HEADER SIGNALING PROTEIN, ELECTRON TRANSPORT 07-DEC-12 4IAQ TITLE CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF 5-HT1B-BRIL IN COMPLEX TITLE 2 WITH DIHYDROERGOTAMINE (PSI COMMUNITY TARGET) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERA PROTEIN OF HUMAN 5-HYDROXYTRYPTAMINE RECEPTOR 1B COMPND 3 AND E. COLI SOLUBLE CYTOCHROME B562; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: 5-HT-1B, 5-HT1B, S12, SEROTONIN 1D BETA RECEPTOR, 5-HT-1D- COMPND 6 BETA, SEROTONIN RECEPTOR 1B; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 9606, 562; SOURCE 4 GENE: 5HT1B_HUMAN, HTR1B, HTR1DB, CYBC; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS DIHYDROERGOTAMINE, NOVEL PROTEIN ENGINEERING, GPCR NETWORK, MEMBRANE KEYWDS 2 PROTEIN, PSI-BIOLOGY, STRUCTURAL GENOMICS, GPCR, SIGNALING PROTEIN, KEYWDS 3 ELECTRON TRANSPORT, GPCR DOCK EXPDTA X-RAY DIFFRACTION AUTHOR C.WANG,Y.JIANG,J.MA,H.WU,D.WACKER,V.KATRITCH,G.W.HAN,W.LIU,X.HUANG, AUTHOR 2 E.VARDY,J.D.MCCORVY,X.GAO,E.X.ZHOU,K.MELCHER,C.ZHANG,F.BAI,H.YANG, AUTHOR 3 L.YANG,H.JIANG,B.L.ROTH,V.CHEREZOV,R.C.STEVENS,H.E.XU,GPCR NETWORK AUTHOR 4 (GPCR) REVDAT 5 15-NOV-17 4IAQ 1 REMARK REVDAT 4 26-JUL-17 4IAQ 1 SOURCE REMARK REVDAT 3 15-MAY-13 4IAQ 1 JRNL REVDAT 2 10-APR-13 4IAQ 1 JRNL REVDAT 1 13-MAR-13 4IAQ 0 JRNL AUTH C.WANG,Y.JIANG,J.MA,H.WU,D.WACKER,V.KATRITCH,G.W.HAN,W.LIU, JRNL AUTH 2 X.P.HUANG,E.VARDY,J.D.MCCORVY,X.GAO,X.E.ZHOU,K.MELCHER, JRNL AUTH 3 C.ZHANG,F.BAI,H.YANG,L.YANG,H.JIANG,B.L.ROTH,V.CHEREZOV, JRNL AUTH 4 R.C.STEVENS,H.E.XU JRNL TITL STRUCTURAL BASIS FOR MOLECULAR RECOGNITION AT SEROTONIN JRNL TITL 2 RECEPTORS. JRNL REF SCIENCE V. 340 610 2013 JRNL REFN ISSN 0036-8075 JRNL PMID 23519210 JRNL DOI 10.1126/SCIENCE.1232807 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.06 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.4 REMARK 3 NUMBER OF REFLECTIONS : 12993 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) : 0.237 REMARK 3 R VALUE (WORKING SET) : 0.236 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 647 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 : 7 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.02 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.42 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1302 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2579 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1242 REMARK 3 BIN R VALUE (WORKING SET) : 0.2566 REMARK 3 BIN FREE R VALUE : 0.2858 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.61 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 60 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 : 2752 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 43 REMARK 3 SOLVENT ATOMS : 5 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 79.31 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.29 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 12.66690 REMARK 3 B22 (A**2) : 0.06410 REMARK 3 B33 (A**2) : -12.73100 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) : 0.578 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.873 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 2869 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 3948 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1227 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 39 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 421 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 2869 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 415 ; 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 : 3541 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.09 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.31 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.15 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|38 - A|387 } REMARK 3 ORIGIN FOR THE GROUP (A): -21.5753 -3.6383 19.2809 REMARK 3 T TENSOR REMARK 3 T11: 0.3862 T22: -0.1934 REMARK 3 T33: -0.3437 T12: -0.0442 REMARK 3 T13: -0.0497 T23: -0.0149 REMARK 3 L TENSOR REMARK 3 L11: 0.8862 L22: 3.0338 REMARK 3 L33: 4.8226 L12: -0.1759 REMARK 3 L13: 0.1246 L23: -0.4022 REMARK 3 S TENSOR REMARK 3 S11: -0.1260 S12: -0.0613 S13: -0.1410 REMARK 3 S21: 0.1702 S22: -0.0710 S23: -0.0915 REMARK 3 S31: -0.1182 S32: -0.1836 S33: 0.1970 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1001- A|1106 } REMARK 3 ORIGIN FOR THE GROUP (A): -7.1107 -46.3869 29.0148 REMARK 3 T TENSOR REMARK 3 T11: -0.1681 T22: 0.0899 REMARK 3 T33: 0.3062 T12: 0.2270 REMARK 3 T13: -0.2131 T23: -0.1021 REMARK 3 L TENSOR REMARK 3 L11: 3.9833 L22: 7.4235 REMARK 3 L33: 9.3765 L12: 0.4063 REMARK 3 L13: -3.8590 L23: 0.6767 REMARK 3 S TENSOR REMARK 3 S11: -0.0050 S12: -0.2546 S13: -0.7722 REMARK 3 S21: -0.1783 S22: -0.1132 S23: 0.5002 REMARK 3 S31: 0.3999 S32: 1.0885 S33: 0.1182 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4IAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-13. REMARK 100 THE DEPOSITION ID IS D_1000076517. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : AUG-12; AUG-12 REMARK 200 TEMPERATURE (KELVIN) : 100; NULL REMARK 200 PH : 8.7 REMARK 200 NUMBER OF CRYSTALS USED : 56 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-D; 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330; 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL; DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS; MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC REMARK 200 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14244 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 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 (%) : 92.8 REMARK 200 DATA REDUNDANCY : 11.10 REMARK 200 R MERGE (I) : 0.14000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9 REMARK 200 DATA REDUNDANCY IN SHELL : 6.30 REMARK 200 R MERGE FOR SHELL (I) : 0.86000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.7, 32-36% (V/V) REMARK 280 PEG400, 90 MM SODIUM CITRATE TRIBASIC DIHYDRATE, 120 MM AMMONIUM REMARK 280 SULFATE , LIPID CUBIC PHASE (LCP), TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y+1/2,-Z REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.37000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 96.28950 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.37000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 96.28950 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.37000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 96.28950 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.37000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 96.28950 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 36360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 74.34100 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 GLY A 30 REMARK 465 GLY A 31 REMARK 465 THR A 32 REMARK 465 CYS A 33 REMARK 465 SER A 34 REMARK 465 ALA A 35 REMARK 465 LYS A 36 REMARK 465 ASP A 37 REMARK 465 LYS A 191 REMARK 465 ALA A 192 REMARK 465 GLU A 193 REMARK 465 GLU A 194 REMARK 465 GLU A 195 REMARK 465 VAL A 196 REMARK 465 GLU A 1018 REMARK 465 LYS A 1019 REMARK 465 ALA A 1020 REMARK 465 ASP A 1021 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 CYS A 340 REMARK 465 LYS A 341 REMARK 465 ASP A 342 REMARK 465 ALA A 343 REMARK 465 CYS A 344 REMARK 465 TRP A 345 REMARK 465 PHE A 346 REMARK 465 CYS A 388 REMARK 465 THR A 389 REMARK 465 SER A 390 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 ILE A 39 CG1 CG2 CD1 REMARK 470 MET A 54 SD CE REMARK 470 ARG A 76 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 78 CD NE CZ NH1 NH2 REMARK 470 ARG A 114 NE CZ NH1 NH2 REMARK 470 LYS A 160 CD CE NZ REMARK 470 LYS A 164 CG CD CE NZ REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 189 CG CD OE1 NE2 REMARK 470 SER A 197 OG REMARK 470 GLU A 198 CG CD OE1 OE2 REMARK 470 ARG A 230 CD NE CZ NH1 NH2 REMARK 470 GLU A 234 CG CD OE1 OE2 REMARK 470 ARG A 236 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 239 CG1 CG2 CD1 REMARK 470 LEU A1003 CG CD1 CD2 REMARK 470 GLN A1025 CG CD OE1 NE2 REMARK 470 LYS A1027 CG CD CE NZ REMARK 470 LEU A1030 CG CD1 CD2 REMARK 470 MET A1033 CG SD CE REMARK 470 ARG A1034 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1042 CD CE NZ REMARK 470 ASP A1054 CG OD1 OD2 REMARK 470 SER A1055 OG REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ASP A1066 CG OD1 OD2 REMARK 470 GLN A1071 CG CD OE1 NE2 REMARK 470 ASP A1073 CG OD1 OD2 REMARK 470 ASP A1074 CG OD1 OD2 REMARK 470 LEU A1078 CG CD1 CD2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 GLU A1092 CD OE1 OE2 REMARK 470 ARG A1098 CG CD NE CZ NH1 NH2 REMARK 470 ILE A1102 CG1 CG2 CD1 REMARK 470 GLN A1103 CG CD OE1 NE2 REMARK 470 LYS A1104 CD CE NZ REMARK 470 TYR A1105 CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 304 CG CD1 CD2 REMARK 470 MET A 305 SD CE REMARK 470 ARG A 308 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 309 CG CD OE1 OE2 REMARK 470 ARG A 310 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 311 CG CD CE NZ REMARK 470 LYS A 314 CD CE NZ REMARK 470 GLN A 378 CG CD OE1 NE2 REMARK 470 ARG A 385 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 ASP A 153 49.17 -148.58 REMARK 500 ARG A 161 67.10 -67.37 REMARK 500 TRP A 187 75.68 -63.10 REMARK 500 GLN A 189 -48.45 -139.64 REMARK 500 PHE A 217 -70.40 -134.20 REMARK 500 GLU A1057 -43.68 81.52 REMARK 500 ALA A1100 -32.94 -151.04 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2GM A 2001 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-118 RELATED DB: TARGETTRACK REMARK 900 RELATED ID: 4IAR RELATED DB: PDB DBREF 4IAQ A 33 239 UNP P28222 5HT1B_HUMAN 33 239 DBREF 4IAQ A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4IAQ A 304 390 UNP P28222 5HT1B_HUMAN 304 390 SEQADV 4IAQ GLY A 30 UNP P28222 EXPRESSION TAG SEQADV 4IAQ GLY A 31 UNP P28222 EXPRESSION TAG SEQADV 4IAQ THR A 32 UNP P28222 EXPRESSION TAG SEQADV 4IAQ TRP A 138 UNP P28222 LEU 138 ENGINEERED MUTATION SEQADV 4IAQ TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4IAQ ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4IAQ LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQRES 1 A 403 GLY GLY THR CYS SER ALA LYS ASP TYR ILE TYR GLN ASP SEQRES 2 A 403 SER ILE SER LEU PRO TRP LYS VAL LEU LEU VAL MET LEU SEQRES 3 A 403 LEU ALA LEU ILE THR LEU ALA THR THR LEU SER ASN ALA SEQRES 4 A 403 PHE VAL ILE ALA THR VAL TYR ARG THR ARG LYS LEU HIS SEQRES 5 A 403 THR PRO ALA ASN TYR LEU ILE ALA SER LEU ALA VAL THR SEQRES 6 A 403 ASP LEU LEU VAL SER ILE LEU VAL MET PRO ILE SER THR SEQRES 7 A 403 MET TYR THR VAL THR GLY ARG TRP THR LEU GLY GLN VAL SEQRES 8 A 403 VAL CYS ASP PHE TRP LEU SER SER ASP ILE THR CYS CYS SEQRES 9 A 403 THR ALA SER ILE TRP HIS LEU CYS VAL ILE ALA LEU ASP SEQRES 10 A 403 ARG TYR TRP ALA ILE THR ASP ALA VAL GLU TYR SER ALA SEQRES 11 A 403 LYS ARG THR PRO LYS ARG ALA ALA VAL MET ILE ALA LEU SEQRES 12 A 403 VAL TRP VAL PHE SER ILE SER ILE SER LEU PRO PRO PHE SEQRES 13 A 403 PHE TRP ARG GLN ALA LYS ALA GLU GLU GLU VAL SER GLU SEQRES 14 A 403 CYS VAL VAL ASN THR ASP HIS ILE LEU TYR THR VAL TYR SEQRES 15 A 403 SER THR VAL GLY ALA PHE TYR PHE PRO THR LEU LEU LEU SEQRES 16 A 403 ILE ALA LEU TYR GLY ARG ILE TYR VAL GLU ALA ARG SER SEQRES 17 A 403 ARG ILE ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN SEQRES 18 A 403 ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA SEQRES 19 A 403 GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA SEQRES 20 A 403 LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP SEQRES 21 A 403 LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS SEQRES 22 A 403 GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU SEQRES 23 A 403 LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA SEQRES 24 A 403 ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE SEQRES 25 A 403 GLN LYS TYR LEU LEU MET ALA ALA ARG GLU ARG LYS ALA SEQRES 26 A 403 THR LYS THR LEU GLY ILE ILE LEU GLY ALA PHE ILE VAL SEQRES 27 A 403 CYS TRP LEU PRO PHE PHE ILE ILE SER LEU VAL MET PRO SEQRES 28 A 403 ILE CYS LYS ASP ALA CYS TRP PHE HIS LEU ALA ILE PHE SEQRES 29 A 403 ASP PHE PHE THR TRP LEU GLY TYR LEU ASN SER LEU ILE SEQRES 30 A 403 ASN PRO ILE ILE TYR THR MET SER ASN GLU ASP PHE LYS SEQRES 31 A 403 GLN ALA PHE HIS LYS LEU ILE ARG PHE LYS CYS THR SER HET 2GM A2001 43 HETNAM 2GM DIHYDROERGOTAMINE FORMUL 2 2GM C33 H37 N5 O5 FORMUL 3 HOH *5(H2 O) HELIX 1 1 ILE A 39 ILE A 44 5 6 HELIX 2 2 SER A 45 THR A 77 1 33 HELIX 3 3 THR A 82 VAL A 102 1 21 HELIX 4 4 VAL A 102 GLY A 113 1 12 HELIX 5 5 LEU A 117 ARG A 161 1 45 HELIX 6 6 THR A 162 LEU A 182 1 21 HELIX 7 7 HIS A 205 PHE A 217 1 13 HELIX 8 8 PHE A 217 ARG A 238 1 22 HELIX 9 9 ALA A 1001 LYS A 1015 1 15 HELIX 10 10 ALA A 1023 LYS A 1042 1 20 HELIX 11 11 GLU A 1057 GLU A 1081 1 25 HELIX 12 12 VAL A 1084 ASN A 1099 1 16 HELIX 13 13 ILE A 1102 MET A 337 1 39 HELIX 14 14 LEU A 348 ASN A 373 1 26 HELIX 15 15 ASN A 373 ARG A 385 1 13 SSBOND 1 CYS A 122 CYS A 199 1555 1555 2.04 SITE 1 AC1 14 ASP A 129 ILE A 130 CYS A 133 THR A 134 SITE 2 AC1 14 CYS A 199 VAL A 200 VAL A 201 ALA A 216 SITE 3 AC1 14 TRP A 327 PHE A 330 LEU A 348 PHE A 351 SITE 4 AC1 14 ASP A 352 THR A 355 CRYST1 84.740 192.579 74.341 90.00 90.00 90.00 C 2 2 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011801 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005193 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013452 0.00000 ATOM 1 N TYR A 38 -14.433 26.356 16.716 1.00132.53 N ANISOU 1 N TYR A 38 29883 10181 10291 -2803 -2753 163 N ATOM 2 CA TYR A 38 -13.449 25.933 15.721 1.00131.90 C ANISOU 2 CA TYR A 38 29393 10312 10412 -3224 -2652 299 C ATOM 3 C TYR A 38 -13.537 24.404 15.468 1.00128.80 C ANISOU 3 C TYR A 38 28164 10428 10348 -3053 -2490 303 C ATOM 4 O TYR A 38 -13.649 23.615 16.415 1.00127.46 O ANISOU 4 O TYR A 38 27634 10481 10314 -2931 -2518 242 O ATOM 5 CB TYR A 38 -12.019 26.361 16.153 1.00136.79 C ANISOU 5 CB TYR A 38 30072 10854 11049 -3913 -2789 391 C ATOM 6 CG TYR A 38 -10.882 25.530 15.586 1.00138.77 C ANISOU 6 CG TYR A 38 29644 11486 11594 -4331 -2683 519 C ATOM 7 CD1 TYR A 38 -10.471 25.681 14.262 1.00141.98 C ANISOU 7 CD1 TYR A 38 30013 11908 12023 -4537 -2531 635 C ATOM 8 CD2 TYR A 38 -10.208 24.601 16.378 1.00138.31 C ANISOU 8 CD2 TYR A 38 28999 11774 11779 -4502 -2728 529 C ATOM 9 CE1 TYR A 38 -9.435 24.906 13.732 1.00142.73 C ANISOU 9 CE1 TYR A 38 29478 12371 12381 -4883 -2405 753 C ATOM 10 CE2 TYR A 38 -9.171 23.822 15.859 1.00138.82 C ANISOU 10 CE2 TYR A 38 28430 12204 12113 -4832 -2620 648 C ATOM 11 CZ TYR A 38 -8.783 23.982 14.537 1.00147.19 C ANISOU 11 CZ TYR A 38 29445 13287 13194 -5020 -2450 758 C ATOM 12 OH TYR A 38 -7.755 23.219 14.030 1.00146.36 O ANISOU 12 OH TYR A 38 28715 13554 13343 -5320 -2320 876 O ATOM 13 N ILE A 39 -13.468 24.010 14.182 1.00119.92 N ANISOU 13 N ILE A 39 26779 9458 9326 -3054 -2323 378 N ATOM 14 CA ILE A 39 -13.488 22.628 13.733 1.00114.11 C ANISOU 14 CA ILE A 39 25329 9157 8873 -2925 -2159 390 C ATOM 15 C ILE A 39 -12.098 22.265 13.221 1.00115.80 C ANISOU 15 C ILE A 39 25159 9567 9271 -3442 -2083 526 C ATOM 16 O ILE A 39 -11.608 22.908 12.291 1.00117.57 O ANISOU 16 O ILE A 39 25617 9648 9405 -3710 -2027 622 O ATOM 17 CB ILE A 39 -14.574 22.433 12.645 1.00115.45 C ANISOU 17 CB ILE A 39 25518 9355 8993 -2482 -2029 358 C ATOM 18 N TYR A 40 -11.458 21.240 13.827 1.00109.11 N ANISOU 18 N TYR A 40 23727 9055 8676 -3572 -2074 541 N ATOM 19 CA TYR A 40 -10.127 20.755 13.427 1.00109.05 C ANISOU 19 CA TYR A 40 23258 9304 8874 -4009 -1991 670 C ATOM 20 C TYR A 40 -10.127 20.204 11.971 1.00111.98 C ANISOU 20 C TYR A 40 23368 9847 9332 -3929 -1748 731 C ATOM 21 O TYR A 40 -9.094 20.260 11.303 1.00113.53 O ANISOU 21 O TYR A 40 23396 10142 9597 -4309 -1648 855 O ATOM 22 CB TYR A 40 -9.602 19.692 14.419 1.00108.20 C ANISOU 22 CB TYR A 40 22586 9522 9004 -4051 -2041 661 C ATOM 23 CG TYR A 40 -10.186 18.298 14.269 1.00105.84 C ANISOU 23 CG TYR A 40 21787 9531 8898 -3651 -1895 607 C ATOM 24 CD1 TYR A 40 -9.499 17.301 13.577 1.00106.40 C ANISOU 24 CD1 TYR A 40 21309 9926 9194 -3733 -1721 686 C ATOM 25 CD2 TYR A 40 -11.390 17.955 14.878 1.00104.28 C ANISOU 25 CD2 TYR A 40 21663 9305 8655 -3204 -1928 480 C ATOM 26 CE1 TYR A 40 -10.022 16.014 13.451 1.00102.51 C ANISOU 26 CE1 TYR A 40 20409 9680 8860 -3385 -1596 633 C ATOM 27 CE2 TYR A 40 -11.914 16.666 14.773 1.00101.64 C ANISOU 27 CE2 TYR A 40 20885 9242 8491 -2886 -1802 434 C ATOM 28 CZ TYR A 40 -11.236 15.705 14.042 1.00105.61 C ANISOU 28 CZ TYR A 40 20900 10026 9202 -2981 -1643 509 C ATOM 29 OH TYR A 40 -11.760 14.441 13.923 1.00102.17 O ANISOU 29 OH TYR A 40 20085 9820 8915 -2681 -1526 460 O ATOM 30 N GLN A 41 -11.288 19.678 11.498 1.00105.08 N ANISOU 30 N GLN A 41 22463 9018 8446 -3444 -1656 645 N ATOM 31 CA GLN A 41 -11.506 19.111 10.158 1.00102.86 C ANISOU 31 CA GLN A 41 21991 8878 8213 -3295 -1450 675 C ATOM 32 C GLN A 41 -11.347 20.160 9.046 1.00108.64 C ANISOU 32 C GLN A 41 23189 9352 8736 -3473 -1395 758 C ATOM 33 O GLN A 41 -10.923 19.819 7.943 1.00107.09 O ANISOU 33 O GLN A 41 22815 9285 8590 -3574 -1211 836 O ATOM 34 CB GLN A 41 -12.903 18.478 10.059 1.00100.81 C ANISOU 34 CB GLN A 41 21673 8683 7947 -2752 -1427 552 C ATOM 35 CG GLN A 41 -13.067 17.213 10.878 1.00109.87 C ANISOU 35 CG GLN A 41 22307 10123 9315 -2578 -1419 487 C ATOM 36 CD GLN A 41 -13.884 17.404 12.136 1.00128.14 C ANISOU 36 CD GLN A 41 24785 12340 11560 -2335 -1576 379 C ATOM 37 OE1 GLN A 41 -13.882 18.466 12.773 1.00123.96 O ANISOU 37 OE1 GLN A 41 24694 11545 10859 -2424 -1722 367 O ATOM 38 NE2 GLN A 41 -14.570 16.349 12.557 1.00119.12 N ANISOU 38 NE2 GLN A 41 23305 11412 10545 -2037 -1541 301 N ATOM 39 N ASP A 42 -11.668 21.438 9.345 1.00108.11 N ANISOU 39 N ASP A 42 23751 8907 8421 -3509 -1546 742 N ATOM 40 CA ASP A 42 -11.567 22.547 8.389 1.00110.56 C ANISOU 40 CA ASP A 42 24607 8908 8493 -3675 -1518 822 C ATOM 41 C ASP A 42 -10.097 22.832 7.995 1.00115.77 C ANISOU 41 C ASP A 42 25168 9613 9208 -4289 -1431 980 C ATOM 42 O ASP A 42 -9.866 23.476 6.969 1.00118.30 O ANISOU 42 O ASP A 42 25812 9764 9374 -4466 -1334 1073 O ATOM 43 CB ASP A 42 -12.256 23.821 8.936 1.00114.37 C ANISOU 43 CB ASP A 42 25817 8952 8688 -3546 -1714 761 C ATOM 44 CG ASP A 42 -13.770 23.905 8.714 1.00123.38 C ANISOU 44 CG ASP A 42 27217 9981 9681 -2930 -1746 648 C ATOM 45 OD1 ASP A 42 -14.315 23.071 7.942 1.00123.62 O ANISOU 45 OD1 ASP A 42 26919 10245 9804 -2639 -1623 626 O ATOM 46 OD2 ASP A 42 -14.404 24.817 9.290 1.00126.74 O ANISOU 46 OD2 ASP A 42 28180 10088 9887 -2739 -1898 583 O ATOM 47 N SER A 43 -9.118 22.306 8.770 1.00110.55 N ANISOU 47 N SER A 43 24034 9205 8766 -4601 -1457 1017 N ATOM 48 CA SER A 43 -7.689 22.462 8.493 1.00112.33 C ANISOU 48 CA SER A 43 24042 9556 9082 -5181 -1376 1170 C ATOM 49 C SER A 43 -7.081 21.214 7.792 1.00112.87 C ANISOU 49 C SER A 43 23408 10070 9407 -5181 -1129 1235 C ATOM 50 O SER A 43 -5.907 21.261 7.409 1.00115.04 O ANISOU 50 O SER A 43 23438 10504 9767 -5622 -1013 1372 O ATOM 51 CB SER A 43 -6.921 22.789 9.771 1.00117.57 C ANISOU 51 CB SER A 43 24654 10215 9802 -5554 -1588 1183 C ATOM 52 OG SER A 43 -7.079 21.787 10.759 1.00123.39 O ANISOU 52 OG SER A 43 24926 11216 10741 -5315 -1664 1096 O ATOM 53 N ILE A 44 -7.879 20.128 7.586 1.00103.91 N ANISOU 53 N ILE A 44 21972 9128 8382 -4693 -1041 1140 N ATOM 54 CA ILE A 44 -7.440 18.901 6.890 1.00101.47 C ANISOU 54 CA ILE A 44 21073 9197 8284 -4620 -805 1180 C ATOM 55 C ILE A 44 -7.447 19.141 5.341 1.00105.05 C ANISOU 55 C ILE A 44 21731 9585 8600 -4641 -580 1255 C ATOM 56 O ILE A 44 -8.348 19.817 4.825 1.00104.46 O ANISOU 56 O ILE A 44 22181 9216 8293 -4442 -622 1213 O ATOM 57 CB ILE A 44 -8.297 17.664 7.314 1.00100.27 C ANISOU 57 CB ILE A 44 20578 9240 8279 -4129 -815 1047 C ATOM 58 CG1 ILE A 44 -8.094 17.340 8.826 1.00 99.56 C ANISOU 58 CG1 ILE A 44 20245 9251 8332 -4155 -1007 998 C ATOM 59 CG2 ILE A 44 -7.996 16.431 6.443 1.00 99.07 C ANISOU 59 CG2 ILE A 44 19939 9410 8295 -4002 -565 1074 C ATOM 60 CD1 ILE A 44 -9.032 16.261 9.432 1.00 96.65 C ANISOU 60 CD1 ILE A 44 19631 9018 8075 -3696 -1044 866 C ATOM 61 N SER A 45 -6.429 18.598 4.623 1.00101.50 N ANISOU 61 N SER A 45 20872 9413 8281 -4867 -341 1369 N ATOM 62 CA SER A 45 -6.272 18.742 3.169 1.00102.41 C ANISOU 62 CA SER A 45 21137 9504 8269 -4923 -94 1454 C ATOM 63 C SER A 45 -7.267 17.859 2.378 1.00103.78 C ANISOU 63 C SER A 45 21273 9739 8420 -4418 13 1353 C ATOM 64 O SER A 45 -7.778 16.869 2.910 1.00100.04 O ANISOU 64 O SER A 45 20477 9433 8102 -4091 -41 1242 O ATOM 65 CB SER A 45 -4.832 18.446 2.745 1.00107.82 C ANISOU 65 CB SER A 45 21374 10492 9101 -5324 141 1609 C ATOM 66 OG SER A 45 -4.557 17.078 2.492 1.00112.85 O ANISOU 66 OG SER A 45 21427 11499 9950 -5101 329 1593 O ATOM 67 N LEU A 46 -7.547 18.242 1.109 1.00102.42 N ANISOU 67 N LEU A 46 21459 9418 8038 -4376 154 1394 N ATOM 68 CA LEU A 46 -8.472 17.529 0.219 1.00100.04 C ANISOU 68 CA LEU A 46 21192 9149 7671 -3944 239 1308 C ATOM 69 C LEU A 46 -8.097 16.038 0.105 1.00103.18 C ANISOU 69 C LEU A 46 20970 9924 8308 -3799 418 1280 C ATOM 70 O LEU A 46 -8.977 15.223 0.390 1.00100.24 O ANISOU 70 O LEU A 46 20458 9620 8009 -3422 331 1148 O ATOM 71 CB LEU A 46 -8.544 18.179 -1.176 1.00102.13 C ANISOU 71 CB LEU A 46 21916 9223 7667 -4003 386 1388 C ATOM 72 CG LEU A 46 -9.846 18.038 -1.976 1.00105.15 C ANISOU 72 CG LEU A 46 22621 9468 7861 -3556 333 1288 C ATOM 73 CD1 LEU A 46 -9.809 18.896 -3.221 1.00108.60 C ANISOU 73 CD1 LEU A 46 23590 9671 8002 -3671 443 1388 C ATOM 74 CD2 LEU A 46 -10.060 16.647 -2.462 1.00105.31 C ANISOU 74 CD2 LEU A 46 22232 9769 8011 -3277 472 1214 C ATOM 75 N PRO A 47 -6.839 15.633 -0.247 1.00101.77 N ANISOU 75 N PRO A 47 20413 10000 8257 -4074 663 1398 N ATOM 76 CA PRO A 47 -6.541 14.192 -0.349 1.00100.11 C ANISOU 76 CA PRO A 47 19660 10123 8255 -3872 830 1363 C ATOM 77 C PRO A 47 -6.809 13.403 0.936 1.00100.74 C ANISOU 77 C PRO A 47 19380 10339 8559 -3680 649 1260 C ATOM 78 O PRO A 47 -7.307 12.286 0.839 1.00 97.06 O ANISOU 78 O PRO A 47 18704 9998 8177 -3348 690 1164 O ATOM 79 CB PRO A 47 -5.053 14.165 -0.705 1.00105.05 C ANISOU 79 CB PRO A 47 19952 10986 8975 -4242 1089 1526 C ATOM 80 CG PRO A 47 -4.802 15.455 -1.356 1.00112.20 C ANISOU 80 CG PRO A 47 21315 11661 9653 -4577 1137 1639 C ATOM 81 CD PRO A 47 -5.651 16.430 -0.617 1.00107.01 C ANISOU 81 CD PRO A 47 21118 10668 8871 -4565 814 1572 C ATOM 82 N TRP A 48 -6.523 13.989 2.122 1.00 98.79 N ANISOU 82 N TRP A 48 19106 10045 8385 -3891 442 1278 N ATOM 83 CA TRP A 48 -6.743 13.322 3.409 1.00 96.92 C ANISOU 83 CA TRP A 48 18568 9922 8336 -3731 262 1191 C ATOM 84 C TRP A 48 -8.221 13.155 3.726 1.00 96.53 C ANISOU 84 C TRP A 48 18765 9704 8208 -3338 86 1034 C ATOM 85 O TRP A 48 -8.603 12.093 4.208 1.00 93.38 O ANISOU 85 O TRP A 48 18077 9453 7952 -3077 61 947 O ATOM 86 CB TRP A 48 -6.017 14.028 4.558 1.00 97.91 C ANISOU 86 CB TRP A 48 18633 10035 8531 -4078 81 1254 C ATOM 87 CG TRP A 48 -4.562 13.678 4.598 1.00102.02 C ANISOU 87 CG TRP A 48 18660 10867 9236 -4382 226 1387 C ATOM 88 CD1 TRP A 48 -3.514 14.503 4.315 1.00108.85 C ANISOU 88 CD1 TRP A 48 19529 11759 10070 -4843 300 1536 C ATOM 89 CD2 TRP A 48 -4.002 12.372 4.806 1.00101.57 C ANISOU 89 CD2 TRP A 48 18026 11155 9413 -4228 342 1393 C ATOM 90 NE1 TRP A 48 -2.330 13.805 4.383 1.00110.28 N ANISOU 90 NE1 TRP A 48 19123 12314 10466 -4983 448 1635 N ATOM 91 CE2 TRP A 48 -2.601 12.491 4.673 1.00109.35 C ANISOU 91 CE2 TRP A 48 18651 12388 10508 -4589 477 1549 C ATOM 92 CE3 TRP A 48 -4.550 11.106 5.102 1.00100.11 C ANISOU 92 CE3 TRP A 48 17601 11089 9349 -3821 345 1285 C ATOM 93 CZ2 TRP A 48 -1.738 11.397 4.837 1.00109.51 C ANISOU 93 CZ2 TRP A 48 18073 12779 10755 -4510 610 1598 C ATOM 94 CZ3 TRP A 48 -3.696 10.024 5.259 1.00102.20 C ANISOU 94 CZ3 TRP A 48 17326 11681 9825 -3757 475 1332 C ATOM 95 CH2 TRP A 48 -2.308 10.175 5.133 1.00106.47 C ANISOU 95 CH2 TRP A 48 17508 12472 10472 -4076 603 1486 C ATOM 96 N LYS A 49 -9.047 14.166 3.412 1.00 92.75 N ANISOU 96 N LYS A 49 18813 8928 7500 -3288 -25 1003 N ATOM 97 CA LYS A 49 -10.496 14.136 3.605 1.00 89.56 C ANISOU 97 CA LYS A 49 18652 8378 6999 -2906 -185 864 C ATOM 98 C LYS A 49 -11.154 13.075 2.718 1.00 91.29 C ANISOU 98 C LYS A 49 18738 8721 7228 -2586 -60 791 C ATOM 99 O LYS A 49 -12.042 12.379 3.206 1.00 88.48 O ANISOU 99 O LYS A 49 18257 8424 6939 -2295 -157 677 O ATOM 100 CB LYS A 49 -11.106 15.511 3.319 1.00 93.12 C ANISOU 100 CB LYS A 49 19707 8489 7183 -2918 -310 869 C ATOM 101 CG LYS A 49 -11.004 16.460 4.490 1.00 94.07 C ANISOU 101 CG LYS A 49 20045 8428 7268 -3084 -517 871 C ATOM 102 CD LYS A 49 -11.873 17.665 4.300 1.00 92.53 C ANISOU 102 CD LYS A 49 20472 7885 6803 -2963 -658 842 C ATOM 103 CE LYS A 49 -12.273 18.191 5.640 1.00 89.09 C ANISOU 103 CE LYS A 49 20199 7304 6346 -2906 -884 772 C ATOM 104 NZ LYS A 49 -13.016 19.468 5.547 1.00 96.28 N ANISOU 104 NZ LYS A 49 21757 7847 6978 -2791 -1023 751 N ATOM 105 N VAL A 50 -10.712 12.945 1.427 1.00 88.95 N ANISOU 105 N VAL A 50 18480 8464 6854 -2657 156 859 N ATOM 106 CA VAL A 50 -11.208 11.963 0.438 1.00 87.31 C ANISOU 106 CA VAL A 50 18194 8356 6622 -2395 288 797 C ATOM 107 C VAL A 50 -10.762 10.566 0.872 1.00 91.13 C ANISOU 107 C VAL A 50 18161 9115 7351 -2317 390 766 C ATOM 108 O VAL A 50 -11.597 9.665 0.971 1.00 89.04 O ANISOU 108 O VAL A 50 17790 8908 7133 -2037 338 653 O ATOM 109 CB VAL A 50 -10.766 12.300 -1.017 1.00 93.15 C ANISOU 109 CB VAL A 50 19168 9042 7182 -2513 501 886 C ATOM 110 CG1 VAL A 50 -11.038 11.149 -1.983 1.00 91.77 C ANISOU 110 CG1 VAL A 50 18871 9000 6997 -2281 661 827 C ATOM 111 CG2 VAL A 50 -11.448 13.567 -1.513 1.00 94.27 C ANISOU 111 CG2 VAL A 50 19883 8884 7052 -2505 376 900 C ATOM 112 N LEU A 51 -9.458 10.403 1.176 1.00 89.96 N ANISOU 112 N LEU A 51 17692 9135 7355 -2568 521 871 N ATOM 113 CA LEU A 51 -8.870 9.151 1.668 1.00 89.30 C ANISOU 113 CA LEU A 51 17117 9309 7502 -2496 613 863 C ATOM 114 C LEU A 51 -9.624 8.639 2.894 1.00 90.46 C ANISOU 114 C LEU A 51 17140 9463 7766 -2301 398 755 C ATOM 115 O LEU A 51 -9.857 7.438 3.006 1.00 88.60 O ANISOU 115 O LEU A 51 16670 9354 7641 -2085 444 687 O ATOM 116 CB LEU A 51 -7.399 9.373 2.022 1.00 92.02 C ANISOU 116 CB LEU A 51 17157 9825 7981 -2819 715 1004 C ATOM 117 CG LEU A 51 -6.517 8.147 2.004 1.00 97.28 C ANISOU 117 CG LEU A 51 17338 10782 8841 -2747 910 1039 C ATOM 118 CD1 LEU A 51 -5.356 8.338 1.025 1.00100.96 C ANISOU 118 CD1 LEU A 51 17687 11390 9283 -2964 1198 1178 C ATOM 119 CD2 LEU A 51 -6.046 7.798 3.411 1.00 97.89 C ANISOU 119 CD2 LEU A 51 17058 11004 9131 -2789 758 1050 C ATOM 120 N LEU A 52 -10.034 9.563 3.783 1.00 87.10 N ANISOU 120 N LEU A 52 16913 8885 7295 -2374 173 738 N ATOM 121 CA LEU A 52 -10.789 9.272 4.996 1.00 84.97 C ANISOU 121 CA LEU A 52 16583 8601 7101 -2206 -28 642 C ATOM 122 C LEU A 52 -12.240 8.946 4.686 1.00 84.85 C ANISOU 122 C LEU A 52 16747 8503 6989 -1886 -97 514 C ATOM 123 O LEU A 52 -12.846 8.188 5.436 1.00 83.30 O ANISOU 123 O LEU A 52 16388 8375 6888 -1704 -177 432 O ATOM 124 CB LEU A 52 -10.713 10.447 5.989 1.00 86.62 C ANISOU 124 CB LEU A 52 16995 8659 7260 -2390 -230 667 C ATOM 125 CG LEU A 52 -10.360 10.106 7.445 1.00 92.24 C ANISOU 125 CG LEU A 52 17446 9470 8132 -2435 -363 661 C ATOM 126 CD1 LEU A 52 -11.554 9.561 8.197 1.00 90.26 C ANISOU 126 CD1 LEU A 52 17204 9197 7893 -2129 -485 534 C ATOM 127 CD2 LEU A 52 -9.154 9.145 7.556 1.00 96.45 C ANISOU 127 CD2 LEU A 52 17501 10272 8873 -2539 -230 739 C ATOM 128 N VAL A 53 -12.802 9.508 3.606 1.00 80.22 N ANISOU 128 N VAL A 53 16491 7780 6211 -1825 -74 503 N ATOM 129 CA VAL A 53 -14.177 9.219 3.205 1.00 78.20 C ANISOU 129 CA VAL A 53 16382 7475 5855 -1529 -154 389 C ATOM 130 C VAL A 53 -14.223 7.795 2.642 1.00 80.78 C ANISOU 130 C VAL A 53 16453 7969 6273 -1396 -15 341 C ATOM 131 O VAL A 53 -15.134 7.054 3.002 1.00 78.28 O ANISOU 131 O VAL A 53 16033 7705 6003 -1196 -97 241 O ATOM 132 CB VAL A 53 -14.752 10.287 2.232 1.00 83.37 C ANISOU 132 CB VAL A 53 17485 7930 6260 -1488 -200 398 C ATOM 133 CG1 VAL A 53 -15.899 9.746 1.376 1.00 81.83 C ANISOU 133 CG1 VAL A 53 17374 7752 5965 -1213 -228 303 C ATOM 134 CG2 VAL A 53 -15.209 11.516 3.006 1.00 83.94 C ANISOU 134 CG2 VAL A 53 17851 7812 6231 -1486 -396 394 C ATOM 135 N MET A 54 -13.228 7.398 1.814 1.00 79.25 N ANISOU 135 N MET A 54 16157 7857 6099 -1513 203 413 N ATOM 136 CA MET A 54 -13.174 6.046 1.235 1.00 79.01 C ANISOU 136 CA MET A 54 15933 7957 6132 -1380 355 367 C ATOM 137 C MET A 54 -12.974 5.007 2.335 1.00 82.52 C ANISOU 137 C MET A 54 16021 8541 6793 -1321 337 337 C ATOM 138 O MET A 54 -13.744 4.047 2.402 1.00 81.85 O ANISOU 138 O MET A 54 15873 8487 6739 -1138 301 239 O ATOM 139 CB MET A 54 -12.081 5.909 0.157 1.00 83.39 C ANISOU 139 CB MET A 54 16465 8572 6647 -1498 618 458 C ATOM 140 CG MET A 54 -12.344 6.739 -1.099 1.00 88.60 C ANISOU 140 CG MET A 54 17515 9088 7061 -1530 663 483 C ATOM 141 N LEU A 55 -11.985 5.236 3.232 1.00 78.50 N ANISOU 141 N LEU A 55 15298 8107 6421 -1487 338 422 N ATOM 142 CA LEU A 55 -11.635 4.354 4.357 1.00 76.76 C ANISOU 142 CA LEU A 55 14751 8017 6399 -1446 309 416 C ATOM 143 C LEU A 55 -12.852 4.039 5.241 1.00 76.42 C ANISOU 143 C LEU A 55 14742 7923 6372 -1280 120 307 C ATOM 144 O LEU A 55 -13.094 2.868 5.552 1.00 75.40 O ANISOU 144 O LEU A 55 14445 7868 6337 -1141 144 253 O ATOM 145 CB LEU A 55 -10.508 4.997 5.198 1.00 78.15 C ANISOU 145 CB LEU A 55 14760 8257 6676 -1682 272 528 C ATOM 146 CG LEU A 55 -10.077 4.300 6.492 1.00 82.25 C ANISOU 146 CG LEU A 55 14969 8902 7380 -1659 196 539 C ATOM 147 CD1 LEU A 55 -9.392 2.963 6.220 1.00 82.48 C ANISOU 147 CD1 LEU A 55 14698 9102 7537 -1535 379 560 C ATOM 148 CD2 LEU A 55 -9.159 5.192 7.291 1.00 87.25 C ANISOU 148 CD2 LEU A 55 15516 9568 8066 -1922 96 639 C ATOM 149 N LEU A 56 -13.610 5.082 5.615 1.00 70.35 N ANISOU 149 N LEU A 56 14205 7026 5498 -1290 -51 278 N ATOM 150 CA LEU A 56 -14.800 4.997 6.450 1.00 68.19 C ANISOU 150 CA LEU A 56 13976 6717 5217 -1135 -218 184 C ATOM 151 C LEU A 56 -15.971 4.302 5.735 1.00 71.18 C ANISOU 151 C LEU A 56 14414 7103 5530 -937 -214 82 C ATOM 152 O LEU A 56 -16.670 3.508 6.362 1.00 68.83 O ANISOU 152 O LEU A 56 13990 6862 5300 -821 -267 12 O ATOM 153 CB LEU A 56 -15.193 6.402 6.893 1.00 68.90 C ANISOU 153 CB LEU A 56 14331 6661 5186 -1181 -374 190 C ATOM 154 CG LEU A 56 -14.823 6.817 8.326 1.00 73.83 C ANISOU 154 CG LEU A 56 14900 7272 5879 -1277 -495 217 C ATOM 155 CD1 LEU A 56 -13.404 6.376 8.725 1.00 74.56 C ANISOU 155 CD1 LEU A 56 14714 7486 6128 -1468 -421 311 C ATOM 156 CD2 LEU A 56 -15.005 8.312 8.513 1.00 76.69 C ANISOU 156 CD2 LEU A 56 15602 7448 6086 -1352 -622 234 C ATOM 157 N ALA A 57 -16.168 4.570 4.430 1.00 69.91 N ANISOU 157 N ALA A 57 14447 6887 5230 -915 -156 76 N ATOM 158 CA ALA A 57 -17.225 3.932 3.636 1.00 69.81 C ANISOU 158 CA ALA A 57 14502 6886 5137 -754 -173 -19 C ATOM 159 C ALA A 57 -16.899 2.436 3.437 1.00 76.32 C ANISOU 159 C ALA A 57 15122 7807 6070 -725 -38 -48 C ATOM 160 O ALA A 57 -17.796 1.575 3.491 1.00 74.60 O ANISOU 160 O ALA A 57 14853 7627 5866 -619 -90 -137 O ATOM 161 CB ALA A 57 -17.379 4.638 2.300 1.00 71.37 C ANISOU 161 CB ALA A 57 14986 6990 5140 -748 -152 -6 C ATOM 162 N LEU A 58 -15.592 2.136 3.281 1.00 75.50 N ANISOU 162 N LEU A 58 14895 7746 6044 -822 134 33 N ATOM 163 CA LEU A 58 -15.075 0.784 3.125 1.00 75.87 C ANISOU 163 CA LEU A 58 14770 7870 6188 -771 285 22 C ATOM 164 C LEU A 58 -15.329 -0.048 4.397 1.00 78.71 C ANISOU 164 C LEU A 58 14925 8282 6698 -716 208 -11 C ATOM 165 O LEU A 58 -15.767 -1.187 4.276 1.00 79.01 O ANISOU 165 O LEU A 58 14936 8328 6757 -623 237 -80 O ATOM 166 CB LEU A 58 -13.577 0.827 2.770 1.00 77.94 C ANISOU 166 CB LEU A 58 14916 8196 6501 -867 486 133 C ATOM 167 CG LEU A 58 -12.876 -0.505 2.486 1.00 84.33 C ANISOU 167 CG LEU A 58 15566 9084 7392 -773 677 135 C ATOM 168 CD1 LEU A 58 -13.549 -1.277 1.349 1.00 84.86 C ANISOU 168 CD1 LEU A 58 15835 9084 7326 -650 745 38 C ATOM 169 CD2 LEU A 58 -11.413 -0.281 2.184 1.00 90.31 C ANISOU 169 CD2 LEU A 58 16168 9944 8200 -862 875 258 C ATOM 170 N ILE A 59 -15.109 0.517 5.597 1.00 74.06 N ANISOU 170 N ILE A 59 14232 7713 6194 -781 104 35 N ATOM 171 CA ILE A 59 -15.357 -0.240 6.823 1.00 72.87 C ANISOU 171 CA ILE A 59 13919 7604 6163 -730 34 10 C ATOM 172 C ILE A 59 -16.887 -0.332 7.103 1.00 73.05 C ANISOU 172 C ILE A 59 14033 7597 6124 -643 -102 -92 C ATOM 173 O ILE A 59 -17.313 -1.302 7.721 1.00 72.17 O ANISOU 173 O ILE A 59 13824 7515 6081 -591 -115 -133 O ATOM 174 CB ILE A 59 -14.536 0.251 8.064 1.00 76.74 C ANISOU 174 CB ILE A 59 14266 8134 6756 -825 -33 94 C ATOM 175 CG1 ILE A 59 -15.028 1.574 8.630 1.00 77.25 C ANISOU 175 CG1 ILE A 59 14478 8130 6744 -889 -193 92 C ATOM 176 CG2 ILE A 59 -13.027 0.288 7.766 1.00 80.01 C ANISOU 176 CG2 ILE A 59 14529 8626 7244 -922 98 203 C ATOM 177 CD1 ILE A 59 -14.322 1.977 9.880 1.00 92.60 C ANISOU 177 CD1 ILE A 59 16320 10097 8767 -990 -283 158 C ATOM 178 N THR A 60 -17.697 0.643 6.630 1.00 67.33 N ANISOU 178 N THR A 60 13490 6824 5269 -625 -197 -127 N ATOM 179 CA THR A 60 -19.162 0.653 6.801 1.00 65.18 C ANISOU 179 CA THR A 60 13267 6564 4934 -526 -324 -217 C ATOM 180 C THR A 60 -19.764 -0.466 5.952 1.00 68.05 C ANISOU 180 C THR A 60 13630 6954 5271 -481 -282 -293 C ATOM 181 O THR A 60 -20.608 -1.210 6.447 1.00 68.12 O ANISOU 181 O THR A 60 13549 7015 5318 -450 -331 -352 O ATOM 182 CB THR A 60 -19.768 2.040 6.431 1.00 67.90 C ANISOU 182 CB THR A 60 13816 6850 5132 -482 -437 -224 C ATOM 183 OG1 THR A 60 -19.125 3.067 7.176 1.00 67.73 O ANISOU 183 OG1 THR A 60 13848 6769 5118 -551 -474 -155 O ATOM 184 CG2 THR A 60 -21.267 2.118 6.670 1.00 61.56 C ANISOU 184 CG2 THR A 60 13018 6100 4271 -349 -569 -307 C ATOM 185 N LEU A 61 -19.326 -0.578 4.670 1.00 63.62 N ANISOU 185 N LEU A 61 13189 6353 4632 -494 -187 -289 N ATOM 186 CA LEU A 61 -19.805 -1.591 3.733 1.00 62.36 C ANISOU 186 CA LEU A 61 13090 6190 4413 -464 -151 -365 C ATOM 187 C LEU A 61 -19.363 -2.974 4.181 1.00 66.56 C ANISOU 187 C LEU A 61 13496 6729 5064 -474 -47 -372 C ATOM 188 O LEU A 61 -20.166 -3.906 4.102 1.00 68.23 O ANISOU 188 O LEU A 61 13715 6944 5265 -469 -86 -451 O ATOM 189 CB LEU A 61 -19.327 -1.304 2.303 1.00 62.78 C ANISOU 189 CB LEU A 61 13339 6184 4330 -468 -59 -351 C ATOM 190 CG LEU A 61 -19.806 -2.285 1.220 1.00 66.75 C ANISOU 190 CG LEU A 61 13970 6661 4733 -439 -33 -437 C ATOM 191 CD1 LEU A 61 -21.224 -1.972 0.756 1.00 66.33 C ANISOU 191 CD1 LEU A 61 14018 6632 4552 -402 -231 -519 C ATOM 192 CD2 LEU A 61 -18.880 -2.279 0.052 1.00 69.32 C ANISOU 192 CD2 LEU A 61 14455 6926 4957 -441 141 -402 C ATOM 193 N ALA A 62 -18.099 -3.109 4.656 1.00 61.00 N ANISOU 193 N ALA A 62 12682 6029 4467 -490 75 -288 N ATOM 194 CA ALA A 62 -17.568 -4.377 5.143 1.00 60.24 C ANISOU 194 CA ALA A 62 12477 5931 4479 -460 173 -281 C ATOM 195 C ALA A 62 -18.382 -4.844 6.344 1.00 65.91 C ANISOU 195 C ALA A 62 13103 6671 5271 -468 60 -314 C ATOM 196 O ALA A 62 -18.687 -6.028 6.416 1.00 67.21 O ANISOU 196 O ALA A 62 13283 6799 5453 -455 90 -360 O ATOM 197 CB ALA A 62 -16.096 -4.258 5.487 1.00 61.07 C ANISOU 197 CB ALA A 62 12444 6075 4686 -460 293 -172 C ATOM 198 N THR A 63 -18.818 -3.912 7.223 1.00 63.08 N ANISOU 198 N THR A 63 12682 6356 4929 -493 -65 -296 N ATOM 199 CA THR A 63 -19.676 -4.192 8.385 1.00 62.75 C ANISOU 199 CA THR A 63 12558 6351 4934 -497 -159 -323 C ATOM 200 C THR A 63 -21.061 -4.660 7.924 1.00 67.66 C ANISOU 200 C THR A 63 13230 6996 5483 -506 -225 -421 C ATOM 201 O THR A 63 -21.619 -5.585 8.520 1.00 67.96 O ANISOU 201 O THR A 63 13214 7046 5562 -539 -231 -452 O ATOM 202 CB THR A 63 -19.792 -2.956 9.279 1.00 69.98 C ANISOU 202 CB THR A 63 13442 7300 5850 -498 -262 -286 C ATOM 203 OG1 THR A 63 -18.477 -2.546 9.620 1.00 75.07 O ANISOU 203 OG1 THR A 63 14039 7929 6556 -531 -219 -196 O ATOM 204 CG2 THR A 63 -20.582 -3.214 10.560 1.00 66.36 C ANISOU 204 CG2 THR A 63 12901 6885 5427 -489 -330 -305 C ATOM 205 N THR A 64 -21.614 -4.019 6.875 1.00 63.18 N ANISOU 205 N THR A 64 12765 6439 4801 -489 -283 -465 N ATOM 206 CA THR A 64 -22.927 -4.385 6.355 1.00 62.86 C ANISOU 206 CA THR A 64 12748 6450 4685 -505 -376 -555 C ATOM 207 C THR A 64 -22.866 -5.799 5.769 1.00 66.64 C ANISOU 207 C THR A 64 13298 6864 5159 -568 -303 -604 C ATOM 208 O THR A 64 -23.621 -6.670 6.198 1.00 65.62 O ANISOU 208 O THR A 64 13114 6761 5057 -640 -336 -648 O ATOM 209 CB THR A 64 -23.403 -3.355 5.332 1.00 66.41 C ANISOU 209 CB THR A 64 13314 6919 5000 -450 -469 -580 C ATOM 210 OG1 THR A 64 -23.462 -2.080 5.963 1.00 64.94 O ANISOU 210 OG1 THR A 64 13106 6761 4809 -382 -535 -536 O ATOM 211 CG2 THR A 64 -24.764 -3.702 4.739 1.00 64.56 C ANISOU 211 CG2 THR A 64 13077 6770 4684 -464 -596 -670 C ATOM 212 N LEU A 65 -21.949 -6.015 4.810 1.00 63.36 N ANISOU 212 N LEU A 65 13019 6356 4698 -544 -193 -592 N ATOM 213 CA LEU A 65 -21.777 -7.288 4.136 1.00 63.31 C ANISOU 213 CA LEU A 65 13144 6255 4655 -571 -107 -642 C ATOM 214 C LEU A 65 -21.406 -8.402 5.110 1.00 65.55 C ANISOU 214 C LEU A 65 13367 6486 5053 -586 -29 -620 C ATOM 215 O LEU A 65 -22.073 -9.442 5.082 1.00 65.77 O ANISOU 215 O LEU A 65 13467 6466 5058 -666 -54 -684 O ATOM 216 CB LEU A 65 -20.747 -7.180 2.997 1.00 63.92 C ANISOU 216 CB LEU A 65 13378 6255 4654 -505 31 -622 C ATOM 217 CG LEU A 65 -21.120 -6.264 1.799 1.00 68.33 C ANISOU 217 CG LEU A 65 14081 6826 5054 -495 -36 -649 C ATOM 218 CD1 LEU A 65 -20.009 -6.235 0.772 1.00 68.79 C ANISOU 218 CD1 LEU A 65 14294 6809 5033 -438 143 -616 C ATOM 219 CD2 LEU A 65 -22.403 -6.710 1.110 1.00 69.52 C ANISOU 219 CD2 LEU A 65 14345 6983 5085 -556 -185 -759 C ATOM 220 N SER A 66 -20.405 -8.174 6.004 1.00 60.39 N ANISOU 220 N SER A 66 12592 5842 4513 -525 46 -527 N ATOM 221 CA SER A 66 -19.946 -9.197 6.963 1.00 60.18 C ANISOU 221 CA SER A 66 12522 5759 4584 -507 113 -491 C ATOM 222 C SER A 66 -21.044 -9.654 7.942 1.00 61.36 C ANISOU 222 C SER A 66 12617 5935 4762 -606 17 -520 C ATOM 223 O SER A 66 -21.109 -10.839 8.248 1.00 60.15 O ANISOU 223 O SER A 66 12542 5688 4622 -637 61 -534 O ATOM 224 CB SER A 66 -18.719 -8.730 7.735 1.00 64.28 C ANISOU 224 CB SER A 66 12898 6317 5210 -427 171 -381 C ATOM 225 OG SER A 66 -19.027 -7.574 8.491 1.00 77.94 O ANISOU 225 OG SER A 66 14504 8141 6967 -465 59 -349 O ATOM 226 N ASN A 67 -21.913 -8.743 8.396 1.00 57.96 N ANISOU 226 N ASN A 67 12070 5625 4328 -648 -101 -529 N ATOM 227 CA ASN A 67 -23.002 -9.121 9.295 1.00 58.93 C ANISOU 227 CA ASN A 67 12114 5807 4470 -742 -168 -553 C ATOM 228 C ASN A 67 -24.125 -9.826 8.537 1.00 66.15 C ANISOU 228 C ASN A 67 13101 6727 5307 -869 -224 -646 C ATOM 229 O ASN A 67 -24.605 -10.866 9.005 1.00 66.25 O ANISOU 229 O ASN A 67 13140 6699 5333 -985 -210 -664 O ATOM 230 CB ASN A 67 -23.529 -7.931 10.069 1.00 59.59 C ANISOU 230 CB ASN A 67 12050 6026 4566 -713 -255 -530 C ATOM 231 CG ASN A 67 -22.602 -7.528 11.191 1.00 83.37 C ANISOU 231 CG ASN A 67 15001 9021 7653 -645 -222 -441 C ATOM 232 OD1 ASN A 67 -22.502 -8.213 12.214 1.00 79.69 O ANISOU 232 OD1 ASN A 67 14512 8528 7238 -669 -190 -405 O ATOM 233 ND2 ASN A 67 -21.893 -6.413 11.026 1.00 72.93 N ANISOU 233 ND2 ASN A 67 13672 7709 6328 -575 -240 -400 N ATOM 234 N ALA A 68 -24.485 -9.298 7.335 1.00 64.43 N ANISOU 234 N ALA A 68 12938 6545 4995 -861 -291 -703 N ATOM 235 CA ALA A 68 -25.505 -9.830 6.412 1.00 65.45 C ANISOU 235 CA ALA A 68 13145 6693 5029 -983 -380 -797 C ATOM 236 C ALA A 68 -25.285 -11.328 6.160 1.00 70.21 C ANISOU 236 C ALA A 68 13943 7124 5611 -1086 -305 -834 C ATOM 237 O ALA A 68 -26.241 -12.106 6.202 1.00 70.65 O ANISOU 237 O ALA A 68 14012 7192 5639 -1264 -371 -888 O ATOM 238 CB ALA A 68 -25.478 -9.060 5.094 1.00 66.28 C ANISOU 238 CB ALA A 68 13350 6812 5022 -913 -439 -833 C ATOM 239 N PHE A 69 -24.006 -11.721 5.974 1.00 66.85 N ANISOU 239 N PHE A 69 13660 6541 5198 -971 -162 -797 N ATOM 240 CA PHE A 69 -23.529 -13.090 5.769 1.00 67.94 C ANISOU 240 CA PHE A 69 14028 6478 5309 -992 -59 -819 C ATOM 241 C PHE A 69 -23.841 -13.982 6.996 1.00 74.42 C ANISOU 241 C PHE A 69 14824 7251 6202 -1094 -45 -789 C ATOM 242 O PHE A 69 -24.395 -15.071 6.833 1.00 76.71 O ANISOU 242 O PHE A 69 15288 7426 6433 -1249 -60 -846 O ATOM 243 CB PHE A 69 -22.008 -13.056 5.504 1.00 69.11 C ANISOU 243 CB PHE A 69 14250 6530 5478 -783 104 -759 C ATOM 244 CG PHE A 69 -21.335 -14.392 5.645 1.00 71.82 C ANISOU 244 CG PHE A 69 14794 6674 5819 -725 231 -753 C ATOM 245 CD1 PHE A 69 -21.387 -15.323 4.620 1.00 76.65 C ANISOU 245 CD1 PHE A 69 15710 7113 6300 -745 275 -838 C ATOM 246 CD2 PHE A 69 -20.697 -14.744 6.828 1.00 73.79 C ANISOU 246 CD2 PHE A 69 14960 6895 6180 -643 294 -666 C ATOM 247 CE1 PHE A 69 -20.786 -16.572 4.760 1.00 79.20 C ANISOU 247 CE1 PHE A 69 16264 7225 6604 -664 395 -835 C ATOM 248 CE2 PHE A 69 -20.138 -16.011 6.984 1.00 77.98 C ANISOU 248 CE2 PHE A 69 15705 7229 6696 -565 400 -657 C ATOM 249 CZ PHE A 69 -20.169 -16.908 5.945 1.00 77.87 C ANISOU 249 CZ PHE A 69 16003 7031 6552 -565 457 -742 C ATOM 250 N VAL A 70 -23.440 -13.526 8.211 1.00 68.22 N ANISOU 250 N VAL A 70 13855 6537 5528 -1016 -17 -698 N ATOM 251 CA VAL A 70 -23.639 -14.230 9.468 1.00 67.68 C ANISOU 251 CA VAL A 70 13768 6429 5518 -1088 6 -651 C ATOM 252 C VAL A 70 -25.135 -14.480 9.652 1.00 72.55 C ANISOU 252 C VAL A 70 14324 7141 6101 -1328 -91 -706 C ATOM 253 O VAL A 70 -25.512 -15.614 9.947 1.00 73.98 O ANISOU 253 O VAL A 70 14649 7204 6257 -1483 -68 -719 O ATOM 254 CB VAL A 70 -23.010 -13.442 10.651 1.00 69.99 C ANISOU 254 CB VAL A 70 13870 6813 5911 -959 23 -551 C ATOM 255 CG1 VAL A 70 -23.343 -14.072 11.998 1.00 69.35 C ANISOU 255 CG1 VAL A 70 13777 6706 5865 -1039 36 -500 C ATOM 256 CG2 VAL A 70 -21.497 -13.318 10.485 1.00 69.82 C ANISOU 256 CG2 VAL A 70 13878 6720 5932 -753 113 -488 C ATOM 257 N ILE A 71 -25.980 -13.442 9.420 1.00 68.44 N ANISOU 257 N ILE A 71 13600 6833 5571 -1359 -199 -737 N ATOM 258 CA ILE A 71 -27.446 -13.529 9.526 1.00 69.44 C ANISOU 258 CA ILE A 71 13593 7119 5673 -1567 -298 -785 C ATOM 259 C ILE A 71 -27.951 -14.575 8.535 1.00 76.15 C ANISOU 259 C ILE A 71 14643 7860 6429 -1766 -346 -872 