C ATOM 1302 C THR A 201 -9.911 27.492 -9.102 1.00 44.69 C ANISOU 1302 C THR A 201 5766 4437 6777 -15 -649 925 C ATOM 1303 O THR A 201 -8.806 28.000 -9.263 1.00 44.73 O ANISOU 1303 O THR A 201 5792 4429 6774 -69 -562 964 O ATOM 1304 CB THR A 201 -10.216 25.849 -10.882 1.00 54.57 C ANISOU 1304 CB THR A 201 7204 5830 7702 -29 -701 1004 C ATOM 1305 OG1 THR A 201 -10.486 25.735 -12.274 1.00 62.19 O ANISOU 1305 OG1 THR A 201 8312 6805 8513 -51 -774 1121 O ATOM 1306 CG2 THR A 201 -10.723 24.628 -10.149 1.00 51.82 C ANISOU 1306 CG2 THR A 201 6790 5557 7343 14 -708 877 C ATOM 1307 N CYS A 202 -10.387 27.147 -7.913 1.00 38.94 N ANISOU 1307 N CYS A 202 4931 3725 6141 34 -647 796 N ATOM 1308 CA CYS A 202 -9.583 27.157 -6.708 1.00 37.90 C ANISOU 1308 CA CYS A 202 4713 3616 6070 30 -547 681 C ATOM 1309 C CYS A 202 -9.289 25.648 -6.527 1.00 43.98 C ANISOU 1309 C CYS A 202 5491 4522 6697 34 -492 609 C ATOM 1310 O CYS A 202 -10.209 24.880 -6.227 1.00 43.37 O ANISOU 1310 O CYS A 202 5387 4482 6609 75 -538 560 O ATOM 1311 CB CYS A 202 -10.339 27.740 -5.518 1.00 37.24 C ANISOU 1311 CB CYS A 202 4522 3464 6162 84 -578 587 C ATOM 1312 SG CYS A 202 -9.502 27.500 -3.924 1.00 39.83 S ANISOU 1312 SG CYS A 202 4762 3845 6525 86 -474 425 S ATOM 1313 N TYR A 203 -8.046 25.216 -6.820 1.00 43.21 N ANISOU 1313 N TYR A 203 5431 4492 6496 -9 -397 613 N ATOM 1314 CA TYR A 203 -7.643 23.805 -6.746 1.00 43.51 C ANISOU 1314 CA TYR A 203 5481 4645 6405 -3 -346 550 C ATOM 1315 C TYR A 203 -7.728 23.215 -5.340 1.00 48.48 C ANISOU 1315 C TYR A 203 6019 5313 7088 32 -327 424 C ATOM 1316 O TYR A 203 -7.022 23.674 -4.430 1.00 47.61 O ANISOU 1316 O TYR A 203 5843 5190 7056 24 -277 365 O ATOM 1317 CB TYR A 203 -6.209 23.591 -7.267 1.00 45.82 C ANISOU 1317 CB TYR A 203 5809 4991 6609 -50 -236 571 C ATOM 1318 CG TYR A 203 -5.975 23.830 -8.743 1.00 50.25 C ANISOU 1318 CG TYR A 203 6485 5552 7057 -90 -223 692 C ATOM 1319 CD1 TYR A 203 -6.723 23.159 -9.706 1.00 53.12 C ANISOU 1319 CD1 TYR A 203 6948 5948 7286 -74 -289 734 C ATOM 1320 CD2 TYR A 203 -4.897 24.597 -9.178 1.00 51.91 C ANISOU 1320 CD2 TYR A 203 6705 5741 7277 -148 -135 760 C ATOM 1321 CE1 TYR A 203 -6.476 23.336 -11.068 1.00 56.68 C ANISOU 1321 CE1 TYR A 203 7524 6410 7601 -112 -274 843 C ATOM 1322 CE2 TYR A 203 -4.630 24.769 -10.535 1.00 54.09 C ANISOU 1322 CE2 TYR A 203 7097 6030 7425 -191 -104 877 C ATOM 1323 CZ TYR A 203 -5.424 24.138 -11.478 1.00 63.49 C ANISOU 1323 CZ TYR A 203 8403 7257 8464 -170 -174 918 C ATOM 1324 OH TYR A 203 -5.162 24.312 -12.814 1.00 68.33 O ANISOU 1324 OH TYR A 203 9147 7888 8925 -212 -143 1033 O ATOM 1325 N ASP A 204 -8.561 22.166 -5.186 1.00 46.73 N ANISOU 1325 N ASP A 204 5799 5139 6819 66 -370 387 N ATOM 1326 CA ASP A 204 -8.703 21.403 -3.940 1.00 46.31 C ANISOU 1326 CA ASP A 204 5676 5133 6785 93 -349 285 C ATOM 1327 C ASP A 204 -7.433 20.562 -3.719 1.00 48.85 C ANISOU 1327 C ASP A 204 6004 5528 7027 79 -271 240 C ATOM 1328 O ASP A 204 -7.057 20.323 -2.577 1.00 49.02 O ANISOU 1328 O ASP A 204 5968 5575 7081 89 -239 164 O ATOM 1329 CB ASP A 204 -9.951 20.505 -3.970 1.00 48.36 C ANISOU 1329 CB ASP A 204 5936 5414 7023 121 -415 277 C ATOM 1330 CG ASP A 204 -10.100 19.594 -2.753 1.00 62.58 C ANISOU 1330 CG ASP A 204 7681 7269 8828 140 -385 191 C ATOM 1331 OD1 ASP A 204 -9.887 20.079 -1.613 1.00 63.07 O ANISOU 1331 OD1 ASP A 204 7681 7325 8956 150 -345 131 O ATOM 1332 OD2 ASP A 204 -10.439 18.398 -2.940 1.00 68.85 O ANISOU 1332 OD2 ASP A 204 8500 8107 9554 143 -406 185 O ATOM 1333 N THR A 205 -6.781 20.114 -4.804 1.00 43.85 N ANISOU 1333 N THR A 205 5442 4929 6290 58 -241 285 N ATOM 1334 CA THR A 205 -5.521 19.374 -4.703 1.00 42.42 C ANISOU 1334 CA THR A 205 5255 4810 6052 51 -161 243 C ATOM 1335 C THR A 205 -4.411 20.319 -5.152 1.00 46.14 C ANISOU 1335 C THR A 205 5721 5261 6550 9 -91 286 C ATOM 1336 O THR A 205 -4.000 21.164 -4.354 1.00 45.41 O ANISOU 1336 O THR A 205 5559 5131 6565 -5 -78 262 O ATOM 1337 CB THR A 205 -5.567 17.949 -5.333 1.00 41.76 C ANISOU 1337 CB THR A 205 5235 4785 5846 69 -163 229 C ATOM 1338 OG1 THR A 205 -5.778 18.022 -6.740 1.00 41.59 O ANISOU 1338 OG1 THR A 205 5312 4761 5730 53 -174 300 O ATOM 1339 CG2 THR A 205 -6.618 17.048 -4.693 1.00 35.09 C ANISOU 1339 CG2 THR A 205 4377 3949 5006 99 -231 187 C ATOM 1340 N THR A 206 -3.996 20.250 -6.437 1.00 42.92 N ANISOU 1340 N THR A 206 5389 4872 6046 -15 -47 353 N ATOM 1341 CA THR A 206 -2.950 21.100 -7.036 1.00 42.93 C ANISOU 1341 CA THR A 206 5392 4860 6061 -67 38 413 C ATOM 1342 C THR A 206 -2.997 20.984 -8.570 1.00 48.65 C ANISOU 1342 C THR A 206 6237 5606 6642 -88 65 502 C ATOM 1343 O THR A 206 -3.882 20.311 -9.102 1.00 48.20 O ANISOU 1343 O THR A 206 6261 5568 6486 -61 -2 508 O ATOM 1344 CB THR A 206 -1.550 20.727 -6.452 1.00 43.97 C ANISOU 1344 CB THR A 206 5437 5037 6232 -74 131 345 C ATOM 1345 OG1 THR A 206 -0.579 21.687 -6.866 1.00 41.72 O ANISOU 1345 OG1 THR A 206 5126 4727 6000 -132 212 404 O ATOM 1346 CG2 THR A 206 -1.092 19.323 -6.832 1.00 37.13 C ANISOU 1346 CG2 THR A 206 4598 4253 5257 -42 180 296 C ATOM 1347 N SER A 207 -2.029 21.615 -9.273 1.00 47.07 N ANISOU 1347 N SER A 207 6052 5407 6426 -141 165 570 N ATOM 1348 CA SER A 207 -1.870 21.527 -10.731 1.00 48.05 C ANISOU 1348 CA SER A 207 6300 5567 6390 -169 220 656 C ATOM 1349 C SER A 207 -1.285 20.138 -11.064 1.00 51.82 C ANISOU 1349 C SER A 207 6802 6142 6746 -136 297 575 C ATOM 1350 O SER A 207 -0.705 19.506 -10.177 1.00 50.64 O ANISOU 1350 O SER A 207 6553 6020 6667 -106 327 476 O ATOM 1351 CB SER A 207 -0.917 22.611 -11.220 1.00 51.59 C ANISOU 1351 CB SER A 207 6739 5989 6875 -242 325 751 C ATOM 1352 OG SER A 207 0.323 22.510 -10.539 1.00 58.22 O ANISOU 1352 OG SER A 207 7451 6854 7817 -256 428 684 O ATOM 1353 N ASP A 208 -1.411 19.678 -12.333 1.00 48.78 N ANISOU 1353 N ASP A 208 6553 5804 6177 -139 324 613 N ATOM 1354 CA ASP A 208 -0.914 18.370 -12.796 1.00 48.49 C ANISOU 1354 CA ASP A 208 6558 5852 6015 -102 398 529 C ATOM 1355 C ASP A 208 0.593 18.165 -12.617 1.00 51.00 C ANISOU 1355 C ASP A 208 6778 6219 6381 -110 565 480 C ATOM 1356 O ASP A 208 1.037 17.037 -12.389 1.00 49.72 O ANISOU 1356 O ASP A 208 6583 6104 6204 -59 604 374 O ATOM 1357 CB ASP A 208 -1.328 18.102 -14.255 1.00 51.95 C ANISOU 1357 CB ASP A 208 7177 6328 6235 -111 395 581 C ATOM 1358 CG ASP A 208 -2.829 17.995 -14.474 1.00 64.43 C ANISOU 1358 CG ASP A 208 8848 7867 7765 -92 210 608 C ATOM 1359 OD1 ASP A 208 -3.529 17.466 -13.577 1.00 62.86 O ANISOU 1359 OD1 ASP A 208 8583 7640 7660 -52 106 537 O ATOM 1360 OD2 ASP A 208 -3.302 18.420 -15.554 1.00 75.06 O ANISOU 1360 OD2 ASP A 208 10332 9210 8977 -121 169 704 O ATOM 1361 N GLU A 209 1.367 19.259 -12.708 1.00 47.23 N ANISOU 1361 N GLU A 209 6245 5722 5977 -173 658 558 N ATOM 1362 CA GLU A 209 2.819 19.295 -12.546 1.00 46.87 C ANISOU 1362 CA GLU A 209 6083 5714 6012 -194 816 529 C ATOM 1363 C GLU A 209 3.254 18.851 -11.137 1.00 47.87 C ANISOU 1363 C GLU A 209 6049 5830 6310 -152 778 417 C ATOM 1364 O GLU A 209 4.269 18.172 -11.010 1.00 49.01 O ANISOU 1364 O GLU A 209 6112 6025 6486 -126 875 342 O ATOM 1365 CB GLU A 209 3.334 20.720 -12.831 1.00 49.24 C ANISOU 1365 CB GLU A 209 6354 5970 6385 -284 889 653 C ATOM 1366 CG GLU A 209 4.829 20.791 -13.097 1.00 60.54 C ANISOU 1366 CG GLU A 209 7688 7452 7862 -323 1083 651 C ATOM 1367 CD GLU A 209 5.508 22.148 -13.011 1.00 75.36 C ANISOU 1367 CD GLU A 209 9481 9270 9884 -418 1149 753 C ATOM 1368 OE1 GLU A 209 6.757 22.166 -12.919 1.00 65.38 O ANISOU 1368 OE1 GLU A 209 8087 8038 8717 -448 1288 731 O ATOM 1369 OE2 GLU A 209 4.808 23.187 -13.054 1.00 65.45 O ANISOU 1369 OE2 GLU A 209 8281 7931 8657 -462 1059 854 O ATOM 1370 N TYR A 210 2.498 19.234 -10.093 1.00 41.69 N ANISOU 1370 N TYR A 210 5224 4982 5634 -143 639 405 N ATOM 1371 CA TYR A 210 2.833 18.915 -8.702 1.00 39.94 C ANISOU 1371 CA TYR A 210 4870 4749 5557 -110 588 310 C ATOM 1372 C TYR A 210 1.949 17.836 -8.058 1.00 40.03 C ANISOU 1372 C TYR A 210 4908 4767 5532 -40 473 231 C ATOM 1373 O TYR A 210 2.107 17.548 -6.868 1.00 38.30 O ANISOU 1373 O TYR A 210 4600 4540 5412 -13 420 162 O ATOM 1374 CB TYR A 210 2.855 20.206 -7.857 1.00 40.97 C ANISOU 1374 CB TYR A 210 4917 4803 5845 -157 538 341 C ATOM 1375 CG TYR A 210 3.852 21.233 -8.353 1.00 43.93 C ANISOU 1375 CG TYR A 210 5241 5159 6291 -235 650 416 C ATOM 1376 CD1 TYR A 210 5.218 21.069 -8.138 1.00 46.60 C ANISOU 1376 CD1 TYR A 210 5453 5531 6723 -250 752 374 C ATOM 1377 CD2 TYR A 210 3.433 22.362 -9.050 1.00 45.21 C ANISOU 1377 CD2 TYR A 210 5475 5263 6439 -295 651 536 C ATOM 1378 CE1 TYR A 210 6.144 21.994 -8.619 1.00 49.32 C ANISOU 1378 CE1 TYR A 210 5738 5857 7145 -332 864 448 C ATOM 1379 CE2 TYR A 210 4.349 23.305 -9.522 1.00 47.16 C ANISOU 1379 CE2 TYR A 210 5677 5484 6756 -378 760 619 C ATOM 1380 CZ TYR A 210 5.705 23.119 -9.297 1.00 56.88 C ANISOU 1380 CZ TYR A 210 6775 6754 8083 -399 871 574 C ATOM 1381 OH TYR A 210 6.624 24.036 -9.754 1.00 60.25 O ANISOU 1381 OH TYR A 210 7143 7155 8595 -489 986 659 O ATOM 1382 N LEU A 211 1.046 17.226 -8.844 1.00 35.43 N ANISOU 1382 N LEU A 211 4453 4201 4809 -16 433 244 N ATOM 1383 CA LEU A 211 0.078 16.234 -8.375 1.00 33.64 C ANISOU 1383 CA LEU A 211 4261 3972 4550 37 323 186 C ATOM 1384 C LEU A 211 0.675 14.986 -7.708 1.00 35.11 C ANISOU 1384 C LEU A 211 4386 4190 4766 92 334 84 C ATOM 1385 O LEU A 211 0.218 14.600 -6.631 1.00 33.28 O ANISOU 1385 O LEU A 211 4111 3938 4594 118 246 44 O ATOM 1386 CB LEU A 211 -0.954 15.893 -9.472 1.00 34.17 C ANISOU 1386 CB LEU A 211 4473 4042 4467 42 271 223 C ATOM 1387 CG LEU A 211 -2.200 15.095 -9.047 1.00 39.06 C ANISOU 1387 CG LEU A 211 5125 4640 5075 78 137 186 C ATOM 1388 CD1 LEU A 211 -3.051 15.868 -8.044 1.00 39.29 C ANISOU 1388 CD1 LEU A 211 5092 4615 5220 68 46 212 C ATOM 1389 CD2 LEU A 211 -3.047 14.751 -10.244 1.00 43.14 C ANISOU 1389 CD2 LEU A 211 5783 5162 5447 78 83 217 C ATOM 1390 N ARG A 212 1.702 14.387 -8.322 1.00 31.98 N ANISOU 1390 N ARG A 212 3981 3839 4331 110 444 47 N ATOM 1391 CA ARG A 212 2.367 13.200 -7.785 1.00 31.36 C ANISOU 1391 CA ARG A 212 3840 3780 4295 169 455 -47 C ATOM 1392 C ARG A 212 3.049 13.523 -6.451 1.00 34.88 C ANISOU 1392 C ARG A 212 4142 4210 4899 169 431 -72 C ATOM 1393 O ARG A 212 2.916 12.756 -5.493 1.00 33.25 O ANISOU 1393 O ARG A 212 3903 3993 4737 211 351 -123 O ATOM 1394 CB ARG A 212 3.337 12.590 -8.810 1.00 30.03 C ANISOU 1394 CB ARG A 212 3689 3661 4061 194 591 -86 C ATOM 1395 CG ARG A 212 3.561 11.105 -8.586 1.00 36.95 C ANISOU 1395 CG ARG A 212 4559 4540 4938 271 571 -186 C ATOM 1396 CD ARG A 212 4.149 10.397 -9.795 1.00 46.64 C ANISOU 1396 CD ARG A 212 5846 5810 6064 305 694 -239 C ATOM 1397 NE ARG A 212 3.167 10.127 -10.852 1.00 50.68 N ANISOU 1397 NE ARG A 212 6530 6327 6399 299 665 -228 N ATOM 1398 CZ ARG A 212 2.360 9.068 -10.887 1.00 56.86 C ANISOU 1398 CZ ARG A 212 7397 7080 7126 340 563 -282 C ATOM 1399 NH1 ARG A 212 2.378 8.178 -9.903 1.00 37.42 N ANISOU 1399 NH1 ARG A 212 4870 4580 4770 388 486 -341 N ATOM 1400 NH2 ARG A 212 1.518 8.902 -11.896 1.00 47.63 N ANISOU 1400 NH2 ARG A 212 6381 5916 5800 328 527 -273 N ATOM 1401 N SER A 213 3.694 14.707 -6.377 1.00 32.05 N ANISOU 1401 N SER A 213 3710 3845 4621 116 486 -29 N ATOM 1402 CA SER A 213 4.357 15.224 -5.178 1.00 30.95 C ANISOU 1402 CA SER A 213 3440 3687 4633 102 454 -51 C ATOM 1403 C SER A 213 3.303 15.420 -4.075 1.00 32.93 C ANISOU 1403 C SER A 213 3710 3900 4902 106 318 -55 C ATOM 1404 O SER A 213 3.516 15.010 -2.931 1.00 30.90 O ANISOU 1404 O SER A 213 3392 3641 4707 134 251 -107 O ATOM 1405 CB SER A 213 5.063 16.539 -5.507 1.00 32.52 C ANISOU 1405 CB SER A 213 3577 3872 4907 31 535 6 C ATOM 1406 OG SER A 213 5.607 17.162 -4.361 1.00 36.07 O ANISOU 1406 OG SER A 213 3909 4292 5504 9 484 -19 O ATOM 1407 N TYR A 214 2.136 15.973 -4.450 1.00 29.63 N ANISOU 1407 N TYR A 214 3382 3455 4423 82 279 0 N ATOM 1408 CA TYR A 214 1.019 16.190 -3.539 1.00 28.63 C ANISOU 1408 CA TYR A 214 3272 3294 4311 88 171 -4 C ATOM 1409 C TYR A 214 0.491 14.870 -2.944 1.00 31.46 C ANISOU 1409 C TYR A 214 3655 3671 4627 140 105 -53 C ATOM 1410 O TYR A 214 0.195 14.818 -1.750 1.00 29.85 O ANISOU 1410 O TYR A 214 3416 3458 4465 151 39 -83 O ATOM 1411 CB TYR A 214 -0.105 16.972 -4.236 1.00 29.16 C ANISOU 1411 CB TYR A 214 3420 3325 4333 60 144 67 C ATOM 1412 CG TYR A 214 -1.248 17.281 -3.309 1.00 29.46 C ANISOU 1412 CG TYR A 214 3456 3328 4407 68 50 57 C ATOM 1413 CD1 TYR A 214 -1.162 18.320 -2.392 1.00 31.58 C ANISOU 1413 CD1 TYR A 214 3662 3560 4779 48 28 42 C ATOM 1414 CD2 TYR A 214 -2.392 16.488 -3.293 1.00 29.84 C ANISOU 1414 CD2 TYR A 214 3561 3382 4395 97 -13 53 C ATOM 1415 CE1 TYR A 214 -2.211 18.610 -1.529 1.00 33.03 C ANISOU 1415 CE1 TYR A 214 3842 3717 4992 62 -40 21 C ATOM 1416 CE2 TYR A 214 -3.444 16.756 -2.420 1.00 30.59 C ANISOU 1416 CE2 TYR A 214 3640 3451 4531 105 -80 42 C ATOM 1417 CZ TYR A 214 -3.352 17.827 -1.546 1.00 39.12 C ANISOU 1417 CZ TYR A 214 4661 4500 5702 91 -87 24 C ATOM 1418 OH TYR A 214 -4.369 18.098 -0.666 1.00 39.61 O ANISOU 1418 OH TYR A 214 4706 4543 5802 104 -135 1 O ATOM 1419 N PHE A 215 0.379 13.819 -3.767 1.00 28.88 N ANISOU 1419 N PHE A 215 3393 3365 4214 170 123 -62 N ATOM 1420 CA PHE A 215 -0.061 12.490 -3.309 1.00 28.95 C ANISOU 1420 CA PHE A 215 3428 3377 4194 215 62 -104 C ATOM 1421 C PHE A 215 0.901 11.946 -2.260 1.00 32.12 C ANISOU 1421 C PHE A 215 3744 3788 4670 246 50 -155 C ATOM 1422 O PHE A 215 0.447 11.403 -1.251 1.00 32.24 O ANISOU 1422 O PHE A 215 3757 3795 4697 263 -25 -169 O ATOM 1423 CB PHE A 215 -0.145 11.499 -4.482 1.00 31.55 C ANISOU 1423 CB PHE A 215 3841 3717 4428 241 89 -118 C ATOM 1424 CG PHE A 215 -0.540 10.094 -4.086 1.00 34.04 C ANISOU 1424 CG PHE A 215 4185 4018 4730 284 23 -161 C ATOM 1425 CD1 PHE A 215 -1.844 9.801 -3.705 1.00 36.89 C ANISOU 1425 CD1 PHE A 215 4589 4353 5075 274 -67 -140 C ATOM 1426 CD2 PHE A 215 0.387 9.062 -4.106 1.00 38.38 C ANISOU 1426 CD2 PHE A 215 4712 4574 5298 333 53 -218 C ATOM 1427 CE1 PHE A 215 -2.212 8.506 -3.341 1.00 38.43 C ANISOU 1427 CE1 PHE A 215 4809 4525 5268 303 -126 -168 C ATOM 1428 CE2 PHE A 215 0.015 7.761 -3.750 1.00 41.67 C ANISOU 1428 CE2 PHE A 215 5159 4959 5713 370 -16 -250 C ATOM 1429 CZ PHE A 215 -1.279 7.496 -3.357 1.00 39.06 C ANISOU 1429 CZ PHE A 215 4877 4601 5364 350 -105 -221 C ATOM 1430 N ILE A 216 2.218 12.078 -2.514 1.00 28.16 N ANISOU 1430 N ILE A 216 3172 3306 4220 251 124 -177 N ATOM 1431 CA ILE A 216 3.288 11.624 -1.612 1.00 28.50 C ANISOU 1431 CA ILE A 216 3118 3356 4354 283 105 -224 C ATOM 1432 C ILE A 216 3.192 12.366 -0.283 1.00 31.40 C ANISOU 1432 C ILE A 216 3436 3714 4782 258 30 -223 C ATOM 1433 O ILE A 216 3.133 11.739 0.776 1.00 32.66 O ANISOU 1433 O ILE A 216 3587 3872 4952 285 -51 -245 O ATOM 1434 CB ILE A 216 4.687 11.718 -2.285 1.00 32.40 C ANISOU 1434 CB ILE A 216 3529 3873 4909 290 211 -246 C ATOM 1435 CG1 ILE A 216 4.799 10.697 -3.443 1.00 33.02 C ANISOU 1435 CG1 ILE A 216 3667 3966 4915 333 284 -273 C ATOM 1436 CG2 ILE A 216 5.817 11.522 -1.263 1.00 33.00 C ANISOU 1436 CG2 ILE A 216 3479 3950 5109 315 173 -289 C ATOM 1437 CD1 ILE A 216 5.825 11.042 -4.488 1.00 36.46 C ANISOU 1437 CD1 ILE A 216 4056 4434 5365 323 430 -278 C ATOM 1438 N TYR A 217 3.091 13.690 -0.356 1.00 26.64 N ANISOU 1438 N TYR A 217 2815 3099 4209 205 52 -196 N ATOM 1439 CA TYR A 217 2.937 14.550 0.801 1.00 25.20 C ANISOU 1439 CA TYR A 217 2597 2900 4077 179 -13 -208 C ATOM 1440 C TYR A 217 1.668 14.181 1.585 1.00 29.00 C ANISOU 1440 C TYR A 217 3148 3378 4493 194 -88 -207 C ATOM 1441 O TYR A 217 1.733 14.060 2.805 1.00 28.09 O ANISOU 1441 O TYR A 217 3012 3270 4390 204 -153 -239 O ATOM 1442 CB TYR A 217 2.942 16.030 0.372 1.00 25.96 C ANISOU 1442 CB TYR A 217 2675 2966 4222 121 30 -176 C ATOM 1443 CG TYR A 217 2.309 16.936 1.401 1.00 26.68 C ANISOU 1443 CG TYR A 217 2767 3027 4342 100 -37 -193 C ATOM 1444 CD1 TYR A 217 2.915 17.148 2.637 1.00 28.88 C ANISOU 1444 CD1 TYR A 217 2984 3307 4681 99 -100 -250 C ATOM 1445 CD2 TYR A 217 1.067 17.515 1.176 1.00 27.05 C ANISOU 1445 CD2 TYR A 217 2879 3045 4354 87 -46 -160 C ATOM 1446 CE1 TYR A 217 2.306 17.927 3.617 1.00 29.40 C ANISOU 1446 CE1 TYR A 217 3064 3349 4757 85 -156 -282 C ATOM 1447 CE2 TYR A 217 0.454 18.313 2.143 1.00 28.30 C ANISOU 1447 CE2 TYR A 217 3035 3174 4543 78 -97 -190 C ATOM 1448 CZ TYR A 217 1.076 18.510 3.364 1.00 35.27 C ANISOU 1448 CZ TYR A 217 3867 4063 5471 77 -146 -256 C ATOM 1449 OH TYR A 217 0.476 19.277 4.331 1.00 34.89 O ANISOU 1449 OH TYR A 217 3828 3990 5439 72 -189 -301 O ATOM 1450 N SER A 218 0.527 13.993 0.886 1.00 26.64 N ANISOU 1450 N SER A 218 2928 3070 4124 193 -78 -171 N ATOM 1451 CA SER A 218 -0.742 13.614 1.520 1.00 27.14 C ANISOU 1451 CA SER A 218 3042 3129 4138 201 -134 -164 C ATOM 1452 C SER A 218 -0.669 12.274 2.238 1.00 30.88 C ANISOU 1452 C SER A 218 3528 3620 4584 237 -181 -182 C ATOM 1453 O SER A 218 -1.283 12.130 3.292 1.00 29.34 O ANISOU 1453 O SER A 218 3346 3431 4369 236 -226 -185 O ATOM 1454 CB SER A 218 -1.894 13.631 0.518 1.00 30.28 C ANISOU 1454 CB SER A 218 3508 3511 4487 192 -125 -120 C ATOM 1455 OG SER A 218 -2.014 14.950 0.016 1.00 38.02 O ANISOU 1455 OG SER A 218 4480 4465 5500 159 -98 -93 O ATOM 1456 N MET A 219 0.105 11.315 1.695 1.00 29.45 N ANISOU 1456 N MET A 219 3344 3444 4403 268 -166 -193 N ATOM 1457 CA MET A 219 0.307 10.005 2.320 1.00 30.05 C ANISOU 1457 CA MET A 219 3430 3519 4471 307 -219 -205 C ATOM 1458 C MET A 219 1.058 10.156 3.637 1.00 30.49 C ANISOU 1458 C MET A 219 3430 3588 4566 314 -272 -227 C ATOM 1459 O MET A 219 0.722 9.460 4.590 1.00 27.52 O ANISOU 1459 O MET A 219 3084 3214 4159 326 -336 -216 O ATOM 1460 CB MET A 219 1.066 9.042 1.402 1.00 34.41 C ANISOU 1460 CB MET A 219 3981 4061 5033 348 -187 -226 C ATOM 1461 CG MET A 219 0.234 8.456 0.281 1.00 41.53 C ANISOU 1461 CG MET A 219 4965 4945 5871 351 -167 -214 C ATOM 1462 SD MET A 219 -1.368 7.696 0.722 1.00 48.95 S ANISOU 1462 SD MET A 219 5982 5857 6760 336 -242 -178 S ATOM 1463 CE MET A 219 -0.860 6.468 2.000 1.00 45.84 C ANISOU 1463 CE MET A 219 5574 5445 6400 374 -315 -182 C ATOM 1464 N CYS A 220 2.064 11.083 3.688 1.00 26.52 N ANISOU 1464 N CYS A 220 2850 3094 4131 301 -252 -253 N ATOM 1465 CA CYS A 220 2.878 11.346 4.872 1.00 26.78 C ANISOU 1465 CA CYS A 220 2825 3139 4210 303 -318 -283 C ATOM 1466 C CYS A 220 2.029 11.905 6.008 1.00 30.56 C ANISOU 1466 C CYS A 220 3348 3630 4635 277 -366 -285 C ATOM 1467 O CYS A 220 2.106 11.390 7.120 1.00 30.48 O ANISOU 1467 O CYS A 220 3356 3635 4591 292 -441 -290 O ATOM 1468 CB CYS A 220 4.067 12.248 4.542 1.00 27.60 C ANISOU 1468 CB CYS A 220 2830 3242 4415 284 -284 -312 C ATOM 1469 SG CYS A 220 5.274 11.498 3.417 1.00 32.56 S ANISOU 1469 SG CYS A 220 3386 3870 5116 324 -215 -322 S ATOM 1470 N THR A 221 1.169 12.897 5.711 1.00 27.41 N ANISOU 1470 N THR A 221 2971 3222 4222 242 -322 -280 N ATOM 1471 CA THR A 221 0.249 13.481 6.685 1.00 27.99 C ANISOU 1471 CA THR A 221 3082 3304 4248 223 -344 -293 C ATOM 1472 C THR A 221 -0.891 12.521 7.092 1.00 31.89 C ANISOU 1472 C THR A 221 3647 3813 4657 235 -355 -258 C ATOM 1473 O THR A 221 -1.295 12.530 8.257 1.00 31.70 O ANISOU 1473 O THR A 221 3653 3813 4577 230 -384 -270 O ATOM 1474 CB THR A 221 -0.237 14.865 6.253 1.00 31.14 C ANISOU 1474 CB THR A 221 3469 3676 4687 191 -298 -303 C ATOM 1475 OG1 THR A 221 -0.897 14.769 4.990 1.00 33.09 O ANISOU 1475 OG1 THR A 221 3740 3902 4928 188 -245 -255 O ATOM 1476 CG2 THR A 221 0.892 15.879 6.199 1.00 26.20 C ANISOU 1476 CG2 THR A 221 2772 3029 4152 167 -300 -339 C ATOM 1477 N THR A 222 -1.385 11.692 6.149 1.00 27.56 N ANISOU 1477 N THR A 222 3127 3249 4096 245 -329 -216 N ATOM 1478 CA THR A 222 -2.421 10.672 6.403 1.00 27.22 C ANISOU 1478 CA THR A 222 3141 3207 3994 248 -342 -176 C ATOM 1479 C THR A 222 -1.905 9.665 7.436 1.00 32.06 C ANISOU 1479 C THR A 222 3773 3834 4573 267 -405 -165 C ATOM 1480 O THR A 222 -2.617 9.354 8.379 1.00 32.68 O ANISOU 1480 O THR A 222 3894 3932 4591 254 -420 -142 O ATOM 1481 CB THR A 222 -2.861 9.998 5.083 1.00 27.88 C ANISOU 1481 CB THR A 222 3249 3261 4084 253 -320 -145 C ATOM 1482 OG1 THR A 222 -3.571 10.969 4.312 1.00 27.14 O ANISOU 1482 OG1 THR A 222 3150 3155 4005 231 -279 -141 O ATOM 1483 CG2 THR A 222 -3.764 8.770 5.297 1.00 26.99 C ANISOU 1483 CG2 THR A 222 3185 3134 3934 251 -346 -104 C ATOM 1484 N VAL A 223 -0.672 9.185 7.263 1.00 29.08 N ANISOU 1484 N VAL A 223 3364 3447 4238 298 -440 -179 N ATOM 1485 CA VAL A 223 -0.053 8.217 8.165 1.00 29.32 C ANISOU 1485 CA VAL A 223 3409 3478 4253 325 -519 -163 C ATOM 1486 C VAL A 223 0.260 8.862 9.522 1.00 32.02 C ANISOU 1486 C VAL A 223 3752 3860 4554 312 -571 -185 C ATOM 1487 O VAL A 223 -0.163 8.344 10.564 1.00 30.56 O ANISOU 1487 O VAL A 223 3628 3694 4288 306 -613 -151 O ATOM 1488 CB VAL A 223 1.189 7.515 7.532 1.00 33.81 C ANISOU 1488 CB VAL A 223 3927 4017 4900 373 -543 -178 C ATOM 1489 CG1 VAL A 223 1.888 6.589 8.534 1.00 34.37 C ANISOU 1489 CG1 VAL A 223 4005 4080 4973 407 -646 -158 C ATOM 1490 CG2 VAL A 223 0.813 6.741 6.265 1.00 33.14 C ANISOU 1490 CG2 VAL A 223 3866 3893 4831 389 -496 -166 C ATOM 1491 N ALA A 224 0.988 9.996 9.507 1.00 28.26 N ANISOU 1491 N ALA A 224 3214 3393 4128 303 -568 -242 N ATOM 1492 CA ALA A 224 1.428 10.638 10.739 1.00 28.31 C ANISOU 1492 CA ALA A 224 3221 3431 4104 292 -634 -281 C ATOM 1493 C ALA A 224 0.351 11.333 11.559 1.00 