HEADER SIGNALING PROTEIN 31-MAY-14 4QIM TITLE STRUCTURE OF THE HUMAN SMOOTHENED RECEPTOR IN COMPLEX WITH ANTA XV COMPND MOL_ID: 1; COMPND 2 MOLECULE: SMOOTHENED HOMOLOG/SOLUBLE CYTOCHROME B562 CHIMERIC COMPND 3 PROTEIN; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP Q99835 RESIDUES 190-433, P0ABE7 RESIDUES 23-128, Q99835 COMPND 6 RESIDUES 441-555; 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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS HUMAN SMOOTHENED RECEPTOR, ANTITUMOR AGENT, NOVEL PROTEIN KEYWDS 2 ENGINEERING, GPCR NETWORK, PSI-BIOLOGY, STRUCTURAL GENOMICS, KEYWDS 3 MEMBRANE PROTEIN, GPCR, MEMBRANE, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR C.WANG,H.WU,T.EVRON,E.VARDY,G.W.HAN,X.-P.HUANG,S.J.HUFEISEN, AUTHOR 2 T.J.MANGANO,D.J.URBAN,V.KATRITCH,V.CHEREZOV,M.G.CARON,B.L.ROTH, AUTHOR 3 R.C.STEVENS,GPCR NETWORK (GPCR) REVDAT 4 22-NOV-17 4QIM 1 REMARK REVDAT 3 02-AUG-17 4QIM 1 SOURCE REMARK REVDAT 2 13-AUG-14 4QIM 1 JRNL REVDAT 1 23-JUL-14 4QIM 0 JRNL AUTH C.WANG,H.WU,T.EVRON,E.VARDY,G.W.HAN,X.P.HUANG,S.J.HUFEISEN, JRNL AUTH 2 T.J.MANGANO,D.J.URBAN,V.KATRITCH,V.CHEREZOV,M.G.CARON, JRNL AUTH 3 B.L.ROTH,R.C.STEVENS JRNL TITL STRUCTURAL BASIS FOR SMOOTHENED RECEPTOR MODULATION AND JRNL TITL 2 CHEMORESISTANCE TO ANTICANCER DRUGS. JRNL REF NAT COMMUN V. 5 4355 2014 JRNL REFN ESSN 2041-1723 JRNL PMID 25008467 JRNL DOI 10.1038/NCOMMS5355 REMARK 2 REMARK 2 RESOLUTION. 2.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.64 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 3 NUMBER OF REFLECTIONS : 17377 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) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190 REMARK 3 FREE R VALUE TEST SET COUNT : 901 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 : 9 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.77 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.99 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2320 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2275 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2178 REMARK 3 BIN R VALUE (WORKING SET) : 0.2205 REMARK 3 BIN FREE R VALUE : 0.3379 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.12 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142 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 : 3519 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 34 REMARK 3 SOLVENT ATOMS : 23 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 79.08 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 97.89 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.87370 REMARK 3 B22 (A**2) : -11.84470 REMARK 3 B33 (A**2) : 13.71850 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) : 0.466 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) : 0.640 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 : 0.934 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3650 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4980 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1622 ; 4.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 69 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 539 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3650 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 483 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : 2 ; 1.000 ; HARMONIC REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 4377 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 0.97 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.35 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.57 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|190 - A|553 } REMARK 3 ORIGIN FOR THE GROUP (A): 15.2152 -10.5374 -33.3500 REMARK 3 T TENSOR REMARK 3 T11: -0.1493 T22: 0.1149 REMARK 3 T33: -0.3054 T12: -0.1116 REMARK 3 T13: -0.0333 T23: 0.0823 REMARK 3 L TENSOR REMARK 3 L11: 0.9208 L22: 0.5652 REMARK 3 L33: 4.1131 L12: 0.0139 REMARK 3 L13: 0.2798 L23: -0.5485 REMARK 3 S TENSOR REMARK 3 S11: -0.1378 S12: 0.0705 S13: 0.0047 REMARK 3 S21: -0.1188 S22: 0.0341 S23: -0.0329 REMARK 3 S31: -0.1481 S32: -0.1085 S33: 0.1037 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1001 - A|1106 } REMARK 3 ORIGIN FOR THE GROUP (A): -14.0532 -7.7742 -84.2355 REMARK 3 T TENSOR REMARK 3 T11: -0.1036 T22: 0.0990 REMARK 3 T33: -0.3589 T12: -0.1613 REMARK 3 T13: 0.0988 T23: -0.0994 REMARK 3 L TENSOR REMARK 3 L11: 1.3363 L22: 8.7400 REMARK 3 L33: 4.0699 L12: 1.5482 REMARK 3 L13: 0.6437 L23: -0.5135 REMARK 3 S TENSOR REMARK 3 S11: -0.0394 S12: -0.0094 S13: -0.0772 REMARK 3 S21: -0.4273 S22: 0.0491 S23: -0.0318 REMARK 3 S31: 0.3597 S32: 0.0143 S33: -0.0097 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4QIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-14. REMARK 100 THE DEPOSITION ID IS D_1000086101. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAY-13 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.2 REMARK 200 NUMBER OF CRYSTALS USED : 6 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17421 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 200 DATA REDUNDANCY : 7.700 REMARK 200 R MERGE (I) : 0.09100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 35.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6 REMARK 200 DATA REDUNDANCY IN SHELL : 6.30 REMARK 200 R MERGE FOR SHELL (I) : 0.72300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: TWO INDEPENDENT SEARCH MODELS OF SMO AND BRIL REMARK 200 DOMAINS FROM PDB ENTRY 4JKV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100-115MM NH4CL, 100MM HEPES PH7.2, REMARK 280 36% PEG400, LIPIDIC CUBIC PHASE (LCP), TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.41500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.03500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.92000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.03500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.41500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.92000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 187 REMARK 465 GLY A 188 REMARK 465 THR A 189 REMARK 465 GLY A 347 REMARK 465 THR A 348 REMARK 465 THR A 349 REMARK 465 TYR A 350 REMARK 465 GLN A 351 REMARK 465 PRO A 352 REMARK 465 GLY A 554 REMARK 465 GLN A 555 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 GLU A 194 CG CD OE1 OE2 REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 261 CG CD NE CZ NH1 NH2 REMARK 470 SER A 354 OG REMARK 470 LYS A 356 CG CD CE NZ REMARK 470 ASN A 432 OD1 ND2 REMARK 470 GLU A1004 CG CD OE1 OE2 REMARK 470 ASP A1005 CG OD1 OD2 REMARK 470 LYS A1042 CD CE NZ REMARK 470 LYS A1047 CG CD CE NZ REMARK 470 LEU A1048 CG CD1 CD2 REMARK 470 GLU A1049 CG CD OE1 OE2 REMARK 470 ASP A1050 CG OD1 OD2 REMARK 470 LYS A1051 CG CD CE NZ REMARK 470 ASP A1054 CG OD1 OD2 REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 LEU A1106 CG CD1 CD2 REMARK 470 SER A 443 OG REMARK 470 LYS A 444 CG CD CE NZ REMARK 470 GLU A 447 CG CD OE1 OE2 REMARK 470 ARG A 482 CZ NH1 NH2 REMARK 470 THR A 495 OG1 CG2 REMARK 470 GLU A 508 CG CD OE1 OE2 REMARK 470 LYS A 539 CG CD CE NZ REMARK 470 ARG A 546 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 547 CZ NH1 NH2 REMARK 470 LEU A 552 CG CD1 CD2 REMARK 470 THR A 553 OG1 CG2 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 PRO A 196 30.44 -98.55 REMARK 500 GLU A 208 -112.00 39.81 REMARK 500 ASN A 219 114.07 -25.82 REMARK 500 ASP A 287 112.78 -38.64 REMARK 500 ASN A 309 -5.03 72.76 REMARK 500 ALA A 379 70.01 47.03 REMARK 500 VAL A 404 -61.70 -127.51 REMARK 500 PRO A 513 151.73 -48.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1202 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 433 NE2 REMARK 620 2 HOH A1311 O 85.0 REMARK 620 3 HOH A1312 O 117.7 114.6 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A8T A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1202 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4O9R RELATED DB: PDB REMARK 900 HUMAN SMOOTHENED RECEPTOR STRUCTURE IN COMPLEX WITH CYCLOPAMINE REMARK 900 RELATED ID: GPCR-131 RELATED DB: TARGETTRACK REMARK 900 RELATED ID: 4QIN RELATED DB: PDB DBREF 4QIM A 190 433 UNP Q99835 SMO_HUMAN 190 433 DBREF 4QIM A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4QIM A 441 555 UNP Q99835 SMO_HUMAN 441 555 SEQADV 4QIM GLY A 187 UNP Q99835 EXPRESSION TAG SEQADV 4QIM GLY A 188 UNP Q99835 EXPRESSION TAG SEQADV 4QIM THR A 189 UNP Q99835 EXPRESSION TAG SEQADV 4QIM TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4QIM ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4QIM LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQRES 1 A 468 GLY GLY THR SER GLY GLN CYS GLU VAL PRO LEU VAL ARG SEQRES 2 A 468 THR ASP ASN PRO LYS SER TRP TYR GLU ASP VAL GLU GLY SEQRES 3 A 468 CYS GLY ILE GLN CYS GLN ASN PRO LEU PHE THR GLU ALA SEQRES 4 A 468 GLU HIS GLN ASP MET HIS SER TYR ILE ALA ALA PHE GLY SEQRES 5 A 468 ALA VAL THR GLY LEU CYS THR LEU PHE THR LEU ALA THR SEQRES 6 A 468 PHE VAL ALA ASP TRP ARG ASN SER ASN ARG TYR PRO ALA SEQRES 7 A 468 VAL ILE LEU PHE TYR VAL ASN ALA CYS PHE PHE VAL GLY SEQRES 8 A 468 SER ILE GLY TRP LEU ALA GLN PHE MET ASP GLY ALA ARG SEQRES 9 A 468 ARG GLU ILE VAL CYS ARG ALA ASP GLY THR MET ARG LEU SEQRES 10 A 468 GLY GLU PRO THR SER ASN GLU THR LEU SER CYS VAL ILE SEQRES 11 A 468 ILE PHE VAL ILE VAL TYR TYR ALA LEU MET ALA GLY VAL SEQRES 12 A 468 VAL TRP PHE VAL VAL LEU THR TYR ALA TRP HIS THR SER SEQRES 13 A 468 PHE LYS ALA LEU GLY THR THR TYR GLN PRO LEU SER GLY SEQRES 14 A 468 LYS THR SER TYR PHE HIS LEU LEU THR TRP SER LEU PRO SEQRES 15 A 468 PHE VAL LEU THR VAL ALA ILE LEU ALA VAL ALA GLN VAL SEQRES 16 A 468 ASP GLY ASP SER VAL SER GLY ILE CYS PHE VAL GLY TYR SEQRES 17 A 468 LYS ASN TYR ARG TYR ARG ALA GLY PHE VAL LEU ALA PRO SEQRES 18 A 468 ILE GLY LEU VAL LEU ILE VAL GLY GLY TYR PHE LEU ILE SEQRES 19 A 468 ARG GLY VAL MET THR LEU PHE SER ILE LYS SER ASN HIS SEQRES 20 A 468 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 21 A 468 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 22 A 468 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 23 A 468 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 24 A 468 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 25 A 468 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 26 A 468 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 27 A 468 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 28 A 468 TYR LEU ALA ALA SER LYS ILE ASN GLU THR MET LEU ARG SEQRES 29 A 468 LEU GLY ILE PHE GLY PHE LEU ALA PHE GLY PHE VAL LEU SEQRES 30 A 468 ILE THR PHE SER CYS HIS PHE TYR ASP PHE PHE ASN GLN SEQRES 31 A 468 ALA GLU TRP GLU ARG SER PHE ARG ASP TYR VAL LEU CYS SEQRES 32 A 468 GLN ALA ASN VAL THR ILE GLY LEU PRO THR LYS GLN PRO SEQRES 33 A 468 ILE PRO ASP CYS GLU ILE LYS ASN ARG PRO SER LEU LEU SEQRES 34 A 468 VAL GLU LYS ILE ASN LEU PHE ALA MET PHE GLY THR GLY SEQRES 35 A 468 ILE ALA MET SER THR TRP VAL TRP THR LYS ALA THR LEU SEQRES 36 A 468 LEU ILE TRP ARG ARG THR TRP CYS ARG LEU THR GLY GLN HET A8T A1201 33 HET ZN A1202 1 HETNAM A8T 2-{6-[4-(4-BENZYLPHTHALAZIN-1-YL)PIPERAZIN-1- HETNAM 2 A8T YL]PYRIDIN-3-YL}PROPAN-2-OL HETNAM ZN ZINC ION FORMUL 2 A8T C27 H29 N5 O FORMUL 3 ZN ZN 2+ FORMUL 4 HOH *23(H2 O) HELIX 1 1 ASN A 202 TRP A 206 5 5 HELIX 2 2 THR A 223 ASP A 255 1 33 HELIX 3 3 ASP A 255 ASN A 260 1 6 HELIX 4 4 VAL A 265 ALA A 283 1 19 HELIX 5 5 GLN A 284 MET A 286 5 3 HELIX 6 6 GLY A 288 CYS A 295 1 8 HELIX 7 7 LEU A 312 SER A 342 1 31 HELIX 8 8 PHE A 343 ALA A 345 5 3 HELIX 9 9 LYS A 356 ALA A 379 1 24 HELIX 10 10 ASN A 396 VAL A 404 1 9 HELIX 11 11 VAL A 404 LYS A 1019 1 49 HELIX 12 12 ASN A 1022 ALA A 1043 1 22 HELIX 13 13 PRO A 1045 GLU A 1049 5 5 HELIX 14 14 SER A 1055 GLY A 1082 1 28 HELIX 15 15 VAL A 1084 ILE A 1102 1 19 HELIX 16 16 ILE A 1102 ALA A 442 1 7 HELIX 17 17 ASN A 446 ALA A 492 1 47 HELIX 18 18 SER A 514 THR A 534 1 21 HELIX 19 19 TRP A 535 TRP A 537 5 3 HELIX 20 20 THR A 538 THR A 553 1 16 SHEET 1 A 2 LEU A 197 ARG A 199 0 SHEET 2 A 2 CYS A 213 ILE A 215 -1 O GLY A 214 N VAL A 198 SHEET 1 B 2 VAL A 381 ASP A 384 0 SHEET 2 B 2 ILE A 389 VAL A 392 -1 O PHE A 391 N ASP A 382 SSBOND 1 CYS A 193 CYS A 213 1555 1555 2.03 SSBOND 2 CYS A 217 CYS A 295 1555 1555 2.03 SSBOND 3 CYS A 314 CYS A 390 1555 1555 2.04 SSBOND 4 CYS A 490 CYS A 507 1555 1555 2.05 LINK NE2 HIS A 433 ZN ZN A1202 1555 1555 2.09 LINK ZN ZN A1202 O HOH A1311 1555 1555 2.22 LINK ZN ZN A1202 O HOH A1312 1555 1555 2.23 CISPEP 1 VAL A 195 PRO A 196 0 10.66 CISPEP 2 TYR A 262 PRO A 263 0 5.04 CISPEP 3 GLU A 305 PRO A 306 0 3.76 SITE 1 AC1 14 ASN A 219 LEU A 221 TRP A 281 ASP A 384 SITE 2 AC1 14 VAL A 386 PHE A 391 TYR A 394 LYS A 395 SITE 3 AC1 14 ARG A 400 HIS A 470 ASP A 473 GLN A 477 SITE 4 AC1 14 GLU A 518 ASN A 521 SITE 1 AC2 4 HIS A 433 ASP A1021 HOH A1311 HOH A1312 CRYST1 42.830 79.840 170.070 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023348 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012525 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005880 0.00000 ATOM 1 N SER A 190 26.877 -21.786 3.134 1.00110.78 N ANISOU 1 N SER A 190 12581 18185 11325 -9 -465 2081 N ATOM 2 CA SER A 190 25.873 -20.791 2.746 1.00108.80 C ANISOU 2 CA SER A 190 12372 17848 11120 -147 -472 1948 C ATOM 3 C SER A 190 26.276 -19.381 3.254 1.00110.83 C ANISOU 3 C SER A 190 12552 18246 11313 -254 -555 1865 C ATOM 4 O SER A 190 27.106 -19.269 4.164 1.00111.23 O ANISOU 4 O SER A 190 12519 18470 11271 -246 -607 1915 O ATOM 5 CB SER A 190 24.492 -21.194 3.270 1.00111.67 C ANISOU 5 CB SER A 190 12830 18123 11476 -177 -435 1943 C ATOM 6 OG SER A 190 24.495 -21.487 4.659 1.00117.28 O ANISOU 6 OG SER A 190 13522 18952 12087 -155 -455 2009 O ATOM 7 N GLY A 191 25.701 -18.334 2.650 1.00104.90 N ANISOU 7 N GLY A 191 11844 17414 10599 -355 -571 1742 N ATOM 8 CA GLY A 191 25.998 -16.950 3.009 1.00104.33 C ANISOU 8 CA GLY A 191 11759 17422 10460 -468 -653 1651 C ATOM 9 C GLY A 191 24.824 -15.998 3.165 1.00105.67 C ANISOU 9 C GLY A 191 12032 17505 10614 -527 -664 1526 C ATOM 10 O GLY A 191 23.725 -16.405 3.555 1.00105.52 O ANISOU 10 O GLY A 191 12058 17443 10592 -481 -617 1523 O ATOM 11 N GLN A 192 25.080 -14.702 2.886 1.00 99.63 N ANISOU 11 N GLN A 192 11310 16724 9820 -629 -729 1428 N ATOM 12 CA GLN A 192 24.138 -13.576 2.982 1.00 97.98 C ANISOU 12 CA GLN A 192 11227 16429 9573 -666 -754 1297 C ATOM 13 C GLN A 192 22.981 -13.660 1.977 1.00 97.00 C ANISOU 13 C GLN A 192 11161 16153 9542 -617 -688 1251 C ATOM 14 O GLN A 192 21.892 -13.140 2.243 1.00 96.43 O ANISOU 14 O GLN A 192 11167 16042 9430 -582 -679 1172 O ATOM 15 CB GLN A 192 24.882 -12.245 2.726 1.00 99.96 C ANISOU 15 CB GLN A 192 11540 16669 9771 -799 -846 1219 C ATOM 16 CG GLN A 192 25.866 -11.807 3.810 1.00122.16 C ANISOU 16 CG GLN A 192 14325 19636 12453 -891 -934 1233 C ATOM 17 CD GLN A 192 26.579 -10.507 3.476 1.00142.51 C ANISOU 17 CD GLN A 192 16990 22191 14969 -1064 -1031 1162 C ATOM 18 OE1 GLN A 192 27.766 -10.335 3.785 1.00140.67 O ANISOU 18 OE1 GLN A 192 16678 22108 14663 -1185 -1101 1212 O ATOM 19 NE2 GLN A 192 25.882 -9.556 2.843 1.00128.11 N ANISOU 19 NE2 GLN A 192 15332 20186 13158 -1088 -1043 1051 N ATOM 20 N CYS A 193 23.248 -14.235 0.794 1.00 89.31 N ANISOU 20 N CYS A 193 10149 15108 8677 -612 -646 1295 N ATOM 21 CA CYS A 193 22.279 -14.312 -0.292 1.00 86.42 C ANISOU 21 CA CYS A 193 9831 14608 8396 -587 -592 1256 C ATOM 22 C CYS A 193 21.871 -15.749 -0.555 1.00 87.99 C ANISOU 22 C CYS A 193 9990 14781 8661 -524 -512 1346 C ATOM 23 O CYS A 193 22.680 -16.669 -0.423 1.00 87.46 O ANISOU 23 O CYS A 193 9867 14756 8607 -492 -496 1442 O ATOM 24 CB CYS A 193 22.841 -13.664 -1.554 1.00 85.40 C ANISOU 24 CB CYS A 193 9725 14397 8326 -652 -616 1217 C ATOM 25 SG CYS A 193 23.621 -12.050 -1.271 1.00 89.60 S ANISOU 25 SG CYS A 193 10331 14948 8764 -775 -726 1135 S ATOM 26 N GLU A 194 20.598 -15.924 -0.918 1.00 83.14 N ANISOU 26 N GLU A 194 9414 14103 8073 -506 -465 1317 N ATOM 27 CA GLU A 194 20.002 -17.204 -1.267 1.00 82.53 C ANISOU 27 CA GLU A 194 9333 13978 8045 -486 -395 1390 C ATOM 28 C GLU A 194 19.701 -17.204 -2.768 1.00 86.00 C ANISOU 28 C GLU A 194 9806 14295 8575 -508 -368 1356 C ATOM 29 O GLU A 194 19.575 -16.129 -3.359 1.00 86.09 O ANISOU 29 O GLU A 194 9842 14272 8598 -529 -398 1269 O ATOM 30 CB GLU A 194 18.737 -17.444 -0.421 1.00 84.19 C ANISOU 30 CB GLU A 194 9543 14258 8187 -478 -367 1396 C ATOM 31 N VAL A 195 19.625 -18.394 -3.398 1.00 81.21 N ANISOU 31 N VAL A 195 9221 13611 8025 -505 -315 1424 N ATOM 32 CA VAL A 195 19.314 -18.532 -4.826 1.00 79.33 C ANISOU 32 CA VAL A 195 9022 13257 7863 -531 -286 1396 C ATOM 33 C VAL A 195 17.898 -17.886 -5.051 1.00 78.83 C ANISOU 33 C VAL A 195 8964 13208 7781 -566 -283 1324 C ATOM 34 O VAL A 195 17.055 -17.994 -4.165 1.00 78.22 O ANISOU 34 O VAL A 195 8864 13219 7636 -568 -275 1336 O ATOM 35 CB VAL A 195 19.438 -20.017 -5.318 1.00 84.64 C ANISOU 35 CB VAL A 195 9753 13833 8574 -519 -232 1481 C ATOM 36 CG1 VAL A 195 18.536 -20.966 -4.546 1.00 85.74 C ANISOU 36 CG1 VAL A 195 9929 13986 8663 -552 -202 1547 C ATOM 37 CG2 VAL A 195 19.189 -20.158 -6.816 1.00 84.37 C ANISOU 37 CG2 VAL A 195 9770 13680 8608 -549 -205 1445 C ATOM 38 N PRO A 196 17.660 -17.075 -6.111 1.00 73.01 N ANISOU 38 N PRO A 196 8244 12416 7082 -580 -295 1248 N ATOM 39 CA PRO A 196 18.505 -16.827 -7.288 1.00 70.98 C ANISOU 39 CA PRO A 196 8007 12067 6894 -590 -303 1228 C ATOM 40 C PRO A 196 19.335 -15.540 -7.193 1.00 73.67 C ANISOU 40 C PRO A 196 8347 12427 7216 -594 -365 1172 C ATOM 41 O PRO A 196 19.653 -14.938 -8.216 1.00 72.54 O ANISOU 41 O PRO A 196 8229 12223 7112 -622 -381 1133 O ATOM 42 CB PRO A 196 17.470 -16.754 -8.403 1.00 72.09 C ANISOU 42 CB PRO A 196 8174 12150 7067 -620 -281 1187 C ATOM 43 CG PRO A 196 16.286 -16.086 -7.766 1.00 77.17 C ANISOU 43 CG PRO A 196 8798 12883 7639 -601 -294 1143 C ATOM 44 CD PRO A 196 16.332 -16.448 -6.287 1.00 73.94 C ANISOU 44 CD PRO A 196 8357 12574 7164 -580 -294 1188 C ATOM 45 N LEU A 197 19.719 -15.139 -5.977 1.00 70.67 N ANISOU 45 N LEU A 197 7950 12133 6768 -583 -404 1173 N ATOM 46 CA LEU A 197 20.567 -13.967 -5.808 1.00 69.69 C ANISOU 46 CA LEU A 197 7847 12026 6608 -622 -473 1127 C ATOM 47 C LEU A 197 21.984 -14.416 -5.446 1.00 75.47 C ANISOU 47 C LEU A 197 8508 12834 7332 -639 -488 1200 C ATOM 48 O LEU A 197 22.161 -15.434 -4.777 1.00 77.04 O ANISOU 48 O LEU A 197 8659 13091 7523 -590 -458 1276 O ATOM 49 CB LEU A 197 20.015 -12.974 -4.761 1.00 69.16 C ANISOU 49 CB LEU A 197 7834 12001 6445 -605 -520 1057 C ATOM 50 CG LEU A 197 18.574 -12.444 -4.940 1.00 72.31 C ANISOU 50 CG LEU A 197 8289 12370 6817 -546 -505 986 C ATOM 51 CD1 LEU A 197 18.288 -11.346 -3.949 1.00 72.90 C ANISOU 51 CD1 LEU A 197 8442 12477 6778 -505 -557 910 C ATOM 52 CD2 LEU A 197 18.316 -11.902 -6.344 1.00 72.64 C ANISOU 52 CD2 LEU A 197 8384 12303 6914 -561 -507 941 C ATOM 53 N VAL A 198 22.984 -13.668 -5.923 1.00 71.22 N ANISOU 53 N VAL A 198 7964 12309 6789 -709 -536 1186 N ATOM 54 CA VAL A 198 24.423 -13.864 -5.689 1.00 71.16 C ANISOU 54 CA VAL A 198 7863 12421 6753 -739 -562 1256 C ATOM 55 C VAL A 198 24.951 -12.643 -4.929 1.00 77.24 C ANISOU 55 C VAL A 198 8662 13259 7428 -845 -654 1212 C ATOM 56 O VAL A 198 24.357 -11.570 -5.029 1.00 77.25 O ANISOU 56 O VAL A 198 8781 13167 7403 -895 -695 1123 O ATOM 57 CB VAL A 198 25.249 -14.136 -6.990 1.00 74.13 C ANISOU 57 CB VAL A 198 8186 12797 7185 -752 -535 1294 C ATOM 58 CG1 VAL A 198 24.957 -15.519 -7.573 1.00 73.38 C ANISOU 58 CG1 VAL A 198 8079 12644 7160 -638 -447 1347 C ATOM 59 CG2 VAL A 198 25.072 -13.040 -8.044 1.00 73.21 C ANISOU 59 CG2 VAL A 198 8143 12587 7088 -847 -565 1221 C ATOM 60 N ARG A 199 26.054 -12.802 -4.178 1.00 75.53 N ANISOU 60 N ARG A 199 8350 13202 7147 -877 -691 1277 N ATOM 61 CA ARG A 199 26.662 -11.721 -3.392 1.00 76.67 C ANISOU 61 CA ARG A 199 8522 13427 7181 -1007 -789 1244 C ATOM 62 C ARG A 199 27.360 -10.694 -4.318 1.00 80.54 C ANISOU 62 C ARG A 199 9045 13900 7654 -1166 -846 1217 C ATOM 63 O ARG A 199 28.092 -11.084 -5.242 1.00 81.55 O ANISOU 63 O ARG A 199 9069 14090 7824 -1179 -817 1279 O ATOM 64 CB ARG A 199 27.652 -12.319 -2.376 1.00 79.38 C ANISOU 64 CB ARG A 199 8728 13979 7454 -995 -809 1337 C ATOM 65 CG ARG A 199 28.312 -11.345 -1.387 1.00 90.03 C ANISOU 65 CG ARG A 199 10096 15443 8669 -1143 -916 1314 C ATOM 66 CD ARG A 199 27.372 -10.802 -0.332 1.00 92.35 C ANISOU 66 CD ARG A 199 10530 15659 8898 -1128 -946 1226 C ATOM 67 NE ARG A 199 28.052 -9.864 0.559 1.00104.84 N ANISOU 67 NE ARG A 199 12157 17337 10339 -1282 -1053 1197 N ATOM 68 CZ ARG A 199 28.188 -8.561 0.327 1.00127.49 C ANISOU 68 CZ ARG A 199 15181 20119 13142 -1446 -1137 1112 C ATOM 69 NH1 ARG A 199 28.819 -7.789 1.201 1.00124.31 N ANISOU 69 NH1 ARG A 199 14835 19802 12596 -1602 -1240 1088 N ATOM 70 NH2 ARG A 199 27.698 -8.020 -0.783 1.00113.91 N ANISOU 70 NH2 ARG A 199 13575 18219 11486 -1462 -1122 1053 N ATOM 71 N THR A 200 27.106 -9.383 -4.079 1.00 75.29 N ANISOU 71 N THR A 200 8543 13146 6917 -1284 -925 1126 N ATOM 72 CA THR A 200 27.704 -8.301 -4.874 1.00 75.00 C ANISOU 72 CA THR A 200 8584 13068 6844 -1466 -993 1100 C ATOM 73 C THR A 200 27.936 -7.046 -4.022 1.00 80.29 C ANISOU 73 C THR A 200 9415 13718 7375 -1628 -1108 1033 C ATOM 74 O THR A 200 27.107 -6.679 -3.184 1.00 79.08 O ANISOU 74 O THR A 200 9401 13473 7174 -1559 -1125 954 O ATOM 75 CB THR A 200 26.883 -7.954 -6.148 1.00 78.11 C ANISOU 75 CB THR A 200 9091 13264 7321 -1432 -956 1044 C ATOM 76 OG1 THR A 200 27.514 -6.849 -6.791 1.00 77.77 O ANISOU 76 OG1 THR A 200 9143 13182 7223 -1627 -1032 1026 O ATOM 77 CG2 THR A 200 25.410 -7.606 -5.870 1.00 71.82 C ANISOU 77 CG2 THR A 200 8460 12294 6533 -1305 -939 945 C ATOM 78 N ASP A 201 29.081 -6.391 -4.271 1.00 79.21 N ANISOU 78 N ASP A 201 9262 13675 7160 -1850 -1187 1068 N ATOM 79 CA ASP A 201 29.503 -5.164 -3.597 1.00 80.40 C ANISOU 79 CA ASP A 201 9585 13806 7159 -2064 -1312 1014 C ATOM 80 C ASP A 201 29.109 -3.934 -4.406 1.00 84.65 C ANISOU 80 C ASP A 201 10386 14105 7674 -2175 -1365 931 C ATOM 81 O ASP A 201 29.274 -2.815 -3.921 1.00 87.17 O ANISOU 81 O ASP A 201 10925 14335 7860 -2345 -1471 868 O ATOM 82 CB ASP A 201 31.018 -5.167 -3.350 1.00 83.39 C ANISOU 82 CB ASP A 201 9789 14457 7439 -2279 -1380 1114 C ATOM 83 CG ASP A 201 31.482 -5.943 -2.136 1.00 93.83 C ANISOU 83 CG ASP A 201 10932 16009 8710 -2217 -1380 1177 C ATOM 84 OD1 ASP A 201 30.688 -6.060 -1.160 1.00 92.67 O ANISOU 84 OD1 ASP A 201 10876 15784 8549 -2086 -1370 1116 O ATOM 85 OD2 ASP A 201 32.675 -6.341 -2.107 1.00100.55 O ANISOU 85 OD2 ASP A 201 11557 17137 9511 -2309 -1399 1288 O ATOM 86 N ASN A 202 28.603 -4.138 -5.629 1.00 78.58 N ANISOU 86 N ASN A 202 9611 13223 7021 -2084 -1294 932 N ATOM 87 CA ASN A 202 28.163 -3.068 -6.508 1.00 79.11 C ANISOU 87 CA ASN A 202 9922 13060 7076 -2156 -1333 865 C ATOM 88 C ASN A 202 26.702 -2.728 -6.195 1.00 84.62 C ANISOU 88 C ASN A 202 10829 13538 7784 -1946 -1310 752 C ATOM 89 O ASN A 202 25.807 -3.535 -6.481 1.00 83.14 O ANISOU 89 O ASN A 202 10544 13336 7707 -1726 -1211 751 O ATOM 90 CB ASN A 202 28.346 -3.467 -7.983 1.00 78.89 C ANISOU 90 CB ASN A 202 9773 13044 7157 -2154 -1268 927 C ATOM 91 CG ASN A 202 27.957 -2.420 -9.010 1.00100.32 C ANISOU 91 CG ASN A 202 12723 15535 9861 -2232 -1306 876 C ATOM 92 OD1 ASN A 202 27.836 -1.218 -8.723 1.00 95.54 O ANISOU 92 OD1 ASN A 202 12396 14762 9144 -2350 -1402 807 O ATOM 93 ND2 ASN A 202 27.802 -2.858 -10.256 1.00 90.06 N ANISOU 93 ND2 ASN A 202 11330 14223 8667 -2171 -1233 913 N ATOM 94 N PRO A 203 26.447 -1.529 -5.619 1.00 83.10 N ANISOU 94 N PRO A 203 10932 13182 7460 -2011 -1403 657 N ATOM 95 CA PRO A 203 25.059 -1.138 -5.278 1.00 82.70 C ANISOU 95 CA PRO A 203 11083 12948 7390 -1779 -1381 548 C ATOM 96 C PRO A 203 24.118 -1.042 -6.492 1.00 86.48 C ANISOU 96 C PRO A 203 11623 13275 7961 -1632 -1322 525 C ATOM 97 O PRO A 203 22.932 -1.348 -6.362 1.00 85.61 O ANISOU 97 O PRO A 203 11508 13132 7888 -1387 -1254 481 O ATOM 98 CB PRO A 203 25.239 0.230 -4.622 1.00 86.21 C ANISOU 98 CB PRO A 203 11867 13234 7656 -1914 -1506 458 C ATOM 99 CG PRO A 203 26.667 0.224 -4.134 1.00 91.33 C ANISOU 99 CG PRO A 203 12416 14057 8229 -2203 -1585 527 C ATOM 100 CD PRO A 203 27.406 -0.484 -5.206 1.00 85.97 C ANISOU 100 CD PRO A 203 11469 13528 7666 -2297 -1536 645 C ATOM 101 N LYS A 204 24.645 -0.677 -7.674 1.00 83.43 N ANISOU 101 N LYS A 204 11268 12827 7605 -1784 -1345 566 N ATOM 102 CA LYS A 204 23.872 -0.601 -8.922 1.00 83.19 C ANISOU 102 CA LYS A 204 11280 12670 7658 -1668 -1295 557 C ATOM 103 C LYS A 204 23.301 -2.018 -9.301 1.00 84.86 C ANISOU 103 C LYS A 204 11200 13021 8023 -1480 -1166 608 C ATOM 104 O LYS A 204 22.341 -2.100 -10.071 1.00 83.66 O ANISOU 104 O LYS A 204 11067 12788 7931 -1328 -1113 586 O ATOM 105 CB LYS A 204 24.762 -0.002 -10.046 1.00 86.79 C ANISOU 105 CB LYS A 204 11801 13070 8103 -1910 -1349 608 C ATOM 106 CG LYS A 204 24.263 -0.101 -11.498 1.00113.21 C ANISOU 106 CG LYS A 204 15130 16338 11547 -1836 -1293 629 C ATOM 107 CD LYS A 204 22.947 0.638 -11.790 1.00128.65 C ANISOU 107 CD LYS A 204 17336 18070 13474 -1633 -1296 542 C ATOM 108 CE LYS A 204 22.410 0.285 -13.157 1.00137.77 C ANISOU 108 CE LYS A 204 18407 19202 14735 -1540 -1227 573 C ATOM 109 NZ LYS A 204 20.997 0.712 -13.324 1.00148.04 N ANISOU 109 NZ LYS A 204 19867 20364 16018 -1285 -1209 499 N ATOM 110 N SER A 205 23.847 -3.109 -8.701 1.00 79.84 N ANISOU 110 N SER A 205 10315 12588 7432 -1487 -1122 674 N ATOM 111 CA SER A 205 23.409 -4.486 -8.940 1.00 77.54 C ANISOU 111 CA SER A 205 9786 12410 7264 -1335 -1011 726 C ATOM 112 C SER A 205 22.477 -5.013 -7.841 1.00 82.00 C ANISOU 112 C SER A 205 10315 13024 7819 -1153 -968 693 C ATOM 113 O SER A 205 21.941 -6.111 -7.992 1.00 81.27 O ANISOU 113 O SER A 205 10063 13002 7812 -1035 -881 732 O ATOM 114 CB SER A 205 24.609 -5.421 -9.045 1.00 79.76 C ANISOU 114 CB SER A 205 9834 12879 7594 -1435 -984 829 C ATOM 115 OG SER A 205 25.537 -5.032 -10.044 1.00 85.75 O ANISOU 115 OG SER A 205 10583 13647 8352 -1607 -1015 874 O ATOM 116 N TRP A 206 22.287 -4.261 -6.741 1.00 79.26 N ANISOU 116 N TRP A 206 10121 12641 7353 -1140 -1029 625 N ATOM 117 CA TRP A 206 21.454 -4.727 -5.628 1.00 78.82 C ANISOU 117 CA TRP A 206 10023 12660 7267 -974 -988 599 C ATOM 118 C TRP A 206 19.990 -4.787 -6.015 1.00 84.92 C ANISOU 118 C TRP A 206 10822 13380 8065 -770 -926 555 C ATOM 119 O TRP A 206 19.471 -3.872 -6.664 1.00 84.47 O ANISOU 119 O TRP A 206 10940 13180 7977 -723 -953 495 O ATOM 120 CB TRP A 206 21.625 -3.866 -4.366 1.00 78.02 C ANISOU 120 CB TRP A 206 10092 12539 7014 -1002 -1069 530 C ATOM 121 CG TRP A 206 23.011 -3.881 -3.783 1.00 78.66 C ANISOU 121 CG TRP A 206 10118 12722 7046 -1209 -1135 579 C ATOM 122 CD1 TRP A 206 24.052 -4.695 -4.136 1.00 80.81 C ANISOU 122 CD1 TRP A 206 10174 13137 7392 -1326 -1117 685 C ATOM 123 CD2 TRP A 206 23.482 -3.076 -2.701 1.00 79.60 C ANISOU 123 CD2 TRP A 206 10394 12835 7015 -1310 -1230 526 C ATOM 124 NE1 TRP A 206 25.158 -4.404 -3.380 1.00 81.18 N ANISOU 124 NE1 TRP A 206 10215 13287 7343 -1501 -1197 709 N ATOM 125 CE2 TRP A 206 24.838 -3.417 -2.484 1.00 83.56 C ANISOU 125 CE2 TRP A 206 10748 13494 7507 -1511 -1271 611 C ATOM 126 CE3 TRP A 206 22.903 -2.064 -1.917 1.00 81.63 C ANISOU 126 CE3 TRP A 206 10916 12969 7130 -1246 -1286 412 C ATOM 127 CZ2 TRP A 206 25.622 -2.781 -1.517 1.00 83.88 C ANISOU 127 CZ2 TRP A 206 10887 13582 7402 -1680 -1373 590 C ATOM 128 CZ3 TRP A 206 23.684 -1.440 -0.952 1.00 84.24 C ANISOU 128 CZ3 TRP A 206 11373 13317 7318 -1407 -1386 382 C ATOM 129 CH2 TRP A 206 25.023 -1.802 -0.759 1.00 85.01 C ANISOU 129 CH2 TRP A 206 11308 13580 7411 -1636 -1432 472 C ATOM 130 N TYR A 207 19.343 -5.895 -5.621 1.00 82.56 N ANISOU 130 N TYR A 207 10345 13210 7814 -657 -845 596 N ATOM 131 CA TYR A 207 17.947 -6.178 -5.891 1.00 82.47 C ANISOU 131 CA TYR A 207 10298 13219 7818 -484 -778 577 C ATOM 132 C TYR A 207 17.065 -5.607 -4.785 1.00 91.41 C ANISOU 132 C TYR A 207 11527 14387 8818 -330 -788 503 C ATOM 133 O TYR A 207 17.050 -6.126 -3.665 1.00 91.01 O ANISOU 133 O TYR A 207 11393 14461 8725 -307 -770 523 O ATOM 134 CB TYR A 207 17.734 -7.696 -6.039 1.00 82.14 C ANISOU 134 CB TYR A 207 10031 13301 7878 -478 -692 668 C ATOM 135 CG TYR A 207 16.314 -8.082 -6.391 1.00 83.11 C ANISOU 135 CG TYR A 207 10092 13475 8010 -346 -627 664 C ATOM 136 CD1 TYR A 207 15.886 -8.111 -7.717 1.00 84.37 C ANISOU 136 CD1 TYR A 207 10244 13574 8237 -342 -604 668 C ATOM 137 CD2 TYR A 207 15.397 -8.427 -5.400 1.00 84.02 C ANISOU 137 CD2 TYR A 207 10144 13727 8054 -238 -590 663 C ATOM 138 CE1 TYR A 207 14.576 -8.450 -8.046 1.00 84.67 C ANISOU 138 CE1 TYR A 207 10212 13692 8268 -239 -551 671 C ATOM 139 CE2 TYR A 207 14.085 -8.771 -5.717 1.00 84.83 C ANISOU 139 CE2 TYR A 207 10167 13921 8145 -137 -533 670 C ATOM 140 CZ TYR A 207 13.681 -8.785 -7.042 1.00 92.98 C ANISOU 140 CZ TYR A 207 11188 14897 9242 -142 -517 675 C ATOM 141 OH TYR A 207 12.392 -9.120 -7.358 1.00 95.96 O ANISOU 141 OH TYR A 207 11472 15395 9595 -60 -468 688 O ATOM 142 N GLU A 208 16.342 -4.528 -5.120 1.00 92.32 N ANISOU 142 N GLU A 208 11824 14395 8858 -211 -815 421 N ATOM 143 CA GLU A 208 15.349 -3.821 -4.306 1.00 95.58 C ANISOU 143 CA GLU A 208 12360 14830 9126 -8 -819 337 C ATOM 144 C GLU A 208 15.750 -3.682 -2.811 1.00103.44 C ANISOU 144 C GLU A 208 13405 15885 10012 -18 -852 306 C ATOM 145 O GLU A 208 16.689 -2.951 -2.490 1.00105.15 O ANISOU 145 O GLU A 208 13794 15987 10172 -141 -936 267 O ATOM 146 CB GLU A 208 13.987 -4.541 -4.409 1.00 97.11 C ANISOU 146 CB GLU A 208 12373 15196 9329 162 -728 366 C ATOM 147 CG GLU A 208 13.366 -4.532 -5.802 1.00110.91 C ANISOU 147 CG GLU A 208 14091 16904 11148 205 -701 382 C ATOM 148 CD GLU A 208 11.960 -5.099 -5.906 1.00139.75 C ANISOU 148 CD GLU A 208 17571 20750 14776 361 -623 408 C ATOM 149 OE1 GLU A 208 11.213 -5.060 -4.898 1.00141.88 O ANISOU 149 OE1 GLU A 208 17807 21173 14930 509 -597 384 O ATOM 150 OE2 GLU A 208 11.589 -5.542 -7.017 1.00131.96 O ANISOU 150 OE2 GLU A 208 16486 19778 13874 332 -591 452 O ATOM 151 N ASP A 209 15.024 -4.372 -1.912 1.00100.32 N ANISOU 151 N ASP A 209 12862 15680 9575 97 -790 326 N ATOM 152 CA ASP A 209 15.230 -4.323 -0.468 1.00101.42 C ANISOU 152 CA ASP A 209 13028 15906 9600 115 -809 300 C ATOM 153 C ASP A 209 16.382 -5.219 0.003 1.00103.56 C ANISOU 153 C ASP A 209 13156 16250 9944 -83 -819 387 C ATOM 154 O ASP A 209 16.800 -5.088 1.161 1.00104.99 O ANISOU 154 O ASP A 209 13376 16486 10028 -108 -854 367 O ATOM 155 CB ASP A 209 13.938 -4.744 0.260 1.00104.30 C ANISOU 155 CB ASP A 209 13271 16475 9881 318 -731 300 C ATOM 156 CG ASP A 209 12.802 -3.750 0.121 1.00120.61 C ANISOU 156 CG ASP A 209 15486 18521 11821 566 -725 205 C ATOM 157 OD1 ASP A 209 11.855 -4.029 -0.660 1.00120.98 O ANISOU 157 OD1 ASP A 209 15417 18646 11906 669 -667 234 O ATOM 158 OD2 ASP A 209 12.855 -2.691 0.791 1.00130.04 O ANISOU 158 OD2 ASP A 209 16920 19625 12866 664 -781 101 O ATOM 159 N VAL A 210 16.896 -6.115 -0.867 1.00 96.15 N ANISOU 159 N VAL A 210 12057 15315 9159 -207 -788 482 N ATOM 160 CA VAL A 210 17.946 -7.070 -0.492 1.00 94.07 C ANISOU 160 CA VAL A 210 11645 15138 8961 -352 -787 577 C ATOM 161 C VAL A 210 19.356 -6.492 -0.819 1.00 95.55 C ANISOU 161 C VAL A 210 11918 15229 9159 -538 -873 576 C ATOM 162 O VAL A 210 19.946 -6.817 -1.850 1.00 94.93 O ANISOU 162 O VAL A 210 11771 15109 9188 -634 -866 630 O ATOM 163 CB VAL A 210 17.709 -8.462 -1.154 1.00 96.21 C ANISOU 163 CB VAL A 210 11709 15479 9369 -361 -702 683 C ATOM 164 CG1 VAL A 210 18.612 -9.526 -0.534 1.00 95.70 C ANISOU 164 CG1 VAL A 210 11506 15518 9339 -446 -691 784 C ATOM 165 CG2 VAL A 210 16.246 -8.886 -1.030 1.00 95.77 C ANISOU 165 CG2 VAL A 210 11581 15520 9289 -217 -627 684 C ATOM 166 N GLU A 211 19.896 -5.666 0.097 1.00 91.46 N ANISOU 166 N GLU A 211 11541 14696 8512 -597 -955 518 N ATOM 167 CA GLU A 211 21.230 -5.051 -0.008 1.00 91.26 C ANISOU 167 CA GLU A 211 11599 14620 8457 -807 -1050 520 C ATOM 168 C GLU A 211 22.362 -6.098 -0.035 1.00 91.83 C ANISOU 168 C GLU A 211 11441 14840 8611 -933 -1037 645 C ATOM 169 O GLU A 211 22.357 -7.039 0.759 1.00 90.59 O ANISOU 169 O GLU A 211 11132 14830 8458 -878 -995 707 O ATOM 170 CB GLU A 211 21.488 -4.094 1.171 1.00 94.47 C ANISOU 170 CB GLU A 211 12201 15006 8687 -849 -1139 436 C ATOM 171 CG GLU A 211 20.659 -2.821 1.210 1.00107.82 C ANISOU 171 CG GLU A 211 14190 16517 10260 -737 -1178 301 C ATOM 172 CD GLU A 211 20.948 -1.975 2.441 1.00133.84 C ANISOU 172 CD GLU A 211 17696 19789 13367 -779 -1266 215 C ATOM 173 OE1 GLU A 211 21.489 -0.857 2.274 1.00136.23 O ANISOU 173 OE1 GLU A 211 18259 19924 13577 -920 -1367 149 O ATOM 174 OE2 GLU A 211 20.678 -2.444 3.573 1.00119.42 O ANISOU 174 OE2 GLU A 211 15785 18112 11478 -690 -1238 217 O ATOM 175 N GLY A 212 23.335 -5.895 -0.916 1.00 86.83 N ANISOU 175 N GLY A 212 10791 14176 8023 -1093 -1075 683 N ATOM 176 CA GLY A 212 24.486 -6.780 -1.047 1.00 85.54 C ANISOU 176 CA GLY A 212 10414 14170 7917 -1193 -1066 801 C ATOM 177 C GLY A 212 24.264 -8.027 -1.881 1.00 87.11 C ANISOU 177 C GLY A 212 10432 14403 8264 -1093 -962 885 C ATOM 178 O GLY A 212 25.166 -8.864 -1.964 1.00 84.98 O ANISOU 178 O GLY A 212 9992 14265 8034 -1127 -943 984 O ATOM 179 N CYS A 213 23.062 -8.163 -2.505 1.00 84.46 N ANISOU 179 N CYS A 213 10139 13956 7996 -964 -897 846 N ATOM 180 CA CYS A 213 22.673 -9.295 -3.361 1.00 83.39 C ANISOU 180 CA CYS A 213 9875 13822 7989 -881 -804 910 C ATOM 181 C CYS A 213 22.142 -8.807 -4.697 1.00 86.03 C ANISOU 181 C CYS A 213 10290 14013 8384 -877 -789 865 C ATOM 182 O CYS A 213 21.315 -7.891 -4.740 1.00 86.63 O ANISOU 182 O CYS A 213 10516 13987 8411 -829 -813 777 O ATOM 183 CB CYS A 213 21.634 -10.182 -2.682 1.00 84.01 C ANISOU 183 CB CYS A 213 9893 13953 8074 -743 -734 929 C ATOM 184 SG CYS A 213 22.079 -10.753 -1.025 1.00 89.22 S ANISOU 184 SG CYS A 213 10474 14779 8648 -730 -747 984 S ATOM 185 N GLY A 214 22.531 -9.504 -5.758 1.00 80.02 N ANISOU 185 N GLY A 214 9431 13250 7722 -897 -744 926 N ATOM 186 CA GLY A 214 22.071 -9.244 -7.117 1.00 77.72 C ANISOU 186 CA GLY A 214 9190 12842 7497 -893 -721 899 C ATOM 187 C GLY A 214 21.583 -10.504 -7.793 1.00 78.35 C ANISOU 187 C GLY A 214 9163 12929 7676 -814 -630 952 C ATOM 188 O GLY A 214 21.846 -11.596 -7.301 1.00 77.17 O ANISOU 188 O GLY A 214 8910 12864 7548 -779 -589 1021 O ATOM 189 N ILE A 215 20.889 -10.374 -8.941 1.00 74.12 N ANISOU 189 N ILE A 215 8669 12298 7193 -792 -603 923 N ATOM 190 CA ILE A 215 20.337 -11.528 -9.665 1.00 72.53 C ANISOU 190 CA ILE A 215 8395 12090 7074 -739 -524 964 C ATOM 191 C ILE A 215 21.468 -12.324 -10.352 1.00 75.55 C ANISOU 191 C ILE A 215 8696 12497 7514 -779 -494 1035 C ATOM 192 O ILE A 215 22.215 -11.752 -11.146 1.00 73.95 O ANISOU 192 O ILE A 215 8504 12274 7318 -850 -520 1032 O ATOM 193 CB ILE A 215 19.233 -11.116 -10.696 1.00 74.57 C ANISOU 193 CB ILE A 215 8716 12261 7355 -707 -509 912 C ATOM 194 CG1 ILE A 215 18.127 -10.247 -10.048 1.00 75.36 C ANISOU 194 CG1 ILE A 215 8896 12361 7377 -628 -537 841 C ATOM 195 CG2 ILE A 215 18.631 -12.355 -11.352 1.00 73.52 C ANISOU 195 CG2 ILE A 215 8517 12130 7288 -681 -436 953 C ATOM 196 CD1 ILE A 215 17.245 -9.447 -11.053 1.00 77.29 C ANISOU 196 CD1 ILE A 215 9225 12527 7616 -582 -547 785 C ATOM 197 N GLN A 216 21.539 -13.657 -10.083 1.00 73.39 N ANISOU 197 N GLN A 216 8350 12264 7270 -724 -436 1102 N ATOM 198 CA GLN A 216 22.508 -14.579 -10.695 1.00 74.21 C ANISOU 198 CA GLN A 216 8392 12391 7415 -708 -395 1171 C ATOM 199 C GLN A 216 22.460 -14.432 -12.228 1.00 82.20 C ANISOU 199 C GLN A 216 9432 13323 8478 -734 -373 1147 C ATOM 200 O GLN A 216 21.378 -14.238 -12.791 1.00 81.56 O ANISOU 200 O GLN A 216 9411 13158 8419 -737 -363 1098 O ATOM 201 CB GLN A 216 22.265 -16.045 -10.267 1.00 74.81 C ANISOU 201 CB GLN A 216 8451 12467 7506 -626 -334 1235 C ATOM 202 CG GLN A 216 20.955 -16.661 -10.762 1.00 78.04 C ANISOU 202 CG GLN A 216 8922 12781 7949 -618 -288 1217 C ATOM 203 CD GLN A 216 20.833 -18.140 -10.503 1.00 95.15 C ANISOU 203 CD GLN A 216 11112 14918 10122 -569 -234 1288 C ATOM 204 OE1 GLN A 216 20.856 -18.607 -9.363 1.00 98.42 O ANISOU 204 OE1 GLN A 216 11512 15385 10497 -540 -234 1335 O ATOM 205 NE2 GLN A 216 20.625 -18.910 -11.552 1.00 79.69 N ANISOU 205 NE2 GLN A 216 9213 12863 8202 -565 -188 1295 N ATOM 206 N CYS A 217 23.633 -14.479 -12.889 1.00 81.94 N ANISOU 206 N CYS A 217 9344 13340 8449 -753 -368 1183 N ATOM 207 CA CYS A 217 23.745 -14.287 -14.338 1.00 82.09 C ANISOU 207 CA CYS A 217 9383 13305 8503 -783 -348 1166 C ATOM 208 C CYS A 217 23.005 -15.381 -15.133 1.00 84.28 C ANISOU 208 C CYS A 217 9703 13487 8833 -716 -277 1166 C ATOM 209 O CYS A 217 22.449 -15.064 -16.185 1.00 85.29 O ANISOU 209 O CYS A 217 9881 13539 8988 -749 -271 1124 O ATOM 210 CB CYS A 217 25.200 -14.194 -14.781 1.00 83.88 C ANISOU 210 CB CYS A 217 9518 13651 8703 -811 -351 1218 C ATOM 211 SG CYS A 217 25.378 -13.780 -16.531 1.00 88.27 S ANISOU 211 SG CYS A 217 10093 14162 9283 -866 -333 1197 S ATOM 212 N GLN A 218 23.021 -16.648 -14.673 1.00 78.95 N ANISOU 212 N GLN A 218 9026 12810 8162 -631 -229 1215 N ATOM 213 CA GLN A 218 22.295 -17.723 -15.356 1.00 77.69 C ANISOU 213 CA GLN A 218 8944 12540 8034 -594 -171 1214 C ATOM 214 C GLN A 218 20.818 -17.522 -15.062 1.00 80.96 C ANISOU 214 C GLN A 218 9406 12902 8452 -648 -186 1172 C ATOM 215 O GLN A 218 20.362 -17.912 -13.987 1.00 80.66 O ANISOU 215 O GLN A 218 9369 12888 8391 -636 -187 1195 O ATOM 216 CB GLN A 218 22.797 -19.115 -14.926 1.00 79.43 C ANISOU 216 CB GLN A 218 9187 12753 8240 -489 -122 1284 C ATOM 217 CG GLN A 218 23.026 -20.052 -16.109 1.00 96.89 C ANISOU 217 CG GLN A 218 11475 14875 10463 -427 -61 1291 C ATOM 218 CD GLN A 218 22.442 -21.436 -15.940 1.00124.17 C ANISOU 218 CD GLN A 218 15065 18205 13909 -384 -18 1320 C ATOM 219 OE1 GLN A 218 21.607 -21.710 -15.059 1.00122.44 O ANISOU 219 OE1 GLN A 218 14880 17960 13680 -433 -32 1334 O ATOM 220 NE2 GLN A 218 22.828 -22.333 -16.838 1.00116.47 N ANISOU 220 NE2 GLN A 218 14186 17143 12924 -303 34 1329 N ATOM 221 N ASN A 219 20.097 -16.825 -15.986 1.00 77.21 N ANISOU 221 N ASN A 219 8959 12385 7994 -703 -200 1114 N ATOM 222 CA ASN A 219 18.682 -16.422 -15.890 1.00 76.41 C ANISOU 222 CA ASN A 219 8877 12274 7879 -739 -218 1072 C ATOM 223 C ASN A 219 17.877 -17.356 -14.967 1.00 80.43 C ANISOU 223 C ASN A 219 9391 12803 8364 -738 -195 1106 C ATOM 224 O ASN A 219 17.730 -18.544 -15.263 1.00 81.54 O ANISOU 224 O ASN A 219 9584 12887 8513 -751 -153 1142 O ATOM 225 CB ASN A 219 18.009 -16.337 -17.264 1.00 74.70 C ANISOU 225 CB ASN A 219 8700 12000 7683 -778 -206 1035 C ATOM 226 CG ASN A 219 16.714 -15.530 -17.304 1.00 90.10 C ANISOU 226 CG ASN A 219 10646 13982 9605 -793 -237 989 C ATOM 227 OD1 ASN A 219 15.991 -15.348 -16.312 1.00 86.25 O ANISOU 227 OD1 ASN A 219 10131 13563 9077 -773 -252 987 O ATOM 228 ND2 ASN A 219 16.376 -15.041 -18.475 1.00 77.17 N ANISOU 228 ND2 ASN A 219 9033 12312 7977 -814 -246 956 N ATOM 229 N PRO A 220 17.396 -16.812 -13.825 1.00 75.49 N ANISOU 229 N PRO A 220 8728 12258 7696 -725 -225 1098 N ATOM 230 CA PRO A 220 16.655 -17.631 -12.852 1.00 75.01 C ANISOU 230 CA PRO A 220 8658 12245 7597 -735 -205 1140 C ATOM 231 C PRO A 220 15.259 -18.085 -13.299 1.00 78.65 C ANISOU 231 C PRO A 220 9127 12722 8036 -801 -185 1138 C ATOM 232 O PRO A 220 14.694 -18.976 -12.661 1.00 78.98 O ANISOU 232 O PRO A 220 9173 12797 8041 -845 -164 1189 O ATOM 233 CB PRO A 220 16.504 -16.690 -11.656 1.00 76.67 C ANISOU 233 CB PRO A 220 8822 12554 7755 -696 -245 1117 C ATOM 234 CG PRO A 220 17.466 -15.604 -11.863 1.00 80.96 C ANISOU 234 CG PRO A 220 9373 13077 8312 -675 -287 1076 C ATOM 235 CD PRO A 220 17.550 -15.432 -13.332 1.00 76.90 C ANISOU 235 CD PRO A 220 8889 12484 7846 -703 -279 1051 C ATOM 236 N LEU A 221 14.692 -17.478 -14.355 1.00 74.70 N ANISOU 236 N LEU A 221 8625 12215 7545 -820 -196 1088 N ATOM 237 CA LEU A 221 13.359 -17.836 -14.851 1.00 74.64 C ANISOU 237 CA LEU A 221 8601 12259 7501 -893 -185 1090 C ATOM 238 C LEU A 221 13.395 -19.127 -15.683 1.00 80.06 C ANISOU 238 C LEU A 221 9371 12841 8209 -986 -150 1124 C ATOM 239 O LEU A 221 12.339 -19.685 -15.974 1.00 80.09 O ANISOU 239 O LEU A 221 9373 12889 8168 -1088 -143 1141 O ATOM 240 CB LEU A 221 12.737 -16.692 -15.684 1.00 73.99 C ANISOU 240 CB LEU A 221 8488 12218 7406 -862 -214 1029 C ATOM 241 CG LEU A 221 12.637 -15.295 -15.037 1.00 77.64 C ANISOU 241 CG LEU A 221 8919 12749 7831 -753 -254 982 C ATOM 242 CD1 LEU A 221 11.935 -14.325 -15.961 1.00 77.02 C ANISOU 242 CD1 LEU A 221 8839 12695 7729 -710 -279 933 C ATOM 243 CD2 LEU A 221 11.924 -15.342 -13.697 1.00 79.90 C ANISOU 243 CD2 LEU A 221 9140 13178 8041 -719 -251 1001 C ATOM 244 N PHE A 222 14.597 -19.610 -16.049 1.00 77.59 N ANISOU 244 N PHE A 222 9134 12401 7947 -951 -131 1135 N ATOM 245 CA PHE A 222 14.753 -20.824 -16.847 1.00 78.34 C ANISOU 245 CA PHE A 222 9346 12369 8049 -1006 -96 1157 C ATOM 246 C PHE A 222 15.724 -21.793 -16.210 1.00 83.06 C ANISOU 246 C PHE A 222 10024 12882 8652 -947 -68 1213 C ATOM 247 O PHE A 222 16.698 -21.382 -15.586 1.00 82.38 O ANISOU 247 O PHE A 222 9887 12828 8585 -846 -74 1224 O ATOM 248 CB PHE A 222 15.235 -20.490 -18.259 1.00 79.98 C ANISOU 248 CB PHE A 222 9586 12504 8297 -988 -91 1109 C ATOM 249 CG PHE A 222 14.358 -19.572 -19.069 1.00 81.69 C ANISOU 249 CG PHE A 222 9745 12788 8506 -1031 -119 1059 C ATOM 250 CD1 PHE A 222 13.457 -20.085 -19.994 1.00 86.44 C ANISOU 250 CD1 PHE A 222 10391 13374 9078 -1138 -115 1049 C ATOM 251 CD2 PHE A 222 14.479 -18.191 -18.959 1.00 83.84 C ANISOU 251 CD2 PHE A 222 9937 13129 8790 -965 -154 1022 C ATOM 252 CE1 PHE A 222 12.671 -19.229 -20.780 1.00 87.52 C ANISOU 252 CE1 PHE A 222 10464 13590 9199 -1161 -143 1009 C ATOM 253 CE2 PHE A 222 13.686 -17.335 -19.737 1.00 87.02 C ANISOU 253 CE2 PHE A 222 10306 13583 9176 -979 -182 981 C ATOM 254 CZ PHE A 222 12.801 -17.861 -20.654 1.00 85.88 C ANISOU 254 CZ PHE A 222 10181 13446 9006 -1067 -174 977 C ATOM 255 N THR A 223 15.476 -23.087 -16.409 1.00 81.86 N ANISOU 255 N THR A 223 10012 12621 8471 -1011 -42 1251 N ATOM 256 CA THR A 223 16.301 -24.182 -15.886 1.00 82.80 C ANISOU 256 CA THR A 223 10253 12631 8576 -940 -13 1312 C ATOM 257 C THR A 223 17.556 -24.351 -16.760 1.00 87.25 C ANISOU 257 C THR A 223 10877 13101 9172 -807 17 1294 C ATOM 258 O THR A 223 17.582 -23.843 -17.880 1.00 87.41 O ANISOU 258 O THR A 223 10877 13116 9218 -817 18 1237 O ATOM 259 CB THR A 223 15.463 -25.478 -15.829 1.00 91.94 C ANISOU 259 CB THR A 223 11578 13683 9671 -1076 -2 1359 C ATOM 260 OG1 THR A 223 15.068 -25.858 -17.152 1.00 96.91 O ANISOU 260 OG1 THR A 223 12320 14211 10292 -1163 6 1317 O ATOM 261 CG2 THR A 223 14.226 -25.337 -14.959 1.00 86.46 C ANISOU 261 CG2 THR A 223 10797 13127 8926 -1218 -27 1390 C ATOM 262 N GLU A 224 18.589 -25.056 -16.251 1.00 84.77 N ANISOU 262 N GLU A 224 10631 12734 8845 -671 43 1347 N ATOM 263 CA GLU A 224 19.838 -25.336 -16.973 1.00 85.18 C ANISOU 263 CA GLU A 224 10729 12733 8903 -511 79 1344 C ATOM 264 C GLU A 224 19.547 -26.156 -18.233 1.00 88.93 C ANISOU 264 C GLU A 224 11395 13039 9354 -542 111 1309 C ATOM 265 O GLU A 224 20.117 -25.865 -19.281 1.00 89.71 O ANISOU 265 O GLU A 224 11478 13140 9468 -477 131 1266 O ATOM 266 CB GLU A 224 20.850 -26.061 -16.063 1.00 88.00 C ANISOU 266 CB GLU A 224 11127 13083 9226 -345 100 1421 C ATOM 267 CG GLU A 224 22.001 -26.781 -16.770 1.00106.78 C ANISOU 267 CG GLU A 224 13608 15390 11576 -149 151 1435 C ATOM 268 CD GLU A 224 23.117 -25.973 -17.419 1.00141.73 C ANISOU 268 CD GLU A 224 17870 19959 16020 -37 163 1411 C ATOM 269 OE1 GLU A 224 22.823 -24.985 -18.133 1.00133.62 O ANISOU 269 OE1 GLU A 224 16739 18995 15035 -143 143 1350 O ATOM 270 OE2 GLU A 224 24.290 -26.394 -17.283 1.00143.46 O ANISOU 270 OE2 GLU A 224 18079 20232 16198 163 195 1460 O ATOM 271 N ALA A 225 18.633 -27.150 -18.136 1.00 84.12 N ANISOU 271 N ALA A 225 10970 12293 8698 -663 110 1330 N ATOM 272 CA ALA A 225 18.217 -28.013 -19.241 1.00 82.90 C ANISOU 272 CA ALA A 225 11036 11960 8501 -733 129 1296 C ATOM 273 C ALA A 225 17.577 -27.194 -20.345 1.00 85.70 C ANISOU 273 C ALA A 225 11297 12379 8885 -852 110 1220 C ATOM 274 O ALA A 225 17.794 -27.490 -21.523 1.00 86.43 O ANISOU 274 O ALA A 225 11502 12375 8960 -828 134 1173 O ATOM 275 CB ALA A 225 17.253 -29.071 -18.745 1.00 84.34 C ANISOU 275 CB ALA A 225 11413 12016 8617 -897 114 1343 C ATOM 276 N GLU A 226 16.812 -26.144 -19.969 1.00 80.41 N ANISOU 276 N GLU A 226 10426 11876 8248 -960 69 1209 N ATOM 277 CA GLU A 226 16.174 -25.234 -20.917 1.00 79.03 C ANISOU 277 CA GLU A 226 10147 11785 8095 -1051 46 1146 C ATOM 278 C GLU A 226 17.232 -24.410 -21.640 1.00 81.38 C ANISOU 278 C GLU A 226 10354 12126 8442 -912 61 1107 C ATOM 279 O GLU A 226 17.195 -24.354 -22.868 1.00 80.28 O ANISOU 279 O GLU A 226 10260 11944 8297 -934 71 1058 O ATOM 280 CB GLU A 226 15.152 -24.334 -20.230 1.00 79.64 C ANISOU 280 CB GLU A 226 10047 12035 8178 -1153 2 1150 C ATOM 281 CG GLU A 226 13.800 -24.996 -20.056 1.00 90.29 C ANISOU 281 CG GLU A 226 11454 13394 9460 -1350 -18 1176 C ATOM 282 CD GLU A 226 12.769 -24.170 -19.310 1.00111.78 C ANISOU 282 CD GLU A 226 13986 16321 12163 -1421 -53 1188 C ATOM 283 OE1 GLU A 226 13.157 -23.397 -18.404 1.00 90.20 O ANISOU 283 OE1 GLU A 226 11128 13683 9462 -1311 -60 1195 O ATOM 284 OE2 GLU A 226 11.562 -24.327 -19.609 1.00111.50 O ANISOU 284 OE2 GLU A 226 13932 16365 12067 -1587 -75 1192 O ATOM 285 N HIS A 227 18.207 -23.832 -20.880 1.00 77.64 N ANISOU 285 N HIS A 227 9758 11742 8001 -782 62 1133 N ATOM 286 CA HIS A 227 19.358 -23.063 -21.389 1.00 76.52 C ANISOU 286 CA HIS A 227 9515 11671 7888 -667 73 1116 C ATOM 287 C HIS A 227 20.081 -23.836 -22.478 1.00 82.37 C ANISOU 287 C HIS A 227 10383 12314 8601 -573 126 1101 C ATOM 288 O HIS A 227 20.225 -23.325 -23.583 1.00 82.13 O ANISOU 288 O HIS A 227 10323 12305 8577 -584 132 1058 O ATOM 289 CB HIS A 227 20.367 -22.739 -20.257 1.00 76.62 C ANISOU 289 CB HIS A 227 9416 11787 7911 -556 68 1166 C ATOM 290 CG HIS A 227 20.144 -21.459 -19.514 1.00 78.58 C ANISOU 290 CG HIS A 227 9506 12166 8185 -611 14 1158 C ATOM 291 ND1 HIS A 227 19.261 -21.386 -18.452 1.00 80.04 N ANISOU 291 ND1 HIS A 227 9670 12380 8363 -677 -15 1172 N ATOM 292 CD2 HIS A 227 20.775 -20.268 -19.640 1.00 79.32 C ANISOU 292 CD2 HIS A 227 9478 12364 8296 -603 -14 1142 C ATOM 293 CE1 HIS A 227 19.349 -20.148 -17.992 1.00 78.54 C ANISOU 293 CE1 HIS A 227 9359 12298 8186 -688 -59 1154 C ATOM 294 NE2 HIS A 227 20.247 -19.438 -18.674 1.00 78.63 N ANISOU 294 NE2 HIS A 227 9318 12346 8212 -657 -63 1136 N ATOM 295 N GLN A 228 20.508 -25.083 -22.173 1.00 81.28 N ANISOU 295 N GLN A 228 10401 12061 8418 -471 165 1139 N ATOM 296 CA GLN A 228 21.250 -25.946 -23.095 1.00 83.14 C ANISOU 296 CA GLN A 228 10791 12193 8605 -333 222 1125 C ATOM 297 C GLN A 228 20.404 -26.323 -24.330 1.00 88.23 C ANISOU 297 C GLN A 228 11593 12707 9223 -455 226 1061 C ATOM 298 O GLN A 228 20.961 -26.452 -25.428 1.00 90.05 O ANISOU 298 O GLN A 228 11878 12912 9424 -368 264 1023 O ATOM 299 CB GLN A 228 21.763 -27.207 -22.388 1.00 86.13 C ANISOU 299 CB GLN A 228 11341 12456 8930 -185 256 1182 C ATOM 300 CG GLN A 228 22.916 -26.921 -21.427 1.00110.15 C ANISOU 300 CG GLN A 228 14223 15652 11976 -12 264 1248 C ATOM 301 CD GLN A 228 23.472 -28.167 -20.772 1.00144.81 C ANISOU 301 CD GLN A 228 18786 19935 16301 169 299 1312 C ATOM 302 OE1 GLN A 228 24.574 -28.628 -21.099 1.00145.47 O ANISOU 302 OE1 GLN A 228 18903 20038 16329 402 350 1332 O ATOM 303 NE2 GLN A 228 22.746 -28.722 -19.806 1.00137.99 N ANISOU 303 NE2 GLN A 228 18030 18972 15429 79 273 1353 N ATOM 304 N ASP A 229 19.079 -26.442 -24.166 1.00 82.97 N ANISOU 304 N ASP A 229 10980 11990 8555 -659 184 1050 N ATOM 305 CA ASP A 229 18.170 -26.745 -25.267 1.00 82.88 C ANISOU 305 CA ASP A 229 11097 11888 8507 -811 174 995 C ATOM 306 C ASP A 229 18.027 -25.531 -26.217 1.00 84.93 C ANISOU 306 C ASP A 229 11186 12278 8805 -857 156 945 C ATOM 307 O ASP A 229 17.983 -25.705 -27.434 1.00 84.49 O ANISOU 307 O ASP A 229 11221 12166 8716 -876 172 894 O ATOM 308 CB ASP A 229 16.800 -27.168 -24.720 1.00 85.05 C ANISOU 308 CB ASP A 229 11436 12127 8752 -1031 130 1015 C ATOM 309 CG ASP A 229 15.788 -27.546 -25.783 1.00 99.72 C ANISOU 309 CG ASP A 229 13422 13914 10553 -1223 109 968 C ATOM 310 OD1 ASP A 229 14.623 -27.124 -25.664 1.00101.49 O ANISOU 310 OD1 ASP A 229 13541 14249 10772 -1410 61 971 O ATOM 311 OD2 ASP A 229 16.164 -28.265 -26.738 1.00108.55 O ANISOU 311 OD2 ASP A 229 14744 14881 11619 -1179 140 927 O ATOM 312 N MET A 230 17.954 -24.311 -25.647 1.00 79.76 N ANISOU 312 N MET A 230 10307 11788 8211 -872 120 959 N ATOM 313 CA MET A 230 17.820 -23.058 -26.376 1.00 78.09 C ANISOU 313 CA MET A 230 9948 11691 8031 -909 94 924 C ATOM 314 C MET A 230 19.127 -22.719 -27.110 1.00 80.82 C ANISOU 314 C MET A 230 10255 12071 8382 -770 133 914 C ATOM 315 O MET A 230 19.081 -22.188 -28.229 1.00 79.45 O ANISOU 315 O MET A 230 10060 11925 8203 -803 132 877 O ATOM 316 CB MET A 230 17.407 -21.914 -25.431 1.00 79.73 C ANISOU 316 CB MET A 230 9976 12035 8283 -946 44 943 C ATOM 317 CG MET A 230 17.042 -20.615 -26.147 1.00 83.82 C ANISOU 317 CG MET A 230 10383 12645 8820 -993 6 909 C ATOM 318 SD MET A 230 15.793 -20.776 -27.478 1.00 89.44 S ANISOU 318 SD MET A 230 11162 13335 9488 -1133 -11 863 S ATOM 319 CE MET A 230 14.385 -20.520 -26.603 1.00 86.21 C ANISOU 319 CE MET A 230 10674 13022 9061 -1235 -60 881 C ATOM 320 N HIS A 231 20.284 -23.048 -26.503 1.00 77.16 N ANISOU 320 N HIS A 231 9775 11627 7916 -617 169 955 N ATOM 321 CA HIS A 231 21.580 -22.762 -27.121 1.00 76.90 C ANISOU 321 CA HIS A 231 9674 11677 7868 -483 209 961 C ATOM 322 C HIS A 231 21.782 -23.617 -28.376 1.00 80.95 C ANISOU 322 C HIS A 231 10350 12089 8319 -419 264 920 C ATOM 323 O HIS A 231 22.221 -23.084 -29.396 1.00 79.49 O ANISOU 323 O HIS A 231 10107 11978 8119 -404 281 898 O ATOM 324 CB HIS A 231 22.724 -22.953 -26.127 1.00 78.00 C ANISOU 324 CB HIS A 231 9738 11899 8001 -329 231 1024 C ATOM 325 CG HIS A 231 22.655 -22.013 -24.956 1.00 80.53 C ANISOU 325 CG HIS A 231 9899 12330 8369 -393 175 1058 C ATOM 326 ND1 HIS A 231 23.214 -22.342 -23.728 1.00 82.52 N ANISOU 326 ND1 HIS A 231 10111 12628 8616 -304 177 1115 N ATOM 327 CD2 HIS A 231 22.055 -20.801 -24.850 1.00 80.97 C ANISOU 327 CD2 HIS A 231 9853 12447 8466 -527 116 1038 C ATOM 328 CE1 HIS A 231 22.974 -21.307 -22.940 1.00 80.87 C ANISOU 328 CE1 HIS A 231 9773 12509 8443 -396 119 1123 C ATOM 329 NE2 HIS A 231 22.266 -20.364 -23.565 1.00 80.23 N ANISOU 329 NE2 HIS A 231 9662 12431 8389 -524 82 1076 N ATOM 330 N SER A 232 21.387 -24.906 -28.322 1.00 78.42 N ANISOU 330 N SER A 232 10251 11594 7952 -400 287 909 N ATOM 331 CA SER A 232 21.446 -25.827 -29.461 1.00 79.15 C ANISOU 331 CA SER A 232 10556 11550 7968 -348 334 859 C ATOM 332 C SER A 232 20.500 -25.381 -30.590 1.00 80.94 C ANISOU 332 C SER A 232 10798 11764 8192 -527 303 797 C ATOM 333 O SER A 232 20.880 -25.441 -31.759 1.00 81.51 O ANISOU 333 O SER A 232 10922 11833 8216 -474 339 755 O ATOM 334 CB SER A 232 21.102 -27.245 -29.020 1.00 84.38 C ANISOU 334 CB SER A 232 11487 11999 8573 -327 348 863 C ATOM 335 OG SER A 232 22.152 -27.772 -28.228 1.00 95.40 O ANISOU 335 OG SER A 232 12898 13400 9947 -105 389 918 O ATOM 336 N TYR A 233 19.294 -24.907 -30.227 1.00 74.67 N ANISOU 336 N TYR A 233 9944 10988 7438 -725 237 797 N ATOM 337 CA TYR A 233 18.258 -24.408 -31.133 1.00 73.19 C ANISOU 337 CA TYR A 233 9740 10824 7244 -899 195 753 C ATOM 338 C TYR A 233 18.783 -23.202 -31.909 1.00 74.47 C ANISOU 338 C TYR A 233 9736 11127 7434 -863 195 743 C ATOM 339 O TYR A 233 18.807 -23.241 -33.138 1.00 74.51 O ANISOU 339 O TYR A 233 9801 11116 7392 -875 213 700 O ATOM 340 CB TYR A 233 16.999 -24.041 -30.315 1.00 74.26 C ANISOU 340 CB TYR A 233 9794 11011 7411 -1069 129 776 C ATOM 341 CG TYR A 233 15.760 -23.726 -31.127 1.00 76.72 C ANISOU 341 CG TYR A 233 10095 11362 7693 -1250 82 742 C ATOM 342 CD1 TYR A 233 14.935 -24.745 -31.599 1.00 79.86 C ANISOU 342 CD1 TYR A 233 10677 11654 8012 -1395 71 716 C ATOM 343 CD2 TYR A 233 15.366 -22.408 -31.354 1.00 76.34 C ANISOU 343 CD2 TYR A 233 9861 11463 7681 -1283 40 742 C ATOM 344 CE1 TYR A 233 13.774 -24.464 -32.317 1.00 79.80 C ANISOU 344 CE1 TYR A 233 10637 11720 7962 -1572 21 694 C ATOM 345 CE2 TYR A 233 14.203 -22.113 -32.069 1.00 77.24 C ANISOU 345 CE2 TYR A 233 9951 11639 7756 -1428 -6 720 C ATOM 346 CZ TYR A 233 13.407 -23.146 -32.546 1.00 83.46 C ANISOU 346 CZ TYR A 233 10892 12355 8466 -1575 -15 698 C ATOM 347 OH TYR A 233 12.254 -22.883 -33.249 1.00 78.69 O ANISOU 347 OH TYR A 233 10245 11845 7807 -1728 -65 684 O ATOM 348 N ILE A 234 19.277 -22.172 -31.181 1.00 69.76 N ANISOU 348 N ILE A 234 8948 10660 6899 -820 176 786 N ATOM 349 CA ILE A 234 19.839 -20.919 -31.703 1.00 68.61 C ANISOU 349 CA ILE A 234 8649 10646 6775 -808 165 793 C ATOM 350 C ILE A 234 21.082 -21.214 -32.540 1.00 75.17 C ANISOU 350 C ILE A 234 9498 11508 7556 -676 233 791 C ATOM 351 O ILE A 234 21.214 -20.601 -33.589 1.00 75.40 O ANISOU 351 O ILE A 234 9488 11597 7565 -708 234 774 O ATOM 352 CB ILE A 234 20.129 -19.893 -30.565 1.00 70.33 C ANISOU 352 CB ILE A 234 8704 10969 7051 -806 124 840 C ATOM 353 CG1 ILE A 234 18.800 -19.351 -30.002 1.00 69.82 C ANISOU 353 CG1 ILE A 234 8607 10904 7017 -925 58 833 C ATOM 354 CG2 ILE A 234 21.040 -18.731 -31.032 1.00 70.00 C ANISOU 354 CG2 ILE A 234 8535 11050 7012 -793 118 861 C ATOM 355 CD1 ILE A 234 18.883 -18.594 -28.722 1.00 79.46 C ANISOU 355 CD1 ILE A 234 9720 12192 8279 -915 19 867 C ATOM 356 N ALA A 235 21.959 -22.157 -32.116 1.00 74.35 N ANISOU 356 N ALA A 235 9453 11376 7420 -517 290 810 N ATOM 357 CA ALA A 235 23.172 -22.538 -32.864 1.00 75.64 C ANISOU 357 CA ALA A 235 