C ATOM 260 O ILE A 71 -28.674 -15.501 8.932 1.00 77.60 O ANISOU 260 O ILE A 71 14862 8020 6603 -1998 -353 -886 O ATOM 261 CB ILE A 71 -28.166 -12.159 9.324 1.00 71.95 C ANISOU 261 CB ILE A 71 13665 7687 5985 -1495 -410 -801 C ATOM 262 CG1 ILE A 71 -27.722 -11.107 10.373 1.00 70.57 C ANISOU 262 CG1 ILE A 71 13338 7595 5880 -1314 -370 -721 C ATOM 263 CG2 ILE A 71 -29.698 -12.335 9.342 1.00 74.06 C ANISOU 263 CG2 ILE A 71 13755 8156 6228 -1700 -514 -849 C ATOM 264 CD1 ILE A 71 -27.640 -9.682 9.851 1.00 74.83 C ANISOU 264 CD1 ILE A 71 13799 8239 6393 -1140 -443 -725 C ATOM 265 N ALA A 72 -27.537 -14.444 7.254 1.00 73.10 N ANISOU 265 N ALA A 72 14418 7395 5963 -1688 -374 -929 N ATOM 266 CA ALA A 72 -27.912 -15.365 6.179 1.00 74.68 C ANISOU 266 CA ALA A 72 14866 7466 6043 -1856 -431 -1024 C ATOM 267 C ALA A 72 -27.538 -16.806 6.517 1.00 79.61 C ANISOU 267 C ALA A 72 15772 7827 6649 -1959 -329 -1022 C ATOM 268 O ALA A 72 -28.389 -17.670 6.383 1.00 81.43 O ANISOU 268 O ALA A 72 16110 8012 6819 -2229 -398 -1077 O ATOM 269 CB ALA A 72 -27.253 -14.951 4.878 1.00 75.13 C ANISOU 269 CB ALA A 72 15091 7449 6006 -1697 -431 -1068 C ATOM 270 N THR A 73 -26.305 -17.046 7.017 1.00 75.16 N ANISOU 270 N THR A 73 15318 7102 6136 -1752 -175 -952 N ATOM 271 CA THR A 73 -25.761 -18.365 7.358 1.00 76.50 C ANISOU 271 CA THR A 73 15790 6997 6281 -1766 -65 -936 C ATOM 272 C THR A 73 -26.637 -19.090 8.401 1.00 82.13 C ANISOU 272 C THR A 73 16483 7704 7019 -2026 -87 -910 C ATOM 273 O THR A 73 -26.971 -20.256 8.200 1.00 83.78 O ANISOU 273 O THR A 73 16982 7711 7141 -2224 -89 -956 O ATOM 274 CB THR A 73 -24.297 -18.227 7.813 1.00 84.63 C ANISOU 274 CB THR A 73 16834 7939 7383 -1451 82 -847 C ATOM 275 OG1 THR A 73 -23.554 -17.598 6.765 1.00 87.88 O ANISOU 275 OG1 THR A 73 17262 8368 7760 -1255 118 -870 O ATOM 276 CG2 THR A 73 -23.651 -19.561 8.158 1.00 81.28 C ANISOU 276 CG2 THR A 73 16731 7226 6925 -1397 195 -822 C ATOM 277 N VAL A 74 -27.024 -18.404 9.482 1.00 78.18 N ANISOU 277 N VAL A 74 15670 7415 6619 -2038 -98 -839 N ATOM 278 CA VAL A 74 -27.867 -18.989 10.525 1.00 79.03 C ANISOU 278 CA VAL A 74 15731 7552 6746 -2283 -94 -802 C ATOM 279 C VAL A 74 -29.246 -19.295 9.911 1.00 86.72 C ANISOU 279 C VAL A 74 16662 8635 7654 -2625 -220 -888 C ATOM 280 O VAL A 74 -29.776 -20.388 10.116 1.00 89.13 O ANISOU 280 O VAL A 74 17154 8807 7905 -2904 -214 -899 O ATOM 281 CB VAL A 74 -27.941 -18.074 11.781 1.00 80.43 C ANISOU 281 CB VAL A 74 15588 7946 7027 -2183 -65 -710 C ATOM 282 CG1 VAL A 74 -28.756 -18.718 12.902 1.00 81.45 C ANISOU 282 CG1 VAL A 74 15690 8099 7159 -2427 -25 -660 C ATOM 283 CG2 VAL A 74 -26.543 -17.730 12.283 1.00 78.25 C ANISOU 283 CG2 VAL A 74 15347 7575 6808 -1866 22 -631 C ATOM 284 N TYR A 75 -29.770 -18.369 9.095 1.00 83.81 N ANISOU 284 N TYR A 75 16078 8491 7276 -2606 -342 -947 N ATOM 285 CA TYR A 75 -31.059 -18.511 8.428 1.00 86.47 C ANISOU 285 CA TYR A 75 16318 8984 7553 -2901 -498 -1028 C ATOM 286 C TYR A 75 -31.046 -19.673 7.429 1.00 91.43 C ANISOU 286 C TYR A 75 17349 9344 8047 -3095 -545 -1118 C ATOM 287 O TYR A 75 -31.943 -20.514 7.479 1.00 94.62 O ANISOU 287 O TYR A 75 17815 9732 8403 -3452 -609 -1149 O ATOM 288 CB TYR A 75 -31.464 -17.191 7.724 1.00 88.06 C ANISOU 288 CB TYR A 75 16235 9466 7760 -2761 -629 -1064 C ATOM 289 CG TYR A 75 -32.917 -17.157 7.292 1.00 93.54 C ANISOU 289 CG TYR A 75 16707 10416 8417 -3037 -807 -1124 C ATOM 290 CD1 TYR A 75 -33.935 -16.930 8.215 1.00 96.64 C ANISOU 290 CD1 TYR A 75 16742 11091 8885 -3179 -815 -1078 C ATOM 291 CD2 TYR A 75 -33.276 -17.371 5.962 1.00 96.21 C ANISOU 291 CD2 TYR A 75 17188 10729 8637 -3156 -969 -1226 C ATOM 292 CE1 TYR A 75 -35.275 -16.935 7.833 1.00100.40 C ANISOU 292 CE1 TYR A 75 16966 11843 9338 -3436 -979 -1125 C ATOM 293 CE2 TYR A 75 -34.615 -17.370 5.566 1.00 99.91 C ANISOU 293 CE2 TYR A 75 17430 11458 9074 -3422 -1161 -1277 C ATOM 294 CZ TYR A 75 -35.611 -17.145 6.507 1.00111.12 C ANISOU 294 CZ TYR A 75 18448 13183 10587 -3560 -1165 -1224 C ATOM 295 OH TYR A 75 -36.939 -17.137 6.149 1.00118.52 O ANISOU 295 OH TYR A 75 19104 14424 11506 -3818 -1352 -1265 O ATOM 296 N ARG A 76 -30.029 -19.730 6.549 1.00 85.85 N ANISOU 296 N ARG A 76 16926 8422 7271 -2871 -505 -1157 N ATOM 297 CA ARG A 76 -29.877 -20.751 5.506 1.00 87.13 C ANISOU 297 CA ARG A 76 17529 8300 7278 -2987 -534 -1252 C ATOM 298 C ARG A 76 -29.587 -22.151 6.088 1.00 92.00 C ANISOU 298 C ARG A 76 18514 8588 7853 -3119 -424 -1231 C ATOM 299 O ARG A 76 -30.277 -23.097 5.718 1.00 94.37 O ANISOU 299 O ARG A 76 19060 8751 8044 -3450 -508 -1300 O ATOM 300 CB ARG A 76 -28.776 -20.356 4.498 1.00 83.42 C ANISOU 300 CB ARG A 76 17248 7706 6741 -2659 -474 -1286 C ATOM 301 N THR A 77 -28.599 -22.273 7.004 1.00 86.63 N ANISOU 301 N THR A 77 17881 7783 7252 -2873 -253 -1134 N ATOM 302 CA THR A 77 -28.156 -23.546 7.586 1.00 87.94 C ANISOU 302 CA THR A 77 18430 7613 7371 -2914 -139 -1099 C ATOM 303 C THR A 77 -29.114 -24.082 8.655 1.00 92.34 C ANISOU 303 C THR A 77 18914 8213 7958 -3263 -155 -1046 C ATOM 304 O THR A 77 -29.416 -23.401 9.645 1.00 90.14 O ANISOU 304 O THR A 77 18263 8186 7800 -3253 -134 -962 O ATOM 305 CB THR A 77 -26.727 -23.433 8.145 1.00 98.44 C ANISOU 305 CB THR A 77 19811 8824 8770 -2495 28 -1007 C ATOM 306 OG1 THR A 77 -25.904 -22.718 7.214 1.00 98.15 O ANISOU 306 OG1 THR A 77 19734 8833 8727 -2192 55 -1039 O ATOM 307 CG2 THR A 77 -26.102 -24.794 8.457 1.00100.01 C ANISOU 307 CG2 THR A 77 20488 8629 8884 -2448 140 -984 C ATOM 308 N ARG A 78 -29.511 -25.360 8.456 1.00 91.92 N ANISOU 308 N ARG A 78 19271 7877 7777 -3564 -174 -1092 N ATOM 309 CA ARG A 78 -30.415 -26.173 9.275 1.00 93.76 C ANISOU 309 CA ARG A 78 19570 8064 7991 -3973 -179 -1052 C ATOM 310 C ARG A 78 -29.777 -26.541 10.620 1.00 96.59 C ANISOU 310 C ARG A 78 20021 8277 8401 -3821 -16 -921 C ATOM 311 O ARG A 78 -30.448 -26.470 11.649 1.00 95.51 O ANISOU 311 O ARG A 78 19660 8305 8326 -4026 11 -841 O ATOM 312 CB ARG A 78 -30.811 -27.444 8.504 1.00 97.58 C ANISOU 312 CB ARG A 78 20565 8217 8292 -4310 -250 -1149 C ATOM 313 CG ARG A 78 -32.191 -27.986 8.853 1.00110.60 C ANISOU 313 CG ARG A 78 22147 9963 9915 -4881 -343 -1150 C ATOM 314 N LYS A 79 -28.483 -26.930 10.599 1.00 93.46 N ANISOU 314 N LYS A 79 19952 7587 7972 -3449 94 -895 N ATOM 315 CA LYS A 79 -27.659 -27.314 11.753 1.00 93.26 C ANISOU 315 CA LYS A 79 20067 7391 7977 -3222 231 -771 C ATOM 316 C LYS A 79 -27.517 -26.151 12.731 1.00 95.92 C ANISOU 316 C LYS A 79 19902 8067 8474 -3038 258 -672 C ATOM 317 O LYS A 79 -27.430 -26.357 13.950 1.00 95.34 O ANISOU 317 O LYS A 79 19831 7966 8429 -3032 331 -562 O ATOM 318 CB LYS A 79 -26.266 -27.746 11.249 1.00 96.03 C ANISOU 318 CB LYS A 79 20775 7441 8270 -2794 319 -781 C ATOM 319 CG LYS A 79 -25.343 -28.408 12.283 1.00113.49 C ANISOU 319 CG LYS A 79 23240 9404 10475 -2537 439 -662 C ATOM 320 CD LYS A 79 -23.844 -28.068 12.088 1.00124.10 C ANISOU 320 CD LYS A 79 24563 10721 11871 -1987 523 -626 C ATOM 321 CE LYS A 79 -23.195 -28.673 10.853 1.00140.69 C ANISOU 321 CE LYS A 79 27054 12555 13848 -1786 570 -723 C ATOM 322 NZ LYS A 79 -23.222 -27.744 9.686 1.00146.12 N ANISOU 322 NZ LYS A 79 27482 13474 14564 -1738 525 -819 N ATOM 323 N LEU A 80 -27.499 -24.923 12.183 1.00 91.51 N ANISOU 323 N LEU A 80 18953 7814 8004 -2890 196 -713 N ATOM 324 CA LEU A 80 -27.320 -23.691 12.943 1.00 88.61 C ANISOU 324 CA LEU A 80 18140 7757 7772 -2694 207 -638 C ATOM 325 C LEU A 80 -28.621 -23.175 13.581 1.00 91.91 C ANISOU 325 C LEU A 80 18199 8484 8238 -2989 160 -619 C ATOM 326 O LEU A 80 -28.608 -22.105 14.194 1.00 88.47 O ANISOU 326 O LEU A 80 17409 8309 7896 -2840 165 -568 O ATOM 327 CB LEU A 80 -26.679 -22.623 12.044 1.00 86.42 C ANISOU 327 CB LEU A 80 17659 7629 7547 -2403 170 -685 C ATOM 328 CG LEU A 80 -25.224 -22.896 11.630 1.00 90.66 C ANISOU 328 CG LEU A 80 18437 7943 8068 -2037 256 -672 C ATOM 329 CD1 LEU A 80 -24.644 -21.722 10.898 1.00 88.56 C ANISOU 329 CD1 LEU A 80 17920 7869 7861 -1790 236 -696 C ATOM 330 CD2 LEU A 80 -24.349 -23.204 12.832 1.00 93.05 C ANISOU 330 CD2 LEU A 80 18805 8134 8416 -1823 347 -548 C ATOM 331 N HIS A 81 -29.720 -23.955 13.504 1.00 91.55 N ANISOU 331 N HIS A 81 18254 8408 8121 -3407 126 -653 N ATOM 332 CA HIS A 81 -30.984 -23.566 14.123 1.00 92.47 C ANISOU 332 CA HIS A 81 18012 8841 8281 -3697 104 -627 C ATOM 333 C HIS A 81 -30.983 -24.032 15.609 1.00 98.03 C ANISOU 333 C HIS A 81 18792 9472 8984 -3762 239 -501 C ATOM 334 O HIS A 81 -31.698 -24.956 16.007 1.00 99.46 O ANISOU 334 O HIS A 81 19137 9557 9097 -4126 277 -474 O ATOM 335 CB HIS A 81 -32.187 -24.074 13.307 1.00 96.05 C ANISOU 335 CB HIS A 81 18466 9359 8668 -4133 -10 -717 C ATOM 336 CG HIS A 81 -32.361 -23.367 11.993 1.00 98.95 C ANISOU 336 CG HIS A 81 18671 9889 9038 -4061 -160 -829 C ATOM 337 ND1 HIS A 81 -32.560 -21.998 11.926 1.00 98.63 N ANISOU 337 ND1 HIS A 81 18183 10203 9090 -3856 -212 -831 N ATOM 338 CD2 HIS A 81 -32.394 -23.868 10.738 1.00102.29 C ANISOU 338 CD2 HIS A 81 19356 10150 9361 -4173 -269 -938 C ATOM 339 CE1 HIS A 81 -32.674 -21.710 10.638 1.00 98.03 C ANISOU 339 CE1 HIS A 81 18110 10167 8969 -3840 -350 -933 C ATOM 340 NE2 HIS A 81 -32.577 -22.801 9.885 1.00100.46 N ANISOU 340 NE2 HIS A 81 18833 10177 9159 -4027 -389 -1003 N ATOM 341 N THR A 82 -30.126 -23.355 16.407 1.00 93.61 N ANISOU 341 N THR A 82 18126 8953 8489 -3406 303 -421 N ATOM 342 CA THR A 82 -29.855 -23.543 17.837 1.00 93.89 C ANISOU 342 CA THR A 82 18226 8930 8518 -3347 416 -296 C ATOM 343 C THR A 82 -30.067 -22.197 18.537 1.00 96.61 C ANISOU 343 C THR A 82 18129 9629 8948 -3186 424 -258 C ATOM 344 O THR A 82 -29.699 -21.180 17.936 1.00 94.68 O ANISOU 344 O THR A 82 17665 9536 8772 -2946 350 -309 O ATOM 345 CB THR A 82 -28.400 -24.065 17.992 1.00104.36 C ANISOU 345 CB THR A 82 19914 9920 9819 -3016 453 -247 C ATOM 346 OG1 THR A 82 -28.312 -25.341 17.365 1.00109.58 O ANISOU 346 OG1 THR A 82 21021 10238 10377 -3163 458 -287 O ATOM 347 CG2 THR A 82 -27.928 -24.185 19.454 1.00104.65 C ANISOU 347 CG2 THR A 82 20034 9887 9840 -2885 539 -113 C ATOM 348 N PRO A 83 -30.600 -22.139 19.798 1.00 93.61 N ANISOU 348 N PRO A 83 17648 9368 8552 -3294 520 -169 N ATOM 349 CA PRO A 83 -30.751 -20.833 20.476 1.00 91.11 C ANISOU 349 CA PRO A 83 16962 9361 8293 -3104 533 -140 C ATOM 350 C PRO A 83 -29.432 -20.055 20.588 1.00 90.57 C ANISOU 350 C PRO A 83 16903 9235 8274 -2683 487 -121 C ATOM 351 O PRO A 83 -29.460 -18.827 20.545 1.00 88.34 O ANISOU 351 O PRO A 83 16331 9187 8048 -2508 441 -145 O ATOM 352 CB PRO A 83 -31.298 -21.208 21.859 1.00 94.62 C ANISOU 352 CB PRO A 83 17442 9836 8673 -3272 671 -36 C ATOM 353 CG PRO A 83 -31.941 -22.523 21.668 1.00102.34 C ANISOU 353 CG PRO A 83 18658 10646 9579 -3670 715 -32 C ATOM 354 CD PRO A 83 -31.087 -23.235 20.662 1.00 97.84 C ANISOU 354 CD PRO A 83 18428 9750 8996 -3592 630 -89 C ATOM 355 N ALA A 84 -28.285 -20.769 20.690 1.00 86.35 N ANISOU 355 N ALA A 84 16701 8392 7715 -2524 494 -76 N ATOM 356 CA ALA A 84 -26.937 -20.203 20.770 1.00 84.04 C ANISOU 356 CA ALA A 84 16421 8039 7472 -2151 446 -46 C ATOM 357 C ALA A 84 -26.599 -19.409 19.507 1.00 87.09 C ANISOU 357 C ALA A 84 16633 8527 7930 -2005 359 -138 C ATOM 358 O ALA A 84 -26.130 -18.273 19.632 1.00 85.19 O ANISOU 358 O ALA A 84 16182 8440 7747 -1793 312 -131 O ATOM 359 CB ALA A 84 -25.914 -21.305 20.981 1.00 85.69 C ANISOU 359 CB ALA A 84 17014 7912 7634 -2029 473 16 C ATOM 360 N ASN A 85 -26.866 -19.992 18.300 1.00 83.62 N ANISOU 360 N ASN A 85 16305 7994 7472 -2137 334 -225 N ATOM 361 CA ASN A 85 -26.636 -19.347 17.001 1.00 81.76 C ANISOU 361 CA ASN A 85 15952 7836 7275 -2029 258 -315 C ATOM 362 C ASN A 85 -27.655 -18.236 16.733 1.00 84.80 C ANISOU 362 C ASN A 85 15983 8544 7693 -2114 195 -370 C ATOM 363 O ASN A 85 -27.373 -17.359 15.916 1.00 84.08 O ANISOU 363 O ASN A 85 15758 8554 7635 -1963 129 -420 O ATOM 364 CB ASN A 85 -26.664 -20.342 15.837 1.00 82.92 C ANISOU 364 CB ASN A 85 16372 7773 7361 -2147 248 -394 C ATOM 365 CG ASN A 85 -25.642 -21.454 15.862 1.00 99.81 C ANISOU 365 CG ASN A 85 18899 9573 9452 -2014 312 -357 C ATOM 366 OD1 ASN A 85 -25.996 -22.629 15.983 1.00106.74 O ANISOU 366 OD1 ASN A 85 20081 10231 10247 -2213 350 -355 O ATOM 367 ND2 ASN A 85 -24.370 -21.136 15.645 1.00 78.06 N ANISOU 367 ND2 ASN A 85 16154 6764 6740 -1680 326 -331 N ATOM 368 N TYR A 86 -28.841 -18.272 17.386 1.00 81.41 N ANISOU 368 N TYR A 86 15407 8281 7246 -2346 220 -356 N ATOM 369 CA TYR A 86 -29.843 -17.214 17.224 1.00 80.60 C ANISOU 369 CA TYR A 86 14948 8508 7170 -2383 167 -399 C ATOM 370 C TYR A 86 -29.354 -15.937 17.911 1.00 81.89 C ANISOU 370 C TYR A 86 14937 8804 7373 -2100 167 -356 C ATOM 371 O TYR A 86 -29.732 -14.834 17.501 1.00 80.53 O ANISOU 371 O TYR A 86 14532 8844 7223 -2000 101 -400 O ATOM 372 CB TYR A 86 -31.225 -17.627 17.758 1.00 84.20 C ANISOU 372 CB TYR A 86 15262 9135 7596 -2698 216 -388 C ATOM 373 CG TYR A 86 -31.918 -18.728 16.978 1.00 88.78 C ANISOU 373 CG TYR A 86 15968 9634 8132 -3040 181 -444 C ATOM 374 CD1 TYR A 86 -32.615 -19.739 17.633 1.00 92.81 C ANISOU 374 CD1 TYR A 86 16572 10097 8594 -3368 267 -398 C ATOM 375 CD2 TYR A 86 -31.923 -18.730 15.585 1.00 90.06 C ANISOU 375 CD2 TYR A 86 16165 9768 8284 -3060 59 -543 C ATOM 376 CE1 TYR A 86 -33.259 -20.750 16.927 1.00 95.54 C ANISOU 376 CE1 TYR A 86 17058 10355 8889 -3724 221 -451 C ATOM 377 CE2 TYR A 86 -32.557 -19.743 14.866 1.00 93.70 C ANISOU 377 CE2 TYR A 86 16776 10140 8686 -3394 6 -602 C ATOM 378 CZ TYR A 86 -33.229 -20.748 15.543 1.00103.88 C ANISOU 378 CZ TYR A 86 18162 11375 9934 -3737 81 -557 C ATOM 379 OH TYR A 86 -33.874 -21.740 14.848 1.00108.69 O ANISOU 379 OH TYR A 86 18937 11887 10475 -4107 16 -616 O ATOM 380 N LEU A 87 -28.491 -16.088 18.938 1.00 77.64 N ANISOU 380 N LEU A 87 14540 8127 6831 -1968 227 -269 N ATOM 381 CA LEU A 87 -27.892 -14.959 19.648 1.00 75.52 C ANISOU 381 CA LEU A 87 14167 7943 6586 -1720 210 -226 C ATOM 382 C LEU A 87 -26.805 -14.335 18.780 1.00 77.19 C ANISOU 382 C LEU A 87 14389 8093 6846 -1505 130 -253 C ATOM 383 O LEU A 87 -26.694 -13.114 18.751 1.00 76.55 O ANISOU 383 O LEU A 87 14154 8147 6783 -1359 76 -264 O ATOM 384 CB LEU A 87 -27.318 -15.360 21.016 1.00 75.89 C ANISOU 384 CB LEU A 87 14372 7866 6598 -1665 275 -123 C ATOM 385 CG LEU A 87 -28.216 -16.029 22.067 1.00 82.25 C ANISOU 385 CG LEU A 87 15222 8697 7334 -1870 385 -70 C ATOM 386 CD1 LEU A 87 -27.417 -16.345 23.321 1.00 82.45 C ANISOU 386 CD1 LEU A 87 15452 8567 7309 -1762 422 34 C ATOM 387 CD2 LEU A 87 -29.413 -15.170 22.431 1.00 83.80 C ANISOU 387 CD2 LEU A 87 15137 9191 7511 -1926 422 -94 C ATOM 388 N ILE A 88 -26.022 -15.167 18.059 1.00 73.11 N ANISOU 388 N ILE A 88 14069 7370 6339 -1485 134 -261 N ATOM 389 CA ILE A 88 -24.972 -14.721 17.127 1.00 72.00 C ANISOU 389 CA ILE A 88 13944 7175 6239 -1298 90 -282 C ATOM 390 C ILE A 88 -25.631 -13.905 16.011 1.00 75.83 C ANISOU 390 C ILE A 88 14274 7817 6720 -1328 23 -371 C ATOM 391 O ILE A 88 -25.142 -12.829 15.667 1.00 74.20 O ANISOU 391 O ILE A 88 13968 7687 6539 -1175 -24 -375 O ATOM 392 CB ILE A 88 -24.129 -15.897 16.522 1.00 76.01 C ANISOU 392 CB ILE A 88 14706 7435 6737 -1260 135 -280 C ATOM 393 CG1 ILE A 88 -23.802 -17.069 17.501 1.00 77.55 C ANISOU 393 CG1 ILE A 88 15126 7436 6904 -1277 200 -202 C ATOM 394 CG2 ILE A 88 -22.915 -15.410 15.722 1.00 75.07 C ANISOU 394 CG2 ILE A 88 14574 7287 6661 -1041 125 -281 C ATOM 395 CD1 ILE A 88 -23.212 -16.758 18.847 1.00 87.76 C ANISOU 395 CD1 ILE A 88 16384 8746 8214 -1147 197 -100 C ATOM 396 N ALA A 89 -26.746 -14.428 15.460 1.00 74.01 N ANISOU 396 N ALA A 89 14036 7633 6450 -1538 9 -437 N ATOM 397 CA ALA A 89 -27.528 -13.782 14.408 1.00 74.10 C ANISOU 397 CA ALA A 89 13906 7806 6442 -1582 -78 -521 C ATOM 398 C ALA A 89 -28.143 -12.451 14.905 1.00 78.02 C ANISOU 398 C ALA A 89 14144 8551 6951 -1492 -122 -514 C ATOM 399 O ALA A 89 -28.053 -11.459 14.189 1.00 76.33 O ANISOU 399 O ALA A 89 13855 8417 6731 -1364 -194 -548 O ATOM 400 CB ALA A 89 -28.613 -14.721 13.901 1.00 76.65 C ANISOU 400 CB ALA A 89 14265 8141 6718 -1858 -101 -583 C ATOM 401 N SER A 90 -28.719 -12.410 16.132 1.00 76.39 N ANISOU 401 N SER A 90 13833 8447 6744 -1538 -69 -467 N ATOM 402 CA SER A 90 -29.295 -11.164 16.676 1.00 76.54 C ANISOU 402 CA SER A 90 13642 8686 6755 -1416 -91 -462 C ATOM 403 C SER A 90 -28.199 -10.128 16.953 1.00 78.02 C ANISOU 403 C SER A 90 13881 8807 6955 -1177 -116 -426 C ATOM 404 O SER A 90 -28.428 -8.936 16.731 1.00 77.35 O ANISOU 404 O SER A 90 13695 8843 6851 -1041 -178 -450 O ATOM 405 CB SER A 90 -30.124 -11.419 17.929 1.00 81.42 C ANISOU 405 CB SER A 90 14162 9424 7352 -1514 0 -419 C ATOM 406 OG SER A 90 -29.341 -12.066 18.914 1.00 93.27 O ANISOU 406 OG SER A 90 15847 10742 8851 -1519 79 -342 O ATOM 407 N LEU A 91 -26.996 -10.596 17.373 1.00 72.39 N ANISOU 407 N LEU A 91 13334 7902 6270 -1131 -81 -366 N ATOM 408 CA LEU A 91 -25.811 -9.762 17.588 1.00 70.18 C ANISOU 408 CA LEU A 91 13099 7555 6011 -952 -117 -323 C ATOM 409 C LEU A 91 -25.393 -9.155 16.258 1.00 74.84 C ANISOU 409 C LEU A 91 13688 8137 6612 -881 -177 -368 C ATOM 410 O LEU A 91 -24.945 -8.016 16.220 1.00 74.79 O ANISOU 410 O LEU A 91 13658 8159 6601 -761 -229 -357 O ATOM 411 CB LEU A 91 -24.661 -10.595 18.201 1.00 69.74 C ANISOU 411 CB LEU A 91 13190 7320 5987 -928 -75 -248 C ATOM 412 CG LEU A 91 -23.254 -9.971 18.229 1.00 72.91 C ANISOU 412 CG LEU A 91 13616 7656 6429 -776 -122 -197 C ATOM 413 CD1 LEU A 91 -23.175 -8.767 19.186 1.00 72.65 C ANISOU 413 CD1 LEU A 91 13533 7705 6368 -695 -181 -166 C ATOM 414 CD2 LEU A 91 -22.211 -11.009 18.566 1.00 74.33 C ANISOU 414 CD2 LEU A 91 13915 7683 6645 -739 -85 -130 C ATOM 415 N ALA A 92 -25.568 -9.920 15.166 1.00 72.22 N ANISOU 415 N ALA A 92 13410 7754 6278 -970 -170 -419 N ATOM 416 CA ALA A 92 -25.249 -9.510 13.805 1.00 71.63 C ANISOU 416 CA ALA A 92 13369 7660 6187 -920 -212 -465 C ATOM 417 C ALA A 92 -26.326 -8.574 13.237 1.00 74.79 C ANISOU 417 C ALA A 92 13649 8231 6535 -909 -300 -526 C ATOM 418 O ALA A 92 -26.034 -7.820 12.308 1.00 74.21 O ANISOU 418 O ALA A 92 13607 8157 6432 -826 -350 -548 O ATOM 419 CB ALA A 92 -25.087 -10.737 12.916 1.00 73.22 C ANISOU 419 CB ALA A 92 13716 7728 6376 -1013 -171 -503 C ATOM 420 N VAL A 93 -27.565 -8.625 13.779 1.00 71.30 N ANISOU 420 N VAL A 93 13071 7945 6077 -984 -315 -548 N ATOM 421 CA VAL A 93 -28.654 -7.756 13.319 1.00 71.65 C ANISOU 421 CA VAL A 93 12968 8185 6072 -937 -405 -599 C ATOM 422 C VAL A 93 -28.386 -6.364 13.862 1.00 76.81 C ANISOU 422 C VAL A 93 13602 8877 6706 -738 -429 -567 C ATOM 423 O VAL A 93 -28.492 -5.398 13.107 1.00 77.18 O ANISOU 423 O VAL A 93 13658 8962 6703 -622 -510 -594 O ATOM 424 CB VAL A 93 -30.074 -8.273 13.688 1.00 76.57 C ANISOU 424 CB VAL A 93 13406 9000 6687 -1079 -404 -626 C ATOM 425 CG1 VAL A 93 -31.144 -7.206 13.450 1.00 76.70 C ANISOU 425 CG1 VAL A 93 13228 9256 6657 -959 -492 -663 C ATOM 426 CG2 VAL A 93 -30.415 -9.540 12.911 1.00 77.73 C ANISOU 426 CG2 VAL A 93 13606 9098 6830 -1309 -418 -672 C ATOM 427 N THR A 94 -27.991 -6.269 15.154 1.00 73.20 N ANISOU 427 N THR A 94 13159 8385 6270 -701 -366 -509 N ATOM 428 CA THR A 94 -27.699 -4.992 15.800 1.00 72.56 C ANISOU 428 CA THR A 94 13108 8309 6152 -532 -394 -482 C ATOM 429 C THR A 94 -26.517 -4.339 15.078 1.00 75.18 C ANISOU 429 C THR A 94 13578 8500 6487 -469 -442 -464 C ATOM 430 O THR A 94 -26.624 -3.172 14.712 1.00 75.23 O ANISOU 430 O THR A 94 13623 8527 6434 -350 -510 -479 O ATOM 431 CB THR A 94 -27.495 -5.106 17.348 1.00 80.42 C ANISOU 431 CB THR A 94 14123 9284 7149 -524 -326 -425 C ATOM 432 OG1 THR A 94 -26.179 -5.548 17.686 1.00 80.47 O ANISOU 432 OG1 THR A 94 14252 9119 7204 -559 -309 -366 O ATOM 433 CG2 THR A 94 -28.535 -5.966 18.027 1.00 77.92 C ANISOU 433 CG2 THR A 94 13687 9089 6829 -632 -243 -427 C ATOM 434 N ASP A 95 -25.446 -5.107 14.795 1.00 70.81 N ANISOU 434 N ASP A 95 13100 7811 5993 -544 -399 -431 N ATOM 435 CA ASP A 95 -24.263 -4.590 14.099 1.00 70.61 C ANISOU 435 CA ASP A 95 13172 7679 5979 -505 -416 -403 C ATOM 436 C ASP A 95 -24.583 -4.177 12.637 1.00 73.16 C ANISOU 436 C ASP A 95 13532 8019 6245 -484 -460 -456 C ATOM 437 O ASP A 95 -23.915 -3.287 12.105 1.00 72.76 O ANISOU 437 O ASP A 95 13567 7914 6166 -433 -486 -434 O ATOM 438 CB ASP A 95 -23.097 -5.596 14.144 1.00 73.18 C ANISOU 438 CB ASP A 95 13536 7888 6381 -558 -342 -353 C ATOM 439 CG ASP A 95 -22.466 -5.845 15.516 1.00 89.64 C ANISOU 439 CG ASP A 95 15614 9934 8510 -553 -326 -282 C ATOM 440 OD1 ASP A 95 -22.421 -4.897 16.336 1.00 89.56 O ANISOU 440 OD1 ASP A 95 15608 9949 8470 -506 -381 -257 O ATOM 441 OD2 ASP A 95 -21.951 -6.973 15.740 1.00 99.51 O ANISOU 441 OD2 ASP A 95 16885 11112 9811 -584 -266 -250 O ATOM 442 N LEU A 96 -25.613 -4.784 12.015 1.00 69.00 N ANISOU 442 N LEU A 96 12953 7572 5692 -538 -478 -521 N ATOM 443 CA LEU A 96 -26.067 -4.426 10.668 1.00 69.36 C ANISOU 443 CA LEU A 96 13042 7650 5663 -514 -547 -575 C ATOM 444 C LEU A 96 -26.867 -3.127 10.735 1.00 74.04 C ANISOU 444 C LEU A 96 13599 8352 6181 -377 -645 -591 C ATOM 445 O LEU A 96 -26.840 -2.321 9.794 1.00 74.15 O ANISOU 445 O LEU A 96 13712 8345 6116 -298 -710 -604 O ATOM 446 CB LEU A 96 -26.918 -5.549 10.061 1.00 70.40 C ANISOU 446 CB LEU A 96 13130 7835 5783 -640 -562 -640 C ATOM 447 CG LEU A 96 -27.442 -5.306 8.652 1.00 75.17 C ANISOU 447 CG LEU A 96 13790 8479 6294 -629 -658 -702 C ATOM 448 CD1 LEU A 96 -26.442 -5.755 7.616 1.00 75.05 C ANISOU 448 CD1 LEU A 96 13963 8299 6252 -660 -599 -705 C ATOM 449 CD2 LEU A 96 -28.790 -5.963 8.456 1.00 77.91 C ANISOU 449 CD2 LEU A 96 14006 8978 6620 -741 -737 -767 C ATOM 450 N LEU A 97 -27.578 -2.928 11.864 1.00 70.06 N ANISOU 450 N LEU A 97 12975 7958 5687 -331 -644 -587 N ATOM 451 CA LEU A 97 -28.363 -1.723 12.104 1.00 69.96 C ANISOU 451 CA LEU A 97 12935 8050 5597 -156 -717 -601 C ATOM 452 C LEU A 97 -27.433 -0.544 12.375 1.00 72.91 C ANISOU 452 C LEU A 97 13492 8279 5930 -54 -731 -555 C ATOM 453 O LEU A 97 -27.796 0.571 12.022 1.00 74.15 O ANISOU 453 O LEU A 97 13736 8445 5993 97 -809 -568 O ATOM 454 CB LEU A 97 -29.374 -1.914 13.250 1.00 70.44 C ANISOU 454 CB LEU A 97 12815 8279 5671 -128 -680 -608 C ATOM 455 CG LEU A 97 -30.572 -2.826 12.943 1.00 75.18 C ANISOU 455 CG LEU A 97 13201 9075 6291 -234 -690 -655 C ATOM 456 CD1 LEU A 97 -31.352 -3.131 14.188 1.00 75.65 C ANISOU 456 CD1 LEU A 97 13084 9287 6371 -248 -607 -641 C ATOM 457 CD2 LEU A 97 -31.480 -2.234 11.873 1.00 76.73 C ANISOU 457 CD2 LEU A 97 13328 9413 6412 -124 -820 -706 C ATOM 458 N VAL A 98 -26.223 -0.784 12.951 1.00 67.23 N ANISOU 458 N VAL A 98 12844 7426 5276 -142 -668 -498 N ATOM 459 CA VAL A 98 -25.215 0.269 13.197 1.00 66.35 C ANISOU 459 CA VAL A 98 12901 7178 5133 -108 -692 -447 C ATOM 460 C VAL A 98 -24.637 0.709 11.832 1.00 72.47 C ANISOU 460 C VAL A 98 13803 7866 5867 -126 -717 -440 C ATOM 461 O VAL A 98 -24.453 1.909 11.588 1.00 73.65 O ANISOU 461 O VAL A 98 14117 7939 5929 -56 -775 -425 O ATOM 462 CB VAL A 98 -24.076 -0.132 14.191 1.00 68.14 C ANISOU 462 CB VAL A 98 13129 7318 5441 -207 -641 -383 C ATOM 463 CG1 VAL A 98 -23.189 1.060 14.529 1.00 67.34 C ANISOU 463 CG1 VAL A 98 13191 7100 5294 -198 -696 -335 C ATOM 464 CG2 VAL A 98 -24.627 -0.744 15.472 1.00 68.13 C ANISOU 464 CG2 VAL A 98 13029 7391 5466 -204 -603 -385 C ATOM 465 N SER A 99 -24.381 -0.270 10.944 1.00 68.14 N ANISOU 465 N SER A 99 13209 7316 5364 -220 -664 -452 N ATOM 466 CA SER A 99 -23.817 -0.034 9.626 1.00 68.08 C ANISOU 466 CA SER A 99 13326 7234 5308 -244 -656 -444 C ATOM 467 C SER A 99 -24.811 0.657 8.689 1.00 75.24 C ANISOU 467 C SER A 99 14315 8186 6088 -134 -756 -495 C ATOM 468 O SER A 99 -24.377 1.303 7.738 1.00 76.55 O ANISOU 468 O SER A 99 14647 8266 6171 -123 -769 -476 O ATOM 469 CB SER A 99 -23.336 -1.345 9.019 1.00 70.26 C ANISOU 469 CB SER A 99 13555 7491 5648 -346 -562 -452 C ATOM 470 OG SER A 99 -24.412 -2.189 8.653 1.00 77.08 O ANISOU 470 OG SER A 99 14348 8441 6497 -361 -591 -525 O ATOM 471 N ILE A 100 -26.127 0.537 8.944 1.00 72.81 N ANISOU 471 N ILE A 100 13886 8022 5758 -51 -827 -551 N ATOM 472 CA ILE A 100 -27.142 1.166 8.090 1.00 74.08 C ANISOU 472 CA ILE A 100 14090 8260 5799 83 -947 -596 C ATOM 473 C ILE A 100 -27.575 2.536 8.649 1.00 77.06 C ANISOU 473 C ILE A 100 14556 8635 6090 279 -1021 -584 C ATOM 474 O ILE A 100 -27.490 3.527 7.937 1.00 77.54 O ANISOU 474 O ILE A 100 14822 8607 6032 379 -1088 -571 O ATOM 475 CB ILE A 100 -28.370 0.218 7.873 1.00 78.56 C ANISOU 475 CB ILE A 100 14446 9018 6384 55 -997 -665 C ATOM 476 CG1 ILE A 100 -28.008 -0.968 6.965 1.00 79.13 C ANISOU 476 CG1 ILE A 100 14539 9045 6481 -118 -956 -691 C ATOM 477 CG2 ILE A 100 -29.590 0.966 7.296 1.00 81.50 C ANISOU 477 CG2 ILE A 100 14793 9531 6641 236 -1148 -706 C ATOM 478 CD1 ILE A 100 -28.966 -2.174 7.109 1.00 91.62 C ANISOU 478 CD1 ILE A 100 15919 10777 8117 -238 -975 -747 C ATOM 479 N LEU A 101 -28.052 2.571 9.908 1.00 72.90 N ANISOU 479 N LEU A 101 13902 8193 5604 342 -1000 -588 N ATOM 480 CA LEU A 101 -28.644 3.716 10.613 1.00 73.08 C ANISOU 480 CA LEU A 101 13994 8235 5538 561 -1052 -591 C ATOM 481 C LEU A 101 -27.662 4.728 11.233 1.00 76.96 C ANISOU 481 C LEU A 101 14741 8516 5983 572 -1040 -539 C ATOM 482 O LEU A 101 -28.078 5.856 11.528 1.00 77.56 O ANISOU 482 O LEU A 101 14978 8548 5941 771 -1100 -545 O ATOM 483 CB LEU A 101 -29.492 3.146 11.772 1.00 72.90 C ANISOU 483 CB LEU A 101 13725 8397 5578 594 -998 -614 C ATOM 484 CG LEU A 101 -31.014 3.008 11.644 1.00 78.36 C ANISOU 484 CG LEU A 101 14179 9352 6242 738 -1048 -666 C ATOM 485 CD1 LEU A 101 -31.450 2.502 10.281 1.00 78.93 C ANISOU 485 CD1 LEU A 101 14170 9513 6306 676 -1138 -700 C ATOM 486 CD2 LEU A 101 -31.541 2.074 12.709 1.00 79.07 C ANISOU 486 CD2 LEU A 101 14011 9607 6425 648 -946 -672 C ATOM 487 N VAL A 102 -26.413 4.314 11.530 1.00 71.36 N ANISOU 487 N VAL A 102 14062 7688 5362 366 -968 -491 N ATOM 488 CA VAL A 102 -25.495 5.176 12.270 1.00 69.96 C ANISOU 488 CA VAL A 102 14088 7340 5153 331 -974 -441 C ATOM 489 C VAL A 102 -24.194 5.531 11.511 1.00 73.82 C ANISOU 489 C VAL A 102 14744 7663 5639 164 -965 -380 C ATOM 490 O VAL A 102 -23.874 6.719 11.417 1.00 73.47 O ANISOU 490 O VAL A 102 14962 7468 5485 192 -1022 -353 O ATOM 491 CB VAL A 102 -25.191 4.516 13.640 1.00 71.96 C ANISOU 491 CB VAL A 102 14210 7628 5503 247 -912 -426 C ATOM 492 CG1 VAL A 102 -24.117 5.265 14.406 1.00 71.85 C ANISOU 492 CG1 VAL A 102 14389 7446 5464 162 -939 -373 C ATOM 493 CG2 VAL A 102 -26.452 4.419 14.478 1.00 72.16 C ANISOU 493 CG2 VAL A 102 14115 7804 5498 417 -902 -475 C ATOM 494 N MET A 103 -23.437 4.520 11.032 1.00 70.08 N ANISOU 494 N MET A 103 14132 7214 5280 -6 -883 -354 N ATOM 495 CA MET A 103 -22.124 4.687 10.396 1.00 69.89 C ANISOU 495 CA MET A 103 14199 7080 5275 -174 -834 -286 C ATOM 496 C MET A 103 -22.102 5.516 9.101 1.00 76.60 C ANISOU 496 C MET A 103 15272 7838 5996 -151 -861 -275 C ATOM 497 O MET A 103 -21.172 6.319 8.989 1.00 76.67 O ANISOU 497 O MET A 103 15451 7717 5964 -266 -855 -209 O ATOM 498 CB MET A 103 -21.455 3.337 10.121 1.00 71.29 C ANISOU 498 CB MET A 103 14173 7324 5590 -299 -723 -270 C ATOM 499 CG MET A 103 -20.554 2.851 11.252 1.00 74.29 C ANISOU 499 CG MET A 103 14424 7709 6091 -405 -686 -219 C ATOM 500 SD MET A 103 -19.836 1.217 10.907 1.00 77.37 S ANISOU 500 SD MET A 103 14605 8166 6625 -487 -552 -201 S ATOM 501 CE MET A 103 -20.630 0.316 12.072 1.00 73.94 C ANISOU 501 CE MET A 103 14035 7808 6251 -434 -565 -241 C ATOM 502 N PRO A 104 -23.000 5.360 8.086 1.00 75.33 N ANISOU 502 N PRO A 104 15129 7734 5758 -34 -892 -326 N ATOM 503 CA PRO A 104 -22.808 6.138 6.849 1.00 75.70 C ANISOU 503 CA PRO A 104 15426 7671 5666 -28 -911 -300 C ATOM 504 C PRO A 104 -22.944 7.634 7.075 1.00 81.11 C ANISOU 504 C PRO A 104 16406 8207 6206 64 -1007 -275 C ATOM 505 O PRO A 104 -22.129 8.409 6.579 1.00 83.19 O ANISOU 505 O PRO A 104 16903 8315 6390 -49 -987 -209 O ATOM 506 CB PRO A 104 -23.880 5.597 5.902 1.00 77.44 C ANISOU 506 CB PRO A 104 15591 8004 5829 97 -961 -369 C ATOM 507 CG PRO A 104 -24.864 4.960 6.735 1.00 81.80 C ANISOU 507 CG PRO A 104 15904 8717 6460 189 -1001 -432 C ATOM 508 CD PRO A 104 -24.166 4.462 7.963 1.00 76.94 C ANISOU 508 CD PRO A 104 15139 8104 5990 68 -917 -403 C ATOM 509 N ILE A 105 -23.928 8.023 7.885 1.00 76.51 N ANISOU 509 N ILE A 105 15820 7666 5584 260 -1097 -323 N ATOM 510 CA ILE A 105 -24.281 9.398 8.251 1.00 76.75 C ANISOU 510 CA ILE A 105 16149 7553 5459 418 -1196 -318 C ATOM 511 C ILE A 105 -23.192 9.964 9.204 1.00 76.95 C ANISOU 511 C ILE A 105 16311 7420 5507 236 -1175 -262 C ATOM 512 O ILE A 105 -23.013 11.170 9.274 1.00 76.45 O ANISOU 512 O ILE A 105 16587 7159 5301 259 -1240 -234 O ATOM 513 CB ILE A 105 -25.756 9.397 8.803 1.00 80.85 C ANISOU 513 CB ILE A 105 16549 8225 5945 715 -1270 -396 C ATOM 514 CG1 ILE A 105 -26.069 10.484 9.823 1.00 82.54 C ANISOU 514 CG1 ILE A 105 16983 8328 6052 890 -1328 -404 C ATOM 515 CG2 ILE A 105 -26.245 7.988 9.255 1.00 82.69 C ANISOU 515 CG2 ILE A 105 16371 8703 6346 680 -1209 -443 C ATOM 516 CD1 ILE A 105 -27.548 10.698 9.952 1.00 96.75 C ANISOU 516 CD1 ILE A 105 18709 10280 7773 1236 -1395 -469 C ATOM 517 N SER A 106 -22.406 9.082 9.831 1.00 72.59 N ANISOU 517 N SER A 106 15514 6943 5123 40 -1095 -239 N ATOM 518 CA SER A 106 -21.316 9.431 10.734 1.00 72.57 C ANISOU 518 CA SER A 106 15573 6836 5163 -161 -1094 -183 C ATOM 519 C SER A 106 -20.026 9.727 9.972 1.00 78.49 C ANISOU 519 C SER A 106 16418 7485 5919 -422 -1041 -94 C ATOM 520 O SER A 106 -19.163 10.404 10.513 1.00 78.39 O ANISOU 520 O SER A 106 16545 7352 5890 -603 -1075 -38 O ATOM 521 CB SER A 106 -21.080 8.311 11.739 1.00 74.00 C ANISOU 521 CB SER A 106 15440 7163 5515 -228 -1044 -191 C ATOM 522 OG SER A 106 -19.917 8.546 12.513 1.00 83.62 O ANISOU 522 OG SER A 106 16684 8306 6783 -441 -1058 -128 O ATOM 523 N THR A 107 -19.865 9.194 8.753 1.00 77.65 N ANISOU 523 N THR A 107 16230 7439 5833 -460 -954 -79 N ATOM 524 CA THR A 107 -18.661 9.461 7.941 1.00 79.69 C ANISOU 524 CA THR A 107 16566 7625 6086 -699 -868 12 C ATOM 525 C THR A 107 -18.698 10.922 7.490 1.00 88.58 C ANISOU 525 C THR A 107 18118 8529 7009 -713 -942 48 C ATOM 526 O THR A 107 -17.681 11.622 7.513 1.00 89.23 O ANISOU 526 O THR A 107 18349 8492 7064 -957 -927 131 O ATOM 527 CB THR A 107 -18.551 8.518 6.717 1.00 82.63 C ANISOU 527 CB THR A 107 16788 8108 6499 -703 -740 11 C ATOM 528 OG1 THR A 107 -19.488 8.950 5.732 1.00 84.96 O ANISOU 528 OG1 THR A 107 17305 8346 6629 -530 -792 -28 O ATOM 529 CG2 THR A 107 -18.764 7.045 7.054 1.00 73.68 C ANISOU 529 CG2 THR A 107 15305 7161 5531 -644 -680 -40 C ATOM 530 N MET A 108 -19.909 11.365 7.091 1.00 87.93 N ANISOU 530 N MET A 108 18231 8399 6780 -445 -1028 -14 N ATOM 531 CA MET A 108 -20.241 12.713 6.638 1.00 90.50 C ANISOU 531 CA MET A 108 19004 8500 6882 -360 -1118 5 C ATOM 532 C MET A 108 -19.879 13.725 7.727 1.00 90.17 C ANISOU 532 C MET A 108 19208 8273 6780 -445 -1204 27 C ATOM 533 O MET A 108 -19.195 14.699 7.449 1.00 90.43 O ANISOU 533 O MET A 108 19569 8095 6695 -631 -1217 100 O ATOM 534 CB MET A 108 -21.750 12.812 6.272 1.00 94.75 C ANISOU 534 CB MET A 108 19613 9084 7305 13 -1217 -78 C ATOM 535 CG MET A 108 -22.286 11.642 5.406 1.00 99.97 C ANISOU 535 CG MET A 108 19985 9961 8038 99 -1169 -123 C ATOM 536 SD MET A 108 -23.944 11.892 4.650 1.00107.81 S ANISOU 536 SD MET A 108 21078 11019 8866 490 -1314 -198 S ATOM 537 CE MET A 108 -24.289 10.202 4.027 1.00102.58 C ANISOU 537 CE MET A 108 19988 10633 8354 457 -1249 -257 C ATOM 538 N TYR A 109 -20.279 13.443 8.978 1.00 84.08 N ANISOU 538 N TYR A 109 18285 7578 6085 -339 -1254 -32 N ATOM 539 CA TYR A 109 -20.068 14.304 10.142 1.00 83.88 C ANISOU 539 CA TYR A 109 18499 7383 5987 -384 -1348 -32 C ATOM 540 C TYR A 109 -18.603 14.294 10.629 1.00 86.35 C ANISOU 540 C TYR A 109 18745 7663 6403 -782 -1325 49 C ATOM 541 O TYR A 109 -18.083 15.359 10.949 1.00 88.12 O ANISOU 541 O TYR A 109 19315 7661 6506 -947 -1403 89 O ATOM 542 CB TYR A 109 -21.039 13.904 11.273 1.00 83.71 C ANISOU 542 CB TYR A 109 18322 7483 6002 -120 -1388 -123 C ATOM 543 CG TYR A 109 -21.136 14.877 12.435 1.00 87.21 C ANISOU 543 CG TYR A 109 19089 7734 6312 -62 -1489 -148 C ATOM 544 CD1 TYR A 109 -21.412 16.226 12.223 1.00 91.33 C ANISOU 544 CD1 TYR A 109 20118 7983 6602 51 -1577 -147 C ATOM 545 CD2 TYR A 109 -21.039 14.432 13.754 1.00 86.99 C ANISOU 545 CD2 TYR A 109 18897 7786 6369 -87 -1499 -178 C ATOM 546 CE1 TYR A 109 -21.528 17.116 13.289 1.00 93.68 C ANISOU 546 CE1 TYR A 109 20763 8078 6753 122 -1668 -180 C ATOM 547 CE2 TYR A 109 -21.158 15.313 14.828 1.00 88.97 C ANISOU 547 CE2 TYR A 109 19481 7851 6472 -21 -1591 -209 C ATOM 548 CZ TYR A 109 -21.412 16.653 14.591 1.00 98.39 C ANISOU 548 CZ TYR A 109 21188 8764 7433 88 -1673 -215 C ATOM 549 OH TYR A 109 -21.533 17.526 15.646 1.00100.63 O ANISOU 549 OH TYR A 109 21850 8838 7549 165 -1762 -254 O ATOM 550 N THR A 110 -17.948 13.117 10.681 1.00 79.68 N ANISOU 550 N THR A 110 17469 7038 5770 -932 -1228 75 N ATOM 551 CA THR A 110 -16.557 12.951 11.125 1.00 79.23 C ANISOU 551 CA THR A 110 17252 7015 5836 -1281 -1207 158 C ATOM 552 C THR A 110 -15.571 13.684 10.198 1.00 84.64 C ANISOU 552 C THR A 110 18122 7581 6457 -1575 -1160 261 C ATOM 553 O THR A 110 -14.606 14.273 10.687 1.00 84.96 O ANISOU 553 O THR A 110 18251 7536 6495 -1874 -1216 329 O ATOM 554 CB THR A 110 -16.216 11.445 11.216 1.00 84.46 C ANISOU 554 CB THR A 110 17418 7948 6726 -1293 -1099 160 C ATOM 555 OG1 THR A 110 -17.094 10.843 12.163 1.00 84.96 O ANISOU 555 OG1 THR A 110 17350 8099 6831 -1065 -1142 75 O ATOM 556 CG2 THR A 110 -14.770 11.169 11.636 1.00 82.97 C ANISOU 556 CG2 THR A 110 17002 7844 6679 -1610 -1077 252 C ATOM 557 N VAL A 111 -15.801 13.629 8.871 1.00 82.23 N ANISOU 557 N VAL A 111 17873 7278 6094 -1509 -1059 277 N ATOM 558 CA VAL A 111 -14.890 14.217 7.883 1.00 83.60 C ANISOU 558 CA VAL A 111 18207 7359 6199 -1785 -974 383 C ATOM 559 C VAL A 111 -15.124 15.732 7.748 1.00 89.84 C ANISOU 559 C VAL A 111 19565 7828 6742 -1823 -1085 403 C ATOM 560 O VAL A 111 -14.151 16.484 7.708 1.00 91.39 O ANISOU 560 O VAL A 111 19938 7897 6890 -2168 -1085 498 O ATOM 561 CB VAL A 111 -14.946 13.479 6.514 1.00 86.08 C ANISOU 561 CB VAL A 111 18369 7802 6535 -1712 -806 396 C ATOM 562 CG1 VAL A 111 -14.044 14.149 5.477 1.00 88.02 C ANISOU 562 CG1 VAL A 111 18815 7946 6682 -1992 -695 513 C ATOM 563 CG2 VAL A 111 -14.548 12.012 6.678 1.00 83.89 C ANISOU 563 CG2 VAL A 111 17580 7806 6491 -1704 -691 385 C ATOM 564 N THR A 112 -16.384 16.181 7.702 1.00 86.26 N ANISOU 564 N THR A 112 19397 7247 6131 -1478 -1181 321 N ATOM 565 CA THR A 112 -16.670 17.605 7.529 1.00 88.23 C ANISOU 565 CA THR A 112 20231 7167 6123 -1456 -1285 338 C ATOM 566 C THR A 112 -16.579 18.339 8.859 1.00 94.09 C ANISOU 566 C THR A 112 21203 7737 6808 -1519 -1432 312 C ATOM 567 O THR A 112 -16.032 19.443 8.898 1.00 98.07 O ANISOU 567 O THR A 112 22129 7971 7160 -1759 -1496 372 O ATOM 568 CB THR A 112 -18.022 17.828 6.833 1.00 93.12 C ANISOU 568 CB THR A 112 21074 7728 6581 -1032 -1331 271 C ATOM 569 OG1 THR A 112 -19.087 17.377 7.666 1.00 92.37 O ANISOU 569 OG1 THR A 112 20800 7759 6537 -685 -1404 159 O ATOM 570 CG2 THR A 112 -18.102 17.118 5.498 1.00 89.83 C ANISOU 570 CG2 THR A 112 20473 7465 6194 -988 -1207 293 C ATOM 571 N GLY A 113 -17.093 17.719 9.921 1.00 87.51 N ANISOU 571 N GLY A 113 20116 7050 6083 -1324 -1481 225 N ATOM 572 CA GLY A 113 -17.134 18.286 11.262 1.00 87.25 C ANISOU 572 CA GLY A 113 20290 6875 5985 -1327 -1616 182 C ATOM 573 C GLY A 113 -18.371 19.123 11.506 1.00 91.42 C ANISOU 573 C GLY A 113 21247 7199 6288 -929 -1712 98 C ATOM 574 O GLY A 113 -18.478 19.762 12.550 1.00 92.49 O ANISOU 574 O GLY A 113 21665 7163 6315 -896 -1821 56 O ATOM 575 N ARG A 114 -19.308 19.143 10.547 1.00 87.83 N ANISOU 575 N ARG A 114 20857 6763 5750 -612 -1680 72 N ATOM 576 CA ARG A 114 -20.524 19.946 10.643 1.00 88.97 C ANISOU 576 CA ARG A 114 21387 6742 5677 -181 -1769 1 C ATOM 577 C ARG A 114 -21.763 19.127 10.297 1.00 91.82 C ANISOU 577 C ARG A 114 21402 7379 6107 231 -1729 -72 C ATOM 578 O ARG A 114 -21.773 18.374 9.329 1.00 89.59 O ANISOU 578 O ARG A 114 20827 7284 5929 203 -1653 -50 O ATOM 579 CB ARG A 114 -20.420 21.181 9.736 1.00 91.41 C ANISOU 579 CB ARG A 114 22281 6713 5736 -211 -1818 63 C ATOM 580 CG ARG A 114 -21.351 22.315 10.127 1.00105.79 C ANISOU 580 CG ARG A 114 24648 8256 7290 169 -1937 4 C ATOM 581 CD ARG A 114 -21.076 23.562 9.311 1.00122.38 C ANISOU 581 CD ARG A 114 27393 9974 9132 80 -1992 79 C ATOM 582 N TRP A 115 -22.799 19.265 11.121 1.00 90.18 N ANISOU 582 N TRP A 115 21225 7203 5836 603 -1779 -161 N ATOM 583 CA TRP A 115 -24.076 18.590 10.936 1.00 88.96 C ANISOU 583 CA TRP A 115 20744 7324 5734 1000 -1756 -233 C ATOM 584 C TRP A 115 -24.887 19.371 9.917 1.00 94.40 C ANISOU 584 C TRP A 115 21757 7894 6215 1320 -1825 -231 C ATOM 585 O TRP A 115 -25.030 20.597 10.041 1.00 96.76 O ANISOU 585 O TRP A 115 22597 7887 6281 1469 -1909 -227 O ATOM 586 CB TRP A 115 -24.825 18.475 12.267 1.00 87.57 C ANISOU 586 CB TRP A 115 20466 7245 5562 1261 -1760 -318 C ATOM 587 CG TRP A 115 -26.051 17.640 12.137 1.00 87.93 C ANISOU 587 CG TRP A 115 20086 7628 5698 1593 -1719 -380 C ATOM 588 CD1 TRP A 115 -27.326 18.080 11.948 1.00 92.68 C ANISOU 588 CD1 TRP A 115 20767 8285 6163 2054 -1764 -430 C ATOM 589 CD2 TRP A 115 -26.099 16.213 12.050 1.00 85.53 C ANISOU 589 CD2 TRP A 115 19209 7655 5635 1471 -1631 -390 C ATOM 590 NE1 TRP A 115 -28.177 17.012 11.797 1.00 91.40 N ANISOU 590 NE1 TRP A 115 20082 8492 6153 2198 -1714 -470 N ATOM 591 CE2 TRP A 115 -27.452 15.850 11.872 1.00 90.25 C ANISOU 591 CE2 TRP A 115 19555 8502 6233 1836 -1632 -449 C ATOM 592 CE3 TRP A 115 -25.135 15.197 12.172 1.00 84.56 C ANISOU 592 CE3 TRP A 115 18765 7643 5722 1097 -1554 -354 C ATOM 593 CZ2 TRP A 115 -27.864 14.518 11.787 1.00 87.67 C ANISOU 593 CZ2 TRP A 115 18697 8508 6104 1796 -1562 -474 C ATOM 594 CZ3 TRP A 115 -25.547 13.879 12.109 1.00 84.46 C ANISOU 594 CZ3 TRP A 115 18257 7939 5896 1099 -1479 -382 C ATOM 595 CH2 TRP A 115 -26.899 13.550 11.932 1.00 85.60 C ANISOU 595 CH2 TRP A 115 18188 8306 6031 1425 -1485 -442 C ATOM 596 N THR A 116 -25.398 18.682 8.899 1.00 89.14 N ANISOU 596 N THR A 116 20800 7451 5617 1427 -1803 -232 N ATOM 597 CA THR A 116 -26.124 19.361 7.826 1.00 91.00 C ANISOU 597 CA THR A 116 21330 7593 5654 1722 -1889 -220 C ATOM 598 C THR A 116 -27.444 18.650 7.463 1.00 97.06 C ANISOU 598 C THR A 116 21702 8699 6477 2091 -1919 -286 C ATOM 599 O THR A 116 -27.952 18.853 6.356 1.00 98.30 O ANISOU 599 O THR A 116 21965 8864 6520 2271 -1991 -270 O ATOM 600 CB THR A 116 -25.205 19.472 6.587 1.00 91.40 C ANISOU 600 CB THR A 116 21560 7503 5665 1402 -1858 -127 C ATOM 601 OG1 THR A 116 -24.827 18.165 6.147 1.00 84.58 O ANISOU 601 OG1 THR A 116 20193 6918 5027 1171 -1755 -121 O ATOM 602 CG2 THR A 116 -23.957 20.333 6.835 1.00 89.26 C ANISOU 602 CG2 THR A 116 21714 6891 5309 1028 -1841 -48 C ATOM 603 N LEU A 117 -28.027 17.863 8.392 1.00 93.73 N ANISOU 603 N LEU A 117 20846 8555 6212 2202 -1873 -356 N ATOM 604 CA LEU A 117 -29.257 17.108 8.096 1.00 93.57 C ANISOU 604 CA LEU A 117 20396 8891 6265 2489 -1898 -413 C ATOM 605 C LEU A 117 -30.479 17.480 8.999 1.00 98.52 C ANISOU 605 C LEU A 117 20966 9644 6821 2944 -1928 -481 C ATOM 606 O LEU A 117 -31.485 16.756 9.004 1.00 98.22 O ANISOU 606 O LEU A 117 20488 9954 6878 3139 -1928 -529 O ATOM 607 CB LEU A 117 -28.975 15.598 8.184 1.00 90.78 C ANISOU 607 CB LEU A 117 19492 8822 6177 2196 -1795 -428 C ATOM 608 CG LEU A 117 -27.768 15.096 7.409 1.00 93.72 C ANISOU 608 CG LEU A 117 19860 9114 6637 1777 -1731 -367 C ATOM 609 CD1 LEU A 117 -27.019 14.025 8.198 1.00 91.03 C ANISOU 609 CD1 LEU A 117 19167 8894 6528 1460 -1608 -369 C ATOM 610 CD2 LEU A 117 -28.163 14.632 6.023 1.00 96.25 C ANISOU 610 CD2 LEU A 117 20073 9561 6937 1815 -1776 -364 C ATOM 611 N GLY A 118 -30.406 18.612 9.701 1.00 95.46 N ANISOU 611 N GLY A 118 21033 8980 6256 3112 -1951 -485 N ATOM 612 CA GLY A 118 -31.512 19.087 10.526 1.00 96.98 C ANISOU 612 CA GLY A 118 21241 9261 6346 3583 -1960 -546 C ATOM 613 C GLY A 118 -31.650 18.419 11.875 1.00 99.56 C ANISOU 613 C GLY A 118 21232 9782 6815 3542 -1838 -597 C ATOM 614 O GLY A 118 -30.974 17.428 12.161 1.00 95.71 O ANISOU 614 O GLY A 118 20431 9403 6531 3155 -1756 -587 O ATOM 615 N GLN A 119 -32.541 18.968 12.714 1.00 99.43 N ANISOU 615 N GLN A 119 21297 9807 6675 3966 -1817 -650 N ATOM 616 CA GLN A 119 -32.756 18.499 14.077 1.00 99.29 C ANISOU 616 CA GLN A 119 21042 9945 6738 3984 -1689 -698 C ATOM 617 C GLN A 119 -33.485 17.132 14.139 1.00102.93 C ANISOU 617 C GLN A 119 20793 10887 7430 3952 -1602 -719 C ATOM 618 O GLN A 119 -33.081 16.288 14.945 1.00101.07 O ANISOU 618 O GLN A 119 20305 10751 7347 3676 -1494 -725 O ATOM 619 CB GLN A 119 -33.498 19.559 14.911 1.00103.82 C ANISOU 619 CB GLN A 119 21962 10406 7079 4476 -1674 -747 C ATOM 620 CG GLN A 119 -33.443 19.330 16.431 1.00124.68 C ANISOU 620 CG GLN A 119 24556 13081 9737 4454 -1538 -792 C ATOM 621 CD GLN A 119 -32.063 19.499 17.042 1.00145.48 C ANISOU 621 CD GLN A 119 27539 15374 12362 4013 -1549 -772 C ATOM 622 OE1 GLN A 119 -31.301 18.535 17.205 1.00136.33 O ANISOU 622 OE1 GLN A 119 26082 14309 11410 3577 -1510 -744 O ATOM 623 NE2 GLN A 119 -31.731 20.720 17.440 1.00141.88 N ANISOU 623 NE2 GLN A 119 27727 14519 11661 4126 -1610 -786 N ATOM 624 N VAL A 120 -34.527 16.907 13.308 1.00100.12 N ANISOU 624 N VAL A 120 20133 10818 7090 4213 -1659 -727 N ATOM 625 CA VAL A 120 -35.303 15.650 13.313 1.00 98.93 C ANISOU 625 CA VAL A 120 19321 11126 7143 4167 -1594 -747 C ATOM 626 C VAL A 120 -34.384 14.416 13.039 1.00 99.92 C ANISOU 626 C VAL A 120 19186 11286 7491 3618 -1554 -720 C ATOM 627 O VAL A 120 -34.484 13.421 13.762 1.00 97.59 O ANISOU 627 O VAL A 120 18519 11206 7355 3446 -1436 -734 O ATOM 628 CB VAL A 120 -36.506 15.704 12.330 1.00104.67 C ANISOU 628 CB VAL A 120 19799 12139 7833 4509 -1708 -754 C ATOM 629 CG1 VAL A 120 -37.384 14.461 12.450 1.00104.09 C ANISOU 629 CG1 VAL A 120 19044 12549 7955 4448 -1644 -777 C ATOM 630 CG2 VAL A 120 -37.341 