HEADER TRANSPORT PROTEIN/INHIBITOR 30-MAR-15 4Z34 TITLE CRYSTAL STRUCTURE OF HUMAN LYSOPHOSPHATIDIC ACID RECEPTOR 1 IN COMPLEX TITLE 2 WITH ONO9780307 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOPHOSPHATIDIC ACID RECEPTOR 1, SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 2-232; UNP RESIDUES 23-64; UNP RESIDUES 73- COMPND 5 127; UNP RESIDUES 248-326; COMPND 6 SYNONYM: LPA-1,LYSOPHOSPHATIDIC ACID RECEPTOR EDG-2,CYTOCHROME B-562, COMPND 7 CYTOCHROME B-562,LPA-1,LYSOPHOSPHATIDIC ACID RECEPTOR EDG-2; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: LPAR1, EDG2, LPA1, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1711; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS HUMAN LYSOPHOSPHATIDIC ACID RECEPTOR 1 (LPA1), G-PROTEIN COUPLED KEYWDS 2 RECEPTOR (GPCR), MEMBRANE PROTEIN, ANTAGONIST, ENDOGENOUS LIGAND, KEYWDS 3 PSI-BIOLOGY, STRUCTURAL GENOMICS, GPCR NETWORK, LIPIDIC CUBIC PHASE KEYWDS 4 (LCP), COMPOUND DESIGN, POLYPHARMACOLOGY, LIPID RECEPTOR EXPDTA X-RAY DIFFRACTION AUTHOR J.E.CHRENCIK,C.B.ROTH,M.TERAKADO,H.KURATA,R.OMI,Y.KIHARA, AUTHOR 2 D.WARSHAVIAK,S.NAKADE,G.ASMAR-ROVIRA,M.MILENI,H.MIZUNO,M.T.GRIFFITH, AUTHOR 3 C.RODGERS,G.W.HAN,J.VELASQUEZ,J.CHUN,R.C.STEVENS,M.A.HANSON,GPCR AUTHOR 4 NETWORK (GPCR) REVDAT 2 01-JUL-15 4Z34 1 JRNL REVDAT 1 03-JUN-15 4Z34 0 JRNL AUTH J.E.CHRENCIK,C.B.ROTH,M.TERAKADO,H.KURATA,R.OMI,Y.KIHARA, JRNL AUTH 2 D.WARSHAVIAK,S.NAKADE,G.ASMAR-ROVIRA,M.MILENI,H.MIZUNO, JRNL AUTH 3 M.T.GRIFFITH,C.RODGERS,G.W.HAN,J.VELASQUEZ,J.CHUN, JRNL AUTH 4 R.C.STEVENS,M.A.HANSON JRNL TITL CRYSTAL STRUCTURE OF ANTAGONIST BOUND HUMAN LYSOPHOSPHATIDIC JRNL TITL 2 ACID RECEPTOR 1. JRNL REF CELL V. 161 1633 2015 JRNL REFN ISSN 1097-4172 JRNL PMID 26091040 JRNL DOI 10.1016/J.CELL.2015.06.002 REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 83.6 REMARK 3 NUMBER OF REFLECTIONS : 10576 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) : 0.256 REMARK 3 R VALUE (WORKING SET) : 0.254 REMARK 3 FREE R VALUE : 0.281 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 531 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 : 5 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.35 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.60 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2591 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2418 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2460 REMARK 3 BIN R VALUE (WORKING SET) : 0.2404 REMARK 3 BIN FREE R VALUE : 0.2670 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.06 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 131 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 : 2991 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 56 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.83 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.03 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.09530 REMARK 3 B22 (A**2) : -1.50130 REMARK 3 B33 (A**2) : 4.59660 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) : 0.579 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.475 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL 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 : 0.825 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.775 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3113 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4234 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1424 ; 4.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 63 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 475 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3113 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 422 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 3594 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.08 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.08 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.95 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): -0.4492 -18.8645 31.0201 REMARK 3 T TENSOR REMARK 3 T11: -0.3040 T22: 0.2548 REMARK 3 T33: 0.2089 T12: -0.1247 REMARK 3 T13: -0.0276 T23: -0.0160 REMARK 3 L TENSOR REMARK 3 L11: 0.6849 L22: 0.7507 REMARK 3 L33: 0.9927 L12: -0.3199 REMARK 3 L13: 0.1559 L23: -0.8961 REMARK 3 S TENSOR REMARK 3 S11: -0.0245 S12: 0.0825 S13: -0.3207 REMARK 3 S21: -0.0163 S22: 0.2294 S23: 0.0434 REMARK 3 S31: -0.0464 S32: -0.1408 S33: -0.2049 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4Z34 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-15. REMARK 100 THE DEPOSITION ID IS D_1000208425. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-JUN-12; 19-JUN-12 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-D; 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033; 1.033 REMARK 200 MONOCHROMATOR : MIRRORS; MIRRORS REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; MARMOSAIC REMARK 200 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10576 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 45.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.0 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.19000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 75.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.10 REMARK 200 R MERGE FOR SHELL (I) : 0.46000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB IDS 3V2Y AND 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE (PH 5.5), 34 - REMARK 280 38% (V/V) PEG400 AND 200 MM AMMONIUM ACETATE, LIPIDIC CUBIC REMARK 280 PHASE, 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 17.14000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.31500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.07500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.31500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.14000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.07500 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 HAVE INDICATED 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 MET A -17 REMARK 465 LYS A -16 REMARK 465 THR A -15 REMARK 465 ILE A -14 REMARK 465 ILE A -13 REMARK 465 ALA A -12 REMARK 465 LEU A -11 REMARK 465 SER A -10 REMARK 465 TYR A -9 REMARK 465 ILE A -8 REMARK 465 PHE A -7 REMARK 465 CYS A -6 REMARK 465 LEU A -5 REMARK 465 VAL A -4 REMARK 465 PHE A -3 REMARK 465 ALA A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 ILE A 4 REMARK 465 SER A 5 REMARK 465 THR A 6 REMARK 465 SER A 7 REMARK 465 ILE A 8 REMARK 465 PRO A 9 REMARK 465 VAL A 10 REMARK 465 ILE A 11 REMARK 465 SER A 12 REMARK 465 GLN A 13 REMARK 465 PRO A 14 REMARK 465 GLN A 15 REMARK 465 PHE A 16 REMARK 465 THR A 17 REMARK 465 ALA A 18 REMARK 465 MET A 19 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 ARG A 328 REMARK 465 PRO A 329 REMARK 465 LEU A 330 REMARK 465 GLU A 331 REMARK 465 VAL A 332 REMARK 465 LEU A 333 REMARK 465 PHE A 334 REMARK 465 GLN A 335 REMARK 465 GLY A 336 REMARK 465 PRO A 337 REMARK 465 HIS A 338 REMARK 465 HIS A 339 REMARK 465 HIS A 340 REMARK 465 HIS A 341 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 HIS A 345 REMARK 465 HIS A 346 REMARK 465 HIS A 347 REMARK 465 ASP A 348 REMARK 465 TYR A 349 REMARK 465 LYS A 350 REMARK 465 ASP A 351 REMARK 465 ASP A 352 REMARK 465 ASP A 353 REMARK 465 ASP A 354 REMARK 465 LYS A 355 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 ASN A 20 CG OD1 ND2 REMARK 470 PHE A 25 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A 26 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN A 27 CG OD1 ND2 REMARK 470 GLU A 28 CG CD OE1 OE2 REMARK 470 LEU A 41 CG CD1 CD2 REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 151 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2 REMARK 470 MET A 153 CG SD CE REMARK 470 LEU A 155 CG CD1 CD2 REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 191 CG OD1 OD2 REMARK 470 LEU A1106 CG CD1 CD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 CYS A 24 27.73 -78.47 REMARK 500 PHE A 25 20.17 -162.36 REMARK 500 HIS A 81 58.65 -100.87 REMARK 500 ARG A 152 -140.42 -140.24 REMARK 500 ASP A 191 49.50 -140.48 REMARK 500 ASN A 194 33.78 -96.00 REMARK 500 ALA A1020 91.27 -65.10 REMARK 500 ASP A1021 -155.87 -123.28 REMARK 500 LYS A1042 74.95 -69.61 REMARK 500 ARG A 248 -26.11 74.87 REMARK 500 GLN A 286 -8.23 86.