9627 11599 7514 -349 365 812 C ATOM 358 C ALA A 235 22.802 -23.136 -34.217 1.00 81.75 C ANISOU 358 C ALA A 235 10572 12272 8219 -359 396 744 C ATOM 359 O ALA A 235 23.396 -22.755 -35.226 1.00 82.49 O ANISOU 359 O ALA A 235 10611 12466 8268 -317 429 735 O ATOM 360 CB ALA A 235 24.016 -23.528 -32.071 1.00 77.24 C ANISOU 360 CB ALA A 235 9884 11780 7682 -151 417 848 C ATOM 361 N ALA A 236 21.797 -24.040 -34.236 1.00 78.61 N ANISOU 361 N ALA A 236 10380 11686 7802 -435 381 700 N ATOM 362 CA ALA A 236 21.298 -24.691 -35.442 1.00 79.61 C ANISOU 362 CA ALA A 236 10703 11693 7851 -479 398 629 C ATOM 363 C ALA A 236 20.706 -23.658 -36.413 1.00 84.98 C ANISOU 363 C ALA A 236 11279 12466 8545 -633 356 606 C ATOM 364 O ALA A 236 21.178 -23.537 -37.546 1.00 85.17 O ANISOU 364 O ALA A 236 11312 12538 8509 -583 393 578 O ATOM 365 CB ALA A 236 20.249 -25.735 -35.074 1.00 80.64 C ANISOU 365 CB ALA A 236 11059 11622 7957 -590 369 602 C ATOM 366 N PHE A 237 19.710 -22.884 -35.939 1.00 81.64 N ANISOU 366 N PHE A 237 10750 12081 8190 -802 279 624 N ATOM 367 CA PHE A 237 19.001 -21.861 -36.702 1.00 80.87 C ANISOU 367 CA PHE A 237 10558 12066 8104 -938 228 613 C ATOM 368 C PHE A 237 19.911 -20.716 -37.113 1.00 83.05 C ANISOU 368 C PHE A 237 10668 12491 8397 -882 238 646 C ATOM 369 O PHE A 237 19.782 -20.223 -38.232 1.00 82.85 O ANISOU 369 O PHE A 237 10632 12512 8335 -933 232 627 O ATOM 370 CB PHE A 237 17.820 -21.314 -35.894 1.00 82.12 C ANISOU 370 CB PHE A 237 10634 12249 8319 -1078 150 634 C ATOM 371 CG PHE A 237 16.513 -21.999 -36.188 1.00 84.84 C ANISOU 371 CG PHE A 237 11100 12520 8615 -1232 114 598 C ATOM 372 CD1 PHE A 237 15.710 -21.578 -37.244 1.00 88.51 C ANISOU 372 CD1 PHE A 237 11555 13036 9037 -1347 75 571 C ATOM 373 CD2 PHE A 237 16.079 -23.063 -35.410 1.00 88.05 C ANISOU 373 CD2 PHE A 237 11631 12819 9006 -1277 113 600 C ATOM 374 CE1 PHE A 237 14.495 -22.210 -37.513 1.00 90.02 C ANISOU 374 CE1 PHE A 237 11842 13195 9168 -1513 34 546 C ATOM 375 CE2 PHE A 237 14.864 -23.699 -35.684 1.00 91.60 C ANISOU 375 CE2 PHE A 237 12191 13221 9392 -1459 72 576 C ATOM 376 CZ PHE A 237 14.081 -23.268 -36.731 1.00 89.71 C ANISOU 376 CZ PHE A 237 11922 13057 9107 -1580 32 549 C ATOM 377 N GLY A 238 20.814 -20.317 -36.217 1.00 78.30 N ANISOU 377 N GLY A 238 9944 11969 7839 -795 250 699 N ATOM 378 CA GLY A 238 21.773 -19.244 -36.452 1.00 78.08 C ANISOU 378 CA GLY A 238 9758 12094 7815 -771 254 744 C ATOM 379 C GLY A 238 22.789 -19.578 -37.523 1.00 83.76 C ANISOU 379 C GLY A 238 10490 12885 8450 -666 329 737 C ATOM 380 O GLY A 238 23.123 -18.716 -38.337 1.00 83.83 O ANISOU 380 O GLY A 238 10417 13002 8433 -715 325 756 O ATOM 381 N ALA A 239 23.266 -20.844 -37.545 1.00 81.61 N ANISOU 381 N ALA A 239 10337 12550 8122 -513 400 712 N ATOM 382 CA ALA A 239 24.239 -21.334 -38.528 1.00 82.64 C ANISOU 382 CA ALA A 239 10499 12752 8150 -364 485 698 C ATOM 383 C ALA A 239 23.601 -21.495 -39.913 1.00 85.86 C ANISOU 383 C ALA A 239 11036 13094 8495 -434 489 630 C ATOM 384 O ALA A 239 24.215 -21.096 -40.901 1.00 85.43 O ANISOU 384 O ALA A 239 10917 13167 8374 -405 526 636 O ATOM 385 CB ALA A 239 24.836 -22.659 -38.070 1.00 84.57 C ANISOU 385 CB ALA A 239 10869 12924 8341 -151 554 687 C ATOM 386 N VAL A 240 22.371 -22.075 -39.979 1.00 81.83 N ANISOU 386 N VAL A 240 10698 12401 7992 -541 449 572 N ATOM 387 CA VAL A 240 21.624 -22.321 -41.226 1.00 81.03 C ANISOU 387 CA VAL A 240 10735 12230 7822 -634 440 504 C ATOM 388 C VAL A 240 21.266 -20.961 -41.874 1.00 83.16 C ANISOU 388 C VAL A 240 10852 12628 8119 -776 386 531 C ATOM 389 O VAL A 240 21.442 -20.819 -43.080 1.00 82.60 O ANISOU 389 O VAL A 240 10803 12610 7972 -779 410 507 O ATOM 390 CB VAL A 240 20.369 -23.234 -41.015 1.00 83.96 C ANISOU 390 CB VAL A 240 11312 12405 8185 -753 397 449 C ATOM 391 CG1 VAL A 240 19.515 -23.330 -42.285 1.00 84.14 C ANISOU 391 CG1 VAL A 240 11448 12389 8132 -890 370 387 C ATOM 392 CG2 VAL A 240 20.777 -24.633 -40.557 1.00 84.46 C ANISOU 392 CG2 VAL A 240 11586 12309 8195 -609 453 421 C ATOM 393 N THR A 241 20.808 -19.968 -41.075 1.00 79.34 N ANISOU 393 N THR A 241 10228 12189 7731 -878 314 582 N ATOM 394 CA THR A 241 20.474 -18.627 -41.569 1.00 78.55 C ANISOU 394 CA THR A 241 10011 12185 7651 -992 256 615 C ATOM 395 C THR A 241 21.757 -18.011 -42.105 1.00 84.25 C ANISOU 395 C THR A 241 10623 13055 8332 -928 303 661 C ATOM 396 O THR A 241 21.751 -17.489 -43.222 1.00 85.89 O ANISOU 396 O THR A 241 10822 13327 8486 -981 301 662 O ATOM 397 CB THR A 241 19.783 -17.765 -40.484 1.00 82.41 C ANISOU 397 CB THR A 241 10405 12674 8234 -1075 176 656 C ATOM 398 OG1 THR A 241 18.573 -18.413 -40.092 1.00 81.38 O ANISOU 398 OG1 THR A 241 10360 12444 8116 -1141 139 619 O ATOM 399 CG2 THR A 241 19.455 -16.335 -40.957 1.00 77.29 C ANISOU 399 CG2 THR A 241 9673 12101 7595 -1166 112 693 C ATOM 400 N GLY A 242 22.849 -18.163 -41.355 1.00 79.68 N ANISOU 400 N GLY A 242 9963 12547 7765 -817 348 702 N ATOM 401 CA GLY A 242 24.164 -17.669 -41.739 1.00 79.77 C ANISOU 401 CA GLY A 242 9843 12744 7722 -761 396 759 C ATOM 402 C GLY A 242 24.658 -18.202 -43.070 1.00 83.93 C ANISOU 402 C GLY A 242 10425 13334 8130 -677 473 726 C ATOM 403 O GLY A 242 25.132 -17.424 -43.894 1.00 84.38 O ANISOU 403 O GLY A 242 10393 13533 8134 -731 480 765 O ATOM 404 N LEU A 243 24.509 -19.521 -43.306 1.00 80.96 N ANISOU 404 N LEU A 243 10217 12842 7701 -552 529 652 N ATOM 405 CA LEU A 243 24.948 -20.200 -44.531 1.00 82.46 C ANISOU 405 CA LEU A 243 10503 13066 7761 -439 609 602 C ATOM 406 C LEU A 243 24.028 -19.923 -45.739 1.00 88.14 C ANISOU 406 C LEU A 243 11314 13732 8442 -582 572 553 C ATOM 407 O LEU A 243 24.537 -19.677 -46.830 1.00 89.16 O ANISOU 407 O LEU A 243 11412 13989 8477 -560 615 556 O ATOM 408 CB LEU A 243 25.042 -21.716 -44.298 1.00 83.45 C ANISOU 408 CB LEU A 243 10830 13043 7833 -255 672 533 C ATOM 409 CG LEU A 243 26.214 -22.199 -43.434 1.00 88.79 C ANISOU 409 CG LEU A 243 11433 13811 8493 -35 739 579 C ATOM 410 CD1 LEU A 243 25.892 -23.523 -42.762 1.00 89.94 C ANISOU 410 CD1 LEU A 243 11807 13732 8636 85 756 526 C ATOM 411 CD2 LEU A 243 27.508 -22.290 -44.235 1.00 91.06 C ANISOU 411 CD2 LEU A 243 11630 14323 8645 155 839 601 C ATOM 412 N CYS A 244 22.694 -19.979 -45.555 1.00 84.83 N ANISOU 412 N CYS A 244 10997 13154 8082 -725 494 514 N ATOM 413 CA CYS A 244 21.704 -19.754 -46.617 1.00 84.73 C ANISOU 413 CA CYS A 244 11062 13104 8027 -866 447 472 C ATOM 414 C CYS A 244 21.733 -18.309 -47.119 1.00 87.06 C ANISOU 414 C CYS A 244 11200 13542 8338 -977 401 541 C ATOM 415 O CYS A 244 21.574 -18.095 -48.321 1.00 87.62 O ANISOU 415 O CYS A 244 11303 13662 8328 -1024 403 524 O ATOM 416 CB CYS A 244 20.305 -20.128 -46.141 1.00 84.53 C ANISOU 416 CB CYS A 244 11142 12923 8053 -995 370 432 C ATOM 417 SG CYS A 244 20.086 -21.892 -45.823 1.00 89.74 S ANISOU 417 SG CYS A 244 12061 13377 8658 -922 411 345 S ATOM 418 N THR A 245 21.885 -17.328 -46.214 1.00 81.17 N ANISOU 418 N THR A 245 10308 12846 7686 -1024 353 618 N ATOM 419 CA THR A 245 21.919 -15.924 -46.615 1.00 80.17 C ANISOU 419 CA THR A 245 10074 12820 7566 -1135 301 689 C ATOM 420 C THR A 245 23.247 -15.616 -47.307 1.00 85.78 C ANISOU 420 C THR A 245 10693 13709 8191 -1088 369 739 C ATOM 421 O THR A 245 23.249 -14.870 -48.299 1.00 86.49 O ANISOU 421 O THR A 245 10763 13877 8222 -1172 353 771 O ATOM 422 CB THR A 245 21.670 -14.975 -45.441 1.00 82.25 C ANISOU 422 CB THR A 245 10252 13063 7938 -1201 225 748 C ATOM 423 OG1 THR A 245 22.643 -15.206 -44.424 1.00 82.81 O ANISOU 423 OG1 THR A 245 10242 13177 8043 -1118 264 779 O ATOM 424 CG2 THR A 245 20.252 -15.073 -44.890 1.00 77.58 C ANISOU 424 CG2 THR A 245 9723 12343 7410 -1256 151 711 C ATOM 425 N LEU A 246 24.368 -16.206 -46.815 1.00 81.11 N ANISOU 425 N LEU A 246 10039 13200 7578 -950 447 752 N ATOM 426 CA LEU A 246 25.679 -15.990 -47.430 1.00 81.25 C ANISOU 426 CA LEU A 246 9939 13439 7494 -894 521 807 C ATOM 427 C LEU A 246 25.661 -16.492 -48.874 1.00 86.41 C ANISOU 427 C LEU A 246 10683 14128 8021 -846 580 752 C ATOM 428 O LEU A 246 26.168 -15.791 -49.751 1.00 86.44 O ANISOU 428 O LEU A 246 10605 14295 7945 -907 595 807 O ATOM 429 CB LEU A 246 26.824 -16.650 -46.629 1.00 81.23 C ANISOU 429 CB LEU A 246 9846 13544 7474 -722 597 830 C ATOM 430 CG LEU A 246 28.260 -16.529 -47.191 1.00 85.52 C ANISOU 430 CG LEU A 246 10230 14376 7889 -638 683 896 C ATOM 431 CD1 LEU A 246 28.653 -15.082 -47.457 1.00 84.71 C ANISOU 431 CD1 LEU A 246 9977 14436 7771 -844 631 1003 C ATOM 432 CD2 LEU A 246 29.257 -17.187 -46.271 1.00 87.00 C ANISOU 432 CD2 LEU A 246 10320 14676 8060 -453 747 923 C ATOM 433 N PHE A 247 25.046 -17.675 -49.116 1.00 83.64 N ANISOU 433 N PHE A 247 10516 13620 7644 -755 607 647 N ATOM 434 CA PHE A 247 24.933 -18.268 -50.449 1.00 85.22 C ANISOU 434 CA PHE A 247 10843 13822 7715 -707 658 576 C ATOM 435 C PHE A 247 24.167 -17.327 -51.391 1.00 89.03 C ANISOU 435 C PHE A 247 11324 14320 8183 -895 587 594 C ATOM 436 O PHE A 247 24.640 -17.093 -52.502 1.00 88.81 O ANISOU 436 O PHE A 247 11270 14432 8041 -891 631 608 O ATOM 437 CB PHE A 247 24.267 -19.653 -50.391 1.00 87.47 C ANISOU 437 CB PHE A 247 11364 13892 7978 -622 676 459 C ATOM 438 CG PHE A 247 23.948 -20.243 -51.745 1.00 90.16 C ANISOU 438 CG PHE A 247 11876 14199 8182 -609 708 372 C ATOM 439 CD1 PHE A 247 24.955 -20.775 -52.546 1.00 95.05 C ANISOU 439 CD1 PHE A 247 12523 14939 8652 -424 818 345 C ATOM 440 CD2 PHE A 247 22.642 -20.266 -52.222 1.00 91.91 C ANISOU 440 CD2 PHE A 247 12225 14288 8408 -777 628 318 C ATOM 441 CE1 PHE A 247 24.662 -21.308 -53.806 1.00 97.10 C ANISOU 441 CE1 PHE A 247 12957 15165 8773 -410 847 258 C ATOM 442 CE2 PHE A 247 22.349 -20.800 -53.483 1.00 96.10 C ANISOU 442 CE2 PHE A 247 12919 14795 8801 -782 651 237 C ATOM 443 CZ PHE A 247 23.360 -21.322 -54.264 1.00 95.90 C ANISOU 443 CZ PHE A 247 12941 14865 8630 -599 761 202 C ATOM 444 N THR A 248 23.019 -16.763 -50.930 1.00 84.91 N ANISOU 444 N THR A 248 10821 13674 7767 -1045 481 603 N ATOM 445 CA THR A 248 22.196 -15.818 -51.698 1.00 84.85 C ANISOU 445 CA THR A 248 10814 13676 7749 -1203 402 630 C ATOM 446 C THR A 248 22.993 -14.511 -51.944 1.00 90.65 C ANISOU 446 C THR A 248 11400 14574 8467 -1273 392 745 C ATOM 447 O THR A 248 22.898 -13.950 -53.041 1.00 91.32 O ANISOU 447 O THR A 248 11491 14734 8471 -1348 380 772 O ATOM 448 CB THR A 248 20.858 -15.571 -50.986 1.00 90.82 C ANISOU 448 CB THR A 248 11607 14290 8610 -1302 298 620 C ATOM 449 OG1 THR A 248 20.210 -16.829 -50.831 1.00 92.91 O ANISOU 449 OG1 THR A 248 12011 14424 8865 -1268 309 523 O ATOM 450 CG2 THR A 248 19.926 -14.631 -51.761 1.00 87.50 C ANISOU 450 CG2 THR A 248 11191 13888 8168 -1431 213 650 C ATOM 451 N LEU A 249 23.794 -14.052 -50.951 1.00 87.27 N ANISOU 451 N LEU A 249 10849 14206 8102 -1263 396 815 N ATOM 452 CA LEU A 249 24.631 -12.854 -51.107 1.00 87.19 C ANISOU 452 CA LEU A 249 10713 14352 8062 -1362 383 930 C ATOM 453 C LEU A 249 25.684 -13.085 -52.184 1.00 91.64 C ANISOU 453 C LEU A 249 11215 15128 8478 -1310 480 951 C ATOM 454 O LEU A 249 25.797 -12.259 -53.088 1.00 93.48 O ANISOU 454 O LEU A 249 11427 15455 8636 -1425 461 1014 O ATOM 455 CB LEU A 249 25.308 -12.423 -49.789 1.00 86.66 C ANISOU 455 CB LEU A 249 10534 14318 8075 -1375 365 996 C ATOM 456 CG LEU A 249 24.418 -11.889 -48.659 1.00 89.79 C ANISOU 456 CG LEU A 249 10970 14540 8605 -1440 265 997 C ATOM 457 CD1 LEU A 249 25.240 -11.610 -47.415 1.00 89.12 C ANISOU 457 CD1 LEU A 249 10778 14508 8574 -1443 261 1053 C ATOM 458 CD2 LEU A 249 23.631 -10.639 -49.079 1.00 91.76 C ANISOU 458 CD2 LEU A 249 11282 14722 8861 -1585 165 1044 C ATOM 459 N ALA A 250 26.412 -14.226 -52.115 1.00 86.70 N ANISOU 459 N ALA A 250 10572 14574 7796 -1126 584 900 N ATOM 460 CA ALA A 250 27.455 -14.628 -53.067 1.00 87.44 C ANISOU 460 CA ALA A 250 10602 14891 7729 -1019 694 908 C ATOM 461 C ALA A 250 26.878 -14.863 -54.470 1.00 92.37 C ANISOU 461 C ALA A 250 11355 15491 8252 -1030 708 846 C ATOM 462 O ALA A 250 27.533 -14.526 -55.456 1.00 93.85 O ANISOU 462 O ALA A 250 11470 15881 8309 -1048 758 894 O ATOM 463 CB ALA A 250 28.154 -15.884 -52.580 1.00 88.75 C ANISOU 463 CB ALA A 250 10767 15093 7861 -774 795 852 C ATOM 464 N THR A 251 25.655 -15.419 -54.559 1.00 87.29 N ANISOU 464 N THR A 251 10892 14620 7656 -1037 661 746 N ATOM 465 CA THR A 251 24.974 -15.680 -55.831 1.00 87.38 C ANISOU 465 CA THR A 251 11038 14595 7569 -1068 659 679 C ATOM 466 C THR A 251 24.624 -14.341 -56.514 1.00 91.88 C ANISOU 466 C THR A 251 11552 15231 8126 -1261 581 770 C ATOM 467 O THR A 251 24.728 -14.255 -57.741 1.00 93.62 O ANISOU 467 O THR A 251 11797 15558 8217 -1281 611 769 O ATOM 468 CB THR A 251 23.733 -16.562 -55.599 1.00 86.89 C ANISOU 468 CB THR A 251 11167 14289 7559 -1065 612 564 C ATOM 469 OG1 THR A 251 24.134 -17.761 -54.933 1.00 85.24 O ANISOU 469 OG1 THR A 251 11032 14001 7352 -889 681 492 O ATOM 470 CG2 THR A 251 23.037 -16.930 -56.871 1.00 81.22 C ANISOU 470 CG2 THR A 251 10595 13541 6726 -1106 605 488 C ATOM 471 N PHE A 252 24.237 -13.303 -55.731 1.00 86.24 N ANISOU 471 N PHE A 252 10782 14453 7534 -1392 484 849 N ATOM 472 CA PHE A 252 23.894 -11.981 -56.268 1.00 85.44 C ANISOU 472 CA PHE A 252 10663 14381 7420 -1560 402 943 C ATOM 473 C PHE A 252 25.131 -11.267 -56.784 1.00 93.57 C ANISOU 473 C PHE A 252 11568 15637 8348 -1619 450 1054 C ATOM 474 O PHE A 252 25.103 -10.740 -57.903 1.00 93.58 O ANISOU 474 O PHE A 252 11586 15725 8244 -1703 443 1098 O ATOM 475 CB PHE A 252 23.197 -11.101 -55.225 1.00 84.69 C ANISOU 475 CB PHE A 252 10572 14141 7465 -1651 290 991 C ATOM 476 CG PHE A 252 21.704 -10.941 -55.374 1.00 84.26 C ANISOU 476 CG PHE A 252 10625 13937 7452 -1694 195 952 C ATOM 477 CD1 PHE A 252 20.824 -11.806 -54.722 1.00 86.19 C ANISOU 477 CD1 PHE A 252 10928 14047 7771 -1633 177 858 C ATOM 478 CD2 PHE A 252 21.171 -9.879 -56.091 1.00 84.98 C ANISOU 478 CD2 PHE A 252 10753 14033 7501 -1797 118 1021 C ATOM 479 CE1 PHE A 252 19.434 -11.642 -54.837 1.00 85.33 C ANISOU 479 CE1 PHE A 252 10888 13849 7685 -1680 88 833 C ATOM 480 CE2 PHE A 252 19.781 -9.724 -56.218 1.00 86.72 C ANISOU 480 CE2 PHE A 252 11052 14154 7746 -1815 30 993 C ATOM 481 CZ PHE A 252 18.922 -10.599 -55.579 1.00 83.64 C ANISOU 481 CZ PHE A 252 10692 13666 7423 -1759 16 901 C ATOM 482 N VAL A 253 26.224 -11.271 -55.988 1.00 92.25 N ANISOU 482 N VAL A 253 11268 15586 8197 -1584 498 1104 N ATOM 483 CA VAL A 253 27.474 -10.596 -56.357 1.00 94.54 C ANISOU 483 CA VAL A 253 11408 16134 8380 -1665 542 1225 C ATOM 484 C VAL A 253 28.177 -11.363 -57.525 1.00100.35 C ANISOU 484 C VAL A 253 12102 17086 8939 -1542 666 1192 C ATOM 485 O VAL A 253 28.853 -10.718 -58.329 1.00101.23 O ANISOU 485 O VAL A 253 12126 17412 8926 -1644 691 1288 O ATOM 486 CB VAL A 253 28.432 -10.346 -55.152 1.00 99.19 C ANISOU 486 CB VAL A 253 11848 16821 9021 -1682 549 1297 C ATOM 487 CG1 VAL A 253 27.718 -9.609 -54.014 1.00 96.95 C ANISOU 487 CG1 VAL A 253 11626 16314 8894 -1790 429 1317 C ATOM 488 CG2 VAL A 253 29.077 -11.630 -54.640 1.00 99.96 C ANISOU 488 CG2 VAL A 253 11874 16999 9107 -1450 656 1226 C ATOM 489 N ALA A 254 27.960 -12.699 -57.657 1.00 96.90 N ANISOU 489 N ALA A 254 11753 16584 8482 -1333 739 1058 N ATOM 490 CA ALA A 254 28.525 -13.518 -58.742 1.00 98.72 C ANISOU 490 CA ALA A 254 11989 16984 8536 -1179 858 1004 C ATOM 491 C ALA A 254 27.991 -13.093 -60.117 1.00103.20 C ANISOU 491 C ALA A 254 12638 17572 9000 -1289 833 1007 C ATOM 492 O ALA A 254 28.677 -13.286 -61.122 1.00105.01 O ANISOU 492 O ALA A 254 12820 18020 9058 -1229 923 1016 O ATOM 493 CB ALA A 254 28.221 -14.988 -58.513 1.00 99.69 C ANISOU 493 CB ALA A 254 12257 16954 8664 -951 916 852 C ATOM 494 N ASP A 255 26.770 -12.530 -60.157 1.00 98.42 N ANISOU 494 N ASP A 255 12151 16758 8488 -1436 715 1001 N ATOM 495 CA ASP A 255 26.113 -12.027 -61.367 1.00 98.43 C ANISOU 495 CA ASP A 255 12234 16761 8405 -1551 669 1014 C ATOM 496 C ASP A 255 25.719 -10.556 -61.151 1.00101.59 C ANISOU 496 C ASP A 255 12613 17106 8879 -1764 548 1143 C ATOM 497 O ASP A 255 24.725 -10.088 -61.706 1.00 99.59 O ANISOU 497 O ASP A 255 12464 16750 8626 -1852 464 1146 O ATOM 498 CB ASP A 255 24.890 -12.908 -61.696 1.00 99.79 C ANISOU 498 CB ASP A 255 12595 16732 8589 -1493 638 871 C ATOM 499 CG ASP A 255 24.235 -12.653 -63.048 1.00116.71 C ANISOU 499 CG ASP A 255 14828 18903 10615 -1577 605 863 C ATOM 500 OD1 ASP A 255 24.973 -12.334 -64.029 1.00117.46 O ANISOU 500 OD1 ASP A 255 14861 19208 10559 -1596 665 921 O ATOM 501 OD2 ASP A 255 22.994 -12.791 -63.138 1.00125.28 O ANISOU 501 OD2 ASP A 255 16034 19823 11745 -1627 521 802 O ATOM 502 N TRP A 256 26.545 -9.814 -60.373 1.00100.30 N ANISOU 502 N TRP A 256 12324 17025 8759 -1845 538 1255 N ATOM 503 CA TRP A 256 26.287 -8.437 -59.937 1.00100.21 C ANISOU 503 CA TRP A 256 12326 16928 8821 -2037 422 1374 C ATOM 504 C TRP A 256 25.894 -7.500 -61.090 1.00105.21 C ANISOU 504 C TRP A 256 13036 17583 9356 -2183 363 1455 C ATOM 505 O TRP A 256 25.064 -6.620 -60.864 1.00104.33 O ANISOU 505 O TRP A 256 13028 17297 9315 -2277 248 1499 O ATOM 506 CB TRP A 256 27.464 -7.835 -59.151 1.00 99.45 C ANISOU 506 CB TRP A 256 12085 16971 8731 -2130 434 1487 C ATOM 507 CG TRP A 256 27.085 -6.585 -58.409 1.00100.03 C ANISOU 507 CG TRP A 256 12226 16881 8901 -2302 306 1577 C ATOM 508 CD1 TRP A 256 27.522 -5.320 -58.664 1.00103.91 C ANISOU 508 CD1 TRP A 256 12726 17430 9324 -2519 247 1722 C ATOM 509 CD2 TRP A 256 26.095 -6.465 -57.370 1.00 98.59 C ANISOU 509 CD2 TRP A 256 12145 16433 8881 -2267 216 1524 C ATOM 510 NE1 TRP A 256 26.897 -4.422 -57.831 1.00102.71 N ANISOU 510 NE1 TRP A 256 12696 17046 9282 -2607 126 1757 N ATOM 511 CE2 TRP A 256 26.014 -5.098 -57.025 1.00102.83 C ANISOU 511 CE2 TRP A 256 12757 16874 9439 -2445 108 1636 C ATOM 512 CE3 TRP A 256 25.274 -7.385 -56.687 1.00 98.16 C ANISOU 512 CE3 TRP A 256 12134 16218 8946 -2107 216 1395 C ATOM 513 CZ2 TRP A 256 25.167 -4.632 -56.007 1.00100.63 C ANISOU 513 CZ2 TRP A 256 12586 16356 9294 -2437 9 1616 C ATOM 514 CZ3 TRP A 256 24.408 -6.914 -55.714 1.00 98.08 C ANISOU 514 CZ3 TRP A 256 12206 15994 9067 -2120 116 1385 C ATOM 515 CH2 TRP A 256 24.362 -5.555 -55.380 1.00 98.84 C ANISOU 515 CH2 TRP A 256 12367 16008 9178 -2268 17 1491 C ATOM 516 N ARG A 257 26.423 -7.714 -62.306 1.00103.71 N ANISOU 516 N ARG A 257 12806 17599 8998 -2181 442 1470 N ATOM 517 CA ARG A 257 26.088 -6.897 -63.480 1.00104.80 C ANISOU 517 CA ARG A 257 13018 17777 9026 -2313 393 1549 C ATOM 518 C ARG A 257 24.585 -6.981 -63.816 1.00107.93 C ANISOU 518 C ARG A 257 13576 17962 9470 -2277 306 1472 C ATOM 519 O ARG A 257 23.986 -5.956 -64.146 1.00107.76 O ANISOU 519 O ARG A 257 13644 17858 9440 -2393 206 1558 O ATOM 520 CB ARG A 257 26.924 -7.325 -64.698 1.00106.45 C ANISOU 520 CB ARG A 257 13145 18265 9035 -2284 510 1558 C ATOM 521 N ASN A 258 23.980 -8.188 -63.691 1.00103.48 N ANISOU 521 N ASN A 258 13055 17315 8949 -2122 339 1318 N ATOM 522 CA ASN A 258 22.564 -8.442 -63.988 1.00102.49 C ANISOU 522 CA ASN A 258 13057 17034 8853 -2097 262 1237 C ATOM 523 C ASN A 258 21.685 -8.404 -62.737 1.00105.45 C ANISOU 523 C ASN A 258 13466 17195 9404 -2070 177 1201 C ATOM 524 O ASN A 258 20.548 -7.928 -62.809 1.00105.32 O ANISOU 524 O ASN A 258 13527 17071 9419 -2103 74 1212 O ATOM 525 CB ASN A 258 22.384 -9.810 -64.663 1.00102.70 C ANISOU 525 CB ASN A 258 13133 17097 8790 -1978 341 1089 C ATOM 526 CG ASN A 258 23.218 -10.071 -65.898 1.00121.93 C ANISOU 526 CG ASN A 258 15543 19751 11035 -1960 441 1094 C ATOM 527 OD1 ASN A 258 23.752 -9.163 -66.553 1.00109.45 O ANISOU 527 OD1 ASN A 258 13909 18317 9360 -2066 441 1218 O ATOM 528 ND2 ASN A 258 23.319 -11.340 -66.256 1.00115.23 N ANISOU 528 ND2 ASN A 258 14748 18924 10110 -1824 528 957 N ATOM 529 N SER A 259 22.194 -8.954 -61.615 1.00100.25 N ANISOU 529 N SER A 259 12746 16497 8847 -1995 224 1158 N ATOM 530 CA SER A 259 21.511 -9.073 -60.329 1.00 98.19 C ANISOU 530 CA SER A 259 12503 16056 8748 -1957 164 1117 C ATOM 531 C SER A 259 21.148 -7.722 -59.696 1.00100.27 C ANISOU 531 C SER A 259 12785 16221 9094 -2047 53 1225 C ATOM 532 O SER A 259 20.077 -7.629 -59.099 1.00 98.44 O ANISOU 532 O SER A 259 12603 15849 8950 -2019 -26 1195 O ATOM 533 CB SER A 259 22.380 -9.851 -59.350 1.00102.08 C ANISOU 533 CB SER A 259 12918 16562 9306 -1863 247 1072 C ATOM 534 OG SER A 259 22.607 -11.176 -59.800 1.00113.69 O ANISOU 534 OG SER A 259 14415 18079 10703 -1742 343 958 O ATOM 535 N ASN A 260 22.019 -6.687 -59.812 1.00 97.26 N ANISOU 535 N ASN A 260 12373 15913 8668 -2157 46 1352 N ATOM 536 CA ASN A 260 21.778 -5.361 -59.228 1.00 96.97 C ANISOU 536 CA ASN A 260 12400 15756 8687 -2249 -60 1457 C ATOM 537 C ASN A 260 20.652 -4.621 -59.989 1.00101.71 C ANISOU 537 C ASN A 260 13126 16282 9239 -2269 -158 1496 C ATOM 538 O ASN A 260 20.894 -3.621 -60.672 1.00101.68 O ANISOU 538 O ASN A 260 13185 16304 9143 -2377 -198 1610 O ATOM 539 CB ASN A 260 23.069 -4.528 -59.207 1.00100.45 C ANISOU 539 CB ASN A 260 12794 16303 9069 -2394 -42 1584 C ATOM 540 CG ASN A 260 23.021 -3.275 -58.349 1.00122.25 C ANISOU 540 CG ASN A 260 15644 18913 11891 -2496 -146 1678 C ATOM 541 OD1 ASN A 260 22.053 -3.004 -57.624 1.00115.67 O ANISOU 541 OD1 ASN A 260 14901 17893 11156 -2427 -226 1646 O ATOM 542 ND2 ASN A 260 24.095 -2.495 -58.386 1.00111.86 N ANISOU 542 ND2 ASN A 260 14310 17687 10504 -2666 -145 1798 N ATOM 543 N ARG A 261 19.409 -5.119 -59.832 1.00 98.05 N ANISOU 543 N ARG A 261 12694 15732 8827 -2168 -201 1409 N ATOM 544 CA ARG A 261 18.216 -4.573 -60.462 1.00 98.14 C ANISOU 544 CA ARG A 261 12796 15702 8789 -2151 -294 1435 C ATOM 545 C ARG A 261 17.017 -4.639 -59.510 1.00100.24 C ANISOU 545 C ARG A 261 13077 15848 9161 -2051 -368 1384 C ATOM 546 O ARG A 261 16.708 -5.696 -58.957 1.00 99.47 O ANISOU 546 O ARG A 261 12918 15746 9130 -1991 -331 1277 O ATOM 547 CB ARG A 261 17.911 -5.326 -61.770 1.00 99.69 C ANISOU 547 CB ARG A 261 12985 16028 8867 -2148 -255 1379 C ATOM 548 N TYR A 262 16.354 -3.495 -59.320 1.00 96.27 N ANISOU 548 N TYR A 262 12668 15252 8660 -2027 -470 1465 N ATOM 549 CA TYR A 262 15.168 -3.367 -58.478 1.00 95.13 C ANISOU 549 CA TYR A 262 12535 15024 8587 -1911 -546 1436 C ATOM 550 C TYR A 262 13.945 -3.875 -59.250 1.00100.77 C ANISOU 550 C TYR A 262 13219 15840 9229 -1859 -580 1391 C ATOM 551 O TYR A 262 13.906 -3.736 -60.475 1.00101.33 O ANISOU 551 O TYR A 262 13320 15998 9182 -1903 -585 1427 O ATOM 552 CB TYR A 262 14.984 -1.908 -58.014 1.00 96.01 C ANISOU 552 CB TYR A 262 12780 14998 8702 -1878 -640 1542 C ATOM 553 CG TYR A 262 16.032 -1.474 -57.012 1.00 96.82 C ANISOU 553 CG TYR A 262 12913 14992 8881 -1942 -621 1572 C ATOM 554 CD1 TYR A 262 17.273 -1.003 -57.432 1.00 99.49 C ANISOU 554 CD1 TYR A 262 13288 15348 9165 -2095 -589 1650 C ATOM 555 CD2 TYR A 262 15.802 -1.576 -55.640 1.00 96.33 C ANISOU 555 CD2 TYR A 262 12830 14837 8934 -1866 -634 1523 C ATOM 556 CE1 TYR A 262 18.259 -0.638 -56.515 1.00100.92 C ANISOU 556 CE1 TYR A 262 13481 15462 9402 -2180 -577 1682 C ATOM 557 CE2 TYR A 262 16.774 -1.196 -54.711 1.00 96.50 C ANISOU 557 CE2 TYR A 262 12877 14772 9016 -1937 -622 1549 C ATOM 558 CZ TYR A 262 18.003 -0.731 -55.154 1.00104.51 C ANISOU 558 CZ TYR A 262 13925 15813 9973 -2100 -596 1629 C ATOM 559 OH TYR A 262 18.975 -0.364 -54.255 1.00103.56 O ANISOU 559 OH TYR A 262 13816 15636 9895 -2195 -590 1660 O ATOM 560 N PRO A 263 12.968 -4.533 -58.587 1.00 97.38 N ANISOU 560 N PRO A 263 12721 15424 8856 -1783 -601 1314 N ATOM 561 CA PRO A 263 12.843 -4.769 -57.139 1.00 96.12 C ANISOU 561 CA PRO A 263 12518 15180 8826 -1723 -598 1269 C ATOM 562 C PRO A 263 13.468 -6.093 -56.649 1.00 97.10 C ANISOU 562 C PRO A 263 12565 15306 9020 -1768 -502 1166 C ATOM 563 O PRO A 263 13.314 -6.403 -55.465 1.00 96.11 O ANISOU 563 O PRO A 263 12399 15121 8996 -1722 -498 1126 O ATOM 564 CB PRO A 263 11.313 -4.778 -56.925 1.00 98.27 C ANISOU 564 CB PRO A 263 12746 15515 9077 -1625 -677 1256 C ATOM 565 CG PRO A 263 10.665 -4.772 -58.319 1.00103.52 C ANISOU 565 CG PRO A 263 13415 16317 9600 -1649 -714 1280 C ATOM 566 CD PRO A 263 11.775 -5.024 -59.297 1.00 99.41 C ANISOU 566 CD PRO A 263 12935 15808 9028 -1763 -642 1279 C ATOM 567 N ALA A 264 14.190 -6.852 -57.512 1.00 91.37 N ANISOU 567 N ALA A 264 11833 14648 8237 -1839 -423 1125 N ATOM 568 CA ALA A 264 14.795 -8.135 -57.119 1.00 89.51 C ANISOU 568 CA ALA A 264 11556 14405 8047 -1849 -330 1027 C ATOM 569 C ALA A 264 15.968 -7.977 -56.133 1.00 90.40 C ANISOU 569 C ALA A 264 11642 14451 8255 -1838 -277 1047 C ATOM 570 O ALA A 264 16.095 -8.796 -55.220 1.00 88.07 O ANISOU 570 O ALA A 264 11311 14111 8042 -1802 -237 981 O ATOM 571 CB ALA A 264 15.272 -8.890 -58.338 1.00 91.13 C ANISOU 571 CB ALA A 264 11784 14700 8141 -1896 -260 980 C ATOM 572 N VAL A 265 16.817 -6.936 -56.313 1.00 86.76 N ANISOU 572 N VAL A 265 11202 13990 7773 -1882 -281 1145 N ATOM 573 CA VAL A 265 17.986 -6.675 -55.460 1.00 85.37 C ANISOU 573 CA VAL A 265 10990 13784 7662 -1903 -241 1181 C ATOM 574 C VAL A 265 17.536 -6.294 -54.007 1.00 88.70 C ANISOU 574 C VAL A 265 11416 14082 8204 -1851 -299 1181 C ATOM 575 O VAL A 265 18.374 -6.268 -53.106 1.00 88.81 O ANISOU 575 O VAL A 265 11391 14068 8282 -1863 -269 1192 O ATOM 576 CB VAL A 265 18.932 -5.614 -56.079 1.00 89.13 C ANISOU 576 CB VAL A 265 11496 14307 8060 -2006 -244 1296 C ATOM 577 CG1 VAL A 265 18.385 -4.206 -55.908 1.00 88.70 C ANISOU 577 CG1 VAL A 265 11554 14143 8004 -2030 -356 1389 C ATOM 578 CG2 VAL A 265 20.351 -5.724 -55.513 1.00 88.92 C ANISOU 578 CG2 VAL A 265 11390 14339 8057 -2054 -172 1322 C ATOM 579 N ILE A 266 16.227 -6.042 -53.775 1.00 83.92 N ANISOU 579 N ILE A 266 10844 13426 7617 -1788 -378 1169 N ATOM 580 CA ILE A 266 15.717 -5.770 -52.422 1.00 82.07 C ANISOU 580 CA ILE A 266 10607 13095 7479 -1718 -425 1160 C ATOM 581 C ILE A 266 15.938 -7.035 -51.583 1.00 83.49 C ANISOU 581 C ILE A 266 10703 13278 7741 -1694 -356 1071 C ATOM 582 O ILE A 266 16.329 -6.916 -50.423 1.00 83.91 O ANISOU 582 O ILE A 266 10737 13268 7879 -1672 -353 1073 O ATOM 583 CB ILE A 266 14.230 -5.293 -52.426 1.00 84.93 C ANISOU 583 CB ILE A 266 11000 13451 7817 -1631 -517 1170 C ATOM 584 CG1 ILE A 266 14.132 -3.850 -52.984 1.00 85.50 C ANISOU 584 CG1 ILE A 266 11195 13477 7816 -1623 -593 1273 C ATOM 585 CG2 ILE A 266 13.570 -5.406 -51.021 1.00 84.54 C ANISOU 585 CG2 ILE A 266 10913 13350 7858 -1540 -545 1133 C ATOM 586 CD1 ILE A 266 12.787 -3.431 -53.433 1.00 89.23 C ANISOU 586 CD1 ILE A 266 11693 13993 8218 -1525 -672 1295 C ATOM 587 N LEU A 267 15.788 -8.228 -52.203 1.00 78.52 N ANISOU 587 N LEU A 267 10045 12715 7075 -1703 -301 997 N ATOM 588 CA LEU A 267 15.988 -9.531 -51.565 1.00 77.87 C ANISOU 588 CA LEU A 267 9923 12617 7047 -1679 -234 912 C ATOM 589 C LEU A 267 17.452 -9.725 -51.177 1.00 81.41 C ANISOU 589 C LEU A 267 10338 13068 7526 -1675 -155 923 C ATOM 590 O LEU A 267 17.715 -10.392 -50.166 1.00 81.11 O ANISOU 590 O LEU A 267 10268 12989 7563 -1631 -120 884 O ATOM 591 CB LEU A 267 15.500 -10.716 -52.436 1.00 78.43 C ANISOU 591 CB LEU A 267 10022 12734 7043 -1702 -201 830 C ATOM 592 CG LEU A 267 13.974 -11.062 -52.467 1.00 82.04 C ANISOU 592 CG LEU A 267 10481 13213 7476 -1722 -269 793 C ATOM 593 CD1 LEU A 267 13.406 -11.345 -51.095 1.00 79.69 C ANISOU 593 CD1 LEU A 267 10141 12866 7273 -1690 -293 773 C ATOM 594 CD2 LEU A 267 13.153 -10.018 -53.209 1.00 86.03 C ANISOU 594 CD2 LEU A 267 10987 13788 7914 -1729 -354 857 C ATOM 595 N PHE A 268 18.392 -9.095 -51.914 1.00 77.28 N ANISOU 595 N PHE A 268 9812 12611 6939 -1724 -131 988 N ATOM 596 CA PHE A 268 19.821 -9.142 -51.565 1.00 77.18 C ANISOU 596 CA PHE A 268 9737 12654 6934 -1731 -61 1019 C ATOM 597 C PHE A 268 20.054 -8.422 -50.213 1.00 83.58 C ANISOU 597 C PHE A 268 10523 13393 7839 -1741 -108 1066 C ATOM 598 O PHE A 268 20.687 -8.993 -49.317 1.00 83.74 O ANISOU 598 O PHE A 268 10481 13421 7915 -1699 -60 1044 O ATOM 599 CB PHE A 268 20.698 -8.531 -52.680 1.00 78.74 C ANISOU 599 CB PHE A 268 9924 12971 7022 -1809 -34 1094 C ATOM 600 CG PHE A 268 22.128 -8.210 -52.309 1.00 79.95 C ANISOU 600 CG PHE A 268 9991 13223 7163 -1855 13 1163 C ATOM 601 CD1 PHE A 268 23.128 -9.170 -52.428 1.00 83.01 C ANISOU 601 CD1 PHE A 268 10290 13741 7510 -1788 122 1132 C ATOM 602 CD2 PHE A 268 22.485 -6.937 -51.876 1.00 81.63 C ANISOU 602 CD2 PHE A 268 10218 13411 7387 -1966 -54 1263 C ATOM 603 CE1 PHE A 268 24.462 -8.865 -52.120 1.00 83.73 C ANISOU 603 CE1 PHE A 268 10268 13976 7568 -1832 165 1208 C ATOM 604 CE2 PHE A 268 23.818 -6.635 -51.556 1.00 84.52 C ANISOU 604 CE2 PHE A 268 10491 13899 7722 -2044 -18 1335 C ATOM 605 CZ PHE A 268 24.793 -7.606 -51.669 1.00 82.71 C ANISOU 605 CZ PHE A 268 10136 13839 7452 -1976 92 1311 C ATOM 606 N TYR A 269 19.528 -7.183 -50.072 1.00 80.49 N ANISOU 606 N TYR A 269 10200 12929 7455 -1786 -202 1128 N ATOM 607 CA TYR A 269 19.685 -6.378 -48.864 1.00 80.43 C ANISOU 607 CA TYR A 269 10210 12835 7515 -1800 -256 1168 C ATOM 608 C TYR A 269 18.958 -7.013 -47.662 1.00 83.95 C ANISOU 608 C TYR A 269 10629 13208 8059 -1703 -265 1097 C ATOM 609 O TYR A 269 19.471 -6.912 -46.549 1.00 83.53 O ANISOU 609 O TYR A 269 10546 13124 8067 -1701 -265 1105 O ATOM 610 CB TYR A 269 19.215 -4.941 -49.102 1.00 82.37 C ANISOU 610 CB TYR A 269 10581 12996 7721 -1847 -355 1244 C ATOM 611 CG TYR A 269 20.123 -4.202 -50.062 1.00 86.50 C ANISOU 611 CG TYR A 269 11139 13582 8146 -1979 -352 1334 C ATOM 612 CD1 TYR A 269 21.399 -3.796 -49.676 1.00 89.63 C ANISOU 612 CD1 TYR A 269 11503 14026 8528 -2097 -335 1398 C ATOM 613 CD2 TYR A 269 19.725 -3.945 -51.371 1.00 88.04 C ANISOU 613 CD2 TYR A 269 11388 13813 8249 -2000 -366 1363 C ATOM 614 CE1 TYR A 269 22.263 -3.165 -50.573 1.00 91.91 C ANISOU 614 CE1 TYR A 269 11807 14405 8710 -2244 -329 1491 C ATOM 615 CE2 TYR A 269 20.572 -3.296 -52.270 1.00 90.11 C ANISOU 615 CE2 TYR A 269 11680 14147 8411 -2134 -360 1453 C ATOM 616 CZ TYR A 269 21.841 -2.906 -51.866 1.00 98.44 C ANISOU 616 CZ TYR A 269 12698 15256 9450 -2262 -341 1520 C ATOM 617 OH TYR A 269 22.687 -2.271 -52.744 1.00100.52 O ANISOU 617 OH TYR A 269 12978 15617 9599 -2419 -335 1621 O ATOM 618 N VAL A 270 17.816 -7.702 -47.888 1.00 79.67 N ANISOU 618 N VAL A 270 10091 12659 7522 -1639 -272 1033 N ATOM 619 CA VAL A 270 17.068 -8.415 -46.843 1.00 78.55 C ANISOU 619 CA VAL A 270 9917 12474 7455 -1568 -276 971 C ATOM 620 C VAL A 270 17.971 -9.525 -46.281 1.00 81.60 C ANISOU 620 C VAL A 270 10242 12877 7884 -1550 -190 930 C ATOM 621 O VAL A 270 18.071 -9.676 -45.063 1.00 81.98 O ANISOU 621 O VAL A 270 10258 12883 8006 -1514 -191 920 O ATOM 622 CB VAL A 270 15.699 -8.983 -47.363 1.00 82.60 C ANISOU 622 CB VAL A 270 10437 13015 7935 -1544 -301 921 C ATOM 623 CG1 VAL A 270 15.057 -9.936 -46.356 1.00 81.60 C ANISOU 623 CG1 VAL A 270 10268 12868 7868 -1507 -292 861 C ATOM 624 CG2 VAL A 270 14.725 -7.867 -47.715 1.00 82.76 C ANISOU 624 CG2 VAL A 270 10501 13036 7910 -1520 -391 969 C ATOM 625 N ASN A 271 18.643 -10.274 -47.179 1.00 77.22 N ANISOU 625 N ASN A 271 9678 12391 7272 -1558 -114 908 N ATOM 626 CA ASN A 271 19.540 -11.382 -46.854 1.00 76.66 C ANISOU 626 CA ASN A 271 9568 12347 7213 -1503 -24 870 C ATOM 627 C ASN A 271 20.810 -10.892 -46.148 1.00 79.69 C ANISOU 627 C ASN A 271 9875 12784 7621 -1510 -2 932 C ATOM 628 O ASN A 271 21.356 -11.620 -45.324 1.00 78.32 O ANISOU 628 O ASN A 271 9656 12615 7487 -1443 45 912 O ATOM 629 CB ASN A 271 19.897 -12.154 -48.116 1.00 79.84 C ANISOU 629 CB ASN A 271 10000 12816 7519 -1489 47 832 C ATOM 630 CG ASN A 271 18.941 -13.275 -48.430 1.00100.63 C ANISOU 630 CG ASN A 271 12715 15388 10131 -1469 55 743 C ATOM 631 OD1 ASN A 271 19.192 -14.420 -48.083 1.00 95.56 O ANISOU 631 OD1 ASN A 271 12108 14706 9494 -1403 114 686 O ATOM 632 ND2 ASN A 271 17.836 -12.987 -49.109 1.00 92.78 N ANISOU 632 ND2 ASN A 271 11764 14389 9100 -1531 -7 733 N ATOM 633 N ALA A 272 21.266 -9.661 -46.458 1.00 77.13 N ANISOU 633 N ALA A 272 9544 12500 7263 -1600 -43 1012 N ATOM 634 CA ALA A 272 22.425 -9.033 -45.821 1.00 77.17 C ANISOU 634 CA ALA A 272 9480 12569 7271 -1656 -42 1084 C ATOM 635 C ALA A 272 22.125 -8.742 -44.342 1.00 80.43 C ANISOU 635 C ALA A 272 9897 12884 7778 -1641 -96 1080 C ATOM 636 O ALA A 272 22.967 -9.028 -43.494 1.00 80.77 O ANISOU 636 O ALA A 272 9860 12981 7846 -1625 -65 1094 O ATOM 637 CB ALA A 272 22.802 -7.758 -46.553 1.00 78.68 C ANISOU 637 CB ALA A 272 9705 12801 7389 -1791 -88 1173 C ATOM 638 N CYS A 273 20.907 -8.232 -44.037 1.00 76.16 N ANISOU 638 N CYS A 273 9441 12218 7276 -1629 -174 1061 N ATOM 639 CA CYS A 273 20.413 -7.958 -42.677 1.00 75.11 C ANISOU 639 CA CYS A 273 9326 11993 7220 -1592 -227 1047 C ATOM 640 C CYS A 273 20.367 -9.257 -41.847 1.00 80.08 C ANISOU 640 C CYS A 273 9888 12627 7911 -1502 -169 987 C ATOM 641 O CYS A 273 20.766 -9.256 -40.682 1.00 79.77 O ANISOU 641 O CYS A 273 9810 12578 7921 -1486 -174 994 O ATOM 642 CB CYS A 273 19.036 -7.298 -42.728 1.00 74.49 C ANISOU 642 CB CYS A 273 9339 11820 7143 -1559 -306 1035 C ATOM 643 SG CYS A 273 19.013 -5.689 -43.550 1.00 79.00 S ANISOU 643 SG CYS A 273 10037 12343 7635 -1641 -387 1114 S ATOM 644 N PHE A 274 19.888 -10.365 -42.453 1.00 76.49 N ANISOU 644 N PHE A 274 9437 12181 7444 -1450 -120 929 N ATOM 645 CA PHE A 274 19.783 -11.642 -41.763 1.00 75.31 C ANISOU 645 CA PHE A 274 9267 12009 7337 -1375 -70 874 C ATOM 646 C PHE A 274 21.144 -12.325 -41.619 1.00 78.89 C ANISOU 646 C PHE A 274 9659 12539 7776 -1327 12 886 C ATOM 647 O PHE A 274 21.304 -13.119 -40.698 1.00 79.62 O ANISOU 647 O PHE A 274 9734 12608 7911 -1257 42 864 O ATOM 648 CB PHE A 274 18.773 -12.560 -42.454 1.00 77.10 C ANISOU 648 CB PHE A 274 9554 12204 7536 -1363 -57 811 C ATOM 649 CG PHE A 274 17.363 -12.200 -42.038 1.00 78.26 C ANISOU 649 CG PHE A 274 9719 12308 7709 -1378 -133 799 C ATOM 650 CD1 PHE A 274 16.856 -12.609 -40.808 1.00 79.02 C ANISOU 650 CD1 PHE A 274 9795 12366 7863 -1347 -146 781 C ATOM 651 CD2 PHE A 274 16.547 -11.433 -42.867 1.00 81.44 C ANISOU 651 CD2 PHE A 274 10149 12730 8064 -1413 -190 813 C ATOM 652 CE1 PHE A 274 15.563 -12.256 -40.412 1.00 79.46 C ANISOU 652 CE1 PHE A 274 9843 12424 7924 -1349 -210 777 C ATOM 653 CE2 PHE A 274 15.253 -11.078 -42.467 1.00 83.57 C ANISOU 653 CE2 PHE A 274 10414 12999 8340 -1399 -257 810 C ATOM 654 CZ PHE A 274 14.774 -11.489 -41.237 1.00 80.29 C ANISOU 654 CZ PHE A 274 9963 12566 7978 -1366 -264 792 C ATOM 655 N PHE A 275 22.132 -11.981 -42.456 1.00 75.47 N ANISOU 655 N PHE A 275 9186 12214 7275 -1357 47 928 N ATOM 656 CA PHE A 275 23.493 -12.525 -42.354 1.00 75.94 C ANISOU 656 CA PHE A 275 9156 12401 7298 -1295 127 953 C ATOM 657 C PHE A 275 24.217 -11.876 -41.152 1.00 79.72 C ANISOU 657 C PHE A 275 9546 12929 7815 -1333 94 1015 C ATOM 658 O PHE A 275 24.721 -12.588 -40.274 1.00 79.31 O ANISOU 658 O PHE A 275 9438 12906 7789 -1244 133 1010 O ATOM 659 CB PHE A 275 24.287 -12.315 -43.672 1.00 78.83 C ANISOU 659 CB PHE A 275 9485 12908 7557 -1324 175 988 C ATOM 660 CG PHE A 275 25.711 -12.803 -43.562 1.00 81.43 C ANISOU 660 CG PHE A 275 9694 13418 7828 -1244 259 1025 C ATOM 661 CD1 PHE A 275 25.998 -14.165 -43.560 1.00 85.04 C ANISOU 661 CD1 PHE A 275 10166 13885 8260 -1068 347 970 C ATOM 662 CD2 PHE A 275 26.757 -11.907 -43.390 1.00 84.18 C ANISOU 662 CD2 PHE A 275 9918 13931 8135 -1342 246 1120 C ATOM 663 CE1 PHE A 275 27.306 -14.619 -43.400 1.00 87.06 C ANISOU 663 CE1 PHE A 275 10300 14329 8449 -955 426 1010 C ATOM 664 CE2 PHE A 275 28.064 -12.362 -43.227 1.00 88.44 C ANISOU 664 CE2 PHE A 275 10313 14685 8607 -1262 322 1164 C ATOM 665 CZ PHE A 275 28.330 -13.716 -43.234 1.00 87.25 C ANISOU 665 CZ PHE A 275 10163 14557 8430 -1050 415 1109 C ATOM 666 N VAL A 276 24.229 -10.521 -41.110 1.00 76.44 N ANISOU 666 N VAL A 276 9138 12510 7395 -1469 17 1072 N ATOM 667 CA VAL A 276 24.831 -9.700 -40.053 1.00 76.63 C ANISOU 667 CA VAL A 276 9114 12563 7437 -1550 -34 1130 C ATOM 668 C VAL A 276 24.146 -10.046 -38.714 1.00 81.93 C ANISOU 668 C VAL A 276 9811 13118 8200 -1477 -63 1084 C ATOM 669 O VAL A 276 24.834 -10.211 -37.697 1.00 81.66 O ANISOU 669 O VAL A 276 9700 13143 8183 -1460 -56 1107 O ATOM 670 CB VAL A 276 24.744 -8.189 -40.406 1.00 80.16 C ANISOU 670 CB VAL A 276 9639 12972 7847 -1714 -121 1188 C ATOM 671 CG1 VAL A 276 25.188 -7.300 -39.242 1.00 79.95 C ANISOU 671 CG1 VAL A 276 9615 12930 7833 -1813 -192 1233 C ATOM 672 CG2 VAL A 276 25.565 -7.879 -41.655 1.00 80.72 C ANISOU 672 CG2 VAL A 276 9667 13189 7816 -1805 -88 1249 C ATOM 673 N GLY A 277 22.821 -10.232 -38.761 1.00 78.34 N ANISOU 673 N GLY A 277 9449 12527 7789 -1432 -91 1025 N ATOM 674 CA GLY A 277 22.012 -10.632 -37.620 1.00 77.76 C ANISOU 674 CA GLY A 277 9396 12361 7787 -1365 -113 982 C ATOM 675 C GLY A 277 22.486 -11.925 -36.985 1.00 84.19 C ANISOU 675 C GLY A 277 10152 13211 8627 -1265 -42 961 C ATOM 676 O GLY A 277 22.615 -11.990 -35.760 1.00 83.25 O ANISOU 676 O GLY A 277 10000 13082 8550 -1240 -58 969 O ATOM 677 N SER A 278 22.804 -12.948 -37.823 1.00 83.10 N ANISOU 677 N SER A 278 10014 13110 8449 -1198 36 938 N ATOM 678 CA SER A 278 23.294 -14.261 -37.375 1.00 83.45 C ANISOU 678 CA SER A 278 10042 13170 8496 -1073 109 918 C ATOM 679 C SER A 278 24.622 -14.182 -36.627 1.00 87.27 C ANISOU 679 C SER A 278 10403 13790 8965 -1035 134 979 C ATOM 680 O SER A 278 24.820 -14.953 -35.692 1.00 87.39 O ANISOU 680 O SER A 278 10404 13793 9006 -940 159 975 O ATOM 681 CB SER A 278 23.452 -15.208 -38.554 1.00 88.73 C ANISOU 681 CB SER A 278 10767 13849 9099 -1000 185 880 C ATOM 682 OG SER A 278 22.172 -15.723 -38.878 1.00102.47 O ANISOU 682 OG SER A 278 12627 15453 10853 -1020 166 816 O ATOM 683 N ILE A 279 25.518 -13.256 -37.018 1.00 83.10 N ANISOU 683 N ILE A 279 9787 13401 8385 -1122 122 1041 N ATOM 684 CA ILE A 279 26.828 -13.089 -36.382 1.00 82.95 C ANISOU 684 CA ILE A 279 9625 13561 8330 -1119 137 1112 C ATOM 685 C ILE A 279 26.614 -12.689 -34.894 1.00 85.94 C ANISOU 685 C ILE A 279 9995 13883 8775 -1158 70 1122 C ATOM 686 O ILE A 279 27.237 -13.288 -34.018 1.00 86.73 O ANISOU 686 O ILE A 279 10017 14059 8875 -1069 98 1143 O ATOM 687 CB ILE A 279 27.709 -12.082 -37.189 1.00 86.29 C ANISOU 687 CB ILE A 279 9965 14153 8668 -1257 126 1184 C ATOM 688 CG1 ILE A 279 28.124 -12.709 -38.540 1.00 87.07 C ANISOU 688 CG1 ILE A 279 10043 14356 8683 -1175 214 1177 C ATOM 689 CG2 ILE A 279 28.953 -11.632 -36.407 1.00 87.06 C ANISOU 689 CG2 ILE A 279 9906 14454 8718 -1322 112 1270 C ATOM 690 CD1 ILE A 279 28.404 -11.717 -39.663 1.00 93.03 C ANISOU 690 CD1 ILE A 279 10782 15202 9364 -1330 194 1227 C ATOM 691 N GLY A 280 25.692 -11.761 -34.638 1.00 80.25 N ANISOU 691 N GLY A 280 9364 13028 8099 -1264 -14 1104 N ATOM 692 CA GLY A 280 25.342 -11.311 -33.294 1.00 78.50 C ANISOU 692 CA GLY A 280 9160 12737 7928 -1293 -80 1101 C ATOM 693 C GLY A 280 24.803 -12.418 -32.411 1.00 80.08 C ANISOU 693 C GLY A 280 9375 12866 8187 -1162 -49 1059 C ATOM 694 O GLY A 280 25.098 -12.463 -31.212 1.00 80.55 O ANISOU 694 O GLY A 280 9388 12952 8265 -1144 -68 1077 O ATOM 695 N TRP A 281 24.018 -13.323 -33.011 1.00 74.88 N ANISOU 695 N TRP A 281 8787 12118 7544 -1084 -6 1007 N ATOM 696 CA TRP A 281 23.393 -14.479 -32.363 1.00 73.68 C ANISOU 696 CA TRP A 281 8683 11880 7433 -985 23 968 C ATOM 697 C TRP A 281 24.400 -15.605 -32.107 1.00 78.10 C ANISOU 697 C TRP A 281 9196 12513 7964 -853 100 990 C ATOM 698 O TRP A 281 24.245 -16.334 -31.129 1.00 77.85 O ANISOU 698 O TRP A 281 9183 12435 7961 -781 109 988 O ATOM 699 CB TRP A 281 22.234 -15.026 -33.233 1.00 71.57 C ANISOU 699 CB TRP A 281 8524 11501 7167 -986 35 910 C ATOM 700 CG TRP A 281 20.963 -14.230 -33.161 1.00 70.97 C ANISOU 700 CG TRP A 281 8492 11354 7118 -1065 -38 886 C ATOM 701 CD1 TRP A 281 20.496 -13.345 -34.084 1.00 73.40 C ANISOU 701 CD1 TRP A 281 8830 11656 7405 -1133 -77 881 C ATOM 702 CD2 TRP A 281 20.007 -14.243 -32.095 1.00 70.29 C ANISOU 702 CD2 TRP A 281 8419 11216 7072 -1064 -78 871 C ATOM 703 NE1 TRP A 281 19.309 -12.802 -33.664 1.00 72.45 N ANISOU 703 NE1 TRP A 281 8740 11485 7304 -1155 -138 863 N ATOM 704 CE2 TRP A 281 18.990 -13.323 -32.433 1.00 73.75 C ANISOU 704 CE2 TRP A 281 8887 11631 7504 -1115 -138 856 C ATOM 705 CE3 TRP A 281 19.903 -14.953 -30.883 1.00 71.33 C ANISOU 705 CE3 TRP A 281 8540 11329 7232 -1016 -67 873 C ATOM 706 CZ2 TRP A 281 17.881 -13.089 -31.602 1.00 72.46 C ANISOU 706 CZ2 TRP A 281 8727 11448 7356 -1107 -183 841 C ATOM 707 CZ3 TRP A 281 18.820 -14.702 -30.050 1.00 72.45 C ANISOU 707 CZ3 TRP A 281 8686 11446 7394 -1033 -113 861 C ATOM 708 CH2 TRP A 281 17.817 -13.791 -30.417 1.00 72.85 C ANISOU 708 CH2 TRP A 281 8752 11494 7432 -1072 -168 843 C ATOM 709 N LEU A 282 25.406 -15.765 -32.989 1.00 75.02 N ANISOU 709 N LEU A 282 8752 12245 7509 -808 156 1016 N ATOM 710 CA LEU A 282 26.397 -16.846 -32.891 1.00 75.77 C ANISOU 710 CA LEU A 282 8807 12429 7553 -638 237 1038 C ATOM 711 C LEU A 282 27.631 -16.483 -32.053 1.00 79.19 C ANISOU 711 C LEU A 282 9072 13062 7956 -619 232 1116 C ATOM 712 O LEU A 282 28.337 -17.399 -31.620 1.00 80.09 O ANISOU 712 O LEU A 282 9148 13249 8034 -453 289 1142 O ATOM 713 CB LEU A 282 26.864 -17.299 -34.282 1.00 76.61 C ANISOU 713 CB LEU A 282 8934 12595 7580 -563 310 1023 C ATOM 714 CG LEU A 282 25.804 -17.965 -35.163 1.00 80.91 C ANISOU 714 CG LEU A 282 9657 12957 8127 -556 328 943 C ATOM 715 CD1 LEU A 282 26.205 -17.915 -36.634 1.00 80.85 C ANISOU 715 CD1 LEU A 282 9653 13029 8038 -542 377 931 C ATOM 716 CD2 LEU A 282 25.443 -19.375 -34.665 1.00 83.58 C ANISOU 716 CD2 LEU A 282 10139 13148 8470 -422 367 904 C ATOM 717 N ALA A 283 27.882 -15.179 -31.801 1.00 73.87 N ANISOU 717 N ALA A 283 8310 12473 7283 -787 162 1157 N ATOM 718 CA ALA A 283 29.026 -14.697 -31.011 1.00 73.85 C ANISOU 718 CA ALA A 283 8146 12676 7237 -824 140 1236 C ATOM 719 C ALA A 283 29.110 -15.370 -29.628 1.00 80.12 C ANISOU 719 C ALA A 283 8919 13461 8061 -716 140 1247 C ATOM 720 O ALA A 283 30.213 -15.603 -29.142 1.00 81.15 O ANISOU 720 O ALA A 283 8907 13794 8132 -646 163 1313 O ATOM 721 CB ALA A 283 28.939 -13.193 -30.840 1.00 73.77 C ANISOU 721 CB ALA A 283 8127 12671 7231 -1052 44 1259 C ATOM 722 N GLN A 284 27.945 -15.701 -29.011 1.00 76.44 N ANISOU 722 N GLN A 284 8585 12783 7677 -701 114 1190 N ATOM 723 CA GLN A 284 27.821 -16.355 -27.698 1.00 75.61 C ANISOU 723 CA GLN A 284 8488 12639 7603 -612 110 1198 C ATOM 724 C GLN A 284 28.466 -17.758 -27.653 1.00 84.23 C ANISOU 724 C GLN A 284 9577 13778 8651 -388 197 1221 C ATOM 725 O GLN A 284 28.703 -18.286 -26.562 1.00 85.02 O ANISOU 725 O GLN A 284 9654 13898 8752 -298 198 1252 O ATOM 726 CB GLN A 284 26.340 -16.489 -27.321 1.00 74.40 C ANISOU 726 CB GLN A 284 8479 12262 7526 -650 77 1134 C ATOM 727 CG GLN A 284 25.564 -17.449 -28.207 1.00 68.11 C ANISOU 727 CG GLN A 284 7822 11317 6739 -584 129 1079 C ATOM 728 CD GLN A 284 24.131 -17.575 -27.807 1.00 85.56 C ANISOU 728 CD GLN A 284 10143 13360 9005 -644 92 1031 C ATOM 729 OE1 GLN A 284 23.793 -18.242 -26.821 1.00 83.45 O ANISOU 729 OE1 GLN A 284 9913 13036 8757 -598 93 1037 O ATOM 730 NE2 GLN A 284 23.251 -16.926 -28.559 1.00 69.07 N ANISOU 730 NE2 GLN A 284 8102 11210 6933 -749 58 989 N ATOM 731 N PHE A 285 28.708 -18.372 -28.828 1.00 83.12 N ANISOU 731 N PHE A 285 9479 13641 8462 -286 268 1203 N ATOM 732 CA PHE A 285 29.256 -19.718 -28.907 1.00 84.69 C ANISOU 732 CA PHE A 285 9725 13851 8603 -44 354 1213 C ATOM 733 C PHE A 285 30.817 -19.698 -28.907 1.00 93.03 C ANISOU 733 C PHE A 285 10577 15215 9556 80 397 1298 C ATOM 734 O PHE A 285 31.422 -20.763 -28.827 1.00 92.90 O ANISOU 734 O PHE A 285 10579 15245 9473 321 467 1321 O ATOM 735 CB PHE A 285 28.674 -20.459 -30.125 1.00 85.94 C ANISOU 735 CB PHE A 285 10064 13845 8743 18 409 1142 C ATOM 736 CG PHE A 285 27.174 -20.601 -30.014 1.00 85.23 C ANISOU 736 CG PHE A 285 10152 13498 8735 -103 364 1074 C ATOM 737 CD1 PHE A 285 26.327 -19.850 -30.823 1.00 86.69 C ANISOU 737 CD1 PHE A 285 10370 13614 8953 -274 325 1026 C ATOM 738 CD2 PHE A 285 26.605 -21.431 -29.050 1.00 86.10 C ANISOU 738 CD2 PHE A 285 10379 13457 8877 -55 357 1068 C ATOM 739 CE1 PHE A 285 24.939 -19.954 -30.696 1.00 86.44 C ANISOU 739 CE1 PHE A 285 10468 13395 8980 -383 282 974 C ATOM 740 CE2 PHE A 285 25.218 -21.532 -28.923 1.00 87.64 C ANISOU 740 CE2 PHE A 285 10707 13461 9130 -188 315 1017 C ATOM 741 CZ PHE A 285 24.395 -20.779 -29.733 1.00 84.99 C ANISOU 741 CZ PHE A 285 10381 13090 8823 -348 277 971 C ATOM 742 N MET A 286 31.444 -18.493 -28.898 1.00 93.45 N ANISOU 742 N MET A 286 10442 15480 9584 -86 349 1351 N ATOM 743 CA MET A 286 32.904 -18.313 -28.750 1.00 96.98 C ANISOU 743 CA MET A 286 10654 16273 9922 -26 371 1448 C ATOM 744 C MET A 286 33.281 -18.630 -27.312 1.00102.97 C ANISOU 744 C MET A 286 11340 17104 10680 52 346 1500 C ATOM 745 O MET A 286 32.635 -18.086 -26.406 1.00102.43 O ANISOU 745 O MET A 286 11314 16913 10691 -102 267 1483 O ATOM 746 CB MET A 286 33.366 -16.870 -29.112 1.00100.22 C ANISOU 746 CB MET A 286 10912 16870 10298 -290 310 1493 C ATOM 747 CG MET A 286 32.864 -16.325 -30.449 1.00104.39 C ANISOU 747 CG MET A 286 11523 17306 10835 -415 313 1446 C ATOM 748 SD MET A 286 33.434 -17.192 -31.904 1.00111.30 S ANISOU 748 SD MET A 286 12384 18299 11605 -203 436 1440 S ATOM 749 CE MET A 286 35.145 -16.728 -31.891 1.00110.52 C ANISOU 749 CE MET A 286 11964 18676 11351 -215 456 1573 C ATOM 750 N ASP A 287 34.307 -19.488 -27.074 1.00101.58 N ANISOU 750 N ASP A 287 11056 17133 10405 301 412 1566 N ATOM 751 CA ASP A 287 34.725 -19.891 -25.714 1.00102.01 C ANISOU 751 CA ASP A 287 11039 17276 10445 406 393 1626 C ATOM 752 C ASP A 287 34.623 -18.659 -24.793 1.00100.16 C ANISOU 752 C ASP A 287 10693 17117 10248 139 283 1656 C ATOM 753 O ASP A 287 35.349 -17.668 -24.967 1.00 99.69 O ANISOU 753 O ASP A 287 10428 17338 10114 -10 245 1723 O ATOM 754 CB ASP A 287 36.128 -20.529 -25.707 1.00108.19 C ANISOU 754 CB ASP A 287 11628 18399 11079 667 463 1721 C ATOM 755 CG ASP A 287 36.252 -21.903 -26.358 1.00133.29 C ANISOU 755 CG ASP A 287 14950 21496 14197 1015 575 1698 C ATOM 756 OD1 ASP A 287 35.235 -22.645 -26.394 1.00136.11 O ANISOU 756 OD1 ASP A 287 15587 21496 14634 1077 589 1617 O ATOM 757 OD2 ASP A 287 37.385 -22.269 -26.759 1.00141.32 O ANISOU 757 OD2 ASP A 287 15805 22816 15073 1234 646 1765 O ATOM 758 N GLY A 288 33.682 -18.735 -23.851 1.00 92.27 N ANISOU 758 N GLY A 288 9845 15862 9352 70 231 1605 N ATOM 759 CA GLY A 288 33.499 -17.758 -22.781 1.00 90.09 C ANISOU 759 CA GLY A 288 9518 15602 9110 -147 130 1616 C ATOM 760 C GLY A 288 32.859 -16.421 -23.115 1.00 89.53 C ANISOU 760 C GLY A 288 9500 15425 9090 -433 52 1565 C ATOM 761 O GLY A 288 32.660 -15.607 -22.206 1.00 88.77 O ANISOU 761 O GLY A 288 9401 15316 9013 -598 -33 1563 O ATOM 762 N ALA A 289 32.522 -16.174 -24.398 1.00 82.53 N ANISOU 762 N ALA A 289 8682 14457 8219 -484 79 1522 N ATOM 763 CA ALA A 289 31.932 -14.899 -24.812 1.00 80.21 C ANISOU 763 CA ALA A 289 8456 14058 7961 -734 6 1481 C ATOM 764 C ALA A 289 30.502 -14.719 -24.265 1.00 79.26 C ANISOU 764 C ALA A 289 8523 13645 7947 -785 -41 1398 C ATOM 765 O ALA A 289 30.138 -13.606 -23.888 1.00 77.84 O ANISOU 765 O ALA A 289 8386 13408 7782 -966 -125 1379 O ATOM 766 CB ALA A 289 31.933 -14.779 -26.328 1.00 81.03 C ANISOU 766 CB ALA A 289 8583 14160 8045 -753 52 1463 C ATOM 767 N ARG A 290 29.713 -15.811 -24.181 1.00 72.96 N ANISOU 767 N ARG A 290 7841 12673 7206 -624 10 1354 N ATOM 768 CA ARG A 290 28.333 -15.758 -23.696 1.00 70.55 C ANISOU 768 CA ARG A 290 7687 12134 6984 -664 -26 1286 C ATOM 769 C ARG A 290 28.262 -15.064 -22.344 1.00 75.68 C ANISOU 769 C ARG A 290 8310 12807 7639 -756 -103 1297 C ATOM 770 O ARG A 290 27.492 -14.116 -22.210 1.00 74.58 O ANISOU 770 O ARG A 290 8248 12562 7528 -884 -167 1251 O ATOM 771 CB ARG A 290 27.720 -17.159 -23.634 1.00 67.03 C ANISOU 771 CB ARG A 290 7351 11547 6571 -497 38 1262 C ATOM 772 CG ARG A 290 26.507 -17.295 -22.721 1.00 70.64 C ANISOU 772 CG ARG A 290 7913 11840 7088 -527 4 1223 C ATOM 773 CD ARG A 290 25.181 -17.683 -23.346 1.00 67.71 C ANISOU 773 CD ARG A 290 7689 11275 6763 -548 18 1158 C ATOM 774 NE ARG A 290 25.271 -18.463 -24.585 1.00 80.55 N ANISOU 774 NE ARG A 290 9385 12849 8370 -474 84 1140 N ATOM 775 CZ ARG A 290 25.676 -19.726 -24.682 1.00 85.96 C ANISOU 775 CZ ARG A 290 10132 13506 9024 -318 150 1158 C ATOM 776 NH1 ARG A 290 26.162 -20.357 -23.625 1.00 66.25 N ANISOU 776 NH1 ARG A 290 7615 11048 6509 -209 162 1208 N ATOM 777 NH2 ARG A 290 25.672 -20.339 -25.856 1.00 72.29 N ANISOU 777 NH2 ARG A 290 8492 11711 7264 -259 205 1128 N ATOM 778 N ARG A 291 29.096 -15.497 -21.374 1.00 74.69 N ANISOU 778 N ARG A 291 8078 12829 7471 -681 -100 1358 N ATOM 779 CA ARG A 291 29.164 -14.942 -20.022 1.00 74.59 C ANISOU 779 CA ARG A 291 8030 12864 7445 -758 -171 1372 C ATOM 780 C ARG A 291 29.725 -13.501 -20.077 1.00 79.43 C ANISOU 780 C ARG A 291 8591 13583 8005 -973 -253 1385 C ATOM 781 O ARG A 291 29.269 -12.646 -19.320 1.00 79.73 O ANISOU 781 O ARG A 291 8698 13549 8046 -1090 -329 1352 O ATOM 782 CB ARG A 291 30.006 -15.866 -19.129 1.00 74.51 C ANISOU 782 CB ARG A 291 7912 13009 7390 -609 -142 1445 C ATOM 783 CG ARG A 291 29.972 -15.535 -17.650 1.00 82.21 C ANISOU 783 CG ARG A 291 8864 14021 8350 -661 -207 1459 C ATOM 784 CD ARG A 291 30.127 -16.773 -16.787 1.00 92.50 C ANISOU 784 CD ARG A 291 10150 15350 9645 -470 -164 1506 C ATOM 785 NE ARG A 291 29.954 -16.463 -15.367 1.00 95.88 N ANISOU 785 NE ARG A 291 10569 15800 10060 -522 -226 1513 N ATOM 786 CZ ARG A 291 28.792 -16.493 -14.724 1.00111.97 C ANISOU 786 CZ ARG A 291 12731 17662 12150 -539 -243 1460 C ATOM 787 NH1 ARG A 291 27.678 -16.825 -15.366 1.00102.98 N ANISOU 787 NH1 ARG A 291 11725 16321 11079 -520 -207 1402 N ATOM 788 NH2 ARG A 291 28.734 -16.190 -13.435 1.00103.82 N ANISOU 788 NH2 ARG A 291 11682 16677 11089 -580 -297 1469 N ATOM 789 N GLU A 292 30.655 -13.225 -21.004 1.00 76.06 N ANISOU 789 N GLU A 292 8064 13316 7519 -1029 -237 1431 N ATOM 790 CA GLU A 292 31.195 -11.879 -21.202 1.00 77.04 C ANISOU 790 CA GLU A 292 8161 13533 7579 -1266 -316 1453 C ATOM 791 C GLU A 292 30.094 -10.905 -21.718 1.00 82.05 C ANISOU 791 C GLU A 292 8990 13922 8262 -1388 -365 1374 C ATOM 792 O GLU A 292 30.022 -9.763 -21.269 1.00 82.85 O ANISOU 792 O GLU A 292 9171 13978 8330 -1562 -456 1360 O ATOM 793 CB GLU A 292 32.398 -11.913 -22.173 1.00 79.34 C ANISOU 793 CB GLU A 292 8288 14074 7785 -1294 -277 1530 C ATOM 794 CG GLU A 292 32.866 -10.557 -22.696 1.00 88.60 C ANISOU 794 CG GLU A 292 9458 15320 8885 -1568 -351 1557 C ATOM 795 CD GLU A 292 33.199 -9.464 -21.692 1.00102.95 C ANISOU 795 CD GLU A 292 11295 17183 10639 -1798 -466 1576 C ATOM 796 OE1 GLU A 292 33.303 -8.290 -22.116 1.00 93.92 O ANISOU 796 OE1 GLU A 292 10234 16007 9444 -2036 -539 1580 O ATOM 797 OE2 GLU A 292 33.339 -9.770 -20.485 1.00 94.67 O ANISOU 797 OE2 GLU A 292 10199 16190 9582 -1746 -489 1585 O ATOM 798 N ILE A 293 29.237 -11.370 -22.629 1.00 77.83 N ANISOU 798 N ILE A 293 8544 13232 7795 -1290 -309 1324 N ATOM 799 CA ILE A 293 28.156 -10.571 -23.192 1.00 77.01 C ANISOU 799 CA ILE A 293 8608 12921 7731 -1365 -348 1257 C ATOM 800 C ILE A 293 27.039 -10.297 -22.134 1.00 80.62 C ANISOU 800 C ILE A 293 9189 13212 8231 -1341 -396 1194 C ATOM 801 O ILE A 293 26.670 -9.147 -21.917 1.00 80.56 O ANISOU 801 O ILE A 293 9297 13111 8200 -1453 -473 1164 O ATOM 802 CB ILE A 293 27.579 -11.295 -24.460 1.00 79.11 C ANISOU 802 CB ILE A 293 8912 13104 8044 -1258 -270 1227 C ATOM 803 CG1 ILE A 293 28.634 -11.361 -25.607 1.00 79.22 C ANISOU 803 CG1 ILE A 293 8820 13284 7998 -1289 -226 1283 C ATOM 804 CG2 ILE A 293 26.280 -10.619 -24.955 1.00 79.07 C ANISOU 804 CG2 ILE A 293 9070 12894 8080 -1299 -307 1159 C ATOM 805 CD1 ILE A 293 28.399 -12.467 -26.727 1.00 71.30 C ANISOU 805 CD1 ILE A 293 7822 12250 7017 -1134 -128 1262 C ATOM 806 N VAL A 294 26.550 -11.350 -21.480 1.00 77.03 N ANISOU 806 N VAL A 294 8716 12728 7823 -1192 -349 1180 N ATOM 807 CA VAL A 294 25.376 -11.421 -20.606 1.00 76.64 C ANISOU 807 CA VAL A 294 8756 12551 7813 -1133 -368 1127 C ATOM 808 C VAL A 294 25.620 -11.044 -19.087 1.00 82.84 C ANISOU 808 C VAL A 294 9527 13387 8561 -1163 -425 1134 C ATOM 809 O VAL A 294 24.651 -10.642 -18.425 1.00 81.26 O ANISOU 809 O VAL A 294 9421 13085 8368 -1148 -460 1082 O ATOM 810 CB VAL A 294 24.862 -12.876 -20.751 1.00 80.15 C ANISOU 810 CB VAL A 294 9186 12958 8310 -984 -285 1125 C ATOM 811 CG1 VAL A 294 23.907 -13.282 -19.654 1.00 80.26 C ANISOU 811 CG1 VAL A 294 9242 12906 8348 -921 -289 1100 C ATOM 812 CG2 VAL A 294 24.230 -13.095 -22.125 1.00 79.35 C ANISOU 812 CG2 VAL A 294 9146 12764 8239 -970 -246 1093 C ATOM 813 N CYS A 295 26.854 -11.150 -18.542 1.00 81.16 N ANISOU 813 N CYS A 295 9195 13345 8296 -1200 -437 1198 N ATOM 814 CA CYS A 295 27.042 -10.829 -17.127 1.00 81.78 C ANISOU 814 CA CYS A 295 9266 13475 8332 -1233 -494 1202 C ATOM 815 C CYS A 295 27.700 -9.479 -16.906 1.00 81.96 C ANISOU 815 C CYS A 295 9327 13543 8271 -1430 -589 1206 C ATOM 816 O CYS A 295 28.441 -8.977 -17.749 1.00 81.81 O ANISOU 816 O CYS A 295 9277 13593 8212 -1553 -605 1240 O ATOM 817 CB CYS A 295 27.850 -11.910 -16.420 1.00 84.74 C ANISOU 817 CB CYS A 295 9493 14014 8691 -1132 -453 1272 C ATOM 818 SG CYS A 295 27.378 -13.604 -16.844 1.00 89.54 S ANISOU 818 SG CYS A 295 10087 14563 9370 -916 -340 1285 S ATOM 819 N ARG A 296 27.465 -8.933 -15.701 1.00 75.74 N ANISOU 819 N ARG A 296 8610 12725 7442 -1469 -654 1174 N ATOM 820 CA ARG A 296 28.124 -7.749 -15.168 1.00 74.63 C ANISOU 820 CA ARG A 296 8530 12625 7202 -1665 -756 1176 C ATOM 821 C ARG A 296 29.449 -8.224 -14.583 1.00 77.91 C ANISOU 821 C ARG A 296 8747 13300 7555 -1714 -761 1265 C ATOM 822 O ARG A 296 29.609 -9.428 -14.391 1.00 76.89 O ANISOU 822 O ARG A 296 8477 13271 7466 -1551 -687 1308 O ATOM 823 CB ARG A 296 27.242 -7.056 -14.113 1.00 70.82 C ANISOU 823 CB ARG A 296 8222 11997 6690 -1653 -817 1095 C ATOM 824 CG ARG A 296 26.136 -6.205 -14.678 1.00 72.90 C ANISOU 824 CG ARG A 296 8696 12035 6967 -1635 -839 1015 C ATOM 825 CD ARG A 296 25.499 -5.371 -13.600 1.00 74.95 C ANISOU 825 CD ARG A 296 9137 12182 7160 -1626 -908 940 C ATOM 826 NE ARG A 296 24.386 -4.566 -14.108 1.00 88.14 N ANISOU 826 NE ARG A 296 11013 13647 8828 -1561 -926 864 N ATOM 827 CZ ARG A 296 23.688 -3.704 -13.374 1.00108.32 C ANISOU 827 CZ ARG A 296 13768 16075 11312 -1515 -983 787 C ATOM 828 NH1 ARG A 296 23.985 -3.519 -12.095 1.00101.77 N ANISOU 828 NH1 ARG A 296 12967 15292 10409 -1546 -1029 769 N ATOM 829 NH2 ARG A 296 22.691 -3.017 -13.914 1.00 94.45 N ANISOU 829 NH2 ARG A 296 12189 14152 9547 -1422 -993 728 N ATOM 830 N ALA A 297 30.380 -7.312 -14.261 1.00 75.95 N ANISOU 830 N ALA A 297 8496 13166 7197 -1933 -851 1297 N ATOM 831 CA ALA A 297 31.680 -7.668 -13.674 1.00 76.62 C ANISOU 831 CA ALA A 297 8370 13545 7199 -1998 -867 1391 C ATOM 832 C ALA A 297 31.534 -8.482 -12.390 1.00 79.99 C ANISOU 832 C ALA A 297 8727 14032 7635 -1843 -849 1397 C ATOM 833 O ALA A 297 32.417 -9.290 -12.115 1.00 82.31 O ANISOU 833 O ALA A 297 8814 14564 7897 -1775 -816 1484 O ATOM 834 CB ALA A 297 32.493 -6.419 -13.387 1.00 78.61 C ANISOU 834 CB ALA A 297 8673 13881 7314 -2300 -987 1411 C ATOM 835 N ASP A 298 30.418 -8.313 -11.639 1.00 73.63 N ANISOU 835 N ASP A 298 8087 13025 6864 -1769 -864 1311 N ATOM 836 CA ASP A 298 30.185 -8.988 -10.354 1.00 72.76 C ANISOU 836 CA ASP A 298 7933 12961 6751 -1641 -852 1314 C ATOM 837 C ASP A 298 29.416 -10.325 -10.453 1.00 75.13 C ANISOU 837 C ASP A 298 8191 13194 7160 -1391 -744 1319 C ATOM 838 O ASP A 298 29.113 -10.916 -9.415 1.00 76.04 O ANISOU 838 O ASP A 298 8288 13329 7274 -1286 -731 1325 O ATOM 839 CB ASP A 298 29.432 -8.062 -9.368 1.00 74.42 C ANISOU 839 CB ASP A 298 8342 13022 6912 -1701 -929 1222 C ATOM 840 CG ASP A 298 28.117 -7.452 -9.840 1.00 83.95 C ANISOU 840 CG ASP A 298 9766 13962 8170 -1653 -925 1120 C ATOM 841 OD1 ASP A 298 27.578 -7.908 -10.875 1.00 83.29 O ANISOU 841 OD1 ASP A 298 9673 13795 8181 -1554 -853 1116 O ATOM 842 OD2 ASP A 298 27.640 -6.508 -9.187 1.00 88.24 O ANISOU 842 OD2 ASP A 298 10491 14388 8647 -1706 -995 1044 O ATOM 843 N GLY A 299 29.130 -10.805 -11.651 1.00 69.76 N ANISOU 843 N GLY A 299 7505 12440 6560 -1312 -672 1320 N ATOM 844 CA GLY A 299 28.438 -12.083 -11.802 1.00 68.62 C ANISOU 844 CA GLY A 299 7348 12222 6501 -1108 -578 1327 C ATOM 845 C GLY A 299 26.927 -12.035 -11.735 1.00 72.90 C ANISOU 845 C GLY A 299 8040 12555 7105 -1049 -561 1245 C ATOM 846 O GLY A 299 26.282 -13.079 -11.599 1.00 71.83 O ANISOU 846 O GLY A 299 7905 12367 7021 -914 -497 1254 O ATOM 847 N THR A 300 26.357 -10.824 -11.847 1.00 70.99 N ANISOU 847 N THR A 300 7932 12198 6843 -1149 -621 1169 N ATOM 848 CA THR A 300 24.917 -10.562 -11.902 1.00 70.35 C ANISOU 848 CA THR A 300 7985 11947 6798 -1088 -612 1090 C ATOM 849 C THR A 300 24.492 -10.333 -13.382 1.00 76.58 C ANISOU 849 C THR A 300 8830 12628 7641 -1099 -586 1064 C ATOM 850 O THR A 300 25.353 -10.150 -14.261 1.00 75.39 O ANISOU 850 O THR A 300 8636 12522 7487 -1179 -589 1098 O ATOM 851 CB THR A 300 24.528 -9.355 -11.014 1.00 77.64 C ANISOU 851 CB THR A 300 9042 12814 7643 -1148 -695 1021 C ATOM 852 OG1 THR A 300 25.222 -8.189 -11.456 1.00 80.03 O ANISOU 852 OG1 THR A 300 9424 13095 7888 -1310 -770 1008 O ATOM 853 CG2 THR A 300 24.795 -9.585 -9.534 1.00 75.34 C ANISOU 853 CG2 THR A 300 8707 12627 7292 -1131 -719 1039 C ATOM 854 N MET A 301 23.164 -10.338 -13.645 1.00 74.11 N ANISOU 854 N MET A 301 8600 12195 7364 -1021 -562 1008 N ATOM 855 CA MET A 301 22.604 -10.103 -14.975 1.00 73.50 C ANISOU 855 CA MET A 301 8580 12019 7328 -1022 -543 980 C ATOM 856 C MET A 301 22.879 -8.694 -15.469 1.00 81.04 C ANISOU 856 C MET A 301 9651 12905 8234 -1134 -616 948 C ATOM 857 O MET A 301 22.749 -7.739 -14.711 1.00 82.62 O ANISOU 857 O MET A 301 9961 13064 8367 -1167 -684 906 O ATOM 858 CB MET A 301 21.083 -10.323 -14.996 1.00 74.69 C ANISOU 858 CB MET A 301 8780 12098 7503 -919 -514 934 C ATOM 859 CG MET A 301 20.653 -11.756 -14.843 1.00 77.34 C ANISOU 859 CG MET A 301 9031 12469 7884 -843 -440 970 C ATOM 860 SD MET A 301 18.909 -11.941 -15.272 1.00 80.27 S ANISOU 860 SD MET A 301 9440 12791 8268 -777 -410 928 S ATOM 861 CE MET A 301 19.061 -12.471 -16.966 1.00 76.66 C ANISOU 861 CE MET A 301 8978 12279 7871 -811 -367 942 C ATOM 862 N ARG A 302 23.212 -8.563 -16.749 1.00 79.28 N ANISOU 862 N ARG A 302 9428 12660 8035 -1190 -603 965 N ATOM 863 CA ARG A 302 23.411 -7.278 -17.403 1.00 79.79 C ANISOU 863 CA ARG A 302 9622 12642 8052 -1307 -669 944 C ATOM 864 C ARG A 302 22.053 -6.584 -17.520 1.00 82.97 C ANISOU 864 C ARG A 302 10183 12897 8445 -1220 -691 872 C ATOM 865 O ARG A 302 21.136 -7.146 -18.114 1.00 81.94 O ANISOU 865 O ARG A 302 10023 12743 8367 -1116 -638 859 O ATOM 866 CB ARG A 302 24.051 -7.502 -18.773 1.00 79.45 C ANISOU 866 CB ARG A 302 9514 12636 8036 -1372 -634 990 C ATOM 867 CG ARG A 302 25.004 -6.418 -19.170 1.00 86.46 C ANISOU 867 CG ARG A 302 10463 13535 8852 -1561 -704 1017 C ATOM 868 CD ARG A 302 26.361 -7.016 -19.382 1.00 84.17 C ANISOU 868 CD ARG A 302 9988 13445 8548 -1636 -673 1100 C ATOM 869 NE ARG A 302 27.314 -6.017 -19.855 1.00 84.32 N ANISOU 869 NE ARG A 302 10042 13513 8485 -1852 -738 1141 N ATOM 870 CZ ARG A 302 28.566 -6.289 -20.184 1.00 93.39 C ANISOU 870 CZ ARG A 302 11023 14871 9590 -1949 -722 1223 C ATOM 871 NH1 ARG A 302 29.031 -7.526 -20.085 1.00 89.95 N ANISOU 871 NH1 ARG A 302 10389 14599 9187 -1819 -641 1267 N ATOM 872 NH2 ARG A 302 29.363 -5.330 -20.625 1.00 71.45 N ANISOU 872 NH2 ARG A 302 8280 12147 6723 -2175 -786 1267 N ATOM 873 N LEU A 303 21.887 -5.429 -16.872 1.00 80.07 N ANISOU 873 N LEU A 303 9982 12442 7997 -1248 -770 825 N ATOM 874 CA LEU A 303 20.613 -4.709 -16.879 1.00 79.82 C ANISOU 874 CA LEU A 303 10110 12285 7932 -1123 -792 757 C ATOM 875 C LEU A 303 20.809 -3.215 -17.051 1.00 84.15 C ANISOU 875 C LEU A 303 10903 12683 8388 -1208 -886 724 C ATOM 876 O LEU A 303 21.791 -2.664 -16.554 1.00 84.70 O ANISOU 876 O LEU A 303 11039 12749 8395 -1365 -949 736 O ATOM 877 CB LEU A 303 19.842 -4.967 -15.576 1.00 79.76 C ANISOU 877 CB LEU A 303 10089 12318 7898 -986 -781 717 C ATOM 878 CG LEU A 303 19.187 -6.331 -15.406 1.00 82.92 C ANISOU 878 CG LEU A 303 10303 12832 8369 -878 -694 740 C ATOM 879 CD1 LEU A 303 19.047 -6.682 -13.940 1.00 83.08 C ANISOU 879 CD1 LEU A 303 10279 12933 8355 -821 -690 731 C ATOM 880 CD2 LEU A 303 17.864 -6.387 -16.101 1.00 84.46 C ANISOU 880 CD2 LEU A 303 10508 13004 8578 -754 -661 714 C ATOM 881 N GLY A 304 19.863 -2.584 -17.752 1.00 79.97 N ANISOU 881 N GLY A 304 10513 12035 7840 -1106 -897 687 N ATOM 882 CA GLY A 304 19.843 -1.150 -18.020 1.00 80.89 C ANISOU 882 CA GLY A 304 10910 11967 7859 -1148 -985 654 C ATOM 883 C GLY A 304 21.112 -0.635 -18.657 1.00 85.94 C ANISOU 883 C GLY A 304 11609 12571 8473 -1401 -1037 708 C ATOM 884 O GLY A 304 21.583 0.454 -18.317 1.00 87.74 O ANISOU 884 O GLY A 304 12064 12674 8597 -1527 -1129 691 O ATOM 885 N GLU A 305 21.687 -1.452 -19.555 1.00 81.33 N ANISOU 885 N GLU A 305 10822 12108 7971 -1484 -978 774 N ATOM 886 CA GLU A 305 22.916 -1.189 -20.298 1.00 81.46 C ANISOU 886 CA GLU A 305 10822 12163 7968 -1719 -1005 843 C ATOM 887 C GLU A 305 22.624 -0.116 -21.401 1.00 85.86 C ANISOU 887 C GLU A 305 11605 12545 8473 -1767 -1057 843 C ATOM 888 O GLU A 305 21.496 -0.086 -21.889 1.00 83.96 O ANISOU 888 O GLU A 305 11421 12223 8258 -1583 -1031 807 O ATOM 889 CB GLU A 305 23.419 -2.528 -20.884 1.00 81.62 C ANISOU 889 CB GLU A 305 10549 12377 8084 -1718 -909 904 C ATOM 890 CG GLU A 305 24.891 -2.592 -21.257 1.00 96.09 C ANISOU 890 CG GLU A 305 12266 14355 9888 -1936 -917 986 C ATOM 891 CD GLU A 305 25.910 -2.499 -20.134 1.00114.87 C ANISOU 891 CD GLU A 305 14590 16851 12203 -2074 -964 1013 C ATOM 892 OE1 GLU A 305 25.727 -3.175 -19.094 1.00 80.10 O ANISOU 892 OE1 GLU A 305 10091 12515 7830 -1960 -937 992 O ATOM 893 OE2 GLU A 305 26.924 -1.785 -20.320 1.00114.73 O ANISOU 893 OE2 GLU A 305 14613 16880 12098 -2311 -1029 1065 O ATOM 894 N PRO A 306 23.544 0.813 -21.781 1.00 85.45 N ANISOU 894 N PRO A 306 11700 12432 8336 -2008 -1134 887 N ATOM 895 CA PRO A 306 24.951 0.972 -21.341 1.00 87.01 C ANISOU 895 CA PRO A 306 11842 12747 8471 -2277 -1181 944 C ATOM 896 C PRO A 306 25.062 1.409 -19.867 1.00 93.71 C ANISOU 896 C PRO A 306 12813 13551 9244 -2306 -1250 895 C ATOM 897 O PRO A 306 24.465 2.405 -19.443 1.00 94.35 O ANISOU 897 O PRO A 306 13194 13413 9242 -2262 -1324 829 O ATOM 898 CB PRO A 306 25.511 2.029 -22.309 1.00 89.87 C ANISOU 898 CB PRO A 306 12395 13008 8743 -2511 -1254 997 C ATOM 899 CG PRO A 306 24.316 2.779 -22.820 1.00 93.63 C ANISOU 899 CG PRO A 306 13141 13232 9203 -2347 -1279 941 C ATOM 900 CD PRO A 306 23.192 1.787 -22.840 1.00 87.36 C ANISOU 900 CD PRO A 306 12175 12494 8526 -2039 -1181 893 C ATOM 901 N THR A 307 25.800 0.599 -19.083 1.00 91.01 N ANISOU 901 N THR A 307 12234 13423 8924 -2353 -1221 925 N ATOM 902 CA THR A 307 26.069 0.774 -17.651 1.00 91.95 C ANISOU 902 CA THR A 307 12396 13564 8975 -2393 -1275 892 C ATOM 903 C THR A 307 27.506 1.256 -17.496 1.00 98.90 C ANISOU 903 C THR A 307 13264 14564 9749 -2728 -1355 964 C ATOM 904 O THR A 307 28.399 0.730 -18.166 1.00 98.41 O ANISOU 904 O THR A 307 12970 14710 9709 -2847 -1316 1055 O ATOM 905 CB THR A 307 25.808 -0.564 -16.892 1.00 98.68 C ANISOU 905 CB THR A 307 12979 14589 9925 -2193 -1183 885 C ATOM 906 OG1 THR A 307 24.479 -1.028 -17.147 1.00 99.34 O ANISOU 906 OG1 THR A 307 13061 14590 10096 -1923 -1111 832 O ATOM 907 CG2 THR A 307 26.015 -0.454 -15.390 1.00 96.41 C ANISOU 907 CG2 THR A 307 12723 14339 9569 -2213 -1233 851 C ATOM 908 N SER A 308 27.731 2.247 -16.619 1.00 98.46 N ANISOU 908 N SER A 308 13456 14392 9562 -2879 -1467 926 N ATOM 909 CA SER A 308 29.058 2.800 -16.343 1.00100.82 C ANISOU 909 CA SER A 308 13767 14808 9731 -3236 -1562 993 C ATOM 910 C SER A 308 30.004 1.745 -15.756 1.00104.81 C ANISOU 910 C SER A 308 13899 15663 10262 -3277 -1516 1065 C ATOM 911 O SER A 308 29.581 0.913 -14.938 1.00102.75 O ANISOU 911 O SER A 308 13498 15470 10071 -3056 -1457 1028 O ATOM 912 CB SER A 308 28.956 3.980 -15.379 1.00107.49 C ANISOU 912 CB SER A 308 14980 15436 10426 -3360 -1691 918 C ATOM 913 OG SER A 308 28.296 5.088 -15.969 1.00121.37 O ANISOU 913 OG SER A 308 17121 16871 12125 -3359 -1750 868 O ATOM 914 N ASN A 309 31.281 1.776 -16.222 1.00102.63 N ANISOU 914 N ASN A 309 13457 15622 9918 -3555 -1542 1176 N ATOM 915 CA ASN A 309 32.438 0.946 -15.827 1.00102.83 C ANISOU 915 CA ASN A 309 13123 16025 9922 -3642 -1515 1272 C ATOM 916 C ASN A 309 32.357 -0.519 -16.338 1.00103.43 C ANISOU 916 C ASN A 309 12859 16292 10147 -3365 -1365 1312 C ATOM 917 O ASN A 309 33.338 -1.256 -16.182 1.00104.36 O ANISOU 917 O ASN A 309 12675 16733 10243 -3397 -1331 1402 O ATOM 918 CB ASN A 309 32.661 0.947 -14.298 1.00104.03 C ANISOU 918 CB ASN A 309 13280 16245 10003 -3672 -1575 1240 C ATOM 919 CG ASN A 309 32.834 2.324 -13.697 1.00124.89 C ANISOU 919 CG ASN A 309 16267 18709 12476 -3957 -1728 1197 C ATOM 920 OD1 ASN A 309 32.193 2.668 -12.701 1.00120.35 O ANISOU 920 OD1 ASN A 309 15906 17950 11871 -3866 -1772 1098 O ATOM 921 ND2 ASN A 309 33.670 3.160 -14.304 1.00117.35 N ANISOU 921 ND2 ASN A 309 15397 17792 11396 -4310 -1814 1268 N ATOM 922 N GLU A 310 31.241 -0.921 -16.977 1.00 95.44 N ANISOU 922 N GLU A 310 11903 15094 9266 -3103 -1282 1253 N ATOM 923 CA GLU A 310 31.089 -2.258 -17.566 1.00 92.18 C ANISOU 923 CA GLU A 310 11230 14813 8982 -2860 -1148 1282 C ATOM 924 C GLU A 310 31.641 -2.247 -18.992 1.00 94.65 C ANISOU 924 C GLU A 310 11448 15225 9288 -2960 -1112 1356 C ATOM 925 O GLU A 310 31.644 -1.181 -19.615 1.00 95.08 O ANISOU 925 O GLU A 310 11702 15145 9277 -3153 -1181 1358 O ATOM 926 CB GLU A 310 29.613 -2.706 -17.559 1.00 91.36 C ANISOU 926 CB GLU A 310 11227 14484 9003 -2564 -1083 1187 C ATOM 927 CG GLU A 310 28.985 -2.867 -16.184 1.00 96.52 C ANISOU 927 CG GLU A 310 11940 15069 9663 -2430 -1098 1118 C ATOM 928 CD GLU A 310 29.520 -3.986 -15.305 1.00110.29 C ANISOU 928 CD GLU A 310 13433 17043 11428 -2339 -1049 1164 C ATOM 929 OE1 GLU A 310 30.069 -4.974 -15.847 1.00101.25 O ANISOU 929 OE1 GLU A 310 12055 16083 10331 -2269 -968 1235 O ATOM 930 OE2 GLU A 310 29.377 -3.872 -14.065 1.00 98.00 O ANISOU 930 OE2 GLU A 310 11928 15478 9831 -2322 -1092 1128 O ATOM 931 N THR A 311 32.089 -3.420 -19.523 1.00 89.53 N ANISOU 931 N THR A 311 10519 14801 8698 -2821 -1004 1416 N ATOM 932 CA THR A 311 32.619 -3.541 -20.904 1.00 88.95 C ANISOU 932 CA THR A 311 10331 14852 8613 -2880 -953 1485 C ATOM 933 C THR A 311 31.530 -3.232 -21.955 1.00 92.73 C ANISOU 933 C THR A 311 11007 15058 9168 -2796 -930 1422 C ATOM 934 O THR A 311 30.352 -3.138 -21.611 1.00 90.87 O ANISOU 934 O THR A 311 10949 14574 9003 -2647 -935 1330 O ATOM 935 CB THR A 311 33.219 -4.934 -21.180 1.00 86.62 C ANISOU 935 CB THR A 311 9726 14829 8357 -2688 -836 1546 C ATOM 936 OG1 THR A 311 32.200 -5.939 -21.116 1.00 85.86 O ANISOU 936 OG1 THR A 311 9645 14582 8395 -2385 -749 1475 O ATOM 937 CG2 THR A 311 34.391 -5.261 -20.286 1.00 77.62 C ANISOU 937 CG2 THR A 311 8358 14008 7125 -2754 -854 1628 C ATOM 938 N LEU A 312 31.920 -3.095 -23.236 1.00 91.43 N ANISOU 938 N LEU A 312 10796 14966 8978 -2883 -902 1477 N ATOM 939 CA LEU A 312 30.976 -2.762 -24.305 1.00 90.45 C ANISOU 939 CA LEU A 312 10849 14611 8908 -2822 -885 1431 C ATOM 940 C LEU A 312 30.408 -4.000 -25.035 1.00 92.16 C ANISOU 940 C LEU A 312 10936 14840 9240 -2547 -759 1404 C ATOM 941 O LEU A 312 29.572 -3.829 -25.917 1.00 91.80 O ANISOU 941 O LEU A 312 11016 14624 9240 -2482 -742 1365 O ATOM 942 CB LEU A 312 31.639 -1.822 -25.323 1.00 92.21 C ANISOU 942 CB LEU A 312 11132 14877 9025 -3091 -934 1505 C ATOM 943 CG LEU A 312 31.954 -0.402 -24.837 1.00 99.05 C ANISOU 943 CG LEU A 312 12235 15634 9767 -3394 -1075 1521 C ATOM 944 CD1 LEU A 312 32.579 0.419 -25.949 1.00100.99 C ANISOU 944 CD1 LEU A 312 12539 15925 9906 -3667 -1116 1607 C ATOM 945 CD2 LEU A 312 30.701 0.310 -24.313 1.00100.92 C ANISOU 945 CD2 LEU A 312 12803 15503 10038 -3298 -1139 1412 C ATOM 946 N SER A 313 30.792 -5.228 -24.631 1.00 87.36 N ANISOU 946 N SER A 313 10107 14415 8671 -2383 -678 1422 N ATOM 947 CA SER A 313 30.347 -6.488 -25.247 1.00 85.58 C ANISOU 947 CA SER A 313 9783 14196 8537 -2135 -563 1398 C ATOM 948 C SER A 313 28.816 -6.599 -25.378 1.00 87.33 C ANISOU 948 C SER A 313 10181 14142 8859 -1982 -551 1301 C ATOM 949 O SER A 313 28.325 -7.115 -26.386 1.00 85.26 O ANISOU 949 O SER A 313 9921 13832 8644 -1877 -487 1281 O ATOM 950 CB SER A 313 30.866 -7.684 -24.457 1.00 88.37 C ANISOU 950 CB SER A 313 9944 14727 8907 -1973 -500 1423 C ATOM 951 OG SER A 313 32.285 -7.726 -24.496 1.00 97.47 O ANISOU 951 OG SER A 313 10891 16187 9955 -2074 -495 1522 O ATOM 952 N CYS A 314 28.073 -6.087 -24.394 1.00 83.92 N ANISOU 952 N CYS A 314 9892 13550 8444 -1974 -615 1245 N ATOM 953 CA CYS A 314 26.613 -6.153 -24.390 1.00 82.55 C ANISOU 953 CA CYS A 314 9858 13162 8344 -1825 -607 1162 C ATOM 954 C CYS A 314 25.992 -5.223 -25.467 1.00 86.36 C ANISOU 954 C CYS A 314 10514 13490 8811 -1884 -644 1142 C ATOM 955 O CYS A 314 25.134 -5.677 -26.237 1.00 84.04 O ANISOU 955 O CYS A 314 10234 13126 8572 -1761 -594 1109 O ATOM 956 CB CYS A 314 26.082 -5.817 -23.001 1.00 82.64 C ANISOU 956 CB CYS A 314 9962 13085 8353 -1790 -663 1113 C ATOM 957 SG CYS A 314 24.282 -5.934 -22.831 1.00 85.58 S ANISOU 957 SG CYS A 314 10464 13262 8792 -1593 -650 1022 S ATOM 958 N VAL A 315 26.419 -3.940 -25.516 1.00 84.36 N ANISOU 958 N VAL A 315 10400 13181 8471 -2077 -734 1165 N ATOM 959 CA VAL A 315 25.850 -2.944 -26.437 1.00 84.40 C ANISOU 959 CA VAL A 315 10607 13016 8444 -2131 -781 1154 C ATOM 960 C VAL A 315 26.130 -3.339 -27.914 1.00 85.01 C ANISOU 960 C VAL A 315 10589 13181 8531 -2150 -718 1198 C ATOM 961 O VAL A 315 25.198 -3.286 -28.710 1.00 84.07 O ANISOU 961 O VAL A 315 10555 12944 8443 -2054 -703 1165 O ATOM 962 CB VAL A 315 26.280 -1.473 -26.136 1.00 90.51 C ANISOU 962 CB VAL A 315 11600 13683 9107 -2350 -900 1173 C ATOM 963 CG1 VAL A 315 25.848 -1.055 -24.727 1.00 90.45 C ANISOU 963 CG1 VAL A 315 11726 13562 9080 -2302 -962 1111 C ATOM 964 CG2 VAL A 315 27.779 -1.242 -26.330 1.00 91.75 C ANISOU 964 CG2 VAL A 315 11650 14035 9178 -2611 -923 1268 C ATOM 965 N ILE A 316 27.356 -3.809 -28.240 1.00 79.87 N ANISOU 965 N ILE A 316 9746 12754 7846 -2248 -675 1271 N ATOM 966 CA ILE A 316 27.789 -4.232 -29.578 1.00 78.99 C ANISOU 966 CA ILE A 316 9523 12765 7723 -2261 -607 1317 C ATOM 967 C ILE A 316 26.860 -5.345 -30.109 1.00 79.92 C ANISOU 967 C ILE A 316 9596 12836 7935 -2028 -518 1258 C ATOM 968 O ILE A 316 26.359 -5.219 -31.227 1.00 79.97 O ANISOU 968 O ILE A 316 9666 12776 7943 -2012 -502 1249 O ATOM 969 CB ILE A 316 29.283 -4.676 -29.555 1.00 82.95 C ANISOU 969 CB ILE A 316 9794 13565 8160 -2359 -569 1404 C ATOM 970 CG1 ILE A 316 30.202 -3.481 -29.224 1.00 84.89 C ANISOU 970 CG1 ILE A 316 10090 13876 8286 -2650 -668 1475 C ATOM 971 CG2 ILE A 316 29.713 -5.341 -30.876 1.00 83.07 C ANISOU 971 CG2 ILE A 316 9671 13735 8158 -2311 -476 1442 C ATOM 972 CD1 ILE A 316 31.560 -3.865 -28.643 1.00 94.32 C ANISOU 972 CD1 ILE A 316 11047 15382 9409 -2740 -654 1554 C ATOM 973 N ILE A 317 26.610 -6.387 -29.298 1.00 73.75 N ANISOU 973 N ILE A 317 8722 12081 7220 -1866 -468 1221 N ATOM 974 CA ILE A 317 25.744 -7.531 -29.612 1.00 72.00 C ANISOU 974 CA ILE A 317 8471 11809 7075 -1672 -391 1167 C ATOM 975 C ILE A 317 24.299 -7.038 -29.800 1.00 75.31 C ANISOU 975 C ILE A 317 9056 12031 7529 -1620 -432 1105 C ATOM 976 O ILE A 317 23.656 -7.453 -30.765 1.00 75.56 O ANISOU 976 O ILE A 317 9102 12026 7581 -1554 -392 1081 O ATOM 977 CB ILE A 317 25.869 -8.654 -28.523 1.00 74.33 C ANISOU 977 CB ILE A 317 8660 12168 7416 -1541 -344 1155 C ATOM 978 CG1 ILE A 317 27.285 -9.306 -28.554 1.00 75.15 C ANISOU 978 CG1 ILE A 317 8582 12498 7473 -1539 -288 1223 C ATOM 979 CG2 ILE A 317 24.767 -9.735 -28.622 1.00 73.65 C ANISOU 979 CG2 ILE A 317 8597 11986 7401 -1375 -287 1095 C ATOM 980 CD1 ILE A 317 27.793 -9.847 -29.986 1.00 76.52 C ANISOU 980 CD1 ILE A 317 8683 12779 7612 -1505 -209 1248 C ATOM 981 N PHE A 318 23.810 -6.141 -28.917 1.00 71.15 N ANISOU 981 N PHE A 318 8651 11391 6990 -1643 -510 1080 N ATOM 982 CA PHE A 318 22.482 -5.534 -29.034 1.00 70.17 C ANISOU 982 CA PHE A 318 8682 11106 6874 -1570 -554 1029 C ATOM 983 C PHE A 318 22.373 -4.774 -30.377 1.00 76.58 C ANISOU 983 C PHE A 318 9596 11861 7641 -1641 -578 1052 C ATOM 984 O PHE A 318 21.423 -5.004 -31.133 1.00 76.24 O ANISOU 984 O PHE A 318 9576 11775 7617 -1548 -557 1024 O ATOM 985 CB PHE A 318 22.169 -4.591 -27.836 1.00 71.82 C ANISOU 985 CB PHE A 318 9026 11211 7050 -1573 -635 1002 C ATOM 986 CG PHE A 318 21.134 -3.535 -28.171 1.00 73.18 C ANISOU 986 CG PHE A 318 9399 11223 7183 -1522 -698 970 C ATOM 987 CD1 PHE A 318 19.775 -3.858 -28.230 1.00 75.38 C ANISOU 987 CD1 PHE A 318 9681 11468 7491 -1346 -678 922 C ATOM 988 CD2 PHE A 318 21.522 -2.240 -28.512 1.00 75.40 C ANISOU 988 CD2 PHE A 318 9866 11398 7383 -1650 -777 997 C ATOM 989 CE1 PHE A 318 18.824 -2.898 -28.606 1.00 76.06 C ANISOU 989 CE1 PHE A 318 9938 11435 7526 -1266 -732 901 C ATOM 990 CE2 PHE A 318 20.573 -1.290 -28.916 1.00 78.55 C ANISOU 990 CE2 PHE A 318 10471 11639 7735 -1573 -833 974 C ATOM 991 CZ PHE A 318 19.236 -1.631 -28.978 1.00 75.92 C ANISOU 991 CZ PHE A 318 10121 11294 7432 -1366 -807 927 C ATOM 992 N VAL A 319 23.357 -3.882 -30.662 1.00 73.59 N ANISOU 992 N VAL A 319 9273 11495 7191 -1820 -626 1109 N ATOM 993 CA VAL A 319 23.414 -3.045 -31.865 1.00 73.90 C ANISOU 993 CA VAL A 319 9427 11480 7170 -1922 -659 1147 C ATOM 994 C VAL A 319 23.307 -3.933 -33.121 1.00 79.09 C ANISOU 994 C VAL A 319 9966 12230 7856 -1864 -575 1153 C ATOM 995 O VAL A 319 22.429 -3.689 -33.942 1.00 79.85 O ANISOU 995 O VAL A 319 10151 12242 7948 -1806 -585 1135 O ATOM 996 CB VAL A 319 24.680 -2.135 -31.888 1.00 77.72 C ANISOU 996 CB VAL A 319 9959 12009 7563 -2167 -716 1224 C ATOM 997 CG1 VAL A 319 24.933 -1.557 -33.278 1.00 77.55 C ANISOU 997 CG1 VAL A 319 10004 11985 7477 -2289 -727 1282 C ATOM 998 CG2 VAL A 319 24.564 -1.011 -30.853 1.00 77.79 C ANISOU 998 CG2 VAL A 319 10177 11860 7520 -2237 -821 1208 C ATOM 999 N ILE A 320 24.143 -4.977 -33.233 1.00 75.25 N ANISOU 999 N ILE A 320 9289 11916 7388 -1861 -495 1173 N ATOM 1000 CA ILE A 320 24.140 -5.917 -34.352 1.00 74.29 C ANISOU 1000 CA ILE A 320 9068 11880 7277 -1795 -409 1170 C ATOM 1001 C ILE A 320 22.742 -6.574 -34.507 1.00 77.51 C ANISOU 1001 C ILE A 320 9513 12191 7747 -1633 -386 1097 C ATOM 1002 O ILE A 320 22.134 -6.419 -35.558 1.00 76.98 O ANISOU 1002 O ILE A 320 9504 12084 7662 -1622 -387 1088 O ATOM 1003 CB ILE A 320 25.256 -6.987 -34.176 1.00 77.43 C ANISOU 1003 CB ILE A 320 9275 12470 7675 -1768 -326 1196 C ATOM 1004 CG1 ILE A 320 26.666 -6.339 -34.198 1.00 78.68 C ANISOU 1004 CG1 ILE A 320 9360 12789 7746 -1947 -347 1284 C ATOM 1005 CG2 ILE A 320 25.138 -8.075 -35.253 1.00 78.49 C ANISOU 1005 CG2 ILE A 320 9345 12662 7814 -1662 -234 1173 C ATOM 1006 CD1 ILE A 320 27.803 -7.208 -33.607 1.00 79.47 C ANISOU 1006 CD1 ILE A 320 9260 13104 7830 -1906 -285 1320 C ATOM 1007 N VAL A 321 22.229 -7.256 -33.454 1.00 73.18 N ANISOU 1007 N VAL A 321 8928 11618 7258 -1526 -372 1051 N ATOM 1008 CA VAL A 321 20.964 -7.997 -33.479 1.00 71.37 C ANISOU 1008 CA VAL A 321 8708 11335 7075 -1402 -349 993 C ATOM 1009 C VAL A 321 19.771 -7.061 -33.748 1.00 76.61 C ANISOU 1009 C VAL A 321 9496 11896 7718 -1376 -417 973 C ATOM 1010 O VAL A 321 19.000 -7.337 -34.669 1.00 77.17 O ANISOU 1010 O VAL A 321 9577 11964 7780 -1340 -403 955 O ATOM 1011 CB VAL A 321 20.746 -8.835 -32.187 1.00 73.19 C ANISOU 1011 CB VAL A 321 8877 11573 7358 -1319 -326 964 C ATOM 1012 CG1 VAL A 321 19.310 -9.373 -32.093 1.00 71.92 C ANISOU 1012 CG1 VAL A 321 8736 11366 7224 -1229 -323 914 C ATOM 1013 CG2 VAL A 321 21.750 -9.985 -32.115 1.00 72.84 C ANISOU 1013 CG2 VAL A 321 8722 11627 7326 -1295 -248 981 C ATOM 1014 N TYR A 322 19.609 -5.989 -32.958 1.00 73.20 N ANISOU 1014 N TYR A 322 9164 11385 7266 -1383 -490 976 N ATOM 1015 CA TYR A 322 18.480 -5.071 -33.107 1.00 72.34 C ANISOU 1015 CA TYR A 322 9186 11179 7120 -1313 -554 959 C ATOM 1016 C TYR A 322 18.526 -4.337 -34.454 1.00 76.92 C ANISOU 1016 C TYR A 322 9859 11723 7644 -1374 -581 995 C ATOM 1017 O TYR A 322 17.513 -4.337 -35.153 1.00 77.19 O ANISOU 1017 O TYR A 322 9915 11752 7662 -1293 -587 981 O ATOM 1018 CB TYR A 322 18.417 -4.059 -31.947 1.00 72.58 C ANISOU 1018 CB TYR A 322 9338 11115 7122 -1294 -626 950 C ATOM 1019 CG TYR A 322 17.240 -3.112 -32.033 1.00 72.94 C ANISOU 1019 CG TYR A 322 9535 11064 7114 -1173 -688 930 C ATOM 1020 CD1 TYR A 322 17.379 -1.843 -32.591 1.00 75.32 C ANISOU 1020 CD1 TYR A 322 10032 11244 7341 -1217 -758 961 C ATOM 1021 CD2 TYR A 322 15.978 -3.495 -31.589 1.00 72.74 C ANISOU 1021 CD2 TYR A 322 9458 11083 7098 -1008 -678 888 C ATOM 1022 CE1 TYR A 322 16.291 -0.982 -32.711 1.00 76.10 C ANISOU 1022 CE1 TYR A 322 10284 11252 7376 -1068 -814 947 C ATOM 1023 CE2 TYR A 322 14.886 -2.637 -31.690 1.00 74.39 C ANISOU 1023 CE2 TYR A 322 9785 11239 7239 -863 -730 876 C ATOM 1024 CZ TYR A 322 15.045 -1.380 -32.253 1.00 80.95 C ANISOU 1024 CZ TYR A 322 10824 11936 7997 -877 -798 903 C ATOM 1025 OH TYR A 322 13.967 -0.529 -32.352 1.00 78.78 O ANISOU 1025 OH TYR A 322 10683 11607 7643 -697 -849 894 O ATOM 1026 N TYR A 323 19.665 -3.708 -34.808 1.00 74.08 N ANISOU 1026 N TYR A 323 9548 11354 7243 -1524 -601 1049 N ATOM 1027 CA TYR A 323 19.778 -2.961 -36.061 1.00 75.45 C ANISOU 1027 CA TYR A 323 9822 11494 7353 -1602 -629 1095 C ATOM 1028 C TYR A 323 19.459 -3.862 -37.259 1.00 80.65 C ANISOU 1028 C TYR A 323 10375 12246 8023 -1567 -562 1086 C ATOM 1029 O TYR A 323 18.681 -3.449 -38.122 1.00 80.98 O ANISOU 1029 O TYR A 323 10496 12247 8026 -1524 -590 1091 O ATOM 1030 CB TYR A 323 21.166 -2.316 -36.228 1.00 77.48 C ANISOU 1030 CB TYR A 323 10113 11771 7554 -1805 -651 1165 C ATOM 1031 CG TYR A 323 21.273 -1.414 -37.440 1.00 80.47 C ANISOU 1031 CG TYR A 323 10625 12099 7852 -1906 -691 1224 C ATOM 1032 CD1 TYR A 323 20.940 -0.064 -37.361 1.00 83.89 C ANISOU 1032 CD1 TYR A 323 11304 12354 8216 -1935 -789 1247 C ATOM 1033 CD2 TYR A 323 21.727 -1.904 -38.663 1.00 80.70 C ANISOU 1033 CD2 TYR A 323 10550 12251 7860 -1967 -632 1258 C ATOM 1034 CE1 TYR A 323 21.017 0.766 -38.479 1.00 85.58 C ANISOU 1034 CE1 TYR A 323 11661 12507 8347 -2028 -830 1310 C ATOM 1035 CE2 TYR A 323 21.807 -1.084 -39.786 1.00 82.25 C ANISOU 1035 CE2 TYR A 323 10868 12409 7975 -2064 -668 1319 C ATOM 1036 CZ TYR A 323 21.448 0.250 -39.689 1.00 89.23 C ANISOU 1036 CZ TYR A 323 11998 13109 8795 -2099 -769 1349 C ATOM 1037 OH TYR A 323 21.557 1.070 -40.782 1.00 89.34 O ANISOU 1037 OH TYR A 323 12151 13072 8720 -2202 -809 1419 O ATOM 1038 N ALA A 324 20.039 -5.087 -37.295 1.00 76.39 N ANISOU 1038 N ALA A 324 9673 11825 7525 -1572 -478 1072 N ATOM 1039 CA ALA A 324 19.826 -6.058 -38.369 1.00 75.34 C ANISOU 1039 CA ALA A 324 9462 11770 7393 -1541 -411 1053 C ATOM 1040 C ALA A 324 18.358 -6.527 -38.421 1.00 79.69 C ANISOU 1040 C ALA A 324 10018 12294 7965 -1423 -416 998 C ATOM 1041 O ALA A 324 17.800 -6.684 -39.518 1.00 80.26 O ANISOU 1041 O ALA A 324 10103 12390 8003 -1415 -410 992 O ATOM 1042 CB ALA A 324 20.748 -7.245 -38.189 1.00 75.24 C ANISOU 1042 CB ALA A 324 9312 11866 7408 -1540 -324 1045 C ATOM 1043 N LEU A 325 17.730 -6.721 -37.245 1.00 74.50 N ANISOU 1043 N LEU A 325 9345 11609 7353 -1343 -432 963 N ATOM 1044 CA LEU A 325 16.341 -7.160 -37.158 1.00 73.21 C ANISOU 1044 CA LEU A 325 9161 11461 7195 -1247 -440 922 C ATOM 1045 C LEU A 325 15.399 -6.075 -37.703 1.00 77.33 C ANISOU 1045 C LEU A 325 9779 11948 7655 -1193 -511 939 C ATOM 1046 O LEU A 325 14.474 -6.403 -38.455 1.00 77.74 O ANISOU 1046 O LEU A 325 9803 12059 7676 -1159 -511 926 O ATOM 1047 CB LEU A 325 15.968 -7.536 -35.707 1.00 72.31 C ANISOU 1047 CB LEU A 325 9001 11347 7128 -1181 -440 893 C ATOM 1048 CG LEU A 325 14.487 -7.887 -35.421 1.00 76.27 C ANISOU 1048 CG LEU A 325 9462 11900 7619 -1092 -454 863 C ATOM 1049 CD1 LEU A 325 14.090 -9.186 -36.080 1.00 75.53 C ANISOU 1049 CD1 LEU A 325 9297 11874 7526 -1133 -403 839 C ATOM 1050 CD2 LEU A 325 14.212 -7.953 -33.919 1.00 77.25 C ANISOU 1050 CD2 LEU A 325 9555 12025 7771 -1028 -462 846 C ATOM 1051 N MET A 326 15.656 -4.799 -37.356 1.00 73.25 N ANISOU 1051 N MET A 326 9388 11337 7108 -1188 -574 969 N ATOM 1052 CA MET A 326 14.805 -3.684 -37.758 1.00 74.00 C ANISOU 1052 CA MET A 326 9612 11374 7132 -1102 -645 988 C ATOM 1053 C MET A 326 15.056 -3.256 -39.209 1.00 78.65 C ANISOU 1053 C MET A 326 10265 11953 7663 -1174 -657 1034 C ATOM 1054 O MET A 326 14.084 -2.923 -39.896 1.00 78.51 O ANISOU 1054 O MET A 326 10284 11955 7589 -1088 -690 1043 O ATOM 1055 CB MET A 326 14.966 -2.488 -36.818 1.00 77.05 C ANISOU 1055 CB MET A 326 10158 11629 7490 -1062 -713 998 C ATOM 1056 CG MET A 326 14.403 -2.745 -35.441 1.00 80.45 C ANISOU 1056 CG MET A 326 10540 12079 7951 -948 -712 952 C ATOM 1057 SD MET A 326 12.612 -3.027 -35.388 1.00 84.49 S ANISOU 1057 SD MET A 326 10967 12710 8424 -745 -718 923 S ATOM 1058 CE MET A 326 12.523 -4.236 -34.144 1.00 80.12 C ANISOU 1058 CE MET A 326 10242 12254 7945 -746 -660 880 C ATOM 1059 N ALA A 327 16.325 -3.281 -39.691 1.00 74.82 N ANISOU 1059 N ALA A 327 9782 11466 7182 -1327 -628 1068 N ATOM 1060 CA ALA A 327 16.609 -2.933 -41.093 1.00 74.67 C ANISOU 1060 CA ALA A 327 9812 11458 7099 -1408 -632 1117 C ATOM 1061 C ALA A 327 15.966 -3.966 -42.026 1.00 78.19 C ANISOU 1061 C ALA A 327 10143 12020 7544 -1374 -581 1085 C ATOM 1062 O ALA A 327 15.406 -3.592 -43.050 1.00 79.22 O ANISOU 1062 O ALA A 327 10325 12164 7611 -1355 -610 1109 O ATOM 1063 CB ALA A 327 18.104 -2.825 -41.341 1.00 75.26 C ANISOU 1063 CB ALA A 327 9879 11553 7164 -1580 -604 1164 C ATOM 1064 N GLY A 328 15.952 -5.223 -41.598 1.00 73.65 N ANISOU 1064 N GLY A 328 9435 11519 7030 -1361 -517 1031 N ATOM 1065 CA GLY A 328 15.343 -6.323 -42.329 1.00 73.29 C ANISOU 1065 CA GLY A 328 9304 11566 6977 -1349 -473 990 C ATOM 1066 C GLY A 328 13.845 -6.179 -42.499 1.00 78.13 C ANISOU 1066 C GLY A 328 9917 12220 7551 -1256 -523 978 C ATOM 1067 O GLY A 328 13.318 -6.553 -43.549 1.00 78.44 O ANISOU 1067 O GLY A 328 9934 12332 7538 -1274 -518 971 O ATOM 1068 N VAL A 329 13.143 -5.617 -41.489 1.00 75.45 N ANISOU 1068 N VAL A 329 9596 11853 7220 -1151 -572 976 N ATOM 1069 CA VAL A 329 11.682 -5.463 -41.566 1.00 76.36 C ANISOU 1069 CA VAL A 329 9680 12052 7280 -1037 -617 973 C ATOM 1070 C VAL A 329 11.312 -4.166 -42.328 1.00 81.30 C ANISOU 1070 C VAL A 329 10430 12641 7819 -963 -687 1027 C ATOM 1071 O VAL A 329 10.281 -4.159 -42.982 1.00 81.69 O ANISOU 1071 O VAL A 329 10440 12798 7799 -898 -716 1037 O ATOM 1072 CB VAL A 329 10.932 -5.559 -40.208 1.00 80.87 C ANISOU 1072 CB VAL A 329 10193 12659 7875 -930 -630 947 C ATOM 1073 CG1 VAL A 329 11.045 -6.961 -39.611 1.00 79.88 C ANISOU 1073 CG1 VAL A 329 9947 12588 7814 -1006 -567 901 C ATOM 1074 CG2 VAL A 329 11.391 -4.501 -39.209 1.00 81.00 C ANISOU 1074 CG2 VAL A 329 10325 12545 7907 -858 -666 960 C ATOM 1075 N VAL A 330 12.145 -3.104 -42.286 1.00 79.34 N ANISOU 1075 N VAL A 330 10336 12247 7563 -984 -718 1068 N ATOM 1076 CA VAL A 330 11.895 -1.857 -43.045 1.00 80.16 C ANISOU 1076 CA VAL A 330 10602 12280 7574 -925 -788 1128 C ATOM 1077 C VAL A 330 12.094 -2.182 -44.544 1.00 83.41 C ANISOU 1077 C VAL A 330 10986 12762 7944 -1029 -766 1155 C ATOM 1078 O VAL A 330 11.368 -1.646 -45.390 1.00 84.07 O ANISOU 1078 O VAL A 330 11123 12880 7942 -955 -814 1193 O ATOM 1079 CB VAL A 330 12.743 -0.628 -42.576 1.00 84.41 C ANISOU 1079 CB VAL A 330 11350 12623 8099 -954 -836 1169 C ATOM 1080 CG1 VAL A 330 12.365 0.633 -43.354 1.00 85.60 C ANISOU 1080 CG1 VAL A 330 11704 12680 8141 -879 -913 1235 C ATOM 1081 CG2 VAL A 330 12.567 -0.373 -41.082 1.00 83.81 C ANISOU 1081 CG2 VAL A 330 11308 12481 8057 -853 -854 1132 C ATOM 1082 N TRP A 331 13.029 -3.116 -44.856 1.00 78.67 N ANISOU 1082 N TRP A 331 10297 12200 7394 -1181 -692 1132 N ATOM 1083 CA TRP A 331 13.247 -3.608 -46.220 1.00 78.24 C ANISOU 1083 CA TRP A 331 10205 12228 7294 -1274 -658 1141 C ATOM 1084 C TRP A 331 12.030 -4.409 -46.682 1.00 83.53 C ANISOU 1084 C TRP A 331 10768 13039 7931 -1221 -657 1102 C ATOM 1085 O TRP A 331 11.725 -4.394 -47.864 1.00 85.04 O ANISOU 1085 O TRP A 331 10966 13298 8047 -1246 -669 1122 O ATOM 1086 CB TRP A 331 14.528 -4.452 -46.347 1.00 75.98 C ANISOU 1086 CB TRP A 331 9852 11961 7055 -1410 -573 1119 C ATOM 1087 CG TRP A 331 15.787 -3.663 -46.591 1.00 77.25 C ANISOU 1087 CG TRP A 331 10098 12059 7193 -1519 -573 1184 C ATOM 1088 CD1 TRP A 331 16.841 -3.521 -45.739 1.00 79.71 C ANISOU 1088 CD1 TRP A 331 10408 12325 7552 -1587 -555 1196 C ATOM 1089 CD2 TRP A 331 16.129 -2.923 -47.779 1.00 78.17 C ANISOU 1089 CD2 TRP A 331 10305 12175 7221 -1596 -596 1254 C ATOM 1090 NE1 TRP A 331 17.813 -2.735 -46.312 1.00 79.67 N ANISOU 1090 NE1 TRP A 331 10481 12303 7489 -1715 -566 1272 N ATOM 1091 CE2 TRP A 331 17.396 -2.338 -47.557 1.00 81.79 C ANISOU 1091 CE2 TRP A 331 10814 12589 7673 -1723 -591 1310 C ATOM 1092 CE3 TRP A 331 15.461 -2.648 -48.988 1.00 80.27 C ANISOU 1092 CE3 TRP A 331 10616 12483 7401 -1575 -626 1283 C ATOM 1093 CZ2 TRP A 331 18.022 -1.517 -48.505 1.00 82.24 C ANISOU 1093 CZ2 TRP A 331 10967 12639 7640 -1845 -613 1397 C ATOM 1094 CZ3 TRP A 331 16.094 -1.848 -49.935 1.00 82.79 C ANISOU 1094 CZ3 TRP A 331 11035 12784 7636 -1678 -645 1365 C ATOM 1095 CH2 TRP A 331 17.356 -1.289 -49.687 1.00 83.60 C ANISOU 1095 CH2 TRP A 331 11191 12839 7734 -1816 -637 1423 C ATOM 1096 N PHE A 332 11.319 -5.084 -45.757 1.00 81.20 N ANISOU 1096 N PHE A 332 10373 12800 7680 -1163 -649 1052 N ATOM 1097 CA PHE A 332 10.105 -5.841 -46.082 1.00 81.62 C ANISOU 1097 CA PHE A 332 10315 13009 7686 -1143 -658 1022 C ATOM 1098 C PHE A 332 9.025 -4.879 -46.586 1.00 86.78 C ANISOU 1098 C PHE A 332 10997 13738 8239 -1015 -737 1076 C ATOM 1099 O PHE A 332 8.395 -5.188 -47.590 1.00 87.31 O ANISOU 1099 O PHE A 332 11015 13932 8228 -1044 -753 1082 O ATOM 1100 CB PHE A 332 9.597 -6.689 -44.892 1.00 82.78 C ANISOU 1100 CB PHE A 332 10355 13209 7890 -1125 -636 973 C ATOM 1101 CG PHE A 332 8.162 -7.147 -45.040 1.00 85.02 C ANISOU 1101 CG PHE A 332 10524 13680 8101 -1098 -669 966 C ATOM 1102 CD1 PHE A 332 7.824 -8.155 -45.932 1.00 87.64 C ANISOU 1102 CD1 PHE A 332 10802 14115 8383 -1224 -652 937 C ATOM 1103 CD2 PHE A 332 7.141 -6.539 -44.314 1.00 88.58 C ANISOU 1103 CD2 PHE A 332 10922 14221 8513 -946 -721 991 C ATOM 1104 CE1 PHE A 332 6.493 -8.552 -46.091 1.00 89.68 C ANISOU 1104 CE1 PHE A 332 10944 14574 8555 -1232 -692 940 C ATOM 1105 CE2 PHE A 332 5.806 -6.936 -44.478 1.00 92.05 C ANISOU 1105 CE2 PHE A 332 11225 14886 8864 -928 -753 998 C ATOM 1106 CZ PHE A 332 5.494 -7.949 -45.355 1.00 89.94 C ANISOU 1106 CZ PHE A 332 10894 14730 8550 -1088 -741 975 C ATOM 1107 N VAL A 333 8.845 -3.710 -45.922 1.00 84.27 N ANISOU 1107 N VAL A 333 10772 13336 7909 -868 -790 1114 N ATOM 1108 CA VAL A 333 7.897 -2.660 -46.343 1.00 86.12 C ANISOU 1108 CA VAL A 333 11069 13618 8036 -698 -867 1173 C ATOM 1109 C VAL A 333 8.297 -2.144 -47.750 1.00 90.81 C ANISOU 1109 C VAL A 333 11769 14173 8561 -761 -888 1227 C ATOM 1110 O VAL A 333 7.412 -1.905 -48.578 1.00 92.06 O ANISOU 1110 O VAL A 333 11905 14457 8617 -684 -933 1265 O ATOM 1111 CB VAL A 333 7.802 -1.501 -45.312 1.00 90.77 C ANISOU 1111 CB VAL A 333 11792 14077 8619 -519 -915 1195 C ATOM 1112 CG1 VAL A 333 7.074 -0.284 -45.884 1.00 92.60 C ANISOU 1112 CG1 VAL A 333 12155 14304 8726 -328 -994 1265 C ATOM 1113 CG2 VAL A 333 7.108 -1.967 -44.062 1.00 90.00 C ANISOU 1113 CG2 VAL A 333 11565 14077 8552 -423 -901 1150 C ATOM 1114 N VAL A 334 9.624 -2.012 -48.012 1.00 85.88 N ANISOU 1114 N VAL A 334 11245 13403 7984 -905 -854 1237 N ATOM 1115 CA VAL A 334 10.185 -1.572 -49.296 1.00 85.96 C ANISOU 1115 CA VAL A 334 11353 13380 7930 -996 -862 1293 C ATOM 1116 C VAL A 334 9.858 -2.647 -50.358 1.00 89.52 C ANISOU 1116 C VAL A 334 11667 14004 8343 -1088 -825 1261 C ATOM 1117 O VAL A 334 9.430 -2.281 -51.455 1.00 90.22 O ANISOU 1117 O VAL A 334 11789 14159 8331 -1071 -863 1308 O ATOM 1118 CB VAL A 334 11.700 -1.244 -49.183 1.00 89.17 C ANISOU 1118 CB VAL A 334 11864 13633 8385 -1144 -828 1315 C ATOM 1119 CG1 VAL A 334 12.372 -1.137 -50.540 1.00 89.03 C ANISOU 1119 CG1 VAL A 334 11890 13636 8302 -1277 -812 1364 C ATOM 1120 CG2 VAL A 334 11.908 0.043 -48.393 1.00 89.79 C ANISOU 1120 CG2 VAL A 334 12133 13527 8456 -1071 -891 1362 C ATOM 1121 N LEU A 335 9.946 -3.949 -50.002 1.00 84.61 N ANISOU 1121 N LEU A 335 10910 13452 7786 -1171 -760 1182 N ATOM 1122 CA LEU A 335 9.576 -5.048 -50.907 1.00 84.60 C ANISOU 1122 CA LEU A 335 10811 13595 7738 -1266 -730 1137 C ATOM 1123 C LEU A 335 8.081 -4.938 -51.299 1.00 89.86 C ANISOU 1123 C LEU A 335 11404 14436 8304 -1177 -799 1158 C ATOM 1124 O LEU A 335 7.767 -5.036 -52.480 1.00 91.12 O ANISOU 1124 O LEU A 335 11557 14695 8368 -1223 -817 1175 O ATOM 1125 CB LEU A 335 9.863 -6.424 -50.251 1.00 83.51 C ANISOU 1125 CB LEU A 335 10583 13465 7681 -1353 -657 1050 C ATOM 1126 CG LEU A 335 9.998 -7.675 -51.146 1.00 87.62 C ANISOU 1126 CG LEU A 335 11072 14058 8164 -1486 -604 989 C ATOM 1127 CD1 LEU A 335 10.547 -8.836 -50.357 1.00 86.51 C ANISOU 1127 CD1 LEU A 335 10904 13860 8108 -1543 -532 915 C ATOM 1128 CD2 LEU A 335 8.668 -8.125 -51.717 1.00 91.81 C ANISOU 1128 CD2 LEU A 335 11530 14758 8597 -1507 -653 975 C ATOM 1129 N THR A 336 7.175 -4.724 -50.321 1.00 85.58 N ANISOU 1129 N THR A 336 10796 13952 7769 -1046 -838 1161 N ATOM 1130 CA THR A 336 5.730 -4.636 -50.568 1.00 86.25 C ANISOU 1130 CA THR A 336 10774 14253 7745 -946 -902 1189 C ATOM 1131 C THR A 336 5.367 -3.377 -51.383 1.00 92.55 C ANISOU 1131 C THR A 336 11668 15063 8434 -804 -973 1278 C ATOM 1132 O THR A 336 4.503 -3.459 -52.255 1.00 91.91 O ANISOU 1132 O THR A 336 11511 15173 8237 -790 -1016 1306 O ATOM 1133 CB THR A 336 4.942 -4.666 -49.257 1.00 86.60 C ANISOU 1133 CB THR A 336 10716 14374 7812 -824 -917 1177 C ATOM 1134 OG1 THR A 336 5.244 -3.499 -48.497 1.00 83.83 O ANISOU 1134 OG1 THR A 336 10492 13865 7493 -653 -940 1212 O ATOM 1135 CG2 THR A 336 5.210 -5.920 -48.440 1.00 82.20 C ANISOU 1135 CG2 THR A 336 10072 13810 7349 -965 -853 1100 C ATOM 1136 N TYR A 337 6.019 -2.227 -51.093 1.00 90.90 N ANISOU 1136 N TYR A 337 11637 14649 8250 -707 -991 1324 N ATOM 1137 CA TYR A 337 5.783 -0.970 -51.807 1.00 92.43 C ANISOU 1137 CA TYR A 337 11978 14802 8338 -570 -1061 1415 C ATOM 1138 C TYR A 337 6.223 -1.102 -53.273 1.00 96.48 C ANISOU 1138 C TYR A 337 12528 15338 8791 -716 -1054 1443 C ATOM 1139 O TYR A 337 5.443 -0.775 -54.165 1.00 97.68 O ANISOU 1139 O TYR A 337 12667 15628 8821 -639 -1109 1498 O ATOM 1140 CB TYR A 337 6.504 0.216 -51.121 1.00 93.91 C ANISOU 1140 CB TYR A 337 12392 14727 8564 -482 -1082 1453 C ATOM 1141 CG TYR A 337 6.493 1.492 -51.945 1.00 97.31 C ANISOU 1141 CG TYR A 337 13033 15056 8883 -382 -1152 1552 C ATOM 1142 CD1 TYR A 337 5.400 2.356 -51.917 1.00100.63 C ANISOU 1142 CD1 TYR A 337 13512 15533 9189 -113 -1228 1610 C ATOM 1143 CD2 TYR A 337 7.571 1.831 -52.761 1.00 98.29 C ANISOU 1143 CD2 TYR A 337 13302 15040 9004 -550 -1140 1595 C ATOM 1144 CE1 TYR A 337 5.383 3.526 -52.672 1.00102.74 C ANISOU 1144 CE1 TYR A 337 14003 15687 9345 -8 -1296 1706 C ATOM 1145 CE2 TYR A 337 7.554 2.986 -53.541 1.00100.85 C ANISOU 1145 CE2 TYR A 337 13838 15265 9217 -478 -1207 1695 C ATOM 1146 CZ TYR A 337 6.460 3.835 -53.487 1.00110.13 C ANISOU 1146 CZ TYR A 337 15096 16466 10283 -204 -1287 1750 C ATOM 1147 OH TYR A 337 6.438 4.982 -54.244 1.00113.88 O ANISOU 1147 OH TYR A 337 15810 16821 10638 -117 -1357 1854 O ATOM 1148 N ALA A 338 7.472 -1.557 -53.509 1.00 91.82 N ANISOU 1148 N ALA A 338 11980 14632 8275 -912 -986 1411 N ATOM 1149 CA ALA A 338 8.059 -1.731 -54.839 1.00 91.30 C ANISOU 1149 CA ALA A 338 11950 14587 8152 -1057 -964 1431 C ATOM 1150 C ALA A 338 7.242 -2.705 -55.674 1.00 94.99 C ANISOU 1150 C ALA A 338 12269 15281 8543 -1116 -963 1391 C ATOM 1151 O ALA A 338 6.975 -2.404 -56.841 1.00 96.65 O ANISOU 1151 O ALA A 338 12508 15574 8639 -1124 -998 1442 O ATOM 1152 CB ALA A 338 9.496 -2.211 -54.730 1.00 90.90 C ANISOU 1152 CB ALA A 338 11928 14419 8192 -1231 -878 1392 C ATOM 1153 N TRP A 339 6.798 -3.839 -55.077 1.00 89.22 N ANISOU 1153 N TRP A 339 11389 14649 7860 -1167 -931 1307 N ATOM 1154 CA TRP A 339 5.949 -4.812 -55.775 1.00 89.30 C ANISOU 1154 CA TRP A 339 11271 14875 7784 -1254 -941 1266 C ATOM 1155 C TRP A 339 4.611 -4.167 -56.168 1.00 95.63 C ANISOU 1155 C TRP A 339 12007 15875 8454 -1110 -1036 1339 C ATOM 1156 O TRP A 339 4.132 -4.414 -57.265 1.00 96.42 O ANISOU 1156 O TRP A 339 12066 16134 8437 -1173 -1065 1352 O ATOM 1157 CB TRP A 339 5.713 -6.070 -54.936 1.00 86.77 C ANISOU 1157 CB TRP A 339 10835 14601 7531 -1346 -898 1174 C ATOM 1158 CG TRP A 339 4.885 -7.103 -55.637 1.00 88.38 C ANISOU 1158 CG TRP A 339 10937 15008 7634 -1479 -915 1130 C ATOM 1159 CD1 TRP A 339 5.224 -7.804 -56.757 1.00 91.63 C ANISOU 1159 CD1 TRP A 339 11391 15442 7980 -1634 -888 1087 C ATOM 1160 CD2 TRP A 339 3.591 -7.581 -55.241 1.00 88.93 C ANISOU 1160 CD2 TRP A 339 10851 15296 7642 -1486 -964 1124 C ATOM 1161 NE1 TRP A 339 4.213 -8.671 -57.100 1.00 92.02 N ANISOU 1161 NE1 TRP A 339 11343 15692 7930 -1750 -924 1052 N ATOM 1162 CE2 TRP A 339 3.196 -8.554 -56.188 1.00 93.66 C ANISOU 1162 CE2 TRP A 339 11416 16035 8136 -1674 -973 1079 C ATOM 1163 CE3 TRP A 339 2.726 -7.289 -54.169 1.00 90.06 C ANISOU 1163 CE3 TRP A 339 10876 15547 7795 -1358 -1002 1155 C ATOM 1164 CZ2 TRP A 339 1.978 -9.244 -56.091 1.00 93.69 C ANISOU 1164 CZ2 TRP A 339 11270 16283 8044 -1767 -1024 1070 C ATOM 1165 CZ3 TRP A 339 1.520 -7.970 -54.079 1.00 92.22 C ANISOU 1165 CZ3 TRP A 339 10980 16085 7974 -1433 -1045 1150 C ATOM 1166 CH2 TRP A 339 1.156 -8.933 -55.032 1.00 93.59 C ANISOU 1166 CH2 TRP A 339 11121 16397 8043 -1649 -1059 1111 C ATOM 1167 N HIS A 340 4.047 -3.307 -55.304 1.00 93.12 N ANISOU 1167 N HIS A 340 11688 15552 8140 -903 -1082 1389 N ATOM 1168 CA HIS A 340 2.804 -2.590 -55.583 1.00 95.17 C ANISOU 1168 CA HIS A 340 11887 16008 8263 -708 -1170 1468 C ATOM 1169 C HIS A 340 3.011 -1.549 -56.708 1.00101.06 C ANISOU 1169 C HIS A 340 12789 16696 8912 -635 -1217 1560 C ATOM 1170 O HIS A 340 2.211 -1.524 -57.641 1.00101.66 O ANISOU 1170 O HIS A 340 12791 16984 8850 -609 -1270 1606 O ATOM 1171 CB HIS A 340 2.259 -1.920 -54.300 1.00 96.39 C ANISOU 1171 CB HIS A 340 12028 16152 8443 -474 -1197 1492 C ATOM 1172 CG HIS A 340 1.220 -0.867 -54.541 1.00101.93 C ANISOU 1172 CG HIS A 340 12733 16996 8999 -200 -1283 1588 C ATOM 1173 ND1 HIS A 340 1.492 0.474 -54.331 1.00104.55 N ANISOU 1173 ND1 HIS A 340 13285 17122 9317 14 -1318 1655 N ATOM 1174 CD2 HIS A 340 -0.044 -0.987 -55.013 1.00105.37 C ANISOU 1174 CD2 HIS A 340 12988 17760 9286 -113 -1340 1632 C ATOM 1175 CE1 HIS A 340 0.385 1.121 -54.658 1.00105.85 C ANISOU 1175 CE1 HIS A 340 13406 17484 9328 256 -1392 1734 C ATOM 1176 NE2 HIS A 340 -0.565 0.285 -55.078 1.00106.75 N ANISOU 1176 NE2 HIS A 340 13262 17942 9355 191 -1407 1726 N ATOM 1177 N THR A 341 4.075 -0.714 -56.629 1.00 98.36 N ANISOU 1177 N THR A 341 12661 16080 8631 -620 -1201 1594 N ATOM 1178 CA THR A 341 4.347 0.356 -57.603 1.00 99.84 C ANISOU 1178 CA THR A 341 13032 16177 8724 -564 -1247 1693 C ATOM 1179 C THR A 341 4.904 -0.148 -58.947 1.00103.39 C ANISOU 1179 C THR A 341 13483 16675 9125 -774 -1217 1690 C ATOM 1180 O THR A 341 4.740 0.556 -59.949 1.00104.24 O ANISOU 1180 O THR A 341 13682 16810 9113 -724 -1269 1777 O ATOM 1181 CB THR A 341 5.302 1.422 -57.040 1.00112.29 C ANISOU 1181 CB THR A 341 14853 17446 10366 -516 -1248 1737 C ATOM 1182 OG1 THR A 341 6.194 0.834 -56.089 1.00116.16 O ANISOU 1182 OG1 THR A 341 15320 17807 11009 -649 -1173 1654 O ATOM 1183 CG2 THR A 341 4.560 2.568 -56.385 1.00113.18 C ANISOU 1183 CG2 THR A 341 15083 17499 10421 -224 -1323 1801 C ATOM 1184 N SER A 342 5.513 -1.347 -59.000 1.00 98.57 N ANISOU 1184 N SER A 342 12781 16081 8589 -988 -1137 1592 N ATOM 1185 CA SER A 342 6.081 -1.849 -60.254 1.00 98.56 C ANISOU 1185 CA SER A 342 12794 16126 8529 -1169 -1100 1578 C ATOM 1186 C SER A 342 4.997 -2.355 -61.240 1.00104.26 C ANISOU 1186 C SER A 342 13391 17116 9106 -1190 -1148 1577 C ATOM 1187 O SER A 342 5.319 -2.586 -62.414 1.00105.60 O ANISOU 1187 O SER A 342 13591 17339 9192 -1309 -1135 1581 O ATOM 1188 CB SER A 342 7.114 -2.938 -59.994 1.00101.60 C ANISOU 1188 CB SER A 342 13150 16433 9022 -1354 -996 1474 C ATOM 1189 OG SER A 342 8.151 -2.464 -59.149 1.00112.00 O ANISOU 1189 OG SER A 342 14563 17536 10454 -1350 -955 1484 O ATOM 1190 N PHE A 343 3.717 -2.460 -60.806 1.00100.75 N ANISOU 1190 N PHE A 343 12805 16861 8614 -1074 -1208 1582 N ATOM 1191 CA PHE A 343 2.602 -2.841 -61.693 1.00101.31 C ANISOU 1191 CA PHE A 343 12740 17226 8526 -1096 -1270 1597 C ATOM 1192 C PHE A 343 2.271 -1.711 -62.676 1.00110.92 C ANISOU 1192 C PHE A 343 14044 18499 9601 -954 -1346 1723 C ATOM 1193 O PHE A 343 1.699 -1.967 -63.744 1.00111.65 O ANISOU 1193 O PHE A 343 14066 18804 9551 -1012 -1388 1743 O ATOM 1194 CB PHE A 343 1.342 -3.217 -60.902 1.00102.00 C ANISOU 1194 CB PHE A 343 12629 17539 8586 -1016 -1314 1584 C ATOM 1195 CG PHE A 343 1.368 -4.605 -60.318 1.00101.17 C ANISOU 1195 CG PHE A 343 12415 17468 8557 -1217 -1259 1464 C ATOM 1196 CD1 PHE A 343 1.224 -5.722 -61.131 1.00103.18 C ANISOU 1196 CD1 PHE A 343 12615 17853 8736 -1449 -1249 1396 C ATOM 1197 CD2 PHE A 343 1.493 -4.796 -58.947 1.00101.48 C ANISOU 1197 CD2 PHE A 343 12423 17405 8729 -1173 -1221 1422 C ATOM 1198 CE1 PHE A 343 1.248 -7.009 -60.589 1.00103.05 C ANISOU 1198 CE1 PHE A 343 12542 17836 8778 -1637 -1203 1288 C ATOM 1199 CE2 PHE A 343 1.511 -6.082 -58.405 1.00103.17 C ANISOU 1199 CE2 PHE A 343 12558 17638 9005 -1359 -1173 1321 C ATOM 1200 CZ PHE A 343 1.390 -7.180 -59.231 1.00101.49 C ANISOU 1200 CZ PHE A 343 12315 17530 8715 -1590 -1165 1256 C ATOM 1201 N LYS A 344 2.653 -0.467 -62.313 1.00110.73 N ANISOU 1201 N LYS A 344 14192 18271 9609 -777 -1366 1807 N ATOM 1202 CA LYS A 344 2.441 0.759 -63.086 1.00113.80 C ANISOU 1202 CA LYS A 344 14725 18644 9871 -615 -1440 1939 C ATOM 1203 C LYS A 344 3.362 0.822 -64.327 1.00122.35 C ANISOU 1203 C LYS A 344 15933 19648 10905 -791 -1413 1966 C ATOM 1204 O LYS A 344 3.175 1.711 -65.168 1.00124.62 O ANISOU 1204 O LYS A 344 16336 19948 11067 -695 -1475 2079 O ATOM 1205 CB LYS A 344 2.655 1.992 -62.192 1.00116.41 C ANISOU 1205 CB LYS A 344 15247 18732 10253 -396 -1467 2006 C ATOM 1206 CG LYS A 344 1.633 2.099 -61.060 1.00129.55 C ANISOU 1206 CG LYS A 344 16795 20503 11924 -166 -1501 1996 C ATOM 1207 CD LYS A 344 2.012 3.152 -60.027 1.00137.82 C ANISOU 1207 CD LYS A 344 18056 21268 13040 19 -1511 2029 C ATOM 1208 CE LYS A 344 0.994 3.276 -58.915 1.00148.12 C ANISOU 1208 CE LYS A 344 19247 22694 14335 271 -1540 2017 C ATOM 1209 NZ LYS A 344 -0.266 3.934 -59.367 1.00159.36 N ANISOU 1209 NZ LYS A 344 20626 24352 15572 562 -1629 2117 N ATOM 1210 N ALA A 345 4.321 -0.136 -64.461 1.00119.44 N ANISOU 1210 N ALA A 345 15541 19218 10621 -1034 -1320 1867 N ATOM 1211 CA ALA A 345 5.250 -0.237 -65.594 1.00120.23 C ANISOU 1211 CA ALA A 345 15732 19279 10671 -1209 -1276 1878 C ATOM 1212 C ALA A 345 4.489 -0.501 -66.907 1.00128.00 C ANISOU 1212 C ALA A 345 16640 20515 11477 -1243 -1327 1904 C ATOM 1213 O ALA A 345 4.543 0.335 -67.816 1.00129.73 O ANISOU 1213 O ALA A 345 16975 20736 11581 -1199 -1372 2013 O ATOM 1214 CB ALA A 345 6.273 -1.337 -65.343 1.00119.35 C ANISOU 1214 CB ALA A 345 15581 19093 10673 -1412 -1163 1755 C ATOM 1215 N LEU A 346 3.771 -1.649 -66.993 1.00124.68 N ANISOU 1215 N LEU A 346 16040 20309 11024 -1333 -1326 1808 N ATOM 1216 CA LEU A 346 2.956 -2.060 -68.148 1.00147.89 C ANISOU 1216 CA LEU A 346 18886 23521 13787 -1396 -1380 1815 C ATOM 1217 C LEU A 346 1.746 -2.867 -67.671 1.00165.51 C ANISOU 1217 C LEU A 346 20909 25990 15987 -1405 -1424 1755 C ATOM 1218 O LEU A 346 1.882 -3.754 -66.823 1.00119.00 O ANISOU 1218 O LEU A 346 14956 20050 10210 -1501 -1370 1647 O ATOM 1219 CB LEU A 346 3.768 -2.883 -69.180 1.00147.77 C ANISOU 1219 CB LEU A 346 18916 23508 13724 -1626 -1309 1738 C ATOM 1220 CG LEU A 346 4.886 -2.187 -69.973 1.00152.88 C ANISOU 1220 CG LEU A 346 19733 24011 14343 -1659 -1269 1808 C ATOM 1221 CD1 LEU A 346 5.846 -3.202 -70.558 1.00152.67 C ANISOU 1221 CD1 LEU A 346 19731 23964 14314 -1864 -1166 1698 C ATOM 1222 CD2 LEU A 346 4.331 -1.281 -71.069 1.00157.11 C ANISOU 1222 CD2 LEU A 346 20318 24677 14701 -1573 -1359 1944 C ATOM 1223 N LEU A 353 10.310 2.836 -60.475 1.00111.39 N ANISOU 1223 N LEU A 353 15319 16842 10161 -1291 -1131 1957 N ATOM 1224 CA LEU A 353 11.075 3.003 -59.239 1.00110.66 C ANISOU 1224 CA LEU A 353 15281 16576 10190 -1333 -1104 1929 C ATOM 1225 C LEU A 353 12.307 3.930 -59.440 1.00115.98 C ANISOU 1225 C LEU A 353 16159 17077 10831 -1500 -1109 2027 C ATOM 1226 O LEU A 353 13.153 4.021 -58.539 1.00114.52 O ANISOU 1226 O LEU A 353 16008 16773 10731 -1593 -1081 2010 O ATOM 1227 CB LEU A 353 11.532 1.626 -58.683 1.00108.90 C ANISOU 1227 CB LEU A 353 14840 16448 10090 -1435 -1002 1801 C ATOM 1228 CG LEU A 353 10.455 0.612 -58.234 1.00112.32 C ANISOU 1228 CG LEU A 353 15079 17028 10569 -1324 -993 1698 C ATOM 1229 CD1 LEU A 353 11.078 -0.747 -57.939 1.00110.55 C ANISOU 1229 CD1 LEU A 353 14693 16871 10439 -1455 -890 1587 C ATOM 1230 CD2 LEU A 353 9.675 1.106 -57.016 1.00114.68 C ANISOU 1230 CD2 LEU A 353 15408 17249 10916 -1132 -1049 1693 C ATOM 1231 N SER A 354 12.382 4.642 -60.596 1.00115.10 N ANISOU 1231 N SER A 354 16187 16961 10585 -1547 -1151 2137 N ATOM 1232 CA SER A 354 13.479 5.561 -60.947 1.00116.39 C ANISOU 1232 CA SER A 354 16555 16984 10684 -1735 -1166 2252 C ATOM 1233 C SER A 354 13.478 6.802 -60.036 1.00122.00 C ANISOU 1233 C SER A 354 17545 17416 11393 -1668 -1253 2316 C ATOM 1234 O SER A 354 12.515 7.576 -60.033 1.00122.58 O ANISOU 1234 O SER A 354 17788 17390 11398 -1454 -1343 2364 O ATOM 1235 CB SER A 354 13.389 5.977 -62.413 1.00121.24 C ANISOU 1235 CB SER A 354 17251 17672 11143 -1784 -1195 2356 C ATOM 1236 N GLY A 355 14.553 6.945 -59.256 1.00118.90 N ANISOU 1236 N GLY A 355 17198 16912 11067 -1843 -1226 2313 N ATOM 1237 CA GLY A 355 14.746 8.033 -58.299 1.00119.65 C ANISOU 1237 CA GLY A 355 17568 16732 11161 -1833 -1302 2359 C ATOM 1238 C GLY A 355 14.483 7.629 -56.860 1.00121.46 C ANISOU 1238 C GLY A 355 17710 16913 11525 -1708 -1287 2245 C ATOM 1239 O GLY A 355 15.195 8.065 -55.948 1.00120.95 O ANISOU 1239 O GLY A 355 17767 16689 11498 -1817 -1302 2249 O ATOM 1240 N LYS A 356 13.462 6.771 -56.660 1.00116.25 N ANISOU 1240 N LYS A 356 16834 16407 10927 -1497 -1258 2146 N ATOM 1241 CA LYS A 356 12.993 6.256 -55.371 1.00114.62 C ANISOU 1241 CA LYS A 356 16509 16202 10839 -1351 -1239 2036 C ATOM 1242 C LYS A 356 14.017 5.336 -54.660 1.00115.74 C ANISOU 1242 C LYS A 356 16460 16408 11109 -1536 -1147 1957 C ATOM 1243 O LYS A 356 13.974 5.232 -53.436 1.00114.72 O ANISOU 1243 O LYS A 356 16315 16207 11067 -1471 -1145 1894 O ATOM 1244 CB LYS A 356 11.682 5.481 -55.575 1.00116.73 C ANISOU 1244 CB LYS A 356 16567 16672 11112 -1135 -1229 1970 C ATOM 1245 N THR A 357 14.919 4.680 -55.420 1.00110.80 N ANISOU 1245 N THR A 357 15692 15925 10483 -1744 -1070 1963 N ATOM 1246 CA THR A 357 15.950 3.741 -54.954 1.00108.63 C ANISOU 1246 CA THR A 357 15221 15749 10303 -1900 -973 1899 C ATOM 1247 C THR A 357 16.783 4.325 -53.783 1.00111.11 C ANISOU 1247 C THR A 357 15648 15903 10664 -2003 -995 1916 C ATOM 1248 O THR A 357 17.048 3.596 -52.827 1.00109.33 O ANISOU 1248 O THR A 357 15274 15719 10547 -1996 -943 1833 O ATOM 1249 CB THR A 357 16.831 3.345 -56.151 1.00117.21 C ANISOU 1249 CB THR A 357 16216 16997 11324 -2090 -906 1942 C ATOM 1250 OG1 THR A 357 16.145 2.315 -56.864 1.00116.17 O ANISOU 1250 OG1 THR A 357 15907 17041 11191 -1996 -857 1870 O ATOM 1251 CG2 THR A 357 18.229 2.854 -55.754 1.00115.99 C ANISOU 1251 CG2 THR A 357 15934 16921 11215 -2282 -824 1931 C ATOM 1252 N SER A 358 17.182 5.610 -53.856 1.00108.77 N ANISOU 1252 N SER A 358 15625 15425 10279 -2107 -1076 2023 N ATOM 1253 CA SER A 358 17.968 6.266 -52.802 1.00108.52 C ANISOU 1253 CA SER A 358 15738 15230 10265 -2237 -1113 2046 C ATOM 1254 C SER A 358 17.132 6.516 -51.546 1.00109.87 C ANISOU 1254 C SER A 358 16004 15243 10499 -2018 -1164 1974 C ATOM 1255 O SER A 358 17.689 6.549 -50.444 1.00108.95 O ANISOU 1255 O SER A 358 15897 15058 10441 -2090 -1164 1941 O ATOM 1256 CB SER A 358 18.561 7.581 -53.296 1.00114.41 C ANISOU 1256 CB SER A 358 16787 15809 10875 -2431 -1195 2184 C ATOM 1257 OG SER A 358 19.905 7.401 -53.709 1.00123.70 O ANISOU 1257 OG SER A 358 17857 17128 12016 -2732 -1142 2246 O ATOM 1258 N TYR A 359 15.802 6.687 -51.713 1.00104.94 N ANISOU 1258 N TYR A 359 15437 14585 9850 -1748 -1207 1953 N ATOM 1259 CA TYR A 359 14.878 6.911 -50.604 1.00103.83 C ANISOU 1259 CA TYR A 359 15368 14336 9747 -1500 -1250 1887 C ATOM 1260 C TYR A 359 14.592 5.585 -49.891 1.00104.93 C ANISOU 1260 C TYR A 359 15188 14660 10020 -1421 -1165 1768 C ATOM 1261 O TYR A 359 14.255 5.599 -48.706 1.00104.03 O ANISOU 1261 O TYR A 359 15086 14479 9962 -1298 -1178 1706 O ATOM 1262 CB TYR A 359 13.589 7.592 -51.081 1.00105.93 C ANISOU 1262 CB TYR A 359 15792 14541 9914 -1229 -1324 1923 C ATOM 1263 CG TYR A 359 13.822 9.011 -51.556 1.00109.46 C ANISOU 1263 CG TYR A 359 16624 14743 10222 -1275 -1421 2041 C ATOM 1264 CD1 TYR A 359 13.910 10.065 -50.650 1.00112.58 C ANISOU 1264 CD1 TYR A 359 17343 14858 10572 -1229 -1501 2055 C ATOM 1265 CD2 TYR A 359 13.972 9.298 -52.908 1.00111.01 C ANISOU 1265 CD2 TYR A 359 16883 14976 10320 -1374 -1436 2138 C ATOM 1266 CE1 TYR A 359 14.142 11.370 -51.078 1.00115.37 C ANISOU 1266 CE1 TYR A 359 18096 14955 10785 -1287 -1597 2166 C ATOM 1267 CE2 TYR A 359 14.201 10.600 -53.350 1.00114.17 C ANISOU 1267 CE2 TYR A 359 17660 15137 10582 -1432 -1529 2257 C ATOM 1268 CZ TYR A 359 14.280 11.634 -52.431 1.00123.46 C ANISOU 1268 CZ TYR A 359 19177 16017 11714 -1391 -1611 2271 C ATOM 1269 OH TYR A 359 14.508 12.921 -52.858 1.00127.84 O ANISOU 1269 OH TYR A 359 20148 16305 12120 -1460 -1710 2390 O ATOM 1270 N PHE A 360 14.782 4.444 -50.593 1.00 99.84 N ANISOU 1270 N PHE A 360 14279 14236 9418 -1502 -1080 1736 N ATOM 1271 CA PHE A 360 14.650 3.106 -50.012 1.00 97.82 C ANISOU 1271 CA PHE A 360 13747 14141 9279 -1468 -997 1629 C ATOM 1272 C PHE A 360 15.789 2.871 -49.009 1.00100.51 C ANISOU 1272 C PHE A 360 14045 14442 9701 -1617 -957 1603 C ATOM 1273 O PHE A 360 15.529 2.436 -47.895 1.00 98.44 O ANISOU 1273 O PHE A 360 13703 14178 9522 -1528 -941 1531 O ATOM 1274 CB PHE A 360 14.644 2.008 -51.101 1.00 98.96 C ANISOU 1274 CB PHE A 360 13681 14497 9421 -1527 -922 1604 C ATOM 1275 CG PHE A 360 13.455 1.937 -52.037 1.00101.03 C ANISOU 1275 CG PHE A 360 13918 14858 9609 -1388 -951 1612 C ATOM 1276 CD1 PHE A 360 13.554 1.290 -53.265 1.00104.12 C ANISOU 1276 CD1 PHE A 360 14203 15403 9955 -1473 -906 1614 C ATOM 1277 CD2 PHE A 360 12.219 2.467 -51.669 1.00103.70 C ANISOU 1277 CD2 PHE A 360 14327 15161 9914 -1163 -1023 1614 C ATOM 1278 CE1 PHE A 360 12.449 1.196 -54.116 1.00105.56 C ANISOU 1278 CE1 PHE A 360 14352 15697 10060 -1361 -939 1621 C ATOM 1279 CE2 PHE A 360 11.116 2.375 -52.524 1.00107.02 C ANISOU 1279 CE2 PHE A 360 14695 15715 10252 -1036 -1052 1628 C ATOM 1280 CZ PHE A 360 11.238 1.739 -53.738 1.00105.26 C ANISOU 1280 CZ PHE A 360 14367 15640 9987 -1147 -1014 1632 C ATOM 1281 N HIS A 361 17.041 3.216 -49.399 1.00 98.29 N ANISOU 1281 N HIS A 361 13816 14147 9381 -1849 -946 1672 N ATOM 1282 CA HIS A 361 18.258 3.098 -48.586 1.00 97.61 C ANISOU 1282 CA HIS A 361 13683 