32.14 C ANISOU 1493 C ALA A 224 3767 3948 4496 261 -605 -298 C ATOM 1494 O ALA A 224 0.429 11.313 12.789 1.00 31.86 O ANISOU 1494 O ALA A 224 3780 3949 4377 258 -665 -310 O ATOM 1495 CB ALA A 224 2.595 11.581 10.459 1.00 29.02 C ANISOU 1495 CB ALA A 224 3217 3509 4299 287 -648 -340 C ATOM 1496 N MET A 225 -0.635 11.967 10.902 1.00 29.09 N ANISOU 1496 N MET A 225 3380 3551 4123 241 -515 -301 N ATOM 1497 CA MET A 225 -1.657 12.741 11.625 1.00 29.18 C ANISOU 1497 CA MET A 225 3430 3587 4071 219 -474 -331 C ATOM 1498 C MET A 225 -3.076 12.205 11.590 1.00 32.25 C ANISOU 1498 C MET A 225 3862 3986 4405 210 -410 -280 C ATOM 1499 O MET A 225 -3.983 12.808 12.165 1.00 30.99 O ANISOU 1499 O MET A 225 3722 3848 4203 197 -361 -307 O ATOM 1500 CB MET A 225 -1.574 14.227 11.299 1.00 31.29 C ANISOU 1500 CB MET A 225 3649 3829 4412 204 -443 -397 C ATOM 1501 CG MET A 225 -0.262 14.853 11.759 1.00 36.08 C ANISOU 1501 CG MET A 225 4216 4430 5062 201 -517 -460 C ATOM 1502 SD MET A 225 -0.259 16.638 11.634 1.00 41.07 S ANISOU 1502 SD MET A 225 4805 5018 5781 174 -490 -542 S ATOM 1503 CE MET A 225 -0.482 16.825 9.876 1.00 36.84 C ANISOU 1503 CE MET A 225 4218 4429 5348 167 -410 -480 C ATOM 1504 N PHE A 226 -3.254 11.053 10.967 1.00 28.94 N ANISOU 1504 N PHE A 226 3455 3548 3995 218 -413 -212 N ATOM 1505 CA PHE A 226 -4.536 10.380 10.957 1.00 28.88 C ANISOU 1505 CA PHE A 226 3481 3543 3950 201 -367 -155 C ATOM 1506 C PHE A 226 -4.359 8.944 11.468 1.00 33.41 C ANISOU 1506 C PHE A 226 4107 4118 4469 205 -418 -88 C ATOM 1507 O PHE A 226 -4.889 8.635 12.531 1.00 33.97 O ANISOU 1507 O PHE A 226 4230 4227 4452 186 -409 -57 O ATOM 1508 CB PHE A 226 -5.252 10.475 9.592 1.00 29.88 C ANISOU 1508 CB PHE A 226 3574 3628 4151 196 -321 -137 C ATOM 1509 CG PHE A 226 -6.374 9.481 9.438 1.00 31.06 C ANISOU 1509 CG PHE A 226 3748 3766 4288 178 -302 -72 C ATOM 1510 CD1 PHE A 226 -7.582 9.663 10.103 1.00 33.77 C ANISOU 1510 CD1 PHE A 226 4094 4137 4601 153 -246 -60 C ATOM 1511 CD2 PHE A 226 -6.198 8.320 8.689 1.00 33.56 C ANISOU 1511 CD2 PHE A 226 4082 4042 4629 185 -338 -28 C ATOM 1512 CE1 PHE A 226 -8.604 8.720 9.998 1.00 35.01 C ANISOU 1512 CE1 PHE A 226 4259 4279 4763 126 -228 5 C ATOM 1513 CE2 PHE A 226 -7.224 7.375 8.585 1.00 36.71 C ANISOU 1513 CE2 PHE A 226 4500 4419 5028 160 -332 30 C ATOM 1514 CZ PHE A 226 -8.423 7.589 9.233 1.00 34.33 C ANISOU 1514 CZ PHE A 226 4192 4145 4707 127 -278 51 C ATOM 1515 N CYS A 227 -3.558 8.101 10.762 1.00 29.94 N ANISOU 1515 N CYS A 227 3655 3636 4083 231 -470 -65 N ATOM 1516 CA CYS A 227 -3.310 6.693 11.131 1.00 30.66 C ANISOU 1516 CA CYS A 227 3793 3705 4151 242 -532 0 C ATOM 1517 C CYS A 227 -2.769 6.486 12.523 1.00 34.56 C ANISOU 1517 C CYS A 227 4335 4237 4561 245 -600 17 C ATOM 1518 O CYS A 227 -3.368 5.715 13.281 1.00 33.63 O ANISOU 1518 O CYS A 227 4283 4128 4368 222 -606 88 O ATOM 1519 CB CYS A 227 -2.461 5.976 10.088 1.00 31.14 C ANISOU 1519 CB CYS A 227 3823 3709 4299 281 -569 -3 C ATOM 1520 SG CYS A 227 -3.267 5.819 8.480 1.00 34.79 S ANISOU 1520 SG CYS A 227 4271 4126 4821 274 -506 -4 S ATOM 1521 N VAL A 228 -1.652 7.179 12.866 1.00 31.10 N ANISOU 1521 N VAL A 228 3865 3818 4133 267 -655 -42 N ATOM 1522 CA VAL A 228 -1.021 7.098 14.186 1.00 31.56 C ANISOU 1522 CA VAL A 228 3971 3913 4106 271 -744 -37 C ATOM 1523 C VAL A 228 -1.987 7.597 15.272 1.00 36.66 C ANISOU 1523 C VAL A 228 4689 4624 4614 232 -692 -37 C ATOM 1524 O VAL A 228 -2.312 6.798 16.145 1.00 37.19 O ANISOU 1524 O VAL A 228 4839 4712 4579 217 -717 37 O ATOM 1525 CB VAL A 228 0.404 7.705 14.274 1.00 34.78 C ANISOU 1525 CB VAL A 228 4318 4323 4576 300 -829 -105 C ATOM 1526 CG1 VAL A 228 0.953 7.604 15.699 1.00 35.21 C ANISOU 1526 CG1 VAL A 228 4436 4417 4527 302 -943 -96 C ATOM 1527 CG2 VAL A 228 1.350 7.030 13.282 1.00 33.96 C ANISOU 1527 CG2 VAL A 228 4138 4158 4605 344 -865 -99 C ATOM 1528 N PRO A 229 -2.562 8.825 15.205 1.00 33.26 N ANISOU 1528 N PRO A 229 4234 4223 4181 213 -609 -110 N ATOM 1529 CA PRO A 229 -3.561 9.207 16.217 1.00 33.62 C ANISOU 1529 CA PRO A 229 4345 4330 4100 183 -541 -117 C ATOM 1530 C PRO A 229 -4.731 8.215 16.336 1.00 36.67 C ANISOU 1530 C PRO A 229 4775 4721 4436 153 -472 -18 C ATOM 1531 O PRO A 229 -5.176 7.964 17.450 1.00 36.60 O ANISOU 1531 O PRO A 229 4847 4768 4293 129 -451 16 O ATOM 1532 CB PRO A 229 -4.018 10.591 15.750 1.00 34.49 C ANISOU 1532 CB PRO A 229 4394 4439 4271 180 -458 -210 C ATOM 1533 CG PRO A 229 -2.831 11.132 15.013 1.00 38.05 C ANISOU 1533 CG PRO A 229 4774 4847 4838 202 -523 -263 C ATOM 1534 CD PRO A 229 -2.327 9.939 14.260 1.00 33.39 C ANISOU 1534 CD PRO A 229 4165 4213 4309 220 -572 -188 C ATOM 1535 N LEU A 230 -5.199 7.629 15.215 1.00 32.80 N ANISOU 1535 N LEU A 230 4238 4174 4052 151 -442 28 N ATOM 1536 CA LEU A 230 -6.281 6.634 15.227 1.00 32.97 C ANISOU 1536 CA LEU A 230 4287 4183 4058 116 -389 123 C ATOM 1537 C LEU A 230 -5.901 5.387 16.026 1.00 38.49 C ANISOU 1537 C LEU A 230 5070 4877 4679 107 -465 221 C ATOM 1538 O LEU A 230 -6.729 4.901 16.788 1.00 39.11 O ANISOU 1538 O LEU A 230 5206 4986 4669 65 -413 294 O ATOM 1539 CB LEU A 230 -6.767 6.265 13.804 1.00 31.82 C ANISOU 1539 CB LEU A 230 4078 3968 4045 115 -367 139 C ATOM 1540 CG LEU A 230 -7.880 5.197 13.652 1.00 36.77 C ANISOU 1540 CG LEU A 230 4717 4563 4691 73 -330 232 C ATOM 1541 CD1 LEU A 230 -9.127 5.520 14.508 1.00 38.26 C ANISOU 1541 CD1 LEU A 230 4912 4813 4811 26 -219 254 C ATOM 1542 CD2 LEU A 230 -8.293 5.050 12.195 1.00 36.69 C ANISOU 1542 CD2 LEU A 230 4647 4488 4807 77 -326 222 C ATOM 1543 N VAL A 231 -4.663 4.881 15.870 1.00 36.67 N ANISOU 1543 N VAL A 231 4843 4604 4485 148 -585 227 N ATOM 1544 CA VAL A 231 -4.212 3.702 16.615 1.00 38.09 C ANISOU 1544 CA VAL A 231 5103 4765 4606 149 -680 326 C ATOM 1545 C VAL A 231 -4.094 4.032 18.109 1.00 44.21 C ANISOU 1545 C VAL A 231 5969 5623 5206 131 -702 336 C ATOM 1546 O VAL A 231 -4.485 3.221 18.951 1.00 44.88 O ANISOU 1546 O VAL A 231 6145 5720 5186 99 -712 441 O ATOM 1547 CB VAL A 231 -2.974 2.968 16.013 1.00 42.06 C ANISOU 1547 CB VAL A 231 5575 5188 5218 205 -804 332 C ATOM 1548 CG1 VAL A 231 -3.156 2.710 14.520 1.00 40.68 C ANISOU 1548 CG1 VAL A 231 5325 4942 5189 222 -765 307 C ATOM 1549 CG2 VAL A 231 -1.666 3.709 16.270 1.00 42.36 C ANISOU 1549 CG2 VAL A 231 5578 5252 5267 250 -890 251 C ATOM 1550 N LEU A 232 -3.652 5.272 18.411 1.00 40.43 N ANISOU 1550 N LEU A 232 5470 5201 4691 146 -700 225 N ATOM 1551 CA LEU A 232 -3.496 5.793 19.760 1.00 41.85 C ANISOU 1551 CA LEU A 232 5738 5464 4698 134 -724 201 C ATOM 1552 C LEU A 232 -4.839 5.984 20.458 1.00 46.18 C ANISOU 1552 C LEU A 232 6347 6083 5116 82 -579 224 C ATOM 1553 O LEU A 232 -4.968 5.613 21.626 1.00 47.44 O ANISOU 1553 O LEU A 232 6622 6301 5103 56 -589 284 O ATOM 1554 CB LEU A 232 -2.657 7.082 19.768 1.00 41.71 C ANISOU 1554 CB LEU A 232 5672 5469 4706 163 -769 62 C ATOM 1555 CG LEU A 232 -2.082 7.473 21.125 1.00 48.90 C ANISOU 1555 CG LEU A 232 6680 6449 5452 161 -860 28 C ATOM 1556 CD1 LEU A 232 -1.052 6.438 21.624 1.00 50.55 C ANISOU 1556 CD1 LEU A 232 6941 6632 5634 184 -1036 115 C ATOM 1557 CD2 LEU A 232 -1.440 8.818 21.057 1.00 52.00 C ANISOU 1557 CD2 LEU A 232 7015 6851 5893 179 -891 -118 C ATOM 1558 N ILE A 233 -5.840 6.515 19.737 1.00 40.88 N ANISOU 1558 N ILE A 233 5597 5406 4528 68 -443 182 N ATOM 1559 CA ILE A 233 -7.196 6.708 20.256 1.00 41.39 C ANISOU 1559 CA ILE A 233 5684 5530 4511 24 -287 196 C ATOM 1560 C ILE A 233 -7.823 5.339 20.615 1.00 46.15 C ANISOU 1560 C ILE A 233 6349 6125 5060 -25 -261 354 C ATOM 1561 O ILE A 233 -8.326 5.177 21.730 1.00 47.42 O ANISOU 1561 O ILE A 233 6601 6360 5055 -64 -194 403 O ATOM 1562 CB ILE A 233 -8.059 7.565 19.273 1.00 42.95 C ANISOU 1562 CB ILE A 233 5763 5705 4849 29 -174 119 C ATOM 1563 CG1 ILE A 233 -7.631 9.054 19.318 1.00 42.14 C ANISOU 1563 CG1 ILE A 233 5628 5626 4757 65 -174 -32 C ATOM 1564 CG2 ILE A 233 -9.557 7.437 19.563 1.00 43.93 C ANISOU 1564 CG2 ILE A 233 5876 5869 4948 -17 -15 161 C ATOM 1565 CD1 ILE A 233 -8.024 9.868 18.095 1.00 34.29 C ANISOU 1565 CD1 ILE A 233 4515 4577 3936 83 -126 -98 C ATOM 1566 N LEU A 234 -7.722 4.355 19.694 1.00 42.17 N ANISOU 1566 N LEU A 234 5803 5527 4691 -25 -319 431 N ATOM 1567 CA LEU A 234 -8.235 2.982 19.852 1.00 42.99 C ANISOU 1567 CA LEU A 234 5956 5590 4790 -72 -317 583 C ATOM 1568 C LEU A 234 -7.654 2.259 21.062 1.00 47.40 C ANISOU 1568 C LEU A 234 6650 6174 5185 -86 -402 684 C ATOM 1569 O LEU A 234 -8.386 1.550 21.755 1.00 48.38 O ANISOU 1569 O LEU A 234 6846 6321 5216 -147 -338 802 O ATOM 1570 CB LEU A 234 -7.989 2.151 18.584 1.00 42.30 C ANISOU 1570 CB LEU A 234 5804 5383 4887 -53 -392 615 C ATOM 1571 CG LEU A 234 -8.867 2.450 17.381 1.00 46.62 C ANISOU 1571 CG LEU A 234 6239 5891 5583 -62 -310 568 C ATOM 1572 CD1 LEU A 234 -8.248 1.874 16.121 1.00 46.10 C ANISOU 1572 CD1 LEU A 234 6126 5721 5669 -23 -408 556 C ATOM 1573 CD2 LEU A 234 -10.278 1.914 17.575 1.00 50.49 C ANISOU 1573 CD2 LEU A 234 6720 6383 6081 -137 -198 657 C ATOM 1574 N GLY A 235 -6.349 2.431 21.279 1.00 43.30 N ANISOU 1574 N GLY A 235 6162 5650 4640 -31 -550 642 N ATOM 1575 CA GLY A 235 -5.623 1.869 22.408 1.00 44.62 C ANISOU 1575 CA GLY A 235 6458 5840 4656 -31 -669 725 C ATOM 1576 C GLY A 235 -6.145 2.442 23.708 1.00 50.10 C ANISOU 1576 C GLY A 235 7260 6660 5118 -72 -581 719 C ATOM 1577 O GLY A 235 -6.496 1.683 24.613 1.00 50.92 O ANISOU 1577 O GLY A 235 7481 6792 5073 -120 -569 851 O ATOM 1578 N CYS A 236 -6.258 3.798 23.776 1.00 46.75 N ANISOU 1578 N CYS A 236 6795 6307 4662 -54 -508 564 N ATOM 1579 CA CYS A 236 -6.804 4.548 24.915 1.00 48.07 C ANISOU 1579 CA CYS A 236 7051 6596 4616 -82 -401 514 C ATOM 1580 C CYS A 236 -8.222 4.072 25.229 1.00 50.97 C ANISOU 1580 C CYS A 236 7440 7003 4922 -151 -211 610 C ATOM 1581 O CYS A 236 -8.510 3.769 26.383 1.00 51.81 O ANISOU 1581 O CYS A 236 7681 7191 4816 -194 -166 686 O ATOM 1582 CB CYS A 236 -6.774 6.054 24.652 1.00 48.04 C ANISOU 1582 CB CYS A 236 6970 6627 4657 -45 -348 322 C ATOM 1583 SG CYS A 236 -5.118 6.793 24.693 1.00 51.82 S ANISOU 1583 SG CYS A 236 7447 7088 5154 18 -558 201 S ATOM 1584 N TYR A 237 -9.085 3.959 24.195 1.00 46.05 N ANISOU 1584 N TYR A 237 6687 6323 4488 -166 -108 616 N ATOM 1585 CA TYR A 237 -10.477 3.526 24.343 1.00 46.47 C ANISOU 1585 CA TYR A 237 6722 6401 4534 -236 72 703 C ATOM 1586 C TYR A 237 -10.607 2.079 24.792 1.00 53.54 C ANISOU 1586 C TYR A 237 7709 7262 5371 -297 40 904 C ATOM 1587 O TYR A 237 -11.482 1.773 25.600 1.00 54.85 O ANISOU 1587 O TYR A 237 7935 7495 5410 -365 179 992 O ATOM 1588 CB TYR A 237 -11.308 3.807 23.078 1.00 45.36 C ANISOU 1588 CB TYR A 237 6411 6199 4626 -233 157 651 C ATOM 1589 CG TYR A 237 -11.543 5.275 22.778 1.00 45.36 C ANISOU 1589 CG TYR A 237 6324 6239 4672 -188 236 474 C ATOM 1590 CD1 TYR A 237 -11.091 6.269 23.646 1.00 47.98 C ANISOU 1590 CD1 TYR A 237 6726 6657 4847 -157 242 360 C ATOM 1591 CD2 TYR A 237 -12.225 5.673 21.632 1.00 44.31 C ANISOU 1591 CD2 TYR A 237 6042 6051 4742 -177 292 421 C ATOM 1592 CE1 TYR A 237 -11.306 7.615 23.378 1.00 47.72 C ANISOU 1592 CE1 TYR A 237 6615 6643 4872 -115 308 197 C ATOM 1593 CE2 TYR A 237 -12.457 7.021 21.358 1.00 44.33 C ANISOU 1593 CE2 TYR A 237 5967 6077 4798 -134 356 270 C ATOM 1594 CZ TYR A 237 -11.968 7.989 22.222 1.00 50.07 C ANISOU 1594 CZ TYR A 237 6763 6878 5383 -102 363 157 C ATOM 1595 OH TYR A 237 -12.158 9.321 21.966 1.00 46.41 O ANISOU 1595 OH TYR A 237 6227 6422 4986 -58 416 6 O ATOM 1596 N GLY A 238 -9.719 1.218 24.302 1.00 50.34 N ANISOU 1596 N GLY A 238 7316 6752 5060 -272 -138 973 N ATOM 1597 CA GLY A 238 -9.683 -0.184 24.694 1.00 51.24 C ANISOU 1597 CA GLY A 238 7523 6807 5140 -320 -204 1165 C ATOM 1598 C GLY A 238 -9.324 -0.315 26.161 1.00 57.20 C ANISOU 1598 C GLY A 238 8457 7653 5623 -343 -235 1243 C ATOM 1599 O GLY A 238 -9.952 -1.087 26.888 1.00 57.78 O ANISOU 1599 O GLY A 238 8623 7747 5584 -420 -162 1400 O ATOM 1600 N LEU A 239 -8.339 0.489 26.606 1.00 54.31 N ANISOU 1600 N LEU A 239 8142 7345 5147 -282 -339 1131 N ATOM 1601 CA LEU A 239 -7.871 0.535 27.987 1.00 56.66 C ANISOU 1601 CA LEU A 239 8619 7737 5170 -293 -398 1173 C ATOM 1602 C LEU A 239 -8.898 1.217 28.907 1.00 62.86 C ANISOU 1602 C LEU A 239 9470 8670 5744 -346 -179 1138 C ATOM 1603 O LEU A 239 -9.034 0.804 30.060 1.00 64.45 O ANISOU 1603 O LEU A 239 9837 8947 5704 -396 -157 1251 O ATOM 1604 CB LEU A 239 -6.478 1.194 28.088 1.00 56.48 C ANISOU 1604 CB LEU A 239 8613 7720 5128 -211 -595 1050 C ATOM 1605 CG LEU A 239 -5.309 0.445 27.407 1.00 60.44 C ANISOU 1605 CG LEU A 239 9069 8089 5807 -154 -822 1096 C ATOM 1606 CD1 LEU A 239 -4.171 1.387 27.068 1.00 59.64 C ANISOU 1606 CD1 LEU A 239 8894 7984 5782 -75 -954 926 C ATOM 1607 CD2 LEU A 239 -4.806 -0.717 28.248 1.00 64.41 C ANISOU 1607 CD2 LEU A 239 9726 8561 6185 -172 -973 1282 C ATOM 1608 N ILE A 240 -9.648 2.223 28.386 1.00 58.86 N ANISOU 1608 N ILE A 240 8834 8200 5330 -335 -13 987 N ATOM 1609 CA ILE A 240 -10.706 2.922 29.129 1.00 59.89 C ANISOU 1609 CA ILE A 240 8993 8461 5303 -373 218 931 C ATOM 1610 C ILE A 240 -11.844 1.934 29.400 1.00 65.69 C ANISOU 1610 C ILE A 240 9744 9203 6012 -469 380 1114 C ATOM 1611 O ILE A 240 -12.254 1.790 30.552 1.00 67.91 O ANISOU 1611 O ILE A 240 10163 9592 6046 -523 490 1186 O ATOM 1612 CB ILE A 240 -11.174 4.234 28.418 1.00 61.30 C ANISOU 1612 CB ILE A 240 9012 8651 5627 -326 333 725 C ATOM 1613 CG1 ILE A 240 -10.171 5.384 28.669 1.00 61.25 C ANISOU 1613 CG1 ILE A 240 9043 8681 5549 -253 217 542 C ATOM 1614 CG2 ILE A 240 -12.599 4.660 28.837 1.00 62.59 C ANISOU 1614 CG2 ILE A 240 9140 8910 5732 -371 608 697 C ATOM 1615 CD1 ILE A 240 -10.185 6.505 27.611 1.00 61.72 C ANISOU 1615 CD1 ILE A 240 8932 8688 5831 -193 232 364 C ATOM 1616 N VAL A 241 -12.313 1.229 28.347 1.00 61.04 N ANISOU 1616 N VAL A 241 9021 8498 5674 -493 388 1191 N ATOM 1617 CA VAL A 241 -13.382 0.228 28.435 1.00 61.89 C ANISOU 1617 CA VAL A 241 9116 8584 5815 -591 523 1368 C ATOM 1618 C VAL A 241 -12.957 -0.961 29.327 1.00 67.82 C ANISOU 1618 C VAL A 241 10052 9322 6393 -647 428 1581 C ATOM 1619 O VAL A 241 -13.748 -1.373 30.171 1.00 68.96 O ANISOU 1619 O VAL A 241 10276 9538 6386 -734 585 1708 O ATOM 1620 CB VAL A 241 -13.956 -0.169 27.041 1.00 63.63 C ANISOU 1620 CB VAL A 241 9147 8674 6354 -600 529 1378 C ATOM 1621 CG1 VAL A 241 -15.004 -1.278 27.147 1.00 64.57 C ANISOU 1621 CG1 VAL A 241 9253 8755 6527 -711 642 1569 C ATOM 1622 CG2 VAL A 241 -14.555 1.047 26.335 1.00 61.90 C ANISOU 1622 CG2 VAL A 241 8762 8486 6271 -557 648 1190 C ATOM 1623 N ARG A 242 -11.690 -1.432 29.209 1.00 64.89 N ANISOU 1623 N ARG A 242 9752 8867 6034 -594 176 1616 N ATOM 1624 CA ARG A 242 -11.133 -2.524 30.027 1.00 67.06 C ANISOU 1624 CA ARG A 242 10206 9113 6160 -630 43 1816 C ATOM 1625 C ARG A 242 -11.133 -2.168 31.523 1.00 74.35 C ANISOU 1625 C ARG A 242 11326 10198 6726 -662 108 1846 C ATOM 1626 O ARG A 242 -11.524 -3.006 32.337 1.00 75.82 O ANISOU 1626 O ARG A 242 11647 10407 6756 -747 161 2043 O ATOM 1627 CB ARG A 242 -9.708 -2.910 29.572 1.00 66.26 C ANISOU 1627 CB ARG A 242 10118 8895 6163 -546 -245 1809 C ATOM 1628 CG ARG A 242 -9.223 -4.259 30.120 1.00 76.26 C ANISOU 1628 CG ARG A 242 11530 10076 7368 -579 -403 2037 C ATOM 1629 CD ARG A 242 -7.712 -4.323 30.302 1.00 83.65 C ANISOU 1629 CD ARG A 242 12538 10970 8277 -490 -679 2015 C ATOM 1630 NE ARG A 242 -7.260 -3.592 31.490 1.00 92.83 N ANISOU 1630 NE ARG A 242 13853 12279 9140 -477 -713 1967 N ATOM 1631 CZ ARG A 242 -7.149 -4.119 32.708 1.00110.81 C ANISOU 1631 CZ ARG A 242 16339 14612 11154 -526 -763 2131 C ATOM 1632 NH1 ARG A 242 -7.451 -5.395 32.918 1.00100.91 N ANISOU 1632 NH1 ARG A 242 15162 13271 9909 -593 -783 2366 N ATOM 1633 NH2 ARG A 242 -6.738 -3.374 33.725 1.00 97.23 N ANISOU 1633 NH2 ARG A 242 14757 13029 9156 -511 -800 2062 N ATOM 1634 N ALA A 243 -10.701 -0.933 31.878 1.00 71.49 N ANISOU 1634 N ALA A 243 10987 9943 6232 -598 105 1651 N ATOM 1635 CA ALA A 243 -10.659 -0.460 33.268 1.00 73.99 C ANISOU 1635 CA ALA A 243 11498 10421 6196 -617 160 1639 C ATOM 1636 C ALA A 243 -12.058 -0.289 33.866 1.00 81.13 C ANISOU 1636 C ALA A 243 12417 11447 6961 -702 474 1670 C ATOM 1637 O ALA A 243 -12.249 -0.580 35.051 1.00 83.67 O ANISOU 1637 O ALA A 243 12929 11875 6985 -762 543 1782 O ATOM 1638 CB ALA A 243 -9.881 0.842 33.369 1.00 73.72 C ANISOU 1638 CB ALA A 243 11463 10450 6099 -527 72 1402 C ATOM 1639 N LEU A 244 -13.032 0.164 33.048 1.00 77.02 N ANISOU 1639 N LEU A 244 11695 10913 6658 -707 663 1575 N ATOM 1640 CA LEU A 244 -14.410 0.376 33.493 1.00 79.04 C ANISOU 1640 CA LEU A 244 11919 11276 6838 -779 974 1587 C ATOM 1641 C LEU A 244 -15.190 -0.924 33.682 1.00 86.25 C ANISOU 1641 C LEU A 244 12853 12151 7767 -898 1076 1844 C ATOM 1642 O LEU A 244 -15.847 -1.080 34.716 1.00 88.60 O ANISOU 1642 O LEU A 244 13266 12570 7829 -976 1268 1938 O ATOM 1643 CB LEU A 244 -15.170 1.349 32.576 1.00 77.34 C ANISOU 1643 CB LEU A 244 11472 11054 6861 -737 1123 1394 C ATOM 1644 CG LEU A 244 -14.715 2.817 32.594 1.00 81.36 C ANISOU 1644 CG LEU A 244 11962 11626 7324 -636 1102 1132 C ATOM 1645 CD1 LEU A 244 -15.267 3.567 31.402 1.00 79.13 C ANISOU 1645 CD1 LEU A 244 11440 11279 7348 -588 1170 980 C ATOM 1646 CD2 LEU A 244 -15.103 3.518 33.894 1.00 86.63 C ANISOU 1646 CD2 LEU A 244 12769 12473 7675 -648 1289 1051 C ATOM 1647 N ILE A 245 -15.110 -1.858 32.704 1.00 82.43 N ANISOU 1647 N ILE A 245 12265 11498 7557 -915 952 1957 N ATOM 1648 CA ILE A 245 -15.811 -3.154 32.754 1.00 84.21 C ANISOU 1648 CA ILE A 245 12496 11652 7848 -1031 1021 2203 C ATOM 1649 C ILE A 245 -15.331 -4.081 33.884 1.00 92.33 C ANISOU 1649 C ILE A 245 13772 12699 8608 -1093 937 2427 C ATOM 1650 O ILE A 245 -16.119 -4.888 34.383 1.00 93.87 O ANISOU 1650 O ILE A 245 14018 12905 8746 -1210 1081 2629 O ATOM 1651 CB ILE A 245 -15.940 -3.872 31.374 1.00 85.11 C ANISOU 1651 CB ILE A 245 12430 11573 8335 -1034 918 2242 C ATOM 1652 CG1 ILE A 245 -14.571 -4.366 30.830 1.00 84.02 C ANISOU 1652 CG1 ILE A 245 12338 11295 8290 -954 600 2252 C ATOM 1653 CG2 ILE A 245 -16.717 -3.008 30.360 1.00 83.61 C ANISOU 1653 CG2 ILE A 245 12001 11381 8385 -999 1047 2055 C ATOM 1654 CD1 ILE A 245 -14.627 -5.430 29.716 1.00 90.38 C ANISOU 1654 CD1 ILE A 245 13035 11901 9403 -974 483 2348 C ATOM 1655 N TYR A 246 -14.053 -3.945 34.294 1.00 90.41 N ANISOU 1655 N TYR A 246 13683 12463 8207 -1018 701 2396 N ATOM 1656 CA TYR A 246 -13.444 -4.736 35.365 1.00 93.49 C ANISOU 1656 CA TYR A 246 14322 12869 8333 -1058 574 2598 C ATOM 1657 C TYR A 246 -13.796 -4.253 36.784 1.00103.02 C ANISOU 1657 C TYR A 246 15724 14282 9135 -1107 748 2613 C ATOM 1658 O TYR A 246 -13.480 -4.949 37.754 1.00104.64 O ANISOU 1658 O TYR A 246 16153 14516 9090 -1160 675 2807 O ATOM 1659 CB TYR A 246 -11.922 -4.867 35.166 1.00 93.33 C ANISOU 1659 CB TYR A 246 14367 12754 8342 -956 228 2568 C ATOM 1660 CG TYR A 246 -11.514 -6.152 34.477 1.00 94.03 C ANISOU 1660 CG TYR A 246 14418 12634 8674 -963 34 2738 C ATOM 1661 CD1 TYR A 246 -11.249 -7.306 35.210 1.00 98.16 C ANISOU 1661 CD1 TYR A 246 15125 13100 9070 -1025 -79 2998 C ATOM 1662 CD2 TYR A 246 -11.388 -6.216 33.091 1.00 91.82 C ANISOU 1662 CD2 TYR A 246 13927 12210 8750 -906 -38 2638 C ATOM 1663 CE1 TYR A 246 -10.876 -8.495 34.582 1.00 98.05 C ANISOU 1663 CE1 TYR A 246 15078 12880 9298 -1025 -260 3147 C ATOM 1664 CE2 TYR A 246 -11.016 -7.398 32.451 1.00 92.13 C ANISOU 1664 CE2 TYR A 246 13938 12054 9014 -907 -211 2775 C ATOM 1665 CZ TYR A 246 -10.759 -8.535 33.202 1.00100.95 C ANISOU 1665 CZ TYR A 246 15232 13107 10020 -964 -323 3025 C ATOM 1666 OH TYR A 246 -10.385 -9.701 32.579 1.00100.32 O ANISOU 1666 OH TYR A 246 15123 12820 10175 -957 -498 3152 O ATOM 1667 N LYS A 247 -14.471 -3.086 36.907 1.00102.07 N ANISOU 1667 N LYS A 247 15527 14303 8950 -1088 979 2411 N ATOM 1668 CA LYS A 247 -14.885 -2.553 38.207 1.00106.08 C ANISOU 1668 CA LYS A 247 16212 15016 9077 -1128 1177 2392 C ATOM 1669 C LYS A 247 -16.405 -2.564 38.433 1.00115.27 C ANISOU 1669 C LYS A 247 17291 16271 10235 -1229 1550 2442 C ATOM 1670 O LYS A 247 -17.173 -2.259 37.515 1.00112.82 O ANISOU 1670 O LYS A 247 16735 15912 10218 -1222 1684 2346 O ATOM 1671 CB LYS A 247 -14.229 -1.191 38.526 1.00107.74 C ANISOU 1671 CB LYS A 247 16474 15337 9126 -1019 1116 2119 C ATOM 1672 CG LYS A 247 -14.805 0.023 37.807 1.00116.68 C ANISOU 1672 CG LYS A 247 17384 16496 10453 -954 1278 1851 C ATOM 1673 CD LYS A 247 -14.441 1.297 38.554 1.00126.15 C ANISOU 1673 CD LYS A 247 18694 17842 11396 -882 1299 1616 C ATOM 1674 CE LYS A 247 -15.176 2.505 38.035 1.00134.91 C ANISOU 1674 CE LYS A 247 19604 18990 12663 -827 1503 1366 C ATOM 1675 NZ LYS A 247 -14.931 3.699 38.884 1.00144.77 N ANISOU 1675 NZ LYS A 247 20980 20382 13645 -767 1547 1142 N ATOM 1676 N MET A1001 -16.826 -2.938 39.658 1.00 78.95 N ATOM 1677 CA MET A1001 -18.232 -3.017 40.075 1.00 80.13 C ATOM 1678 C MET A1001 -18.841 -1.626 40.297 1.00 85.53 C ATOM 1679 O MET A1001 -18.116 -0.680 40.612 1.00 84.92 O ATOM 1680 CB MET A1001 -18.378 -3.893 41.333 1.00 82.79 C ATOM 1681 CG MET A1001 -18.184 -5.370 41.064 1.00 86.91 C ATOM 1682 SD MET A1001 -17.623 -6.275 42.526 1.00 91.61 S ATOM 1683 CE MET A1001 -17.311 -7.881 41.803 1.00 88.30 C ATOM 1684 N LYS A1002 -20.173 -1.510 40.128 1.00 83.61 N ATOM 1685 CA LYS A1002 -20.910 -0.251 40.269 1.00 84.25 C ATOM 1686 C LYS A1002 -21.455 -0.018 41.686 1.00 89.40 C ATOM 1687 