16.956 12.560 1.00108.18 C ANISOU 630 CG2 VAL A 120 20527 12531 8045 5090 -1751 -774 C ATOM 631 N VAL A 121 -33.484 14.507 12.029 1.00 95.87 N ANISOU 631 N VAL A 121 18899 10552 6976 3362 -1638 -678 N ATOM 632 CA VAL A 121 -32.549 13.436 11.664 1.00 93.10 C ANISOU 632 CA VAL A 121 18354 10209 6811 2890 -1596 -649 C ATOM 633 C VAL A 121 -31.447 13.333 12.743 1.00 97.22 C ANISOU 633 C VAL A 121 19010 10538 7392 2606 -1497 -632 C ATOM 634 O VAL A 121 -31.019 12.216 13.046 1.00 95.46 O ANISOU 634 O VAL A 121 18483 10436 7351 2312 -1414 -626 O ATOM 635 CB VAL A 121 -31.991 13.603 10.214 1.00 96.65 C ANISOU 635 CB VAL A 121 19001 10506 7216 2745 -1697 -607 C ATOM 636 CG1 VAL A 121 -30.763 12.733 9.957 1.00 93.79 C ANISOU 636 CG1 VAL A 121 18554 10069 7010 2276 -1626 -571 C ATOM 637 CG2 VAL A 121 -33.069 13.298 9.176 1.00 97.52 C ANISOU 637 CG2 VAL A 121 18862 10878 7312 2948 -1801 -629 C ATOM 638 N CYS A 122 -31.049 14.468 13.367 1.00 95.95 N ANISOU 638 N CYS A 122 19303 10085 7068 2706 -1517 -627 N ATOM 639 CA CYS A 122 -30.044 14.510 14.447 1.00 95.19 C ANISOU 639 CA CYS A 122 19372 9800 6995 2455 -1460 -614 C ATOM 640 C CYS A 122 -30.516 13.690 15.659 1.00100.16 C ANISOU 640 C CYS A 122 19661 10667 7728 2482 -1340 -650 C ATOM 641 O CYS A 122 -29.762 12.851 16.155 1.00 98.43 O ANISOU 641 O CYS A 122 19271 10471 7654 2163 -1280 -629 O ATOM 642 CB CYS A 122 -29.716 15.954 14.838 1.00 97.42 C ANISOU 642 CB CYS A 122 20245 9723 7047 2587 -1527 -612 C ATOM 643 SG CYS A 122 -28.673 16.131 16.319 1.00100.70 S ANISOU 643 SG CYS A 122 20895 9919 7447 2327 -1493 -610 S ATOM 644 N ASP A 123 -31.768 13.914 16.101 1.00 99.12 N ANISOU 644 N ASP A 123 19423 10723 7516 2873 -1301 -699 N ATOM 645 CA ASP A 123 -32.379 13.244 17.250 1.00 98.87 C ANISOU 645 CA ASP A 123 19088 10933 7548 2944 -1165 -730 C ATOM 646 C ASP A 123 -32.571 11.742 17.002 1.00 99.97 C ANISOU 646 C ASP A 123 18686 11380 7916 2699 -1097 -719 C ATOM 647 O ASP A 123 -32.300 10.946 17.903 1.00 98.23 O ANISOU 647 O ASP A 123 18298 11230 7794 2506 -994 -713 O ATOM 648 CB ASP A 123 -33.719 13.906 17.615 1.00103.79 C ANISOU 648 CB ASP A 123 19706 11710 8019 3450 -1126 -778 C ATOM 649 CG ASP A 123 -33.613 15.374 18.000 1.00116.65 C ANISOU 649 CG ASP A 123 21916 13012 9392 3738 -1177 -799 C ATOM 650 OD1 ASP A 123 -32.683 15.727 18.764 1.00116.39 O ANISOU 650 OD1 ASP A 123 22235 12693 9294 3552 -1177 -795 O ATOM 651 OD2 ASP A 123 -34.473 16.166 17.558 1.00126.14 O ANISOU 651 OD2 ASP A 123 23235 14243 10451 4156 -1226 -819 O ATOM 652 N PHE A 124 -33.005 11.356 15.790 1.00 96.06 N ANISOU 652 N PHE A 124 17961 11046 7490 2696 -1163 -715 N ATOM 653 CA PHE A 124 -33.212 9.946 15.440 1.00 94.43 C ANISOU 653 CA PHE A 124 17293 11104 7482 2452 -1117 -710 C ATOM 654 C PHE A 124 -31.869 9.226 15.346 1.00 91.55 C ANISOU 654 C PHE A 124 16969 10569 7245 2030 -1102 -670 C ATOM 655 O PHE A 124 -31.767 8.103 15.840 1.00 89.85 O ANISOU 655 O PHE A 124 16485 10484 7170 1817 -1010 -664 O ATOM 656 CB PHE A 124 -34.015 9.784 14.128 1.00 98.37 C ANISOU 656 CB PHE A 124 17583 11800 7993 2558 -1221 -723 C ATOM 657 CG PHE A 124 -35.496 10.140 14.142 1.00104.32 C ANISOU 657 CG PHE A 124 18118 12846 8671 2955 -1239 -756 C ATOM 658 CD1 PHE A 124 -36.089 10.714 15.270 1.00110.27 C ANISOU 658 CD1 PHE A 124 18907 13661 9329 3254 -1141 -777 C ATOM 659 CD2 PHE A 124 -36.293 9.917 13.023 1.00108.27 C ANISOU 659 CD2 PHE A 124 18381 13571 9187 3043 -1355 -767 C ATOM 660 CE1 PHE A 124 -37.448 11.060 15.271 1.00114.46 C ANISOU 660 CE1 PHE A 124 19206 14492 9792 3654 -1143 -802 C ATOM 661 CE2 PHE A 124 -37.654 10.257 13.028 1.00114.44 C ANISOU 661 CE2 PHE A 124 18918 14659 9905 3422 -1385 -791 C ATOM 662 CZ PHE A 124 -38.220 10.829 14.150 1.00114.65 C ANISOU 662 CZ PHE A 124 18953 14762 9849 3735 -1270 -806 C ATOM 663 N TRP A 125 -30.834 9.889 14.767 1.00 84.10 N ANISOU 663 N TRP A 125 16371 9338 6246 1916 -1182 -638 N ATOM 664 CA TRP A 125 -29.479 9.335 14.614 1.00 80.02 C ANISOU 664 CA TRP A 125 15894 8669 5842 1542 -1166 -591 C ATOM 665 C TRP A 125 -28.767 9.162 15.973 1.00 79.93 C ANISOU 665 C TRP A 125 15937 8567 5864 1398 -1099 -574 C ATOM 666 O TRP A 125 -28.125 8.134 16.182 1.00 76.68 O ANISOU 666 O TRP A 125 15337 8198 5600 1140 -1043 -546 O ATOM 667 CB TRP A 125 -28.627 10.203 13.670 1.00 78.55 C ANISOU 667 CB TRP A 125 16055 8223 5568 1466 -1256 -552 C ATOM 668 CG TRP A 125 -27.193 9.767 13.522 1.00 77.56 C ANISOU 668 CG TRP A 125 15959 7960 5549 1103 -1228 -496 C ATOM 669 CD1 TRP A 125 -26.728 8.697 12.814 1.00 78.89 C ANISOU 669 CD1 TRP A 125 15895 8218 5861 882 -1181 -475 C ATOM 670 CD2 TRP A 125 -26.033 10.444 14.036 1.00 77.38 C ANISOU 670 CD2 TRP A 125 16224 7694 5485 931 -1250 -450 C ATOM 671 NE1 TRP A 125 -25.351 8.661 12.856 1.00 77.21 N ANISOU 671 NE1 TRP A 125 15778 7853 5707 613 -1158 -415 N ATOM 672 CE2 TRP A 125 -24.899 9.706 13.622 1.00 79.58 C ANISOU 672 CE2 TRP A 125 16372 7962 5904 617 -1207 -396 C ATOM 673 CE3 TRP A 125 -25.841 11.602 14.816 1.00 80.06 C ANISOU 673 CE3 TRP A 125 16926 7822 5673 1008 -1306 -450 C ATOM 674 CZ2 TRP A 125 -23.593 10.090 13.955 1.00 78.81 C ANISOU 674 CZ2 TRP A 125 16441 7687 5816 370 -1224 -335 C ATOM 675 CZ3 TRP A 125 -24.548 11.979 15.145 1.00 81.26 C ANISOU 675 CZ3 TRP A 125 17280 7771 5826 732 -1338 -396 C ATOM 676 CH2 TRP A 125 -23.442 11.229 14.717 1.00 80.75 C ANISOU 676 CH2 TRP A 125 17026 7737 5919 412 -1299 -335 C ATOM 677 N LEU A 126 -28.861 10.156 16.876 1.00 76.98 N ANISOU 677 N LEU A 126 15850 8057 5341 1573 -1113 -589 N ATOM 678 CA LEU A 126 -28.216 10.069 18.184 1.00 76.42 C ANISOU 678 CA LEU A 126 15875 7891 5271 1447 -1074 -577 C ATOM 679 C LEU A 126 -28.812 8.937 19.017 1.00 78.43 C ANISOU 679 C LEU A 126 15781 8393 5626 1441 -951 -591 C ATOM 680 O LEU A 126 -28.066 8.189 19.655 1.00 76.39 O ANISOU 680 O LEU A 126 15445 8116 5463 1207 -916 -558 O ATOM 681 CB LEU A 126 -28.327 11.389 18.959 1.00 78.59 C ANISOU 681 CB LEU A 126 16570 7960 5330 1662 -1118 -604 C ATOM 682 CG LEU A 126 -27.459 12.554 18.512 1.00 84.18 C ANISOU 682 CG LEU A 126 17723 8345 5915 1580 -1241 -579 C ATOM 683 CD1 LEU A 126 -27.938 13.826 19.168 1.00 87.62 C ANISOU 683 CD1 LEU A 126 18584 8598 6110 1879 -1276 -624 C ATOM 684 CD2 LEU A 126 -25.982 12.332 18.841 1.00 83.81 C ANISOU 684 CD2 LEU A 126 17748 8145 5950 1185 -1284 -522 C ATOM 685 N SER A 127 -30.158 8.812 18.990 1.00 74.93 N ANISOU 685 N SER A 127 15125 8188 5158 1697 -889 -632 N ATOM 686 CA SER A 127 -30.893 7.790 19.720 1.00 74.17 C ANISOU 686 CA SER A 127 14690 8349 5141 1692 -756 -642 C ATOM 687 C SER A 127 -30.596 6.419 19.147 1.00 75.63 C ANISOU 687 C SER A 127 14565 8649 5521 1396 -732 -613 C ATOM 688 O SER A 127 -30.227 5.525 19.906 1.00 73.93 O ANISOU 688 O SER A 127 14246 8456 5387 1210 -655 -587 O ATOM 689 CB SER A 127 -32.389 8.078 19.705 1.00 80.32 C ANISOU 689 CB SER A 127 15292 9381 5847 2029 -700 -685 C ATOM 690 OG SER A 127 -32.717 9.090 20.645 1.00 94.23 O ANISOU 690 OG SER A 127 17319 11061 7424 2318 -662 -713 O ATOM 691 N SER A 128 -30.673 6.272 17.799 1.00 71.79 N ANISOU 691 N SER A 128 13984 8203 5092 1353 -805 -617 N ATOM 692 CA SER A 128 -30.379 5.018 17.114 1.00 69.36 C ANISOU 692 CA SER A 128 13440 7972 4944 1088 -790 -600 C ATOM 693 C SER A 128 -28.923 4.617 17.343 1.00 72.09 C ANISOU 693 C SER A 128 13910 8114 5366 825 -788 -550 C ATOM 694 O SER A 128 -28.649 3.427 17.359 1.00 72.08 O ANISOU 694 O SER A 128 13729 8169 5488 626 -731 -531 O ATOM 695 CB SER A 128 -30.691 5.111 15.628 1.00 71.72 C ANISOU 695 CB SER A 128 13690 8318 5244 1117 -883 -619 C ATOM 696 OG SER A 128 -29.610 5.701 14.934 1.00 79.41 O ANISOU 696 OG SER A 128 14935 9050 6187 1036 -958 -590 O ATOM 697 N ASP A 129 -28.003 5.583 17.570 1.00 67.79 N ANISOU 697 N ASP A 129 13672 7341 4745 822 -852 -525 N ATOM 698 CA ASP A 129 -26.602 5.277 17.898 1.00 66.23 C ANISOU 698 CA ASP A 129 13560 6986 4620 580 -861 -470 C ATOM 699 C ASP A 129 -26.537 4.607 19.261 1.00 69.82 C ANISOU 699 C ASP A 129 13938 7484 5104 525 -791 -455 C ATOM 700 O ASP A 129 -25.999 3.505 19.376 1.00 68.99 O ANISOU 700 O ASP A 129 13683 7408 5123 344 -747 -419 O ATOM 701 CB ASP A 129 -25.728 6.550 17.896 1.00 68.43 C ANISOU 701 CB ASP A 129 14179 7028 4794 567 -959 -446 C ATOM 702 CG ASP A 129 -24.216 6.357 18.008 1.00 72.65 C ANISOU 702 CG ASP A 129 14767 7429 5409 300 -992 -379 C ATOM 703 OD1 ASP A 129 -23.472 7.199 17.471 1.00 73.29 O ANISOU 703 OD1 ASP A 129 15053 7352 5441 219 -1064 -350 O ATOM 704 OD2 ASP A 129 -23.779 5.385 18.659 1.00 74.71 O ANISOU 704 OD2 ASP A 129 14865 7747 5773 175 -947 -351 O ATOM 705 N ILE A 130 -27.109 5.266 20.278 1.00 66.32 N ANISOU 705 N ILE A 130 13626 7040 4533 702 -774 -481 N ATOM 706 CA ILE A 130 -27.099 4.798 21.655 1.00 66.27 C ANISOU 706 CA ILE A 130 13612 7058 4509 676 -706 -466 C ATOM 707 C ILE A 130 -27.767 3.414 21.766 1.00 70.27 C ANISOU 707 C ILE A 130 13798 7774 5126 606 -583 -461 C ATOM 708 O ILE A 130 -27.135 2.523 22.326 1.00 70.27 O ANISOU 708 O ILE A 130 13753 7746 5200 435 -554 -417 O ATOM 709 CB ILE A 130 -27.720 5.848 22.632 1.00 70.67 C ANISOU 709 CB ILE A 130 14401 7577 4874 920 -692 -506 C ATOM 710 CG1 ILE A 130 -26.864 7.119 22.670 1.00 71.42 C ANISOU 710 CG1 ILE A 130 14878 7408 4850 922 -829 -504 C ATOM 711 CG2 ILE A 130 -27.867 5.279 24.039 1.00 71.39 C ANISOU 711 CG2 ILE A 130 14478 7720 4927 908 -597 -493 C ATOM 712 CD1 ILE A 130 -27.581 8.400 23.087 1.00 85.69 C ANISOU 712 CD1 ILE A 130 16978 9137 6444 1219 -838 -560 C ATOM 713 N THR A 131 -28.991 3.220 21.222 1.00 66.90 N ANISOU 713 N THR A 131 13158 7551 4708 721 -524 -501 N ATOM 714 CA THR A 131 -29.701 1.940 21.362 1.00 67.31 C ANISOU 714 CA THR A 131 12919 7804 4852 618 -410 -496 C ATOM 715 C THR A 131 -28.928 0.766 20.745 1.00 72.12 C ANISOU 715 C THR A 131 13433 8358 5610 357 -422 -462 C ATOM 716 O THR A 131 -28.679 -0.214 21.432 1.00 71.35 O ANISOU 716 O THR A 131 13288 8257 5563 216 -351 -424 O ATOM 717 CB THR A 131 -31.134 1.970 20.806 1.00 74.41 C ANISOU 717 CB THR A 131 13575 8957 5739 759 -370 -542 C ATOM 718 OG1 THR A 131 -31.097 1.927 19.388 1.00 83.25 O ANISOU 718 OG1 THR A 131 14626 10083 6921 714 -467 -561 O ATOM 719 CG2 THR A 131 -31.927 3.161 21.262 1.00 71.24 C ANISOU 719 CG2 THR A 131 13259 8622 5187 1075 -354 -578 C ATOM 720 N CYS A 132 -28.528 0.883 19.476 1.00 70.28 N ANISOU 720 N CYS A 132 13205 8069 5429 312 -506 -472 N ATOM 721 CA CYS A 132 -27.842 -0.158 18.720 1.00 69.87 C ANISOU 721 CA CYS A 132 13084 7966 5499 109 -508 -450 C ATOM 722 C CYS A 132 -26.492 -0.538 19.329 1.00 74.33 C ANISOU 722 C CYS A 132 13763 8366 6114 -17 -510 -387 C ATOM 723 O CYS A 132 -26.213 -1.732 19.457 1.00 74.76 O ANISOU 723 O CYS A 132 13738 8416 6253 -153 -453 -359 O ATOM 724 CB CYS A 132 -27.691 0.262 17.265 1.00 70.23 C ANISOU 724 CB CYS A 132 13157 7978 5549 124 -589 -475 C ATOM 725 SG CYS A 132 -29.260 0.660 16.452 1.00 75.88 S ANISOU 725 SG CYS A 132 13722 8906 6201 285 -627 -543 S ATOM 726 N CYS A 133 -25.676 0.448 19.725 1.00 70.80 N ANISOU 726 N CYS A 133 13506 7785 5611 27 -583 -363 N ATOM 727 CA CYS A 133 -24.358 0.178 20.288 1.00 69.82 C ANISOU 727 CA CYS A 133 13461 7534 5535 -91 -614 -298 C ATOM 728 C CYS A 133 -24.464 -0.462 21.655 1.00 72.93 C ANISOU 728 C CYS A 133 13854 7946 5910 -109 -562 -269 C ATOM 729 O CYS A 133 -23.661 -1.350 21.927 1.00 73.28 O ANISOU 729 O CYS A 133 13869 7942 6032 -217 -555 -216 O ATOM 730 CB CYS A 133 -23.492 1.431 20.318 1.00 71.04 C ANISOU 730 CB CYS A 133 13815 7551 5626 -82 -725 -279 C ATOM 731 SG CYS A 133 -23.058 2.075 18.674 1.00 74.87 S ANISOU 731 SG CYS A 133 14335 7979 6132 -112 -774 -286 S ATOM 732 N THR A 134 -25.475 -0.073 22.485 1.00 68.44 N ANISOU 732 N THR A 134 13318 7454 5232 13 -512 -301 N ATOM 733 CA THR A 134 -25.732 -0.660 23.819 1.00 68.43 C ANISOU 733 CA THR A 134 13337 7482 5182 4 -435 -273 C ATOM 734 C THR A 134 -26.239 -2.125 23.677 1.00 71.76 C ANISOU 734 C THR A 134 13570 8002 5695 -113 -320 -258 C ATOM 735 O THR A 134 -25.811 -2.998 24.436 1.00 70.62 O ANISOU 735 O THR A 134 13461 7806 5566 -203 -287 -203 O ATOM 736 CB THR A 134 -26.738 0.203 24.603 1.00 76.71 C ANISOU 736 CB THR A 134 14467 8602 6076 187 -384 -316 C ATOM 737 OG1 THR A 134 -26.280 1.552 24.617 1.00 78.08 O ANISOU 737 OG1 THR A 134 14866 8649 6154 288 -498 -337 O ATOM 738 CG2 THR A 134 -26.960 -0.281 26.038 1.00 74.67 C ANISOU 738 CG2 THR A 134 14275 8362 5734 185 -292 -283 C ATOM 739 N ALA A 135 -27.160 -2.366 22.707 1.00 68.35 N ANISOU 739 N ALA A 135 12961 7701 5306 -117 -275 -305 N ATOM 740 CA ALA A 135 -27.740 -3.666 22.393 1.00 67.86 C ANISOU 740 CA ALA A 135 12736 7728 5320 -260 -185 -303 C ATOM 741 C ALA A 135 -26.652 -4.614 21.913 1.00 72.08 C ANISOU 741 C ALA A 135 13312 8117 5957 -397 -215 -264 C ATOM 742 O ALA A 135 -26.635 -5.753 22.369 1.00 72.27 O ANISOU 742 O ALA A 135 13339 8113 6008 -511 -144 -225 O ATOM 743 CB ALA A 135 -28.842 -3.529 21.351 1.00 68.92 C ANISOU 743 CB ALA A 135 12687 8032 5469 -236 -181 -367 C ATOM 744 N SER A 136 -25.695 -4.133 21.068 1.00 68.07 N ANISOU 744 N SER A 136 12858 7511 5494 -375 -309 -264 N ATOM 745 CA SER A 136 -24.564 -4.951 20.598 1.00 67.17 C ANISOU 745 CA SER A 136 12773 7275 5473 -462 -324 -223 C ATOM 746 C SER A 136 -23.732 -5.436 21.800 1.00 71.21 C ANISOU 746 C SER A 136 13379 7694 5985 -480 -325 -146 C ATOM 747 O SER A 136 -23.379 -6.617 21.870 1.00 72.49 O ANISOU 747 O SER A 136 13552 7792 6197 -548 -280 -108 O ATOM 748 CB SER A 136 -23.686 -4.167 19.625 1.00 69.30 C ANISOU 748 CB SER A 136 13074 7484 5773 -428 -405 -227 C ATOM 749 OG SER A 136 -22.789 -3.301 20.306 1.00 75.82 O ANISOU 749 OG SER A 136 13997 8240 6569 -388 -485 -183 O ATOM 750 N ILE A 137 -23.458 -4.516 22.756 1.00 65.02 N ANISOU 750 N ILE A 137 12689 6892 5124 -409 -387 -125 N ATOM 751 CA ILE A 137 -22.715 -4.792 23.983 1.00 63.54 C ANISOU 751 CA ILE A 137 12609 6627 4905 -413 -423 -54 C ATOM 752 C ILE A 137 -23.527 -5.745 24.857 1.00 69.79 C ANISOU 752 C ILE A 137 13421 7449 5646 -451 -309 -37 C ATOM 753 O ILE A 137 -22.967 -6.722 25.336 1.00 71.41 O ANISOU 753 O ILE A 137 13684 7575 5875 -494 -300 27 O ATOM 754 CB ILE A 137 -22.353 -3.482 24.742 1.00 65.01 C ANISOU 754 CB ILE A 137 12927 6782 4992 -345 -531 -52 C ATOM 755 CG1 ILE A 137 -21.269 -2.660 24.002 1.00 62.67 C ANISOU 755 CG1 ILE A 137 12635 6428 4749 -364 -653 -42 C ATOM 756 CG2 ILE A 137 -21.938 -3.777 26.182 1.00 65.38 C ANISOU 756 CG2 ILE A 137 13107 6772 4962 -345 -565 10 C ATOM 757 CD1 ILE A 137 -21.283 -1.126 24.317 1.00 48.62 C ANISOU 757 CD1 ILE A 137 11010 4611 2854 -313 -752 -73 C ATOM 758 N TRP A 138 -24.833 -5.480 25.060 1.00 66.66 N ANISOU 758 N TRP A 138 12976 7173 5177 -430 -218 -85 N ATOM 759 CA TRP A 138 -25.668 -6.336 25.903 1.00 67.65 C ANISOU 759 CA TRP A 138 13108 7350 5246 -493 -85 -61 C ATOM 760 C TRP A 138 -25.922 -7.726 25.297 1.00 71.87 C ANISOU 760 C TRP A 138 13572 7870 5866 -645 -7 -50 C ATOM 761 O TRP A 138 -26.124 -8.663 26.071 1.00 72.56 O ANISOU 761 O TRP A 138 13737 7920 5914 -730 79 2 O ATOM 762 CB TRP A 138 -26.975 -5.657 26.298 1.00 67.40 C ANISOU 762 CB TRP A 138 13009 7486 5115 -421 8 -109 C ATOM 763 CG TRP A 138 -26.817 -4.909 27.587 1.00 69.47 C ANISOU 763 CG TRP A 138 13449 7713 5234 -306 -3 -88 C ATOM 764 CD1 TRP A 138 -26.674 -3.561 27.739 1.00 72.12 C ANISOU 764 CD1 TRP A 138 13882 8033 5488 -156 -86 -127 C ATOM 765 CD2 TRP A 138 -26.617 -5.485 28.888 1.00 70.62 C ANISOU 765 CD2 TRP A 138 13754 7792 5285 -340 48 -20 C ATOM 766 NE1 TRP A 138 -26.455 -3.254 29.061 1.00 72.57 N ANISOU 766 NE1 TRP A 138 14148 8026 5400 -96 -89 -97 N ATOM 767 CE2 TRP A 138 -26.419 -4.416 29.792 1.00 74.98 C ANISOU 767 CE2 TRP A 138 14488 8307 5693 -203 -7 -29 C ATOM 768 CE3 TRP A 138 -26.625 -6.804 29.388 1.00 72.48 C ANISOU 768 CE3 TRP A 138 14032 7982 5524 -472 135 49 C ATOM 769 CZ2 TRP A 138 -26.226 -4.624 31.168 1.00 75.71 C ANISOU 769 CZ2 TRP A 138 14792 8333 5643 -192 18 26 C ATOM 770 CZ3 TRP A 138 -26.435 -7.009 30.748 1.00 75.58 C ANISOU 770 CZ3 TRP A 138 14631 8306 5779 -456 165 111 C ATOM 771 CH2 TRP A 138 -26.222 -5.930 31.620 1.00 76.28 C ANISOU 771 CH2 TRP A 138 14887 8371 5724 -317 103 99 C ATOM 772 N HIS A 139 -25.830 -7.881 23.948 1.00 67.16 N ANISOU 772 N HIS A 139 12877 7274 5366 -682 -41 -95 N ATOM 773 CA HIS A 139 -25.956 -9.177 23.263 1.00 67.35 C ANISOU 773 CA HIS A 139 12889 7246 5457 -826 13 -95 C ATOM 774 C HIS A 139 -24.798 -10.075 23.655 1.00 73.11 C ANISOU 774 C HIS A 139 13779 7787 6212 -828 -4 -19 C ATOM 775 O HIS A 139 -24.998 -11.275 23.885 1.00 73.54 O ANISOU 775 O HIS A 139 13923 7761 6259 -939 72 14 O ATOM 776 CB HIS A 139 -26.011 -9.008 21.739 1.00 67.36 C ANISOU 776 CB HIS A 139 12791 7274 5528 -837 -34 -164 C ATOM 777 CG HIS A 139 -27.407 -8.886 21.222 1.00 71.54 C ANISOU 777 CG HIS A 139 13159 7984 6040 -909 3 -231 C ATOM 778 ND1 HIS A 139 -28.119 -7.702 21.325 1.00 73.49 N ANISOU 778 ND1 HIS A 139 13292 8395 6237 -793 -17 -269 N ATOM 779 CD2 HIS A 139 -28.197 -9.819 20.652 1.00 74.38 C ANISOU 779 CD2 HIS A 139 13457 8387 6418 -1083 50 -262 C ATOM 780 CE1 HIS A 139 -29.311 -7.954 20.819 1.00 74.02 C ANISOU 780 CE1 HIS A 139 13192 8627 6305 -883 17 -316 C ATOM 781 NE2 HIS A 139 -29.403 -9.211 20.392 1.00 75.20 N ANISOU 781 NE2 HIS A 139 13363 8714 6496 -1080 50 -315 N ATOM 782 N LEU A 140 -23.596 -9.467 23.794 1.00 70.20 N ANISOU 782 N LEU A 140 13452 7353 5866 -705 -110 15 N ATOM 783 CA LEU A 140 -22.362 -10.114 24.228 1.00 70.99 C ANISOU 783 CA LEU A 140 13666 7314 5994 -655 -157 97 C ATOM 784 C LEU A 140 -22.558 -10.797 25.568 1.00 77.15 C ANISOU 784 C LEU A 140 14594 8035 6685 -683 -112 165 C ATOM 785 O LEU A 140 -22.212 -11.970 25.682 1.00 79.41 O ANISOU 785 O LEU A 140 14997 8194 6980 -706 -77 217 O ATOM 786 CB LEU A 140 -21.242 -9.080 24.334 1.00 70.76 C ANISOU 786 CB LEU A 140 13609 7290 5988 -547 -291 122 C ATOM 787 CG LEU A 140 -20.053 -9.225 23.403 1.00 75.62 C ANISOU 787 CG LEU A 140 14163 7859 6710 -495 -340 142 C ATOM 788 CD1 LEU A 140 -20.381 -8.732 22.000 1.00 75.17 C ANISOU 788 CD1 LEU A 140 14002 7859 6701 -520 -314 64 C ATOM 789 CD2 LEU A 140 -18.894 -8.428 23.927 1.00 77.59 C ANISOU 789 CD2 LEU A 140 14393 8119 6969 -430 -477 199 C ATOM 790 N CYS A 141 -23.167 -10.095 26.558 1.00 72.58 N ANISOU 790 N CYS A 141 14039 7537 6001 -673 -98 165 N ATOM 791 CA CYS A 141 -23.448 -10.627 27.901 1.00 73.24 C ANISOU 791 CA CYS A 141 14284 7576 5967 -700 -38 231 C ATOM 792 C CYS A 141 -24.465 -11.753 27.841 1.00 75.22 C ANISOU 792 C CYS A 141 14559 7823 6199 -862 122 233 C ATOM 793 O CYS A 141 -24.357 -12.703 28.618 1.00 76.28 O ANISOU 793 O CYS A 141 14875 7840 6267 -910 171 309 O ATOM 794 CB CYS A 141 -23.919 -9.523 28.842 1.00 74.63 C ANISOU 794 CB CYS A 141 14487 7850 6021 -638 -41 216 C ATOM 795 SG CYS A 141 -22.660 -8.277 29.206 1.00 78.43 S ANISOU 795 SG CYS A 141 15026 8292 6483 -498 -252 228 S ATOM 796 N VAL A 142 -25.461 -11.653 26.936 1.00 68.97 N ANISOU 796 N VAL A 142 13596 7156 5454 -958 193 155 N ATOM 797 CA VAL A 142 -26.482 -12.695 26.771 1.00 68.56 C ANISOU 797 CA VAL A 142 13538 7121 5390 -1163 330 152 C ATOM 798 C VAL A 142 -25.800 -13.943 26.163 1.00 67.48 C ANISOU 798 C VAL A 142 13549 6776 5313 -1225 312 178 C ATOM 799 O VAL A 142 -26.039 -15.053 26.635 1.00 67.13 O ANISOU 799 O VAL A 142 13678 6615 5214 -1356 398 233 O ATOM 800 CB VAL A 142 -27.707 -12.188 25.964 1.00 72.55 C ANISOU 800 CB VAL A 142 13792 7845 5928 -1243 378 62 C ATOM 801 CG1 VAL A 142 -28.635 -13.332 25.570 1.00 74.21 C ANISOU 801 CG1 VAL A 142 13977 8071 6147 -1500 482 55 C ATOM 802 CG2 VAL A 142 -28.480 -11.142 26.765 1.00 72.52 C ANISOU 802 CG2 VAL A 142 13682 8037 5837 -1157 434 50 C ATOM 803 N ILE A 143 -24.880 -13.736 25.206 1.00 61.15 N ANISOU 803 N ILE A 143 12714 5915 4607 -1111 209 148 N ATOM 804 CA ILE A 143 -24.092 -14.804 24.580 1.00 61.11 C ANISOU 804 CA ILE A 143 12855 5713 4650 -1101 196 169 C ATOM 805 C ILE A 143 -23.141 -15.421 25.633 1.00 66.25 C ANISOU 805 C ILE A 143 13724 6196 5251 -992 169 278 C ATOM 806 O ILE A 143 -22.914 -16.632 25.617 1.00 67.53 O ANISOU 806 O ILE A 143 14094 6171 5393 -1025 211 319 O ATOM 807 CB ILE A 143 -23.340 -14.265 23.316 1.00 62.16 C ANISOU 807 CB ILE A 143 12870 5863 4886 -982 113 112 C ATOM 808 CG1 ILE A 143 -24.293 -14.184 22.113 1.00 61.92 C ANISOU 808 CG1 ILE A 143 12719 5926 4883 -1115 143 11 C ATOM 809 CG2 ILE A 143 -22.078 -15.083 22.952 1.00 62.01 C ANISOU 809 CG2 ILE A 143 12993 5657 4911 -854 87 157 C ATOM 810 CD1 ILE A 143 -24.040 -13.017 21.124 1.00 67.23 C ANISOU 810 CD1 ILE A 143 13216 6715 5614 -1013 65 -53 C ATOM 811 N ALA A 144 -22.609 -14.594 26.540 1.00 62.94 N ANISOU 811 N ALA A 144 13281 5835 4799 -861 88 323 N ATOM 812 CA ALA A 144 -21.695 -15.034 27.593 1.00 64.75 C ANISOU 812 CA ALA A 144 13696 5936 4969 -743 25 429 C ATOM 813 C ALA A 144 -22.429 -15.669 28.804 1.00 70.81 C ANISOU 813 C ALA A 144 14670 6641 5591 -854 123 493 C ATOM 814 O ALA A 144 -21.830 -16.517 29.468 1.00 70.75 O ANISOU 814 O ALA A 144 14893 6466 5523 -791 101 585 O ATOM 815 CB ALA A 144 -20.819 -13.885 28.045 1.00 64.87 C ANISOU 815 CB ALA A 144 13615 6039 4995 -589 -125 448 C ATOM 816 N LEU A 145 -23.712 -15.294 29.074 1.00 69.10 N ANISOU 816 N LEU A 145 14375 6564 5314 -1010 240 451 N ATOM 817 CA LEU A 145 -24.519 -15.919 30.142 1.00 71.59 C ANISOU 817 CA LEU A 145 14867 6845 5487 -1150 375 514 C ATOM 818 C LEU A 145 -24.925 -17.293 29.690 1.00 79.01 C ANISOU 818 C LEU A 145 15955 7633 6430 -1336 478 530 C ATOM 819 O LEU A 145 -24.860 -18.236 30.467 1.00 81.24 O ANISOU 819 O LEU A 145 16516 7745 6607 -1389 532 621 O ATOM 820 CB LEU A 145 -25.770 -15.102 30.516 1.00 71.98 C ANISOU 820 CB LEU A 145 14751 7123 5474 -1245 490 467 C ATOM 821 CG LEU A 145 -25.575 -13.973 31.528 1.00 76.48 C ANISOU 821 CG LEU A 145 15329 7783 5945 -1088 438 479 C ATOM 822 CD1 LEU A 145 -26.549 -12.828 31.283 1.00 76.52 C ANISOU 822 CD1 LEU A 145 15090 8032 5954 -1082 500 390 C ATOM 823 CD2 LEU A 145 -25.622 -14.479 32.952 1.00 78.30 C ANISOU 823 CD2 LEU A 145 15832 7919 5997 -1107 508 581 C ATOM 824 N ASP A 146 -25.307 -17.407 28.406 1.00 76.32 N ANISOU 824 N ASP A 146 15464 7336 6198 -1435 491 442 N ATOM 825 CA ASP A 146 -25.685 -18.647 27.743 1.00 78.00 C ANISOU 825 CA ASP A 146 15823 7396 6418 -1630 564 433 C ATOM 826 C ASP A 146 -24.502 -19.625 27.756 1.00 82.66 C ANISOU 826 C ASP A 146 16714 7695 6997 -1483 503 501 C ATOM 827 O ASP A 146 -24.702 -20.796 28.062 1.00 84.70 O ANISOU 827 O ASP A 146 17264 7747 7170 -1613 580 558 O ATOM 828 CB ASP A 146 -26.165 -18.347 26.314 1.00 79.33 C ANISOU 828 CB ASP A 146 15761 7684 6697 -1716 545 315 C ATOM 829 CG ASP A 146 -25.991 -19.484 25.334 1.00 93.35 C ANISOU 829 CG ASP A 146 17723 9247 8497 -1813 548 287 C ATOM 830 OD1 ASP A 146 -25.113 -19.370 24.448 1.00 94.89 O ANISOU 830 OD1 ASP A 146 17906 9376 8770 -1635 463 247 O ATOM 831 OD2 ASP A 146 -26.716 -20.495 25.464 1.00 96.38 O ANISOU 831 OD2 ASP A 146 18286 9523 8812 -2070 643 307 O ATOM 832 N ARG A 147 -23.276 -19.138 27.476 1.00 77.76 N ANISOU 832 N ARG A 147 16028 7064 6454 -1207 370 503 N ATOM 833 CA ARG A 147 -22.068 -19.962 27.509 1.00 78.96 C ANISOU 833 CA ARG A 147 16412 6987 6604 -1004 305 573 C ATOM 834 C ARG A 147 -21.778 -20.420 28.948 1.00 86.58 C ANISOU 834 C ARG A 147 17635 7828 7435 -942 295 699 C ATOM 835 O ARG A 147 -21.481 -21.598 29.171 1.00 87.01 O ANISOU 835 O ARG A 147 18012 7632 7415 -916 321 769 O ATOM 836 CB ARG A 147 -20.855 -19.194 26.939 1.00 77.62 C ANISOU 836 CB ARG A 147 16037 6902 6554 -738 171 555 C ATOM 837 CG ARG A 147 -20.088 -19.931 25.835 1.00 90.80 C ANISOU 837 CG ARG A 147 17784 8422 8293 -605 169 533 C ATOM 838 CD ARG A 147 -19.531 -21.284 26.269 1.00104.58 C ANISOU 838 CD ARG A 147 19892 9886 9957 -491 185 624 C ATOM 839 NE ARG A 147 -19.569 -22.278 25.189 1.00122.45 N ANISOU 839 NE ARG A 147 22346 11953 12225 -512 263 571 N ATOM 840 CZ ARG A 147 -20.644 -22.979 24.834 1.00143.88 C ANISOU 840 CZ ARG A 147 25243 14549 14875 -794 367 520 C ATOM 841 NH1 ARG A 147 -21.804 -22.791 25.451 1.00134.89 N ANISOU 841 NH1 ARG A 147 24073 13501 13677 -1079 423 519 N ATOM 842 NH2 ARG A 147 -20.572 -23.865 23.849 1.00135.52 N ANISOU 842 NH2 ARG A 147 24397 13289 13804 -798 417 467 N ATOM 843 N TYR A 148 -21.873 -19.469 29.914 1.00 84.69 N ANISOU 843 N TYR A 148 17284 7751 7144 -910 253 726 N ATOM 844 CA TYR A 148 -21.646 -19.669 31.346 1.00 86.42 C ANISOU 844 CA TYR A 148 17733 7891 7213 -849 229 839 C ATOM 845 C TYR A 148 -22.579 -20.746 31.877 1.00 96.54 C ANISOU 845 C TYR A 148 19307 9017 8355 -1082 396 893 C ATOM 846 O TYR A 148 -22.091 -21.676 32.509 1.00 98.52 O ANISOU 846 O TYR A 148 19892 9039 8501 -1008 380 997 O ATOM 847 CB TYR A 148 -21.810 -18.343 32.127 1.00 85.45 C ANISOU 847 CB TYR A 148 17436 7984 7046 -815 176 826 C ATOM 848 CG TYR A 148 -21.928 -18.494 33.627 1.00 87.48 C ANISOU 848 CG TYR A 148 17948 8181 7110 -814 193 927 C ATOM 849 CD1 TYR A 148 -20.799 -18.666 34.422 1.00 89.77 C ANISOU 849 CD1 TYR A 148 18420 8358 7329 -601 27 1025 C ATOM 850 CD2 TYR A 148 -23.167 -18.433 34.258 1.00 88.97 C ANISOU 850 CD2 TYR A 148 18184 8446 7176 -1020 372 926 C ATOM 851 CE1 TYR A 148 -20.903 -18.810 35.804 1.00 90.95 C ANISOU 851 CE1 TYR A 148 18838 8442 7276 -596 31 1119 C ATOM 852 CE2 TYR A 148 -23.286 -18.596 35.637 1.00 91.45 C ANISOU 852 CE2 TYR A 148 18761 8697 7288 -1020 409 1022 C ATOM 853 CZ TYR A 148 -22.149 -18.767 36.410 1.00 99.53 C ANISOU 853 CZ TYR A 148 20005 9584 8230 -807 231 1116 C ATOM 854 OH TYR A 148 -22.267 -18.902 37.778 1.00103.76 O ANISOU 854 OH TYR A 148 20830 10052 8543 -803 257 1211 O ATOM 855 N TRP A 149 -23.899 -20.655 31.588 1.00 95.94 N ANISOU 855 N TRP A 149 19109 9066 8278 -1365 553 830 N ATOM 856 CA TRP A 149 -24.887 -21.637 32.061 1.00 99.68 C ANISOU 856 CA TRP A 149 19824 9426 8623 -1651 730 883 C ATOM 857 C TRP A 149 -24.675 -23.034 31.426 1.00105.86 C ANISOU 857 C TRP A 149 20911 9908 9403 -1730 752 903 C ATOM 858 O TRP A 149 -24.937 -24.044 32.073 1.00107.49 O ANISOU 858 O TRP A 149 21474 9900 9466 -1870 844 994 O ATOM 859 CB TRP A 149 -26.321 -21.143 31.818 1.00 98.92 C ANISOU 859 CB TRP A 149 19450 9588 8547 -1931 880 808 C ATOM 860 CG TRP A 149 -26.712 -19.926 32.610 1.00 99.39 C ANISOU 860 CG TRP A 149 19297 9908 8558 -1862 907 800 C ATOM 861 CD1 TRP A 149 -26.466 -19.690 33.931 1.00103.23 C ANISOU 861 CD1 TRP A 149 19957 10373 8892 -1755 913 887 C ATOM 862 CD2 TRP A 149 -27.504 -18.821 32.147 1.00 98.12 C ANISOU 862 CD2 TRP A 149 18750 10055 8477 -1897 941 698 C ATOM 863 NE1 TRP A 149 -26.995 -18.476 34.303 1.00101.92 N ANISOU 863 NE1 TRP A 149 19549 10470 8705 -1707 950 838 N ATOM 864 CE2 TRP A 149 -27.651 -17.928 33.230 1.00102.26 C ANISOU 864 CE2 TRP A 149 19244 10719 8891 -1784 972 725 C ATOM 865 CE3 TRP A 149 -28.072 -18.478 30.905 1.00 98.70 C ANISOU 865 CE3 TRP A 149 18519 10291 8691 -1989 936 586 C ATOM 866 CZ2 TRP A 149 -28.368 -16.727 33.119 1.00100.78 C ANISOU 866 CZ2 TRP A 149 18742 10819 8730 -1746 1013 643 C ATOM 867 CZ3 TRP A 149 -28.764 -17.280 30.792 1.00 99.01 C ANISOU 867 CZ3 TRP A 149 18230 10626 8763 -1948 960 513 C ATOM 868 CH2 TRP A 149 -28.904 -16.418 31.888 1.00100.06 C ANISOU 868 CH2 TRP A 149 18348 10884 8786 -1818 1003 541 C ATOM 869 N ALA A 150 -24.173 -23.078 30.184 1.00101.80 N ANISOU 869 N ALA A 150 20292 9361 9026 -1631 672 821 N ATOM 870 CA ALA A 150 -23.877 -24.316 29.473 1.00102.94 C ANISOU 870 CA ALA A 150 20741 9209 9163 -1654 683 821 C ATOM 871 C ALA A 150 -22.650 -25.019 30.063 1.00109.50 C ANISOU 871 C ALA A 150 21913 9773 9918 -1350 597 934 C ATOM 872 O ALA A 150 -22.675 -26.229 30.226 1.00111.76 O ANISOU 872 O ALA A 150 22615 9757 10091 -1418 654 995 O ATOM 873 CB ALA A 150 -23.652 -24.024 28.002 1.00101.66 C ANISOU 873 CB ALA A 150 20358 9115 9154 -1595 628 698 C ATOM 874 N ILE A 151 -21.580 -24.270 30.371 1.00105.99 N ANISOU 874 N ILE A 151 21302 9439 9530 -1019 451 962 N ATOM 875 CA ILE A 151 -20.343 -24.828 30.923 1.00107.71 C ANISOU 875 CA ILE A 151 21772 9462 9692 -690 336 1072 C ATOM 876 C ILE A 151 -20.496 -25.075 32.434 1.00113.81 C ANISOU 876 C ILE A 151 22816 10150 10277 -717 343 1201 C ATOM 877 O ILE A 151 -19.768 -25.903 32.986 1.00115.34 O ANISOU 877 O ILE A 151 23352 10104 10366 -516 281 1310 O ATOM 878 CB ILE A 151 -19.118 -23.916 30.580 1.00109.39 C ANISOU 878 CB ILE A 151 21653 9860 10049 -355 164 1053 C ATOM 879 CG1 ILE A 151 -17.775 -24.671 30.701 1.00111.67 C ANISOU 879 CG1 ILE A 151 22149 9959 10322 15 51 1147 C ATOM 880 CG2 ILE A 151 -19.110 -22.590 31.360 1.00109.20 C ANISOU 880 CG2 ILE A 151 21345 10111 10034 -343 74 1058 C ATOM 881 CD1 ILE A 151 -16.603 -24.076 29.874 1.00118.10 C ANISOU 881 CD1 ILE A 151 22626 10935 11310 308 -67 1111 C ATOM 882 N THR A 152 -21.449 -24.378 33.090 1.00110.94 N ANISOU 882 N THR A 152 22317 9978 9857 -947 425 1190 N ATOM 883 CA THR A 152 -21.657 -24.485 34.536 1.00112.70 C ANISOU 883 CA THR A 152 22786 10149 9884 -981 452 1305 C ATOM 884 C THR A 152 -22.783 -25.494 34.895 1.00119.47 C ANISOU 884 C THR A 152 23979 10828 10588 -1331 665 1356 C ATOM 885 O THR A 152 -22.735 -26.059 35.986 1.00120.97 O ANISOU 885 O THR A 152 24534 10845 10586 -1327 692 1481 O ATOM 886 CB THR A 152 -21.872 -23.072 35.150 1.00117.82 C ANISOU 886 CB THR A 152 23123 11109 10536 -967 412 1273 C ATOM 887 OG1 THR A 152 -21.150 -22.961 36.372 1.00123.64 O ANISOU 887 OG1 THR A 152 24057 11791 11129 -763 285 1383 O ATOM 888 CG2 THR A 152 -23.347 -22.677 35.345 1.00113.91 C ANISOU 888 CG2 THR A 152 22496 10792 9992 -1300 620 1225 C ATOM 889 N ASP A 153 -23.780 -25.712 34.004 1.00116.72 N ANISOU 889 N ASP A 153 23512 10524 10312 -1645 807 1266 N ATOM 890 CA ASP A 153 -24.907 -26.608 34.287 1.00119.55 C ANISOU 890 CA ASP A 153 24135 10751 10537 -2038 1010 1310 C ATOM 891 C ASP A 153 -25.441 -27.294 33.015 1.00124.45 C ANISOU 891 C ASP A 153 24766 11272 11246 -2289 1072 1220 C ATOM 892 O ASP A 153 -26.656 -27.339 32.808 1.00125.12 O ANISOU 892 O ASP A 153 24724 11485 11330 -2675 1220 1179 O ATOM 893 CB ASP A 153 -26.038 -25.818 34.982 1.00121.52 C ANISOU 893 CB ASP A 153 24135 11303 10734 -2278 1161 1306 C ATOM 894 CG ASP A 153 -26.541 -26.451 36.263 1.00139.40 C ANISOU 894 CG ASP A 153 26771 13433 12762 -2461 1316 1445 C ATOM 895 OD1 ASP A 153 -26.645 -25.728 37.278 1.00141.03 O ANISOU 895 OD1 ASP A 153 26913 13803 12868 -2383 1345 1489 O ATOM 896 OD2 ASP A 153 -26.827 -27.676 36.254 1.00148.25 O ANISOU 896 OD2 ASP A 153 28281 14268 13780 -2687 1412 1511 O ATOM 897 N ALA A 154 -24.535 -27.883 32.203 1.00120.94 N ANISOU 897 N ALA A 154 24496 10596 10862 -2071 962 1194 N ATOM 898 CA ALA A 154 -24.821 -28.569 30.933 1.00121.31 C ANISOU 898 CA ALA A 154 24623 10497 10972 -2242 989 1101 C ATOM 899 C ALA A 154 -26.053 -29.495 30.989 1.00129.35 C ANISOU 899 C ALA A 154 25903 11373 11872 -2744 1158 1120 C ATOM 900 O ALA A 154 -26.867 -29.479 30.063 1.00128.79 O ANISOU 900 O ALA A 154 25644 11411 11880 -3040 1200 1014 O ATOM 901 CB ALA A 154 -23.603 -29.367 30.495 1.00122.74 C ANISOU 901 CB ALA A 154 25144 10351 11143 -1898 884 1123 C ATOM 902 N VAL A 155 -26.192 -30.275 32.079 1.00129.69 N ANISOU 902 N VAL A 155 26373 11184 11719 -2853 1246 1260 N ATOM 903 CA VAL A 155 -27.279 -31.238 32.287 1.00133.06 C ANISOU 903 CA VAL A 155 27110 11441 12005 -3351 1417 1308 C ATOM 904 C VAL A 155 -28.649 -30.542 32.485 1.00136.06 C ANISOU 904 C VAL A 155 27052 12220 12423 -3754 1565 1275 C ATOM 905 O VAL A 155 -29.573 -30.815 31.713 1.00137.46 O ANISOU 905 O VAL A 155 27116 12464 12649 -4145 1628 1200 O ATOM 906 CB VAL A 155 -26.982 -32.235 33.441 1.00140.49 C ANISOU 906 CB VAL A 155 28664 12010 12707 -3335 1474 1481 C ATOM 907 CG1 VAL A 155 -26.189 -33.432 32.932 1.00142.33 C ANISOU 907 CG1 VAL A 155 29453 11761 12866 -3167 1396 1500 C ATOM 908 CG2 VAL A 155 -26.263 -31.560 34.615 1.00139.28 C ANISOU 908 CG2 VAL A 155 28458 11967 12496 -2964 1409 1579 C ATOM 909 N GLU A 156 -28.773 -29.648 33.488 1.00129.56 N ANISOU 909 N GLU A 156 25985 11669 11573 -3648 1613 1329 N ATOM 910 CA GLU A 156 -30.026 -28.962 33.815 1.00128.52 C ANISOU 910 CA GLU A 156 25448 11927 11456 -3959 1776 1312 C ATOM 911 C GLU A 156 -30.397 -27.866 32.800 1.00126.32 C ANISOU 911 C GLU A 156 24564 12036 11395 -3927 1708 1155 C ATOM 912 O GLU A 156 -31.574 -27.766 32.445 1.00127.03 O ANISOU 912 O GLU A 156 24368 12369 11529 -4293 1820 1107 O ATOM 913 CB GLU A 156 -29.965 -28.360 35.232 1.00130.05 C ANISOU 913 CB GLU A 156 25639 12253 11520 -3804 1853 1417 C ATOM 914 CG GLU A 156 -29.802 -29.401 36.332 1.00147.78 C ANISOU 914 CG GLU A 156 28480 14151 13519 -3887 1948 1586 C ATOM 915 CD GLU A 156 -29.937 -28.907 37.762 1.00178.51 C ANISOU 915 CD GLU A 156 32415 18169 17241 -3811 2058 1694 C ATOM 916 OE1 GLU A 156 -29.217 -27.953 38.139 1.00176.75 O ANISOU 916 OE1 GLU A 156 32025 18084 17048 -3419 1925 1675 O ATOM 917 OE2 GLU A 156 -30.725 -29.515 38.524 1.00176.25 O ANISOU 917 OE2 GLU A 156 32371 17822 16773 -4151 2276 1804 O ATOM 918 N TYR A 157 -29.406 -27.053 32.346 1.00116.62 N ANISOU 918 N TYR A 157 23141 10873 10295 -3498 1524 1082 N ATOM 919 CA TYR A 157 -29.580 -25.913 31.430 1.00112.07 C ANISOU 919 CA TYR A 157 22037 10635 9909 -3398 1440 943 C ATOM 920 C TYR A 157 -30.132 -26.300 30.058 1.00115.70 C ANISOU 920 C TYR A 157 22385 11102 10474 -3654 1413 830 C ATOM 921 O TYR A 157 -30.843 -25.488 29.464 1.00114.20 O ANISOU 921 O TYR A 157 21748 11247 10397 -3741 1410 735 O ATOM 922 CB TYR A 157 -28.258 -25.134 31.246 1.00108.78 C ANISOU 922 CB TYR A 157 21530 10216 9584 -2911 1248 909 C ATOM 923 CG TYR A 157 -28.352 -23.875 30.408 1.00105.32 C ANISOU 923 CG TYR A 157 20596 10104 9318 -2785 1162 781 C ATOM 924 CD1 TYR A 157 -27.475 -23.651 29.355 1.00104.86 C ANISOU 924 CD1 TYR A 157 20462 9990 9389 -2549 1006 701 C ATOM 925 CD2 TYR A 157 -29.316 -22.905 30.674 1.00105.25 C ANISOU 925 CD2 TYR A 157 20208 10453 9329 -2887 1246 745 C ATOM 926 CE1 TYR A 157 -27.551 -22.492 28.583 1.00103.28 C ANISOU 926 CE1 TYR A 157 19847 10066 9328 -2441 930 592 C ATOM 927 CE2 TYR A 157 -29.407 -21.745 29.908 1.00103.71 C ANISOU 927 CE2 TYR A 157 19600 10530 9273 -2752 1161 633 C ATOM 928 CZ TYR A 157 -28.518 -21.537 28.865 1.00108.72 C ANISOU 928 CZ TYR A 157 20192 11087 10029 -2540 998 559 C ATOM 929 OH TYR A 157 -28.616 -20.394 28.099 1.00103.90 O ANISOU 929 OH TYR A 157 19211 10727 9541 -2420 918 456 O ATOM 930 N SER A 158 -29.811 -27.511 29.558 1.00113.51 N ANISOU 930 N SER A 158 22529 10454 10145 -3760 1386 839 N ATOM 931 CA SER A 158 -30.251 -28.021 28.253 1.00114.00 C ANISOU 931 CA SER A 158 22588 10454 10271 -4010 1344 732 C ATOM 932 C SER A 158 -31.772 -27.852 28.028 1.00118.98 C ANISOU 932 C SER A 158 22876 11401 10929 -4481 1444 689 C ATOM 933 O SER A 158 -32.172 -27.343 26.975 1.00117.67 O ANISOU 933 O SER A 158 22368 11453 10887 -4537 1362 567 O ATOM 934 CB SER A 158 -29.856 -29.490 28.085 1.00120.61 C ANISOU 934 CB SER A 158 24040 10803 10983 -4115 1346 776 C ATOM 935 OG SER A 158 -30.299 -30.319 29.148 1.00131.93 O ANISOU 935 OG SER A 158 25831 12053 12243 -4384 1490 910 O ATOM 936 N ALA A 159 -32.599 -28.237 29.031 1.00117.63 N ANISOU 936 N ALA A 159 22778 11276 10640 -4801 1622 795 N ATOM 937 CA ALA A 159 -34.067 -28.168 29.008 1.00119.27 C ANISOU 937 CA ALA A 159 22651 11808 10859 -5269 1749 785 C ATOM 938 C ALA A 159 -34.594 -26.727 29.039 1.00119.96 C ANISOU 938 C ALA A 159 22104 12408 11067 -5114 1760 727 C ATOM 939 O ALA A 159 -35.664 -26.457 28.491 1.00120.42 O ANISOU 939 O ALA A 159 21765 12789 11199 -5392 1781 665 O ATOM 940 CB ALA A 159 -34.640 -28.944 30.184 1.00123.61 C ANISOU 940 CB ALA A 159 23477 12255 11233 -5602 1960 935 C ATOM 941 N LYS A 160 -33.844 -25.817 29.686 1.00113.35 N ANISOU 941 N LYS A 160 21191 11640 10238 -4670 1735 750 N ATOM 942 CA LYS A 160 -34.175 -24.398 29.857 1.00110.62 C ANISOU 942 CA LYS A 160 20341 11715 9973 -4448 1744 702 C ATOM 943 C LYS A 160 -33.799 -23.565 28.623 1.00110.94 C ANISOU 943 C LYS A 160 20091 11880 10180 -4201 1546 562 C ATOM 944 O LYS A 160 -34.544 -22.648 28.269 1.00109.98 O ANISOU 944 O LYS A 160 19512 12131 10142 -4198 1546 492 O ATOM 945 CB LYS A 160 -33.470 -23.830 31.103 1.00111.45 C ANISOU 945 CB LYS A 160 20572 11788 9986 -4102 1784 786 C ATOM 946 CG LYS A 160 -33.856 -24.505 32.423 1.00123.33 C ANISOU 946 CG LYS A 160 22362 13198 11300 -4310 1994 932 C ATOM 947 N ARG A 161 -32.649 -23.890 27.973 1.00105.32 N ANISOU 947 N ARG A 161 19653 10858 9504 -3982 1388 526 N ATOM 948 CA ARG A 161 -32.073 -23.228 26.786 1.00101.71 C ANISOU 948 CA ARG A 161 19015 10447 9183 -3731 1209 406 C ATOM 949 C ARG A 161 -32.953 -23.442 25.537 1.00108.40 C ANISOU 949 C ARG A 161 19666 11420 10100 -4031 1157 301 C ATOM 950 O ARG A 161 -32.550 -24.114 24.580 1.00108.70 O ANISOU 950 O ARG A 161 19931 11219 10152 -4077 1060 244 O ATOM 951 CB ARG A 161 -30.640 -23.743 26.538 1.00 96.96 C ANISOU 951 CB ARG A 161 18797 9468 8575 -3453 1099 420 C ATOM 952 CG ARG A 161 -29.756 -22.778 25.780 1.00 97.43 C ANISOU 952 CG ARG A 161 18661 9602 8754 -3084 948 339 C ATOM 953 CD ARG A 161 -29.014 -23.449 24.651 1.00103.25 C ANISOU 953 CD ARG A 161 19631 10075 9525 -3013 852 279 C ATOM 954 NE ARG A 161 -27.791 -24.132 25.083 1.00108.52 N ANISOU 954 NE ARG A 161 20687 10410 10136 -2769 832 358 N ATOM 955 CZ ARG A 161 -26.556 -23.733 24.783 1.00120.85 C ANISOU 955 CZ ARG A 161 22243 11913 11762 -2393 733 350 C ATOM 956 NH1 ARG A 161 -26.359 -22.625 24.080 1.00105.84 N ANISOU 956 NH1 ARG A 161 19999 10241 9976 -2234 652 269 N ATOM 957 NH2 ARG A 161 -25.510 -24.438 25.186 1.00107.94 N ANISOU 957 NH2 ARG A 161 20944 9996 10072 -2172 714 429 N ATOM 958 N THR A 162 -34.155 -22.854 25.553 1.00106.69 N ANISOU 958 N THR A 162 19028 11591 9918 -4217 1217 276 N ATOM 959 CA THR A 162 -35.130 -22.953 24.468 1.00108.17 C ANISOU 959 CA THR A 162 18958 11972 10168 -4515 1153 184 C ATOM 960 C THR A 162 -35.029 -21.709 23.570 1.00111.10 C ANISOU 960 C THR A 162 18967 12591 10656 -4223 1006 75 C ATOM 961 O THR A 162 -34.582 -20.662 24.056 1.00109.10 O ANISOU 961 O THR A 162 18572 12455 10428 -3869 1009 86 O ATOM 962 CB THR A 162 -36.554 -23.141 25.046 1.00117.13 C ANISOU 962 CB THR A 162 19828 13410 11266 -4913 1311 236 C ATOM 963 OG1 THR A 162 -36.887 -22.057 25.912 1.00112.92 O ANISOU 963 OG1 THR A 162 18961 13204 10739 -4694 1420 273 O ATOM 964 CG2 THR A 162 -36.716 -24.458 25.790 1.00120.71 C ANISOU 964 CG2 THR A 162 20679 13594 11592 -5273 1455 345 C ATOM 965 N PRO A 163 -35.435 -21.765 22.273 1.00108.33 N ANISOU 965 N PRO A 163 18486 12314 10361 -4364 869 -30 N ATOM 966 CA PRO A 163 -35.382 -20.547 21.442 1.00105.74 C ANISOU 966 CA PRO A 163 17833 12220 10124 -4083 733 -124 C ATOM 967 C PRO A 163 -36.349 -19.467 21.949 1.00109.74 C ANISOU 967 C PRO A 163 17859 13174 10663 -4018 797 -114 C ATOM 968 O PRO A 163 -36.085 -18.287 21.737 1.00107.20 O ANISOU 968 O PRO A 163 17341 13002 10390 -3678 727 -156 O ATOM 969 CB PRO A 163 -35.772 -21.047 20.041 1.00108.82 C ANISOU 969 CB PRO A 163 18233 12582 10531 -4322 583 -226 C ATOM 970 CG PRO A 163 -35.631 -22.542 20.095 1.00115.61 C ANISOU 970 CG PRO A 163 19535 13084 11306 -4645 626 -194 C ATOM 971 CD PRO A 163 -35.983 -22.901 21.504 1.00112.83 C ANISOU 971 CD PRO A 163 19220 12753 10897 -4792 820 -70 C ATOM 972 N LYS A 164 -37.445 -19.872 22.648 1.00109.36 N ANISOU 972 N LYS A 164 17642 13333 10577 -4336 943 -52 N ATOM 973 CA LYS A 164 -38.447 -18.986 23.262 1.00109.97 C ANISOU 973 CA LYS A 164 17266 13851 10667 -4284 1053 -28 C ATOM 974 C LYS A 164 -37.822 -18.147 24.379 1.00111.08 C ANISOU 974 C LYS A 164 17465 13975 10766 -3898 1159 29 C ATOM 975 O LYS A 164 -38.211 -16.993 24.543 1.00110.07 O ANISOU 975 O LYS A 164 17019 14143 10657 -3645 1173 5 O ATOM 976 CB LYS A 164 -39.638 -19.787 23.808 1.00116.69 C ANISOU 976 CB LYS A 164 17968 14893 11474 -4745 1216 42 C ATOM 977 N ARG A 165 -36.841 -18.717 25.125 1.00106.40 N ANISOU 977 N ARG A 165 17299 13025 10103 -3842 1217 101 N ATOM 978 CA ARG A 165 -36.097 -18.040 26.200 1.00104.17 C ANISOU 978 CA ARG A 165 17146 12670 9762 -3499 1283 157 C ATOM 979 C ARG A 165 -35.218 -16.919 25.611 1.00103.63 C ANISOU 979 C ARG A 165 17037 12575 9763 -3092 1110 81 C ATOM 980 O ARG A 165 -35.230 -15.802 26.130 1.00101.70 O ANISOU 980 O ARG A 165 16644 12498 9499 -2816 1134 77 O ATOM 981 CB ARG A 165 -35.241 -19.045 27.000 1.00104.95 C ANISOU 981 CB ARG A 165 17724 12384 9769 -3557 1345 253 C ATOM 982 CG ARG A 165 -34.491 -18.412 28.165 1.00118.18 C ANISOU 982 CG ARG A 165 19549 13989 11367 -3234 1392 316 C ATOM 983 CD ARG A 165 -33.607 -19.385 28.921 1.00137.49 C ANISOU 983 CD ARG A 165 22466 16060 13715 -3255 1421 415 C ATOM 984 NE ARG A 165 -32.952 -18.725 30.056 1.00150.30 N ANISOU 984 NE ARG A 165 24211 17647 15250 -2958 1443 474 N ATOM 985 CZ ARG A 165 -32.346 -19.357 31.058 1.00164.72 C ANISOU 985 CZ ARG A 165 26411 19223 16953 -2938 1491 579 C ATOM 986 NH1 ARG A 165 -32.309 -20.684 31.090 1.00151.77 N ANISOU 986 NH1 ARG A 165 25079 17327 15259 -3188 1539 644 N ATOM 987 NH2 ARG A 165 -31.782 -18.667 32.041 1.00150.52 N ANISOU 987 NH2 ARG A 165 24708 17417 15068 -2670 1482 622 N ATOM 988 N ALA A 166 -34.480 -17.227 24.518 1.00 98.51 N ANISOU 988 N ALA A 166 16539 11712 9180 -3067 947 21 N ATOM 989 CA ALA A 166 -33.609 -16.295 23.795 1.00 95.22 C ANISOU 989 CA ALA A 166 16102 11250 8828 -2738 787 -47 C ATOM 990 C ALA A 166 -34.404 -15.097 23.262 1.00 98.57 C ANISOU 990 C ALA A 166 16136 12019 9296 -2612 733 -121 C ATOM 991 O ALA A 166 -33.924 -13.965 23.369 1.00 97.08 O ANISOU 991 O ALA A 166 15900 11872 9114 -2298 679 -139 O ATOM 992 CB ALA A 166 -32.905 -17.010 22.650 1.00 95.17 C ANISOU 992 CB ALA A 166 16308 10986 8867 -2794 663 -96 C ATOM 993 N ALA A 167 -35.638 -15.340 22.750 1.00 95.72 N ANISOU 993 N ALA A 167 15502 11910 8956 -2860 744 -156 N ATOM 994 CA ALA A 167 -36.548 -14.311 22.232 1.00 95.41 C ANISOU 994 CA ALA A 167 15066 12232 8953 -2748 689 -219 C ATOM 995 C ALA A 167 -36.819 -13.229 23.277 1.00 