14060 9342 -2023 -915 1672 C ATOM 1283 C HIS A 361 18.265 4.087 -47.418 1.00101.79 C ANISOU 1283 C HIS A 361 14431 14377 9869 -2011 -998 1680 C ATOM 1284 O HIS A 361 18.655 3.714 -46.303 1.00100.71 O ANISOU 1284 O HIS A 361 14211 14246 9808 -2028 -975 1628 O ATOM 1285 CB HIS A 361 19.502 3.305 -49.454 1.00 99.03 C ANISOU 1285 CB HIS A 361 13857 14323 9446 -2277 -889 1762 C ATOM 1286 CG HIS A 361 19.806 2.104 -50.279 1.00101.70 C ANISOU 1286 CG HIS A 361 13945 14895 9801 -2295 -783 1730 C ATOM 1287 ND1 HIS A 361 20.702 1.144 -49.846 1.00102.65 N ANISOU 1287 ND1 HIS A 361 13854 15167 9982 -2359 -693 1688 N ATOM 1288 CD2 HIS A 361 19.257 1.697 -51.448 1.00103.49 C ANISOU 1288 CD2 HIS A 361 14117 15218 9984 -2232 -755 1725 C ATOM 1289 CE1 HIS A 361 20.704 0.209 -50.782 1.00101.82 C ANISOU 1289 CE1 HIS A 361 13595 15229 9863 -2329 -613 1658 C ATOM 1290 NE2 HIS A 361 19.844 0.495 -51.763 1.00102.51 N ANISOU 1290 NE2 HIS A 361 13769 15291 9890 -2264 -648 1675 N ATOM 1291 N LEU A 362 17.829 5.332 -47.667 1.00 99.28 N ANISOU 1291 N LEU A 362 14406 13863 9453 -1972 -1095 1744 N ATOM 1292 CA LEU A 362 17.748 6.361 -46.641 1.00100.39 C ANISOU 1292 CA LEU A 362 14815 13765 9562 -1939 -1184 1748 C ATOM 1293 C LEU A 362 16.826 5.886 -45.529 1.00104.49 C ANISOU 1293 C LEU A 362 15245 14287 10167 -1687 -1172 1642 C ATOM 1294 O LEU A 362 17.255 5.868 -44.380 1.00104.66 O ANISOU 1294 O LEU A 362 15272 14258 10238 -1730 -1174 1601 O ATOM 1295 CB LEU A 362 17.265 7.695 -47.250 1.00102.76 C ANISOU 1295 CB LEU A 362 15468 13849 9727 -1886 -1287 1832 C ATOM 1296 CG LEU A 362 17.336 8.988 -46.404 1.00109.36 C ANISOU 1296 CG LEU A 362 16685 14381 10485 -1890 -1395 1856 C ATOM 1297 CD1 LEU A 362 16.034 9.274 -45.671 1.00109.76 C ANISOU 1297 CD1 LEU A 362 16850 14318 10534 -1533 -1436 1786 C ATOM 1298 CD2 LEU A 362 18.591 9.062 -45.527 1.00111.57 C ANISOU 1298 CD2 LEU A 362 16975 14629 10787 -2167 -1397 1858 C ATOM 1299 N LEU A 363 15.607 5.413 -45.879 1.00100.39 N ANISOU 1299 N LEU A 363 14614 13866 9663 -1447 -1153 1600 N ATOM 1300 CA LEU A 363 14.599 4.938 -44.930 1.00 99.17 C ANISOU 1300 CA LEU A 363 14352 13758 9569 -1205 -1140 1511 C ATOM 1301 C LEU A 363 15.033 3.646 -44.200 1.00 99.28 C ANISOU 1301 C LEU A 363 14080 13931 9712 -1275 -1050 1434 C ATOM 1302 O LEU A 363 14.877 3.576 -42.980 1.00 98.44 O ANISOU 1302 O LEU A 363 13965 13783 9653 -1194 -1054 1378 O ATOM 1303 CB LEU A 363 13.255 4.708 -45.651 1.00 99.76 C ANISOU 1303 CB LEU A 363 14347 13953 9605 -978 -1144 1505 C ATOM 1304 CG LEU A 363 12.026 4.361 -44.783 1.00104.90 C ANISOU 1304 CG LEU A 363 14891 14686 10281 -711 -1142 1432 C ATOM 1305 CD1 LEU A 363 11.531 5.579 -43.983 1.00106.70 C ANISOU 1305 CD1 LEU A 363 15399 14713 10429 -507 -1225 1439 C ATOM 1306 CD2 LEU A 363 10.894 3.814 -45.642 1.00107.34 C ANISOU 1306 CD2 LEU A 363 15029 15202 10554 -570 -1129 1432 C ATOM 1307 N THR A 364 15.570 2.646 -44.924 1.00 93.04 N ANISOU 1307 N THR A 364 13073 13312 8965 -1410 -971 1431 N ATOM 1308 CA THR A 364 15.960 1.358 -44.327 1.00 90.42 C ANISOU 1308 CA THR A 364 12492 13121 8742 -1453 -884 1362 C ATOM 1309 C THR A 364 17.232 1.405 -43.474 1.00 93.81 C ANISOU 1309 C THR A 364 12920 13512 9210 -1621 -869 1368 C ATOM 1310 O THR A 364 17.371 0.540 -42.608 1.00 92.92 O ANISOU 1310 O THR A 364 12650 13473 9184 -1597 -817 1308 O ATOM 1311 CB THR A 364 16.165 0.285 -45.390 1.00 91.23 C ANISOU 1311 CB THR A 364 12403 13403 8859 -1524 -804 1353 C ATOM 1312 OG1 THR A 364 17.109 0.751 -46.356 1.00 92.80 O ANISOU 1312 OG1 THR A 364 12669 13601 8990 -1700 -804 1430 O ATOM 1313 CG2 THR A 364 14.873 -0.124 -46.053 1.00 85.66 C ANISOU 1313 CG2 THR A 364 11631 12786 8128 -1373 -806 1326 C ATOM 1314 N TRP A 365 18.181 2.333 -43.733 1.00 90.15 N ANISOU 1314 N TRP A 365 12618 12958 8678 -1806 -913 1446 N ATOM 1315 CA TRP A 365 19.408 2.346 -42.930 1.00 89.38 C ANISOU 1315 CA TRP A 365 12491 12868 8602 -1987 -903 1460 C ATOM 1316 C TRP A 365 19.371 3.431 -41.831 1.00 94.20 C ANISOU 1316 C TRP A 365 13344 13270 9179 -1986 -995 1461 C ATOM 1317 O TRP A 365 20.009 3.237 -40.793 1.00 92.40 O ANISOU 1317 O TRP A 365 13060 13058 8992 -2060 -987 1437 O ATOM 1318 CB TRP A 365 20.688 2.508 -43.786 1.00 88.55 C ANISOU 1318 CB TRP A 365 12358 12856 8432 -2243 -882 1549 C ATOM 1319 CG TRP A 365 20.852 1.511 -44.906 1.00 88.48 C ANISOU 1319 CG TRP A 365 12138 13049 8432 -2247 -789 1548 C ATOM 1320 CD1 TRP A 365 20.957 1.791 -46.236 1.00 92.05 C ANISOU 1320 CD1 TRP A 365 12629 13545 8800 -2323 -787 1613 C ATOM 1321 CD2 TRP A 365 20.901 0.079 -44.795 1.00 86.64 C ANISOU 1321 CD2 TRP A 365 11650 12987 8283 -2162 -688 1475 C ATOM 1322 NE1 TRP A 365 21.084 0.628 -46.961 1.00 90.41 N ANISOU 1322 NE1 TRP A 365 12203 13531 8617 -2290 -689 1579 N ATOM 1323 CE2 TRP A 365 21.048 -0.438 -46.104 1.00 90.34 C ANISOU 1323 CE2 TRP A 365 12024 13591 8708 -2189 -628 1494 C ATOM 1324 CE3 TRP A 365 20.840 -0.820 -43.718 1.00 86.46 C ANISOU 1324 CE3 TRP A 365 11488 13006 8358 -2066 -643 1399 C ATOM 1325 CZ2 TRP A 365 21.144 -1.809 -46.363 1.00 88.49 C ANISOU 1325 CZ2 TRP A 365 11587 13515 8521 -2118 -527 1431 C ATOM 1326 CZ3 TRP A 365 20.929 -2.179 -43.978 1.00 86.94 C ANISOU 1326 CZ3 TRP A 365 11347 13219 8468 -2002 -545 1346 C ATOM 1327 CH2 TRP A 365 21.074 -2.661 -45.286 1.00 87.68 C ANISOU 1327 CH2 TRP A 365 11375 13428 8513 -2024 -489 1358 C ATOM 1328 N SER A 366 18.625 4.549 -42.035 1.00 93.16 N ANISOU 1328 N SER A 366 13490 12941 8963 -1889 -1084 1487 N ATOM 1329 CA SER A 366 18.578 5.621 -41.030 1.00 94.38 C ANISOU 1329 CA SER A 366 13926 12870 9066 -1873 -1175 1481 C ATOM 1330 C SER A 366 17.483 5.385 -39.971 1.00 96.78 C ANISOU 1330 C SER A 366 14209 13144 9420 -1591 -1175 1386 C ATOM 1331 O SER A 366 17.698 5.773 -38.826 1.00 96.68 O ANISOU 1331 O SER A 366 14310 13022 9401 -1598 -1213 1353 O ATOM 1332 CB SER A 366 18.401 6.996 -41.668 1.00100.24 C ANISOU 1332 CB SER A 366 15028 13386 9672 -1899 -1275 1557 C ATOM 1333 OG SER A 366 17.135 7.162 -42.282 1.00111.25 O ANISOU 1333 OG SER A 366 16482 14751 11035 -1634 -1290 1549 O ATOM 1334 N LEU A 367 16.345 4.745 -40.320 1.00 92.26 N ANISOU 1334 N LEU A 367 13483 12687 8883 -1361 -1133 1346 N ATOM 1335 CA LEU A 367 15.278 4.477 -39.341 1.00 91.63 C ANISOU 1335 CA LEU A 367 13350 12628 8836 -1102 -1128 1266 C ATOM 1336 C LEU A 367 15.767 3.531 -38.197 1.00 92.24 C ANISOU 1336 C LEU A 367 13216 12810 9019 -1161 -1067 1205 C ATOM 1337 O LEU A 367 15.621 3.910 -37.027 1.00 91.52 O ANISOU 1337 O LEU A 367 13227 12627 8919 -1080 -1101 1163 O ATOM 1338 CB LEU A 367 14.026 3.892 -40.002 1.00 91.65 C ANISOU 1338 CB LEU A 367 13193 12786 8844 -893 -1095 1249 C ATOM 1339 CG LEU A 367 12.704 4.383 -39.444 1.00 98.31 C ANISOU 1339 CG LEU A 367 14127 13599 9627 -586 -1137 1215 C ATOM 1340 CD1 LEU A 367 12.218 5.608 -40.217 1.00101.00 C ANISOU 1340 CD1 LEU A 367 14751 13789 9836 -463 -1218 1276 C ATOM 1341 CD2 LEU A 367 11.651 3.297 -39.531 1.00100.81 C ANISOU 1341 CD2 LEU A 367 14154 14163 9988 -441 -1078 1175 C ATOM 1342 N PRO A 368 16.391 2.350 -38.475 1.00 85.29 N ANISOU 1342 N PRO A 368 12069 12110 8226 -1293 -982 1200 N ATOM 1343 CA PRO A 368 16.874 1.509 -37.374 1.00 83.16 C ANISOU 1343 CA PRO A 368 11629 11925 8043 -1333 -932 1152 C ATOM 1344 C PRO A 368 18.039 2.161 -36.638 1.00 86.51 C ANISOU 1344 C PRO A 368 12179 12250 8442 -1517 -975 1177 C ATOM 1345 O PRO A 368 18.298 1.812 -35.478 1.00 86.52 O ANISOU 1345 O PRO A 368 12110 12274 8488 -1514 -961 1136 O ATOM 1346 CB PRO A 368 17.311 0.217 -38.070 1.00 83.82 C ANISOU 1346 CB PRO A 368 11454 12198 8196 -1418 -838 1153 C ATOM 1347 CG PRO A 368 16.713 0.271 -39.400 1.00 88.79 C ANISOU 1347 CG PRO A 368 12095 12859 8782 -1376 -837 1180 C ATOM 1348 CD PRO A 368 16.678 1.706 -39.767 1.00 85.94 C ANISOU 1348 CD PRO A 368 12008 12325 8321 -1392 -927 1235 C ATOM 1349 N PHE A 369 18.718 3.121 -37.289 1.00 82.07 N ANISOU 1349 N PHE A 369 11808 11581 7796 -1689 -1032 1248 N ATOM 1350 CA PHE A 369 19.810 3.858 -36.664 1.00 82.75 C ANISOU 1350 CA PHE A 369 12039 11573 7829 -1906 -1089 1283 C ATOM 1351 C PHE A 369 19.249 4.722 -35.510 1.00 87.91 C ANISOU 1351 C PHE A 369 12942 12023 8435 -1781 -1169 1233 C ATOM 1352 O PHE A 369 19.741 4.635 -34.379 1.00 87.58 O ANISOU 1352 O PHE A 369 12881 11984 8411 -1842 -1177 1202 O ATOM 1353 CB PHE A 369 20.567 4.713 -37.698 1.00 85.63 C ANISOU 1353 CB PHE A 369 12568 11873 8095 -2137 -1138 1382 C ATOM 1354 CG PHE A 369 21.656 5.547 -37.076 1.00 88.69 C ANISOU 1354 CG PHE A 369 13127 12166 8404 -2399 -1212 1427 C ATOM 1355 CD1 PHE A 369 22.934 5.030 -36.898 1.00 91.93 C ANISOU 1355 CD1 PHE A 369 13330 12771 8830 -2634 -1172 1467 C ATOM 1356 CD2 PHE A 369 21.398 6.839 -36.629 1.00 92.13 C ANISOU 1356 CD2 PHE A 369 13940 12328 8737 -2406 -1324 1429 C ATOM 1357 CE1 PHE A 369 23.939 5.796 -36.298 1.00 93.98 C ANISOU 1357 CE1 PHE A 369 13732 12975 9001 -2904 -1248 1515 C ATOM 1358 CE2 PHE A 369 22.403 7.603 -36.029 1.00 96.23 C ANISOU 1358 CE2 PHE A 369 14640 12754 9170 -2682 -1401 1469 C ATOM 1359 CZ PHE A 369 23.666 7.078 -35.871 1.00 94.23 C ANISOU 1359 CZ PHE A 369 14152 12720 8932 -2944 -1365 1514 C ATOM 1360 N VAL A 370 18.202 5.521 -35.804 1.00 85.40 N ANISOU 1360 N VAL A 370 12856 11545 8048 -1585 -1224 1225 N ATOM 1361 CA VAL A 370 17.513 6.409 -34.862 1.00 86.15 C ANISOU 1361 CA VAL A 370 13223 11439 8072 -1404 -1297 1174 C ATOM 1362 C VAL A 370 16.975 5.578 -33.681 1.00 88.11 C ANISOU 1362 C VAL A 370 13268 11809 8401 -1225 -1243 1087 C ATOM 1363 O VAL A 370 17.170 5.978 -32.535 1.00 88.86 O ANISOU 1363 O VAL A 370 13492 11804 8466 -1225 -1283 1045 O ATOM 1364 CB VAL A 370 16.387 7.228 -35.570 1.00 91.10 C ANISOU 1364 CB VAL A 370 14081 11928 8607 -1167 -1347 1188 C ATOM 1365 CG1 VAL A 370 15.530 8.013 -34.571 1.00 91.88 C ANISOU 1365 CG1 VAL A 370 14435 11853 8624 -901 -1406 1125 C ATOM 1366 CG2 VAL A 370 16.974 8.169 -36.617 1.00 92.42 C ANISOU 1366 CG2 VAL A 370 14503 11936 8675 -1360 -1413 1281 C ATOM 1367 N LEU A 371 16.357 4.415 -33.960 1.00 82.41 N ANISOU 1367 N LEU A 371 12238 11301 7772 -1101 -1155 1063 N ATOM 1368 CA LEU A 371 15.800 3.522 -32.944 1.00 81.22 C ANISOU 1368 CA LEU A 371 11878 11286 7695 -951 -1099 994 C ATOM 1369 C LEU A 371 16.886 2.959 -32.032 1.00 85.63 C ANISOU 1369 C LEU A 371 12311 11906 8318 -1135 -1071 982 C ATOM 1370 O LEU A 371 16.671 2.909 -30.826 1.00 85.79 O ANISOU 1370 O LEU A 371 12336 11919 8343 -1046 -1076 929 O ATOM 1371 CB LEU A 371 15.001 2.366 -33.576 1.00 80.01 C ANISOU 1371 CB LEU A 371 11442 11345 7614 -841 -1018 985 C ATOM 1372 CG LEU A 371 13.666 2.722 -34.260 1.00 85.63 C ANISOU 1372 CG LEU A 371 12205 12072 8260 -607 -1038 988 C ATOM 1373 CD1 LEU A 371 13.072 1.510 -34.962 1.00 84.52 C ANISOU 1373 CD1 LEU A 371 11778 12153 8182 -580 -964 987 C ATOM 1374 CD2 LEU A 371 12.651 3.303 -33.267 1.00 88.70 C ANISOU 1374 CD2 LEU A 371 12710 12415 8578 -339 -1074 939 C ATOM 1375 N THR A 372 18.052 2.567 -32.596 1.00 82.06 N ANISOU 1375 N THR A 372 11747 11530 7901 -1379 -1043 1035 N ATOM 1376 CA THR A 372 19.200 2.018 -31.859 1.00 80.60 C ANISOU 1376 CA THR A 372 11420 11441 7762 -1557 -1016 1041 C ATOM 1377 C THR A 372 19.790 3.093 -30.929 1.00 84.92 C ANISOU 1377 C THR A 372 12212 11829 8225 -1675 -1107 1040 C ATOM 1378 O THR A 372 20.004 2.805 -29.752 1.00 84.28 O ANISOU 1378 O THR A 372 12072 11785 8167 -1668 -1104 1001 O ATOM 1379 CB THR A 372 20.246 1.456 -32.843 1.00 85.84 C ANISOU 1379 CB THR A 372 11917 12248 8453 -1759 -965 1108 C ATOM 1380 OG1 THR A 372 19.610 0.450 -33.632 1.00 84.91 O ANISOU 1380 OG1 THR A 372 11608 12253 8401 -1635 -886 1094 O ATOM 1381 CG2 THR A 372 21.472 0.851 -32.147 1.00 81.83 C ANISOU 1381 CG2 THR A 372 11234 11880 7977 -1920 -933 1126 C ATOM 1382 N VAL A 373 20.018 4.319 -31.437 1.00 83.14 N ANISOU 1382 N VAL A 373 12277 11419 7893 -1787 -1193 1082 N ATOM 1383 CA VAL A 373 20.572 5.427 -30.643 1.00 84.80 C ANISOU 1383 CA VAL A 373 12778 11443 7998 -1930 -1294 1082 C ATOM 1384 C VAL A 373 19.589 5.792 -29.503 1.00 88.93 C ANISOU 1384 C VAL A 373 13462 11836 8492 -1674 -1326 991 C ATOM 1385 O VAL A 373 20.041 6.045 -28.376 1.00 90.02 O ANISOU 1385 O VAL A 373 13682 11925 8594 -1751 -1367 958 O ATOM 1386 CB VAL A 373 20.925 6.661 -31.522 1.00 90.80 C ANISOU 1386 CB VAL A 373 13856 12007 8636 -2104 -1384 1153 C ATOM 1387 CG1 VAL A 373 21.380 7.846 -30.674 1.00 92.59 C ANISOU 1387 CG1 VAL A 373 14442 12003 8735 -2253 -1500 1145 C ATOM 1388 CG2 VAL A 373 21.995 6.315 -32.555 1.00 90.36 C ANISOU 1388 CG2 VAL A 373 13624 12116 8592 -2377 -1350 1249 C ATOM 1389 N ALA A 374 18.260 5.765 -29.778 1.00 83.91 N ANISOU 1389 N ALA A 374 12845 11176 7862 -1370 -1304 952 N ATOM 1390 CA ALA A 374 17.220 6.075 -28.785 1.00 83.91 C ANISOU 1390 CA ALA A 374 12967 11098 7818 -1085 -1322 871 C ATOM 1391 C ALA A 374 17.218 5.070 -27.608 1.00 86.65 C ANISOU 1391 C ALA A 374 13052 11623 8250 -1036 -1259 817 C ATOM 1392 O ALA A 374 17.061 5.483 -26.456 1.00 87.58 O ANISOU 1392 O ALA A 374 13309 11657 8310 -953 -1296 758 O ATOM 1393 CB ALA A 374 15.852 6.103 -29.442 1.00 84.55 C ANISOU 1393 CB ALA A 374 13044 11198 7883 -782 -1300 860 C ATOM 1394 N ILE A 375 17.424 3.773 -27.892 1.00 80.31 N ANISOU 1394 N ILE A 375 11894 11051 7570 -1089 -1167 838 N ATOM 1395 CA ILE A 375 17.451 2.728 -26.865 1.00 78.49 C ANISOU 1395 CA ILE A 375 11416 10988 7420 -1052 -1105 801 C ATOM 1396 C ILE A 375 18.645 2.951 -25.932 1.00 83.43 C ANISOU 1396 C ILE A 375 12094 11584 8023 -1266 -1146 804 C ATOM 1397 O ILE A 375 18.489 2.828 -24.709 1.00 82.83 O ANISOU 1397 O ILE A 375 12009 11525 7939 -1188 -1148 752 O ATOM 1398 CB ILE A 375 17.466 1.321 -27.514 1.00 79.08 C ANISOU 1398 CB ILE A 375 11152 11280 7615 -1073 -1004 829 C ATOM 1399 CG1 ILE A 375 16.098 1.062 -28.193 1.00 78.67 C ANISOU 1399 CG1 ILE A 375 11041 11282 7570 -850 -971 814 C ATOM 1400 CG2 ILE A 375 17.767 0.241 -26.463 1.00 76.81 C ANISOU 1400 CG2 ILE A 375 10639 11143 7403 -1084 -947 808 C ATOM 1401 CD1 ILE A 375 16.038 0.000 -29.228 1.00 78.63 C ANISOU 1401 CD1 ILE A 375 10805 11426 7644 -892 -897 846 C ATOM 1402 N LEU A 376 19.819 3.306 -26.511 1.00 80.52 N ANISOU 1402 N LEU A 376 11776 11189 7630 -1540 -1181 869 N ATOM 1403 CA LEU A 376 21.058 3.563 -25.772 1.00 80.37 C ANISOU 1403 CA LEU A 376 11791 11177 7568 -1790 -1229 891 C ATOM 1404 C LEU A 376 20.931 4.828 -24.916 1.00 87.50 C ANISOU 1404 C LEU A 376 13059 11846 8341 -1793 -1337 842 C ATOM 1405 O LEU A 376 21.409 4.839 -23.785 1.00 87.97 O ANISOU 1405 O LEU A 376 13127 11926 8374 -1869 -1365 815 O ATOM 1406 CB LEU A 376 22.257 3.680 -26.729 1.00 80.43 C ANISOU 1406 CB LEU A 376 11754 11248 7558 -2084 -1241 984 C ATOM 1407 CG LEU A 376 22.593 2.461 -27.612 1.00 82.69 C ANISOU 1407 CG LEU A 376 11701 11768 7948 -2098 -1135 1033 C ATOM 1408 CD1 LEU A 376 23.748 2.773 -28.550 1.00 83.15 C ANISOU 1408 CD1 LEU A 376 11745 11892 7955 -2378 -1154 1127 C ATOM 1409 CD2 LEU A 376 22.938 1.232 -26.787 1.00 83.38 C ANISOU 1409 CD2 LEU A 376 11495 12062 8122 -2055 -1061 1019 C ATOM 1410 N ALA A 377 20.248 5.867 -25.435 1.00 86.86 N ANISOU 1410 N ALA A 377 13290 11539 8172 -1691 -1397 830 N ATOM 1411 CA ALA A 377 20.005 7.136 -24.736 1.00 89.07 C ANISOU 1411 CA ALA A 377 13983 11551 8308 -1649 -1501 777 C ATOM 1412 C ALA A 377 19.163 6.930 -23.472 1.00 93.92 C ANISOU 1412 C ALA A 377 14588 12179 8917 -1377 -1480 680 C ATOM 1413 O ALA A 377 19.446 7.571 -22.458 1.00 96.15 O ANISOU 1413 O ALA A 377 15097 12334 9102 -1429 -1550 632 O ATOM 1414 CB ALA A 377 19.309 8.120 -25.667 1.00 91.24 C ANISOU 1414 CB ALA A 377 14569 11601 8496 -1528 -1552 788 C ATOM 1415 N VAL A 378 18.151 6.021 -23.524 1.00 88.59 N ANISOU 1415 N VAL A 378 13650 11675 8336 -1106 -1385 655 N ATOM 1416 CA VAL A 378 17.259 5.688 -22.395 1.00 87.55 C ANISOU 1416 CA VAL A 378 13451 11613 8199 -839 -1349 576 C ATOM 1417 C VAL A 378 17.837 4.491 -21.591 1.00 90.88 C ANISOU 1417 C VAL A 378 13538 12266 8726 -947 -1284 581 C ATOM 1418 O VAL A 378 17.298 4.151 -20.527 1.00 89.92 O ANISOU 1418 O VAL A 378 13346 12220 8600 -781 -1256 525 O ATOM 1419 CB VAL A 378 15.785 5.416 -22.829 1.00 90.15 C ANISOU 1419 CB VAL A 378 13686 12023 8542 -498 -1290 555 C ATOM 1420 CG1 VAL A 378 15.183 6.619 -23.549 1.00 91.70 C ANISOU 1420 CG1 VAL A 378 14223 12000 8620 -349 -1356 553 C ATOM 1421 CG2 VAL A 378 15.653 4.152 -23.673 1.00 87.73 C ANISOU 1421 CG2 VAL A 378 13003 11951 8378 -529 -1195 608 C ATOM 1422 N ALA A 379 18.937 3.873 -22.108 1.00 87.10 N ANISOU 1422 N ALA A 379 12861 11903 8329 -1211 -1260 652 N ATOM 1423 CA ALA A 379 19.667 2.727 -21.542 1.00 85.44 C ANISOU 1423 CA ALA A 379 12341 11910 8212 -1326 -1201 677 C ATOM 1424 C ALA A 379 18.698 1.607 -21.105 1.00 87.45 C ANISOU 1424 C ALA A 379 12344 12330 8551 -1089 -1107 646 C ATOM 1425 O ALA A 379 18.510 1.370 -19.910 1.00 86.64 O ANISOU 1425 O ALA A 379 12206 12279 8435 -1009 -1100 603 O ATOM 1426 CB ALA A 379 20.544 3.170 -20.377 1.00 87.04 C ANISOU 1426 CB ALA A 379 12654 12077 8338 -1491 -1269 660 C ATOM 1427 N GLN A 380 18.072 0.935 -22.088 1.00 82.82 N ANISOU 1427 N GLN A 380 11595 11830 8041 -994 -1039 670 N ATOM 1428 CA GLN A 380 17.110 -0.125 -21.802 1.00 80.91 C ANISOU 1428 CA GLN A 380 11129 11748 7867 -808 -957 651 C ATOM 1429 C GLN A 380 17.531 -1.460 -22.441 1.00 82.27 C ANISOU 1429 C GLN A 380 11022 12081 8156 -903 -875 704 C ATOM 1430 O GLN A 380 16.679 -2.282 -22.790 1.00 81.06 O ANISOU 1430 O GLN A 380 10716 12031 8053 -788 -813 704 O ATOM 1431 CB GLN A 380 15.702 0.289 -22.253 1.00 82.61 C ANISOU 1431 CB GLN A 380 11423 11931 8033 -568 -956 621 C ATOM 1432 CG GLN A 380 15.051 1.324 -21.329 1.00 93.34 C ANISOU 1432 CG GLN A 380 13019 13178 9268 -383 -1013 555 C ATOM 1433 CD GLN A 380 14.799 0.838 -19.913 1.00104.39 C ANISOU 1433 CD GLN A 380 14317 14689 10660 -295 -985 514 C ATOM 1434 OE1 GLN A 380 14.484 -0.333 -19.661 1.00 93.22 O ANISOU 1434 OE1 GLN A 380 12635 13463 9322 -272 -911 531 O ATOM 1435 NE2 GLN A 380 14.897 1.751 -18.956 1.00 97.97 N ANISOU 1435 NE2 GLN A 380 13737 13750 9739 -244 -1048 459 N ATOM 1436 N VAL A 381 18.851 -1.701 -22.512 1.00 77.74 N ANISOU 1436 N VAL A 381 10384 11542 7611 -1109 -877 749 N ATOM 1437 CA VAL A 381 19.426 -2.953 -23.009 1.00 75.49 C ANISOU 1437 CA VAL A 381 9860 11406 7419 -1181 -799 798 C ATOM 1438 C VAL A 381 19.651 -3.893 -21.805 1.00 78.15 C ANISOU 1438 C VAL A 381 10040 11860 7793 -1153 -760 794 C ATOM 1439 O VAL A 381 20.284 -3.502 -20.816 1.00 77.64 O ANISOU 1439 O VAL A 381 10025 11792 7684 -1222 -804 789 O ATOM 1440 CB VAL A 381 20.723 -2.727 -23.816 1.00 78.90 C ANISOU 1440 CB VAL A 381 10285 11852 7842 -1391 -814 859 C ATOM 1441 CG1 VAL A 381 21.349 -4.049 -24.236 1.00 77.79 C ANISOU 1441 CG1 VAL A 381 9905 11874 7779 -1423 -728 903 C ATOM 1442 CG2 VAL A 381 20.471 -1.842 -25.023 1.00 79.03 C ANISOU 1442 CG2 VAL A 381 10460 11751 7816 -1424 -852 871 C ATOM 1443 N ASP A 382 19.122 -5.124 -21.901 1.00 73.04 N ANISOU 1443 N ASP A 382 9222 11313 7217 -1063 -681 799 N ATOM 1444 CA ASP A 382 19.222 -6.152 -20.864 1.00 71.96 C ANISOU 1444 CA ASP A 382 8945 11281 7117 -1025 -636 806 C ATOM 1445 C ASP A 382 19.855 -7.407 -21.431 1.00 75.22 C ANISOU 1445 C ASP A 382 9197 11784 7598 -1067 -564 854 C ATOM 1446 O ASP A 382 19.611 -7.741 -22.589 1.00 76.87 O ANISOU 1446 O ASP A 382 9384 11986 7837 -1066 -529 862 O ATOM 1447 CB ASP A 382 17.823 -6.482 -20.297 1.00 73.30 C ANISOU 1447 CB ASP A 382 9093 11476 7281 -866 -613 767 C ATOM 1448 CG ASP A 382 16.935 -5.282 -19.981 1.00 83.00 C ANISOU 1448 CG ASP A 382 10483 12625 8427 -759 -671 714 C ATOM 1449 OD1 ASP A 382 17.331 -4.453 -19.120 1.00 83.59 O ANISOU 1449 OD1 ASP A 382 10682 12640 8440 -775 -729 689 O ATOM 1450 OD2 ASP A 382 15.818 -5.206 -20.546 1.00 86.09 O ANISOU 1450 OD2 ASP A 382 10881 13025 8805 -648 -659 697 O ATOM 1451 N GLY A 383 20.654 -8.089 -20.626 1.00 70.47 N ANISOU 1451 N GLY A 383 8496 11269 7011 -1091 -542 885 N ATOM 1452 CA GLY A 383 21.301 -9.336 -21.011 1.00 69.99 C ANISOU 1452 CA GLY A 383 8301 11292 6999 -1091 -471 931 C ATOM 1453 C GLY A 383 20.444 -10.536 -20.664 1.00 74.53 C ANISOU 1453 C GLY A 383 8821 11883 7616 -988 -412 924 C ATOM 1454 O GLY A 383 19.594 -10.460 -19.767 1.00 75.03 O ANISOU 1454 O GLY A 383 8904 11941 7665 -930 -427 898 O ATOM 1455 N ASP A 384 20.642 -11.654 -21.375 1.00 69.86 N ANISOU 1455 N ASP A 384 8171 11310 7062 -968 -346 949 N ATOM 1456 CA ASP A 384 19.901 -12.882 -21.099 1.00 68.74 C ANISOU 1456 CA ASP A 384 8005 11165 6947 -903 -294 951 C ATOM 1457 C ASP A 384 20.749 -14.070 -21.507 1.00 73.52 C ANISOU 1457 C ASP A 384 8569 11792 7571 -876 -230 991 C ATOM 1458 O ASP A 384 21.210 -14.136 -22.641 1.00 73.99 O ANISOU 1458 O ASP A 384 8632 11846 7634 -892 -206 995 O ATOM 1459 CB ASP A 384 18.538 -12.894 -21.800 1.00 69.66 C ANISOU 1459 CB ASP A 384 8164 11236 7066 -895 -290 914 C ATOM 1460 CG ASP A 384 17.842 -14.243 -21.861 1.00 76.88 C ANISOU 1460 CG ASP A 384 9070 12146 7995 -879 -238 924 C ATOM 1461 OD1 ASP A 384 17.794 -14.939 -20.820 1.00 75.13 O ANISOU 1461 OD1 ASP A 384 8826 11949 7773 -855 -222 947 O ATOM 1462 OD2 ASP A 384 17.330 -14.594 -22.946 1.00 82.46 O ANISOU 1462 OD2 ASP A 384 9804 12822 8705 -905 -218 909 O ATOM 1463 N SER A 385 20.952 -15.011 -20.581 1.00 70.21 N ANISOU 1463 N SER A 385 8123 11399 7156 -822 -202 1023 N ATOM 1464 CA SER A 385 21.767 -16.191 -20.831 1.00 70.56 C ANISOU 1464 CA SER A 385 8153 11455 7203 -756 -141 1065 C ATOM 1465 C SER A 385 21.037 -17.249 -21.702 1.00 76.63 C ANISOU 1465 C SER A 385 9007 12125 7983 -740 -90 1047 C ATOM 1466 O SER A 385 21.734 -17.972 -22.425 1.00 76.56 O ANISOU 1466 O SER A 385 9020 12104 7965 -683 -40 1062 O ATOM 1467 CB SER A 385 22.243 -16.816 -19.525 1.00 72.11 C ANISOU 1467 CB SER A 385 8311 11701 7385 -693 -133 1112 C ATOM 1468 OG SER A 385 21.203 -16.913 -18.570 1.00 80.96 O ANISOU 1468 OG SER A 385 9459 12794 8508 -707 -153 1100 O ATOM 1469 N VAL A 386 19.676 -17.319 -21.699 1.00 73.99 N ANISOU 1469 N VAL A 386 8721 11737 7654 -791 -103 1015 N ATOM 1470 CA VAL A 386 19.033 -18.335 -22.544 1.00 74.82 C ANISOU 1470 CA VAL A 386 8916 11758 7755 -810 -64 1001 C ATOM 1471 C VAL A 386 19.140 -17.907 -24.035 1.00 77.33 C ANISOU 1471 C VAL A 386 9252 12058 8073 -838 -59 967 C ATOM 1472 O VAL A 386 19.647 -18.711 -24.831 1.00 78.50 O ANISOU 1472 O VAL A 386 9461 12158 8209 -801 -10 968 O ATOM 1473 CB VAL A 386 17.583 -18.783 -22.169 1.00 80.06 C ANISOU 1473 CB VAL A 386 9616 12401 8402 -881 -76 993 C ATOM 1474 CG1 VAL A 386 17.581 -19.663 -20.946 1.00 80.20 C ANISOU 1474 CG1 VAL A 386 9655 12410 8408 -859 -61 1039 C ATOM 1475 CG2 VAL A 386 16.625 -17.632 -21.989 1.00 80.08 C ANISOU 1475 CG2 VAL A 386 9554 12477 8398 -921 -127 965 C ATOM 1476 N SER A 387 18.780 -16.652 -24.407 1.00 71.15 N ANISOU 1476 N SER A 387 8430 11311 7293 -885 -106 941 N ATOM 1477 CA SER A 387 18.935 -16.242 -25.819 1.00 70.53 C ANISOU 1477 CA SER A 387 8372 11219 7208 -914 -101 918 C ATOM 1478 C SER A 387 20.429 -16.011 -26.158 1.00 76.52 C ANISOU 1478 C SER A 387 9087 12026 7959 -879 -80 946 C ATOM 1479 O SER A 387 20.811 -16.116 -27.331 1.00 76.89 O ANISOU 1479 O SER A 387 9153 12070 7990 -881 -51 938 O ATOM 1480 CB SER A 387 18.099 -15.005 -26.160 1.00 70.67 C ANISOU 1480 CB SER A 387 8383 11251 7217 -962 -159 891 C ATOM 1481 OG SER A 387 18.488 -13.836 -25.459 1.00 73.92 O ANISOU 1481 OG SER A 387 8765 11695 7627 -959 -209 898 O ATOM 1482 N GLY A 388 21.247 -15.766 -25.125 1.00 73.46 N ANISOU 1482 N GLY A 388 8635 11704 7573 -851 -93 982 N ATOM 1483 CA GLY A 388 22.684 -15.529 -25.244 1.00 73.34 C ANISOU 1483 CA GLY A 388 8543 11788 7533 -831 -80 1023 C ATOM 1484 C GLY A 388 23.057 -14.216 -25.909 1.00 75.40 C ANISOU 1484 C GLY A 388 8780 12094 7775 -927 -123 1024 C ATOM 1485 O GLY A 388 24.178 -14.072 -26.400 1.00 73.68 O ANISOU 1485 O GLY A 388 8496 11977 7522 -936 -104 1061 O ATOM 1486 N ILE A 389 22.123 -13.239 -25.914 1.00 72.55 N ANISOU 1486 N ILE A 389 8476 11668 7423 -994 -183 990 N ATOM 1487 CA ILE A 389 22.309 -11.910 -26.506 1.00 73.02 C ANISOU 1487 CA ILE A 389 8561 11728 7454 -1089 -237 991 C ATOM 1488 C ILE A 389 21.856 -10.816 -25.528 1.00 77.19 C ANISOU 1488 C ILE A 389 9141 12215 7972 -1126 -315 974 C ATOM 1489 O ILE A 389 21.306 -11.096 -24.467 1.00 75.60 O ANISOU 1489 O ILE A 389 8939 12000 7786 -1073 -323 958 O ATOM 1490 CB ILE A 389 21.556 -11.750 -27.880 1.00 75.99 C ANISOU 1490 CB ILE A 389 9003 12041 7829 -1107 -231 961 C ATOM 1491 CG1 ILE A 389 20.013 -11.795 -27.724 1.00 76.47 C ANISOU 1491 CG1 ILE A 389 9123 12024 7907 -1072 -251 915 C ATOM 1492 CG2 ILE A 389 22.061 -12.702 -28.965 1.00 76.01 C ANISOU 1492 CG2 ILE A 389 8980 12079 7823 -1076 -157 969 C ATOM 1493 CD1 ILE A 389 19.225 -10.821 -28.673 1.00 82.54 C ANISOU 1493 CD1 ILE A 389 9964 12745 8651 -1104 -296 895 C ATOM 1494 N CYS A 390 22.064 -9.568 -25.922 1.00 76.19 N ANISOU 1494 N CYS A 390 9078 12061 7808 -1216 -374 978 N ATOM 1495 CA CYS A 390 21.597 -8.394 -25.203 1.00 77.19 C ANISOU 1495 CA CYS A 390 9309 12114 7904 -1242 -454 953 C ATOM 1496 C CYS A 390 20.506 -7.779 -26.032 1.00 78.68 C ANISOU 1496 C CYS A 390 9605 12208 8084 -1213 -479 919 C ATOM 1497 O CYS A 390 20.667 -7.716 -27.252 1.00 79.32 O ANISOU 1497 O CYS A 390 9694 12285 8158 -1255 -463 935 O ATOM 1498 CB CYS A 390 22.736 -7.418 -24.940 1.00 79.14 C ANISOU 1498 CB CYS A 390 9585 12391 8094 -1379 -513 989 C ATOM 1499 SG CYS A 390 23.698 -7.789 -23.460 1.00 83.78 S ANISOU 1499 SG CYS A 390 10069 13094 8668 -1400 -519 1019 S ATOM 1500 N PHE A 391 19.384 -7.367 -25.414 1.00 72.34 N ANISOU 1500 N PHE A 391 8872 11346 7268 -1127 -513 877 N ATOM 1501 CA PHE A 391 18.256 -6.838 -26.182 1.00 71.19 C ANISOU 1501 CA PHE A 391 8808 11140 7099 -1066 -534 851 C ATOM 1502 C PHE A 391 17.479 -5.783 -25.385 1.00 75.18 C ANISOU 1502 C PHE A 391 9440 11577 7550 -981 -599 815 C ATOM 1503 O PHE A 391 17.705 -5.618 -24.191 1.00 76.85 O ANISOU 1503 O PHE A 391 9665 11789 7746 -969 -620 801 O ATOM 1504 CB PHE A 391 17.334 -8.011 -26.596 1.00 72.07 C ANISOU 1504 CB PHE A 391 8822 11312 7249 -998 -473 839 C ATOM 1505 CG PHE A 391 16.460 -7.771 -27.801 1.00 73.89 C ANISOU 1505 CG PHE A 391 9089 11529 7458 -972 -480 830 C ATOM 1506 CD1 PHE A 391 17.021 -7.584 -29.063 1.00 76.53 C ANISOU 1506 CD1 PHE A 391 9451 11841 7787 -1048 -474 852 C ATOM 1507 CD2 PHE A 391 15.077 -7.778 -27.687 1.00 75.86 C ANISOU 1507 CD2 PHE A 391 9327 11816 7680 -872 -489 806 C ATOM 1508 CE1 PHE A 391 16.214 -7.355 -30.175 1.00 77.45 C ANISOU 1508 CE1 PHE A 391 9600 11951 7875 -1023 -484 848 C ATOM 1509 CE2 PHE A 391 14.268 -7.565 -28.807 1.00 79.03 C ANISOU 1509 CE2 PHE A 391 9746 12232 8049 -846 -499 805 C ATOM 1510 CZ PHE A 391 14.841 -7.352 -30.041 1.00 77.10 C ANISOU 1510 CZ PHE A 391 9544 11945 7804 -921 -499 824 C ATOM 1511 N VAL A 392 16.568 -5.073 -26.055 1.00 71.29 N ANISOU 1511 N VAL A 392 9043 11031 7014 -906 -631 798 N ATOM 1512 CA VAL A 392 15.757 -3.990 -25.494 1.00 72.03 C ANISOU 1512 CA VAL A 392 9283 11053 7031 -780 -691 763 C ATOM 1513 C VAL A 392 14.433 -4.532 -24.909 1.00 77.20 C ANISOU 1513 C VAL A 392 9838 11817 7677 -618 -661 735 C ATOM 1514 O VAL A 392 13.751 -5.338 -25.548 1.00 76.86 O ANISOU 1514 O VAL A 392 9673 11872 7660 -599 -617 745 O ATOM 1515 CB VAL A 392 15.491 -2.866 -26.556 1.00 75.75 C ANISOU 1515 CB VAL A 392 9927 11414 7442 -761 -745 771 C ATOM 1516 CG1 VAL A 392 14.862 -3.415 -27.846 1.00 75.06 C ANISOU 1516 CG1 VAL A 392 9745 11397 7376 -740 -707 790 C ATOM 1517 CG2 VAL A 392 14.662 -1.718 -25.981 1.00 76.22 C ANISOU 1517 CG2 VAL A 392 10173 11383 7404 -592 -807 732 C ATOM 1518 N GLY A 393 14.086 -4.045 -23.716 1.00 74.12 N ANISOU 1518 N GLY A 393 9509 11419 7234 -515 -688 701 N ATOM 1519 CA GLY A 393 12.824 -4.352 -23.057 1.00 74.62 C ANISOU 1519 CA GLY A 393 9485 11608 7258 -352 -666 679 C ATOM 1520 C GLY A 393 12.594 -5.766 -22.558 1.00 79.15 C ANISOU 1520 C GLY A 393 9852 12332 7889 -391 -599 696 C ATOM 1521 O GLY A 393 11.437 -6.171 -22.400 1.00 79.68 O ANISOU 1521 O GLY A 393 9815 12540 7921 -295 -574 696 O ATOM 1522 N TYR A 394 13.676 -6.525 -22.291 1.00 74.97 N ANISOU 1522 N TYR A 394 9265 11786 7434 -530 -570 718 N ATOM 1523 CA TYR A 394 13.591 -7.854 -21.688 1.00 74.05 C ANISOU 1523 CA TYR A 394 8997 11777 7363 -566 -512 739 C ATOM 1524 C TYR A 394 12.957 -7.722 -20.278 1.00 80.29 C ANISOU 1524 C TYR A 394 9766 12646 8096 -459 -518 718 C ATOM 1525 O TYR A 394 11.986 -8.428 -19.955 1.00 79.52 O ANISOU 1525 O TYR A 394 9554 12684 7978 -416 -483 729 O ATOM 1526 CB TYR A 394 14.990 -8.505 -21.613 1.00 73.90 C ANISOU 1526 CB TYR A 394 8948 11715 7413 -695 -488 768 C ATOM 1527 CG TYR A 394 15.470 -9.300 -22.820 1.00 73.72 C ANISOU 1527 CG TYR A 394 8881 11681 7449 -785 -447 796 C ATOM 1528 CD1 TYR A 394 14.582 -9.710 -23.818 1.00 75.12 C ANISOU 1528 CD1 TYR A 394 9027 11890 7624 -778 -425 795 C ATOM 1529 CD2 TYR A 394 16.793 -9.734 -22.909 1.00 73.48 C ANISOU 1529 CD2 TYR A 394 8828 11631 7461 -869 -425 826 C ATOM 1530 CE1 TYR A 394 15.007 -10.508 -24.884 1.00 73.53 C ANISOU 1530 CE1 TYR A 394 8801 11673 7464 -856 -385 813 C ATOM 1531 CE2 TYR A 394 17.225 -10.536 -23.964 1.00 73.63 C ANISOU 1531 CE2 TYR A 394 8810 11649 7517 -921 -378 847 C ATOM 1532 CZ TYR A 394 16.325 -10.936 -24.939 1.00 79.94 C ANISOU 1532 CZ TYR A 394 9605 12453 8316 -915 -358 836 C ATOM 1533 OH TYR A 394 16.766 -11.722 -25.970 1.00 77.84 O ANISOU 1533 OH TYR A 394 9326 12176 8074 -963 -312 848 O ATOM 1534 N LYS A 395 13.454 -6.730 -19.486 1.00 78.20 N ANISOU 1534 N LYS A 395 9624 12301 7785 -420 -567 687 N ATOM 1535 CA LYS A 395 12.978 -6.435 -18.128 1.00 79.11 C ANISOU 1535 CA LYS A 395 9752 12476 7830 -308 -578 658 C ATOM 1536 C LYS A 395 11.770 -5.453 -18.154 1.00 83.68 C ANISOU 1536 C LYS A 395 10410 13083 8301 -111 -606 617 C ATOM 1537 O LYS A 395 10.677 -5.839 -17.739 1.00 83.45 O ANISOU 1537 O LYS A 395 10265 13220 8222 -3 -573 620 O ATOM 1538 CB LYS A 395 14.124 -5.884 -17.262 1.00 81.94 C ANISOU 1538 CB LYS A 395 10219 12737 8176 -371 -621 641 C ATOM 1539 CG LYS A 395 14.225 -6.535 -15.894 1.00 99.02 C ANISOU 1539 CG LYS A 395 12293 14998 10332 -365 -597 647 C ATOM 1540 CD LYS A 395 13.565 -5.715 -14.790 1.00111.40 C ANISOU 1540 CD LYS A 395 13951 16588 11787 -212 -628 592 C ATOM 1541 CE LYS A 395 13.860 -6.265 -13.410 1.00125.36 C ANISOU 1541 CE LYS A 395 15647 18443 13541 -228 -612 601 C ATOM 1542 NZ LYS A 395 13.220 -7.589 -13.164 1.00134.56 N ANISOU 1542 NZ LYS A 395 16613 19771 14742 -228 -541 651 N ATOM 1543 N ASN A 396 11.954 -4.217 -18.658 1.00 80.58 N ANISOU 1543 N ASN A 396 10216 12541 7860 -63 -665 587 N ATOM 1544 CA ASN A 396 10.879 -3.224 -18.741 1.00 81.57 C ANISOU 1544 CA ASN A 396 10450 12672 7870 158 -695 550 C ATOM 1545 C ASN A 396 10.135 -3.389 -20.082 1.00 86.74 C ANISOU 1545 C ASN A 396 11030 13391 8534 190 -679 581 C ATOM 1546 O ASN A 396 10.547 -2.846 -21.114 1.00 86.65 O ANISOU 1546 O ASN A 396 11139 13243 8540 137 -713 590 O ATOM 1547 CB ASN A 396 11.436 -1.813 -18.558 1.00 81.82 C ANISOU 1547 CB ASN A 396 10775 12485 7827 198 -773 504 C ATOM 1548 CG ASN A 396 12.196 -1.639 -17.265 1.00 99.11 C ANISOU 1548 CG ASN A 396 13043 14618 9994 142 -796 471 C ATOM 1549 OD1 ASN A 396 11.632 -1.699 -16.169 1.00 91.73 O ANISOU 1549 OD1 ASN A 396 12076 13786 8993 276 -780 440 O ATOM 1550 ND2 ASN A 396 13.501 -1.437 -17.364 1.00 88.81 N ANISOU 1550 ND2 ASN A 396 11834 13176 8735 -65 -836 483 N ATOM 1551 N TYR A 397 9.030 -4.158 -20.042 1.00 83.92 N ANISOU 1551 N TYR A 397 10470 13259 8156 261 -631 604 N ATOM 1552 CA TYR A 397 8.189 -4.559 -21.180 1.00 84.04 C ANISOU 1552 CA TYR A 397 10362 13401 8169 269 -611 640 C ATOM 1553 C TYR A 397 7.614 -3.368 -21.996 1.00 88.56 C ANISOU 1553 C TYR A 397 11076 13922 8650 448 -659 627 C ATOM 1554 O TYR A 397 7.276 -3.563 -23.167 1.00 88.42 O ANISOU 1554 O TYR A 397 11001 13948 8647 412 -657 659 O ATOM 1555 CB TYR A 397 7.032 -5.467 -20.713 1.00 85.69 C ANISOU 1555 CB TYR A 397 10336 13892 8332 312 -561 668 C ATOM 1556 CG TYR A 397 6.185 -4.891 -19.603 1.00 89.58 C ANISOU 1556 CG TYR A 397 10820 14524 8693 542 -563 641 C ATOM 1557 CD1 TYR A 397 5.053 -4.129 -19.886 1.00 93.24 C ANISOU 1557 CD1 TYR A 397 11280 15123 9023 783 -579 636 C ATOM 1558 CD2 TYR A 397 6.490 -5.136 -18.268 1.00 90.86 C ANISOU 1558 CD2 TYR A 397 10969 14704 8851 535 -545 624 C ATOM 1559 CE1 TYR A 397 4.274 -3.586 -18.866 1.00 96.39 C ANISOU 1559 CE1 TYR A 397 11672 15669 9284 1028 -574 610 C ATOM 1560 CE2 TYR A 397 5.713 -4.607 -17.239 1.00 93.32 C ANISOU 1560 CE2 TYR A 397 11274 15155 9028 758 -541 595 C ATOM 1561 CZ TYR A 397 4.605 -3.834 -17.542 1.00103.36 C ANISOU 1561 CZ TYR A 397 12547 16561 10163 1011 -553 586 C ATOM 1562 OH TYR A 397 3.850 -3.306 -16.525 1.00106.68 O ANISOU 1562 OH TYR A 397 12963 17135 10435 1261 -543 556 O ATOM 1563 N ARG A 398 7.508 -2.162 -21.399 1.00 85.30 N ANISOU 1563 N ARG A 398 10865 13410 8137 643 -704 582 N ATOM 1564 CA ARG A 398 7.016 -0.966 -22.092 1.00 85.51 C ANISOU 1564 CA ARG A 398 11075 13352 8062 839 -755 571 C ATOM 1565 C ARG A 398 7.952 -0.584 -23.219 1.00 87.05 C ANISOU 1565 C ARG A 398 11428 13321 8326 675 -795 589 C ATOM 1566 O ARG A 398 7.492 -0.078 -24.232 1.00 88.22 O ANISOU 1566 O ARG A 398 11638 13454 8427 763 -820 610 O ATOM 1567 CB ARG A 398 6.846 0.231 -21.130 1.00 87.74 C ANISOU 1567 CB ARG A 398 11598 13528 8213 1077 -798 510 C ATOM 1568 CG ARG A 398 5.590 0.161 -20.257 1.00102.08 C ANISOU 1568 CG ARG A 398 13274 15608 9902 1341 -762 496 C ATOM 1569 CD ARG A 398 5.182 1.536 -19.757 1.00119.82 C ANISOU 1569 CD ARG A 398 15799 17746 11982 1658 -809 437 C ATOM 1570 NE ARG A 398 4.023 1.492 -18.858 1.00139.59 N ANISOU 1570 NE ARG A 398 18162 20529 14348 1934 -768 422 N ATOM 1571 CZ ARG A 398 4.092 1.535 -17.527 1.00158.20 C ANISOU 1571 CZ ARG A 398 20548 22911 16649 2004 -753 372 C ATOM 1572 NH1 ARG A 398 5.270 1.625 -16.916 1.00143.55 N ANISOU 1572 NH1 ARG A 398 18859 20815 14866 1812 -781 333 N ATOM 1573 NH2 ARG A 398 2.984 1.494 -16.797 1.00146.50 N ANISOU 1573 NH2 ARG A 398 18919 21718 15027 2265 -710 366 N ATOM 1574 N TYR A 399 9.262 -0.845 -23.056 1.00 81.74 N ANISOU 1574 N TYR A 399 10806 12499 7755 436 -799 589 N ATOM 1575 CA TYR A 399 10.279 -0.515 -24.057 1.00 80.48 C ANISOU 1575 CA TYR A 399 10776 12151 7651 253 -832 614 C ATOM 1576 C TYR A 399 10.286 -1.512 -25.210 1.00 81.10 C ANISOU 1576 C TYR A 399 10659 12337 7821 111 -786 662 C ATOM 1577 O TYR A 399 10.681 -1.143 -26.314 1.00 80.51 O ANISOU 1577 O TYR A 399 10673 12159 7757 32 -810 689 O ATOM 1578 CB TYR A 399 11.654 -0.403 -23.417 1.00 80.94 C ANISOU 1578 CB TYR A 399 10936 12059 7759 59 -854 603 C ATOM 1579 CG TYR A 399 11.744 0.869 -22.611 1.00 84.09 C ANISOU 1579 CG TYR A 399 11620 12285 8045 170 -923 553 C ATOM 1580 CD1 TYR A 399 11.496 0.869 -21.240 1.00 85.79 C ANISOU 1580 CD1 TYR A 399 11836 12551 8211 278 -918 506 C ATOM 1581 CD2 TYR A 399 11.969 2.096 -23.233 1.00 86.33 C ANISOU 1581 CD2 TYR A 399 12197 12351 8252 184 -997 553 C ATOM 1582 CE1 TYR A 399 11.555 2.045 -20.495 1.00 87.49 C ANISOU 1582 CE1 TYR A 399 12343 12593 8305 389 -984 450 C ATOM 1583 CE2 TYR A 399 12.010 3.281 -22.501 1.00 89.06 C ANISOU 1583 CE2 TYR A 399 12854 12508 8476 290 -1067 502 C ATOM 1584 CZ TYR A 399 11.817 3.248 -21.130 1.00 96.03 C ANISOU 1584 CZ TYR A 399 13739 13437 9312 393 -1060 446 C ATOM 1585 OH TYR A 399 11.859 4.416 -20.411 1.00 99.02 O ANISOU 1585 OH TYR A 399 14453 13615 9556 502 -1132 387 O ATOM 1586 N ARG A 400 9.801 -2.734 -24.981 1.00 76.25 N ANISOU 1586 N ARG A 400 9796 11921 7253 81 -723 674 N ATOM 1587 CA ARG A 400 9.625 -3.717 -26.043 1.00 75.73 C ANISOU 1587 CA ARG A 400 9565 11960 7248 -37 -682 711 C ATOM 1588 C ARG A 400 8.448 -3.262 -26.906 1.00 81.06 C ANISOU 1588 C ARG A 400 10230 12734 7834 118 -703 726 C ATOM 1589 O ARG A 400 8.521 -3.305 -28.129 1.00 81.13 O ANISOU 1589 O ARG A 400 10243 12722 7859 47 -709 752 O ATOM 1590 CB ARG A 400 9.383 -5.096 -25.441 1.00 75.20 C ANISOU 1590 CB ARG A 400 9283 12057 7233 -116 -620 719 C ATOM 1591 CG ARG A 400 9.398 -6.249 -26.420 1.00 77.74 C ANISOU 1591 CG ARG A 400 9473 12446 7618 -273 -578 749 C ATOM 1592 CD ARG A 400 8.813 -7.442 -25.697 1.00 89.26 C ANISOU 1592 CD ARG A 400 10758 14073 9085 -314 -530 760 C ATOM 1593 NE ARG A 400 9.257 -8.706 -26.265 1.00 92.73 N ANISOU 1593 NE ARG A 400 11127 14506 9600 -498 -486 779 N ATOM 1594 CZ ARG A 400 10.040 -9.582 -25.647 1.00 96.60 C ANISOU 1594 CZ ARG A 400 11597 14948 10159 -600 -449 783 C ATOM 1595 NH1 ARG A 400 10.449 -9.358 -24.404 1.00 72.71 N ANISOU 1595 NH1 ARG A 400 8591 11895 7140 -554 -451 774 N ATOM 1596 NH2 ARG A 400 10.385 -10.706 -26.249 1.00 86.05 N ANISOU 1596 NH2 ARG A 400 10230 13593 8874 -737 -410 798 N ATOM 1597 N ALA A 401 7.386 -2.760 -26.249 1.00 77.19 N ANISOU 1597 N ALA A 401 9731 12362 7236 348 -716 711 N ATOM 1598 CA ALA A 401 6.197 -2.236 -26.898 1.00 77.43 C ANISOU 1598 CA ALA A 401 9741 12526 7155 547 -739 729 C ATOM 1599 C ALA A 401 6.538 -1.068 -27.846 1.00 82.46 C ANISOU 1599 C ALA A 401 10622 12956 7754 605 -799 737 C ATOM 1600 O ALA A 401 6.100 -1.066 -28.999 1.00 81.72 O ANISOU 1600 O ALA A 401 10488 12927 7637 612 -809 773 O ATOM 1601 CB ALA A 401 5.198 -1.787 -25.846 1.00 78.85 C ANISOU 1601 CB ALA A 401 9893 12857 7210 811 -740 708 C ATOM 1602 N GLY A 402 7.344 -0.123 -27.366 1.00 79.74 N ANISOU 1602 N GLY A 402 10534 12365 7399 622 -842 707 N ATOM 1603 CA GLY A 402 7.722 1.061 -28.126 1.00 80.79 C ANISOU 1603 CA GLY A 402 10944 12271 7480 659 -907 718 C ATOM 1604 C GLY A 402 8.809 0.892 -29.165 1.00 84.61 C ANISOU 1604 C GLY A 402 11472 12619 8056 394 -913 753 C ATOM 1605 O GLY A 402 8.800 1.607 -30.176 1.00 85.66 O ANISOU 1605 O GLY A 402 11755 12651 8142 418 -956 785 O ATOM 1606 N PHE A 403 9.766 -0.032 -28.930 1.00 78.91 N ANISOU 1606 N PHE A 403 10626 11902 7454 153 -870 752 N ATOM 1607 CA PHE A 403 10.904 -0.216 -29.837 1.00 77.49 C ANISOU 1607 CA PHE A 403 10473 11621 7349 -90 -867 785 C ATOM 1608 C PHE A 403 10.885 -1.543 -30.625 1.00 80.86 C ANISOU 1608 C PHE A 403 10653 12208 7860 -223 -801 807 C ATOM 1609 O PHE A 403 11.751 -1.742 -31.485 1.00 80.27 O ANISOU 1609 O PHE A 403 10586 12078 7833 -397 -790 835 O ATOM 1610 CB PHE A 403 12.224 -0.112 -29.059 1.00 78.08 C ANISOU 1610 CB PHE A 403 10631 11563 7472 -263 -876 774 C ATOM 1611 CG PHE A 403 12.507 1.295 -28.596 1.00 80.35 C ANISOU 1611 CG PHE A 403 11227 11636 7667 -209 -957 758 C ATOM 1612 CD1 PHE A 403 12.955 2.263 -29.491 1.00 83.49 C ANISOU 1612 CD1 PHE A 403 11851 11860 8011 -281 -1016 795 C ATOM 1613 CD2 PHE A 403 12.342 1.651 -27.263 1.00 82.62 C ANISOU 1613 CD2 PHE A 403 11598 11886 7908 -98 -977 708 C ATOM 1614 CE1 PHE A 403 13.215 3.566 -29.064 1.00 85.83 C ANISOU 1614 CE1 PHE A 403 12477 11929 8206 -250 -1099 781 C ATOM 1615 CE2 PHE A 403 12.611 2.955 -26.834 1.00 86.81 C ANISOU 1615 CE2 PHE A 403 12454 12193 8336 -56 -1057 686 C ATOM 1616 CZ PHE A 403 13.039 3.905 -27.740 1.00 85.77 C ANISOU 1616 CZ PHE A 403 12568 11871 8150 -136 -1121 723 C ATOM 1617 N VAL A 404 9.923 -2.431 -30.360 1.00 77.69 N ANISOU 1617 N VAL A 404 10050 12007 7463 -152 -758 797 N ATOM 1618 CA VAL A 404 9.833 -3.701 -31.085 1.00 77.34 C ANISOU 1618 CA VAL A 404 9812 12095 7479 -285 -703 813 C ATOM 1619 C VAL A 404 8.388 -3.842 -31.647 1.00 80.34 C ANISOU 1619 C VAL A 404 10078 12669 7779 -160 -708 827 C ATOM 1620 O VAL A 404 8.234 -3.868 -32.863 1.00 78.71 O ANISOU 1620 O VAL A 404 9866 12484 7555 -203 -716 852 O ATOM 1621 CB VAL A 404 10.281 -4.939 -30.234 1.00 80.73 C ANISOU 1621 CB VAL A 404 10098 12581 7994 -402 -643 797 C ATOM 1622 CG1 VAL A 404 10.089 -6.245 -31.002 1.00 80.07 C ANISOU 1622 CG1 VAL A 404 9863 12608 7950 -527 -592 808 C ATOM 1623 CG2 VAL A 404 11.734 -4.807 -29.795 1.00 80.14 C ANISOU 1623 CG2 VAL A 404 10111 12356 7984 -523 -640 794 C ATOM 1624 N LEU A 405 7.355 -3.885 -30.776 1.00 77.36 N ANISOU 1624 N LEU A 405 9605 12449 7340 -6 -707 817 N ATOM 1625 CA LEU A 405 5.960 -4.060 -31.183 1.00 78.21 C ANISOU 1625 CA LEU A 405 9565 12800 7353 108 -711 840 C ATOM 1626 C LEU A 405 5.428 -2.895 -32.027 1.00 84.55 C ANISOU 1626 C LEU A 405 10487 13585 8052 289 -768 864 C ATOM 1627 O LEU A 405 4.766 -3.159 -33.028 1.00 83.88 O ANISOU 1627 O LEU A 405 10302 13648 7922 277 -775 896 O ATOM 1628 CB LEU A 405 5.034 -4.265 -29.975 1.00 78.87 C ANISOU 1628 CB LEU A 405 9513 13080 7373 243 -695 831 C ATOM 1629 CG LEU A 405 5.041 -5.638 -29.299 1.00 82.36 C ANISOU 1629 CG LEU A 405 9777 13638 7877 71 -640 829 C ATOM 1630 CD1 LEU A 405 4.050 -5.665 -28.177 1.00 83.24 C ANISOU 1630 CD1 LEU A 405 9760 13968 7900 219 -629 832 C ATOM 1631 CD2 LEU A 405 4.676 -6.745 -30.270 1.00 84.24 C ANISOU 1631 CD2 LEU A 405 9872 14008 8128 -114 -619 856 C ATOM 1632 N ALA A 406 5.674 -1.627 -31.632 1.00 83.45 N ANISOU 1632 N ALA A 406 10573 13271 7864 457 -814 851 N ATOM 1633 CA ALA A 406 5.179 -0.482 -32.411 1.00 84.87 C ANISOU 1633 CA ALA A 406 10907 13406 7932 650 -872 879 C ATOM 1634 C ALA A 406 5.843 -0.445 -33.807 1.00 88.49 C ANISOU 1634 C ALA A 406 11443 13743 8434 478 -887 913 C ATOM 1635 O ALA A 406 5.071 -0.443 -34.768 1.00 88.80 O ANISOU 1635 O ALA A 406 11408 13927 8406 542 -902 950 O ATOM 1636 CB ALA A 406 5.391 0.835 -31.672 1.00 86.73 C ANISOU 1636 CB ALA A 406 11422 13433 8098 847 -921 854 C ATOM 1637 N PRO A 407 7.208 -0.521 -33.987 1.00 83.61 N ANISOU 1637 N PRO A 407 10936 12913 7918 253 -879 906 N ATOM 1638 CA PRO A 407 7.752 -0.514 -35.366 1.00 82.35 C ANISOU 1638 CA PRO A 407 10826 12684 7779 101 -887 944 C ATOM 1639 C PRO A 407 7.304 -1.735 -36.173 1.00 84.56 C ANISOU 1639 C PRO A 407 10868 13174 8088 -16 -842 953 C ATOM 1640 O PRO A 407 6.848 -1.531 -37.296 1.00 86.74 O ANISOU 1640 O PRO A 407 11144 13511 8303 11 -866 989 O ATOM 1641 CB PRO A 407 9.273 -0.483 -35.181 1.00 82.99 C ANISOU 1641 CB PRO A 407 11020 12560 7951 -112 -876 936 C ATOM 1642 CG PRO A 407 9.514 -0.863 -33.786 1.00 86.90 C ANISOU 1642 CG PRO A 407 11463 13058 8498 -115 -849 892 C ATOM 1643 CD PRO A 407 8.300 -0.534 -32.983 1.00 83.52 C ANISOU 1643 CD PRO A 407 11009 12740 7986 137 -866 872 C ATOM 1644 N ILE A 408 7.350 -2.969 -35.608 1.00 78.26 N ANISOU 1644 N ILE A 408 9885 12485 7364 -136 -783 923 N ATOM 1645 CA ILE A 408 6.892 -4.175 -36.320 1.00 77.81 C ANISOU 1645 CA ILE A 408 9638 12608 7318 -264 -747 927 C ATOM 1646 C ILE A 408 5.386 -4.039 -36.639 1.00 85.21 C ANISOU 1646 C ILE A 408 10455 13788 8134 -110 -778 954 C ATOM 1647 O ILE A 408 4.969 -4.349 -37.758 1.00 85.32 O ANISOU 1647 O ILE A 408 10403 13910 8104 -171 -787 978 O ATOM 1648 CB ILE A 408 7.208 -5.495 -35.567 1.00 79.44 C ANISOU 1648 CB ILE A 408 9713 12858 7612 -413 -685 894 C ATOM 1649 CG1 ILE A 408 8.738 -5.767 -35.546 1.00 78.04 C ANISOU 1649 CG1 ILE A 408 9625 12486 7541 -570 -649 878 C ATOM 1650 CG2 ILE A 408 6.444 -6.690 -36.183 1.00 80.89 C ANISOU 1650 CG2 ILE A 408 9727 13237 7770 -529 -661 897 C ATOM 1651 CD1 ILE A 408 9.198 -6.989 -34.670 1.00 77.70 C ANISOU 1651 CD1 ILE A 408 9488 12453 7581 -682 -589 850 C ATOM 1652 N GLY A 409 4.611 -3.539 -35.675 1.00 84.07 N ANISOU 1652 N GLY A 409 10283 13739 7922 96 -796 953 N ATOM 1653 CA GLY A 409 3.174 -3.297 -35.823 1.00 85.87 C ANISOU 1653 CA GLY A 409 10379 14237 8012 285 -825 987 C ATOM 1654 C GLY A 409 2.838 -2.403 -37.002 1.00 91.27 C ANISOU 1654 C GLY A 409 11159 14915 8603 409 -879 1031 C ATOM 1655 O GLY A 409 1.993 -2.759 -37.830 1.00 91.98 O ANISOU 1655 O GLY A 409 11099 15234 8614 398 -893 1066 O ATOM 1656 N LEU A 410 3.550 -1.269 -37.117 1.00 87.53 N ANISOU 1656 N LEU A 410 10948 14175 8134 499 -914 1033 N ATOM 1657 CA LEU A 410 3.378 -0.310 -38.199 1.00 88.43 C ANISOU 1657 CA LEU A 410 11210 14229 8160 616 -970 1081 C ATOM 1658 C LEU A 410 3.801 -0.926 -39.558 1.00 91.57 C ANISOU 1658 C LEU A 410 11562 14630 8600 379 -960 1102 C ATOM 1659 O LEU A 410 3.146 -0.622 -40.555 1.00 91.08 O ANISOU 1659 O LEU A 410 11480 14685 8440 459 -997 1149 O ATOM 1660 CB LEU A 410 4.166 0.981 -37.892 1.00 89.14 C ANISOU 1660 CB LEU A 410 11628 13995 8245 717 -1011 1078 C ATOM 1661 CG LEU A 410 3.971 2.236 -38.786 1.00 96.16 C ANISOU 1661 CG LEU A 410 12751 14767 9021 891 -1081 1134 C ATOM 1662 CD1 LEU A 410 4.965 2.289 -39.931 1.00 96.21 C ANISOU 1662 CD1 LEU A 410 12874 14600 9080 655 -1089 1164 C ATOM 1663 CD2 LEU A 410 2.504 2.468 -39.217 1.00 99.21 C ANISOU 1663 CD2 LEU A 410 13010 15433 9252 1163 -1111 1179 C ATOM 1664 N VAL A 411 4.833 -1.821 -39.602 1.00 87.57 N ANISOU 1664 N VAL A 411 11029 14021 8222 107 -908 1067 N ATOM 1665 CA VAL A 411 5.251 -2.440 -40.878 1.00 87.01 C ANISOU 1665 CA VAL A 411 10924 13958 8178 -100 -891 1079 C ATOM 1666 C VAL A 411 4.183 -3.456 -41.328 1.00 90.91 C ANISOU 1666 C VAL A 411 11180 14744 8615 -155 -881 1081 C ATOM 1667 O VAL A 411 4.021 -3.665 -42.529 1.00 91.44 O ANISOU 1667 O VAL A 411 11222 14884 8637 -237 -894 1104 O ATOM 1668 CB VAL A 411 6.684 -3.071 -40.937 1.00 90.12 C ANISOU 1668 CB VAL A 411 11368 14174 8700 -342 -837 1046 C ATOM 1669 CG1 VAL A 411 7.754 -2.136 -40.379 1.00 90.11 C ANISOU 1669 CG1 VAL A 411 11575 13921 8743 -329 -850 1049 C ATOM 1670 CG2 VAL A 411 6.767 -4.455 -40.304 1.00 89.10 C ANISOU 1670 CG2 VAL A 411 11075 14130 8650 -483 -774 997 C ATOM 1671 N LEU A 412 3.452 -4.073 -40.387 1.00 87.14 N ANISOU 1671 N LEU A 412 10536 14445 8130 -127 -863 1063 N ATOM 1672 CA LEU A 412 2.403 -5.027 -40.754 1.00 86.98 C ANISOU 1672 CA LEU A 412 10292 14721 8037 -213 -862 1073 C ATOM 1673 C LEU A 412 1.190 -4.319 -41.381 1.00 92.60 C ANISOU 1673 C LEU A 412 10927 15669 8587 -17 -924 1135 C ATOM 1674 O LEU A 412 0.617 -4.865 -42.318 1.00 92.29 O ANISOU 1674 O LEU A 412 10769 15821 8477 -128 -941 1156 O ATOM 1675 CB LEU A 412 1.947 -5.872 -39.550 1.00 86.16 C ANISOU 1675 CB LEU A 412 10028 14758 7951 -259 -828 1050 C ATOM 1676 CG LEU A 412 2.896 -6.965 -39.053 1.00 87.83 C ANISOU 1676 CG LEU A 412 10261 14814 8296 -485 -766 998 C ATOM 1677 CD1 LEU A 412 2.407 -7.528 -37.737 1.00 87.49 C ANISOU 1677 CD1 LEU A 412 10088 14898 8257 -482 -741 988 C ATOM 1678 CD2 LEU A 412 3.055 -8.098 -40.077 1.00 87.47 C ANISOU 1678 CD2 LEU A 412 10185 14791 8260 -738 -747 982 C ATOM 1679 N ILE A 413 0.811 -3.115 -40.888 1.00 91.21 N ANISOU 1679 N ILE A 413 10832 15482 8342 279 -960 1162 N ATOM 1680 CA ILE A 413 -0.360 -2.386 -41.408 1.00 93.56 C ANISOU 1680 CA ILE A 413 11060 16018 8468 522 -1017 1227 C ATOM 1681 C ILE A 413 0.005 -1.690 -42.764 1.00 96.44 C ANISOU 1681 C ILE A 413 11596 16246 8801 535 -1060 1266 C ATOM 1682 O ILE A 413 -0.852 -1.629 -43.636 1.00 97.06 O ANISOU 1682 O ILE A 413 11563 16560 8755 594 -1100 1319 O ATOM 1683 CB ILE A 413 -1.003 -1.388 -40.367 1.00 98.33 C ANISOU 1683 CB ILE A 413 11696 16682 8982 878 -1037 1242 C ATOM 1684 CG1 ILE A 413 -0.306 -0.013 -40.257 1.00 99.70 C ANISOU 1684 CG1 ILE A 413 12203 16515 9163 1081 -1069 1241 C ATOM 1685 CG2 ILE A 413 -1.224 -2.020 -38.988 1.00 97.78 C ANISOU 1685 CG2 ILE A 413 11480 16723 8948 859 -991 1203 C ATOM 1686 CD1 ILE A 413 -0.987 1.132 -41.102 1.00108.41 C ANISOU 1686 CD1 ILE A 413 13415 17673 10105 1371 -1137 1312 C ATOM 1687 N VAL A 414 1.260 -1.195 -42.932 1.00 91.57 N ANISOU 1687 N VAL A 414 11232 15275 8284 464 -1052 1247 N ATOM 1688 CA VAL A 414 1.754 -0.514 -44.145 1.00 90.92 C ANISOU 1688 CA VAL A 414 11333 15037 8176 449 -1088 1289 C ATOM 1689 C VAL A 414 2.099 -1.584 -45.221 1.00 94.01 C ANISOU 1689 C VAL A 414 11620 15490 8608 151 -1060 1275 C ATOM 1690 O VAL A 414 1.619 -1.485 -46.356 1.00 94.36 O ANISOU 1690 O VAL A 414 11631 15666 8556 156 -1096 1321 O ATOM 1691 CB VAL A 414 2.953 0.436 -43.836 1.00 93.59 C ANISOU 1691 CB VAL A 414 11976 14999 8585 463 -1094 1282 C ATOM 1692 CG1 VAL A 414 3.590 0.979 -45.110 1.00 93.53 C ANISOU 1692 CG1 VAL A 414 12145 14835 8556 378 -1123 1330 C ATOM 1693 CG2 VAL A 414 2.518 1.593 -42.936 1.00 94.59 C ANISOU 1693 CG2 VAL A 414 12257 15048 8635 778 -1136 1295 C ATOM 1694 N GLY A 415 2.895 -2.589 -44.842 1.00 88.73 N ANISOU 1694 N GLY A 415 10912 14733 8068 -85 -996 1213 N ATOM 1695 CA GLY A 415 3.266 -3.703 -45.711 1.00 87.54 C ANISOU 1695 CA GLY A 415 10688 14621 7953 -350 -960 1184 C ATOM 1696 C GLY A 415 2.056 -4.515 -46.121 1.00 92.48 C ANISOU 1696 C GLY A 415 11093 15569 8478 -405 -978 1192 C ATOM 1697 O GLY A 415 1.969 -4.953 -47.269 1.00 93.89 O ANISOU 1697 O GLY A 415 11242 15826 8604 -541 -987 1198 O ATOM 1698 N GLY A 416 1.104 -4.660 -45.196 1.00 88.77 N ANISOU 1698 N GLY A 416 10465 15300 7962 -301 -988 1198 N ATOM 1699 CA GLY A 416 -0.160 -5.352 -45.419 1.00 89.90 C ANISOU 1699 CA GLY A 416 10372 15800 7985 -353 -1014 1220 C ATOM 1700 C GLY A 416 -1.011 -4.655 -46.458 1.00 96.23 C ANISOU 1700 C GLY A 416 11127 16806 8629 -211 -1082 1292 C ATOM 1701 O GLY A 416 -1.470 -5.295 -47.405 1.00 97.12 O ANISOU 1701 O GLY A 416 11135 17105 8663 -374 -1104 1303 O ATOM 1702 N TYR A 417 -1.162 -3.320 -46.325 1.00 93.11 N ANISOU 1702 N TYR A 417 10841 16353 8182 94 -1120 1342 N ATOM 1703 CA TYR A 417 -1.913 -2.463 -47.249 1.00 94.26 C ANISOU 1703 CA TYR A 417 10983 16660 8171 294 -1189 1422 C ATOM 1704 C TYR A 417 -1.352 -2.541 -48.680 1.00 96.89 C ANISOU 1704 C TYR A 417 11422 16889 8502 125 -1202 1433 C ATOM 1705 O TYR A 417 -2.145 -2.610 -49.618 1.00 98.46 O ANISOU 1705 O TYR A 417 11503 17343 8566 126 -1250 1483 O ATOM 1706 CB TYR A 417 -1.904 -1.002 -46.751 1.00 96.21 C ANISOU 1706 CB TYR A 417 11419 16754 8381 651 -1219 1462 C ATOM 1707 CG TYR A 417 -2.484 0.007 -47.723 1.00 99.01 C ANISOU 1707 CG TYR A 417 11843 17196 8580 885 -1290 1549 C ATOM 1708 CD1 TYR A 417 -3.847 0.296 -47.729 1.00102.73 C ANISOU 1708 CD1 TYR A 417 12121 18043 8870 1139 -1337 1616 C ATOM 1709 CD2 TYR A 417 -1.662 0.720 -48.594 1.00 99.29 C ANISOU 1709 CD2 TYR A 417 12140 16950 8637 871 -1311 1575 C ATOM 1710 CE1 TYR A 417 -4.381 1.241 -48.604 1.00105.67 C ANISOU 1710 CE1 TYR A 417 12564 18498 9087 1386 -1404 1703 C ATOM 1711 CE2 TYR A 417 -2.186 1.660 -49.479 1.00101.94 C ANISOU 1711 CE2 TYR A 417 12560 17350 8822 1093 -1380 1663 C ATOM 1712 CZ TYR A 417 -3.546 1.920 -49.478 1.00110.04 C ANISOU 1712 CZ TYR A 417 13400 18740 9671 1362 -1427 1726 C ATOM 1713 OH TYR A 417 -4.059 2.846 -50.351 1.00110.70 O ANISOU 1713 OH TYR A 417 13572 18891 9597 1604 -1495 1820 O ATOM 1714 N PHE A 418 -0.010 -2.511 -48.856 1.00 91.11 N ANISOU 1714 N PHE A 418 10900 15814 7905 -15 -1161 1391 N ATOM 1715 CA PHE A 418 0.583 -2.562 -50.197 1.00 90.46 C ANISOU 1715 CA PHE A 418 10918 15640 7812 -168 -1166 1402 C ATOM 1716 C PHE A 418 0.516 -3.974 -50.790 1.00 93.28 C ANISOU 1716 C PHE A 418 11132 16140 8171 -465 -1137 1350 C ATOM 1717 O PHE A 418 0.511 -4.096 -52.013 1.00 93.44 O ANISOU 1717 O PHE A 418 11166 16218 8119 -563 -1158 1368 O ATOM 1718 CB PHE A 418 2.026 -2.039 -50.223 1.00 91.01 C ANISOU 1718 CB PHE A 418 11240 15341 7999 -222 -1132 1388 C ATOM 1719 CG PHE A 418 2.140 -0.541 -50.055 1.00 93.61 C ANISOU 1719 CG PHE A 418 11781 15498 8288 29 -1180 1452 C ATOM 1720 CD1 PHE A 418 1.500 0.326 -50.937 1.00 98.93 C ANISOU 1720 CD1 PHE A 418 12514 16258 8818 204 -1250 1538 C ATOM 1721 CD2 PHE A 418 2.932 0.003 -49.053 1.00 95.34 C ANISOU 1721 CD2 PHE A 418 12166 15453 8604 78 -1160 1430 C ATOM 1722 CE1 PHE A 418 1.611 1.712 -50.786 1.00101.16 C ANISOU 1722 CE1 PHE A 418 13039 16347 9050 441 -1299 1599 C ATOM 1723 CE2 PHE A 418 3.048 1.389 -48.903 1.00 99.51 C ANISOU 1723 CE2 PHE A 418 12936 15792 9081 291 -1212 1486 C ATOM 1724 CZ PHE A 418 2.386 2.234 -49.771 1.00 99.85 C ANISOU 1724 CZ PHE A 418 13058 15902 8977 476 -1281 1570 C ATOM 1725 N LEU A 419 0.444 -5.025 -49.944 1.00 88.60 N ANISOU 1725 N LEU A 419 10422 15598 7646 -606 -1093 1287 N ATOM 1726 CA LEU A 419 0.296 -6.407 -50.417 1.00 87.76 C ANISOU 1726 CA LEU A 419 10212 15610 7522 -890 -1072 1234 C ATOM 1727 C LEU A 419 -1.110 -6.625 -50.967 1.00 92.91 C ANISOU 1727 C LEU A 419 10659 16644 7996 -900 -1140 1283 C ATOM 1728 O LEU A 419 -1.246 -7.236 -52.027 1.00 93.59 O ANISOU 1728 O LEU A 419 10727 16826 8008 -1088 -1157 1271 O ATOM 1729 CB LEU A 419 0.601 -7.439 -49.308 1.00 86.49 C ANISOU 1729 CB LEU A 419 10012 15378 7472 -1033 -1012 1163 C ATOM 1730 CG LEU A 419 2.075 -7.782 -49.082 1.00 88.88 C ANISOU 1730 CG LEU A 419 10489 15350 7932 -1135 -936 1098 C ATOM 1731 CD1 LEU A 419 2.267 -8.548 -47.791 1.00 87.34 C ANISOU 1731 CD1 LEU A 419 10254 15095 7836 -1200 -886 1048 C ATOM 1732 CD2 LEU A 419 2.678 -8.549 -50.272 1.00 90.73 C ANISOU 1732 CD2 LEU A 419 10805 15515 8153 -1345 -909 1053 C ATOM 1733 N ILE A 420 -2.154 -6.111 -50.261 1.00 90.01 N ANISOU 1733 N ILE A 420 10137 16517 7547 -694 -1180 1341 N ATOM 1734 CA ILE A 420 -3.563 -6.227 -50.681 1.00 91.15 C ANISOU 1734 CA ILE A 420 10044 17088 7499 -675 -1249 1405 C ATOM 1735 C ILE A 420 -3.759 -5.430 -51.960 1.00 95.26 C ANISOU 1735 C ILE A 420 10616 17674 7906 -558 -1308 1471 C ATOM 1736 O ILE A 420 -4.364 -5.956 -52.885 1.00 96.74 O ANISOU 1736 O ILE A 420 10687 18105 7967 -717 -1351 1488 O ATOM 1737 CB ILE A 420 -4.612 -5.815 -49.600 1.00 94.92 C ANISOU 1737 CB ILE A 420 10327 17841 7898 -443 -1271 1459 C ATOM 1738 CG1 ILE A 420 -4.284 -6.405 -48.215 1.00 93.78 C ANISOU 1738 CG1 ILE A 420 10168 17585 7881 -516 -1208 1400 C ATOM 1739 CG2 ILE A 420 -6.046 -6.207 -50.033 1.00 96.58 C ANISOU 1739 CG2 ILE A 420 10245 18555 7898 -497 -1337 1526 C ATOM 1740 CD1 ILE A 420 -5.038 -5.698 -47.018 1.00102.51 C ANISOU 1740 CD1 ILE A 420 11146 18872 8930 -209 -1215 1446 C ATOM 1741 N ARG A 421 -3.216 -4.195 -52.040 1.00 91.08 N ANISOU 1741 N ARG A 421 10278 16915 7412 -307 -1313 1507 N ATOM 1742 CA ARG A 421 -3.342 -3.353 -53.241 1.00 91.88 C ANISOU 1742 CA ARG A 421 10463 17046 7403 -182 -1370 1580 C ATOM 1743 C ARG A 421 -2.631 -3.965 -54.451 1.00 95.14 C ANISOU 1743 C ARG A 421 10969 17345 