O LYS A1002 -21.879 -0.964 42.356 1.00 89.21 O ATOM 1688 CB LYS A1002 -22.033 -0.162 39.218 1.00 87.10 C ATOM 1689 CG LYS A1002 -22.451 1.267 38.868 1.00104.33 C ATOM 1690 CD LYS A1002 -22.999 1.371 37.446 1.00115.48 C ATOM 1691 CE LYS A1002 -23.627 2.714 37.148 1.00126.71 C ATOM 1692 NZ LYS A1002 -22.617 3.799 37.009 1.00135.73 N ATOM 1693 N LYS A1003 -21.445 1.258 42.124 1.00 86.39 N ATOM 1694 CA LYS A1003 -21.942 1.708 43.427 1.00 86.30 C ATOM 1695 C LYS A1003 -23.474 1.777 43.414 1.00 91.16 C ATOM 1696 O LYS A1003 -24.075 1.988 42.357 1.00 90.53 O ATOM 1697 CB LYS A1003 -21.362 3.089 43.788 1.00 88.56 C ATOM 1698 CG LYS A1003 -19.846 3.134 43.919 1.00101.19 C ATOM 1699 CD LYS A1003 -19.348 4.567 44.068 1.00111.07 C ATOM 1700 CE LYS A1003 -17.854 4.689 43.879 1.00122.77 C ATOM 1701 NZ LYS A1003 -17.454 4.557 42.451 1.00132.32 N ATOM 1702 N TYR A1004 -24.098 1.620 44.594 1.00 88.67 N ATOM 1703 CA TYR A1004 -25.551 1.658 44.763 1.00 88.84 C ATOM 1704 C TYR A1004 -25.966 2.695 45.809 1.00 92.73 C ATOM 1705 O TYR A1004 -25.334 2.792 46.860 1.00 92.19 O ATOM 1706 CB TYR A1004 -26.080 0.263 45.138 1.00 90.35 C ATOM 1707 CG TYR A1004 -26.283 -0.667 43.959 1.00 92.47 C ATOM 1708 CD1 TYR A1004 -25.206 -1.330 43.374 1.00 94.48 C ATOM 1709 CD2 TYR A1004 -27.556 -0.930 43.464 1.00 93.40 C ATOM 1710 CE1 TYR A1004 -25.388 -2.201 42.300 1.00 95.32 C ATOM 1711 CE2 TYR A1004 -27.752 -1.800 42.392 1.00 94.46 C ATOM 1712 CZ TYR A1004 -26.665 -2.437 41.815 1.00102.69 C ATOM 1713 OH TYR A1004 -26.852 -3.296 40.759 1.00104.61 O ATOM 1714 N THR A1005 -27.017 3.477 45.513 1.00 89.68 N ATOM 1715 CA THR A1005 -27.535 4.513 46.410 1.00 89.95 C ATOM 1716 C THR A1005 -28.958 4.230 46.892 1.00 94.36 C ATOM 1717 O THR A1005 -29.761 3.670 46.143 1.00 93.76 O ATOM 1718 CB THR A1005 -27.323 5.933 45.840 1.00100.14 C ATOM 1719 OG1 THR A1005 -27.597 6.899 46.856 1.00101.53 O ATOM 1720 CG2 THR A1005 -28.166 6.221 44.590 1.00 98.88 C ATOM 1721 N CYS A1006 -29.263 4.627 48.144 1.00 91.54 N ATOM 1722 CA CYS A1006 -30.581 4.439 48.751 1.00 91.52 C ATOM 1723 C CYS A1006 -31.542 5.567 48.361 1.00 96.04 C ATOM 1724 O CYS A1006 -31.195 6.745 48.468 1.00 95.24 O ATOM 1725 CB CYS A1006 -30.473 4.284 50.266 1.00 91.75 C ATOM 1726 SG CYS A1006 -32.030 3.834 51.081 1.00 95.59 S ATOM 1727 N THR A1007 -32.749 5.195 47.904 1.00 93.69 N ATOM 1728 CA THR A1007 -33.798 6.131 47.489 1.00 94.22 C ATOM 1729 C THR A1007 -34.531 6.736 48.694 1.00 99.83 C ATOM 1730 O THR A1007 -35.138 7.803 48.570 1.00 99.73 O ATOM 1731 CB THR A1007 -34.775 5.455 46.511 1.00103.40 C ATOM 1732 OG1 THR A1007 -35.278 4.251 47.096 1.00103.44 O ATOM 1733 CG2 THR A1007 -34.144 5.164 45.149 1.00101.90 C ATOM 1734 N VAL A1008 -34.471 6.052 49.854 1.00 97.32 N ATOM 1735 CA VAL A1008 -35.108 6.463 51.110 1.00 97.54 C ATOM 1736 C VAL A1008 -34.241 7.491 51.867 1.00102.13 C ATOM 1737 O VAL A1008 -34.755 8.541 52.259 1.00101.69 O ATOM 1738 CB VAL A1008 -35.481 5.238 52.004 1.00101.54 C ATOM 1739 CG1 VAL A1008 -36.225 5.669 53.268 1.00101.36 C ATOM 1740 CG2 VAL A1008 -36.303 4.210 51.229 1.00101.37 C ATOM 1741 N CYS A1009 -32.939 7.189 52.069 1.00 99.17 N ATOM 1742 CA CYS A1009 -32.027 8.054 52.818 1.00 99.37 C ATOM 1743 C CYS A1009 -30.990 8.821 51.993 1.00105.39 C ATOM 1744 O CYS A1009 -30.873 10.038 52.146 1.00105.13 O ATOM 1745 CB CYS A1009 -31.390 7.300 53.984 1.00 99.39 C ATOM 1746 SG CYS A1009 -29.974 6.262 53.538 1.00103.05 S ATOM 1747 N GLY A1010 -30.236 8.103 51.162 1.00103.43 N ATOM 1748 CA GLY A1010 -29.182 8.671 50.328 1.00103.81 C ATOM 1749 C GLY A1010 -27.802 8.085 50.564 1.00108.83 C ATOM 1750 O GLY A1010 -26.808 8.674 50.131 1.00108.42 O ATOM 1751 N TYR A1011 -27.724 6.923 51.249 1.00106.44 N ATOM 1752 CA TYR A1011 -26.459 6.238 51.531 1.00106.92 C ATOM 1753 C TYR A1011 -25.910 5.579 50.265 1.00113.05 C ATOM 1754 O TYR A1011 -26.636 4.854 49.582 1.00112.42 O ATOM 1755 CB TYR A1011 -26.613 5.215 52.685 1.00107.81 C ATOM 1756 CG TYR A1011 -25.506 4.183 52.774 1.00109.13 C ATOM 1757 CD1 TYR A1011 -24.271 4.501 53.334 1.00110.90 C ATOM 1758 CD2 TYR A1011 -25.697 2.884 52.310 1.00109.86 C ATOM 1759 CE1 TYR A1011 -23.247 3.557 53.412 1.00111.47 C ATOM 1760 CE2 TYR A1011 -24.677 1.935 52.371 1.00110.73 C ATOM 1761 CZ TYR A1011 -23.456 2.273 52.932 1.00117.83 C ATOM 1762 OH TYR A1011 -22.454 1.335 53.007 1.00118.38 O ATOM 1763 N ILE A1012 -24.626 5.823 49.972 1.00111.69 N ATOM 1764 CA ILE A1012 -23.944 5.258 48.811 1.00112.65 C ATOM 1765 C ILE A1012 -23.077 4.075 49.253 1.00119.12 C ATOM 1766 O ILE A1012 -22.126 4.254 50.020 1.00118.58 O ATOM 1767 CB ILE A1012 -23.157 6.344 48.009 1.00115.84 C ATOM 1768 CG1 ILE A1012 -24.099 7.426 47.441 1.00116.34 C ATOM 1769 CG2 ILE A1012 -22.304 5.732 46.890 1.00116.47 C ATOM 1770 CD1 ILE A1012 -24.010 8.758 48.146 1.00124.07 C ATOM 1771 N TYR A1013 -23.429 2.865 48.781 1.00117.89 N ATOM 1772 CA TYR A1013 -22.704 1.633 49.076 1.00118.73 C ATOM 1773 C TYR A1013 -21.587 1.443 48.049 1.00125.32 C ATOM 1774 O TYR A1013 -21.863 1.277 46.858 1.00124.91 O ATOM 1775 CB TYR A1013 -23.659 0.417 49.115 1.00119.84 C ATOM 1776 CG TYR A1013 -22.955 -0.925 49.137 1.00121.54 C ATOM 1777 CD1 TYR A1013 -22.419 -1.435 50.316 1.00123.46 C ATOM 1778 CD2 TYR A1013 -22.824 -1.685 47.978 1.00122.35 C ATOM 1779 CE1 TYR A1013 -21.756 -2.662 50.338 1.00124.26 C ATOM 1780 CE2 TYR A1013 -22.160 -2.910 47.986 1.00123.27 C ATOM 1781 CZ TYR A1013 -21.630 -3.398 49.170 1.00130.61 C ATOM 1782 OH TYR A1013 -20.983 -4.610 49.185 1.00131.23 O ATOM 1783 N ASN A1014 -20.330 1.481 48.513 1.00124.09 N ATOM 1784 CA ASN A1014 -19.156 1.290 47.665 1.00125.03 C ATOM 1785 C ASN A1014 -18.817 -0.211 47.632 1.00131.74 C ATOM 1786 O ASN A1014 -18.724 -0.820 48.703 1.00131.33 O ATOM 1787 CB ASN A1014 -17.971 2.112 48.192 1.00125.64 C ATOM 1788 CG ASN A1014 -16.922 2.446 47.156 1.00147.49 C ATOM 1789 OD1 ASN A1014 -16.312 1.567 46.532 1.00141.77 O ATOM 1790 ND2 ASN A1014 -16.646 3.731 46.993 1.00138.57 N ATOM 1791 N PRO A1015 -18.667 -0.842 46.438 1.00130.54 N ATOM 1792 CA PRO A1015 -18.357 -2.285 46.405 1.00131.24 C ATOM 1793 C PRO A1015 -16.983 -2.638 46.976 1.00137.75 C ATOM 1794 O PRO A1015 -16.832 -3.710 47.562 1.00137.32 O ATOM 1795 CB PRO A1015 -18.466 -2.646 44.917 1.00132.85 C ATOM 1796 CG PRO A1015 -19.153 -1.487 44.268 1.00136.96 C ATOM 1797 CD PRO A1015 -18.766 -0.293 45.073 1.00132.32 C ATOM 1798 N GLU A1016 -15.995 -1.732 46.823 1.00136.29 N ATOM 1799 CA GLU A1016 -14.630 -1.912 47.325 1.00137.03 C ATOM 1800 C GLU A1016 -14.542 -1.728 48.844 1.00143.00 C ATOM 1801 O GLU A1016 -13.831 -2.488 49.503 1.00142.52 O ATOM 1802 CB GLU A1016 -13.649 -0.982 46.596 1.00138.43 C ATOM 1803 CG GLU A1016 -13.271 -1.479 45.211 1.00149.31 C ATOM 1804 CD GLU A1016 -12.390 -0.542 44.410 1.00171.03 C ATOM 1805 OE1 GLU A1016 -12.868 -0.022 43.376 1.00166.35 O ATOM 1806 OE2 GLU A1016 -11.220 -0.335 44.806 1.00165.20 O ATOM 1807 N ASP A1017 -15.264 -0.729 49.395 1.00141.25 N ATOM 1808 CA ASP A1017 -15.296 -0.436 50.832 1.00141.87 C ATOM 1809 C ASP A1017 -16.157 -1.443 51.605 1.00147.68 C ATOM 1810 O ASP A1017 -15.778 -1.855 52.702 1.00147.22 O ATOM 1811 CB ASP A1017 -15.785 1.004 51.095 1.00143.71 C ATOM 1812 CG ASP A1017 -14.956 2.116 50.469 1.00153.72 C ATOM 1813 OD1 ASP A1017 -13.821 1.837 50.016 1.00154.23 O ATOM 1814 OD2 ASP A1017 -15.431 3.271 50.453 1.00159.44 O ATOM 1815 N GLY A1018 -17.303 -1.810 51.029 1.00145.89 N ATOM 1816 CA GLY A1018 -18.251 -2.755 51.609 1.00146.49 C ATOM 1817 C GLY A1018 -18.961 -2.244 52.846 1.00152.35 C ATOM 1818 O GLY A1018 -19.078 -1.030 53.044 1.00151.96 O ATOM 1819 N ASP A1019 -19.447 -3.179 53.684 1.00150.40 N ATOM 1820 CA ASP A1019 -20.147 -2.886 54.936 1.00150.92 C ATOM 1821 C ASP A1019 -19.815 -3.970 55.988 1.00156.50 C ATOM 1822 O ASP A1019 -20.581 -4.926 56.148 1.00156.06 O ATOM 1823 CB ASP A1019 -21.665 -2.747 54.694 1.00152.72 C ATOM 1824 CG ASP A1019 -22.421 -2.084 55.827 1.00162.35 C ATOM 1825 OD1 ASP A1019 -22.092 -0.924 56.165 1.00162.64 O ATOM 1826 OD2 ASP A1019 -23.378 -2.702 56.341 1.00168.40 O ATOM 1827 N PRO A1020 -18.655 -3.864 56.688 1.00154.47 N ATOM 1828 CA PRO A1020 -18.280 -4.911 57.659 1.00154.74 C ATOM 1829 C PRO A1020 -19.106 -4.958 58.946 1.00159.64 C ATOM 1830 O PRO A1020 -19.101 -5.988 59.622 1.00159.16 O ATOM 1831 CB PRO A1020 -16.796 -4.627 57.946 1.00156.49 C ATOM 1832 CG PRO A1020 -16.372 -3.583 56.945 1.00160.83 C ATOM 1833 CD PRO A1020 -17.611 -2.825 56.607 1.00156.25 C ATOM 1834 N ASP A1021 -19.806 -3.856 59.283 1.00157.08 N ATOM 1835 CA ASP A1021 -20.639 -3.733 60.484 1.00157.36 C ATOM 1836 C ASP A1021 -21.832 -4.694 60.506 1.00162.41 C ATOM 1837 O ASP A1021 -22.213 -5.156 61.582 1.00161.99 O ATOM 1838 CB ASP A1021 -21.113 -2.283 60.669 1.00159.20 C ATOM 1839 CG ASP A1021 -19.994 -1.298 60.942 1.00169.11 C ATOM 1840 OD1 ASP A1021 -19.214 -1.012 60.008 1.00169.59 O ATOM 1841 OD2 ASP A1021 -19.915 -0.793 62.082 1.00174.93 O ATOM 1842 N ASN A1022 -22.416 -4.990 59.327 1.00159.91 N ATOM 1843 CA ASN A1022 -23.567 -5.887 59.184 1.00160.17 C ATOM 1844 C ASN A1022 -23.194 -7.322 58.783 1.00165.11 C ATOM 1845 O ASN A1022 -23.917 -8.256 59.135 1.00164.69 O ATOM 1846 CB ASN A1022 -24.607 -5.296 58.224 1.00160.95 C ATOM 1847 CG ASN A1022 -25.364 -4.096 58.759 1.00182.85 C ATOM 1848 OD1 ASN A1022 -24.906 -3.364 59.647 1.00176.81 O ATOM 1849 ND2 ASN A1022 -26.541 -3.850 58.204 1.00174.25 N ATOM 1850 N GLY A1023 -22.087 -7.477 58.056 1.00162.50 N ATOM 1851 CA GLY A1023 -21.592 -8.776 57.611 1.00162.72 C ATOM 1852 C GLY A1023 -21.281 -8.874 56.129 1.00167.48 C ATOM 1853 O GLY A1023 -21.578 -9.896 55.504 1.00166.98 O ATOM 1854 N VAL A1024 -20.682 -7.808 55.556 1.00164.77 N ATOM 1855 CA VAL A1024 -20.295 -7.739 54.140 1.00164.91 C ATOM 1856 C VAL A1024 -18.790 -7.439 54.062 1.00169.64 C ATOM 1857 O VAL A1024 -18.346 -6.390 54.535 1.00169.17 O ATOM 1858 CB VAL A1024 -21.142 -6.719 53.316 1.00168.78 C ATOM 1859 CG1 VAL A1024 -20.807 -6.793 51.828 1.00168.55 C ATOM 1860 CG2 VAL A1024 -22.641 -6.922 53.531 1.00168.60 C ATOM 1861 N ASN A1025 -18.012 -8.370 53.483 1.00166.94 N ATOM 1862 CA ASN A1025 -16.559 -8.238 53.339 1.00167.11 C ATOM 1863 C ASN A1025 -16.176 -7.192 52.274 1.00171.89 C ATOM 1864 O ASN A1025 -16.821 -7.149 51.224 1.00171.43 O ATOM 1865 CB ASN A1025 -15.918 -9.597 53.032 1.00167.60 C ATOM 1866 CG ASN A1025 -15.990 -10.581 54.175 1.00187.68 C ATOM 1867 OD1 ASN A1025 -15.377 -10.397 55.233 1.00181.34 O ATOM 1868 ND2 ASN A1025 -16.717 -11.669 53.974 1.00178.84 N ATOM 1869 N PRO A1026 -15.139 -6.344 52.517 1.00169.17 N ATOM 1870 CA PRO A1026 -14.762 -5.329 51.515 1.00169.21 C ATOM 1871 C PRO A1026 -14.204 -5.927 50.223 1.00173.60 C ATOM 1872 O PRO A1026 -13.281 -6.744 50.260 1.00173.10 O ATOM 1873 CB PRO A1026 -13.718 -4.469 52.246 1.00170.96 C ATOM 1874 CG PRO A1026 -13.861 -4.813 53.696 1.00175.36 C ATOM 1875 CD PRO A1026 -14.280 -6.246 53.713 1.00170.86 C ATOM 1876 N GLY A1027 -14.794 -5.524 49.099 1.00170.62 N ATOM 1877 CA GLY A1027 -14.421 -5.992 47.768 1.00170.65 C ATOM 1878 C GLY A1027 -15.519 -6.757 47.052 1.00174.87 C ATOM 1879 O GLY A1027 -15.485 -6.878 45.824 1.00174.37 O ATOM 1880 N THR A1028 -16.501 -7.280 47.817 1.00171.75 N ATOM 1881 CA THR A1028 -17.633 -8.064 47.303 1.00171.64 C ATOM 1882 C THR A1028 -18.683 -7.213 46.579 1.00175.44 C ATOM 1883 O THR A1028 -18.872 -6.040 46.910 1.00174.89 O ATOM 1884 CB THR A1028 -18.269 -8.921 48.414 1.00179.87 C ATOM 1885 OG1 THR A1028 -18.668 -8.080 49.497 1.00179.54 O ATOM 1886 CG2 THR A1028 -17.346 -10.028 48.913 1.00178.47 C ATOM 1887 N ASP A1029 -19.374 -7.828 45.599 1.00172.03 N ATOM 1888 CA ASP A1029 -20.433 -7.217 44.790 1.00171.84 C ATOM 1889 C ASP A1029 -21.713 -7.009 45.614 1.00175.65 C ATOM 1890 O ASP A1029 -21.879 -7.640 46.661 1.00175.28 O ATOM 1891 CB ASP A1029 -20.717 -8.099 43.554 1.00173.65 C ATOM 1892 CG ASP A1029 -21.622 -7.480 42.504 1.00183.20 C ATOM 1893 OD1 ASP A1029 -21.264 -6.410 41.965 1.00183.67 O ATOM 1894 OD2 ASP A1029 -22.674 -8.078 42.203 1.00188.83 O ATOM 1895 N PHE A1030 -22.611 -6.122 45.136 1.00172.08 N ATOM 1896 CA PHE A1030 -23.896 -5.810 45.767 1.00171.83 C ATOM 1897 C PHE A1030 -24.841 -7.022 45.767 1.00175.78 C ATOM 1898 O PHE A1030 -25.602 -7.193 46.719 1.00175.42 O ATOM 1899 CB PHE A1030 -24.554 -4.599 45.077 1.00173.55 C ATOM 1900 CG PHE A1030 -25.840 -4.110 45.704 1.00174.99 C ATOM 1901 CD1 PHE A1030 -25.819 -3.304 46.836 1.00177.98 C ATOM 1902 CD2 PHE A1030 -27.070 -4.428 45.143 1.00177.08 C ATOM 1903 CE1 PHE A1030 -27.008 -2.847 47.411 1.00178.86 C ATOM 1904 CE2 PHE A1030 -28.259 -3.971 45.718 1.00179.86 C ATOM 1905 CZ PHE A1030 -28.219 -3.186 46.849 1.00177.93 C ATOM 1906 N LYS A1031 -24.780 -7.859 44.710 1.00172.26 N ATOM 1907 CA LYS A1031 -25.614 -9.058 44.553 1.00171.98 C ATOM 1908 C LYS A1031 -25.229 -10.198 45.513 1.00175.70 C ATOM 1909 O LYS A1031 -26.053 -11.081 45.762 1.00175.22 O ATOM 1910 CB LYS A1031 -25.604 -9.554 43.091 1.00174.45 C ATOM 1911 CG LYS A1031 -26.062 -8.531 42.046 1.00188.56 C ATOM 1912 CD LYS A1031 -27.584 -8.431 41.921 1.00198.50 C ATOM 1913 CE LYS A1031 -28.125 -7.110 42.417 1.00209.15 C ATOM 1914 NZ LYS A1031 -27.801 -5.987 41.497 1.00218.16 N ATOM 1915 N ASP A1032 -23.987 -10.175 46.048 1.00172.25 N ATOM 1916 CA ASP A1032 -23.452 -11.183 46.974 1.00172.06 C ATOM 1917 C ASP A1032 -24.146 -11.196 48.347 1.00175.75 C ATOM 1918 O ASP A1032 -24.112 -12.222 49.031 1.00175.26 O ATOM 1919 CB ASP A1032 -21.927 -11.014 47.151 1.00173.91 C ATOM 1920 CG ASP A1032 -21.095 -11.093 45.879 1.00183.93 C ATOM 1921 OD1 ASP A1032 -21.539 -11.754 44.913 1.00184.48 O ATOM 1922 OD2 ASP A1032 -19.979 -10.533 45.868 1.00189.69 O ATOM 1923 N ILE A1033 -24.761 -10.064 48.749 1.00172.16 N ATOM 1924 CA ILE A1033 -25.458 -9.911 50.031 1.00199.91 C ATOM 1925 C ILE A1033 -26.786 -10.674 50.004 1.00222.20 C ATOM 1926 O ILE A1033 -27.075 -11.440 50.920 1.00180.90 O ATOM 1927 CB ILE A1033 -25.647 -8.412 50.415 1.00203.02 C ATOM 1928 CG1 ILE A1033 -24.343 -7.600 50.214 1.00203.43 C ATOM 1929 CG2 ILE A1033 -26.169 -8.270 51.855 1.00203.82 C ATOM 1930 CD1 ILE A1033 -24.542 -6.141 49.809 1.00210.69 C ATOM 1931 N VAL A1038 -29.736 -5.141 54.416 1.00105.76 N ATOM 1932 CA VAL A1038 -30.289 -3.931 55.029 1.00105.65 C ATOM 1933 C VAL A1038 -29.301 -2.757 55.040 1.00108.82 C ATOM 1934 O VAL A1038 -28.103 -2.961 55.254 1.00108.23 O ATOM 1935 CB VAL A1038 -30.938 -4.167 56.422 1.00109.87 C ATOM 1936 CG1 VAL A1038 -32.253 -4.932 56.300 1.00109.76 C ATOM 1937 CG2 VAL A1038 -29.981 -4.864 57.392 1.00109.75 C ATOM 1938 N CYS A1039 -29.817 -1.531 54.820 1.00105.05 N ATOM 1939 CA CYS A1039 -29.037 -0.291 54.793 1.00104.81 C ATOM 1940 C CYS A1039 -28.482 0.055 56.189 1.00109.56 C ATOM 1941 O CYS A1039 -29.255 0.078 57.149 1.00109.17 O ATOM 1942 CB CYS A1039 -29.864 0.857 54.215 1.00104.86 C ATOM 1943 SG CYS A1039 -28.955 2.416 54.025 1.00108.57 S ATOM 1944 N PRO A1040 -27.158 0.333 56.328 1.00106.73 N ATOM 1945 CA PRO A1040 -26.613 0.666 57.660 1.00106.79 C ATOM 1946 C PRO A1040 -27.087 2.009 58.222 1.00111.36 C ATOM 1947 O PRO A1040 -27.104 2.181 59.441 1.00110.91 O ATOM 1948 CB PRO A1040 -25.099 0.650 57.438 1.00108.50 C ATOM 1949 CG PRO A1040 -24.927 0.961 56.001 1.00112.88 C ATOM 1950 CD PRO A1040 -26.098 0.336 55.300 1.00108.34 C ATOM 1951 N LEU A1041 -27.471 2.950 57.339 1.00108.63 N ATOM 1952 CA LEU A1041 -27.949 4.274 57.730 1.00108.84 C ATOM 1953 C LEU A1041 -29.402 4.261 58.223 1.00113.23 C ATOM 1954 O LEU A1041 -29.613 4.319 59.435 1.00113.03 O ATOM 1955 CB LEU A1041 -27.720 5.308 56.610 1.00108.99 C ATOM 1956 CG LEU A1041 -26.658 6.376 56.886 1.00113.82 C ATOM 1957 CD1 LEU A1041 -25.248 5.838 56.656 1.00114.05 C ATOM 1958 CD2 LEU A1041 -26.884 7.599 56.018 1.00116.30 C ATOM 1959 N CYS A1042 -30.393 4.156 57.311 1.00109.93 N ATOM 1960 CA CYS A1042 -31.813 4.148 57.678 1.00110.01 C ATOM 1961 C CYS A1042 -32.328 2.789 58.174 1.00113.75 C ATOM 1962 O CYS A1042 -32.969 2.733 59.225 1.00113.26 O ATOM 1963 CB CYS A1042 -32.685 4.722 56.565 1.00110.49 C ATOM 1964 SG CYS A1042 -32.622 3.794 55.011 1.00114.47 S ATOM 1965 N GLY A1043 -32.044 1.723 57.425 1.00110.14 N ATOM 1966 CA GLY A1043 -32.451 0.367 57.783 1.00109.86 C ATOM 1967 C GLY A1043 -33.326 -0.364 56.785 1.00113.37 C ATOM 1968 O GLY A1043 -33.748 -1.492 57.060 1.00112.85 O ATOM 1969 N VAL A1044 -33.607 0.258 55.621 1.00109.79 N ATOM 1970 CA VAL A1044 -34.446 -0.346 54.574 1.00109.55 C ATOM 1971 C VAL A1044 -33.723 -1.480 53.821 1.00112.86 C ATOM 1972 O VAL A1044 -32.492 -1.558 53.858 1.00112.23 O ATOM 1973 CB VAL A1044 -35.122 0.685 53.621 1.00113.55 C ATOM 1974 CG1 VAL A1044 -35.944 1.715 54.395 1.00113.38 C ATOM 1975 CG2 VAL A1044 -34.108 1.365 52.707 1.00113.36 C ATOM 1976 N GLY A1045 -34.502 -2.329 53.147 1.00109.15 N ATOM 1977 CA GLY A1045 -34.003 -3.461 52.372 1.00108.75 C ATOM 1978 C GLY A1045 -33.265 -3.084 51.102 1.00112.05 C ATOM 1979 O GLY A1045 -33.218 -1.908 50.725 1.00111.80 O ATOM 1980 N LYS A1046 -32.694 -4.098 50.424 1.00107.99 N ATOM 1981 CA LYS A1046 -31.929 -3.955 49.177 1.00107.48 C ATOM 1982 C LYS A1046 -32.765 -3.454 47.989 1.00110.58 C ATOM 1983 O LYS A1046 -32.207 -2.858 47.065 1.00110.09 O ATOM 1984 CB LYS A1046 -31.238 -5.277 48.814 1.00110.00 C ATOM 1985 CG LYS A1046 -30.049 -5.626 49.708 1.00125.73 C ATOM 1986 CD LYS A1046 -29.514 -7.032 49.436 1.00137.08 C ATOM 1987 CE LYS A1046 -28.574 -7.094 48.254 1.00149.25 C ATOM 1988 NZ LYS A1046 -28.172 -8.489 47.939 1.00158.86 N ATOM 1989 N ASP A1047 -34.093 -3.695 48.020 1.00106.55 N ATOM 1990 CA ASP A1047 -35.061 -3.307 46.985 1.00106.05 C ATOM 1991 C ASP A1047 -35.162 -1.792 46.749 1.00108.40 C ATOM 1992 O ASP A1047 -35.557 -1.372 45.658 1.00107.82 O ATOM 1993 CB ASP A1047 -36.450 -3.901 47.294 1.00108.13 C ATOM 1994 CG ASP A1047 -37.033 -3.473 48.629 1.00119.27 C ATOM 1995 OD1 ASP A1047 -36.566 -3.982 49.672 1.00119.86 O ATOM 1996 OD2 ASP A1047 -37.971 -2.646 48.629 1.00125.48 O ATOM 1997 N GLN A1048 -34.803 -0.983 47.767 1.00103.95 N ATOM 1998 CA GLN A1048 -34.845 0.483 47.717 1.00103.20 C ATOM 1999 C GLN A1048 -33.522 1.120 47.238 1.00105.20 C ATOM 2000 O GLN A1048 -33.337 2.333 47.380 1.00104.64 O ATOM 2001 CB GLN A1048 -35.294 1.060 49.078 1.00104.64 C ATOM 2002 CG GLN A1048 -36.721 0.682 49.502 1.00121.24 C ATOM 2003 CD GLN A1048 -37.799 1.196 48.571 1.00140.43 C ATOM 2004 OE1 GLN A1048 -37.891 2.393 48.270 1.00135.58 O ATOM 2005 NE2 GLN A1048 -38.655 0.296 48.112 1.00132.48 N ATOM 2006 N PHE A1049 -32.624 0.307 46.645 1.00100.38 N ATOM 2007 CA PHE A1049 -31.324 0.751 46.136 1.00 99.43 C ATOM 2008 C PHE A1049 -31.245 0.759 44.606 1.00101.68 C ATOM 2009 O PHE A1049 -31.723 -0.173 43.955 1.00101.18 O ATOM 2010 CB PHE A1049 -30.195 -0.113 46.717 1.00101.13 C ATOM 2011 CG PHE A1049 -29.719 0.278 48.096 1.00102.66 C ATOM 2012 CD1 PHE A1049 -30.437 -0.091 49.228 1.00105.72 C ATOM 2013 CD2 PHE A1049 -28.527 0.970 48.266 1.00104.80 C ATOM 2014 CE1 PHE A1049 -29.987 0.259 50.504 1.00106.63 C ATOM 2015 CE2 PHE A1049 -28.077 1.316 49.543 1.00107.60 C ATOM 2016 CZ PHE A1049 -28.808 0.957 50.653 1.00105.67 C ATOM 2017 N GLU A1050 -30.619 1.810 44.045 1.00 96.98 N ATOM 2018 CA GLU A1050 -30.399 1.990 42.604 1.00 96.23 C ATOM 2019 C GLU A1050 -28.947 2.395 42.314 1.00 98.96 C ATOM 2020 O GLU A1050 -28.303 3.000 43.172 1.00 98.33 O ATOM 2021 CB GLU A1050 -31.401 2.994 41.993 1.00 97.57 C ATOM 2022 CG GLU A1050 -31.299 4.421 42.521 1.00107.83 C ATOM 2023 CD GLU A1050 -32.024 5.502 41.739 1.00126.72 C ATOM 2024 OE1 GLU A1050 -32.893 5.169 40.900 1.00119.96 O ATOM 2025 OE2 GLU A1050 -31.732 6.694 41.985 1.00119.51 O ATOM 2026 N GLU A1051 -28.440 2.064 41.107 1.00 95.05 N ATOM 2027 CA GLU A1051 -27.069 2.362 40.668 1.00 94.75 C ATOM 2028 C GLU A1051 -26.749 3.862 40.641 1.00 98.46 C ATOM 2029 O GLU A1051 -27.536 4.652 40.115 1.00 98.03 O ATOM 2030 CB GLU A1051 -26.777 1.715 39.305 1.00 96.07 C ATOM 2031 CG GLU A1051 -26.403 0.243 39.395 1.00104.64 C ATOM 2032 CD GLU A1051 -26.393 -0.531 38.088 1.00118.21 C ATOM 2033 OE1 GLU A1051 -26.108 0.073 37.028 1.00108.72 O ATOM 2034 OE2 GLU A1051 -26.650 -1.756 38.130 1.00106.76 O ATOM 2035 N VAL A1052 -25.595 4.241 41.226 1.00 94.92 N ATOM 2036 CA VAL A1052 -25.108 5.625 41.325 1.00 94.76 C ATOM 2037 C VAL A1052 -24.655 6.138 39.952 1.00 98.10 C ATOM 2038 O VAL A1052 -24.014 5.399 39.199 1.00 97.95 O ATOM 2039 CB VAL A1052 -23.976 5.766 42.393 1.00 98.93 C ATOM 2040 CG1 VAL A1052 -23.498 7.212 42.537 1.00 98.76 C ATOM 2041 CG2 VAL A1052 -24.423 5.229 43.746 1.00 98.82 C ATOM 2042 N GLU A1053 -24.985 7.411 39.641 1.00 93.57 N ATOM 2043 CA GLU A1053 -24.588 8.090 38.408 1.00 92.58 C ATOM 2044 C GLU A1053 -23.105 8.452 38.519 1.00 93.83 C ATOM 2045 O GLU A1053 -22.740 9.305 39.336 1.00 93.69 O ATOM 2046 CB GLU A1053 -25.439 9.354 38.181 1.00 94.00 C ATOM 2047 CG GLU A1053 -26.809 9.072 37.589 1.00105.56 C ATOM 2048 CD GLU A1053 -27.112 9.795 36.289 1.00129.08 C ATOM 2049 OE1 GLU A1053 -26.283 9.718 35.353 1.00125.37 O ATOM 2050 OE2 GLU A1053 -28.199 10.408 36.195 1.00123.39 O ATOM 2051 N GLU A1054 -22.248 7.758 37.746 1.00 87.64 N ATOM 2052 CA GLU A1054 -20.802 7.995 37.754 1.00 86.03 C ATOM 2053 C GLU A1054 -20.456 9.034 36.674 1.00 85.52 C ATOM 2054 O GLU A1054 -20.689 8.767 35.490 1.00 85.24 O ATOM 2055 CB GLU A1054 -20.014 6.685 37.570 1.00 87.53 C ATOM 2056 CG GLU A1054 -20.158 