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 1WV A 2002 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ON7 A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1WV A 2002 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-235 RELATED DB: TARGETTRACK REMARK 900 RELATED ID: 4Z35 RELATED DB: PDB REMARK 900 RELATED ID: 4Z36 RELATED DB: PDB DBREF 4Z34 A 2 232 UNP Q92633 LPAR1_HUMAN 2 232 DBREF 4Z34 A 1001 1042 UNP P0ABE7 C562_ECOLX 23 64 DBREF 4Z34 A 1051 1105 UNP P0ABE7 C562_ECOLX 73 127 DBREF 4Z34 A 248 326 UNP Q92633 LPAR1_HUMAN 248 326 SEQADV 4Z34 MET A -17 UNP Q92633 INITIATING METHIONINE SEQADV 4Z34 LYS A -16 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 THR A -15 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ILE A -14 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ILE A -13 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ALA A -12 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 LEU A -11 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 SER A -10 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 TYR A -9 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ILE A -8 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 PHE A -7 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 CYS A -6 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 LEU A -5 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 VAL A -4 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 PHE A -3 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ALA A -2 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 GLY A -1 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ALA A 0 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 PRO A 1 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4Z34 ALA A 1043 UNP P0ABE7 LINKER SEQADV 4Z34 THR A 1044 UNP P0ABE7 LINKER SEQADV 4Z34 PRO A 1045 UNP P0ABE7 LINKER SEQADV 4Z34 PRO A 1046 UNP P0ABE7 LINKER SEQADV 4Z34 LYS A 1047 UNP P0ABE7 LINKER SEQADV 4Z34 LEU A 1048 UNP P0ABE7 LINKER SEQADV 4Z34 GLU A 1049 UNP P0ABE7 LINKER SEQADV 4Z34 ASP A 1050 UNP P0ABE7 LINKER SEQADV 4Z34 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4Z34 LEU A 1106 UNP P0ABE7 LINKER SEQADV 4Z34 GLY A 327 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ARG A 328 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 PRO A 329 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 LEU A 330 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 GLU A 331 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 VAL A 332 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 LEU A 333 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 PHE A 334 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 GLN A 335 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 GLY A 336 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 PRO A 337 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 338 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 339 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 340 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 341 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 342 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 343 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 344 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 345 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 346 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 HIS A 347 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ASP A 348 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 TYR A 349 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 LYS A 350 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ASP A 351 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ASP A 352 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ASP A 353 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 ASP A 354 UNP Q92633 EXPRESSION TAG SEQADV 4Z34 LYS A 355 UNP Q92633 EXPRESSION TAG SEQRES 1 A 464 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 464 VAL PHE ALA GLY ALA PRO ALA ALA ILE SER THR SER ILE SEQRES 3 A 464 PRO VAL ILE SER GLN PRO GLN PHE THR ALA MET ASN GLU SEQRES 4 A 464 PRO GLN CYS PHE TYR ASN GLU SER ILE ALA PHE PHE TYR SEQRES 5 A 464 ASN ARG SER GLY LYS HIS LEU ALA THR GLU TRP ASN THR SEQRES 6 A 464 VAL SER LYS LEU VAL MET GLY LEU GLY ILE THR VAL CYS SEQRES 7 A 464 ILE PHE ILE MET LEU ALA ASN LEU LEU VAL MET VAL ALA SEQRES 8 A 464 ILE TYR VAL ASN ARG ARG PHE HIS PHE PRO ILE TYR TYR SEQRES 9 A 464 LEU MET ALA ASN LEU ALA ALA ALA ASP PHE PHE ALA GLY SEQRES 10 A 464 LEU ALA TYR PHE TYR LEU MET PHE ASN THR GLY PRO ASN SEQRES 11 A 464 THR ARG ARG LEU THR VAL SER THR TRP LEU LEU ARG GLN SEQRES 12 A 464 GLY LEU ILE ASP THR SER LEU THR ALA SER VAL ALA ASN SEQRES 13 A 464 LEU LEU ALA ILE ALA ILE GLU ARG HIS ILE THR VAL PHE SEQRES 14 A 464 ARG MET GLN LEU HIS THR ARG MET SER ASN ARG ARG VAL SEQRES 15 A 464 VAL VAL VAL ILE VAL VAL ILE TRP THR MET ALA ILE VAL SEQRES 16 A 464 MET GLY ALA ILE PRO SER VAL GLY TRP ASN CYS ILE CYS SEQRES 17 A 464 ASP ILE GLU ASN CYS SER ASN MET ALA PRO LEU TYR SER SEQRES 18 A 464 ASP SER TYR LEU VAL PHE TRP ALA ILE PHE ASN LEU VAL SEQRES 19 A 464 THR PHE VAL VAL MET VAL VAL LEU TYR ALA HIS ILE PHE SEQRES 20 A 464 GLY TYR VAL ALA ASP LEU GLU ASP ASN TRP GLU THR LEU SEQRES 21 A 464 ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA SEQRES 22 A 464 ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA SEQRES 23 A 464 ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU SEQRES 24 A 464 ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG SEQRES 25 A 464 HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA SEQRES 26 A 464 LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN SEQRES 27 A 464 ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR SEQRES 28 A 464 ILE GLN LYS TYR LEU ARG ASN ARG ASP THR MET MET SER SEQRES 29 A 464 LEU LEU LYS THR VAL VAL ILE VAL LEU GLY ALA PHE ILE SEQRES 30 A 464 ILE CYS TRP THR PRO GLY LEU VAL LEU LEU LEU LEU ASP SEQRES 31 A 464 VAL CYS CYS PRO GLN CYS ASP VAL LEU ALA TYR GLU LYS SEQRES 32 A 464 PHE PHE LEU LEU LEU ALA GLU PHE ASN SER ALA MET ASN SEQRES 33 A 464 PRO ILE ILE TYR SER TYR ARG ASP LYS GLU MET SER ALA SEQRES 34 A 464 THR PHE ARG GLN ILE LEU GLY ARG PRO LEU GLU VAL LEU SEQRES 35 A 464 PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 36 A 464 HIS ASP TYR LYS ASP ASP ASP ASP LYS HET ON7 A2001 38 HET 1WV A2002 18 HETNAM ON7 {1-[(2S,3S)-2-(2,3-DIHYDRO-1H-INDEN-2-YLMETHYL)-3-(3,5- HETNAM 2 ON7 DIMETHOXY-4-METHYLPHENYL)-3-HYDROXYPROPYL]-4- HETNAM 3 ON7 (METHOXYCARBONYL)-1H-PYRROL-3-YL}ACETIC ACID HETNAM 1WV (2S)-2,3-DIHYDROXYPROPYL (7Z)-TETRADEC-7-ENOATE HETSYN ON7 ONO9780307 FORMUL 2 ON7 C30 H35 N O7 FORMUL 3 1WV C17 H32 O4 HELIX 1 AA1 GLU A 28 SER A 37 1 10 HELIX 2 AA2 ASN A 46 ASN A 77 1 32 HELIX 3 AA3 ARG A 78 HIS A 81 5 4 HELIX 4 AA4 PHE A 82 PHE A 107 1 26 HELIX 5 AA5 ASN A 108 ARG A 114 5 7 HELIX 6 AA6 THR A 117 VAL A 150 1 34 HELIX 7 AA7 THR A 157 GLY A 179 1 23 HELIX 8 AA8 ALA A 180 VAL A 184 5 5 HELIX 9 AA9 ASP A 191 CYS A 195 5 5 HELIX 10 AB1 SER A 203 LYS A 1019 1 49 HELIX 11 AB2 ASN A 1022 ALA A 1040 1 19 HELIX 12 AB3 LYS A 1059 GLY A 1082 1 24 HELIX 13 AB4 LYS A 1083 LEU A 1106 1 24 HELIX 14 AB5 ASN A 249 CYS A 284 1 36 HELIX 15 AB6 GLU A 293 ASP A 315 1 23 HELIX 16 AB7 ASP A 315 GLY A 327 1 13 SSBOND 1 CYS A 24 CYS A 190 1555 1555 2.05 SSBOND 2 CYS A 188 CYS A 195 1555 1555 2.04 SSBOND 3 CYS A 284 CYS A 287 1555 1555 2.04 SITE 1 AC1 19 TYR A 34 LYS A 39 HIS A 40 VAL A 52 SITE 2 AC1 19 THR A 109 THR A 113 ARG A 124 GLN A 125 SITE 3 AC1 19 ILE A 128 ASP A 129 LEU A 132 MET A 198 SITE 4 AC1 19 TRP A 271 GLY A 274 LEU A 278 GLU A 293 SITE 5 AC1 19 LYS A 294 PHE A 296 LEU A 297 SITE 1 AC2 3 LEU A 122 THR A 130 GLY A 179 CRYST1 34.280 112.150 154.630 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 0.029172 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008917 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006467 0.00000 ATOM 1 N ASN A 20 15.789 -33.791 77.975 1.00 83.31 N1+ ANISOU 1 N ASN A 20 6399 13122 12133 829 -839 2358 N1+ ATOM 2 CA ASN A 20 15.660 -34.448 76.678 1.00 82.04 C ANISOU 2 CA ASN A 20 6096 12890 12187 720 -793 2307 C ATOM 3 C ASN A 20 14.519 -33.827 75.855 1.00 85.46 C ANISOU 3 C ASN A 20 6612 13277 12584 743 -740 2248 C ATOM 4 O ASN A 20 13.631 -33.183 76.421 1.00 85.39 O ANISOU 4 O ASN A 20 6732 13300 12413 869 -715 2281 O ATOM 5 CB ASN A 20 15.433 -35.948 76.864 1.00 82.23 C ANISOU 5 CB ASN A 20 5879 12931 12434 746 -722 2433 C ATOM 6 N GLU A 21 14.553 -34.019 74.519 1.00 81.29 N ANISOU 6 N GLU A 21 6011 12674 12202 626 -721 