7835 -460 -1355 1541 C ATOM 1744 O ARG A 421 -3.151 -3.876 -55.561 1.00 96.95 O ANISOU 1744 O ARG A 421 11145 17768 7924 -477 -1410 1591 O ATOM 1745 CB ARG A 421 -2.833 -1.935 -53.000 1.00 91.93 C ANISOU 1745 CB ARG A 421 10702 16784 7443 116 -1379 1626 C ATOM 1746 CG ARG A 421 -3.870 -1.071 -52.288 1.00107.19 C ANISOU 1746 CG ARG A 421 12548 18917 9262 480 -1424 1695 C ATOM 1747 CD ARG A 421 -3.712 0.396 -52.625 1.00120.75 C ANISOU 1747 CD ARG A 421 14508 20452 10919 790 -1470 1772 C ATOM 1748 NE ARG A 421 -3.998 0.682 -54.034 1.00128.26 N ANISOU 1748 NE ARG A 421 15472 21522 11740 794 -1527 1845 N ATOM 1749 CZ ARG A 421 -3.776 1.853 -54.620 1.00139.65 C ANISOU 1749 CZ ARG A 421 17151 22791 13120 1001 -1572 1920 C ATOM 1750 NH1 ARG A 421 -3.271 2.867 -53.925 1.00124.32 N ANISOU 1750 NH1 ARG A 421 15471 20536 11229 1215 -1570 1929 N ATOM 1751 NH2 ARG A 421 -4.052 2.020 -55.905 1.00126.60 N ANISOU 1751 NH2 ARG A 421 15492 21267 11343 986 -1623 1988 N ATOM 1752 N GLY A 422 -1.497 -4.613 -54.220 1.00 89.66 N ANISOU 1752 N GLY A 422 10401 16369 7298 -664 -1280 1453 N ATOM 1753 CA GLY A 422 -0.734 -5.282 -55.264 1.00 89.29 C ANISOU 1753 CA GLY A 422 10451 16207 7270 -914 -1250 1403 C ATOM 1754 C GLY A 422 -1.383 -6.568 -55.742 1.00 94.08 C ANISOU 1754 C GLY A 422 10904 17054 7786 -1176 -1264 1357 C ATOM 1755 O GLY A 422 -1.362 -6.860 -56.944 1.00 92.48 O ANISOU 1755 O GLY A 422 10730 16913 7495 -1313 -1284 1353 O ATOM 1756 N VAL A 423 -1.963 -7.356 -54.798 1.00 92.16 N ANISOU 1756 N VAL A 423 10513 16948 7556 -1264 -1255 1324 N ATOM 1757 CA VAL A 423 -2.602 -8.631 -55.140 1.00 93.37 C ANISOU 1757 CA VAL A 423 10543 17318 7615 -1552 -1275 1282 C ATOM 1758 C VAL A 423 -3.939 -8.336 -55.868 1.00 99.62 C ANISOU 1758 C VAL A 423 11135 18525 8191 -1511 -1373 1370 C ATOM 1759 O VAL A 423 -4.296 -9.079 -56.787 1.00100.24 O ANISOU 1759 O VAL A 423 11176 18760 8152 -1747 -1408 1350 O ATOM 1760 CB VAL A 423 -2.754 -9.606 -53.935 1.00 96.96 C ANISOU 1760 CB VAL A 423 10923 17778 8140 -1694 -1238 1227 C ATOM 1761 CG1 VAL A 423 -3.873 -9.201 -52.982 1.00 97.69 C ANISOU 1761 CG1 VAL A 423 10789 18164 8165 -1531 -1278 1300 C ATOM 1762 CG2 VAL A 423 -2.934 -11.045 -54.408 1.00 97.41 C ANISOU 1762 CG2 VAL A 423 10982 17900 8129 -2052 -1241 1158 C ATOM 1763 N MET A 424 -4.615 -7.214 -55.524 1.00 97.07 N ANISOU 1763 N MET A 424 10706 18371 7806 -1198 -1417 1467 N ATOM 1764 CA MET A 424 -5.854 -6.789 -56.187 1.00 98.94 C ANISOU 1764 CA MET A 424 10743 19021 7828 -1095 -1509 1566 C ATOM 1765 C MET A 424 -5.568 -6.386 -57.627 1.00102.12 C ANISOU 1765 C MET A 424 11264 19380 8155 -1101 -1544 1593 C ATOM 1766 O MET A 424 -6.302 -6.792 -58.527 1.00104.51 O ANISOU 1766 O MET A 424 11438 19981 8290 -1247 -1607 1620 O ATOM 1767 CB MET A 424 -6.532 -5.631 -55.438 1.00102.48 C ANISOU 1767 CB MET A 424 11087 19623 8227 -702 -1538 1660 C ATOM 1768 CG MET A 424 -7.247 -6.063 -54.184 1.00106.95 C ANISOU 1768 CG MET A 424 11444 20409 8784 -696 -1527 1660 C ATOM 1769 SD MET A 424 -8.234 -4.750 -53.430 1.00113.69 S ANISOU 1769 SD MET A 424 12146 21531 9521 -205 -1566 1774 S ATOM 1770 CE MET A 424 -6.974 -3.697 -52.785 1.00108.37 C ANISOU 1770 CE MET A 424 11813 20315 9048 56 -1505 1738 C ATOM 1771 N THR A 425 -4.485 -5.615 -57.842 1.00 95.90 N ANISOU 1771 N THR A 425 10722 18232 7484 -968 -1503 1588 N ATOM 1772 CA THR A 425 -4.026 -5.137 -59.147 1.00 95.51 C ANISOU 1772 CA THR A 425 10819 18089 7380 -965 -1524 1618 C ATOM 1773 C THR A 425 -3.618 -6.330 -60.027 1.00100.73 C ANISOU 1773 C THR A 425 11524 18724 8025 -1322 -1501 1529 C ATOM 1774 O THR A 425 -3.952 -6.347 -61.210 1.00102.05 O ANISOU 1774 O THR A 425 11671 19056 8047 -1395 -1553 1560 O ATOM 1775 CB THR A 425 -2.875 -4.140 -58.953 1.00 95.89 C ANISOU 1775 CB THR A 425 11123 17743 7566 -787 -1477 1630 C ATOM 1776 OG1 THR A 425 -3.300 -3.132 -58.041 1.00 95.87 O ANISOU 1776 OG1 THR A 425 11107 17751 7569 -465 -1501 1697 O ATOM 1777 CG2 THR A 425 -2.423 -3.483 -60.250 1.00 93.13 C ANISOU 1777 CG2 THR A 425 10930 17306 7149 -760 -1502 1683 C ATOM 1778 N LEU A 426 -2.922 -7.320 -59.445 1.00 97.17 N ANISOU 1778 N LEU A 426 11142 18069 7709 -1529 -1425 1419 N ATOM 1779 CA LEU A 426 -2.454 -8.529 -60.123 1.00 97.56 C ANISOU 1779 CA LEU A 426 11276 18043 7749 -1846 -1392 1317 C ATOM 1780 C LEU A 426 -3.640 -9.328 -60.696 1.00101.24 C ANISOU 1780 C LEU A 426 11568 18878 8019 -2062 -1471 1320 C ATOM 1781 O LEU A 426 -3.618 -9.644 -61.881 1.00102.03 O ANISOU 1781 O LEU A 426 11724 19037 8007 -2211 -1497 1301 O ATOM 1782 CB LEU A 426 -1.619 -9.396 -59.146 1.00 96.87 C ANISOU 1782 CB LEU A 426 11286 17686 7835 -1971 -1301 1211 C ATOM 1783 CG LEU A 426 -0.807 -10.550 -59.752 1.00102.76 C ANISOU 1783 CG LEU A 426 12197 18251 8598 -2233 -1242 1095 C ATOM 1784 CD1 LEU A 426 0.485 -10.723 -59.030 1.00101.72 C ANISOU 1784 CD1 LEU A 426 12221 17770 8658 -2199 -1139 1030 C ATOM 1785 CD2 LEU A 426 -1.570 -11.863 -59.709 1.00107.82 C ANISOU 1785 CD2 LEU A 426 12767 19059 9140 -2516 -1273 1034 C ATOM 1786 N PHE A 427 -4.674 -9.632 -59.884 1.00 97.49 N ANISOU 1786 N PHE A 427 10881 18672 7489 -2087 -1512 1349 N ATOM 1787 CA PHE A 427 -5.831 -10.398 -60.370 1.00 98.88 C ANISOU 1787 CA PHE A 427 10874 19234 7462 -2327 -1595 1363 C ATOM 1788 C PHE A 427 -6.699 -9.548 -61.297 1.00102.37 C ANISOU 1788 C PHE A 427 11167 20016 7713 -2177 -1689 1479 C ATOM 1789 O PHE A 427 -7.384 -10.109 -62.151 1.00103.86 O ANISOU 1789 O PHE A 427 11263 20480 7718 -2400 -1760 1484 O ATOM 1790 CB PHE A 427 -6.666 -10.987 -59.224 1.00101.69 C ANISOU 1790 CB PHE A 427 11031 19807 7799 -2423 -1611 1372 C ATOM 1791 CG PHE A 427 -5.913 -11.971 -58.353 1.00102.53 C ANISOU 1791 CG PHE A 427 11286 19605 8067 -2605 -1528 1262 C ATOM 1792 CD1 PHE A 427 -5.014 -12.879 -58.911 1.00105.38 C ANISOU 1792 CD1 PHE A 427 11890 19673 8476 -2838 -1479 1147 C ATOM 1793 CD2 PHE A 427 -6.144 -12.029 -56.982 1.00105.20 C ANISOU 1793 CD2 PHE A 427 11519 19964 8490 -2537 -1501 1276 C ATOM 1794 CE1 PHE A 427 -4.315 -13.784 -58.105 1.00105.18 C ANISOU 1794 CE1 PHE A 427 12012 19363 8588 -2975 -1403 1052 C ATOM 1795 CE2 PHE A 427 -5.450 -12.942 -56.176 1.00106.62 C ANISOU 1795 CE2 PHE A 427 11840 19860 8810 -2698 -1427 1183 C ATOM 1796 CZ PHE A 427 -4.532 -13.804 -56.742 1.00103.93 C ANISOU 1796 CZ PHE A 427 11751 19217 8521 -2907 -1380 1073 C ATOM 1797 N SER A 428 -6.621 -8.209 -61.184 1.00 96.75 N ANISOU 1797 N SER A 428 10460 19266 7033 -1809 -1694 1570 N ATOM 1798 CA SER A 428 -7.326 -7.293 -62.087 1.00 96.94 C ANISOU 1798 CA SER A 428 10387 19566 6881 -1614 -1779 1688 C ATOM 1799 C SER A 428 -6.682 -7.340 -63.484 1.00 99.00 C ANISOU 1799 C SER A 428 10829 19688 7098 -1739 -1781 1660 C ATOM 1800 O SER A 428 -7.404 -7.409 -64.484 1.00101.23 O ANISOU 1800 O SER A 428 11003 20278 7183 -1820 -1863 1709 O ATOM 1801 CB SER A 428 -7.316 -5.873 -61.529 1.00 99.19 C ANISOU 1801 CB SER A 428 10694 19778 7216 -1180 -1777 1784 C ATOM 1802 OG SER A 428 -7.996 -4.965 -62.377 1.00108.71 O ANISOU 1802 OG SER A 428 11826 21236 8243 -960 -1860 1905 O ATOM 1803 N ILE A 429 -5.328 -7.348 -63.550 1.00 92.07 N ANISOU 1803 N ILE A 429 10216 18375 6393 -1767 -1692 1583 N ATOM 1804 CA ILE A 429 -4.575 -7.408 -64.811 1.00 91.57 C ANISOU 1804 CA ILE A 429 10336 18160 6296 -1879 -1676 1551 C ATOM 1805 C ILE A 429 -4.761 -8.808 -65.425 1.00 98.06 C ANISOU 1805 C ILE A 429 11150 19089 7018 -2258 -1687 1447 C ATOM 1806 O ILE A 429 -5.145 -8.906 -66.604 1.00 99.83 O ANISOU 1806 O ILE A 429 11355 19509 7068 -2365 -1748 1468 O ATOM 1807 CB ILE A 429 -3.075 -7.019 -64.642 1.00 91.84 C ANISOU 1807 CB ILE A 429 10628 17743 6526 -1801 -1575 1506 C ATOM 1808 CG1 ILE A 429 -2.946 -5.531 -64.233 1.00 91.87 C ANISOU 1808 CG1 ILE A 429 10679 17642 6585 -1448 -1586 1620 C ATOM 1809 CG2 ILE A 429 -2.271 -7.287 -65.928 1.00 91.85 C ANISOU 1809 CG2 ILE A 429 10800 17618 6480 -1955 -1546 1460 C ATOM 1810 CD1 ILE A 429 -1.625 -5.130 -63.616 1.00 95.36 C ANISOU 1810 CD1 ILE A 429 11328 17675 7229 -1375 -1494 1586 C ATOM 1811 N LYS A 430 -4.546 -9.867 -64.615 1.00 93.82 N ANISOU 1811 N LYS A 430 10639 18431 6577 -2456 -1635 1342 N ATOM 1812 CA LYS A 430 -4.691 -11.262 -65.025 1.00 95.00 C ANISOU 1812 CA LYS A 430 10833 18626 6638 -2823 -1643 1234 C ATOM 1813 C LYS A 430 -6.086 -11.558 -65.616 1.00104.33 C ANISOU 1813 C LYS A 430 11797 20273 7571 -2990 -1766 1291 C ATOM 1814 O LYS A 430 -6.148 -12.124 -66.709 1.00106.68 O ANISOU 1814 O LYS A 430 12169 20641 7725 -3212 -1802 1244 O ATOM 1815 CB LYS A 430 -4.409 -12.205 -63.853 1.00 95.83 C ANISOU 1815 CB LYS A 430 10983 18549 6877 -2962 -1581 1143 C ATOM 1816 CG LYS A 430 -2.960 -12.652 -63.741 1.00 98.05 C ANISOU 1816 CG LYS A 430 11535 18390 7329 -2987 -1463 1028 C ATOM 1817 CD LYS A 430 -2.860 -13.794 -62.730 1.00110.57 C ANISOU 1817 CD LYS A 430 13172 19843 8997 -3172 -1420 937 C ATOM 1818 CE LYS A 430 -1.514 -14.476 -62.696 1.00117.05 C ANISOU 1818 CE LYS A 430 14261 20267 9945 -3222 -1310 815 C ATOM 1819 NZ LYS A 430 -1.489 -15.596 -61.712 1.00124.03 N ANISOU 1819 NZ LYS A 430 15207 21025 10892 -3393 -1276 736 N ATOM 1820 N SER A 431 -7.189 -11.142 -64.942 1.00102.34 N ANISOU 1820 N SER A 431 11274 20359 7254 -2874 -1832 1395 N ATOM 1821 CA SER A 431 -8.568 -11.371 -65.426 1.00104.60 C ANISOU 1821 CA SER A 431 11304 21153 7287 -3023 -1953 1469 C ATOM 1822 C SER A 431 -8.875 -10.617 -66.719 1.00109.59 C ANISOU 1822 C SER A 431 11896 21991 7752 -2908 -2025 1554 C ATOM 1823 O SER A 431 -9.466 -11.208 -67.628 1.00111.57 O ANISOU 1823 O SER A 431 12088 22503 7800 -3170 -2104 1546 O ATOM 1824 CB SER A 431 -9.596 -10.973 -64.375 1.00109.11 C ANISOU 1824 CB SER A 431 11578 22056 7823 -2864 -1995 1574 C ATOM 1825 OG SER A 431 -9.396 -11.701 -63.176 1.00121.18 O ANISOU 1825 OG SER A 431 13128 23428 9486 -2990 -1935 1504 O ATOM 1826 N ASN A 432 -8.503 -9.318 -66.805 1.00105.08 N ANISOU 1826 N ASN A 432 11367 21306 7251 -2529 -2006 1640 N ATOM 1827 CA ASN A 432 -8.757 -8.505 -68.007 1.00106.09 C ANISOU 1827 CA ASN A 432 11478 21608 7224 -2386 -2073 1736 C ATOM 1828 C ASN A 432 -7.967 -9.046 -69.205 1.00109.09 C ANISOU 1828 C ASN A 432 12089 21788 7572 -2620 -2049 1642 C ATOM 1829 O ASN A 432 -8.496 -9.052 -70.309 1.00110.23 O ANISOU 1829 O ASN A 432 12172 22198 7513 -2711 -2130 1684 O ATOM 1830 CB ASN A 432 -8.432 -7.032 -67.771 1.00105.17 C ANISOU 1830 CB ASN A 432 11417 21345 7196 -1946 -2053 1843 C ATOM 1831 CG ASN A 432 -9.363 -6.355 -66.795 1.00120.81 C ANISOU 1831 CG ASN A 432 13166 23587 9147 -1657 -2092 1952 C ATOM 1832 N HIS A 433 -6.733 -9.551 -68.967 1.00104.14 N ANISOU 1832 N HIS A 433 11716 20721 7132 -2717 -1938 1515 N ATOM 1833 CA HIS A 433 -5.853 -10.144 -69.976 1.00104.03 C ANISOU 1833 CA HIS A 433 11939 20487 7100 -2917 -1892 1409 C ATOM 1834 C HIS A 433 -6.452 -11.424 -70.538 1.00109.06 C ANISOU 1834 C HIS A 433 12557 21325 7557 -3306 -1951 1321 C ATOM 1835 O HIS A 433 -6.529 -11.577 -71.759 1.00109.60 O ANISOU 1835 O HIS A 433 12681 21505 7458 -3433 -1995 1310 O ATOM 1836 CB HIS A 433 -4.458 -10.433 -69.386 1.00102.94 C ANISOU 1836 CB HIS A 433 12040 19874 7197 -2904 -1756 1300 C ATOM 1837 CG HIS A 433 -3.534 -11.107 -70.352 1.00106.40 C ANISOU 1837 CG HIS A 433 12716 20104 7607 -3085 -1698 1185 C ATOM 1838 ND1 HIS A 433 -3.068 -10.457 -71.478 1.00108.52 N ANISOU 1838 ND1 HIS A 433 13077 20350 7805 -2996 -1695 1228 N ATOM 1839 CD2 HIS A 433 -3.055 -12.372 -70.350 1.00108.16 C ANISOU 1839 CD2 HIS A 433 13102 20151 7844 -3338 -1643 1033 C ATOM 1840 CE1 HIS A 433 -2.319 -11.340 -72.117 1.00107.96 C ANISOU 1840 CE1 HIS A 433 13206 20109 7706 -3190 -1634 1099 C ATOM 1841 NE2 HIS A 433 -2.282 -12.505 -71.479 1.00107.99 N ANISOU 1841 NE2 HIS A 433 13268 20007 7757 -3389 -1601 976 N ATOM 1842 N ALA A1001 -6.866 -12.340 -69.643 1.00 86.63 N ANISOU 1842 N ALA A1001 12841 11930 8144 -1817 -1629 -81 N ATOM 1843 CA ALA A1001 -7.507 -13.609 -69.982 1.00 86.65 C ANISOU 1843 CA ALA A1001 12955 11875 8093 -1761 -1456 -89 C ATOM 1844 C ALA A1001 -8.837 -13.368 -70.704 1.00 90.69 C ANISOU 1844 C ALA A1001 13398 12590 8470 -1823 -921 -230 C ATOM 1845 O ALA A1001 -9.163 -14.130 -71.613 1.00 89.76 O ANISOU 1845 O ALA A1001 13119 12506 8478 -1715 -737 -269 O ATOM 1846 CB ALA A1001 -7.721 -14.435 -68.731 1.00 90.09 C ANISOU 1846 CB ALA A1001 13996 12045 8188 -1926 -1713 24 C ATOM 1847 N ASP A1002 -9.584 -12.290 -70.335 1.00 88.10 N ANISOU 1847 N ASP A1002 13185 12375 7914 -1987 -691 -305 N ATOM 1848 CA ASP A1002 -10.840 -11.911 -71.008 1.00 85.90 C ANISOU 1848 CA ASP A1002 12769 12282 7587 -2030 -227 -429 C ATOM 1849 C ASP A1002 -10.574 -11.559 -72.450 1.00 87.96 C ANISOU 1849 C ASP A1002 12533 12716 8171 -1846 -108 -497 C ATOM 1850 O ASP A1002 -11.293 -12.033 -73.324 1.00 87.62 O ANISOU 1850 O ASP A1002 12363 12743 8186 -1814 117 -548 O ATOM 1851 CB ASP A1002 -11.537 -10.726 -70.312 1.00 88.17 C ANISOU 1851 CB ASP A1002 13243 12623 7637 -2190 -18 -499 C ATOM 1852 CG ASP A1002 -12.195 -11.017 -68.976 1.00101.29 C ANISOU 1852 CG ASP A1002 15463 14121 8903 -2417 59 -473 C ATOM 1853 OD1 ASP A1002 -12.512 -12.204 -68.709 1.00103.31 O ANISOU 1853 OD1 ASP A1002 15945 14259 9049 -2490 50 -410 O ATOM 1854 OD2 ASP A1002 -12.417 -10.057 -68.208 1.00107.23 O ANISOU 1854 OD2 ASP A1002 16466 14843 9434 -2535 158 -522 O ATOM 1855 N LEU A1003 -9.532 -10.738 -72.698 1.00 84.86 N ANISOU 1855 N LEU A1003 11893 12373 7979 -1753 -270 -489 N ATOM 1856 CA LEU A1003 -9.095 -10.321 -74.028 1.00 83.83 C ANISOU 1856 CA LEU A1003 11336 12380 8135 -1602 -149 -545 C ATOM 1857 C LEU A1003 -8.685 -11.526 -74.853 1.00 88.88 C ANISOU 1857 C LEU A1003 11836 12958 8978 -1435 -147 -530 C ATOM 1858 O LEU A1003 -9.137 -11.656 -75.984 1.00 87.15 O ANISOU 1858 O LEU A1003 11480 12819 8814 -1378 98 -605 O ATOM 1859 CB LEU A1003 -7.924 -9.336 -73.932 1.00 85.11 C ANISOU 1859 CB LEU A1003 11290 12565 8482 -1577 -351 -512 C ATOM 1860 CG LEU A1003 -8.226 -7.885 -74.258 1.00 89.08 C ANISOU 1860 CG LEU A1003 11694 13207 8945 -1647 -184 -589 C ATOM 1861 CD1 LEU A1003 -8.680 -7.114 -73.009 1.00 90.05 C ANISOU 1861 CD1 LEU A1003 12172 13270 8771 -1822 -255 -592 C ATOM 1862 CD2 LEU A1003 -6.998 -7.216 -74.816 1.00 92.91 C ANISOU 1862 CD2 LEU A1003 11836 13738 9727 -1586 -292 -563 C ATOM 1863 N GLU A1004 -7.862 -12.426 -74.270 1.00 88.67 N ANISOU 1863 N GLU A1004 11891 12753 9047 -1357 -440 -432 N ATOM 1864 CA GLU A1004 -7.374 -13.645 -74.913 1.00 89.86 C ANISOU 1864 CA GLU A1004 11949 12785 9409 -1163 -457 -418 C ATOM 1865 C GLU A1004 -8.544 -14.525 -75.330 1.00 95.08 C ANISOU 1865 C GLU A1004 12839 13420 9865 -1220 -237 -469 C ATOM 1866 O GLU A1004 -8.525 -15.066 -76.434 1.00 95.36 O ANISOU 1866 O GLU A1004 12763 13446 10024 -1093 -63 -530 O ATOM 1867 CB GLU A1004 -6.420 -14.412 -73.986 1.00 94.30 C ANISOU 1867 CB GLU A1004 12613 13119 10097 -1082 -876 -286 C ATOM 1868 N ASP A1005 -9.580 -14.619 -74.477 1.00 92.47 N ANISOU 1868 N ASP A1005 12840 13073 9222 -1433 -218 -448 N ATOM 1869 CA ASP A1005 -10.783 -15.405 -74.740 1.00 92.41 C ANISOU 1869 CA ASP A1005 13030 13043 9038 -1548 -25 -478 C ATOM 1870 C ASP A1005 -11.622 -14.757 -75.836 1.00 95.94 C ANISOU 1870 C ASP A1005 13259 13682 9513 -1582 269 -583 C ATOM 1871 O ASP A1005 -12.215 -15.476 -76.642 1.00 95.94 O ANISOU 1871 O ASP A1005 13291 13651 9509 -1594 381 -616 O ATOM 1872 CB ASP A1005 -11.601 -15.565 -73.467 1.00 94.22 C ANISOU 1872 CB ASP A1005 13636 13203 8958 -1789 -36 -423 C ATOM 1873 N ASN A1006 -11.646 -13.407 -75.892 1.00 92.08 N ANISOU 1873 N ASN A1006 12577 13356 9051 -1602 353 -628 N ATOM 1874 CA ASN A1006 -12.399 -12.674 -76.913 1.00 90.84 C ANISOU 1874 CA ASN A1006 12227 13354 8935 -1625 570 -713 C ATOM 1875 C ASN A1006 -11.664 -12.744 -78.242 1.00 97.09 C ANISOU 1875 C ASN A1006 12832 14151 9905 -1461 607 -755 C ATOM 1876 O ASN A1006 -12.306 -12.949 -79.268 1.00 96.67 O ANISOU 1876 O ASN A1006 12777 14114 9840 -1481 727 -804 O ATOM 1877 CB ASN A1006 -12.658 -11.226 -76.496 1.00 91.32 C ANISOU 1877 CB ASN A1006 12196 13542 8959 -1689 638 -745 C ATOM 1878 CG ASN A1006 -13.714 -11.090 -75.411 1.00120.24 C ANISOU 1878 CG ASN A1006 16053 17198 12433 -1862 744 -742 C ATOM 1879 OD1 ASN A1006 -14.866 -11.534 -75.553 1.00116.60 O ANISOU 1879 OD1 ASN A1006 15613 16748 11941 -1966 900 -756 O ATOM 1880 ND2 ASN A1006 -13.358 -10.450 -74.307 1.00110.88 N ANISOU 1880 ND2 ASN A1006 15024 15981 11125 -1914 678 -725 N ATOM 1881 N TRP A1007 -10.317 -12.621 -78.218 1.00 95.85 N ANISOU 1881 N TRP A1007 12539 13960 9921 -1312 504 -732 N ATOM 1882 CA TRP A1007 -9.439 -12.745 -79.387 1.00 96.57 C ANISOU 1882 CA TRP A1007 12451 14030 10209 -1144 609 -776 C ATOM 1883 C TRP A1007 -9.630 -14.124 -80.025 1.00101.54 C ANISOU 1883 C TRP A1007 13258 14504 10817 -1071 670 -800 C ATOM 1884 O TRP A1007 -9.748 -14.218 -81.245 1.00101.13 O ANISOU 1884 O TRP A1007 13224 14441 10761 -1036 854 -873 O ATOM 1885 CB TRP A1007 -7.967 -12.522 -78.972 1.00 97.28 C ANISOU 1885 CB TRP A1007 12316 14086 10559 -1009 467 -724 C ATOM 1886 CG TRP A1007 -6.935 -12.809 -80.031 1.00100.10 C ANISOU 1886 CG TRP A1007 12457 14391 11185 -816 631 -766 C ATOM 1887 CD1 TRP A1007 -6.474 -14.036 -80.412 1.00105.06 C ANISOU 1887 CD1 TRP A1007 13127 14845 11947 -635 677 -779 C ATOM 1888 CD2 TRP A1007 -6.129 -11.847 -80.723 1.00100.44 C ANISOU 1888 CD2 TRP A1007 12211 14531 11422 -780 790 -797 C ATOM 1889 NE1 TRP A1007 -5.476 -13.899 -81.347 1.00106.38 N ANISOU 1889 NE1 TRP A1007 13039 14996 12383 -476 909 -832 N ATOM 1890 CE2 TRP A1007 -5.241 -12.566 -81.556 1.00106.88 C ANISOU 1890 CE2 TRP A1007 12891 15231 12486 -578 987 -838 C ATOM 1891 CE3 TRP A1007 -6.096 -10.443 -80.751 1.00100.80 C ANISOU 1891 CE3 TRP A1007 12123 14728 11447 -908 813 -798 C ATOM 1892 CZ2 TRP A1007 -4.339 -11.930 -82.418 1.00107.59 C ANISOU 1892 CZ2 TRP A1007 12705 15370 12806 -522 1247 -880 C ATOM 1893 CZ3 TRP A1007 -5.184 -9.813 -81.585 1.00103.72 C ANISOU 1893 CZ3 TRP A1007 12234 15142 12033 -866 1014 -825 C ATOM 1894 CH2 TRP A1007 -4.325 -10.552 -82.412 1.00106.85 C ANISOU 1894 CH2 TRP A1007 12486 15438 12676 -685 1249 -865 C ATOM 1895 N GLU A1008 -9.672 -15.181 -79.189 1.00 99.67 N ANISOU 1895 N GLU A1008 13218 14118 10534 -1067 503 -736 N ATOM 1896 CA GLU A1008 -9.849 -16.570 -79.599 1.00101.30 C ANISOU 1896 CA GLU A1008 13656 14131 10704 -1008 516 -747 C ATOM 1897 C GLU A1008 -11.221 -16.788 -80.226 1.00104.11 C ANISOU 1897 C GLU A1008 14197 14514 10847 -1198 631 -791 C ATOM 1898 O GLU A1008 -11.319 -17.567 -81.170 1.00104.65 O ANISOU 1898 O GLU A1008 14422 14452 10887 -1153 715 -844 O ATOM 1899 CB GLU A1008 -9.642 -17.521 -78.412 1.00104.90 C ANISOU 1899 CB GLU A1008 14320 14407 11130 -1000 264 -646 C ATOM 1900 CG GLU A1008 -8.327 -18.291 -78.462 1.00122.20 C ANISOU 1900 CG GLU A1008 16439 16397 13595 -719 148 -621 C ATOM 1901 CD GLU A1008 -7.033 -17.492 -78.465 1.00150.78 C ANISOU 1901 CD GLU A1008 19659 20086 17544 -543 108 -610 C ATOM 1902 OE1 GLU A1008 -6.540 -17.151 -77.365 1.00149.33 O ANISOU 1902 OE1 GLU A1008 19416 19894 17427 -568 -182 -507 O ATOM 1903 OE2 GLU A1008 -6.479 -17.263 -79.566 1.00145.97 O ANISOU 1903 OE2 GLU A1008 18823 19510 17128 -395 361 -697 O ATOM 1904 N THR A1009 -12.264 -16.077 -79.738 1.00 99.30 N ANISOU 1904 N THR A1009 13564 14056 10112 -1407 637 -772 N ATOM 1905 CA THR A1009 -13.630 -16.141 -80.284 1.00 98.22 C ANISOU 1905 CA THR A1009 13500 13959 9859 -1601 709 -796 C ATOM 1906 C THR A1009 -13.634 -15.522 -81.700 1.00101.48 C ANISOU 1906 C THR A1009 13818 14429 10309 -1558 812 -872 C ATOM 1907 O THR A1009 -14.231 -16.100 -82.609 1.00101.57 O ANISOU 1907 O THR A1009 13997 14349 10245 -1635 814 -900 O ATOM 1908 CB THR A1009 -14.619 -15.444 -79.331 1.00103.28 C ANISOU 1908 CB THR A1009 14067 14735 10438 -1790 733 -760 C ATOM 1909 OG1 THR A1009 -14.577 -16.111 -78.074 1.00107.20 O ANISOU 1909 OG1 THR A1009 14760 15135 10835 -1858 658 -689 O ATOM 1910 CG2 THR A1009 -16.053 -15.443 -79.850 1.00100.19 C ANISOU 1910 CG2 THR A1009 13645 14392 10032 -1984 790 -770 C ATOM 1911 N LEU A1010 -12.951 -14.365 -81.877 1.00 97.65 N ANISOU 1911 N LEU A1010 13116 14069 9916 -1461 875 -899 N ATOM 1912 CA LEU A1010 -12.832 -13.661 -83.156 1.00 97.57 C ANISOU 1912 CA LEU A1010 13063 14098 9912 -1435 982 -962 C ATOM 1913 C LEU A1010 -12.053 -14.501 -84.159 1.00104.36 C ANISOU 1913 C LEU A1010 14095 14787 10770 -1303 1097 -1020 C ATOM 1914 O LEU A1010 -12.441 -14.541 -85.321 1.00104.24 O ANISOU 1914 O LEU A1010 14265 14705 10637 -1364 1158 -1069 O ATOM 1915 CB LEU A1010 -12.163 -12.281 -82.997 1.00 96.69 C ANISOU 1915 CB LEU A1010 12707 14131 9898 -1380 1030 -967 C ATOM 1916 CG LEU A1010 -12.915 -11.230 -82.178 1.00100.47 C ANISOU 1916 CG LEU A1010 13057 14753 10364 -1489 966 -938 C ATOM 1917 CD1 LEU A1010 -11.990 -10.090 -81.778 1.00100.14 C ANISOU 1917 CD1 LEU A1010 12834 14802 10413 -1428 975 -934 C ATOM 1918 CD2 LEU A1010 -14.144 -10.707 -82.919 1.00102.93 C ANISOU 1918 CD2 LEU A1010 13380 15105 10625 -1609 957 -955 C ATOM 1919 N ASN A1011 -10.981 -15.193 -83.701 1.00103.23 N ANISOU 1919 N ASN A1011 13919 14544 10761 -1122 1118 -1012 N ATOM 1920 CA ASN A1011 -10.127 -16.061 -84.521 1.00105.77 C ANISOU 1920 CA ASN A1011 14375 14671 11141 -940 1282 -1079 C ATOM 1921 C ASN A1011 -10.876 -17.298 -85.041 1.00111.53 C ANISOU 1921 C ASN A1011 15500 15195 11680 -1011 1252 -1109 C ATOM 1922 O ASN A1011 -10.674 -17.687 -86.192 1.00112.73 O ANISOU 1922 O ASN A1011 15892 15194 11746 -960 1429 -1197 O ATOM 1923 CB ASN A1011 -8.897 -16.512 -83.728 1.00108.03 C ANISOU 1923 CB ASN A1011 14471 14884 11693 -715 1245 -1042 C ATOM 1924 CG ASN A1011 -7.780 -15.499 -83.649 1.00137.72 C ANISOU 1924 CG ASN A1011 17852 18769 15707 -606 1332 -1035 C ATOM 1925 OD1 ASN A1011 -7.981 -14.276 -83.704 1.00129.97 O ANISOU 1925 OD1 ASN A1011 16726 17972 14684 -731 1348 -1029 O ATOM 1926 ND2 ASN A1011 -6.563 -15.998 -83.495 1.00135.37 N ANISOU 1926 ND2 ASN A1011 17367 18353 15713 -370 1372 -1029 N ATOM 1927 N ASP A1012 -11.726 -17.907 -84.199 1.00108.00 N ANISOU 1927 N ASP A1012 15159 14725 11151 -1149 1045 -1037 N ATOM 1928 CA ASP A1012 -12.487 -19.106 -84.537 1.00109.44 C ANISOU 1928 CA ASP A1012 15713 14705 11165 -1263 970 -1043 C ATOM 1929 C ASP A1012 -13.648 -18.794 -85.494 1.00112.85 C ANISOU 1929 C ASP A1012 16294 15165 11420 -1503 930 -1064 C ATOM 1930 O ASP A1012 -13.895 -19.587 -86.404 1.00114.36 O ANISOU 1930 O ASP A1012 16848 15146 11459 -1555 932 -1115 O ATOM 1931 CB ASP A1012 -13.013 -19.785 -83.261 1.00111.56 C ANISOU 1931 CB ASP A1012 16035 14943 11411 -1376 777 -942 C ATOM 1932 CG ASP A1012 -11.928 -20.305 -82.329 1.00125.52 C ANISOU 1932 CG ASP A1012 17764 16604 13325 -1158 714 -898 C ATOM 1933 OD1 ASP A1012 -10.726 -20.137 -82.654 1.00127.99 O ANISOU 1933 OD1 ASP A1012 17922 16880 13827 -897 824 -945 O ATOM 1934 OD2 ASP A1012 -12.276 -20.836 -81.253 1.00131.90 O ANISOU 1934 OD2 ASP A1012 18683 17357 14074 -1261 549 -808 O ATOM 1935 N ASN A1013 -14.351 -17.658 -85.300 1.00107.03 N ANISOU 1935 N ASN A1013 15302 14653 10710 -1645 868 -1024 N ATOM 1936 CA ASN A1013 -15.465 -17.270 -86.168 1.00106.54 C ANISOU 1936 CA ASN A1013 15322 14609 10548 -1859 759 -1022 C ATOM 1937 C ASN A1013 -14.954 -16.713 -87.491 1.00111.20 C ANISOU 1937 C ASN A1013 16064 15145 11041 -1794 875 -1101 C ATOM 1938 O ASN A1013 -15.711 -16.724 -88.461 1.00113.06 O ANISOU 1938 O ASN A1013 16542 15284 11130 -1964 746 -1107 O ATOM 1939 CB ASN A1013 -16.405 -16.274 -85.498 1.00105.42 C ANISOU 1939 CB ASN A1013 14845 14691 10520 -1997 662 -955 C ATOM 1940 CG ASN A1013 -17.371 -16.893 -84.522 1.00122.14 C ANISOU 1940 CG ASN A1013 16908 16820 12681 -2174 566 -878 C ATOM 1941 OD1 ASN A1013 -17.365 -16.566 -83.335 1.00120.44 O ANISOU 1941 OD1 ASN A1013 16489 16728 12543 -2160 626 -841 O ATOM 1942 ND2 ASN A1013 -18.224 -17.801 -84.992 1.00110.65 N ANISOU 1942 ND2 ASN A1013 15666 15217 11158 -2372 422 -852 N ATOM 1943 N LEU A1014 -13.678 -16.263 -87.552 1.00106.84 N ANISOU 1943 N LEU A1014 15396 14630 10569 -1574 1108 -1155 N ATOM 1944 CA LEU A1014 -13.058 -15.809 -88.801 1.00107.86 C ANISOU 1944 CA LEU A1014 15711 14682 10590 -1521 1309 -1237 C ATOM 1945 C LEU A1014 -12.767 -17.015 -89.703 1.00115.21 C ANISOU 1945 C LEU A1014 17117 15313 11343 -1477 1439 -1325 C ATOM 1946 O LEU A1014 -12.837 -16.899 -90.932 1.00116.24 O ANISOU 1946 O LEU A1014 17619 15300 11246 -1558 1522 -1388 O ATOM 1947 CB LEU A1014 -11.776 -14.997 -88.561 1.00107.41 C ANISOU 1947 CB LEU A1014 15342 14750 10720 -1326 1552 -1261 C ATOM 1948 CG LEU A1014 -11.961 -13.511 -88.259 1.00110.19 C ANISOU 1948 CG LEU A1014 15388 15333 11145 -1398 1483 -1211 C ATOM 1949 CD1 LEU A1014 -10.674 -12.894 -87.742 1.00110.47 C ANISOU 1949 CD1 LEU A1014 15086 15481 11408 -1231 1662 -1212 C ATOM 1950 CD2 LEU A1014 -12.484 -12.751 -89.459 1.00112.27 C ANISOU 1950 CD2 LEU A1014 15889 15561 11209 -1550 1464 -1228 C ATOM 1951 N LYS A1015 -12.459 -18.176 -89.079 1.00112.92 N ANISOU 1951 N LYS A1015 16874 14897 11131 -1355 1445 -1328 N ATOM 1952 CA LYS A1015 -12.204 -19.445 -89.763 1.00115.83 C ANISOU 1952 CA LYS A1015 17714 14945 11352 -1287 1560 -1416 C ATOM 1953 C LYS A1015 -13.502 -19.960 -90.399 1.00120.66 C ANISOU 1953 C LYS A1015 18761 15404 11681 -1586 1290 -1397 C ATOM 1954 O LYS A1015 -13.473 -20.469 -91.526 1.00123.08 O ANISOU 1954 O LYS A1015 19587 15446 11733 -1628 1382 -1488 O ATOM 1955 CB LYS A1015 -11.618 -20.492 -88.794 1.00118.99 C ANISOU 1955 CB LYS A1015 18031 15239 11940 -1081 1561 -1399 C ATOM 1956 CG LYS A1015 -10.179 -20.226 -88.359 1.00130.85 C ANISOU 1956 CG LYS A1015 19161 16797 13758 -758 1803 -1424 C ATOM 1957 CD LYS A1015 -9.685 -21.302 -87.388 1.00141.94 C ANISOU 1957 CD LYS A1015 20522 18055 15356 -562 1703 -1384 C ATOM 1958 CE LYS A1015 -8.316 -21.026 -86.802 1.00155.06 C ANISOU 1958 CE LYS A1015 21738 19771 17408 -258 1826 -1371 C ATOM 1959 NZ LYS A1015 -7.224 -21.146 -87.808 1.00168.83 N ANISOU 1959 NZ LYS A1015 23498 21355 19294 -2 2253 -1506 N ATOM 1960 N VAL A1016 -14.642 -19.776 -89.684 1.00114.39 N ANISOU 1960 N VAL A1016 17751 14768 10943 -1808 966 -1278 N ATOM 1961 CA VAL A1016 -15.994 -20.180 -90.087 1.00114.80 C ANISOU 1961 CA VAL A1016 18058 14719 10840 -2129 640 -1221 C ATOM 1962 C VAL A1016 -16.424 -19.407 -91.370 1.00121.30 C ANISOU 1962 C VAL A1016 19116 15500 11473 -2288 544 -1242 C ATOM 1963 O VAL A1016 -16.897 -20.042 -92.319 1.00123.29 O ANISOU 1963 O VAL A1016 19888 15487 11471 -2467 390 -1268 O ATOM 1964 CB VAL A1016 -16.994 -19.987 -88.913 1.00115.91 C ANISOU 1964 CB VAL A1016 17781 15078 11182 -2297 412 -1090 C ATOM 1965 CG1 VAL A1016 -18.446 -20.118 -89.363 1.00116.77 C ANISOU 1965 CG1 VAL A1016 17991 15135 11243 -2644 68 -1013 C ATOM 1966 CG2 VAL A1016 -16.700 -20.972 -87.790 1.00115.69 C ANISOU 1966 CG2 VAL A1016 17725 14997 11234 -2216 453 -1060 C ATOM 1967 N ILE A1017 -16.222 -18.067 -91.407 1.00117.21 N ANISOU 1967 N ILE A1017 18280 15203 11050 -2232 611 -1227 N ATOM 1968 CA ILE A1017 -16.569 -17.200 -92.551 1.00118.18 C ANISOU 1968 CA ILE A1017 18628 15280 10996 -2374 497 -1229 C ATOM 1969 C ILE A1017 -15.690 -17.566 -93.777 1.00125.20 C ANISOU 1969 C ILE A1017 20118 15889 11564 -2307 781 -1361 C ATOM 1970 O ILE A1017 -16.160 -17.476 -94.916 1.00126.91 O ANISOU 1970 O ILE A1017 20832 15904 11486 -2509 613 -1369 O ATOM 1971 CB ILE A1017 -16.443 -15.683 -92.177 1.00118.77 C ANISOU 1971 CB ILE A1017 18227 15639 11260 -2304 533 -1184 C ATOM 1972 CG1 ILE A1017 -17.289 -15.345 -90.931 1.00116.67 C ANISOU 1972 CG1 ILE A1017 17414 15617 11298 -2350 335 -1078 C ATOM 1973 CG2 ILE A1017 -16.837 -14.763 -93.356 1.00120.83 C ANISOU 1973 CG2 ILE A1017 18760 15820 11328 -2459 366 -1166 C ATOM 1974 CD1 ILE A1017 -16.915 -14.062 -90.206 1.00119.92 C ANISOU 1974 CD1 ILE A1017 17357 16292 11914 -2213 457 -1059 C ATOM 1975 N GLU A1018 -14.438 -18.004 -93.531 1.00122.50 N ANISOU 1975 N GLU A1018 19744 15511 11289 -2030 1206 -1461 N ATOM 1976 CA GLU A1018 -13.479 -18.392 -94.572 1.00125.53 C ANISOU 1976 CA GLU A1018 20632 15628 11436 -1913 1607 -1608 C ATOM 1977 C GLU A1018 -13.903 -19.693 -95.288 1.00132.02 C ANISOU 1977 C GLU A1018 22148 16072 11943 -2037 1512 -1672 C ATOM 1978 O GLU A1018 -13.687 -19.818 -96.493 1.00134.59 O ANISOU 1978 O GLU A1018 23104 16121 11914 -2106 1684 -1774 O ATOM 1979 CB GLU A1018 -12.075 -18.565 -93.960 1.00126.97 C ANISOU 1979 CB GLU A1018 20460 15878 11904 -1557 2057 -1681 C ATOM 1980 CG GLU A1018 -10.949 -18.570 -94.981 1.00142.94 C ANISOU 1980 CG GLU A1018 22815 17701 13794 -1406 2594 -1833 C ATOM 1981 CD GLU A1018 -9.573 -18.920 -94.451 1.00170.46 C ANISOU 1981 CD GLU A1018 25929 21199 17639 -1039 3026 -1905 C ATOM 1982 OE1 GLU A1018 -8.872 -19.714 -95.120 1.00175.01 O ANISOU 1982 OE1 GLU A1018 26881 21482 18135 -874 3428 -2048 O ATOM 1983 OE2 GLU A1018 -9.191 -18.404 -93.376 1.00163.28 O ANISOU 1983 OE2 GLU A1018 24367 20568 17104 -915 2957 -1819 O ATOM 1984 N LYS A1019 -14.484 -20.655 -94.546 1.00128.09 N ANISOU 1984 N LYS A1019 21586 15536 11546 -2083 1254 -1616 N ATOM 1985 CA LYS A1019 -14.895 -21.950 -95.094 1.00130.90 C ANISOU 1985 CA LYS A1019 22592 15520 11625 -2214 1129 -1667 C ATOM 1986 C LYS A1019 -16.442 -22.067 -95.210 1.00134.44 C ANISOU 1986 C LYS A1019 23167 15942 11973 -2621 533 -1533 C ATOM 1987 O LYS A1019 -16.971 -23.183 -95.291 1.00136.08 O ANISOU 1987 O LYS A1019 23761 15899 12046 -2778 320 -1527 O ATOM 1988 CB LYS A1019 -14.320 -23.093 -94.234 1.00133.68 C ANISOU 1988 CB LYS A1019 22852 15777 12163 -1971 1288 -1704 C ATOM 1989 CG LYS A1019 -12.810 -23.265 -94.391 1.00146.89 C ANISOU 1989 CG LYS A1019 24531 17345 13936 -1572 1855 -1853 C ATOM 1990 CD LYS A1019 -12.284 -24.465 -93.619 1.00157.19 C ANISOU 1990 CD LYS A1019 25804 18487 15433 -1321 1939 -1880 C ATOM 1991 CE LYS A1019 -10.815 -24.703 -93.880 1.00169.52 C ANISOU 1991 CE LYS A1019 27358 19896 17156 -906 2496 -2032 C ATOM 1992 NZ LYS A1019 -10.318 -25.921 -93.185 1.00179.72 N ANISOU 1992 NZ LYS A1019 28662 20971 18654 -637 2526 -2053 N ATOM 1993 N ALA A1020 -17.149 -20.913 -95.283 1.00128.65 N ANISOU 1993 N ALA A1020 22122 15437 11322 -2793 258 -1424 N ATOM 1994 CA ALA A1020 -18.611 -20.835 -95.419 1.00128.45 C ANISOU 1994 CA ALA A1020 22086 15409 11310 -3160 -318 -1281 C ATOM 1995 C ALA A1020 -19.047 -20.907 -96.882 1.00133.61 C ANISOU 1995 C ALA A1020 23501 15722 11543 -3429 -585 -1302 C ATOM 1996 O ALA A1020 -18.302 -20.473 -97.763 1.00134.57 O ANISOU 1996 O ALA A1020 24033 15716 11383 -3341 -309 -1406 O ATOM 1997 CB ALA A1020 -19.126 -19.549 -94.796 1.00126.31 C ANISOU 1997 CB ALA A1020 21110 15508 11373 -3171 -476 -1161 C ATOM 1998 N ASP A1021 -20.260 -21.441 -97.136 1.00130.58 N ANISOU 1998 N ASP A1021 23321 15177 11115 -3783 -1132 -1195 N ATOM 1999 CA ASP A1021 -20.819 -21.568 -98.488 1.00133.86 C ANISOU 1999 CA ASP A1021 24507 15229 11124 -4103 -1525 -1185 C ATOM 2000 C ASP A1021 -22.240 -20.955 -98.574 1.00137.78 C ANISOU 2000 C ASP A1021 24682 15815 11855 -4435 -2218 -981 C ATOM 2001 O ASP A1021 -22.911 -21.112 -99.601 1.00141.24 O ANISOU 2001 O ASP A1021 25708 15940 12016 -4762 -2709 -926 O ATOM 2002 CB ASP A1021 -20.830 -23.043 -98.950 1.00138.95 C ANISOU 2002 CB ASP A1021 25917 15451 11426 -4246 -1571 -1267 C ATOM 2003 CG ASP A1021 -21.599 -24.025 -98.079 1.00146.86 C ANISOU 2003 CG ASP A1021 26639 16473 12689 -4406 -1844 -1170 C ATOM 2004 OD1 ASP A1021 -22.048 -23.628 -96.980 1.00145.03 O ANISOU 2004 OD1 ASP A1021 25573 16607 12924 -4372 -1906 -1051 O ATOM 2005 OD2 ASP A1021 -21.715 -25.200 -98.475 1.00153.12 O ANISOU 2005 OD2 ASP A1021 28081 16896 13201 -4565 -1953 -1221 O ATOM 2006 N ASN A1022 -22.682 -20.248 -97.504 1.00130.39 N ANISOU 2006 N ASN A1022 22828 15279 11436 -4347 -2258 -870 N ATOM 2007 CA ASN A1022 -23.975 -19.553 -97.444 1.00130.71 C ANISOU 2007 CA ASN A1022 22392 15441 11829 -4581 -2828 -683 C ATOM 2008 C ASN A1022 -23.901 -18.364 -96.470 1.00130.73 C ANISOU 2008 C ASN A1022 21529 15870 12272 -4326 -2603 -643 C ATOM 2009 O ASN A1022 -23.087 -18.376 -95.543 1.00126.68 O ANISOU 2009 O ASN A1022 20692 15577 11861 -4043 -2093 -727 O ATOM 2010 CB ASN A1022 -25.139 -20.493 -97.079 1.00131.66 C ANISOU 2010 CB ASN A1022 22345 15489 12191 -4903 -3260 -557 C ATOM 2011 CG ASN A1022 -25.009 -21.235 -95.777 1.00143.63 C ANISOU 2011 CG ASN A1022 23418 17196 13958 -4794 -2915 -574 C ATOM 2012 OD1 ASN A1022 -25.440 -20.767 -94.719 1.00134.57 O ANISOU 2012 OD1 ASN A1022 21491 16372 13266 -4729 -2834 -496 O ATOM 2013 ND2 ASN A1022 -24.512 -22.459 -95.847 1.00134.00 N ANISOU 2013 ND2 ASN A1022 22741 15733 12437 -4807 -2744 -668 N ATOM 2014 N ALA A1023 -24.751 -17.337 -96.708 1.00128.46 N ANISOU 2014 N ALA A1023 20909 15660 12240 -4429 -3020 -513 N ATOM 2015 CA ALA A1023 -24.845 -16.091 -95.933 1.00125.43 C ANISOU 2015 CA ALA A1023 19773 15618 12266 -4214 -2887 -470 C ATOM 2016 C ALA A1023 -25.306 -16.320 -94.488 1.00126.77 C ANISOU 2016 C ALA A1023 19178 16079 12912 -4152 -2702 -429 C ATOM 2017 O ALA A1023 -24.961 -15.516 -93.621 1.00123.67 O ANISOU 2017 O ALA A1023 18280 15965 12742 -3903 -2366 -457 O ATOM 2018 CB ALA A1023 -25.797 -15.123 -96.614 1.00128.87 C ANISOU 2018 CB ALA A1023 20096 15984 12886 -4364 -3463 -328 C ATOM 2019 N ALA A1024 -26.089 -17.387 -94.230 1.00124.77 N ANISOU 2019 N ALA A1024 18879 15739 12790 -4404 -2916 -360 N ATOM 2020 CA ALA A1024 -26.570 -17.732 -92.889 1.00123.07 C ANISOU 2020 CA ALA A1024 18031 15755 12973 -4406 -2713 -316 C ATOM 2021 C ALA A1024 -25.402 -18.151 -91.977 1.00122.69 C ANISOU 2021 C ALA A1024 18033 15833 12751 -4141 -2117 -445 C ATOM 2022 O ALA A1024 -25.416 -17.817 -90.791 1.00120.15 O ANISOU 2022 O ALA A1024 17179 15771 12703 -4007 -1820 -440 O ATOM 2023 CB ALA A1024 -27.604 -18.839 -92.970 1.00127.36 C ANISOU 2023 CB ALA A1024 18619 16128 13644 -4785 -3087 -209 C ATOM 2024 N GLN A1025 -24.387 -18.857 -92.539 1.00118.41 N ANISOU 2024 N GLN A1025 18145 15084 11763 -4060 -1950 -560 N ATOM 2025 CA GLN A1025 -23.177 -19.281 -91.822 1.00115.42 C ANISOU 2025 CA GLN A1025 17844 14771 11241 -3784 -1446 -677 C ATOM 2026 C GLN A1025 -22.297 -18.067 -91.510 1.00116.46 C ANISOU 2026 C GLN A1025 17686 15136 11426 -3465 -1117 -740 C ATOM 2027 O GLN A1025 -21.689 -18.003 -90.438 1.00113.70 O ANISOU 2027 O GLN A1025 17040 14971 11190 -3261 -783 -773 O ATOM 2028 CB GLN A1025 -22.388 -20.322 -92.631 1.00118.27 C ANISOU 2028 CB GLN A1025 18961 14805 11172 -3766 -1361 -786 C ATOM 2029 CG GLN A1025 -23.003 -21.720 -92.618 1.00137.43 C ANISOU 2029 CG GLN A1025 21702 16992 13524 -4036 -1583 -744 C ATOM 2030 CD GLN A1025 -22.284 -22.727 -93.493 1.00160.60 C ANISOU 2030 CD GLN A1025 25452 19551 16019 -4012 -1504 -867 C ATOM 2031 OE1 GLN A1025 -21.504 -22.386 -94.394 1.00155.20 O ANISOU 2031 OE1 GLN A1025 25181 18739 15051 -3864 -1340 -977 O ATOM 2032 NE2 GLN A1025 -22.586 -24.002 -93.288 1.00156.43 N ANISOU 2032 NE2 GLN A1025 25214 18807 15414 -4183 -1611 -850 N ATOM 2033 N VAL A1026 -22.261 -17.096 -92.448 1.00113.17 N ANISOU 2033 N VAL A1026 17393 14689 10918 -3453 -1254 -743 N ATOM 2034 CA VAL A1026 -21.515 -15.839 -92.356 1.00110.41 C ANISOU 2034 CA VAL A1026 16829 14521 10599 -3210 -1008 -789 C ATOM 2035 C VAL A1026 -22.203 -14.929 -91.314 1.00113.64 C ANISOU 2035 C VAL A1026 16534 15216 11429 -3166 -1032 -710 C ATOM 2036 O VAL A1026 -21.522 -14.456 -90.403 1.00110.46 O ANISOU 2036 O VAL A1026 15834 15014 11121 -2949 -698 -755 O ATOM 2037 CB VAL A1026 -21.377 -15.159 -93.753 1.00115.36 C ANISOU 2037 CB VAL A1026 17906 14970 10956 -3270 -1183 -802 C ATOM 2038 CG1 VAL A1026 -20.843 -13.733 -93.647 1.00112.99 C ANISOU 2038 CG1 VAL A1026 17339 14856 10736 -3078 -1005 -817 C ATOM 2039 CG2 VAL A1026 -20.491 -15.988 -94.678 1.00116.73 C ANISOU 2039 CG2 VAL A1026 18806 14863 10685 -3264 -992 -919 C ATOM 2040 N LYS A1027 -23.540 -14.713 -91.433 1.00113.34 N ANISOU 2040 N LYS A1027 16235 15172 11658 -3371 -1423 -594 N ATOM 2041 CA LYS A1027 -24.332 -13.879 -90.513 1.00113.19 C ANISOU 2041 CA LYS A1027 15545 15382 12081 -3329 -1421 -526 C ATOM 2042 C LYS A1027 -24.223 -14.387 -89.054 1.00115.47 C ANISOU 2042 C LYS A1027 15513 15847 12513 -3266 -1055 -549 C ATOM 2043 O LYS A1027 -24.088 -13.572 -88.137 1.00113.48 O ANISOU 2043 O LYS A1027 14880 15797 12438 -3098 -801 -570 O ATOM 2044 CB LYS A1027 -25.815 -13.823 -90.946 1.00119.67 C ANISOU 2044 CB LYS A1027 16124 16118 13225 -3578 -1914 -391 C ATOM 2045 CG LYS A1027 -26.645 -12.788 -90.175 1.00137.55 C ANISOU 2045 CG LYS A1027 17684 18584 15995 -3490 -1891 -333 C ATOM 2046 CD LYS A1027 -28.145 -13.027 -90.280 1.00151.77 C ANISOU 2046 CD LYS A1027 19090 20327 18248 -3738 -2290 -194 C ATOM 2047 CE LYS A1027 -28.912 -12.105 -89.361 1.00160.98 C ANISOU 2047 CE LYS A1027 19520 21690 19956 -3611 -2130 -163 C ATOM 2048 NZ LYS A1027 -30.374 -12.371 -89.399 1.00173.45 N ANISOU 2048 NZ LYS A1027 20607 23221 22074 -3846 -2467 -24 N ATOM 2049 N ASP A1028 -24.266 -15.720 -88.853 1.00112.64 N ANISOU 2049 N ASP A1028 15377 15380 12042 -3413 -1040 -543 N ATOM 2050 CA ASP A1028 -24.166 -16.339 -87.534 1.00111.82 C ANISOU 2050 CA ASP A1028 15093 15384 12008 -3399 -738 -549 C ATOM 2051 C ASP A1028 -22.797 -16.079 -86.888 1.00111.71 C ANISOU 2051 C ASP A1028 15160 15469 11815 -3108 -369 -645 C ATOM 2052 O ASP A1028 -22.749 -15.733 -85.704 1.00110.67 O ANISOU 2052 O ASP A1028 14729 15505 11814 -3026 -128 -645 O ATOM 2053 CB ASP A1028 -24.428 -17.851 -87.620 1.00116.42 C ANISOU 2053 CB ASP A1028 16005 15770 12460 -3629 -851 -516 C ATOM 2054 CG ASP A1028 -24.366 -18.565 -86.282 1.00131.46 C ANISOU 2054 CG ASP A1028 17806 17742 14401 -3654 -574 -504 C ATOM 2055 OD1 ASP A1028 -25.222 -18.271 -85.408 1.00133.43 O ANISOU 2055 OD1 ASP A1028 17609 18142 14945 -3762 -474 -441 O ATOM 2056 OD2 ASP A1028 -23.464 -19.414 -86.106 1.00138.45 O ANISOU 2056 OD2 ASP A1028 19073 18508 15024 -3562 -446 -556 O ATOM 2057 N ALA A1029 -21.699 -16.241 -87.655 1.00106.31 N ANISOU 2057 N ALA A1029 14883 14665 10847 -2966 -321 -724 N ATOM 2058 CA ALA A1029 -20.337 -16.032 -87.163 1.00103.56 C ANISOU 2058 CA ALA A1029 14572 14387 10389 -2697 -12 -804 C ATOM 2059 C ALA A1029 -20.050 -14.547 -86.901 1.00105.77 C ANISOU 2059 C ALA A1029 14530 14867 10792 -2540 97 -819 C ATOM 2060 O ALA A1029 -19.358 -14.243 -85.924 1.00103.97 O ANISOU 2060 O ALA A1029 14138 14764 10603 -2387 313 -843 O ATOM 2061 CB ALA A1029 -19.330 -16.594 -88.144 1.00104.86 C ANISOU 2061 CB ALA A1029 15207 14351 10283 -2596 50 -886 C ATOM 2062 N LEU A1030 -20.608 -13.630 -87.735 1.00102.56 N ANISOU 2062 N LEU A1030 14062 14464 10443 -2593 -92 -797 N ATOM 2063 CA LEU A1030 -20.450 -12.178 -87.572 1.00101.10 C ANISOU 2063 CA LEU A1030 13610 14429 10374 -2461 -29 -806 C ATOM 2064 C LEU A1030 -21.119 -11.675 -86.287 1.00105.95 C ANISOU 2064 C LEU A1030 13778 15219 11261 -2447 71 -775 C ATOM 2065 O LEU A1030 -20.538 -10.816 -85.618 1.00104.69 O ANISOU 2065 O LEU A1030 13466 15182 11127 -2293 260 -811 O ATOM 2066 CB LEU A1030 -20.998 -11.391 -88.774 1.00102.45 C ANISOU 2066 CB LEU A1030 13870 14511 10544 -2535 -313 -771 C ATOM 2067 CG LEU A1030 -20.164 -11.408 -90.067 1.00107.83 C ANISOU 2067 CG LEU A1030 15047 15024 10901 -2527 -326 -820 C ATOM 2068 CD1 LEU A1030 -20.935 -10.791 -91.224 1.00110.02 C ANISOU 2068 CD1 LEU A1030 15495 15160 11149 -2666 -702 -757 C ATOM 2069 CD2 LEU A1030 -18.818 -10.709 -89.894 1.00107.27 C ANISOU 2069 CD2 LEU A1030 14979 15044 10736 -2326 1 -894 C ATOM 2070 N THR A1031 -22.321 -12.206 -85.934 1.00104.43 N ANISOU 2070 N THR A1031 13392 15021 11267 -2622 -30 -710 N ATOM 2071 CA THR A1031 -23.043 -11.813 -84.706 1.00104.59 C ANISOU 2071 CA THR A1031 13008 15182 11548 -2628 149 -692 C ATOM 2072 C THR A1031 -22.265 -12.258 -83.462 1.00105.10 C ANISOU 2072 C THR A1031 13160 15309 11465 -2561 450 -730 C ATOM 2073 O THR A1031 -22.207 -11.506 -82.492 1.00103.80 O ANISOU 2073 O THR A1031 12815 15256 11370 -2470 662 -758 O ATOM 2074 CB THR A1031 -24.481 -12.353 -84.665 1.00117.96 C ANISOU 2074 CB THR A1031 14450 16844 13525 -2858 11 -608 C ATOM 2075 OG1 THR A1031 -24.467 -13.771 -84.832 1.00120.80 O ANISOU 2075 OG1 THR A1031 15094 17079 13723 -3039 -71 -579 O ATOM 2076 CG2 THR A1031 -25.388 -11.690 -85.695 1.00118.28 C ANISOU 2076 CG2 THR A1031 14299 16826 13816 -2912 -342 -548 C ATOM 2077 N LYS A1032 -21.642 -13.455 -83.512 1.00100.60 N ANISOU 2077 N LYS A1032 12911 14633 10679 -2600 444 -732 N ATOM 2078 CA LYS A1032 -20.806 -13.995 -82.432 1.00 98.95 C ANISOU 2078 CA LYS A1032 12848 14429 10319 -2532 636 -748 C ATOM 2079 C LYS A1032 -19.515 -13.153 -82.294 1.00100.05 C ANISOU 2079 C LYS A1032 13014 14633 10368 -2298 728 -806 C ATOM 2080 O LYS A1032 -19.010 -12.983 -81.177 1.00 98.57 O ANISOU 2080 O LYS A1032 12817 14497 10137 -2235 863 -811 O ATOM 2081 CB LYS A1032 -20.481 -15.481 -82.668 1.00101.38 C ANISOU 2081 CB LYS A1032 13498 14561 10458 -2606 557 -731 C ATOM 2082 CG LYS A1032 -21.692 -16.402 -82.526 1.00109.79 C ANISOU 2082 CG LYS A1032 14558 15555 11604 -2883 483 -659 C ATOM 2083 CD LYS A1032 -21.335 -17.854 -82.799 1.00116.90 C ANISOU 2083 CD LYS A1032 15863 16243 12313 -2954 385 -647 C ATOM 2084 CE LYS A1032 -22.536 -18.758 -82.731 1.00124.64 C ANISOU 2084 CE LYS A1032 16852 17133 13370 -3273 283 -566 C ATOM 2085 NZ LYS A1032 -22.160 -20.182 -82.925 1.00133.34 N ANISOU 2085 NZ LYS A1032 18408 17995 14261 -3341 187 -557 N ATOM 2086 N MET A1033 -19.019 -12.597 -83.429 1.00 95.15 N ANISOU 2086 N MET A1033 12445 13994 9714 -2201 643 -842 N ATOM 2087 CA MET A1033 -17.862 -11.702 -83.477 1.00 93.49 C ANISOU 2087 CA MET A1033 12219 13845 9460 -2020 729 -888 C ATOM 2088 C MET A1033 -18.222 -10.335 -82.915 1.00 96.40 C ANISOU 2088 C MET A1033 12333 14344 9949 -1986 784 -893 C ATOM 2089 O MET A1033 -17.396 -9.710 -82.247 1.00 95.63 O ANISOU 2089 O MET A1033 12199 14309 9827 -1883 879 -915 O ATOM 2090 CB MET A1033 -17.335 -11.554 -84.906 1.00 96.27 C ANISOU 2090 CB MET A1033 12749 14111 9717 -1974 672 -922 C ATOM 2091 CG MET A1033 -16.444 -12.684 -85.333 1.00100.98 C ANISOU 2091 CG MET A1033 13619 14567 10183 -1912 731 -954 C ATOM 2092 SD MET A1033 -15.801 -12.483 -87.004 1.00106.59 S ANISOU 2092 SD MET A1033 14614 15148 10738 -1873 774 -1015 S ATOM 2093 CE MET A1033 -14.584 -11.186 -86.732 1.00102.38 C ANISOU 2093 CE MET A1033 13855 14756 10288 -1713 959 -1041 C ATOM 2094 N ARG A1034 -19.463 -9.876 -83.178 1.00 92.93 N ANISOU 2094 N ARG A1034 11717 13926 9667 -2072 705 -871 N ATOM 2095 CA ARG A1034 -19.978 -8.597 -82.694 1.00 91.93 C ANISOU 2095 CA ARG A1034 11345 13886 9699 -2018 770 -885 C ATOM 2096 C ARG A1034 -20.146 -8.629 -81.168 1.00 95.45 C ANISOU 2096 C ARG A1034 11716 14392 10159 -2030 997 -898 C ATOM 2097 O ARG A1034 -19.869 -7.625 -80.510 1.00 94.53 O ANISOU 2097 O ARG A1034 11552 14324 10042 -1940 1114 -938 O ATOM 2098 CB ARG A1034 -21.309 -8.257 -83.378 1.00 92.21 C ANISOU 2098 CB ARG A1034 11174 13892 9969 -2092 602 -846 C ATOM 2099 CG ARG A1034 -21.570 -6.760 -83.429 1.00 97.11 C ANISOU 2099 CG ARG A1034 11611 14543 10742 -1972 593 -866 C ATOM 2100 CD ARG A1034 -22.946 -6.451 -83.960 1.00 98.42 C ANISOU 2100 CD ARG A1034 11507 14662 11226 -2020 398 -814 C ATOM 2101 NE ARG A1034 -23.164 -5.010 -84.095 1.00 99.26 N ANISOU 2101 NE ARG A1034 11469 14756 11491 -1874 354 -830 N ATOM 2102 CZ ARG A1034 -23.732 -4.239 -83.172 1.00106.98 C ANISOU 2102 CZ ARG A1034 12179 15772 12696 -1770 563 -871 C ATOM 2103 NH1 ARG A1034 -24.145 -4.761 -82.021 1.00 86.66 N ANISOU 2103 NH1 ARG A1034 9465 13262 10198 -1817 864 -898 N ATOM 2104 NH2 ARG A1034 -23.897 -2.942 -83.395 1.00 91.07 N ANISOU 2104 NH2 ARG A1034 10078 13705 10820 -1622 492 -887 N ATOM 2105 N ALA A1035 -20.586 -9.787 -80.613 1.00 92.69 N ANISOU 2105 N ALA A1035 11419 14011 9788 -2164 1058 -864 N ATOM 2106 CA ALA A1035 -20.771 -9.997 -79.172 1.00 92.97 C ANISOU 2106 CA ALA A1035 11491 14064 9771 -2225 1290 -868 C ATOM 2107 C ALA A1035 -19.420 -9.938 -78.450 1.00 96.43 C ANISOU 2107 C ALA A1035 12174 14488 9977 -2133 1307 -885 C ATOM 2108 O ALA A1035 -19.305 -9.227 -77.453 1.00 96.69 O ANISOU 2108 O ALA A1035 12243 14543 9951 -2109 1452 -916 O ATOM 2109 CB ALA A1035 -21.457 -11.329 -78.910 1.00 94.94 C ANISOU 2109 CB ALA A1035 11801 14252 10019 -2422 1319 -812 C ATOM 2110 N ALA A1036 -18.394 -10.639 -78.996 1.00 91.69 N ANISOU 2110 N ALA A1036 11739 13831 9268 -2074 1149 -866 N ATOM 2111 CA ALA A1036 -17.027 -10.689 -78.474 1.00 90.56 C ANISOU 2111 CA ALA A1036 11758 13656 8995 -1973 1096 -863 C ATOM 2112 C ALA A1036 -16.379 -9.291 -78.474 1.00 93.27 C ANISOU 2112 C ALA A1036 12000 14072 9366 -1862 1096 -902 C ATOM 2113 O ALA A1036 -15.784 -8.902 -77.464 1.00 92.57 O ANISOU 2113 O ALA A1036 12009 13974 9190 -1851 1098 -899 O ATOM 2114 CB ALA A1036 -16.187 -11.658 -79.300 1.00 90.97 C ANISOU 2114 CB ALA A1036 11920 13621 9025 -1899 969 -847 C ATOM 2115 N ALA A1037 -16.524 -8.533 -79.596 1.00 88.55 N ANISOU 2115 N ALA A1037 11256 13520 8870 -1808 1066 -931 N ATOM 2116 CA ALA A1037 -15.980 -7.181 -79.759 1.00 87.11 C ANISOU 2116 CA ALA A1037 10997 13386 8714 -1727 1060 -963 C ATOM 2117 C ALA A1037 -16.551 -6.209 -78.701 1.00 91.46 C ANISOU 2117 C ALA A1037 11525 13962 9264 -1745 1173 -995 C ATOM 2118 O ALA A1037 -15.777 -5.479 -78.076 1.00 90.13 O ANISOU 2118 O ALA A1037 11433 13790 9023 -1717 1159 -1008 O ATOM 2119 CB ALA A1037 -16.264 -6.660 -81.163 1.00 87.21 C ANISOU 2119 CB ALA A1037 10932 13403 8803 -1703 999 -975 C ATOM 2120 N LEU A1038 -17.884 -6.237 -78.470 1.00 89.65 N ANISOU 2120 N LEU A1038 11198 13738 9127 -1800 1297 -1008 N ATOM 2121 CA LEU A1038 -18.545 -5.365 -77.488 1.00 90.95 C ANISOU 2121 CA LEU A1038 11344 13898 9313 -1798 1492 -1060 C ATOM 2122 C LEU A1038 -18.215 -5.786 -76.037 1.00 96.34 C ANISOU 2122 C LEU A1038 12294 14531 9780 -1881 1612 -1061 C ATOM 2123 O LEU A1038 -18.208 -4.928 -75.147 1.00 96.20 O ANISOU 2123 O LEU A1038 12408 14474 9669 -1873 1743 -1113 O ATOM 2124 CB LEU A1038 -20.070 -5.346 -77.700 1.00 92.53 C ANISOU 2124 CB LEU A1038 11295 14108 9755 -1823 1623 -1070 C ATOM 2125 CG LEU A1038 -20.554 -4.715 -79.012 1.00 97.21 C ANISOU 2125 CG LEU A1038 11658 14707 10572 -1745 1450 -1060 C ATOM 2126 CD1 LEU A1038 -21.980 -5.111 -79.310 1.00 99.60 C ANISOU 2126 CD1 LEU A1038 11678 15005 11160 -1807 1476 -1031 C ATOM 2127 CD2 LEU A1038 -20.388 -3.199 -79.015 1.00 98.89 C ANISOU 2127 CD2 LEU A1038 11853 14895 10826 -1612 1460 -1113 C ATOM 2128 N ASP A1039 -17.926 -7.092 -75.818 1.00 93.76 N ANISOU 2128 N ASP A1039 12105 14172 9347 -1967 1547 -1001 N ATOM 2129 CA ASP A1039 -17.560 -7.654 -74.519 1.00 95.39 C ANISOU 2129 CA ASP A1039 12634 14292 9317 -2067 1585 -974 C ATOM 2130 C ASP A1039 -16.112 -7.307 -74.170 1.00 99.14 C ANISOU 2130 C ASP A1039 13283 14723 9662 -2012 1351 -950 C ATOM 2131 O ASP A1039 -15.818 -7.018 -73.007 1.00100.80 O ANISOU 2131 O ASP A1039 13784 14847 9668 -2082 1359 -952 O ATOM 2132 CB ASP A1039 -17.757 -9.177 -74.497 1.00 98.28 C ANISOU 2132 CB ASP A1039 13099 14606 9637 -2173 1549 -905 C ATOM 2133 CG ASP A1039 -17.776 -9.753 -73.095 1.00115.22 C ANISOU 2133 CG ASP A1039 15621 16634 11524 -2324 1640 -872 C ATOM 2134 OD1 ASP A1039 -18.885 -10.046 -72.590 1.00118.84 O ANISOU 2134 OD1 ASP A1039 16113 17074 11966 -2470 1921 -883 O ATOM 2135 OD2 ASP A1039 -16.683 -9.876 -72.483 1.00120.73 O ANISOU 2135 OD2 ASP A1039 16587 17241 12045 -2311 1427 -829 O ATOM 2136 N ALA A1040 -15.212 -7.372 -75.168 1.00 93.92 N ANISOU 2136 N ALA A1040 12459 14102 9124 -1905 1146 -924 N ATOM 2137 CA ALA A1040 -13.796 -7.045 -75.022 1.00 93.76 C ANISOU 2137 CA ALA A1040 12480 14053 9091 -1849 919 -889 C ATOM 2138 C ALA A1040 -13.607 -5.543 -74.826 1.00 98.95 C ANISOU 2138 C ALA A1040 13128 14733 9735 -1840 933 -939 C ATOM 2139 O ALA A1040 -12.653 -5.128 -74.167 1.00 99.74 O ANISOU 2139 O ALA A1040 13361 14773 9762 -1870 754 -909 O ATOM 2140 CB ALA A1040 -13.027 -7.517 -76.238 1.00 93.43 C ANISOU 2140 CB ALA A1040 12231 14044 9223 -1739 809 -865 C ATOM 2141 N GLN A1041 -14.530 -4.732 -75.388 1.00 95.61 N ANISOU 2141 N GLN A1041 12561 14370 9396 -1805 1111 -1007 N ATOM 2142 CA GLN A1041 -14.560 -3.273 -75.280 1.00 95.60 C ANISOU 2142 CA GLN A1041 12572 14360 9391 -1781 1152 -1065 C ATOM 2143 C GLN A1041 -14.835 -2.860 -73.829 1.00103.04 C ANISOU 2143 C GLN A1041 13835 15198 10118 -1863 1263 -1107 C ATOM 2144 O GLN A1041 -14.313 -1.841 -73.378 1.00103.32 O ANISOU 2144 O GLN A1041 14028 15168 10059 -1882 1190 -1133 O ATOM 2145 CB GLN A1041 -15.624 -2.690 -76.226 1.00 95.99 C ANISOU 2145 CB GLN A1041 12397 14460 9613 -1704 1289 -1115 C ATOM 2146 CG GLN A1041 -15.489 -1.187 -76.471 1.00 98.30 C ANISOU 2146 CG GLN A1041 12684 14725 9940 -1649 1271 -1162 C ATOM 2147 CD GLN A1041 -16.505 -0.627 -77.435 1.00104.37 C ANISOU 2147 CD GLN A1041 13248 15507 10903 -1559 1331 -1190 C ATOM 2148 OE1 GLN A1041 -17.521 -1.252 -77.763 1.00101.79 O ANISOU 2148 OE1 GLN A1041 12760 15206 10708 -1546 1408 -1185 O ATOM 2149 NE2 GLN A1041 -16.261 0.588 -77.898 1.00 89.35 N ANISOU 2149 NE2 GLN A1041 11355 13562 9033 -1509 1259 -1210 N ATOM 2150 N LYS A1042 -15.648 -3.665 -73.108 1.00102.63 N ANISOU 2150 N LYS A1042 13921 15107 9965 -1936 1451 -1113 N ATOM 2151 CA LYS A1042 -16.022 -3.469 -71.699 1.00105.32 C ANISOU 2151 CA LYS A1042 14651 15320 10046 -2045 1638 -1159 C ATOM 2152 C LYS A1042 -14.809 -3.648 -70.777 1.00113.80 C ANISOU 2152 C LYS A1042 16104 16272 10863 -2153 1340 -1091 C ATOM 2153 O LYS A1042 -14.713 -2.954 -69.765 1.00115.18 O ANISOU 2153 O LYS A1042 16662 16310 10790 -2239 1376 -1135 O ATOM 2154 CB LYS A1042 -17.141 -4.444 -71.288 1.00107.69 C ANISOU 2154 CB LYS A1042 14987 15611 10320 -2131 1931 -1163 C ATOM 2155 CG LYS A1042 -18.517 -4.082 -71.833 1.00114.21 C ANISOU 2155 CG LYS A1042 15469 16510 11414 -2055 2256 -1236 C ATOM 2156 N ALA A1043 -13.883 -4.563 -71.140 1.00112.82 N ANISOU 2156 N ALA A1043 15881 16172 10812 -2144 1029 -984 N ATOM 2157 CA ALA A1043 -12.660 -4.857 -70.391 1.00116.00 C ANISOU 2157 CA ALA A1043 16548 16452 11076 -2224 654 -889 C ATOM 2158 C ALA A1043 -11.757 -3.625 -70.271 1.00126.45 C ANISOU 2158 C ALA A1043 17904 17738 12403 -2237 431 -894 C ATOM 2159 O ALA A1043 -11.805 -2.728 -71.112 1.00125.13 O ANISOU 2159 O ALA A1043 17461 17672 12410 -2151 516 -949 O ATOM 2160 CB ALA A1043 -11.894 -5.991 -71.058 1.00115.72 C ANISOU 2160 CB ALA A1043 16268 16454 11245 -2143 408 -788 C ATOM 2161 N THR A1044 -10.958 -3.577 -69.204 1.00129.62 N ANISOU 2161 N THR A1044 18685 17969 12595 -2372 118 -827 N ATOM 2162 CA THR A1044 -10.028 -2.487 -68.942 1.00132.37 C ANISOU 2162 CA THR A1044 19119 18245 12931 -2442 -170 -810 C ATOM 2163 C THR A1044 -8.649 -2.908 -69.476 1.00141.12 C ANISOU 2163 C THR A1044 19863 19395 14359 -2395 -589 -677 C ATOM 2164 O THR A1044 -8.118 -3.932 -69.033 1.00142.03 O ANISOU 2164 O THR A1044 20061 19421 14483 -2414 -865 -569 O ATOM 2165 CB THR A1044 -10.040 -2.141 -67.441 1.00142.86 C ANISOU 2165 CB THR A1044 21128 19326 13826 -2646 -281 -816 C ATOM 2166 OG1 THR A1044 -11.321 -1.600 -67.119 1.00142.33 O ANISOU 2166 OG1 THR A1044 21309 19231 13539 -2649 217 -966 O ATOM 2167 CG2 THR A1044 -8.947 -1.147 -67.044 1.00142.88 C ANISOU 2167 CG2 THR A1044 21289 19206 13795 -2770 -700 -768 C ATOM 2168 N PRO A1045 -8.064 -2.148 -70.437 1.00140.35 N ANISOU 2168 N PRO A1045 19361 19418 14549 -2330 -620 -683 N ATOM 2169 CA PRO A1045 -6.731 -2.507 -70.948 1.00142.11 C ANISOU 2169 CA PRO A1045 19189 19676 15131 -2287 -942 -565 C ATOM 2170 C PRO A1045 -5.659 -2.452 -69.848 1.00153.33 C ANISOU 2170 C PRO A1045 20837 20907 16516 -2446 -1473 -439 C ATOM 2171 O PRO A1045 -5.761 -1.623 -68.935 1.00155.11 O ANISOU 2171 O PRO A1045 21505 20989 16440 -2621 -1598 -460 O ATOM 2172 CB PRO A1045 -6.471 -1.448 -72.026 1.00142.24 C ANISOU 2172 CB PRO A1045 18855 19824 15365 -2255 -801 -611 C ATOM 2173 CG PRO A1045 -7.319 -0.294 -71.644 1.00146.00 C ANISOU 2173 CG PRO A1045 19667 20251 15555 -2334 -620 -719 C ATOM 2174 CD PRO A1045 -8.560 -0.915 -71.080 1.00140.91 C ANISOU 2174 CD PRO A1045 19328 19570 14640 -2301 -361 -790 C ATOM 2175 N PRO A1046 -4.633 -3.332 -69.908 1.00153.42 N ANISOU 2175 N PRO A1046 20571 20883 16837 -2384 -1809 -307 N ATOM 2176 CA PRO A1046 -3.586 -3.328 -68.864 1.00157.85 C ANISOU 2176 CA PRO A1046 21318 21237 17420 -2538 -2413 -158 C ATOM 2177 C PRO A1046 -2.743 -2.052 -68.822 1.00164.89 C ANISOU 2177 C PRO A1046 22094 22106 18451 -2701 -2675 -122 C ATOM 2178 O PRO A1046 -2.183 -1.737 -67.770 1.00167.62 O ANISOU 2178 O PRO A1046 22787 22243 18660 -2906 -3168 -26 O ATOM 2179 CB PRO A1046 -2.708 -4.503 -69.258 1.00160.79 C ANISOU 2179 CB PRO A1046 21247 21608 18238 -2365 -2638 -38 C ATOM 2180 CG PRO A1046 -2.945 -4.664 -70.736 1.00161.83 C ANISOU 2180 CG PRO A1046 20864 21974 18650 -2155 -2142 -134 C ATOM 2181 CD PRO A1046 -4.385 -4.390 -70.907 1.00153.94 C ANISOU 2181 CD PRO A1046 20168 21063 17258 -2165 -1674 -285 C ATOM 2182 N LYS A1047 -2.639 -1.340 -69.970 1.00160.76 N ANISOU 2182 N LYS A1047 21123 21774 18184 -2637 -2372 -187 N ATOM 2183 CA LYS A1047 -1.902 -0.081 -70.119 1.00162.57 C ANISOU 2183 CA LYS A1047 21206 22001 18563 -2805 -2541 -160 C ATOM 2184 C LYS A1047 -2.568 1.031 -69.299 1.00168.04 C ANISOU 2184 C LYS A1047 22530 22554 18762 -2999 -2541 -247 C ATOM 2185 O LYS A1047 -1.880 1.917 -68.783 1.00170.51 O ANISOU 2185 O LYS A1047 22993 22733 19060 -3223 -2911 -186 O ATOM 2186 CB LYS A1047 -1.825 0.317 -71.600 1.00162.87 C ANISOU 2186 CB LYS A1047 20714 22258 18911 -2691 -2127 -222 C ATOM 2187 N LEU A1048 -3.910 0.959 -69.172 1.00162.71 N ANISOU 2187 N LEU A1048 22223 21894 17706 -2914 -2120 -390 N ATOM 2188 CA LEU A1048 -4.746 1.893 -68.420 1.00162.91 C ANISOU 2188 CA LEU A1048 22859 21775 17263 -3034 -1978 -508 C ATOM 2189 C LEU A1048 -5.528 1.147 -67.310 1.00166.80 C ANISOU 2189 C LEU A1048 23931 22115 17332 -3062 -1921 -539 C ATOM 2190 O LEU A1048 -6.689 1.469 -67.037 1.00165.24 