98.53 C ANISOU 995 C ALA A 167 15307 12830 9299 -2476 802 -185 C ATOM 996 O ALA A 167 -36.826 -12.050 22.934 1.00 96.56 O ANISOU 996 O ALA A 167 14914 12712 9062 -2183 719 -236 O ATOM 997 CB ALA A 167 -37.861 -14.944 21.794 1.00 99.33 C ANISOU 997 CB ALA A 167 15288 12984 9469 -3106 703 -235 C ATOM 998 N VAL A 168 -37.005 -13.638 24.552 1.00 96.28 N ANISOU 998 N VAL A 168 15100 12543 8938 -2566 994 -98 N ATOM 999 CA VAL A 168 -37.268 -12.752 25.690 1.00 96.34 C ANISOU 999 CA VAL A 168 15025 12716 8865 -2327 1135 -60 C ATOM 1000 C VAL A 168 -35.988 -11.987 26.048 1.00 97.72 C ANISOU 1000 C VAL A 168 15484 12640 9006 -1992 1051 -62 C ATOM 1001 O VAL A 168 -36.057 -10.789 26.325 1.00 97.25 O ANISOU 1001 O VAL A 168 15339 12704 8906 -1694 1047 -90 O ATOM 1002 CB VAL A 168 -37.842 -13.500 26.935 1.00102.49 C ANISOU 1002 CB VAL A 168 15838 13555 9551 -2550 1378 40 C ATOM 1003 CG1 VAL A 168 -38.434 -12.517 27.943 1.00103.34 C ANISOU 1003 CG1 VAL A 168 15776 13923 9564 -2305 1543 61 C ATOM 1004 CG2 VAL A 168 -38.891 -14.533 26.542 1.00105.28 C ANISOU 1004 CG2 VAL A 168 15984 14077 9942 -2983 1444 56 C ATOM 1005 N MET A 169 -34.831 -12.680 26.047 1.00 92.09 N ANISOU 1005 N MET A 169 15110 11578 8302 -2043 982 -32 N ATOM 1006 CA MET A 169 -33.530 -12.096 26.379 1.00 89.14 C ANISOU 1006 CA MET A 169 14991 10971 7906 -1775 887 -22 C ATOM 1007 C MET A 169 -33.131 -11.031 25.367 1.00 91.13 C ANISOU 1007 C MET A 169 15150 11249 8227 -1548 714 -105 C ATOM 1008 O MET A 169 -32.573 -10.008 25.762 1.00 89.01 O ANISOU 1008 O MET A 169 14957 10944 7917 -1292 665 -111 O ATOM 1009 CB MET A 169 -32.455 -13.179 26.462 1.00 90.72 C ANISOU 1009 CB MET A 169 15521 10834 8116 -1882 846 32 C ATOM 1010 CG MET A 169 -32.735 -14.214 27.523 1.00 96.41 C ANISOU 1010 CG MET A 169 16410 11478 8743 -2089 1009 127 C ATOM 1011 SD MET A 169 -31.224 -14.884 28.230 1.00 99.63 S ANISOU 1011 SD MET A 169 17255 11499 9100 -2001 952 213 S ATOM 1012 CE MET A 169 -31.350 -14.223 29.918 1.00 97.31 C ANISOU 1012 CE MET A 169 17048 11283 8643 -1852 1072 285 C ATOM 1013 N ILE A 170 -33.449 -11.255 24.068 1.00 87.85 N ANISOU 1013 N ILE A 170 14590 10889 7898 -1656 621 -169 N ATOM 1014 CA ILE A 170 -33.182 -10.313 22.972 1.00 85.84 C ANISOU 1014 CA ILE A 170 14253 10665 7696 -1469 462 -246 C ATOM 1015 C ILE A 170 -34.128 -9.113 23.109 1.00 90.34 C ANISOU 1015 C ILE A 170 14572 11528 8226 -1273 483 -282 C ATOM 1016 O ILE A 170 -33.675 -7.970 23.013 1.00 89.65 O ANISOU 1016 O ILE A 170 14536 11410 8115 -1009 402 -310 O ATOM 1017 CB ILE A 170 -33.292 -10.997 21.575 1.00 88.93 C ANISOU 1017 CB ILE A 170 14603 11023 8164 -1651 361 -301 C ATOM 1018 CG1 ILE A 170 -32.301 -12.178 21.406 1.00 88.72 C ANISOU 1018 CG1 ILE A 170 14867 10681 8161 -1796 350 -270 C ATOM 1019 CG2 ILE A 170 -33.159 -9.991 20.432 1.00 88.40 C ANISOU 1019 CG2 ILE A 170 14449 11012 8127 -1462 208 -375 C ATOM 1020 CD1 ILE A 170 -30.860 -11.953 21.945 1.00 96.77 C ANISOU 1020 CD1 ILE A 170 16137 11456 9175 -1600 325 -221 C ATOM 1021 N ALA A 171 -35.431 -9.378 23.355 1.00 87.95 N ANISOU 1021 N ALA A 171 14003 11505 7907 -1400 597 -277 N ATOM 1022 CA ALA A 171 -36.452 -8.348 23.551 1.00 88.69 C ANISOU 1022 CA ALA A 171 13823 11916 7956 -1194 646 -303 C ATOM 1023 C ALA A 171 -36.119 -7.477 24.765 1.00 90.24 C ANISOU 1023 C ALA A 171 14175 12067 8044 -927 738 -273 C ATOM 1024 O ALA A 171 -36.222 -6.260 24.662 1.00 89.74 O ANISOU 1024 O ALA A 171 14079 12081 7937 -630 686 -316 O ATOM 1025 CB ALA A 171 -37.822 -8.984 23.716 1.00 92.72 C ANISOU 1025 CB ALA A 171 14008 12747 8476 -1422 777 -284 C ATOM 1026 N LEU A 172 -35.667 -8.095 25.881 1.00 85.27 N ANISOU 1026 N LEU A 172 13760 11283 7356 -1027 858 -202 N ATOM 1027 CA LEU A 172 -35.253 -7.419 27.116 1.00 84.36 C ANISOU 1027 CA LEU A 172 13855 11084 7113 -813 935 -169 C ATOM 1028 C LEU A 172 -34.072 -6.483 26.851 1.00 84.57 C ANISOU 1028 C LEU A 172 14119 10879 7136 -587 753 -203 C ATOM 1029 O LEU A 172 -34.079 -5.350 27.345 1.00 84.09 O ANISOU 1029 O LEU A 172 14134 10842 6976 -323 754 -226 O ATOM 1030 CB LEU A 172 -34.882 -8.459 28.184 1.00 84.96 C ANISOU 1030 CB LEU A 172 14148 11002 7130 -1008 1058 -80 C ATOM 1031 CG LEU A 172 -35.886 -8.722 29.324 1.00 93.10 C ANISOU 1031 CG LEU A 172 15087 12239 8047 -1071 1311 -23 C ATOM 1032 CD1 LEU A 172 -37.339 -8.793 28.843 1.00 96.15 C ANISOU 1032 CD1 LEU A 172 15045 13006 8481 -1169 1419 -47 C ATOM 1033 CD2 LEU A 172 -35.545 -10.005 30.051 1.00 96.36 C ANISOU 1033 CD2 LEU A 172 15722 12469 8421 -1341 1408 69 C ATOM 1034 N VAL A 173 -33.091 -6.945 26.024 1.00 78.16 N ANISOU 1034 N VAL A 173 13424 9850 6425 -694 602 -208 N ATOM 1035 CA VAL A 173 -31.902 -6.191 25.603 1.00 75.52 C ANISOU 1035 CA VAL A 173 13278 9307 6110 -542 430 -230 C ATOM 1036 C VAL A 173 -32.343 -4.986 24.748 1.00 81.79 C ANISOU 1036 C VAL A 173 13943 10229 6904 -338 341 -305 C ATOM 1037 O VAL A 173 -31.861 -3.873 24.978 1.00 82.67 O ANISOU 1037 O VAL A 173 14209 10254 6947 -129 270 -322 O ATOM 1038 CB VAL A 173 -30.869 -7.093 24.876 1.00 76.92 C ANISOU 1038 CB VAL A 173 13563 9268 6395 -706 331 -211 C ATOM 1039 CG1 VAL A 173 -29.980 -6.301 23.925 1.00 74.60 C ANISOU 1039 CG1 VAL A 173 13332 8860 6152 -583 166 -250 C ATOM 1040 CG2 VAL A 173 -30.016 -7.855 25.877 1.00 76.38 C ANISOU 1040 CG2 VAL A 173 13724 9003 6294 -782 365 -131 C ATOM 1041 N TRP A 174 -33.283 -5.188 23.807 1.00 78.11 N ANISOU 1041 N TRP A 174 13215 9963 6499 -400 336 -346 N ATOM 1042 CA TRP A 174 -33.777 -4.087 22.993 1.00 78.05 C ANISOU 1042 CA TRP A 174 13091 10087 6478 -187 244 -410 C ATOM 1043 C TRP A 174 -34.571 -3.088 23.818 1.00 83.98 C ANISOU 1043 C TRP A 174 13789 11011 7108 77 338 -422 C ATOM 1044 O TRP A 174 -34.430 -1.890 23.592 1.00 83.25 O ANISOU 1044 O TRP A 174 13801 10878 6953 331 252 -460 O ATOM 1045 CB TRP A 174 -34.605 -4.596 21.824 1.00 77.79 C ANISOU 1045 CB TRP A 174 12790 10241 6527 -320 195 -448 C ATOM 1046 CG TRP A 174 -33.739 -4.960 20.665 1.00 77.10 C ANISOU 1046 CG TRP A 174 12818 9956 6518 -435 53 -468 C ATOM 1047 CD1 TRP A 174 -33.355 -6.213 20.292 1.00 79.60 C ANISOU 1047 CD1 TRP A 174 13179 10156 6909 -703 54 -453 C ATOM 1048 CD2 TRP A 174 -33.019 -4.051 19.823 1.00 75.66 C ANISOU 1048 CD2 TRP A 174 12779 9637 6330 -276 -91 -500 C ATOM 1049 NE1 TRP A 174 -32.495 -6.146 19.220 1.00 77.77 N ANISOU 1049 NE1 TRP A 174 13081 9749 6719 -701 -73 -479 N ATOM 1050 CE2 TRP A 174 -32.281 -4.828 18.902 1.00 78.47 C ANISOU 1050 CE2 TRP A 174 13220 9832 6763 -455 -160 -504 C ATOM 1051 CE3 TRP A 174 -32.966 -2.648 19.720 1.00 76.79 C ANISOU 1051 CE3 TRP A 174 13004 9774 6397 1 -162 -525 C ATOM 1052 CZ2 TRP A 174 -31.521 -4.251 17.874 1.00 76.23 C ANISOU 1052 CZ2 TRP A 174 13068 9410 6486 -375 -282 -528 C ATOM 1053 CZ3 TRP A 174 -32.199 -2.080 18.711 1.00 76.98 C ANISOU 1053 CZ3 TRP A 174 13180 9640 6429 57 -296 -545 C ATOM 1054 CH2 TRP A 174 -31.473 -2.879 17.816 1.00 76.15 C ANISOU 1054 CH2 TRP A 174 13129 9401 6406 -134 -347 -544 C ATOM 1055 N VAL A 175 -35.363 -3.577 24.798 1.00 83.28 N ANISOU 1055 N VAL A 175 13572 11097 6972 19 525 -386 N ATOM 1056 CA VAL A 175 -36.174 -2.766 25.713 1.00 85.30 C ANISOU 1056 CA VAL A 175 13773 11539 7097 275 665 -391 C ATOM 1057 C VAL A 175 -35.242 -1.911 26.568 1.00 87.75 C ANISOU 1057 C VAL A 175 14465 11594 7283 467 636 -388 C ATOM 1058 O VAL A 175 -35.454 -0.701 26.647 1.00 87.28 O ANISOU 1058 O VAL A 175 14489 11553 7121 771 612 -431 O ATOM 1059 CB VAL A 175 -37.139 -3.645 26.560 1.00 91.81 C ANISOU 1059 CB VAL A 175 14381 12603 7901 114 896 -340 C ATOM 1060 CG1 VAL A 175 -37.541 -2.974 27.876 1.00 93.39 C ANISOU 1060 CG1 VAL A 175 14668 12886 7930 357 1080 -325 C ATOM 1061 CG2 VAL A 175 -38.378 -4.013 25.749 1.00 93.87 C ANISOU 1061 CG2 VAL A 175 14203 13213 8249 17 918 -359 C ATOM 1062 N PHE A 176 -34.193 -2.525 27.160 1.00 83.21 N ANISOU 1062 N PHE A 176 14135 10770 6710 294 620 -338 N ATOM 1063 CA PHE A 176 -33.229 -1.798 27.983 1.00 82.13 C ANISOU 1063 CA PHE A 176 14359 10390 6456 427 560 -330 C ATOM 1064 C PHE A 176 -32.439 -0.763 27.172 1.00 83.41 C ANISOU 1064 C PHE A 176 14682 10377 6633 556 353 -376 C ATOM 1065 O PHE A 176 -32.132 0.306 27.699 1.00 83.47 O ANISOU 1065 O PHE A 176 14939 10267 6507 754 308 -399 O ATOM 1066 CB PHE A 176 -32.254 -2.743 28.703 1.00 83.11 C ANISOU 1066 CB PHE A 176 14678 10309 6590 212 556 -259 C ATOM 1067 CG PHE A 176 -31.226 -1.984 29.512 1.00 84.84 C ANISOU 1067 CG PHE A 176 15253 10294 6689 326 455 -251 C ATOM 1068 CD1 PHE A 176 -29.919 -1.850 29.055 1.00 86.88 C ANISOU 1068 CD1 PHE A 176 15665 10328 7020 258 255 -242 C ATOM 1069 CD2 PHE A 176 -31.590 -1.310 30.677 1.00 89.13 C ANISOU 1069 CD2 PHE A 176 15973 10855 7037 511 554 -258 C ATOM 1070 CE1 PHE A 176 -28.985 -1.094 29.773 1.00 88.00 C ANISOU 1070 CE1 PHE A 176 16113 10272 7050 334 137 -235 C ATOM 1071 CE2 PHE A 176 -30.652 -0.562 31.399 1.00 91.73 C ANISOU 1071 CE2 PHE A 176 16657 10958 7239 598 433 -260 C ATOM 1072 CZ PHE A 176 -29.354 -0.470 30.951 1.00 88.27 C ANISOU 1072 CZ PHE A 176 16348 10305 6884 492 214 -246 C ATOM 1073 N SER A 177 -32.087 -1.087 25.920 1.00 77.34 N ANISOU 1073 N SER A 177 13804 9575 6009 430 231 -388 N ATOM 1074 CA SER A 177 -31.303 -0.202 25.062 1.00 75.16 C ANISOU 1074 CA SER A 177 13675 9133 5750 510 51 -419 C ATOM 1075 C SER A 177 -32.108 1.025 24.623 1.00 80.46 C ANISOU 1075 C SER A 177 14324 9913 6336 791 26 -480 C ATOM 1076 O SER A 177 -31.612 2.147 24.754 1.00 79.74 O ANISOU 1076 O SER A 177 14499 9656 6143 951 -63 -500 O ATOM 1077 CB SER A 177 -30.786 -0.965 23.854 1.00 75.92 C ANISOU 1077 CB SER A 177 13662 9179 6004 307 -37 -412 C ATOM 1078 OG SER A 177 -30.003 -2.069 24.273 1.00 79.92 O ANISOU 1078 OG SER A 177 14221 9568 6577 92 -15 -354 O ATOM 1079 N ILE A 178 -33.356 0.824 24.149 1.00 79.47 N ANISOU 1079 N ILE A 178 13892 10064 6239 854 99 -506 N ATOM 1080 CA ILE A 178 -34.222 1.932 23.727 1.00 81.62 C ANISOU 1080 CA ILE A 178 14111 10473 6427 1164 74 -558 C ATOM 1081 C ILE A 178 -34.482 2.854 24.932 1.00 88.13 C ANISOU 1081 C ILE A 178 15143 11276 7068 1438 171 -571 C ATOM 1082 O ILE A 178 -34.459 4.070 24.768 1.00 89.01 O ANISOU 1082 O ILE A 178 15467 11289 7066 1701 93 -610 O ATOM 1083 CB ILE A 178 -35.538 1.496 22.993 1.00 86.64 C ANISOU 1083 CB ILE A 178 14331 11456 7135 1177 116 -578 C ATOM 1084 CG1 ILE A 178 -36.475 0.596 23.858 1.00 89.90 C ANISOU 1084 CG1 ILE A 178 14462 12137 7559 1074 324 -546 C ATOM 1085 CG2 ILE A 178 -35.220 0.814 21.662 1.00 84.87 C ANISOU 1085 CG2 ILE A 178 13993 11203 7053 944 -19 -582 C ATOM 1086 CD1 ILE A 178 -37.552 1.309 24.836 1.00101.58 C ANISOU 1086 CD1 ILE A 178 15852 13853 8893 1396 503 -556 C ATOM 1087 N SER A 179 -34.626 2.275 26.141 1.00 85.65 N ANISOU 1087 N SER A 179 14826 11011 6705 1367 335 -536 N ATOM 1088 CA SER A 179 -34.877 2.996 27.384 1.00 87.79 C ANISOU 1088 CA SER A 179 15314 11261 6782 1607 453 -547 C ATOM 1089 C SER A 179 -33.662 3.828 27.847 1.00 93.26 C ANISOU 1089 C SER A 179 16480 11594 7360 1645 316 -556 C ATOM 1090 O SER A 179 -33.772 4.526 28.862 1.00 96.14 O ANISOU 1090 O SER A 179 17104 11891 7536 1848 387 -575 O ATOM 1091 CB SER A 179 -35.296 2.029 28.489 1.00 91.61 C ANISOU 1091 CB SER A 179 15680 11887 7243 1473 667 -497 C ATOM 1092 OG SER A 179 -34.184 1.377 29.081 1.00 97.08 O ANISOU 1092 OG SER A 179 16596 12340 7950 1223 622 -447 O ATOM 1093 N ILE A 180 -32.515 3.752 27.136 1.00 87.14 N ANISOU 1093 N ILE A 180 15822 10598 6690 1444 127 -541 N ATOM 1094 CA ILE A 180 -31.333 4.530 27.512 1.00 86.03 C ANISOU 1094 CA ILE A 180 16090 10141 6455 1431 -21 -542 C ATOM 1095 C ILE A 180 -31.321 5.838 26.719 1.00 92.04 C ANISOU 1095 C ILE A 180 17038 10789 7146 1636 -150 -593 C ATOM 1096 O ILE A 180 -31.155 6.890 27.312 1.00 93.14 O ANISOU 1096 O ILE A 180 17529 10757 7102 1813 -187 -625 O ATOM 1097 CB ILE A 180 -30.006 3.718 27.402 1.00 86.18 C ANISOU 1097 CB ILE A 180 16140 9995 6609 1099 -135 -483 C ATOM 1098 CG1 ILE A 180 -29.958 2.578 28.443 1.00 86.70 C ANISOU 1098 CG1 ILE A 180 16144 10114 6685 944 -17 -428 C ATOM 1099 CG2 ILE A 180 -28.750 4.592 27.524 1.00 85.55 C ANISOU 1099 CG2 ILE A 180 16419 9625 6462 1051 -323 -480 C ATOM 1100 CD1 ILE A 180 -30.420 2.923 29.913 1.00 95.21 C ANISOU 1100 CD1 ILE A 180 17427 11200 7548 1108 112 -435 C ATOM 1101 N SER A 181 -31.542 5.785 25.414 1.00 89.58 N ANISOU 1101 N SER A 181 16525 10559 6954 1621 -215 -602 N ATOM 1102 CA SER A 181 -31.538 6.976 24.579 1.00 90.78 C ANISOU 1102 CA SER A 181 16868 10592 7031 1809 -340 -640 C ATOM 1103 C SER A 181 -32.782 7.864 24.780 1.00 99.45 C ANISOU 1103 C SER A 181 17992 11826 7969 2220 -257 -694 C ATOM 1104 O SER A 181 -32.756 9.035 24.401 1.00100.07 O ANISOU 1104 O SER A 181 18354 11747 7923 2434 -354 -727 O ATOM 1105 CB SER A 181 -31.438 6.567 23.114 1.00 93.20 C ANISOU 1105 CB SER A 181 16955 10959 7500 1673 -429 -629 C ATOM 1106 OG SER A 181 -32.644 5.974 22.662 1.00103.51 O ANISOU 1106 OG SER A 181 17875 12579 8876 1754 -341 -644 O ATOM 1107 N LEU A 182 -33.867 7.307 25.334 1.00 99.49 N ANISOU 1107 N LEU A 182 17702 12126 7975 2333 -74 -697 N ATOM 1108 CA LEU A 182 -35.130 8.020 25.502 1.00103.52 C ANISOU 1108 CA LEU A 182 18145 12836 8352 2744 31 -740 C ATOM 1109 C LEU A 182 -35.088 9.117 26.594 1.00112.89 C ANISOU 1109 C LEU A 182 19776 13831 9286 3033 81 -778 C ATOM 1110 O LEU A 182 -35.481 10.232 26.245 1.00114.24 O ANISOU 1110 O LEU A 182 20146 13938 9323 3371 29 -821 O ATOM 1111 CB LEU A 182 -36.301 7.047 25.736 1.00104.94 C ANISOU 1111 CB LEU A 182 17827 13427 8619 2743 226 -722 C ATOM 1112 CG LEU A 182 -37.218 6.745 24.523 1.00110.29 C ANISOU 1112 CG LEU A 182 18069 14408 9426 2786 185 -728 C ATOM 1113 CD1 LEU A 182 -38.226 7.858 24.285 1.00113.59 C ANISOU 1113 CD1 LEU A 182 18478 14974 9709 3267 193 -771 C ATOM 1114 CD2 LEU A 182 -36.429 6.430 23.240 1.00109.78 C ANISOU 1114 CD2 LEU A 182 18008 14195 9509 2518 -20 -716 C ATOM 1115 N PRO A 183 -34.610 8.899 27.863 1.00111.97 N ANISOU 1115 N PRO A 183 19872 13594 9078 2929 163 -766 N ATOM 1116 CA PRO A 183 -34.581 10.010 28.840 1.00114.37 C ANISOU 1116 CA PRO A 183 20653 13689 9111 3214 193 -814 C ATOM 1117 C PRO A 183 -33.898 11.298 28.333 1.00120.24 C ANISOU 1117 C PRO A 183 21874 14078 9735 3313 -19 -851 C ATOM 1118 O PRO A 183 -34.534 12.334 28.519 1.00122.59 O ANISOU 1118 O PRO A 183 22416 14331 9830 3715 24 -906 O ATOM 1119 CB PRO A 183 -33.830 9.424 30.035 1.00115.32 C ANISOU 1119 CB PRO A 183 20943 13683 9189 2961 233 -783 C ATOM 1120 CG PRO A 183 -34.061 7.975 29.947 1.00118.66 C ANISOU 1120 CG PRO A 183 20892 14373 9822 2691 339 -722 C ATOM 1121 CD PRO A 183 -34.112 7.651 28.481 1.00112.59 C ANISOU 1121 CD PRO A 183 19802 13709 9269 2572 227 -709 C ATOM 1122 N PRO A 184 -32.713 11.313 27.640 1.00115.98 N ANISOU 1122 N PRO A 184 21469 13298 9300 2992 -230 -823 N ATOM 1123 CA PRO A 184 -32.150 12.595 27.172 1.00117.06 C ANISOU 1123 CA PRO A 184 22075 13101 9301 3078 -412 -852 C ATOM 1124 C PRO A 184 -32.953 13.237 26.034 1.00124.25 C ANISOU 1124 C PRO A 184 22915 14094 10199 3381 -442 -876 C ATOM 1125 O PRO A 184 -32.448 13.471 24.927 1.00122.72 O ANISOU 1125 O PRO A 184 22763 13781 10085 3246 -597 -855 O ATOM 1126 CB PRO A 184 -30.737 12.216 26.720 1.00116.06 C ANISOU 1126 CB PRO A 184 21989 12784 9326 2618 -589 -798 C ATOM 1127 CG PRO A 184 -30.844 10.812 26.328 1.00118.24 C ANISOU 1127 CG PRO A 184 21736 13339 9852 2393 -515 -749 C ATOM 1128 CD PRO A 184 -31.792 10.206 27.316 1.00114.75 C ANISOU 1128 CD PRO A 184 21081 13148 9371 2545 -303 -759 C ATOM 1129 N PHE A 185 -34.219 13.526 26.335 1.00124.87 N ANISOU 1129 N PHE A 185 22887 14391 10168 3807 -289 -916 N ATOM 1130 CA PHE A 185 -35.156 14.204 25.461 1.00127.26 C ANISOU 1130 CA PHE A 185 23128 14807 10417 4194 -306 -942 C ATOM 1131 C PHE A 185 -35.662 15.426 26.212 1.00135.96 C ANISOU 1131 C PHE A 185 24686 15754 11220 4667 -242 -1004 C ATOM 1132 O PHE A 185 -36.692 15.995 25.852 1.00137.98 O ANISOU 1132 O PHE A 185 24879 16162 11386 5116 -194 -1032 O ATOM 1133 CB PHE A 185 -36.276 13.261 24.984 1.00129.36 C ANISOU 1133 CB PHE A 185 22731 15557 10864 4264 -185 -922 C ATOM 1134 CG PHE A 185 -36.001 12.637 23.630 1.00128.81 C ANISOU 1134 CG PHE A 185 22359 15567 11015 3982 -327 -882 C ATOM 1135 CD1 PHE A 185 -34.986 11.698 23.467 1.00128.77 C ANISOU 1135 CD1 PHE A 185 22254 15483 11192 3490 -383 -838 C ATOM 1136 CD2 PHE A 185 -36.766 12.978 22.521 1.00132.33 C ANISOU 1136 CD2 PHE A 185 22633 16173 11475 4229 -404 -889 C ATOM 1137 CE1 PHE A 185 -34.732 11.124 22.216 1.00127.71 C ANISOU 1137 CE1 PHE A 185 21876 15411 11239 3252 -497 -808 C ATOM 1138 CE2 PHE A 185 -36.508 12.406 21.269 1.00133.23 C ANISOU 1138 CE2 PHE A 185 22510 16345 11766 3969 -537 -858 C ATOM 1139 CZ PHE A 185 -35.496 11.480 21.126 1.00128.13 C ANISOU 1139 CZ PHE A 185 21787 15607 11290 3483 -572 -820 C ATOM 1140 N PHE A 186 -34.868 15.876 27.225 1.00134.36 N ANISOU 1140 N PHE A 186 24983 15221 10847 4567 -263 -1028 N ATOM 1141 CA PHE A 186 -35.151 17.064 28.038 1.00138.40 C ANISOU 1141 CA PHE A 186 26053 15495 11036 4970 -218 -1096 C ATOM 1142 C PHE A 186 -34.883 18.364 27.236 1.00147.96 C ANISOU 1142 C PHE A 186 27776 16349 12092 5145 -410 -1121 C ATOM 1143 O PHE A 186 -35.034 19.455 27.796 1.00150.17 O ANISOU 1143 O PHE A 186 28614 16361 12084 5477 -403 -1181 O ATOM 1144 CB PHE A 186 -34.337 17.099 29.372 1.00139.34 C ANISOU 1144 CB PHE A 186 26580 15356 11008 4762 -209 -1116 C ATOM 1145 CG PHE A 186 -33.685 15.852 29.934 1.00136.85 C ANISOU 1145 CG PHE A 186 25966 15157 10873 4300 -181 -1063 C ATOM 1146 CD1 PHE A 186 -32.329 15.609 29.738 1.00136.19 C ANISOU 1146 CD1 PHE A 186 26005 14840 10900 3810 -386 -1020 C ATOM 1147 CD2 PHE A 186 -34.390 14.995 30.768 1.00138.49 C ANISOU 1147 CD2 PHE A 186 25829 15685 11107 4370 56 -1053 C ATOM 1148 CE1 PHE A 186 -31.709 14.489 30.307 1.00134.34 C ANISOU 1148 CE1 PHE A 186 25532 14699 10812 3430 -368 -969 C ATOM 1149 CE2 PHE A 186 -33.771 13.871 31.332 1.00138.53 C ANISOU 1149 CE2 PHE A 186 25628 15759 11249 3961 76 -1000 C ATOM 1150 CZ PHE A 186 -32.437 13.622 31.092 1.00133.63 C ANISOU 1150 CZ PHE A 186 25125 14906 10744 3512 -143 -959 C ATOM 1151 N TRP A 187 -34.497 18.245 25.934 1.00146.38 N ANISOU 1151 N TRP A 187 27421 16133 12065 4928 -572 -1073 N ATOM 1152 CA TRP A 187 -34.151 19.364 25.045 1.00149.07 C ANISOU 1152 CA TRP A 187 28229 16133 12279 5016 -760 -1076 C ATOM 1153 C TRP A 187 -35.341 20.327 24.789 1.00158.66 C ANISOU 1153 C TRP A 187 29614 17384 13286 5668 -711 -1122 C ATOM 1154 O TRP A 187 -35.926 20.357 23.700 1.00158.69 O ANISOU 1154 O TRP A 187 29367 17560 13366 5852 -762 -1099 O ATOM 1155 CB TRP A 187 -33.526 18.877 23.712 1.00145.55 C ANISOU 1155 CB TRP A 187 27523 15713 12068 4635 -909 -1008 C ATOM 1156 CG TRP A 187 -34.319 17.851 22.952 1.00145.85 C ANISOU 1156 CG TRP A 187 26860 16211 12344 4662 -839 -977 C ATOM 1157 CD1 TRP A 187 -34.374 16.514 23.205 1.00146.64 C ANISOU 1157 CD1 TRP A 187 26407 16634 12674 4394 -732 -950 C ATOM 1158 CD2 TRP A 187 -35.047 18.058 21.730 1.00146.87 C ANISOU 1158 CD2 TRP A 187 26808 16494 12504 4912 -903 -965 C ATOM 1159 NE1 TRP A 187 -35.155 15.884 22.263 1.00145.94 N ANISOU 1159 NE1 TRP A 187 25802 16897 12750 4463 -719 -930 N ATOM 1160 CE2 TRP A 187 -35.573 16.806 21.339 1.00149.18 C ANISOU 1160 CE2 TRP A 187 26414 17222 13045 4779 -831 -938 C ATOM 1161 CE3 TRP A 187 -35.326 19.186 20.937 1.00150.66 C ANISOU 1161 CE3 TRP A 187 27663 16775 12807 5243 -1025 -973 C ATOM 1162 CZ2 TRP A 187 -36.374 16.650 20.200 1.00149.09 C ANISOU 1162 CZ2 TRP A 187 26062 17472 13113 4957 -889 -924 C ATOM 1163 CZ3 TRP A 187 -36.122 19.029 19.809 1.00152.78 C ANISOU 1163 CZ3 TRP A 187 27590 17306 13153 5448 -1078 -953 C ATOM 1164 CH2 TRP A 187 -36.635 17.774 19.450 1.00151.73 C ANISOU 1164 CH2 TRP A 187 26755 17624 13271 5298 -1017 -931 C ATOM 1165 N ARG A 188 -35.651 21.166 25.797 1.00159.52 N ANISOU 1165 N ARG A 188 30199 17301 13109 6031 -626 -1189 N ATOM 1166 CA ARG A 188 -36.691 22.191 25.701 1.00164.03 C ANISOU 1166 CA ARG A 188 31035 17851 13440 6699 -574 -1238 C ATOM 1167 C ARG A 188 -36.048 23.422 25.053 1.00170.57 C ANISOU 1167 C ARG A 188 32580 18157 14071 6712 -795 -1242 C ATOM 1168 O ARG A 188 -35.955 24.489 25.668 1.00173.59 O ANISOU 1168 O ARG A 188 33655 18155 14146 6962 -810 -1301 O ATOM 1169 CB ARG A 188 -37.286 22.490 27.088 1.00167.29 C ANISOU 1169 CB ARG A 188 31658 18285 13620 7085 -360 -1309 C ATOM 1170 N GLN A 189 -35.562 23.241 23.805 1.00165.60 N ANISOU 1170 N GLN A 189 31805 17501 13613 6409 -963 -1177 N ATOM 1171 CA GLN A 189 -34.852 24.259 23.034 1.00166.49 C ANISOU 1171 CA GLN A 189 32537 17143 13579 6311 -1173 -1156 C ATOM 1172 C GLN A 189 -35.258 24.260 21.543 1.00170.44 C ANISOU 1172 C GLN A 189 32791 17786 14182 6428 -1275 -1101 C ATOM 1173 O GLN A 189 -35.538 25.331 20.992 1.00172.51 O ANISOU 1173 O GLN A 189 33536 17787 14224 6783 -1372 -1105 O ATOM 1174 CB GLN A 189 -33.337 24.042 23.174 1.00164.95 C ANISOU 1174 CB GLN A 189 32544 16659 13471 5613 -1297 -1120 C ATOM 1175 N ALA A 190 -35.276 23.074 20.894 1.00163.95 N ANISOU 1175 N ALA A 190 31267 17354 13674 6133 -1263 -1049 N ATOM 1176 CA ALA A 190 -35.624 22.946 19.477 1.00192.16 C ANISOU 1176 CA ALA A 190 34579 21085 17350 6193 -1370 -998 C ATOM 1177 C ALA A 190 -36.964 22.236 19.276 1.00212.54 C ANISOU 1177 C ALA A 190 35379 24605 20770 5766 -1107 -937 C ATOM 1178 O ALA A 190 -37.836 22.275 20.142 1.00182.95 O ANISOU 1178 O ALA A 190 32578 20693 16242 6948 -1110 -1054 O ATOM 1179 CB ALA A 190 -34.527 22.199 18.741 1.00188.93 C ANISOU 1179 CB ALA A 190 33971 20644 17171 5550 -1461 -932 C ATOM 1180 N SER A 197 -26.268 22.619 12.778 1.00103.17 N ANISOU 1180 N SER A 197 24275 8257 6668 2164 -2036 -384 N ATOM 1181 CA SER A 197 -24.843 22.947 12.801 1.00103.69 C ANISOU 1181 CA SER A 197 24596 8064 6737 1622 -2061 -312 C ATOM 1182 C SER A 197 -24.020 21.862 13.521 1.00106.86 C ANISOU 1182 C SER A 197 24502 8696 7404 1231 -1992 -305 C ATOM 1183 O SER A 197 -23.037 21.362 12.969 1.00105.58 O ANISOU 1183 O SER A 197 24124 8598 7395 816 -1956 -230 O ATOM 1184 CB SER A 197 -24.620 24.298 13.475 1.00110.52 C ANISOU 1184 CB SER A 197 26183 8485 7326 1645 -2158 -325 C ATOM 1185 N GLU A 198 -24.414 21.523 14.759 1.00103.47 N ANISOU 1185 N GLU A 198 23914 8387 7013 1381 -1970 -379 N ATOM 1186 CA GLU A 198 -23.758 20.520 15.595 1.00100.90 C ANISOU 1186 CA GLU A 198 23162 8268 6908 1080 -1919 -378 C ATOM 1187 C GLU A 198 -24.771 19.516 16.107 1.00102.45 C ANISOU 1187 C GLU A 198 22869 8823 7234 1387 -1824 -447 C ATOM 1188 O GLU A 198 -25.890 19.891 16.471 1.00103.01 O ANISOU 1188 O GLU A 198 23055 8913 7170 1830 -1813 -515 O ATOM 1189 CB GLU A 198 -23.034 21.184 16.779 1.00103.66 C ANISOU 1189 CB GLU A 198 23896 8352 7140 867 -2003 -389 C ATOM 1190 N CYS A 199 -24.377 18.241 16.138 1.00 96.35 N ANISOU 1190 N CYS A 199 21556 8336 6718 1156 -1748 -424 N ATOM 1191 CA CYS A 199 -25.223 17.166 16.637 1.00 95.13 C ANISOU 1191 CA CYS A 199 20922 8520 6703 1360 -1651 -476 C ATOM 1192 C CYS A 199 -24.450 16.374 17.705 1.00 97.16 C ANISOU 1192 C CYS A 199 20946 8864 7105 1072 -1621 -465 C ATOM 1193 O CYS A 199 -23.518 15.643 17.369 1.00 94.82 O ANISOU 1193 O CYS A 199 20387 8651 6989 731 -1606 -405 O ATOM 1194 CB CYS A 199 -25.689 16.280 15.488 1.00 94.30 C ANISOU 1194 CB CYS A 199 20395 8685 6751 1408 -1591 -462 C ATOM 1195 SG CYS A 199 -26.971 15.078 15.929 1.00 97.42 S ANISOU 1195 SG CYS A 199 20239 9492 7283 1680 -1481 -527 S ATOM 1196 N VAL A 200 -24.789 16.596 18.994 1.00 94.15 N ANISOU 1196 N VAL A 200 20708 8444 6622 1222 -1619 -519 N ATOM 1197 CA VAL A 200 -24.172 15.931 20.151 1.00 93.25 C ANISOU 1197 CA VAL A 200 20437 8395 6599 1003 -1609 -514 C ATOM 1198 C VAL A 200 -25.244 15.537 21.181 1.00 97.52 C ANISOU 1198 C VAL A 200 20845 9109 7098 1324 -1508 -584 C ATOM 1199 O VAL A 200 -26.296 16.179 21.254 1.00 98.48 O ANISOU 1199 O VAL A 200 21152 9210 7056 1712 -1475 -642 O ATOM 1200 CB VAL A 200 -23.035 16.748 20.829 1.00 98.76 C ANISOU 1200 CB VAL A 200 21557 8789 7179 709 -1745 -490 C ATOM 1201 CG1 VAL A 200 -21.737 16.665 20.040 1.00 97.90 C ANISOU 1201 CG1 VAL A 200 21374 8625 7198 274 -1809 -398 C ATOM 1202 CG2 VAL A 200 -23.439 18.198 21.067 1.00101.82 C ANISOU 1202 CG2 VAL A 200 22565 8852 7270 932 -1823 -540 C ATOM 1203 N VAL A 201 -24.967 14.478 21.976 1.00 93.37 N ANISOU 1203 N VAL A 201 20002 8760 6713 1171 -1452 -571 N ATOM 1204 CA VAL A 201 -25.859 13.992 23.047 1.00 93.44 C ANISOU 1204 CA VAL A 201 19874 8941 6686 1409 -1336 -622 C ATOM 1205 C VAL A 201 -25.841 15.011 24.211 1.00 99.52 C ANISOU 1205 C VAL A 201 21152 9462 7199 1533 -1390 -671 C ATOM 1206 O VAL A 201 -24.803 15.617 24.503 1.00 99.40 O ANISOU 1206 O VAL A 201 21476 9187 7106 1278 -1533 -650 O ATOM 1207 CB VAL A 201 -25.523 12.548 23.537 1.00 94.41 C ANISOU 1207 CB VAL A 201 19561 9294 7016 1194 -1263 -584 C ATOM 1208 CG1 VAL A 201 -26.665 11.950 24.354 1.00 94.24 C ANISOU 1208 CG1 VAL A 201 19336 9499 6972 1452 -1105 -627 C ATOM 1209 CG2 VAL A 201 -25.162 11.628 22.375 1.00 91.81 C ANISOU 1209 CG2 VAL A 201 18840 9122 6923 992 -1245 -530 C ATOM 1210 N ASN A 202 -27.013 15.216 24.834 1.00 98.25 N ANISOU 1210 N ASN A 202 21046 9386 6897 1927 -1274 -737 N ATOM 1211 CA ASN A 202 -27.224 16.127 25.962 1.00101.04 C ANISOU 1211 CA ASN A 202 21888 9527 6977 2132 -1284 -800 C ATOM 1212 C ASN A 202 -26.396 15.673 27.193 1.00105.27 C ANISOU 1212 C ASN A 202 22485 10008 7505 1858 -1326 -785 C ATOM 1213 O ASN A 202 -26.517 14.534 27.660 1.00102.07 O ANISOU 1213 O ASN A 202 21692 9850 7240 1788 -1223 -761 O ATOM 1214 CB ASN A 202 -28.720 16.200 26.280 1.00101.85 C ANISOU 1214 CB ASN A 202 21902 9825 6971 2631 -1103 -862 C ATOM 1215 CG ASN A 202 -29.068 17.050 27.459 1.00118.66 C ANISOU 1215 CG ASN A 202 24514 11765 8805 2906 -1069 -933 C ATOM 1216 OD1 ASN A 202 -29.182 16.569 28.588 1.00116.91 O ANISOU 1216 OD1 ASN A 202 24250 11631 8539 2914 -972 -949 O ATOM 1217 ND2 ASN A 202 -29.287 18.322 27.211 1.00109.84 N ANISOU 1217 ND2 ASN A 202 23890 10378 7464 3159 -1137 -978 N ATOM 1218 N THR A 203 -25.530 16.567 27.675 1.00105.43 N ANISOU 1218 N THR A 203 23010 9695 7354 1684 -1494 -795 N ATOM 1219 CA THR A 203 -24.636 16.309 28.808 1.00106.44 C ANISOU 1219 CA THR A 203 23265 9734 7442 1405 -1592 -780 C ATOM 1220 C THR A 203 -25.080 17.106 30.086 1.00112.57 C ANISOU 1220 C THR A 203 24573 10309 7890 1661 -1580 -866 C ATOM 1221 O THR A 203 -24.451 16.962 31.140 1.00113.02 O ANISOU 1221 O THR A 203 24799 10280 7865 1471 -1667 -865 O ATOM 1222 CB THR A 203 -23.165 16.594 28.388 1.00122.27 C ANISOU 1222 CB THR A 203 25383 11548 9524 931 -1817 -714 C ATOM 1223 OG1 THR A 203 -22.297 16.558 29.528 1.00128.48 O ANISOU 1223 OG1 THR A 203 26366 12221 10229 676 -1958 -706 O ATOM 1224 CG2 THR A 203 -22.989 17.918 27.640 1.00125.09 C ANISOU 1224 CG2 THR A 203 26197 11598 9732 926 -1931 -729 C ATOM 1225 N ASP A 204 -26.190 17.880 29.984 1.00109.97 N ANISOU 1225 N ASP A 204 24487 9926 7372 2114 -1465 -938 N ATOM 1226 CA ASP A 204 -26.790 18.743 31.010 1.00112.59 C ANISOU 1226 CA ASP A 204 25350 10062 7367 2458 -1414 -1030 C ATOM 1227 C ASP A 204 -26.890 18.112 32.386 1.00116.71 C ANISOU 1227 C ASP A 204 25846 10690 7809 2474 -1322 -1049 C ATOM 1228 O ASP A 204 -26.496 18.752 33.363 1.00119.61 O ANISOU 1228 O ASP A 204 26747 10781 7917 2442 -1422 -1098 O ATOM 1229 CB ASP A 204 -28.200 19.184 30.585 1.00116.09 C ANISOU 1229 CB ASP A 204 25777 10616 7714 3014 -1226 -1085 C ATOM 1230 CG ASP A 204 -28.270 20.236 29.488 1.00128.83 C ANISOU 1230 CG ASP A 204 27688 12006 9257 3139 -1327 -1093 C ATOM 1231 OD1 ASP A 204 -27.201 20.750 29.079 1.00129.61 O ANISOU 1231 OD1 ASP A 204 28077 11818 9350 2775 -1538 -1061 O ATOM 1232 OD2 ASP A 204 -29.391 20.531 29.023 1.00135.51 O ANISOU 1232 OD2 ASP A 204 28462 12975 10051 3596 -1196 -1125 O ATOM 1233 N HIS A 205 -27.444 16.882 32.476 1.00109.73 N ANISOU 1233 N HIS A 205 24382 10190 7122 2523 -1132 -1011 N ATOM 1234 CA HIS A 205 -27.639 16.175 33.741 1.00108.25 C ANISOU 1234 CA HIS A 205 24137 10132 6862 2550 -1010 -1016 C ATOM 1235 C HIS A 205 -26.583 15.083 33.930 1.00105.54 C ANISOU 1235 C HIS A 205 23485 9880 6735 2088 -1125 -929 C ATOM 1236 O HIS A 205 -26.712 13.975 33.409 1.00102.13 O ANISOU 1236 O HIS A 205 22497 9736 6573 1983 -1033 -865 O ATOM 1237 CB HIS A 205 -29.066 15.607 33.836 1.00109.70 C ANISOU 1237 CB HIS A 205 23939 10669 7073 2940 -699 -1031 C ATOM 1238 CG HIS A 205 -30.125 16.667 33.832 1.00116.74 C ANISOU 1238 CG HIS A 205 25134 11497 7725 3453 -573 -1115 C ATOM 1239 ND1 HIS A 205 -30.470 17.354 34.992 1.00122.26 N ANISOU 1239 ND1 HIS A 205 26344 12026 8085 3737 -491 -1192 N ATOM 1240 CD2 HIS A 205 -30.866 17.146 32.804 1.00119.58 C ANISOU 1240 CD2 HIS A 205 25375 11934 8127 3741 -526 -1132 C ATOM 1241 CE1 HIS A 205 -31.415 18.211 34.635 1.00124.35 C ANISOU 1241 CE1 HIS A 205 26767 12276 8203 4206 -383 -1253 C ATOM 1242 NE2 HIS A 205 -31.689 18.122 33.329 1.00123.11 N ANISOU 1242 NE2 HIS A 205 26236 12270 8269 4228 -409 -1216 N ATOM 1243 N ILE A 206 -25.544 15.420 34.714 1.00101.15 N ANISOU 1243 N ILE A 206 23322 9070 6041 1824 -1337 -929 N ATOM 1244 CA ILE A 206 -24.381 14.604 35.084 1.00 98.04 C ANISOU 1244 CA ILE A 206 22755 8706 5790 1402 -1503 -851 C ATOM 1245 C ILE A 206 -24.782 13.185 35.508 1.00 98.34 C ANISOU 1245 C ILE A 206 22324 9063 5977 1420 -1316 -796 C ATOM 1246 O ILE A 206 -24.155 12.235 35.053 1.00 95.42 O ANISOU 1246 O ILE A 206 21542 8842 5870 1151 -1371 -713 O ATOM 1247 CB ILE A 206 -23.577 15.342 36.210 1.00103.27 C ANISOU 1247 CB ILE A 206 24016 9052 6171 1245 -1728 -888 C ATOM 1248 CG1 ILE A 206 -22.031 15.194 36.122 1.00102.99 C ANISOU 1248 CG1 ILE A 206 23942 8924 6266 740 -2038 -812 C ATOM 1249 CG2 ILE A 206 -24.160 15.230 37.628 1.00104.27 C ANISOU 1249 CG2 ILE A 206 24422 9169 6025 1478 -1600 -940 C ATOM 1250 CD1 ILE A 206 -21.409 13.834 35.975 1.00105.64 C ANISOU 1250 CD1 ILE A 206 23714 9527 6899 489 -2055 -705 C ATOM 1251 N LEU A 207 -25.830 13.051 36.356 1.00 95.38 N ANISOU 1251 N LEU A 207 22026 8788 5425 1741 -1085 -841 N ATOM 1252 CA LEU A 207 -26.324 11.779 36.881 1.00 93.84 C ANISOU 1252 CA LEU A 207 21460 8874 5320 1766 -880 -791 C ATOM 1253 C LEU A 207 -26.796 10.850 35.754 1.00 96.81 C ANISOU 1253 C LEU A 207 21214 9550 6020 1741 -742 -736 C ATOM 1254 O LEU A 207 -26.574 9.645 35.858 1.00 93.97 O ANISOU 1254 O LEU A 207 20513 9359 5832 1554 -700 -661 O ATOM 1255 CB LEU A 207 -27.438 12.014 37.926 1.00 96.14 C ANISOU 1255 CB LEU A 207 21987 9212 5330 2139 -630 -854 C ATOM 1256 CG LEU A 207 -27.991 10.811 38.729 1.00 99.18 C ANISOU 1256 CG LEU A 207 22103 9852 5730 2164 -395 -801 C ATOM 1257 CD1 LEU A 207 -26.887 9.988 39.378 1.00 97.56 C ANISOU 1257 CD1 LEU A 207 21913 9585 5570 1812 -571 -723 C ATOM 1258 CD2 LEU A 207 -28.966 11.276 39.782 1.00102.41 C ANISOU 1258 CD2 LEU A 207 22831 10264 5814 2531 -159 -869 C ATOM 1259 N TYR A 208 -27.399 11.391 34.668 1.00 95.41 N ANISOU 1259 N TYR A 208 20917 9421 5914 1918 -692 -771 N ATOM 1260 CA TYR A 208 -27.801 10.518 33.569 1.00 94.15 C ANISOU 1260 CA TYR A 208 20194 9532 6045 1867 -593 -724 C ATOM 1261 C TYR A 208 -26.564 10.113 32.744 1.00 94.61 C ANISOU 1261 C TYR A 208 20082 9526 6340 1488 -806 -657 C ATOM 1262 O TYR A 208 -26.449 8.934 32.399 1.00 92.67 O ANISOU 1262 O TYR A 208 19424 9468 6316 1321 -753 -594 O ATOM 1263 CB TYR A 208 -28.908 11.117 32.677 1.00 97.90 C ANISOU 1263 CB TYR A 208 20557 10120 6520 2192 -473 -776 C ATOM 1264 CG TYR A 208 -29.010 10.414 31.337 1.00100.57 C ANISOU 1264 CG TYR A 208 20403 10658 7151 2064 -471 -731 C ATOM 1265 CD1 TYR A 208 -28.424 10.960 30.197 1.00102.77 C ANISOU 1265 CD1 TYR A 208 20729 10800 7521 1957 -644 -727 C ATOM 1266 CD2 TYR A 208 -29.582 9.146 31.232 1.00100.85 C ANISOU 1266 CD2 TYR A 208 19958 10997 7364 2003 -305 -688 C ATOM 1267 CE1 TYR A 208 -28.443 10.285 28.978 1.00103.07 C ANISOU 1267 CE1 TYR A 208 20352 11002 7806 1827 -646 -688 C ATOM 1268 CE2 TYR A 208 -29.602 8.458 30.019 1.00100.24 C ANISOU 1268 CE2 TYR A 208 19474 11074 7539 1857 -322 -652 C ATOM 1269 CZ TYR A 208 -29.029 9.034 28.894 1.00112.00 C ANISOU 1269 CZ TYR A 208 21025 12427 9104 1781 -492 -655 C ATOM 1270 OH TYR A 208 -29.035 8.391 27.680 1.00117.06 O ANISOU 1270 OH TYR A 208 21307 13203 9965 1649 -508 -625 O ATOM 1271 N THR A 209 -25.648 11.069 32.440 1.00 89.72 N ANISOU 1271 N THR A 209 19785 8642 5664 1351 -1033 -669 N ATOM 1272 CA THR A 209 -24.410 10.807 31.688 1.00 87.31 C ANISOU 1272 CA THR A 209 19330 8281 5563 994 -1226 -601 C ATOM 1273 C THR A 209 -23.686 9.558 32.275 1.00 89.94 C ANISOU 1273 C THR A 209 19420 8724 6030 747 -1257 -522 C ATOM 1274 O THR A 209 -23.368 8.632 31.529 1.00 87.31 O ANISOU 1274 O THR A 209 18690 8540 5942 593 -1239 -461 O ATOM 1275 CB THR A 209 -23.496 12.056 31.682 1.00 98.50 C ANISOU 1275 CB THR A 209 21205 9383 6837 848 -1464 -621 C ATOM 1276 OG1 THR A 209 -24.237 13.217 31.299 1.00102.00 O ANISOU 1276 OG1 THR A 209 21955 9690 7111 1121 -1426 -696 O ATOM 1277 CG2 THR A 209 -22.288 11.906 30.767 1.00 96.05 C ANISOU 1277 CG2 THR A 209 20711 9046 6739 492 -1634 -547 C ATOM 1278 N VAL A 210 -23.494 9.523 33.612 1.00 88.56 N ANISOU 1278 N VAL A 210 19506 8469 5673 743 -1293 -526 N ATOM 1279 CA VAL A 210 -22.840 8.424 34.330 1.00 87.53 C ANISOU 1279 CA VAL A 210 19226 8415 5617 553 -1338 -450 C ATOM 1280 C VAL A 210 -23.768 7.173 34.358 1.00 90.78 C ANISOU 1280 C VAL A 210 19267 9084 6140 667 -1080 -421 C ATOM 1281 O VAL A 210 -23.271 6.085 34.067 1.00 89.54 O ANISOU 1281 O VAL A 210 18797 9036 6188 491 -1092 -346 O ATOM 1282 CB VAL A 210 -22.322 8.847 35.736 1.00 92.86 C ANISOU 1282 CB VAL A 210 20343 8906 6033 506 -1486 -463 C ATOM 1283 CG1 VAL A 210 -23.410 9.477 36.571 1.00 94.97 C ANISOU 1283 CG1 VAL A 210 20958 9116 6010 821 -1323 -550 C ATOM 1284 CG2 VAL A 210 -21.662 7.694 36.480 1.00 91.92 C ANISOU 1284 CG2 VAL A 210 20079 8869 5977 337 -1547 -377 C ATOM 1285 N TYR A 211 -25.093 7.313 34.638 1.00 87.03 N ANISOU 1285 N TYR A 211 18813 8712 5541 951 -845 -477 N ATOM 1286 CA TYR A 211 -26.000 6.154 34.600 1.00 85.04 C ANISOU 1286 CA TYR A 211 18190 8718 5401 1012 -600 -445 C ATOM 1287 C TYR A 211 -25.972 5.492 33.196 1.00 85.84 C ANISOU 1287 C TYR A 211 17855 8963 5798 891 -589 -411 C ATOM 1288 O TYR A 211 -25.855 4.269 33.107 1.00 85.38 O ANISOU 1288 O TYR A 211 17521 9024 5896 746 -531 -347 O ATOM 1289 CB TYR A 211 -27.448 6.510 35.010 1.00 87.51 C ANISOU 1289 CB TYR A 211 18544 9161 5546 1337 -344 -507 C ATOM 1290 CG TYR A 211 -28.451 5.460 34.584 1.00 88.03 C ANISOU 1290 CG TYR A 211 18151 9523 5771 1365 -107 -477 C ATOM 1291 CD1 TYR A 211 -29.236 5.641 33.452 1.00 89.51 C ANISOU 1291 CD1 TYR A 211 18055 9871 6085 1484 -32 -510 C ATOM 1292 CD2 TYR A 211 -28.536 4.237 35.250 1.00 89.04 C ANISOU 1292 CD2 TYR A 211 18135 9762 5933 1233 14 -407 C ATOM 1293 CE1 TYR A 211 -30.094 4.641 32.996 1.00 91.17 C ANISOU 1293 CE1 TYR A 211 17832 10357 6452 1454 149 -480 C ATOM 1294 CE2 TYR A 211 -29.402 3.232 34.813 1.00 89.94 C ANISOU 1294 CE2 TYR A 211 17842 10132 6200 1197 214 -375 C ATOM 1295 CZ TYR A 211 -30.174 3.435 33.677 1.00 99.81 C ANISOU 1295 CZ TYR A 211 18795 11550 7579 1295 274 -414 C ATOM 1296 OH TYR A 211 -31.030 2.452 33.219 1.00101.12 O ANISOU 1296 OH TYR A 211 18556 11974 7891 1226 447 -384 O ATOM 1297 N SER A 212 -26.050 6.291 32.115 1.00 79.89 N ANISOU 1297 N SER A 212 17082 8174 5099 951 -650 -454 N ATOM 1298 CA SER A 212 -26.012 5.769 30.749 1.00 76.92 C ANISOU 1298 CA SER A 212 16345 7912 4968 848 -649 -430 C ATOM 1299 C SER A 212 -24.676 5.048 30.447 1.00 81.57 C ANISOU 1299 C SER A 212 16817 8443 5735 549 -801 -354 C ATOM 1300 O SER A 212 -24.652 4.092 29.670 1.00 80.58 O ANISOU 1300 O SER A 212 16370 8440 5807 446 -749 -317 O ATOM 1301 CB SER A 212 -26.235 6.889 29.742 1.00 76.50 C ANISOU 1301 CB SER A 212 16379 7791 4895 973 -710 -485 C ATOM 1302 OG SER A 212 -25.029 7.597 29.523 1.00 76.36 O ANISOU 1302 OG SER A 212 16598 7549 4866 801 -927 -470 O ATOM 1303 N THR A 213 -23.579 5.520 31.062 1.00 78.88 N ANISOU 1303 N THR A 213 16740 7919 5313 420 -991 -331 N ATOM 1304 CA THR A 213 -22.231 4.980 30.897 1.00 77.43 C ANISOU 1304 CA THR A 213 16452 7693 5277 162 -1154 -254 C ATOM 1305 C THR A 213 -22.122 3.629 31.659 1.00 80.44 C ANISOU 1305 C THR A 213 16688 8167 5707 104 -1089 -188 C ATOM 1306 O THR A 213 -21.406 2.728 31.220 1.00 78.63 O ANISOU 1306 O THR A 213 16228 7989 5660 -40 -1128 -121 O ATOM 1307 CB THR A 213 -21.219 6.074 31.322 1.00 83.96 C ANISOU 1307 CB THR A 213 17612 8312 5977 43 -1390 -256 C ATOM 1308 OG1 THR A 213 -20.264 6.306 30.292 1.00 81.70 O ANISOU 1308 OG1 THR A 213 17203 7994 5847 -148 -1518 -219 O ATOM 1309 CG2 THR A 213 -20.541 5.814 32.642 1.00 81.44 C ANISOU 1309 CG2 THR A 213 17471 7926 5545 -49 -1516 -216 C ATOM 1310 N VAL A 214 -22.883 3.483 32.757 1.00 78.28 N ANISOU 1310 N VAL A 214 16565 7917 5263 235 -972 -206 N ATOM 1311 CA VAL A 214 -22.912 2.289 33.611 1.00 77.76 C ANISOU 1311 CA VAL A 214 16440 7913 5191 195 -893 -142 C ATOM 1312 C VAL A 214 -23.772 1.192 32.971 1.00 81.98 C ANISOU 1312 C VAL A 214 16640 8628 5880 208 -676 -127 C ATOM 1313 O VAL A 214 -23.292 0.072 32.815 1.00 81.86 O ANISOU 1313 O VAL A 214 16458 8641 6003 81 -681 -58 O ATOM 1314 CB VAL A 214 -23.398 2.649 35.033 1.00 82.43 C ANISOU 1314 CB VAL A 214 17363 8449 5509 322 -838 -166 C ATOM 1315 CG1 VAL A 214 -23.938 1.427 35.768 1.00 82.62 C ANISOU 1315 CG1 VAL A 214 17306 8577 5507 328 -656 -110 C ATOM 1316 CG2 VAL A 214 -22.286 3.323 35.829 1.00 83.06 C ANISOU 1316 CG2 VAL A 214 17775 8339 5445 232 -1098 -155 C ATOM 1317 N GLY A 215 -25.017 1.525 32.618 1.00 78.51 N ANISOU 1317 N GLY A 215 16118 8307 5407 361 -500 -190 N ATOM 1318 CA GLY A 215 -25.963 0.598 32.008 1.00 77.85 C ANISOU 1318 CA GLY A 215 15716 8412 5451 355 -306 -185 C ATOM 1319 C GLY A 215 -25.509 0.058 30.664 1.00 81.47 C ANISOU 1319 C GLY A 215 15916 8897 6143 221 -367 -168 C ATOM 1320 O GLY A 215 -25.785 -1.098 30.340 1.00 81.94 O ANISOU 1320 O GLY A 215 15766 9046 6321 123 -266 -134 O ATOM 1321 N ALA A 216 -24.777 0.874 29.890 1.00 76.61 N ANISOU 1321 N ALA A 216 15343 8186 5580 203 -528 -190 N ATOM 1322 CA ALA A 216 -24.294 0.501 28.567 1.00 74.54 C ANISOU 1322 CA ALA A 216 14867 7939 5515 93 -578 -177 C ATOM 1323 C ALA A 216 -22.895 -0.120 28.558 1.00 76.98 C ANISOU 1323 C ALA A 216 15158 8158 5934 -71 -708 -101 C ATOM 1324 O ALA A 216 -22.594 -0.827 27.604 1.00 75.55 O ANISOU 1324 O ALA A 216 14780 8012 5914 -153 -692 -80 O ATOM 1325 CB ALA A 216 -24.302 1.710 27.659 1.00 75.03 C ANISOU 1325 CB ALA A 216 14982 7959 5566 163 -657 -233 C ATOM 1326 N PHE A 217 -22.028 0.145 29.562 1.00 73.70 N ANISOU 1326 N PHE A 217 14939 7634 5428 -111 -842 -60 N ATOM 1327 CA PHE A 217 -20.671 -0.406 29.500 1.00 72.86 C ANISOU 1327 CA PHE A 217 14767 7479 5436 -245 -980 18 C ATOM 1328 C PHE A 217 -20.183 -1.036 30.794 1.00 76.80 C ANISOU 1328 C PHE A 217 15389 7934 5856 -267 -1040 86 C ATOM 1329 O PHE A 217 -19.996 -2.249 30.835 1.00 76.34 O ANISOU 1329 O PHE A 217 15217 7904 5885 -296 -988 145 O ATOM 1330 CB PHE A 217 -19.669 0.675 29.068 1.00 74.96 C ANISOU 1330 CB PHE A 217 15098 7666 5719 -326 -1166 19 C ATOM 1331 CG PHE A 217 -18.234 0.216 28.923 1.00 76.64 C ANISOU 1331 CG PHE A 217 15186 7872 6061 -460 -1307 105 C ATOM 1332 CD1 PHE A 217 -17.275 0.568 29.868 1.00 80.61 C ANISOU 1332 CD1 PHE A 217 15826 8313 6488 -539 -1505 153 C ATOM 1333 CD2 PHE A 217 -17.839 -0.558 27.831 1.00 77.62 C ANISOU 1333 CD2 PHE A 217 15054 8065 6375 -497 -1245 137 C ATOM 1334 CE1 PHE A 217 -15.946 0.161 29.722 1.00 82.18 C ANISOU 1334 CE1 PHE A 217 15860 8548 6815 -649 -1642 239 C ATOM 1335 CE2 PHE A 217 -16.510 -0.971 27.688 1.00 80.67 C ANISOU 1335 CE2 PHE A 217 15299 8471 6879 -585 -1357 220 C ATOM 1336 CZ PHE A 217 -15.578 -0.620 28.640 1.00 80.63 C ANISOU 1336 CZ PHE A 217 15387 8436 6814 -656 -1555 274 C ATOM 1337 N TYR A 218 -19.916 -0.215 31.819 1.00 73.26 N ANISOU 1337 N TYR A 218 15202 7400 5234 -255 -1166 79 N ATOM 1338 CA TYR A 218 -19.340 -0.636 33.092 1.00 73.03 C ANISOU 1338 CA TYR A 218 15336 7316 5097 -278 -1273 144 C ATOM 1339 C TYR A 218 -20.105 -1.766 33.753 1.00 78.56 C ANISOU 1339 C TYR A 218 16048 8057 5745 -217 -1093 175 C ATOM 1340 O TYR A 218 -19.446 -2.633 34.324 1.00 79.84 O ANISOU 1340 O TYR A 218 16227 8191 5915 -253 -1165 259 O ATOM 1341 CB TYR A 218 -19.189 0.547 34.043 1.00 73.96 C ANISOU 1341 CB TYR A 218 15784 7323 4993 -265 -1417 106 C ATOM 1342 CG TYR A 218 -18.263 1.603 33.486 1.00 73.53 C ANISOU 1342 CG TYR A 218 15751 7205 4983 -382 -1624 93 C ATOM 1343 CD1 TYR A 218 -16.881 1.460 33.573 1.00 75.72 C ANISOU 1343 CD1 TYR A 218 15951 7477 5343 -535 -1851 171 C ATOM 1344 CD2 TYR A 218 -18.764 2.717 32.822 1.00 73.04 C ANISOU 1344 CD2 TYR A 218 15770 7100 4883 -345 -1591 12 C ATOM 1345 CE1 TYR A 218 -16.021 2.424 33.044 1.00 75.99 C ANISOU 1345 CE1 TYR A 218 15983 7469 5420 -685 -2030 169 C ATOM 1346 CE2 TYR A 218 -17.914 3.685 32.287 1.00 73.37 C ANISOU 1346 CE2 TYR A 218 15859 7064 4954 -484 -1771 8 C ATOM 1347 CZ TYR A 218 -16.544 3.541 32.411 1.00 77.10 C ANISOU 1347 CZ TYR A 218 16247 7538 5509 -673 -1986 88 C ATOM 1348 OH TYR A 218 -15.708 4.510 31.918 1.00 72.30 O ANISOU 1348 OH TYR A 218 15679 6867 4924 -849 -2157 92 O ATOM 1349 N PHE A 219 -21.461 -1.793 33.675 1.00 74.81 N ANISOU 1349 N PHE A 219 15554 7655 5215 -131 -866 118 N ATOM 1350 CA PHE A 219 -22.221 -2.915 34.246 1.00 75.23 C ANISOU 1350 CA PHE A 219 15599 7760 5225 -119 -674 158 C ATOM 1351 C PHE A 219 -21.947 -4.145 33.350 1.00 78.88 C ANISOU 1351 C PHE A 219 15815 8254 5900 -209 -630 208 C ATOM 1352 O PHE A 219 -21.353 -5.102 33.871 1.00 78.41 O ANISOU 1352 O PHE A 219 15813 8135 5846 -247 -673 292 O ATOM 1353 CB PHE A 219 -23.725 -2.604 34.436 1.00 77.17 C ANISOU 1353 CB PHE A 219 15853 8112 5357 -17 -439 92 C ATOM 1354 CG PHE A 219 -24.613 -3.733 34.922 1.00 78.73 C ANISOU 1354 CG PHE A 219 16007 8390 5518 -48 -212 136 C ATOM 1355 CD1 PHE A 219 -24.093 -4.781 