2161 N ATOM 7 CA GLU A 21 13.546 -33.488 73.595 1.00 80.46 C ANISOU 7 CA GLU A 21 5966 12523 12084 627 -675 2101 C ATOM 8 C GLU A 21 13.047 -34.593 72.622 1.00 84.73 C ANISOU 8 C GLU A 21 6312 13018 12862 583 -604 2129 C ATOM 9 O GLU A 21 13.832 -35.489 72.284 1.00 84.37 O ANISOU 9 O GLU A 21 6128 12944 12983 495 -613 2121 O ATOM 10 CB GLU A 21 14.120 -32.272 72.815 1.00 81.18 C ANISOU 10 CB GLU A 21 6214 12559 12073 515 -741 1937 C ATOM 11 CG GLU A 21 14.952 -32.558 71.561 1.00 88.67 C ANISOU 11 CG GLU A 21 7068 13443 13180 353 -760 1838 C ATOM 12 CD GLU A 21 16.144 -33.495 71.664 1.00103.31 C ANISOU 12 CD GLU A 21 8776 15303 15173 276 -790 1864 C ATOM 13 OE1 GLU A 21 16.888 -33.424 72.668 1.00103.07 O ANISOU 13 OE1 GLU A 21 8766 15327 15070 305 -841 1920 O ATOM 14 OE2 GLU A 21 16.338 -34.299 70.724 1.00 87.85 O1- ANISOU 14 OE2 GLU A 21 6688 13297 13393 189 -762 1829 O1- ATOM 15 N PRO A 22 11.777 -34.551 72.135 1.00 81.51 N ANISOU 15 N PRO A 22 5894 12600 12476 640 -538 2164 N ATOM 16 CA PRO A 22 11.336 -35.565 71.161 1.00 81.04 C ANISOU 16 CA PRO A 22 5665 12488 12639 582 -488 2181 C ATOM 17 C PRO A 22 12.008 -35.334 69.802 1.00 85.08 C ANISOU 17 C PRO A 22 6185 12918 13224 430 -516 2023 C ATOM 18 O PRO A 22 12.597 -34.272 69.581 1.00 84.30 O ANISOU 18 O PRO A 22 6225 12808 12995 375 -568 1911 O ATOM 19 CB PRO A 22 9.811 -35.377 71.097 1.00 82.75 C ANISOU 19 CB PRO A 22 5897 12723 12821 681 -426 2259 C ATOM 20 CG PRO A 22 9.471 -34.413 72.198 1.00 87.83 C ANISOU 20 CG PRO A 22 6694 13443 13235 817 -428 2312 C ATOM 21 CD PRO A 22 10.697 -33.585 72.403 1.00 83.41 C ANISOU 21 CD PRO A 22 6278 12875 12541 756 -508 2191 C ATOM 22 N GLN A 23 11.937 -36.327 68.901 1.00 82.27 N ANISOU 22 N GLN A 23 5684 12503 13072 362 -485 2018 N ATOM 23 CA GLN A 23 12.605 -36.270 67.602 1.00 81.84 C ANISOU 23 CA GLN A 23 5623 12373 13100 228 -502 1878 C ATOM 24 C GLN A 23 11.923 -35.350 66.580 1.00 85.81 C ANISOU 24 C GLN A 23 6229 12844 13530 199 -492 1787 C ATOM 25 O GLN A 23 10.696 -35.323 66.440 1.00 85.49 O ANISOU 25 O GLN A 23 6175 12808 13498 256 -450 1847 O ATOM 26 CB GLN A 23 12.736 -37.672 66.978 1.00 83.23 C ANISOU 26 CB GLN A 23 5621 12490 13514 177 -471 1903 C ATOM 27 CG GLN A 23 13.772 -38.578 67.656 1.00102.35 C ANISOU 27 CG GLN A 23 7936 14924 16029 169 -485 1954 C ATOM 28 CD GLN A 23 15.201 -38.124 67.440 1.00122.18 C ANISOU 28 CD GLN A 23 10498 17431 18496 80 -534 1849 C ATOM 29 OE1 GLN A 23 15.784 -38.301 66.364 1.00116.91 O ANISOU 29 OE1 GLN A 23 9798 16702 17920 -11 -532 1755 O ATOM 30 NE2 GLN A 23 15.803 -37.547 68.470 1.00114.49 N ANISOU 30 NE2 GLN A 23 9602 16521 17377 107 -583 1869 N ATOM 31 N CYS A 24 12.771 -34.640 65.816 1.00 82.30 N ANISOU 31 N CYS A 24 5879 12370 13023 106 -532 1648 N ATOM 32 CA CYS A 24 12.404 -33.783 64.690 1.00 81.56 C ANISOU 32 CA CYS A 24 5881 12240 12866 57 -529 1541 C ATOM 33 C CYS A 24 12.122 -34.655 63.440 1.00 86.93 C ANISOU 33 C CYS A 24 6448 12851 13731 -26 -500 1491 C ATOM 34 O CYS A 24 12.368 -34.200 62.329 1.00 86.01 O ANISOU 34 O CYS A 24 6376 12694 13611 -113 -512 1371 O ATOM 35 CB CYS A 24 13.472 -32.702 64.461 1.00 81.24 C ANISOU 35 CB CYS A 24 5980 12198 12688 -9 -588 1427 C ATOM 36 SG CYS A 24 13.071 -31.043 65.106 1.00 85.06 S ANISOU 36 SG CYS A 24 6678 12733 12908 82 -620 1436 S ATOM 37 N PHE A 25 11.680 -35.934 63.628 1.00 85.39 N ANISOU 37 N PHE A 25 6109 12640 13697 2 -465 1586 N ATOM 38 CA PHE A 25 11.456 -36.935 62.568 1.00 85.89 C ANISOU 38 CA PHE A 25 6064 12627 13942 -66 -443 1551 C ATOM 39 C PHE A 25 10.558 -38.129 63.015 1.00 92.55 C ANISOU 39 C PHE A 25 6788 13461 14918 -11 -409 1683 C ATOM 40 O PHE A 25 10.599 -39.174 62.359 1.00 92.47 O ANISOU 40 O PHE A 25 6714 13383 15037 -64 -398 1658 O ATOM 41 CB PHE A 25 12.803 -37.496 62.052 1.00 87.74 C ANISOU 41 CB PHE A 25 6225 12823 14288 -135 -457 1497 C ATOM 42 N TYR A 26 9.750 -37.980 64.093 1.00 90.88 N ANISOU 42 N TYR A 26 6547 13314 14668 94 -397 1826 N ATOM 43 CA TYR A 26 8.883 -39.060 64.600 1.00 91.68 C ANISOU 43 CA TYR A 26 6524 13421 14890 156 -367 1981 C ATOM 44 C TYR A 26 7.552 -39.129 63.818 1.00 96.58 C ANISOU 44 C TYR A 26 7142 14024 15531 156 -348 2010 C ATOM 45 O TYR A 26 7.236 -38.208 63.068 1.00 95.73 O ANISOU 45 O TYR A 26 7148 13927 15298 143 -350 1934 O ATOM 46 CB TYR A 26 8.626 -38.877 66.103 1.00 93.40 C ANISOU 46 CB TYR A 26 6743 13732 15013 282 -354 2123 C ATOM 47 N ASN A 27 6.811 -40.254 63.955 1.00 94.42 N ANISOU 47 N ASN A 27 6734 13723 15420 167 -333 2129 N ATOM 48 CA ASN A 27 5.514 -40.489 63.301 1.00 94.59 C ANISOU 48 CA ASN A 27 6721 13726 15492 158 -324 2186 C ATOM 49 C ASN A 27 4.376 -39.799 64.067 1.00 98.50 C ANISOU 49 C ASN A 27 7261 14321 15843 277 -293 2313 C ATOM 50 O ASN A 27 3.360 -39.419 63.471 1.00 97.80 O ANISOU 50 O ASN A 27 7221 14240 15696 270 -285 2304 O ATOM 51 CB ASN A 27 5.226 -41.987 63.187 1.00 96.68 C ANISOU 51 CB ASN A 27 6825 13927 15982 129 -330 2286 C ATOM 52 N GLU A 28 4.539 -39.685 65.399 1.00 95.16 N ANISOU 52 N GLU A 28 6821 13977 15358 392 -271 2437 N ATOM 53 CA GLU A 28 3.613 -39.026 66.320 1.00 94.88 C ANISOU 53 CA GLU A 28 6834 14044 15173 530 -233 2569 C ATOM 54 C GLU A 28 3.844 -37.524 66.276 1.00 95.94 C ANISOU 54 C GLU A 28 7163 14219 15070 565 -235 2456 C ATOM 55 O GLU A 28 3.066 -36.744 66.829 1.00 95.66 O ANISOU 55 O GLU A 28 7204 14259 14883 681 -200 2536 O ATOM 56 CB GLU A 28 3.813 -39.570 67.740 1.00 97.16 C ANISOU 56 CB GLU A 28 7031 14399 15487 643 -210 2742 C ATOM 57 N SER A 29 4.925 -37.135 65.574 1.00 89.97 N ANISOU 57 N SER A 29 6488 13413 14285 469 -274 2277 N ATOM 58 CA SER A 29 5.327 -35.765 65.383 1.00 88.52 C ANISOU 58 CA SER A 29 6488 13250 13895 477 -291 2158 C ATOM 59 C SER A 29 4.290 -34.976 64.572 1.00 90.53 C ANISOU 59 C SER A 29 6826 13503 14067 474 -271 2123 C ATOM 60 O SER A 29 4.253 -33.780 64.823 1.00 90.25 O ANISOU 60 O SER A 29 6933 13517 13841 556 -258 2120 O ATOM 61 CB SER A 29 6.698 -35.672 64.723 1.00 90.99 C ANISOU 61 CB SER A 29 6839 13505 14228 358 -339 1992 C ATOM 62 OG SER A 29 7.757 -35.812 65.656 1.00 98.02 O ANISOU 62 OG SER A 29 7705 14422 15117 384 -360 2022 O ATOM 63 N ILE A 30 3.387 -35.586 63.709 1.00 85.71 N ANISOU 63 N ILE A 30 6127 12839 13599 391 -269 2111 N ATOM 64 CA ILE A 30 2.403 -34.741 62.987 1.00 84.70 C ANISOU 64 CA ILE A 30 6053 12709 13421 375 -252 2087 C ATOM 65 C ILE A 30 1.508 -34.052 64.047 1.00 88.41 C ANISOU 65 C ILE A 30 6564 13269 13759 525 -201 2239 C ATOM 66 O ILE A 30 1.318 -32.846 63.948 1.00 87.76 O ANISOU 66 O ILE A 30 6575 13203 13565 544 -182 2214 O ATOM 67 CB ILE A 30 1.575 -35.373 61.776 1.00 87.52 C ANISOU 67 CB ILE A 30 6279 12999 13976 270 -265 2089 C ATOM 68 CG1 ILE A 30 2.003 -34.698 60.452 1.00 87.22 C ANISOU 68 CG1 ILE A 30 6316 12926 13896 188 -274 1968 C ATOM 69 CG2 ILE A 30 0.036 -35.253 61.875 1.00 88.83 C ANISOU 69 CG2 ILE A 30 6300 13193 14258 329 -241 2291 C ATOM 70 CD1 ILE A 30 3.367 -35.106 59.940 1.00 91.94 C ANISOU 70 CD1 ILE A 30 6979 13461 14494 78 -309 1773 C ATOM 71 N ALA A 31 1.117 -34.768 65.107 1.00 85.28 N ANISOU 71 N ALA A 31 6097 12931 13373 638 -175 2400 N ATOM 72 CA ALA A 31 0.266 -34.272 66.187 1.00 85.57 C ANISOU 72 CA ALA A 31 6166 13063 13286 800 -119 2562 C ATOM 73 C ALA A 31 0.888 -33.108 66.969 1.00 88.97 C ANISOU 73 C ALA A 31 6799 13534 13470 894 -111 2498 C ATOM 74 O ALA A 31 0.149 -32.204 67.370 1.00 88.61 O ANISOU 74 O ALA A 31 6853 13527 13287 973 -73 2524 O ATOM 75 CB ALA A 31 -0.034 -35.414 67.140 1.00 87.16 C ANISOU 75 CB ALA A 31 6220 13313 13583 888 -95 2756 C ATOM 76 N PHE A 32 2.239 -33.110 67.168 1.00 85.10 N ANISOU 76 N PHE A 32 6376 13033 12924 884 -151 2414 N ATOM 77 CA PHE A 32 2.847 -32.032 67.955 1.00 84.91 C ANISOU 77 CA PHE A 32 6558 13040 12665 965 -159 2350 C ATOM 78 C PHE A 32 3.004 -30.759 67.085 1.00 87.05 C ANISOU 78 C PHE A 32 6977 13256 12843 877 -187 2175 C ATOM 79 O PHE A 32 2.843 -29.683 67.652 1.00 87.02 O ANISOU 79 O PHE A 32 7155 13273 12637 957 -181 2141 O ATOM 80 CB PHE A 32 4.123 -32.379 68.763 1.00 87.20 C ANISOU 80 CB PHE A 32 6880 13338 12913 976 -204 2323 C ATOM 81 CG PHE A 32 5.528 -32.488 68.227 1.00 88.45 C ANISOU 81 CG PHE A 32 6993 13430 13184 820 -271 2190 C ATOM 82 CD1 PHE A 32 6.213 -31.362 67.787 1.00 91.00 C ANISOU 82 CD1 PHE A 32 7437 13696 13441 712 -322 2013 C ATOM 83 CD2 PHE A 32 6.242 -33.673 68.363 1.00 91.01 C ANISOU 83 CD2 PHE A 32 7165 13755 13658 799 -282 2254 C ATOM 84 CE1 PHE A 32 7.540 -31.452 67.362 1.00 91.66 C ANISOU 84 CE1 PHE A 32 7475 13729 13623 580 -378 1907 C ATOM 85 CE2 PHE A 32 7.572 -33.759 67.959 1.00 93.48 C ANISOU 85 CE2 PHE A 32 7440 14014 14064 671 -337 2144 C ATOM 86 CZ PHE A 32 8.213 -32.653 67.453 1.00 91.06 C ANISOU 86 CZ PHE A 32 7243 13656 13698 564 -383 1974 C ATOM 87 N PHE A 33 3.156 -30.852 65.748 1.00 81.80 N ANISOU 87 N PHE A 33 6238 12520 12321 721 -215 2069 N ATOM 88 CA PHE A 33 3.199 -29.662 64.890 1.00 80.54 C ANISOU 88 CA PHE A 33 6195 12314 12092 635 -234 1917 C ATOM 89 C PHE A 33 1.791 -29.080 64.674 1.00 83.61 C ANISOU 89 C PHE A 33 6618 12738 12411 711 -177 1992 C ATOM 90 O PHE A 33 1.619 -27.858 64.716 1.00 83.18 O ANISOU 90 O PHE A 33 6724 12682 12200 735 -172 1922 O ATOM 91 CB PHE A 33 3.835 -29.973 63.518 1.00 81.66 C ANISOU 91 CB PHE A 33 6243 12379 12406 460 -273 1795 C ATOM 92 CG PHE A 33 5.234 -30.534 63.537 1.00 83.18 C ANISOU 92 CG PHE A 33 6427 12535 12644 377 -329 1700 C ATOM 93 CD1 PHE A 33 6.334 -29.696 63.630 1.00 86.14 C ANISOU 93 CD1 PHE A 33 6952 12895 12883 342 -375 1578 C ATOM 94 CD2 PHE A 33 5.456 -31.891 63.383 1.00 85.51 C ANISOU 94 CD2 PHE A 33 6560 12806 13125 326 -339 1734 C ATOM 95 CE1 PHE A 33 7.628 -30.216 63.641 1.00 86.94 C ANISOU 95 CE1 PHE A 33 7033 12970 13030 262 -428 1507 C ATOM 96 CE2 PHE A 33 6.755 -32.414 63.379 1.00 88.27 C ANISOU 96 CE2 PHE A 33 6894 13128 13516 256 -384 1659 C ATOM 97 CZ PHE A 33 7.833 -31.574 63.505 1.00 86.14 C ANISOU 97 CZ PHE A 33 6765 12854 13108 223 -429 1550 C ATOM 98 N TYR A 34 0.794 -29.955 64.430 1.00 79.66 N ANISOU 98 N TYR A 34 5965 12272 12029 754 -134 2148 N ATOM 99 CA TYR A 34 -0.606 -29.601 64.165 1.00 79.35 C ANISOU 99 CA TYR A 34 5913 12280 11956 832 -76 2264 C ATOM 100 C TYR A 34 -1.331 -29.040 65.388 1.00 84.27 C ANISOU 100 C TYR A 34 6601 12996 12424 1036 -14 2425 C ATOM 101 O TYR A 34 -2.264 -28.254 65.203 1.00 84.53 O ANISOU 101 O TYR A 34 6633 13080 12403 1126 45 2540 O ATOM 102 CB TYR A 34 -1.370 -30.820 63.653 1.00 80.23 C ANISOU 102 CB TYR A 34 5817 12381 12287 764 -72 2365 C ATOM 103 CG TYR A 34 -1.339 -30.948 62.145 1.00 80.65 C ANISOU 103 CG TYR A 34 5843 12367 12434 609 -104 2245 C ATOM 104 CD1 TYR A 34 -0.256 -31.534 61.498 1.00 81.71 C ANISOU 104 CD1 TYR A 34 5950 12417 12679 460 -161 2088 C ATOM 105 CD2 TYR A 34 -2.400 -30.496 61.365 1.00 81.28 C ANISOU 105 CD2 TYR A 34 5918 12471 12496 616 -74 2298 C ATOM 106 CE1 TYR A 34 -0.227 -31.659 60.113 1.00 81.15 C ANISOU 106 CE1 TYR A 34 5861 12288 12686 327 -188 1978 C ATOM 107 CE2 TYR A 34 -2.373 -30.604 59.980 1.00 81.44 C ANISOU 107 CE2 TYR A 34 5916 12433 12596 475 -107 2188 C ATOM 108 CZ TYR A 34 -1.293 -31.196 59.362 1.00 86.81 C ANISOU 108 CZ TYR A 34 6580 13029 13376 333 -163 2025 C ATOM 109 OH TYR A 34 -1.315 -31.285 58.002 1.00 85.90 O ANISOU 109 OH TYR A 34 6451 12858 13327 204 -193 1916 O ATOM 110 N ASN A 35 -0.935 -29.446 66.619 1.00 81.11 N ANISOU 110 N ASN A 35 6252 12618 11948 1112 -25 2439 N ATOM 111 CA ASN A 35 -1.589 -28.975 67.843 1.00 81.99 C ANISOU 111 CA ASN A 35 6436 12816 11900 1315 31 2583 C ATOM 112 C ASN A 35 -1.105 -27.571 68.206 1.00 85.61 C ANISOU 112 C ASN A 35 7148 13269 12111 1388 28 2479 C ATOM 113 O ASN A 35 -1.911 -26.763 68.679 1.00 85.69 O ANISOU 113 O ASN A 35 7253 13333 11973 1537 93 2566 O ATOM 114 CB ASN A 35 -1.344 -29.952 69.019 1.00 84.76 C ANISOU 114 CB ASN A 35 6703 13197 12304 1362 17 2664 C ATOM 115 CG ASN A 35 -1.624 -29.425 70.416 1.00115.40 C ANISOU 115 CG ASN A 35 10646 17173 16027 1578 75 2821 C ATOM 116 OD1 ASN A 35 -2.740 -29.005 70.770 1.00114.54 O ANISOU 116 OD1 ASN A 35 10591 17125 15804 1719 146 2933 O ATOM 117 ND2 ASN A 35 -0.599 -29.439 71.249 1.00106.83 N ANISOU 117 ND2 ASN A 35 9547 16108 14936 1613 50 2844 N ATOM 118 N ARG A 36 0.210 -27.298 68.027 1.00 81.79 N ANISOU 118 N ARG A 36 6764 12722 11589 1288 -46 2307 N ATOM 119 CA ARG A 36 0.832 -26.011 68.370 1.00 81.94 C ANISOU 119 CA ARG A 36 7026 12721 11388 1332 -73 2195 C ATOM 120 C ARG A 36 0.225 -24.870 67.548 1.00 85.76 C ANISOU 120 C ARG A 36 7611 13173 11799 1308 -53 2122 C ATOM 121 O ARG A 36 -0.072 -23.814 68.102 1.00 85.73 O ANISOU 121 O ARG A 36 7815 13162 11598 1387 -49 2073 O ATOM 122 CB ARG A 36 2.344 -26.054 68.162 1.00 82.11 C ANISOU 122 CB ARG A 36 7094 12680 11423 1201 -169 2040 C ATOM 123 CG ARG A 36 3.070 -26.740 69.302 1.00 93.69 C ANISOU 123 CG ARG A 36 8378 14156 13062 1146 -195 2090 C ATOM 124 CD ARG A 36 4.499 -26.316 69.409 1.00105.89 C ANISOU 124 CD ARG A 36 9992 15660 14582 1052 -285 1964 C ATOM 125 NE ARG A 36 4.977 -26.398 70.795 1.00120.01 N ANISOU 125 NE ARG A 36 11857 17499 16241 1177 -297 2034 N ATOM 126 CZ ARG A 36 4.835 -25.441 71.713 1.00138.30 C ANISOU 126 CZ ARG A 36 14364 19847 18335 1327 -277 2062 C ATOM 127 NH1 ARG A 36 4.207 -24.306 71.413 1.00127.76 N ANISOU 127 NH1 ARG A 36 13158 18498 16888 1373 -241 2032 N ATOM 128 NH2 ARG A 36 5.316 -25.614 72.940 1.00126.24 N1+ ANISOU 128 NH2 ARG A 36 12905 18367 16695 1437 -293 2122 N1+ ATOM 129 N SER A 37 0.042 -25.091 66.232 1.00 82.06 N ANISOU 129 N SER A 37 7001 12681 11495 1190 -46 2109 N ATOM 130 CA SER A 37 -0.564 -24.132 65.326 1.00 81.78 C ANISOU 130 CA SER A 37 7026 12624 11421 1156 -23 2055 C ATOM 131 C SER A 37 -2.098 -24.296 65.305 1.00 87.01 C ANISOU 131 C SER A 37 7552 13354 12152 1238 55 2237 C ATOM 132 O SER A 37 -2.605 -25.346 65.697 1.00 86.69 O ANISOU 132 O SER A 37 7317 13331 12291 1199 57 2330 O ATOM 133 CB SER A 37 0.028 -24.272 63.927 1.00 84.23 C ANISOU 133 CB SER A 37 7268 12860 11874 948 -82 1902 C ATOM 134 OG SER A 37 1.435 -24.063 63.909 1.00 92.48 O ANISOU 134 OG SER A 37 8454 13846 12838 870 -152 1737 O ATOM 135 N GLY A 38 -2.798 -23.263 64.875 1.00 84.66 N ANISOU 135 N GLY A 38 7353 13094 11719 1352 119 2298 N ATOM 136 CA GLY A 38 -4.250 -23.258 64.787 1.00 85.37 C ANISOU 136 CA GLY A 38 7321 13267 11847 1469 200 2511 C ATOM 137 C GLY A 38 -4.745 -24.066 63.607 1.00 89.05 C ANISOU 137 C GLY A 38 7614 13724 12499 1339 196 2535 C ATOM 138 O GLY A 38 -5.256 -23.489 62.642 1.00 88.32 O ANISOU 138 O GLY A 38 7569 13614 12374 1293 206 2479 O ATOM 139 N LYS A 39 -4.595 -25.411 63.678 1.00 85.75 N ANISOU 139 N LYS A 39 6990 13316 12274 1284 180 2630 N ATOM 140 CA LYS A 39 -4.977 -26.359 62.641 1.00 85.14 C ANISOU 140 CA LYS A 39 6744 13215 12390 1143 157 2645 C ATOM 141 C LYS A 39 -5.583 -27.651 63.246 1.00 90.08 C ANISOU 141 C LYS A 39 7160 13886 13178 1170 171 2843 C ATOM 142 O LYS A 39 -5.216 -28.046 64.358 1.00 90.10 O ANISOU 142 O LYS A 39 7139 13932 13164 1276 191 2944 O ATOM 143 CB LYS A 39 -3.780 -26.687 61.751 1.00 86.50 C ANISOU 143 CB LYS A 39 6908 13286 12670 943 73 2434 C ATOM 144 CG LYS A 39 -4.075 -26.318 60.310 1.00 96.21 C ANISOU 144 CG LYS A 39 8251 14471 13834 853 57 2274 C ATOM 145 CD LYS A 39 -4.153 -27.458 59.368 1.00102.40 C ANISOU 145 CD LYS A 39 8913 15192 14803 666 3 2186 C ATOM 146 CE LYS A 39 -4.569 -26.978 58.008 1.00108.85 C ANISOU 146 CE LYS A 39 9698 16029 15629 637 26 2228 C ATOM 147 NZ LYS A 39 -4.513 -28.062 56.997 1.00116.19 N1+ ANISOU 147 NZ LYS A 39 10509 16899 16739 460 -31 2153 N1+ ATOM 148 N HIS A 40 -6.480 -28.327 62.476 1.00 87.20 N ANISOU 148 N HIS A 40 6646 13514 12970 1072 156 2904 N ATOM 149 CA HIS A 40 -7.254 -29.537 62.812 1.00 88.11 C ANISOU 149 CA HIS A 40 6556 13669 13254 1084 162 3108 C ATOM 150 C HIS A 40 -6.410 -30.824 62.984 1.00 91.65 C ANISOU 150 C HIS A 40 6892 14059 13870 995 104 3076 C ATOM 151 O HIS A 40 -5.377 -30.979 62.326 1.00 90.65 O ANISOU 151 O HIS A 40 6786 13842 13813 852 41 2889 O ATOM 152 CB HIS A 40 -8.274 -29.799 61.657 1.00 89.20 C ANISOU 152 CB HIS A 40 6578 13796 13516 973 141 3155 C ATOM 153 CG HIS A 40 -7.672 -30.306 60.374 1.00 92.01 C ANISOU 153 CG HIS A 40 6925 14043 13993 765 58 2950 C ATOM 154 ND1 HIS A 40 -7.403 -31.654 60.179 1.00 93.91 N ANISOU 154 ND1 HIS A 40 7016 14218 14447 635 -7 2947 N ATOM 155 CD2 HIS A 40 -7.309 -29.635 59.265 1.00 93.00 C ANISOU 155 CD2 HIS A 40 7173 14113 14051 672 33 2746 C ATOM 156 CE1 HIS A 40 -6.870 -31.750 58.968 1.00 92.52 C ANISOU 156 CE1 HIS A 40 6878 13952 14323 478 -65 2746 C ATOM 157 NE2 HIS A 40 -6.794 -30.557 58.384 1.00 92.32 N ANISOU 157 NE2 HIS A 40 7011 13935 14131 496 -42 2625 N ATOM 158 N LEU A 41 -6.904 -31.755 63.826 1.00 88.78 N ANISOU 158 N LEU A 41 6401 13754 13578 1086 130 3275 N ATOM 159 CA LEU A 41 -6.333 -33.090 64.013 1.00 88.65 C ANISOU 159 CA LEU A 41 6258 13693 13732 1023 84 3288 C ATOM 