O ANISOU 2190 O LEU A1048 24089 21882 16813 -3033 -1503 -684 O ATOM 2191 CB LEU A1048 -5.700 2.616 -69.388 1.00159.99 C ANISOU 2191 CB LEU A1048 22334 21555 16901 -2892 -1447 -660 C ATOM 2192 N GLU A1049 -4.869 0.159 -66.663 1.00165.56 N ANISOU 2192 N GLU A1049 23866 21844 17195 -3123 -2343 -396 N ATOM 2193 CA GLU A1049 -5.433 -0.654 -65.577 1.00167.16 C ANISOU 2193 CA GLU A1049 24664 21866 16985 -3195 -2361 -388 C ATOM 2194 C GLU A1049 -5.639 0.174 -64.295 1.00174.57 C ANISOU 2194 C GLU A1049 26436 22514 17380 -3452 -2484 -437 C ATOM 2195 O GLU A1049 -6.508 -0.166 -63.489 1.00175.26 O ANISOU 2195 O GLU A1049 27107 22461 17021 -3514 -2230 -507 O ATOM 2196 CB GLU A1049 -4.532 -1.860 -65.280 1.00170.55 C ANISOU 2196 CB GLU A1049 24977 22210 17614 -3192 -2871 -199 C ATOM 2197 N ASP A1050 -4.848 1.255 -64.117 1.00173.28 N ANISOU 2197 N ASP A1050 26354 22243 17243 -3619 -2848 -403 N ATOM 2198 CA ASP A1050 -4.916 2.170 -62.971 1.00176.81 C ANISOU 2198 CA ASP A1050 27630 22379 17172 -3884 -3012 -453 C ATOM 2199 C ASP A1050 -5.303 3.606 -63.414 1.00179.45 C ANISOU 2199 C ASP A1050 27964 22747 17473 -3870 -2677 -612 C ATOM 2200 O ASP A1050 -5.319 4.519 -62.582 1.00181.97 O ANISOU 2200 O ASP A1050 28958 22795 17388 -4077 -2789 -674 O ATOM 2201 CB ASP A1050 -3.570 2.184 -62.222 1.00183.08 C ANISOU 2201 CB ASP A1050 28637 22934 17993 -4150 -3872 -249 C ATOM 2202 N LYS A1051 -5.637 3.790 -64.714 1.00171.83 N ANISOU 2202 N LYS A1051 26308 22079 16902 -3630 -2277 -679 N ATOM 2203 CA LYS A1051 -6.012 5.081 -65.307 1.00170.18 C ANISOU 2203 CA LYS A1051 26027 21907 16724 -3580 -1975 -811 C ATOM 2204 C LYS A1051 -7.539 5.267 -65.380 1.00171.55 C ANISOU 2204 C LYS A1051 26389 22108 16684 -3385 -1275 -1017 C ATOM 2205 O LYS A1051 -8.290 4.289 -65.323 1.00170.09 O ANISOU 2205 O LYS A1051 26158 22009 16459 -3261 -970 -1044 O ATOM 2206 CB LYS A1051 -5.408 5.222 -66.715 1.00169.89 C ANISOU 2206 CB LYS A1051 25167 22142 17243 -3463 -1998 -743 C ATOM 2207 N SER A1052 -7.974 6.544 -65.524 1.00167.29 N ANISOU 2207 N SER A1052 26036 21478 16049 -3361 -1040 -1153 N ATOM 2208 CA SER A1052 -9.360 7.030 -65.622 1.00165.69 C ANISOU 2208 CA SER A1052 25972 21255 15727 -3159 -407 -1355 C ATOM 2209 C SER A1052 -10.183 6.285 -66.706 1.00164.18 C ANISOU 2209 C SER A1052 25117 21367 15895 -2881 -10 -1374 C ATOM 2210 O SER A1052 -9.622 5.963 -67.757 1.00161.74 O ANISOU 2210 O SER A1052 24212 21281 15959 -2820 -186 -1267 O ATOM 2211 CB SER A1052 -9.351 8.526 -65.936 1.00169.25 C ANISOU 2211 CB SER A1052 26541 21584 16182 -3155 -373 -1446 C ATOM 2212 OG SER A1052 -10.649 9.070 -66.114 1.00176.32 O ANISOU 2212 OG SER A1052 27498 22441 17053 -2919 205 -1633 O ATOM 2213 N PRO A1053 -11.512 6.046 -66.511 1.00158.83 N ANISOU 2213 N PRO A1053 24529 20688 15130 -2721 534 -1510 N ATOM 2214 CA PRO A1053 -12.298 5.362 -67.560 1.00154.64 C ANISOU 2214 CA PRO A1053 23371 20424 14959 -2491 838 -1513 C ATOM 2215 C PRO A1053 -12.566 6.257 -68.786 1.00153.46 C ANISOU 2215 C PRO A1053 22794 20380 15135 -2311 932 -1554 C ATOM 2216 O PRO A1053 -13.127 5.783 -69.776 1.00150.36 O ANISOU 2216 O PRO A1053 21899 20186 15044 -2143 1094 -1540 O ATOM 2217 CB PRO A1053 -13.611 4.993 -66.847 1.00158.26 C ANISOU 2217 CB PRO A1053 24087 20806 15241 -2421 1372 -1641 C ATOM 2218 CG PRO A1053 -13.372 5.250 -65.385 1.00167.04 C ANISOU 2218 CG PRO A1053 26008 21616 15845 -2636 1336 -1689 C ATOM 2219 CD PRO A1053 -12.356 6.342 -65.337 1.00163.68 C ANISOU 2219 CD PRO A1053 25810 21047 15334 -2758 912 -1663 C ATOM 2220 N ASP A1054 -12.154 7.541 -68.724 1.00149.15 N ANISOU 2220 N ASP A1054 22495 19669 14506 -2368 795 -1595 N ATOM 2221 CA ASP A1054 -12.300 8.523 -69.800 1.00146.56 C ANISOU 2221 CA ASP A1054 21884 19376 14428 -2236 824 -1622 C ATOM 2222 C ASP A1054 -10.932 9.175 -70.130 1.00147.16 C ANISOU 2222 C ASP A1054 21954 19425 14534 -2435 364 -1510 C ATOM 2223 O ASP A1054 -10.887 10.275 -70.692 1.00146.59 O ANISOU 2223 O ASP A1054 21887 19275 14536 -2411 338 -1539 O ATOM 2224 CB ASP A1054 -13.345 9.586 -69.413 1.00150.81 C ANISOU 2224 CB ASP A1054 22751 19688 14861 -2083 1192 -1803 C ATOM 2225 N SER A1055 -9.822 8.467 -69.809 1.00141.55 N ANISOU 2225 N SER A1055 21202 18772 13807 -2634 -6 -1373 N ATOM 2226 CA SER A1055 -8.446 8.913 -70.061 1.00140.98 C ANISOU 2226 CA SER A1055 21029 18693 13844 -2852 -452 -1243 C ATOM 2227 C SER A1055 -8.121 8.842 -71.574 1.00140.16 C ANISOU 2227 C SER A1055 20305 18822 14127 -2769 -429 -1165 C ATOM 2228 O SER A1055 -8.837 8.133 -72.291 1.00137.45 O ANISOU 2228 O SER A1055 19638 18652 13935 -2567 -161 -1187 O ATOM 2229 CB SER A1055 -7.451 8.082 -69.247 1.00145.72 C ANISOU 2229 CB SER A1055 21711 19270 14385 -3052 -856 -1113 C ATOM 2230 OG SER A1055 -7.311 6.751 -69.715 1.00151.27 O ANISOU 2230 OG SER A1055 21951 20197 15328 -2949 -844 -1025 O ATOM 2231 N PRO A1056 -7.074 9.551 -72.094 1.00135.47 N ANISOU 2231 N PRO A1056 19567 18222 13685 -2945 -691 -1074 N ATOM 2232 CA PRO A1056 -6.788 9.477 -73.545 1.00132.29 C ANISOU 2232 CA PRO A1056 18650 18014 13599 -2887 -597 -1009 C ATOM 2233 C PRO A1056 -6.516 8.049 -74.026 1.00131.34 C ANISOU 2233 C PRO A1056 18073 18122 13709 -2795 -553 -932 C ATOM 2234 O PRO A1056 -6.939 7.693 -75.124 1.00128.68 O ANISOU 2234 O PRO A1056 17444 17930 13520 -2645 -315 -943 O ATOM 2235 CB PRO A1056 -5.538 10.353 -73.713 1.00136.25 C ANISOU 2235 CB PRO A1056 19117 18445 14209 -3163 -901 -907 C ATOM 2236 CG PRO A1056 -5.518 11.240 -72.529 1.00143.63 C ANISOU 2236 CG PRO A1056 20625 19107 14841 -3322 -1112 -958 C ATOM 2237 CD PRO A1056 -6.120 10.452 -71.410 1.00139.74 C ANISOU 2237 CD PRO A1056 20428 18558 14108 -3231 -1070 -1022 C ATOM 2238 N GLU A1057 -5.844 7.235 -73.184 1.00126.78 N ANISOU 2238 N GLU A1057 17490 17539 13141 -2884 -807 -854 N ATOM 2239 CA GLU A1057 -5.482 5.836 -73.439 1.00124.34 C ANISOU 2239 CA GLU A1057 16804 17390 13048 -2794 -820 -777 C ATOM 2240 C GLU A1057 -6.725 4.932 -73.459 1.00122.34 C ANISOU 2240 C GLU A1057 16600 17207 12675 -2575 -510 -863 C ATOM 2241 O GLU A1057 -6.782 3.985 -74.245 1.00119.16 O ANISOU 2241 O GLU A1057 15858 16957 12460 -2445 -371 -839 O ATOM 2242 CB GLU A1057 -4.480 5.335 -72.372 1.00128.32 C ANISOU 2242 CB GLU A1057 17374 17802 13581 -2953 -1255 -662 C ATOM 2243 CG GLU A1057 -3.049 5.848 -72.530 1.00138.68 C ANISOU 2243 CG GLU A1057 18412 19094 15188 -3169 -1603 -530 C ATOM 2244 CD GLU A1057 -2.788 7.314 -72.230 1.00151.80 C ANISOU 2244 CD GLU A1057 20381 20591 16707 -3401 -1776 -540 C ATOM 2245 OE1 GLU A1057 -3.187 7.785 -71.139 1.00140.87 O ANISOU 2245 OE1 GLU A1057 19570 18999 14954 -3495 -1922 -597 O ATOM 2246 OE2 GLU A1057 -2.149 7.984 -73.073 1.00141.13 O ANISOU 2246 OE2 GLU A1057 18731 19294 15597 -3509 -1757 -491 O ATOM 2247 N MET A1058 -7.711 5.234 -72.595 1.00117.63 N ANISOU 2247 N MET A1058 16436 16483 11775 -2548 -383 -967 N ATOM 2248 CA MET A1058 -8.960 4.484 -72.469 1.00115.28 C ANISOU 2248 CA MET A1058 16195 16229 11376 -2380 -69 -1049 C ATOM 2249 C MET A1058 -9.885 4.701 -73.675 1.00112.41 C ANISOU 2249 C MET A1058 15570 15979 11163 -2200 238 -1114 C ATOM 2250 O MET A1058 -10.525 3.751 -74.132 1.00109.17 O ANISOU 2250 O MET A1058 14954 15685 10843 -2077 411 -1120 O ATOM 2251 CB MET A1058 -9.681 4.888 -71.183 1.00120.05 C ANISOU 2251 CB MET A1058 17344 16637 11633 -2423 35 -1149 C ATOM 2252 CG MET A1058 -10.511 3.785 -70.596 1.00124.39 C ANISOU 2252 CG MET A1058 18006 17201 12056 -2360 248 -1180 C ATOM 2253 SD MET A1058 -9.524 2.353 -70.117 1.00129.73 S ANISOU 2253 SD MET A1058 18641 17902 12748 -2464 -106 -1025 S ATOM 2254 CE MET A1058 -10.720 1.493 -69.083 1.00127.75 C ANISOU 2254 CE MET A1058 18791 17564 12185 -2462 205 -1095 C ATOM 2255 N LYS A1059 -9.962 5.952 -74.170 1.00107.27 N ANISOU 2255 N LYS A1059 14965 15262 10529 -2202 264 -1155 N ATOM 2256 CA LYS A1059 -10.764 6.336 -75.328 1.00104.79 C ANISOU 2256 CA LYS A1059 14462 15002 10352 -2053 460 -1196 C ATOM 2257 C LYS A1059 -10.230 5.647 -76.581 1.00107.23 C ANISOU 2257 C LYS A1059 14393 15480 10871 -2045 433 -1109 C ATOM 2258 O LYS A1059 -11.026 5.180 -77.400 1.00105.57 O ANISOU 2258 O LYS A1059 14016 15347 10749 -1915 585 -1126 O ATOM 2259 CB LYS A1059 -10.761 7.861 -75.500 1.00107.90 C ANISOU 2259 CB LYS A1059 15061 15240 10697 -2085 422 -1238 C ATOM 2260 N ASP A1060 -8.877 5.546 -76.693 1.00104.02 N ANISOU 2260 N ASP A1060 13856 15112 10556 -2192 242 -1015 N ATOM 2261 CA ASP A1060 -8.130 4.916 -77.785 1.00102.70 C ANISOU 2261 CA ASP A1060 13349 15075 10596 -2200 264 -939 C ATOM 2262 C ASP A1060 -8.461 3.427 -77.903 1.00102.41 C ANISOU 2262 C ASP A1060 13151 15144 10617 -2074 359 -934 C ATOM 2263 O ASP A1060 -8.752 2.958 -79.004 1.00101.70 O ANISOU 2263 O ASP A1060 12911 15127 10604 -1994 510 -938 O ATOM 2264 CB ASP A1060 -6.611 5.103 -77.582 1.00107.27 C ANISOU 2264 CB ASP A1060 13786 15650 11321 -2381 50 -842 C ATOM 2265 CG ASP A1060 -6.085 6.521 -77.786 1.00127.71 C ANISOU 2265 CG ASP A1060 16477 18146 13902 -2556 -40 -823 C ATOM 2266 OD1 ASP A1060 -6.722 7.295 -78.543 1.00129.07 O ANISOU 2266 OD1 ASP A1060 16766 18277 13996 -2522 100 -869 O ATOM 2267 OD2 ASP A1060 -5.015 6.846 -77.218 1.00138.57 O ANISOU 2267 OD2 ASP A1060 17813 19472 15365 -2742 -283 -748 O ATOM 2268 N PHE A1061 -8.428 2.696 -76.772 1.00 97.33 N ANISOU 2268 N PHE A1061 12602 14476 9904 -2076 255 -923 N ATOM 2269 CA PHE A1061 -8.745 1.267 -76.676 1.00 95.76 C ANISOU 2269 CA PHE A1061 12320 14336 9727 -1978 314 -912 C ATOM 2270 C PHE A1061 -10.174 1.003 -77.171 1.00 97.65 C ANISOU 2270 C PHE A1061 12584 14612 9908 -1861 551 -986 C ATOM 2271 O PHE A1061 -10.378 0.153 -78.046 1.00 96.30 O ANISOU 2271 O PHE A1061 12248 14512 9828 -1787 644 -975 O ATOM 2272 CB PHE A1061 -8.565 0.765 -75.222 1.00 98.59 C ANISOU 2272 CB PHE A1061 12904 14606 9947 -2041 133 -884 C ATOM 2273 CG PHE A1061 -9.068 -0.634 -74.939 1.00 99.44 C ANISOU 2273 CG PHE A1061 13032 14734 10018 -1965 195 -875 C ATOM 2274 CD1 PHE A1061 -8.288 -1.747 -75.237 1.00102.74 C ANISOU 2274 CD1 PHE A1061 13238 15183 10614 -1914 86 -798 C ATOM 2275 CD2 PHE A1061 -10.315 -0.838 -74.353 1.00101.03 C ANISOU 2275 CD2 PHE A1061 13464 14901 10022 -1948 381 -943 C ATOM 2276 CE1 PHE A1061 -8.752 -3.041 -74.965 1.00103.49 C ANISOU 2276 CE1 PHE A1061 13402 15264 10656 -1856 123 -785 C ATOM 2277 CE2 PHE A1061 -10.780 -2.131 -74.087 1.00103.56 C ANISOU 2277 CE2 PHE A1061 13823 15226 10301 -1919 441 -924 C ATOM 2278 CZ PHE A1061 -9.991 -3.224 -74.382 1.00101.89 C ANISOU 2278 CZ PHE A1061 13452 15033 10230 -1879 289 -842 C ATOM 2279 N ARG A1062 -11.152 1.746 -76.621 1.00 93.66 N ANISOU 2279 N ARG A1062 12280 14036 9272 -1845 645 -1060 N ATOM 2280 CA ARG A1062 -12.558 1.598 -76.985 1.00 92.29 C ANISOU 2280 CA ARG A1062 12066 13879 9119 -1736 848 -1122 C ATOM 2281 C ARG A1062 -12.798 1.925 -78.460 1.00 94.22 C ANISOU 2281 C ARG A1062 12138 14166 9497 -1679 867 -1112 C ATOM 2282 O ARG A1062 -13.570 1.216 -79.105 1.00 93.13 O ANISOU 2282 O ARG A1062 11881 14073 9432 -1617 935 -1112 O ATOM 2283 CB ARG A1062 -13.451 2.472 -76.107 1.00 92.78 C ANISOU 2283 CB ARG A1062 12344 13831 9077 -1707 982 -1211 C ATOM 2284 CG ARG A1062 -13.659 1.926 -74.698 1.00100.58 C ANISOU 2284 CG ARG A1062 13578 14757 9881 -1766 1060 -1237 C ATOM 2285 CD ARG A1062 -14.810 2.632 -73.998 1.00110.83 C ANISOU 2285 CD ARG A1062 15056 15943 11111 -1704 1329 -1350 C ATOM 2286 NE ARG A1062 -14.545 4.058 -73.786 1.00118.94 N ANISOU 2286 NE ARG A1062 16295 16834 12063 -1704 1286 -1406 N ATOM 2287 CZ ARG A1062 -14.042 4.570 -72.667 1.00136.01 C ANISOU 2287 CZ ARG A1062 18861 18845 13970 -1817 1232 -1439 C ATOM 2288 NH1 ARG A1062 -13.759 3.783 -71.636 1.00121.43 N ANISOU 2288 NH1 ARG A1062 17266 16960 11911 -1940 1201 -1415 N ATOM 2289 NH2 ARG A1062 -13.831 5.876 -72.566 1.00126.27 N ANISOU 2289 NH2 ARG A1062 17838 17468 12671 -1824 1181 -1492 N ATOM 2290 N HIS A1063 -12.106 2.956 -78.996 1.00 90.33 N ANISOU 2290 N HIS A1063 11669 13635 9015 -1730 783 -1095 N ATOM 2291 CA HIS A1063 -12.227 3.411 -80.384 1.00 89.22 C ANISOU 2291 CA HIS A1063 11470 13490 8939 -1716 783 -1076 C ATOM 2292 C HIS A1063 -11.928 2.266 -81.383 1.00 90.12 C ANISOU 2292 C HIS A1063 11447 13688 9106 -1716 821 -1033 C ATOM 2293 O HIS A1063 -12.692 2.090 -82.337 1.00 88.31 O ANISOU 2293 O HIS A1063 11218 13445 8893 -1673 835 -1033 O ATOM 2294 CB HIS A1063 -11.322 4.627 -80.656 1.00 91.09 C ANISOU 2294 CB HIS A1063 11799 13661 9151 -1825 702 -1051 C ATOM 2295 CG HIS A1063 -11.418 5.145 -82.062 1.00 95.24 C ANISOU 2295 CG HIS A1063 12353 14146 9688 -1844 705 -1023 C ATOM 2296 ND1 HIS A1063 -12.644 5.474 -82.636 1.00 97.30 N ANISOU 2296 ND1 HIS A1063 12676 14331 9964 -1738 682 -1045 N ATOM 2297 CD2 HIS A1063 -10.441 5.358 -82.972 1.00 97.56 C ANISOU 2297 CD2 HIS A1063 12642 14445 9982 -1969 727 -968 C ATOM 2298 CE1 HIS A1063 -12.370 5.856 -83.870 1.00 97.16 C ANISOU 2298 CE1 HIS A1063 12750 14262 9906 -1812 648 -997 C ATOM 2299 NE2 HIS A1063 -11.058 5.817 -84.115 1.00 97.79 N ANISOU 2299 NE2 HIS A1063 12809 14389 9958 -1959 712 -956 N ATOM 2300 N GLY A1064 -10.872 1.488 -81.122 1.00 85.58 N ANISOU 2300 N GLY A1064 10778 13172 8567 -1758 818 -997 N ATOM 2301 CA GLY A1064 -10.497 0.328 -81.924 1.00 84.64 C ANISOU 2301 CA GLY A1064 10556 13101 8504 -1732 894 -974 C ATOM 2302 C GLY A1064 -11.610 -0.694 -82.085 1.00 88.20 C ANISOU 2302 C GLY A1064 11025 13560 8925 -1658 928 -996 C ATOM 2303 O GLY A1064 -11.800 -1.244 -83.175 1.00 88.05 O ANISOU 2303 O GLY A1064 11031 13528 8895 -1649 979 -994 O ATOM 2304 N PHE A1065 -12.379 -0.935 -81.009 1.00 85.28 N ANISOU 2304 N PHE A1065 10678 13193 8530 -1631 910 -1016 N ATOM 2305 CA PHE A1065 -13.504 -1.867 -81.045 1.00 84.76 C ANISOU 2305 CA PHE A1065 10601 13134 8469 -1598 949 -1028 C ATOM 2306 C PHE A1065 -14.704 -1.237 -81.734 1.00 89.94 C ANISOU 2306 C PHE A1065 11242 13756 9177 -1573 935 -1046 C ATOM 2307 O PHE A1065 -15.467 -1.967 -82.350 1.00 90.16 O ANISOU 2307 O PHE A1065 11238 13776 9244 -1576 911 -1034 O ATOM 2308 CB PHE A1065 -13.871 -2.353 -79.646 1.00 86.60 C ANISOU 2308 CB PHE A1065 10881 13368 8657 -1608 984 -1038 C ATOM 2309 CG PHE A1065 -12.842 -3.308 -79.098 1.00 87.92 C ANISOU 2309 CG PHE A1065 11079 13534 8794 -1625 922 -996 C ATOM 2310 CD1 PHE A1065 -12.863 -4.654 -79.451 1.00 90.02 C ANISOU 2310 CD1 PHE A1065 11331 13795 9078 -1605 928 -971 C ATOM 2311 CD2 PHE A1065 -11.832 -2.859 -78.252 1.00 90.70 C ANISOU 2311 CD2 PHE A1065 11485 13861 9115 -1660 815 -972 C ATOM 2312 CE1 PHE A1065 -11.893 -5.533 -78.970 1.00 91.70 C ANISOU 2312 CE1 PHE A1065 11565 13974 9304 -1587 844 -926 C ATOM 2313 CE2 PHE A1065 -10.860 -3.739 -77.771 1.00 94.12 C ANISOU 2313 CE2 PHE A1065 11914 14268 9579 -1660 691 -914 C ATOM 2314 CZ PHE A1065 -10.904 -5.074 -78.122 1.00 92.07 C ANISOU 2314 CZ PHE A1065 11623 13998 9359 -1607 713 -893 C ATOM 2315 N ASP A1066 -14.852 0.104 -81.678 1.00 87.86 N ANISOU 2315 N ASP A1066 11009 13446 8928 -1553 911 -1067 N ATOM 2316 CA ASP A1066 -15.929 0.814 -82.372 1.00 88.90 C ANISOU 2316 CA ASP A1066 11115 13508 9155 -1503 842 -1071 C ATOM 2317 C ASP A1066 -15.737 0.671 -83.868 1.00 94.21 C ANISOU 2317 C ASP A1066 11868 14143 9786 -1551 730 -1025 C ATOM 2318 O ASP A1066 -16.724 0.483 -84.582 1.00 95.56 O ANISOU 2318 O ASP A1066 12017 14259 10033 -1540 611 -1001 O ATOM 2319 CB ASP A1066 -16.001 2.301 -81.979 1.00 91.76 C ANISOU 2319 CB ASP A1066 11544 13789 9533 -1454 834 -1106 C ATOM 2320 CG ASP A1066 -16.489 2.606 -80.576 1.00104.98 C ANISOU 2320 CG ASP A1066 13216 15443 11229 -1396 977 -1174 C ATOM 2321 OD1 ASP A1066 -17.408 1.896 -80.093 1.00105.26 O ANISOU 2321 OD1 ASP A1066 13130 15507 11356 -1362 1091 -1194 O ATOM 2322 OD2 ASP A1066 -16.007 3.604 -79.987 1.00113.85 O ANISOU 2322 OD2 ASP A1066 14489 16497 12271 -1400 990 -1209 O ATOM 2323 N ILE A1067 -14.463 0.729 -84.335 1.00 90.78 N ANISOU 2323 N ILE A1067 11535 13719 9238 -1620 772 -1008 N ATOM 2324 CA ILE A1067 -14.080 0.542 -85.743 1.00 91.66 C ANISOU 2324 CA ILE A1067 11803 13773 9249 -1691 756 -977 C ATOM 2325 C ILE A1067 -14.387 -0.904 -86.139 1.00 98.32 C ANISOU 2325 C ILE A1067 12659 14628 10072 -1695 770 -976 C ATOM 2326 O ILE A1067 -15.114 -1.135 -87.107 1.00 98.70 O ANISOU 2326 O ILE A1067 12842 14587 10073 -1734 644 -953 O ATOM 2327 CB ILE A1067 -12.587 0.902 -86.017 1.00 94.26 C ANISOU 2327 CB ILE A1067 12185 14117 9513 -1769 891 -968 C ATOM 2328 CG1 ILE A1067 -12.295 2.379 -85.722 1.00 94.79 C ANISOU 2328 CG1 ILE A1067 12292 14143 9582 -1808 843 -960 C ATOM 2329 CG2 ILE A1067 -12.204 0.558 -87.458 1.00 95.53 C ANISOU 2329 CG2 ILE A1067 12557 14202 9540 -1850 972 -953 C ATOM 2330 CD1 ILE A1067 -10.908 2.626 -85.227 1.00100.97 C ANISOU 2330 CD1 ILE A1067 12981 14981 10401 -1882 945 -950 C ATOM 2331 N LEU A1068 -13.856 -1.865 -85.353 1.00 96.25 N ANISOU 2331 N LEU A1068 12286 14446 9838 -1665 883 -993 N ATOM 2332 CA LEU A1068 -14.021 -3.305 -85.535 1.00 96.90 C ANISOU 2332 CA LEU A1068 12398 14520 9898 -1663 909 -995 C ATOM 2333 C LEU A1068 -15.509 -3.688 -85.609 1.00101.83 C ANISOU 2333 C LEU A1068 13004 15113 10574 -1685 763 -980 C ATOM 2334 O LEU A1068 -15.856 -4.542 -86.425 1.00102.63 O ANISOU 2334 O LEU A1068 13242 15141 10610 -1738 699 -969 O ATOM 2335 CB LEU A1068 -13.323 -4.054 -84.385 1.00 96.62 C ANISOU 2335 CB LEU A1068 12243 14553 9916 -1613 993 -1002 C ATOM 2336 CG LEU A1068 -13.087 -5.559 -84.558 1.00101.85 C ANISOU 2336 CG LEU A1068 12965 15176 10556 -1590 1042 -1005 C ATOM 2337 CD1 LEU A1068 -11.877 -5.829 -85.444 1.00103.10 C ANISOU 2337 CD1 LEU A1068 13192 15285 10697 -1559 1192 -1023 C ATOM 2338 CD2 LEU A1068 -12.868 -6.221 -83.207 1.00103.54 C ANISOU 2338 CD2 LEU A1068 13089 15427 10823 -1553 1030 -990 C ATOM 2339 N VAL A1069 -16.381 -3.031 -84.798 1.00 98.23 N ANISOU 2339 N VAL A1069 12384 14692 10249 -1651 719 -982 N ATOM 2340 CA VAL A1069 -17.836 -3.265 -84.785 1.00 98.98 C ANISOU 2340 CA VAL A1069 12353 14761 10493 -1668 605 -961 C ATOM 2341 C VAL A1069 -18.441 -2.734 -86.100 1.00104.43 C ANISOU 2341 C VAL A1069 13140 15335 11204 -1703 368 -919 C ATOM 2342 O VAL A1069 -19.259 -3.431 -86.712 1.00105.35 O ANISOU 2342 O VAL A1069 13273 15387 11369 -1778 195 -878 O ATOM 2343 CB VAL A1069 -18.521 -2.659 -83.530 1.00102.88 C ANISOU 2343 CB VAL A1069 12637 15303 11149 -1602 710 -990 C ATOM 2344 CG1 VAL A1069 -20.033 -2.528 -83.705 1.00104.32 C ANISOU 2344 CG1 VAL A1069 12607 15442 11587 -1595 605 -966 C ATOM 2345 CG2 VAL A1069 -18.200 -3.489 -82.291 1.00102.28 C ANISOU 2345 CG2 VAL A1069 12552 15297 11011 -1622 891 -1012 C ATOM 2346 N GLY A1070 -17.997 -1.544 -86.528 1.00100.46 N ANISOU 2346 N GLY A1070 12742 14783 10645 -1673 328 -918 N ATOM 2347 CA GLY A1070 -18.435 -0.907 -87.766 1.00101.45 C ANISOU 2347 CA GLY A1070 13045 14760 10740 -1717 74 -865 C ATOM 2348 C GLY A1070 -18.192 -1.780 -88.981 1.00106.26 C ANISOU 2348 C GLY A1070 13968 15273 11132 -1846 -14 -839 C ATOM 2349 O GLY A1070 -19.092 -1.968 -89.803 1.00108.06 O ANISOU 2349 O GLY A1070 14302 15372 11383 -1920 -307 -781 O ATOM 2350 N GLN A1071 -16.988 -2.372 -89.055 1.00101.27 N ANISOU 2350 N GLN A1071 13483 14684 10310 -1871 236 -883 N ATOM 2351 CA GLN A1071 -16.545 -3.270 -90.120 1.00101.67 C ANISOU 2351 CA GLN A1071 13877 14628 10126 -1970 274 -890 C ATOM 2352 C GLN A1071 -17.247 -4.643 -90.036 1.00108.29 C ANISOU 2352 C GLN A1071 14699 15448 11000 -2010 183 -887 C ATOM 2353 O GLN A1071 -17.325 -5.339 -91.052 1.00109.23 O ANISOU 2353 O GLN A1071 15164 15416 10924 -2117 98 -882 O ATOM 2354 CB GLN A1071 -15.029 -3.443 -90.065 1.00101.71 C ANISOU 2354 CB GLN A1071 13941 14686 10018 -1941 624 -947 C ATOM 2355 CG GLN A1071 -14.273 -2.141 -90.283 1.00111.28 C ANISOU 2355 CG GLN A1071 15202 15896 11182 -1960 720 -940 C ATOM 2356 CD GLN A1071 -12.777 -2.282 -90.177 1.00131.84 C ANISOU 2356 CD GLN A1071 17764 18562 13768 -1943 1065 -983 C ATOM 2357 OE1 GLN A1071 -12.236 -3.276 -89.672 1.00126.80 O ANISOU 2357 OE1 GLN A1071 16979 17988 13210 -1867 1225 -1019 O ATOM 2358 NE2 GLN A1071 -12.074 -1.258 -90.629 1.00127.04 N ANISOU 2358 NE2 GLN A1071 17260 17920 13089 -2018 1174 -970 N ATOM 2359 N ILE A1072 -17.750 -5.033 -88.836 1.00105.39 N ANISOU 2359 N ILE A1072 13986 15208 10849 -1948 212 -889 N ATOM 2360 CA ILE A1072 -18.512 -6.273 -88.641 1.00106.51 C ANISOU 2360 CA ILE A1072 14086 15331 11052 -2016 124 -873 C ATOM 2361 C ILE A1072 -19.929 -6.000 -89.172 1.00115.37 C ANISOU 2361 C ILE A1072 15142 16362 12332 -2110 -235 -797 C ATOM 2362 O ILE A1072 -20.471 -6.819 -89.918 1.00116.52 O ANISOU 2362 O ILE A1072 15484 16376 12410 -2249 -453 -760 O ATOM 2363 CB ILE A1072 -18.477 -6.775 -87.157 1.00107.98 C ANISOU 2363 CB ILE A1072 13984 15664 11381 -1949 316 -895 C ATOM 2364 CG1 ILE A1072 -17.168 -7.544 -86.879 1.00106.93 C ANISOU 2364 CG1 ILE A1072 13980 15548 11101 -1888 548 -943 C ATOM 2365 CG2 ILE A1072 -19.689 -7.666 -86.814 1.00109.87 C ANISOU 2365 CG2 ILE A1072 14085 15891 11771 -2053 194 -853 C ATOM 2366 CD1 ILE A1072 -16.766 -7.674 -85.404 1.00110.36 C ANISOU 2366 CD1 ILE A1072 14207 16102 11622 -1809 707 -956 C ATOM 2367 N ASP A1073 -20.490 -4.819 -88.828 1.00114.74 N ANISOU 2367 N ASP A1073 14800 16321 12473 -2031 -320 -773 N ATOM 2368 CA ASP A1073 -21.815 -4.362 -89.256 1.00118.05 C ANISOU 2368 CA ASP A1073 15060 16645 13148 -2071 -680 -692 C ATOM 2369 C ASP A1073 -21.871 -4.110 -90.769 1.00126.66 C ANISOU 2369 C ASP A1073 16567 17521 14038 -2186 -1032 -630 C ATOM 2370 O ASP A1073 -22.903 -4.393 -91.380 1.00128.51 O ANISOU 2370 O ASP A1073 16800 17623 14406 -2303 -1423 -545 O ATOM 2371 CB ASP A1073 -22.225 -3.090 -88.497 1.00119.63 C ANISOU 2371 CB ASP A1073 14913 16909 13631 -1908 -627 -700 C ATOM 2372 CG ASP A1073 -22.624 -3.338 -87.057 1.00126.82 C ANISOU 2372 CG ASP A1073 15433 17974 14779 -1834 -341 -746 C ATOM 2373 OD1 ASP A1073 -22.938 -4.500 -86.720 1.00127.37 O ANISOU 2373 OD1 ASP A1073 15429 18088 14877 -1936 -279 -738 O ATOM 2374 OD2 ASP A1073 -22.670 -2.363 -86.279 1.00131.22 O ANISOU 2374 OD2 ASP A1073 15801 18580 15477 -1689 -177 -789 O ATOM 2375 N ASP A1074 -20.771 -3.598 -91.369 1.00124.83 N ANISOU 2375 N ASP A1074 16706 17237 13486 -2180 -902 -665 N ATOM 2376 CA ASP A1074 -20.681 -3.340 -92.810 1.00128.10 C ANISOU 2376 CA ASP A1074 17638 17419 13614 -2318 -1167 -615 C ATOM 2377 C ASP A1074 -20.731 -4.663 -93.584 1.00135.43 C ANISOU 2377 C ASP A1074 18947 18213 14299 -2493 -1260 -615 C ATOM 2378 O ASP A1074 -21.357 -4.726 -94.644 1.00137.86 O ANISOU 2378 O ASP A1074 19603 18292 14485 -2655 -1672 -537 O ATOM 2379 CB ASP A1074 -19.409 -2.541 -93.160 1.00129.43 C ANISOU 2379 CB ASP A1074 18102 17576 13500 -2294 -892 -662 C ATOM 2380 CG ASP A1074 -19.419 -1.069 -92.757 1.00141.26 C ANISOU 2380 CG ASP A1074 19404 19107 15159 -2178 -918 -642 C ATOM 2381 OD1 ASP A1074 -20.410 -0.625 -92.121 1.00142.05 O ANISOU 2381 OD1 ASP A1074 19111 19246 15616 -2070 -1109 -607 O ATOM 2382 OD2 ASP A1074 -18.429 -0.363 -93.062 1.00147.41 O ANISOU 2382 OD2 ASP A1074 20422 19864 15724 -2196 -722 -665 O ATOM 2383 N ALA A1075 -20.107 -5.721 -93.031 1.00131.86 N ANISOU 2383 N ALA A1075 18452 17870 13778 -2463 -917 -696 N ATOM 2384 CA ALA A1075 -20.123 -7.066 -93.601 1.00133.83 C ANISOU 2384 CA ALA A1075 19056 17983 13811 -2602 -955 -715 C ATOM 2385 C ALA A1075 -21.465 -7.743 -93.319 1.00142.23 C ANISOU 2385 C ALA A1075 19865 19030 15146 -2710 -1308 -636 C ATOM 2386 O ALA A1075 -21.902 -8.590 -94.102 1.00144.32 O ANISOU 2386 O ALA A1075 20486 19098 15252 -2899 -1574 -604 O ATOM 2387 CB ALA A1075 -18.983 -7.892 -93.030 1.00132.55 C ANISOU 2387 CB ALA A1075 18896 17925 13544 -2495 -481 -822 C ATOM 2388 N LEU A1076 -22.123 -7.358 -92.200 1.00140.02 N ANISOU 2388 N LEU A1076 18983 18940 15279 -2608 -1294 -607 N ATOM 2389 CA LEU A1076 -23.425 -7.886 -91.780 1.00142.48 C ANISOU 2389 CA LEU A1076 18927 19267 15944 -2707 -1549 -530 C ATOM 2390 C LEU A1076 -24.542 -7.359 -92.695 1.00151.88 C ANISOU 2390 C LEU A1076 20126 20273 17310 -2832 -2122 -405 C ATOM 2391 O LEU A1076 -25.456 -8.120 -93.007 1.00153.91 O ANISOU 2391 O LEU A1076 20358 20420 17702 -3025 -2467 -324 O ATOM 2392 CB LEU A1076 -23.711 -7.523 -90.310 1.00141.03 C ANISOU 2392 CB LEU A1076 18139 19320 16125 -2552 -1265 -553 C ATOM 2393 CG LEU A1076 -24.802 -8.317 -89.577 1.00147.32 C ANISOU 2393 CG LEU A1076 18536 20176 17263 -2659 -1306 -504 C ATOM 2394 CD1 LEU A1076 -24.339 -9.734 -89.248 1.00146.57 C ANISOU 2394 CD1 LEU A1076 18658 20087 16945 -2760 -1107 -545 C ATOM 2395 CD2 LEU A1076 -25.190 -7.624 -88.283 1.00149.26 C ANISOU 2395 CD2 LEU A1076 18243 20608 17861 -2503 -1021 -529 C ATOM 2396 N LYS A1077 -24.456 -6.074 -93.130 1.00150.41 N ANISOU 2396 N LYS A1077 19991 20028 17128 -2735 -2260 -377 N ATOM 2397 CA LYS A1077 -25.418 -5.417 -94.035 1.00154.47 C ANISOU 2397 CA LYS A1077 20555 20328 17807 -2823 -2860 -245 C ATOM 2398 C LYS A1077 -25.527 -6.171 -95.364 1.00162.03 C ANISOU 2398 C LYS A1077 22165 21001 18399 -3099 -3274 -184 C ATOM 2399 O LYS A1077 -26.637 -6.427 -95.836 1.00165.19 O ANISOU 2399 O LYS A1077 22494 21240 19031 -3268 -3830 -57 O ATOM 2400 CB LYS A1077 -25.014 -3.951 -94.307 1.00156.94 C ANISOU 2400 CB LYS A1077 20971 20595 18063 -2673 -2877 -240 C ATOM 2401 CG LYS A1077 -25.232 -2.996 -93.140 1.00172.63 C ANISOU 2401 CG LYS A1077 22343 22776 20472 -2415 -2633 -274 C ATOM 2402 CD LYS A1077 -24.535 -1.658 -93.376 1.00181.67 C ANISOU 2402 CD LYS A1077 23709 23870 21448 -2286 -2562 -294 C ATOM 2403 CE LYS A1077 -24.546 -0.785 -92.143 1.00188.85 C ANISOU 2403 CE LYS A1077 24116 24958 22681 -2035 -2238 -360 C ATOM 2404 NZ LYS A1077 -23.774 0.470 -92.344 1.00193.82 N ANISOU 2404 NZ LYS A1077 25005 25527 23112 -1939 -2156 -383 N ATOM 2405 N LEU A1078 -24.366 -6.540 -95.943 1.00158.11 N ANISOU 2405 N LEU A1078 22302 20427 17345 -3150 -2988 -278 N ATOM 2406 CA LEU A1078 -24.230 -7.265 -97.209 1.00161.01 C ANISOU 2406 CA LEU A1078 23444 20494 17237 -3402 -3240 -264 C ATOM 2407 C LEU A1078 -24.768 -8.702 -97.091 1.00167.38 C ANISOU 2407 C LEU A1078 24252 21256 18090 -3576 -3363 -256 C ATOM 2408 O LEU A1078 -25.512 -9.152 -97.968 1.00170.53 O ANISOU 2408 O LEU A1078 25010 21387 18397 -3834 -3912 -158 O ATOM 2409 CB LEU A1078 -22.748 -7.291 -97.649 1.00159.37 C ANISOU 2409 CB LEU A1078 23812 20250 16490 -3358 -2718 -400 C ATOM 2410 CG LEU A1078 -22.021 -5.942 -97.778 1.00162.84 C ANISOU 2410 CG LEU A1078 24315 20730 16829 -3228 -2514 -417 C ATOM 2411 CD1 LEU A1078 -20.524 -6.126 -97.732 1.00160.78 C ANISOU 2411 CD1 LEU A1078 24302 20549 16239 -3138 -1847 -565 C ATOM 2412 CD2 LEU A1078 -22.428 -5.195 -99.041 1.00169.42 C ANISOU 2412 CD2 LEU A1078 25715 21243 17415 -3408 -3028 -304 C ATOM 2413 N ALA A1079 -24.396 -9.403 -95.996 1.00162.09 N ANISOU 2413 N ALA A1079 23210 20824 17552 -3453 -2889 -348 N ATOM 2414 CA ALA A1079 -24.782 -10.786 -95.704 1.00163.06 C ANISOU 2414 CA ALA A1079 23319 20922 17713 -3601 -2914 -350 C ATOM 2415 C ALA A1079 -26.283 -10.921 -95.392 1.00170.34 C ANISOU 2415 C ALA A1079 23707 21856 19157 -3753 -3393 -204 C ATOM 2416 O ALA A1079 -26.897 -11.894 -95.837 1.00172.80 O ANISOU 2416 O ALA A1079 24242 21983 19429 -4018 -3742 -142 O ATOM 2417 CB ALA A1079 -23.963 -11.316 -94.537 1.00160.13 C ANISOU 2417 CB ALA A1079 22678 20794 17369 -3409 -2301 -470 C ATOM 2418 N ASN A1080 -26.866 -9.956 -94.634 1.00166.67 N ANISOU 2418 N ASN A1080 22541 21588 19198 -3592 -3392 -152 N ATOM 2419 CA ASN A1080 -28.281 -9.940 -94.227 1.00169.23 C ANISOU 2419 CA ASN A1080 22215 21950 20135 -3687 -3747 -20 C ATOM 2420 C ASN A1080 -29.213 -9.848 -95.439 1.00177.67 C ANISOU 2420 C ASN A1080 23507 22715 21282 -3934 -4540 141 C ATOM 2421 O ASN A1080 -30.311 -10.411 -95.402 1.00180.83 O ANISOU 2421 O ASN A1080 23572 23058 22076 -4145 -4924 260 O ATOM 2422 CB ASN A1080 -28.559 -8.769 -93.273 1.00168.82 C ANISOU 2422 CB ASN A1080 21462 22124 20557 -3412 -3511 -26 C ATOM 2423 CG ASN A1080 -29.790 -8.923 -92.410 1.00192.80 C ANISOU 2423 CG ASN A1080 23714 25284 24257 -3446 -3546 50 C ATOM 2424 OD1 ASN A1080 -29.705 -9.260 -91.224 1.00184.20 O ANISOU 2424 OD1 ASN A1080 22270 24412 23306 -3369 -3037 -23 O ATOM 2425 ND2 ASN A1080 -30.958 -8.625 -92.964 1.00189.32 N ANISOU 2425 ND2 ASN A1080 22976 24693 24264 -3560 -4137 204 N ATOM 2426 N GLU A1081 -28.780 -9.147 -96.505 1.00174.44 N ANISOU 2426 N GLU A1081 23678 22097 20504 -3933 -4802 156 N ATOM 2427 CA GLU A1081 -29.581 -8.987 -97.714 1.00179.12 C ANISOU 2427 CA GLU A1081 24609 22353 21096 -4178 -5616 320 C ATOM 2428 C GLU A1081 -29.395 -10.173 -98.678 1.00184.72 C ANISOU 2428 C GLU A1081 26160 22771 21256 -4511 -5868 317 C ATOM 2429 O GLU A1081 -30.397 -10.693 -99.178 1.00188.69 O ANISOU 2429 O GLU A1081 26686 23063 21945 -4803 -6520 463 O ATOM 2430 CB GLU A1081 -29.274 -7.657 -98.418 1.00181.02 C ANISOU 2430 CB GLU A1081 25158 22455 21167 -4055 -5821 355 C ATOM 2431 CG GLU A1081 -29.979 -6.465 -97.785 1.00191.31 C ANISOU 2431 CG GLU A1081 25657 23894 23138 -3804 -5931 430 C ATOM 2432 CD GLU A1081 -31.497 -6.520 -97.784 1.00214.85 C ANISOU 2432 CD GLU A1081 28015 26785 26832 -3917 -6585 617 C ATOM 2433 OE1 GLU A1081 -32.099 -6.516 -98.882 1.00210.58 O ANISOU 2433 OE1 GLU A1081 27848 25910 26252 -4154 -7374 778 O ATOM 2434 OE2 GLU A1081 -32.086 -6.564 -96.680 1.00207.03 O ANISOU 2434 OE2 GLU A1081 26166 26044 26451 -3780 -6308 607 O ATOM 2435 N GLY A1082 -28.149 -10.596 -98.916 1.00178.16 N ANISOU 2435 N GLY A1082 25988 21914 19791 -4469 -5359 153 N ATOM 2436 CA GLY A1082 -27.872 -11.725 -99.801 1.00179.85 C ANISOU 2436 CA GLY A1082 27065 21827 19444 -4746 -5488 114 C ATOM 2437 C GLY A1082 -26.446 -11.906-100.287 1.00180.80 C ANISOU 2437 C GLY A1082 27966 21858 18870 -4659 -4923 -68 C ATOM 2438 O GLY A1082 -26.068 -13.024-100.649 1.00181.14 O ANISOU 2438 O GLY A1082 28589 21723 18514 -4799 -4786 -155 O ATOM 2439 N LYS A1083 -25.649 -10.816-100.319 1.00174.48 N ANISOU 2439 N LYS A1083 27192 21160 17942 -4434 -4580 -127 N ATOM 2440 CA LYS A1083 -24.254 -10.830-100.785 1.00172.62 C ANISOU 2440 CA LYS A1083 27610 20856 17123 -4344 -3988 -293 C ATOM 2441 C LYS A1083 -23.371 -11.669 -99.841 1.00171.83 C ANISOU 2441 C LYS A1083 27246 20993 17047 -4135 -3271 -457 C ATOM 2442 O LYS A1083 -23.242 -11.340 -98.660 1.00168.01 O ANISOU 2442 O LYS A1083 26004 20853 16978 -3897 -2961 -476 O ATOM 2443 CB LYS A1083 -23.707 -9.398-100.918 1.00173.89 C ANISOU 2443 CB LYS A1083 27734 21095 17243 -4178 -3821 -291 C ATOM 2444 CG LYS A1083 -24.400 -8.575-101.999 1.00192.49 C ANISOU 2444 CG LYS A1083 30536 23140 19461 -4385 -4521 -133 C ATOM 2445 CD LYS A1083 -23.905 -7.141-102.020 1.00201.26 C ANISOU 2445 CD LYS A1083 31570 24328 20571 -4217 -4360 -122 C ATOM 2446 CE LYS A1083 -24.604 -6.316-103.070 1.00215.23 C ANISOU 2446 CE LYS A1083 33812 25757 22209 -4416 -5102 51 C ATOM 2447 NZ LYS A1083 -24.109 -4.915-103.083 1.00220.24 N ANISOU 2447 NZ LYS A1083 34414 26441 22826 -4263 -4943 65 N ATOM 2448 N VAL A1084 -22.795 -12.771-100.369 1.00168.65 N ANISOU 2448 N VAL A1084 27513 20371 16197 -4229 -3041 -571 N ATOM 2449 CA VAL A1084 -21.964 -13.725 -99.617 1.00165.20 C ANISOU 2449 CA VAL A1084 26939 20071 15759 -4042 -2437 -719 C ATOM 2450 C VAL A1084 -20.464 -13.420 -99.838 1.00166.24 C ANISOU 2450 C VAL A1084 27359 20222 15582 -3822 -1741 -881 C ATOM 2451 O VAL A1084 -19.712 -13.363 -98.865 1.00162.40 O ANISOU 2451 O VAL A1084 26348 20017 15340 -3550 -1253 -954 O ATOM 2452 CB VAL A1084 -22.302 -15.203 -99.990 1.00171.73 C ANISOU 2452 CB VAL A1084 28281 20617 16354 -4259 -2613 -746 C ATOM 2453 CG1 VAL A1084 -21.494 -16.198 -99.156 1.00169.03 C ANISOU 2453 CG1 VAL A1084 27777 20391 16057 -4043 -2041 -883 C ATOM 2454 CG2 VAL A1084 -23.797 -15.485 -99.848 1.00173.58 C ANISOU 2454 CG2 VAL A1084 28216 20814 16924 -4529 -3329 -568 C ATOM 2455 N LYS A1085 -20.038 -13.249-101.105 1.00164.83 N ANISOU 2455 N LYS A1085 28023 19729 14877 -3960 -1699 -930 N ATOM 2456 CA LYS A1085 -18.645 -12.977-101.484 1.00163.85 C ANISOU 2456 CA LYS A1085 28230 19576 14450 -3801 -1008 -1083 C ATOM 2457 C LYS A1085 -18.164 -11.625-100.945 1.00162.90 C ANISOU 2457 C LYS A1085 27530 19763 14602 -3613 -785 -1051 C ATOM 2458 O LYS A1085 -17.030 -11.526-100.470 1.00160.06 O ANISOU 2458 O LYS A1085 26904 19580 14332 -3378 -169 -1160 O ATOM 2459 CB LYS A1085 -18.485 -13.006-103.019 1.00171.20 C ANISOU 2459 CB LYS A1085 30265 20061 14721 -4056 -1054 -1124 C ATOM 2460 CG LYS A1085 -18.660 -14.381-103.668 1.00189.34 C ANISOU 2460 CG LYS A1085 33324 21988 16629 -4232 -1125 -1205 C ATOM 2461 CD LYS A1085 -17.407 -15.251-103.576 1.00200.04 C ANISOU 2461 CD LYS A1085 34868 23294 17843 -3996 -310 -1424 C ATOM 2462 CE LYS A1085 -17.586 -16.570-104.284 1.00212.43 C ANISOU 2462 CE LYS A1085 36826 24641 19248 -3951 -376 -1516 C ATOM 2463 NZ LYS A1085 -16.347 -17.389-104.246 1.00216.94 N ANISOU 2463 NZ LYS A1085 37016 25381 20030 -3443 370 -1718 N ATOM 2464 N GLU A1086 -19.038 -10.598-101.014 1.00158.48 N ANISOU 2464 N GLU A1086 26771 19244 14201 -3717 -1317 -896 N ATOM 2465 CA GLU A1086 -18.784 -9.215-100.593 1.00155.35 C ANISOU 2465 CA GLU A1086 25910 19078 14039 -3580 -1231 -846 C ATOM 2466 C GLU A1086 -18.632 -9.108 -99.059 1.00151.66 C ANISOU 2466 C GLU A1086 24489 19019 14117 -3305 -991 -860 C ATOM 2467 O GLU A1086 -17.966 -8.188 -98.578 1.00148.88 O ANISOU 2467 O GLU A1086 23790 18868 13909 -3145 -691 -879 O ATOM 2468 CB GLU A1086 -19.926 -8.306-101.089 1.00158.95 C ANISOU 2468 CB GLU A1086 26440 19403 14552 -3755 -1952 -670 C ATOM 2469 CG GLU A1086 -19.509 -6.871-101.376 1.00171.41 C ANISOU 2469 CG GLU A1086 28079 20993 16056 -3723 -1885 -629 C ATOM 2470 CD GLU A1086 -20.428 -6.079-102.292 1.00198.03 C ANISOU 2470 CD GLU A1086 31867 24081 19293 -3939 -2594 -465 C ATOM 2471 OE1 GLU A1086 -20.810 -6.607-103.363 1.00195.19 O ANISOU 2471 OE1 GLU A1086 32279 23363 18521 -4208 -2952 -428 O ATOM 2472 OE2 GLU A1086 -20.704 -4.900-101.974 1.00192.39 O ANISOU 2472 OE2 GLU A1086 30774 23470 18857 -3842 -2792 -374 O ATOM 2473 N ALA A1087 -19.236 -10.054 -98.310 1.00144.70 N ANISOU 2473 N ALA A1087 23248 18231 13499 -3281 -1128 -848 N ATOM 2474 CA ALA A1087 -19.189 -10.124 -96.850 1.00139.52 C ANISOU 2474 CA ALA A1087 21805 17910 13295 -3067 -928 -858 C ATOM 2475 C ALA A1087 -17.941 -10.883 -96.359 1.00139.10 C ANISOU 2475 C ALA A1087 21722 17940 13188 -2879 -334 -996 C ATOM 2476 O ALA A1087 -17.328 -10.457 -95.380 1.00136.04 O ANISOU 2476 O ALA A1087 20827 17807 13054 -2677 -39 -1022 O ATOM 2477 CB ALA A1087 -20.449 -10.794 -96.323 1.00140.53 C ANISOU 2477 CB ALA A1087 21613 18066 13715 -3171 -1341 -768 C ATOM 2478 N GLN A1088 -17.573 -11.996 -97.034 1.00135.61 N ANISOU 2478 N GLN A1088 21837 17257 12431 -2942 -184 -1082 N ATOM 2479 CA GLN A1088 -16.420 -12.846 -96.704 1.00133.89 C ANISOU 2479 CA GLN A1088 21640 17047 12186 -2745 350 -1215 C ATOM 2480 C GLN A1088 -15.090 -12.120 -96.882 1.00135.16 C ANISOU 2480 C GLN A1088 21780 17276 12299 -2585 869 -1298 C ATOM 2481 O GLN A1088 -14.162 -12.375 -96.114 1.00132.55 O ANISOU 2481 O GLN A1088 21078 17095 12190 -2358 1251 -1361 O ATOM 2482 CB GLN A1088 -16.407 -14.115 -97.569 1.00138.65 C ANISOU 2482 CB GLN A1088 22947 17305 12428 -2857 380 -1297 C ATOM 2483 CG GLN A1088 -17.404 -15.175 -97.138 1.00155.40 C ANISOU 2483 CG GLN A1088 25020 19371 14654 -2976 1 -1240 C ATOM 2484 CD GLN A1088 -17.365 -16.361 -98.061 1.00174.64 C ANISOU 2484 CD GLN A1088 28241 21424 16691 -3105 14 -1327 C ATOM 2485 OE1 GLN A1088 -18.046 -16.395 -99.088 1.00172.06 O ANISOU 2485 OE1 GLN A1088 28501 20828 16045 -3380 -357 -1288 O ATOM 2486 NE2 GLN A1088 -16.568 -17.359 -97.713 1.00166.34 N ANISOU 2486 NE2 GLN A1088 27247 20309 15647 -2910 414 -1443 N ATOM 2487 N ALA A1089 -14.988 -11.248 -97.908 1.00133.06 N ANISOU 2487 N ALA A1089 21929 16877 11751 -2722 867 -1288 N ATOM 2488 CA ALA A1089 -13.775 -10.480 -98.207 1.00133.27 C ANISOU 2488 CA ALA A1089 21980 16943 11713 -2635 1369 -1354 C ATOM 2489 C ALA A1089 -13.517 -9.413 -97.133 1.00133.64 C ANISOU 2489 C ALA A1089 21291 17328 12157 -2495 1388 -1290 C ATOM 2490 O ALA A1089 -12.358 -9.121 -96.825 1.00132.80 O ANISOU 2490 O ALA A1089 20925 17341 12190 -2350 1839 -1348 O ATOM 2491 CB ALA A1089 -13.890 -9.830 -99.574 1.00137.29 C ANISOU 2491 CB ALA A1089 23205 17189 11770 -2874 1303 -1340 C ATOM 2492 N ALA A1090 -14.603 -8.861 -96.552 1.00127.61 N ANISOU 2492 N ALA A1090 20190 16698 11598 -2542 900 -1173 N ATOM 2493 CA ALA A1090 -14.575 -7.848 -95.499 1.00124.30 C ANISOU 2493 CA ALA A1090 19145 16559 11526 -2425 859 -1115 C ATOM 2494 C ALA A1090 -14.027 -8.418 -94.177 1.00125.93 C ANISOU 2494 C ALA A1090 18808 16984 12054 -2216 1085 -1154 C ATOM 2495 O ALA A1090 -13.451 -7.668 -93.384 1.00123.14 O ANISOU 2495 O ALA A1090 18038 16827 11921 -2105 1225 -1145 O ATOM 2496 CB ALA A1090 -15.973 -7.292 -95.287 1.00124.41 C ANISOU 2496 CB ALA A1090 18987 16601 11682 -2513 315 -998 C ATOM 2497 N ALA A1091 -14.204 -9.742 -93.953 1.00123.45 N ANISOU 2497 N ALA A1091 18553 16607 11746 -2181 1084 -1190 N ATOM 2498 CA ALA A1091 -13.741 -10.473 -92.767 1.00121.81 C ANISOU 2498 CA ALA A1091 17944 16540 11796 -2001 1239 -1215 C ATOM 2499 C ALA A1091 -12.213 -10.581 -92.746 1.00126.31 C ANISOU 2499 C ALA A1091 18439 17122 12430 -1828 1709 -1299 C ATOM 2500 O ALA A1091 -11.618 -10.615 -91.672 1.00124.78 O ANISOU 2500 O ALA A1091 17810 17089 12512 -1673 1802 -1290 O ATOM 2501 CB ALA A1091 -14.365 -11.859 -92.721 1.00123.39 C ANISOU 2501 CB ALA A1091 18337 16607 11938 -2044 1091 -1224 C ATOM 2502 N GLU A1092 -11.582 -10.611 -93.928 1.00125.28 N ANISOU 2502 N GLU A1092 18736 16806 12059 -1865 2003 -1374 N ATOM 2503 CA GLU A1092 -10.126 -10.658 -94.065 1.00126.46 C ANISOU 2503 CA GLU A1092 18788 16945 12315 -1710 2513 -1457 C ATOM 2504 C GLU A1092 -9.522 -9.314 -93.606 1.00127.84 C ANISOU 2504 C GLU A1092 18540 17333 12698 -1702 2590 -1405 C ATOM 2505 O GLU A1092 -8.437 -9.296 -93.019 1.00127.31 O ANISOU 2505 O GLU A1092 18073 17371 12927 -1546 2849 -1422 O ATOM 2506 CB GLU A1092 -9.743 -10.981 -95.528 1.00131.66 C ANISOU 2506 CB GLU A1092 20090 17318 12615 -1791 2857 -1560 C ATOM 2507 CG GLU A1092 -8.263 -11.269 -95.766 1.00145.33 C ANISOU 2507 CG GLU A1092 21732 18992 14495 -1611 3477 -1669 C ATOM 2508 CD GLU A1092 -7.660 -12.485 -95.081 1.00167.56 C ANISOU 2508 CD GLU A1092 24276 21781 17608 -1339 3640 -1728 C ATOM 2509 OE1 GLU A1092 -8.385 -13.485 -94.871 1.00162.93 O ANISOU 2509 OE1 GLU A1092 23884 21089 16932 -1325 3377 -1731 O ATOM 2510 OE2 GLU A1092 -6.441 -12.451 -94.794 1.00161.52 O ANISOU 2510 OE2 GLU A1092 23114 21075 17183 -1148 4024 -1766 O ATOM 2511 N GLN A1093 -10.254 -8.203 -93.849 1.00122.74 N ANISOU 2511 N GLN A1093 17984 16732 11921 -1872 2321 -1331 N ATOM 2512 CA GLN A1093 -9.855 -6.838 -93.489 1.00121.26 C ANISOU 2512 CA GLN A1093 17495 16705 11873 -1903 2333 -1276 C ATOM 2513 C GLN A1093 -9.969 -6.611 -91.972 1.00121.29 C ANISOU 2513 C GLN A1093 16935 16940 12210 -1788 2118 -1219 C ATOM 2514 O GLN A1093 -9.289 -5.735 -91.436 1.00120.03 O ANISOU 2514 O GLN A1093 16462 16911 12232 -1770 2193 -1191 O ATOM 2515 CB GLN A1093 -10.695 -5.793 -94.254 1.00122.88 C ANISOU 2515 CB GLN A1093 18041 16827 11821 -2103 2068 -1214 C ATOM 2516 CG GLN A1093 -10.698 -5.950 -95.787 1.00140.14 C ANISOU 2516 CG GLN A1093 20920 18737 13588 -2271 2209 -1254 C ATOM 2517 CD GLN A1093 -9.329 -5.887 -96.428 1.00157.32 C ANISOU 2517 CD GLN A1093 23236 20842 15698 -2275 2802 -1335 C ATOM 2518 OE1 GLN A1093 -8.655 -4.853 -96.422 1.00152.43 O ANISOU 2518 OE1 GLN A1093 22462 20300 15153 -2332 2985 -1307 O ATOM 2519 NE2 GLN A1093 -8.909 -6.989 -97.032 1.00150.46 N ANISOU 2519 NE2 GLN A1093 22682 19799 14688 -2228 3136 -1441 N ATOM 2520 N LEU A1094 -10.820 -7.410 -91.291 1.00116.06 N ANISOU 2520 N LEU A1094 16189 16304 11604 -1738 1859 -1201 N ATOM 2521 CA LEU A1094 -11.026 -7.385 -89.840 1.00113.22 C ANISOU 2521 CA LEU A1094 15407 16119 11492 -1650 1682 -1156 C ATOM 2522 C LEU A1094 -9.786 -7.885 -89.096 1.00115.42 C ANISOU 2522 C LEU A1094 15391 16456 12008 -1491 1889 -1175 C ATOM 2523 O LEU A1094 -9.554 -7.454 -87.965 1.00114.25 O ANISOU 2523 O LEU A1094 14918 16443 12048 -1448 1781 -1131 O ATOM 2524 CB LEU A1094 -12.248 -8.236 -89.439 1.00112.70 C ANISOU 2524 CB LEU A1094 15390 16030 11400 -1676 1416 -1132 C ATOM 2525 CG LEU A1094 -13.629 -7.594 -89.600 1.00117.31 C ANISOU 2525 CG LEU A1094 16022 16620 11932 -1804 1104 -1077 C ATOM 2526 CD1 LEU A1094 -14.719 -8.641 -89.610 1.00117.90 C ANISOU 2526 CD1 LEU A1094 16205 16616 11974 -1875 897 -1058 C ATOM 2527 CD2 LEU A1094 -13.907 -6.601 -88.485 1.00119.15 C ANISOU 2527 CD2 LEU A1094 15899 17019 12352 -1768 1006 -1037 C ATOM 2528 N LYS A1095 -9.000 -8.792 -89.728 1.00111.61 N ANISOU 2528 N LYS A1095 15041 15842 11524 -1402 2172 -1242 N ATOM 2529 CA LYS A1095 -7.762 -9.374 -89.187 1.00111.68 C ANISOU 2529 CA LYS A1095 14752 15857 11822 -1217 2370 -1260 C ATOM 2530 C LYS A1095 -6.670 -8.303 -89.018 1.00113.92 C ANISOU 2530 C LYS A1095 14700 16254 12332 -1221 2525 -1232 C ATOM 2531 O LYS A1095 -5.882 -8.369 -88.072 1.00113.29 O ANISOU 2531 O LYS A1095 14235 16249 12563 -1113 2474 -1191 O ATOM 2532 CB LYS A1095 -7.240 -10.505 -90.098 1.00117.03 C ANISOU 2532 CB LYS A1095 15688 16326 12451 -1106 2696 -1356 C ATOM 2533 CG LYS A1095 -8.198 -11.679 -90.265 1.00128.74 C ANISOU 2533 CG LYS A1095 17533 17660 13720 -1115 2535 -1382 C ATOM 2534 CD LYS A1095 -7.684 -12.713 -91.262 1.00138.55 C ANISOU 2534 CD LYS A1095 19129 18650 14862 -1014 2884 -1496 C ATOM 2535 CE LYS A1095 -8.693 -13.816 -91.481 1.00145.80 C ANISOU 2535 CE LYS A1095 20471 19395 15532 -1072 2679 -1516 C ATOM 2536 NZ LYS A1095 -8.203 -14.850 -92.429 1.00154.27 N ANISOU 2536 NZ LYS A1095 21965 20179 16473 -969 3022 -1642 N ATOM 2537 N THR A1096 -6.621 -7.330 -89.948 1.00109.77 N ANISOU 2537 N THR A1096 14346 15715 11644 -1369 2684 -1245 N ATOM 2538 CA THR A1096 -5.654 -6.229 -89.943 1.00109.65 C ANISOU 2538 CA THR A1096 14069 15787 11806 -1434 2848 -1214 C ATOM 2539 C THR A1096 -5.987 -5.282 -88.792 1.00109.02 C ANISOU 2539 C THR A1096 13740 15866 11816 -1495 2483 -1128 C ATOM 2540 O THR A1096 -5.098 -4.947 -88.012 1.00108.99 O ANISOU 2540 O THR A1096 13359 15948 12104 -1465 2457 -1082 O ATOM 2541 CB THR A1096 -5.655 -5.514 -91.304 1.00116.24 C ANISOU 2541 CB THR A1096 15280 16521 12364 -1610 3107 -1246 C ATOM 2542 OG1 THR A1096 -5.548 -6.491 -92.338 1.00118.29 O ANISOU 2542 OG1 THR A1096 15899 16592 12452 -1564 3426 -1341 O ATOM 2543 CG2 THR A1096 -4.532 -4.490 -91.433 1.00115.29 C ANISOU 2543 CG2 THR A1096 14908 16462 12435 -1705 3364 -1218 C ATOM 2544 N THR A1097 -7.275 -4.883 -88.684 1.00102.08 N ANISOU 2544 N THR A1097 13079 15002 10705 -1577 2198 -1108 N ATOM 2545 CA THR A1097 -7.826 -4.001 -87.647 1.00 99.38 C ANISOU 2545 CA THR A1097 12594 14770 10396 -1622 1892 -1051 C ATOM 2546 C THR A1097 -7.615 -4.644 -86.260 1.00101.32 C ANISOU 2546 C THR A1097 12573 15086 10840 -1509 1729 -1024 C ATOM 2547 O THR A1097 -7.241 -3.940 -85.321 1.00100.19 O ANISOU 2547 O THR A1097 12232 15017 10819 -1537 1590 -979 O ATOM 2548 CB THR A1097 -9.303 -3.714 -87.954 1.00103.13 C ANISOU 2548 CB THR A1097 13336 15208 10641 -1688 1678 -1048 C ATOM 2549 OG1 THR A1097 -9.374 -3.142 -89.261 1.00105.76 O ANISOU 2549 OG1 THR A1097 13970 15436 10776 -1805 1781 -1057 O ATOM 2550 CG2 THR A1097 -9.953 -2.770 -86.948 1.00 97.10 C ANISOU 2550 CG2 THR A1097 12447 14526 9920 -1708 1434 -1011 C ATOM 2551 N ARG A1098 -7.805 -5.977 -86.160 1.00 97.59 N ANISOU 2551 N ARG A1098 12149 14557 10374 -1399 1735 -1046 N ATOM 2552 CA ARG A1098 -7.598 -6.765 -84.945 1.00 97.15 C ANISOU 2552 CA ARG A1098 11927 14517 10468 -1298 1574 -1012 C ATOM 2553 C ARG A1098 -6.135 -6.651 -84.470 1.00101.91 C ANISOU 2553 C ARG A1098 12199 15138 11384 -1230 1606 -972 C ATOM 2554 O ARG A1098 -5.904 -6.333 -83.306 1.00101.09 O ANISOU 2554 O ARG A1098 11949 15082 11379 -1249 1365 -910 O ATOM 2555 CB ARG A1098 -7.975 -8.236 -85.198 1.00 98.47 C ANISOU 2555 CB ARG A1098 12266 14574 10574 -1204 1611 -1046 C ATOM 2556 CG ARG A1098 -7.817 -9.162 -83.991 1.00113.15 C ANISOU 2556 CG ARG A1098 14034 16406 12550 -1110 1426 -1000 C ATOM 2557 CD ARG A1098 -7.663 -10.610 -84.420 1.00129.57 C ANISOU 2557 CD ARG A1098 16250 18332 14649 -980 1527 -1037 C ATOM 2558 NE ARG A1098 -6.422 -10.830 -85.169 1.00143.62 N ANISOU 2558 NE ARG A1098 17891 20035 16642 -838 1799 -1080 N ATOM 2559 CZ ARG A1098 -6.160 -11.914 -85.893 1.00161.70 C ANISOU 2559 CZ ARG A1098 20336 22157 18945 -706 2005 -1147 C ATOM 2560 NH1 ARG A1098 -7.055 -12.890 -85.989 1.00148.74 N ANISOU 2560 NH1 ARG A1098 19019 20403 17091 -721 1920 -1169 N ATOM 2561 NH2 ARG A1098 -5.006 -12.025 -86.537 1.00151.58 N ANISOU 2561 NH2 ARG A1098 18893 20802 17897 -566 2323 -1196 N ATOM 2562 N ASN A1099 -5.162 -6.882 -85.372 1.00 99.96 N ANISOU 2562 N ASN A1099 11844 14837 11300 -1165 1903 -1006 N ATOM 2563 CA ASN A1099 -3.736 -6.821 -85.052 1.00102.05 C ANISOU 2563 CA ASN A1099 11707 15108 11958 -1093 1960 -963 C ATOM 2564 C ASN A1099 -3.265 -5.394 -84.749 1.00104.37 C ANISOU 2564 C ASN A1099 11811 15504 12342 -1262 1873 -904 C ATOM 2565 O ASN A1099 -2.370 -5.217 -83.922 1.00106.25 O ANISOU 2565 O ASN A1099 11719 15764 12887 -1256 1691 -828 O ATOM 2566 CB ASN A1099 -2.898 -7.390 -86.204 1.00108.75 C ANISOU 2566 CB ASN A1099 12488 15860 12973 -982 2403 -1033 C ATOM 2567 CG ASN A1099 -3.114 -8.855 -86.523 1.00143.91 C ANISOU 2567 CG ASN A1099 17126 20164 17387 -793 2516 -1099 C ATOM 2568 OD1 ASN A1099 -3.649 -9.640 -85.724 1.00138.71 O ANISOU 2568 OD1 ASN A1099 16554 19472 16679 -718 2231 -1071 O ATOM 2569 ND2 ASN A1099 -2.665 -9.265 -87.704 1.00140.34 N ANISOU 2569 ND2 ASN A1099 16781 19596 16948 -722 2962 -1193 N ATOM 2570 N ALA A1100 -3.845 -4.385 -85.421 1.00 97.43 N ANISOU 2570 N ALA A1100 11159 14658 11204 -1423 1965 -930 N ATOM 2571 CA ALA A1100 -3.437 -2.992 -85.261 1.00 96.59 C ANISOU 2571 CA ALA A1100 10942 14613 11144 -1601 1903 -880 C ATOM 2572 C ALA A1100 -4.031 -2.331 -84.019 1.00 97.35 C ANISOU 2572 C ALA A1100 11099 14756 11134 -1671 1510 -833 C ATOM 2573 O ALA A1100 -3.403 -1.428 -83.469 1.00 97.24 O ANISOU 2573 O ALA A1100 10929 14768 11250 -1792 1366 -775 O ATOM 2574 CB ALA A1100 -3.833 -2.195 -86.488 1.00 96.94 C ANISOU 2574 CB ALA A1100 11271 14629 10933 -1739 2137 -920 C ATOM 2575 N TYR A1101 -5.225 -2.758 -83.583 1.00 91.90 N ANISOU 2575 N TYR A1101 10648 14059 10210 -1614 1360 -861 N ATOM 2576 CA TYR A1101 -5.911 -2.136 -82.456 1.00 90.29 C ANISOU 2576 CA TYR A1101 10561 13875 9871 -1675 1083 -842 C ATOM 2577 C TYR A1101 -6.057 -3.040 -81.201 1.00 98.13 C ANISOU 2577 C TYR A1101 11557 14847 10881 -1598 861 -813 C ATOM 2578 O TYR A1101 -6.321 -2.495 -80.125 1.00 99.13 O ANISOU 2578 O TYR A1101 11789 14965 10912 -1670 652 -791 O ATOM 2579 CB TYR A1101 -7.318 -1.675 -82.892 1.00 87.97 C ANISOU 2579 CB TYR A1101 10545 13574 9305 -1700 1112 -894 C ATOM 2580 CG TYR A1101 -7.342 -0.455 -83.793 1.00 87.60 C ANISOU 2580 CG TYR A1101 10595 13509 9179 -1811 1202 -901 C ATOM 2581 CD1 TYR A1101 -7.260 0.829 -83.263 1.00 88.79 C ANISOU 2581 CD1 TYR A1101 10781 13650 9306 -1916 1072 -881 C ATOM 2582 CD2 TYR A1101 -7.512 -0.582 -85.169 1.00 88.29 C ANISOU 2582 CD2 TYR A1101 10820 13554 9172 -1825 1399 -928 C ATOM 2583 CE1 TYR A1101 -7.330 1.955 -84.079 1.00 88.39 C ANISOU 2583 CE1 TYR A1101 10868 13551 9165 -2022 1129 -879 C ATOM 2584 CE2 TYR A1101 -7.576 0.539 -85.997 1.00 89.03 C ANISOU 2584 CE2 TYR A1101 11079 13597 9152 -1947 1453 -921 C ATOM 2585 CZ TYR A1101 -7.478 1.806 -85.447 1.00 91.64 C ANISOU 2585 CZ TYR A1101 11412 13921 9486 -2041 1314 -893 C ATOM 2586 OH TYR A1101 -7.542 2.922 -86.244 1.00 87.22 O ANISOU 2586 OH TYR A1101 11052 13282 8805 -2166 1343 -877 O ATOM 2587 N ILE A1102 -5.922 -4.381 -81.312 1.00 95.71 N ANISOU 2587 N ILE A1102 11204 14502 10657 -1466 909 -814 N ATOM 2588 CA ILE A1102 -6.123 -5.251 -80.136 1.00 95.78 C ANISOU 2588 CA ILE A1102 11291 14460 10639 -1416 683 -775 C ATOM 2589 C ILE A1102 -4.786 -5.858 -79.662 1.00101.13 C ANISOU 2589 C ILE A1102 11711 15075 11636 -1333 522 -697 C ATOM 2590 O ILE A1102 -4.460 -5.710 -78.485 1.00100.77 O ANISOU 2590 O ILE A1102 11688 14987 11613 -1391 209 -624 O ATOM 2591 CB ILE A1102 -7.185 -6.375 -80.410 1.00 97.95 C ANISOU 2591 CB ILE A1102 11772 14701 10746 -1345 778 -820 C ATOM 2592 CG1 ILE A1102 -8.532 -5.780 -80.887 1.00 96.47 C ANISOU 2592 CG1 ILE A1102 11766 14563 10326 -1424 885 -879 C ATOM 2593 CG2 ILE A1102 -7.375 -7.306 -79.186 1.00 99.00 C ANISOU 2593 CG2 ILE A1102 12034 14757 10824 -1324 564 -770 C ATOM 2594 CD1 ILE A1102 -9.465 -6.750 -81.561 1.00104.44 C ANISOU 2594 CD1 ILE A1102 12920 15535 11226 -1392 987 -918 C ATOM 2595 N GLN A1103 -4.042 -6.554 -80.563 1.00 99.38 N ANISOU 2595 N GLN A1103 11271 14822 11665 -1194 728 -713 N ATOM 2596 CA GLN A1103 -2.776 -7.265 -80.309 1.00102.49 C ANISOU 2596 CA GLN A1103 11344 15134 12464 -1054 625 -647 C ATOM 2597 C GLN A1103 -1.820 -6.477 -79.382 1.00108.67 C ANISOU 2597 C GLN A1103 11880 15921 13488 -1161 287 -537 C ATOM 2598 O GLN A1103 -1.143 -7.083 -78.551 1.00111.04 O ANISOU 2598 O GLN A1103 12044 16120 14027 -1086 -35 -443 O ATOM 2599 CB GLN A1103 -2.074 -7.572 -81.635 1.00105.60 C ANISOU 2599 CB GLN A1103 11504 15514 13107 -930 1035 -708 C ATOM 2600 CG GLN A1103 -1.010 -8.665 -81.556 1.00121.52 C ANISOU 2600 CG GLN A1103 13209 17404 15561 -699 1025 -672 C ATOM 2601 CD GLN A1103 -0.333 -8.911 -82.886 1.00138.45 C ANISOU 2601 CD GLN A1103 15149 19515 17941 -575 1531 -757 C ATOM 2602 OE1 GLN A1103 -0.975 -9.032 -83.940 1.00129.93 O ANISOU 2602 OE1 GLN A1103 14366 18430 16573 -587 1886 -867 O ATOM 2603 NE2 GLN A1103 0.986 -9.038 -82.859 1.00133.41 N ANISOU 2603 NE2 GLN A1103 14012 18830 17849 -453 1576 -706 N ATOM 2604 N LYS A1104 -1.802 -5.137 -79.514 1.00104.01 N ANISOU 2604 N LYS A1104 11276 15420 12824 -1349 316 -540 N ATOM 2605 CA LYS A1104 -1.023 -4.184 -78.715 1.00105.03 C ANISOU 2605 CA LYS A1104 11247 15544 13114 -1516 -10 -443 C ATOM 2606 C LYS A1104 -1.364 -4.301 -77.200 1.00107.07 C ANISOU 2606 C LYS A1104 11809 15710 13164 -1588 -477 -375 C ATOM 2607 O LYS A1104 -0.459 -4.189 -76.370 1.00109.54 O ANISOU 2607 O LYS A1104 11969 15940 13711 -1655 -876 -259 O ATOM 2608 CB LYS A1104 -1.319 -2.763 -79.243 1.00106.04 C ANISOU 2608 CB LYS A1104 11470 15759 13062 -1708 160 -489 C ATOM 2609 CG LYS A1104 -0.805 -1.581 -78.414 1.00120.37 C ANISOU 2609 CG LYS A1104 13273 17551 14910 -1933 -175 -409 C ATOM 2610 CD LYS A1104 -0.972 -0.244 -79.156 1.00130.29 C ANISOU 2610 CD LYS A1104 14599 18866 16038 -2104 42 -454 C ATOM 2611 CE LYS A1104 -2.406 0.194 -79.379 1.00136.42 C ANISOU 2611 CE LYS A1104 15815 19660 16360 -2101 195 -558 C ATOM 2612 NZ LYS A1104 -2.498 1.268 -80.400 1.00144.61 N ANISOU 2612 NZ LYS A1104 16895 20726 17322 -2217 441 -594 N ATOM 2613 N TYR A1105 -2.653 -4.557 -76.862 1.00 99.52 N ANISOU 2613 N TYR A1105 11284 14747 11780 -1587 -423 -442 N ATOM 2614 CA TYR A1105 -3.183 -4.663 -75.491 1.00 98.37 C ANISOU 2614 CA TYR A1105 11535 14502 11339 -1678 -740 -404 C ATOM 2615 C TYR A1105 -3.064 -6.082 -74.894 1.00102.79 C ANISOU 2615 C TYR A1105 12175 14934 11947 -1554 -946 -338 C ATOM 2616 O TYR A1105 -3.021 -6.210 -73.676 1.00102.87 O ANISOU 2616 O TYR A1105 12469 14811 11804 -1650 -1311 -261 O ATOM 2617 CB TYR A1105 -4.651 -4.211 -75.451 1.00 95.84 C ANISOU 2617 CB TYR A1105 11595 14231 10587 -1743 -507 -512 C ATOM 2618 CG TYR A1105 -4.811 -2.747 -75.800 1.00 96.04 C ANISOU 2618 CG TYR A1105 11633 14324 10534 -1865 -394 -564 C ATOM 2619 CD1 TYR A1105 -5.216 -2.353 -77.073 1.00 95.31 C ANISOU 2619 CD1 TYR A1105 11417 14337 10460 -1819 -56 -640 C ATOM 2620 CD2 TYR A1105 -4.491 -1.753 -74.882 1.00 98.60 C ANISOU 2620 CD2 TYR A1105 12133 14573 10759 -2039 -659 -527 C ATOM 2621 CE1 TYR A1105 -5.329 -1.005 -77.411 1.00 94.17 C ANISOU 2621 CE1 TYR A1105 11313 14220 10246 -1931 16 -675 C ATOM 2622 CE2 TYR A1105 -4.604 -0.402 -75.207 1.00 99.08 C ANISOU 2622 CE2 TYR A1105 12235 14662 10749 -2149 -569 -574 C ATOM 2623 CZ TYR A1105 -5.022 -0.032 -76.474 1.00102.36 C ANISOU 2623 CZ TYR A1105 12510 15182 11199 -2088 -232 -644 C ATOM 2624 OH TYR A1105 -5.128 1.302 -76.783 1.00102.86 O ANISOU 2624 OH TYR A1105 12654 15242 11187 -2198 -175 -678 O ATOM 2625 N LEU A1106 -2.989 -7.130 -75.730 1.00100.43 N ANISOU 2625 N LEU A1106 11687 14640 11834 -1354 -729 -367 N ATOM 2626 CA LEU A1106 -2.823 -8.511 -75.267 1.00102.21 C ANISOU 2626 CA LEU A1106 11988 14713 12135 -1214 -921 -304 C ATOM 2627 C LEU A1106 -1.355 -8.778 -74.866 1.00111.98 C ANISOU 2627 C LEU A1106 12867 15828 13850 -1129 -1306 -170 C ATOM 2628 O LEU A1106 -1.057 -9.814 -74.276 1.00114.08 O ANISOU 2628 O LEU A1106 13208 15922 14218 -1019 -1596 -84 O ATOM 2629 CB LEU A1106 -3.276 -9.505 -76.355 1.00100.83 C ANISOU 2629 CB LEU A1106 11778 14553 11981 -1031 -545 -394 C ATOM 2630 N ALA A 441 -0.444 -7.844 -75.185 1.00125.32 N ANISOU 2630 N ALA A 441 15659 22187 9768 -2652 -1600 1417 N ATOM 2631 CA ALA A 441 0.983 -7.955 -74.885 1.00123.81 C ANISOU 2631 CA ALA A 441 15641 21662 9740 -2637 -1466 1348 C ATOM 2632 C ALA A 441 1.356 -7.196 -73.610 1.00127.16 C ANISOU 2632 C ALA A 441 16051 21887 10379 -2438 -1429 1411 C ATOM 2633 O ALA A 441 2.208 -7.663 -72.848 1.00126.07 O ANISOU 2633 O ALA A 441 15985 21516 10401 -2463 -1332 1323 O ATOM 2634 CB ALA A 441 1.794 -7.425 -76.055 1.00125.13 C ANISOU 2634 CB ALA A 441 15938 21786 9820 -2616 -1429 1395 C ATOM 2635 N ALA A 442 0.696 -6.044 -73.368 1.00123.89 N ANISOU 2635 N ALA A 442 15550 21568 9954 -2231 -1511 1560 N ATOM 2636 CA ALA A 442 0.922 -5.136 -72.238 1.00122.16 C ANISOU 2636 CA ALA A 442 15339 21174 9903 -2016 -1496 1636 C ATOM 2637 C ALA A 442 0.400 -5.681 -70.882 1.00124.36 C ANISOU 2637 C ALA A 442 15494 21455 10302 -2010 -1495 1573 C ATOM 2638 O ALA A 442 0.494 -4.970 -69.879 1.00122.41 O ANISOU 2638 O ALA A 442 15247 21078 