5.716 38.732 1.00 99.06 C ATOM 2057 CD GLU A1054 -19.134 4.599 38.791 1.00124.61 C ATOM 2058 OE1 GLU A1054 -18.607 4.343 39.897 1.00124.26 O ATOM 2059 OE2 GLU A1054 -18.863 3.974 37.739 1.00119.11 O ATOM 2060 N PRO A 253 -19.971 10.244 37.060 1.00109.38 N ANISOU 2060 N PRO A 253 15456 16061 10042 -429 2817 -153 N ATOM 2061 CA PRO A 253 -19.699 11.287 36.051 1.00104.96 C ANISOU 2061 CA PRO A 253 14728 15378 9775 -326 2690 -350 C ATOM 2062 C PRO A 253 -18.583 10.965 35.061 1.00100.84 C ANISOU 2062 C PRO A 253 14179 14702 9433 -310 2353 -281 C ATOM 2063 O PRO A 253 -18.746 11.241 33.876 1.00 97.78 O ANISOU 2063 O PRO A 253 13585 14190 9379 -273 2293 -314 O ATOM 2064 CB PRO A 253 -19.384 12.536 36.888 1.00108.55 C ANISOU 2064 CB PRO A 253 15312 15917 10014 -246 2730 -615 C ATOM 2065 CG PRO A 253 -19.828 12.214 38.275 1.00117.03 C ANISOU 2065 CG PRO A 253 16574 17178 10716 -303 2966 -576 C ATOM 2066 CD PRO A 253 -19.682 10.738 38.420 1.00113.11 C ANISOU 2066 CD PRO A 253 16175 16690 10112 -414 2895 -272 C ATOM 2067 N LEU A 254 -17.466 10.380 35.541 1.00 94.01 N ANISOU 2067 N LEU A 254 13520 13848 8352 -337 2137 -183 N ATOM 2068 CA LEU A 254 -16.313 10.018 34.715 1.00 89.46 C ANISOU 2068 CA LEU A 254 12928 13135 7926 -320 1821 -118 C ATOM 2069 C LEU A 254 -16.628 8.879 33.747 1.00 87.73 C ANISOU 2069 C LEU A 254 12571 12810 7952 -378 1784 100 C ATOM 2070 O LEU A 254 -16.196 8.939 32.598 1.00 84.31 O ANISOU 2070 O LEU A 254 12004 12243 7786 -341 1619 87 O ATOM 2071 CB LEU A 254 -15.076 9.703 35.586 1.00 90.45 C ANISOU 2071 CB LEU A 254 13305 13306 7755 -329 1604 -79 C ATOM 2072 CG LEU A 254 -13.720 9.492 34.876 1.00 92.84 C ANISOU 2072 CG LEU A 254 13603 13481 8192 -297 1269 -47 C ATOM 2073 CD1 LEU A 254 -13.292 10.714 34.063 1.00 90.92 C ANISOU 2073 CD1 LEU A 254 13221 13148 8176 -209 1171 -265 C ATOM 2074 CD2 LEU A 254 -12.635 9.141 35.871 1.00 97.00 C ANISOU 2074 CD2 LEU A 254 14376 14067 8414 -310 1074 3 C ATOM 2075 N ARG A 255 -17.396 7.866 34.201 1.00 83.19 N ANISOU 2075 N ARG A 255 12027 12291 7289 -471 1944 294 N ATOM 2076 CA ARG A 255 -17.813 6.709 33.399 1.00 80.45 C ANISOU 2076 CA ARG A 255 11562 11846 7161 -540 1928 506 C ATOM 2077 C ARG A 255 -18.733 7.131 32.244 1.00 79.16 C ANISOU 2077 C ARG A 255 11126 11601 7351 -515 2033 433 C ATOM 2078 O ARG A 255 -18.552 6.655 31.122 1.00 76.49 O ANISOU 2078 O ARG A 255 10666 11129 7267 -517 1890 505 O ATOM 2079 CB ARG A 255 -18.514 5.670 34.291 1.00 83.60 C ANISOU 2079 CB ARG A 255 12065 12334 7364 -653 2104 717 C ATOM 2080 CG ARG A 255 -18.789 4.328 33.618 1.00 93.99 C ANISOU 2080 CG ARG A 255 13299 13539 8875 -737 2057 956 C ATOM 2081 CD ARG A 255 -19.677 3.451 34.479 1.00107.99 C ANISOU 2081 CD ARG A 255 15146 15402 10483 -856 2279 1152 C ATOM 2082 NE ARG A 255 -19.390 2.028 34.293 1.00116.98 N ANISOU 2082 NE ARG A 255 16340 16441 11666 -940 2140 1409 N ATOM 2083 CZ ARG A 255 -18.583 1.315 35.072 1.00132.78 C ANISOU 2083 CZ ARG A 255 18574 18460 13417 -975 2002 1558 C ATOM 2084 NH1 ARG A 255 -17.972 1.883 36.105 1.00120.92 N ANISOU 2084 NH1 ARG A 255 17277 17081 11585 -939 1978 1476 N ATOM 2085 NH2 ARG A 255 -18.383 0.028 34.827 1.00120.57 N ANISOU 2085 NH2 ARG A 255 17059 16802 11952 -1046 1876 1789 N ATOM 2086 N ARG A 256 -19.714 8.012 32.529 1.00 74.33 N ANISOU 2086 N ARG A 256 10423 11070 6748 -489 2278 289 N ATOM 2087 CA ARG A 256 -20.692 8.529 31.569 1.00 72.03 C ANISOU 2087 CA ARG A 256 9874 10716 6779 -458 2392 206 C ATOM 2088 C ARG A 256 -20.017 9.385 30.486 1.00 72.08 C ANISOU 2088 C ARG A 256 9783 10601 7002 -361 2188 55 C ATOM 2089 O ARG A 256 -20.272 9.172 29.301 1.00 69.62 O ANISOU 2089 O ARG A 256 9301 10173 6978 -358 2115 97 O ATOM 2090 CB ARG A 256 -21.783 9.323 32.309 1.00 73.03 C ANISOU 2090 CB ARG A 256 9948 10967 6833 -441 2700 73 C ATOM 2091 CG ARG A 256 -22.949 9.774 31.434 1.00 79.96 C ANISOU 2091 CG ARG A 256 10547 11787 8049 -415 2839 8 C ATOM 2092 CD ARG A 256 -23.921 10.677 32.174 1.00 93.86 C ANISOU 2092 CD ARG A 256 12246 13662 9754 -376 3134 -155 C ATOM 2093 NE ARG A 256 -23.316 11.953 32.565 1.00106.10 N ANISOU 2093 NE ARG A 256 13888 15239 11185 -269 3094 -398 N ATOM 2094 CZ ARG A 256 -23.054 12.311 33.819 1.00124.05 C ANISOU 2094 CZ ARG A 256 16363 17647 13122 -258 3195 -491 C ATOM 2095 NH1 ARG A 256 -23.345 11.494 34.826 1.00113.85 N ANISOU 2095 NH1 ARG A 256 15210 16485 11562 -348 3352 -351 N ATOM 2096 NH2 ARG A 256 -22.503 13.490 34.078 1.00110.24 N ANISOU 2096 NH2 ARG A 256 14685 15902 11299 -161 3138 -723 N ATOM 2097 N LYS A 257 -19.147 10.332 30.899 1.00 67.96 N ANISOU 2097 N LYS A 257 9379 10107 6338 -288 2092 -114 N ATOM 2098 CA LYS A 257 -18.397 11.236 30.020 1.00 64.94 C ANISOU 2098 CA LYS A 257 8927 9617 6131 -201 1903 -260 C ATOM 2099 C LYS A 257 -17.393 10.473 29.157 1.00 66.27 C ANISOU 2099 C LYS A 257 9104 9670 6406 -216 1639 -135 C ATOM 2100 O LYS A 257 -17.148 10.876 28.020 1.00 63.83 O ANISOU 2100 O LYS A 257 8665 9248 6339 -170 1523 -187 O ATOM 2101 CB LYS A 257 -17.690 12.336 30.833 1.00 67.94 C ANISOU 2101 CB LYS A 257 9445 10056 6313 -135 1866 -463 C ATOM 2102 CG LYS A 257 -18.635 13.402 31.379 1.00 76.56 C ANISOU 2102 CG LYS A 257 10485 11224 7381 -88 2109 -649 C ATOM 2103 CD LYS A 257 -17.915 14.382 32.291 1.00 85.32 C ANISOU 2103 CD LYS A 257 11760 12394 8263 -31 2067 -849 C ATOM 2104 CE LYS A 257 -18.886 15.281 33.019 1.00 98.62 C ANISOU 2104 CE LYS A 257 13426 14172 9875 12 2335 -1028 C ATOM 2105 NZ LYS A 257 -18.186 16.303 33.844 1.00108.34 N ANISOU 2105 NZ LYS A 257 14814 15443 10906 73 2279 -1249 N ATOM 2106 N SER A 258 -16.823 9.370 29.694 1.00 63.13 N ANISOU 2106 N SER A 258 8859 9298 5828 -277 1548 31 N ATOM 2107 CA SER A 258 -15.873 8.516 28.982 1.00 60.83 C ANISOU 2107 CA SER A 258 8584 8900 5630 -289 1309 156 C ATOM 2108 C SER A 258 -16.563 7.701 27.902 1.00 62.53 C ANISOU 2108 C SER A 258 8638 9018 6102 -330 1327 287 C ATOM 2109 O SER A 258 -16.061 7.676 26.783 1.00 59.47 O ANISOU 2109 O SER A 258 8162 8516 5917 -297 1170 278 O ATOM 2110 CB SER A 258 -15.111 7.607 29.940 1.00 65.34 C ANISOU 2110 CB SER A 258 9365 9520 5940 -335 1206 293 C ATOM 2111 OG SER A 258 -14.166 8.360 30.679 1.00 74.93 O ANISOU 2111 OG SER A 258 10722 10793 6954 -286 1104 163 O ATOM 2112 N ILE A 259 -17.716 7.061 28.213 1.00 60.78 N ANISOU 2112 N ILE A 259 8376 8841 5876 -405 1520 402 N ATOM 2113 CA ILE A 259 -18.465 6.276 27.222 1.00 60.01 C ANISOU 2113 CA ILE A 259 8121 8649 6032 -454 1536 522 C ATOM 2114 C ILE A 259 -18.992 7.155 26.087 1.00 60.70 C ANISOU 2114 C ILE A 259 8003 8667 6394 -395 1552 390 C ATOM 2115 O ILE A 259 -18.876 6.762 24.925 1.00 58.08 O ANISOU 2115 O ILE A 259 7576 8219 6274 -393 1423 435 O ATOM 2116 CB ILE A 259 -19.514 5.268 27.789 1.00 65.85 C ANISOU 2116 CB ILE A 259 8857 9435 6726 -562 1717 699 C ATOM 2117 CG1 ILE A 259 -20.720 5.954 28.456 1.00 69.04 C ANISOU 2117 CG1 ILE A 259 9189 9958 7087 -573 2005 619 C ATOM 2118 CG2 ILE A 259 -18.875 4.222 28.708 1.00 68.48 C ANISOU 2118 CG2 ILE A 259 9401 9802 6816 -625 1649 869 C ATOM 2119 CD1 ILE A 259 -21.989 5.930 27.605 1.00 79.09 C ANISOU 2119 CD1 ILE A 259 10218 11176 8657 -596 2127 628 C ATOM 2120 N TYR A 260 -19.508 8.366 26.423 1.00 57.27 N ANISOU 2120 N TYR A 260 7513 8299 5948 -341 1698 221 N ATOM 2121 CA TYR A 260 -20.001 9.340 25.444 1.00 55.66 C ANISOU 2121 CA TYR A 260 7124 8027 5996 -276 1709 89 C ATOM 2122 C TYR A 260 -18.886 9.714 24.467 1.00 54.76 C ANISOU 2122 C TYR A 260 7013 7808 5985 -215 1471 30 C ATOM 2123 O TYR A 260 -19.101 9.652 23.261 1.00 52.02 O ANISOU 2123 O TYR A 260 6535 7361 5871 -204 1394 48 O ATOM 2124 CB TYR A 260 -20.592 10.595 26.115 1.00 58.60 C ANISOU 2124 CB TYR A 260 7461 8483 6319 -218 1893 -92 C ATOM 2125 CG TYR A 260 -22.064 10.493 26.455 1.00 63.50 C ANISOU 2125 CG TYR A 260 7954 9167 7007 -257 2151 -68 C ATOM 2126 CD1 TYR A 260 -23.005 10.157 25.484 1.00 65.28 C ANISOU 2126 CD1 TYR A 260 7977 9315 7511 -283 2176 0 C ATOM 2127 CD2 TYR A 260 -22.529 10.810 27.728 1.00 66.96 C ANISOU 2127 CD2 TYR A 260 8464 9742 7235 -262 2372 -130 C ATOM 2128 CE1 TYR A 260 -24.363 10.078 25.788 1.00 68.46 C ANISOU 2128 CE1 TYR A 260 8238 9773 8001 -319 2411 20 C ATOM 2129 CE2 TYR A 260 -23.886 10.747 28.041 1.00 69.98 C ANISOU 2129 CE2 TYR A 260 8711 10187 7691 -296 2628 -114 C ATOM 2130 CZ TYR A 260 -24.800 10.381 27.067 1.00 78.48 C ANISOU 2130 CZ TYR A 260 9569 11181 9068 -325 2646 -37 C ATOM 2131 OH TYR A 260 -26.136 10.315 27.376 1.00 83.89 O ANISOU 2131 OH TYR A 260 10101 11926 9847 -361 2898 -20 O ATOM 2132 N LEU A 261 -17.681 10.008 24.992 1.00 50.20 N ANISOU 2132 N LEU A 261 6588 7255 5229 -182 1351 -28 N ATOM 2133 CA LEU A 261 -16.500 10.330 24.193 1.00 47.28 C ANISOU 2133 CA LEU A 261 6230 6796 4938 -131 1133 -78 C ATOM 2134 C LEU A 261 -16.116 9.153 23.288 1.00 48.69 C ANISOU 2134 C LEU A 261 6389 6882 5228 -167 988 75 C ATOM 2135 O LEU A 261 -15.885 9.363 22.100 1.00 46.56 O ANISOU 2135 O LEU A 261 6026 6516 5148 -136 885 50 O ATOM 2136 CB LEU A 261 -15.323 10.742 25.099 1.00 47.69 C ANISOU 2136 CB LEU A 261 6450 6902 4768 -103 1037 -154 C ATOM 2137 CG LEU A 261 -13.994 11.053 24.401 1.00 50.18 C ANISOU 2137 CG LEU A 261 6777 7132 5156 -57 815 -202 C ATOM 2138 CD1 LEU A 261 -14.041 12.391 23.696 1.00 49.41 C ANISOU 2138 CD1 LEU A 261 6569 6978 5227 7 813 -361 C ATOM 2139 CD2 LEU A 261 -12.838 10.997 25.376 1.00 52.80 C ANISOU 2139 CD2 LEU A 261 7281 7518 5264 -53 697 -220 C ATOM 2140 N VAL A 262 -16.080 7.921 23.844 1.00 45.40 N ANISOU 2140 N VAL A 262 6067 6490 4694 -234 984 233 N ATOM 2141 CA VAL A 262 -15.748 6.699 23.106 1.00 43.69 C ANISOU 2141 CA VAL A 262 5845 6179 4575 -270 852 378 C ATOM 2142 C VAL A 262 -16.730 6.520 21.930 1.00 47.07 C ANISOU 2142 C VAL A 262 6101 6528 5256 -288 892 404 C ATOM 2143 O VAL A 262 -16.289 6.439 20.786 1.00 44.30 O ANISOU 2143 O VAL A 262 5694 6080 5057 -259 757 395 O ATOM 2144 CB VAL A 262 -15.657 5.465 24.049 1.00 48.33 C ANISOU 2144 CB VAL A 262 6570 6805 4990 -342 857 547 C ATOM 2145 CG1 VAL A 262 -15.668 4.146 23.274 1.00 47.23 C ANISOU 2145 CG1 VAL A 262 6400 6554 4990 -389 759 700 C ATOM 2146 CG2 VAL A 262 -14.420 5.553 24.940 1.00 48.38 C ANISOU 2146 CG2 VAL A 262 6750 6861 4773 -315 739 529 C ATOM 2147 N ILE A 263 -18.051 6.580 22.213 1.00 45.82 N ANISOU 2147 N ILE A 263 5853 6415 5139 -329 1080 420 N ATOM 2148 CA ILE A 263 -19.130 6.450 21.228 1.00 45.02 C ANISOU 2148 CA ILE A 263 5578 6248 5279 -351 1125 443 C ATOM 2149 C ILE A 263 -19.059 7.517 20.129 1.00 47.61 C ANISOU 2149 C ILE A 263 5796 6515 5780 -273 1055 309 C ATOM 2150 O ILE A 263 -19.008 7.146 18.958 1.00 45.95 O ANISOU 2150 O ILE A 263 5521 6206 5731 -273 936 343 O ATOM 2151 CB ILE A 263 -20.526 6.367 21.912 1.00 49.76 C ANISOU 2151 CB ILE A 263 6096 6922 5886 -410 1353 483 C ATOM 2152 CG1 ILE A 263 -20.671 5.044 22.711 1.00 51.21 C ANISOU 2152 CG1 ILE A 263 6377 7135 5945 -510 1403 664 C ATOM 2153 CG2 ILE A 263 -21.676 6.538 20.892 1.00 49.88 C ANISOU 2153 CG2 ILE A 263 5902 6873 6175 -416 1394 469 C ATOM 2154 CD1 ILE A 263 -21.680 5.080 23.847 1.00 58.02 C ANISOU 2154 CD1 ILE A 263 7232 8117 6697 -565 1653 694 C ATOM 2155 N ILE A 264 -19.059 8.819 20.507 1.00 44.37 N ANISOU 2155 N ILE A 264 5371 6156 5331 -210 1125 161 N ATOM 2156 CA ILE A 264 -19.031 9.964 19.582 1.00 43.15 C ANISOU 2156 CA ILE A 264 5118 5941 5335 -136 1071 36 C ATOM 2157 C ILE A 264 -17.792 9.976 18.678 1.00 45.50 C ANISOU 2157 C ILE A 264 5465 6157 5664 -102 867 27 C ATOM 2158 O ILE A 264 -17.939 10.154 17.470 1.00 44.51 O ANISOU 2158 O ILE A 264 5250 5950 5714 -83 789 23 O ATOM 2159 CB ILE A 264 -19.281 11.332 20.296 1.00 46.82 C ANISOU 2159 CB ILE A 264 5568 6469 5753 -76 1192 -124 C ATOM 2160 CG1 ILE A 264 -20.689 11.394 20.921 1.00 49.07 C ANISOU 2160 CG1 ILE A 264 5755 6822 6068 -100 1412 -127 C ATOM 2161 CG2 ILE A 264 -19.064 12.531 19.347 1.00 45.34 C ANISOU 2161 CG2 ILE A 264 5299 6200 5727 0 1108 -242 C ATOM 2162 CD1 ILE A 264 -20.819 12.351 22.121 1.00 56.58 C ANISOU 2162 CD1 ILE A 264 6760 7873 6866 -59 1567 -264 C ATOM 2163 N VAL A 265 -16.592 9.785 19.256 1.00 41.41 N ANISOU 2163 N VAL A 265 5088 5666 4979 -94 783 26 N ATOM 2164 CA VAL A 265 -15.333 9.796 18.517 1.00 39.68 C ANISOU 2164 CA VAL A 265 4910 5380 4785 -61 605 14 C ATOM 2165 C VAL A 265 -15.214 8.635 17.537 1.00 42.63 C ANISOU 2165 C VAL A 265 5265 5674 5258 -93 503 130 C ATOM 2166 O VAL A 265 -14.851 8.869 16.385 1.00 41.14 O ANISOU 2166 O VAL A 265 5028 5411 5191 -63 407 104 O ATOM 2167 CB VAL A 265 -14.098 9.994 19.430 1.00 43.68 C ANISOU 2167 CB VAL A 265 5552 5935 5107 -41 536 -29 C ATOM 2168 CG1 VAL A 265 -12.784 9.690 18.707 1.00 41.78 C ANISOU 2168 CG1 VAL A 265 5343 5626 4904 -18 357 -13 C ATOM 2169 CG2 VAL A 265 -14.078 11.408 19.998 1.00 44.13 C ANISOU 2169 CG2 VAL A 265 5612 6037 5119 6 597 -185 C ATOM 2170 N LEU A 266 -15.564 7.406 17.965 1.00 40.06 N ANISOU 2170 N LEU A 266 4980 5359 4884 -155 528 256 N ATOM 2171 CA LEU A 266 -15.524 6.241 17.081 1.00 39.67 C ANISOU 2171 CA LEU A 266 4916 5221 4935 -187 432 359 C ATOM 2172 C LEU A 266 -16.495 6.391 15.906 1.00 41.67 C ANISOU 2172 C LEU A 266 5033 5411 5388 -193 442 349 C ATOM 2173 O LEU A 266 -16.122 6.075 14.772 1.00 39.28 O ANISOU 2173 O LEU A 266 4713 5027 5184 -178 326 356 O ATOM 2174 CB LEU A 266 -15.743 4.914 17.841 1.00 41.44 C ANISOU 2174 CB LEU A 266 5214 5455 5077 -258 453 503 C ATOM 2175 CG LEU A 266 -14.591 4.465 18.769 1.00 47.27 C ANISOU 2175 CG LEU A 266 6103 6224 5632 -252 378 544 C ATOM 2176 CD1 LEU A 266 -14.993 3.275 19.603 1.00 49.08 C ANISOU 2176 CD1 LEU A 266 6406 6467 5775 -328 422 696 C ATOM 2177 CD2 LEU A 266 -13.326 4.140 17.991 1.00 48.38 C ANISOU 2177 CD2 LEU A 266 6275 6284 5822 -204 200 533 C ATOM 2178 N THR A 267 -17.709 6.938 16.166 1.00 38.75 N ANISOU 2178 N THR A 267 4565 5081 5077 -207 579 323 N ATOM 2179 CA THR A 267 -18.723 7.176 15.132 1.00 38.66 C ANISOU 2179 CA THR A 267 4412 5014 5264 -210 583 311 C ATOM 2180 C THR A 267 -18.172 8.170 14.109 1.00 41.36 C ANISOU 2180 C THR A 267 4728 5307 5679 -139 486 215 C ATOM 2181 O THR A 267 -18.220 7.915 12.907 1.00 40.37 O ANISOU 2181 O THR A 267 4564 5104 5670 -137 385 233 O ATOM 2182 CB THR A 267 -20.036 7.673 15.763 1.00 46.41 C ANISOU 2182 CB THR A 267 5286 6055 6293 -228 758 291 C ATOM 2183 OG1 THR A 267 -20.524 6.676 16.667 1.00 46.15 O ANISOU 2183 OG1 THR A 267 5281 6067 6186 -306 857 397 O ATOM 2184 CG2 THR A 267 -21.098 7.997 14.722 1.00 43.64 C ANISOU 2184 CG2 THR A 267 4774 5643 6163 -224 748 275 C ATOM 2185 N VAL A 268 -17.626 9.283 14.608 1.00 37.15 N ANISOU 2185 N VAL A 268 4228 4818 5070 -85 515 114 N ATOM 2186 CA VAL A 268 -17.031 10.347 13.822 1.00 36.15 C ANISOU 2186 CA VAL A 268 4086 4649 5000 -23 439 25 C ATOM 2187 C VAL A 268 -15.852 9.824 12.944 1.00 37.54 C ANISOU 2187 C VAL A 268 4329 4767 5167 -14 290 54 C ATOM 2188 O VAL A 268 -15.757 10.213 11.781 1.00 35.22 O ANISOU 2188 O VAL A 268 3995 4412 4974 11 218 34 O ATOM 2189 CB VAL A 268 -16.708 11.526 14.777 1.00 40.43 C ANISOU 2189 CB VAL A 268 4657 5249 5454 21 511 -87 C ATOM 2190 CG1 VAL A 268 -15.331 12.123 14.570 1.00 38.36 C ANISOU 2190 CG1 VAL A 268 4466 4966 5144 62 408 -148 C ATOM 2191 CG2 VAL A 268 -17.810 12.581 14.756 1.00 40.94 C ANISOU 2191 CG2 VAL A 268 4605 5312 5636 52 609 -162 C ATOM 2192 N PHE A 269 -15.013 8.902 13.473 1.00 33.54 N ANISOU 2192 N PHE A 269 3922 4277 4545 -34 247 107 N ATOM 2193 CA PHE A 269 -13.930 8.316 12.675 1.00 32.48 C ANISOU 2193 CA PHE A 269 3838 4087 4415 -20 120 131 C ATOM 2194 C PHE A 269 -14.495 7.392 11.595 1.00 35.99 C ANISOU 2194 C PHE A 269 4245 4460 4968 -49 67 198 C ATOM 2195 O PHE A 269 -14.057 7.456 10.448 1.00 34.88 O ANISOU 2195 O PHE A 269 4099 4265 4888 -25 -14 178 O ATOM 2196 CB PHE A 269 -12.887 7.583 13.545 1.00 34.37 C ANISOU 2196 CB PHE A 269 4184 4354 4522 -25 76 167 C ATOM 2197 CG PHE A 269 -11.759 8.475 14.000 1.00 35.96 C ANISOU 2197 CG PHE A 269 4428 4589 4646 20 44 84 C ATOM 2198 CD1 PHE A 269 -11.883 9.251 15.144 1.00 39.74 C ANISOU 2198 CD1 PHE A 269 4933 5141 5027 24 117 26 C ATOM 2199 CD2 PHE A 269 -10.593 8.583 13.254 1.00 38.22 C ANISOU 2199 CD2 PHE A 269 4722 4832 4967 55 -55 54 C ATOM 2200 CE1 PHE A 269 -10.846 10.093 15.553 1.00 41.27 C ANISOU 2200 CE1 PHE A 269 5163 5356 5161 60 72 -59 C ATOM 2201 CE2 PHE A 269 -9.556 9.433 13.660 1.00 41.00 C ANISOU 2201 CE2 PHE A 269 5097 5208 5272 88 -89 -23 C ATOM 2202 CZ PHE A 269 -9.688 10.177 14.808 1.00 39.89 C ANISOU 2202 CZ PHE A 269 4985 5132 5038 89 -35 -80 C ATOM 2203 N ALA A 270 -15.513 6.600 11.949 1.00 33.84 N ANISOU 2203 N ALA A 270 3946 4189 4722 -105 119 272 N ATOM 2204 CA ALA A 270 -16.163 5.647 11.048 1.00 34.45 C ANISOU 2204 CA ALA A 270 3986 4194 4909 -145 65 335 C ATOM 2205 C ALA A 270 -16.980 6.302 9.948 1.00 38.65 C ANISOU 2205 C ALA A 270 4420 4689 5578 -134 46 297 C ATOM 2206 O ALA A 270 -17.036 5.770 8.847 1.00 38.01 O ANISOU 2206 O ALA A 270 4336 4539 5569 -141 -48 313 O ATOM 2207 CB ALA A 270 -17.025 4.674 11.835 1.00 36.00 C ANISOU 2207 CB ALA A 270 4173 4401 5105 -218 132 430 C ATOM 2208 N VAL A 271 -17.618 7.434 10.240 1.00 36.22 N ANISOU 2208 N VAL A 271 4035 4421 5305 -113 128 243 N ATOM 2209 CA VAL A 271 -18.481 8.143 9.295 1.00 36.56 C ANISOU 2209 CA VAL A 271 3976 4427 5489 -97 107 213 C ATOM 2210 C VAL A 271 -17.731 9.224 8.498 1.00 40.72 C ANISOU 2210 C VAL A 271 4524 4931 6016 -34 43 143 C ATOM 2211 O VAL A 271 -18.019 9.415 7.318 1.00 40.74 O ANISOU 2211 O VAL A 271 4496 4878 6105 -24 -39 143 O ATOM 2212 CB VAL A 271 -19.751 8.692 10.023 1.00 41.20 C ANISOU 2212 CB VAL A 271 4448 5057 6150 -108 234 201 C ATOM 2213 CG1 VAL A 271 -20.531 9.677 9.162 1.00 41.24 C ANISOU 2213 CG1 VAL A 271 4342 5022 6305 -73 206 157 C ATOM 2214 CG2 VAL A 271 -20.657 7.554 10.482 1.00 41.64 C ANISOU 2214 CG2 VAL A 271 4460 5118 6245 -185 288 288 C ATOM 2215 N SER A 272 -16.784 9.919 9.125 1.00 37.07 N ANISOU 2215 N SER A 272 4117 4509 5458 3 76 87 N ATOM 2216 CA SER A 272 -16.097 11.032 8.473 1.00 36.95 C ANISOU 2216 CA SER A 272 4113 4470 5457 53 30 26 C ATOM 2217 C SER A 272 -14.613 10.827 8.189 1.00 39.95 C ANISOU 2217 C SER A 272 4586 4842 5750 69 -36 18 C ATOM 2218 O SER A 272 -14.222 10.826 7.023 1.00 40.96 O ANISOU 2218 O SER A 272 4730 4924 5908 79 -111 25 O ATOM 2219 CB SER A 272 -16.291 12.323 9.261 1.00 40.37 C ANISOU 2219 CB SER A 272 4506 4935 5898 87 113 -51 C ATOM 2220 OG SER A 272 -17.625 12.461 9.716 1.00 57.92 O ANISOU 2220 OG SER A 272 6635 7175 8197 77 200 -51 O ATOM 2221 N TYR A 273 -13.787 10.708 9.235 1.00 34.03 N ANISOU 2221 N TYR A 273 3895 4142 4895 72 -8 -1 N ATOM 2222 CA TYR A 273 -12.334 10.630 9.088 1.00 32.36 C ANISOU 2222 CA TYR A 273 3750 3926 4620 93 -67 -18 C ATOM 2223 C TYR A 273 -11.802 9.487 8.240 1.00 34.66 C ANISOU 2223 C TYR A 273 4082 4177 4911 85 -144 31 C ATOM 2224 O TYR A 273 -11.076 9.758 7.286 1.00 33.78 O ANISOU 2224 O TYR A 273 3981 4035 4819 108 -190 11 O ATOM 2225 CB TYR A 273 -11.621 10.760 10.435 1.00 33.60 C ANISOU 2225 CB TYR A 273 3956 4142 4670 98 -39 -49 C ATOM 2226 CG TYR A 273 -11.928 12.042 11.176 1.00 36.27 C ANISOU 2226 CG TYR A 273 4266 4513 5003 116 29 -128 C ATOM 2227 CD1 TYR A 273 -11.902 13.271 10.526 1.00 37.81 C ANISOU 2227 CD1 TYR A 273 4416 4669 5282 144 23 -186 C ATOM 2228 CD2 TYR A 273 -12.172 12.035 12.545 1.00 38.84 C ANISOU 2228 CD2 TYR A 273 4622 4904 5232 107 97 -147 C ATOM 2229 CE1 TYR A 273 -12.158 14.459 11.212 1.00 39.10 C ANISOU 2229 CE1 TYR A 273 4556 4847 5455 166 80 -269 C ATOM 2230 CE2 TYR A 273 -12.412 13.219 13.244 1.00 40.23 C ANISOU 2230 CE2 TYR A 273 4781 5107 5396 129 162 -239 C ATOM 2231 CZ TYR A 273 -12.409 14.427 12.571 1.00 44.77 C ANISOU 2231 CZ TYR A 273 5302 5631 6076 161 151 -304 C ATOM 2232 OH TYR A 273 -12.657 15.588 13.258 1.00 43.05 O ANISOU 2232 OH TYR A 273 5068 5426 5862 188 210 -404 O ATOM 2233 N ILE A 274 -12.200 8.229 8.545 1.00 30.65 N ANISOU 2233 N ILE A 274 3596 3662 4386 53 -152 95 N ATOM 2234 CA ILE A 274 -11.786 7.055 7.773 1.00 29.40 C ANISOU 2234 CA ILE A 274 3479 3452 4240 48 -227 133 C ATOM 2235 C ILE A 274 -12.311 7.119 6.332 1.00 31.90 C ANISOU 2235 C ILE A 274 3769 3717 4635 48 -270 128 C ATOM 2236 O ILE A 274 -11.466 7.091 5.443 1.00 31.33 O ANISOU 2236 O ILE A 274 3730 3619 4554 75 -315 104 O ATOM 2237 CB ILE A 274 -12.019 5.686 8.467 1.00 32.79 C ANISOU 2237 CB ILE A 274 3947 3871 4643 12 -236 205 C ATOM 2238 CG1 ILE A 274 -11.388 5.647 9.879 1.00 33.21 C ANISOU 2238 CG1 ILE A 274 4046 3979 4593 15 -210 216 C ATOM 2239 CG2 ILE A 274 -11.501 4.523 7.590 1.00 34.26 C ANISOU 2239 CG2 ILE A 274 4176 3985 4855 19 -322 226 C ATOM 2240 CD1 ILE A 274 -12.010 4.592 10.845 1.00 34.84 C ANISOU 2240 CD1 ILE A 274 4283 4193 4762 -37 -182 305 C ATOM 2241 N PRO A 275 -13.636 7.276 6.035 1.00 28.94 N ANISOU 2241 N PRO A 275 3334 3326 4334 20 -258 148 N ATOM 2242 CA PRO A 275 -14.049 7.346 4.620 1.00 28.27 C ANISOU 2242 CA PRO A 275 3239 3192 4311 22 -325 144 C ATOM 2243 C PRO A 275 -13.307 8.421 3.819 1.00 30.24 C ANISOU 2243 C PRO A 275 3504 3441 4544 63 -338 99 C ATOM 2244 O PRO A 275 -12.834 8.121 2.733 1.00 29.83 O ANISOU 2244 O PRO A 275 3500 3358 4475 74 -394 93 O ATOM 2245 CB PRO A 275 -15.563 7.586 4.692 1.00 30.02 C ANISOU 2245 CB PRO A 275 3373 3407 4628 -10 -307 168 C ATOM 2246 CG PRO A 275 -15.962 7.077 5.999 1.00 34.95 C ANISOU 2246 CG PRO A 275 3976 4067 