160 C LEU A 41 -7.484 -34.056 64.346 1.00 93.08 C ANISOU 160 C LEU A 41 6614 14304 14449 1053 98 3540 C ATOM 161 O LEU A 41 -7.958 -34.088 65.485 1.00 93.35 O ANISOU 161 O LEU A 41 6601 14428 14441 1210 154 3732 O ATOM 162 CB LEU A 41 -5.221 -33.121 65.081 1.00 88.80 C ANISOU 162 CB LEU A 41 6367 13732 13643 1122 98 3251 C ATOM 163 N ALA A 42 -7.992 -34.763 63.328 1.00 89.34 N ANISOU 163 N ALA A 42 6026 13775 14145 906 46 3546 N ATOM 164 CA ALA A 42 -9.133 -35.653 63.478 1.00 89.97 C ANISOU 164 CA ALA A 42 5907 13887 14390 900 39 3781 C ATOM 165 C ALA A 42 -8.700 -37.100 63.648 1.00 93.97 C ANISOU 165 C ALA A 42 6268 14346 15091 850 -4 3842 C ATOM 166 O ALA A 42 -7.640 -37.494 63.163 1.00 92.74 O ANISOU 166 O ALA A 42 6128 14085 15023 729 -63 3665 O ATOM 167 CB ALA A 42 -10.060 -35.519 62.274 1.00 90.55 C ANISOU 167 CB ALA A 42 5931 13912 14563 749 -14 3749 C ATOM 168 N THR A 43 -9.546 -37.877 64.355 1.00 91.96 N ANISOU 168 N THR A 43 5868 14172 14899 954 30 4105 N ATOM 169 CA THR A 43 -9.386 -39.296 64.699 1.00 92.63 C ANISOU 169 CA THR A 43 5788 14231 15176 931 -1 4228 C ATOM 170 C THR A 43 -10.443 -40.138 63.973 1.00 96.67 C ANISOU 170 C THR A 43 6123 14701 15905 805 -64 4364 C ATOM 171 O THR A 43 -10.176 -41.282 63.589 1.00 96.84 O ANISOU 171 O THR A 43 6019 14644 16131 708 -126 4397 O ATOM 172 CB THR A 43 -9.531 -39.479 66.243 1.00104.18 C ANISOU 172 CB THR A 43 7214 15819 16549 1142 82 4438 C ATOM 173 OG1 THR A 43 -8.945 -38.404 66.983 1.00104.48 O ANISOU 173 OG1 THR A 43 7447 15901 16350 1262 136 4310 O ATOM 174 CG2 THR A 43 -9.031 -40.833 66.748 1.00104.26 C ANISOU 174 CG2 THR A 43 7076 15804 16735 1132 56 4539 C ATOM 175 N GLU A 44 -11.673 -39.590 63.857 1.00 92.61 N ANISOU 175 N GLU A 44 5606 14237 15345 803 -53 4441 N ATOM 176 CA GLU A 44 -12.757 -40.312 63.207 1.00 92.72 C ANISOU 176 CA GLU A 44 5465 14224 15539 683 -118 4580 C ATOM 177 C GLU A 44 -13.121 -39.627 61.875 1.00 94.95 C ANISOU 177 C GLU A 44 5833 14509 15736 616 -129 4489 C ATOM 178 O GLU A 44 -12.661 -38.528 61.538 1.00 93.58 O ANISOU 178 O GLU A 44 5816 14388 15351 707 -64 4391 O ATOM 179 CB GLU A 44 -13.991 -40.519 64.116 1.00 95.53 C ANISOU 179 CB GLU A 44 5646 14701 15952 808 -74 4927 C ATOM 180 CG GLU A 44 -14.784 -41.764 63.720 1.00107.67 C ANISOU 180 CG GLU A 44 6978 16183 17749 668 -166 5094 C ATOM 181 CD GLU A 44 -15.559 -42.506 64.796 1.00130.82 C ANISOU 181 CD GLU A 44 9719 19225 20761 786 -128 5443 C ATOM 182 OE1 GLU A 44 -14.918 -42.977 65.763 1.00125.84 O ANISOU 182 OE1 GLU A 44 9038 18607 20170 866 -101 5508 O ATOM 183 OE2 GLU A 44 -16.781 -42.718 64.611 1.00125.98 O1- ANISOU 183 OE2 GLU A 44 8998 18689 20180 795 -126 5660 O1- ATOM 184 N TRP A 45 -13.868 -40.373 61.078 1.00 91.39 N ANISOU 184 N TRP A 45 5282 13993 15451 451 -219 4521 N ATOM 185 CA TRP A 45 -14.273 -40.046 59.732 1.00 90.59 C ANISOU 185 CA TRP A 45 5228 13884 15307 360 -249 4455 C ATOM 186 C TRP A 45 -15.501 -39.122 59.729 1.00 93.63 C ANISOU 186 C TRP A 45 5575 14422 15580 494 -172 4688 C ATOM 187 O TRP A 45 -16.626 -39.563 59.979 1.00 94.26 O ANISOU 187 O TRP A 45 5520 14598 15696 609 -129 4960 O ATOM 188 CB TRP A 45 -14.558 -41.361 58.976 1.00 89.89 C ANISOU 188 CB TRP A 45 5028 13683 15444 148 -377 4453 C ATOM 189 CG TRP A 45 -13.365 -41.909 58.253 1.00 90.09 C ANISOU 189 CG TRP A 45 5119 13548 15563 5 -453 4193 C ATOM 190 CD1 TRP A 45 -12.592 -42.978 58.607 1.00 93.37 C ANISOU 190 CD1 TRP A 45 5459 13873 16142 -44 -500 4192 C ATOM 191 CD2 TRP A 45 -12.795 -41.368 57.065 1.00 88.89 C ANISOU 191 CD2 TRP A 45 5121 13311 15343 -98 -483 3903 C ATOM 192 NE1 TRP A 45 -11.586 -43.156 57.686 1.00 91.98 N ANISOU 192 NE1 TRP A 45 5385 13562 16003 -166 -554 3919 N ATOM 193 CE2 TRP A 45 -11.683 -42.180 56.730 1.00 92.55 C ANISOU 193 CE2 TRP A 45 5596 13636 15933 -202 -545 3740 C ATOM 194 CE3 TRP A 45 -13.119 -40.278 56.240 1.00 89.38 C ANISOU 194 CE3 TRP A 45 5312 13403 15247 -108 -460 3771 C ATOM 195 CZ2 TRP A 45 -10.888 -41.924 55.613 1.00 91.02 C ANISOU 195 CZ2 TRP A 45 5534 13339 15710 -308 -582 3456 C ATOM 196 CZ3 TRP A 45 -12.324 -40.018 55.143 1.00 89.96 C ANISOU 196 CZ3 TRP A 45 5513 13373 15295 -220 -500 3489 C ATOM 197 CH2 TRP A 45 -11.222 -40.836 54.838 1.00 90.42 C ANISOU 197 CH2 TRP A 45 5578 13301 15478 -315 -558 3336 C ATOM 198 N ASN A 46 -15.278 -37.834 59.418 1.00 88.26 N ANISOU 198 N ASN A 46 5004 13764 14767 478 -155 4588 N ATOM 199 CA ASN A 46 -16.334 -36.804 59.342 1.00 87.77 C ANISOU 199 CA ASN A 46 4923 13838 14587 595 -81 4782 C ATOM 200 C ASN A 46 -17.164 -36.939 58.042 1.00 88.74 C ANISOU 200 C ASN A 46 5015 13930 14771 435 -156 4758 C ATOM 201 O ASN A 46 -16.720 -37.602 57.105 1.00 87.15 O ANISOU 201 O ASN A 46 4893 13611 14606 274 -233 4512 O ATOM 202 CB ASN A 46 -15.720 -35.398 59.432 1.00 89.47 C ANISOU 202 CB ASN A 46 5332 14124 14538 774 35 4686 C ATOM 203 CG ASN A 46 -16.682 -34.335 59.935 1.00117.74 C ANISOU 203 CG ASN A 46 8898 17863 17976 967 144 4927 C ATOM 204 OD1 ASN A 46 -17.530 -33.826 59.196 1.00114.33 O ANISOU 204 OD1 ASN A 46 8331 17497 17610 949 136 5140 O ATOM 205 ND2 ASN A 46 -16.626 -34.017 61.229 1.00110.82 N ANISOU 205 ND2 ASN A 46 8170 17048 16888 1159 249 4895 N ATOM 206 N THR A 47 -18.362 -36.317 57.993 1.00 84.72 N ANISOU 206 N THR A 47 4391 13535 14266 486 -131 5021 N ATOM 207 CA THR A 47 -19.286 -36.367 56.850 1.00 84.03 C ANISOU 207 CA THR A 47 4247 13451 14229 354 -195 5066 C ATOM 208 C THR A 47 -18.753 -35.495 55.685 1.00 84.73 C ANISOU 208 C THR A 47 4525 13485 14182 286 -199 4776 C ATOM 209 O THR A 47 -18.801 -35.934 54.533 1.00 84.18 O ANISOU 209 O THR A 47 4445 13344 14198 103 -298 4677 O ATOM 210 CB THR A 47 -20.708 -35.945 57.282 1.00 91.15 C ANISOU 210 CB THR A 47 5037 14522 15075 497 -116 5395 C ATOM 211 OG1 THR A 47 -21.077 -36.664 58.467 1.00 90.95 O ANISOU 211 OG1 THR A 47 4844 14556 15157 585 -98 5663 O ATOM 212 CG2 THR A 47 -21.745 -36.180 56.201 1.00 89.43 C ANISOU 212 CG2 THR A 47 4726 14321 14931 358 -191 5491 C ATOM 213 N VAL A 48 -18.253 -34.280 55.974 1.00 78.83 N ANISOU 213 N VAL A 48 3954 12771 13228 431 -96 4642 N ATOM 214 CA VAL A 48 -17.737 -33.380 54.933 1.00 76.80 C ANISOU 214 CA VAL A 48 3884 12468 12830 389 -87 4376 C ATOM 215 C VAL A 48 -16.332 -33.856 54.453 1.00 78.15 C ANISOU 215 C VAL A 48 4130 12483 13081 232 -174 4084 C ATOM 216 O VAL A 48 -15.964 -33.596 53.297 1.00 77.38 O ANISOU 216 O VAL A 48 4069 12311 13020 75 -247 3922 O ATOM 217 CB VAL A 48 -17.716 -31.885 55.359 1.00 80.38 C ANISOU 217 CB VAL A 48 4501 13004 13035 600 46 4351 C ATOM 218 CG1 VAL A 48 -19.127 -31.314 55.452 1.00 80.91 C ANISOU 218 CG1 VAL A 48 4539 13204 12999 715 124 4564 C ATOM 219 CG2 VAL A 48 -16.946 -31.665 56.657 1.00 80.53 C ANISOU 219 CG2 VAL A 48 4534 13052 13011 760 111 4415 C ATOM 220 N SER A 49 -15.579 -34.580 55.330 1.00 72.86 N ANISOU 220 N SER A 49 3470 11768 12445 277 -166 4034 N ATOM 221 CA SER A 49 -14.244 -35.130 55.022 1.00 71.00 C ANISOU 221 CA SER A 49 3296 11395 12286 155 -234 3783 C ATOM 222 C SER A 49 -14.331 -36.239 53.957 1.00 73.64 C ANISOU 222 C SER A 49 3528 11622 12829 -53 -360 3747 C ATOM 223 O SER A 49 -13.412 -36.395 53.140 1.00 72.12 O ANISOU 223 O SER A 49 3421 11322 12662 -181 -419 3505 O ATOM 224 CB SER A 49 -13.566 -35.671 56.278 1.00 74.09 C ANISOU 224 CB SER A 49 3669 11780 12703 249 -203 3815 C ATOM 225 OG SER A 49 -13.237 -34.638 57.193 1.00 81.50 O ANISOU 225 OG SER A 49 4734 12794 13439 429 -100 3801 O ATOM 226 N LYS A 50 -15.443 -37.001 53.971 1.00 70.66 N ANISOU 226 N LYS A 50 2972 11276 12599 -84 -404 3993 N ATOM 227 CA LYS A 50 -15.726 -38.074 53.018 1.00 70.74 C ANISOU 227 CA LYS A 50 2879 11186 12813 -280 -536 3996 C ATOM 228 C LYS A 50 -16.086 -37.509 51.654 1.00 73.68 C ANISOU 228 C LYS A 50 3313 11543 13140 -399 -584 3884 C ATOM 229 O LYS A 50 -15.737 -38.115 50.641 1.00 73.26 O ANISOU 229 O LYS A 50 3288 11368 13179 -565 -683 3711 O ATOM 230 CB LYS A 50 -16.874 -38.971 53.514 1.00 74.55 C ANISOU 230 CB LYS A 50 3153 11722 13449 -273 -568 4318 C ATOM 231 CG LYS A 50 -16.501 -39.889 54.658 1.00 87.41 C ANISOU 231 CG LYS A 50 4695 13352 15164 -183 -541 4442 C ATOM 232 CD LYS A 50 -17.708 -40.643 55.181 1.00 97.90 C ANISOU 232 CD LYS A 50 5810 14753 16635 -168 -567 4787 C ATOM 233 CE LYS A 50 -17.338 -41.512 56.354 1.00107.15 C ANISOU 233 CE LYS A 50 6880 15935 17898 -77 -539 4934 C ATOM 234 NZ LYS A 50 -18.525 -42.201 56.918 1.00115.73 N1+ ANISOU 234 NZ LYS A 50 7754 17109 19110 -49 -554 5291 N1+ ATOM 235 N LEU A 51 -16.802 -36.365 51.628 1.00 69.35 N ANISOU 235 N LEU A 51 2792 11117 12441 -303 -509 3980 N ATOM 236 CA LEU A 51 -17.232 -35.725 50.397 1.00 68.63 C ANISOU 236 CA LEU A 51 2755 11033 12290 -396 -541 3897 C ATOM 237 C LEU A 51 -16.077 -34.970 49.741 1.00 70.37 C ANISOU 237 C LEU A 51 3167 11188 12382 -420 -520 3582 C ATOM 238 O LEU A 51 -16.006 -34.991 48.518 1.00 69.89 O ANISOU 238 O LEU A 51 3150 11061 12343 -564 -594 3430 O ATOM 239 CB LEU A 51 -18.425 -34.788 50.657 1.00 69.25 C ANISOU 239 CB LEU A 51 2795 11270 12249 -270 -457 4120 C ATOM 240 CG LEU A 51 -19.315 -34.390 49.461 1.00 74.10 C ANISOU 240 CG LEU A 51 3425 11919 12811 -357 -488 4108 C ATOM 241 CD1 LEU A 51 -18.829 -33.143 48.782 1.00 72.88 C ANISOU 241 CD1 LEU A 51 3462 11773 12454 -305 -415 3886 C ATOM 242 CD2 LEU A 51 -19.583 -35.544 48.496 1.00 77.64 C ANISOU 242 CD2 LEU A 51 3798 12268 13435 -584 -644 4064 C ATOM 243 N VAL A 52 -15.193 -34.309 50.526 1.00 65.61 N ANISOU 243 N VAL A 52 2680 10611 11639 -278 -423 3495 N ATOM 244 CA VAL A 52 -14.018 -33.575 50.007 1.00 64.16 C ANISOU 244 CA VAL A 52 2678 10376 11325 -286 -396 3214 C ATOM 245 C VAL A 52 -13.032 -34.587 49.355 1.00 67.22 C ANISOU 245 C VAL A 52 3085 10615 11840 -450 -493 2996 C ATOM 246 O VAL A 52 -12.401 -34.286 48.331 1.00 66.19 O ANISOU 246 O VAL A 52 3035 10433 11683 -556 -533 2813 O ATOM 247 CB VAL A 52 -13.339 -32.725 51.123 1.00 67.52 C ANISOU 247 CB VAL A 52 3210 10849 11594 -109 -289 3188 C ATOM 248 CG1 VAL A 52 -11.869 -32.459 50.838 1.00 66.14 C ANISOU 248 CG1 VAL A 52 3199 10597 11333 -146 -288 2899 C ATOM 249 CG2 VAL A 52 -14.096 -31.438 51.383 1.00 67.53 C ANISOU 249 CG2 VAL A 52 3246 10984 11429 53 -188 3344 C ATOM 250 N MET A 53 -12.929 -35.787 49.957 1.00 63.60 N ANISOU 250 N MET A 53 2551 10094 11519 -463 -527 3028 N ATOM 251 CA MET A 53 -12.099 -36.874 49.444 1.00 63.04 C ANISOU 251 CA MET A 53 2489 9881 11583 -601 -613 2852 C ATOM 252 C MET A 53 -12.752 -37.499 48.197 1.00 67.22 C ANISOU 252 C MET A 53 2959 10347 12234 -770 -724 2850 C ATOM 253 O MET A 53 -12.082 -37.753 47.191 1.00 66.59 O ANISOU 253 O MET A 53 2966 10184 12151 -879 -773 2637 O ATOM 254 CB MET A 53 -11.875 -37.936 50.527 1.00 65.94 C ANISOU 254 CB MET A 53 2767 10208 12079 -566 -621 2938 C ATOM 255 CG MET A 53 -10.973 -39.058 50.075 1.00 70.11 C ANISOU 255 CG MET A 53 3288 10585 12765 -704 -712 2790 C ATOM 256 SD MET A 53 -10.818 -40.342 51.329 1.00 75.51 S ANISOU 256 SD MET A 53 3845 11216 13628 -678 -732 2921 S ATOM 257 CE MET A 53 -9.772 -41.511 50.484 1.00 72.54 C ANISOU 257 CE MET A 53 3482 10654 13426 -864 -852 2736 C ATOM 258 N GLY A 54 -14.054 -37.749 48.298 1.00 64.63 N ANISOU 258 N GLY A 54 2486 10064 12006 -788 -765 3093 N ATOM 259 CA GLY A 54 -14.866 -38.333 47.239 1.00 65.36 C ANISOU 259 CA GLY A 54 2505 10106 12224 -949 -883 3139 C ATOM 260 C GLY A 54 -14.863 -37.502 45.975 1.00 68.85 C ANISOU 260 C GLY A 54 3044 10547 12568 -1033 -908 2986 C ATOM 261 O GLY A 54 -14.652 -38.037 44.885 1.00 68.79 O ANISOU 261 O GLY A 54 3064 10431 12641 -1184 -1010 2849 O ATOM 262 N LEU A 55 -15.065 -36.177 46.120 1.00 64.59 N ANISOU 262 N LEU A 55 2566 10126 11851 -929 -813 3007 N ATOM 263 CA LEU A 55 -15.068 -35.218 45.013 1.00 63.52 C ANISOU 263 CA LEU A 55 2526 10011 11598 -983 -815 2875 C ATOM 264 C LEU A 55 -13.647 -35.024 44.501 1.00 66.20 C ANISOU 264 C LEU A 55 3021 10264 11868 -1014 -804 2572 C ATOM 265 O LEU A 55 -13.453 -34.945 43.292 1.00 65.41 O ANISOU 265 O LEU A 55 2983 10116 11753 -1125 -859 2420 O ATOM 266 CB LEU A 55 -15.686 -33.876 45.451 1.00 63.21 C ANISOU 266 CB LEU A 55 2505 10122 11390 -843 -706 3004 C ATOM 267 CG LEU A 55 -15.943 -32.823 44.374 1.00 67.50 C ANISOU 267 CG LEU A 55 3112 10707 11828 -897 -711 2934 C ATOM 268 CD1 LEU A 55 -17.161 -33.176 43.522 1.00 68.93 C ANISOU 268 CD1 LEU A 55 3159 10938 12094 -980 -785 3141 C ATOM 269 CD2 LEU A 55 -16.173 -31.485 44.999 1.00 68.98 C ANISOU 269 CD2 LEU A 55 3396 10999 11816 -741 -582 2939 C ATOM 270 N GLY A 56 -12.679 -35.004 45.424 1.00 62.72 N ANISOU 270 N GLY A 56 2638 9810 11382 -913 -733 2499 N ATOM 271 CA GLY A 56 -11.253 -34.844 45.147 1.00 61.77 C ANISOU 271 CA GLY A 56 2653 9619 11198 -926 -714 2237 C ATOM 272 C GLY A 56 -10.669 -35.894 44.222 1.00 66.45 C ANISOU 272 C GLY A 56 3260 10074 11913 -1073 -812 2068 C ATOM 273 O GLY A 56 -9.991 -35.556 43.252 1.00 65.05 O ANISOU 273 O GLY A 56 3183 9860 11674 -1137 -825 1873 O ATOM 274 N ILE A 57 -10.965 -37.176 44.489 1.00 65.18 N ANISOU 274 N ILE A 57 3001 9838 11926 -1126 -880 2149 N ATOM 275 CA ILE A 57 -10.506 -38.320 43.688 1.00 66.16 C ANISOU 275 CA ILE A 57 3136 9818 12183 -1259 -979 2010 C ATOM 276 C ILE A 57 -11.226 -38.309 42.310 1.00 71.84 C ANISOU 276 C ILE A 57 3857 10518 12922 -1392 -1072 1991 C ATOM 277 O ILE A 57 -10.564 -38.483 41.288 1.00 71.97 O ANISOU 277 O ILE A 57 3952 10435 12958 -1489 -1130 1799 O ATOM 278 CB ILE A 57 -10.727 -39.657 44.464 1.00 70.36 C ANISOU 278 CB ILE A 57 3558 10279 12896 -1267 -1024 2131 C ATOM 279 CG1 ILE A 57 -9.853 -39.732 45.738 1.00 70.45 C ANISOU 279 CG1 ILE A 57 3609 10259 12898 -1179 -956 2041 C ATOM 280 CG2 ILE A 57 -10.458 -40.869 43.568 1.00 72.13 C ANISOU 280 CG2 ILE A 57 3757 10364 13286 -1421 -1156 2086 C ATOM 281 CD1 ILE A 57 -10.165 -40.985 46.744 1.00 81.65 C ANISOU 281 CD1 ILE A 57 4986 11786 14251 -1029 -862 2192 C ATOM 282 N THR A 58 -12.557 -38.058 42.289 1.00 69.19 N ANISOU 282 N THR A 58 3442 10282 12567 -1391 -1082 2188 N ATOM 283 CA THR A 58 -13.387 -37.998 41.074 1.00 69.90 C ANISOU 283 CA THR A 58 3522 10372 12665 -1514 -1171 2197 C ATOM 284 C THR A 58 -12.824 -36.956 40.082 1.00 73.88 C ANISOU 284 C THR A 58 4164 10898 13010 -1525 -1134 1990 C ATOM 285 O THR A 58 -12.764 -37.231 38.880 1.00 73.98 O ANISOU 285 O THR A 58 4231 10838 13041 -1645 -1217 1850 O ATOM 286 CB THR A 58 -14.849 -37.692 41.445 1.00 76.55 C ANISOU 286 CB THR A 58 4236 11334 13514 -1489 -1172 2478 C ATOM 287 OG1 THR A 58 -15.292 -38.654 42.406 1.00 78.03 O ANISOU 287 OG1 THR A 58 4293 11508 13846 -1466 -1195 2676 O ATOM 288 CG2 THR A 58 -15.789 -37.705 40.242 1.00 74.59 C ANISOU 288 CG2 THR A 58 3960 11088 13293 -1628 -1279 2514 C ATOM 289 N VAL A 59 -12.390 -35.784 40.591 1.00 69.91 N ANISOU 289 N VAL A 59 3719 10492 12350 -1398 -1013 1973 N ATOM 290 CA VAL A 59 -11.802 -34.710 39.789 1.00 69.25 C ANISOU 290 CA VAL A 59 3762 10438 12113 -1393 -967 1792 C ATOM 291 C VAL A 59 -10.400 -35.172 39.309 1.00 74.73 C ANISOU 291 C VAL A 59 4557 11013 12823 -1439 -983 1536 C ATOM 292 O VAL A 59 -10.091 -35.003 38.130 1.00 74.56 O ANISOU 292 O VAL A 59 4616 10962 12750 -1512 -1013 1374 O ATOM 293 CB VAL A 59 -11.765 -33.356 40.561 1.00 72.11 C ANISOU 293 CB VAL A 59 4167 10920 12311 -1242 -838 1846 C ATOM 294 CG1 VAL A 59 -10.984 -32.294 39.803 1.00 71.03 C ANISOU 294 CG1 VAL A 59 4152 10814 12023 -1248 -798 1679 C ATOM 295 CG2 VAL A 59 -13.168 -32.843 40.841 1.00 72.54 C ANISOU 295 CG2 VAL A 59 4117 11090 12357 -1177 -812 2114 C ATOM 296 N CYS A 60 -9.597 -35.798 40.204 1.00 72.07 N ANISOU 296 N CYS A 60 4208 10610 12565 -1398 -969 1515 N ATOM 297 CA CYS A 60 -8.248 -36.310 39.926 1.00 71.89 C ANISOU 297 CA CYS A 60 4264 10479 12572 -1425 -976 1303 C ATOM 298 C CYS A 60 -8.246 -37.311 38.767 1.00 75.94 C ANISOU 298 C CYS A 60 4798 10878 13179 -1562 -1086 1192 C ATOM 299 O CYS A 60 -7.369 -37.217 37.904 1.00 75.15 O ANISOU 299 O CYS A 60 4799 10739 13016 -1598 -1086 996 O ATOM 300 CB CYS A 60 -7.633 -36.933 41.174 1.00 72.72 C ANISOU 300 CB CYS A 60 4325 10544 12763 -1357 -947 1349 C ATOM 301 SG CYS A 60 -6.880 -35.736 42.300 1.00 75.89 S ANISOU 301 SG CYS A 60 4762 11047 13025 -1194 -816 1379 S ATOM 302 N ILE A 61 -9.205 -38.257 38.751 1.00 73.39 N ANISOU 302 N ILE A 61 4382 10498 13004 -1637 -1182 1320 N ATOM 303 CA ILE A 61 -9.325 -39.273 37.699 1.00 74.07 C ANISOU 303 CA ILE A 61 4492 10461 13190 -1773 -1304 1231 C ATOM 304 C ILE A 61 -9.626 -38.572 36.357 1.00 77.68 C ANISOU 304 C ILE A 61 5024 10955 13537 -1840 -1332 1132 C ATOM 305 O ILE A 61 -9.011 -38.915 35.349 1.00 77.35 O ANISOU 305 O ILE A 61 5083 10830 13477 -1894 -1363 933 O ATOM 306 CB ILE A 61 -10.390 -40.363 38.058 1.00 78.55 C ANISOU 306 CB ILE A 61 4938 10979 13930 -1848 -1410 1424 C ATOM 307 CG1 ILE A 61 -10.085 -41.090 39.408 1.00 78.98 C ANISOU 307 CG1 ILE A 61 4911 10998 14099 -1778 -1381 1531 C ATOM 308 CG2 ILE A 61 -10.613 -41.368 36.905 1.00 80.66 C