10184 -1828 -1488 1628 O ATOM 2639 CB ALA A 442 0.263 -3.794 -72.530 1.00124.20 C ANISOU 2639 CB ALA A 442 15571 21549 10068 -1783 -1593 1810 C ATOM 2640 N SER A 443 -0.137 -6.919 -70.844 1.00121.68 N ANISOU 2640 N SER A 443 15067 21255 9910 -2217 -1504 1463 N ATOM 2641 CA SER A 443 -0.674 -7.528 -69.619 1.00120.65 C ANISOU 2641 CA SER A 443 14818 21152 9871 -2249 -1506 1408 C ATOM 2642 C SER A 443 0.047 -8.808 -69.217 1.00122.27 C ANISOU 2642 C SER A 443 15120 21162 10173 -2455 -1413 1248 C ATOM 2643 O SER A 443 -0.377 -9.453 -68.256 1.00122.41 O ANISOU 2643 O SER A 443 15058 21197 10254 -2521 -1414 1196 O ATOM 2644 CB SER A 443 -2.152 -7.844 -69.794 1.00127.04 C ANISOU 2644 CB SER A 443 15420 22342 10508 -2321 -1620 1441 C ATOM 2645 N LYS A 444 1.117 -9.188 -69.941 1.00117.06 N ANISOU 2645 N LYS A 444 14636 20329 9514 -2546 -1333 1174 N ATOM 2646 CA LYS A 444 1.894 -10.381 -69.622 1.00115.21 C ANISOU 2646 CA LYS A 444 14524 19895 9357 -2699 -1237 1023 C ATOM 2647 C LYS A 444 2.777 -10.081 -68.396 1.00116.05 C ANISOU 2647 C LYS A 444 14664 19740 9688 -2560 -1151 1023 C ATOM 2648 O LYS A 444 3.829 -9.429 -68.516 1.00114.94 O ANISOU 2648 O LYS A 444 14614 19434 9622 -2452 -1086 1059 O ATOM 2649 CB LYS A 444 2.716 -10.847 -70.834 1.00118.30 C ANISOU 2649 CB LYS A 444 15081 20222 9648 -2804 -1177 949 C ATOM 2650 N ILE A 445 2.291 -10.505 -67.205 1.00110.41 N ANISOU 2650 N ILE A 445 13865 19016 9068 -2572 -1161 994 N ATOM 2651 CA ILE A 445 2.971 -10.338 -65.917 1.00107.85 C ANISOU 2651 CA ILE A 445 13557 18473 8949 -2459 -1092 986 C ATOM 2652 C ILE A 445 4.123 -11.345 -65.859 1.00109.67 C ANISOU 2652 C ILE A 445 13945 18477 9247 -2557 -978 859 C ATOM 2653 O ILE A 445 3.884 -12.558 -65.890 1.00108.73 O ANISOU 2653 O ILE A 445 13877 18361 9075 -2729 -970 752 O ATOM 2654 CB ILE A 445 2.000 -10.476 -64.701 1.00110.59 C ANISOU 2654 CB ILE A 445 13752 18916 9352 -2439 -1142 1003 C ATOM 2655 CG1 ILE A 445 0.813 -9.488 -64.808 1.00112.24 C ANISOU 2655 CG1 ILE A 445 13792 19390 9463 -2305 -1253 1132 C ATOM 2656 CG2 ILE A 445 2.754 -10.287 -63.374 1.00109.04 C ANISOU 2656 CG2 ILE A 445 13583 18487 9362 -2321 -1069 993 C ATOM 2657 CD1 ILE A 445 -0.378 -9.804 -63.896 1.00120.92 C ANISOU 2657 CD1 ILE A 445 14704 20697 10543 -2327 -1315 1147 C ATOM 2658 N ASN A 446 5.368 -10.820 -65.782 1.00105.22 N ANISOU 2658 N ASN A 446 13466 17728 8786 -2445 -894 878 N ATOM 2659 CA ASN A 446 6.620 -11.586 -65.734 1.00104.45 C ANISOU 2659 CA ASN A 446 13501 17437 8748 -2479 -775 779 C ATOM 2660 C ASN A 446 6.732 -12.414 -64.436 1.00107.88 C ANISOU 2660 C ASN A 446 13939 17736 9316 -2496 -733 703 C ATOM 2661 O ASN A 446 6.121 -12.057 -63.425 1.00107.21 O ANISOU 2661 O ASN A 446 13745 17672 9318 -2442 -779 751 O ATOM 2662 CB ASN A 446 7.827 -10.651 -65.876 1.00103.36 C ANISOU 2662 CB ASN A 446 13404 17191 8675 -2357 -710 850 C ATOM 2663 CG ASN A 446 7.905 -9.576 -64.820 1.00117.90 C ANISOU 2663 CG ASN A 446 15178 18957 10660 -2217 -731 949 C ATOM 2664 OD1 ASN A 446 8.277 -9.825 -63.673 1.00110.23 O ANISOU 2664 OD1 ASN A 446 14196 17859 9829 -2180 -689 918 O ATOM 2665 ND2 ASN A 446 7.567 -8.356 -65.190 1.00106.51 N ANISOU 2665 ND2 ASN A 446 13711 17582 9175 -2132 -800 1071 N ATOM 2666 N GLU A 447 7.535 -13.505 -64.478 1.00104.42 N ANISOU 2666 N GLU A 447 13635 17159 8881 -2555 -642 587 N ATOM 2667 CA GLU A 447 7.762 -14.455 -63.381 1.00103.40 C ANISOU 2667 CA GLU A 447 13552 16879 8855 -2576 -593 506 C ATOM 2668 C GLU A 447 8.337 -13.793 -62.133 1.00105.35 C ANISOU 2668 C GLU A 447 13722 17015 9289 -2430 -557 566 C ATOM 2669 O GLU A 447 8.002 -14.232 -61.037 1.00104.96 O ANISOU 2669 O GLU A 447 13642 16911 9328 -2443 -564 543 O ATOM 2670 CB GLU A 447 8.698 -15.585 -63.821 1.00105.33 C ANISOU 2670 CB GLU A 447 13984 16987 9048 -2610 -493 382 C ATOM 2671 N THR A 448 9.209 -12.764 -62.288 1.00100.78 N ANISOU 2671 N THR A 448 13123 16406 8761 -2310 -521 644 N ATOM 2672 CA THR A 448 9.829 -12.034 -61.168 1.00 98.48 C ANISOU 2672 CA THR A 448 12777 16011 8632 -2188 -494 706 C ATOM 2673 C THR A 448 8.724 -11.424 -60.306 1.00101.96 C ANISOU 2673 C THR A 448 13103 16509 9127 -2149 -587 771 C ATOM 2674 O THR A 448 8.688 -11.665 -59.097 1.00100.73 O ANISOU 2674 O THR A 448 12911 16277 9086 -2117 -575 754 O ATOM 2675 CB THR A 448 10.816 -10.970 -61.692 1.00102.84 C ANISOU 2675 CB THR A 448 13340 16551 9183 -2117 -461 792 C ATOM 2676 OG1 THR A 448 11.895 -11.631 -62.351 1.00102.81 O ANISOU 2676 OG1 THR A 448 13419 16519 9125 -2136 -361 729 O ATOM 2677 CG2 THR A 448 11.358 -10.053 -60.587 1.00 98.85 C ANISOU 2677 CG2 THR A 448 12791 15947 8822 -2019 -456 869 C ATOM 2678 N MET A 449 7.799 -10.694 -60.954 1.00 99.25 N ANISOU 2678 N MET A 449 12703 16320 8688 -2141 -677 843 N ATOM 2679 CA MET A 449 6.646 -10.040 -60.347 1.00 99.55 C ANISOU 2679 CA MET A 449 12623 16466 8734 -2070 -769 913 C ATOM 2680 C MET A 449 5.695 -11.067 -59.709 1.00106.25 C ANISOU 2680 C MET A 449 13400 17396 9573 -2171 -797 849 C ATOM 2681 O MET A 449 5.059 -10.771 -58.693 1.00106.30 O ANISOU 2681 O MET A 449 13305 17446 9639 -2100 -836 886 O ATOM 2682 CB MET A 449 5.908 -9.231 -61.414 1.00102.92 C ANISOU 2682 CB MET A 449 13017 17066 9021 -2041 -853 997 C ATOM 2683 CG MET A 449 5.214 -8.025 -60.876 1.00106.25 C ANISOU 2683 CG MET A 449 13363 17547 9460 -1872 -929 1106 C ATOM 2684 SD MET A 449 6.356 -6.728 -60.349 1.00108.92 S ANISOU 2684 SD MET A 449 13806 17659 9919 -1720 -895 1185 S ATOM 2685 CE MET A 449 5.218 -5.602 -59.841 1.00106.22 C ANISOU 2685 CE MET A 449 13400 17412 9547 -1524 -997 1286 C ATOM 2686 N LEU A 450 5.622 -12.274 -60.298 1.00104.09 N ANISOU 2686 N LEU A 450 13194 17140 9214 -2341 -778 754 N ATOM 2687 CA LEU A 450 4.795 -13.369 -59.803 1.00104.53 C ANISOU 2687 CA LEU A 450 13222 17257 9238 -2490 -806 691 C ATOM 2688 C LEU A 450 5.353 -13.922 -58.484 1.00105.73 C ANISOU 2688 C LEU A 450 13406 17226 9541 -2466 -740 645 C ATOM 2689 O LEU A 450 4.571 -14.110 -57.549 1.00106.36 O ANISOU 2689 O LEU A 450 13387 17375 9650 -2492 -779 659 O ATOM 2690 CB LEU A 450 4.708 -14.480 -60.864 1.00106.37 C ANISOU 2690 CB LEU A 450 13579 17512 9323 -2686 -803 597 C ATOM 2691 CG LEU A 450 3.463 -15.376 -60.854 1.00112.60 C ANISOU 2691 CG LEU A 450 14328 18463 9992 -2900 -881 562 C ATOM 2692 CD1 LEU A 450 3.114 -15.822 -62.256 1.00113.80 C ANISOU 2692 CD1 LEU A 450 14559 18729 9951 -3061 -922 520 C ATOM 2693 CD2 LEU A 450 3.643 -16.590 -59.938 1.00115.45 C ANISOU 2693 CD2 LEU A 450 14792 18660 10413 -3014 -837 474 C ATOM 2694 N ARG A 451 6.677 -14.183 -58.390 1.00 99.29 N ANISOU 2694 N ARG A 451 12714 16203 8809 -2411 -641 596 N ATOM 2695 CA ARG A 451 7.206 -14.746 -57.145 1.00 97.88 C ANISOU 2695 CA ARG A 451 12565 15863 8762 -2382 -581 556 C ATOM 2696 C ARG A 451 7.540 -13.650 -56.100 1.00 99.21 C ANISOU 2696 C ARG A 451 12634 15988 9075 -2212 -577 637 C ATOM 2697 O ARG A 451 7.610 -13.970 -54.913 1.00 97.78 O ANISOU 2697 O ARG A 451 12430 15728 8994 -2189 -556 624 O ATOM 2698 CB ARG A 451 8.412 -15.676 -57.361 1.00 97.63 C ANISOU 2698 CB ARG A 451 12705 15649 8743 -2388 -477 464 C ATOM 2699 CG ARG A 451 9.663 -15.081 -57.989 1.00107.02 C ANISOU 2699 CG ARG A 451 13933 16784 9945 -2273 -406 484 C ATOM 2700 CD ARG A 451 10.921 -15.774 -57.465 1.00112.08 C ANISOU 2700 CD ARG A 451 14669 17257 10661 -2199 -297 426 C ATOM 2701 NE ARG A 451 10.810 -17.236 -57.429 1.00116.40 N ANISOU 2701 NE ARG A 451 15368 17707 11151 -2285 -268 316 N ATOM 2702 CZ ARG A 451 11.677 -18.039 -56.823 1.00122.97 C ANISOU 2702 CZ ARG A 451 16300 18388 12036 -2215 -184 260 C ATOM 2703 NH1 ARG A 451 12.731 -17.536 -56.200 1.00103.42 N ANISOU 2703 NH1 ARG A 451 13756 15868 9670 -2068 -121 304 N ATOM 2704 NH2 ARG A 451 11.494 -19.351 -56.832 1.00111.50 N ANISOU 2704 NH2 ARG A 451 15026 16826 10514 -2295 -167 162 N ATOM 2705 N LEU A 452 7.682 -12.371 -56.525 1.00 94.69 N ANISOU 2705 N LEU A 452 12018 15461 8498 -2103 -604 722 N ATOM 2706 CA LEU A 452 7.935 -11.226 -55.634 1.00 92.59 C ANISOU 2706 CA LEU A 452 11696 15142 8342 -1951 -615 801 C ATOM 2707 C LEU A 452 6.737 -11.021 -54.711 1.00 95.49 C ANISOU 2707 C LEU A 452 11941 15619 8723 -1911 -685 833 C ATOM 2708 O LEU A 452 6.899 -10.532 -53.595 1.00 95.31 O ANISOU 2708 O LEU A 452 11885 15525 8803 -1806 -680 861 O ATOM 2709 CB LEU A 452 8.214 -9.953 -56.454 1.00 93.07 C ANISOU 2709 CB LEU A 452 11779 15225 8358 -1870 -643 887 C ATOM 2710 CG LEU A 452 8.896 -8.773 -55.754 1.00 97.38 C ANISOU 2710 CG LEU A 452 12345 15653 9001 -1743 -640 960 C ATOM 2711 CD1 LEU A 452 10.391 -9.025 -55.549 1.00 97.01 C ANISOU 2711 CD1 LEU A 452 12364 15463 9034 -1766 -545 932 C ATOM 2712 CD2 LEU A 452 8.767 -7.531 -56.588 1.00100.80 C ANISOU 2712 CD2 LEU A 452 12817 16127 9357 -1679 -697 1056 C ATOM 2713 N GLY A 453 5.558 -11.422 -55.186 1.00 91.37 N ANISOU 2713 N GLY A 453 11348 15285 8082 -2001 -748 830 N ATOM 2714 CA GLY A 453 4.312 -11.381 -54.436 1.00 90.89 C ANISOU 2714 CA GLY A 453 11141 15396 7995 -1986 -814 863 C ATOM 2715 C GLY A 453 4.209 -12.531 -53.457 1.00 93.13 C ANISOU 2715 C GLY A 453 11417 15635 8334 -2100 -782 799 C ATOM 2716 O GLY A 453 3.706 -12.351 -52.345 1.00 92.17 O ANISOU 2716 O GLY A 453 11193 15567 8261 -2035 -799 828 O ATOM 2717 N ILE A 454 4.695 -13.725 -53.866 1.00 89.17 N ANISOU 2717 N ILE A 454 11040 15029 7813 -2263 -733 712 N ATOM 2718 CA ILE A 454 4.702 -14.946 -53.055 1.00 88.49 C ANISOU 2718 CA ILE A 454 11002 14857 7763 -2388 -700 646 C ATOM 2719 C ILE A 454 5.604 -14.712 -51.842 1.00 89.88 C ANISOU 2719 C ILE A 454 11194 14853 8104 -2250 -635 649 C ATOM 2720 O ILE A 454 5.200 -14.979 -50.702 1.00 89.14 O ANISOU 2720 O ILE A 454 11034 14775 8062 -2256 -641 657 O ATOM 2721 CB ILE A 454 5.139 -16.176 -53.911 1.00 92.36 C ANISOU 2721 CB ILE A 454 11678 15238 8177 -2556 -660 549 C ATOM 2722 CG1 ILE A 454 3.950 -16.646 -54.790 1.00 94.58 C ANISOU 2722 CG1 ILE A 454 11931 15725 8278 -2757 -744 542 C ATOM 2723 CG2 ILE A 454 5.660 -17.338 -53.031 1.00 92.47 C ANISOU 2723 CG2 ILE A 454 11817 15057 8259 -2619 -598 479 C ATOM 2724 CD1 ILE A 454 4.283 -17.583 -55.966 1.00104.58 C ANISOU 2724 CD1 ILE A 454 13397 16912 9429 -2909 -723 450 C ATOM 2725 N PHE A 455 6.795 -14.153 -52.093 1.00 84.28 N ANISOU 2725 N PHE A 455 10558 14000 7465 -2131 -579 652 N ATOM 2726 CA PHE A 455 7.786 -13.868 -51.066 1.00 82.09 C ANISOU 2726 CA PHE A 455 10296 13564 7329 -2011 -520 659 C ATOM 2727 C PHE A 455 7.284 -12.786 -50.085 1.00 85.46 C ANISOU 2727 C PHE A 455 10600 14053 7817 -1880 -568 733 C ATOM 2728 O PHE A 455 7.497 -12.931 -48.892 1.00 83.62 O ANISOU 2728 O PHE A 455 10346 13750 7677 -1838 -544 728 O ATOM 2729 CB PHE A 455 9.119 -13.478 -51.721 1.00 82.62 C ANISOU 2729 CB PHE A 455 10451 13518 7422 -1945 -458 658 C ATOM 2730 CG PHE A 455 9.980 -14.696 -51.980 1.00 83.20 C ANISOU 2730 CG PHE A 455 10652 13472 7488 -2003 -376 574 C ATOM 2731 CD1 PHE A 455 9.645 -15.609 -52.976 1.00 86.57 C ANISOU 2731 CD1 PHE A 455 11174 13924 7794 -2125 -376 510 C ATOM 2732 CD2 PHE A 455 11.113 -14.941 -51.217 1.00 83.20 C ANISOU 2732 CD2 PHE A 455 10688 13339 7587 -1925 -300 559 C ATOM 2733 CE1 PHE A 455 10.428 -16.747 -53.198 1.00 87.39 C ANISOU 2733 CE1 PHE A 455 11431 13898 7875 -2148 -298 426 C ATOM 2734 CE2 PHE A 455 11.894 -16.078 -51.440 1.00 86.20 C ANISOU 2734 CE2 PHE A 455 11194 13615 7943 -1937 -221 484 C ATOM 2735 CZ PHE A 455 11.539 -16.981 -52.421 1.00 85.36 C ANISOU 2735 CZ PHE A 455 11206 13513 7716 -2040 -219 415 C ATOM 2736 N GLY A 456 6.583 -11.771 -50.589 1.00 83.69 N ANISOU 2736 N GLY A 456 10309 13963 7526 -1810 -636 797 N ATOM 2737 CA GLY A 456 6.002 -10.706 -49.779 1.00 83.40 C ANISOU 2737 CA GLY A 456 10181 13993 7514 -1655 -686 864 C ATOM 2738 C GLY A 456 4.965 -11.235 -48.808 1.00 88.13 C ANISOU 2738 C GLY A 456 10658 14727 8102 -1683 -713 860 C ATOM 2739 O GLY A 456 4.985 -10.883 -47.624 1.00 86.88 O ANISOU 2739 O GLY A 456 10460 14532 8019 -1579 -706 876 O ATOM 2740 N PHE A 457 4.076 -12.123 -49.292 1.00 86.03 N ANISOU 2740 N PHE A 457 10334 14623 7730 -1843 -742 840 N ATOM 2741 CA PHE A 457 3.043 -12.735 -48.458 1.00 87.03 C ANISOU 2741 CA PHE A 457 10334 14915 7819 -1920 -771 845 C ATOM 2742 C PHE A 457 3.655 -13.706 -47.442 1.00 90.43 C ANISOU 2742 C PHE A 457 10833 15176 8352 -2001 -707 791 C ATOM 2743 O PHE A 457 3.237 -13.704 -46.279 1.00 89.85 O ANISOU 2743 O PHE A 457 10666 15160 8312 -1960 -711 812 O ATOM 2744 CB PHE A 457 1.981 -13.443 -49.307 1.00 90.54 C ANISOU 2744 CB PHE A 457 10711 15585 8105 -2113 -827 843 C ATOM 2745 CG PHE A 457 0.889 -12.506 -49.746 1.00 93.46 C ANISOU 2745 CG PHE A 457 10920 16236 8356 -2004 -907 924 C ATOM 2746 CD1 PHE A 457 -0.223 -12.282 -48.940 1.00 97.61 C ANISOU 2746 CD1 PHE A 457 11250 17015 8822 -1944 -951 981 C ATOM 2747 CD2 PHE A 457 0.972 -11.838 -50.966 1.00 96.34 C ANISOU 2747 CD2 PHE A 457 11323 16628 8654 -1946 -936 949 C ATOM 2748 CE1 PHE A 457 -1.243 -11.416 -49.352 1.00100.33 C ANISOU 2748 CE1 PHE A 457 11437 17644 9038 -1807 -1024 1062 C ATOM 2749 CE2 PHE A 457 -0.040 -10.961 -51.373 1.00100.75 C ANISOU 2749 CE2 PHE A 457 11740 17450 9092 -1818 -1013 1031 C ATOM 2750 CZ PHE A 457 -1.141 -10.754 -50.563 1.00100.16 C ANISOU 2750 CZ PHE A 457 11469 17632 8955 -1738 -1055 1087 C ATOM 2751 N LEU A 458 4.658 -14.499 -47.868 1.00 86.73 N ANISOU 2751 N LEU A 458 10527 14504 7922 -2093 -647 725 N ATOM 2752 CA LEU A 458 5.370 -15.450 -47.015 1.00 85.93 C ANISOU 2752 CA LEU A 458 10520 14220 7908 -2146 -582 674 C ATOM 2753 C LEU A 458 6.122 -14.700 -45.914 1.00 87.03 C ANISOU 2753 C LEU A 458 10636 14247 8183 -1964 -547 700 C ATOM 2754 O LEU A 458 6.041 -15.098 -44.747 1.00 86.60 O ANISOU 2754 O LEU A 458 10552 14169 8184 -1967 -531 699 O ATOM 2755 CB LEU A 458 6.326 -16.295 -47.869 1.00 86.77 C ANISOU 2755 CB LEU A 458 10815 14150 8005 -2225 -524 602 C ATOM 2756 CG LEU A 458 6.968 -17.539 -47.252 1.00 92.42 C ANISOU 2756 CG LEU A 458 11670 14679 8766 -2293 -461 542 C ATOM 2757 CD1 LEU A 458 5.958 -18.379 -46.465 1.00 93.70 C ANISOU 2757 CD1 LEU A 458 11800 14917 8886 -2450 -498 546 C ATOM 2758 CD2 LEU A 458 7.611 -18.389 -48.337 1.00 96.56 C ANISOU 2758 CD2 LEU A 458 12386 15077 9224 -2365 -418 468 C ATOM 2759 N ALA A 459 6.776 -13.571 -46.265 1.00 81.43 N ANISOU 2759 N ALA A 459 9942 13484 7514 -1819 -543 729 N ATOM 2760 CA ALA A 459 7.493 -12.738 -45.298 1.00 80.11 C ANISOU 2760 CA ALA A 459 9770 13213 7456 -1667 -523 756 C ATOM 2761 C ALA A 459 6.519 -12.114 -44.289 1.00 84.72 C ANISOU 2761 C ALA A 459 10229 13924 8035 -1570 -573 800 C ATOM 2762 O ALA A 459 6.827 -12.108 -43.107 1.00 84.64 O ANISOU 2762 O ALA A 459 10207 13847 8105 -1514 -550 799 O ATOM 2763 CB ALA A 459 8.290 -11.659 -46.005 1.00 80.54 C ANISOU 2763 CB ALA A 459 9884 13195 7522 -1576 -522 786 C ATOM 2764 N PHE A 460 5.333 -11.652 -44.747 1.00 82.64 N ANISOU 2764 N PHE A 460 9868 13865 7666 -1544 -639 840 N ATOM 2765 CA PHE A 460 4.256 -11.079 -43.919 1.00 82.53 C ANISOU 2765 CA PHE A 460 9716 14029 7611 -1428 -687 886 C ATOM 2766 C PHE A 460 3.828 -12.046 -42.808 1.00 85.98 C ANISOU 2766 C PHE A 460 10075 14529 8065 -1521 -667 869 C ATOM 2767 O PHE A 460 3.681 -11.615 -41.668 1.00 85.87 O ANISOU 2767 O PHE A 460 10005 14534 8089 -1399 -666 888 O ATOM 2768 CB PHE A 460 3.032 -10.718 -44.787 1.00 85.38 C ANISOU 2768 CB PHE A 460 9969 14646 7826 -1412 -756 932 C ATOM 2769 CG PHE A 460 1.905 -10.050 -44.038 1.00 87.46 C ANISOU 2769 CG PHE A 460 10077 15133 8020 -1249 -803 987 C ATOM 2770 CD1 PHE A 460 1.851 -8.666 -43.919 1.00 90.50 C ANISOU 2770 CD1 PHE A 460 10490 15504 8393 -996 -834 1031 C ATOM 2771 CD2 PHE A 460 0.893 -10.804 -43.451 1.00 90.70 C ANISOU 2771 CD2 PHE A 460 10324 15777 8361 -1345 -817 998 C ATOM 2772 CE1 PHE A 460 0.815 -8.048 -43.209 1.00 92.21 C ANISOU 2772 CE1 PHE A 460 10573 15932 8528 -805 -871 1077 C ATOM 2773 CE2 PHE A 460 -0.134 -10.186 -42.728 1.00 94.22 C ANISOU 2773 CE2 PHE A 460 10606 16465 8727 -1173 -852 1053 C ATOM 2774 CZ PHE A 460 -0.169 -8.811 -42.618 1.00 92.23 C ANISOU 2774 CZ PHE A 460 10385 16196 8463 -886 -876 1088 C ATOM 2775 N GLY A 461 3.621 -13.318 -43.159 1.00 82.18 N ANISOU 2775 N GLY A 461 9607 14074 7543 -1738 -655 836 N ATOM 2776 CA GLY A 461 3.217 -14.376 -42.235 1.00 81.94 C ANISOU 2776 CA GLY A 461 9534 14088 7510 -1874 -641 826 C ATOM 2777 C GLY A 461 4.176 -14.565 -41.080 1.00 83.45 C ANISOU 2777 C GLY A 461 9798 14076 7833 -1814 -582 803 C ATOM 2778 O GLY A 461 3.758 -14.563 -39.925 1.00 83.24 O ANISOU 2778 O GLY A 461 9682 14127 7820 -1776 -583 827 O ATOM 2779 N PHE A 462 5.476 -14.677 -41.389 1.00 78.92 N ANISOU 2779 N PHE A 462 9375 13263 7347 -1794 -530 763 N ATOM 2780 CA PHE A 462 6.553 -14.827 -40.409 1.00 77.04 C ANISOU 2780 CA PHE A 462 9206 12837 7228 -1729 -473 745 C ATOM 2781 C PHE A 462 6.688 -13.582 -39.517 1.00 81.97 C ANISOU 2781 C PHE A 462 9767 13469 7910 -1537 -488 780 C ATOM 2782 O PHE A 462 6.986 -13.720 -38.325 1.00 81.60 O ANISOU 2782 O PHE A 462 9709 13369 7927 -1497 -464 780 O ATOM 2783 CB PHE A 462 7.890 -15.100 -41.110 1.00 77.94 C ANISOU 2783 CB PHE A 462 9466 12753 7393 -1732 -418 705 C ATOM 2784 CG PHE A 462 8.082 -16.476 -41.704 1.00 80.16 C ANISOU 2784 CG PHE A 462 9871 12954 7634 -1885 -384 654 C ATOM 2785 CD1 PHE A 462 8.156 -17.599 -40.889 1.00 83.24 C ANISOU 2785 CD1 PHE A 462 10322 13262 8042 -1964 -354 635 C ATOM 2786 CD2 PHE A 462 8.295 -16.638 -43.066 1.00 83.21 C ANISOU 2786 CD2 PHE A 462 10339 13319 7958 -1939 -379 624 C ATOM 2787 CE1 PHE A 462 8.384 -18.867 -41.433 1.00 84.94 C ANISOU 2787 CE1 PHE A 462 10701 13364 8208 -2090 -324 584 C ATOM 2788 CE2 PHE A 462 8.502 -17.909 -43.613 1.00 86.89 C ANISOU 2788 CE2 PHE A 462 10955 13688 8372 -2065 -347 567 C ATOM 2789 CZ PHE A 462 8.552 -19.013 -42.792 1.00 85.22 C ANISOU 2789 CZ PHE A 462 10827 13379 8175 -2136 -321 546 C ATOM 2790 N VAL A 463 6.497 -12.372 -40.090 1.00 79.20 N ANISOU 2790 N VAL A 463 9397 13169 7526 -1417 -528 808 N ATOM 2791 CA VAL A 463 6.596 -11.108 -39.338 1.00 79.16 C ANISOU 2791 CA VAL A 463 9380 13144 7552 -1230 -551 837 C ATOM 2792 C VAL A 463 5.347 -10.994 -38.408 1.00 84.90 C ANISOU 2792 C VAL A 463 9966 14073 8219 -1160 -583 863 C ATOM 2793 O VAL A 463 5.473 -10.500 -37.286 1.00 84.76 O ANISOU 2793 O VAL A 463 9940 14024 8240 -1042 -580 868 O ATOM 2794 CB VAL A 463 6.790 -9.877 -40.276 1.00 83.15 C ANISOU 2794 CB VAL A 463 9953 13615 8027 -1127 -588 863 C ATOM 2795 CG1 VAL A 463 6.800 -8.558 -39.501 1.00 83.09 C ANISOU 2795 CG1 VAL A 463 9978 13565 8027 -935 -621 890 C ATOM 2796 CG2 VAL A 463 8.077 -10.014 -41.082 1.00 82.26 C ANISOU 2796 CG2 VAL A 463 9958 13332 7964 -1205 -548 844 C ATOM 2797 N LEU A 464 4.180 -11.520 -38.844 1.00 82.31 N ANISOU 2797 N LEU A 464 9522 13966 7786 -1248 -612 881 N ATOM 2798 CA LEU A 464 2.950 -11.551 -38.050 1.00 82.69 C ANISOU 2798 CA LEU A 464 9403 14265 7751 -1208 -639 916 C ATOM 2799 C LEU A 464 3.113 -12.474 -36.839 1.00 85.73 C ANISOU 2799 C LEU A 464 9767 14615 8190 -1303 -598 902 C ATOM 2800 O LEU A 464 2.603 -12.153 -35.766 1.00 85.75 O ANISOU 2800 O LEU A 464 9673 14738 8172 -1196 -602 925 O ATOM 2801 CB LEU A 464 1.769 -12.012 -38.921 1.00 84.26 C ANISOU 2801 CB LEU A 464 9477 14727 7812 -1331 -682 945 C ATOM 2802 CG LEU A 464 0.387 -12.148 -38.259 1.00 90.63 C ANISOU 2802 CG LEU A 464 10067 15870 8497 -1325 -712 995 C ATOM 2803 CD1 LEU A 464 -0.084 -10.826 -37.645 1.00 91.36 C ANISOU 2803 CD1 LEU A 464 10082 16082 8548 -1019 -734 1031 C ATOM 2804 CD2 LEU A 464 -0.639 -12.683 -39.247 1.00 93.36 C ANISOU 2804 CD2 LEU A 464 10296 16478 8699 -1497 -759 1026 C ATOM 2805 N ILE A 465 3.836 -13.604 -37.008 1.00 81.34 N ANISOU 2805 N ILE A 465 9316 13897 7694 -1487 -557 866 N ATOM 2806 CA ILE A 465 4.099 -14.584 -35.942 1.00 80.43 C ANISOU 2806 CA ILE A 465 9218 13713 7628 -1586 -517 857 C ATOM 2807 C ILE A 465 5.034 -13.937 -34.917 1.00 82.63 C ANISOU 2807 C ILE A 465 9546 13835 8015 -1420 -487 847 C ATOM 2808 O ILE A 465 4.728 -13.933 -33.728 1.00 81.78 O ANISOU 2808 O ILE A 465 9366 13798 7909 -1372 -482 864 O ATOM 2809 CB ILE A 465 4.652 -15.912 -36.533 1.00 83.06 C ANISOU 2809 CB ILE A 465 9691 13891 7978 -1793 -484 819 C ATOM 2810 CG1 ILE A 465 3.503 -16.688 -37.253 1.00 84.36 C ANISOU 2810 CG1 ILE A 465 9802 14243 8009 -2006 -525 833 C ATOM 2811 CG2 ILE A 465 5.302 -16.775 -35.447 1.00 81.84 C ANISOU 2811 CG2 ILE A 465 9612 13586 7897 -1839 -436 808 C ATOM 2812 CD1 ILE A 465 3.922 -17.694 -38.315 1.00 85.94 C ANISOU 2812 CD1 ILE A 465 10171 14296 8187 -2185 -511 786 C ATOM 2813 N THR A 466 6.127 -13.334 -35.398 1.00 79.34 N ANISOU 2813 N THR A 466 9243 13231 7671 -1340 -473 824 N ATOM 2814 CA THR A 466 7.127 -12.588 -34.628 1.00 77.84 C ANISOU 2814 CA THR A 466 9116 12891 7571 -1207 -456 817 C ATOM 2815 C THR A 466 6.383 -11.579 -33.748 1.00 82.51 C ANISOU 2815 C THR A 466 9625 13606 8120 -1040 -493 840 C ATOM 2816 O THR A 466 6.569 -11.587 -32.539 1.00 83.75 O ANISOU 2816 O THR A 466 9767 13743 8312 -990 -477 839 O ATOM 2817 CB THR A 466 8.123 -11.953 -35.629 1.00 84.27 C ANISOU 2817 CB THR A 466 10040 13558 8421 -1178 -454 805 C ATOM 2818 OG1 THR A 466 9.050 -12.959 -36.028 1.00 80.68 O ANISOU 2818 OG1 THR A 466 9662 12979 8014 -1292 -402 779 O ATOM 2819 CG2 THR A 466 8.883 -10.767 -35.073 1.00 85.34 C ANISOU 2819 CG2 THR A 466 10236 13586 8605 -1044 -466 812 C ATOM 2820 N PHE A 467 5.487 -10.781 -34.343 1.00 79.47 N ANISOU 2820 N PHE A 467 9187 13362 7645 -944 -540 862 N ATOM 2821 CA PHE A 467 4.684 -9.777 -33.656 1.00 79.39 C ANISOU 2821 CA PHE A 467 9112 13486 7566 -744 -575 884 C ATOM 2822 C PHE A 467 3.863 -10.402 -32.519 1.00 82.59 C ANISOU 2822 C PHE A 467 9371 14081 7928 -760 -561 899 C ATOM 2823 O PHE A 467 3.889 -9.868 -31.410 1.00 82.64 O ANISOU 2823 O PHE A 467 9376 14084 7939 -619 -558 895 O ATOM 2824 CB PHE A 467 3.757 -9.052 -34.649 1.00 82.07 C ANISOU 2824 CB PHE A 467 9405 13983 7794 -644 -625 914 C ATOM 2825 CG PHE A 467 2.880 -7.999 -34.011 1.00 84.96 C ANISOU 2825 CG PHE A 467 9715 14500 8065 -391 -660 937 C ATOM 2826 CD1 PHE A 467 3.356 -6.709 -33.796 1.00 88.15 C ANISOU 2826 CD1 PHE A 467 10276 14738 8478 -191 -684 927 C ATOM 2827 CD2 PHE A 467 1.582 -8.300 -33.614 1.00 88.48 C ANISOU 2827 CD2 PHE A 467 9960 15261 8396 -353 -669 971 C ATOM 2828 CE1 PHE A 467 2.553 -5.741 -33.190 1.00 89.91 C ANISOU 2828 CE1 PHE A 467 10483 15081 8598 72 -714 942 C ATOM 2829 CE2 PHE A 467 0.785 -7.336 -32.997 1.00 92.85 C ANISOU 2829 CE2 PHE A 467 10459 15974 8846 -83 -692 992 C ATOM 2830 CZ PHE A 467 1.279 -6.063 -32.786 1.00 90.89 C ANISOU 2830 CZ PHE A 467 10394 15531 8609 143 -714 972 C ATOM 2831 N SER A 468 3.133 -11.508 -32.801 1.00 77.83 N ANISOU 2831 N SER A 468 8655 13645 7270 -942 -555 919 N ATOM 2832 CA SER A 468 2.271 -12.223 -31.847 1.00 77.31 C ANISOU 2832 CA SER A 468 8441 13794 7142 -1011 -545 948 C ATOM 2833 C SER A 468 3.062 -12.750 -30.640 1.00 79.12 C ANISOU 2833 C SER A 468 8730 13866 7465 -1049 -500 931 C ATOM 2834 O SER A 468 2.579 -12.639 -29.514 1.00 78.92 O ANISOU 2834 O SER A 468 8611 13976 7401 -973 -494 950 O ATOM 2835 CB SER A 468 1.561 -13.385 -32.533 1.00 80.40 C ANISOU 2835 CB SER A 468 8754 14336 7458 -1263 -554 972 C ATOM 2836 OG SER A 468 0.950 -12.955 -33.736 1.00 90.65 O ANISOU 2836 OG SER A 468 10003 15768 8671 -1245 -597 987 O ATOM 2837 N CYS A 469 4.267 -13.315 -30.873 1.00 73.44 N ANISOU 2837 N CYS A 469 8161 12884 6858 -1153 -469 898 N ATOM 2838 CA CYS A 469 5.116 -13.836 -29.807 1.00 72.55 C ANISOU 2838 CA CYS A 469 8112 12622 6832 -1179 -428 887 C ATOM 2839 C CYS A 469 5.671 -12.674 -28.979 1.00 77.79 C ANISOU 2839 C CYS A 469 8811 13206 7538 -973 -433 871 C ATOM 2840 O CYS A 469 5.607 -12.723 -27.751 1.00 77.74 O ANISOU 2840 O CYS A 469 8763 13241 7532 -926 -420 879 O ATOM 2841 CB CYS A 469 6.229 -14.709 -30.370 1.00 72.07 C ANISOU 2841 CB CYS A 469 8194 12334 6856 -1309 -393 860 C ATOM 2842 SG CYS A 469 5.642 -16.130 -31.331 1.00 76.90 S ANISOU 2842 SG CYS A 469 8829 12988 7402 -1562 -391 865 S ATOM 2843 N HIS A 470 6.157 -11.606 -29.636 1.00 74.88 N ANISOU 2843 N HIS A 470 8529 12732 7191 -859 -457 851 N ATOM 2844 CA HIS A 470 6.629 -10.419 -28.919 1.00 75.22 C ANISOU 2844 CA HIS A 470 8641 12686 7251 -683 -475 835 C ATOM 2845 C HIS A 470 5.495 -9.782 -28.107 1.00 80.76 C ANISOU 2845 C HIS A 470 9247 13587 7852 -513 -497 848 C ATOM 2846 O HIS A 470 5.750 -9.183 -27.057 1.00 79.13 O ANISOU 2846 O HIS A 470 9083 13336 7648 -391 -500 832 O ATOM 2847 CB HIS A 470 7.206 -9.385 -29.886 1.00 76.06 C ANISOU 2847 CB HIS A 470 8874 12653 7372 -618 -506 824 C ATOM 2848 CG HIS A 470 8.650 -9.564 -30.207 1.00 78.86 C ANISOU 2848 CG HIS A 470 9341 12799 7825 -717 -483 809 C ATOM 2849 ND1 HIS A 470 9.631 -9.326 -29.263 1.00 80.25 N ANISOU 2849 ND1 HIS A 470 9579 12852 8058 -699 -474 798 N ATOM 2850 CD2 HIS A 470 9.242 -9.829 -31.395 1.00 80.88 C ANISOU 2850 CD2 HIS A 470 9647 12973 8109 -816 -472 809 C ATOM 2851 CE1 HIS A 470 10.784 -9.513 -29.884 1.00 79.36 C ANISOU 2851 CE1 HIS A 470 9535 12611 8007 -793 -455 797 C ATOM 2852 NE2 HIS A 470 10.603 -9.808 -31.171 1.00 80.07 N ANISOU 2852 NE2 HIS A 470 9624 12717 8082 -857 -450 802 N ATOM 2853 N PHE A 471 4.245 -9.902 -28.605 1.00 80.32 N ANISOU 2853 N PHE A 471 9058 13769 7692 -502 -514 878 N ATOM 2854 CA PHE A 471 3.078 -9.365 -27.915 1.00 82.66 C ANISOU 2854 CA PHE A 471 9228 14313 7864 -324 -529 899 C ATOM 2855 C PHE A 471 2.836 -10.165 -26.637 1.00 87.56 C ANISOU 2855 C PHE A 471 9743 15049 8477 -390 -494 913 C ATOM 2856 O PHE A 471 2.609 -9.563 -25.587 1.00 88.98 O ANISOU 2856 O PHE A 471 9906 15292 8610 -217 -492 905 O ATOM 2857 CB PHE A 471 1.813 -9.348 -28.806 1.00 86.13 C ANISOU 2857 CB PHE A 471 9521 15027 8179 -305 -557 940 C ATOM 2858 CG PHE A 471 0.701 -8.527 -28.194 1.00 90.20 C ANISOU 2858 CG PHE A 471 9918 15803 8549 -49 -574 962 C ATOM 2859 CD1 PHE A 471 0.580 -7.171 -28.476 1.00 94.83 C ANISOU 2859 CD1 PHE A 471 10606 16345 9078 222 -611 949 C ATOM 2860 CD2 PHE A 471 -0.187 -9.093 -27.285 1.00 94.44 C ANISOU 2860 CD2 PHE A 471 10258 16628 8998 -67 -552 997 C ATOM 2861 CE1 PHE A 471 -0.416 -6.399 -27.872 1.00 97.52 C ANISOU 2861 CE1 PHE A 471 10860 16922 9272 503 -622 965 C ATOM 2862 CE2 PHE A 471 -1.171 -8.315 -26.664 1.00 99.25 C ANISOU 2862 CE2 PHE A 471 10752 17500 9460 201 -559 1017 C ATOM 2863 CZ PHE A 471 -1.284 -6.976 -26.970 1.00 98.06 C ANISOU 2863 CZ PHE A 471 10709 17300 9250 499 -593 997 C ATOM 2864 N TYR A 472 2.893 -11.513 -26.735 1.00 82.47 N ANISOU 2864 N TYR A 472 9049 14418 7867 -639 -467 934 N ATOM 2865 CA TYR A 472 2.710 -12.454 -25.633 1.00 82.39 C ANISOU 2865 CA TYR A 472 8959 14496 7849 -751 -434 960 C ATOM 2866 C TYR A 472 3.666 -12.125 -24.471 1.00 84.54 C ANISOU 2866 C TYR A 472 9331 14589 8200 -655 -414 929 C ATOM 2867 O TYR A 472 3.219 -12.023 -23.331 1.00 84.72 O ANISOU 2867 O TYR A 472 9271 14753 8165 -572 -402 943 O ATOM 2868 CB TYR A 472 2.937 -13.893 -26.135 1.00 83.50 C ANISOU 2868 CB TYR A 472 9128 14567 8032 -1036 -415 977 C ATOM 2869 CG TYR A 472 2.704 -14.967 -25.098 1.00 85.18 C ANISOU 2869 CG TYR A 472 9285 14857 8224 -1184 -387 1016 C ATOM 2870 CD1 TYR A 472 1.434 -15.495 -24.887 1.00 88.78 C ANISOU 2870 CD1 TYR A 472 9566 15618 8546 -1299 -395 1076 C ATOM 2871 CD2 TYR A 472 3.760 -15.480 -24.345 1.00 84.27 C ANISOU 2871 CD2 TYR A 472 9288 14522 8210 -1221 -354 1003 C ATOM 2872 CE1 TYR A 472 1.209 -16.473 -23.917 1.00 90.71 C ANISOU 2872 CE1 TYR A 472 9771 15935 8760 -1455 -372 1122 C ATOM 2873 CE2 TYR A 472 3.551 -16.474 -23.389 1.00 85.04 C ANISOU 2873 CE2 TYR A 472 9352 14677 8280 -1356 -330 1047 C ATOM 2874 CZ TYR A 472 2.273 -16.963 -23.176 1.00 94.91 C ANISOU 2874 CZ TYR A 472 10445 16218 9399 -1480 -340 1107 C ATOM 2875 OH TYR A 472 2.053 -17.947 -22.248 1.00 99.35 O ANISOU 2875 OH TYR A 472 10986 16837 9925 -1636 -319 1160 O ATOM 2876 N ASP A 473 4.962 -11.925 -24.773 1.00 79.13 N ANISOU 2876 N ASP A 473 8812 13621 7633 -664 -411 891 N ATOM 2877 CA ASP A 473 5.993 -11.598 -23.786 1.00 77.88 C ANISOU 2877 CA ASP A 473 8751 13294 7546 -598 -401 865 C ATOM 2878 C ASP A 473 5.762 -10.221 -23.151 1.00 83.41 C ANISOU 2878 C ASP A 473 9484 14024 8185 -362 -430 837 C ATOM 2879 O ASP A 473 5.948 -10.087 -21.935 1.00 84.15 O ANISOU 2879 O ASP A 473 9581 14121 8270 -297 -421 827 O ATOM 2880 CB ASP A 473 7.387 -11.674 -24.405 1.00 77.73 C ANISOU 2880 CB ASP A 473 8876 13016 7642 -673 -395 842 C ATOM 2881 CG ASP A 473 7.987 -13.069 -24.396 1.00 87.64 C ANISOU 2881 CG ASP A 473 10145 14190 8963 -852 -354 860 C ATOM 2882 OD1 ASP A 473 7.216 -14.054 -24.374 1.00 89.81 O ANISOU 2882 OD1 ASP A 473 10344 14585 9195 -969 -338 891 O ATOM 2883 OD2 ASP A 473 9.222 -13.177 -24.365 1.00 94.47 O ANISOU 2883 OD2 ASP A 473 11102 14881 9910 -873 -339 848 O ATOM 2884 N PHE A 474 5.325 -9.227 -23.948 1.00 79.80 N ANISOU 2884 N PHE A 474 9062 13586 7671 -229 -467 825 N ATOM 2885 CA PHE A 474 5.008 -7.874 -23.481 1.00 80.44 C ANISOU 2885 CA PHE A 474 9215 13678 7670 22 -500 796 C ATOM 2886 C PHE A 474 3.869 -7.920 -22.471 1.00 87.61 C ANISOU 2886 C PHE A 474 9969 14860 8457 151 -484 813 C ATOM 2887 O PHE A 474 3.959 -7.328 -21.393 1.00 88.95 O ANISOU 2887 O PHE A 474 10195 15014 8587 299 -486 783 O ATOM 2888 CB PHE A 474 4.624 -6.953 -24.674 1.00 82.30 C ANISOU 2888 CB PHE A 474 9517 13900 7853 139 -542 795 C ATOM 2889 CG PHE A 474 3.706 -5.790 -24.337 1.00 84.33 C ANISOU 2889 CG PHE A 474 9794 14278 7968 433 -572 784 C ATOM 2890 CD1 PHE A 474 4.205 -4.630 -23.752 1.00 87.14 C ANISOU 2890 CD1 PHE A 474 10359 14447 8301 605 -603 737 C ATOM 2891 CD2 PHE A 474 2.341 -5.860 -24.595 1.00 85.94 C ANISOU 2891 CD2 PHE A 474 9816 14793 8046 543 -570 823 C ATOM 2892 CE1 PHE A 474 3.352 -3.561 -23.436 1.00 88.72 C ANISOU 2892 CE1 PHE A 474 10614 14742 8355 909 -628 722 C ATOM 2893 CE2 PHE A 474 1.490 -4.794 -24.266 1.00 89.27 C ANISOU 2893 CE2 PHE A 474 10254 15347 8319 857 -592 815 C ATOM 2894 CZ PHE A 474 2.005 -3.645 -23.710 1.00 87.33 C ANISOU 2894 CZ PHE A 474 10246 14882 8053 1052 -620 761 C ATOM 2895 N PHE A 475 2.791 -8.608 -22.845 1.00 84.85 N ANISOU 2895 N PHE A 475 9426 14778 8036 88 -470 862 N ATOM 2896 CA PHE A 475 1.560 -8.712 -22.079 1.00 86.42 C ANISOU 2896 CA PHE A 475 9431 15312 8093 192 -454 896 C ATOM 2897 C PHE A 475 1.745 -9.436 -20.740 1.00 88.30 C ANISOU 2897 C PHE A 475 9611 15593 8345 107 -415 907 C ATOM 2898 O PHE A 475 1.078 -9.082 -19.767 1.00 88.67 O ANISOU 2898 O PHE A 475 9570 15841 8280 273 -402 910 O ATOM 2899 CB PHE A 475 0.520 -9.462 -22.925 1.00 89.39 C ANISOU 2899 CB PHE A 475 9608 15960 8395 56 -454 958 C ATOM 2900 CG PHE A 475 -0.893 -9.419 -22.408 1.00 93.98 C ANISOU 2900 CG PHE A 475 9954 16958 8796 176 -444 1008 C ATOM 2901 CD1 PHE A 475 -1.741 -8.368 -22.741 1.00 99.14 C ANISOU 2901 CD1 PHE A 475 10554 17801 9312 458 -469 1011 C ATOM 2902 CD2 PHE A 475 -1.398 -10.455 -21.627 1.00 98.16 C ANISOU 2902 CD2 PHE A 475 10310 17711 9276 5 -411 1061 C ATOM 2903 CE1 PHE A 475 -3.065 -8.341 -22.282 1.00102.44 C ANISOU 2903 CE1 PHE A 475 10725 18655 9543 587 -456 1066 C ATOM 2904 CE2 PHE A 475 -2.725 -10.431 -21.171 1.00103.17 C ANISOU 2904 CE2 PHE A 475 10696 18779 9724 99 -400 1119 C ATOM 2905 CZ PHE A 475 -3.549 -9.374 -21.502 1.00102.51 C ANISOU 2905 CZ PHE A 475 10538 18910 9502 398 -421 1121 C ATOM 2906 N ASN A 476 2.627 -10.449 -20.698 1.00 82.42 N ANISOU 2906 N ASN A 476 8917 14671 7726 -135 -395 914 N ATOM 2907 CA ASN A 476 2.779 -11.322 -19.541 1.00 81.59 C ANISOU 2907 CA ASN A 476 8757 14610 7633 -247 -359 940 C ATOM 2908 C ASN A 476 4.022 -11.044 -18.678 1.00 83.49 C ANISOU 2908 C ASN A 476 9155 14599 7967 -208 -356 896 C ATOM 2909 O ASN A 476 4.153 -11.684 -17.640 1.00 82.29 O ANISOU 2909 O ASN A 476 8963 14489 7816 -274 -329 920 O ATOM 2910 CB ASN A 476 2.815 -12.774 -20.021 1.00 80.09 C ANISOU 2910 CB ASN A 476 8524 14414 7493 -542 -340 991 C ATOM 2911 CG ASN A 476 1.486 -13.290 -20.528 1.00 89.65 C ANISOU 2911 CG ASN A 476 9548 15932 8582 -645 -344 1050 C ATOM 2912 OD1 ASN A 476 0.463 -13.221 -19.841 1.00 87.61 O ANISOU 2912 OD1 ASN A 476 9118 15980 8191 -581 -334 1090 O ATOM 2913 ND2 ASN A 476 1.474 -13.862 -21.723 1.00 76.01 N ANISOU 2913 ND2 ASN A 476 7845 14151 6885 -819 -357 1061 N ATOM 2914 N GLN A 477 4.889 -10.084 -19.061 1.00 79.38 N ANISOU 2914 N GLN A 477 8808 13844 7508 -109 -387 841 N ATOM 2915 CA GLN A 477 6.105 -9.759 -18.310 1.00 77.49 C ANISOU 2915 CA GLN A 477 8714 13387 7343 -96 -394 803 C ATOM 2916 C GLN A 477 5.809 -9.212 -16.907 1.00 81.75 C ANISOU 2916 C GLN A 477 9246 14023 7791 68 -392 781 C ATOM 2917 O GLN A 477 6.586 -9.502 -15.992 1.00 81.78 O ANISOU 2917 O GLN A 477 9292 13941 7840 13 -383 776 O ATOM 2918 CB GLN A 477 6.977 -8.751 -19.077 1.00 77.72 C ANISOU 2918 CB GLN A 477 8927 13176 7426 -47 -436 757 C ATOM 2919 CG GLN A 477 8.396 -8.543 -18.500 1.00 77.33 C ANISOU 2919 CG GLN A 477 9015 12909 7456 -101 -449 731 C ATOM 2920 CD GLN A 477 9.173 -9.826 -18.267 1.00 89.37 C ANISOU 2920 CD GLN A 477 10486 14392 9077 -288 -411 769 C ATOM 2921 OE1 GLN A 477 9.669 -10.089 -17.165 1.00 81.22 O ANISOU 2921 OE1 GLN A 477 9454 13352 8055 -302 -401 773 O ATOM 2922 NE2 GLN A 477 9.265 -10.677 -19.279 1.00 84.56 N ANISOU 2922 NE2 GLN A 477 9841 13760 8529 -423 -389 799 N ATOM 2923 N ALA A 478 4.717 -8.441 -16.721 1.00 79.45 N ANISOU 2923 N ALA A 478 8903 13921 7363 280 -400 768 N ATOM 2924 CA ALA A 478 4.382 -7.882 -15.395 1.00 80.47 C ANISOU 2924 CA ALA A 478 9036 14157 7384 466 -394 739 C ATOM 2925 C ALA A 478 4.083 -8.989 -14.372 1.00 85.49 C ANISOU 2925 C ALA A 478 9503 14981 7997 350 -347 792 C ATOM 2926 O ALA A 478 4.453 -8.859 -13.203 1.00 86.26 O ANISOU 2926 O ALA A 478 9644 15059 8073 399 -340 770 O ATOM 2927 CB ALA A 478 3.202 -6.934 -15.487 1.00 82.68 C ANISOU 2927 CB ALA A 478 9279 14633 7502 741 -404 721 C ATOM 2928 N GLU A 479 3.464 -10.086 -14.825 1.00 82.34 N ANISOU 2928 N GLU A 479 8933 14752 7601 175 -319 864 N ATOM 2929 CA GLU A 479 3.147 -11.214 -13.969 1.00 83.00 C ANISOU 2929 CA GLU A 479 8875 15004 7656 26 -278 929 C ATOM 2930 C GLU A 479 4.366 -12.111 -13.781 1.00 85.44 C ANISOU 2930 C GLU A 479 9283 15071 8109 -179 -271 944 C ATOM 2931 O GLU A 479 4.504 -12.740 -12.720 1.00 86.47 O ANISOU 2931 O GLU A 479 9376 15252 8226 -245 -246 978 O ATOM 2932 CB GLU A 479 1.950 -12.004 -14.506 1.00 85.63 C ANISOU 2932 CB GLU A 479 9004 15623 7907 -100 -260 1006 C ATOM 2933 CG GLU A 479 0.626 -11.300 -14.225 1.00103.33 C ANISOU 2933 CG GLU A 479 11081 18218 9963 120 -253 1015 C ATOM 2934 CD GLU A 479 0.341 -10.915 -12.777 1.00127.45 C ANISOU 2934 CD GLU A 479 14087 21435 12904 295 -227 1004 C ATOM 2935 OE1 GLU A 479 -0.136 -9.778 -12.552 1.00123.59 O ANISOU 2935 OE1 GLU A 479 13608 21049 12300 594 -234 954 O ATOM 2936 OE2 GLU A 479 0.631 -11.726 -11.867 1.00116.63 O ANISOU 2936 OE2 GLU A 479 12689 20073 11553 148 -201 1042 O ATOM 2937 N TRP A 480 5.276 -12.130 -14.757 1.00 78.85 N ANISOU 2937 N TRP A 480 8576 13985 7400 -260 -291 921 N ATOM 2938 CA TRP A 480 6.486 -12.924 -14.599 1.00 78.05 C ANISOU 2938 CA TRP A 480 8565 13670 7420 -413 -281 936 C ATOM 2939 C TRP A 480 7.433 -12.250 -13.589 1.00 82.92 C ANISOU 2939 C TRP A 480 9286 14165 8057 -309 -297 892 C ATOM 2940 O TRP A 480 8.168 -12.952 -12.888 1.00 81.75 O ANISOU 2940 O TRP A 480 9156 13948 7955 -397 -282 921 O ATOM 2941 CB TRP A 480 7.174 -13.185 -15.935 1.00 75.50 C ANISOU 2941 CB TRP A 480 8330 13151 7205 -520 -291 928 C ATOM 2942 CG TRP A 480 6.358 -14.048 -16.856 1.00 77.15 C ANISOU 2942 CG TRP A 480 8458 13461 7393 -665 -277 972 C ATOM 2943 CD1 TRP A 480 5.428 -14.987 -16.502 1.00 81.05 C ANISOU 2943 CD1 TRP A 480 8832 14151 7811 -787 -254 1036 C ATOM 2944 CD2 TRP A 480 6.405 -14.049 -18.294 1.00 76.62 C ANISOU 2944 CD2 TRP A 480 8432 13310 7368 -723 -291 959 C ATOM 2945 NE1 TRP A 480 4.875 -15.556 -17.628 1.00 81.12 N ANISOU 2945 NE1 TRP A 480 8811 14202 7808 -928 -258 1060 N ATOM 2946 CE2 TRP A 480 5.469 -15.012 -18.743 1.00 81.49 C ANISOU 2946 CE2 TRP A 480 8956 14076 7929 -883 -278 1010 C ATOM 2947 CE3 TRP A 480 7.151 -13.331 -19.246 1.00 76.79 C ANISOU 2947 CE3 TRP A 480 8564 13153 7459 -671 -314 912 C ATOM 2948 CZ2 TRP A 480 5.264 -15.280 -20.102 1.00 80.46 C ANISOU 2948 CZ2 TRP A 480 8844 13915 7811 -983 -290 1009 C ATOM 2949 CZ3 TRP A 480 6.955 -13.601 -20.588 1.00 78.49 C ANISOU 2949 CZ3 TRP A 480 8790 13342 7691 -758 -319 915 C ATOM 2950 CH2 TRP A 480 6.010 -14.554 -21.007 1.00 80.09 C ANISOU 2950 CH2 TRP A 480 8901 13691 7837 -906 -308 959 C ATOM 2951 N GLU A 481 7.346 -10.908 -13.461 1.00 80.41 N ANISOU 2951 N GLU A 481 9041 13830 7682 -121 -331 826 N ATOM 2952 CA GLU A 481 8.137 -10.138 -12.512 1.00 80.42 C ANISOU 2952 CA GLU A 481 9162 13722 7673 -29 -358 776 C ATOM 2953 C GLU A 481 7.586 -10.252 -11.095 1.00 85.34 C ANISOU 2953 C GLU A 481 9705 14530 8192 50 -335 786 C ATOM 2954 O GLU A 481 8.400 -10.349 -10.181 1.00 85.56 O ANISOU 2954 O GLU A 481 9786 14484 8239 20 -342 781 O ATOM 2955 CB GLU A 481 8.227 -8.670 -12.922 1.00 82.51 C ANISOU 2955 CB GLU A 481 9580 13871 7898 130 -408 702 C ATOM 2956 CG GLU A 481 9.551 -8.337 -13.595 1.00 95.61 C ANISOU 2956 CG GLU A 481 11389 15274 9664 29 -446 681 C ATOM 2957 CD GLU A 481 9.485 -7.658 -14.954 1.00118.26 C ANISOU 2957 CD GLU A 481 14343 18040 12553 53 -475 661 C ATOM 2958 OE1 GLU A 481 10.512 -7.687 -15.671 1.00104.25 O ANISOU 2958 OE1 GLU A 481 12641 16099 10870 -73 -492 667 O ATOM 2959 OE2 GLU A 481 8.424 -7.087 -15.300 1.00112.42 O ANISOU 2959 OE2 GLU A 481 13591 17399 11724 204 -481 645 O ATOM 2960 N ARG A 482 6.239 -10.258 -10.886 1.00 83.16 N ANISOU 2960 N ARG A 482 9290 14515 7793 148 -309 805 N ATOM 2961 CA ARG A 482 5.717 -10.383 -9.511 1.00 84.09 C ANISOU 2961 CA ARG A 482 9320 14835 7795 224 -281 819 C ATOM 2962 C ARG A 482 5.964 -11.829 -9.000 1.00 84.79 C ANISOU 2962 C ARG A 482 9313 14966 7936 4 -245 906 C ATOM 2963 O ARG A 482 6.278 -12.000 -7.814 1.00 84.56 O ANISOU 2963 O ARG A 482 9287 14968 7874 12 -236 915 O ATOM 2964 CB ARG A 482 4.237 -9.943 -9.351 1.00 85.65 C ANISOU 2964 CB ARG A 482 9379 15342 7823 409 -259 822 C ATOM 2965 CG ARG A 482 3.172 -10.918 -9.835 1.00 99.14 C ANISOU 2965 CG ARG A 482 10869 17311 9490 279 -223 912 C ATOM 2966 CD ARG A 482 2.427 -11.575 -8.680 1.00 99.79 C ANISOU 2966 CD ARG A 482 10775 17690 9451 249 -177 977 C ATOM 2967 NE ARG A 482 1.636 -12.721 -9.124 1.00 93.74 N ANISOU 2967 NE ARG A 482 9828 17130 8661 29 -151 1079 N ATOM 2968 N SER A 483 5.889 -12.839 -9.907 1.00 77.96 N ANISOU 2968 N SER A 483 8397 14078 7147 -188 -231 968 N ATOM 2969 CA SER A 483 6.173 -14.239 -9.585 1.00 76.50 C ANISOU 2969 CA SER A 483 8178 13879 7011 -398 -203 1051 C ATOM 2970 C SER A 483 7.597 -14.392 -9.064 1.00 79.12 C ANISOU 2970 C SER A 483 8637 13985 7440 -427 -215 1040 C ATOM 2971 O SER A 483 7.799 -15.008 -8.012 1.00 78.97 O ANISOU 2971 O SER A 483 8596 14011 7396 -474 -198 1087 O ATOM 2972 CB SER A 483 5.967 -15.137 -10.801 1.00 77.94 C ANISOU 2972 CB SER A 483 8345 14015 7253 -582 -195 1096 C ATOM 2973 OG SER A 483 4.592 -15.377 -11.032 1.00 87.09 O ANISOU 2973 OG SER A 483 9348 15444 8299 -624 -180 1141 O ATOM 2974 N PHE A 484 8.570 -13.807 -9.803 1.00 74.20 N ANISOU 2974 N PHE A 484 8138 13142 6914 -399 -248 984 N ATOM 2975 CA PHE A 484 10.001 -13.803 -9.515 1.00 72.75 C ANISOU 2975 CA PHE A 484 8061 12766 6816 -424 -268 973 C ATOM 2976 C PHE A 484 10.269 -13.095 -8.184 1.00 77.83 C ANISOU 2976 C PHE A 484 8731 13455 7387 -313 -288 937 C ATOM 2977 O PHE A 484 10.943 -13.677 -7.335 1.00 78.19 O ANISOU 2977 O PHE A 484 8778 13484 7447 -365 -282 977 O ATOM 2978 CB PHE A 484 10.784 -13.146 -10.671 1.00 73.47 C ANISOU 2978 CB PHE A 484 8254 12668 6992 -419 -300 923 C ATOM 2979 CG PHE A 484 12.275 -13.052 -10.440 1.00 74.30 C ANISOU 2979 CG PHE A 484 8444 12619 7168 -451 -324 917 C ATOM 2980 CD1 PHE A 484 12.868 -11.840 -10.102 1.00 77.33 C ANISOU 2980 CD1 PHE A 484 8919 12937 7524 -378 -375 854 C ATOM 2981 CD2 PHE A 484 13.076 -14.188 -10.485 1.00 75.51 C ANISOU 2981 CD2 PHE A 484 8591 12707 7393 -553 -299 979 C ATOM 2982 CE1 PHE A 484 14.238 -11.763 -9.837 1.00 77.77 C ANISOU 2982 CE1 PHE A 484 9029 12895 7625 -433 -402 859 C ATOM 2983 CE2 PHE A 484 14.448 -14.107 -10.234 1.00 77.84 C ANISOU 2983 CE2 PHE A 484 8933 12911 7733 -568 -320 985 C ATOM 2984 CZ PHE A 484 15.021 -12.896 -9.914 1.00 76.27 C ANISOU 2984 CZ PHE A 484 8794 12679 7506 -521 -373 928 C ATOM 2985 N ARG A 485 9.706 -11.875 -7.983 1.00 75.29 N ANISOU 2985 N ARG A 485 8439 13193 6974 -152 -312 865 N ATOM 2986 CA ARG A 485 9.838 -11.076 -6.749 1.00 75.60 C ANISOU 2986 CA ARG A 485 8534 13273 6918 -28 -334 814 C ATOM 2987 C ARG A 485 9.360 -11.867 -5.531 1.00 81.78 C ANISOU 2987 C ARG A 485 9200 14249 7625 -45 -294 873 C ATOM 2988 O ARG A 485 10.061 -11.889 -4.523 1.00 83.24 O ANISOU 2988 O ARG A 485 9424 14411 7794 -51 -308 873 O ATOM 2989 CB ARG A 485 9.059 -9.750 -6.859 1.00 75.34 C ANISOU 2989 CB ARG A 485 8567 13284 6777 174 -357 730 C ATOM 2990 CG ARG A 485 9.231 -8.809 -5.663 1.00 87.40 C ANISOU 2990 CG ARG A 485 10204 14815 8191 317 -387 658 C ATOM 2991 CD ARG A 485 8.044 -7.873 -5.458 1.00109.76 C ANISOU 2991 CD ARG A 485 13051 17788 10865 561 -381 598 C ATOM 2992 NE ARG A 485 6.788 -8.597 -5.201 1.00125.99 N ANISOU 2992 NE ARG A 485 14886 20145 12840 598 -317 663 N ATOM 2993 CZ ARG A 485 5.699 -8.530 -5.967 1.00136.58 C ANISOU 2993 CZ ARG A 485 16122 21639 14131 680 -293 679 C ATOM 2994 NH1 ARG A 485 4.620 -9.235 -5.657 1.00120.17 N ANISOU 2994 NH1 ARG A 485 13827 19866 11966 675 -239 750 N ATOM 2995 NH2 ARG A 485 5.676 -7.744 -7.037 1.00122.77 N ANISOU 2995 NH2 ARG A 485 14481 19758 12408 760 -327 632 N ATOM 2996 N ASP A 486 8.186 -12.524 -5.628 1.00 79.20 N ANISOU 2996 N ASP A 486 8727 14124 7241 -69 -248 931 N ATOM 2997 CA ASP A 486 7.610 -13.328 -4.551 1.00 79.87 C ANISOU 2997 CA ASP A 486 8690 14418 7239 -111 -207 1003 C ATOM 2998 C ASP A 486 8.487 -14.526 -4.253 1.00 80.51 C ANISOU 2998 C ASP A 486 8790 14390 7409 -288 -198 1084 C ATOM 2999 O ASP A 486 8.734 -14.802 -3.090 1.00 81.42 O ANISOU 2999 O ASP A 486 8893 14567 7474 -288 -191 1114 O ATOM 3000 CB ASP A 486 6.177 -13.775 -4.886 1.00 84.03 C ANISOU 3000 CB ASP A 486 9051 15199 7678 -139 -167 1059 C ATOM 3001 CG ASP A 486 5.107 -12.704 -4.709 1.00106.82 C ANISOU 3001 CG ASP A 486 11871 18302 10414 86 -161 1001 C ATOM 3002 OD1 ASP A 486 4.067 -12.778 -5.412 1.00111.02 O ANISOU 3002 OD1 ASP A 486 12280 19011 10891 89 -143 1028 O ATOM 3003 OD2 ASP A 486 5.286 -11.813 -3.837 1.00114.49 O ANISOU 3003 OD2 ASP A 486 12914 19280 11306 264 -175 931 O ATOM 3004 N TYR A 487 9.018 -15.181 -5.286 1.00 75.39 N ANISOU 3004 N TYR A 487 8186 13573 6884 -416 -200 1114 N ATOM 3005 CA TYR A 487 9.931 -16.320 -5.175 1.00 74.69 C ANISOU 3005 CA TYR A 487 8146 13351 6881 -550 -191 1188 C ATOM 3006 C TYR A 487 11.254 -15.926 -4.476 1.00 79.89 C ANISOU 3006 C TYR A 487 8886 13895 7575 -493 -224 1161 C ATOM 3007 O TYR A 487 11.737 -16.682 -3.630 1.00 79.93 O ANISOU 3007 O TYR A 487 8891 13905 7572 -539 -215 1227 O ATOM 3008 CB TYR A 487 10.220 -16.895 -6.574 1.00 74.62 C ANISOU 3008 CB TYR A 487 8189 13181 6982 -653 -187 1202 C ATOM 3009 CG TYR A 487 11.356 -17.895 -6.605 1.00 74.49 C ANISOU 3009 CG TYR A 487 8257 12994 7053 -734 -181 1260 C ATOM 3010 CD1 TYR A 487 11.258 -19.115 -5.936 1.00 76.34 C ANISOU 3010 CD1 TYR A 487 8495 13252 7256 -830 -154 1357 C ATOM 3011 CD2 TYR A 487 12.525 -17.631 -7.317 1.00 73.36 C ANISOU 3011 CD2 TYR A 487 8193 12674 7008 -708 -202 1225 C ATOM 3012 CE1 TYR A 487 12.291 -20.042 -5.973 1.00 76.14 C ANISOU 3012 CE1 TYR A 487 8567 13066 7297 -867 -147 1412 C ATOM 3013 CE2 TYR A 487 13.556 -18.562 -7.378 1.00 73.80 C ANISOU 3013 CE2 TYR A 487 8314 12600 7126 -746 -190 1281 C ATOM 3014 CZ TYR A 487 13.444 -19.758 -6.685 1.00 83.23 C ANISOU 3014 CZ TYR A 487 9526 13808 8288 -810 -163 1373 C ATOM 3015 OH TYR A 487 14.464 -20.676 -6.704 1.00 87.47 O ANISOU 3015 OH TYR A 487 10146 14216 8871 -811 -152 1431 O ATOM 3016 N VAL A 488 11.837 -14.761 -4.849 1.00 77.21 N ANISOU 3016 N VAL A 488 8619 13454 7262 -408 -267 1071 N ATOM 3017 CA VAL A 488 13.079 -14.220 -4.283 1.00 76.90 C ANISOU 3017 CA VAL A 488 8655 13324 7238 -380 -312 1040 C ATOM 3018 C VAL A 488 12.868 -13.971 -2.787 1.00 83.30 C ANISOU 3018 C VAL A 488 9444 14274 7932 -313 -317 1034 C ATOM 3019 O VAL A 488 13.632 -14.507 -1.989 1.00 84.62 O ANISOU 3019 O VAL A 488 9607 14443 8101 -353 -323 1086 O ATOM 3020 CB VAL A 488 13.560 -12.936 -5.034 1.00 79.99 C ANISOU 3020 CB VAL A 488 9146 13590 7656 -332 -363 946 C ATOM 3021 CG1 VAL A 488 14.574 -12.141 -4.214 1.00 80.34 C ANISOU 3021 CG1 VAL A 488 9271 13592 7662 -313 -420 903 C ATOM 3022 CG2 VAL A 488 14.135 -13.276 -6.398 1.00 78.26 C ANISOU 3022 CG2 VAL A 488 8948 13231 7555 -413 -359 964 C ATOM 3023 N LEU A 489 11.811 -13.219 -2.407 1.00 81.17 N ANISOU 3023 N LEU A 489 9155 14136 7551 -200 -312 978 N ATOM 3024 CA LEU A 489 11.489 -12.901 -1.002 1.00 82.14 C ANISOU 3024 CA LEU A 489 9260 14409 7539 -112 -312 962 C ATOM 3025 C LEU A 489 11.077 -14.142 -0.195 1.00 85.98 C ANISOU 3025 C LEU A 489 9631 15051 7987 -188 -262 1072 C ATOM 3026 O LEU A 489 11.202 -14.125 1.030 1.00 88.00 O ANISOU 3026 O LEU A 489 9877 15404 8154 -153 -265 1081 O ATOM 3027 CB LEU A 489 10.383 -11.839 -0.906 1.00 83.31 C ANISOU 3027 CB LEU A 489 9416 14675 7562 61 -309 878 C ATOM 3028 CG LEU A 489 10.656 -10.494 -1.614 1.00 88.27 C ANISOU 3028 CG LEU A 489 10200 15142 8199 158 -362 766 C ATOM 3029 CD1 LEU A 489 9.424 -9.620 -1.593 1.00 89.52 C ANISOU 3029 CD1 LEU A 489 10361 15429 8222 360 -348 700 C ATOM 3030 CD2 LEU A 489 11.873 -9.758 -1.022 1.00 90.42 C ANISOU 3030 CD2 LEU A 489 10628 15266 8461 146 -430 706 C ATOM 3031 N CYS A 490 10.598 -15.202 -0.861 1.00 81.60 N ANISOU 3031 N CYS A 490 9006 14512 7486 -303 -222 1155 N ATOM 3032 CA CYS A 490 10.257 -16.477 -0.232 1.00 82.63 C ANISOU 3032 CA CYS A 490 9063 14750 7583 -415 -181 1273 C ATOM 3033 C CYS A 490 11.563 -17.187 0.155 1.00 86.41 C ANISOU 3033 C CYS A 490 9612 15084 8135 -479 -198 1332 C ATOM 3034 O CYS A 490 11.708 -17.654 1.293 1.00 87.28 O ANISOU 3034 O CYS A 490 9703 15280 8179 -491 -191 1392 O ATOM 3035 CB CYS A 490 9.396 -17.333 -1.165 1.00 83.74 C ANISOU 3035 CB CYS A 490 9147 14922 7748 -541 -145 1338 C ATOM 3036 SG CYS A 490 8.968 -18.980 -0.517 1.00 89.16 S ANISOU 3036 SG CYS A 490 9793 15701 8385 -729 -103 1495 S ATOM 3037 N GLN A 491 12.511 -17.254 -0.799 1.00 81.41 N ANISOU 3037 N GLN A 491 9055 14250 7628 -508 -220 1318 N ATOM 3038 CA GLN A 491 13.819 -17.902 -0.643 1.00 80.94 C ANISOU 3038 CA GLN A 491 9051 14065 7638 -541 -235 1374 C ATOM 3039 C GLN A 491 14.729 -17.167 0.342 1.00 85.19 C ANISOU 3039 C GLN A 491 9604 14632 8132 -469 -281 1337 C ATOM 3040 O GLN A 491 15.537 -17.808 1.012 1.00 85.33 O ANISOU 3040 O GLN A 491 9627 14647 8148 -483 -288 1408 O ATOM 3041 CB GLN A 491 14.534 -17.997 -2.006 1.00 80.85 C ANISOU 3041 CB GLN A 491 9098 13871 7752 -568 -242 1357 C ATOM 3042 CG GLN A 491 14.015 -19.095 -2.922 1.00 83.63 C ANISOU 3042 CG GLN A 491 9472 14151 8154 -663 -200 1418 C ATOM 3043 CD GLN A 491 14.490 -20.471 -2.528 1.00101.43 C ANISOU 3043 CD GLN A 491 11780 16343 10415 -714 -177 1531 C ATOM 3044 OE1 GLN A 491 13.739 -21.290 -1.988 1.00101.86 O ANISOU 3044 OE1 GLN A 491 11832 16465 10405 -791 -150 1608 O ATOM 3045 NE2 GLN A 491 15.744 -20.765 -2.804 1.00 89.46 N ANISOU 3045 NE2 GLN A 491 10320 14706 8965 -672 -188 1551 N ATOM 3046 N ALA A 492 14.631 -15.829 0.393 1.00 82.26 N ANISOU 3046 N ALA A 492 9257 14281 7718 -395 -319 1226 N ATOM 3047 CA ALA A 492 15.457 -14.985 1.252 1.00 82.80 C ANISOU 3047 CA ALA A 492 9367 14364 7728 -350 -375 1174 C ATOM 3048 C ALA A 492 14.943 -14.990 2.704 1.00 90.29 C ANISOU 3048 C ALA A 492 10280 15485 8541 -302 -367 1186 C ATOM 3049 O ALA A 492 15.685 -14.603 3.603 1.00 89.70 O ANISOU 3049 O ALA A 492 10235 15440 8406 -287 -411 1169 O ATOM 3050 CB ALA A 492 15.505 -13.568 0.698 1.00 83.23 C ANISOU 3050 CB ALA A 492 9509 14341 7775 -302 -423 1050 C ATOM 3051 N ASN A 493 13.700 -15.468 2.931 1.00 90.73 N ANISOU 3051 N ASN A 493 10265 15673 8537 -291 -311 1224 N ATOM 3052 CA ASN A 493 13.070 -15.624 4.250 1.00 93.58 C ANISOU 3052 CA ASN A 493 10568 16230 8758 -253 -289 1253 C ATOM 3053 C ASN A 493 13.615 -16.908 4.917 1.00101.15 C ANISOU 3053 C ASN A 493 11499 17205 9728 -342 -274 1388 C ATOM 3054 O ASN A 493 12.885 -17.880 5.126 1.00100.53 O ANISOU 3054 O ASN A 493 11364 17216 9619 -408 -225 1485 O ATOM 3055 CB ASN A 493 11.534 -15.659 4.109 1.00 96.86 C ANISOU 3055 CB ASN A 493 10896 16812 9096 -222 -233 1255 C ATOM 3056 CG ASN A 493 10.815 -14.444 4.647 1.00129.07 C ANISOU 3056 CG ASN A 493 14980 21028 13034 -60 -238 1146 C ATOM 3057 OD1 ASN A 493 11.025 -14.010 5.789 1.00124.13 O ANISOU 3057 OD1 ASN A 493 14382 20484 12299 12 -257 1113 O ATOM 3058 ND2 ASN A 493 9.885 -13.915 3.861 1.00122.86 N ANISOU 3058 ND2 ASN A 493 14168 20285 12231 15 -219 1093 N ATOM 3059 N VAL A 494 14.923 -16.896 5.219 1.00101.31 N ANISOU 3059 N VAL A 494 11565 17142 9785 -348 -321 1399 N ATOM 3060 CA VAL A 494 15.695 -18.000 5.790 1.00103.13 C ANISOU 3060 CA VAL A 494 11789 17368 10029 -395 -320 1522 C ATOM 3061 C VAL A 494 15.749 -17.896 7.334 1.00110.85 C ANISOU 3061 C VAL A 494 12741 18511 10867 -361 -335 1543 C ATOM 3062 O VAL A 494 15.790 -16.794 7.895 1.00110.81 O ANISOU 3062 O VAL A 494 12754 18572 10778 -298 -374 1441 O ATOM 3063 CB VAL A 494 17.127 -18.044 5.163 1.00106.79 C ANISOU 3063 CB VAL A 494 12291 17686 10598 -404 -361 1530 C ATOM 3064 CG1 VAL A 494 17.913 -16.751 5.406 1.00106.42 C ANISOU 3064 CG1 VAL A 494 12271 17647 10518 -374 -433 1425 C ATOM 3065 CG2 VAL A 494 17.917 -19.270 5.620 1.00107.30 C ANISOU 3065 CG2 VAL A 494 12355 17742 10674 -416 -354 1667 C ATOM 3066 N THR A 495 15.752 -19.072 7.997 1.00109.88 N ANISOU 3066 N THR A 495 12597 18441 10713 -404 -307 1678 N ATOM 3067 CA THR A 495 15.830 -19.221 9.445 1.00111.82 C ANISOU 3067 CA THR A 495 12815 18845 10827 -383 -317 1728 C ATOM 3068 C THR A 495 17.222 -18.809 9.924 1.00117.96 C ANISOU 3068 C THR A 495 13613 19607 11600 -347 -387 1710 C ATOM 3069 O THR A 495 18.229 -19.271 9.380 1.00117.52 O ANISOU 3069 O THR A 495 13575 19439 11638 -358 -407 1762 O ATOM 3070 CB THR A 495 15.492 -20.661 9.849 1.00120.79 C ANISOU 3070 CB THR A 495 13946 20009 11940 -455 -271 1891 C ATOM 3071 N ILE A 496 17.265 -17.912 10.923 1.00116.01 N ANISOU 3071 N ILE A 496 13364 19487 11229 -304 -425 1634 N ATOM 3072 CA ILE A 496 18.496 -17.385 11.515 1.00116.19 C ANISOU 3072 CA ILE A 496 13402 19534 11209 -296 -503 1608 C ATOM 3073 C ILE A 496 18.702 -18.001 12.900 1.00120.00 C ANISOU 3073 C ILE A 496 13848 20174 11572 -288 -508 1709 C ATOM 3074 O ILE A 496 17.767 -18.082 13.707 1.00120.43 O ANISOU 3074 O ILE A 496 13882 20360 11514 -269 -471 1718 O ATOM 3075 CB ILE A 496 18.529 -15.825 11.564 1.00119.88 C ANISOU 3075 CB ILE A 496 13938 19998 11612 -271 -560 1437 C ATOM 3076 CG1 ILE A 496 17.135 -15.190 11.852 1.00121.35 C ANISOU 3076 CG1 ILE A 496 14147 20262 11697 -196 -519 1344 C ATOM 3077 CG2 ILE A 496 19.116 -15.263 10.272 1.00119.44 C ANISOU 3077 CG2 ILE A 496 13928 19773 11681 -307 -594 1372 C ATOM 3078 CD1 ILE A 496 16.776 -14.957 13.345 1.00133.69 C ANISOU 3078 CD1 ILE A 496 15706 22018 13072 -142 -522 1329 C ATOM 3079 N GLY A 497 19.928 -18.456 13.139 1.00115.90 N ANISOU 3079 N GLY A 497 13310 19657 11069 -297 -553 1792 N ATOM 3080 CA GLY A 497 20.325 -19.084 14.394 1.00116.33 C ANISOU 3080 CA GLY A 497 13330 19855 11014 -282 -568 1902 C ATOM 3081 C GLY A 497 20.098 -20.581 14.426 1.00118.95 C ANISOU 3081 C GLY A 497 13661 20156 11379 -280 -509 2073 C ATOM 3082 O GLY A 497 19.939 -21.217 13.376 1.00117.63 O ANISOU 3082 O GLY A 497 13526 19836 11334 -293 -467 2114 O ATOM 3083 N LEU A 498 20.105 -21.152 15.645 1.00115.78 N ANISOU 3083 N LEU A 498 13242 19892 10856 -268 -510 2176 N ATOM 3084 CA LEU A 498 19.933 -22.582 15.903 1.00116.03 C ANISOU 3084 CA LEU A 498 13305 19897 10883 -273 -464 2354 C ATOM 3085 C LEU A 498 18.570 -23.098 15.369 1.00119.32 C ANISOU 3085 C LEU A 498 13758 20246 11333 -346 -385 2375 C ATOM 3086 O LEU A 498 17.567 -22.367 15.414 1.00118.75 O ANISOU 3086 O LEU A 498 13648 20259 11214 -373 -360 2274 O ATOM 3087 CB LEU A 498 20.079 -22.899 17.406 1.00117.53 C ANISOU 3087 CB LEU A 498 13471 20272 10912 -256 -484 2447 C ATOM 3088 CG LEU A 498 21.503 -22.914 18.027 1.00123.07 C ANISOU 3088 CG LEU A 498 14138 21058 11565 -190 -560 2502 C ATOM 3089 CD1 LEU A 498 22.448 -23.887 17.307 1.00122.96 C ANISOU 3089 CD1 LEU A 498 14157 20907 11656 -123 -561 2622 C ATOM 3090 CD2 LEU A 498 22.103 -21.514 18.152 1.00125.90 C ANISOU 3090 CD2 LEU A 498 14444 21504 11887 -196 -634 2345 C ATOM 3091 N PRO A 499 18.534 -24.344 14.824 1.00114.55 N ANISOU 3091 N PRO A 499 13235 19491 10798 -376 -348 2505 N ATOM 3092 CA PRO A 499 17.283 -24.841 14.230 1.00113.05 C ANISOU 3092 CA PRO A 499 13083 19238 10633 -482 -284 2528 C ATOM 3093 C PRO A 499 16.153 -25.112 15.230 1.00114.75 C ANISOU 3093 C PRO A 499 13263 19637 10698 -567 -245 2593 C ATOM 3094 O PRO A 499 16.262 -25.914 16.164 1.00115.47 O ANISOU 3094 O PRO A 499 13393 19788 10695 -586 -244 2732 O ATOM 3095 CB PRO A 499 17.702 -26.145 13.540 1.00115.26 C ANISOU 3095 CB PRO A 499 13498 19297 10997 -494 -267 2657 C ATOM 3096 CG PRO A 499 18.946 -26.567 14.231 1.00120.90 C ANISOU 3096 CG PRO A 499 14237 20022 11676 -381 -310 2751 C ATOM 3097 CD PRO A 499 19.642 -25.308 14.634 1.00116.15 C ANISOU 3097 CD PRO A 499 13509 19569 11051 -307 -367 2630 C ATOM 3098 N THR A 500 15.043 -24.404 14.994 1.00108.24 N ANISOU 3098 N THR A 500 12361 18919 9845 -610 -212 2492 N ATOM 3099 CA THR A 500 13.755 -24.566 15.668 1.00106.81 C ANISOU 3099 CA THR A 500 12114 18947 9522 -698 -161 2539 C ATOM 