35.674 1.00 81.44 C ANISOU 1355 CD1 PHE A 219 16468 8650 5826 -124 -232 231 C ATOM 1356 CD2 PHE A 219 -25.978 -3.719 34.671 1.00 81.24 C ANISOU 1356 CD2 PHE A 219 16175 8869 5822 -2 19 88 C ATOM 1357 CE1 PHE A 219 -24.917 -5.813 36.130 1.00 83.38 C ANISOU 1357 CE1 PHE A 219 16711 8948 6021 -181 -15 278 C ATOM 1358 CE2 PHE A 219 -26.803 -4.753 35.133 1.00 84.94 C ANISOU 1358 CE2 PHE A 219 16596 9424 6254 -74 235 136 C ATOM 1359 CZ PHE A 219 -26.267 -5.790 35.862 1.00 83.12 C ANISOU 1359 CZ PHE A 219 16517 9083 5983 -174 223 232 C ATOM 1360 N PRO A 220 -22.208 -4.088 32.003 1.00 74.19 N ANISOU 1360 N PRO A 220 14987 7730 5472 -231 -579 160 N ATOM 1361 CA PRO A 220 -21.850 -5.226 31.146 1.00 72.63 C ANISOU 1361 CA PRO A 220 14607 7535 5454 -308 -550 200 C ATOM 1362 C PRO A 220 -20.407 -5.734 31.296 1.00 76.48 C ANISOU 1362 C PRO A 220 15113 7934 6012 -331 -721 285 C ATOM 1363 O PRO A 220 -20.271 -6.940 31.396 1.00 78.86 O ANISOU 1363 O PRO A 220 15412 8198 6355 -351 -667 346 O ATOM 1364 CB PRO A 220 -22.047 -4.686 29.731 1.00 73.06 C ANISOU 1364 CB PRO A 220 14470 7654 5637 -312 -541 130 C ATOM 1365 CG PRO A 220 -22.999 -3.606 29.849 1.00 78.02 C ANISOU 1365 CG PRO A 220 15144 8346 6154 -231 -487 54 C ATOM 1366 CD PRO A 220 -22.908 -3.040 31.224 1.00 75.13 C ANISOU 1366 CD PRO A 220 15028 7921 5598 -170 -538 67 C ATOM 1367 N THR A 221 -19.346 -4.880 31.323 1.00 70.21 N ANISOU 1367 N THR A 221 14338 7110 5228 -332 -923 296 N ATOM 1368 CA THR A 221 -17.964 -5.405 31.402 1.00 69.29 C ANISOU 1368 CA THR A 221 14171 6959 5198 -346 -1085 385 C ATOM 1369 C THR A 221 -17.654 -6.063 32.747 1.00 72.96 C ANISOU 1369 C THR A 221 14825 7359 5536 -312 -1153 467 C ATOM 1370 O THR A 221 -16.929 -7.049 32.750 1.00 72.70 O ANISOU 1370 O THR A 221 14743 7302 5579 -282 -1197 547 O ATOM 1371 CB THR A 221 -16.843 -4.396 31.034 1.00 75.49 C ANISOU 1371 CB THR A 221 14879 7761 6043 -396 -1288 390 C ATOM 1372 OG1 THR A 221 -16.103 -3.980 32.177 1.00 76.45 O ANISOU 1372 OG1 THR A 221 15159 7843 6046 -414 -1494 438 O ATOM 1373 CG2 THR A 221 -17.320 -3.216 30.287 1.00 73.12 C ANISOU 1373 CG2 THR A 221 14560 7479 5741 -428 -1261 302 C ATOM 1374 N LEU A 222 -18.170 -5.537 33.874 1.00 70.60 N ANISOU 1374 N LEU A 222 14764 7027 5035 -295 -1162 450 N ATOM 1375 CA LEU A 222 -17.922 -6.131 35.201 1.00 71.81 C ANISOU 1375 CA LEU A 222 15142 7109 5033 -261 -1227 529 C ATOM 1376 C LEU A 222 -18.616 -7.496 35.302 1.00 75.09 C ANISOU 1376 C LEU A 222 15586 7496 5448 -249 -1020 573 C ATOM 1377 O LEU A 222 -18.148 -8.394 36.019 1.00 75.36 O ANISOU 1377 O LEU A 222 15753 7456 5424 -215 -1074 667 O ATOM 1378 CB LEU A 222 -18.393 -5.209 36.328 1.00 73.02 C ANISOU 1378 CB LEU A 222 15574 7227 4944 -242 -1257 490 C ATOM 1379 CG LEU A 222 -17.478 -4.040 36.683 1.00 79.83 C ANISOU 1379 CG LEU A 222 16535 8058 5739 -276 -1527 476 C ATOM 1380 CD1 LEU A 222 -18.255 -2.941 37.420 1.00 81.46 C ANISOU 1380 CD1 LEU A 222 17020 8218 5713 -241 -1491 393 C ATOM 1381 CD2 LEU A 222 -16.306 -4.487 37.550 1.00 84.73 C ANISOU 1381 CD2 LEU A 222 17251 8636 6308 -282 -1774 579 C ATOM 1382 N LEU A 223 -19.718 -7.645 34.537 1.00 69.09 N ANISOU 1382 N LEU A 223 14704 6795 4751 -286 -796 508 N ATOM 1383 CA LEU A 223 -20.509 -8.858 34.456 1.00 68.39 C ANISOU 1383 CA LEU A 223 14624 6690 4673 -330 -588 535 C ATOM 1384 C LEU A 223 -19.711 -9.916 33.737 1.00 73.50 C ANISOU 1384 C LEU A 223 15173 7274 5480 -326 -631 592 C ATOM 1385 O LEU A 223 -19.629 -11.044 34.229 1.00 75.26 O ANISOU 1385 O LEU A 223 15544 7397 5657 -322 -589 672 O ATOM 1386 CB LEU A 223 -21.837 -8.564 33.743 1.00 66.98 C ANISOU 1386 CB LEU A 223 14297 6624 4528 -385 -380 442 C ATOM 1387 CG LEU A 223 -22.704 -9.732 33.307 1.00 71.22 C ANISOU 1387 CG LEU A 223 14770 7172 5118 -488 -175 452 C ATOM 1388 CD1 LEU A 223 -23.169 -10.553 34.480 1.00 72.35 C ANISOU 1388 CD1 LEU A 223 15140 7253 5097 -533 -54 529 C ATOM 1389 CD2 LEU A 223 -23.896 -9.236 32.552 1.00 74.06 C ANISOU 1389 CD2 LEU A 223 14934 7685 5521 -533 -28 358 C ATOM 1390 N LEU A 224 -19.089 -9.530 32.606 1.00 68.40 N ANISOU 1390 N LEU A 224 14307 6675 5006 -314 -711 555 N ATOM 1391 CA LEU A 224 -18.269 -10.367 31.731 1.00 67.87 C ANISOU 1391 CA LEU A 224 14117 6569 5100 -279 -740 593 C ATOM 1392 C LEU A 224 -16.999 -10.819 32.412 1.00 73.49 C ANISOU 1392 C LEU A 224 14904 7220 5798 -175 -922 701 C ATOM 1393 O LEU A 224 -16.590 -11.949 32.171 1.00 73.64 O ANISOU 1393 O LEU A 224 14945 7160 5875 -109 -895 760 O ATOM 1394 CB LEU A 224 -17.929 -9.639 30.433 1.00 66.35 C ANISOU 1394 CB LEU A 224 13684 6463 5064 -290 -772 527 C ATOM 1395 CG LEU A 224 -19.113 -9.350 29.538 1.00 69.79 C ANISOU 1395 CG LEU A 224 14024 6961 5532 -368 -609 427 C ATOM 1396 CD1 LEU A 224 -18.898 -8.066 28.778 1.00 68.79 C ANISOU 1396 CD1 LEU A 224 13754 6918 5464 -373 -684 362 C ATOM 1397 CD2 LEU A 224 -19.416 -10.527 28.602 1.00 71.91 C ANISOU 1397 CD2 LEU A 224 14243 7184 5895 -402 -473 418 C ATOM 1398 N ILE A 225 -16.379 -9.970 33.263 1.00 71.58 N ANISOU 1398 N ILE A 225 14717 7008 5470 -152 -1117 727 N ATOM 1399 CA ILE A 225 -15.198 -10.378 34.028 1.00 74.41 C ANISOU 1399 CA ILE A 225 15141 7333 5798 -53 -1323 836 C ATOM 1400 C ILE A 225 -15.634 -11.583 34.877 1.00 82.73 C ANISOU 1400 C ILE A 225 16462 8253 6719 -6 -1231 908 C ATOM 1401 O ILE A 225 -15.091 -12.678 34.707 1.00 83.85 O ANISOU 1401 O ILE A 225 16620 8321 6918 96 -1235 983 O ATOM 1402 CB ILE A 225 -14.569 -9.236 34.891 1.00 78.60 C ANISOU 1402 CB ILE A 225 15724 7914 6225 -77 -1567 845 C ATOM 1403 CG1 ILE A 225 -14.055 -8.068 34.020 1.00 78.50 C ANISOU 1403 CG1 ILE A 225 15472 8013 6342 -152 -1662 787 C ATOM 1404 CG2 ILE A 225 -13.432 -9.775 35.760 1.00 81.10 C ANISOU 1404 CG2 ILE A 225 16111 8210 6493 28 -1795 967 C ATOM 1405 CD1 ILE A 225 -14.140 -6.665 34.689 1.00 86.29 C ANISOU 1405 CD1 ILE A 225 16591 9009 7185 -245 -1803 734 C ATOM 1406 N ALA A 226 -16.696 -11.391 35.696 1.00 80.51 N ANISOU 1406 N ALA A 226 16395 7937 6259 -80 -1116 882 N ATOM 1407 CA ALA A 226 -17.291 -12.400 36.576 1.00 81.93 C ANISOU 1407 CA ALA A 226 16860 7993 6278 -82 -993 948 C ATOM 1408 C ALA A 226 -17.773 -13.646 35.808 1.00 86.21 C ANISOU 1408 C ALA A 226 17393 8450 6912 -117 -793 959 C ATOM 1409 O ALA A 226 -17.585 -14.765 36.290 1.00 89.08 O ANISOU 1409 O ALA A 226 17974 8669 7204 -65 -778 1053 O ATOM 1410 CB ALA A 226 -18.444 -11.792 37.352 1.00 82.77 C ANISOU 1410 CB ALA A 226 17124 8126 6198 -170 -857 899 C ATOM 1411 N LEU A 227 -18.372 -13.449 34.621 1.00 78.49 N ANISOU 1411 N LEU A 227 16198 7547 6078 -205 -656 864 N ATOM 1412 CA LEU A 227 -18.914 -14.512 33.783 1.00 77.49 C ANISOU 1412 CA LEU A 227 16065 7344 6032 -276 -476 852 C ATOM 1413 C LEU A 227 -17.805 -15.307 33.099 1.00 82.95 C ANISOU 1413 C LEU A 227 16715 7948 6853 -138 -565 900 C ATOM 1414 O LEU A 227 -17.745 -16.524 33.269 1.00 83.40 O ANISOU 1414 O LEU A 227 16983 7838 6866 -104 -509 969 O ATOM 1415 CB LEU A 227 -19.836 -13.876 32.728 1.00 75.29 C ANISOU 1415 CB LEU A 227 15554 7199 5856 -399 -347 729 C ATOM 1416 CG LEU A 227 -21.282 -14.349 32.594 1.00 78.93 C ANISOU 1416 CG LEU A 227 16048 7672 6270 -581 -114 689 C ATOM 1417 CD1 LEU A 227 -21.890 -14.755 33.913 1.00 80.35 C ANISOU 1417 CD1 LEU A 227 16482 7796 6252 -644 -16 758 C ATOM 1418 CD2 LEU A 227 -22.116 -13.276 31.954 1.00 77.72 C ANISOU 1418 CD2 LEU A 227 15656 7704 6168 -647 -53 577 C ATOM 1419 N TYR A 228 -16.934 -14.615 32.313 1.00 79.46 N ANISOU 1419 N TYR A 228 16013 7617 6562 -53 -690 867 N ATOM 1420 CA TYR A 228 -15.828 -15.226 31.568 1.00 79.30 C ANISOU 1420 CA TYR A 228 15894 7561 6674 105 -757 908 C ATOM 1421 C TYR A 228 -14.755 -15.807 32.504 1.00 85.06 C ANISOU 1421 C TYR A 228 16761 8218 7339 296 -927 1037 C ATOM 1422 O TYR A 228 -14.133 -16.816 32.163 1.00 86.16 O ANISOU 1422 O TYR A 228 16955 8256 7527 454 -922 1095 O ATOM 1423 CB TYR A 228 -15.185 -14.252 30.552 1.00 78.26 C ANISOU 1423 CB TYR A 228 15437 7593 6705 125 -830 850 C ATOM 1424 CG TYR A 228 -14.238 -14.964 29.608 1.00 79.63 C ANISOU 1424 CG TYR A 228 15497 7743 7014 283 -826 879 C ATOM 1425 CD1 TYR A 228 -14.709 -15.910 28.699 1.00 81.25 C ANISOU 1425 CD1 TYR A 228 15784 7830 7257 276 -649 838 C ATOM 1426 CD2 TYR A 228 -12.862 -14.793 29.713 1.00 81.15 C ANISOU 1426 CD2 TYR A 228 15527 8028 7280 451 -1000 956 C ATOM 1427 CE1 TYR A 228 -13.838 -16.644 27.899 1.00 81.90 C ANISOU 1427 CE1 TYR A 228 15817 7867 7435 458 -629 866 C ATOM 1428 CE2 TYR A 228 -11.980 -15.522 28.916 1.00 83.01 C ANISOU 1428 CE2 TYR A 228 15659 8253 7627 640 -973 993 C ATOM 1429 CZ TYR A 228 -12.473 -16.447 28.010 1.00 88.58 C ANISOU 1429 CZ TYR A 228 16481 8821 8356 657 -779 945 C ATOM 1430 OH TYR A 228 -11.616 -17.156 27.205 1.00 89.27 O ANISOU 1430 OH TYR A 228 16498 8885 8533 869 -734 974 O ATOM 1431 N GLY A 229 -14.549 -15.179 33.654 1.00 81.62 N ANISOU 1431 N GLY A 229 16398 7829 6783 296 -1080 1080 N ATOM 1432 CA GLY A 229 -13.589 -15.669 34.632 1.00 84.03 C ANISOU 1432 CA GLY A 229 16845 8078 7003 472 -1273 1206 C ATOM 1433 C GLY A 229 -13.891 -17.104 35.014 1.00 89.66 C ANISOU 1433 C GLY A 229 17888 8568 7610 543 -1163 1282 C ATOM 1434 O GLY A 229 -12.993 -17.951 34.997 1.00 90.81 O ANISOU 1434 O GLY A 229 18084 8637 7781 759 -1249 1371 O ATOM 1435 N ARG A 230 -15.188 -17.384 35.285 1.00 86.06 N ANISOU 1435 N ARG A 230 17650 8012 7036 358 -959 1247 N ATOM 1436 CA ARG A 230 -15.731 -18.703 35.624 1.00 87.45 C ANISOU 1436 CA ARG A 230 18178 7959 7092 338 -812 1310 C ATOM 1437 C ARG A 230 -15.542 -19.663 34.464 1.00 92.11 C ANISOU 1437 C ARG A 230 18752 8434 7813 405 -711 1294 C ATOM 1438 O ARG A 230 -15.082 -20.780 34.685 1.00 94.25 O ANISOU 1438 O ARG A 230 19278 8509 8023 562 -728 1386 O ATOM 1439 CB ARG A 230 -17.220 -18.610 35.993 1.00 87.09 C ANISOU 1439 CB ARG A 230 18272 7895 6923 72 -593 1261 C ATOM 1440 CG ARG A 230 -17.484 -17.874 37.301 1.00 98.94 C ANISOU 1440 CG ARG A 230 19897 9458 8236 32 -653 1290 C ATOM 1441 N ILE A 231 -15.864 -19.208 33.228 1.00 87.14 N ANISOU 1441 N ILE A 231 17848 7915 7345 306 -615 1178 N ATOM 1442 CA ILE A 231 -15.729 -19.943 31.965 1.00 87.43 C ANISOU 1442 CA ILE A 231 17850 7865 7505 354 -513 1135 C ATOM 1443 C ILE A 231 -14.247 -20.343 31.744 1.00 95.12 C ANISOU 1443 C ILE A 231 18759 8823 8559 682 -661 1212 C ATOM 1444 O ILE A 231 -13.982 -21.502 31.430 1.00 96.65 O ANISOU 1444 O ILE A 231 19170 8817 8736 822 -601 1252 O ATOM 1445 CB ILE A 231 -16.309 -19.097 30.793 1.00 88.07 C ANISOU 1445 CB ILE A 231 17626 8112 7725 190 -422 997 C ATOM 1446 CG1 ILE A 231 -17.855 -19.053 30.853 1.00 87.57 C ANISOU 1446 CG1 ILE A 231 17642 8044 7585 -108 -246 928 C ATOM 1447 CG2 ILE A 231 -15.823 -19.588 29.427 1.00 89.17 C ANISOU 1447 CG2 ILE A 231 17673 8208 8000 296 -368 952 C ATOM 1448 CD1 ILE A 231 -18.510 -17.920 30.065 1.00 90.02 C ANISOU 1448 CD1 ILE A 231 17645 8565 7992 -253 -202 806 C ATOM 1449 N TYR A 232 -13.298 -19.411 31.962 1.00 93.41 N ANISOU 1449 N TYR A 232 18262 8814 8415 803 -854 1237 N ATOM 1450 CA TYR A 232 -11.858 -19.653 31.821 1.00 95.67 C ANISOU 1450 CA TYR A 232 18404 9159 8788 1110 -1008 1319 C ATOM 1451 C TYR A 232 -11.339 -20.648 32.867 1.00 99.89 C ANISOU 1451 C TYR A 232 19249 9524 9181 1331 -1117 1458 C ATOM 1452 O TYR A 232 -10.411 -21.391 32.571 1.00 99.31 O ANISOU 1452 O TYR A 232 19176 9402 9156 1621 -1162 1525 O ATOM 1453 CB TYR A 232 -11.067 -18.334 31.910 1.00 98.04 C ANISOU 1453 CB TYR A 232 18323 9740 9185 1112 -1202 1317 C ATOM 1454 CG TYR A 232 -9.649 -18.458 31.392 1.00103.81 C ANISOU 1454 CG TYR A 232 18780 10604 10059 1383 -1315 1380 C ATOM 1455 CD1 TYR A 232 -8.581 -18.664 32.263 1.00109.06 C ANISOU 1455 CD1 TYR A 232 19420 11328 10688 1611 -1544 1508 C ATOM 1456 CD2 TYR A 232 -9.375 -18.401 30.026 1.00104.10 C ANISOU 1456 CD2 TYR A 232 18578 10719 10256 1423 -1187 1316 C ATOM 1457 CE1 TYR A 232 -7.277 -18.820 31.788 1.00112.61 C ANISOU 1457 CE1 TYR A 232 19575 11937 11275 1878 -1638 1575 C ATOM 1458 CE2 TYR A 232 -8.075 -18.547 29.540 1.00107.02 C ANISOU 1458 CE2 TYR A 232 18677 11234 10754 1686 -1257 1380 C ATOM 1459 CZ TYR A 232 -7.027 -18.754 30.425 1.00118.69 C ANISOU 1459 CZ TYR A 232 20093 12794 12209 1915 -1481 1511 C ATOM 1460 OH TYR A 232 -5.742 -18.899 29.954 1.00122.63 O ANISOU 1460 OH TYR A 232 20276 13477 12841 2186 -1544 1582 O ATOM 1461 N VAL A 233 -11.917 -20.641 34.084 1.00 98.65 N ANISOU 1461 N VAL A 233 19361 9282 8840 1215 -1157 1504 N ATOM 1462 CA VAL A 233 -11.556 -21.549 35.186 1.00102.18 C ANISOU 1462 CA VAL A 233 20165 9546 9111 1398 -1261 1641 C ATOM 1463 C VAL A 233 -12.067 -22.961 34.845 1.00109.00 C ANISOU 1463 C VAL A 233 21415 10098 9903 1425 -1062 1659 C ATOM 1464 O VAL A 233 -11.349 -23.937 35.051 1.00110.90 O ANISOU 1464 O VAL A 233 21872 10177 10089 1712 -1129 1762 O ATOM 1465 CB VAL A 233 -12.068 -21.026 36.563 1.00106.27 C ANISOU 1465 CB VAL A 233 20873 10072 9433 1244 -1345 1678 C ATOM 1466 CG1 VAL A 233 -12.171 -22.136 37.605 1.00108.92 C ANISOU 1466 CG1 VAL A 233 21700 10144 9542 1343 -1354 1805 C ATOM 1467 CG2 VAL A 233 -11.177 -19.903 37.082 1.00106.04 C ANISOU 1467 CG2 VAL A 233 20562 10292 9436 1311 -1622 1700 C ATOM 1468 N GLU A 234 -13.276 -23.051 34.272 1.00105.73 N ANISOU 1468 N GLU A 234 21077 9604 9490 1133 -828 1558 N ATOM 1469 CA GLU A 234 -13.887 -24.307 33.845 1.00107.54 C ANISOU 1469 CA GLU A 234 21670 9538 9652 1073 -634 1555 C ATOM 1470 C GLU A 234 -13.167 -24.906 32.618 1.00111.67 C ANISOU 1470 C GLU A 234 22121 9997 10312 1308 -598 1525 C ATOM 1471 O GLU A 234 -12.978 -26.119 32.572 1.00113.81 O ANISOU 1471 O GLU A 234 22761 9987 10496 1468 -548 1583 O ATOM 1472 CB GLU A 234 -15.371 -24.088 33.530 1.00107.43 C ANISOU 1472 CB GLU A 234 21674 9523 9620 665 -420 1449 C ATOM 1473 N ALA A 235 -12.765 -24.065 31.640 1.00106.05 N ANISOU 1473 N ALA A 235 20971 9530 9795 1337 -614 1436 N ATOM 1474 CA ALA A 235 -12.074 -24.498 30.414 1.00106.25 C ANISOU 1474 CA ALA A 235 20889 9533 9947 1561 -557 1398 C ATOM 1475 C ALA A 235 -10.626 -24.963 30.670 1.00114.06 C ANISOU 1475 C ALA A 235 21850 10532 10955 2013 -711 1519 C ATOM 1476 O ALA A 235 -10.140 -25.843 29.958 1.00115.54 O ANISOU 1476 O ALA A 235 22169 10570 11161 2265 -633 1525 O ATOM 1477 CB ALA A 235 -12.075 -23.378 29.383 1.00103.90 C ANISOU 1477 CB ALA A 235 20135 9511 9832 1443 -526 1282 C ATOM 1478 N ARG A 236 -9.939 -24.365 31.660 1.00112.13 N ANISOU 1478 N ARG A 236 21433 10471 10700 2124 -933 1612 N ATOM 1479 CA ARG A 236 -8.549 -24.681 31.992 1.00115.04 C ANISOU 1479 CA ARG A 236 21701 10915 11093 2546 -1120 1736 C ATOM 1480 C ARG A 236 -8.447 -25.837 32.981 1.00122.76 C ANISOU 1480 C ARG A 236 23172 11603 11869 2753 -1184 1865 C ATOM 1481 O ARG A 236 -7.590 -26.704 32.813 1.00126.03 O ANISOU 1481 O ARG A 236 23692 11917 12277 3147 -1217 1943 O ATOM 1482 CB ARG A 236 -7.827 -23.445 32.552 1.00114.92 C ANISOU 1482 CB ARG A 236 21250 11252 11161 2538 -1361 1773 C ATOM 1483 N SER A 237 -9.299 -25.861 34.010 1.00118.77 N ANISOU 1483 N SER A 237 22982 10961 11186 2512 -1193 1893 N ATOM 1484 CA SER A 237 -9.222 -26.933 34.996 1.00121.77 C ANISOU 1484 CA SER A 237 23870 11050 11349 2690 -1253 2027 C ATOM 1485 C SER A 237 -9.984 -28.209 34.577 1.00126.72 C ANISOU 1485 C SER A 237 25018 11272 11859 2628 -1018 2009 C ATOM 1486 O SER A 237 -9.727 -29.261 35.164 1.00130.76 O ANISOU 1486 O SER A 237 25981 11501 12200 2855 -1056 2125 O ATOM 1487 CB SER A 237 -9.726 -26.453 36.354 1.00124.95 C ANISOU 1487 CB SER A 237 24425 11471 11581 2478 -1363 2082 C ATOM 1488 OG SER A 237 -11.108 -26.137 36.315 1.00130.81 O ANISOU 1488 OG SER A 237 25268 12161 12275 2036 -1158 1984 O ATOM 1489 N ARG A 238 -10.911 -28.138 33.600 1.00119.56 N ANISOU 1489 N ARG A 238 24080 10322 11026 2318 -792 1870 N ATOM 1490 CA ARG A 238 -11.689 -29.324 33.251 1.00120.33 C ANISOU 1490 CA ARG A 238 24692 10032 10998 2195 -589 1850 C ATOM 1491 C ARG A 238 -11.658 -29.669 31.769 1.00123.40 C ANISOU 1491 C ARG A 238 25017 10358 11511 2240 -435 1734 C ATOM 1492 O ARG A 238 -11.452 -30.840 31.446 1.00126.78 O ANISOU 1492 O ARG A 238 25862 10461 11847 2442 -363 1763 O ATOM 1493 CB ARG A 238 -13.142 -29.178 33.713 1.00118.82 C ANISOU 1493 CB ARG A 238 24687 9766 10694 1691 -449 1809 C ATOM 1494 CG ARG A 238 -13.721 -30.453 34.307 1.00132.70 C ANISOU 1494 CG ARG A 238 27104 11104 12213 1598 -348 1895 C ATOM 1495 CD ARG A 238 -15.230 -30.372 34.447 1.00148.24 C ANISOU 1495 CD ARG A 238 29195 13027 14104 1059 -156 1835 C ATOM 1496 NE ARG A 238 -15.916 -30.483 33.155 1.00162.10 N ANISOU 1496 NE ARG A 238 30860 14760 15972 812 13 1689 N ATOM 1497 CZ ARG A 238 -17.222 -30.688 33.010 1.00178.77 C ANISOU 1497 CZ ARG A 238 33110 16790 18024 350 193 1631 C ATOM 1498 NH1 ARG A 238 -18.003 -30.830 34.075 1.00171.43 N ANISOU 1498 NH1 ARG A 238 32418 15792 16925 82 259 1710 N ATOM 1499 NH2 ARG A 238 -17.754 -30.773 31.798 1.00161.43 N ANISOU 1499 NH2 ARG A 238 30817 14589 15931 149 307 1498 N ATOM 1500 N ILE A 239 -11.867 -28.693 30.871 1.00115.41 N ANISOU 1500 N ILE A 239 23540 9626 10683 2063 -383 1605 N ATOM 1501 CA ILE A 239 -11.878 -28.968 29.431 1.00114.69 C ANISOU 1501 CA ILE A 239 23403 9482 10692 2089 -234 1489 C ATOM 1502 C ILE A 239 -10.444 -29.214 28.887 1.00121.60 C ANISOU 1502 C ILE A 239 24116 10425 11661 2608 -295 1531 C ATOM 1503 O ILE A 239 -10.278 -29.430 27.683 1.00122.22 O ANISOU 1503 O ILE A 239 24149 10474 11815 2699 -169 1442 O ATOM 1504 CB ILE A 239 -12.611 -27.849 28.648 1.00113.62 C ANISOU 1504 CB ILE A 239 22855 9614 10702 1733 -159 1343 C ATOM 1505 N ALA A1001 -9.429 -29.195 29.771 1.00100.51 N ANISOU 1505 N ALA A1001 14630 10562 12997 -191 941 -1479 N ATOM 1506 CA ALA A1001 -8.017 -29.416 29.447 1.00 99.46 C ANISOU 1506 CA ALA A1001 14410 10897 12484 -673 885 -1664 C ATOM 1507 C ALA A1001 -7.470 -30.616 30.217 1.00100.59 C ANISOU 1507 C ALA A1001 13877 11657 12685 -837 569 -1739 C ATOM 1508 O ALA A1001 -6.467 -31.204 29.819 1.00 98.70 O ANISOU 1508 O ALA A1001 13336 11886 12278 -1007 366 -1825 O ATOM 1509 CB ALA A1001 -7.205 -28.171 29.768 1.00103.59 C ANISOU 1509 CB ALA A1001 15517 11290 12553 -1324 1456 -1879 C ATOM 1510 N ASP A1002 -8.129 -30.967 31.330 1.00 97.08 N ANISOU 1510 N ASP A1002 13225 11195 12468 -757 568 -1689 N ATOM 1511 CA ASP A1002 -7.771 -32.111 32.162 1.00 94.85 C ANISOU 1511 CA ASP A1002 12390 11412 12236 -823 295 -1696 C ATOM 1512 C ASP A1002 -8.229 -33.393 31.463 1.00 93.91 C ANISOU 1512 C ASP A1002 11812 11369 12501 -295 -175 -1535 C ATOM 1513 O ASP A1002 -7.521 -34.397 31.523 1.00 91.85 O ANISOU 1513 O ASP A1002 11146 11556 12195 -307 -442 -1541 O ATOM 1514 CB ASP A1002 -8.379 -31.977 33.577 1.00 98.04 C ANISOU 1514 CB ASP A1002 12857 11689 12704 -931 533 -1691 C ATOM 1515 CG ASP A1002 -7.427 -31.486 34.671 1.00112.46 C ANISOU 1515 CG ASP A1002 14832 13859 14037 -1589 778 -1903 C ATOM 1516 OD1 ASP A1002 -6.265 -31.129 34.343 1.00115.14 O ANISOU 1516 OD1 ASP A1002 15199 14551 13997 -2020 794 -2081 O ATOM 1517 OD2 ASP A1002 -7.840 -31.467 35.855 1.00117.58 O ANISOU 1517 OD2 ASP A1002 15561 14451 14663 -1701 956 -1909 O ATOM 1518 N LEU A1003 -9.391 -33.344 30.768 1.00 88.96 N ANISOU 1518 N LEU A1003 11255 10312 12232 169 -272 -1400 N ATOM 1519 CA LEU A1003 -9.905 -34.472 29.992 1.00 86.28 C ANISOU 1519 CA LEU A1003 10538 10009 12235 600 -713 -1301 C ATOM 1520 C LEU A1003 -9.035 -34.653 28.746 1.00 90.11 C ANISOU 1520 C LEU A1003 11073 10691 12474 595 -910 -1360 C ATOM 1521 O LEU A1003 -8.575 -35.764 28.479 1.00 89.40 O ANISOU 1521 O LEU A1003 10641 10897 12430 672 -1182 -1376 O ATOM 1522 CB LEU A1003 -11.380 -34.276 29.606 1.00 86.96 C ANISOU 1522 CB LEU A1003 10634 9670 12738 1047 -789 -1172 C ATOM 1523 N GLU A1004 -8.746 -33.543 28.041 1.00 87.06 N ANISOU 1523 N GLU A1004 11168 10114 11797 483 -699 -1394 N ATOM 1524 CA GLU A1004 -7.957 -33.508 26.816 1.00 86.63 C ANISOU 1524 CA GLU A1004 11286 10170 11459 448 -776 -1451 C ATOM 1525 C GLU A1004 -6.484 -33.846 27.035 1.00 92.47 C ANISOU 1525 C GLU A1004 11807 11424 11903 29 -692 -1613 C ATOM 1526 O GLU A1004 -5.929 -34.567 26.205 1.00 92.17 O ANISOU 1526 O GLU A1004 11601 11607 11813 135 -889 -1645 O ATOM 1527 CB GLU A1004 -8.083 -32.150 26.126 1.00 90.37 C ANISOU 1527 CB GLU A1004 12425 10234 11676 427 -480 -1419 C ATOM 1528 CG GLU A1004 -9.472 -31.914 25.567 1.00 97.32 C ANISOU 1528 CG GLU A1004 13467 10687 12822 986 -671 -1218 C ATOM 1529 CD GLU A1004 -9.556 -30.873 24.473 1.00110.39 C ANISOU 1529 CD GLU A1004 15790 11972 14180 1147 -525 -1119 C ATOM 1530 OE1 GLU A1004 -9.371 -29.672 24.779 1.00113.84 O ANISOU 1530 OE1 GLU A1004 16769 12095 14392 926 -28 -1121 O ATOM 1531 OE2 GLU A1004 -9.850 -31.254 23.316 1.00 92.52 O ANISOU 1531 OE2 GLU A1004 13566 9701 11886 1502 -892 -1035 O ATOM 1532 N ASP A1005 -5.843 -33.338 28.118 1.00 91.48 N ANISOU 1532 N ASP A1005 11669 11516 11571 -442 -404 -1728 N ATOM 1533 CA ASP A1005 -4.423 -33.619 28.387 1.00 92.59 C ANISOU 1533 CA ASP A1005 11494 12256 11428 -846 -361 -1888 C ATOM 1534 C ASP A1005 -4.211 -35.068 28.804 1.00 93.45 C ANISOU 1534 C ASP A1005 10991 12778 11738 -584 -718 -1810 C ATOM 1535 O ASP A1005 -3.280 -35.709 28.313 1.00 93.82 O ANISOU 1535 O ASP A1005 10735 13219 11694 -564 -827 -1859 O ATOM 1536 CB ASP A1005 -3.829 -32.677 29.450 1.00 97.62 C ANISOU 1536 CB ASP A1005 12270 13072 11750 -1466 -8 -2061 C ATOM 1537 CG ASP A1005 -2.405 -33.012 29.889 1.00118.31 C ANISOU 1537 CG ASP A1005 14417 16444 14092 -1886 -42 -2230 C ATOM 1538 OD1 ASP A1005 -2.137 -32.973 31.113 1.00121.91 O ANISOU 1538 OD1 ASP A1005 14687 17230 14405 -2191 -30 -2297 O ATOM 1539 OD2 ASP A1005 -1.558 -33.314 29.007 1.00126.69 O ANISOU 1539 OD2 ASP A1005 15281 17792 15065 -1898 -80 -2294 O ATOM 1540 N ASN A1006 -5.069 -35.586 29.685 1.00 87.41 N ANISOU 1540 N ASN A1006 10079 11888 11246 -365 -846 -1682 N ATOM 1541 CA ASN A1006 -4.939 -36.958 30.154 1.00 86.03 C ANISOU 1541 CA ASN A1006 9430 12008 11250 -99 -1122 -1577 C ATOM 1542 C ASN A1006 -5.323 -37.972 29.066 1.00 88.12 C ANISOU 1542 C ASN A1006 9584 12099 11798 361 -1390 -1504 C ATOM 1543 O ASN A1006 -4.956 -39.141 29.175 1.00 87.15 O ANISOU 1543 O ASN A1006 9130 12210 11773 582 -1563 -1441 O ATOM 1544 CB ASN A1006 -5.725 -37.168 31.434 1.00 86.02 C ANISOU 1544 CB ASN A1006 9387 11883 11416 -58 -1098 -1469 C ATOM 1545 CG ASN A1006 -5.050 -36.518 32.615 1.00102.41 C ANISOU 1545 CG ASN A1006 11493 14302 13117 -528 -902 -1561 C ATOM 1546 OD1 ASN A1006 -4.065 -37.030 33.150 1.00104.54 O ANISOU 1546 OD1 ASN A1006 11428 15138 13155 -637 -1025 -1565 O ATOM 1547 ND2 ASN A1006 -5.516 -35.347 33.003 1.00 86.80 N ANISOU 1547 ND2 ASN A1006 9927 12013 11039 -818 -591 -1648 N ATOM 1548 N TRP A1007 -5.992 -37.517 27.994 1.00 84.95 N ANISOU 1548 N TRP A1007 9497 11300 11479 502 -1416 -1518 N ATOM 1549 CA TRP A1007 -6.320 -38.373 26.859 1.00 84.48 C ANISOU 1549 CA TRP A1007 9401 11098 11598 856 -1682 -1504 C ATOM 1550 C TRP A1007 -5.159 -38.423 25.859 1.00 89.51 C ANISOU 1550 C TRP A1007 10086 11988 11934 780 -1631 -1615 C ATOM 1551 O TRP A1007 -4.948 -39.454 25.216 1.00 88.18 O ANISOU 1551 O TRP A1007 9776 11880 11848 1022 -1795 -1630 O ATOM 1552 CB TRP A1007 -7.592 -37.930 26.153 1.00 83.75 C ANISOU 1552 CB TRP A1007 9586 10542 11692 1078 -1807 -1459 C ATOM 1553 CG TRP A1007 -7.921 -38.845 25.022 1.00 85.40 C ANISOU 1553 CG TRP A1007 9761 10662 12028 1372 -2121 -1487 C ATOM 1554 CD1 TRP A1007 -7.739 -38.600 23.694 1.00 89.75 C ANISOU 1554 CD1 TRP A1007 10621 11136 12344 1446 -2207 -1546 C ATOM 1555 CD2 TRP A1007 -8.270 -40.229 25.130 1.00 84.83 C ANISOU 1555 CD2 TRP A1007 9375 10592 12264 1569 -2339 -1488 C ATOM 1556 NE1 TRP A1007 -8.074 -39.712 22.958 1.00 89.74 N ANISOU 1556 NE1 TRP A1007 10517 11088 12493 1675 -2505 -1601 N ATOM 1557 CE2 TRP A1007 -8.398 -40.731 23.817 1.00 90.30 C ANISOU 1557 CE2 TRP A1007 10206 11188 12914 1738 -2573 -1578 C ATOM 1558 CE3 TRP A1007 -8.538 -41.087 26.215 1.00 85.35 C ANISOU 1558 CE3 TRP A1007 9125 10686 12619 1606 -2328 -1422 C ATOM 1559 CZ2 TRP A1007 -8.756 -42.060 23.557 1.00 90.21 C ANISOU 1559 CZ2 TRP A1007 10023 11101 13152 1899 -2779 -1640 C ATOM 1560 CZ3 TRP A1007 -8.901 -42.398 25.958 1.00 87.33 C ANISOU 1560 CZ3 TRP A1007 9219 10831 13133 1792 -2506 -1451 C ATOM 1561 CH2 TRP A1007 -9.009 -42.874 24.644 1.00 89.33 C ANISOU 1561 CH2 TRP A1007 9608 10979 13354 1917 -2723 -1575 C ATOM 1562 N GLU A1008 -4.435 -37.294 25.706 1.00 88.42 N ANISOU 1562 N GLU A1008 10191 11953 11451 419 -1347 -1710 N ATOM 1563 CA GLU A1008 -3.252 -37.194 24.856 1.00 90.11 C ANISOU 1563 CA GLU A1008 10438 12434 11365 253 -1190 -1838 C ATOM 1564 C GLU A1008 -2.246 -38.219 25.358 1.00 93.98 C ANISOU 1564 C GLU A1008 10361 13466 11881 290 -1243 -1856 C ATOM 1565 O GLU A1008 -1.893 -39.130 24.615 1.00 93.79 O ANISOU 1565 O GLU A1008 10207 13517 11910 561 -1332 -1868 O ATOM 1566 CB GLU A1008 -2.684 -35.767 24.893 1.00 93.96 C ANISOU 1566 CB GLU A1008 11261 12934 11504 -247 -800 -1954 C ATOM 1567 CG GLU A1008 -2.626 -35.094 23.534 1.00110.40 C ANISOU 1567 CG GLU A1008 13893 14709 13344 -265 -630 -1997 C ATOM 1568 CD GLU A1008 -1.342 -35.327 22.761 1.00140.72 C ANISOU 1568 CD GLU A1008 17619 18904 16944 -442 -436 -2146 C ATOM 1569 OE1 GLU A1008 -0.302 -34.743 23.146 1.00139.87 O ANISOU 1569 OE1 GLU A1008 17376 19151 16616 -942 -106 -2302 O ATOM 1570 OE2 GLU A1008 -1.381 -36.069 21.752 1.00136.39 O ANISOU 1570 OE2 GLU A1008 17123 18280 16418 -112 -587 -2132 O ATOM 1571 N THR A1009 -1.928 -38.158 26.675 1.00 90.90 N ANISOU 1571 N THR A1009 9657 13413 11467 89 -1217 -1831 N ATOM 1572 CA THR A1009 -1.033 -39.057 27.418 1.00 91.55 C ANISOU 1572 CA THR A1009 9177 14066 11543 174 -1311 -1786 C ATOM 1573 C THR A1009 -1.465 -40.535 27.235 1.00 94.43 C ANISOU 1573 C THR A1009 9379 14272 12227 740 -1552 -1633 C ATOM 1574 O THR A1009 -0.604 -41.404 27.121 1.00 95.84 O ANISOU 1574 O THR A1009 9209 14805 12400 969 -1575 -1604 O ATOM 1575 CB THR A1009 -1.004 -38.630 28.905 1.00 94.70 C ANISOU 1575 CB THR A1009 9430 14724 11826 -119 -1298 -1758 C ATOM 1576 OG1 THR A1009 -0.534 -37.282 28.993 1.00 93.93 O ANISOU 1576 OG1 THR A1009 9533 14744 11411 -708 -1023 -1954 O ATOM 1577 CG2 THR A1009 -0.124 -39.521 29.769 1.00 94.18 C ANISOU 1577 CG2 THR A1009 8798 15293 11695 18 -1455 -1663 C ATOM 1578 N LEU A1010 -2.783 -40.801 27.175 1.00 88.83 N ANISOU 1578 N LEU A1010 8922 13027 11801 956 -1693 -1550 N ATOM 1579 CA LEU A1010 -3.339 -42.145 26.993 1.00 87.85 C ANISOU 1579 CA LEU A1010 8726 12661 11992 1389 -1875 -1453 C ATOM 1580 C LEU A1010 -3.110 -42.649 25.570 1.00 93.17 C ANISOU 1580 C LEU A1010 9541 13200 12660 1586 -1897 -1559 C ATOM 1581 O LEU A1010 -2.773 -43.820 25.389 1.00 93.90 O ANISOU 1581 O LEU A1010 9485 13327 12866 1897 -1923 -1525 O ATOM 1582 CB LEU A1010 -4.842 -42.149 27.316 1.00 85.85 C ANISOU 1582 CB LEU A1010 8655 11916 12048 1454 -1991 -1388 C ATOM 1583 CG LEU A1010 -5.387 -43.413 27.964 1.00 90.05 C ANISOU 1583 CG LEU A1010 9032 12289 12894 1731 -2082 -1256 C ATOM 1584 CD1 LEU A1010 -6.486 -43.079 28.949 1.00 89.28 C ANISOU 1584 CD1 LEU A1010 8978 11944 13001 1630 -2055 -1174 C ATOM 1585 CD2 LEU A1010 -5.896 -44.389 26.929 1.00 92.24 C ANISOU 1585 CD2 LEU A1010 9416 12228 13404 1984 -2214 -1326 C ATOM 1586 N ASN A1011 -3.300 -41.771 24.567 1.00 90.11 N ANISOU 1586 N ASN A1011 9506 12622 12110 1423 -1855 -1680 N ATOM 1587 CA ASN A1011 -3.125 -42.113 23.158 1.00 91.21 C ANISOU 1587 CA ASN A1011 9888 12615 12154 1564 -1864 -1798 C ATOM 1588 C ASN A1011 -1.644 -42.225 22.798 1.00 97.68 C ANISOU 1588 C ASN A1011 10517 13864 12732 1515 -1606 -1880 C ATOM 1589 O ASN A1011 -1.302 -43.059 21.959 1.00 98.64 O ANISOU 1589 O ASN A1011 10686 13937 12854 1755 -1570 -1948 O ATOM 1590 CB ASN A1011 -3.820 -41.096 22.259 1.00 92.89 C ANISOU 1590 CB ASN A1011 10588 12497 12211 1443 -1909 -1855 C ATOM 1591 CG ASN A1011 -4.594 -41.730 21.130 1.00123.45 C ANISOU 1591 CG ASN A1011 14736 16023 16145 1689 -2159 -1919 C ATOM 1592 OD1 ASN A1011 -4.033 -42.101 20.091 1.00125.30 O ANISOU 1592 OD1 ASN A1011 15162 16269 16176 1757 -2090 -2034 O ATOM 1593 ND2 ASN A1011 -5.902 -41.873 21.306 1.00112.59 N ANISOU 1593 ND2 ASN A1011 13379 14358 15042 1803 -2445 -1868 N ATOM 1594 N ASP A1012 -0.772 -41.400 23.436 1.00 95.78 N ANISOU 1594 N ASP A1012 10047 14054 12291 1183 -1405 -1899 N ATOM 1595 CA ASP A1012 0.687 -41.387 23.234 1.00 99.25 C ANISOU 1595 CA ASP A1012 10161 15022 12526 1066 -1143 -1996 C ATOM 1596 C ASP A1012 1.315 -42.731 23.617 1.00106.57 C ANISOU 1596 C ASP A1012 10598 16264 13628 1488 -1194 -1896 C ATOM 1597 O ASP A1012 2.228 -43.195 22.931 1.00108.61 O ANISOU 1597 O ASP A1012 10695 16746 13828 1645 -998 -1971 O ATOM 1598 CB ASP A1012 1.357 -40.260 24.052 1.00102.35 C ANISOU 1598 CB ASP A1012 10342 15850 12696 550 -972 -2061 C ATOM 1599 CG ASP A1012 1.025 -38.829 23.650 1.00113.00 C ANISOU 1599 CG ASP A1012 12220 16900 13814 98 -774 -2173 C ATOM 1600 OD1 ASP A1012 1.246 -37.913 24.478 1.00114.00 O ANISOU 1600 OD1 ASP A1012 12294 17225 13795 -345 -649 -2228 O ATOM 1601 OD2 ASP A1012 0.532 -38.625 22.514 1.00119.10 O ANISOU 1601 OD2 ASP A1012 13507 17221 14523 196 -736 -2200 O ATOM 1602 N ASN A1013 0.822 -43.345 24.716 1.00103.79 N ANISOU 1602 N ASN A1013 10050 15903 13484 1699 -1411 -1712 N ATOM 1603 CA ASN A1013 1.281 -44.633 25.242 1.00106.25 C ANISOU 1603 CA ASN A1013 9985 16431 13956 2169 -1463 -1546 C ATOM 1604 C ASN A1013 0.685 -45.799 24.441 1.00111.74 C ANISOU 1604 C ASN A1013 10991 16581 14885 2590 -1484 -1539 C ATOM 1605 O ASN A1013 1.295 -46.870 24.394 1.00114.62 O ANISOU 1605 O ASN A1013 11159 17051 15340 3019 -1387 -1456 O ATOM 1606 CB ASN A1013 0.956 -44.771 26.736 1.00107.02 C ANISOU 1606 CB ASN A1013 9869 16678 14116 2196 -1645 -1340 C ATOM 1607 CG ASN A1013 1.763 -43.857 27.638 1.00131.70 C ANISOU 1607 CG ASN A1013 12619 20461 16961 1807 -1636 -1360 C ATOM 1608 OD1 ASN A1013 2.998 -43.790 27.575 1.00129.01 O ANISOU 1608 OD1 ASN A1013 11827 20740 16451 1771 -1540 -1414 O ATOM 1609 ND2 ASN A1013 1.079 -43.155 28.527 1.00121.78 N ANISOU 1609 ND2 ASN A1013 11519 19103 15650 1491 -1723 -1335 N ATOM 1610 N LEU A1014 -0.490 -45.593 23.807 1.00106.47 N ANISOU 1610 N LEU A1014 10805 15347 14302 2474 -1604 -1636 N ATOM 1611 CA LEU A1014 -1.116 -46.596 22.942 1.00107.03 C ANISOU 1611 CA LEU A1014 11212 14911 14544 2743 -1648 -1708 C ATOM 1612 C LEU A1014 -0.327 -46.712 21.632 1.00114.54 C ANISOU 1612 C LEU A1014 12329 15898 15292 2809 -1425 -1888 C ATOM 1613 O LEU A1014 -0.205 -47.808 21.081 1.00116.41 O ANISOU 1613 O LEU A1014 12700 15910 15621 3129 -1322 -1936 O ATOM 1614 CB LEU A1014 -2.581 -46.243 22.655 1.00104.68 C ANISOU 1614 CB LEU A1014 11284 14125 14366 2562 -1897 -1776 C ATOM 1615 CG LEU A1014 -3.607 -46.827 23.617 1.00108.21 C ANISOU 1615 CG LEU A1014 11665 14304 15147 2641 -2054 -1647 C ATOM 1616 CD1 LEU A1014 -4.834 -45.959 23.677 1.00106.62 C ANISOU 1616 CD1 LEU A1014 11616 13863 15032 2387 -2259 -1677 C ATOM 1617 CD2 LEU A1014 -3.997 -48.245 23.226 1.00111.68 C ANISOU 1617 CD2 LEU A1014 12271 14348 15815 2910 -2050 -1698 C ATOM 1618 N LYS A1015 0.232 -45.570 21.161 1.00111.75 N ANISOU 1618 N LYS A1015 12011 15801 14649 2485 -1290 -1995 N ATOM 1619 CA LYS A1015 1.059 -45.438 19.956 1.00114.28 C ANISOU 1619 CA LYS A1015 12505 16198 14719 2457 -999 -2170 C ATOM 1620 C LYS A1015 2.427 -46.129 20.122 1.00120.86 C ANISOU 1620 C LYS A1015 12839 17499 15582 2739 -695 -2139 C ATOM 1621 O LYS A1015 3.085 -46.420 19.120 1.00123.41 O ANISOU 1621 O LYS A1015 13291 17817 15781 2852 -396 -2281 O ATOM 1622 CB LYS A1015 1.267 -43.950 19.613 1.00116.87 C ANISOU 1622 CB LYS A1015 13012 16658 14737 1984 -879 -2262 C ATOM 1623 CG LYS A1015 0.123 -43.321 18.829 1.00129.07 C ANISOU 1623 CG LYS A1015 15200 17695 16146 1838 -1077 -2319 C ATOM 1624 CD LYS A1015 0.496 -41.923 18.347 1.00141.23 C ANISOU 1624 CD LYS A1015 17032 19300 17330 1436 -841 -2391 C ATOM 1625 CE LYS A1015 0.258 -41.727 16.865 1.00157.79 C ANISOU 1625 CE LYS A1015 19801 21041 19110 1446 -782 -2507 C ATOM 1626 NZ LYS A1015 1.325 -42.348 16.030 1.00171.46 N ANISOU 1626 NZ LYS A1015 21529 22924 20694 1546 -415 -2656 N ATOM 1627 N VAL A1016 2.852 -46.373 21.384 1.00117.17 N ANISOU 1627 N VAL A1016 11805 17457 15259 2876 -768 -1947 N ATOM 1628 CA VAL A1016 4.118 -47.020 21.750 1.00120.93 C ANISOU 1628 CA VAL A1016 11683 18481 15783 3227 -562 -1852 C ATOM 1629 C VAL A1016 4.081 -48.499 21.302 1.00127.20 C ANISOU 1629 C VAL A1016 12657 18893 16780 3830 -435 -1800 C ATOM 1630 O VAL A1016 5.029 -48.966 20.660 1.00131.49 O ANISOU 1630 O VAL A1016 13049 19611 17299 4111 -93 -1865 O ATOM 1631 CB VAL A1016 4.416 -46.853 23.271 1.00124.52 C ANISOU 1631 CB VAL A1016 11558 19483 16271 3217 -772 -1634 C ATOM 1632 CG1 VAL A1016 5.578 -47.730 23.729 1.00129.45 C ANISOU 1632 CG1 VAL A1016 11547 20669 16971 3741 -657 -1462 C ATOM 1633 CG2 VAL A1016 4.690 -45.392 23.618 1.00123.46 C ANISOU 1633 CG2 VAL A1016 11252 19764 15892 2567 -787 -1755 C ATOM 1634 N ILE A1017 2.971 -49.204 21.605 1.00120.97 N ANISOU 1634 N ILE A1017 12221 17550 16191 3993 -654 -1709 N ATOM 1635 CA ILE A1017 2.744 -50.611 21.254 1.00149.27 C ANISOU 1635 CA ILE A1017 16105 20637 19972 4479 -517 -1685 C ATOM 1636 C ILE A1017 2.647 -50.762 19.719 1.00168.95 C ANISOU 1636 C ILE A1017 19144 22719 22331 4405 -306 -1986 C ATOM 1637 O ILE A1017 3.621 -51.145 19.069 1.00130.07 O ANISOU 1637 O ILE A1017 14151 17934 17337 4671 70 -2060 O ATOM 1638 CB ILE A1017 1.473 -51.142 21.989 1.00149.57 C ANISOU 1638 CB ILE A1017 16404 20181 20246 4493 -788 -1562 C ATOM 1639 CG1 ILE A1017 1.737 -51.335 23.501 1.00150.05 C ANISOU 1639 CG1 ILE A1017 16004 20605 20403 4724 -896 -1225 C ATOM 1640 CG2 ILE A1017 0.934 -52.435 21.367 1.00152.45 C ANISOU 1640 CG2 ILE A1017 17285 19857 20784 4772 -640 -1657 C ATOM 1641 CD1 ILE A1017 1.274 -50.206 24.400 1.00150.63 C ANISOU 1641 CD1 ILE A1017 15886 20952 20394 4270 -1189 -1165 C ATOM 1642 N ASN A1022 10.279 -53.220 23.134 1.00159.45 N ANISOU 1642 N ASN A1022 13519 25567 21497 7561 710 -648 N ATOM 1643 CA ASN A1022 10.601 -54.162 24.205 1.00163.60 C ANISOU 1643 CA ASN A1022 13695 26335 22129 8364 567 -196 C ATOM 1644 C ASN A1022 9.428 -54.284 25.179 1.00162.72 C ANISOU 1644 C ASN A1022 14071 25764 21990 8223 154 6 C ATOM 1645 O ASN A1022 8.816 -53.269 25.523 1.00157.16 O ANISOU 1645 O ASN A1022 13440 25140 21132 7474 -174 -138 O ATOM 1646 CB ASN A1022 11.871 -53.733 24.936 1.00169.04 C ANISOU 1646 CB ASN A1022 13238 28268 22722 8518 396 -41 C ATOM 1647 CG ASN A1022 13.058 -53.581 24.018 1.00195.15 C ANISOU 1647 CG ASN A1022 15956 32098 26093 8622 848 -254 C ATOM 1648 OD1 ASN A1022 13.721 -54.555 23.650 1.00195.06 O ANISOU 1648 OD1 ASN A1022 15776 32061 26277 9456 1239 -104 O ATOM 1649 ND2 ASN A1022 13.328 -52.355 23.600 1.00185.11 N ANISOU 1649 ND2 ASN A1022 14418 31251 24665 7773 870 -617 N ATOM 1650 N ALA A1023 9.121 -55.531 25.620 1.00161.26 N ANISOU 1650 N ALA A1023 14253 25060 21958 8951 236 340 N ATOM 1651 CA ALA A1023 8.014 -55.882 26.528 1.00157.32 C ANISOU 1651 CA ALA A1023 14285 24018 21471 8916 -30 560 C ATOM 1652 C ALA A1023 8.102 -55.181 27.894 1.00159.86 C ANISOU 1652 C ALA A1023 14095 25086 21561 8693 -535 788 C ATOM 1653 O ALA A1023 7.067 -54.916 28.513 1.00154.21 O ANISOU 1653 O ALA A1023 13791 24003 20797 8278 -778 809 O ATOM 1654 CB ALA A1023 7.961 -57.386 26.729 1.00162.95 C ANISOU 1654 CB ALA A1023 15424 24122 22368 9817 265 901 C ATOM 1655 N ALA A1024 9.330 -54.886 28.358 1.00161.73 N ANISOU 1655 N ALA A1024 13422 26385 21643 8947 -682 936 N ATOM 1656 CA ALA A1024 9.579 -54.184 29.618 1.00162.05 C ANISOU 1656 CA ALA A1024 12913 27270 21387 8698 -1178 1106 C ATOM 1657 C ALA A1024 9.068 -52.737 29.532 1.00158.31 C ANISOU 1657 C ALA A1024 12486 26910 20753 7586 -1377 702 C ATOM 1658 O ALA A1024 8.401 -52.267 30.454 1.00154.03 O ANISOU 1658 O ALA A1024 12131 26355 20037 7191 -1693 767 O ATOM 1659 CB ALA A1024 11.069 -54.208 29.942 1.00171.25 C ANISOU 1659 CB ALA A1024 13022 29608 22436 9188 -1280 1285 C ATOM 1660 N GLN A1025 9.353 -52.061 28.397 1.00153.24 N ANISOU 1660 N GLN A1025 11759 26303 20164 7115 -1130 297 N ATOM 1661 CA GLN A1025 8.960 -50.684 28.097 1.00147.73 C ANISOU 1661 CA GLN A1025 11177 25634 19320 6120 -1206 -92 C ATOM 1662 C GLN A1025 7.441 -50.567 27.878 1.00144.44 C ANISOU 1662 C GLN A1025 11681 24201 18998 5747 -1228 -200 C ATOM 1663 O GLN A1025 6.882 -49.485 28.079 1.00139.59 O ANISOU 1663 O GLN A1025 11229 23565 18243 5029 -1388 -390 O ATOM 1664 CB GLN A1025 9.722 -50.173 26.864 1.00150.68 C ANISOU 1664 CB GLN A1025 11297 26236 19717 5849 -848 -441 C ATOM 1665 N VAL A1026 6.782 -51.677 27.473 1.00140.41 N ANISOU 1665 N VAL A1026 11756 22862 18731 6230 -1048 -92 N ATOM 1666 CA VAL A1026 5.331 -51.746 27.255 1.00134.52 C ANISOU 1666 CA VAL A1026 11801 21188 18122 5935 -1075 -194 C ATOM 1667 C VAL A1026 4.625 -51.667 28.619 1.00137.48 C ANISOU 1667 C VAL A1026 12263 21541 18434 5836 -1379 48 C ATOM 1668 O VAL A1026 3.646 -50.933 28.754 1.00132.14 O ANISOU 1668 O VAL A1026 11907 20553 17748 5267 -1514 -101 O ATOM 1669 CB VAL A1026 4.925 -53.013 26.452 1.00139.39 C ANISOU 1669 CB VAL A1026 12982 20982 18998 6424 -768 -191 C ATOM 1670 CG1 VAL A1026 3.410 -53.196 26.406 1.00134.27 C ANISOU 1670 CG1 VAL A1026 13041 19468 18508 6120 -845 -281 C ATOM 1671 CG2 VAL A1026 5.496 -52.971 25.038 1.00140.83 C ANISOU 1671 CG2 VAL A1026 13203 21117 19190 6416 -440 -487 C ATOM 1672 N LYS A1027 5.153 -52.398 29.629 1.00139.38 N ANISOU 1672 N LYS A1027 12219 22134 18606 6421 -1469 435 N ATOM 1673 CA LYS A1027 4.643 -52.439 31.007 1.00138.85 C ANISOU 1673 CA LYS A1027 12245 22106 18405 6420 -1722 718 C ATOM 1674 C LYS A1027 4.668 -51.046 31.662 1.00139.76 C ANISOU 1674 C LYS A1027 12060 22817 18224 5696 -2012 566 C ATOM 1675 O LYS A1027 3.737 -50.706 32.389 1.00135.77 O ANISOU 1675 O LYS A1027 11899 22017 17672 5355 -2129 594 O ATOM 1676 CB LYS A1027 5.455 -53.438 31.849 1.00148.44 C ANISOU 1676 CB LYS A1027 13163 23723 19514 7262 -1769 1184 C ATOM 1677 N ASP A1028 5.720 -50.243 31.385 1.00138.52 N ANISOU 1677 N ASP A1028 11291 23462 17879 5430 -2068 379 N ATOM 1678 CA ASP A1028 5.880 -48.882 31.903 1.00137.19 C ANISOU 1678 CA ASP A1028 10853 23864 17407 4674 -2272 171 C ATOM 1679 C ASP A1028 4.928 -47.923 31.191 1.00134.10 C ANISOU 1679 C ASP A1028 10972 22866 17112 3977 -2140 -182 C ATOM 1680 O ASP A1028 4.503 -46.943 31.800 1.00131.41 O ANISOU 1680 O ASP A1028 10746 22598 16586 3394 -2258 -295 O ATOM 1681 CB ASP A1028 7.338 -48.398 31.773 1.00144.70 C ANISOU 1681 CB ASP A1028 10968 25856 18153 4577 -2318 51 C ATOM 1682 CG ASP A1028 8.272 -48.897 32.867 1.00162.91 C ANISOU 1682 CG ASP A1028 12624 29058 20215 5068 -2620 388 C ATOM 1683 OD1 ASP A1028 7.971 -48.664 34.059 1.00163.90 O ANISOU 1683 OD1 ASP A1028 12819 29397 20059 4902 -2917 537 O ATOM 1684 OD2 ASP A1028 9.328 -49.480 32.528 1.00174.63 O ANISOU 1684 OD2 ASP A1028 13516 31070 21765 5623 -2558 498 O ATOM 1685 N ALA A1029 4.579 -48.215 29.917 1.00128.01 N ANISOU 1685 N ALA A1029 10545 21488 16604 4067 -1895 -344 N ATOM 1686 CA ALA A1029 3.636 -47.421 29.117 1.00122.43 C ANISOU 1686 CA ALA A1029 10354 20182 15982 3536 -1801 -632 C ATOM 1687 C ALA A1029 2.189 -47.741 29.508 1.00121.83 C ANISOU 1687 C ALA A1029 10832 19351 16106 3544 -1878 -535 C ATOM 1688 O ALA A1029 1.375 -46.821 29.601 1.00118.07 O ANISOU 1688 O ALA A1029 10629 18625 15609 3052 -1925 -676 O ATOM 1689 CB ALA A1029 3.847 -47.678 27.631 1.00123.27 C ANISOU 1689 CB ALA A1029 10624 19991 16223 3656 -1548 -829 C ATOM 1690 N LEU A1030 1.879 -49.041 29.746 1.00119.00 N ANISOU 1690 N LEU A1030 10638 18622 15953 4105 -1848 -296 N ATOM 1691 CA LEU A1030 0.559 -49.544 30.146 1.00116.04 C ANISOU 1691 CA LEU A1030 10742 17538 15810 4134 -1859 -201 C ATOM 1692 C LEU A1030 0.141 -49.013 31.531 1.00119.07 C ANISOU 1692 C LEU A1030 11108 18098 16036 3879 -2008 -54 C ATOM 1693 O LEU A1030 -1.044 -48.745 31.740 1.00115.78 O ANISOU 1693 O LEU A1030 11035 17180 15777 3599 -2000 -113 O ATOM 1694 CB LEU A1030 0.540 -51.079 30.143 1.00119.03 C ANISOU 1694 CB LEU A1030 11308 17521 16395 4778 -1711 25 C ATOM 1695 N THR A1031 1.109 -48.850 32.462 1.00118.38 N ANISOU 1695 N THR A1031 10606 18750 15624 3969 -2143 122 N ATOM 1696 CA THR A1031 0.853 -48.323 33.809 1.00118.00 C ANISOU 1696 CA THR A1031 10565 18948 15320 3703 -2286 243 C ATOM 1697 C THR A1031 0.807 -46.789 33.783 1.00118.68 C ANISOU 1697 C THR A1031 10601 19281 15211 2972 -2321 -63 C ATOM 1698 O THR A1031 0.295 -46.178 34.723 1.00117.41 O ANISOU 1698 O THR A1031 10606 19115 14889 2628 -2358 -55 O ATOM 1699 CB THR A1031 1.871 -48.842 34.827 1.00132.13 C ANISOU 1699 CB THR A1031 11971 21446 16784 4117 -2464 565 C ATOM 1700 OG1 THR A1031 3.196 -48.489 34.419 1.00135.99 O ANISOU 1700 OG1 THR A1031 11852 22736 17081 4118 -2560 459 O ATOM 1701 CG2 THR A1031 1.742 -50.345 35.071 1.00133.39 C ANISOU 1701 CG2 THR A1031 12348 21223 17110 4873 -2372 936 C ATOM 1702 N LYS A1032 1.338 -46.173 32.712 1.00114.27 N ANISOU 1702 N LYS A1032 9878 18889 14651 2736 -2251 -330 N ATOM 1703 CA LYS A1032 1.290 -44.725 32.505 1.00112.14 C ANISOU 1703 CA LYS A1032 9671 18725 14213 2053 -2195 -629 C ATOM 1704 C LYS A1032 -0.102 -44.354 31.959 1.00109.88 C ANISOU 1704 C LYS A1032 9932 17608 14207 1872 -2081 -747 C ATOM 1705 O LYS A1032 -0.643 -43.301 32.307 1.00107.70 O ANISOU 1705 O LYS A1032 9883 17201 13838 1414 -2025 -871 O ATOM 1706 CB LYS A1032 2.405 -44.263 31.548 1.00116.92 C ANISOU 1706 CB LYS A1032 9935 19790 14699 1884 -2103 -849 C ATOM 1707 CG LYS A1032 3.673 -43.757 32.236 1.00132.94 C ANISOU 1707 CG LYS A1032 11383 22781 16348 1612 -2206 -901 C ATOM 1708 CD LYS A1032 4.671 -43.131 31.239 1.00143.00 C ANISOU 1708 CD LYS A1032 12347 24450 17536 1299 -2020 -1183 C ATOM 1709 CE LYS A1032 5.595 -44.130 30.569 1.00152.46 C ANISOU 1709 CE LYS A1032 13089 25965 18872 1876 -1972 -1087 C ATOM 1710 NZ LYS A1032 6.561 -43.475 29.648 1.00160.64 N ANISOU 1710 NZ LYS A1032 13817 27398 19822 1518 -1725 -1378 N ATOM 1711 N MET A1033 -0.679 -45.245 31.115 1.00103.65 N ANISOU 1711 N MET A1033 