5239 -43 -233 202 C ATOM 2247 CD PRO A 275 -14.816 7.347 6.924 1.00 30.43 C ANISOU 2247 CD PRO A 275 3460 3544 4559 -15 -188 175 C ATOM 2248 N PHE A 276 -13.145 9.634 4.383 1.00 26.36 N ANISOU 2248 N PHE A 276 2979 2983 4053 83 -283 66 N ATOM 2249 CA PHE A 276 -12.444 10.735 3.727 1.00 25.62 C ANISOU 2249 CA PHE A 276 2896 2883 3958 113 -290 34 C ATOM 2250 C PHE A 276 -11.000 10.415 3.362 1.00 27.96 C ANISOU 2250 C PHE A 276 3252 3181 4189 131 -305 17 C ATOM 2251 O PHE A 276 -10.612 10.675 2.225 1.00 25.87 O ANISOU 2251 O PHE A 276 3015 2894 3920 140 -333 17 O ATOM 2252 CB PHE A 276 -12.526 12.033 4.554 1.00 27.33 C ANISOU 2252 CB PHE A 276 3065 3121 4198 129 -230 -6 C ATOM 2253 CG PHE A 276 -11.779 13.198 3.948 1.00 27.89 C ANISOU 2253 CG PHE A 276 3144 3172 4283 151 -238 -33 C ATOM 2254 CD1 PHE A 276 -12.320 13.917 2.888 1.00 30.40 C ANISOU 2254 CD1 PHE A 276 3445 3445 4662 156 -274 -12 C ATOM 2255 CD2 PHE A 276 -10.522 13.558 4.418 1.00 29.19 C ANISOU 2255 CD2 PHE A 276 3331 3357 4404 162 -218 -70 C ATOM 2256 CE1 PHE A 276 -11.633 14.998 2.332 1.00 30.85 C ANISOU 2256 CE1 PHE A 276 3515 3475 4732 168 -278 -21 C ATOM 2257 CE2 PHE A 276 -9.826 14.624 3.844 1.00 31.59 C ANISOU 2257 CE2 PHE A 276 3635 3634 4733 172 -221 -86 C ATOM 2258 CZ PHE A 276 -10.390 15.342 2.812 1.00 29.39 C ANISOU 2258 CZ PHE A 276 3347 3309 4512 173 -246 -57 C ATOM 2259 N HIS A 277 -10.209 9.864 4.311 1.00 25.88 N ANISOU 2259 N HIS A 277 3010 2947 3876 136 -288 7 N ATOM 2260 CA HIS A 277 -8.806 9.537 4.059 1.00 26.86 C ANISOU 2260 CA HIS A 277 3171 3073 3962 159 -303 -12 C ATOM 2261 C HIS A 277 -8.632 8.435 3.040 1.00 31.40 C ANISOU 2261 C HIS A 277 3791 3612 4528 163 -346 2 C ATOM 2262 O HIS A 277 -7.691 8.502 2.256 1.00 31.15 O ANISOU 2262 O HIS A 277 3780 3574 4481 185 -346 -21 O ATOM 2263 CB HIS A 277 -8.026 9.240 5.351 1.00 27.82 C ANISOU 2263 CB HIS A 277 3300 3229 4043 167 -295 -25 C ATOM 2264 CG HIS A 277 -7.711 10.486 6.111 1.00 30.91 C ANISOU 2264 CG HIS A 277 3661 3652 4432 172 -262 -67 C ATOM 2265 ND1 HIS A 277 -8.556 10.956 7.104 1.00 32.59 N ANISOU 2265 ND1 HIS A 277 3855 3892 4634 159 -224 -75 N ATOM 2266 CD2 HIS A 277 -6.680 11.350 5.962 1.00 32.31 C ANISOU 2266 CD2 HIS A 277 3822 3832 4624 187 -259 -107 C ATOM 2267 CE1 HIS A 277 -8.009 12.084 7.534 1.00 32.26 C ANISOU 2267 CE1 HIS A 277 3796 3864 4597 170 -208 -129 C ATOM 2268 NE2 HIS A 277 -6.890 12.372 6.861 1.00 32.48 N ANISOU 2268 NE2 HIS A 277 3821 3874 4647 183 -233 -146 N ATOM 2269 N VAL A 278 -9.541 7.437 3.040 1.00 27.59 N ANISOU 2269 N VAL A 278 3322 3104 4059 140 -378 35 N ATOM 2270 CA VAL A 278 -9.515 6.328 2.085 1.00 27.46 C ANISOU 2270 CA VAL A 278 3354 3040 4040 143 -430 37 C ATOM 2271 C VAL A 278 -9.818 6.899 0.681 1.00 29.80 C ANISOU 2271 C VAL A 278 3668 3321 4335 144 -451 25 C ATOM 2272 O VAL A 278 -9.092 6.624 -0.270 1.00 29.07 O ANISOU 2272 O VAL A 278 3624 3216 4204 166 -460 -3 O ATOM 2273 CB VAL A 278 -10.515 5.179 2.466 1.00 31.24 C ANISOU 2273 CB VAL A 278 3837 3483 4551 106 -467 80 C ATOM 2274 CG1 VAL A 278 -10.635 4.143 1.349 1.00 31.34 C ANISOU 2274 CG1 VAL A 278 3902 3432 4572 104 -535 69 C ATOM 2275 CG2 VAL A 278 -10.133 4.503 3.784 1.00 30.74 C ANISOU 2275 CG2 VAL A 278 3779 3430 4470 103 -453 108 C ATOM 2276 N MET A 279 -10.899 7.676 0.571 1.00 25.70 N ANISOU 2276 N MET A 279 3109 2802 3855 122 -457 46 N ATOM 2277 CA MET A 279 -11.352 8.246 -0.704 1.00 25.25 C ANISOU 2277 CA MET A 279 3072 2725 3797 119 -497 51 C ATOM 2278 C MET A 279 -10.449 9.328 -1.281 1.00 29.86 C ANISOU 2278 C MET A 279 3674 3328 4343 142 -460 37 C ATOM 2279 O MET A 279 -10.285 9.392 -2.499 1.00 29.55 O ANISOU 2279 O MET A 279 3693 3277 4258 145 -486 37 O ATOM 2280 CB MET A 279 -12.820 8.686 -0.621 1.00 26.79 C ANISOU 2280 CB MET A 279 3206 2904 4068 93 -530 83 C ATOM 2281 CG MET A 279 -13.799 7.522 -0.385 1.00 29.58 C ANISOU 2281 CG MET A 279 3541 3227 4470 58 -577 104 C ATOM 2282 SD MET A 279 -13.461 5.948 -1.241 1.00 31.89 S ANISOU 2282 SD MET A 279 3927 3472 4719 52 -652 86 S ATOM 2283 CE MET A 279 -13.702 6.451 -2.985 1.00 28.43 C ANISOU 2283 CE MET A 279 3551 3013 4237 59 -733 73 C ATOM 2284 N LYS A 280 -9.851 10.156 -0.413 1.00 28.24 N ANISOU 2284 N LYS A 280 3424 3151 4153 152 -399 25 N ATOM 2285 CA LYS A 280 -8.906 11.217 -0.806 1.00 29.49 C ANISOU 2285 CA LYS A 280 3587 3322 4297 163 -357 16 C ATOM 2286 C LYS A 280 -7.735 10.534 -1.522 1.00 34.59 C ANISOU 2286 C LYS A 280 4285 3976 4880 180 -339 -7 C ATOM 2287 O LYS A 280 -7.380 10.925 -2.633 1.00 34.71 O ANISOU 2287 O LYS A 280 4341 3989 4856 180 -326 2 O ATOM 2288 CB LYS A 280 -8.420 11.985 0.448 1.00 30.57 C ANISOU 2288 CB LYS A 280 3666 3481 4468 168 -309 -8 C ATOM 2289 CG LYS A 280 -7.393 13.069 0.222 1.00 42.64 C ANISOU 2289 CG LYS A 280 5184 5014 6005 171 -268 -20 C ATOM 2290 CD LYS A 280 -6.689 13.380 1.533 1.00 50.18 C ANISOU 2290 CD LYS A 280 6093 5992 6981 177 -241 -60 C ATOM 2291 CE LYS A 280 -5.593 14.395 1.361 1.00 55.71 C ANISOU 2291 CE LYS A 280 6769 6687 7709 171 -208 -76 C ATOM 2292 NZ LYS A 280 -5.117 14.887 2.676 1.00 62.44 N ANISOU 2292 NZ LYS A 280 7578 7555 8589 173 -202 -123 N ATOM 2293 N THR A 281 -7.215 9.457 -0.909 1.00 31.95 N ANISOU 2293 N THR A 281 3952 3648 4538 196 -338 -32 N ATOM 2294 CA THR A 281 -6.109 8.640 -1.408 1.00 31.13 C ANISOU 2294 CA THR A 281 3883 3547 4398 224 -320 -66 C ATOM 2295 C THR A 281 -6.501 7.916 -2.704 1.00 32.22 C ANISOU 2295 C THR A 281 4098 3659 4484 226 -354 -73 C ATOM 2296 O THR A 281 -5.743 7.975 -3.674 1.00 29.96 O ANISOU 2296 O THR A 281 3852 3384 4146 242 -314 -96 O ATOM 2297 CB THR A 281 -5.675 7.652 -0.325 1.00 32.21 C ANISOU 2297 CB THR A 281 4000 3681 4557 243 -334 -81 C ATOM 2298 OG1 THR A 281 -5.386 8.366 0.872 1.00 33.99 O ANISOU 2298 OG1 THR A 281 4167 3935 4811 238 -314 -77 O ATOM 2299 CG2 THR A 281 -4.472 6.823 -0.737 1.00 29.05 C ANISOU 2299 CG2 THR A 281 3617 3275 4147 284 -317 -123 C ATOM 2300 N MET A 282 -7.662 7.215 -2.698 1.00 28.60 N ANISOU 2300 N MET A 282 3661 3167 4038 207 -425 -58 N ATOM 2301 CA MET A 282 -8.161 6.468 -3.856 1.00 29.42 C ANISOU 2301 CA MET A 282 3843 3239 4097 204 -482 -73 C ATOM 2302 C MET A 282 -8.320 7.376 -5.073 1.00 30.74 C ANISOU 2302 C MET A 282 4059 3420 4202 195 -483 -58 C ATOM 2303 O MET A 282 -7.911 6.989 -6.160 1.00 29.70 O ANISOU 2303 O MET A 282 4008 3288 3988 209 -479 -91 O ATOM 2304 CB MET A 282 -9.487 5.759 -3.542 1.00 32.46 C ANISOU 2304 CB MET A 282 4219 3581 4534 172 -566 -50 C ATOM 2305 CG MET A 282 -9.327 4.459 -2.764 1.00 37.19 C ANISOU 2305 CG MET A 282 4815 4146 5170 177 -584 -63 C ATOM 2306 SD MET A 282 -10.848 3.464 -2.684 1.00 42.34 S ANISOU 2306 SD MET A 282 5467 4733 5888 126 -684 -34 S ATOM 2307 CE MET A 282 -11.110 3.149 -4.372 1.00 38.34 C ANISOU 2307 CE MET A 282 5058 4193 5318 130 -760 -83 C ATOM 2308 N ASN A 283 -8.882 8.586 -4.876 1.00 28.24 N ANISOU 2308 N ASN A 283 3698 3113 3920 173 -485 -9 N ATOM 2309 CA ASN A 283 -9.112 9.565 -5.939 1.00 29.33 C ANISOU 2309 CA ASN A 283 3881 3254 4010 161 -498 27 C ATOM 2310 C ASN A 283 -7.816 10.095 -6.554 1.00 32.27 C ANISOU 2310 C ASN A 283 4288 3660 4313 174 -406 19 C ATOM 2311 O ASN A 283 -7.727 10.226 -7.779 1.00 31.47 O ANISOU 2311 O ASN A 283 4276 3567 4116 169 -409 30 O ATOM 2312 CB ASN A 283 -9.996 10.708 -5.457 1.00 31.53 C ANISOU 2312 CB ASN A 283 4090 3518 4370 143 -524 78 C ATOM 2313 CG ASN A 283 -10.384 11.652 -6.564 1.00 46.30 C ANISOU 2313 CG ASN A 283 6012 5377 6204 131 -564 130 C ATOM 2314 OD1 ASN A 283 -9.924 12.785 -6.626 1.00 46.08 O ANISOU 2314 OD1 ASN A 283 5970 5353 6187 129 -516 162 O ATOM 2315 ND2 ASN A 283 -11.181 11.180 -7.495 1.00 36.35 N ANISOU 2315 ND2 ASN A 283 4817 4095 4898 121 -662 142 N ATOM 2316 N LEU A 284 -6.817 10.386 -5.713 1.00 28.44 N ANISOU 2316 N LEU A 284 3735 3198 3873 186 -325 3 N ATOM 2317 CA LEU A 284 -5.512 10.856 -6.190 1.00 29.51 C ANISOU 2317 CA LEU A 284 3877 3365 3972 193 -227 -5 C ATOM 2318 C LEU A 284 -4.812 9.746 -6.984 1.00 34.24 C ANISOU 2318 C LEU A 284 4542 3979 4489 222 -192 -62 C ATOM 2319 O LEU A 284 -4.242 10.015 -8.043 1.00 33.98 O ANISOU 2319 O LEU A 284 4568 3972 4372 220 -128 -59 O ATOM 2320 CB LEU A 284 -4.636 11.290 -5.010 1.00 29.75 C ANISOU 2320 CB LEU A 284 3807 3409 4088 198 -171 -20 C ATOM 2321 CG LEU A 284 -4.960 12.620 -4.346 1.00 35.22 C ANISOU 2321 CG LEU A 284 4438 4088 4854 173 -175 18 C ATOM 2322 CD1 LEU A 284 -4.358 12.680 -2.947 1.00 35.07 C ANISOU 2322 CD1 LEU A 284 4334 4081 4912 182 -156 -17 C ATOM 2323 CD2 LEU A 284 -4.490 13.799 -5.189 1.00 37.50 C ANISOU 2323 CD2 LEU A 284 4745 4376 5128 147 -123 65 C ATOM 2324 N ARG A 285 -4.908 8.492 -6.483 1.00 31.05 N ANISOU 2324 N ARG A 285 4134 3556 4109 248 -231 -112 N ATOM 2325 CA ARG A 285 -4.352 7.280 -7.097 1.00 31.90 C ANISOU 2325 CA ARG A 285 4299 3658 4163 286 -213 -182 C ATOM 2326 C ARG A 285 -4.964 7.044 -8.500 1.00 36.36 C ANISOU 2326 C ARG A 285 4989 4218 4608 277 -252 -191 C ATOM 2327 O ARG A 285 -4.232 6.752 -9.442 1.00 36.51 O ANISOU 2327 O ARG A 285 5074 4261 4538 301 -183 -238 O ATOM 2328 CB ARG A 285 -4.563 6.069 -6.155 1.00 29.75 C ANISOU 2328 CB ARG A 285 3997 3344 3963 308 -274 -215 C ATOM 2329 CG ARG A 285 -3.951 4.772 -6.645 1.00 48.39 C ANISOU 2329 CG ARG A 285 6407 5680 6299 357 -263 -295 C ATOM 2330 CD ARG A 285 -2.703 4.389 -5.878 1.00 59.70 C ANISOU 2330 CD ARG A 285 7760 7117 7807 403 -205 -330 C ATOM 2331 NE ARG A 285 -2.519 2.937 -5.838 1.00 70.49 N ANISOU 2331 NE ARG A 285 9156 8426 9202 449 -245 -393 N ATOM 2332 CZ ARG A 285 -1.847 2.234 -6.744 1.00 87.23 C ANISOU 2332 CZ ARG A 285 11325 10535 11283 499 -198 -476 C ATOM 2333 NH1 ARG A 285 -1.287 2.839 -7.785 1.00 76.24 N ANISOU 2333 NH1 ARG A 285 9963 9199 9804 505 -97 -501 N ATOM 2334 NH2 ARG A 285 -1.732 0.918 -6.617 1.00 73.73 N ANISOU 2334 NH2 ARG A 285 9638 8755 9619 544 -246 -535 N ATOM 2335 N ALA A 286 -6.299 7.182 -8.622 1.00 33.60 N ANISOU 2335 N ALA A 286 4669 3839 4258 244 -361 -150 N ATOM 2336 CA ALA A 286 -7.046 7.043 -9.874 1.00 34.15 C ANISOU 2336 CA ALA A 286 4858 3900 4220 228 -435 -150 C ATOM 2337 C ALA A 286 -6.621 8.143 -10.866 1.00 37.50 C ANISOU 2337 C ALA A 286 5343 4369 4537 213 -370 -104 C ATOM 2338 O ALA A 286 -6.356 7.849 -12.031 1.00 37.89 O ANISOU 2338 O ALA A 286 5509 4440 4449 221 -351 -137 O ATOM 2339 CB ALA A 286 -8.551 7.122 -9.605 1.00 34.52 C ANISOU 2339 CB ALA A 286 4884 3903 4328 193 -571 -103 C ATOM 2340 N ARG A 287 -6.509 9.394 -10.388 1.00 34.12 N ANISOU 2340 N ARG A 287 4841 3953 4169 191 -331 -31 N ATOM 2341 CA ARG A 287 -6.083 10.528 -11.210 1.00 34.66 C ANISOU 2341 CA ARG A 287 4956 4053 4159 168 -267 33 C ATOM 2342 C ARG A 287 -4.651 10.358 -11.755 1.00 39.42 C ANISOU 2342 C ARG A 287 5585 4708 4685 186 -115 -9 C ATOM 2343 O ARG A 287 -4.378 10.708 -12.905 1.00 40.97 O ANISOU 2343 O ARG A 287 5883 4938 4747 171 -64 18 O ATOM 2344 CB ARG A 287 -6.211 11.844 -10.424 1.00 33.84 C ANISOU 2344 CB ARG A 287 4753 3933 4171 142 -260 108 C ATOM 2345 CG ARG A 287 -7.656 12.316 -10.259 1.00 44.07 C ANISOU 2345 CG ARG A 287 6038 5181 5524 124 -394 164 C ATOM 2346 CD ARG A 287 -7.748 13.659 -9.563 1.00 46.81 C ANISOU 2346 CD ARG A 287 6296 5505 5986 107 -379 225 C ATOM 2347 NE ARG A 287 -7.134 14.709 -10.373 1.00 53.93 N ANISOU 2347 NE ARG A 287 7248 6414 6830 82 -318 294 N ATOM 2348 CZ ARG A 287 -6.596 15.822 -9.888 1.00 58.50 C ANISOU 2348 CZ ARG A 287 7756 6977 7494 64 -255 332 C ATOM 2349 NH1 ARG A 287 -6.614 16.061 -8.582 1.00 37.67 N ANISOU 2349 NH1 ARG A 287 5001 4321 4992 74 -250 298 N ATOM 2350 NH2 ARG A 287 -6.050 16.711 -10.704 1.00 44.72 N ANISOU 2350 NH2 ARG A 287 6064 5233 5696 32 -199 406 N ATOM 2351 N LEU A 288 -3.756 9.789 -10.946 1.00 34.81 N ANISOU 2351 N LEU A 288 4909 4131 4184 219 -43 -73 N ATOM 2352 CA LEU A 288 -2.352 9.625 -11.318 1.00 34.70 C ANISOU 2352 CA LEU A 288 4884 4164 4137 242 107 -118 C ATOM 2353 C LEU A 288 -1.996 8.361 -12.075 1.00 39.03 C ANISOU 2353 C LEU A 288 5516 4725 4590 289 139 -218 C ATOM 2354 O LEU A 288 -1.205 8.423 -13.014 1.00 40.43 O ANISOU 2354 O LEU A 288 5750 4949 4660 296 258 -240 O ATOM 2355 CB LEU A 288 -1.464 9.708 -10.059 1.00 33.46 C ANISOU 2355 CB LEU A 288 4573 4005 4135 259 161 -138 C ATOM 2356 CG LEU A 288 -1.200 11.091 -9.487 1.00 37.22 C ANISOU 2356 CG LEU A 288 4961 4483 4698 216 193 -63 C ATOM 2357 CD1 LEU A 288 -0.783 10.985 -8.045 1.00 36.54 C ANISOU 2357 CD1 LEU A 288 4743 4381 4758 233 177 -91 C ATOM 2358 CD2 LEU A 288 -0.145 11.834 -10.290 1.00 38.70 C ANISOU 2358 CD2 LEU A 288 5149 4714 4841 192 337 -32 C ATOM 2359 N ASP A 289 -2.498 7.218 -11.616 1.00 35.12 N ANISOU 2359 N ASP A 289 5022 4183 4140 322 44 -282 N ATOM 2360 CA ASP A 289 -2.085 5.907 -12.094 1.00 36.70 C ANISOU 2360 CA ASP A 289 5280 4372 4291 377 66 -395 C ATOM 2361 C ASP A 289 -3.111 5.071 -12.837 1.00 42.30 C ANISOU 2361 C ASP A 289 6125 5043 4902 377 -54 -440 C ATOM 2362 O ASP A 289 -2.745 4.014 -13.348 1.00 43.42 O ANISOU 2362 O ASP A 289 6332 5172 4994 424 -32 -545 O ATOM 2363 CB ASP A 289 -1.499 5.106 -10.907 1.00 37.96 C ANISOU 2363 CB ASP A 289 5322 4496 4606 424 68 -447 C ATOM 2364 CG ASP A 289 -0.358 5.805 -10.186 1.00 44.92 C ANISOU 2364 CG ASP A 289 6066 5412 5589 428 173 -420 C ATOM 2365 OD1 ASP A 289 0.478 6.435 -10.865 1.00 44.89 O ANISOU 2365 OD1 ASP A 289 6059 5464 5534 423 304 -415 O ATOM 2366 OD2 ASP A 289 -0.302 5.719 -8.945 1.00 53.05 O ANISOU 2366 OD2 ASP A 289 6994 6415 6748 433 123 -402 O ATOM 2367 N PHE A 290 -4.374 5.513 -12.897 1.00 38.98 N ANISOU 2367 N PHE A 290 5742 4600 4467 327 -185 -369 N ATOM 2368 CA PHE A 290 -5.410 4.716 -13.540 1.00 40.12 C ANISOU 2368 CA PHE A 290 6002 4701 4541 321 -322 -411 C ATOM 2369 C PHE A 290 -6.104 5.384 -14.720 1.00 44.95 C ANISOU 2369 C PHE A 290 6743 5339 4995 281 -382 -362 C ATOM 2370 O PHE A 290 -7.295 5.169 -14.943 1.00 44.88 O ANISOU 2370 O PHE A 290 6785 5288 4980 254 -541 -348 O ATOM 2371 CB PHE A 290 -6.377 4.126 -12.491 1.00 41.27 C ANISOU 2371 CB PHE A 290 6071 4772 4836 306 -457 -400 C ATOM 2372 CG PHE A 290 -5.692 3.154 -11.550 1.00 43.11 C ANISOU 2372 CG PHE A 290 6224 4969 5188 351 -417 -461 C ATOM 2373 CD1 PHE A 290 -5.442 1.841 -11.939 1.00 48.35 C ANISOU 2373 CD1 PHE A 290 6953 5585 5832 394 -435 -571 C ATOM 2374 CD2 PHE A 290 -5.302 3.550 -10.279 1.00 44.15 C ANISOU 2374 CD2 PHE A 290 6219 5108 5448 352 -372 -410 C ATOM 2375 CE1 PHE A 290 -4.804 0.944 -11.072 1.00 49.24 C ANISOU 2375 CE1 PHE A 290 6992 5652 6066 440 -411 -617 C ATOM 2376 CE2 PHE A 290 -4.662 2.654 -9.414 1.00 47.10 C ANISOU 2376 CE2 PHE A 290 6526 5445 5924 394 -352 -456 C ATOM 2377 CZ PHE A 290 -4.416 1.360 -9.814 1.00 46.49 C ANISOU 2377 CZ PHE A 290 6511 5316 5839 438 -373 -553 C ATOM 2378 N GLN A 291 -5.338 6.157 -15.508 1.00 42.95 N ANISOU 2378 N GLN A 291 6548 5155 4615 277 -257 -333 N ATOM 2379 CA GLN A 291 -5.855 6.842 -16.690 1.00 44.12 C ANISOU 2379 CA GLN A 291 6838 5335 4590 240 -304 -273 C ATOM 2380 C GLN A 291 -5.753 5.962 -17.940 1.00 51.09 C ANISOU 2380 C GLN A 291 7900 6238 5272 264 -306 -377 C ATOM 2381 O GLN A 291 -4.919 6.199 -18.817 1.00 53.03 O ANISOU 2381 O GLN A 291 8237 6554 5358 272 -167 -392 O ATOM 2382 CB GLN A 291 -5.223 8.239 -16.881 1.00 45.33 C ANISOU 2382 CB GLN A 291 6972 5545 4709 208 -182 -161 C ATOM 2383 CG GLN A 291 -5.521 9.240 -15.757 1.00 49.24 C ANISOU 2383 CG GLN A 291 7314 6008 5386 179 -210 -60 C ATOM 2384 CD GLN A 291 -6.999 9.471 -15.549 1.00 58.73 C ANISOU 2384 CD GLN A 291 8512 7152 6649 153 -405 -2 C ATOM 2385 OE1 GLN A 291 -7.711 9.952 -16.438 1.00 56.80 O ANISOU 2385 OE1 GLN A 291 8377 6906 6297 125 -501 61 O ATOM 2386 NE2 GLN A 291 -7.498 9.107 -14.373 1.00 37.74 N ANISOU 2386 NE2 GLN A 291 5728 4446 4165 161 -468 -20 N ATOM 2387 N THR A 292 -6.586 4.905 -17.969 1.00 47.67 N ANISOU 2387 N THR A 292 7513 5742 4858 274 -460 -456 N ATOM 2388 CA THR A 292 -6.772 3.951 -19.067 1.00 49.33 C ANISOU 2388 CA THR A 292 7898 5946 4897 294 -518 -573 C ATOM 2389 C THR A 292 -8.289 3.867 -19.325 1.00 52.53 C ANISOU 2389 C THR A 292 8363 6294 5301 249 -761 -540 C ATOM 2390 O THR A 292 -9.057 4.005 -18.369 1.00 50.39 O ANISOU 2390 O THR A 292 7960 5968 5219 223 -862 -476 O ATOM 2391 CB THR A 292 -6.184 2.559 -18.765 1.00 58.98 C ANISOU 2391 CB THR A 292 9099 7124 6186 356 -470 -727 C ATOM 2392 OG1 THR A 292 -6.703 2.063 -17.536 1.00 60.24 O ANISOU 2392 OG1 THR A 292 9117 7201 6572 352 -565 -715 O ATOM 2393 CG2 THR A 292 -4.669 2.536 -18.775 1.00 58.65 C ANISOU 2393 CG2 THR A 292 9017 7143 6126 410 -236 -781 C ATOM 2394 N PRO A 293 -8.745 3.664 -20.587 1.00 50.28 N ANISOU 2394 N PRO A 293 8271 6023 4809 237 -860 -581 N ATOM 2395 CA PRO A 293 -10.201 3.606 -20.848 1.00 50.13 C ANISOU 2395 CA PRO A 293 8295 5945 4805 191 -1111 -547 C ATOM 2396 C PRO A 293 -10.980 2.578 -20.020 1.00 50.95 C ANISOU 2396 C PRO A 293 8296 5946 5117 187 -1250 -606 C ATOM 2397 O PRO A 293 -12.098 2.870 -19.597 1.00 49.31 O ANISOU 2397 O PRO A 293 8005 5689 5040 144 -1407 -526 O ATOM 2398 CB PRO A 293 -10.284 3.303 -22.348 1.00 54.23 C ANISOU 2398 CB PRO A 293 9057 6501 5047 192 -1173 -621 C ATOM 2399 CG PRO A 293 -8.982 3.740 -22.899 1.00 59.45 C ANISOU 2399 CG PRO A 293 9795 7263 5532 220 -936 -627 C ATOM 2400 CD PRO A 293 -7.972 3.492 -21.834 1.00 53.64 C ANISOU 2400 CD PRO A 293 8884 6522 4974 262 -748 -661 C ATOM 2401 N ALA A 294 -10.382 1.395 -19.775 1.00 46.79 N ANISOU 2401 N ALA A 294 7767 5381 4632 231 -1186 -740 N ATOM 2402 CA ALA A 294 -10.981 0.310 -18.995 1.00 46.03 C ANISOU 2402 CA ALA A 294 7582 5176 4731 225 -1300 -795 C ATOM 2403 C ALA A 294 -11.199 0.667 -17.508 1.00 48.66 C ANISOU 2403 C ALA A 294 7698 5482 5307 206 -1273 -689 C ATOM 2404 O ALA A 294 -12.012 0.020 -16.842 1.00 48.58 O ANISOU 2404 O ALA A 294 7606 5388 5463 177 -1392 -689 O ATOM 2405 CB ALA A 294 -10.134 -0.948 -19.119 1.00 47.31 C ANISOU 2405 CB ALA A 294 7800 5300 4874 285 -1221 -957 C ATOM 2406 N MET A 295 -10.491 1.701 -17.002 1.00 43.49 N ANISOU 2406 N MET A 295 6956 4899 4669 217 -1119 -601 N ATOM 2407 CA MET A 295 -10.576 2.155 -15.614 1.00 41.35 C ANISOU 2407 CA MET A 295 6497 4617 4598 204 -1076 -509 C ATOM 2408 C MET A 295 -11.493 3.354 -15.390 1.00 46.28 C ANISOU 2408 C MET A 295 7051 5255 5276 157 -1150 -376 C ATOM 2409 O MET A 295 -11.863 3.611 -14.245 1.00 43.98 O ANISOU 2409 O MET A 295 6610 4942 5157 141 -1149 -314 O ATOM 2410 CB MET A 295 -9.172 2.462 -15.059 1.00 42.58 C ANISOU 2410 CB MET A 295 6584 4827 4768 250 -869 -511 C ATOM 2411 CG MET A 295 -8.362 1.227 -14.718 1.00 46.25 C ANISOU 2411 CG MET A 295 7040 5252 5282 303 -804 -624 C ATOM 2412 SD MET A 295 -9.191 0.102 -13.568 1.00 49.82 S ANISOU 2412 SD MET A 295 7395 5590 5946 284 -931 -633 S ATOM 2413 CE MET A 295 -9.070 1.042 -12.058 1.00 44.68 C ANISOU 2413 CE MET A 295 6559 4972 5447 268 -855 -508 C ATOM 2414 N CYS A 296 -11.845 4.090 -16.464 1.00 46.59 N ANISOU 2414 N CYS A 296 7201 5330 5169 138 -1213 -334 N ATOM 2415 CA CYS A 296 -12.664 5.310 -16.415 1.00 47.82 C ANISOU 2415 CA CYS A 296 7305 5493 5370 102 -1291 -206 C ATOM 2416 C CYS A 296 -13.972 5.234 -15.630 1.00 47.79 C ANISOU 2416 C CYS A 296 7168 5422 5568 68 -1435 -162 C ATOM 2417 O CYS A 296 -14.239 6.140 -14.832 1.00 44.92 O ANISOU 2417 O CYS A 296 6675 5063 5331 59 -1406 -74 O ATOM 2418 CB CYS A 296 -12.865 5.905 -17.806 1.00 51.63 C ANISOU 2418 CB CYS A 296 7955 6012 5650 88 -1365 -172 C ATOM 2419 SG CYS A 296 -11.330 6.406 -18.631 1.00 57.59 S ANISOU 2419 SG CYS A 296 8841 6864 6176 116 -1153 -180 S ATOM 2420 N ALA A 297 -14.768 4.157 -15.836 1.00 44.03 N ANISOU 2420 N ALA A 297 6717 4882 5129 48 -1582 -228 N ATOM 2421 CA ALA A 297 -16.041 3.933 -15.138 1.00 43.18 C ANISOU 2421 CA ALA A 297 6475 4708 5224 7 -1715 -192 C ATOM 2422 C ALA A 297 -15.818 3.796 -13.629 1.00 44.74 C ANISOU 2422 C ALA A 297 6504 4894 5599 11 -1594 -170 C ATOM 2423 O ALA A 297 -16.545 4.419 -12.851 1.00 43.85 O ANISOU 2423 O ALA A 297 6252 4774 5636 -10 -1609 -93 O ATOM 2424 CB ALA A 297 -16.735 2.689 -15.680 1.00 44.91 C ANISOU 2424 CB ALA A 297 6763 4855 5447 -20 -1882 -277 C ATOM 2425 N PHE A 298 -14.795 3.009 -13.220 1.00 39.90 N ANISOU 2425 N PHE A 298 5908 4284 4968 42 -1473 -240 N ATOM 2426 CA PHE A 298 -14.443 2.824 -11.811 1.00 37.86 C ANISOU 2426 CA PHE A 298 5515 4020 4849 49 -1362 -219 C ATOM 2427 C PHE A 298 -13.961 4.141 -11.199 1.00 39.96 C ANISOU 2427 C PHE A 298 5701 4353 5129 66 -1236 -143 C ATOM 2428 O PHE A 298 -14.393 4.467 -10.095 1.00 38.82 O ANISOU 2428 O PHE A 298 5424 4204 5122 50 -1210 -89 O ATOM 2429 CB PHE A 298 -13.402 1.699 -11.621 1.00 38.93 C ANISOU 2429 CB PHE A 298 5698 4136 4957 86 -1281 -309 C ATOM 2430 CG PHE A 298 -12.882 1.568 -10.205 1.00 39.21 C ANISOU 2430 CG PHE A 298 5613 4173 5110 99 -1170 -281 C ATOM 2431 CD1 PHE A 298 -13.669 1.008 -9.204 1.00 41.55 C ANISOU 2431 CD1 PHE A 298 5811 4415 5562 60 -1217 -244 C ATOM 2432 CD2 PHE A 298 -11.607 2.010 -9.870 1.00 40.50 C ANISOU 2432 CD2 PHE A 298 5765 4395 5228 146 -1020 -286 C ATOM 2433 CE1 PHE A 298 -13.190 0.897 -7.898 1.00 40.74 C ANISOU 2433 CE1 PHE A 298 5617 4321 5543 70 -1120 -211 C ATOM 2434 CE2 PHE A 298 -11.124 1.876 -8.572 1.00 42.24 C ANISOU 2434 CE2 PHE A 298 5886 4617 5547 158 -939 -261 C ATOM 2435 CZ PHE A 298 -11.920 1.322 -7.594 1.00 39.99 C ANISOU 2435 CZ PHE A 298 5520 4281 5392 121 -991 -223 C ATOM 2436 N ASN A 299 -13.086 4.902 -11.917 1.00 35.98 N