3100 C THR A 500 12.961 -25.502 14.745 1.00104.64 C ANISOU 3100 C THR A 500 11895 18560 9303 -851 -116 2623 C ATOM 3101 O THR A 500 13.414 -25.762 13.626 1.00105.72 O ANISOU 3101 O THR A 500 12116 18466 9585 -853 -127 2606 O ATOM 3102 CB THR A 500 13.095 -23.196 15.959 1.00114.33 C ANISOU 3102 CB THR A 500 12948 20103 10389 -618 -155 2378 C ATOM 3103 OG1 THR A 500 13.080 -22.401 14.767 1.00111.59 O ANISOU 3103 OG1 THR A 500 12602 19634 10165 -572 -163 2237 O ATOM 3104 CG2 THR A 500 13.798 -22.434 17.095 1.00111.89 C ANISOU 3104 CG2 THR A 500 12618 19916 9980 -502 -202 2316 C ATOM 3105 N LYS A 501 11.816 -26.018 15.164 1.00 95.38 N ANISOU 3105 N LYS A 501 10680 17552 8010 -989 -70 2715 N ATOM 3106 CA LYS A 501 11.090 -26.929 14.285 1.00 92.79 C ANISOU 3106 CA LYS A 501 10419 17117 7720 -1171 -38 2800 C ATOM 3107 C LYS A 501 10.327 -26.105 13.221 1.00 93.79 C ANISOU 3107 C LYS A 501 10444 17285 7905 -1170 -18 2662 C ATOM 3108 O LYS A 501 9.116 -25.899 13.320 1.00 93.71 O ANISOU 3108 O LYS A 501 10306 17511 7788 -1250 22 2662 O ATOM 3109 CB LYS A 501 10.173 -27.869 15.094 1.00 95.21 C ANISOU 3109 CB LYS A 501 10724 17589 7863 -1362 -2 2970 C ATOM 3110 CG LYS A 501 10.960 -28.850 15.967 1.00 82.68 C ANISOU 3110 CG LYS A 501 9284 15901 6231 -1371 -26 3126 C ATOM 3111 CD LYS A 501 10.084 -29.712 16.843 1.00 84.43 C ANISOU 3111 CD LYS A 501 9512 16293 6274 -1570 5 3300 C ATOM 3112 CE LYS A 501 10.897 -30.766 17.549 1.00 82.17 C ANISOU 3112 CE LYS A 501 9415 15853 5954 -1575 -22 3464 C ATOM 3113 NZ LYS A 501 10.054 -31.709 18.326 1.00 79.45 N ANISOU 3113 NZ LYS A 501 9114 15638 5434 -1802 4 3652 N ATOM 3114 N GLN A 502 11.081 -25.591 12.225 1.00 88.01 N ANISOU 3114 N GLN A 502 9761 16346 7334 -1064 -48 2548 N ATOM 3115 CA GLN A 502 10.560 -24.803 11.103 1.00 86.82 C ANISOU 3115 CA GLN A 502 9545 16185 7259 -1042 -39 2417 C ATOM 3116 C GLN A 502 10.300 -25.703 9.894 1.00 91.10 C ANISOU 3116 C GLN A 502 10188 16530 7894 -1195 -27 2475 C ATOM 3117 O GLN A 502 11.124 -26.578 9.615 1.00 91.12 O ANISOU 3117 O GLN A 502 10353 16292 7976 -1219 -44 2550 O ATOM 3118 CB GLN A 502 11.518 -23.659 10.708 1.00 86.15 C ANISOU 3118 CB GLN A 502 9463 15992 7279 -857 -82 2259 C ATOM 3119 CG GLN A 502 11.587 -22.504 11.709 1.00106.10 C ANISOU 3119 CG GLN A 502 11903 18711 9701 -713 -99 2159 C ATOM 3120 CD GLN A 502 10.261 -21.810 11.979 1.00129.19 C ANISOU 3120 CD GLN A 502 14693 21901 12492 -688 -58 2099 C ATOM 3121 OE1 GLN A 502 9.482 -21.484 11.065 1.00125.12 O ANISOU 3121 OE1 GLN A 502 14127 21408 12005 -701 -35 2043 O ATOM 3122 NE2 GLN A 502 9.996 -21.538 13.254 1.00116.54 N ANISOU 3122 NE2 GLN A 502 13025 20525 10728 -633 -47 2108 N ATOM 3123 N PRO A 503 9.174 -25.532 9.161 1.00 87.66 N ANISOU 3123 N PRO A 503 9669 16198 7440 -1294 2 2445 N ATOM 3124 CA PRO A 503 8.944 -26.385 7.979 1.00 87.41 C ANISOU 3124 CA PRO A 503 9750 15973 7490 -1456 6 2494 C ATOM 3125 C PRO A 503 9.952 -26.088 6.870 1.00 89.96 C ANISOU 3125 C PRO A 503 10172 16016 7992 -1341 -23 2396 C ATOM 3126 O PRO A 503 10.536 -25.000 6.835 1.00 88.46 O ANISOU 3126 O PRO A 503 9921 15831 7857 -1160 -44 2271 O ATOM 3127 CB PRO A 503 7.515 -26.041 7.555 1.00 88.98 C ANISOU 3127 CB PRO A 503 9789 16414 7606 -1564 37 2471 C ATOM 3128 CG PRO A 503 7.287 -24.678 8.065 1.00 92.71 C ANISOU 3128 CG PRO A 503 10088 17117 8020 -1364 43 2348 C ATOM 3129 CD PRO A 503 8.079 -24.555 9.339 1.00 89.02 C ANISOU 3129 CD PRO A 503 9645 16671 7506 -1247 29 2364 C ATOM 3130 N ILE A 504 10.170 -27.074 5.986 1.00 86.39 N ANISOU 3130 N ILE A 504 9888 15320 7616 -1452 -25 2455 N ATOM 3131 CA ILE A 504 11.112 -26.977 4.867 1.00 84.09 C ANISOU 3131 CA ILE A 504 9701 14767 7481 -1355 -44 2380 C ATOM 3132 C ILE A 504 10.636 -25.883 3.909 1.00 88.99 C ANISOU 3132 C ILE A 504 10199 15453 8160 -1311 -44 2239 C ATOM 3133 O ILE A 504 9.429 -25.765 3.686 1.00 88.93 O ANISOU 3133 O ILE A 504 10091 15615 8081 -1428 -24 2238 O ATOM 3134 CB ILE A 504 11.343 -28.335 4.139 1.00 86.51 C ANISOU 3134 CB ILE A 504 10240 14800 7831 -1477 -42 2475 C ATOM 3135 CG1 ILE A 504 10.031 -28.924 3.543 1.00 86.74 C ANISOU 3135 CG1 ILE A 504 10291 14871 7796 -1733 -24 2524 C ATOM 3136 CG2 ILE A 504 12.084 -29.321 5.069 1.00 87.69 C ANISOU 3136 CG2 ILE A 504 10544 14841 7933 -1451 -49 2608 C ATOM 3137 CD1 ILE A 504 10.165 -30.128 2.685 1.00 89.51 C ANISOU 3137 CD1 ILE A 504 10895 14936 8178 -1867 -28 2590 C ATOM 3138 N PRO A 505 11.565 -25.044 3.373 1.00 86.21 N ANISOU 3138 N PRO A 505 9843 14993 7921 -1145 -68 2126 N ATOM 3139 CA PRO A 505 11.144 -23.969 2.458 1.00 85.14 C ANISOU 3139 CA PRO A 505 9614 14901 7833 -1096 -72 1996 C ATOM 3140 C PRO A 505 10.311 -24.504 1.308 1.00 91.51 C ANISOU 3140 C PRO A 505 10454 15655 8662 -1251 -54 2012 C ATOM 3141 O PRO A 505 10.580 -25.603 0.815 1.00 92.65 O ANISOU 3141 O PRO A 505 10753 15606 8845 -1355 -50 2085 O ATOM 3142 CB PRO A 505 12.463 -23.376 1.962 1.00 85.31 C ANISOU 3142 CB PRO A 505 9686 14753 7977 -948 -103 1913 C ATOM 3143 CG PRO A 505 13.510 -24.359 2.334 1.00 90.13 C ANISOU 3143 CG PRO A 505 10418 15215 8611 -931 -109 2008 C ATOM 3144 CD PRO A 505 13.030 -25.034 3.562 1.00 87.04 C ANISOU 3144 CD PRO A 505 10024 14949 8099 -1002 -95 2120 C ATOM 3145 N ASP A 506 9.258 -23.755 0.940 1.00 87.90 N ANISOU 3145 N ASP A 506 9858 15380 8159 -1264 -44 1949 N ATOM 3146 CA ASP A 506 8.344 -24.113 -0.134 1.00 88.32 C ANISOU 3146 CA ASP A 506 9904 15442 8210 -1417 -33 1958 C ATOM 3147 C ASP A 506 8.216 -22.924 -1.105 1.00 91.63 C ANISOU 3147 C ASP A 506 10247 15876 8693 -1295 -45 1825 C ATOM 3148 O ASP A 506 7.215 -22.200 -1.071 1.00 92.82 O ANISOU 3148 O ASP A 506 10246 16263 8760 -1264 -36 1787 O ATOM 3149 CB ASP A 506 6.983 -24.522 0.466 1.00 91.74 C ANISOU 3149 CB ASP A 506 10218 16157 8482 -1582 -8 2049 C ATOM 3150 CG ASP A 506 6.004 -25.197 -0.477 1.00103.99 C ANISOU 3150 CG ASP A 506 11772 17742 9997 -1811 -3 2099 C ATOM 3151 OD1 ASP A 506 6.397 -25.509 -1.628 1.00105.39 O ANISOU 3151 OD1 ASP A 506 12079 17684 10280 -1854 -17 2068 O ATOM 3152 OD2 ASP A 506 4.858 -25.448 -0.054 1.00110.09 O ANISOU 3152 OD2 ASP A 506 12416 18789 10623 -1960 15 2175 O ATOM 3153 N CYS A 507 9.249 -22.711 -1.948 1.00 85.10 N ANISOU 3153 N CYS A 507 9525 14807 8002 -1214 -65 1760 N ATOM 3154 CA CYS A 507 9.300 -21.593 -2.897 1.00 83.35 C ANISOU 3154 CA CYS A 507 9264 14559 7846 -1103 -82 1641 C ATOM 3155 C CYS A 507 9.391 -22.109 -4.328 1.00 84.41 C ANISOU 3155 C CYS A 507 9492 14512 8070 -1197 -83 1635 C ATOM 3156 O CYS A 507 10.160 -23.023 -4.620 1.00 82.95 O ANISOU 3156 O CYS A 507 9449 14120 7947 -1248 -80 1681 O ATOM 3157 CB CYS A 507 10.471 -20.658 -2.588 1.00 83.31 C ANISOU 3157 CB CYS A 507 9287 14464 7904 -925 -111 1561 C ATOM 3158 SG CYS A 507 10.612 -20.159 -0.845 1.00 88.31 S ANISOU 3158 SG CYS A 507 9855 15268 8430 -820 -118 1566 S ATOM 3159 N GLU A 508 8.636 -21.488 -5.226 1.00 80.53 N ANISOU 3159 N GLU A 508 8926 14099 7574 -1199 -87 1575 N ATOM 3160 CA GLU A 508 8.640 -21.828 -6.645 1.00 80.25 C ANISOU 3160 CA GLU A 508 8965 13914 7610 -1282 -90 1556 C ATOM 3161 C GLU A 508 8.174 -20.645 -7.457 1.00 83.41 C ANISOU 3161 C GLU A 508 9275 14396 8020 -1187 -105 1461 C ATOM 3162 O GLU A 508 7.320 -19.896 -6.981 1.00 84.65 O ANISOU 3162 O GLU A 508 9297 14783 8085 -1115 -104 1440 O ATOM 3163 CB GLU A 508 7.740 -23.049 -6.923 1.00 82.87 C ANISOU 3163 CB GLU A 508 9329 14284 7874 -1520 -76 1648 C ATOM 3164 N ILE A 509 8.728 -20.457 -8.670 1.00 77.18 N ANISOU 3164 N ILE A 509 8565 13428 7330 -1168 -117 1407 N ATOM 3165 CA ILE A 509 8.244 -19.403 -9.572 1.00 75.55 C ANISOU 3165 CA ILE A 509 8294 13283 7129 -1091 -134 1328 C ATOM 3166 C ILE A 509 6.928 -19.907 -10.137 1.00 82.21 C ANISOU 3166 C ILE A 509 9057 14288 7890 -1242 -126 1371 C ATOM 3167 O ILE A 509 6.930 -20.927 -10.827 1.00 82.27 O ANISOU 3167 O ILE A 509 9153 14183 7922 -1410 -121 1412 O ATOM 3168 CB ILE A 509 9.242 -18.996 -10.683 1.00 75.86 C ANISOU 3168 CB ILE A 509 8435 13101 7287 -1033 -151 1262 C ATOM 3169 CG1 ILE A 509 10.673 -18.834 -10.115 1.00 74.76 C ANISOU 3169 CG1 ILE A 509 8374 12814 7218 -941 -159 1249 C ATOM 3170 CG2 ILE A 509 8.740 -17.724 -11.389 1.00 74.26 C ANISOU 3170 CG2 ILE A 509 8172 12972 7071 -926 -174 1184 C ATOM 3171 CD1 ILE A 509 11.776 -18.795 -11.094 1.00 68.80 C ANISOU 3171 CD1 ILE A 509 7713 11863 6565 -921 -166 1217 C ATOM 3172 N LYS A 510 5.808 -19.246 -9.779 1.00 80.62 N ANISOU 3172 N LYS A 510 8693 14364 7576 -1185 -125 1366 N ATOM 3173 CA LYS A 510 4.455 -19.631 -10.193 1.00 82.09 C ANISOU 3173 CA LYS A 510 8753 14787 7652 -1327 -120 1418 C ATOM 3174 C LYS A 510 4.350 -19.641 -11.707 1.00 87.90 C ANISOU 3174 C LYS A 510 9531 15428 8440 -1392 -139 1385 C ATOM 3175 O LYS A 510 4.179 -20.708 -12.307 1.00 89.51 O ANISOU 3175 O LYS A 510 9802 15564 8644 -1611 -139 1436 O ATOM 3176 CB LYS A 510 3.372 -18.691 -9.599 1.00 85.29 C ANISOU 3176 CB LYS A 510 8957 15532 7917 -1180 -113 1407 C ATOM 3177 CG LYS A 510 3.432 -18.476 -8.081 1.00105.44 C ANISOU 3177 CG LYS A 510 11460 18204 10399 -1076 -94 1423 C ATOM 3178 CD LYS A 510 3.927 -17.060 -7.673 1.00113.49 C ANISOU 3178 CD LYS A 510 12508 19180 11434 -786 -107 1317 C ATOM 3179 CE LYS A 510 2.870 -15.983 -7.864 1.00121.07 C ANISOU 3179 CE LYS A 510 13332 20395 12273 -597 -108 1273 C ATOM 3180 NZ LYS A 510 3.251 -14.690 -7.236 1.00121.32 N ANISOU 3180 NZ LYS A 510 13426 20387 12282 -323 -121 1177 N ATOM 3181 N ASN A 511 4.496 -18.452 -12.318 1.00 82.85 N ANISOU 3181 N ASN A 511 8877 14764 7838 -1204 -157 1299 N ATOM 3182 CA ASN A 511 4.365 -18.238 -13.752 1.00 81.70 C ANISOU 3182 CA ASN A 511 8756 14553 7732 -1229 -177 1262 C ATOM 3183 C ASN A 511 5.646 -17.725 -14.294 1.00 83.25 C ANISOU 3183 C ASN A 511 9103 14462 8064 -1122 -189 1190 C ATOM 3184 O ASN A 511 6.175 -16.738 -13.786 1.00 83.04 O ANISOU 3184 O ASN A 511 9095 14394 8061 -939 -199 1138 O ATOM 3185 CB ASN A 511 3.220 -17.254 -14.037 1.00 83.50 C ANISOU 3185 CB ASN A 511 8817 15057 7850 -1102 -190 1242 C ATOM 3186 CG ASN A 511 1.903 -17.682 -13.436 1.00 98.42 C ANISOU 3186 CG ASN A 511 10514 17303 9577 -1196 -175 1322 C ATOM 3187 OD1 ASN A 511 1.519 -18.852 -13.512 1.00 93.55 O ANISOU 3187 OD1 ASN A 511 9886 16736 8922 -1454 -169 1399 O ATOM 3188 ND2 ASN A 511 1.213 -16.759 -12.777 1.00 84.85 N ANISOU 3188 ND2 ASN A 511 8651 15841 7747 -991 -168 1308 N ATOM 3189 N ARG A 512 6.169 -18.396 -15.312 1.00 78.39 N ANISOU 3189 N ARG A 512 8603 13654 7528 -1242 -190 1189 N ATOM 3190 CA ARG A 512 7.437 -18.001 -15.905 1.00 76.67 C ANISOU 3190 CA ARG A 512 8514 13187 7430 -1157 -197 1132 C ATOM 3191 C ARG A 512 7.345 -18.012 -17.435 1.00 80.75 C ANISOU 3191 C ARG A 512 9074 13631 7977 -1216 -208 1104 C ATOM 3192 O ARG A 512 6.448 -18.676 -17.972 1.00 82.09 O ANISOU 3192 O ARG A 512 9207 13899 8084 -1367 -209 1138 O ATOM 3193 CB ARG A 512 8.558 -18.917 -15.403 1.00 75.42 C ANISOU 3193 CB ARG A 512 8477 12838 7340 -1205 -175 1162 C ATOM 3194 CG ARG A 512 8.453 -20.356 -15.844 1.00 82.99 C ANISOU 3194 CG ARG A 512 9532 13707 8294 -1395 -157 1215 C ATOM 3195 CD ARG A 512 9.477 -21.189 -15.112 1.00 87.00 C ANISOU 3195 CD ARG A 512 10157 14054 8845 -1392 -135 1255 C ATOM 3196 NE ARG A 512 9.553 -22.534 -15.676 1.00 92.69 N ANISOU 3196 NE ARG A 512 11032 14623 9561 -1544 -119 1294 N ATOM 3197 CZ ARG A 512 10.335 -22.879 -16.690 1.00104.81 C ANISOU 3197 CZ ARG A 512 12701 15964 11157 -1529 -109 1262 C ATOM 3198 NH1 ARG A 512 11.120 -21.981 -17.269 1.00 98.69 N ANISOU 3198 NH1 ARG A 512 11902 15139 10456 -1389 -113 1200 N ATOM 3199 NH2 ARG A 512 10.339 -24.127 -17.133 1.00 91.66 N ANISOU 3199 NH2 ARG A 512 11207 14151 9467 -1657 -96 1294 N ATOM 3200 N PRO A 513 8.257 -17.299 -18.153 1.00 75.41 N ANISOU 3200 N PRO A 513 8475 12794 7384 -1118 -220 1047 N ATOM 3201 CA PRO A 513 8.204 -17.290 -19.632 1.00 74.31 C ANISOU 3201 CA PRO A 513 8378 12589 7267 -1170 -229 1021 C ATOM 3202 C PRO A 513 8.073 -18.670 -20.292 1.00 78.69 C ANISOU 3202 C PRO A 513 9009 13072 7816 -1363 -211 1054 C ATOM 3203 O PRO A 513 8.491 -19.703 -19.752 1.00 77.83 O ANISOU 3203 O PRO A 513 8982 12868 7721 -1441 -187 1091 O ATOM 3204 CB PRO A 513 9.542 -16.668 -20.029 1.00 74.63 C ANISOU 3204 CB PRO A 513 8514 12439 7402 -1072 -233 977 C ATOM 3205 CG PRO A 513 9.897 -15.786 -18.911 1.00 79.19 C ANISOU 3205 CG PRO A 513 9066 13043 7978 -939 -246 962 C ATOM 3206 CD PRO A 513 9.354 -16.436 -17.659 1.00 75.74 C ANISOU 3206 CD PRO A 513 8565 12727 7487 -974 -229 1009 C ATOM 3207 N SER A 514 7.455 -18.664 -21.472 1.00 77.06 N ANISOU 3207 N SER A 514 8793 12909 7578 -1437 -227 1040 N ATOM 3208 CA SER A 514 7.252 -19.848 -22.293 1.00 78.10 C ANISOU 3208 CA SER A 514 9020 12967 7686 -1629 -220 1056 C ATOM 3209 C SER A 514 8.411 -19.955 -23.307 1.00 83.39 C ANISOU 3209 C SER A 514 9838 13405 8442 -1590 -204 1010 C ATOM 3210 O SER A 514 8.615 -19.068 -24.143 1.00 81.63 O ANISOU 3210 O SER A 514 9595 13176 8247 -1505 -218 968 O ATOM 3211 CB SER A 514 5.885 -19.799 -22.978 1.00 81.66 C ANISOU 3211 CB SER A 514 9363 13631 8033 -1746 -251 1071 C ATOM 3212 OG SER A 514 5.694 -20.841 -23.922 1.00 90.26 O ANISOU 3212 OG SER A 514 10566 14640 9090 -1947 -255 1076 O ATOM 3213 N LEU A 515 9.187 -21.037 -23.175 1.00 81.62 N ANISOU 3213 N LEU A 515 9766 12999 8248 -1639 -173 1024 N ATOM 3214 CA LEU A 515 10.314 -21.401 -24.025 1.00 81.66 C ANISOU 3214 CA LEU A 515 9918 12798 8310 -1596 -146 990 C ATOM 3215 C LEU A 515 9.805 -21.724 -25.428 1.00 86.27 C ANISOU 3215 C LEU A 515 10566 13362 8849 -1715 -157 960 C ATOM 3216 O LEU A 515 10.485 -21.417 -26.409 1.00 86.07 O ANISOU 3216 O LEU A 515 10591 13250 8861 -1647 -146 917 O ATOM 3217 CB LEU A 515 11.019 -22.620 -23.383 1.00 82.79 C ANISOU 3217 CB LEU A 515 10214 12781 8461 -1609 -110 1023 C ATOM 3218 CG LEU A 515 12.509 -22.920 -23.666 1.00 88.16 C ANISOU 3218 CG LEU A 515 11014 13280 9202 -1472 -70 1006 C ATOM 3219 CD1 LEU A 515 12.721 -23.591 -24.987 1.00 88.79 C ANISOU 3219 CD1 LEU A 515 11252 13224 9259 -1516 -51 968 C ATOM 3220 CD2 LEU A 515 13.429 -21.729 -23.399 1.00 90.01 C ANISOU 3220 CD2 LEU A 515 11127 13564 9507 -1303 -70 989 C ATOM 3221 N LEU A 516 8.590 -22.321 -25.519 1.00 83.10 N ANISOU 3221 N LEU A 516 10155 13063 8355 -1905 -182 987 N ATOM 3222 CA LEU A 516 7.930 -22.678 -26.778 1.00 83.32 C ANISOU 3222 CA LEU A 516 10236 13106 8315 -2058 -205 965 C ATOM 3223 C LEU A 516 7.610 -21.418 -27.599 1.00 85.61 C ANISOU 3223 C LEU A 516 10383 13534 8612 -1971 -232 932 C ATOM 3224 O LEU A 516 7.858 -21.413 -28.799 1.00 85.90 O ANISOU 3224 O LEU A 516 10494 13496 8649 -1984 -233 892 O ATOM 3225 CB LEU A 516 6.646 -23.497 -26.507 1.00 84.77 C ANISOU 3225 CB LEU A 516 10406 13421 8379 -2305 -236 1017 C ATOM 3226 CG LEU A 516 5.779 -23.924 -27.723 1.00 90.19 C ANISOU 3226 CG LEU A 516 11134 14168 8966 -2516 -273 1004 C ATOM 3227 CD1 LEU A 516 6.572 -24.742 -28.751 1.00 89.75 C ANISOU 3227 CD1 LEU A 516 11341 13840 8921 -2552 -252 950 C ATOM 3228 CD2 LEU A 516 4.564 -24.701 -27.267 1.00 93.56 C ANISOU 3228 CD2 LEU A 516 11529 14757 9264 -2783 -307 1071 C ATOM 3229 N VAL A 517 7.084 -20.357 -26.949 1.00 80.30 N ANISOU 3229 N VAL A 517 9523 13052 7935 -1868 -253 950 N ATOM 3230 CA VAL A 517 6.766 -19.065 -27.576 1.00 78.68 C ANISOU 3230 CA VAL A 517 9200 12968 7726 -1750 -283 927 C ATOM 3231 C VAL A 517 8.082 -18.444 -28.091 1.00 82.49 C ANISOU 3231 C VAL A 517 9769 13266 8307 -1604 -263 883 C ATOM 3232 O VAL A 517 8.115 -17.934 -29.219 1.00 82.74 O ANISOU 3232 O VAL A 517 9811 13291 8334 -1584 -278 855 O ATOM 3233 CB VAL A 517 5.989 -18.134 -26.596 1.00 81.57 C ANISOU 3233 CB VAL A 517 9386 13555 8053 -1638 -304 955 C ATOM 3234 CG1 VAL A 517 5.938 -16.684 -27.084 1.00 80.31 C ANISOU 3234 CG1 VAL A 517 9161 13453 7898 -1456 -332 927 C ATOM 3235 CG2 VAL A 517 4.576 -18.666 -26.338 1.00 82.46 C ANISOU 3235 CG2 VAL A 517 9373 13918 8039 -1794 -326 1007 C ATOM 3236 N GLU A 518 9.179 -18.569 -27.309 1.00 78.10 N ANISOU 3236 N GLU A 518 9274 12574 7827 -1520 -230 882 N ATOM 3237 CA GLU A 518 10.490 -18.071 -27.737 1.00 76.95 C ANISOU 3237 CA GLU A 518 9193 12288 7759 -1407 -210 853 C ATOM 3238 C GLU A 518 11.008 -18.859 -28.947 1.00 80.64 C ANISOU 3238 C GLU A 518 9790 12626 8224 -1472 -182 827 C ATOM 3239 O GLU A 518 11.641 -18.272 -29.824 1.00 80.95 O ANISOU 3239 O GLU A 518 9849 12622 8288 -1413 -178 802 O ATOM 3240 CB GLU A 518 11.533 -18.113 -26.606 1.00 77.72 C ANISOU 3240 CB GLU A 518 9306 12307 7918 -1315 -184 868 C ATOM 3241 CG GLU A 518 11.234 -17.373 -25.300 1.00 88.12 C ANISOU 3241 CG GLU A 518 10522 13726 9235 -1238 -206 886 C ATOM 3242 CD GLU A 518 10.296 -16.176 -25.230 1.00108.13 C ANISOU 3242 CD GLU A 518 12953 16407 11724 -1174 -251 878 C ATOM 3243 OE1 GLU A 518 10.247 -15.369 -26.185 1.00 97.11 O ANISOU 3243 OE1 GLU A 518 11562 15012 10324 -1137 -274 854 O ATOM 3244 OE2 GLU A 518 9.653 -16.015 -24.168 1.00113.07 O ANISOU 3244 OE2 GLU A 518 13501 17150 12313 -1143 -261 897 O ATOM 3245 N LYS A 519 10.724 -20.178 -28.996 1.00 76.26 N ANISOU 3245 N LYS A 519 9340 12007 7626 -1598 -165 833 N ATOM 3246 CA LYS A 519 11.117 -21.060 -30.096 1.00 75.23 C ANISOU 3246 CA LYS A 519 9372 11740 7471 -1659 -138 801 C ATOM 3247 C LYS A 519 10.265 -20.784 -31.322 1.00 77.96 C ANISOU 3247 C LYS A 519 9695 12172 7754 -1757 -174 777 C ATOM 3248 O LYS A 519 10.768 -20.940 -32.421 1.00 77.91 O ANISOU 3248 O LYS A 519 9783 12080 7740 -1751 -155 739 O ATOM 3249 CB LYS A 519 11.022 -22.539 -29.700 1.00 78.41 C ANISOU 3249 CB LYS A 519 9938 12023 7830 -1768 -118 816 C ATOM 3250 CG LYS A 519 12.198 -23.054 -28.871 1.00 82.40 C ANISOU 3250 CG LYS A 519 10529 12392 8388 -1639 -70 832 C ATOM 3251 CD LYS A 519 12.058 -24.539 -28.607 1.00 86.45 C ANISOU 3251 CD LYS A 519 11249 12756 8841 -1743 -54 848 C ATOM 3252 CE LYS A 519 13.351 -25.195 -28.208 1.00 95.66 C ANISOU 3252 CE LYS A 519 12552 13758 10038 -1582 1 856 C ATOM 3253 NZ LYS A 519 13.290 -26.670 -28.387 1.00109.88 N ANISOU 3253 NZ LYS A 519 14631 15360 11760 -1665 18 854 N ATOM 3254 N ILE A 520 8.999 -20.361 -31.156 1.00 74.44 N ANISOU 3254 N ILE A 520 9117 11915 7254 -1836 -222 801 N ATOM 3255 CA ILE A 520 8.143 -20.010 -32.294 1.00 75.21 C ANISOU 3255 CA ILE A 520 9164 12131 7279 -1916 -263 788 C ATOM 3256 C ILE A 520 8.652 -18.666 -32.885 1.00 79.33 C ANISOU 3256 C ILE A 520 9621 12671 7851 -1753 -270 770 C ATOM 3257 O ILE A 520 8.831 -18.565 -34.105 1.00 79.06 O ANISOU 3257 O ILE A 520 9641 12603 7796 -1770 -272 742 O ATOM 3258 CB ILE A 520 6.633 -19.983 -31.913 1.00 79.13 C ANISOU 3258 CB ILE A 520 9515 12869 7683 -2036 -312 831 C ATOM 3259 CG1 ILE A 520 6.138 -21.398 -31.527 1.00 80.53 C ANISOU 3259 CG1 ILE A 520 9789 13020 7790 -2256 -312 854 C ATOM 3260 CG2 ILE A 520 5.778 -19.442 -33.065 1.00 79.58 C ANISOU 3260 CG2 ILE A 520 9487 13088 7660 -2082 -359 826 C ATOM 3261 CD1 ILE A 520 4.830 -21.436 -30.750 1.00 88.50 C ANISOU 3261 CD1 ILE A 520 10631 14285 8709 -2373 -349 915 C ATOM 3262 N ASN A 521 8.933 -17.670 -32.011 1.00 75.99 N ANISOU 3262 N ASN A 521 9105 12282 7483 -1604 -275 788 N ATOM 3263 CA ASN A 521 9.459 -16.342 -32.375 1.00 75.03 C ANISOU 3263 CA ASN A 521 8953 12153 7401 -1462 -289 780 C ATOM 3264 C ASN A 521 10.763 -16.451 -33.155 1.00 78.16 C ANISOU 3264 C ASN A 521 9458 12393 7846 -1436 -250 754 C ATOM 3265 O ASN A 521 10.878 -15.835 -34.215 1.00 76.84 O ANISOU 3265 O ASN A 521 9302 12232 7662 -1420 -264 744 O ATOM 3266 CB ASN A 521 9.701 -15.467 -31.119 1.00 73.27 C ANISOU 3266 CB ASN A 521 8666 11949 7223 -1329 -298 797 C ATOM 3267 CG ASN A 521 9.785 -13.964 -31.370 1.00 79.94 C ANISOU 3267 CG ASN A 521 9489 12815 8070 -1202 -336 797 C ATOM 3268 OD1 ASN A 521 9.558 -13.152 -30.472 1.00 73.76 O ANISOU 3268 OD1 ASN A 521 8661 12079 7284 -1097 -360 806 O ATOM 3269 ND2 ASN A 521 10.084 -13.537 -32.581 1.00 70.53 N ANISOU 3269 ND2 ASN A 521 8345 11582 6870 -1205 -344 786 N ATOM 3270 N LEU A 522 11.748 -17.221 -32.621 1.00 74.72 N ANISOU 3270 N LEU A 522 9094 11838 7458 -1421 -200 751 N ATOM 3271 CA LEU A 522 13.061 -17.406 -33.245 1.00 73.82 C ANISOU 3271 CA LEU A 522 9061 11612 7375 -1373 -154 734 C ATOM 3272 C LEU A 522 12.946 -18.190 -34.555 1.00 79.67 C ANISOU 3272 C LEU A 522 9907 12308 8058 -1452 -134 700 C ATOM 3273 O LEU A 522 13.694 -17.909 -35.490 1.00 79.21 O ANISOU 3273 O LEU A 522 9880 12220 7997 -1413 -112 685 O ATOM 3274 CB LEU A 522 14.045 -18.087 -32.284 1.00 73.19 C ANISOU 3274 CB LEU A 522 9020 11448 7340 -1312 -107 747 C ATOM 3275 CG LEU A 522 14.527 -17.237 -31.088 1.00 75.67 C ANISOU 3275 CG LEU A 522 9243 11798 7709 -1225 -122 777 C ATOM 3276 CD1 LEU A 522 15.292 -18.071 -30.107 1.00 75.28 C ANISOU 3276 CD1 LEU A 522 9225 11691 7689 -1177 -82 796 C ATOM 3277 CD2 LEU A 522 15.382 -16.083 -31.524 1.00 76.19 C ANISOU 3277 CD2 LEU A 522 9272 11878 7796 -1168 -132 783 C ATOM 3278 N PHE A 523 11.975 -19.119 -34.641 1.00 78.34 N ANISOU 3278 N PHE A 523 9792 12145 7830 -1579 -147 689 N ATOM 3279 CA PHE A 523 11.685 -19.893 -35.843 1.00 79.27 C ANISOU 3279 CA PHE A 523 10028 12219 7871 -1685 -142 651 C ATOM 3280 C PHE A 523 11.216 -18.963 -36.959 1.00 85.64 C ANISOU 3280 C PHE A 523 10765 13133 8641 -1701 -181 644 C ATOM 3281 O PHE A 523 11.672 -19.111 -38.088 1.00 86.07 O ANISOU 3281 O PHE A 523 10902 13138 8663 -1704 -159 612 O ATOM 3282 CB PHE A 523 10.631 -20.994 -35.576 1.00 81.77 C ANISOU 3282 CB PHE A 523 10415 12538 8116 -1860 -165 651 C ATOM 3283 CG PHE A 523 10.046 -21.593 -36.830 1.00 84.94 C ANISOU 3283 CG PHE A 523 10924 12932 8416 -2010 -184 613 C ATOM 3284 CD1 PHE A 523 10.739 -22.563 -37.546 1.00 89.24 C ANISOU 3284 CD1 PHE A 523 11682 13303 8923 -2017 -139 562 C ATOM 3285 CD2 PHE A 523 8.819 -21.156 -37.322 1.00 88.32 C ANISOU 3285 CD2 PHE A 523 11241 13541 8774 -2129 -247 627 C ATOM 3286 CE1 PHE A 523 10.221 -23.079 -38.738 1.00 91.70 C ANISOU 3286 CE1 PHE A 523 12111 13602 9130 -2159 -159 519 C ATOM 3287 CE2 PHE A 523 8.298 -21.673 -38.514 1.00 92.58 C ANISOU 3287 CE2 PHE A 523 11875 14090 9211 -2280 -271 592 C ATOM 3288 CZ PHE A 523 9.004 -22.631 -39.215 1.00 91.50 C ANISOU 3288 CZ PHE A 523 11967 13760 9039 -2303 -229 534 C ATOM 3289 N ALA A 524 10.279 -18.043 -36.656 1.00 82.50 N ANISOU 3289 N ALA A 524 10225 12887 8235 -1700 -237 676 N ATOM 3290 CA ALA A 524 9.728 -17.107 -37.637 1.00 82.45 C ANISOU 3290 CA ALA A 524 10153 12993 8183 -1695 -282 682 C ATOM 3291 C ALA A 524 10.718 -15.992 -37.960 1.00 86.95 C ANISOU 3291 C ALA A 524 10714 13516 8807 -1563 -271 690 C ATOM 3292 O ALA A 524 10.693 -15.460 -39.070 1.00 86.67 O ANISOU 3292 O ALA A 524 10688 13510 8732 -1563 -288 687 O ATOM 3293 CB ALA A 524 8.431 -16.515 -37.125 1.00 83.33 C ANISOU 3293 CB ALA A 524 10120 13290 8252 -1699 -342 719 C ATOM 3294 N MET A 525 11.583 -15.641 -36.990 1.00 83.80 N ANISOU 3294 N MET A 525 10302 13053 8487 -1467 -248 705 N ATOM 3295 CA MET A 525 12.610 -14.604 -37.107 1.00 83.74 C ANISOU 3295 CA MET A 525 10291 13004 8523 -1375 -242 722 C ATOM 3296 C MET A 525 13.716 -15.107 -38.037 1.00 85.45 C ANISOU 3296 C MET A 525 10586 13149 8733 -1384 -185 702 C ATOM 3297 O MET A 525 13.956 -14.490 -39.078 1.00 85.20 O ANISOU 3297 O MET A 525 10566 13136 8670 -1386 -193 707 O ATOM 3298 CB MET A 525 13.135 -14.263 -35.706 1.00 86.71 C ANISOU 3298 CB MET A 525 10629 13352 8966 -1301 -239 743 C ATOM 3299 CG MET A 525 13.809 -12.930 -35.590 1.00 91.60 C ANISOU 3299 CG MET A 525 11239 13956 9610 -1235 -265 769 C ATOM 3300 SD MET A 525 15.573 -13.003 -35.935 1.00 97.44 S ANISOU 3300 SD MET A 525 12009 14635 10377 -1231 -209 780 S ATOM 3301 CE MET A 525 16.135 -14.013 -34.596 1.00 93.67 C ANISOU 3301 CE MET A 525 11512 14127 9952 -1197 -163 779 C ATOM 3302 N PHE A 526 14.335 -16.262 -37.703 1.00 80.75 N ANISOU 3302 N PHE A 526 10051 12479 8152 -1381 -127 681 N ATOM 3303 CA PHE A 526 15.372 -16.888 -38.533 1.00 80.39 C ANISOU 3303 CA PHE A 526 10086 12379 8082 -1355 -63 658 C ATOM 3304 C PHE A 526 14.767 -17.507 -39.800 1.00 83.86 C ANISOU 3304 C PHE A 526 10615 12810 8437 -1437 -62 614 C ATOM 3305 O PHE A 526 15.442 -17.581 -40.826 1.00 83.81 O ANISOU 3305 O PHE A 526 10659 12797 8389 -1414 -23 596 O ATOM 3306 CB PHE A 526 16.153 -17.954 -37.753 1.00 82.46 C ANISOU 3306 CB PHE A 526 10403 12560 8367 -1291 -3 650 C ATOM 3307 CG PHE A 526 17.039 -17.454 -36.630 1.00 83.56 C ANISOU 3307 CG PHE A 526 10456 12720 8574 -1205 6 693 C ATOM 3308 CD1 PHE A 526 18.089 -16.574 -36.887 1.00 85.90 C ANISOU 3308 CD1 PHE A 526 10683 13076 8879 -1158 17 725 C ATOM 3309 CD2 PHE A 526 16.896 -17.948 -35.336 1.00 85.27 C ANISOU 3309 CD2 PHE A 526 10666 12903 8830 -1185 6 706 C ATOM 3310 CE1 PHE A 526 18.940 -16.156 -35.862 1.00 86.38 C ANISOU 3310 CE1 PHE A 526 10666 13169 8986 -1104 20 766 C ATOM 3311 CE2 PHE A 526 17.754 -17.535 -34.312 1.00 87.44 C ANISOU 3311 CE2 PHE A 526 10864 13206 9155 -1110 12 745 C ATOM 3312 CZ PHE A 526 18.768 -16.640 -34.582 1.00 85.46 C ANISOU 3312 CZ PHE A 526 10542 13020 8910 -1075 17 773 C ATOM 3313 N GLY A 527 13.499 -17.912 -39.716 1.00 80.09 N ANISOU 3313 N GLY A 527 10151 12356 7924 -1541 -106 601 N ATOM 3314 CA GLY A 527 12.737 -18.482 -40.820 1.00 80.18 C ANISOU 3314 CA GLY A 527 10242 12380 7842 -1656 -123 562 C ATOM 3315 C GLY A 527 12.506 -17.496 -41.942 1.00 84.13 C ANISOU 3315 C GLY A 527 10688 12974 8302 -1663 -157 573 C ATOM 3316 O GLY A 527 12.425 -17.914 -43.100 1.00 85.83 O ANISOU 3316 O GLY A 527 10988 13186 8439 -1722 -149 536 O ATOM 3317 N THR A 528 12.424 -16.174 -41.623 1.00 78.17 N ANISOU 3317 N THR A 528 9816 12295 7592 -1597 -197 623 N ATOM 3318 CA THR A 528 12.243 -15.126 -42.634 1.00 77.07 C ANISOU 3318 CA THR A 528 9643 12229 7411 -1589 -235 646 C ATOM 3319 C THR A 528 13.468 -15.117 -43.523 1.00 80.18 C ANISOU 3319 C THR A 528 10098 12574 7792 -1557 -178 635 C ATOM 3320 O THR A 528 13.320 -15.224 -44.738 1.00 81.02 O ANISOU 3320 O THR A 528 10252 12712 7822 -1605 -178 616 O ATOM 3321 CB THR A 528 11.962 -13.747 -42.012 1.00 85.04 C ANISOU 3321 CB THR A 528 10561 13291 8460 -1510 -289 701 C ATOM 3322 OG1 THR A 528 10.764 -13.803 -41.234 1.00 84.15 O ANISOU 3322 OG1 THR A 528 10376 13260 8337 -1521 -336 710 O ATOM 3323 CG2 THR A 528 11.813 -12.650 -43.066 1.00 84.51 C ANISOU 3323 CG2 THR A 528 10493 13276 8341 -1491 -331 733 C ATOM 3324 N GLY A 529 14.650 -15.070 -42.903 1.00 75.22 N ANISOU 3324 N GLY A 529 9463 11892 7225 -1482 -129 649 N ATOM 3325 CA GLY A 529 15.946 -15.076 -43.574 1.00 74.70 C ANISOU 3325 CA GLY A 529 9423 11820 7140 -1438 -65 652 C ATOM 3326 C GLY A 529 16.186 -16.301 -44.433 1.00 79.42 C ANISOU 3326 C GLY A 529 10131 12382 7665 -1445 -4 590 C ATOM 3327 O GLY A 529 16.649 -16.163 -45.566 1.00 80.29 O ANISOU 3327 O GLY A 529 10267 12531 7708 -1443 23 584 O ATOM 3328 N ILE A 530 15.858 -17.503 -43.910 1.00 76.13 N ANISOU 3328 N ILE A 530 9797 11882 7247 -1456 15 544 N ATOM 3329 CA ILE A 530 16.001 -18.785 -44.617 1.00 77.75 C ANISOU 3329 CA ILE A 530 10164 12011 7369 -1460 67 474 C ATOM 3330 C ILE A 530 15.011 -18.812 -45.810 1.00 82.51 C ANISOU 3330 C ILE A 530 10821 12652 7878 -1585 22 441 C ATOM 3331 O ILE A 530 15.407 -19.167 -46.920 1.00 82.89 O ANISOU 3331 O ILE A 530 10961 12694 7840 -1574 61 400 O ATOM 3332 CB ILE A 530 15.805 -19.999 -43.651 1.00 81.55 C ANISOU 3332 CB ILE A 530 10751 12369 7866 -1461 84 444 C ATOM 3333 CG1 ILE A 530 16.907 -20.027 -42.560 1.00 81.24 C ANISOU 3333 CG1 ILE A 530 10658 12306 7903 -1317 135 479 C ATOM 3334 CG2 ILE A 530 15.774 -21.335 -44.423 1.00 84.57 C ANISOU 3334 CG2 ILE A 530 11356 12636 8140 -1484 123 365 C ATOM 3335 CD1 ILE A 530 16.652 -20.970 -41.380 1.00 87.00 C ANISOU 3335 CD1 ILE A 530 11464 12928 8665 -1316 138 474 C ATOM 3336 N ALA A 531 13.746 -18.400 -45.580 1.00 78.48 N ANISOU 3336 N ALA A 531 10242 12203 7374 -1693 -61 463 N ATOM 3337 CA ALA A 531 12.711 -18.321 -46.613 1.00 78.55 C ANISOU 3337 CA ALA A 531 10266 12290 7288 -1816 -118 446 C ATOM 3338 C ALA A 531 13.066 -17.293 -47.705 1.00 80.79 C ANISOU 3338 C ALA A 531 10497 12661 7539 -1778 -123 475 C ATOM 3339 O ALA A 531 12.913 -17.608 -48.877 1.00 80.67 O ANISOU 3339 O ALA A 531 10560 12667 7423 -1836 -121 437 O ATOM 3340 CB ALA A 531 11.371 -17.966 -45.992 1.00 79.07 C ANISOU 3340 CB ALA A 531 10225 12454 7365 -1902 -202 483 C ATOM 3341 N MET A 532 13.545 -16.085 -47.328 1.00 75.92 N ANISOU 3341 N MET A 532 9767 12086 6995 -1694 -133 542 N ATOM 3342 CA MET A 532 13.906 -15.038 -48.290 1.00 75.84 C ANISOU 3342 CA MET A 532 9721 12146 6948 -1674 -143 584 C ATOM 3343 C MET A 532 15.136 -15.438 -49.113 1.00 81.66 C ANISOU 3343 C MET A 532 10526 12867 7636 -1631 -58 558 C ATOM 3344 O MET A 532 15.245 -15.010 -50.259 1.00 81.37 O ANISOU 3344 O MET A 532 10500 12895 7523 -1654 -60 570 O ATOM 3345 CB MET A 532 14.153 -13.677 -47.606 1.00 77.01 C ANISOU 3345 CB MET A 532 9773 12314 7173 -1613 -179 663 C ATOM 3346 CG MET A 532 12.918 -13.034 -47.001 1.00 79.99 C ANISOU 3346 CG MET A 532 10085 12736 7570 -1616 -265 695 C ATOM 3347 SD MET A 532 11.512 -12.743 -48.114 1.00 84.07 S ANISOU 3347 SD MET A 532 10587 13380 7974 -1680 -343 703 S ATOM 3348 CE MET A 532 10.494 -14.200 -47.740 1.00 80.69 C ANISOU 3348 CE MET A 532 10167 12979 7513 -1789 -349 639 C ATOM 3349 N SER A 533 16.041 -16.271 -48.534 1.00 78.32 N ANISOU 3349 N SER A 533 10143 12372 7243 -1557 18 527 N ATOM 3350 CA SER A 533 17.256 -16.764 -49.183 1.00 78.24 C ANISOU 3350 CA SER A 533 10186 12370 7174 -1475 110 502 C ATOM 3351 C SER A 533 16.922 -17.708 -50.354 1.00 83.99 C ANISOU 3351 C SER A 533 11064 13073 7777 -1512 134 420 C ATOM 3352 O SER A 533 17.740 -17.863 -51.266 1.00 84.27 O ANISOU 3352 O SER A 533 11137 13154 7728 -1452 199 403 O ATOM 3353 CB SER A 533 18.154 -17.477 -48.172 1.00 79.60 C ANISOU 3353 CB SER A 533 10366 12480 7398 -1361 178 492 C ATOM 3354 OG SER A 533 17.853 -18.855 -48.032 1.00 85.58 O ANISOU 3354 OG SER A 533 11280 13117 8119 -1347 206 413 O ATOM 3355 N THR A 534 15.717 -18.321 -50.337 1.00 81.46 N ANISOU 3355 N THR A 534 10826 12695 7429 -1622 78 373 N ATOM 3356 CA THR A 534 15.285 -19.236 -51.392 1.00 83.06 C ANISOU 3356 CA THR A 534 11195 12863 7502 -1694 84 290 C ATOM 3357 C THR A 534 14.832 -18.440 -52.652 1.00 89.27 C ANISOU 3357 C THR A 534 11936 13777 8207 -1771 38 312 C ATOM 3358 O THR A 534 14.345 -19.051 -53.611 1.00 91.07 O ANISOU 3358 O THR A 534 12287 14001 8315 -1855 27 248 O ATOM 3359 CB THR A 534 14.208 -20.206 -50.898 1.00 88.65 C ANISOU 3359 CB THR A 534 12014 13476 8193 -1819 35 241 C ATOM 3360 OG1 THR A 534 12.997 -19.500 -50.631 1.00 89.70 O ANISOU 3360 OG1 THR A 534 12015 13710 8355 -1940 -64 292 O ATOM 3361 CG2 THR A 534 14.654 -21.006 -49.683 1.00 85.31 C ANISOU 3361 CG2 THR A 534 11655 12918 7839 -1744 78 227 C ATOM 3362 N TRP A 535 15.059 -17.099 -52.675 1.00 84.76 N ANISOU 3362 N TRP A 535 11209 13308 7688 -1741 13 401 N ATOM 3363 CA TRP A 535 14.774 -16.241 -53.830 1.00 85.09 C ANISOU 3363 CA TRP A 535 11212 13464 7654 -1792 -27 439 C ATOM 3364 C TRP A 535 15.604 -16.687 -55.042 1.00 91.28 C ANISOU 3364 C TRP A 535 12088 14275 8317 -1755 50 393 C ATOM 3365 O TRP A 535 15.138 -16.618 -56.183 1.00 91.05 O ANISOU 3365 O TRP A 535 12104 14314 8179 -1827 23 377 O ATOM 3366 CB TRP A 535 15.058 -14.757 -53.516 1.00 82.68 C ANISOU 3366 CB TRP A 535 10769 13224 7424 -1755 -61 547 C ATOM 3367 CG TRP A 535 14.933 -13.878 -54.729 1.00 84.35 C ANISOU 3367 CG TRP A 535 10965 13538 7548 -1794 -94 597 C ATOM 3368 CD1 TRP A 535 15.939 -13.490 -55.570 1.00 87.42 C ANISOU 3368 CD1 TRP A 535 11353 13987 7874 -1769 -40 628 C ATOM 3369 CD2 TRP A 535 13.714 -13.425 -55.329 1.00 84.45 C ANISOU 3369 CD2 TRP A 535 10965 13622 7499 -1867 -185 618 C ATOM 3370 NE1 TRP A 535 15.431 -12.748 -56.604 1.00 86.94 N ANISOU 3370 NE1 TRP A 535 11293 14011 7731 -1826 -95 672 N ATOM 3371 CE2 TRP A 535 14.065 -12.698 -56.490 1.00 88.75 C ANISOU 3371 CE2 TRP A 535 11514 14248 7957 -1877 -185 666 C ATOM 3372 CE3 TRP A 535 12.361 -13.491 -54.953 1.00 85.74 C ANISOU 3372 CE3 TRP A 535 11096 13815 7666 -1920 -269 614 C ATOM 3373 CZ2 TRP A 535 13.106 -12.078 -57.305 1.00 89.05 C ANISOU 3373 CZ2 TRP A 535 11543 14379 7914 -1927 -268 707 C ATOM 3374 CZ3 TRP A 535 11.419 -12.839 -55.734 1.00 88.14 C ANISOU 3374 CZ3 TRP A 535 11366 14234 7887 -1962 -350 657 C ATOM 3375 CH2 TRP A 535 11.787 -12.182 -56.921 1.00 89.51 C ANISOU 3375 CH2 TRP A 535 11563 14471 7975 -1962 -349 699 C ATOM 3376 N VAL A 536 16.844 -17.116 -54.776 1.00 88.86 N ANISOU 3376 N VAL A 536 11802 13938 8024 -1632 148 378 N ATOM 3377 CA VAL A 536 17.803 -17.532 -55.797 1.00 89.51 C ANISOU 3377 CA VAL A 536 11953 14072 7986 -1552 239 339 C ATOM 3378 C VAL A 536 17.780 -19.082 -55.957 1.00 95.88 C ANISOU 3378 C VAL A 536 12971 14752 8708 -1508 292 215 C ATOM 3379 O VAL A 536 18.676 -19.636 -56.597 1.00 96.96 O ANISOU 3379 O VAL A 536 13190 14908 8741 -1389 385 168 O ATOM 3380 CB VAL A 536 19.238 -16.989 -55.479 1.00 91.88 C ANISOU 3380 CB VAL A 536 12126 14464 8322 -1431 316 411 C ATOM 3381 CG1 VAL A 536 19.279 -15.461 -55.511 1.00 90.11 C ANISOU 3381 CG1 VAL A 536 11748 14342 8146 -1506 258 530 C ATOM 3382 CG2 VAL A 536 19.781 -17.529 -54.151 1.00 90.96 C ANISOU 3382 CG2 VAL A 536 11991 14265 8303 -1326 357 405 C ATOM 3383 N TRP A 537 16.749 -19.782 -55.427 1.00 92.76 N ANISOU 3383 N TRP A 537 12678 14231 8335 -1605 233 164 N ATOM 3384 CA TRP A 537 16.699 -21.243 -55.591 1.00 94.17 C ANISOU 3384 CA TRP A 537 13105 14258 8418 -1588 272 48 C ATOM 3385 C TRP A 537 15.978 -21.590 -56.932 1.00 97.79 C ANISOU 3385 C TRP A 537 13707 14734 8716 -1718 236 -23 C ATOM 3386 O TRP A 537 14.970 -22.302 -56.968 1.00 97.14 O ANISOU 3386 O TRP A 537 13768 14562 8579 -1874 172 -82 O ATOM 3387 CB TRP A 537 16.067 -21.928 -54.368 1.00 92.78 C ANISOU 3387 CB TRP A 537 12995 13933 8323 -1647 232 31 C ATOM 3388 CG TRP A 537 16.946 -21.911 -53.142 1.00 93.44 C ANISOU 3388 CG TRP A 537 12998 13977 8528 -1491 287 75 C ATOM 3389 CD1 TRP A 537 17.939 -21.018 -52.848 1.00 95.50 C ANISOU 3389 CD1 TRP A 537 13066 14355 8863 -1365 331 155 C ATOM 3390 CD2 TRP A 537 16.841 -22.780 -52.003 1.00 93.57 C ANISOU 3390 CD2 TRP A 537 13116 13837 8600 -1469 291 53 C ATOM 3391 NE1 TRP A 537 18.472 -21.289 -51.611 1.00 94.53 N ANISOU 3391 NE1 TRP A 537 12912 14170 8837 -1260 363 180 N ATOM 3392 CE2 TRP A 537 17.823 -22.370 -51.071 1.00 96.79 C ANISOU 3392 CE2 TRP A 537 13378 14284 9116 -1310 342 118 C ATOM 3393 CE3 TRP A 537 16.020 -23.879 -51.685 1.00 95.75 C ANISOU 3393 CE3 TRP A 537 13603 13945 8834 -1586 253 -12 C ATOM 3394 CZ2 TRP A 537 18.001 -23.014 -49.838 1.00 96.30 C ANISOU 3394 CZ2 TRP A 537 13364 14101 9123 -1243 358 121 C ATOM 3395 CZ3 TRP A 537 16.201 -24.521 -50.469 1.00 97.48 C ANISOU 3395 CZ3 TRP A 537 13884 14032 9122 -1527 270 -6 C ATOM 3396 CH2 TRP A 537 17.173 -24.082 -49.554 1.00 97.34 C ANISOU 3396 CH2 TRP A 537 13709 14059 9216 -1348 323 60 C ATOM 3397 N THR A 538 16.549 -21.061 -58.038 1.00 94.34 N ANISOU 3397 N THR A 538 13224 14427 8192 -1664 276 -10 N ATOM 3398 CA THR A 538 16.087 -21.221 -59.421 1.00 95.18 C ANISOU 3398 CA THR A 538 13441 14587 8135 -1760 254 -66 C ATOM 3399 C THR A 538 17.195 -21.862 -60.270 1.00 99.83 C ANISOU 3399 C THR A 538 14175 15174 8582 -1590 372 -141 C ATOM 3400 O THR A 538 18.382 -21.704 -59.955 1.00 98.30 O ANISOU 3400 O THR A 538 13897 15029 8425 -1400 466 -105 O ATOM 3401 CB THR A 538 15.642 -19.861 -60.021 1.00102.12 C ANISOU 3401 CB THR A 538 14121 15653 9026 -1853 184 34 C ATOM 3402 OG1 THR A 538 16.756 -18.974 -60.124 1.00104.15 O ANISOU 3402 OG1 THR A 538 14226 16025 9319 -1725 250 117 O ATOM 3403 CG2 THR A 538 14.522 -19.195 -59.233 1.00 97.55 C ANISOU 3403 CG2 THR A 538 13404 15097 8564 -1981 70 107 C ATOM 3404 N LYS A 539 16.799 -22.559 -61.359 1.00 98.93 N ANISOU 3404 N LYS A 539 14271 15024 8294 -1658 366 -241 N ATOM 3405 CA LYS A 539 17.685 -23.225 -62.329 1.00101.10 C ANISOU 3405 CA LYS A 539 14720 15300 8395 -1499 473 -331 C ATOM 3406 C LYS A 539 18.737 -22.262 -62.908 1.00106.15 C ANISOU 3406 C LYS A 539 15150 16166 9016 -1366 549 -246 C ATOM 3407 O LYS A 539 19.849 -22.690 -63.220 1.00107.43 O ANISOU 3407 O LYS A 539 15366 16366 9085 -1154 668 -282 O ATOM 3408 CB LYS A 539 16.865 -23.830 -63.484 1.00104.83 C ANISOU 3408 CB LYS A 539 15420 15730 8681 -1654 423 -436 C ATOM 3409 N ALA A 540 18.382 -20.970 -63.031 1.00101.90 N ANISOU 3409 N ALA A 540 14379 15782 8556 -1488 480 -127 N ATOM 3410 CA ALA A 540 19.229 -19.902 -63.554 1.00102.08 C ANISOU 3410 CA ALA A 540 14201 16020 8565 -1427 527 -23 C ATOM 3411 C ALA A 540 20.487 -19.672 -62.700 1.00107.19 C ANISOU 3411 C ALA A 540 14701 16725 9302 -1252 617 45 C ATOM 3412 O ALA A 540 21.537 -19.355 -63.262 1.00108.20 O ANISOU 3412 O ALA A 540 14737 17029 9346 -1143 705 87 O ATOM 3413 CB ALA A 540 18.434 -18.612 -63.645 1.00101.61 C ANISOU 3413 CB ALA A 540 13970 16053 8582 -1603 414 92 C ATOM 3414 N THR A 541 20.391 -19.826 -61.363 1.00103.52 N ANISOU 3414 N THR A 541 14201 16138 8993 -1233 594 62 N ATOM 3415 CA THR A 541 21.535 -19.623 -60.463 1.00103.07 C ANISOU 3415 CA THR A 541 13996 16144 9021 -1080 667 129 C ATOM 3416 C THR A 541 22.505 -20.818 -60.538 1.00108.21 C ANISOU 3416 C THR A 541 14785 16771 9559 -838 795 39 C ATOM 3417 O THR A 541 23.706 -20.624 -60.359 1.00108.69 O ANISOU 3417 O THR A 541 14704 16991 9601 -679 886 97 O ATOM 3418 CB THR A 541 21.085 -19.352 -59.028 1.00109.78 C ANISOU 3418 CB THR A 541 14765 16882 10065 -1140 597 179 C ATOM 3419 OG1 THR A 541 20.360 -20.476 -58.541 1.00112.27 O ANISOU 3419 OG1 THR A 541 15281 16984 10393 -1149 572 76 O ATOM 3420 CG2 THR A 541 20.249 -18.080 -58.918 1.00106.32 C ANISOU 3420 CG2 THR A 541 14186 16485 9725 -1329 480 276 C ATOM 3421 N LEU A 542 22.003 -22.029 -60.849 1.00105.47 N ANISOU 3421 N LEU A 542 14719 16240 9115 -808 802 -98 N ATOM 3422 CA LEU A 542 22.841 -23.220 -61.032 1.00106.90 C ANISOU 3422 CA LEU A 542 15093 16366 9159 -552 921 -197 C ATOM 3423 C LEU A 542 23.825 -22.971 -62.170 1.00109.92 C ANISOU 3423 C LEU A 542 15400 16991 9372 -413 1024 -185 C ATOM 3424 O LEU A 542 24.979 -23.397 -62.096 1.00110.92 O ANISOU 3424 O LEU A 542 15506 17220 9418 -152 1144 -190 O ATOM 3425 CB LEU A 542 21.962 -24.458 -61.327 1.00108.53 C ANISOU 3425 CB LEU A 542 15662 16308 9268 -602 887 -348 C ATOM 3426 CG LEU A 542 22.363 -25.824 -60.707 1.00114.97 C ANISOU 3426 CG LEU A 542 16744 16905 10036 -390 954 -445 C ATOM 3427 CD1 LEU A 542 23.592 -26.453 -61.387 1.00117.39 C ANISOU 3427 CD1 LEU A 542 17155 17297 10149 -65 1102 -506 C ATOM 3428 CD2 LEU A 542 22.469 -25.766 -59.182 1.00115.10 C ANISOU 3428 CD2 LEU A 542 16646 16847 10241 -363 934 -373 C ATOM 3429 N LEU A 543 23.364 -22.223 -63.195 1.00104.36 N ANISOU 3429 N LEU A 543 14635 16405 8611 -584 976 -156 N ATOM 3430 CA LEU A 543 24.120 -21.803 -64.367 1.00104.55 C ANISOU 3430 CA LEU A 543 14568 16682 8474 -515 1054 -127 C ATOM 3431 C LEU A 543 25.131 -20.707 -64.029 1.00106.17 C ANISOU 3431 C LEU A 543 14444 17152 8743 -488 1094 33 C ATOM 3432 O LEU A 543 26.220 -20.714 -64.593 1.00107.16 O ANISOU 3432 O LEU A 543 14481 17507 8728 -323 1207 57 O ATOM 3433 CB LEU A 543 23.163 -21.303 -65.466 1.00104.69 C ANISOU 3433 CB LEU A 543 14630 16724 8426 -739 968 -135 C ATOM 3434 CG LEU A 543 22.676 -22.310 -66.533 1.00111.63 C ANISOU 3434 CG LEU A 543 15814 17494 9107 -727 980 -293 C ATOM 3435 CD1 LEU A 543 23.831 -22.859 -67.379 1.00114.10 C ANISOU 3435 CD1 LEU A 543 16194 17955 9203 -465 1131 -351 C ATOM 3436 CD2 LEU A 543 21.813 -23.423 -65.939 1.00114.75 C ANISOU 3436 CD2 LEU A 543 16489 17578 9534 -771 922 -416 C ATOM 3437 N ILE A 544 24.777 -19.766 -63.124 1.00100.12 N ANISOU 3437 N ILE A 544 13504 16365 8172 -653 1001 144 N ATOM 3438 CA ILE A 544 25.644 -18.658 -62.684 1.00 98.87 C ANISOU 3438 CA ILE A 544 13059 16426 8083 -681 1016 302 C ATOM 3439 C ILE A 544 26.885 -19.247 -61.987 1.00102.08 C ANISOU 3439 C ILE A 544 13385 16933 8466 -432 1131 308 C ATOM 3440 O ILE A 544 28.007 -18.839 -62.287 1.00102.19 O ANISOU 3440 O ILE A 544 13210 17232 8388 -354 1214 393 O ATOM 3441 CB ILE A 544 24.852 -17.660 -61.775 1.00100.02 C ANISOU 3441 CB ILE A 544 13103 16464 8436 -897 881 393 C ATOM 3442 CG1 ILE A 544 23.821 -16.859 -62.620 1.00100.41 C ANISOU 3442 CG1 ILE A 544 13182 16498 8473 -1112 778 421 C ATOM 3443 CG2 ILE A 544 25.780 -16.706 -60.985 1.00 99.72 C ANISOU 3443 CG2 ILE A 544 12817 16590 8483 -918 891 538 C ATOM 3444 CD1 ILE A 544 22.646 -16.203 -61.832 1.00107.68 C ANISOU 3444 CD1 ILE A 544 14091 17255 9568 -1286 637 461 C ATOM 3445 N TRP A 545 26.679 -20.238 -61.110 1.00 98.33 N ANISOU 3445 N TRP A 545 13058 16245 8057 -307 1138 221 N ATOM 3446 CA TRP A 545 27.767 -20.884 -60.384 1.00 99.05 C ANISOU 3446 CA TRP A 545 13096 16411 8125 -46 1240 224 C ATOM 3447 C TRP A 545 28.549 -21.831 -61.281 1.00104.90 C ANISOU 3447 C TRP A 545 13957 17264 8638 232 1377 137 C ATOM 3448 O TRP A 545 29.750 -21.984 -61.063 1.00106.87 O ANISOU 3448 O TRP A 545 14058 17739 8809 455 1483 185 O ATOM 3449 CB TRP A 545 27.251 -21.613 -59.143 1.00 96.76 C ANISOU 3449 CB TRP A 545 12945 15843 7975 -6 1196 168 C ATOM 3450 CG TRP A 545 26.897 -20.658 -58.046 1.00 95.45 C ANISOU 3450 CG TRP A 545 12598 15649 8018 -200 1095 274 C ATOM 3451 CD1 TRP A 545 25.645 -20.289 -57.656 1.00 96.68 C ANISOU 3451 CD1 TRP A 545 12814 15607 8315 -425 969 269 C ATOM 3452 CD2 TRP A 545 27.808 -19.837 -57.304 1.00 94.80 C ANISOU 3452 CD2 TRP A 545 12239 15777 8005 -199 1108 408 C ATOM 3453 NE1 TRP A 545 25.720 -19.334 -56.670 1.00 94.99 N ANISOU 3453 NE1 TRP A 545 12398 15439 8255 -535 908 381 N ATOM 3454 CE2 TRP A 545 27.038 -19.032 -56.440 1.00 97.22 C ANISOU 3454 CE2 TRP A 545 12481 15961 8498 -416 987 467 C ATOM 3455 CE3 TRP A 545 29.208 -19.720 -57.269 1.00 97.68 C ANISOU 3455 CE3 TRP A 545 12399 16437 8276 -37 1210 487 C ATOM 3456 CZ2 TRP A 545 27.621 -18.143 -55.527 1.00 96.09 C ANISOU 3456 CZ2 TRP A 545 12111 15945 8453 -481 961 590 C ATOM 3457 CZ3 TRP A 545 29.785 -18.835 -56.371 1.00 98.72 C ANISOU 3457 CZ3 TRP A 545 12284 16720 8506 -125 1180 618 C ATOM 3458 CH2 TRP A 545 28.996 -18.057 -55.514 1.00 97.38 C ANISOU 3458 CH2 TRP A 545 12086 16389 8524 -350 1054 664 C ATOM 3459 N ARG A 546 27.898 -22.445 -62.283 1.00101.08 N ANISOU 3459 N ARG A 546 13732 16642 8031 226 1376 12 N ATOM 3460 CA ARG A 546 28.583 -23.309 -63.238 1.00103.94 C ANISOU 3460 CA ARG A 546 14238 17100 8154 494 1504 -82 C ATOM 3461 C ARG A 546 29.581 -22.461 -64.025 1.00110.32 C ANISOU 3461 C ARG A 546 14764 18315 8838 521 1582 30 C ATOM 3462 O ARG A 546 30.768 -22.791 -64.077 1.00111.40 O ANISOU 3462 O ARG A 546 14794 18692 8840 795 1711 51 O ATOM 3463 CB ARG A 546 27.577 -24.010 -64.167 1.00105.03 C ANISOU 3463 CB ARG A 546 14719 17002 8187 422 1465 -235 C ATOM 3464 N ARG A 547 29.096 -21.309 -64.543 1.00107.17 N ANISOU 3464 N ARG A 547 14227 18005 8489 227 1498 118 N ATOM 3465 CA ARG A 547 29.827 -20.288 -65.298 1.00108.08 C ANISOU 3465 CA ARG A 547 14079 18479 8506 150 1538 248 C ATOM 3466 C ARG A 547 30.997 -19.730 -64.464 1.00114.29 C ANISOU 3466 C ARG A 547 14550 19538 9337 209 1588 396 C ATOM 3467 O ARG A 547 32.088 -19.588 -65.007 1.00115.43 O ANISOU 3467 O ARG A 547 14514 20032 9311 334 1697 461 O ATOM 3468 CB ARG A 547 28.844 -19.168 -65.705 1.00105.09 C ANISOU 3468 CB ARG A 547 13667 18041 8222 -198 1403 317 C ATOM 3469 CG ARG A 547 29.430 -17.926 -66.370 1.00110.46 C ANISOU 3469 CG ARG A 547 14096 19040 8833 -352 1410 475 C ATOM 3470 CD ARG A 547 28.340 -16.924 -66.735 1.00115.20 C ANISOU 3470 CD ARG A 547 14723 19525 9524 -661 1268 531 C ATOM 3471 NE ARG A 547 27.656 -16.368 -65.564 1.00115.26 N ANISOU 3471 NE ARG A 547 14702 19325 9768 -820 1145 581 N ATOM 3472 N THR A 548 30.778 -19.456 -63.151 1.00111.44 N ANISOU 3472 N THR A 548 14121 19035 9187 122 1510 448 N ATOM 3473 CA THR A 548 31.801 -18.920 -62.237 1.00112.41 C ANISOU 3473 CA THR A 548 13955 19394 9363 143 1537 586 C ATOM 3474 C THR A 548 32.953 -19.928 -62.047 1.00121.83 C ANISOU 3474 C THR A 548 15106 20775 10409 519 1686 552 C ATOM 3475 O THR A 548 34.100 -19.546 -62.281 1.00123.44 O ANISOU 3475 O THR A 548 15048 21373 10483 588 1771 662 O ATOM 3476 CB THR A 548 31.196 -18.516 -60.882 1.00116.44 C ANISOU 3476 CB THR A 548 14448 19673 10121 -18 1418 624 C ATOM 3477 OG1 THR A 548 30.052 -17.692 -61.103 1.00114.24 O ANISOU 3477 OG1 THR A 548 14239 19211 9956 -313 1286 641 O ATOM 3478 CG2 THR A 548 32.193 -17.770 -59.998 1.00113.61 C ANISOU 3478 CG2 THR A 548 13788 19566 9811 -63 1424 779 C ATOM 3479 N TRP A 549 32.657 -21.193 -61.646 1.00120.99 N ANISOU 3479 N TRP A 549 15258 20405 10307 759 1716 410 N ATOM 3480 CA TRP A 549 33.660 -22.257 -61.438 1.00124.26 C ANISOU 3480 CA TRP A 549 15692 20948 10575 1164 1854 364 C ATOM 3481 C TRP A 549 34.530 -22.468 -62.692 1.00131.67 C ANISOU 3481 C TRP A 549 16569 22222 11236 1374 1993 356 C ATOM 3482 O TRP A 549 35.741 -22.655 -62.570 1.00133.08 O ANISOU 3482 O TRP A 549 16542 22744 11277 1631 2109 420 O ATOM 3483 CB TRP A 549 32.987 -23.589 -61.037 1.00123.42 C ANISOU 3483 CB TRP A 549 15967 20430 10496 1351 1849 196 C ATOM 3484 CG TRP A 549 33.929 -24.764 -60.944 1.00127.08 C ANISOU 3484 CG TRP A 549 16526 20976 10782 1804 1991 133 C ATOM 3485 CD1 TRP A 549 34.291 -25.607 -61.955 1.00132.66 C ANISOU 3485 CD1 TRP A 549 17425 21733 11245 2094 2106 23 C ATOM 3486 CD2 TRP A 549 34.609 -25.231 -59.771 1.00127.32 C ANISOU 3486 CD2 TRP A 549 16479 21042 10854 2040 2031 174 C ATOM 3487 NE1 TRP A 549 35.170 -26.556 -61.490 1.00134.22 N ANISOU 3487 NE1 TRP A 549 17674 21998 11325 2514 2219 -4 N ATOM 3488 CE2 TRP A 549 35.378 -26.353 -60.151 1.00134.20 C ANISOU 3488 CE2 TRP A 549 17503 21991 11495 2488 2173 91 C ATOM 3489 CE3 TRP A 549 34.642 -24.811 -58.430 1.00126.84 C ANISOU 3489 CE3 TRP A 549 16243 20957 10992 1926 1959 273 C ATOM 3490 CZ2 TRP A 549 36.170 -27.061 -59.241 1.00134.84 C ANISOU 3490 CZ2 TRP A 549 17561 22130 11541 2834 2244 111 C ATOM 3491 CZ3 TRP A 549 35.428 -25.514 -57.528 1.00129.50 C ANISOU 3491 CZ3 TRP A 549 16548 21357 11298 2246 2027 292 C ATOM 3492 CH2 TRP A 549 36.177 -26.626 -57.934 1.00133.19 C ANISOU 3492 CH2 TRP A 549 17164 21905 11536 2698 2168 215 C ATOM 3493 N CYS A 550 33.900 -22.451 -63.877 1.00129.52 N ANISOU 3493 N CYS A 550 16470 21869 10874 1272 1980 277 N ATOM 3494 CA CYS A 550 34.548 -22.630 -65.178 1.00132.54 C ANISOU 3494 CA CYS A 550 16830 22540 10988 1443 2102 254 C ATOM 3495 C CYS A 550 35.572 -21.509 -65.425 1.00136.91 C ANISOU 3495 C CYS A 550 16960 23594 11467 1333 2145 449 C ATOM 3496 O CYS A 550 36.647 -21.776 -65.954 1.00139.25 O ANISOU 3496 O CYS A 550 17110 24264 11534 1592 2285 476 O ATOM 3497 CB CYS A 550 33.497 -22.676 -66.282 1.00133.03 C ANISOU 3497 CB CYS A 550 17155 22385 11005 1275 2045 145 C ATOM 3498 SG CYS A 550 34.105 -23.314 -67.860 1.00140.79 S ANISOU 3498 SG CYS A 550 18248 23608 11637 1557 2200 49 S ATOM 3499 N ARG A 551 35.244 -20.272 -65.010 1.00131.44 N ANISOU 3499 N ARG A 551 16080 22909 10953 955 2024 585 N ATOM 3500 CA ARG A 551 36.109 -19.094 -65.128 1.00131.63 C ANISOU 3500 CA ARG A 551 15729 23357 10926 767 2034 783 C ATOM 3501 C ARG A 551 37.246 -19.136 -64.085 1.00137.86 C ANISOU 3501 C ARG A 551 16241 24426 11713 920 2093 889 C ATOM 3502 O ARG A 551 38.363 -18.708 -64.390 1.00139.45 O ANISOU 3502 O ARG A 551 16137 25101 11747 945 2176 1021 O ATOM 3503 CB ARG A 551 35.287 -17.802 -64.973 1.00126.47 C ANISOU 3503 CB ARG A 551 15039 22548 10464 320 1872 881 C ATOM 3504 CG ARG A 551 34.374 -17.512 -66.156 1.00125.17 C ANISOU 3504 CG ARG A 551 15057 22244 10257 146 1820 827 C ATOM 3505 CD ARG A 551 33.412 -16.376 -65.880 1.00122.55 C ANISOU 3505 CD ARG A 551 14744 21693 10126 -236 1652 903 C ATOM 3506 NE ARG A 551 32.654 -16.022 -67.081 1.00125.10 N ANISOU 3506 NE ARG A 551 15202 21950 10380 -392 1608 877 N ATOM 3507 CZ ARG A 551 31.845 -14.970 -67.188 1.00131.52 C ANISOU 3507 CZ ARG A 551 16038 22627 11306 -702 1474 953 C ATOM 3508 NH1 ARG A 551 31.666 -14.152 -66.157 1.00111.38 N ANISOU 3508 NH1 ARG A 551 13402 19972 8945 -892 1371 1051 N ATOM 3509 NH2 ARG A 551 31.212 -14.727 -68.328 1.00114.43 N ANISOU 3509 NH2 ARG A 551 13992 20432 9054 -811 1442 930 N ATOM 3510 N LEU A 552 36.964 -19.650 -62.867 1.00134.04 N ANISOU 3510 N LEU A 552 15855 23673 11401 1012 2048 839 N ATOM 3511 CA LEU A 552 37.944 -19.763 -61.778 1.00135.19 C ANISOU 3511 CA LEU A 552 15761 24048 11556 1165 2091 930 C ATOM 3512 C LEU A 552 38.964 -20.888 -62.060 1.00143.98 C ANISOU 3512 C LEU A 552 16849 25430 12427 1650 2266 878 C ATOM 3513 O LEU A 552 40.168 -20.682 -61.875 1.00145.81 O ANISOU 3513 O LEU A 552 16749 26130 12524 1764 2348 1007 O ATOM 3514 CB LEU A 552 37.240 -20.003 -60.435 1.00132.71 C ANISOU 3514 CB LEU A 552 15589 23340 11493 1119 1988 884 C ATOM 3515 N THR A 553 38.480 -22.063 -62.519 1.00141.64 N ANISOU 3515 N THR A 553 16910 24848 12058 1933 2320 691 N ATOM 3516 CA THR A 553 39.305 -23.226 -62.845 1.00165.85 C ANISOU 3516 CA THR A 553 20043 28090 14882 2435 2483 613 C ATOM 3517 C THR A 553 39.348 -23.428 -64.354 1.00182.55 C ANISOU 3517 C THR A 553 22265 30334 16763 2534 2572 538 C ATOM 3518 O THR A 553 40.347 -23.907 -64.883 1.00145.54 O ANISOU 3518 O THR A 553 17470 26014 11816 2886 2724 542 O ATOM 3519 CB THR A 553 38.765 -24.470 -62.139 1.00173.26 C ANISOU 3519 CB THR A 553 21358 28574 15899 2698 2475 454 C TER 3520 THR A 553 HETATM 3521 C12 A8T A1201 14.929 -12.029 -13.751 1.00 66.87 C HETATM 3522 C11 A8T A1201 14.532 -10.825 -14.515 1.00 68.74 C HETATM 3523 C13 A8T A1201 15.637 -9.764 -14.469 1.00 67.73 C HETATM 3524 O1 A8T A1201 13.403 -10.326 -13.910 1.00 70.37 O HETATM 3525 C2 A8T A1201 14.211 -11.126 -15.975 1.00 70.65 C HETATM 3526 C3 A8T A1201 14.740 -12.274 -16.632 1.00 71.11 C HETATM 3527 N1 A8T A1201 14.467 -12.664 -17.906 1.00 72.05 N HETATM 3528 C1 A8T A1201 13.385 -10.316 -16.794 1.00 70.41 C HETATM 3529 C5 A8T A1201 13.120 -10.691 -18.126 1.00 71.15 C HETATM 3530 C4 A8T A1201 13.676 -11.884 -18.684 1.00 73.34 C HETATM 3531 N2 A8T A1201 13.467 -12.253 -20.102 1.00 74.15 N HETATM 3532 C9 A8T A1201 14.558 -12.990 -20.710 1.00 73.95 C HETATM 3533 C8 A8T A1201 14.481 -12.964 -22.205 1.00 74.33 C HETATM 3534 C6 A8T A1201 12.110 -12.581 -20.547 1.00 74.02 C HETATM 3535 C7 A8T A1201 12.037 -12.569 -22.067 1.00 74.46 C HETATM 3536 N3 A8T A1201 13.121 -13.343 -22.680 1.00 73.66 N HETATM 3537 C10 A8T A1201 13.036 -13.522 -24.143 1.00 71.45 C HETATM 3538 N5 A8T A1201 12.412 -12.571 -24.867 1.00 71.44 N HETATM 3539 N4 A8T A1201 12.330 -12.603 -26.201 1.00 70.92 N HETATM 3540 C14 A8T A1201 13.647 -14.674 -24.843 1.00 68.54 C HETATM 3541 C17 A8T A1201 14.348 -15.703 -24.176 1.00 66.09 C HETATM 3542 C18 A8T A1201 14.919 -16.783 -24.908 1.00 67.07 C HETATM 3543 C19 A8T A1201 14.847 -16.827 -26.298 1.00 68.46 C HETATM 3544 C20 A8T A1201 14.195 -15.773 -26.987 1.00 68.57 C HETATM 3545 C15 A8T A1201 13.570 -14.698 -26.284 1.00 69.75 C HETATM 3546 C16 A8T A1201 12.853 -13.612 -26.925 1.00 72.33 C HETATM 3547 C21 A8T A1201 12.612 -13.550 -28.475 1.00 74.95 C HETATM 3548 C22 A8T A1201 13.524 -12.549 -29.192 1.00 75.80 C HETATM 3549 C23 A8T A1201 14.689 -12.079 -28.609 1.00 75.37 C HETATM 3550 C24 A8T A1201 15.552 -11.092 -29.368 1.00 75.23 C HETATM 3551 C25 A8T A1201 15.187 -10.711 -30.651 1.00 75.08 C HETATM 3552 C26 A8T A1201 13.932 -11.245 -31.286 1.00 73.95 C HETATM 3553 C27 A8T A1201 13.135 -12.136 -30.598 1.00 73.63 C HETATM 3554 ZN ZN A1202 -1.728 -13.985 -72.840 1.00129.24 ZN HETATM 3555 O HOH A1301 14.238 -3.176 -20.148 1.00 80.45 O HETATM 3556 O HOH A1302 16.552 -2.113 -18.096 1.00 80.21 O HETATM 3557 O HOH A1303 24.203 -3.952 -16.874 1.00 82.32 O HETATM 3558 O HOH A1304 23.236 6.089 -21.498 1.00 89.74 O HETATM 3559 O HOH A1305 3.122 -6.608 -18.727 1.00 79.70 O HETATM 3560 O HOH A1306 19.787 -19.810 -49.713 1.00 80.68 O HETATM 3561 O HOH A1307 9.102 -22.614 -20.435 1.00 79.20 O HETATM 3562 O HOH A1308 0.472 -5.672 -19.042 1.00 88.19 O HETATM 3563 O HOH A1309 1.311 -9.308 -16.945 1.00 97.91 O HETATM 3564 O HOH A1310 -0.360 -11.741 -17.388 1.00 83.80 O HETATM 3565 O HOH A1311 -3.597 -14.992 -72.210 1.00 79.19 O HETATM 3566 O HOH A1312 -1.654 -13.433 -75.001 1.00 81.08 O HETATM 3567 O HOH A1313 -23.354 -25.557 -90.848 1.00 98.80 O HETATM 3568 O HOH A1314 1.450 -14.168 -11.974 1.00 75.30 O HETATM 3569 O HOH A1315 10.982 -11.913 -64.906 1.00 77.67 O HETATM 3570 O HOH A1316 15.798 -15.745 -59.339 1.00 90.64 O HETATM 3571 O HOH A1317 13.449 -14.904 -60.183 1.00 77.77 O HETATM 3572 O HOH A1318 -21.350 -8.049 -76.051 1.00 86.61 O HETATM 3573 O HOH A1319 8.167 -0.769 -18.263 1.00 78.79 O HETATM 3574 O HOH A1320 -6.386 -0.932 -54.596 1.00104.55 O HETATM 3575 O HOH A1321 25.296 -18.059 -12.513 1.00 85.89 O HETATM 3576 O HOH A1322 4.968 -21.264 -15.630 1.00 88.53 O HETATM 3577 O HOH A1323 34.269 -5.553 -25.177 1.00 94.17 O CONECT 25 184 CONECT 184 25 CONECT 211 818 CONECT 818 211 CONECT 957 1499 CONECT 1499 957 CONECT 1841 3554 CONECT 3036 3158 CONECT 3158 3036 CONECT 3521 3522 CONECT 3522 3521 3523 3524 3525 CONECT 3523 3522 CONECT 3524 3522 CONECT 3525 3522 3526 3528 CONECT 3526 3525 3527 CONECT 3527 3526 3530 CONECT 3528 3525 3529 CONECT 3529 3528 3530 CONECT 3530 3527 3529 3531 CONECT 3531 3530 3532 3534 CONECT 3532 3531 3533 CONECT 3533 3532 3536 CONECT 3534 3531 3535 CONECT 3535 3534 3536 CONECT 3536 3533 3535 3537 CONECT 3537 3536 3538 3540 CONECT 3538 3537 3539 CONECT 3539 3538 3546 CONECT 3540 3537 3541 3545 CONECT 3541 3540 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3540 3544 3546 CONECT 3546 3539 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 3549 3553 CONECT 3549 3548 3550 CONECT 3550 3549 3551 CONECT 3551 3550 3552 CONECT 3552 3551 3553 CONECT 3553 3548 3552 CONECT 3554 1841 3565 3566 CONECT 3565 3554 CONECT 3566 3554 MASTER 350 0 2 20 4 0 5 6 3576 1 45 36 END