9349 16275 13758 2247 -2044 -713 N ATOM 1712 CA MET A1033 -2.011 -45.102 30.524 1.00 99.27 C ANISOU 1712 CA MET A1033 9218 15004 13499 2157 -2007 -813 C ATOM 1713 C MET A1033 -3.085 -45.239 31.615 1.00100.47 C ANISOU 1713 C MET A1033 9551 14827 13797 2130 -2011 -670 C ATOM 1714 O MET A1033 -4.051 -44.476 31.600 1.00 97.63 O ANISOU 1714 O MET A1033 9422 14122 13551 1855 -1969 -772 O ATOM 1715 CB MET A1033 -2.231 -46.132 29.398 1.00101.46 C ANISOU 1715 CB MET A1033 9629 14878 14043 2522 -1990 -846 C ATOM 1716 N ARG A1034 -2.889 -46.179 32.579 1.00 98.27 N ANISOU 1716 N ARG A1034 9179 14663 13496 2440 -2030 -417 N ATOM 1717 CA ARG A1034 -3.796 -46.428 33.713 1.00 97.42 C ANISOU 1717 CA ARG A1034 9271 14263 13482 2432 -1970 -252 C ATOM 1718 C ARG A1034 -3.948 -45.182 34.594 1.00101.16 C ANISOU 1718 C ARG A1034 9794 14948 13693 1967 -1937 -320 C ATOM 1719 O ARG A1034 -5.069 -44.830 34.959 1.00 99.66 O ANISOU 1719 O ARG A1034 9850 14325 13690 1786 -1810 -350 O ATOM 1720 CB ARG A1034 -3.314 -47.611 34.566 1.00 99.17 C ANISOU 1720 CB ARG A1034 9434 14639 13607 2881 -1979 68 C ATOM 1721 N ALA A1035 -2.826 -44.509 34.906 1.00 99.05 N ANISOU 1721 N ALA A1035 9287 15347 13003 1750 -2023 -373 N ATOM 1722 CA ALA A1035 -2.774 -43.299 35.723 1.00 99.00 C ANISOU 1722 CA ALA A1035 9358 15594 12664 1238 -1969 -491 C ATOM 1723 C ALA A1035 -3.480 -42.133 35.058 1.00100.07 C ANISOU 1723 C ALA A1035 9760 15326 12936 858 -1802 -743 C ATOM 1724 O ALA A1035 -4.166 -41.374 35.738 1.00 99.35 O ANISOU 1724 O ALA A1035 9938 15014 12798 563 -1640 -795 O ATOM 1725 CB ALA A1035 -1.336 -42.927 35.983 1.00103.25 C ANISOU 1725 CB ALA A1035 9515 16973 12744 1053 -2116 -549 C ATOM 1726 N ALA A1036 -3.294 -41.977 33.735 1.00 95.37 N ANISOU 1726 N ALA A1036 9131 14627 12479 894 -1813 -885 N ATOM 1727 CA ALA A1036 -3.914 -40.912 32.952 1.00 93.10 C ANISOU 1727 CA ALA A1036 9136 13949 12289 632 -1675 -1077 C ATOM 1728 C ALA A1036 -5.429 -41.105 32.888 1.00 93.68 C ANISOU 1728 C ALA A1036 9452 13358 12785 812 -1630 -1016 C ATOM 1729 O ALA A1036 -6.157 -40.117 32.975 1.00 92.80 O ANISOU 1729 O ALA A1036 9599 12945 12715 597 -1471 -1096 O ATOM 1730 CB ALA A1036 -3.323 -40.874 31.553 1.00 93.74 C ANISOU 1730 CB ALA A1036 9160 14090 12369 690 -1710 -1204 C ATOM 1731 N ALA A1037 -5.898 -42.374 32.790 1.00 88.56 N ANISOU 1731 N ALA A1037 8711 12485 12453 1196 -1735 -880 N ATOM 1732 CA ALA A1037 -7.320 -42.740 32.738 1.00 86.68 C ANISOU 1732 CA ALA A1037 8595 11681 12660 1336 -1702 -847 C ATOM 1733 C ALA A1037 -8.055 -42.366 34.032 1.00 89.97 C ANISOU 1733 C ALA A1037 9132 11945 13108 1176 -1495 -770 C ATOM 1734 O ALA A1037 -9.199 -41.918 33.965 1.00 88.69 O ANISOU 1734 O ALA A1037 9076 11381 13243 1137 -1383 -817 O ATOM 1735 CB ALA A1037 -7.476 -44.228 32.467 1.00 87.79 C ANISOU 1735 CB ALA A1037 8637 11649 13068 1687 -1797 -750 C ATOM 1736 N LEU A1038 -7.390 -42.527 35.194 1.00 87.76 N ANISOU 1736 N LEU A1038 8832 12013 12501 1100 -1442 -650 N ATOM 1737 CA LEU A1038 -7.940 -42.204 36.520 1.00 88.24 C ANISOU 1737 CA LEU A1038 9076 11972 12480 923 -1213 -578 C ATOM 1738 C LEU A1038 -7.993 -40.692 36.746 1.00 90.75 C ANISOU 1738 C LEU A1038 9605 12304 12571 519 -1026 -753 C ATOM 1739 O LEU A1038 -8.925 -40.211 37.386 1.00 89.99 O ANISOU 1739 O LEU A1038 9721 11866 12604 406 -757 -762 O ATOM 1740 CB LEU A1038 -7.126 -42.880 37.636 1.00 90.89 C ANISOU 1740 CB LEU A1038 9369 12727 12438 994 -1269 -382 C ATOM 1741 CG LEU A1038 -7.077 -44.414 37.611 1.00 96.60 C ANISOU 1741 CG LEU A1038 9998 13357 13349 1443 -1362 -155 C ATOM 1742 CD1 LEU A1038 -5.843 -44.933 38.320 1.00 99.90 C ANISOU 1742 CD1 LEU A1038 10289 14372 13297 1612 -1532 45 C ATOM 1743 CD2 LEU A1038 -8.344 -45.032 38.189 1.00 99.90 C ANISOU 1743 CD2 LEU A1038 10621 13203 14131 1527 -1108 -43 C ATOM 1744 N ASP A1039 -6.999 -39.953 36.224 1.00 87.92 N ANISOU 1744 N ASP A1039 9214 12308 11885 291 -1109 -901 N ATOM 1745 CA ASP A1039 -6.932 -38.491 36.299 1.00 89.04 C ANISOU 1745 CA ASP A1039 9632 12416 11782 -134 -882 -1096 C ATOM 1746 C ASP A1039 -7.903 -37.865 35.270 1.00 91.14 C ANISOU 1746 C ASP A1039 10081 12132 12417 -15 -775 -1164 C ATOM 1747 O ASP A1039 -8.377 -36.748 35.488 1.00 91.83 O ANISOU 1747 O ASP A1039 10495 11936 12460 -225 -483 -1255 O ATOM 1748 CB ASP A1039 -5.487 -37.983 36.079 1.00 93.27 C ANISOU 1748 CB ASP A1039 10054 13542 11843 -472 -972 -1249 C ATOM 1749 CG ASP A1039 -4.566 -38.049 37.296 1.00111.18 C ANISOU 1749 CG ASP A1039 12202 16425 13618 -752 -1038 -1247 C ATOM 1750 OD1 ASP A1039 -4.258 -39.178 37.755 1.00112.85 O ANISOU 1750 OD1 ASP A1039 12143 16928 13807 -437 -1267 -1040 O ATOM 1751 OD2 ASP A1039 -4.099 -36.976 37.748 1.00119.91 O ANISOU 1751 OD2 ASP A1039 13495 17740 14327 -1288 -871 -1457 O ATOM 1752 N ALA A1040 -8.192 -38.582 34.151 1.00 85.38 N ANISOU 1752 N ALA A1040 9167 11254 12019 341 -1010 -1116 N ATOM 1753 CA ALA A1040 -9.145 -38.138 33.123 1.00 83.76 C ANISOU 1753 CA ALA A1040 9082 10603 12140 526 -1017 -1149 C ATOM 1754 C ALA A1040 -10.585 -38.399 33.580 1.00 86.71 C ANISOU 1754 C ALA A1040 9411 10557 12979 729 -916 -1062 C ATOM 1755 O ALA A1040 -11.494 -37.662 33.189 1.00 86.97 O ANISOU 1755 O ALA A1040 9566 10242 13236 833 -816 -1078 O ATOM 1756 CB ALA A1040 -8.881 -38.848 31.807 1.00 83.32 C ANISOU 1756 CB ALA A1040 8864 10601 12191 776 -1326 -1162 C ATOM 1757 N GLN A1041 -10.780 -39.459 34.404 1.00 82.04 N ANISOU 1757 N GLN A1041 8637 10003 12532 807 -919 -957 N ATOM 1758 CA GLN A1041 -12.064 -39.877 34.978 1.00 81.58 C ANISOU 1758 CA GLN A1041 8492 9584 12920 935 -757 -886 C ATOM 1759 C GLN A1041 -12.611 -38.824 35.938 1.00 85.22 C ANISOU 1759 C GLN A1041 9203 9844 13334 754 -348 -902 C ATOM 1760 O GLN A1041 -13.827 -38.637 35.999 1.00 85.81 O ANISOU 1760 O GLN A1041 9210 9558 13836 890 -171 -891 O ATOM 1761 CB GLN A1041 -11.909 -41.223 35.718 1.00 82.91 C ANISOU 1761 CB GLN A1041 8533 9836 13131 1006 -774 -757 C ATOM 1762 CG GLN A1041 -13.227 -41.897 36.102 1.00 88.58 C ANISOU 1762 CG GLN A1041 9126 10159 14373 1115 -599 -707 C ATOM 1763 CD GLN A1041 -13.036 -43.275 36.679 1.00101.48 C ANISOU 1763 CD GLN A1041 10731 11794 16032 1201 -581 -567 C ATOM 1764 OE1 GLN A1041 -13.296 -44.287 36.025 1.00 97.27 O ANISOU 1764 OE1 GLN A1041 10040 11116 15801 1355 -733 -578 O ATOM 1765 NE2 GLN A1041 -12.595 -43.352 37.924 1.00 93.90 N ANISOU 1765 NE2 GLN A1041 9979 10973 14727 1101 -377 -432 N ATOM 1766 N LYS A1042 -11.719 -38.132 36.675 1.00 81.21 N ANISOU 1766 N LYS A1042 8967 9583 12308 433 -184 -949 N ATOM 1767 CA LYS A1042 -12.114 -37.142 37.668 1.00 82.69 C ANISOU 1767 CA LYS A1042 9491 9570 12358 200 257 -1000 C ATOM 1768 C LYS A1042 -12.571 -35.776 37.037 1.00 87.85 C ANISOU 1768 C LYS A1042 10405 9887 13086 206 471 -1099 C ATOM 1769 O LYS A1042 -12.912 -34.857 37.794 1.00 89.83 O ANISOU 1769 O LYS A1042 11007 9896 13229 29 909 -1159 O ATOM 1770 CB LYS A1042 -11.020 -36.959 38.749 1.00 86.12 C ANISOU 1770 CB LYS A1042 10144 10415 12163 -200 337 -1045 C ATOM 1771 CG LYS A1042 -9.715 -36.320 38.303 1.00100.60 C ANISOU 1771 CG LYS A1042 12052 12664 13508 -507 182 -1192 C ATOM 1772 N ALA A1043 -12.664 -35.677 35.680 1.00 82.98 N ANISOU 1772 N ALA A1043 9669 9205 12655 450 199 -1099 N ATOM 1773 CA ALA A1043 -13.129 -34.472 34.974 1.00 84.07 C ANISOU 1773 CA ALA A1043 10085 9000 12856 570 366 -1128 C ATOM 1774 C ALA A1043 -14.654 -34.269 35.153 1.00 91.83 C ANISOU 1774 C ALA A1043 10961 9548 14384 920 586 -1040 C ATOM 1775 O ALA A1043 -15.067 -33.260 35.723 1.00 95.06 O ANISOU 1775 O ALA A1043 11714 9640 14763 877 1051 -1059 O ATOM 1776 CB ALA A1043 -12.771 -34.545 33.496 1.00 83.39 C ANISOU 1776 CB ALA A1043 9926 9008 12750 754 -21 -1125 C ATOM 1777 N THR A1044 -15.474 -35.254 34.724 1.00 88.28 N ANISOU 1777 N THR A1044 10018 9093 14432 1237 291 -964 N ATOM 1778 CA THR A1044 -16.950 -35.310 34.794 1.00114.93 C ANISOU 1778 CA THR A1044 13078 12178 18412 1572 412 -897 C ATOM 1779 C THR A1044 -17.600 -34.033 34.246 1.00136.54 C ANISOU 1779 C THR A1044 16017 14600 21261 1887 581 -844 C ATOM 1780 O THR A1044 -17.622 -33.821 33.036 1.00 94.75 O ANISOU 1780 O THR A1044 10698 9337 15968 2145 225 -803 O ATOM 1781 CB THR A1044 -17.454 -35.614 36.217 1.00123.22 C ANISOU 1781 CB THR A1044 14092 13100 19625 1418 859 -891 C ATOM 1782 OG1 THR A1044 -17.068 -34.559 37.101 1.00124.98 O ANISOU 1782 OG1 THR A1044 14855 13178 19455 1168 1352 -939 O ATOM 1783 CG2 THR A1044 -16.974 -36.972 36.743 1.00118.30 C ANISOU 1783 CG2 THR A1044 13287 12730 18933 1213 699 -882 C ATOM 1784 N PRO A1053 -25.950 -33.408 45.351 1.00174.30 N ANISOU 1784 N PRO A1053 20763 16634 28830 1708 7128 -968 N ATOM 1785 CA PRO A1053 -25.301 -33.488 44.035 1.00169.42 C ANISOU 1785 CA PRO A1053 19905 16355 28111 1848 6227 -917 C ATOM 1786 C PRO A1053 -25.137 -34.945 43.572 1.00169.62 C ANISOU 1786 C PRO A1053 19390 16756 28302 1693 5587 -887 C ATOM 1787 O PRO A1053 -24.040 -35.517 43.647 1.00165.62 O ANISOU 1787 O PRO A1053 19215 16491 27223 1358 5194 -880 O ATOM 1788 CB PRO A1053 -23.962 -32.770 44.250 1.00168.23 C ANISOU 1788 CB PRO A1053 20641 16223 27055 1518 6151 -976 C ATOM 1789 CG PRO A1053 -23.694 -32.866 45.721 1.00174.34 C ANISOU 1789 CG PRO A1053 22038 16855 27350 1061 6752 -1055 C ATOM 1790 CD PRO A1053 -24.978 -33.194 46.441 1.00174.83 C ANISOU 1790 CD PRO A1053 21771 16630 28028 1200 7436 -1042 C ATOM 1791 N ASP A1054 -26.248 -35.537 43.066 1.00167.18 N ANISOU 1791 N ASP A1054 18221 16504 28796 1947 5492 -879 N ATOM 1792 CA ASP A1054 -26.330 -36.917 42.563 1.00164.17 C ANISOU 1792 CA ASP A1054 17279 16399 28699 1800 4976 -893 C ATOM 1793 C ASP A1054 -25.393 -37.153 41.346 1.00161.01 C ANISOU 1793 C ASP A1054 16864 16337 27974 1837 4071 -873 C ATOM 1794 O ASP A1054 -24.818 -36.197 40.809 1.00159.01 O ANISOU 1794 O ASP A1054 16938 16113 27365 2014 3848 -842 O ATOM 1795 CB ASP A1054 -27.784 -37.259 42.200 1.00170.97 C ANISOU 1795 CB ASP A1054 17186 17272 30502 2042 5084 -945 C ATOM 1796 N SER A1055 -25.249 -38.427 40.908 1.00153.80 N ANISOU 1796 N SER A1055 15618 15638 27182 1658 3614 -901 N ATOM 1797 CA SER A1055 -24.362 -38.763 39.794 1.00148.08 C ANISOU 1797 CA SER A1055 14902 15211 26150 1677 2828 -899 C ATOM 1798 C SER A1055 -25.066 -39.396 38.530 1.00150.10 C ANISOU 1798 C SER A1055 14384 15677 26972 1848 2252 -982 C ATOM 1799 O SER A1055 -24.467 -40.291 37.923 1.00147.52 O ANISOU 1799 O SER A1055 14046 15529 26476 1699 1758 -1020 O ATOM 1800 CB SER A1055 -23.243 -39.680 40.283 1.00148.05 C ANISOU 1800 CB SER A1055 15354 15299 25598 1327 2716 -859 C ATOM 1801 N PRO A1056 -26.247 -38.935 38.030 1.00147.75 N ANISOU 1801 N PRO A1056 13448 15403 27286 2176 2243 -1017 N ATOM 1802 CA PRO A1056 -26.779 -39.536 36.792 1.00147.59 C ANISOU 1802 CA PRO A1056 12736 15673 27669 2281 1587 -1121 C ATOM 1803 C PRO A1056 -26.211 -38.832 35.557 1.00144.30 C ANISOU 1803 C PRO A1056 12482 15456 26891 2608 944 -1057 C ATOM 1804 O PRO A1056 -25.939 -37.628 35.624 1.00143.36 O ANISOU 1804 O PRO A1056 12771 15208 26490 2886 1119 -929 O ATOM 1805 CB PRO A1056 -28.294 -39.342 36.920 1.00156.67 C ANISOU 1805 CB PRO A1056 13082 16828 29618 2489 1880 -1178 C ATOM 1806 CG PRO A1056 -28.489 -38.284 37.991 1.00163.52 C ANISOU 1806 CG PRO A1056 14305 17373 30451 2666 2657 -1061 C ATOM 1807 CD PRO A1056 -27.145 -37.868 38.517 1.00153.82 C ANISOU 1807 CD PRO A1056 14074 15971 28399 2493 2798 -967 C ATOM 1808 N GLU A1057 -26.009 -39.580 34.440 1.00135.94 N ANISOU 1808 N GLU A1057 11184 14665 25800 2548 252 -1155 N ATOM 1809 CA GLU A1057 -25.442 -39.097 33.160 1.00132.17 C ANISOU 1809 CA GLU A1057 10891 14388 24938 2811 -392 -1109 C ATOM 1810 C GLU A1057 -23.898 -39.055 33.236 1.00124.59 C ANISOU 1810 C GLU A1057 10728 13380 23231 2609 -424 -1053 C ATOM 1811 O GLU A1057 -23.232 -39.473 32.289 1.00121.00 O ANISOU 1811 O GLU A1057 10394 13107 22476 2565 -942 -1104 O ATOM 1812 CB GLU A1057 -26.030 -37.718 32.748 1.00137.40 C ANISOU 1812 CB GLU A1057 11466 15036 25703 3373 -398 -957 C ATOM 1813 CG GLU A1057 -25.400 -37.043 31.537 1.00148.21 C ANISOU 1813 CG GLU A1057 13202 16525 26588 3672 -935 -859 C ATOM 1814 CD GLU A1057 -25.828 -37.585 30.187 1.00176.92 C ANISOU 1814 CD GLU A1057 16344 20524 30353 3807 -1721 -948 C ATOM 1815 OE1 GLU A1057 -27.037 -37.505 29.869 1.00181.53 O ANISOU 1815 OE1 GLU A1057 16209 21299 31466 4106 -1911 -957 O ATOM 1816 OE2 GLU A1057 -24.946 -38.053 29.431 1.00169.55 O ANISOU 1816 OE2 GLU A1057 15739 19709 28971 3623 -2147 -1015 O ATOM 1817 N MET A1058 -23.339 -38.554 34.356 1.00116.36 N ANISOU 1817 N MET A1058 10203 12123 21884 2473 133 -968 N ATOM 1818 CA MET A1058 -21.894 -38.474 34.572 1.00110.00 C ANISOU 1818 CA MET A1058 10060 11348 20388 2247 131 -931 C ATOM 1819 C MET A1058 -21.346 -39.853 34.916 1.00107.22 C ANISOU 1819 C MET A1058 9715 11078 19945 1911 58 -987 C ATOM 1820 O MET A1058 -20.150 -40.079 34.746 1.00103.50 O ANISOU 1820 O MET A1058 9608 10749 18967 1783 -139 -970 O ATOM 1821 CB MET A1058 -21.509 -37.416 35.633 1.00112.44 C ANISOU 1821 CB MET A1058 10916 11447 20360 2177 714 -857 C ATOM 1822 CG MET A1058 -22.009 -37.701 37.038 1.00118.43 C ANISOU 1822 CG MET A1058 11673 12005 21321 1979 1328 -857 C ATOM 1823 SD MET A1058 -22.224 -36.195 38.035 1.00125.71 S ANISOU 1823 SD MET A1058 13088 12591 22087 2046 2067 -813 S ATOM 1824 CE MET A1058 -23.901 -35.709 37.555 1.00128.16 C ANISOU 1824 CE MET A1058 12728 12746 23220 2571 2189 -780 C ATOM 1825 N LYS A1059 -22.224 -40.782 35.360 1.00103.41 N ANISOU 1825 N LYS A1059 8824 10500 19968 1784 239 -1051 N ATOM 1826 CA LYS A1059 -21.875 -42.179 35.651 1.00100.91 C ANISOU 1826 CA LYS A1059 8537 10168 19636 1505 229 -1089 C ATOM 1827 C LYS A1059 -21.466 -42.896 34.352 1.00100.48 C ANISOU 1827 C LYS A1059 8366 10301 19511 1523 -391 -1193 C ATOM 1828 O LYS A1059 -20.635 -43.799 34.396 1.00 97.47 O ANISOU 1828 O LYS A1059 8242 9934 18860 1383 -468 -1182 O ATOM 1829 CB LYS A1059 -23.042 -42.911 36.331 1.00107.22 C ANISOU 1829 CB LYS A1059 8937 10763 21039 1336 632 -1158 C ATOM 1830 N ASP A1060 -22.030 -42.459 33.200 1.00 97.25 N ANISOU 1830 N ASP A1060 7610 10035 19305 1734 -822 -1281 N ATOM 1831 CA ASP A1060 -21.733 -42.968 31.864 1.00 96.09 C ANISOU 1831 CA ASP A1060 7392 10073 19045 1764 -1422 -1402 C ATOM 1832 C ASP A1060 -20.330 -42.534 31.415 1.00 96.32 C ANISOU 1832 C ASP A1060 7966 10223 18408 1844 -1617 -1316 C ATOM 1833 O ASP A1060 -19.636 -43.340 30.791 1.00 95.31 O ANISOU 1833 O ASP A1060 7977 10174 18062 1760 -1891 -1391 O ATOM 1834 CB ASP A1060 -22.793 -42.513 30.854 1.00101.74 C ANISOU 1834 CB ASP A1060 7597 10950 20108 1993 -1830 -1494 C ATOM 1835 CG ASP A1060 -22.486 -42.855 29.408 1.00112.33 C ANISOU 1835 CG ASP A1060 8953 12502 21225 2041 -2478 -1619 C ATOM 1836 OD1 ASP A1060 -22.026 -43.992 29.147 1.00111.71 O ANISOU 1836 OD1 ASP A1060 8987 12400 21058 1784 -2597 -1757 O ATOM 1837 OD2 ASP A1060 -22.708 -41.991 28.537 1.00121.82 O ANISOU 1837 OD2 ASP A1060 10108 13864 22314 2354 -2838 -1572 O ATOM 1838 N PHE A1061 -19.916 -41.270 31.709 1.00 90.94 N ANISOU 1838 N PHE A1061 7598 9540 17413 1983 -1435 -1180 N ATOM 1839 CA PHE A1061 -18.563 -40.760 31.410 1.00 86.68 C ANISOU 1839 CA PHE A1061 7558 9126 16250 1975 -1523 -1121 C ATOM 1840 C PHE A1061 -17.550 -41.551 32.270 1.00 87.12 C ANISOU 1840 C PHE A1061 7850 9230 16020 1735 -1317 -1083 C ATOM 1841 O PHE A1061 -16.574 -42.089 31.742 1.00 84.48 O ANISOU 1841 O PHE A1061 7666 9057 15376 1703 -1549 -1107 O ATOM 1842 CB PHE A1061 -18.471 -39.229 31.672 1.00 88.45 C ANISOU 1842 CB PHE A1061 8088 9270 16247 2095 -1266 -1018 C ATOM 1843 CG PHE A1061 -17.072 -38.632 31.692 1.00 86.57 C ANISOU 1843 CG PHE A1061 8365 9148 15378 1950 -1198 -989 C ATOM 1844 CD1 PHE A1061 -16.393 -38.445 32.891 1.00 87.57 C ANISOU 1844 CD1 PHE A1061 8763 9293 15218 1691 -811 -956 C ATOM 1845 CD2 PHE A1061 -16.442 -38.251 30.513 1.00 87.11 C ANISOU 1845 CD2 PHE A1061 8643 9335 15121 2038 -1513 -1010 C ATOM 1846 CE1 PHE A1061 -15.093 -37.930 32.904 1.00 86.20 C ANISOU 1846 CE1 PHE A1061 8969 9309 14475 1492 -777 -970 C ATOM 1847 CE2 PHE A1061 -15.157 -37.704 30.531 1.00 87.46 C ANISOU 1847 CE2 PHE A1061 9104 9507 14619 1843 -1401 -1015 C ATOM 1848 CZ PHE A1061 -14.490 -37.549 31.726 1.00 84.38 C ANISOU 1848 CZ PHE A1061 8890 9186 13984 1556 -1048 -1008 C ATOM 1849 N ARG A1062 -17.841 -41.647 33.593 1.00 84.20 N ANISOU 1849 N ARG A1062 7504 8722 15766 1605 -870 -1012 N ATOM 1850 CA ARG A1062 -17.086 -42.358 34.626 1.00 82.84 C ANISOU 1850 CA ARG A1062 7557 8584 15333 1430 -637 -923 C ATOM 1851 C ARG A1062 -16.956 -43.857 34.330 1.00 86.06 C ANISOU 1851 C ARG A1062 7853 8964 15883 1412 -804 -950 C ATOM 1852 O ARG A1062 -15.945 -44.449 34.697 1.00 84.17 O ANISOU 1852 O ARG A1062 7843 8845 15292 1394 -794 -854 O ATOM 1853 CB ARG A1062 -17.761 -42.173 35.995 1.00 85.61 C ANISOU 1853 CB ARG A1062 7953 8726 15847 1317 -110 -853 C ATOM 1854 CG ARG A1062 -17.231 -40.997 36.799 1.00100.38 C ANISOU 1854 CG ARG A1062 10208 10653 17279 1220 180 -797 C ATOM 1855 CD ARG A1062 -16.474 -41.465 38.032 1.00119.83 C ANISOU 1855 CD ARG A1062 12985 13216 19328 1031 413 -685 C ATOM 1856 NE ARG A1062 -17.165 -41.120 39.279 1.00138.94 N ANISOU 1856 NE ARG A1062 15567 15401 21822 908 956 -647 N ATOM 1857 CZ ARG A1062 -16.737 -41.445 40.498 1.00156.83 C ANISOU 1857 CZ ARG A1062 18159 17709 23720 743 1225 -539 C ATOM 1858 NH1 ARG A1062 -15.611 -42.135 40.653 1.00144.32 N ANISOU 1858 NH1 ARG A1062 16719 16428 21686 728 965 -432 N ATOM 1859 NH2 ARG A1062 -17.432 -41.087 41.570 1.00145.15 N ANISOU 1859 NH2 ARG A1062 16869 15981 22300 624 1760 -526 N ATOM 1860 N HIS A1063 -17.980 -44.471 33.696 1.00 84.74 N ANISOU 1860 N HIS A1063 7334 8640 16222 1416 -940 -1085 N ATOM 1861 CA HIS A1063 -17.982 -45.900 33.377 1.00 85.59 C ANISOU 1861 CA HIS A1063 7390 8630 16500 1341 -1032 -1160 C ATOM 1862 C HIS A1063 -16.949 -46.242 32.311 1.00 88.40 C ANISOU 1862 C HIS A1063 7914 9164 16510 1448 -1421 -1209 C ATOM 1863 O HIS A1063 -16.182 -47.187 32.510 1.00 88.34 O ANISOU 1863 O HIS A1063 8125 9122 16318 1468 -1355 -1141 O ATOM 1864 CB HIS A1063 -19.368 -46.395 32.946 1.00 89.72 C ANISOU 1864 CB HIS A1063 7467 8980 17644 1221 -1079 -1356 C ATOM 1865 CG HIS A1063 -19.393 -47.847 32.583 1.00 94.96 C ANISOU 1865 CG HIS A1063 8149 9461 18471 1066 -1124 -1484 C ATOM 1866 ND1 HIS A1063 -19.570 -48.259 31.272 1.00 98.06 N ANISOU 1866 ND1 HIS A1063 8389 9917 18954 1033 -1562 -1715 N ATOM 1867 CD2 HIS A1063 -19.220 -48.939 33.364 1.00 97.79 C ANISOU 1867 CD2 HIS A1063 8745 9545 18864 943 -756 -1407 C ATOM 1868 CE1 HIS A1063 -19.536 -49.582 31.301 1.00 99.13 C ANISOU 1868 CE1 HIS A1063 8664 9788 19211 854 -1414 -1804 C ATOM 1869 NE2 HIS A1063 -19.322 -50.037 32.537 1.00 99.47 N ANISOU 1869 NE2 HIS A1063 8956 9603 19234 819 -920 -1606 N ATOM 1870 N GLY A1064 -16.937 -45.492 31.209 1.00 84.19 N ANISOU 1870 N GLY A1064 7309 8798 15880 1551 -1783 -1308 N ATOM 1871 CA GLY A1064 -16.005 -45.700 30.103 1.00 82.94 C ANISOU 1871 CA GLY A1064 7332 8802 15379 1643 -2115 -1376 C ATOM 1872 C GLY A1064 -14.557 -45.815 30.547 1.00 84.83 C ANISOU 1872 C GLY A1064 7870 9218 15144 1698 -1987 -1230 C ATOM 1873 O GLY A1064 -13.846 -46.728 30.126 1.00 83.81 O ANISOU 1873 O GLY A1064 7860 9103 14881 1766 -2062 -1253 O ATOM 1874 N PHE A1065 -14.129 -44.909 31.442 1.00 80.78 N ANISOU 1874 N PHE A1065 7466 8850 14379 1665 -1775 -1087 N ATOM 1875 CA PHE A1065 -12.780 -44.900 32.001 1.00 79.13 C ANISOU 1875 CA PHE A1065 7448 8915 13702 1678 -1682 -956 C ATOM 1876 C PHE A1065 -12.583 -46.105 32.923 1.00 84.77 C ANISOU 1876 C PHE A1065 8213 9539 14457 1729 -1484 -811 C ATOM 1877 O PHE A1065 -11.599 -46.809 32.743 1.00 85.15 O ANISOU 1877 O PHE A1065 8336 9740 14277 1879 -1554 -747 O ATOM 1878 CB PHE A1065 -12.485 -43.568 32.724 1.00 79.69 C ANISOU 1878 CB PHE A1065 7640 9160 13478 1541 -1509 -896 C ATOM 1879 CG PHE A1065 -12.336 -42.437 31.738 1.00 79.80 C ANISOU 1879 CG PHE A1065 7732 9256 13333 1528 -1665 -1002 C ATOM 1880 CD1 PHE A1065 -11.145 -42.252 31.043 1.00 81.47 C ANISOU 1880 CD1 PHE A1065 8047 9754 13154 1521 -1806 -1044 C ATOM 1881 CD2 PHE A1065 -13.406 -41.603 31.446 1.00 82.48 C ANISOU 1881 CD2 PHE A1065 8043 9371 13924 1561 -1650 -1048 C ATOM 1882 CE1 PHE A1065 -11.025 -41.245 30.085 1.00 82.01 C ANISOU 1882 CE1 PHE A1065 8270 9837 13054 1500 -1899 -1130 C ATOM 1883 CE2 PHE A1065 -13.287 -40.598 30.485 1.00 85.07 C ANISOU 1883 CE2 PHE A1065 8526 9721 14074 1611 -1783 -1102 C ATOM 1884 CZ PHE A1065 -12.097 -40.420 29.815 1.00 82.07 C ANISOU 1884 CZ PHE A1065 8329 9581 13273 1558 -1891 -1144 C ATOM 1885 N ASP A1066 -13.543 -46.386 33.850 1.00 82.31 N ANISOU 1885 N ASP A1066 7875 8948 14450 1637 -1206 -753 N ATOM 1886 CA ASP A1066 -13.516 -47.535 34.770 1.00 83.59 C ANISOU 1886 CA ASP A1066 8176 8926 14657 1683 -947 -590 C ATOM 1887 C ASP A1066 -13.340 -48.860 33.997 1.00 88.54 C ANISOU 1887 C ASP A1066 8845 9360 15435 1821 -1047 -641 C ATOM 1888 O ASP A1066 -12.636 -49.755 34.468 1.00 89.24 O ANISOU 1888 O ASP A1066 9142 9429 15337 2007 -924 -456 O ATOM 1889 CB ASP A1066 -14.786 -47.578 35.628 1.00 87.08 C ANISOU 1889 CB ASP A1066 8573 9028 15487 1508 -593 -583 C ATOM 1890 N ILE A1067 -13.935 -48.952 32.794 1.00 85.68 N ANISOU 1890 N ILE A1067 8321 8868 15364 1753 -1274 -889 N ATOM 1891 CA ILE A1067 -13.820 -50.110 31.905 1.00 87.57 C ANISOU 1891 CA ILE A1067 8650 8900 15723 1817 -1368 -1017 C ATOM 1892 C ILE A1067 -12.419 -50.107 31.281 1.00 92.37 C ANISOU 1892 C ILE A1067 9389 9814 15894 2068 -1554 -968 C ATOM 1893 O ILE A1067 -11.776 -51.149 31.262 1.00 93.16 O ANISOU 1893 O ILE A1067 9687 9800 15910 2270 -1442 -884 O ATOM 1894 CB ILE A1067 -14.970 -50.124 30.845 1.00 91.42 C ANISOU 1894 CB ILE A1067 8905 9218 16611 1605 -1594 -1333 C ATOM 1895 CG1 ILE A1067 -16.287 -50.685 31.431 1.00 94.63 C ANISOU 1895 CG1 ILE A1067 9154 9265 17537 1343 -1326 -1414 C ATOM 1896 CG2 ILE A1067 -14.592 -50.793 29.504 1.00 92.03 C ANISOU 1896 CG2 ILE A1067 9106 9250 16610 1652 -1850 -1543 C ATOM 1897 CD1 ILE A1067 -16.299 -52.178 31.947 1.00107.46 C ANISOU 1897 CD1 ILE A1067 11067 10451 19312 1287 -944 -1367 C ATOM 1898 N LEU A1068 -11.948 -48.934 30.800 1.00 89.12 N ANISOU 1898 N LEU A1068 8881 9766 15213 2062 -1780 -1011 N ATOM 1899 CA LEU A1068 -10.623 -48.739 30.197 1.00 89.02 C ANISOU 1899 CA LEU A1068 8932 10098 14792 2236 -1914 -993 C ATOM 1900 C LEU A1068 -9.547 -49.137 31.200 1.00 95.42 C ANISOU 1900 C LEU A1068 9793 11148 15316 2444 -1741 -727 C ATOM 1901 O LEU A1068 -8.559 -49.750 30.813 1.00 96.20 O ANISOU 1901 O LEU A1068 9935 11385 15232 2697 -1753 -679 O ATOM 1902 CB LEU A1068 -10.445 -47.264 29.774 1.00 87.12 C ANISOU 1902 CB LEU A1068 8622 10155 14324 2108 -2078 -1067 C ATOM 1903 CG LEU A1068 -9.681 -46.963 28.485 1.00 91.75 C ANISOU 1903 CG LEU A1068 9279 10932 14649 2167 -2268 -1204 C ATOM 1904 CD1 LEU A1068 -9.942 -45.544 28.037 1.00 90.86 C ANISOU 1904 CD1 LEU A1068 9190 10925 14408 2013 -2383 -1280 C ATOM 1905 CD2 LEU A1068 -8.188 -47.115 28.673 1.00 95.21 C ANISOU 1905 CD2 LEU A1068 9705 11749 14724 2315 -2179 -1092 C ATOM 1906 N VAL A1069 -9.773 -48.819 32.493 1.00 93.60 N ANISOU 1906 N VAL A1069 9558 10967 15037 2361 -1576 -551 N ATOM 1907 CA VAL A1069 -8.913 -49.142 33.635 1.00 95.63 C ANISOU 1907 CA VAL A1069 9872 11485 14977 2545 -1453 -270 C ATOM 1908 C VAL A1069 -8.906 -50.682 33.826 1.00105.08 C ANISOU 1908 C VAL A1069 11270 12329 16326 2846 -1272 -112 C ATOM 1909 O VAL A1069 -7.828 -51.273 33.962 1.00106.79 O ANISOU 1909 O VAL A1069 11514 12780 16283 3201 -1278 80 O ATOM 1910 CB VAL A1069 -9.380 -48.354 34.894 1.00 98.85 C ANISOU 1910 CB VAL A1069 10314 11958 15287 2313 -1304 -172 C ATOM 1911 CG1 VAL A1069 -8.937 -49.015 36.199 1.00101.50 C ANISOU 1911 CG1 VAL A1069 10811 12387 15367 2500 -1140 140 C ATOM 1912 CG2 VAL A1069 -8.905 -46.906 34.832 1.00 96.56 C ANISOU 1912 CG2 VAL A1069 9912 12089 14687 2079 -1431 -280 C ATOM 1913 N GLY A1070 -10.095 -51.299 33.772 1.00104.32 N ANISOU 1913 N GLY A1070 11300 11677 16659 2704 -1097 -207 N ATOM 1914 CA GLY A1070 -10.275 -52.747 33.866 1.00108.40 C ANISOU 1914 CA GLY A1070 12097 11716 17374 2893 -843 -114 C ATOM 1915 C GLY A1070 -9.655 -53.484 32.690 1.00115.08 C ANISOU 1915 C GLY A1070 13023 12479 18223 3126 -928 -234 C ATOM 1916 O GLY A1070 -9.069 -54.555 32.867 1.00117.02 O ANISOU 1916 O GLY A1070 13524 12543 18396 3492 -731 -42 O ATOM 1917 N GLN A1071 -9.764 -52.887 31.480 1.00111.73 N ANISOU 1917 N GLN A1071 12427 12175 17850 2948 -1198 -538 N ATOM 1918 CA GLN A1071 -9.206 -53.397 30.223 1.00113.27 C ANISOU 1918 CA GLN A1071 12718 12318 18001 3106 -1285 -713 C ATOM 1919 C GLN A1071 -7.672 -53.299 30.254 1.00119.41 C ANISOU 1919 C GLN A1071 13415 13581 18374 3507 -1317 -513 C ATOM 1920 O GLN A1071 -7.007 -54.189 29.722 1.00121.83 O ANISOU 1920 O GLN A1071 13889 13762 18640 3834 -1193 -498 O ATOM 1921 CB GLN A1071 -9.793 -52.650 29.009 1.00112.48 C ANISOU 1921 CB GLN A1071 12488 12259 17990 2793 -1585 -1065 C ATOM 1922 N ILE A1072 -7.119 -52.241 30.905 1.00115.12 N ANISOU 1922 N ILE A1072 12608 13591 17541 3470 -1451 -373 N ATOM 1923 CA ILE A1072 -5.676 -52.037 31.104 1.00116.49 C ANISOU 1923 CA ILE A1072 12578 14354 17330 3775 -1506 -193 C ATOM 1924 C ILE A1072 -5.190 -53.100 32.113 1.00125.74 C ANISOU 1924 C ILE A1072 13872 15485 18418 4234 -1314 176 C ATOM 1925 O ILE A1072 -4.126 -53.693 31.911 1.00128.56 O ANISOU 1925 O ILE A1072 14168 16058 18621 4691 -1267 320 O ATOM 1926 CB ILE A1072 -5.347 -50.568 31.558 1.00117.13 C ANISOU 1926 CB ILE A1072 12374 15009 17122 3476 -1689 -206 C ATOM 1927 CG1 ILE A1072 -5.500 -49.522 30.413 1.00114.67 C ANISOU 1927 CG1 ILE A1072 11998 14771 16802 3150 -1843 -518 C ATOM 1928 CG2 ILE A1072 -3.985 -50.439 32.257 1.00120.27 C ANISOU 1928 CG2 ILE A1072 12502 16078 17118 3721 -1742 23 C ATOM 1929 CD1 ILE A1072 -4.482 -49.552 29.211 1.00124.19 C ANISOU 1929 CD1 ILE A1072 13128 16215 17844 3297 -1876 -656 C ATOM 1930 N ASP A1073 -5.993 -53.355 33.173 1.00123.79 N ANISOU 1930 N ASP A1073 13822 14940 18274 4145 -1170 340 N ATOM 1931 CA ASP A1073 -5.708 -54.346 34.218 1.00128.40 C ANISOU 1931 CA ASP A1073 14643 15395 18748 4569 -957 729 C ATOM 1932 C ASP A1073 -5.618 -55.777 33.629 1.00137.19 C ANISOU 1932 C ASP A1073 16107 15946 20073 4969 -682 773 C ATOM 1933 O ASP A1073 -4.704 -56.529 33.981 1.00140.15 O ANISOU 1933 O ASP A1073 16564 16436 20250 5555 -578 1097 O ATOM 1934 CB ASP A1073 -6.771 -54.277 35.326 1.00130.04 C ANISOU 1934 CB ASP A1073 15071 15285 19053 4291 -784 832 C ATOM 1935 N ASP A1074 -6.552 -56.125 32.713 1.00134.21 N ANISOU 1935 N ASP A1074 15933 14982 20079 4655 -569 435 N ATOM 1936 CA ASP A1074 -6.605 -57.417 32.020 1.00138.07 C ANISOU 1936 CA ASP A1074 16827 14851 20783 4885 -273 364 C ATOM 1937 C ASP A1074 -5.460 -57.532 31.009 1.00144.22 C ANISOU 1937 C ASP A1074 17486 15913 21398 5254 -346 294 C ATOM 1938 O ASP A1074 -4.934 -58.629 30.808 1.00148.39 O ANISOU 1938 O ASP A1074 18325 16117 21939 5737 -52 427 O ATOM 1939 CB ASP A1074 -7.959 -57.604 31.317 1.00138.95 C ANISOU 1939 CB ASP A1074 17115 14374 21306 4320 -205 -49 C ATOM 1940 N ALA A1075 -5.077 -56.401 30.375 1.00137.93 N ANISOU 1940 N ALA A1075 16276 15680 20449 5034 -676 89 N ATOM 1941 CA ALA A1075 -3.974 -56.346 29.413 1.00138.87 C ANISOU 1941 CA ALA A1075 16233 16134 20398 5315 -716 -2 C ATOM 1942 C ALA A1075 -2.636 -56.532 30.129 1.00146.36 C ANISOU 1942 C ALA A1075 16913 17636 21062 5927 -687 396 C ATOM 1943 O ALA A1075 -1.792 -57.287 29.640 1.00149.97 O ANISOU 1943 O ALA A1075 17428 18062 21492 6443 -483 472 O ATOM 1944 CB ALA A1075 -3.991 -55.026 28.655 1.00135.23 C ANISOU 1944 CB ALA A1075 15458 16095 19828 4867 -1029 -302 C ATOM 1945 N LEU A1076 -2.465 -55.882 31.310 1.00142.07 N ANISOU 1945 N LEU A1076 16084 17598 20300 5887 -881 649 N ATOM 1946 CA LEU A1076 -1.251 -55.979 32.126 1.00145.84 C ANISOU 1946 CA LEU A1076 16232 18726 20454 6425 -954 1036 C ATOM 1947 C LEU A1076 -1.088 -57.381 32.737 1.00156.35 C ANISOU 1947 C LEU A1076 17948 19642 21817 7110 -656 1440 C ATOM 1948 O LEU A1076 0.040 -57.780 33.035 1.00160.69 O ANISOU 1948 O LEU A1076 18257 20642 22154 7762 -662 1759 O ATOM 1949 CB LEU A1076 -1.217 -54.905 33.220 1.00143.84 C ANISOU 1949 CB LEU A1076 15655 19091 19908 6105 -1253 1146 C ATOM 1950 CG LEU A1076 -0.479 -53.626 32.834 1.00146.31 C ANISOU 1950 CG LEU A1076 15421 20176 19994 5767 -1526 924 C ATOM 1951 CD1 LEU A1076 -1.070 -52.436 33.525 1.00142.99 C ANISOU 1951 CD1 LEU A1076 14936 19961 19433 5151 -1714 819 C ATOM 1952 CD2 LEU A1076 1.010 -53.722 33.139 1.00153.38 C ANISOU 1952 CD2 LEU A1076 15800 21896 20581 6258 -1646 1161 C ATOM 1953 N LYS A1077 -2.206 -58.133 32.890 1.00153.39 N ANISOU 1953 N LYS A1077 18165 18403 21712 6972 -371 1425 N ATOM 1954 CA LYS A1077 -2.215 -59.516 33.385 1.00158.85 C ANISOU 1954 CA LYS A1077 19398 18493 22465 7554 24 1778 C ATOM 1955 C LYS A1077 -1.482 -60.404 32.379 1.00165.85 C ANISOU 1955 C LYS A1077 20432 19128 23457 8095 299 1740 C ATOM 1956 O LYS A1077 -0.709 -61.269 32.781 1.00171.49 O ANISOU 1956 O LYS A1077 21286 19821 24051 8885 509 2152 O ATOM 1957 CB LYS A1077 -3.657 -60.008 33.611 1.00160.74 C ANISOU 1957 CB LYS A1077 20219 17839 23017 7098 318 1651 C ATOM 1958 CG LYS A1077 -3.840 -60.839 34.875 1.00179.02 C ANISOU 1958 CG LYS A1077 23010 19783 25227 7476 612 2128 C ATOM 1959 CD LYS A1077 -5.313 -61.169 35.116 1.00187.53 C ANISOU 1959 CD LYS A1077 24573 20042 26638 6884 929 1944 C ATOM 1960 CE LYS A1077 -5.581 -61.710 36.503 1.00200.92 C ANISOU 1960 CE LYS A1077 26724 21447 28169 7119 1210 2408 C ATOM 1961 NZ LYS A1077 -5.628 -60.632 37.528 1.00205.60 N ANISOU 1961 NZ LYS A1077 26959 22705 28454 6884 871 2550 N ATOM 1962 N LEU A1078 -1.697 -60.143 31.068 1.00158.74 N ANISOU 1962 N LEU A1078 19504 18064 22744 7699 297 1257 N ATOM 1963 CA LEU A1078 -1.045 -60.831 29.953 1.00161.43 C ANISOU 1963 CA LEU A1078 20000 18171 23165 8092 576 1118 C ATOM 1964 C LEU A1078 0.405 -60.358 29.820 1.00165.75 C ANISOU 1964 C LEU A1078 19892 19627 23458 8577 401 1274 C ATOM 1965 O LEU A1078 1.269 -61.149 29.441 1.00170.95 O ANISOU 1965 O LEU A1078 20612 20218 24121 9266 702 1421 O ATOM 1966 CB LEU A1078 -1.810 -60.582 28.644 1.00157.89 C ANISOU 1966 CB LEU A1078 19748 17325 22917 7427 571 534 C ATOM 1967 N ALA A1079 0.667 -59.075 30.150 1.00157.05 N ANISOU 1967 N ALA A1079 18162 19362 22146 8207 -46 1231 N ATOM 1968 CA ALA A1079 1.996 -58.464 30.087 1.00157.95 C ANISOU 1968 CA ALA A1079 17556 20440 22018 8492 -243 1319 C ATOM 1969 C ALA A1079 2.905 -58.952 31.225 1.00166.84 C ANISOU 1969 C ALA A1079 18396 22072 22922 9275 -295 1877 C ATOM 1970 O ALA A1079 4.093 -59.186 30.985 1.00171.56 O ANISOU 1970 O ALA A1079 18557 23186 23440 9879 -236 2026 O ATOM 1971 CB ALA A1079 1.878 -56.951 30.127 1.00152.94 C ANISOU 1971 CB ALA A1079 16453 20435 21221 7753 -652 1066 C ATOM 1972 N ASN A1080 2.354 -59.106 32.454 1.00162.50 N ANISOU 1972 N ASN A1080 18083 21402 22258 9287 -400 2191 N ATOM 1973 CA ASN A1080 3.095 -59.575 33.634 1.00168.14 C ANISOU 1973 CA ASN A1080 18623 22579 22683 10032 -501 2765 C ATOM 1974 C ASN A1080 3.443 -61.064 33.530 1.00177.99 C ANISOU 1974 C ASN A1080 20342 23227 24059 10986 -40 3120 C ATOM 1975 O ASN A1080 4.479 -61.476 34.053 1.00184.08 O ANISOU 1975 O ASN A1080 20780 24546 24616 11828 -105 3570 O ATOM 1976 CB ASN A1080 2.320 -59.303 34.924 1.00167.58 C ANISOU 1976 CB ASN A1080 18801 22460 22412 9719 -689 2974 C ATOM 1977 CG ASN A1080 2.695 -58.003 35.592 1.00185.30 C ANISOU 1977 CG ASN A1080 20397 25715 24293 9268 -1204 2925 C ATOM 1978 OD1 ASN A1080 3.847 -57.782 35.989 1.00185.05 O ANISOU 1978 OD1 ASN A1080 19738 26625 23946 9666 -1494 3147 O ATOM 1979 ND2 ASN A1080 1.719 -57.123 35.758 1.00169.20 N ANISOU 1979 ND2 ASN A1080 18493 23508 22287 8424 -1313 2627 N ATOM 1980 N GLU A1081 2.589 -61.858 32.840 1.00173.17 N ANISOU 1980 N GLU A1081 20499 21509 23789 10854 429 2908 N ATOM 1981 CA GLU A1081 2.786 -63.291 32.599 1.00179.76 C ANISOU 1981 CA GLU A1081 21954 21562 24783 11652 990 3157 C ATOM 1982 C GLU A1081 4.000 -63.530 31.688 1.00188.13 C ANISOU 1982 C GLU A1081 22607 22986 25889 12283 1150 3127 C ATOM 1983 O GLU A1081 4.570 -64.625 31.697 1.00195.41 O ANISOU 1983 O GLU A1081 23821 23553 26874 13179 1544 3461 O ATOM 1984 CB GLU A1081 1.526 -63.923 31.976 1.00179.05 C ANISOU 1984 CB GLU A1081 22744 20248 25039 11127 1433 2794 C ATOM 1985 CG GLU A1081 0.419 -64.255 32.965 1.00188.96 C ANISOU 1985 CG GLU A1081 24595 20884 26317 10830 1548 2967 C ATOM 1986 CD GLU A1081 0.651 -65.447 33.872 1.00214.43 C ANISOU 1986 CD GLU A1081 28058 23549 29868 10792 1408 3121 C ATOM 1987 OE1 GLU A1081 0.757 -66.584 33.355 1.00212.56 O ANISOU 1987 OE1 GLU A1081 28256 22554 29953 10949 1724 2986 O ATOM 1988 OE2 GLU A1081 0.679 -65.249 35.107 1.00211.96 O ANISOU 1988 OE2 GLU A1081 27699 23575 29262 10975 1202 3557 O ATOM 1989 N GLY A1082 4.381 -62.499 30.931 1.00179.88 N ANISOU 1989 N GLY A1082 20910 22606 24829 11789 874 2723 N ATOM 1990 CA GLY A1082 5.511 -62.532 30.011 1.00183.14 C ANISOU 1990 CA GLY A1082 20851 23448 25286 12234 1036 2618 C ATOM 1991 C GLY A1082 5.109 -62.461 28.552 1.00183.67 C ANISOU 1991 C GLY A1082 21261 22951 25574 11697 1324 2028 C ATOM 1992 O GLY A1082 5.945 -62.147 27.700 1.00184.45 O ANISOU 1992 O GLY A1082 20915 23494 25674 11796 1409 1824 O ATOM 1993 N LYS A1083 3.825 -62.762 28.257 1.00176.87 N ANISOU 1993 N LYS A1083 21189 21131 24883 11110 1481 1744 N ATOM 1994 CA LYS A1083 3.255 -62.755 26.909 1.00174.06 C ANISOU 1994 CA LYS A1083 21267 20182 24686 10534 1695 1169 C ATOM 1995 C LYS A1083 3.270 -61.343 26.329 1.00172.75 C ANISOU 1995 C LYS A1083 20543 20697 24399 9783 1269 782 C ATOM 1996 O LYS A1083 2.834 -60.399 26.992 1.00167.34 O ANISOU 1996 O LYS A1083 19528 20443 23610 9265 814 796 O ATOM 1997 CB LYS A1083 1.829 -63.324 26.919 1.00174.52 C ANISOU 1997 CB LYS A1083 22165 19210 24934 10015 1856 971 C ATOM 1998 N VAL A1084 3.816 -61.199 25.108 1.00171.04 N ANISOU 1998 N VAL A1084 20262 20555 24169 9756 1469 453 N ATOM 1999 CA VAL A1084 3.933 -59.907 24.423 1.00166.15 C ANISOU 1999 CA VAL A1084 19213 20513 23402 9101 1167 95 C ATOM 2000 C VAL A1084 2.827 -59.784 23.365 1.00166.74 C ANISOU 2000 C VAL A1084 19922 19906 23524 8373 1172 -412 C ATOM 2001 O VAL A1084 2.139 -58.766 23.331 1.00159.73 O ANISOU 2001 O VAL A1084 18919 19209 22562 7670 768 -613 O ATOM 2002 CB VAL A1084 5.339 -59.661 23.803 1.00174.01 C ANISOU 2002 CB VAL A1084 19638 22178 24299 9499 1370 73 C ATOM 2003 CG1 VAL A1084 5.607 -58.167 23.638 1.00169.05 C ANISOU 2003 CG1 VAL A1084 18398 22360 23472 8855 996 -134 C ATOM 2004 CG2 VAL A1084 6.449 -60.315 24.628 1.00180.90 C ANISOU 2004 CG2 VAL A1084 20026 23514 25194 10475 1519 580 C ATOM 2005 N LYS A1085 2.658 -60.824 22.518 1.00168.58 N ANISOU 2005 N LYS A1085 20837 19356 23861 8560 1627 -616 N ATOM 2006 CA LYS A1085 1.658 -60.876 21.446 1.00166.86 C ANISOU 2006 CA LYS A1085 21259 18496 23644 7910 1635 -1121 C ATOM 2007 C LYS A1085 0.225 -60.853 21.997 1.00167.76 C ANISOU 2007 C LYS A1085 21651 18190 23902 7334 1326 -1187 C ATOM 2008 O LYS A1085 -0.650 -60.246 21.380 1.00163.51 O ANISOU 2008 O LYS A1085 21247 17565 23316 6638 1021 -1552 O ATOM 2009 CB LYS A1085 1.865 -62.126 20.579 1.00175.79 C ANISOU 2009 CB LYS A1085 23097 18862 24833 8276 2247 -1306 C ATOM 2010 N GLU A1086 -0.003 -61.507 23.153 1.00166.64 N ANISOU 2010 N GLU A1086 21583 17806 23926 7649 1421 -820 N ATOM 2011 CA GLU A1086 -1.304 -61.584 23.830 1.00164.15 C ANISOU 2011 CA GLU A1086 21500 17084 23785 7160 1235 -836 C ATOM 2012 C GLU A1086 -1.663 -60.259 24.512 1.00162.06 C ANISOU 2012 C GLU A1086 20637 17490 23447 6719 682 -753 C ATOM 2013 O GLU A1086 -2.848 -59.960 24.670 1.00158.16 O ANISOU 2013 O GLU A1086 20248 16763 23083 6126 452 -927 O ATOM 2014 CB GLU A1086 -1.305 -62.718 24.869 1.00170.32 C ANISOU 2014 CB GLU A1086 22619 17377 24718 7698 1606 -426 C ATOM 2015 CG GLU A1086 -1.272 -64.116 24.273 1.00187.50 C ANISOU 2015 CG GLU A1086 25581 18644 27015 8019 2229 -544 C ATOM 2016 CD GLU A1086 -0.798 -65.207 25.215 1.00215.48 C ANISOU 2016 CD GLU A1086 29433 21812 30628 8843 2688 -25 C ATOM 2017 OE1 GLU A1086 -1.350 -65.316 26.334 1.00213.51 O ANISOU 2017 OE1 GLU A1086 29235 21441 30446 8796 2620 270 O ATOM 2018 OE2 GLU A1086 0.116 -65.968 24.824 1.00213.36 O ANISOU 2018 OE2 GLU A1086 29396 21338 30334 9567 3151 99 O ATOM 2019 N ALA A1087 -0.642 -59.483 24.930 1.00158.14 N ANISOU 2019 N ALA A1087 19510 17824 22753 7003 500 -501 N ATOM 2020 CA ALA A1087 -0.801 -58.193 25.603 1.00152.97 C ANISOU 2020 CA ALA A1087 18318 17826 21979 6613 43 -423 C ATOM 2021 C ALA A1087 -0.900 -57.032 24.595 1.00153.37 C ANISOU 2021 C ALA A1087 18195 18190 21888 6064 -220 -800 C ATOM 2022 O ALA A1087 -1.712 -56.129 24.806 1.00148.71 O ANISOU 2022 O ALA A1087 17498 17704 21301 5529 -549 -905 O ATOM 2023 CB ALA A1087 0.350 -57.957 26.569 1.00155.55 C ANISOU 2023 CB ALA A1087 18078 18899 22124 7123 -20 -1 C ATOM 2024 N GLN A1088 -0.090 -57.057 23.505 1.00152.10 N ANISOU 2024 N GLN A1088 18050 18146 21596 6223 -33 -988 N ATOM 2025 CA GLN A1088 -0.104 -56.027 22.454 1.00149.14 C ANISOU 2025 CA GLN A1088 17627 18009 21029 5752 -208 -1325 C ATOM 2026 C GLN A1088 -1.459 -55.985 21.754 1.00150.97 C ANISOU 2026 C GLN A1088 18343 17685 21333 5206 -398 -1669 C ATOM 2027 O GLN A1088 -1.948 -54.899 21.434 1.00146.88 O ANISOU 2027 O GLN A1088 17734 17378 20698 4736 -723 -1826 O ATOM 2028 CB GLN A1088 1.009 -56.262 21.426 1.00154.38 C ANISOU 2028 CB GLN A1088 18310 18805 21540 6067 138 -1456 C ATOM 2029 CG GLN A1088 2.378 -55.810 21.901 1.00172.30 C ANISOU 2029 CG GLN A1088 19893 21882 23691 6421 215 -1209 C ATOM 2030 CD GLN A1088 3.433 -56.110 20.877 1.00195.90 C ANISOU 2030 CD GLN A1088 22881 24970 26583 6746 634 -1350 C ATOM 2031 OE1 GLN A1088 3.924 -57.239 20.768 1.00195.83 O ANISOU 2031 OE1 GLN A1088 23035 24678 26695 7354 1032 -1247 O ATOM 2032 NE2 GLN A1088 3.805 -55.101 20.102 1.00187.16 N ANISOU 2032 NE2 GLN A1088 21631 24230 25252 6361 610 -1585 N ATOM 2033 N ALA A1089 -2.070 -57.170 21.543 1.00150.46 N ANISOU 2033 N ALA A1089 18791 16919 21459 5270 -189 -1783 N ATOM 2034 CA ALA A1089 -3.389 -57.328 20.935 1.00149.65 C ANISOU 2034 CA ALA A1089 19106 16302 21454 4742 -373 -2133 C ATOM 2035 C ALA A1089 -4.492 -56.838 21.883 1.00150.06 C ANISOU 2035 C ALA A1089 18927 16377 21713 4377 -706 -2032 C ATOM 2036 O ALA A1089 -5.495 -56.304 21.409 1.00147.76 O ANISOU 2036 O ALA A1089 18679 16021 21441 3885 -1037 -2288 O ATOM 2037 CB ALA A1089 -3.624 -58.782 20.562 1.00155.56 C ANISOU 2037 CB ALA A1089 20455 16302 22348 4882 19 -2294 C ATOM 2038 N ALA A1090 -4.295 -57.001 23.216 1.00146.10 N ANISOU 2038 N ALA A1090 18175 15994 21341 4648 -614 -1649 N ATOM 2039 CA ALA A1090 -5.238 -56.573 24.258 1.00142.92 C ANISOU 2039 CA ALA A1090 17570 15611 21124 4355 -827 -1516 C ATOM 2040 C ALA A1090 -5.318 -55.042 24.359 1.00142.55 C ANISOU 2040 C ALA A1090 17099 16143 20920 4053 -1209 -1515 C ATOM 2041 O ALA A1090 -6.358 -54.516 24.761 1.00139.44 O ANISOU 2041 O ALA A1090 16603 15698 20682 3687 -1425 -1556 O ATOM 2042 CB ALA A1090 -4.840 -57.163 25.599 1.00145.29 C ANISOU 2042 CB ALA A1090 17804 15904 21496 4776 -591 -1090 C ATOM 2043 N ALA A1091 -4.226 -54.339 23.985 1.00139.15 N ANISOU 2043 N ALA A1091 16438 16234 20197 4201 -1236 -1480 N ATOM 2044 CA ALA A1091 -4.127 -52.877 23.980 1.00135.64 C ANISOU 2044 CA ALA A1091 15683 16298 19554 3913 -1503 -1497 C ATOM 2045 C ALA A1091 -4.856 -52.269 22.770 1.00138.97 C ANISOU 2045 C ALA A1091 16330 16570 19904 3533 -1736 -1828 C ATOM 2046 O ALA A1091 -5.543 -51.260 22.926 1.00135.70 O ANISOU 2046 O ALA A1091 15797 16274 19489 3224 -1993 -1849 O ATOM 2047 CB ALA A1091 -2.668 -52.453 23.976 1.00137.26 C ANISOU 2047 CB ALA A1091 15581 17088 19484 4161 -1381 -1374 C ATOM 2048 N GLU A1092 -4.712 -52.882 21.571 1.00138.77 N ANISOU 2048 N GLU A1092 16661 16279 19788 3583 -1639 -2076 N ATOM 2049 CA GLU A1092 -5.368 -52.435 20.333 1.00138.63 C ANISOU 2049 CA GLU A1092 16928 16127 19618 3264 -1889 -2390 C ATOM 2050 C GLU A1092 -6.857 -52.843 20.327 1.00142.52 C ANISOU 2050 C GLU A1092 17549 16211 20391 2968 -2137 -2559 C ATOM 2051 O GLU A1092 -7.630 -52.343 19.505 1.00142.06 O ANISOU 2051 O GLU A1092 17615 16126 20235 2689 -2468 -2777 O ATOM 2052 CB GLU A1092 -4.642 -52.991 19.094 1.00143.54 C ANISOU 2052 CB GLU A1092 17930 16619 19989 3408 -1664 -2611 C ATOM 2053 CG GLU A1092 -4.762 -52.106 17.864 1.00153.47 C ANISOU 2053 CG GLU A1092 19434 17990 20888 3157 -1881 -2835 C ATOM 2054 N GLN A1093 -7.246 -53.756 21.244 1.00139.77 N ANISOU 2054 N GLN A1093 17161 15565 20378 3033 -1968 -2452 N ATOM 2055 CA GLN A1093 -8.623 -54.223 21.418 1.00140.41 C ANISOU 2055 CA GLN A1093 17285 15271 20792 2711 -2113 -2610 C ATOM 2056 C GLN A1093 -9.418 -53.147 22.170 1.00139.93 C ANISOU 2056 C GLN A1093 16821 15465 20882 2508 -2386 -2473 C ATOM 2057 O GLN A1093 -10.511 -52.776 21.727 1.00140.35 O ANISOU 2057 O GLN A1093 16803 15480 21044 2202 -2714 -2670 O ATOM 2058 CB GLN A1093 -8.656 -55.572 22.162 1.00144.48 C ANISOU 2058 CB GLN A1093 17978 15329 21589 2855 -1721 -2521 C ATOM 2059 CG GLN A1093 -9.867 -56.441 21.826 1.00158.88 C ANISOU 2059 CG GLN A1093 20039 16634 23695 2459 -1742 -2848 C ATOM 2060 CD GLN A1093 -9.721 -57.855 22.344 1.00177.72 C ANISOU 2060 CD GLN A1093 22782 18458 26284 2619 -1240 -2789 C ATOM 2061 OE1 GLN A1093 -9.698 -58.106 23.555 1.00172.42 O ANISOU 2061 OE1 GLN A1093 22012 17700 25799 2793 -1000 -2470 O ATOM 2062 NE2 GLN A1093 -9.642 -58.816 21.435 1.00171.11 N ANISOU 2062 NE2 GLN A1093 22440 17186 25387 2560 -1041 -3095 N ATOM 2063 N LEU A1094 -8.845 -52.610 23.274 1.00132.00 N ANISOU 2063 N LEU A1094 15549 14750 19854 2691 -2256 -2143 N ATOM 2064 CA LEU A1094 -9.473 -51.549 24.063 1.00128.15 C ANISOU 2064 CA LEU A1094 14743 14478 19470 2525 -2421 -2005 C ATOM 2065 C LEU A1094 -9.373 -50.184 23.336 1.00127.27 C ANISOU 2065 C LEU A1094 14580 14700 19076 2429 -2692 -2066 C ATOM 2066 O LEU A1094 -10.064 -49.254 23.724 1.00124.12 O ANISOU 2066 O LEU