ANISOU 2436 N ASN A 299 5280 3907 4484 93 -1157 -140 N ATOM 2437 CA ASN A 299 -12.558 6.198 -11.448 1.00 35.01 C ANISOU 2437 CA ASN A 299 5091 3836 4375 104 -1044 -70 C ATOM 2438 C ASN A 299 -13.690 7.194 -11.152 1.00 38.23 C ANISOU 2438 C ASN A 299 5410 4229 4887 76 -1123 18 C ATOM 2439 O ASN A 299 -13.615 7.935 -10.167 1.00 36.83 O ANISOU 2439 O ASN A 299 5122 4065 4808 80 -1049 61 O ATOM 2440 CB ASN A 299 -11.548 6.800 -12.446 1.00 31.88 C ANISOU 2440 CB ASN A 299 4806 3496 3809 124 -959 -72 C ATOM 2441 CG ASN A 299 -10.294 5.985 -12.637 1.00 44.61 C ANISOU 2441 CG ASN A 299 6477 5133 5341 162 -844 -162 C ATOM 2442 OD1 ASN A 299 -10.023 5.024 -11.911 1.00 33.09 O ANISOU 2442 OD1 ASN A 299 4967 3644 3960 181 -822 -218 O ATOM 2443 ND2 ASN A 299 -9.494 6.353 -13.624 1.00 37.00 N ANISOU 2443 ND2 ASN A 299 5618 4220 4220 176 -766 -173 N ATOM 2444 N ASP A 300 -14.749 7.157 -11.969 1.00 35.86 N ANISOU 2444 N ASP A 300 5156 3896 4574 52 -1280 36 N ATOM 2445 CA ASP A 300 -15.939 7.996 -11.816 1.00 36.77 C ANISOU 2445 CA ASP A 300 5181 3984 4806 31 -1380 113 C ATOM 2446 C ASP A 300 -16.673 7.709 -10.519 1.00 38.50 C ANISOU 2446 C ASP A 300 5236 4173 5219 16 -1374 120 C ATOM 2447 O ASP A 300 -17.040 8.647 -9.818 1.00 37.45 O ANISOU 2447 O ASP A 300 4990 4043 5195 20 -1340 172 O ATOM 2448 CB ASP A 300 -16.873 7.847 -13.021 1.00 41.07 C ANISOU 2448 CB ASP A 300 5815 4497 5294 10 -1571 122 C ATOM 2449 CG ASP A 300 -16.669 8.933 -14.044 1.00 62.38 C ANISOU 2449 CG ASP A 300 8619 7223 7861 19 -1597 186 C ATOM 2450 OD1 ASP A 300 -17.532 9.831 -14.131 1.00 65.95 O ANISOU 2450 OD1 ASP A 300 9011 7649 8397 13 -1687 266 O ATOM 2451 OD2 ASP A 300 -15.621 8.914 -14.731 1.00 72.36 O ANISOU 2451 OD2 ASP A 300 10020 8532 8942 32 -1517 160 O ATOM 2452 N ARG A 301 -16.828 6.418 -10.178 1.00 35.35 N ANISOU 2452 N ARG A 301 4827 3744 4860 -2 -1396 65 N ATOM 2453 CA ARG A 301 -17.451 5.957 -8.938 1.00 35.24 C ANISOU 2453 CA ARG A 301 4672 3705 5014 -26 -1375 76 C ATOM 2454 C ARG A 301 -16.615 6.377 -7.735 1.00 36.40 C ANISOU 2454 C ARG A 301 4751 3895 5184 -2 -1206 85 C ATOM 2455 O ARG A 301 -17.177 6.801 -6.728 1.00 36.76 O ANISOU 2455 O ARG A 301 4671 3944 5351 -11 -1165 122 O ATOM 2456 CB ARG A 301 -17.640 4.430 -8.946 1.00 36.97 C ANISOU 2456 CB ARG A 301 4921 3871 5255 -55 -1436 21 C ATOM 2457 CG ARG A 301 -18.514 3.933 -10.088 1.00 49.77 C ANISOU 2457 CG ARG A 301 6609 5440 6862 -86 -1622 -3 C ATOM 2458 CD ARG A 301 -18.839 2.459 -9.939 1.00 62.71 C ANISOU 2458 CD ARG A 301 8253 7008 8567 -124 -1689 -53 C ATOM 2459 NE ARG A 301 -20.229 2.250 -9.526 1.00 75.34 N ANISOU 2459 NE ARG A 301 9716 8556 10353 -182 -1787 -10 N ATOM 2460 CZ ARG A 301 -20.632 2.155 -8.263 1.00 90.53 C ANISOU 2460 CZ ARG A 301 11494 10477 12426 -208 -1704 38 C ATOM 2461 NH1 ARG A 301 -19.759 2.253 -7.271 1.00 76.67 N ANISOU 2461 NH1 ARG A 301 9722 8765 10645 -180 -1538 48 N ATOM 2462 NH2 ARG A 301 -21.913 1.959 -7.983 1.00 79.67 N ANISOU 2462 NH2 ARG A 301 9990 9058 11224 -265 -1786 77 N ATOM 2463 N VAL A 302 -15.277 6.259 -7.839 1.00 30.71 N ANISOU 2463 N VAL A 302 4111 3209 4349 31 -1108 48 N ATOM 2464 CA VAL A 302 -14.331 6.664 -6.797 1.00 28.98 C ANISOU 2464 CA VAL A 302 3839 3032 4139 56 -965 50 C ATOM 2465 C VAL A 302 -14.473 8.192 -6.563 1.00 35.04 C ANISOU 2465 C VAL A 302 4545 3827 4943 65 -925 102 C ATOM 2466 O VAL A 302 -14.545 8.639 -5.414 1.00 33.23 O ANISOU 2466 O VAL A 302 4218 3612 4796 67 -855 117 O ATOM 2467 CB VAL A 302 -12.885 6.260 -7.209 1.00 31.57 C ANISOU 2467 CB VAL A 302 4263 3386 4347 91 -888 -3 C ATOM 2468 CG1 VAL A 302 -11.817 7.013 -6.411 1.00 30.13 C ANISOU 2468 CG1 VAL A 302 4031 3251 4165 117 -757 4 C ATOM 2469 CG2 VAL A 302 -12.687 4.760 -7.087 1.00 31.11 C ANISOU 2469 CG2 VAL A 302 4241 3288 4291 93 -912 -59 C ATOM 2470 N TYR A 303 -14.532 8.968 -7.666 1.00 33.34 N ANISOU 2470 N TYR A 303 4395 3613 4661 70 -974 129 N ATOM 2471 CA TYR A 303 -14.637 10.421 -7.638 1.00 34.47 C ANISOU 2471 CA TYR A 303 4496 3762 4838 79 -953 182 C ATOM 2472 C TYR A 303 -15.942 10.849 -6.947 1.00 37.76 C ANISOU 2472 C TYR A 303 4784 4147 5414 69 -1005 214 C ATOM 2473 O TYR A 303 -15.898 11.698 -6.053 1.00 36.91 O ANISOU 2473 O TYR A 303 4591 4049 5385 83 -929 225 O ATOM 2474 CB TYR A 303 -14.529 10.988 -9.075 1.00 38.04 C ANISOU 2474 CB TYR A 303 5065 4212 5178 79 -1017 218 C ATOM 2475 CG TYR A 303 -14.748 12.481 -9.157 1.00 41.28 C ANISOU 2475 CG TYR A 303 5440 4607 5636 86 -1020 288 C ATOM 2476 CD1 TYR A 303 -13.706 13.373 -8.920 1.00 43.15 C ANISOU 2476 CD1 TYR A 303 5679 4867 5850 97 -904 303 C ATOM 2477 CD2 TYR A 303 -16.002 13.005 -9.442 1.00 43.14 C ANISOU 2477 CD2 TYR A 303 5633 4798 5962 82 -1147 338 C ATOM 2478 CE1 TYR A 303 -13.904 14.749 -8.985 1.00 45.12 C ANISOU 2478 CE1 TYR A 303 5900 5086 6159 101 -913 367 C ATOM 2479 CE2 TYR A 303 -16.219 14.380 -9.480 1.00 44.68 C ANISOU 2479 CE2 TYR A 303 5792 4963 6222 95 -1158 402 C ATOM 2480 CZ TYR A 303 -15.165 15.248 -9.264 1.00 52.36 C ANISOU 2480 CZ TYR A 303 6779 5951 7163 103 -1041 417 C ATOM 2481 OH TYR A 303 -15.381 16.600 -9.313 1.00 57.74 O ANISOU 2481 OH TYR A 303 7429 6587 7921 114 -1058 481 O ATOM 2482 N ALA A 304 -17.084 10.228 -7.339 1.00 33.77 N ANISOU 2482 N ALA A 304 4261 3605 4963 46 -1130 221 N ATOM 2483 CA ALA A 304 -18.407 10.488 -6.774 1.00 33.30 C ANISOU 2483 CA ALA A 304 4065 3515 5072 34 -1182 248 C ATOM 2484 C ALA A 304 -18.450 10.137 -5.279 1.00 36.94 C ANISOU 2484 C ALA A 304 4417 3997 5621 28 -1066 226 C ATOM 2485 O ALA A 304 -18.968 10.923 -4.491 1.00 37.44 O ANISOU 2485 O ALA A 304 4368 4062 5794 40 -1017 240 O ATOM 2486 CB ALA A 304 -19.469 9.705 -7.534 1.00 34.51 C ANISOU 2486 CB ALA A 304 4224 3624 5263 1 -1342 252 C ATOM 2487 N THR A 305 -17.870 8.988 -4.890 1.00 32.60 N ANISOU 2487 N THR A 305 3908 3461 5017 12 -1020 192 N ATOM 2488 CA THR A 305 -17.811 8.557 -3.487 1.00 31.83 C ANISOU 2488 CA THR A 305 3735 3386 4973 2 -915 183 C ATOM 2489 C THR A 305 -16.953 9.504 -2.668 1.00 34.61 C ANISOU 2489 C THR A 305 4071 3784 5296 36 -791 172 C ATOM 2490 O THR A 305 -17.316 9.814 -1.528 1.00 33.97 O ANISOU 2490 O THR A 305 3899 3723 5286 35 -715 173 O ATOM 2491 CB THR A 305 -17.400 7.094 -3.379 1.00 33.53 C ANISOU 2491 CB THR A 305 4010 3588 5141 -21 -921 159 C ATOM 2492 OG1 THR A 305 -18.325 6.325 -4.134 1.00 36.72 O ANISOU 2492 OG1 THR A 305 4421 3939 5592 -58 -1049 163 O ATOM 2493 CG2 THR A 305 -17.367 6.588 -1.933 1.00 29.64 C ANISOU 2493 CG2 THR A 305 3454 3116 4693 -38 -824 168 C ATOM 2494 N TYR A 306 -15.821 9.969 -3.256 1.00 30.70 N ANISOU 2494 N TYR A 306 3664 3305 4697 63 -769 159 N ATOM 2495 CA TYR A 306 -14.923 10.942 -2.635 1.00 29.41 C ANISOU 2495 CA TYR A 306 3488 3174 4513 90 -670 146 C ATOM 2496 C TYR A 306 -15.669 12.261 -2.343 1.00 34.27 C ANISOU 2496 C TYR A 306 4018 3775 5228 103 -664 165 C ATOM 2497 O TYR A 306 -15.561 12.763 -1.232 1.00 35.68 O ANISOU 2497 O TYR A 306 4134 3974 5446 115 -581 143 O ATOM 2498 CB TYR A 306 -13.635 11.141 -3.465 1.00 29.51 C ANISOU 2498 CB TYR A 306 3600 3201 4412 106 -650 136 C ATOM 2499 CG TYR A 306 -12.772 12.299 -3.012 1.00 29.85 C ANISOU 2499 CG TYR A 306 3623 3264 4455 125 -567 130 C ATOM 2500 CD1 TYR A 306 -12.367 12.415 -1.685 1.00 31.26 C ANISOU 2500 CD1 TYR A 306 3744 3469 4662 132 -489 100 C ATOM 2501 CD2 TYR A 306 -12.361 13.281 -3.910 1.00 30.28 C ANISOU 2501 CD2 TYR A 306 3721 3305 4477 130 -573 158 C ATOM 2502 CE1 TYR A 306 -11.620 13.509 -1.253 1.00 33.19 C ANISOU 2502 CE1 TYR A 306 3969 3724 4919 145 -430 85 C ATOM 2503 CE2 TYR A 306 -11.555 14.342 -3.500 1.00 30.54 C ANISOU 2503 CE2 TYR A 306 3732 3345 4528 138 -502 154 C ATOM 2504 CZ TYR A 306 -11.193 14.454 -2.169 1.00 36.60 C ANISOU 2504 CZ TYR A 306 4435 4134 5337 146 -436 111 C ATOM 2505 OH TYR A 306 -10.418 15.506 -1.745 1.00 41.68 O ANISOU 2505 OH TYR A 306 5055 4775 6007 151 -381 98 O ATOM 2506 N GLN A 307 -16.482 12.759 -3.293 1.00 31.04 N ANISOU 2506 N GLN A 307 3605 3325 4863 104 -760 202 N ATOM 2507 CA GLN A 307 -17.316 13.973 -3.130 1.00 30.80 C ANISOU 2507 CA GLN A 307 3487 3263 4955 125 -776 222 C ATOM 2508 C GLN A 307 -18.224 13.840 -1.906 1.00 34.02 C ANISOU 2508 C GLN A 307 3766 3681 5482 124 -721 199 C ATOM 2509 O GLN A 307 -18.305 14.781 -1.133 1.00 33.02 O ANISOU 2509 O GLN A 307 3571 3553 5421 150 -652 176 O ATOM 2510 CB GLN A 307 -18.169 14.273 -4.382 1.00 31.84 C ANISOU 2510 CB GLN A 307 3634 3343 5122 124 -919 273 C ATOM 2511 CG GLN A 307 -17.411 14.584 -5.675 1.00 37.60 C ANISOU 2511 CG GLN A 307 4499 4064 5723 124 -972 308 C ATOM 2512 CD GLN A 307 -16.141 15.377 -5.473 1.00 48.50 C ANISOU 2512 CD GLN A 307 5925 5464 7041 137 -868 302 C ATOM 2513 OE1 GLN A 307 -16.158 16.510 -4.996 1.00 38.46 O ANISOU 2513 OE1 GLN A 307 4595 4166 5851 158 -831 309 O ATOM 2514 NE2 GLN A 307 -15.007 14.778 -5.810 1.00 42.24 N ANISOU 2514 NE2 GLN A 307 5228 4710 6112 126 -818 284 N ATOM 2515 N VAL A 308 -18.833 12.637 -1.695 1.00 30.45 N ANISOU 2515 N VAL A 308 3285 3236 5049 89 -741 201 N ATOM 2516 CA VAL A 308 -19.675 12.336 -0.536 1.00 29.99 C ANISOU 2516 CA VAL A 308 3109 3196 5090 75 -671 190 C ATOM 2517 C VAL A 308 -18.885 12.518 0.764 1.00 33.14 C ANISOU 2517 C VAL A 308 3512 3650 5432 87 -531 150 C ATOM 2518 O VAL A 308 -19.342 13.219 1.663 1.00 34.52 O ANISOU 2518 O VAL A 308 3601 3839 5677 107 -450 124 O ATOM 2519 CB VAL A 308 -20.365 10.943 -0.622 1.00 32.89 C ANISOU 2519 CB VAL A 308 3458 3554 5487 23 -723 212 C ATOM 2520 CG1 VAL A 308 -21.078 10.600 0.687 1.00 33.27 C ANISOU 2520 CG1 VAL A 308 3394 3631 5618 -1 -618 210 C ATOM 2521 CG2 VAL A 308 -21.339 10.885 -1.789 1.00 32.83 C ANISOU 2521 CG2 VAL A 308 3423 3489 5562 11 -875 242 C ATOM 2522 N THR A 309 -17.691 11.925 0.835 1.00 28.91 N ANISOU 2522 N THR A 309 3077 3141 4768 81 -507 139 N ATOM 2523 CA THR A 309 -16.810 11.984 2.007 1.00 28.38 C ANISOU 2523 CA THR A 309 3030 3124 4631 90 -402 104 C ATOM 2524 C THR A 309 -16.302 13.394 2.299 1.00 31.20 C ANISOU 2524 C THR A 309 3376 3484 4994 128 -354 66 C ATOM 2525 O THR A 309 -16.048 13.703 3.453 1.00 30.65 O ANISOU 2525 O THR A 309 3287 3452 4907 138 -269 27 O ATOM 2526 CB THR A 309 -15.693 10.929 1.934 1.00 32.36 C ANISOU 2526 CB THR A 309 3632 3644 5021 78 -409 105 C ATOM 2527 OG1 THR A 309 -14.703 11.337 0.984 1.00 28.05 O ANISOU 2527 OG1 THR A 309 3158 3085 4414 99 -444 96 O ATOM 2528 CG2 THR A 309 -16.223 9.534 1.620 1.00 26.95 C ANISOU 2528 CG2 THR A 309 2960 2936 4345 39 -465 137 C ATOM 2529 N ARG A 310 -16.198 14.253 1.275 1.00 28.92 N ANISOU 2529 N ARG A 310 3106 3152 4732 147 -414 79 N ATOM 2530 CA ARG A 310 -15.784 15.652 1.453 1.00 29.47 C ANISOU 2530 CA ARG A 310 3163 3203 4832 179 -382 51 C ATOM 2531 C ARG A 310 -16.846 16.385 2.301 1.00 34.80 C ANISOU 2531 C ARG A 310 3728 3868 5626 203 -334 18 C ATOM 2532 O ARG A 310 -16.477 17.085 3.240 1.00 34.49 O ANISOU 2532 O ARG A 310 3674 3844 5588 223 -258 -40 O ATOM 2533 CB ARG A 310 -15.587 16.347 0.106 1.00 29.50 C ANISOU 2533 CB ARG A 310 3211 3152 4844 186 -462 94 C ATOM 2534 CG ARG A 310 -14.451 15.769 -0.737 1.00 35.89 C ANISOU 2534 CG ARG A 310 4128 3978 5529 168 -483 115 C ATOM 2535 CD ARG A 310 -14.298 16.551 -2.021 1.00 42.28 C ANISOU 2535 CD ARG A 310 4991 4741 6332 171 -546 166 C ATOM 2536 NE ARG A 310 -13.731 17.880 -1.769 1.00 39.12 N ANISOU 2536 NE ARG A 310 4577 4311 5974 185 -504 157 N ATOM 2537 CZ ARG A 310 -13.741 18.878 -2.640 1.00 50.28 C ANISOU 2537 CZ ARG A 310 6018 5669 7418 188 -551 210 C ATOM 2538 NH1 ARG A 310 -14.318 18.728 -3.824 1.00 39.42 N ANISOU 2538 NH1 ARG A 310 4690 4268 6021 181 -646 275 N ATOM 2539 NH2 ARG A 310 -13.184 20.040 -2.330 1.00 46.53 N ANISOU 2539 NH2 ARG A 310 5528 5156 6994 195 -512 200 N ATOM 2540 N GLY A 311 -18.132 16.114 2.026 1.00 31.29 N ANISOU 2540 N GLY A 311 3207 3402 5280 199 -374 46 N ATOM 2541 CA GLY A 311 -19.262 16.647 2.780 1.00 31.38 C ANISOU 2541 CA GLY A 311 3095 3407 5422 223 -320 14 C ATOM 2542 C GLY A 311 -19.289 16.109 4.204 1.00 34.51 C ANISOU 2542 C GLY A 311 3466 3875 5770 209 -193 -30 C ATOM 2543 O GLY A 311 -19.486 16.873 5.153 1.00 32.22 O ANISOU 2543 O GLY A 311 3125 3600 5517 240 -102 -94 O ATOM 2544 N LEU A 312 -19.048 14.789 4.362 1.00 31.67 N ANISOU 2544 N LEU A 312 3155 3558 5320 163 -190 4 N ATOM 2545 CA LEU A 312 -18.993 14.121 5.673 1.00 31.92 C ANISOU 2545 CA LEU A 312 3188 3660 5282 139 -81 -14 C ATOM 2546 C LEU A 312 -17.837 14.665 6.522 1.00 36.76 C ANISOU 2546 C LEU A 312 3873 4311 5785 161 -19 -74 C ATOM 2547 O LEU A 312 -18.016 14.875 7.727 1.00 37.20 O ANISOU 2547 O LEU A 312 3906 4416 5812 168 84 -121 O ATOM 2548 CB LEU A 312 -18.911 12.586 5.546 1.00 31.21 C ANISOU 2548 CB LEU A 312 3144 3585 5130 84 -112 46 C ATOM 2549 CG LEU A 312 -20.113 11.866 4.896 1.00 36.32 C ANISOU 2549 CG LEU A 312 3715 4195 5889 48 -173 101 C ATOM 2550 CD1 LEU A 312 -19.822 10.356 4.689 1.00 35.63 C ANISOU 2550 CD1 LEU A 312 3697 4104 5738 -5 -222 153 C ATOM 2551 CD2 LEU A 312 -21.380 12.046 5.707 1.00 38.53 C ANISOU 2551 CD2 LEU A 312 3861 4497 6282 40 -78 95 C ATOM 2552 N ALA A 313 -16.679 14.950 5.881 1.00 32.31 N ANISOU 2552 N ALA A 313 3391 3725 5163 172 -82 -76 N ATOM 2553 CA ALA A 313 -15.500 15.532 6.544 1.00 32.21 C ANISOU 2553 CA ALA A 313 3436 3735 5067 189 -48 -133 C ATOM 2554 C ALA A 313 -15.837 16.908 7.130 1.00 37.78 C ANISOU 2554 C ALA A 313 4088 4424 5842 228 7 -210 C ATOM 2555 O ALA A 313 -15.477 17.182 8.273 1.00 37.95 O ANISOU 2555 O ALA A 313 4129 4490 5801 237 75 -275 O ATOM 2556 CB ALA A 313 -14.342 15.649 5.568 1.00 31.74 C ANISOU 2556 CB ALA A 313 3445 3644 4970 189 -122 -114 C ATOM 2557 N SER A 314 -16.577 17.742 6.375 1.00 35.72 N ANISOU 2557 N SER A 314 3762 4096 5713 255 -28 -204 N ATOM 2558 CA SER A 314 -16.970 19.078 6.826 1.00 37.08 C ANISOU 2558 CA SER A 314 3876 4230 5982 301 14 -279 C ATOM 2559 C SER A 314 -17.973 19.063 7.980 1.00 41.78 C ANISOU 2559 C SER A 314 4394 4872 6607 317 128 -336 C ATOM 2560 O SER A 314 -17.894 19.923 8.848 1.00 40.68 O ANISOU 2560 O SER A 314 4246 4736 6474 351 197 -431 O ATOM 2561 CB SER A 314 -17.470 19.931 5.664 1.00 42.26 C ANISOU 2561 CB SER A 314 4486 4792 6778 328 -69 -244 C ATOM 2562 OG SER A 314 -18.628 19.380 5.070 1.00 58.07 O ANISOU 2562 OG SER A 314 6417 6783 8864 322 -107 -185 O ATOM 2563 N LEU A 315 -18.862 18.049 8.018 1.00 40.72 N ANISOU 2563 N LEU A 315 4210 4776 6486 288 152 -283 N ATOM 2564 CA LEU A 315 -19.891 17.855 9.044 1.00 43.11 C ANISOU 2564 CA LEU A 315 4430 5132 6818 291 276 -318 C ATOM 2565 C LEU A 315 -19.387 17.796 10.491 1.00 48.23 C ANISOU 2565 C LEU A 315 5141 5865 7319 287 392 -387 C ATOM 2566 O LEU A 315 -20.145 18.136 11.402 1.00 48.58 O ANISOU 2566 O LEU A 315 5123 5947 7388 308 514 -451 O ATOM 2567 CB LEU A 315 -20.776 16.637 8.729 1.00 43.74 C ANISOU 2567 CB LEU A 315 4451 5230 6936 242 268 -229 C ATOM 2568 CG LEU A 315 -21.806 16.823 7.620 1.00 49.30 C ANISOU 2568 CG LEU A 315 5048 5861 7824 254 181 -184 C ATOM 2569 CD1 LEU A 315 -22.234 15.482 7.056 1.00 49.72 C ANISOU 2569 CD1 LEU A 315 5090 5918 7883 191 120 -91 C ATOM 2570 CD2 LEU A 315 -23.022 17.598 8.115 1.00 53.49 C ANISOU 2570 CD2 LEU A 315 5428 6380 8516 300 271 -243 C ATOM 2571 N ASN A 316 -18.115 17.384 10.698 1.00 44.31 N ANISOU 2571 N ASN A 316 4767 5399 6671 262 352 -378 N ATOM 2572 CA ASN A 316 -17.461 17.308 12.016 1.00 44.51 C ANISOU 2572 CA ASN A 316 4875 5502 6537 256 426 -438 C ATOM 2573 C ASN A 316 -17.551 18.617 12.793 1.00 48.26 C ANISOU 2573 C ASN A 316 5333 5972 7032 309 498 -569 C ATOM 2574 O ASN A 316 -17.752 18.589 14.011 1.00 48.25 O ANISOU 2574 O ASN A 316 5355 6046 6931 311 609 -630 O ATOM 2575 CB ASN A 316 -15.988 16.922 11.868 1.00 42.52 C ANISOU 2575 CB ASN A 316 4736 5255 6166 235 335 -414 C ATOM 2576 CG ASN A 316 -15.776 15.488 11.509 1.00 63.59 C ANISOU 2576 CG ASN A 316 7443 7943 8775 187 287 -307 C ATOM 2577 OD1 ASN A 316 -15.244 15.167 10.442 1.00 63.52 O ANISOU 2577 OD1 ASN A 316 7453 7886 8794 179 190 -255 O ATOM 2578 ND2 ASN A 316 -16.172 14.595 12.399 1.00 52.06 N ANISOU 2578 ND2 ASN A 316 6001 6550 7230 153 358 -272 N ATOM 2579 N SER A 317 -17.406 19.757 12.077 1.00 44.00 N ANISOU 2579 N SER A 317 4760 5340 6618 351 435 -612 N ATOM 2580 CA SER A 317 -17.462 21.118 12.618 1.00 44.85 C ANISOU 2580 CA SER A 317 4848 5410 6783 407 480 -743 C ATOM 2581 C SER A 317 -18.754 21.448 13.362 1.00 49.92 C ANISOU 2581 C SER A 317 5396 6078 7493 447 618 -815 C ATOM 2582 O SER A 317 -18.731 22.244 14.298 1.00 50.66 O ANISOU 2582 O SER A 317 5506 6184 7559 486 696 -945 O ATOM 2583 CB SER A 317 -17.171 22.144 11.530 1.00 47.28 C ANISOU 2583 CB SER A 317 5131 5596 7235 436 375 -742 C ATOM 2584 OG SER A 317 -15.819 22.018 11.121 1.00 52.26 O ANISOU 2584 OG SER A 317 5853 6215 7786 401 280 -706 O ATOM 2585 N CYS A 318 -19.864 20.800 12.986 1.00 46.77 N ANISOU 2585 N CYS A 318 4897 5691 7181 434 653 -739 N ATOM 2586 CA CYS A 318 -21.139 21.009 13.660 1.00 47.93 C ANISOU 2586 CA CYS A 318 4932 5870 7409 467 799 -798 C ATOM 2587 C CYS A 318 -21.576 19.833 14.549 1.00 50.26 C ANISOU 2587 C CYS A 318 5237 6287 7572 412 924 -754 C ATOM 2588 O CYS A 318 -22.593 19.935 15.224 1.00 50.87 O ANISOU 2588 O CYS A 318 5224 6409 7694 431 1074 -803 O ATOM 2589 CB CYS A 318 -22.226 21.444 12.680 1.00 48.67 C ANISOU 2589 CB CYS A 318 4871 5872 7747 505 757 -767 C ATOM 2590 SG CYS A 318 -22.652 20.213 11.430 1.00 51.52 S ANISOU 2590 SG CYS A 318 5186 6218 8169 440 642 -592 S ATOM 2591 N VAL A 319 -20.770 18.747 14.589 1.00 44.92 N ANISOU 2591 N VAL A 319 4673 5661 6734 345 869 -663 N ATOM 2592 CA VAL A 319 -20.985 17.552 15.417 1.00 44.75 C ANISOU 2592 CA VAL A 319 4690 5744 6568 283 965 -598 C ATOM 2593 C VAL A 319 -20.171 17.689 16.725 1.00 47.40 C ANISOU 2593 C VAL A 319 5166 6165 6680 283 1031 -677 C ATOM 2594 O VAL A 319 -20.701 17.415 17.805 1.00 47.24 O ANISOU 2594 O VAL A 319 5155 6237 6556 267 1183 -697 O ATOM 2595 CB VAL A 319 -20.691 16.236 14.635 1.00 48.31 C ANISOU 2595 CB VAL A 319 5174 6183 7001 214 855 -448 C ATOM 2596 CG1 VAL A 319 -20.672 15.013 15.553 1.00 48.86 C ANISOU 2596 CG1 VAL A 319 5314 6346 6905 147 934 -374 C ATOM 2597 CG2 VAL A 319 -21.704 16.033 13.508 1.00 48.21 C ANISOU 2597 CG2 VAL A 319 5021 6101 7195 208 806 -379 C ATOM 2598 N ASN A 320 -18.918 18.194 16.627 1.00 42.71 N ANISOU 2598 N ASN A 320 4674 5538 6016 301 918 -726 N ATOM 2599 CA ASN A 320 -18.014 18.414 17.762 1.00 42.64 C ANISOU 2599 CA ASN A 320 4801 5595 5805 303 936 -808 C ATOM 2600 C ASN A 320 -18.587 19.196 18.955 1.00 49.43 C ANISOU 2600 C ASN A 320 5663 6515 6603 345 1096 -952 C ATOM 2601 O ASN A 320 -18.308 18.761 20.065 1.00 50.09 O ANISOU 2601 O ASN A 320 5855 6699 6476 318 1161 -964 O ATOM 2602 CB ASN A 320 -16.663 18.976 17.319 1.00 40.97 C ANISOU 2602 CB ASN A 320 4663 5320 5585 317 780 -843 C ATOM 2603 CG ASN A 320 -15.813 18.014 16.537 1.00 49.45 C ANISOU 2603 CG ASN A 320 5780 6373 6634 271 646 -716 C ATOM 2604 OD1 ASN A 320 -15.908 16.785 16.675 1.00 43.28 O ANISOU 2604 OD1 ASN A 320 5030 5643 5773 223 655 -609 O ATOM 2605 ND2 ASN A 320 -14.929 18.560 15.720 1.00 34.81 N ANISOU 2605 ND2 ASN A 320 3935 4442 4851 285 524 -729 N ATOM 2606 N PRO A 321 -19.413 20.278 18.809 1.00 47.41 N ANISOU 2606 N PRO A 321 5295 6205 6514 410 1167 -1059 N ATOM 2607 CA PRO A 321 -19.969 20.942 20.006 1.00 49.76 C ANISOU 2607 CA PRO A 321 5599 6567 6740 454 1338 -1208 C ATOM 2608 C PRO A 321 -20.705 20.032 21.002 1.00 56.39 C ANISOU 2608 C PRO A 321 6455 7542 7428 411 1518 -1165 C ATOM 2609 O PRO A 321 -20.625 20.282 22.200 1.00 57.51 O ANISOU 2609 O PRO A 321 6691 7772 7387 422 1630 -1269 O ATOM 2610 CB PRO A 321 -20.888 22.022 19.423 1.00 51.87 C ANISOU 2610 CB PRO A 321 5707 6735 7266 530 1376 -1292 C ATOM 2611 CG PRO A 321 -20.310 22.311 18.098 1.00 54.30 C ANISOU 2611 CG PRO A 321 5990 6917 7725 534 1183 -1228 C ATOM 2612 CD PRO A 321 -19.848 20.982 17.583 1.00 48.25 C ANISOU 2612 CD PRO A 321 5271 6185 6875 453 1093 -1055 C ATOM 2613 N ILE A 322 -21.371 18.961 20.517 1.00 53.51 N ANISOU 2613 N ILE A 322 6009 7194 7129 355 1541 -1010 N ATOM 2614 CA ILE A 322 -22.099 17.972 21.333 1.00 55.73 C ANISOU 2614 CA ILE A 322 6292 7591 7293 295 1708 -932 C ATOM 2615 C ILE A 322 -21.170 17.364 22.416 1.00 60.79 C ANISOU 2615 C ILE A 322 7137 8335 7624 247 1707 -910 C ATOM 2616 O ILE A 322 -21.611 17.111 23.541 1.00 62.44 O ANISOU 2616 O ILE A 322 7398 8659 7666 226 1881 -929 O ATOM 2617 CB ILE A 322 -22.756 16.880 20.419 1.00 58.51 C ANISOU 2617 CB ILE A 322 6529 7909 7792 232 1672 -755 C ATOM 2618 CG1 ILE A 322 -23.737 17.504 19.393 1.00 59.05 C ANISOU 2618 CG1 ILE A 322 6394 7878 8164 282 1659 -778 C ATOM 2619 CG2 ILE A 322 -23.454 15.782 21.233 1.00 61.18 C ANISOU 2619 CG2 ILE A 322 6868 8356 8020 155 1838 -654 C ATOM 2620 CD1 ILE A 322 -24.012 16.631 18.139 1.00 65.95 C ANISOU 2620 CD1 ILE A 322 7183 8680 9197 231 1527 -621 C ATOM 2621 N LEU A 323 -19.882 17.172 22.064 1.00 56.10 N ANISOU 2621 N LEU A 323 6657 7700 6958 232 1511 -871 N ATOM 2622 CA LEU A 323 -18.827 16.617 22.911 1.00 56.21 C ANISOU 2622 CA LEU A 323 6860 7787 6709 193 1452 -842 C ATOM 2623 C LEU A 323 -18.523 17.482 24.138 1.00 60.59 C ANISOU 2623 C LEU A 323 7531 8415 7075 233 1526 -1010 C ATOM 2624 O LEU A 323 -18.131 16.948 25.174 1.00 61.34 O ANISOU 2624 O LEU A 323 7776 8612 6919 196 1555 -986 O ATOM 2625 CB LEU A 323 -17.561 16.427 22.062 1.00 