A1094 13992 14401 18765 2286 -2844 -2008 O ATOM 2067 CB LEU A1094 -8.901 -51.472 25.503 1.00127.06 C ANISOU 2067 CB LEU A1094 14418 14523 19336 2705 -2181 -1663 C ATOM 2068 CG LEU A1094 -7.408 -51.145 25.707 1.00131.33 C ANISOU 2068 CG LEU A1094 14872 15505 19524 2979 -2061 -1474 C ATOM 2069 CD1 LEU A1094 -7.193 -49.659 25.967 1.00128.50 C ANISOU 2069 CD1 LEU A1094 14300 15576 18948 2808 -2196 -1414 C ATOM 2070 CD2 LEU A1094 -6.840 -51.921 26.878 1.00135.27 C ANISOU 2070 CD2 LEU A1094 15321 16023 20051 3278 -1806 -1179 C ATOM 2071 N LYS A1095 -8.532 -50.083 22.281 1.00123.55 N ANISOU 2071 N LYS A1095 14326 14352 18264 2521 -2698 -2178 N ATOM 2072 CA LYS A1095 -8.329 -48.888 21.449 1.00121.61 C ANISOU 2072 CA LYS A1095 14169 14352 17686 2442 -2881 -2236 C ATOM 2073 C LYS A1095 -9.637 -48.493 20.741 1.00124.90 C ANISOU 2073 C LYS A1095 14651 14629 18176 2252 -3275 -2406 C ATOM 2074 O LYS A1095 -9.998 -47.318 20.741 1.00123.09 O ANISOU 2074 O LYS A1095 14357 14549 17862 2199 -3438 -2324 O ATOM 2075 CB LYS A1095 -7.207 -49.160 20.425 1.00125.47 C ANISOU 2075 CB LYS A1095 14934 14918 17823 2575 -2723 -2351 C ATOM 2076 CG LYS A1095 -6.896 -48.048 19.430 1.00133.61 C ANISOU 2076 CG LYS A1095 16179 16137 18448 2487 -2828 -2422 C ATOM 2077 CD LYS A1095 -5.811 -48.512 18.470 1.00144.06 C ANISOU 2077 CD LYS A1095 17782 17490 19466 2613 -2581 -2555 C ATOM 2078 CE LYS A1095 -5.513 -47.525 17.373 1.00155.37 C ANISOU 2078 CE LYS A1095 19537 19039 20455 2508 -2625 -2643 C ATOM 2079 NZ LYS A1095 -4.459 -48.038 16.456 1.00168.07 N ANISOU 2079 NZ LYS A1095 21424 20656 21781 2624 -2308 -2789 N ATOM 2080 N THR A1096 -10.338 -49.478 20.153 1.00123.72 N ANISOU 2080 N THR A1096 14630 14201 18178 2154 -3419 -2644 N ATOM 2081 CA THR A1096 -11.606 -49.270 19.448 1.00125.39 C ANISOU 2081 CA THR A1096 14825 14354 18464 1966 -3858 -2839 C ATOM 2082 C THR A1096 -12.758 -49.195 20.454 1.00127.57 C ANISOU 2082 C THR A1096 14671 14574 19227 1845 -3932 -2762 C ATOM 2083 O THR A1096 -13.611 -48.315 20.343 1.00127.23 O ANISOU 2083 O THR A1096 14428 14666 19249 1815 -4234 -2734 O ATOM 2084 CB THR A1096 -11.866 -50.393 18.402 1.00135.74 C ANISOU 2084 CB THR A1096 16444 15423 19706 1821 -3980 -3189 C ATOM 2085 OG1 THR A1096 -10.639 -50.996 17.978 1.00135.24 O ANISOU 2085 OG1 THR A1096 16747 15273 19366 1975 -3640 -3232 O ATOM 2086 CG2 THR A1096 -12.668 -49.904 17.193 1.00135.15 C ANISOU 2086 CG2 THR A1096 16496 15467 19388 1689 -4509 -3399 C ATOM 2087 N THR A1097 -12.774 -50.128 21.432 1.00122.99 N ANISOU 2087 N THR A1097 13975 13776 18981 1808 -3617 -2712 N ATOM 2088 CA THR A1097 -13.816 -50.273 22.451 1.00122.39 C ANISOU 2088 CA THR A1097 13539 13579 19385 1658 -3562 -2658 C ATOM 2089 C THR A1097 -13.775 -49.086 23.457 1.00120.70 C ANISOU 2089 C THR A1097 13082 13583 19197 1771 -3462 -2359 C ATOM 2090 O THR A1097 -14.801 -48.805 24.075 1.00121.14 O ANISOU 2090 O THR A1097 12819 13602 19605 1663 -3487 -2328 O ATOM 2091 CB THR A1097 -13.737 -51.670 23.113 1.00132.30 C ANISOU 2091 CB THR A1097 14895 14469 20904 1594 -3185 -2681 C ATOM 2092 OG1 THR A1097 -13.339 -52.638 22.132 1.00131.42 O ANISOU 2092 OG1 THR A1097 15165 14146 20624 1565 -3168 -2929 O ATOM 2093 CG2 THR A1097 -15.072 -52.113 23.716 1.00133.89 C ANISOU 2093 CG2 THR A1097 14800 14452 21620 1296 -3155 -2785 C ATOM 2094 N ARG A1098 -12.635 -48.364 23.581 1.00112.42 N ANISOU 2094 N ARG A1098 12176 12761 17778 1950 -3332 -2173 N ATOM 2095 CA ARG A1098 -12.563 -47.144 24.405 1.00108.54 C ANISOU 2095 CA ARG A1098 11542 12463 17235 1987 -3236 -1950 C ATOM 2096 C ARG A1098 -13.181 -46.005 23.608 1.00109.81 C ANISOU 2096 C ARG A1098 11708 12723 17292 1998 -3548 -1995 C ATOM 2097 O ARG A1098 -14.037 -45.290 24.117 1.00109.05 O ANISOU 2097 O ARG A1098 11396 12618 17421 1991 -3573 -1912 O ATOM 2098 CB ARG A1098 -11.122 -46.804 24.808 1.00107.31 C ANISOU 2098 CB ARG A1098 11513 12548 16713 2093 -2988 -1785 C ATOM 2099 N ASN A1099 -12.777 -45.885 22.327 1.00106.27 N ANISOU 2099 N ASN A1099 11539 12344 16494 2049 -3766 -2119 N ATOM 2100 CA ASN A1099 -13.287 -44.930 21.339 1.00107.05 C ANISOU 2100 CA ASN A1099 11764 12521 16390 2121 -4104 -2148 C ATOM 2101 C ASN A1099 -14.636 -45.465 20.789 1.00110.84 C ANISOU 2101 C ASN A1099 12017 12932 17165 2056 -4517 -2341 C ATOM 2102 O ASN A1099 -14.810 -45.685 19.585 1.00112.98 O ANISOU 2102 O ASN A1099 12486 13240 17203 2049 -4864 -2523 O ATOM 2103 CB ASN A1099 -12.239 -44.702 20.220 1.00110.26 C ANISOU 2103 CB ASN A1099 12622 13019 16254 2177 -4118 -2205 C ATOM 2104 CG ASN A1099 -10.948 -44.043 20.681 1.00125.89 C ANISOU 2104 CG ASN A1099 14744 15141 17948 2181 -3730 -2051 C ATOM 2105 OD1 ASN A1099 -10.934 -43.214 21.599 1.00114.93 O ANISOU 2105 OD1 ASN A1099 13234 13808 16626 2154 -3543 -1883 O ATOM 2106 ND2 ASN A1099 -9.837 -44.363 20.016 1.00115.08 N ANISOU 2106 ND2 ASN A1099 13635 13850 16239 2187 -3586 -2133 N ATOM 2107 N ALA A1100 -15.558 -45.724 21.729 1.00104.85 N ANISOU 2107 N ALA A1100 10833 12092 16912 1970 -4448 -2320 N ATOM 2108 CA ALA A1100 -16.916 -46.235 21.581 1.00107.07 C ANISOU 2108 CA ALA A1100 10720 12348 17616 1835 -4741 -2503 C ATOM 2109 C ALA A1100 -17.760 -45.697 22.735 1.00108.05 C ANISOU 2109 C ALA A1100 10406 12454 18193 1864 -4553 -2340 C ATOM 2110 O ALA A1100 -18.947 -45.427 22.558 1.00111.09 O ANISOU 2110 O ALA A1100 10387 12938 18883 1887 -4832 -2397 O ATOM 2111 CB ALA A1100 -16.902 -47.755 21.587 1.00109.23 C ANISOU 2111 CB ALA A1100 11011 12416 18077 1567 -4637 -2745 C ATOM 2112 N TYR A1101 -17.119 -45.518 23.918 1.00 99.18 N ANISOU 2112 N TYR A1101 9359 11236 17089 1876 -4074 -2138 N ATOM 2113 CA TYR A1101 -17.702 -44.953 25.143 1.00 97.39 C ANISOU 2113 CA TYR A1101 8853 10953 17196 1897 -3771 -1969 C ATOM 2114 C TYR A1101 -17.140 -43.561 25.469 1.00 94.24 C ANISOU 2114 C TYR A1101 8692 10629 16487 2085 -3595 -1738 C ATOM 2115 O TYR A1101 -17.856 -42.763 26.068 1.00 94.64 O ANISOU 2115 O TYR A1101 8550 10641 16767 2180 -3456 -1625 O ATOM 2116 CB TYR A1101 -17.442 -45.848 26.384 1.00 98.00 C ANISOU 2116 CB TYR A1101 8909 10843 17483 1720 -3318 -1921 C ATOM 2117 CG TYR A1101 -17.866 -47.300 26.304 1.00103.63 C ANISOU 2117 CG TYR A1101 9509 11365 18502 1486 -3309 -2128 C ATOM 2118 CD1 TYR A1101 -19.215 -47.652 26.253 1.00109.98 C ANISOU 2118 CD1 TYR A1101 9867 12113 19807 1299 -3423 -2309 C ATOM 2119 CD2 TYR A1101 -16.933 -48.325 26.428 1.00103.67 C ANISOU 2119 CD2 TYR A1101 9839 11222 18331 1443 -3106 -2132 C ATOM 2120 CE1 TYR A1101 -19.613 -48.989 26.225 1.00113.79 C ANISOU 2120 CE1 TYR A1101 10287 12372 20575 992 -3341 -2536 C ATOM 2121 CE2 TYR A1101 -17.318 -49.665 26.396 1.00107.71 C ANISOU 2121 CE2 TYR A1101 10350 11460 19116 1220 -3006 -2320 C ATOM 2122 CZ TYR A1101 -18.661 -49.992 26.299 1.00119.71 C ANISOU 2122 CZ TYR A1101 11478 12896 21111 951 -3109 -2538 C ATOM 2123 OH TYR A1101 -19.043 -51.312 26.273 1.00125.23 O ANISOU 2123 OH TYR A1101 12220 13285 22077 646 -2953 -2761 O ATOM 2124 N ILE A1102 -15.844 -43.300 25.143 1.00 85.26 N ANISOU 2124 N ILE A1102 7974 9576 14846 2109 -3530 -1686 N ATOM 2125 CA ILE A1102 -15.114 -42.077 25.505 1.00 81.65 C ANISOU 2125 CA ILE A1102 7798 9177 14048 2165 -3286 -1517 C ATOM 2126 C ILE A1102 -15.146 -40.957 24.436 1.00 84.71 C ANISOU 2126 C ILE A1102 8461 9600 14124 2353 -3504 -1477 C ATOM 2127 O ILE A1102 -15.349 -39.808 24.821 1.00 84.16 O ANISOU 2127 O ILE A1102 8505 9456 14017 2446 -3313 -1337 O ATOM 2128 CB ILE A1102 -13.650 -42.406 25.888 1.00 81.44 C ANISOU 2128 CB ILE A1102 7999 9274 13671 2036 -3038 -1489 C ATOM 2129 N GLN A1103 -14.946 -41.264 23.129 1.00 81.22 N ANISOU 2129 N GLN A1103 8201 9231 13429 2414 -3853 -1590 N ATOM 2130 CA GLN A1103 -14.898 -40.257 22.050 1.00 82.21 C ANISOU 2130 CA GLN A1103 8696 9371 13168 2611 -4049 -1525 C ATOM 2131 C GLN A1103 -16.138 -39.332 22.008 1.00 89.41 C ANISOU 2131 C GLN A1103 9462 10213 14297 2902 -4213 -1385 C ATOM 2132 O GLN A1103 -16.050 -38.227 21.468 1.00 91.18 O ANISOU 2132 O GLN A1103 10073 10372 14199 3115 -4213 -1238 O ATOM 2133 CB GLN A1103 -14.688 -40.909 20.678 1.00 85.21 C ANISOU 2133 CB GLN A1103 9278 9835 13262 2625 -4430 -1692 C ATOM 2134 N LYS A1104 -17.269 -39.768 22.601 1.00 86.38 N ANISOU 2134 N LYS A1104 8530 9827 14463 2928 -4299 -1416 N ATOM 2135 CA LYS A1104 -18.509 -38.995 22.693 1.00 88.88 C ANISOU 2135 CA LYS A1104 8560 10119 15092 3245 -4415 -1283 C ATOM 2136 C LYS A1104 -18.261 -37.753 23.575 1.00 91.28 C ANISOU 2136 C LYS A1104 9140 10211 15332 3345 -3891 -1068 C ATOM 2137 O LYS A1104 -18.396 -36.630 23.092 1.00 93.85 O ANISOU 2137 O LYS A1104 9794 10437 15428 3659 -3900 -893 O ATOM 2138 CB LYS A1104 -19.641 -39.877 23.253 1.00 92.33 C ANISOU 2138 CB LYS A1104 8292 10618 16169 3146 -4513 -1413 C ATOM 2139 CG LYS A1104 -21.036 -39.349 22.979 1.00104.91 C ANISOU 2139 CG LYS A1104 9419 12322 18119 3502 -4816 -1338 C ATOM 2140 N TYR A1105 -17.828 -37.963 24.840 1.00 83.60 N ANISOU 2140 N TYR A1105 8119 9150 14495 3063 -3417 -1084 N ATOM 2141 CA TYR A1105 -17.526 -36.908 25.815 1.00 81.14 C ANISOU 2141 CA TYR A1105 8096 8642 14092 3035 -2877 -948 C ATOM 2142 C TYR A1105 -16.260 -36.127 25.420 1.00 82.77 C ANISOU 2142 C TYR A1105 8950 8813 13686 2917 -2696 -912 C ATOM 2143 O TYR A1105 -16.148 -34.934 25.731 1.00 84.31 O ANISOU 2143 O TYR A1105 9531 8796 13708 2972 -2334 -796 O ATOM 2144 CB TYR A1105 -17.366 -37.508 27.222 1.00 78.96 C ANISOU 2144 CB TYR A1105 7608 8345 14047 2723 -2494 -1002 C ATOM 2145 CG TYR A1105 -18.637 -38.112 27.780 1.00 82.34 C ANISOU 2145 CG TYR A1105 7453 8738 15096 2789 -2502 -1032 C ATOM 2146 N LEU A1106 -15.318 -36.800 24.739 1.00 75.76 N ANISOU 2146 N LEU A1106 8193 8110 12483 2736 -2892 -1028 N ATOM 2147 CA LEU A1106 -14.058 -36.231 24.275 1.00 74.45 C ANISOU 2147 CA LEU A1106 8556 7971 11762 2567 -2717 -1037 C ATOM 2148 C LEU A1106 -14.287 -35.195 23.177 1.00 82.98 C ANISOU 2148 C LEU A1106 10100 8885 12544 2860 -2826 -912 C ATOM 2149 O LEU A1106 -13.677 -34.121 23.219 1.00 83.63 O ANISOU 2149 O LEU A1106 10695 8800 12280 2764 -2451 -845 O ATOM 2150 CB LEU A1106 -13.175 -37.356 23.756 1.00 72.69 C ANISOU 2150 CB LEU A1106 8262 7989 11369 2385 -2907 -1192 C ATOM 2151 CG LEU A1106 -11.674 -37.237 23.956 1.00 75.20 C ANISOU 2151 CG LEU A1106 8821 8467 11286 2062 -2593 -1256 C ATOM 2152 CD1 LEU A1106 -11.273 -37.669 25.356 1.00 72.33 C ANISOU 2152 CD1 LEU A1106 8167 8241 11076 1819 -2333 -1273 C ATOM 2153 CD2 LEU A1106 -10.968 -38.113 22.957 1.00 78.24 C ANISOU 2153 CD2 LEU A1106 9243 9025 11461 2047 -2809 -1379 C ATOM 2154 N LEU A 304 -15.173 -35.510 22.199 1.00107.19 N ANISOU 2154 N LEU A 304 25382 6218 9127 1376 805 777 N ATOM 2155 CA LEU A 304 -15.526 -34.597 21.106 1.00102.97 C ANISOU 2155 CA LEU A 304 24398 5989 8738 1177 833 631 C ATOM 2156 C LEU A 304 -16.237 -33.377 21.688 1.00101.69 C ANISOU 2156 C LEU A 304 23685 6237 8714 810 761 639 C ATOM 2157 O LEU A 304 -15.919 -32.261 21.289 1.00 99.49 O ANISOU 2157 O LEU A 304 22853 6340 8607 888 730 598 O ATOM 2158 CB LEU A 304 -16.382 -35.299 20.037 1.00104.38 C ANISOU 2158 CB LEU A 304 24998 5869 8791 845 919 484 C ATOM 2159 N MET A 305 -17.118 -33.580 22.701 1.00 97.42 N ANISOU 2159 N MET A 305 23308 5616 8090 449 741 706 N ATOM 2160 CA MET A 305 -17.834 -32.513 23.426 1.00 93.91 C ANISOU 2160 CA MET A 305 22406 5531 7743 127 690 728 C ATOM 2161 C MET A 305 -16.854 -31.456 23.947 1.00 94.65 C ANISOU 2161 C MET A 305 21993 5983 7987 479 590 800 C ATOM 2162 O MET A 305 -17.127 -30.263 23.824 1.00 92.00 O ANISOU 2162 O MET A 305 21149 6016 7792 337 553 751 O ATOM 2163 CB MET A 305 -18.653 -33.081 24.609 1.00 97.95 C ANISOU 2163 CB MET A 305 23251 5858 8107 -194 708 827 C ATOM 2164 CG MET A 305 -19.924 -33.788 24.200 1.00103.29 C ANISOU 2164 CG MET A 305 24268 6309 8669 -717 796 752 C ATOM 2165 N ALA A 306 -15.701 -31.902 24.499 1.00 91.44 N ANISOU 2165 N ALA A 306 21736 5463 7544 941 535 918 N ATOM 2166 CA ALA A 306 -14.645 -31.043 25.038 1.00 89.17 C ANISOU 2166 CA ALA A 306 21008 5492 7383 1291 414 1001 C ATOM 2167 C ALA A 306 -14.013 -30.146 23.961 1.00 90.10 C ANISOU 2167 C ALA A 306 20631 5918 7684 1463 416 913 C ATOM 2168 O ALA A 306 -13.719 -28.990 24.258 1.00 85.88 O ANISOU 2168 O ALA A 306 19604 5744 7284 1475 326 932 O ATOM 2169 CB ALA A 306 -13.574 -31.885 25.709 1.00 92.97 C ANISOU 2169 CB ALA A 306 21794 5761 7770 1760 351 1141 C ATOM 2170 N ALA A 307 -13.812 -30.664 22.721 1.00 88.86 N ANISOU 2170 N ALA A 307 20634 5611 7516 1585 524 819 N ATOM 2171 CA ALA A 307 -13.239 -29.876 21.621 1.00 87.43 C ANISOU 2171 CA ALA A 307 20031 5702 7486 1736 556 737 C ATOM 2172 C ALA A 307 -14.176 -28.734 21.266 1.00 91.81 C ANISOU 2172 C ALA A 307 20208 6535 8139 1313 546 638 C ATOM 2173 O ALA A 307 -13.724 -27.593 21.117 1.00 89.81 O ANISOU 2173 O ALA A 307 19460 6630 8034 1376 494 635 O ATOM 2174 CB ALA A 307 -12.982 -30.745 20.406 1.00 89.88 C ANISOU 2174 CB ALA A 307 20675 5754 7721 1922 691 650 C ATOM 2175 N ARG A 308 -15.495 -29.033 21.204 1.00 89.54 N ANISOU 2175 N ARG A 308 20157 6102 7764 875 586 567 N ATOM 2176 CA ARG A 308 -16.549 -28.056 20.928 1.00 86.62 C ANISOU 2176 CA ARG A 308 19467 5981 7466 467 573 476 C ATOM 2177 C ARG A 308 -16.590 -26.989 22.046 1.00 88.03 C ANISOU 2177 C ARG A 308 19263 6459 7726 406 470 555 C ATOM 2178 O ARG A 308 -16.697 -25.803 21.733 1.00 85.02 O ANISOU 2178 O ARG A 308 18455 6386 7463 327 433 505 O ATOM 2179 CB ARG A 308 -17.906 -28.765 20.766 1.00 87.85 C ANISOU 2179 CB ARG A 308 19968 5914 7498 26 630 407 C ATOM 2180 N GLU A 309 -16.437 -27.405 23.330 1.00 85.93 N ANISOU 2180 N GLU A 309 19182 6086 7381 470 420 680 N ATOM 2181 CA GLU A 309 -16.402 -26.490 24.477 1.00 84.42 C ANISOU 2181 CA GLU A 309 18705 6139 7231 442 316 759 C ATOM 2182 C GLU A 309 -15.178 -25.571 24.374 1.00 87.98 C ANISOU 2182 C GLU A 309 18742 6862 7823 765 216 791 C ATOM 2183 O GLU A 309 -15.366 -24.357 24.321 1.00 86.99 O ANISOU 2183 O GLU A 309 18230 7026 7797 640 167 751 O ATOM 2184 CB GLU A 309 -16.420 -27.242 25.819 1.00 87.80 C ANISOU 2184 CB GLU A 309 19484 6361 7514 469 285 891 C ATOM 2185 N ARG A 310 -13.945 -26.143 24.254 1.00 84.99 N ANISOU 2185 N ARG A 310 18442 6395 7454 1174 193 859 N ATOM 2186 CA ARG A 310 -12.665 -25.421 24.101 1.00 83.25 C ANISOU 2186 CA ARG A 310 17822 6439 7371 1494 106 904 C ATOM 2187 C ARG A 310 -12.743 -24.392 22.961 1.00 82.94 C ANISOU 2187 C ARG A 310 17400 6647 7464 1377 153 792 C ATOM 2188 O ARG A 310 -12.327 -23.240 23.137 1.00 79.34 O ANISOU 2188 O ARG A 310 16541 6488 7118 1375 59 809 O ATOM 2189 CB ARG A 310 -11.501 -26.402 23.847 1.00 84.54 C ANISOU 2189 CB ARG A 310 18162 6448 7513 1949 129 971 C ATOM 2190 N LYS A 311 -13.327 -24.808 21.820 1.00 79.98 N ANISOU 2190 N LYS A 311 17193 6135 7062 1256 290 677 N ATOM 2191 CA LYS A 311 -13.518 -23.984 20.630 1.00 78.59 C ANISOU 2191 CA LYS A 311 16745 6140 6975 1138 347 564 C ATOM 2192 C LYS A 311 -14.394 -22.751 20.939 1.00 82.68 C ANISOU 2192 C LYS A 311 16980 6891 7543 804 277 523 C ATOM 2193 O LYS A 311 -13.938 -21.612 20.784 1.00 81.09 O ANISOU 2193 O LYS A 311 16405 6958 7450 832 219 524 O ATOM 2194 CB LYS A 311 -14.139 -24.820 19.502 1.00 81.51 C ANISOU 2194 CB LYS A 311 17444 6268 7259 1038 483 451 C ATOM 2195 N ALA A 312 -15.622 -22.992 21.439 1.00 79.70 N ANISOU 2195 N ALA A 312 16792 6411 7078 499 285 495 N ATOM 2196 CA ALA A 312 -16.615 -21.978 21.780 1.00 76.88 C ANISOU 2196 CA ALA A 312 16219 6250 6741 199 243 454 C ATOM 2197 C ALA A 312 -16.130 -21.003 22.838 1.00 80.79 C ANISOU 2197 C ALA A 312 16458 6954 7284 272 119 536 C ATOM 2198 O ALA A 312 -16.561 -19.844 22.820 1.00 80.68 O ANISOU 2198 O ALA A 312 16181 7154 7319 126 78 491 O ATOM 2199 CB ALA A 312 -17.892 -22.643 22.244 1.00 78.15 C ANISOU 2199 CB ALA A 312 16650 6255 6788 -100 296 436 C ATOM 2200 N THR A 313 -15.250 -21.435 23.758 1.00 77.30 N ANISOU 2200 N THR A 313 16107 6447 6815 500 46 654 N ATOM 2201 CA THR A 313 -14.763 -20.497 24.777 1.00 75.71 C ANISOU 2201 CA THR A 313 15680 6442 6643 552 -100 729 C ATOM 2202 C THR A 313 -13.618 -19.652 24.204 1.00 76.27 C ANISOU 2202 C THR A 313 15397 6732 6851 735 -170 737 C ATOM 2203 O THR A 313 -13.465 -18.514 24.626 1.00 74.02 O ANISOU 2203 O THR A 313 14865 6651 6609 670 -279 747 O ATOM 2204 CB THR A 313 -14.386 -21.194 26.089 1.00 87.54 C ANISOU 2204 CB THR A 313 17415 7807 8040 686 -180 855 C ATOM 2205 OG1 THR A 313 -13.214 -21.977 25.892 1.00 93.78 O ANISOU 2205 OG1 THR A 313 18275 8504 8852 1023 -203 926 O ATOM 2206 CG2 THR A 313 -15.522 -22.053 26.649 1.00 85.34 C ANISOU 2206 CG2 THR A 313 17508 7304 7615 474 -88 858 C ATOM 2207 N LYS A 314 -12.846 -20.184 23.220 1.00 73.23 N ANISOU 2207 N LYS A 314 14997 6305 6523 949 -96 729 N ATOM 2208 CA LYS A 314 -11.744 -19.452 22.583 1.00 72.35 C ANISOU 2208 CA LYS A 314 14535 6414 6540 1110 -127 744 C ATOM 2209 C LYS A 314 -12.296 -18.279 21.788 1.00 74.42 C ANISOU 2209 C LYS A 314 14575 6840 6860 878 -98 644 C ATOM 2210 O LYS A 314 -11.771 -17.182 21.937 1.00 74.29 O ANISOU 2210 O LYS A 314 14267 7040 6918 856 -196 671 O ATOM 2211 CB LYS A 314 -10.877 -20.360 21.692 1.00 76.25 C ANISOU 2211 CB LYS A 314 15089 6821 7060 1409 -14 757 C ATOM 2212 CG LYS A 314 -9.655 -19.669 21.070 1.00 81.30 C ANISOU 2212 CG LYS A 314 15340 7719 7833 1587 -21 792 C ATOM 2213 N THR A 315 -13.371 -18.484 20.991 1.00 69.52 N ANISOU 2213 N THR A 315 14105 6115 6194 693 18 533 N ATOM 2214 CA THR A 315 -13.981 -17.399 20.210 1.00 67.38 C ANISOU 2214 CA THR A 315 13652 5988 5960 491 36 438 C ATOM 2215 C THR A 315 -14.510 -16.307 21.170 1.00 69.00 C ANISOU 2215 C THR A 315 13728 6331 6155 316 -85 448 C ATOM 2216 O THR A 315 -14.211 -15.130 20.958 1.00 65.97 O ANISOU 2216 O THR A 315 13107 6126 5831 276 -145 440 O ATOM 2217 CB THR A 315 -15.066 -17.888 19.210 1.00 79.63 C ANISOU 2217 CB THR A 315 15395 7410 7452 330 154 321 C ATOM 2218 OG1 THR A 315 -16.347 -17.346 19.540 1.00 82.86 O ANISOU 2218 OG1 THR A 315 15796 7869 7819 63 122 264 O ATOM 2219 CG2 THR A 315 -15.132 -19.410 19.052 1.00 79.19 C ANISOU 2219 CG2 THR A 315 15687 7085 7317 413 246 319 C ATOM 2220 N LEU A 316 -15.232 -16.713 22.257 1.00 66.76 N ANISOU 2220 N LEU A 316 13628 5955 5784 222 -113 474 N ATOM 2221 CA LEU A 316 -15.778 -15.802 23.281 1.00 65.17 C ANISOU 2221 CA LEU A 316 13360 5859 5541 85 -205 484 C ATOM 2222 C LEU A 316 -14.674 -14.970 23.939 1.00 65.86 C ANISOU 2222 C LEU A 316 13260 6089 5675 198 -359 564 C ATOM 2223 O LEU A 316 -14.859 -13.767 24.138 1.00 63.46 O ANISOU 2223 O LEU A 316 12816 5920 5375 95 -434 538 O ATOM 2224 CB LEU A 316 -16.573 -16.557 24.354 1.00 66.21 C ANISOU 2224 CB LEU A 316 13744 5856 5555 -3 -182 518 C ATOM 2225 CG LEU A 316 -17.300 -15.660 25.362 1.00 70.56 C ANISOU 2225 CG LEU A 316 14257 6515 6039 -142 -236 516 C ATOM 2226 CD1 LEU A 316 -18.491 -14.947 24.716 1.00 69.72 C ANISOU 2226 CD1 LEU A 316 14041 6513 5936 -332 -166 405 C ATOM 2227 CD2 LEU A 316 -17.718 -16.440 26.591 1.00 74.17 C ANISOU 2227 CD2 LEU A 316 14967 6843 6370 -178 -219 585 C ATOM 2228 N GLY A 317 -13.546 -15.615 24.234 1.00 62.72 N ANISOU 2228 N GLY A 317 12868 5657 5306 411 -412 658 N ATOM 2229 CA GLY A 317 -12.369 -14.965 24.788 1.00 63.18 C ANISOU 2229 CA GLY A 317 12719 5867 5417 520 -576 744 C ATOM 2230 C GLY A 317 -11.890 -13.869 23.865 1.00 66.74 C ANISOU 2230 C GLY A 317 12884 6499 5974 469 -585 707 C ATOM 2231 O GLY A 317 -11.702 -12.731 24.311 1.00 65.08 O ANISOU 2231 O GLY A 317 12539 6420 5770 365 -714 716 O ATOM 2232 N ILE A 318 -11.787 -14.193 22.543 1.00 64.03 N ANISOU 2232 N ILE A 318 12493 6143 5693 520 -437 656 N ATOM 2233 CA ILE A 318 -11.357 -13.258 21.496 1.00 63.48 C ANISOU 2233 CA ILE A 318 12186 6226 5709 471 -406 623 C ATOM 2234 C ILE A 318 -12.397 -12.135 21.345 1.00 67.63 C ANISOU 2234 C ILE A 318 12719 6785 6193 234 -421 533 C ATOM 2235 O ILE A 318 -11.993 -10.971 21.289 1.00 67.40 O ANISOU 2235 O ILE A 318 12521 6891 6199 150 -505 543 O ATOM 2236 CB ILE A 318 -11.035 -13.943 20.137 1.00 67.20 C ANISOU 2236 CB ILE A 318 12653 6657 6224 600 -229 589 C ATOM 2237 CG1 ILE A 318 -10.049 -15.110 20.310 1.00 70.08 C ANISOU 2237 CG1 ILE A 318 13041 6972 6614 886 -201 676 C ATOM 2238 CG2 ILE A 318 -10.452 -12.938 19.144 1.00 67.27 C ANISOU 2238 CG2 ILE A 318 12412 6837 6310 551 -194 577 C ATOM 2239 CD1 ILE A 318 -10.063 -16.131 19.159 1.00 77.29 C ANISOU 2239 CD1 ILE A 318 14109 7747 7511 1034 -4 625 C ATOM 2240 N ILE A 319 -13.715 -12.469 21.322 1.00 64.65 N ANISOU 2240 N ILE A 319 12538 6291 5734 128 -349 453 N ATOM 2241 CA ILE A 319 -14.814 -11.491 21.203 1.00 63.30 C ANISOU 2241 CA ILE A 319 12372 6163 5514 -55 -356 368 C ATOM 2242 C ILE A 319 -14.743 -10.481 22.353 1.00 67.73 C ANISOU 2242 C ILE A 319 12897 6801 6037 -115 -507 405 C ATOM 2243 O ILE A 319 -14.782 -9.269 22.097 1.00 66.73 O ANISOU 2243 O ILE A 319 12681 6760 5912 -199 -560 373 O ATOM 2244 CB ILE A 319 -16.207 -12.180 21.117 1.00 65.92 C ANISOU 2244 CB ILE A 319 12886 6389 5771 -152 -259 294 C ATOM 2245 CG1 ILE A 319 -16.457 -12.676 19.703 1.00 66.67 C ANISOU 2245 CG1 ILE A 319 13009 6434 5887 -158 -139 221 C ATOM 2246 CG2 ILE A 319 -17.358 -11.255 21.556 1.00 65.28 C ANISOU 2246 CG2 ILE A 319 12804 6376 5623 -295 -291 237 C ATOM 2247 CD1 ILE A 319 -16.978 -14.036 19.673 1.00 83.21 C ANISOU 2247 CD1 ILE A 319 15313 8367 7935 -168 -51 205 C ATOM 2248 N LEU A 320 -14.588 -10.988 23.599 1.00 65.65 N ANISOU 2248 N LEU A 320 12736 6488 5722 -65 -579 473 N ATOM 2249 CA LEU A 320 -14.512 -10.181 24.818 1.00 66.06 C ANISOU 2249 CA LEU A 320 12811 6585 5705 -111 -728 508 C ATOM 2250 C LEU A 320 -13.262 -9.305 24.829 1.00 70.70 C ANISOU 2250 C LEU A 320 13213 7291 6358 -102 -877 564 C ATOM 2251 O LEU A 320 -13.366 -8.126 25.180 1.00 70.58 O ANISOU 2251 O LEU A 320 13193 7326 6297 -208 -978 542 O ATOM 2252 CB LEU A 320 -14.592 -11.064 26.064 1.00 67.59 C ANISOU 2252 CB LEU A 320 13186 6684 5811 -50 -762 575 C ATOM 2253 CG LEU A 320 -16.012 -11.338 26.626 1.00 73.00 C ANISOU 2253 CG LEU A 320 14068 7292 6376 -146 -663 527 C ATOM 2254 CD1 LEU A 320 -17.103 -11.433 25.527 1.00 72.80 C ANISOU 2254 CD1 LEU A 320 14020 7266 6376 -244 -503 425 C ATOM 2255 CD2 LEU A 320 -16.033 -12.593 27.450 1.00 76.57 C ANISOU 2255 CD2 LEU A 320 14723 7613 6758 -83 -636 599 C ATOM 2256 N GLY A 321 -12.129 -9.847 24.373 1.00 67.68 N ANISOU 2256 N GLY A 321 12680 6957 6079 17 -879 631 N ATOM 2257 CA GLY A 321 -10.895 -9.081 24.241 1.00 68.79 C ANISOU 2257 CA GLY A 321 12588 7249 6303 3 -1002 693 C ATOM 2258 C GLY A 321 -11.082 -7.928 23.266 1.00 73.14 C ANISOU 2258 C GLY A 321 13050 7860 6881 -146 -960 628 C ATOM 2259 O GLY A 321 -10.725 -6.781 23.567 1.00 73.17 O ANISOU 2259 O GLY A 321 12997 7934 6870 -277 -1095 641 O ATOM 2260 N ALA A 322 -11.724 -8.223 22.112 1.00 69.16 N ANISOU 2260 N ALA A 322 12577 7307 6394 -136 -780 553 N ATOM 2261 CA ALA A 322 -12.037 -7.250 21.067 1.00 68.20 C ANISOU 2261 CA ALA A 322 12417 7218 6277 -253 -722 487 C ATOM 2262 C ALA A 322 -12.992 -6.165 21.583 1.00 71.56 C ANISOU 2262 C ALA A 322 12984 7608 6597 -383 -802 424 C ATOM 2263 O ALA A 322 -12.832 -4.992 21.244 1.00 70.28 O ANISOU 2263 O ALA A 322 12795 7484 6423 -493 -855 410 O ATOM 2264 CB ALA A 322 -12.647 -7.954 19.875 1.00 68.04 C ANISOU 2264 CB ALA A 322 12451 7135 6267 -200 -536 417 C ATOM 2265 N PHE A 323 -13.959 -6.560 22.421 1.00 68.10 N ANISOU 2265 N PHE A 323 12710 7093 6073 -363 -801 391 N ATOM 2266 CA PHE A 323 -14.939 -5.669 23.022 1.00 67.66 C ANISOU 2266 CA PHE A 323 12795 7010 5902 -436 -850 331 C ATOM 2267 C PHE A 323 -14.277 -4.662 23.990 1.00 74.39 C ANISOU 2267 C PHE A 323 13678 7885 6703 -503 -1038 376 C ATOM 2268 O PHE A 323 -14.662 -3.488 24.002 1.00 73.36 O ANISOU 2268 O PHE A 323 13636 7741 6498 -578 -1090 329 O ATOM 2269 CB PHE A 323 -15.996 -6.505 23.750 1.00 69.39 C ANISOU 2269 CB PHE A 323 13153 7166 6045 -396 -780 306 C ATOM 2270 CG PHE A 323 -16.714 -5.790 24.863 1.00 71.34 C ANISOU 2270 CG PHE A 323 13547 7400 6159 -425 -843 282 C ATOM 2271 CD1 PHE A 323 -16.319 -5.957 26.187 1.00 75.12 C ANISOU 2271 CD1 PHE A 323 14124 7850 6568 -405 -947 345 C ATOM 2272 CD2 PHE A 323 -17.755 -4.913 24.588 1.00 73.36 C ANISOU 2272 CD2 PHE A 323 13856 7673 6345 -452 -802 198 C ATOM 2273 CE1 PHE A 323 -16.965 -5.272 27.216 1.00 76.35 C ANISOU 2273 CE1 PHE A 323 14446 7986 6577 -419 -992 318 C ATOM 2274 CE2 PHE A 323 -18.399 -4.227 25.617 1.00 76.63 C ANISOU 2274 CE2 PHE A 323 14418 8076 6622 -443 -841 173 C ATOM 2275 CZ PHE A 323 -18.011 -4.423 26.926 1.00 75.45 C ANISOU 2275 CZ PHE A 323 14383 7889 6396 -431 -926 231 C ATOM 2276 N ILE A 324 -13.328 -5.132 24.829 1.00 73.56 N ANISOU 2276 N ILE A 324 13527 7803 6621 -469 -1151 466 N ATOM 2277 CA ILE A 324 -12.649 -4.274 25.798 1.00 74.85 C ANISOU 2277 CA ILE A 324 13726 7989 6726 -551 -1359 511 C ATOM 2278 C ILE A 324 -11.773 -3.264 25.064 1.00 79.38 C ANISOU 2278 C ILE A 324 14155 8638 7368 -681 -1431 531 C ATOM 2279 O ILE A 324 -11.861 -2.079 25.369 1.00 80.10 O ANISOU 2279 O ILE A 324 14370 8695 7371 -806 -1542 503 O ATOM 2280 CB ILE A 324 -11.857 -5.093 26.863 1.00 79.49 C ANISOU 2280 CB ILE A 324 14293 8597 7313 -472 -1484 609 C ATOM 2281 CG1 ILE A 324 -12.809 -5.741 27.912 1.00 79.72 C ANISOU 2281 CG1 ILE A 324 14558 8522 7209 -396 -1446 592 C ATOM 2282 CG2 ILE A 324 -10.731 -4.274 27.536 1.00 81.39 C ANISOU 2282 CG2 ILE A 324 14471 8913 7543 -581 -1732 676 C ATOM 2283 CD1 ILE A 324 -13.693 -4.766 28.826 1.00 85.74 C ANISOU 2283 CD1 ILE A 324 15569 9219 7790 -466 -1499 528 C ATOM 2284 N VAL A 325 -10.962 -3.722 24.093 1.00 75.37 N ANISOU 2284 N VAL A 325 13413 8223 7002 -655 -1355 578 N ATOM 2285 CA VAL A 325 -10.046 -2.879 23.312 1.00 76.01 C ANISOU 2285 CA VAL A 325 13324 8399 7158 -793 -1389 615 C ATOM 2286 C VAL A 325 -10.815 -1.750 22.556 1.00 80.71 C ANISOU 2286 C VAL A 325 14068 8916 7682 -906 -1331 529 C ATOM 2287 O VAL A 325 -10.346 -0.610 22.521 1.00 81.40 O ANISOU 2287 O VAL A 325 14177 9011 7741 -1080 -1440 545 O ATOM 2288 CB VAL A 325 -9.201 -3.772 22.351 1.00 80.02 C ANISOU 2288 CB VAL A 325 13564 9023 7817 -690 -1255 675 C ATOM 2289 CG1 VAL A 325 -8.556 -2.979 21.213 1.00 80.22 C ANISOU 2289 CG1 VAL A 325 13434 9140 7909 -826 -1196 695 C ATOM 2290 CG2 VAL A 325 -8.147 -4.554 23.122 1.00 81.53 C ANISOU 2290 CG2 VAL A 325 13577 9322 8077 -588 -1366 782 C ATOM 2291 N CYS A 326 -11.997 -2.067 22.000 1.00 77.03 N ANISOU 2291 N CYS A 326 13718 8373 7177 -811 -1176 442 N ATOM 2292 CA CYS A 326 -12.805 -1.167 21.180 1.00 76.26 C ANISOU 2292 CA CYS A 326 13751 8211 7012 -861 -1113 363 C ATOM 2293 C CYS A 326 -13.639 -0.172 21.981 1.00 77.99 C ANISOU 2293 C CYS A 326 14221 8333 7079 -892 -1213 303 C ATOM 2294 O CYS A 326 -13.655 1.009 21.626 1.00 78.12 O ANISOU 2294 O CYS A 326 14354 8296 7030 -991 -1263 281 O ATOM 2295 CB CYS A 326 -13.691 -1.979 20.243 1.00 76.21 C ANISOU 2295 CB CYS A 326 13739 8190 7028 -743 -928 299 C ATOM 2296 SG CYS A 326 -12.781 -2.894 18.966 1.00 80.98 S ANISOU 2296 SG CYS A 326 14123 8875 7771 -696 -778 346 S ATOM 2297 N TRP A 327 -14.349 -0.640 23.028 1.00 72.51 N ANISOU 2297 N TRP A 327 13635 7604 6313 -799 -1227 277 N ATOM 2298 CA TRP A 327 -15.279 0.177 23.817 1.00 71.25 C ANISOU 2298 CA TRP A 327 13720 7361 5993 -777 -1280 212 C ATOM 2299 C TRP A 327 -14.737 0.779 25.136 1.00 73.26 C ANISOU 2299 C TRP A 327 14123 7566 6145 -850 -1471 245 C ATOM 2300 O TRP A 327 -15.404 1.663 25.670 1.00 72.93 O ANISOU 2300 O TRP A 327 14323 7436 5951 -832 -1515 187 O ATOM 2301 CB TRP A 327 -16.542 -0.640 24.147 1.00 69.54 C ANISOU 2301 CB TRP A 327 13544 7147 5733 -637 -1150 159 C ATOM 2302 CG TRP A 327 -17.508 -0.808 23.010 1.00 69.63 C ANISOU 2302 CG TRP A 327 13502 7184 5770 -576 -1000 91 C ATOM 2303 CD1 TRP A 327 -17.986 -1.983 22.504 1.00 71.77 C ANISOU 2303 CD1 TRP A 327 13656 7498 6114 -526 -867 78 C ATOM 2304 CD2 TRP A 327 -18.141 0.240 22.261 1.00 69.33 C ANISOU 2304 CD2 TRP A 327 13552 7121 5667 -559 -988 27 C ATOM 2305 NE1 TRP A 327 -18.871 -1.732 21.477 1.00 69.96 N ANISOU 2305 NE1 TRP A 327 13415 7291 5874 -495 -785 8 N ATOM 2306 CE2 TRP A 327 -18.981 -0.376 21.305 1.00 71.64 C ANISOU 2306 CE2 TRP A 327 13746 7468 6004 -498 -857 -22 C ATOM 2307 CE3 TRP A 327 -18.074 1.645 22.299 1.00 71.26 C ANISOU 2307 CE3 TRP A 327 13978 7288 5808 -590 -1087 6 C ATOM 2308 CZ2 TRP A 327 -19.767 0.363 20.419 1.00 70.51 C ANISOU 2308 CZ2 TRP A 327 13655 7327 5807 -447 -831 -86 C ATOM 2309 CZ3 TRP A 327 -18.832 2.370 21.396 1.00 72.15 C ANISOU 2309 CZ3 TRP A 327 14166 7382 5867 -528 -1046 -55 C ATOM 2310 CH2 TRP A 327 -19.663 1.730 20.467 1.00 71.75 C ANISOU 2310 CH2 TRP A 327 13989 7408 5866 -449 -924 -98 C ATOM 2311 N LEU A 328 -13.600 0.301 25.696 1.00 69.01 N ANISOU 2311 N LEU A 328 13463 7086 5674 -911 -1589 334 N ATOM 2312 CA LEU A 328 -13.078 0.868 26.949 1.00 68.91 C ANISOU 2312 CA LEU A 328 13604 7029 5549 -997 -1802 364 C ATOM 2313 C LEU A 328 -12.580 2.305 26.755 1.00 73.74 C ANISOU 2313 C LEU A 328 14337 7579 6100 -1186 -1943 356 C ATOM 2314 O LEU A 328 -12.956 3.146 27.579 1.00 74.80 O ANISOU 2314 O LEU A 328 14766 7595 6059 -1211 -2049 309 O ATOM 2315 CB LEU A 328 -11.978 0.018 27.610 1.00 69.62 C ANISOU 2315 CB LEU A 328 13523 7212 5718 -1008 -1925 467 C ATOM 2316 CG LEU A 328 -11.492 0.513 28.993 1.00 75.35 C ANISOU 2316 CG LEU A 328 14429 7896 6306 -1093 -2170 497 C ATOM 2317 CD1 LEU A 328 -12.284 -0.108 30.119 1.00 74.92 C ANISOU 2317 CD1 LEU A 328 14576 7774 6115 -944 -2141 476 C ATOM 2318 CD2 LEU A 328 -10.008 0.259 29.195 1.00 78.79 C ANISOU 2318 CD2 LEU A 328 14622 8465 6851 -1196 -2360 610 C ATOM 2319 N PRO A 329 -11.748 2.634 25.726 1.00 69.53 N ANISOU 2319 N PRO A 329 13620 7112 5688 -1328 -1943 401 N ATOM 2320 CA PRO A 329 -11.273 4.019 25.603 1.00 70.78 C ANISOU 2320 CA PRO A 329 13934 7189 5769 -1548 -2083 401 C ATOM 2321 C PRO A 329 -12.428 5.014 25.533 1.00 73.66 C ANISOU 2321 C PRO A 329 14654 7375 5959 -1485 -2040 296 C ATOM 2322 O PRO A 329 -12.462 5.937 26.344 1.00 74.11 O ANISOU 2322 O PRO A 329 15010 7298 5851 -1564 -2193 267 O ATOM 2323 CB PRO A 329 -10.443 4.003 24.313 1.00 72.92 C ANISOU 2323 CB PRO A 329 13929 7573 6203 -1669 -2004 464 C ATOM 2324 CG PRO A 329 -10.048 2.589 24.131 1.00 76.44 C ANISOU 2324 CG PRO A 329 14048 8184 6814 -1533 -1904 522 C ATOM 2325 CD PRO A 329 -11.192 1.790 24.646 1.00 70.21 C ANISOU 2325 CD PRO A 329 13376 7335 5964 -1301 -1808 456 C ATOM 2326 N PHE A 330 -13.413 4.766 24.638 1.00 68.59 N ANISOU 2326 N PHE A 330 13990 6730 5340 -1319 -1838 238 N ATOM 2327 CA PHE A 330 -14.577 5.623 24.455 1.00 67.89 C ANISOU 2327 CA PHE A 330 14190 6506 5098 -1204 -1782 143 C ATOM 2328 C PHE A 330 -15.303 5.876 25.777 1.00 73.05 C ANISOU 2328 C PHE A 330 15116 7068 5571 -1085 -1841 85 C ATOM 2329 O PHE A 330 -15.537 7.041 26.115 1.00 73.51 O ANISOU 2329 O PHE A 330 15506 6967 5456 -1104 -1931 38 O ATOM 2330 CB PHE A 330 -15.558 5.063 23.403 1.00 67.71 C ANISOU 2330 CB PHE A 330 14041 6545 5140 -1025 -1574 95 C ATOM 2331 CG PHE A 330 -16.793 5.932 23.266 1.00 69.02 C ANISOU 2331 CG PHE A 330 14474 6603 5147 -869 -1530 3 C ATOM 2332 CD1 PHE A 330 -16.813 7.007 22.387 1.00 71.44 C ANISOU 2332 CD1 PHE A 330 14950 6805 5390 -915 -1548 -14 C ATOM 2333 CD2 PHE A 330 -17.914 5.714 24.071 1.00 71.16 C ANISOU 2333 CD2 PHE A 330 14840 6880 5317 -667 -1471 -61 C ATOM 2334 CE1 PHE A 330 -17.937 7.834 22.299 1.00 72.86 C ANISOU 2334 CE1 PHE A 330 15391 6882 5411 -729 -1521 -94 C ATOM 2335 CE2 PHE A 330 -19.033 6.553 23.987 1.00 73.86 C ANISOU 2335 CE2 PHE A 330 15408 7147 5508 -488 -1430 -141 C ATOM 2336 CZ PHE A 330 -19.036 7.603 23.102 1.00 72.15 C ANISOU 2336 CZ PHE A 330 15360 6822 5232 -505 -1463 -159 C ATOM 2337 N PHE A 331 -15.668 4.808 26.511 1.00 70.54 N ANISOU 2337 N PHE A 331 14692 6834 5275 -958 -1780 89 N ATOM 2338 CA PHE A 331 -16.393 4.967 27.773 1.00 71.66 C ANISOU 2338 CA PHE A 331 15088 6905 5234 -834 -1801 40 C ATOM 2339 C PHE A 331 -15.521 5.511 28.887 1.00 78.21 C ANISOU 2339 C PHE A 331 16125 7644 5947 -984 -2031 70 C ATOM 2340 O PHE A 331 -16.072 6.163 29.770 1.00 79.91 O ANISOU 2340 O PHE A 331 16670 7736 5954 -906 -2072 11 O ATOM 2341 CB PHE A 331 -17.120 3.696 28.200 1.00 72.45 C ANISOU 2341 CB PHE A 331 15045 7112 5372 -675 -1648 39 C ATOM 2342 CG PHE A 331 -18.355 3.492 27.353 1.00 72.53 C ANISOU 2342 CG PHE A 331 14966 7180 5412 -515 -1442 -24 C ATOM 2343 CD1 PHE A 331 -19.512 4.222 27.596 1.00 75.95 C ANISOU 2343 CD1 PHE A 331 15607 7567 5685 -350 -1371 -106 C ATOM 2344 CD2 PHE A 331 -18.350 2.596 26.294 1.00 73.00 C ANISOU 2344 CD2 PHE A 331 14739 7348 5652 -522 -1328 -2 C ATOM 2345 CE1 PHE A 331 -20.640 4.057 26.794 1.00 76.26 C ANISOU 2345 CE1 PHE A 331 15525 7693 5756 -205 -1206 -159 C ATOM 2346 CE2 PHE A 331 -19.485 2.418 25.504 1.00 75.36 C ANISOU 2346 CE2 PHE A 331 14955 7708 5969 -398 -1170 -61 C ATOM 2347 CZ PHE A 331 -20.617 3.163 25.746 1.00 74.03 C ANISOU 2347 CZ PHE A 331 14955 7519 5654 -246 -1119 -136 C ATOM 2348 N ILE A 332 -14.182 5.360 28.808 1.00 76.28 N ANISOU 2348 N ILE A 332 15705 7458 5819 -1197 -2186 158 N ATOM 2349 CA ILE A 332 -13.303 5.966 29.815 1.00 79.59 C ANISOU 2349 CA ILE A 332 16315 7802 6123 -1380 -2445 189 C ATOM 2350 C ILE A 332 -13.275 7.502 29.589 1.00 84.85 C ANISOU 2350 C ILE A 332 17314 8282 6644 -1520 -2549 138 C ATOM 2351 O ILE A 332 -13.370 8.249 30.561 1.00 84.31 O ANISOU 2351 O ILE A 332 17616 8056 6361 -1549 -2692 93 O ATOM 2352 CB ILE A 332 -11.883 5.299 29.876 1.00 84.05 C ANISOU 2352 CB ILE A 332 16551 8525 6857 -1556 -2595 307 C ATOM 2353 CG1 ILE A 332 -11.787 4.305 31.049 1.00 85.20 C ANISOU 2353 CG1 ILE A 332 16671 8731 6970 -1450 -2658 347 C ATOM 2354 CG2 ILE A 332 -10.748 6.321 30.033 1.00 87.69 C ANISOU 2354 CG2 ILE A 332 17095 8943 7280 -1867 -2855 349 C ATOM 2355 CD1 ILE A 332 -12.817 3.214 31.128 1.00 94.01 C ANISOU 2355 CD1 ILE A 332 17733 9884 8104 -1192 -2427 321 C ATOM 2356 N ILE A 333 -13.219 7.938 28.308 1.00 83.48 N ANISOU 2356 N ILE A 333 17048 8106 6565 -1587 -2465 140 N ATOM 2357 CA ILE A 333 -13.180 9.338 27.847 1.00 86.15 C ANISOU 2357 CA ILE A 333 17696 8255 6780 -1724 -2537 105 C ATOM 2358 C ILE A 333 -14.514 10.069 28.147 1.00 91.72 C ANISOU 2358 C ILE A 333 18814 8775 7260 -1474 -2455 -11 C ATOM 2359 O ILE A 333 -14.467 11.187 28.635 1.00 91.71 O ANISOU 2359 O ILE A 333 19229 8560 7055 -1554 -2595 -53 O ATOM 2360 CB ILE A 333 -12.814 9.419 26.312 1.00 88.94 C ANISOU 2360 CB ILE A 333 17814 8678 7301 -1832 -2429 151 C ATOM 2361 CG1 ILE A 333 -11.411 8.821 25.961 1.00 90.44 C ANISOU 2361 CG1 ILE A 333 17592 9066 7706 -2077 -2495 271 C ATOM 2362 CG2 ILE A 333 -12.962 10.824 25.733 1.00 90.64 C ANISOU 2362 CG2 ILE A 333 18391 8675 7373 -1935 -2467 115 C ATOM 2363 CD1 ILE A 333 -10.169 9.157 26.919 1.00102.27 C ANISOU 2363 CD1 ILE A 333 19105 10578 9175 -2377 -2778 340 C ATOM 2364 N SER A 334 -15.684 9.441 27.858 1.00 89.72 N ANISOU 2364 N SER A 334 18445 8608 7038 -1174 -2233 -60 N ATOM 2365 CA SER A 334 -17.028 10.017 28.050 1.00 90.60 C ANISOU 2365 CA SER A 334 18855 8608 6962 -889 -2122 -162 C ATOM 2366 C SER A 334 -17.410 10.184 29.521 1.00 98.51 C ANISOU 2366 C SER A 334 20160 9521 7750 -775 -2177 -212 C ATOM 2367 O SER A 334 -18.408 10.845 29.802 1.00 99.08 O ANISOU 2367 O SER A 334 20535 9481 7631 -540 -2101 -296 O ATOM 2368 CB SER A 334 -18.085 9.177 27.340 1.00 92.70 C ANISOU 2368 CB SER A 334 18833 9045 7345 -644 -1885 -186 C ATOM 2369 OG SER A 334 -18.167 7.874 27.885 1.00101.65 O ANISOU 2369 OG SER A 334 19692 10350 8582 -596 -1807 -155 O ATOM 2370 N LEU A 335 -16.635 9.573 30.447 1.00 97.76 N ANISOU 2370 N LEU A 335 19987 9480 7676 -917 -2302 -157 N ATOM 2371 CA LEU A 335 -16.775 9.672 31.903 1.00 99.30 C ANISOU 2371 CA LEU A 335 20485 9588 7658 -857 -2387 -190 C ATOM 2372 C LEU A 335 -15.804 10.743 32.409 1.00108.87 C ANISOU 2372 C LEU A 335 22052 10597 8717 -1122 -2671 -188 C ATOM 2373 O LEU A 335 -16.108 11.449 33.368 1.00110.83 O ANISOU 2373 O LEU A 335 22748 10660 8701 -1055 -2748 -255 O ATOM 2374 CB LEU A 335 -16.498 8.310 32.560 1.00 98.21 C ANISOU 2374 CB LEU A 335 20060 9628 7626 -856 -2370 -122 C ATOM 2375 CG LEU A 335 -16.637 8.256 34.084 1.00104.34 C ANISOU 2375 CG LEU A 335 21138 10331 8176 -789 -2447 -143 C ATOM 2376 CD1 LEU A 335 -17.966 7.682 34.497 1.00103.38 C ANISOU 2376 CD1 LEU A 335 21023 10281 7977 -486 -2184 -190 C ATOM 2377 CD2 LEU A 335 -15.501 7.479 34.711 1.00107.59 C ANISOU 2377 CD2 LEU A 335 21383 10829 8666 -977 -2639 -46 C ATOM 2378 N VAL A 336 -14.643 10.868 31.738 1.00108.32 N ANISOU 2378 N VAL A 336 21786 10564 8807 -1432 -2818 -110 N ATOM 2379 CA VAL A 336 -13.593 11.856 32.013 1.00112.17 C ANISOU 2379 CA VAL A 336 22535 10892 9193 -1768 -3099 -90 C ATOM 2380 C VAL A 336 -14.077 13.238 31.512 1.00120.11 C ANISOU 2380 C VAL A 336 23983 11632 10021 -1751 -3088 -167 C ATOM 2381 O VAL A 336 -13.873 14.231 32.207 1.00123.56 O ANISOU 2381 O VAL A 336 24900 11827 10219 -1871 -3274 -214 O ATOM 2382 CB VAL A 336 -12.241 11.403 31.377 1.00116.39 C ANISOU 2382 CB VAL A 336 22622 11614 9986 -2090 -3215 33 C ATOM 2383 CG1 VAL A 336 -11.355 12.576 30.957 1.00118.77 C ANISOU 2383 CG1 VAL A 336 23111 11773 10244 -2457 -3409 59 C ATOM 2384 CG2 VAL A 336 -11.483 10.461 32.306 1.00116.65 C ANISOU 2384 CG2 VAL A 336 22420 11816 10086 -2164 -3363 106 C ATOM 2385 N MET A 337 -14.721 13.279 30.321 1.00115.73 N ANISOU 2385 N MET A 337 23292 11112 9568 -1595 -2881 -181 N ATOM 2386 CA MET A 337 -15.321 14.436 29.639 1.00117.01 C ANISOU 2386 CA MET A 337 23821 11050 9586 -1504 -2829 -244 C ATOM 2387 C MET A 337 -16.054 15.354 30.655 1.00124.74 C ANISOU 2387 C MET A 337 25404 11763 10230 -1304 -2875 -353 C ATOM 2388 O MET A 337 -15.613 16.495 30.789 1.00126.71 O ANISOU 2388 O MET A 337 26107 11741 10297 -1498 -3053 -375 O ATOM 2389 CB MET A 337 -16.244 13.937 28.502 1.00117.15 C ANISOU 2389 CB MET A 337 23543 11218 9752 -1230 -2567 -254 C ATOM 2390 CG MET A 337 -17.294 14.909 28.026 1.00121.60 C ANISOU 2390 CG MET A 337 24471 11593 10137 -962 -2471 -337 C ATOM 2391 SD MET A 337 -18.797 14.000 27.603 1.00123.15 S ANISOU 2391 SD MET A 337 24335 12029 10428 -510 -2178 -383 S ATOM 2392 CE MET A 337 -19.854 15.348 27.234 1.00121.82 C ANISOU 2392 CE MET A 337 24658 11620 10009 -199 -2130 -475 C ATOM 2393 N PRO A 338 -17.050 14.888 31.467 1.00123.08 N ANISOU 2393 N PRO A 338 25234 11612 9917 -959 -2734 -417 N ATOM 2394 CA PRO A 338 -17.660 15.781 32.479 1.00125.53 C ANISOU 2394 CA PRO A 338 26140 11668 9888 -764 -2770 -521 C ATOM 2395 C PRO A 338 -16.675 16.425 33.476 1.00131.58 C ANISOU 2395 C PRO A 338 27321 12214 10460 -1077 -3069 -524 C ATOM 2396 O PRO A 338 -16.899 17.581 33.841 1.00134.45 O ANISOU 2396 O PRO A 338 28281 12267 10539 -1029 -3152 -605 O ATOM 2397 CB PRO A 338 -18.618 14.852 33.232 1.00126.28 C ANISOU 2397 CB PRO A 338 26062 11952 9965 -428 -2567 -552 C ATOM 2398 CG PRO A 338 -18.997 13.821 32.224 1.00128.24 C ANISOU 2398 CG PRO A 338 25723 12494 10510 -338 -2365 -499 C ATOM 2399 CD PRO A 338 -17.720 13.569 31.474 1.00122.88 C ANISOU 2399 CD PRO A 338 24749 11879 10062 -726 -2517 -401 C ATOM 2400 N ILE A 339 -15.602 15.703 33.914 1.00126.25 N ANISOU 2400 N ILE A 339 26355 11690 9923 -1387 -3242 -439 N ATOM 2401 CA ILE A 339 -14.577 16.228 34.840 1.00121.64 C ANISOU 2401 CA ILE A 339 26099 10941 9176 -1729 -3566 -431 C ATOM 2402 C ILE A 339 -13.768 17.307 34.119 1.00153.46 C ANISOU 2402 C ILE A 339 30339 14774 13194 -2098 -3751 -407 C ATOM 2403 O ILE A 339 -13.924 18.490 34.404 1.00121.33 O ANISOU 2403 O ILE A 339 26884 10372 8846 -2125 -3856 -485 O ATOM 2404 CB ILE A 339 -13.656 15.096 35.389 1.00123.55 C ANISOU 2404 CB ILE A 339 25902 11444 9596 -1933 -3702 -332 C ATOM 2405 CG1 ILE A 339 -14.424 14.125 36.296 1.00122.40 C ANISOU 2405 CG1 ILE A 339 25677 11432 9397 -1602 -3545 -356 C ATOM 2406 CG2 ILE A 339 -12.416 15.651 36.104 1.00127.10 C ANISOU 2406 CG2 ILE A 339 26589 11773 9930 -2361 -4081 -301 C ATOM 2407 CD1 ILE A 339 -13.965 12.680 36.167 1.00127.20 C ANISOU 2407 CD1 ILE A 339 25667 12368 10296 -1639 -3502 -246 C ATOM 2408 N HIS A 347 -9.025 16.942 23.139 1.00103.47 N ANISOU 2408 N HIS A 347 21272 9439 8604 -3820 -3059 364 N ATOM 2409 CA HIS A 347 -9.240 17.225 21.722 1.00102.80 C ANISOU 2409 CA HIS A 347 21200 9314 8545 -3800 -2865 396 C ATOM 2410 C HIS A 347 -10.398 16.385 21.140 1.00102.41 C ANISOU 2410 C HIS A 347 20969 9375 8568 -3311 -2626 332 C ATOM 2411 O HIS A 347 -10.620 15.237 21.550 1.00 99.28 O ANISOU 2411 O HIS A 347 20200 9208 8314 -3091 -2564 314 O ATOM 2412 CB HIS A 347 -7.952 17.005 20.912 1.00105.10 C ANISOU 2412 CB HIS A 347 21065 9832 9036 -4191 -2822 539 C ATOM 2413 CG HIS A 347 -7.954 17.678 19.570 1.00109.51 C ANISOU 2413 CG HIS A 347 21795 10268 9547 -4305 -2676 586 C ATOM 2414 ND1 HIS A 347 -7.655 16.979 18.417 1.00110.33 N ANISOU 2414 ND1 HIS A 347 21469 10613 9838 -4285 -2452 662 N ATOM 2415 CD2 HIS A 347 -8.218 18.968 19.242 1.00113.40 C ANISOU 2415 CD2 HIS A 347 22875 10407 9806 -4429 -2727 569 C ATOM 2416 CE1 HIS A 347 -7.743 17.859 17.428 1.00110.91 C ANISOU 2416 CE1 HIS A 347 21869 10486 9788 -4407 -2372 691 C ATOM 2417 NE2 HIS A 347 -8.081 19.068 17.875 1.00113.31 N ANISOU 2417 NE2 HIS A 347 22789 10426 9839 -4496 -2535 641 N ATOM 2418 N LEU A 348 -11.131 16.987 20.178 1.00 97.90 N ANISOU 2418 N LEU A 348 20684 8629 7884 -3157 -2507 302 N ATOM 2419 CA LEU A 348 -12.308 16.424 19.511 1.00 94.14 C ANISOU 2419 CA LEU A 348 20113 8221 7435 -2720 -2310 238 C ATOM 2420 C LEU A 348 -11.965 15.249 18.597 1.00 95.87 C ANISOU 2420 C LEU A 348 19768 8753 7906 -2705 -2127 302 C ATOM 2421 O LEU A 348 -12.827 14.387 18.407 1.00 92.42 O ANISOU 2421 O LEU A 348 19126 8449 7539 -2366 -1997 246 O ATOM 2422 CB LEU A 348 -13.049 17.505 18.713 1.00 94.65 C ANISOU 2422 CB LEU A 348 20667 8005 7292 -2593 -2273 202 C ATOM 2423 CG LEU A 348 -13.662 18.639 19.532 1.00 99.94 C ANISOU 2423 CG LEU A 348 21955 8337 7681 -2479 -2418 117 C ATOM 2424 CD1 LEU A 348 -12.800 19.879 19.454 1.00104.00 C ANISOU 2424 CD1 LEU A 348 22908 8567 8042 -2900 -2566 175 C ATOM 2425 CD2 LEU A 348 -15.053 18.972 19.041 1.00 99.01 C ANISOU 2425 CD2 LEU A 348 22106 8097 7417 -2021 -2319 32 C ATOM 2426 N ALA A 349 -10.725 15.203 18.045 1.00 94.86 N ANISOU 2426 N ALA A 349 19394 8744 7904 -3069 -2111 419 N ATOM 2427 CA ALA A 349 -10.253 14.110 17.176 1.00 94.11 C ANISOU 2427 CA ALA A 349 18779 8942 8035 -3062 -1926 486 C ATOM 2428 C ALA A 349 -10.154 12.791 17.942 1.00 99.10 C ANISOU 2428 C ALA A 349 18979 9829 8845 -2909 -1921 475 C ATOM 2429 O ALA A 349 -10.467 11.739 17.385 1.00 97.14 O ANISOU 2429 O ALA A 349 18424 9757 8728 -2690 -1753 466 O ATOM 2430 CB ALA A 349 -8.906 14.450 16.574 1.00 97.21 C ANISOU 2430 CB ALA A 349 19016 9414 8504 -3489 -1912 618 C ATOM 2431 N ILE A 350 -9.714 12.855 19.219 1.00 98.17 N ANISOU 2431 N ILE A 350 18873 9712 8714 -3032 -2114 478 N ATOM 2432 CA ILE A 350 -9.592 11.717 20.132 1.00 97.10 C ANISOU 2432 CA ILE A 350 18407 9778 8709 -2899 -2149 474 C ATOM 2433 C ILE A 350 -10.974 11.077 20.267 1.00 99.40 C ANISOU 2433 C ILE A 350 18751 10051 8965 -2478 -2035 366 C ATOM 2434 O ILE A 350 -11.093 9.867 20.077 1.00 98.03 O ANISOU 2434 O ILE A 350 18230 10072 8944 -2304 -1908 372 O ATOM 2435 CB ILE A 350 -8.990 12.189 21.498 1.00102.40 C ANISOU 2435 CB ILE A 350 19219 10387 9301 -3118 -2415 485 C ATOM 2436 CG1 ILE A 350 -7.478 12.548 21.393 1.00105.92 C ANISOU 2436 CG1 ILE A 350 19461 10948 9836 -3567 -2535 611 C ATOM 2437 CG2 ILE A 350 -9.284 11.228 22.659 1.00101.31 C ANISOU 2437 CG2 ILE A 350 18938 10356 9199 -2897 -2473 447 C ATOM 2438 CD1 ILE A 350 -6.474 11.382 20.995 1.00114.51 C ANISOU 2438 CD1 ILE A 350 19915 12400 11193 -3609 -2437 721 C ATOM 2439 N PHE A 351 -12.018 11.902 20.520 1.00 96.39 N ANISOU 2439 N PHE A 351 18807 9438 8379 -2318 -2071 273 N ATOM 2440 CA PHE A 351 -13.412 11.468 20.633 1.00 94.48 C ANISOU 2440 CA PHE A 351 18625 9187 8084 -1930 -1964 172 C ATOM 2441 C PHE A 351 -13.934 10.892 19.290 1.00 96.46 C ANISOU 2441 C PHE A 351 18674 9544 8431 -1765 -1760 167 C ATOM 2442 O PHE A 351 -14.586 9.842 19.291 1.00 93.40 O ANISOU 2442 O PHE A 351 18054 9301 8131 -1538 -1650 129 O ATOM 2443 CB PHE A 351 -14.322 12.611 21.125 1.00 97.34 C ANISOU 2443 CB PHE A 351 19501 9288 8196 -1788 -2043 83 C ATOM 2444 CG PHE A 351 -15.071 12.317 22.408 1.00 98.55 C ANISOU 2444 CG PHE A 351 19747 9437 8263 -1560 -2078 7 C ATOM 2445 CD1 PHE A 351 -15.834 11.157 22.542 1.00 99.81 C ANISOU 2445 CD1 PHE A 351 19617 9785 8523 -1302 -1940 -26 C ATOM 2446 CD2 PHE A 351 -15.035 13.209 23.471 1.00102.60 C ANISOU 2446 CD2 PHE A 351 20665 9745 8576 -1613 -2242 -31 C ATOM 2447 CE1 PHE A 351 -16.511 10.876 23.730 1.00100.48 C ANISOU 2447 CE1 PHE A 351 19786 9874 8519 -1111 -1950 -85 C ATOM 2448 CE2 PHE A 351 -15.729 12.939 24.653 1.00105.59 C ANISOU 2448 CE2 PHE A 351 21146 10121 8854 -1393 -2252 -99 C ATOM 2449 CZ PHE A 351 -16.450 11.767 24.779 1.00101.85 C ANISOU 2449 CZ PHE A 351 20352 9856 8491 -1148 -2099 -120 C ATOM 2450 N ASP A 352 -13.616 11.550 18.156 1.00 93.56 N ANISOU 2450 N ASP A 352 18410 9102 8037 -1901 -1716 208 N ATOM 2451 CA ASP A 352 -14.027 11.063 16.837 1.00 92.20 C ANISOU 2451 CA ASP A 352 18085 9017 7929 -1768 -1540 206 C ATOM 2452 C ASP A 352 -13.365 9.717 16.513 1.00 92.72 C ANISOU 2452 C ASP A 352 17676 9336 8217 -1803 -1422 261 C ATOM 2453 O ASP A 352 -13.996 8.864 15.884 1.00 91.39 O ANISOU 2453 O ASP A 352 17342 9270 8112 -1601 -1288 223 O ATOM 2454 CB ASP A 352 -13.701 12.092 15.734 1.00 96.48 C ANISOU 2454 CB ASP A 352 18874 9410 8373 -1934 -1519 253 C ATOM 2455 CG ASP A 352 -14.797 13.109 15.447 1.00110.71 C ANISOU 2455 CG ASP A 352 21124 10984 9958 -1734 -1553 181 C ATOM 2456 OD1 ASP A 352 -15.992 12.726 15.489 1.00111.63 O ANISOU 2456 OD1 ASP A 352 21228 11141 10046 -1401 -1510 96 O ATOM 2457 OD2 ASP A 352 -14.460 14.267 15.106 1.00116.25 O ANISOU 2457 OD2 ASP A 352 22180 11473 10518 -1910 -1615 218 O ATOM 2458 N PHE A 353 -12.102 9.529 16.947 1.00 87.57 N ANISOU 2458 N PHE A 353 16814 8784 7674 -2052 -1482 348 N ATOM 2459 CA PHE A 353 -11.356 8.304 16.689 1.00 85.76 C ANISOU 2459 CA PHE A 353 16147 8792 7647 -2064 -1375 410 C ATOM 2460 C PHE A 353 -11.906 7.166 17.517 1.00 87.06 C ANISOU 2460 C PHE A 353 16148 9052 7879 -1832 -1370 359 C ATOM 2461 O PHE A 353 -12.043 6.060 17.002 1.00 86.08 O ANISOU 2461 O PHE A 353 15785 9054 7865 -1687 -1227 355 O ATOM 2462 CB PHE A 353 -9.848 8.491 16.955 1.00 89.71 C ANISOU 2462 CB PHE A 353 16446 9400 8241 -2382 -1455 526 C ATOM 2463 CG PHE A 353 -9.027 7.240 16.740 1.00 91.31 C ANISOU 2463 CG PHE A 353 16188 9860 8647 -2350 -1345 596 C ATOM 2464 CD1 PHE A 353 -8.605 6.873 15.466 1.00 94.52 C ANISOU 2464 CD1 PHE A 353 16404 10377 9134 -2359 -1144 644 C ATOM 2465 CD2 PHE A 353 -8.690 6.416 17.810 1.00 93.50 C ANISOU 2465 CD2 PHE A 353 16250 10260 9017 -2284 -1437 613 C ATOM 2466 CE1 PHE A 353 -7.876 5.691 15.265 1.00 95.77 C ANISOU 2466 CE1 PHE A 353 16161 10762 9465 -2280 -1027 703 C ATOM 2467 CE2 PHE A 353 -7.966 5.232 17.608 1.00 96.39 C ANISOU 2467 CE2 PHE A 353 16218 10847 9558 -2204 -1334 677 C ATOM 2468 CZ PHE A 353 -7.562 4.879 16.338 1.00 94.81 C ANISOU 2468 CZ PHE A 353 15831 10753 9438 -2194 -1126 719 C ATOM 2469 N PHE A 354 -12.217 7.421 18.788 1.00 82.86 N ANISOU 2469 N PHE A 354 15773 8445 7266 -1802 -1519 322 N ATOM 2470 CA PHE A 354 -12.706 6.373 19.670 1.00 80.87 C ANISOU 2470 CA PHE A 354 15394 8272 7059 -1608 -1512 286 C ATOM 2471 C PHE A 354 -14.139 5.941 19.358 1.00 81.16 C ANISOU 2471 C PHE A 354 15498 8290 7051 -1335 -1387 191 C ATOM 2472 O PHE A 354 -14.421 4.772 19.570 1.00 80.02 O ANISOU 2472 O PHE A 354 15159 8251 6993 -1203 -1310 181 O ATOM 2473 CB PHE A 354 -12.543 6.762 21.139 1.00 84.02 C ANISOU 2473 CB PHE A 354 15951 8603 7368 -1669 -1703 283 C ATOM 2474 CG PHE A 354 -11.091 6.795 21.558 1.00 88.00 C ANISOU 2474 CG PHE A 354 16280 9200 7958 -1927 -1842 385 C ATOM 2475 CD1 PHE A 354 -10.157 5.954 20.961 1.00 91.58 C ANISOU 2475 CD1 PHE A 354 16347 9850 8598 -1979 -1759 472 C ATOM 2476 CD2 PHE A 354 -10.663 7.635 22.574 1.00 93.03 C ANISOU 2476 CD2 PHE A 354 17129 9737 8480 -2106 -2061 395 C ATOM 2477 CE1 PHE A 354 -8.813 5.995 21.332 1.00 94.83 C ANISOU 2477 CE1 PHE A 354 16544 10389 9096 -2206 -1891 575 C ATOM 2478 CE2 PHE A 354 -9.321 7.657 22.965 1.00 98.30 C ANISOU 2478 CE2 PHE A 354 17600 10520 9231 -2363 -2215 494 C ATOM 2479 CZ PHE A 354 -8.402 6.851 22.326 1.00 96.57 C ANISOU 2479 CZ PHE A 354 16952 10527 9212 -2411 -2128 588 C ATOM 2480 N THR A 355 -15.025 6.827 18.820 1.00 76.91 N ANISOU 2480 N THR A 355 15221 7625 6378 -1251 -1370 128 N ATOM 2481 CA THR A 355 -16.403 6.441 18.432 1.00 74.48 C ANISOU 2481 CA THR A 355 14929 7338 6033 -997 -1263 42 C ATOM 2482 C THR A 355 -16.306 5.384 17.328 1.00 76.33 C ANISOU 2482 C THR A 355 14895 7702 6404 -971 -1116 58 C ATOM 2483 O THR A 355 -16.981 4.358 17.398 1.00 75.48 O ANISOU 2483 O THR A 355 14643 7686 6351 -832 -1036 19 O ATOM 2484 CB THR A 355 -17.270 7.641 17.964 1.00 79.21 C ANISOU 2484 CB THR A 355 15845 7791 6460 -893 -1287 -16 C ATOM 2485 OG1 THR A 355 -16.699 8.196 16.783 1.00 86.68 O ANISOU 2485 OG1 THR A 355 16850 8681 7401 -1028 -1265 29 O ATOM 2486 CG2 THR A 355 -17.451 8.725 19.018 1.00 72.64 C ANISOU 2486 CG2 THR A 355 15344 6797 5460 -883 -1421 -45 C ATOM 2487 N TRP A 356 -15.404 5.632 16.340 1.00 71.52 N ANISOU 2487 N TRP A 356 14237 7096 5841 -1125 -1077 120 N ATOM 2488 CA TRP A 356 -15.102 4.766 15.206 1.00 69.50 C ANISOU 2488 CA TRP A 356 13773 6944 5691 -1117 -930 142 C ATOM 2489 C TRP A 356 -14.366 3.525 15.653 1.00 73.15 C ANISOU 2489 C TRP A 356 13947 7539 6308 -1126 -884 190 C ATOM 2490 O TRP A 356 -14.543 2.479 15.040 1.00 73.32 O ANISOU 2490 O TRP A 356 13825 7633 6401 -1028 -761 173 O ATOM 2491 CB TRP A 356 -14.323 5.519 14.132 1.00 69.22 C ANISOU 2491 CB TRP A 356 13800 6869 5632 -1281 -890 203 C ATOM 2492 CG TRP A 356 -15.243 6.287 13.237 1.00 69.78 C ANISOU 2492 CG TRP A 356 14129 6826 5559 -1192 -877 148 C ATOM 2493 CD1 TRP A 356 -15.583 7.602 13.346 1.00 73.42 C ANISOU 2493 CD1 TRP A 356 14910 7123 5865 -1215 -980 134 C ATOM 2494 CD2 TRP A 356 -16.084 5.740 12.214 1.00 68.76 C ANISOU 2494 CD2 TRP A 356 13983 6733 5410 -1030 -779 90 C ATOM 2495 NE1 TRP A 356 -16.532 7.926 12.403 1.00 72.52 N ANISOU 2495 NE1 TRP A 356 14964 6950 5640 -1061 -948 81 N ATOM 2496 CE2 TRP A 356 -16.861 6.800 11.697 1.00 73.02 C ANISOU 2496 CE2 TRP A 356 14814 7144 5785 -956 -833 52 C ATOM 2497 CE3 TRP A 356 -16.256 4.449 11.680 1.00 68.78 C ANISOU 2497 CE3 TRP A 356 13775 6852 5506 -941 -661 65 C ATOM 2498 CZ2 TRP A 356 -17.762 6.621 10.640 1.00 72.20 C ANISOU 2498 CZ2 TRP A 356 14765 7051 5615 -803 -787 -3 C ATOM 2499 CZ3 TRP A 356 -17.149 4.274 10.634 1.00 69.92 C ANISOU 2499 CZ3 TRP A 356 13994 6992 5579 -816 -613 3 C ATOM 2500 CH2 TRP A 356 -17.892 5.348 10.128 1.00 71.03 C ANISOU 2500 CH2 TRP A 356 14394 7031 5563 -749 -683 -29 C ATOM 2501 N LEU A 357 -13.613 3.600 16.757 1.00 70.57 N ANISOU 2501 N LEU A 357 13562 7233 6018 -1224 -997 244 N ATOM 2502 CA LEU A 357 -12.981 2.422 17.365 1.00 69.81 C ANISOU 2502 CA LEU A 357 13217 7255 6050 -1191 -983 292 C ATOM 2503 C LEU A 357 -14.083 1.508 17.938 1.00 70.30 C ANISOU 2503 C LEU A 357 13301 7312 6099 -1000 -949 221 C ATOM 2504 O LEU A 357 -13.973 0.287 17.819 1.00 71.36 O ANISOU 2504 O LEU A 357 13273 7515 6324 -913 -858 232 O ATOM 2505 CB LEU A 357 -11.955 2.814 18.445 1.00 71.21 C ANISOU 2505 CB LEU A 357 13345 7461 6249 -1346 -1148 367 C ATOM 2506 CG LEU A 357 -11.006 1.715 18.898 1.00 76.48 C ANISOU 2506 CG LEU A 357 13728 8275 7058 -1319 -1149 445 C ATOM 2507 CD1 LEU A 357 -9.876 1.518 17.905 1.00 77.37 C ANISOU 2507 CD1 LEU A 357 13588 8519 7288 -1400 -1045 528 C ATOM 2508 CD2 LEU A 357 -10.453 2.023 20.277 1.00 82.17 C ANISOU 2508 CD2 LEU A 357 14465 9003 7754 -1417 -1357 490 C ATOM 2509 N GLY A 358 -15.152 2.110 18.469 1.00 63.33 N ANISOU 2509 N GLY A 358 12627 6344 5091 -936 -1006 150 N ATOM 2510 CA GLY A 358 -16.327 1.395 18.962 1.00 61.86 C ANISOU 2510 CA GLY A 358 12460 6169 4874 -779 -957 84 C ATOM 2511 C GLY A 358 -17.167 0.848 17.815 1.00 63.80 C ANISOU 2511 C GLY A 358 12658 6447 5136 -687 -826 26 C ATOM 2512 O GLY A 358 -17.657 -0.287 17.864 1.00 60.81 O ANISOU 2512 O GLY A 358 12185 6116 4806 -616 -746 3 O ATOM 2513 N TYR A 359 -17.311 1.656 16.748 1.00 61.32 N ANISOU 2513 N TYR A 359 12433 6096 4771 -705 -813 5 N ATOM 2514 CA TYR A 359 -18.028 1.287 15.530 1.00 61.07 C ANISOU 2514 CA TYR A 359 12381 6089 4732 -633 -718 -49 C ATOM 2515 C TYR A 359 -17.344 0.099 14.874 1.00 66.50 C ANISOU 2515 C TYR A 359 12900 6832 5536 -657 -607 -17 C ATOM 2516 O TYR A 359 -18.032 -0.796 14.388 1.00 66.43 O ANISOU 2516 O TYR A 359 12849 6851 5539 -590 -532 -68 O ATOM 2517 CB TYR A 359 -18.089 2.462 14.540 1.00 62.76 C ANISOU 2517 CB TYR A 359 12758 6235 4852 -655 -741 -58 C ATOM 2518 CG TYR A 359 -18.988 3.628 14.907 1.00 64.10 C ANISOU 2518 CG TYR A 359 13144 6333 4880 -569 -835 -106 C ATOM 2519 CD1 TYR A 359 -18.852 4.858 14.273 1.00 67.14 C ANISOU 2519 CD1 TYR A 359 13741 6610 5158 -600 -884 -95 C ATOM 2520 CD2 TYR A 359 -20.029 3.477 15.823 1.00 64.24 C ANISOU 2520 CD2 TYR A 359 13167 6387 4855 -437 -859 -161 C ATOM 2521 CE1 TYR A 359 -19.706 5.922 14.560 1.00 68.97 C ANISOU 2521 CE1 TYR A 359 14207 6756 5243 -477 -967 -142 C ATOM 2522 CE2 TYR A 359 -20.882 4.537 16.129 1.00 66.05 C ANISOU 2522 CE2 TYR A 359 13593 6560 4944 -310 -927 -208 C ATOM 2523 CZ TYR A 359 -20.713 5.763 15.495 1.00 75.74 C ANISOU 2523 CZ TYR A 359 15050 7663 6063 -316 -987 -200 C ATOM 2524 OH TYR A 359 -21.528 6.835 15.775 1.00 75.86 O ANISOU 2524 OH TYR A 359 15299 7600 5924 -156 -1054 -245 O ATOM 2525 N LEU A 360 -15.989 0.067 14.913 1.00 63.60 N ANISOU 2525 N LEU A 360 12435 6484 5247 -751 -599 68 N ATOM 2526 CA LEU A 360 -15.160 -0.999 14.348 1.00 63.43 C ANISOU 2526 CA LEU A 360 12250 6520 5332 -739 -482 111 C ATOM 2527 C LEU A 360 -15.462 -2.368 14.973 1.00 67.35 C ANISOU 2527 C LEU A 360 12671 7032 5885 -643 -445 95 C ATOM 2528 O LEU A 360 -15.328 -3.383 14.286 1.00 68.03 O ANISOU 2528 O LEU A 360 12707 7126 6015 -583 -330 86 O ATOM 2529 CB LEU A 360 -13.674 -0.668 14.516 1.00 64.39 C ANISOU 2529 CB LEU A 360 12239 6697 5528 -848 -500 216 C ATOM 2530 CG LEU A 360 -12.733 -1.338 13.537 1.00 68.93 C ANISOU 2530 CG LEU A 360 12659 7346 6184 -830 -348 265 C ATOM 2531 CD1 LEU A 360 -12.984 -0.865 12.120 1.00 68.92 C ANISOU 2531 CD1 LEU A 360 12768 7310 6108 -854 -247 233 C ATOM 2532 CD2 LEU A 360 -11.305 -1.111 13.930 1.00 72.08 C ANISOU 2532 CD2 LEU A 360 12862 7850 6675 -928 -378 378 C ATOM 2533 N ASN A 361 -15.888 -2.399 16.251 1.00 62.88 N ANISOU 2533 N ASN A 361 12136 6455 5299 -628 -536 91 N ATOM 2534 CA ASN A 361 -16.239 -3.645 16.953 1.00 62.13 C ANISOU 2534 CA ASN A 361 12013 6356 5236 -556 -503 85 C ATOM 2535 C ASN A 361 -17.377 -4.387 16.225 1.00 63.15 C ANISOU 2535 C ASN A 361 12191 6467 5336 -514 -410 1 C ATOM 2536 O ASN A 361 -17.411 -5.617 16.270 1.00 63.03 O ANISOU 2536 O ASN A 361 12161 6427 5359 -477 -340 2 O ATOM 2537 CB ASN A 361 -16.616 -3.353 18.412 1.00 62.06 C ANISOU 2537 CB ASN A 361 12069 6335 5175 -559 -609 92 C ATOM 2538 CG ASN A 361 -17.046 -4.540 19.220 1.00 82.97 C ANISOU 2538 CG ASN A 361 14726 8968 7832 -505 -573 95 C ATOM 2539 OD1 ASN A 361 -18.233 -4.718 19.497 1.00 78.94 O ANISOU 2539 OD1 ASN A 361 14282 8454 7260 -492 -542 37 O ATOM 2540 ND2 ASN A 361 -16.093 -5.358 19.645 1.00 78.84 N ANISOU 2540 ND2 ASN A 361 14135 8442 7377 -471 -577 169 N ATOM 2541 N SER A 362 -18.267 -3.642 15.530 1.00 58.04 N ANISOU 2541 N SER A 362 11613 5826 4614 -524 -421 -66 N ATOM 2542 CA SER A 362 -19.382 -4.185 14.746 1.00 58.01 C ANISOU 2542 CA SER A 362 11638 5830 4572 -507 -367 -148 C ATOM 2543 C SER A 362 -18.876 -4.964 13.521 1.00 61.93 C ANISOU 2543 C SER A 362 12135 6297 5101 -503 -267 -155 C ATOM 2544 O SER A 362 -19.620 -5.777 12.976 1.00 60.33 O ANISOU 2544 O SER A 362 11968 6080 4875 -509 -224 -216 O ATOM 2545 CB SER A 362 -20.320 -3.071 14.285 1.00 62.86 C ANISOU 2545 CB SER A 362 12317 6474 5092 -488 -428 -206 C ATOM 2546 OG SER A 362 -21.031 -2.461 15.346 1.00 76.84 O ANISOU 2546 OG SER A 362 14109 8275 6810 -454 -496 -219 O ATOM 2547 N LEU A 363 -17.636 -4.667 13.068 1.00 60.07 N ANISOU 2547 N LEU A 363 11862 6055 4905 -503 -230 -93 N ATOM 2548 CA LEU A 363 -16.967 -5.319 11.944 1.00 60.77 C ANISOU 2548 CA LEU A 363 11952 6123 5015 -473 -108 -88 C ATOM 2549 C LEU A 363 -16.068 -6.444 12.454 1.00 67.42 C ANISOU 2549 C LEU A 363 12719 6952 5947 -406 -40 -29 C ATOM 2550 O LEU A 363 -15.944 -7.474 11.799 1.00 68.54 O ANISOU 2550 O LEU A 363 12910 7042 6089 -343 66 -53 O ATOM 2551 CB LEU A 363 -16.138 -4.301 11.129 1.00 61.07 C ANISOU 2551 CB LEU A 363 11980 6187 5036 -509 -80 -44 C ATOM 2552 CG LEU A 363 -15.277 -4.877 9.979 1.00 66.55 C ANISOU 2552 CG LEU A 363 12664 6880 5743 -464 78 -24 C ATOM 2553 CD1 LEU A 363 -16.119 -5.534 8.910 1.00 66.37 C ANISOU 2553 CD1 LEU A 363 12792 6794 5633 -429 137 -119 C ATOM 2554 CD2 LEU A 363 -14.355 -3.843 9.396 1.00 68.69 C ANISOU 2554 CD2 LEU A 363 12896 7197 6005 -530 118 44 C ATOM 2555 N ILE A 364 -15.436 -6.238 13.612 1.00 64.72 N ANISOU 2555 N ILE A 364 12279 6647 5665 -407 -112 46 N ATOM 2556 CA ILE A 364 -14.523 -7.197 14.227 1.00 65.71 C ANISOU 2556 CA ILE A 364 12322 6774 5872 -317 -80 117 C ATOM 2557 C ILE A 364 -15.308 -8.449 14.664 1.00 70.41 C ANISOU 2557 C ILE A 364 13033 7275 6445 -272 -55 74 C ATOM 2558 O ILE A 364 -14.882 -9.552 14.324 1.00 71.23 O ANISOU 2558 O ILE A 364 13174 7319 6572 -171 43 84 O ATOM 2559 CB ILE A 364 -13.717 -6.515 15.371 1.00 69.07 C ANISOU 2559 CB ILE A 364 12624 7273 6347 -352 -204 207 C ATOM 2560 CG1 ILE A 364 -12.694 -5.516 14.759 1.00 70.76 C ANISOU 2560 CG1 ILE A 364 12712 7579 6594 -421 -197 264 C ATOM 2561 CG2 ILE A 364 -12.994 -7.527 16.237 1.00 69.67 C ANISOU 2561 CG2 ILE A 364 12631 7351 6488 -241 -214 279 C ATOM 2562 CD1 ILE A 364 -12.337 -4.331 15.621 1.00 79.69 C ANISOU 2562 CD1 ILE A 364 13800 8758 7722 -547 -355 314 C ATOM 2563 N ASN A 365 -16.469 -8.281 15.331 1.00 66.44 N ANISOU 2563 N ASN A 365 12602 6755 5888 -346 -127 27 N ATOM 2564 CA ASN A 365 -17.319 -9.394 15.780 1.00 66.33 C ANISOU 2564 CA ASN A 365 12697 6660 5844 -356 -99 -8 C ATOM 2565 C ASN A 365 -17.635 -10.414 14.647 1.00 69.48 C ANISOU 2565 C ASN A 365 13213 6970 6217 -347 9 -72 C ATOM 2566 O ASN A 365 -17.269 -11.582 14.802 1.00 69.54 O ANISOU 2566 O ASN A 365 13308 6876 6237 -278 71 -49 O ATOM 2567 CB ASN A 365 -18.617 -8.880 16.401 1.00 67.87 C ANISOU 2567 CB ASN A 365 12916 6896 5978 -450 -164 -57 C ATOM 2568 CG ASN A 365 -18.510 -8.453 17.832 1.00 90.50 C ANISOU 2568 CG ASN A 365 15759 9790 8836 -448 -247 0 C ATOM 2569 OD1 ASN A 365 -17.553 -8.768 18.548 1.00 87.64 O ANISOU 2569 OD1 ASN A 365 15380 9406 8514 -388 -275 80 O ATOM 2570 ND2 ASN A 365 -19.526 -7.747 18.286 1.00 83.66 N ANISOU 2570 ND2 ASN A 365 14901 8980 7906 -497 -290 -41 N ATOM 2571 N PRO A 366 -18.222 -10.028 13.489 1.00 65.82 N ANISOU 2571 N PRO A 366 12781 6524 5702 -401 26 -150 N ATOM 2572 CA PRO A 366 -18.476 -11.034 12.440 1.00 66.50 C ANISOU 2572 CA PRO A 366 13015 6509 5742 -402 113 -215 C ATOM 2573 C PRO A 366 -17.216 -11.696 11.883 1.00 70.54 C ANISOU 2573 C PRO A 366 13567 6951 6283 -254 230 -174 C ATOM 2574 O PRO A 366 -17.308 -12.858 11.487 1.00 71.57 O ANISOU 2574 O PRO A 366 13871 6949 6375 -222 305 -211 O ATOM 2575 CB PRO A 366 -19.190 -10.244 11.341 1.00 68.03 C ANISOU 2575 CB PRO A 366 13220 6761 5867 -471 81 -292 C ATOM 2576 CG PRO A 366 -18.855 -8.823 11.603 1.00 71.39 C ANISOU 2576 CG PRO A 366 13513 7295 6315 -459 16 -248 C ATOM 2577 CD PRO A 366 -18.732 -8.706 13.083 1.00 66.42 C ANISOU 2577 CD PRO A 366 12801 6695 5739 -457 -43 -185 C ATOM 2578 N ILE A 367 -16.055 -10.999 11.842 1.00 66.00 N ANISOU 2578 N ILE A 367 12842 6466 5770 -166 252 -99 N ATOM 2579 CA ILE A 367 -14.868 -11.665 11.301 1.00 66.93 C ANISOU 2579 CA ILE A 367 12961 6551 5916 1 385 -55 C ATOM 2580 C ILE A 367 -14.342 -12.665 12.347 1.00 70.11 C ANISOU 2580 C ILE A 367 13373 6892 6373 123 387 13 C ATOM 2581 O ILE A 367 -13.917 -13.738 11.927 1.00 69.99 O ANISOU 2581 O ILE A 367 13487 6767 6338 268 499 9 O ATOM 2582 CB ILE A 367 -13.753 -10.775 10.653 1.00 70.97 C ANISOU 2582 CB ILE A 367 13304 7193 6469 51 450 5 C ATOM 2583 CG1 ILE A 367 -12.474 -10.613 11.504 1.00 73.36 C ANISOU 2583 CG1 ILE A 367 13378 7610 6886 144 434 129 C ATOM 2584 CG2 ILE A 367 -14.277 -9.461 10.035 1.00 69.36 C ANISOU 2584 CG2 ILE A 367 13085 7057 6213 -95 396 -33 C ATOM 2585 CD1 ILE A 367 -11.195 -10.329 10.677 1.00 87.67 C ANISOU 2585 CD1 ILE A 367 15031 9541 8739 238 572 195 C ATOM 2586 N ILE A 368 -14.458 -12.370 13.687 1.00 66.66 N ANISOU 2586 N ILE A 368 12850 6501 5979 75 262 68 N ATOM 2587 CA ILE A 368 -14.051 -13.311 14.754 1.00 67.76 C ANISOU 2587 CA ILE A 368 13032 6567 6144 188 242 137 C ATOM 2588 C ILE A 368 -14.858 -14.604 14.604 1.00 72.93 C ANISOU 2588 C ILE A 368 13967 7023 6721 175 304 73 C ATOM 2589 O ILE A 368 -14.275 -15.688 14.637 1.00 74.50 O ANISOU 2589 O ILE A 368 14293 7100 6914 343 375 106 O ATOM 2590 CB ILE A 368 -14.182 -12.771 16.212 1.00 70.74 C ANISOU 2590 CB ILE A 368 13322 7011 6545 119 93 197 C ATOM 2591 CG1 ILE A 368 -13.578 -11.350 16.443 1.00 71.87 C ANISOU 2591 CG1 ILE A 368 13235 7329 6741 65 -4 246 C ATOM 2592 CG2 ILE A 368 -13.703 -13.792 17.263 1.00 71.91 C ANISOU 2592 CG2 ILE A 368 13548 7074 6702 254 68 277 C ATOM 2593 CD1 ILE A 368 -12.036 -11.189 16.516 1.00 84.20 C ANISOU 2593 CD1 ILE A 368 14584 9012 8396 195 -12 352 C ATOM 2594 N TYR A 369 -16.194 -14.488 14.419 1.00 68.25 N ANISOU 2594 N TYR A 369 13473 6397 6062 -25 273 -16 N ATOM 2595 CA TYR A 369 -17.068 -15.651 14.273 1.00 68.81 C ANISOU 2595 CA TYR A 369 13803 6288 6052 -109 314 -79 C ATOM 2596 C TYR A 369 -16.795 -16.416 12.996 1.00 74.63 C ANISOU 2596 C TYR A 369 14726 6895 6735 -25 429 -139 C ATOM 2597 O TYR A 369 -16.956 -17.632 12.976 1.00 75.56 O ANISOU 2597 O TYR A 369 15105 6813 6790 -6 482 -159 O ATOM 2598 CB TYR A 369 -18.544 -15.250 14.319 1.00 68.93 C ANISOU 2598 CB TYR A 369 13815 6356 6020 -354 247 -155 C ATOM 2599 CG TYR A 369 -19.104 -15.195 15.722 1.00 70.80 C ANISOU 2599 CG TYR A 369 14016 6624 6259 -445 181 -107 C ATOM 2600 CD1 TYR A 369 -19.383 -13.977 16.335 1.00 71.75 C ANISOU 2600 CD1 TYR A 369 13940 6916 6405 -490 98 -90 C ATOM 2601 CD2 TYR A 369 -19.344 -16.360 16.445 1.00 72.55 C ANISOU 2601 CD2 TYR A 369 14436 6690 6440 -480 212 -77 C ATOM 2602 CE1 TYR A 369 -19.897 -13.919 17.629 1.00 72.08 C ANISOU 2602 CE1 TYR A 369 13972 6987 6428 -557 57 -48 C ATOM 2603 CE2 TYR A 369 -19.845 -16.313 17.744 1.00 73.13 C ANISOU 2603 CE2 TYR A 369 14496 6793 6498 -565 171 -26 C ATOM 2604 CZ TYR A 369 -20.127 -15.091 18.329 1.00 80.01 C ANISOU 2604 CZ TYR A 369 15158 7851 7392 -598 98 -14 C ATOM 2605 OH TYR A 369 -20.620 -15.040 19.610 1.00 83.16 O ANISOU 2605 OH TYR A 369 15565 8278 7755 -666 75 33 O ATOM 2606 N THR A 370 -16.387 -15.729 11.932 1.00 71.70 N ANISOU 2606 N THR A 370 14259 6615 6368 24 474 -168 N ATOM 2607 CA THR A 370 -16.144 -16.435 10.679 1.00 73.88 C ANISOU 2607 CA THR A 370 14742 6763 6566 113 596 -232 C ATOM 2608 C THR A 370 -14.768 -17.108 10.681 1.00 79.08 C ANISOU 2608 C THR A 370 15423 7366 7258 406 720 -157 C ATOM 2609 O THR A 370 -14.593 -18.094 9.979 1.00 80.85 O ANISOU 2609 O THR A 370 15906 7414 7399 521 832 -203 O ATOM 2610 CB THR A 370 -16.350 -15.534 9.454 1.00 84.12 C ANISOU 2610 CB THR A 370 15982 8159 7820 47 610 -297 C ATOM 2611 OG1 THR A 370 -15.624 -14.328 9.647 1.00 89.64 O ANISOU 2611 OG1 THR A 370 16398 9054 8608 94 592 -221 O ATOM 2612 CG2 THR A 370 -17.807 -15.202 9.223 1.00 78.59 C ANISOU 2612 CG2 THR A 370 15329 7477 7055 -202 494 -389 C ATOM 2613 N MET A 371 -13.815 -16.626 11.477 1.00 74.70 N ANISOU 2613 N MET A 371 14612 6957 6814 533 694 -45 N ATOM 2614 CA MET A 371 -12.497 -17.256 11.478 1.00 76.66 C ANISOU 2614 CA MET A 371 14832 7194 7101 835 804 35 C ATOM 2615 C MET A 371 -12.341 -18.297 12.583 1.00 81.50 C ANISOU 2615 C MET A 371 15585 7666 7716 959 765 96 C ATOM 2616 O MET A 371 -11.551 -19.227 12.403 1.00 84.24 O ANISOU 2616 O MET A 371 16056 7909 8044 1232 873 129 O ATOM 2617 CB MET A 371 -11.382 -16.215 11.600 1.00 79.11 C ANISOU 2617 CB MET A 371 14763 7765 7528 918 801 133 C ATOM 2618 CG MET A 371 -11.366 -15.205 10.478 1.00 82.51 C ANISOU 2618 CG MET A 371 15082 8321 7945 817 862 92 C ATOM 2619 SD MET A 371 -9.889 -14.171 10.471 1.00 88.20 S ANISOU 2619 SD MET A 371 15387 9332 8793 906 901 219 S ATOM 2620 CE MET A 371 -9.975 -13.455 12.110 1.00 83.74 C ANISOU 2620 CE MET A 371 14620 8874 8324 764 660 299 C ATOM 2621 N SER A 372 -13.072 -18.140 13.721 1.00 75.90 N ANISOU 2621 N SER A 372 14872 6950 7018 781 622 117 N ATOM 2622 CA SER A 372 -12.987 -19.027 14.896 1.00 76.19 C ANISOU 2622 CA SER A 372 15055 6852 7040 869 569 188 C ATOM 2623 C SER A 372 -14.083 -20.097 14.945 1.00 79.13 C ANISOU 2623 C SER A 372 15817 6957 7293 723 588 118 C ATOM 2624 O SER A 372 -13.792 -21.203 15.377 1.00 81.94 O ANISOU 2624 O SER A 372 16423 7114 7598 877 619 161 O ATOM 2625 CB SER A 372 -13.017 -18.225 16.194 1.00 78.19 C ANISOU 2625 CB SER A 372 15089 7261 7359 773 413 267 C ATOM 2626 OG SER A 372 -12.026 -17.212 16.229 1.00 86.31 O ANISOU 2626 OG SER A 372 15770 8531 8492 857 369 334 O ATOM 2627 N ASN A 373 -15.331 -19.774 14.570 1.00 72.71 N ANISOU 2627 N ASN A 373 15053 6141 6433 424 558 20 N ATOM 2628 CA ASN A 373 -16.431 -20.742 14.562 1.00 73.03 C ANISOU 2628 CA ASN A 373 15429 5955 6362 223 568 -47 C ATOM 2629 C ASN A 373 -16.406 -21.446 13.200 1.00 79.23 C ANISOU 2629 C ASN A 373 16479 6568 7056 274 675 -144 C ATOM 2630 O ASN A 373 -16.552 -20.803 12.159 1.00 77.54 O ANISOU 2630 O ASN A 373 16161 6461 6839 220 694 -218 O ATOM 2631 CB ASN A 373 -17.764 -20.047 14.863 1.00 71.84 C ANISOU 2631 CB ASN A 373 15158 5928 6208 -112 477 -96 C ATOM 2632 CG ASN A 373 -18.975 -20.932 15.009 1.00 97.80 C ANISOU 2632 CG ASN A 373 18717 9044 9398 -379 474 -150 C ATOM 2633 OD1 ASN A 373 -19.202 -21.864 14.234 1.00 94.90 O ANISOU 2633 OD1 ASN A 373 18652 8468 8939 -425 529 -218 O ATOM 2634 ND2 ASN A 373 -19.845 -20.579 15.946 1.00 88.36 N ANISOU 2634 ND2 ASN A 373 17411 7951 8212 -588 410 -126 N ATOM 2635 N GLU A 374 -16.172 -22.765 13.217 1.00 80.10 N ANISOU 2635 N GLU A 374 16963 6396 7076 397 746 -140 N ATOM 2636 CA GLU A 374 -16.001 -23.581 12.014 1.00 82.98 C ANISOU 2636 CA GLU A 374 17656 6546 7327 500 860 -227 C ATOM 2637 C GLU A 374 -17.278 -23.767 11.190 1.00 88.00 C ANISOU 2637 C GLU A 374 18498 7083 7854 157 826 -363 C ATOM 2638 O GLU A 374 -17.177 -24.085 10.004 1.00 88.88 O ANISOU 2638 O GLU A 374 18818 7083 7870 212 900 -453 O ATOM 2639 CB GLU A 374 -15.353 -24.927 12.348 1.00 87.45 C ANISOU 2639 CB GLU A 374 18600 6815 7814 761 939 -179 C ATOM 2640 CG GLU A 374 -13.828 -24.843 12.346 1.00105.60 C ANISOU 2640 CG GLU A 374 20725 9214 10186 1213 1027 -87 C ATOM 2641 CD GLU A 374 -13.215 -23.784 13.255 1.00139.98 C ANISOU 2641 CD GLU A 374 24592 13889 14707 1283 939 30 C ATOM 2642 OE1 GLU A 374 -12.832 -22.702 12.745 1.00127.19 O ANISOU 2642 OE1 GLU A 374 22614 12536 13178 1293 950 28 O ATOM 2643 OE2 GLU A 374 -13.185 -24.011 14.488 1.00139.92 O ANISOU 2643 OE2 GLU A 374 24586 13854 14722 1296 850 123 O ATOM 2644 N ASP A 375 -18.453 -23.488 11.770 1.00 83.97 N ANISOU 2644 N ASP A 375 17901 6648 7356 -189 712 -377 N ATOM 2645 CA ASP A 375 -19.713 -23.534 11.038 1.00 84.00 C ANISOU 2645 CA ASP A 375 18010 6630 7276 -535 650 -496 C ATOM 2646 C ASP A 375 -19.752 -22.352 10.059 1.00 85.50 C ANISOU 2646 C ASP A 375 17917 7065 7504 -535 623 -556 C ATOM 2647 O ASP A 375 -20.061 -22.555 8.888 1.00 86.18 O ANISOU 2647 O ASP A 375 18187 7071 7486 -607 630 -662 O ATOM 2648 CB ASP A 375 -20.914 -23.520 11.999 1.00 85.90 C ANISOU 2648 CB ASP A 375 18173 6934 7532 -880 554 -477 C ATOM 2649 CG ASP A 375 -21.038 -24.760 12.880 1.00105.36 C ANISOU 2649 CG ASP A 375 20985 9123 9925 -947 584 -422 C ATOM 2650 OD1 ASP A 375 -21.136 -25.887 12.319 1.00109.82 O ANISOU 2650 OD1 ASP A 375 21987 9382 10357 -999 625 -482 O ATOM 2651 OD2 ASP A 375 -21.080 -24.604 14.131 1.00110.61 O ANISOU 2651 OD2 ASP A 375 21518 9862 10649 -963 564 -322 O ATOM 2652 N PHE A 376 -19.361 -21.138 10.527 1.00 79.12 N ANISOU 2652 N PHE A 376 16704 6532 6827 -440 592 -485 N ATOM 2653 CA PHE A 376 -19.301 -19.910 9.723 1.00 76.28 C ANISOU 2653 CA PHE A 376 16082 6399 6504 -424 568 -520 C ATOM 2654 C PHE A 376 -18.084 -19.918 8.811 1.00 81.00 C ANISOU 2654 C PHE A 376 16732 6961 7083 -133 700 -516 C ATOM 2655 O PHE A 376 -18.168 -19.368 7.712 1.00 82.29 O ANISOU 2655 O PHE A 376 16876 7195 7196 -151 712 -582 O ATOM 2656 CB PHE A 376 -19.292 -18.649 10.608 1.00 75.00 C ANISOU 2656 CB PHE A 376 15525 6503 6468 -436 490 -442 C ATOM 2657 CG PHE A 376 -20.574 -18.447 11.375 1.00 74.82 C ANISOU 2657 CG PHE A 376 15410 6565 6452 -708 380 -454 C ATOM 2658 CD1 PHE A 376 -21.691 -17.893 10.759 1.00 76.31 C ANISOU 2658 CD1 PHE A 376 15512 6878 6602 -919 293 -539 C ATOM 2659 CD2 PHE A 376 -20.680 -18.849 12.699 1.00 76.70 C ANISOU 2659 CD2 PHE A 376 15654 6767 6723 -743 369 -378 C ATOM 2660 CE1 PHE A 376 -22.893 -17.744 11.456 1.00 76.69 C ANISOU 2660 CE1 PHE A 376 15444 7036 6658 -1153 210 -546 C ATOM 2661 CE2 PHE A 376 -21.880 -18.695 13.400 1.00 79.04 C ANISOU 2661 CE2 PHE A 376 15860 7156 7014 -992 299 -385 C ATOM 2662 CZ PHE A 376 -22.977 -18.142 12.774 1.00 76.63 C ANISOU 2662 CZ PHE A 376 15434 6997 6684 -1192 227 -469 C ATOM 2663 N LYS A 377 -16.957 -20.531 9.253 1.00 76.57 N ANISOU 2663 N LYS A 377 16234 6305 6555 146 803 -435 N ATOM 2664 CA LYS A 377 -15.736 -20.635 8.449 1.00 76.79 C ANISOU 2664 CA LYS A 377 16289 6319 6568 457 959 -419 C ATOM 2665 C LYS A 377 -16.004 -21.503 7.225 1.00 83.17 C ANISOU 2665 C LYS A 377 17508 6891 7202 459 1043 -539 C ATOM 2666 O LYS A 377 -15.648 -21.096 6.121 1.00 83.44 O ANISOU 2666 O LYS A 377 17536 6984 7184 545 1130 -583 O ATOM 2667 CB LYS A 377 -14.559 -21.179 9.267 1.00 79.65 C ANISOU 2667 CB LYS A 377 16616 6646 7000 769 1033 -302 C ATOM 2668 CG LYS A 377 -13.214 -20.957 8.595 1.00 86.67 C ANISOU 2668 CG LYS A 377 17366 7643 7921 1096 1192 -256 C ATOM 2669 CD LYS A 377 -12.064 -21.504 9.423 1.00 96.34 C ANISOU 2669 CD LYS A 377 18517 8868 9221 1425 1244 -134 C ATOM 2670 CE LYS A 377 -10.808 -21.652 8.596 1.00105.00 C ANISOU 2670 CE LYS A 377 19557 10025 10312 1780 1444 -105 C ATOM 2671 NZ LYS A 377 -9.625 -21.973 9.436 1.00111.19 N ANISOU 2671 NZ LYS A 377 20154 10896 11197 2113 1470 32 N ATOM 2672 N GLN A 378 -16.673 -22.668 7.411 1.00 81.37 N ANISOU 2672 N GLN A 378 17660 6389 6869 336 1013 -593 N ATOM 2673 CA GLN A 378 -17.056 -23.566 6.315 1.00 83.03 C ANISOU 2673 CA GLN A 378 18326 6334 6889 285 1062 -719 C ATOM 2674 C GLN A 378 -18.045 -22.837 5.385 1.00 85.25 C ANISOU 2674 C GLN A 378 18548 6735 7109 -3 956 -825 C ATOM 2675 O GLN A 378 -17.879 -22.868 4.160 1.00 85.74 O ANISOU 2675 O GLN A 378 18797 6736 7045 66 1026 -908 O ATOM 2676 CB GLN A 378 -17.656 -24.873 6.856 1.00 85.94 C ANISOU 2676 CB GLN A 378 19104 6388 7162 142 1022 -743 C ATOM 2677 N ALA A 379 -19.018 -22.113 5.990 1.00 79.10 N ANISOU 2677 N ALA A 379 17490 6149 6417 -291 792 -813 N ATOM 2678 CA ALA A 379 -20.037 -21.314 5.307 1.00 77.38 C ANISOU 2678 CA ALA A 379 17147 6092 6163 -550 658 -894 C ATOM 2679 C ALA A 379 -19.404 -20.273 4.378 1.00 79.29 C ANISOU 2679 C ALA A 379 17218 6504 6406 -380 720 -896 C ATOM 2680 O ALA A 379 -19.862 -20.114 3.240 1.00 78.60 O ANISOU 2680 O ALA A 379 17273 6403 6189 -473 681 -993 O ATOM 2681 CB ALA A 379 -20.919 -20.623 6.328 1.00 75.85 C ANISOU 2681 CB ALA A 379 16618 6112 6090 -777 513 -848 C ATOM 2682 N PHE A 380 -18.340 -19.583 4.865 1.00 73.60 N ANISOU 2682 N PHE A 380 16206 5941 5819 -145 811 -784 N ATOM 2683 CA PHE A 380 -17.605 -18.567 4.112 1.00 72.20 C ANISOU 2683 CA PHE A 380 15846 5932 5654 6 892 -759 C ATOM 2684 C PHE A 380 -16.866 -19.160 2.919 1.00 78.71 C ANISOU 2684 C PHE A 380 16967 6604 6336 214 1074 -810 C ATOM 2685 O PHE A 380 -16.882 -18.565 1.844 1.00 78.15 O ANISOU 2685 O PHE A 380 16927 6595 6173 206 1102 -857 O ATOM 2686 CB PHE A 380 -16.618 -17.833 5.013 1.00 72.17 C ANISOU 2686 CB PHE A 380 15477 6119 5827 170 939 -622 C ATOM 2687 CG PHE A 380 -15.961 -16.681 4.298 1.00 72.61 C ANISOU 2687 CG PHE A 380 15328 6361 5898 253 1009 -587 C ATOM 2688 CD1 PHE A 380 -16.644 -15.492 4.087 1.00 73.22 C ANISOU 2688 CD1 PHE A 380 15244 6597 5980 73 882 -604 C ATOM 2689 CD2 PHE A 380 -14.662 -16.792 3.818 1.00 75.98 C ANISOU 2689 CD2 PHE A 380 15735 6806 6327 517 1211 -533 C ATOM 2690 CE1 PHE A 380 -16.032 -14.426 3.433 1.00 74.06 C ANISOU 2690 CE1 PHE A 380 15205 6848 6085 131 949 -564 C ATOM 2691 CE2 PHE A 380 -14.051 -15.722 3.167 1.00 78.36 C ANISOU 2691 CE2 PHE A 380 15849 7285 6639 558 1290 -490 C ATOM 2692 CZ PHE A 380 -14.739 -14.548 2.977 1.00 74.70 C ANISOU 2692 CZ PHE A 380 15264 6948 6171 353 1156 -505 C ATOM 2693 N HIS A 381 -16.206 -20.321 3.121 1.00 78.06 N ANISOU 2693 N HIS A 381 17120 6315 6222 422 1204 -797 N ATOM 2694 CA HIS A 381 -15.476 -21.068 2.096 1.00 80.56 C ANISOU 2694 CA HIS A 381 17769 6452 6387 671 1402 -847 C ATOM 2695 C HIS A 381 -16.436 -21.475 0.976 1.00 86.26 C ANISOU 2695 C HIS A 381 18891 6992 6892 470 1334 -1002 C ATOM 2696 O HIS A 381 -16.027 -21.515 -0.181 1.00 87.66 O ANISOU 2696 O HIS A 381 19275 7111 6921 608 1469 -1058 O ATOM 2697 CB HIS A 381 -14.784 -22.307 2.708 1.00 83.20 C ANISOU 2697 CB HIS A 381 18316 6574 6723 925 1516 -806 C ATOM 2698 CG HIS A 381 -13.593 -22.012 3.585 1.00 86.05 C ANISOU 2698 CG HIS A 381 18314 7115 7265 1203 1607 -654 C ATOM 2699 ND1 HIS A 381 -12.823 -23.032 4.110 1.00 89.68 N ANISOU 2699 ND1 HIS A 381 18924 7419 7729 1501 1713 -599 N ATOM 2700 CD2 HIS A 381 -13.078 -20.828 3.998 1.00 85.95 C ANISOU 2700 CD2 HIS A 381 17819 7416 7420 1215 1590 -550 C ATOM 2701 CE1 HIS A 381 -11.869 -22.445 4.813 1.00 88.37 C ANISOU 2701 CE1 HIS A 381 18335 7502 7740 1685 1747 -463 C ATOM 2702 NE2 HIS A 381 -11.982 -21.121 4.777 1.00 86.52 N ANISOU 2702 NE2 HIS A 381 17717 7549 7608 1504 1675 -431 N ATOM 2703 N LYS A 382 -17.726 -21.717 1.319 1.00 82.12 N ANISOU 2703 N LYS A 382 18454 6403 6347 130 1121 -1065 N ATOM 2704 CA LYS A 382 -18.780 -22.060 0.362 1.00 82.70 C ANISOU 2704 CA LYS A 382 18858 6337 6225 -126 997 -1209 C ATOM 2705 C LYS A 382 -19.171 -20.842 -0.499 1.00 85.21 C ANISOU 2705 C LYS A 382 18988 6880 6509 -228 913 -1241 C ATOM 2706 O LYS A 382 -19.286 -21.027 -1.712 1.00 87.04 O ANISOU 2706 O LYS A 382 19532 7000 6540 -230 933 -1341 O ATOM 2707 CB LYS A 382 -20.016 -22.651 1.068 1.00 84.97 C ANISOU 2707 CB LYS A 382 19226 6536 6522 -479 795 -1249 C ATOM 2708 CG LYS A 382 -21.051 -23.246 0.119 1.00103.62 C ANISOU 2708 CG LYS A 382 21975 8724 8673 -763 657 -1399 C ATOM 2709 CD LYS A 382 -22.236 -23.887 0.835 1.00119.16 C ANISOU 2709 CD LYS A 382 24002 10619 10653 -1142 474 -1426 C ATOM 2710 CE LYS A 382 -23.250 -24.420 -0.157 1.00140.93 C ANISOU 2710 CE LYS A 382 27114 13233 13200 -1456 311 -1575 C ATOM 2711 NZ LYS A 382 -24.422 -25.046 0.514 1.00155.20 N ANISOU 2711 NZ LYS A 382 28954 14995 15021 -1869 137 -1595 N ATOM 2712 N LEU A 383 -19.372 -19.612 0.083 1.00 79.39 N ANISOU 2712 N LEU A 383 17790 6435 5938 -301 818 -1160 N ATOM 2713 CA LEU A 383 -19.759 -18.506 -0.795 1.00 78.84 C ANISOU 2713 CA LEU A 383 17613 6539 5805 -378 734 -1191 C ATOM 2714 C LEU A 383 -18.599 -18.062 -1.686 1.00 82.11 C ANISOU 2714 C LEU A 383 18068 6978 6152 -110 951 -1160 C ATOM 2715 O LEU A 383 -18.857 -17.890 -2.876 1.00 83.73 O ANISOU 2715 O LEU A 383 18497 7143 6172 -142 937 -1240 O ATOM 2716 CB LEU A 383 -20.520 -17.291 -0.207 1.00 76.85 C ANISOU 2716 CB LEU A 383 16958 6557 5684 -547 547 -1144 C ATOM 2717 CG LEU A 383 -20.085 -16.465 1.002 1.00 81.39 C ANISOU 2717 CG LEU A 383 17119 7328 6479 -477 561 -1015 C ATOM 2718 CD1 LEU A 383 -18.735 -15.767 0.804 1.00 82.14 C ANISOU 2718 CD1 LEU A 383 17070 7511 6627 -228 749 -921 C ATOM 2719 CD2 LEU A 383 -21.094 -15.342 1.223 1.00 82.62 C ANISOU 2719 CD2 LEU A 383 17011 7701 6681 -652 359 -1013 C ATOM 2720 N ILE A 384 -17.338 -18.008 -1.191 1.00 75.80 N ANISOU 2720 N ILE A 384 17092 6231 5476 150 1154 -1049 N ATOM 2721 CA ILE A 384 -16.213 -17.654 -2.080 1.00 76.04 C ANISOU 2721 CA ILE A 384 17149 6306 5438 396 1391 -1014 C ATOM 2722 C ILE A 384 -15.814 -18.847 -3.004 1.00 81.69 C ANISOU 2722 C ILE A 384 18338 6756 5943 577 1570 -1104 C ATOM 2723 O ILE A 384 -15.063 -18.634 -3.956 1.00 82.91 O ANISOU 2723 O ILE A 384 18590 6928 5984 761 1772 -1100 O ATOM 2724 CB ILE A 384 -14.966 -17.055 -1.368 1.00 78.13 C ANISOU 2724 CB ILE A 384 17017 6769 5901 597 1546 -859 C ATOM 2725 CG1 ILE A 384 -14.468 -17.926 -0.193 1.00 78.70 C ANISOU 2725 CG1 ILE A 384 17012 6776 6113 737 1585 -796 C ATOM 2726 CG2 ILE A 384 -15.219 -15.590 -0.966 1.00 76.50 C ANISOU 2726 CG2 ILE A 384 16434 6812 5820 435 1410 -785 C ATOM 2727 CD1 ILE A 384 -13.049 -17.669 0.242 1.00 83.21 C ANISOU 2727 CD1 ILE A 384 17277 7511 6829 1001 1774 -659 C ATOM 2728 N ARG A 385 -16.369 -20.065 -2.754 1.00 77.85 N ANISOU 2728 N ARG A 385 18175 6019 5387 507 1495 -1187 N ATOM 2729 CA ARG A 385 -16.127 -21.332 -3.461 1.00 79.99 C ANISOU 2729 CA ARG A 385 18967 5979 5446 658 1631 -1284 C ATOM 2730 C ARG A 385 -14.641 -21.706 -3.360 1.00 85.31 C ANISOU 2730 C ARG A 385 19604 6645 6163 1081 1938 -1197 C ATOM 2731 O ARG A 385 -13.932 -21.795 -4.363 1.00 86.07 O ANISOU 2731 O ARG A 385 19894 6701 6107 1314 2162 -1222 O ATOM 2732 CB ARG A 385 -16.641 -21.333 -4.917 1.00 80.45 C ANISOU 2732 CB ARG A 385 19415 5923 5229 562 1603 -1419 C ATOM 2733 N PHE A 386 -14.191 -21.927 -2.111 1.00 82.66 N ANISOU 2733 N PHE A 386 19009 6364 6033 1185 1945 -1090 N ATOM 2734 CA PHE A 386 -12.833 -22.327 -1.731 1.00 84.92 C ANISOU 2734 CA PHE A 386 19183 6679 6404 1588 2187 -987 C ATOM 2735 C PHE A 386 -12.880 -23.690 -1.016 1.00 91.53 C ANISOU 2735 C PHE A 386 20333 7225 7218 1694 2173 -1005 C ATOM 2736 O PHE A 386 -13.766 -23.905 -0.183 1.00 90.40 O ANISOU 2736 O PHE A 386 20197 7010 7139 1424 1956 -1015 O ATOM 2737 CB PHE A 386 -12.199 -21.237 -0.836 1.00 84.80 C ANISOU 2737 CB PHE A 386 18551 7016 6654 1614 2176 -827 C ATOM 2738 CG PHE A 386 -10.825 -21.540 -0.279 1.00 88.57 C ANISOU 2738 CG PHE A 386 18804 7591 7256 1997 2375 -700 C ATOM 2739 CD1 PHE A 386 -9.691 -21.416 -1.075 1.00 94.13 C ANISOU 2739 CD1 PHE A 386 19441 8410 7913 2307 2658 -658 C ATOM 2740 CD2 PHE A 386 -10.662 -21.905 1.054 1.00 90.91 C ANISOU 2740 CD2 PHE A 386 18932 7894 7718 2049 2277 -613 C ATOM 2741 CE1 PHE A 386 -8.421 -21.686 -0.557 1.00 97.13 C ANISOU 2741 CE1 PHE A 386 19562 8926 8420 2672 2833 -533 C ATOM 2742 CE2 PHE A 386 -9.391 -22.171 1.574 1.00 95.55 C ANISOU 2742 CE2 PHE A 386 19290 8596 8420 2417 2433 -490 C ATOM 2743 CZ PHE A 386 -8.280 -22.057 0.765 1.00 96.18 C ANISOU 2743 CZ PHE A 386 19272 8810 8463 2728 2706 -451 C ATOM 2744 N LYS A 387 -11.943 -24.611 -1.344 1.00 91.91 N ANISOU 2744 N LYS A 387 20656 7103 7164 2092 2413 -1006 N ATOM 2745 CA LYS A 387 -11.900 -25.945 -0.721 1.00126.12 C ANISOU 2745 CA LYS A 387 25353 11120 11446 2243 2418 -1018 C ATOM 2746 C LYS A 387 -10.558 -26.254 -0.039 1.00152.24 C ANISOU 2746 C LYS A 387 28437 14521 14885 2707 2603 -878 C ATOM 2747 O LYS A 387 -9.757 -25.365 0.240 1.00114.90 O ANISOU 2747 O LYS A 387 23173 10143 10340 2834 2674 -755 O ATOM 2748 CB LYS A 387 -12.197 -27.040 -1.750 1.00132.06 C ANISOU 2748 CB LYS A 387 26809 11475 11894 2302 2500 -1176 C ATOM 2749 CG LYS A 387 -13.644 -27.093 -2.217 1.00149.64 C ANISOU 2749 CG LYS A 387 29344 13538 13977 1817 2258 -1319 C ATOM 2750 CD LYS A 387 -13.859 -28.273 -3.157 1.00166.68 C ANISOU 2750 CD LYS A 387 32245 15267 15817 1878 2327 -1475 C ATOM 2751 CE LYS A 387 -15.208 -28.248 -3.832 1.00180.56 C ANISOU 2751 CE LYS A 387 34291 16904 17410 1400 2088 -1623 C ATOM 2752 NZ LYS A 387 -15.414 -29.447 -4.690 1.00195.69 N ANISOU 2752 NZ LYS A 387 36978 18374 19003 1433 2133 -1779 N TER 2753 LYS A 387 HETATM 2754 C10 2GM A2001 -22.342 8.358 21.858 1.00 77.76 C HETATM 2755 C11 2GM A2001 -22.843 6.945 22.106 1.00 78.21 C HETATM 2756 C12 2GM A2001 -23.463 6.639 23.480 1.00 77.95 C HETATM 2757 C17 2GM A2001 -23.687 5.328 23.770 1.00 78.72 C HETATM 2758 C13 2GM A2001 -23.910 7.593 24.455 1.00 77.62 C HETATM 2759 C14 2GM A2001 -24.529 7.133 25.679 1.00 78.04 C HETATM 2760 C15 2GM A2001 -24.686 5.751 25.899 1.00 78.03 C HETATM 2761 C16 2GM A2001 -24.266 4.872 24.944 1.00 78.15 C HETATM 2762 N1 2GM A2001 -24.286 3.473 24.837 1.00 76.89 N HETATM 2763 C2 2GM A2001 -23.688 3.102 23.659 1.00 77.14 C HETATM 2764 C3 2GM A2001 -23.315 4.240 22.974 1.00 78.59 C HETATM 2765 C4 2GM A2001 -22.661 4.461 21.654 1.00 78.36 C HETATM 2766 C5 2GM A2001 -21.918 5.804 21.599 1.00 77.81 C HETATM 2767 N6 2GM A2001 -21.284 6.029 20.204 1.00 76.49 N HETATM 2768 C7 2GM A2001 -20.046 5.311 19.946 1.00 75.49 C HETATM 2769 C8 2GM A2001 -20.956 7.475 19.903 1.00 76.75 C HETATM 2770 C9 2GM A2001 -21.928 8.543 20.409 1.00 77.34 C HETATM 2771 C18 2GM A2001 -21.249 9.898 20.291 1.00 78.82 C HETATM 2772 O19 2GM A2001 -20.169 10.100 20.848 1.00 80.38 O HETATM 2773 N20 2GM A2001 -21.962 10.930 19.500 1.00 78.36 N HETATM 2774 C21 2GM A2001 -21.399 12.291 19.298 1.00 76.45 C HETATM 2775 C22 2GM A2001 -22.241 12.983 18.246 1.00 75.80 C HETATM 2776 O43 2GM A2001 -19.959 12.208 18.788 1.00 77.01 O HETATM 2777 C23 2GM A2001 -21.285 13.070 20.570 1.00 74.50 C HETATM 2778 O24 2GM A2001 -22.260 13.363 21.273 1.00 69.17 O HETATM 2779 N25 2GM A2001 -19.998 13.324 20.767 1.00 77.18 N HETATM 2780 C41 2GM A2001 -19.083 12.869 19.809 1.00 78.34 C HETATM 2781 O42 2GM A2001 -18.264 11.893 20.339 1.00 77.12 O HETATM 2782 C40 2GM A2001 -18.168 13.981 19.233 1.00 82.01 C HETATM 2783 C39 2GM A2001 -16.773 13.650 18.584 1.00 83.40 C HETATM 2784 C38 2GM A2001 -16.160 15.141 18.494 1.00 83.65 C HETATM 2785 C37 2GM A2001 -16.804 15.871 19.645 1.00 83.28 C HETATM 2786 N36 2GM A2001 -17.833 14.954 20.117 1.00 82.45 N HETATM 2787 C34 2GM A2001 -18.433 15.082 21.428 1.00 81.11 C HETATM 2788 O35 2GM A2001 -18.074 15.995 22.189 1.00 82.08 O HETATM 2789 C26 2GM A2001 -19.476 14.110 21.943 1.00 77.46 C HETATM 2790 C27 2GM A2001 -19.090 13.448 23.265 1.00 72.40 C HETATM 2791 C28 2GM A2001 -20.213 12.692 23.971 1.00 67.95 C HETATM 2792 C29 2GM A2001 -20.032 11.324 24.275 1.00 65.04 C HETATM 2793 C30 2GM A2001 -21.043 10.610 24.924 1.00 62.96 C HETATM 2794 C31 2GM A2001 -22.226 11.268 25.290 1.00 62.20 C HETATM 2795 C32 2GM A2001 -22.416 12.629 25.029 1.00 63.02 C HETATM 2796 C33 2GM A2001 -21.401 13.348 24.372 1.00 65.23 C HETATM 2797 O HOH A2002 5.715 -49.668 35.878 1.00 74.79 O HETATM 2798 O HOH A2003 -19.574 16.643 17.582 1.00 75.59 O HETATM 2799 O HOH A2004 -24.614 9.582 17.912 1.00 55.76 O HETATM 2800 O HOH A2005 -8.787 -8.378 20.825 1.00 65.95 O HETATM 2801 O HOH A2006 -17.588 23.810 7.013 1.00 93.23 O CONECT 643 1195 CONECT 1195 643 CONECT 2754 2755 2770 CONECT 2755 2754 2756 2766 CONECT 2756 2755 2757 2758 CONECT 2757 2756 2761 2764 CONECT 2758 2756 2759 CONECT 2759 2758 2760 CONECT 2760 2759 2761 CONECT 2761 2757 2760 2762 CONECT 2762 2761 2763 CONECT 2763 2762 2764 CONECT 2764 2757 2763 2765 CONECT 2765 2764 2766 CONECT 2766 2755 2765 2767 CONECT 2767 2766 2768 2769 CONECT 2768 2767 CONECT 2769 2767 2770 CONECT 2770 2754 2769 2771 CONECT 2771 2770 2772 2773 CONECT 2772 2771 CONECT 2773 2771 2774 CONECT 2774 2773 2775 2776 2777 CONECT 2775 2774 CONECT 2776 2774 2780 CONECT 2777 2774 2778 2779 CONECT 2778 2777 CONECT 2779 2777 2780 2789 CONECT 2780 2776 2779 2781 2782 CONECT 2781 2780 CONECT 2782 2780 2783 2786 CONECT 2783 2782 2784 CONECT 2784 2783 2785 CONECT 2785 2784 2786 CONECT 2786 2782 2785 2787 CONECT 2787 2786 2788 2789 CONECT 2788 2787 CONECT 2789 2779 2787 2790 CONECT 2790 2789 2791 CONECT 2791 2790 2792 2796 CONECT 2792 2791 2793 CONECT 2793 2792 2794 CONECT 2794 2793 2795 CONECT 2795 2794 2796 CONECT 2796 2791 2795 MASTER 397 0 1 15 0 0 4 6 2800 1 45 31 END