54.42 C ANISOU 2625 CB LEU A 323 6683 7478 6518 187 1220 -787 C ATOM 2626 CG LEU A 323 -16.606 15.282 22.388 1.00 59.20 C ANISOU 2626 CG LEU A 323 7426 8123 6943 129 1115 -665 C ATOM 2627 CD1 LEU A 323 -17.296 13.925 22.323 1.00 59.65 C ANISOU 2627 CD1 LEU A 323 7458 8209 6998 60 1174 -491 C ATOM 2628 CD2 LEU A 323 -15.444 15.278 21.415 1.00 58.97 C ANISOU 2628 CD2 LEU A 323 7407 8002 6998 139 906 -640 C ATOM 2629 N TYR A 324 -18.716 18.803 24.031 1.00 56.16 N ANISOU 2629 N TYR A 324 6907 7798 6632 309 1551 -1181 N ATOM 2630 CA TYR A 324 -18.446 19.734 25.129 1.00 57.06 C ANISOU 2630 CA TYR A 324 7128 7964 6587 355 1613 -1369 C ATOM 2631 C TYR A 324 -19.526 19.689 26.211 1.00 64.82 C ANISOU 2631 C TYR A 324 8114 9070 7445 359 1868 -1427 C ATOM 2632 O TYR A 324 -19.255 20.047 27.363 1.00 66.41 O ANISOU 2632 O TYR A 324 8458 9358 7416 372 1933 -1546 O ATOM 2633 CB TYR A 324 -18.261 21.177 24.609 1.00 56.70 C ANISOU 2633 CB TYR A 324 7015 7797 6730 436 1545 -1535 C ATOM 2634 CG TYR A 324 -17.420 21.313 23.353 1.00 54.57 C ANISOU 2634 CG TYR A 324 6703 7397 6634 432 1328 -1469 C ATOM 2635 CD1 TYR A 324 -16.265 20.556 23.176 1.00 54.74 C ANISOU 2635 CD1 TYR A 324 6822 7425 6551 377 1164 -1359 C ATOM 2636 CD2 TYR A 324 -17.750 22.238 22.369 1.00 54.04 C ANISOU 2636 CD2 TYR A 324 6501 7200 6830 486 1289 -1519 C ATOM 2637 CE1 TYR A 324 -15.489 20.679 22.029 1.00 53.55 C ANISOU 2637 CE1 TYR A 324 6630 7165 6553 374 988 -1303 C ATOM 2638 CE2 TYR A 324 -16.976 22.378 21.220 1.00 52.63 C ANISOU 2638 CE2 TYR A 324 6295 6911 6792 477 1105 -1452 C ATOM 2639 CZ TYR A 324 -15.851 21.588 21.050 1.00 57.84 C ANISOU 2639 CZ TYR A 324 7048 7589 7341 420 965 -1347 C ATOM 2640 OH TYR A 324 -15.087 21.712 19.922 1.00 53.58 O ANISOU 2640 OH TYR A 324 6478 6948 6932 411 805 -1284 O ATOM 2641 N PHE A 325 -20.743 19.252 25.840 1.00 61.95 N ANISOU 2641 N PHE A 325 7593 8714 7231 345 2012 -1344 N ATOM 2642 CA PHE A 325 -21.883 19.189 26.754 1.00 64.55 C ANISOU 2642 CA PHE A 325 7888 9157 7482 346 2280 -1388 C ATOM 2643 C PHE A 325 -22.203 17.775 27.260 1.00 69.17 C ANISOU 2643 C PHE A 325 8526 9854 7901 245 2377 -1198 C ATOM 2644 O PHE A 325 -22.860 17.645 28.292 1.00 72.13 O ANISOU 2644 O PHE A 325 8938 10353 8116 229 2599 -1228 O ATOM 2645 CB PHE A 325 -23.116 19.899 26.147 1.00 66.97 C ANISOU 2645 CB PHE A 325 7962 9395 8088 412 2404 -1462 C ATOM 2646 CG PHE A 325 -22.825 21.276 25.575 1.00 68.16 C ANISOU 2646 CG PHE A 325 8059 9414 8426 509 2295 -1628 C ATOM 2647 CD1 PHE A 325 -22.721 22.388 26.407 1.00 73.32 C ANISOU 2647 CD1 PHE A 325 8781 10082 8996 584 2373 -1851 C ATOM 2648 CD2 PHE A 325 -22.652 21.457 24.208 1.00 68.09 C ANISOU 2648 CD2 PHE A 325 7939 9261 8671 522 2112 -1560 C ATOM 2649 CE1 PHE A 325 -22.437 23.655 25.878 1.00 73.68 C ANISOU 2649 CE1 PHE A 325 8778 9988 9228 669 2264 -1997 C ATOM 2650 CE2 PHE A 325 -22.357 22.722 23.682 1.00 70.26 C ANISOU 2650 CE2 PHE A 325 8173 9407 9116 604 2008 -1694 C ATOM 2651 CZ PHE A 325 -22.255 23.811 24.519 1.00 70.24 C ANISOU 2651 CZ PHE A 325 8232 9408 9047 675 2082 -1909 C ATOM 2652 N LEU A 326 -21.716 16.727 26.565 1.00 63.31 N ANISOU 2652 N LEU A 326 7797 9068 7191 176 2216 -1007 N ATOM 2653 CA LEU A 326 -21.938 15.323 26.938 1.00 63.44 C ANISOU 2653 CA LEU A 326 7866 9162 7076 75 2275 -810 C ATOM 2654 C LEU A 326 -20.678 14.588 27.440 1.00 66.24 C ANISOU 2654 C LEU A 326 8441 9553 7173 25 2117 -719 C ATOM 2655 O LEU A 326 -20.801 13.610 28.180 1.00 66.52 O ANISOU 2655 O LEU A 326 8576 9679 7018 -50 2195 -589 O ATOM 2656 CB LEU A 326 -22.567 14.537 25.770 1.00 62.20 C ANISOU 2656 CB LEU A 326 7536 8920 7178 29 2232 -649 C ATOM 2657 CG LEU A 326 -24.061 14.737 25.496 1.00 68.33 C ANISOU 2657 CG LEU A 326 8090 9693 8180 39 2423 -665 C ATOM 2658 CD1 LEU A 326 -24.473 13.989 24.250 1.00 67.11 C ANISOU 2658 CD1 LEU A 326 7785 9436 8277 -5 2315 -516 C ATOM 2659 CD2 LEU A 326 -24.923 14.245 26.660 1.00 73.60 C ANISOU 2659 CD2 LEU A 326 8771 10502 8692 -17 2692 -627 C ATOM 2660 N ALA A 327 -19.481 15.028 27.009 1.00 61.08 N ANISOU 2660 N ALA A 327 7855 8823 6528 65 1894 -777 N ATOM 2661 CA ALA A 327 -18.210 14.405 27.395 1.00 60.46 C ANISOU 2661 CA ALA A 327 7962 8764 6245 30 1716 -702 C ATOM 2662 C ALA A 327 -17.271 15.384 28.126 1.00 65.32 C ANISOU 2662 C ALA A 327 8721 9408 6690 83 1638 -879 C ATOM 2663 O ALA A 327 -16.193 14.989 28.583 1.00 64.69 O ANISOU 2663 O ALA A 327 8799 9353 6427 60 1488 -838 O ATOM 2664 CB ALA A 327 -17.525 13.822 26.168 1.00 58.50 C ANISOU 2664 CB ALA A 327 7659 8396 6171 15 1501 -585 C ATOM 2665 N GLY A 328 -17.705 16.637 28.241 1.00 63.00 N ANISOU 2665 N GLY A 328 8365 9104 6467 153 1734 -1074 N ATOM 2666 CA GLY A 328 -16.951 17.697 28.896 1.00 64.01 C ANISOU 2666 CA GLY A 328 8612 9244 6467 207 1670 -1270 C ATOM 2667 C GLY A 328 -17.417 18.034 30.295 1.00 71.58 C ANISOU 2667 C GLY A 328 9693 10339 7163 217 1862 -1391 C ATOM 2668 O GLY A 328 -18.524 17.668 30.702 1.00 72.79 O ANISOU 2668 O GLY A 328 9803 10577 7276 195 2092 -1349 O ATOM 2669 N ASP A 329 -16.567 18.763 31.028 1.00 69.41 N ANISOU 2669 N ASP A 329 9572 10088 6714 249 1770 -1549 N ATOM 2670 CA ASP A 329 -16.821 19.213 32.395 1.00 72.14 C ANISOU 2670 CA ASP A 329 10070 10562 6778 267 1922 -1701 C ATOM 2671 C ASP A 329 -17.875 20.320 32.429 1.00 76.60 C ANISOU 2671 C ASP A 329 10511 11112 7481 345 2134 -1899 C ATOM 2672 O ASP A 329 -17.906 21.168 31.532 1.00 74.34 O ANISOU 2672 O ASP A 329 10076 10689 7480 404 2068 -1988 O ATOM 2673 CB ASP A 329 -15.511 19.701 33.043 1.00 74.74 C ANISOU 2673 CB ASP A 329 10592 10896 6909 279 1715 -1821 C ATOM 2674 CG ASP A 329 -14.447 18.637 33.263 1.00 86.00 C ANISOU 2674 CG ASP A 329 12162 12354 8159 211 1509 -1645 C ATOM 2675 OD1 ASP A 329 -14.740 17.435 33.035 1.00 86.11 O ANISOU 2675 OD1 ASP A 329 12151 12395 8173 149 1539 -1421 O ATOM 2676 OD2 ASP A 329 -13.318 19.001 33.640 1.00 92.92 O ANISOU 2676 OD2 ASP A 329 13168 13220 8919 219 1309 -1730 O ATOM 2677 N THR A 330 -18.723 20.320 33.480 1.00 75.85 N ANISOU 2677 N THR A 330 10481 11156 7182 347 2390 -1966 N ATOM 2678 CA THR A 330 -19.805 21.290 33.693 1.00 77.25 C ANISOU 2678 CA THR A 330 10548 11341 7464 426 2629 -2162 C ATOM 2679 C THR A 330 -19.316 22.740 33.656 1.00 81.37 C ANISOU 2679 C THR A 330 11081 11760 8075 520 2528 -2424 C ATOM 2680 O THR A 330 -18.214 23.026 34.132 1.00 80.69 O ANISOU 2680 O THR A 330 11174 11675 7810 517 2347 -2505 O ATOM 2681 CB THR A 330 -20.544 20.980 34.999 1.00 88.22 C ANISOU 2681 CB THR A 330 12054 12919 8547 404 2910 -2193 C ATOM 2682 N PHE A 331 -20.125 23.646 33.069 1.00 78.76 N ANISOU 2682 N PHE A 331 10555 11330 8039 602 2630 -2550 N ATOM 2683 CA PHE A 331 -19.792 25.070 32.972 1.00 79.32 C ANISOU 2683 CA PHE A 331 10617 11280 8242 695 2547 -2798 C ATOM 2684 C PHE A 331 -20.066 25.787 34.293 1.00 86.39 C ANISOU 2684 C PHE A 331 11655 12278 8892 751 2726 -3050 C ATOM 2685 O PHE A 331 -21.224 26.008 34.660 1.00 87.51 O ANISOU 2685 O PHE A 331 11710 12481 9061 799 3000 -3137 O ATOM 2686 CB PHE A 331 -20.499 25.741 31.776 1.00 80.02 C ANISOU 2686 CB PHE A 331 10447 11206 8752 763 2559 -2819 C ATOM 2687 CG PHE A 331 -19.950 25.311 30.435 1.00 78.48 C ANISOU 2687 CG PHE A 331 10149 10885 8783 719 2328 -2621 C ATOM 2688 CD1 PHE A 331 -18.855 25.958 29.873 1.00 80.21 C ANISOU 2688 CD1 PHE A 331 10402 10969 9107 731 2076 -2669 C ATOM 2689 CD2 PHE A 331 -20.521 24.251 29.739 1.00 79.34 C ANISOU 2689 CD2 PHE A 331 10132 11013 8999 662 2367 -2390 C ATOM 2690 CE1 PHE A 331 -18.327 25.538 28.648 1.00 78.50 C ANISOU 2690 CE1 PHE A 331 10099 10650 9078 689 1882 -2488 C ATOM 2691 CE2 PHE A 331 -20.002 23.842 28.507 1.00 79.58 C ANISOU 2691 CE2 PHE A 331 10084 10934 9219 625 2158 -2220 C ATOM 2692 CZ PHE A 331 -18.911 24.491 27.967 1.00 76.30 C ANISOU 2692 CZ PHE A 331 9707 10396 8889 640 1925 -2270 C ATOM 2693 N ARG A 332 -18.982 26.100 35.029 1.00 84.19 N ANISOU 2693 N ARG A 332 11599 12023 8365 742 2569 -3165 N ATOM 2694 CA ARG A 332 -19.029 26.755 36.336 1.00 87.40 C ANISOU 2694 CA ARG A 332 12190 12530 8489 788 2693 -3415 C ATOM 2695 C ARG A 332 -17.870 27.732 36.541 1.00 91.76 C ANISOU 2695 C ARG A 332 12875 12982 9009 819 2446 -3614 C ATOM 2696 O ARG A 332 -16.747 27.464 36.105 1.00 89.23 O ANISOU 2696 O ARG A 332 12598 12594 8711 764 2169 -3505 O ATOM 2697 CB ARG A 332 -19.040 25.707 37.459 1.00 89.24 C ANISOU 2697 CB ARG A 332 12628 12981 8296 710 2808 -3310 C ATOM 2698 N ARG A 333 -18.153 28.859 37.222 1.00 91.24 N ANISOU 2698 N ARG A 333 12867 12903 8896 906 2552 -3913 N ATOM 2699 CA ARG A 333 -17.174 29.899 37.539 1.00 91.91 C ANISOU 2699 CA ARG A 333 13081 12888 8951 940 2341 -4142 C ATOM 2700 C ARG A 333 -16.895 29.951 39.050 1.00 98.90 C ANISOU 2700 C ARG A 333 14253 13938 9386 935 2394 -4317 C ATOM 2701 O ARG A 333 -17.669 30.540 39.809 1.00101.22 O ANISOU 2701 O ARG A 333 14593 14294 9574 1009 2627 -4542 O ATOM 2702 CB ARG A 333 -17.618 31.269 36.994 1.00 92.43 C ANISOU 2702 CB ARG A 333 12986 12763 9371 1050 2371 -4361 C ATOM 2703 CG ARG A 333 -17.320 31.465 35.512 1.00 98.10 C ANISOU 2703 CG ARG A 333 13492 13278 10503 1045 2183 -4218 C ATOM 2704 CD ARG A 333 -17.774 32.824 35.014 1.00107.47 C ANISOU 2704 CD ARG A 333 14533 14270 12032 1153 2207 -4425 C ATOM 2705 NE ARG A 333 -16.955 33.921 35.537 1.00119.04 N ANISOU 2705 NE ARG A 333 16139 15636 13453 1186 2049 -4685 N ATOM 2706 CZ ARG A 333 -15.868 34.403 34.942 1.00133.39 C ANISOU 2706 CZ ARG A 333 17957 17292 15432 1153 1762 -4676 C ATOM 2707 NH1 ARG A 333 -15.448 33.890 33.791 1.00120.47 N ANISOU 2707 NH1 ARG A 333 16194 15582 13998 1090 1610 -4421 N ATOM 2708 NH2 ARG A 333 -15.190 35.400 35.494 1.00120.71 N ANISOU 2708 NH2 ARG A 333 16479 15598 13788 1179 1630 -4924 N ATOM 2709 N ARG A 334 -15.792 29.304 39.476 1.00 95.06 N ANISOU 2709 N ARG A 334 13960 13525 8634 849 2175 -4209 N ATOM 2710 CA ARG A 334 -15.353 29.230 40.869 1.00123.28 C ANISOU 2710 CA ARG A 334 17831 17258 11753 827 2165 -4337 C ATOM 2711 C ARG A 334 -14.233 30.229 41.141 1.00151.93 C ANISOU 2711 C ARG A 334 21585 20774 15369 849 1889 -4569 C ATOM 2712 O ARG A 334 -14.317 31.383 40.726 1.00113.60 O ANISOU 2712 O ARG A 334 16618 15749 10795 923 1863 -4768 O ATOM 2713 CB ARG A 334 -14.891 27.806 41.211 1.00122.80 C ANISOU 2713 CB ARG A 334 17907 17351 11402 718 2087 -4057 C TER 2714 ARG A 334 HETATM 2715 FAE BUR A1101 -22.516 34.054 10.798 1.00 69.95 F HETATM 2716 CBF BUR A1101 -22.766 35.322 10.367 1.00 68.21 C HETATM 2717 FAF BUR A1101 -23.565 35.893 11.261 1.00 70.42 F HETATM 2718 FAG BUR A1101 -23.428 35.265 9.109 1.00 67.18 F HETATM 2719 OAW BUR A1101 -21.536 36.100 10.285 1.00 63.03 O HETATM 2720 CAZ BUR A1101 -20.594 35.669 9.384 1.00 57.58 C HETATM 2721 CAQ BUR A1101 -19.564 34.807 9.791 1.00 53.89 C HETATM 2722 CAO BUR A1101 -18.600 34.380 8.866 1.00 52.34 C HETATM 2723 CAR BUR A1101 -20.623 36.130 8.058 1.00 55.65 C HETATM 2724 CAP BUR A1101 -19.660 35.691 7.141 1.00 53.91 C HETATM 2725 CAY BUR A1101 -18.627 34.812 7.528 1.00 51.43 C HETATM 2726 NAT BUR A1101 -17.633 34.370 6.711 1.00 48.52 N HETATM 2727 CAX BUR A1101 -17.344 34.868 5.473 1.00 49.06 C HETATM 2728 OAD BUR A1101 -18.037 35.735 4.931 1.00 50.66 O HETATM 2729 NAU BUR A1101 -16.306 34.268 4.819 1.00 47.93 N HETATM 2730 CBA BUR A1101 -15.808 34.701 3.625 1.00 46.23 C HETATM 2731 CAL BUR A1101 -16.550 35.332 2.606 1.00 45.46 C HETATM 2732 CAJ BUR A1101 -15.928 35.768 1.430 1.00 44.62 C HETATM 2733 CAK BUR A1101 -14.555 35.568 1.267 1.00 45.24 C HETATM 2734 NAS BUR A1101 -13.823 34.942 2.302 1.00 45.23 N HETATM 2735 CBC BUR A1101 -14.431 34.503 3.432 1.00 45.17 C HETATM 2736 OAV BUR A1101 -13.763 33.867 4.460 1.00 47.46 O HETATM 2737 CBB BUR A1101 -12.541 33.255 4.260 1.00 47.34 C HETATM 2738 CAM BUR A1101 -12.339 32.374 3.182 1.00 47.05 C HETATM 2739 CAH BUR A1101 -11.101 31.766 2.977 1.00 45.81 C HETATM 2740 CAI BUR A1101 -10.071 31.974 3.890 1.00 46.01 C HETATM 2741 CAN BUR A1101 -10.282 32.814 4.986 1.00 46.98 C HETATM 2742 CBD BUR A1101 -11.508 33.468 5.224 1.00 47.68 C HETATM 2743 CBE BUR A1101 -11.617 34.333 6.389 1.00 46.67 C HETATM 2744 CAC BUR A1101 -12.719 33.863 7.356 1.00 45.71 C HETATM 2745 CAA BUR A1101 -10.304 34.380 7.202 1.00 45.10 C HETATM 2746 CAB BUR A1101 -11.918 35.783 5.979 1.00 45.74 C HETATM 2747 C1 CLR A1102 8.534 17.784 0.156 1.00 36.20 C HETATM 2748 C2 CLR A1102 8.381 17.519 -1.367 1.00 36.02 C HETATM 2749 C3 CLR A1102 8.020 16.026 -1.634 1.00 35.50 C HETATM 2750 C4 CLR A1102 6.731 15.623 -0.867 1.00 34.91 C HETATM 2751 C5 CLR A1102 6.814 15.954 0.611 1.00 34.77 C HETATM 2752 C6 CLR A1102 6.474 14.976 1.490 1.00 32.81 C HETATM 2753 C7 CLR A1102 6.507 15.121 2.985 1.00 34.45 C HETATM 2754 C8 CLR A1102 6.684 16.588 3.480 1.00 35.99 C HETATM 2755 C9 CLR A1102 7.741 17.339 2.563 1.00 37.55 C HETATM 2756 C10 CLR A1102 7.279 17.383 1.033 1.00 36.69 C HETATM 2757 C11 CLR A1102 8.334 18.672 3.156 1.00 40.15 C HETATM 2758 C12 CLR A1102 8.585 18.678 4.700 1.00 40.81 C HETATM 2759 C13 CLR A1102 7.398 18.119 5.557 1.00 41.22 C HETATM 2760 C14 CLR A1102 7.110 16.654 4.988 1.00 38.68 C HETATM 2761 C15 CLR A1102 6.236 15.977 6.052 1.00 39.70 C HETATM 2762 C16 CLR A1102 6.791 16.525 7.373 1.00 39.39 C HETATM 2763 C17 CLR A1102 7.764 17.720 7.061 1.00 40.49 C HETATM 2764 C18 CLR A1102 6.181 19.118 5.500 1.00 42.60 C HETATM 2765 C19 CLR A1102 6.083 18.394 0.799 1.00 34.55 C HETATM 2766 C20 CLR A1102 7.843 18.778 8.239 1.00 40.90 C HETATM 2767 C21 CLR A1102 8.699 20.039 7.921 1.00 39.11 C HETATM 2768 C22 CLR A1102 8.440 18.143 9.542 1.00 45.79 C HETATM 2769 C23 CLR A1102 7.760 18.722 10.797 1.00 49.43 C HETATM 2770 C24 CLR A1102 8.208 18.003 12.093 1.00 52.02 C HETATM 2771 C25 CLR A1102 8.138 18.864 13.418 1.00 53.65 C HETATM 2772 C26 CLR A1102 9.417 19.675 13.679 1.00 53.25 C HETATM 2773 C27 CLR A1102 6.891 19.741 13.594 1.00 52.87 C HETATM 2774 O1 CLR A1102 7.803 15.927 -3.034 1.00 35.39 O HETATM 2775 CAA Y01 A1103 -15.091 -4.185 9.771 1.00 41.91 C HETATM 2776 CBA Y01 A1103 -15.171 -3.377 11.067 1.00 43.35 C HETATM 2777 CAB Y01 A1103 -15.891 -4.216 12.120 1.00 42.92 C HETATM 2778 CAN Y01 A1103 -15.951 -2.069 10.834 1.00 45.72 C HETATM 2779 CAJ Y01 A1103 -14.995 -0.934 10.445 1.00 44.72 C HETATM 2780 CAO Y01 A1103 -15.720 0.430 10.472 1.00 43.98 C HETATM 2781 CBB Y01 A1103 -15.192 1.425 9.397 1.00 43.00 C HETATM 2782 CAC Y01 A1103 -13.644 1.456 9.430 1.00 43.14 C HETATM 2783 CBE Y01 A1103 -15.818 1.147 7.978 1.00 41.30 C HETATM 2784 CAP Y01 A1103 -17.383 1.313 8.011 1.00 42.70 C HETATM 2785 CAQ Y01 A1103 -17.810 1.867 6.641 1.00 42.43 C HETATM 2786 CBG Y01 A1103 -16.554 1.647 5.799 1.00 40.40 C HETATM 2787 CBI Y01 A1103 -15.360 2.013 6.735 1.00 39.23 C HETATM 2788 CAE Y01 A1103 -15.213 3.546 7.060 1.00 38.04 C HETATM 2789 CAU Y01 A1103 -14.074 1.471 6.029 1.00 36.67 C HETATM 2790 CAS Y01 A1103 -13.859 2.088 4.599 1.00 36.89 C HETATM 2791 CBF Y01 A1103 -15.146 1.999 3.662 1.00 38.32 C HETATM 2792 CBD Y01 A1103 -16.501 2.361 4.403 1.00 39.69 C HETATM 2793 CAK Y01 A1103 -17.696 1.978 3.494 1.00 39.65 C HETATM 2794 CAI Y01 A1103 -17.519 2.432 2.173 1.00 39.15 C HETATM 2795 CAZ Y01 A1103 -16.289 2.772 1.577 1.00 39.05 C HETATM 2796 CAV Y01 A1103 -16.374 3.170 0.224 1.00 39.61 C HETATM 2797 CBH Y01 A1103 -15.021 2.791 2.297 1.00 37.28 C HETATM 2798 CAD Y01 A1103 -14.589 4.271 2.573 1.00 35.44 C HETATM 2799 CAT Y01 A1103 -13.934 2.078 1.434 1.00 35.31 C HETATM 2800 CAR Y01 A1103 -13.958 2.520 -0.057 1.00 36.68 C HETATM 2801 CBC Y01 A1103 -15.368 2.423 -0.657 1.00 40.82 C HETATM 2802 OAW Y01 A1103 -15.372 3.061 -1.957 1.00 46.91 O HETATM 2803 CAY Y01 A1103 -15.327 2.274 -3.071 1.00 49.87 C HETATM 2804 OAG Y01 A1103 -15.622 1.077 -3.108 1.00 51.65 O HETATM 2805 CAM Y01 A1103 -14.888 3.035 -4.330 1.00 52.23 C HETATM 2806 CAL Y01 A1103 -15.770 2.758 -5.559 1.00 56.16 C HETATM 2807 CAX Y01 A1103 -17.270 2.770 -5.231 1.00 59.58 C HETATM 2808 OAH Y01 A1103 -17.769 3.835 -4.805 1.00 59.44 O HETATM 2809 OAF Y01 A1103 -17.888 1.701 -5.433 1.00 62.19 O HETATM 2810 CAA Y01 A1104 8.515 9.117 14.329 1.00 41.78 C HETATM 2811 CBA Y01 A1104 8.421 10.553 13.783 1.00 43.38 C HETATM 2812 CAB Y01 A1104 9.731 11.274 14.102 1.00 42.60 C HETATM 2813 CAN Y01 A1104 7.251 11.339 14.412 1.00 45.28 C HETATM 2814 CAJ Y01 A1104 5.892 10.859 13.881 1.00 45.57 C HETATM 2815 CAO Y01 A1104 4.905 12.030 13.711 1.00 44.36 C HETATM 2816 CBB Y01 A1104 3.581 11.842 14.499 1.00 45.29 C HETATM 2817 CAC Y01 A1104 3.160 10.361 14.524 1.00 44.48 C HETATM 2818 CBE Y01 A1104 3.612 12.474 15.936 1.00 47.21 C HETATM 2819 CAP Y01 A1104 4.398 13.834 15.978 1.00 48.90 C HETATM 2820 CAQ Y01 A1104 3.666 14.756 16.959 1.00 48.88 C HETATM 2821 CBG Y01 A1104 2.760 13.767 17.684 1.00 49.35 C HETATM 2822 CBI Y01 A1104 2.223 12.817 16.585 1.00 47.63 C HETATM 2823 CAE Y01 A1104 1.223 13.477 15.575 1.00 46.46 C HETATM 2824 CAU Y01 A1104 1.559 11.593 17.319 1.00 46.38 C HETATM 2825 CAS Y01 A1104 0.425 12.022 18.293 1.00 46.74 C HETATM 2826 CBF Y01 A1104 0.889 13.124 19.332 1.00 48.02 C HETATM 2827 CBD Y01 A1104 1.658 14.339 18.651 1.00 48.69 C HETATM 2828 CAK Y01 A1104 2.275 15.231 19.768 1.00 47.57 C HETATM 2829 CAI Y01 A1104 1.428 15.416 20.876 1.00 47.83 C HETATM 2830 CAZ Y01 A1104 0.268 14.682 21.185 1.00 48.70 C HETATM 2831 CAV Y01 A1104 -0.398 15.085 22.376 1.00 49.42 C HETATM 2832 CBH Y01 A1104 -0.258 13.642 20.313 1.00 48.04 C HETATM 2833 CAD Y01 A1104 -1.448 14.203 19.486 1.00 46.08 C HETATM 2834 CAT Y01 A1104 -0.752 12.430 21.185 1.00 49.19 C HETATM 2835 CAR Y01 A1104 -1.599 12.856 22.428 1.00 49.21 C HETATM 2836 CBC Y01 A1104 -0.837 13.893 23.258 1.00 49.71 C HETATM 2837 OAW Y01 A1104 -1.689 14.380 24.319 1.00 51.91 O HETATM 2838 CAY Y01 A1104 -1.276 14.132 25.607 1.00 55.47 C HETATM 2839 OAG Y01 A1104 -0.132 13.795 25.935 1.00 58.18 O HETATM 2840 CAM Y01 A1104 -2.384 14.314 26.660 1.00 54.61 C HETATM 2841 CAL Y01 A1104 -1.804 14.640 28.044 1.00 55.00 C HETATM 2842 CAX Y01 A1104 -2.929 14.842 29.068 1.00 55.41 C HETATM 2843 OAH Y01 A1104 -3.563 15.919 29.020 1.00 55.16 O HETATM 2844 OAF Y01 A1104 -3.117 13.922 29.892 1.00 55.73 O HETATM 2845 CAA Y01 A1105 -26.177 31.460 12.400 1.00 71.04 C HETATM 2846 CBA Y01 A1105 -26.244 32.587 11.370 1.00 70.97 C HETATM 2847 CAB Y01 A1105 -26.364 33.928 12.097 1.00 71.09 C HETATM 2848 CAN Y01 A1105 -27.470 32.382 10.486 1.00 70.36 C HETATM 2849 CAJ Y01 A1105 -27.044 31.881 9.107 1.00 69.33 C HETATM 2850 CAO Y01 A1105 -27.566 32.841 8.034 1.00 67.81 C HETATM 2851 CBB Y01 A1105 -27.753 32.104 6.692 1.00 66.45 C HETATM 2852 CAC Y01 A1105 -29.231 32.262 6.332 1.00 65.23 C HETATM 2853 CBE Y01 A1105 -26.796 32.683 5.589 1.00 67.63 C HETATM 2854 CAP Y01 A1105 -25.292 32.637 6.050 1.00 68.32 C HETATM 2855 CAQ Y01 A1105 -24.477 32.042 4.906 1.00 68.04 C HETATM 2856 CBG Y01 A1105 -25.344 32.479 3.755 1.00 68.15 C HETATM 2857 CBI Y01 A1105 -26.779 32.025 4.143 1.00 67.66 C HETATM 2858 CAE Y01 A1105 -26.980 30.468 4.138 1.00 67.71 C HETATM 2859 CAU Y01 A1105 -27.778 32.721 3.154 1.00 67.19 C HETATM 2860 CAS Y01 A1105 -27.436 32.451 1.645 1.00 68.02 C HETATM 2861 CBF Y01 A1105 -25.897 32.696 1.282 1.00 69.53 C HETATM 2862 CBD Y01 A1105 -24.891 32.074 2.331 1.00 68.91 C HETATM 2863 CAK Y01 A1105 -23.464 32.588 2.033 1.00 69.19 C HETATM 2864 CAI Y01 A1105 -23.140 32.530 0.667 1.00 69.98 C HETATM 2865 CAZ Y01 A1105 -24.052 32.408 -0.395 1.00 71.15 C HETATM 2866 CAV Y01 A1105 -23.463 32.403 -1.678 1.00 73.02 C HETATM 2867 CBH Y01 A1105 -25.491 32.311 -0.211 1.00 71.07 C HETATM 2868 CAD Y01 A1105 -26.022 30.885 -0.549 1.00 70.84 C HETATM 2869 CAT Y01 A1105 -26.162 33.331 -1.170 1.00 72.41 C HETATM 2870 CAR Y01 A1105 -25.602 33.260 -2.618 1.00 73.72 C HETATM 2871 CBC Y01 A1105 -24.081 33.461 -2.616 1.00 75.54 C HETATM 2872 OAW Y01 A1105 -23.533 33.280 -3.972 1.00 79.15 O HETATM 2873 CAY Y01 A1105 -23.755 34.239 -4.938 1.00 82.08 C HETATM 2874 OAG Y01 A1105 -24.200 35.372 -4.734 1.00 82.68 O HETATM 2875 CAM Y01 A1105 -23.314 33.820 -6.347 1.00 84.13 C HETATM 2876 CAL Y01 A1105 -24.450 34.053 -7.360 1.00 86.56 C HETATM 2877 CAX Y01 A1105 -23.895 34.184 -8.789 1.00 88.52 C HETATM 2878 OAH Y01 A1105 -22.952 34.991 -8.973 1.00 89.38 O HETATM 2879 OAF Y01 A1105 -24.446 33.490 -9.675 1.00 88.87 O HETATM 2880 C10 OLC A1106 -10.680 0.450 7.386 1.00 52.95 C HETATM 2881 C9 OLC A1106 -10.170 0.490 5.933 1.00 51.61 C HETATM 2882 C11 OLC A1106 -9.673 0.679 8.519 1.00 53.53 C HETATM 2883 C8 OLC A1106 -8.665 0.693 5.687 1.00 50.28 C HETATM 2884 C24 OLC A1106 -8.423 -0.993 -6.647 1.00 74.02 C HETATM 2885 C12 OLC A1106 -10.141 -0.050 9.780 1.00 53.37 C HETATM 2886 C7 OLC A1106 -8.431 1.162 4.253 1.00 50.97 C HETATM 2887 C13 OLC A1106 -10.000 0.864 10.996 1.00 54.08 C HETATM 2888 C6 OLC A1106 -8.396 -0.022 3.286 1.00 50.56 C HETATM 2889 C14 OLC A1106 -8.699 0.550 11.737 1.00 55.31 C HETATM 2890 C5 OLC A1106 -9.128 0.369 2.000 1.00 51.12 C HETATM 2891 C4 OLC A1106 -8.118 0.486 0.865 1.00 53.61 C HETATM 2892 C3 OLC A1106 -8.854 0.570 -0.462 1.00 56.95 C HETATM 2893 C2 OLC A1106 -8.531 -0.686 -1.269 1.00 62.61 C HETATM 2894 C21 OLC A1106 -8.440 0.435 -4.563 1.00 71.90 C HETATM 2895 C1 OLC A1106 -7.649 -0.349 -2.474 1.00 68.06 C HETATM 2896 C22 OLC A1106 -7.783 0.194 -5.930 1.00 73.48 C HETATM 2897 O19 OLC A1106 -6.499 0.060 -2.314 1.00 70.91 O HETATM 2898 O25 OLC A1106 -7.387 -1.764 -7.266 1.00 75.44 O HETATM 2899 O23 OLC A1106 -7.917 1.358 -6.750 1.00 74.27 O HETATM 2900 O20 OLC A1106 -8.189 -0.676 -3.686 1.00 70.20 O HETATM 2901 C10 OLC A1107 7.741 25.244 5.377 1.00 59.59 C HETATM 2902 C9 OLC A1107 7.360 24.725 3.980 1.00 60.57 C HETATM 2903 C11 OLC A1107 8.177 24.259 6.462 1.00 58.30 C HETATM 2904 C8 OLC A1107 7.433 23.220 3.674 1.00 60.62 C HETATM 2905 C24 OLC A1107 7.597 18.377 -7.817 1.00 84.32 C HETATM 2906 C12 OLC A1107 7.895 24.899 7.825 1.00 57.99 C HETATM 2907 C7 OLC A1107 7.759 23.008 2.182 1.00 61.12 C HETATM 2908 C13 OLC A1107 9.197 25.424 8.431 1.00 57.61 C HETATM 2909 C6 OLC A1107 6.534 23.264 1.287 1.00 61.38 C HETATM 2910 C14 OLC A1107 9.163 25.272 9.953 1.00 57.11 C HETATM 2911 C5 OLC A1107 6.971 23.397 -0.172 1.00 62.72 C HETATM 2912 C4 OLC A1107 6.497 22.193 -0.991 1.00 64.41 C HETATM 2913 C3 OLC A1107 7.273 22.149 -2.315 1.00 67.76 C HETATM 2914 C2 OLC A1107 6.913 20.877 -3.095 1.00 71.79 C HETATM 2915 C21 OLC A1107 8.362 20.243 -6.310 1.00 80.53 C HETATM 2916 C1 OLC A1107 8.076 20.365 -3.966 1.00 76.68 C HETATM 2917 C22 OLC A1107 8.813 19.061 -7.179 1.00 82.46 C HETATM 2918 O19 OLC A1107 9.242 20.384 -3.558 1.00 78.87 O HETATM 2919 O25 OLC A1107 8.017 17.350 -8.718 1.00 85.71 O HETATM 2920 O23 OLC A1107 9.679 19.545 -8.211 1.00 82.53 O HETATM 2921 O20 OLC A1107 7.682 19.772 -5.135 1.00 79.00 O HETATM 2922 C18 OLC A1108 5.644 31.573 17.123 1.00 88.19 C HETATM 2923 C10 OLC A1108 0.148 30.499 9.178 1.00 83.66 C HETATM 2924 C9 OLC A1108 -0.686 30.816 7.913 1.00 82.13 C HETATM 2925 C17 OLC A1108 4.281 31.513 16.424 1.00 88.22 C HETATM 2926 C11 OLC A1108 0.693 31.660 10.027 1.00 84.99 C HETATM 2927 C8 OLC A1108 -0.959 32.280 7.532 1.00 80.87 C HETATM 2928 C24 OLC A1108 0.037 34.978 -4.445 1.00 86.84 C HETATM 2929 C16 OLC A1108 4.484 31.441 14.908 1.00 88.13 C HETATM 2930 C12 OLC A1108 2.089 31.295 10.543 1.00 86.18 C HETATM 2931 C7 OLC A1108 -0.295 32.586 6.185 1.00 79.83 C HETATM 2932 C15 OLC A1108 3.130 31.275 14.210 1.00 87.68 C HETATM 2933 C13 OLC A1108 2.303 31.905 11.931 1.00 86.97 C HETATM 2934 C6 OLC A1108 -1.339 32.606 5.062 1.00 78.85 C HETATM 2935 C14 OLC A1108 3.350 31.096 12.703 1.00 87.23 C HETATM 2936 C5 OLC A1108 -0.612 32.614 3.716 1.00 78.97 C HETATM 2937 C4 OLC A1108 -1.582 32.930 2.569 1.00 79.54 C HETATM 2938 C3 OLC A1108 -0.912 32.608 1.226 1.00 80.84 C HETATM 2939 C2 OLC A1108 -0.487 33.909 0.526 1.00 82.94 C HETATM 2940 C21 OLC A1108 0.751 33.329 -2.663 1.00 85.70 C HETATM 2941 C1 OLC A1108 0.778 33.721 -0.335 1.00 85.05 C HETATM 2942 C22 OLC A1108 1.137 34.005 -3.988 1.00 86.56 C HETATM 2943 O19 OLC A1108 1.799 33.219 0.142 1.00 86.34 O HETATM 2944 O25 OLC A1108 -0.075 34.960 -5.874 1.00 86.18 O HETATM 2945 O23 OLC A1108 2.384 34.700 -3.844 1.00 86.68 O HETATM 2946 O20 OLC A1108 0.710 34.279 -1.585 1.00 85.16 O HETATM 2947 C18 OLC A1109 -25.595 19.763 16.648 1.00 66.73 C HETATM 2948 C10 OLC A1109 -26.504 16.217 7.992 1.00 75.19 C HETATM 2949 C9 OLC A1109 -26.538 15.339 6.716 1.00 74.12 C HETATM 2950 C17 OLC A1109 -26.325 18.623 15.932 1.00 67.03 C HETATM 2951 C11 OLC A1109 -25.979 15.616 9.315 1.00 74.97 C HETATM 2952 C8 OLC A1109 -26.041 13.884 6.795 1.00 72.92 C HETATM 2953 C24 OLC A1109 -22.926 13.691 -4.289 1.00 82.53 C HETATM 2954 C16 OLC A1109 -25.440 18.044 14.830 1.00 67.50 C HETATM 2955 C12 OLC A1109 -26.705 16.260 10.505 1.00 73.52 C HETATM 2956 C7 OLC A1109 -25.169 13.575 5.573 1.00 71.95 C HETATM 2957 C15 OLC A1109 -26.232 17.965 13.520 1.00 68.29 C HETATM 2958 C13 OLC A1109 -25.890 17.423 11.085 1.00 71.39 C HETATM 2959 C6 OLC A1109 -25.983 12.840 4.507 1.00 70.96 C HETATM 2960 C14 OLC A1109 -25.473 17.084 12.520 1.00 69.82 C HETATM 2961 C5 OLC A1109 -25.032 12.317 3.434 1.00 71.32 C HETATM 2962 C4 OLC A1109 -25.819 11.920 2.185 1.00 72.75 C HETATM 2963 C3 OLC A1109 -24.829 11.626 1.060 1.00 75.35 C HETATM 2964 C2 OLC A1109 -25.508 10.832 -0.061 1.00 78.16 C HETATM 2965 C21 OLC A1109 -24.618 12.113 -3.233 1.00 83.24 C HETATM 2966 C1 OLC A1109 -25.829 11.750 -1.249 1.00 81.25 C HETATM 2967 C22 OLC A1109 -24.412 13.449 -3.953 1.00 83.13 C HETATM 2968 O19 OLC A1109 -26.996 11.925 -1.599 1.00 82.26 O HETATM 2969 O25 OLC A1109 -22.488 12.892 -5.395 1.00 82.20 O HETATM 2970 O23 OLC A1109 -25.233 13.511 -5.120 1.00 83.35 O HETATM 2971 O20 OLC A1109 -24.748 12.361 -1.826 1.00 82.92 O HETATM 2972 C18 OLC A1110 7.980 28.850 14.302 1.00 72.58 C HETATM 2973 C10 OLC A1110 4.265 29.516 5.733 1.00 63.67 C HETATM 2974 C9 OLC A1110 4.301 29.181 4.221 1.00 62.60 C HETATM 2975 C17 OLC A1110 7.477 28.145 13.038 1.00 72.27 C HETATM 2976 C11 OLC A1110 4.637 28.400 6.726 1.00 64.55 C HETATM 2977 C8 OLC A1110 4.666 27.741 3.803 1.00 62.42 C HETATM 2978 C24 OLC A1110 1.536 30.514 -6.637 1.00 71.72 C HETATM 2979 C16 OLC A1110 6.792 29.157 12.113 1.00 72.32 C HETATM 2980 C12 OLC A1110 4.047 28.643 8.117 1.00 65.73 C HETATM 2981 C7 OLC A1110 5.565 27.727 2.566 1.00 62.03 C HETATM 2982 C15 OLC A1110 6.542 28.516 10.741 1.00 71.98 C HETATM 2983 C13 OLC A1110 4.784 27.745 9.120 1.00 67.41 C HETATM 2984 C6 OLC A1110 4.715 27.533 1.305 1.00 62.52 C HETATM 2985 C14 OLC A1110 5.039 28.509 10.423 1.00 70.10 C HETATM 2986 C5 OLC A1110 4.795 28.791 0.434 1.00 61.61 C HETATM 2987 C4 OLC A1110 3.397 29.371 0.206 1.00 61.05 C HETATM 2988 C3 OLC A1110 3.457 30.491 -0.832 1.00 60.86 C HETATM 2989 C2 OLC A1110 2.709 30.109 -2.109 1.00 60.42 C HETATM 2990 C21 OLC A1110 2.905 28.856 -5.293 1.00 65.73 C HETATM 2991 C1 OLC A1110 3.624 29.429 -3.134 1.00 61.09 C HETATM 2992 C22 OLC A1110 2.659 29.457 -6.681 1.00 69.64 C HETATM 2993 O19 OLC A1110 4.472 28.603 -2.792 1.00 61.68 O HETATM 2994 O25 OLC A1110 0.477 30.172 -7.546 1.00 71.87 O HETATM 2995 O23 OLC A1110 3.872 30.062 -7.148 1.00 70.14 O HETATM 2996 O20 OLC A1110 3.458 29.857 -4.416 1.00 62.48 O HETATM 2997 C18 OLC A1111 -30.127 24.737 14.866 1.00 79.07 C HETATM 2998 C10 OLC A1111 -30.391 22.957 5.703 1.00 76.58 C HETATM 2999 C9 OLC A1111 -30.318 22.924 4.159 1.00 74.66 C HETATM 3000 C17 OLC A1111 -30.891 25.403 13.719 1.00 78.94 C HETATM 3001 C11 OLC A1111 -30.310 24.312 6.431 1.00 77.14 C HETATM 3002 C8 OLC A1111 -30.167 24.247 3.399 1.00 72.55 C HETATM 3003 C24 OLC A1111 -26.223 27.034 -8.191 1.00 89.44 C HETATM 3004 C16 OLC A1111 -31.120 24.383 12.599 1.00 79.00 C HETATM 3005 C12 OLC A1111 -29.779 24.086 7.850 1.00 77.61 C HETATM 3006 C7 OLC A1111 -29.451 23.978 2.076 1.00 71.81 C HETATM 3007 C15 OLC A1111 -30.398 24.853 11.334 1.00 78.92 C HETATM 3008 C13 OLC A1111 -30.743 24.695 8.866 1.00 77.97 C HETATM 3009 C6 OLC A1111 -30.233 24.621 0.933 1.00 71.32 C HETATM 3010 C14 OLC A1111 -30.692 23.900 10.173 1.00 78.61 C HETATM 3011 C5 OLC A1111 -29.970 23.854 -0.361 1.00 71.13 C HETATM 3012 C4 OLC A1111 -29.170 24.740 -1.315 1.00 72.01 C HETATM 3013 C3 OLC A1111 -28.628 23.885 -2.456 1.00 74.65 C HETATM 3014 C2 OLC A1111 -27.501 24.645 -3.161 1.00 77.46 C HETATM 3015 C21 OLC A1111 -26.148 25.826 -6.004 1.00 85.53 C HETATM 3016 C1 OLC A1111 -27.706 24.674 -4.689 1.00 81.19 C HETATM 3017 C22 OLC A1111 -26.038 25.671 -7.521 1.00 87.25 C HETATM 3018 O19 OLC A1111 -28.831 24.763 -5.187 1.00 82.52 O HETATM 3019 O25 OLC A1111 -26.366 26.848 -9.603 1.00 91.29 O HETATM 3020 O23 OLC A1111 -24.754 25.142 -7.858 1.00 86.62 O HETATM 3021 O20 OLC A1111 -26.557 24.574 -5.423 1.00 83.55 O HETATM 3022 C10 OLC A1112 -6.191 3.106 9.790 1.00 50.69 C HETATM 3023 C9 OLC A1112 -6.929 3.573 8.514 1.00 52.34 C HETATM 3024 C11 OLC A1112 -4.779 2.523 9.684 1.00 49.38 C HETATM 3025 C8 OLC A1112 -6.222 3.460 7.158 1.00 55.05 C HETATM 3026 C24 OLC A1112 -5.940 3.476 -3.690 1.00 83.67 C HETATM 3027 C12 OLC A1112 -4.430 1.802 10.997 1.00 49.24 C HETATM 3028 C7 OLC A1112 -7.014 4.249 6.099 1.00 57.86 C HETATM 3029 C15 OLC A1112 -2.734 -1.677 11.237 1.00 43.92 C HETATM 3030 C13 OLC A1112 -4.209 0.300 10.734 1.00 47.60 C HETATM 3031 C6 OLC A1112 -6.282 5.536 5.665 1.00 59.79 C HETATM 3032 C14 OLC A1112 -3.149 -0.270 11.686 1.00 46.34 C HETATM 3033 C5 OLC A1112 -5.108 5.220 4.721 1.00 63.12 C HETATM 3034 C4 OLC A1112 -5.434 5.582 3.261 1.00 66.26 C HETATM 3035 C3 OLC A1112 -5.941 4.372 2.458 1.00 69.74 C HETATM 3036 C2 OLC A1112 -4.818 3.361 2.190 1.00 74.07 C HETATM 3037 C21 OLC A1112 -5.873 3.397 -1.193 1.00 82.26 C HETATM 3038 C1 OLC A1112 -4.441 3.328 0.707 1.00 78.64 C HETATM 3039 C22 OLC A1112 -5.086 3.116 -2.479 1.00 83.33 C HETATM 3040 O19 OLC A1112 -3.357 3.788 0.338 1.00 80.03 O HETATM 3041 O25 OLC A1112 -5.647 2.596 -4.775 1.00 84.88 O HETATM 3042 O23 OLC A1112 -3.887 3.900 -2.490 1.00 84.47 O HETATM 3043 O20 OLC A1112 -5.313 2.642 -0.101 1.00 81.28 O HETATM 3044 C18 OLC A1113 -18.936 2.613 18.407 1.00 70.25 C HETATM 3045 C10 OLC A1113 -20.799 3.106 8.787 1.00 66.42 C HETATM 3046 C9 OLC A1113 -20.845 3.856 7.430 1.00 64.77 C HETATM 3047 C17 OLC A1113 -19.787 3.427 17.430 1.00 70.43 C HETATM 3048 C11 OLC A1113 -20.214 3.797 10.031 1.00 67.13 C HETATM 3049 C8 OLC A1113 -20.301 5.289 7.315 1.00 63.98 C HETATM 3050 C24 OLC A1113 -21.534 6.237 -5.076 1.00 82.24 C HETATM 3051 C16 OLC A1113 -19.186 3.366 16.021 1.00 70.08 C HETATM 3052 C12 OLC A1113 -20.152 2.791 11.192 1.00 67.82 C HETATM 3053 C7 OLC A1113 -19.364 5.372 6.103 1.00 63.35 C HETATM 3054 C15 OLC A1113 -20.315 3.497 14.989 1.00 70.07 C HETATM 3055 C13 OLC A1113 -20.556 3.483 12.503 1.00 68.96 C HETATM 3056 C6 OLC A1113 -19.897 6.349 5.054 1.00 63.04 C HETATM 3057 C14 OLC A1113 -19.952 2.744 13.704 1.00 69.78 C HETATM 3058 C5 OLC A1113 -19.161 6.108 3.731 1.00 65.32 C HETATM 3059 C4 OLC A1113 -19.703 7.052 2.651 1.00 68.81 C HETATM 3060 C3 OLC A1113 -19.698 6.358 1.282 1.00 72.40 C HETATM 3061 C2 OLC A1113 -20.854 6.888 0.411 1.00 76.00 C HETATM 3062 C21 OLC A1113 -21.805 7.448 -2.891 1.00 81.60 C HETATM 3063 C1 OLC A1113 -20.714 6.419 -1.053 1.00 80.20 C HETATM 3064 C22 OLC A1113 -21.429 7.596 -4.372 1.00 81.68 C HETATM 3065 O19 OLC A1113 -20.578 5.223 -1.311 1.00 81.71 O HETATM 3066 O25 OLC A1113 -20.643 6.208 -6.202 1.00 82.37 O HETATM 3067 O23 OLC A1113 -22.330 8.515 -5.004 1.00 81.03 O HETATM 3068 O20 OLC A1113 -20.665 7.412 -2.005 1.00 81.90 O HETATM 3069 OH2 1PE A1114 -19.026 37.070 0.018 1.00 84.59 O HETATM 3070 C12 1PE A1114 -20.333 36.662 0.418 1.00 85.02 C HETATM 3071 C22 1PE A1114 -20.277 36.143 1.854 1.00 86.37 C HETATM 3072 OH3 1PE A1114 -21.376 36.679 2.597 1.00 88.21 O HETATM 3073 C13 1PE A1114 -22.303 36.972 4.817 1.00 90.24 C HETATM 3074 C23 1PE A1114 -21.372 36.144 3.924 1.00 89.39 C HETATM 3075 OH4 1PE A1114 -23.630 36.435 4.775 1.00 91.23 O HETATM 3076 C14 1PE A1114 -25.256 36.610 2.982 1.00 92.10 C HETATM 3077 C24 1PE A1114 -24.520 37.344 4.111 1.00 91.90 C HETATM 3078 OH5 1PE A1114 -25.427 37.483 1.858 1.00 91.54 O HETATM 3079 C15 1PE A1114 -24.386 38.138 -0.214 1.00 89.49 C HETATM 3080 C25 1PE A1114 -24.697 36.982 0.734 1.00 90.48 C HETATM 3081 OH6 1PE A1114 -24.551 37.705 -1.565 1.00 88.35 O HETATM 3082 C16 1PE A1114 -24.244 38.587 -3.780 1.00 86.91 C HETATM 3083 C26 1PE A1114 -24.818 38.839 -2.389 1.00 87.52 C HETATM 3084 OH7 1PE A1114 -25.306 38.193 -4.650 1.00 86.26 O HETATM 3085 ZN ZN A1115 -30.771 4.240 53.638 1.00 87.04 ZN2+ HETATM 3086 O HOH A1201 -5.978 21.033 -0.534 1.00 36.15 O HETATM 3087 O HOH A1202 -3.384 13.792 4.392 1.00 28.31 O HETATM 3088 O HOH A1203 -14.574 22.710 2.917 1.00 40.31 O HETATM 3089 O HOH A1204 -6.702 17.321 -1.301 1.00 55.72 O HETATM 3090 O HOH A1205 -16.343 22.221 17.642 1.00 45.87 O HETATM 3091 O HOH A1206 -6.551 36.533 -2.658 1.00 32.43 O HETATM 3092 O HOH A1207 -9.875 34.809 -8.072 1.00 37.46 O HETATM 3093 O HOH A1208 -11.276 9.433 -9.451 1.00 47.38 O HETATM 3094 O HOH A1209 -13.900 0.887 -15.189 1.00 50.90 O HETATM 3095 O HOH A1210 -3.833 21.290 -1.680 1.00 39.60 O HETATM 3096 O HOH A1211 -28.057 5.357 61.365 1.00 44.18 O HETATM 3097 O HOH A1212 -14.987 12.474 28.013 1.00 52.01 O HETATM 3098 O HOH A1213 -3.493 11.568 -18.338 1.00 58.32 O HETATM 3099 O HOH A1214 -15.141 19.369 2.571 1.00 47.22 O HETATM 3100 O HOH A1215 -12.659 25.058 2.815 1.00 46.22 O HETATM 3101 O HOH A1216 2.478 15.165 -10.916 1.00 39.27 O HETATM 3102 O HOH A1217 -21.031 6.596 -8.950 1.00 61.55 O HETATM 3103 O HOH A1218 -3.041 16.866 1.797 1.00 36.84 O HETATM 3104 O HOH A1219 -8.115 19.525 -7.422 1.00 45.87 O HETATM 3105 O HOH A1220 -11.150 23.317 1.125 1.00 40.26 O HETATM 3106 O HOH A1221 4.557 16.023 -8.826 1.00 39.84 O HETATM 3107 O HOH A1222 -2.300 11.956 -14.570 1.00 57.89 O HETATM 3108 O HOH A1223 1.175 6.137 -13.751 1.00 51.39 O HETATM 3109 O HOH A1224 -2.105 17.443 4.229 1.00 28.78 O HETATM 3110 O HOH A1225 -12.884 18.670 1.071 1.00 45.81 O HETATM 3111 O HOH A1226 -2.239 6.733 -15.370 1.00 48.85 O HETATM 3112 O HOH A1227 -13.434 21.425 0.791 1.00 66.96 O HETATM 3113 O HOH A1228 -8.732 17.104 0.519 1.00 56.70 O HETATM 3114 O HOH A1229 0.753 24.962 -7.737 1.00 53.21 O HETATM 3115 O HOH A1230 -10.396 21.226 -7.964 1.00 56.19 O CONECT 32 2419 CONECT 709 1312 CONECT 1312 709 CONECT 1726 3085 CONECT 1746 3085 CONECT 1943 3085 CONECT 1964 3085 CONECT 2419 32 CONECT 2715 2716 CONECT 2716 2715 2717 2718 2719 CONECT 2717 2716 CONECT 2718 2716 CONECT 2719 2716 2720 CONECT 2720 2719 2721 2723 CONECT 2721 2720 2722 CONECT 2722 2721 2725 CONECT 2723 2720 2724 CONECT 2724 2723 2725 CONECT 2725 2722 2724 2726 CONECT 2726 2725 2727 CONECT 2727 2726 2728 2729 CONECT 2728 2727 CONECT 2729 2727 2730 CONECT 2730 2729 2731 2735 CONECT 2731 2730 2732 CONECT 2732 2731 2733 CONECT 2733 2732 2734 CONECT 2734 2733 2735 CONECT 2735 2730 2734 2736 CONECT 2736 2735 2737 CONECT 2737 2736 2738 2742 CONECT 2738 2737 2739 CONECT 2739 2738 2740 CONECT 2740 2739 2741 CONECT 2741 2740 2742 CONECT 2742 2737 2741 2743 CONECT 2743 2742 2744 2745 2746 CONECT 2744 2743 CONECT 2745 2743 CONECT 2746 2743 CONECT 2747 2748 2756 CONECT 2748 2747 2749 CONECT 2749 2748 2750 2774 CONECT 2750 2749 2751 CONECT 2751 2750 2752 2756 CONECT 2752 2751 2753 CONECT 2753 2752 2754 CONECT 2754 2753 2755 2760 CONECT 2755 2754 2756 2757 CONECT 2756 2747 2751 2755 2765 CONECT 2757 2755 2758 CONECT 2758 2757 2759 CONECT 2759 2758 2760 2763 2764 CONECT 2760 2754 2759 2761 CONECT 2761 2760 2762 CONECT 2762 2761 2763 CONECT 2763 2759 2762 2766 CONECT 2764 2759 CONECT 2765 2756 CONECT 2766 2763 2767 2768 CONECT 2767 2766 CONECT 2768 2766 2769 CONECT 2769 2768 2770 CONECT 2770 2769 2771 CONECT 2771 2770 2772 2773 CONECT 2772 2771 CONECT 2773 2771 CONECT 2774 2749 CONECT 2775 2776 CONECT 2776 2775 2777 2778 CONECT 2777 2776 CONECT 2778 2776 2779 CONECT 2779 2778 2780 CONECT 2780 2779 2781 CONECT 2781 2780 2782 2783 CONECT 2782 2781 CONECT 2783 2781 2784 2787 CONECT 2784 2783 2785 CONECT 2785 2784 2786 CONECT 2786 2785 2787 2792 CONECT 2787 2783 2786 2788 2789 CONECT 2788 2787 CONECT 2789 2787 2790 CONECT 2790 2789 2791 CONECT 2791 2790 2792 2797 CONECT 2792 2786 2791 2793 CONECT 2793 2792 2794 CONECT 2794 2793 2795 CONECT 2795 2794 2796 2797 CONECT 2796 2795 2801 CONECT 2797 2791 2795 2798 2799 CONECT 2798 2797 CONECT 2799 2797 2800 CONECT 2800 2799 2801 CONECT 2801 2796 2800 2802 CONECT 2802 2801 2803 CONECT 2803 2802 2804 2805 CONECT 2804 2803 CONECT 2805 2803 2806 CONECT 2806 2805 2807 CONECT 2807 2806 2808 2809 CONECT 2808 2807 CONECT 2809 2807 CONECT 2810 2811 CONECT 2811 2810 2812 2813 CONECT 2812 2811 CONECT 2813 2811 2814 CONECT 2814 2813 2815 CONECT 2815 2814 2816 CONECT 2816 2815 2817 2818 CONECT 2817 2816 CONECT 2818 2816 2819 2822 CONECT 2819 2818 2820 CONECT 2820 2819 2821 CONECT 2821 2820 2822 2827 CONECT 2822 2818 2821 2823 2824 CONECT 2823 2822 CONECT 2824 2822 2825 CONECT 2825 2824 2826 CONECT 2826 2825 2827 2832 CONECT 2827 2821 2826 2828 CONECT 2828 2827 2829 CONECT 2829 2828 2830 CONECT 2830 2829 2831 2832 CONECT 2831 2830 2836 CONECT 2832 2826 2830 2833 2834 CONECT 2833 2832 CONECT 2834 2832 2835 CONECT 2835 2834 2836 CONECT 2836 2831 2835 2837 CONECT 2837 2836 2838 CONECT 2838 2837 2839 2840 CONECT 2839 2838 CONECT 2840 2838 2841 CONECT 2841 2840 2842 CONECT 2842 2841 2843 2844 CONECT 2843 2842 CONECT 2844 2842 CONECT 2845 2846 CONECT 2846 2845 2847 2848 CONECT 2847 2846 CONECT 2848 2846 2849 CONECT 2849 2848 2850 CONECT 2850 2849 2851 CONECT 2851 2850 2852 2853 CONECT 2852 2851 CONECT 2853 2851 2854 2857 CONECT 2854 2853 2855 CONECT 2855 2854 2856 CONECT 2856 2855 2857 2862 CONECT 2857 2853 2856 2858 2859 CONECT 2858 2857 CONECT 2859 2857 2860 CONECT 2860 2859 2861 CONECT 2861 2860 2862 2867 CONECT 2862 2856 2861 2863 CONECT 2863 2862 2864 CONECT 2864 2863 2865 CONECT 2865 2864 2866 2867 CONECT 2866 2865 2871 CONECT 2867 2861 2865 2868 2869 CONECT 2868 2867 CONECT 2869 2867 2870 CONECT 2870 2869 2871 CONECT 2871 2866 2870 2872 CONECT 2872 2871 2873 CONECT 2873 2872 2874 2875 CONECT 2874 2873 CONECT 2875 2873 2876 CONECT 2876 2875 2877 CONECT 2877 2876 2878 2879 CONECT 2878 2877 CONECT 2879 2877 CONECT 2880 2881 2882 CONECT 2881 2880 2883 CONECT 2882 2880 2885 CONECT 2883 2881 2886 CONECT 2884 2896 2898 CONECT 2885 2882 2887 CONECT 2886 2883 2888 CONECT 2887 2885 2889 CONECT 2888 2886 2890 CONECT 2889 2887 CONECT 2890 2888 2891 CONECT 2891 2890 2892 CONECT 2892 2891 2893 CONECT 2893 2892 2895 CONECT 2894 2896 2900 CONECT 2895 2893 2897 2900 CONECT 2896 2884 2894 2899 CONECT 2897 2895 CONECT 2898 2884 CONECT 2899 2896 CONECT 2900 2894 2895 CONECT 2901 2902 2903 CONECT 2902 2901 2904 CONECT 2903 2901 2906 CONECT 2904 2902 2907 CONECT 2905 2917 2919 CONECT 2906 2903 2908 CONECT 2907 2904 2909 CONECT 2908 2906 2910 CONECT 2909 2907 2911 CONECT 2910 2908 CONECT 2911 2909 2912 CONECT 2912 2911 2913 CONECT 2913 2912 2914 CONECT 2914 2913 2916 CONECT 2915 2917 2921 CONECT 2916 2914 2918 2921 CONECT 2917 2905 2915 2920 CONECT 2918 2916 CONECT 2919 2905 CONECT 2920 2917 CONECT 2921 2915 2916 CONECT 2922 2925 CONECT 2923 2924 2926 CONECT 2924 2923 2927 CONECT 2925 2922 2929 CONECT 2926 2923 2930 CONECT 2927 2924 2931 CONECT 2928 2942 2944 CONECT 2929 2925 2932 CONECT 2930 2926 2933 CONECT 2931 2927 2934 CONECT 2932 2929 2935 CONECT 2933 2930 2935 CONECT 2934 2931 2936 CONECT 2935 2932 2933 CONECT 2936 2934 2937 CONECT 2937 2936 2938 CONECT 2938 2937 2939 CONECT 2939 2938 2941 CONECT 2940 2942 2946 CONECT 2941 2939 2943 2946 CONECT 2942 2928 2940 2945 CONECT 2943 2941 CONECT 2944 2928 CONECT 2945 2942 CONECT 2946 2940 2941 CONECT 2947 2950 CONECT 2948 2949 2951 CONECT 2949 2948 2952 CONECT 2950 2947 2954 CONECT 2951 2948 2955 CONECT 2952 2949 2956 CONECT 2953 2967 2969 CONECT 2954 2950 2957 CONECT 2955 2951 2958 CONECT 2956 2952 2959 CONECT 2957 2954 2960 CONECT 2958 2955 2960 CONECT 2959 2956 2961 CONECT 2960 2957 2958 CONECT 2961 2959 2962 CONECT 2962 2961 2963 CONECT 2963 2962 2964 CONECT 2964 2963 2966 CONECT 2965 2967 2971 CONECT 2966 2964 2968 2971 CONECT 2967 2953 2965 2970 CONECT 2968 2966 CONECT 2969 2953 CONECT 2970 2967 CONECT 2971 2965 2966 CONECT 2972 2975 CONECT 2973 2974 2976 CONECT 2974 2973 2977 CONECT 2975 2972 2979 CONECT 2976 2973 2980 CONECT 2977 2974 2981 CONECT 2978 2992 2994 CONECT 2979 2975 2982 CONECT 2980 2976 2983 CONECT 2981 2977 2984 CONECT 2982 2979 2985 CONECT 2983 2980 2985 CONECT 2984 2981 2986 CONECT 2985 2982 2983 CONECT 2986 2984 2987 CONECT 2987 2986 2988 CONECT 2988 2987 2989 CONECT 2989 2988 2991 CONECT 2990 2992 2996 CONECT 2991 2989 2993 2996 CONECT 2992 2978 2990 2995 CONECT 2993 2991 CONECT 2994 2978 CONECT 2995 2992 CONECT 2996 2990 2991 CONECT 2997 3000 CONECT 2998 2999 3001 CONECT 2999 2998 3002 CONECT 3000 2997 3004 CONECT 3001 2998 3005 CONECT 3002 2999 3006 CONECT 3003 3017 3019 CONECT 3004 3000 3007 CONECT 3005 3001 3008 CONECT 3006 3002 3009 CONECT 3007 3004 3010 CONECT 3008 3005 3010 CONECT 3009 3006 3011 CONECT 3010 3007 3008 CONECT 3011 3009 3012 CONECT 3012 3011 3013 CONECT 3013 3012 3014 CONECT 3014 3013 3016 CONECT 3015 3017 3021 CONECT 3016 3014 3018 3021 CONECT 3017 3003 3015 3020 CONECT 3018 3016 CONECT 3019 3003 CONECT 3020 3017 CONECT 3021 3015 3016 CONECT 3022 3023 3024 CONECT 3023 3022 3025 CONECT 3024 3022 3027 CONECT 3025 3023 3028 CONECT 3026 3039 3041 CONECT 3027 3024 3030 CONECT 3028 3025 3031 CONECT 3029 3032 CONECT 3030 3027 3032 CONECT 3031 3028 3033 CONECT 3032 3029 3030 CONECT 3033 3031 3034 CONECT 3034 3033 3035 CONECT 3035 3034 3036 CONECT 3036 3035 3038 CONECT 3037 3039 3043 CONECT 3038 3036 3040 3043 CONECT 3039 3026 3037 3042 CONECT 3040 3038 CONECT 3041 3026 CONECT 3042 3039 CONECT 3043 3037 3038 CONECT 3044 3047 CONECT 3045 3046 3048 CONECT 3046 3045 3049 CONECT 3047 3044 3051 CONECT 3048 3045 3052 CONECT 3049 3046 3053 CONECT 3050 3064 3066 CONECT 3051 3047 3054 CONECT 3052 3048 3055 CONECT 3053 3049 3056 CONECT 3054 3051 3057 CONECT 3055 3052 3057 CONECT 3056 3053 3058 CONECT 3057 3054 3055 CONECT 3058 3056 3059 CONECT 3059 3058 3060 CONECT 3060 3059 3061 CONECT 3061 3060 3063 CONECT 3062 3064 3068 CONECT 3063 3061 3065 3068 CONECT 3064 3050 3062 3067 CONECT 3065 3063 CONECT 3066 3050 CONECT 3067 3064 CONECT 3068 3062 3063 CONECT 3069 3070 CONECT 3070 3069 3071 CONECT 3071 3070 3072 CONECT 3072 3071 3074 CONECT 3073 3074 3075 CONECT 3074 3072 3073 CONECT 3075 3073 3077 CONECT 3076 3077 3078 CONECT 3077 3075 3076 CONECT 3078 3076 3080 CONECT 3079 3080 3081 CONECT 3080 3078 3079 CONECT 3081 3079 3083 CONECT 3082 3083 3084 CONECT 3083 3081 3082 CONECT 3084 3082 CONECT 3085 1726 1746 1943 1964 MASTER 462 0 15 14 5 0 34 6 3114 1 379 33 END