ANISOU 308 CG2 ILE A 61 5246 11111 14290 -1999 -1553 1331 C ATOM 309 CD1 ILE A 61 -8.726 -41.899 39.529 1.00 83.92 C ANISOU 309 CD1 ILE A 61 5606 11503 14776 -1755 -1360 1354 C ATOM 310 N PHE A 62 -10.512 -37.558 36.370 1.00 73.89 N ANISOU 310 N PHE A 62 4497 10603 12975 -1824 -1310 1270 N ATOM 311 CA PHE A 62 -10.884 -36.773 35.189 1.00 73.51 C ANISOU 311 CA PHE A 62 4509 10606 12814 -1879 -1328 1196 C ATOM 312 C PHE A 62 -9.674 -35.990 34.641 1.00 75.17 C ANISOU 312 C PHE A 62 4848 10830 12884 -1825 -1241 979 C ATOM 313 O PHE A 62 -9.526 -35.904 33.421 1.00 74.93 O ANISOU 313 O PHE A 62 4899 10765 12806 -1895 -1282 826 O ATOM 314 CB PHE A 62 -12.052 -35.816 35.505 1.00 75.56 C ANISOU 314 CB PHE A 62 4688 11012 13010 -1850 -1301 1404 C ATOM 315 CG PHE A 62 -12.530 -34.975 34.343 1.00 77.02 C ANISOU 315 CG PHE A 62 4939 11270 13056 -1880 -1291 1327 C ATOM 316 CD1 PHE A 62 -13.346 -35.522 33.356 1.00 81.29 C ANISOU 316 CD1 PHE A 62 5491 11775 13621 -2014 -1407 1291 C ATOM 317 CD2 PHE A 62 -12.184 -33.634 34.245 1.00 78.09 C ANISOU 317 CD2 PHE A 62 5134 11503 13035 -1776 -1170 1283 C ATOM 318 CE1 PHE A 62 -13.786 -34.743 32.280 1.00 82.05 C ANISOU 318 CE1 PHE A 62 5648 11941 13586 -2040 -1396 1217 C ATOM 319 CE2 PHE A 62 -12.630 -32.854 33.173 1.00 80.83 C ANISOU 319 CE2 PHE A 62 5541 11913 13257 -1803 -1159 1211 C ATOM 320 CZ PHE A 62 -13.427 -33.414 32.196 1.00 79.93 C ANISOU 320 CZ PHE A 62 5429 11773 13169 -1932 -1268 1181 C ATOM 321 N ILE A 63 -8.828 -35.417 35.534 1.00 69.80 N ANISOU 321 N ILE A 63 4184 10200 12136 -1703 -1126 973 N ATOM 322 CA ILE A 63 -7.620 -34.666 35.156 1.00 68.34 C ANISOU 322 CA ILE A 63 4109 10034 11824 -1649 -1043 793 C ATOM 323 C ILE A 63 -6.641 -35.618 34.441 1.00 71.38 C ANISOU 323 C ILE A 63 4572 10297 12251 -1709 -1086 584 C ATOM 324 O ILE A 63 -6.102 -35.268 33.392 1.00 70.51 O ANISOU 324 O ILE A 63 4546 10192 12052 -1740 -1084 438 O ATOM 325 CB ILE A 63 -6.957 -33.972 36.391 1.00 70.75 C ANISOU 325 CB ILE A 63 4413 10387 12080 -1519 -936 831 C ATOM 326 CG1 ILE A 63 -7.911 -32.953 37.053 1.00 70.85 C ANISOU 326 CG1 ILE A 63 4393 10532 11994 -1438 -871 996 C ATOM 327 CG2 ILE A 63 -5.659 -33.280 35.998 1.00 70.57 C ANISOU 327 CG2 ILE A 63 4496 10347 11972 -1484 -874 634 C ATOM 328 CD1 ILE A 63 -7.516 -32.514 38.488 1.00 77.29 C ANISOU 328 CD1 ILE A 63 5191 11390 12784 -1309 -786 1088 C ATOM 329 N MET A 64 -6.471 -36.841 34.984 1.00 68.03 N ANISOU 329 N MET A 64 4120 9768 11961 -1720 -1124 579 N ATOM 330 CA MET A 64 -5.573 -37.878 34.456 1.00 68.01 C ANISOU 330 CA MET A 64 4190 9641 12011 -1758 -1156 397 C ATOM 331 C MET A 64 -6.104 -38.489 33.141 1.00 72.97 C ANISOU 331 C MET A 64 4867 10202 12657 -1873 -1262 314 C ATOM 332 O MET A 64 -5.374 -39.232 32.481 1.00 72.92 O ANISOU 332 O MET A 64 4960 10148 12600 -1889 -1260 129 O ATOM 333 CB MET A 64 -5.345 -38.982 35.503 1.00 70.65 C ANISOU 333 CB MET A 64 4470 9878 12495 -1740 -1175 444 C ATOM 334 CG MET A 64 -4.446 -38.537 36.637 1.00 72.99 C ANISOU 334 CG MET A 64 4726 10233 12773 -1626 -1076 514 C ATOM 335 SD MET A 64 -4.318 -39.731 37.982 1.00 77.36 S ANISOU 335 SD MET A 64 5216 10679 13500 -1600 -1091 566 S ATOM 336 CE MET A 64 -2.787 -40.488 37.566 1.00 73.94 C ANISOU 336 CE MET A 64 4890 10153 13050 -1589 -1059 327 C ATOM 337 N LEU A 65 -7.349 -38.169 32.752 1.00 69.68 N ANISOU 337 N LEU A 65 4381 9788 12307 -1951 -1354 455 N ATOM 338 CA LEU A 65 -7.971 -38.677 31.531 1.00 70.36 C ANISOU 338 CA LEU A 65 4506 9809 12417 -2074 -1475 402 C ATOM 339 C LEU A 65 -8.094 -37.576 30.457 1.00 73.01 C ANISOU 339 C LEU A 65 4905 10238 12597 -2093 -1456 326 C ATOM 340 O LEU A 65 -7.776 -37.829 29.297 1.00 73.09 O ANISOU 340 O LEU A 65 5013 10187 12571 -2149 -1505 162 O ATOM 341 CB LEU A 65 -9.363 -39.255 31.866 1.00 71.71 C ANISOU 341 CB LEU A 65 4566 9967 12712 -2154 -1581 608 C ATOM 342 CG LEU A 65 -9.490 -40.709 32.372 1.00 77.82 C ANISOU 342 CG LEU A 65 5317 10584 13666 -2213 -1679 625 C ATOM 343 CD1 LEU A 65 -8.496 -41.111 33.478 1.00 77.34 C ANISOU 343 CD1 LEU A 65 5223 10489 13672 -2112 -1596 639 C ATOM 344 CD2 LEU A 65 -10.920 -41.025 32.756 1.00 81.48 C ANISOU 344 CD2 LEU A 65 5667 11048 14242 -2307 -1794 840 C ATOM 345 N ALA A 66 -8.549 -36.366 30.839 1.00 68.26 N ANISOU 345 N ALA A 66 4255 9782 11900 -2038 -1383 441 N ATOM 346 CA ALA A 66 -8.737 -35.229 29.925 1.00 67.48 C ANISOU 346 CA ALA A 66 4203 9783 11654 -2047 -1355 395 C ATOM 347 C ALA A 66 -7.400 -34.658 29.428 1.00 70.54 C ANISOU 347 C ALA A 66 4699 10176 11926 -1987 -1268 193 C ATOM 348 O ALA A 66 -7.280 -34.340 28.242 1.00 70.17 O ANISOU 348 O ALA A 66 4723 10149 11788 -2027 -1283 80 O ATOM 349 CB ALA A 66 -9.541 -34.135 30.605 1.00 67.59 C ANISOU 349 CB ALA A 66 4136 9939 11605 -1988 -1292 584 C ATOM 350 N ASN A 67 -6.399 -34.536 30.324 1.00 66.41 N ANISOU 350 N ASN A 67 4185 9641 11409 -1894 -1180 156 N ATOM 351 CA ASN A 67 -5.077 -34.020 29.972 1.00 65.62 C ANISOU 351 CA ASN A 67 4174 9545 11214 -1838 -1098 -16 C ATOM 352 C ASN A 67 -4.262 -35.078 29.221 1.00 71.02 C ANISOU 352 C ASN A 67 4934 10104 11947 -1876 -1144 -191 C ATOM 353 O ASN A 67 -3.357 -34.714 28.469 1.00 70.03 O ANISOU 353 O ASN A 67 4885 9979 11746 -1839 -1087 -339 O ATOM 354 CB ASN A 67 -4.329 -33.532 31.202 1.00 64.78 C ANISOU 354 CB ASN A 67 4047 9475 11092 -1732 -997 21 C ATOM 355 CG ASN A 67 -4.917 -32.279 31.786 1.00 85.02 C ANISOU 355 CG ASN A 67 6585 12167 13551 -1675 -929 134 C ATOM 356 OD1 ASN A 67 -4.514 -31.160 31.447 1.00 75.90 O ANISOU 356 OD1 ASN A 67 5487 11073 12278 -1631 -858 63 O ATOM 357 ND2 ASN A 67 -5.906 -32.445 32.656 1.00 77.08 N ANISOU 357 ND2 ASN A 67 5496 11205 12586 -1674 -952 319 N ATOM 358 N LEU A 68 -4.591 -36.374 29.400 1.00 69.64 N ANISOU 358 N LEU A 68 4742 9822 11896 -1948 -1248 -168 N ATOM 359 CA LEU A 68 -3.931 -37.474 28.687 1.00 70.76 C ANISOU 359 CA LEU A 68 4969 9831 12086 -1983 -1300 -329 C ATOM 360 C LEU A 68 -4.428 -37.509 27.241 1.00 75.50 C ANISOU 360 C LEU A 68 5653 10432 12603 -2056 -1363 -438 C ATOM 361 O LEU A 68 -3.649 -37.810 26.336 1.00 75.09 O ANISOU 361 O LEU A 68 5699 10345 12486 -2033 -1336 -610 O ATOM 362 CB LEU A 68 -4.201 -38.820 29.396 1.00 72.06 C ANISOU 362 CB LEU A 68 5089 9869 12420 -2031 -1392 -260 C ATOM 363 CG LEU A 68 -3.325 -40.026 29.003 1.00 77.61 C ANISOU 363 CG LEU A 68 5854 10433 13202 -2003 -1389 -389 C ATOM 364 CD1 LEU A 68 -3.044 -40.889 30.194 1.00 78.38 C ANISOU 364 CD1 LEU A 68 5872 10445 13466 -2013 -1434 -267 C ATOM 365 CD2 LEU A 68 -3.962 -40.895 27.904 1.00 81.70 C ANISOU 365 CD2 LEU A 68 6495 10846 13701 -2065 -1468 -558 C ATOM 366 N LEU A 69 -5.738 -37.207 27.041 1.00 72.79 N ANISOU 366 N LEU A 69 5266 10137 12253 -2138 -1442 -329 N ATOM 367 CA LEU A 69 -6.415 -37.151 25.737 1.00 73.42 C ANISOU 367 CA LEU A 69 5414 10227 12257 -2221 -1519 -404 C ATOM 368 C LEU A 69 -5.825 -36.084 24.830 1.00 75.90 C ANISOU 368 C LEU A 69 5795 10641 12405 -2168 -1426 -519 C ATOM 369 O LEU A 69 -5.640 -36.338 23.641 1.00 76.28 O ANISOU 369 O LEU A 69 5939 10658 12386 -2202 -1464 -662 O ATOM 370 CB LEU A 69 -7.924 -36.861 25.887 1.00 74.14 C ANISOU 370 CB LEU A 69 5418 10380 12372 -2307 -1605 -224 C ATOM 371 CG LEU A 69 -8.897 -37.930 26.374 1.00 80.25 C ANISOU 371 CG LEU A 69 6111 11069 13312 -2378 -1713 -79 C ATOM 372 CD1 LEU A 69 -10.287 -37.346 26.473 1.00 80.74 C ANISOU 372 CD1 LEU A 69 6057 11235 13384 -2429 -1756 140 C ATOM 373 CD2 LEU A 69 -8.903 -39.140 25.478 1.00 84.46 C ANISOU 373 CD2 LEU A 69 6730 11441 13919 -2476 -1850 -192 C ATOM 374 N VAL A 70 -5.552 -34.884 25.385 1.00 70.51 N ANISOU 374 N VAL A 70 5065 10072 11655 -2083 -1309 -456 N ATOM 375 CA VAL A 70 -5.014 -33.747 24.630 1.00 69.15 C ANISOU 375 CA VAL A 70 4946 9995 11334 -2031 -1218 -547 C ATOM 376 C VAL A 70 -3.511 -33.986 24.325 1.00 71.77 C ANISOU 376 C VAL A 70 5359 10259 11650 -1968 -1158 -723 C ATOM 377 O VAL A 70 -3.038 -33.526 23.286 1.00 70.90 O ANISOU 377 O VAL A 70 5324 10180 11435 -1955 -1127 -850 O ATOM 378 CB VAL A 70 -5.277 -32.372 25.324 1.00 71.72 C ANISOU 378 CB VAL A 70 5205 10451 11594 -1966 -1123 -418 C ATOM 379 CG1 VAL A 70 -4.506 -32.213 26.633 1.00 70.64 C ANISOU 379 CG1 VAL A 70 5013 10297 11530 -1891 -1064 -340 C ATOM 380 CG2 VAL A 70 -5.017 -31.196 24.380 1.00 70.75 C ANISOU 380 CG2 VAL A 70 5137 10421 11324 -1922 -1038 -505 C ATOM 381 N MET A 71 -2.794 -34.746 25.184 1.00 68.24 N ANISOU 381 N MET A 71 4895 9722 11312 -1931 -1147 -725 N ATOM 382 CA MET A 71 -1.377 -35.066 24.980 1.00 68.13 C ANISOU 382 CA MET A 71 4947 9637 11301 -1871 -1095 -871 C ATOM 383 C MET A 71 -1.189 -36.018 23.806 1.00 74.19 C ANISOU 383 C MET A 71 5813 10297 12079 -1920 -1176 -1011 C ATOM 384 O MET A 71 -0.211 -35.884 23.067 1.00 73.72 O ANISOU 384 O MET A 71 5834 10208 11970 -1869 -1129 -1154 O ATOM 385 CB MET A 71 -0.748 -35.668 26.243 1.00 70.03 C ANISOU 385 CB MET A 71 5135 9816 11659 -1819 -1064 -816 C ATOM 386 CG MET A 71 -0.259 -34.620 27.219 1.00 72.05 C ANISOU 386 CG MET A 71 5331 10169 11877 -1745 -964 -734 C ATOM 387 SD MET A 71 0.796 -35.299 28.525 1.00 75.69 S ANISOU 387 SD MET A 71 5729 10563 12466 -1683 -930 -670 S ATOM 388 CE MET A 71 2.306 -35.665 27.588 1.00 72.73 C ANISOU 388 CE MET A 71 5434 10114 12085 -1630 -879 -851 C ATOM 389 N VAL A 72 -2.130 -36.968 23.638 1.00 72.67 N ANISOU 389 N VAL A 72 5617 10046 11947 -2017 -1299 -963 N ATOM 390 CA VAL A 72 -2.123 -37.946 22.550 1.00 74.13 C ANISOU 390 CA VAL A 72 5907 10122 12137 -2080 -1401 -1085 C ATOM 391 C VAL A 72 -2.536 -37.217 21.253 1.00 77.67 C ANISOU 391 C VAL A 72 6418 10659 12433 -2105 -1405 -1162 C ATOM 392 O VAL A 72 -1.940 -37.465 20.206 1.00 77.77 O ANISOU 392 O VAL A 72 6544 10627 12379 -2085 -1404 -1323 O ATOM 393 CB VAL A 72 -3.025 -39.178 22.869 1.00 79.32 C ANISOU 393 CB VAL A 72 6532 10680 12926 -2186 -1546 -989 C ATOM 394 CG1 VAL A 72 -3.132 -40.122 21.677 1.00 80.77 C ANISOU 394 CG1 VAL A 72 6840 10749 13100 -2262 -1667 -1120 C ATOM 395 CG2 VAL A 72 -2.511 -39.943 24.085 1.00 79.20 C ANISOU 395 CG2 VAL A 72 6456 10572 13063 -2156 -1540 -919 C ATOM 396 N ALA A 73 -3.521 -36.286 21.350 1.00 73.40 N ANISOU 396 N ALA A 73 5806 10248 11836 -2137 -1400 -1042 N ATOM 397 CA ALA A 73 -4.070 -35.494 20.242 1.00 73.32 C ANISOU 397 CA ALA A 73 5832 10340 11687 -2166 -1404 -1079 C ATOM 398 C ALA A 73 -2.987 -34.672 19.521 1.00 76.90 C ANISOU 398 C ALA A 73 6357 10848 12015 -2079 -1293 -1222 C ATOM 399 O ALA A 73 -2.994 -34.614 18.295 1.00 77.20 O ANISOU 399 O ALA A 73 6485 10887 11959 -2096 -1321 -1340 O ATOM 400 CB ALA A 73 -5.174 -34.568 20.752 1.00 73.19 C ANISOU 400 CB ALA A 73 5708 10457 11644 -2185 -1384 -904 C ATOM 401 N ILE A 74 -2.068 -34.048 20.277 1.00 72.69 N ANISOU 401 N ILE A 74 5783 10357 11479 -1986 -1173 -1206 N ATOM 402 CA ILE A 74 -0.961 -33.239 19.742 1.00 72.20 C ANISOU 402 CA ILE A 74 5768 10353 11312 -1901 -1063 -1312 C ATOM 403 C ILE A 74 0.099 -34.163 19.103 1.00 77.72 C ANISOU 403 C ILE A 74 6563 10939 12026 -1859 -1062 -1471 C ATOM 404 O ILE A 74 0.696 -33.811 18.078 1.00 77.68 O ANISOU 404 O ILE A 74 6626 10969 11919 -1808 -1006 -1584 O ATOM 405 CB ILE A 74 -0.357 -32.355 20.875 1.00 73.81 C ANISOU 405 CB ILE A 74 5892 10630 11520 -1828 -953 -1225 C ATOM 406 CG1 ILE A 74 -1.384 -31.293 21.331 1.00 73.43 C ANISOU 406 CG1 ILE A 74 5773 10696 11433 -1858 -949 -1081 C ATOM 407 CG2 ILE A 74 0.980 -31.697 20.459 1.00 73.89 C ANISOU 407 CG2 ILE A 74 5940 10691 11443 -1745 -845 -1322 C ATOM 408 CD1 ILE A 74 -1.150 -30.678 22.694 1.00 79.11 C ANISOU 408 CD1 ILE A 74 6414 11458 12188 -1808 -882 -958 C ATOM 409 N TYR A 75 0.303 -35.342 19.710 1.00 75.04 N ANISOU 409 N TYR A 75 6233 10466 11813 -1876 -1124 -1472 N ATOM 410 CA TYR A 75 1.270 -36.347 19.295 1.00 75.80 C ANISOU 410 CA TYR A 75 6424 10438 11939 -1831 -1126 -1609 C ATOM 411 C TYR A 75 0.902 -37.014 17.947 1.00 80.69 C ANISOU 411 C TYR A 75 7167 10984 12509 -1887 -1228 -1728 C ATOM 412 O TYR A 75 1.807 -37.257 17.144 1.00 81.12 O ANISOU 412 O TYR A 75 7326 10977 12518 -1825 -1201 -1871 O ATOM 413 CB TYR A 75 1.390 -37.415 20.398 1.00 77.36 C ANISOU 413 CB TYR A 75 6579 10516 12296 -1828 -1153 -1553 C ATOM 414 CG TYR A 75 2.252 -38.601 20.039 1.00 80.52 C ANISOU 414 CG TYR A 75 7066 10792 12737 -1760 -1130 -1678 C ATOM 415 CD1 TYR A 75 3.641 -38.516 20.088 1.00 82.09 C ANISOU 415 CD1 TYR A 75 7254 11022 12914 -1649 -1004 -1715 C ATOM 416 CD2 TYR A 75 1.682 -39.827 19.708 1.00 83.06 C ANISOU 416 CD2 TYR A 75 7477 10960 13122 -1805 -1236 -1748 C ATOM 417 CE1 TYR A 75 4.445 -39.610 19.776 1.00 84.14 C ANISOU 417 CE1 TYR A 75 7587 11171 13210 -1576 -974 -1818 C ATOM 418 CE2 TYR A 75 2.477 -40.926 19.378 1.00 85.10 C ANISOU 418 CE2 TYR A 75 7824 11097 13415 -1730 -1209 -1862 C ATOM 419 CZ TYR A 75 3.860 -40.815 19.427 1.00 92.41 C ANISOU 419 CZ TYR A 75 8732 12065 14316 -1611 -1073 -1893 C ATOM 420 OH TYR A 75 4.661 -41.889 19.122 1.00 95.04 O ANISOU 420 OH TYR A 75 9145 12284 14681 -1527 -1036 -1993 O ATOM 421 N VAL A 76 -0.392 -37.328 17.709 1.00 77.05 N ANISOU 421 N VAL A 76 6696 10526 12053 -1999 -1346 -1667 N ATOM 422 CA VAL A 76 -0.822 -38.023 16.484 1.00 78.10 C ANISOU 422 CA VAL A 76 6951 10578 12145 -2066 -1465 -1775 C ATOM 423 C VAL A 76 -1.157 -37.041 15.333 1.00 81.89 C ANISOU 423 C VAL A 76 7462 11183 12470 -2096 -1471 -1805 C ATOM 424 O VAL A 76 -0.915 -37.392 14.176 1.00 83.05 O ANISOU 424 O VAL A 76 7714 11277 12564 -2154 -1573 -1894 O ATOM 425 CB VAL A 76 -2.004 -39.000 16.702 1.00 82.72 C ANISOU 425 CB VAL A 76 7523 11048 12858 -2186 -1623 -1698 C ATOM 426 CG1 VAL A 76 -1.573 -40.219 17.517 1.00 82.73 C ANISOU 426 CG1 VAL A 76 7514 10910 13011 -2156 -1625 -1687 C ATOM 427 CG2 VAL A 76 -3.233 -38.312 17.308 1.00 81.81 C ANISOU 427 CG2 VAL A 76 7275 11036 12771 -2271 -1666 -1510 C ATOM 428 N ASN A 77 -1.723 -35.850 15.631 1.00 76.88 N ANISOU 428 N ASN A 77 6746 10706 11760 -2057 -1369 -1738 N ATOM 429 CA ASN A 77 -2.096 -34.876 14.598 1.00 76.76 C ANISOU 429 CA ASN A 77 6756 10808 11600 -2082 -1371 -1761 C ATOM 430 C ASN A 77 -0.861 -34.127 14.068 1.00 80.08 C ANISOU 430 C ASN A 77 7219 11308 11900 -1972 -1239 -1862 C ATOM 431 O ASN A 77 -0.033 -33.652 14.846 1.00 78.21 O ANISOU 431 O ASN A 77 6920 11116 11680 -1892 -1123 -1827 O ATOM 432 CB ASN A 77 -3.153 -33.882 15.092 1.00 77.69 C ANISOU 432 CB ASN A 77 6753 11049 11716 -2140 -1376 -1591 C ATOM 433 CG ASN A 77 -3.837 -33.143 13.978 1.00107.86 C ANISOU 433 CG ASN A 77 10593 14979 15408 -2192 -1410 -1593 C ATOM 434 OD1 ASN A 77 -3.287 -32.208 13.385 1.00103.12 O ANISOU 434 OD1 ASN A 77 10099 14381 14702 -2180 -1422 -1728 O ATOM 435 ND2 ASN A 77 -5.038 -33.563 13.643 1.00102.25 N ANISOU 435 ND2 ASN A 77 9781 14366 14702 -2245 -1424 -1437 N ATOM 436 N ARG A 78 -0.759 -34.044 12.726 1.00 78.02 N ANISOU 436 N ARG A 78 7061 11071 11514 -1972 -1263 -1978 N ATOM 437 CA ARG A 78 0.325 -33.419 11.962 1.00 77.93 C ANISOU 437 CA ARG A 78 7099 11141 11372 -1872 -1151 -2077 C ATOM 438 C ARG A 78 0.409 -31.892 12.168 1.00 81.01 C ANISOU 438 C ARG A 78 7391 11701 11688 -1859 -1062 -1981 C ATOM 439 O ARG A 78 1.514 -31.360 12.294 1.00 80.00 O ANISOU 439 O ARG A 78 7259 11645 11494 -1767 -944 -2017 O ATOM 440 CB ARG A 78 0.152 -33.716 10.460 1.00 79.71 C ANISOU 440 CB ARG A 78 7466 11339 11480 -1883 -1219 -2220 C ATOM 441 N ARG A 79 -0.748 -31.200 12.195 1.00 77.44 N ANISOU 441 N ARG A 79 6862 11313 11250 -1948 -1119 -1855 N ATOM 442 CA ARG A 79 -0.823 -29.745 12.340 1.00 76.16 C ANISOU 442 CA ARG A 79 6613 11303 11022 -1942 -1046 -1753 C ATOM 443 C ARG A 79 -0.400 -29.250 13.740 1.00 79.11 C ANISOU 443 C ARG A 79 6886 11696 11475 -1896 -959 -1643 C ATOM 444 O ARG A 79 -0.075 -28.064 13.882 1.00 77.60 O ANISOU 444 O ARG A 79 6637 11618 11230 -1870 -880 -1573 O ATOM 445 CB ARG A 79 -2.241 -29.256 12.035 1.00 76.52 C ANISOU 445 CB ARG A 79 6620 11405 11047 -2048 -1141 -1654 C ATOM 446 N PHE A 80 -0.387 -30.143 14.754 1.00 76.02 N ANISOU 446 N PHE A 80 6480 11194 11210 -1886 -975 -1631 N ATOM 447 CA PHE A 80 -0.016 -29.753 16.111 1.00 74.79 C ANISOU 447 CA PHE A 80 6237 11045 11135 -1844 -905 -1531 C ATOM 448 C PHE A 80 1.480 -30.064 16.420 1.00 79.11 C ANISOU 448 C PHE A 80 6805 11552 11702 -1748 -814 -1608 C ATOM 449 O PHE A 80 1.850 -30.160 17.592 1.00 78.03 O ANISOU 449 O PHE A 80 6611 11383 11655 -1719 -780 -1544 O ATOM 450 CB PHE A 80 -0.954 -30.426 17.133 1.00 76.69 C ANISOU 450 CB PHE A 80 6426 11204 11510 -1904 -989 -1430 C ATOM 451 CG PHE A 80 -2.418 -30.035 17.012 1.00 78.33 C ANISOU 451 CG PHE A 80 6582 11457 11720 -1995 -1072 -1309 C ATOM 452 CD1 PHE A 80 -2.793 -28.698 16.896 1.00 80.84 C ANISOU 452 CD1 PHE A 80 6862 11909 11943 -2001 -1033 -1239 C ATOM 453 CD2 PHE A 80 -3.423 -30.997 17.093 1.00 81.02 C ANISOU 453 CD2 PHE A 80 6901 11711 12170 -2071 -1184 -1247 C ATOM 454 CE1 PHE A 80 -4.138 -28.337 16.793 1.00 81.79 C ANISOU 454 CE1 PHE A 80 6928 12080 12069 -2077 -1102 -1112 C ATOM 455 CE2 PHE A 80 -4.770 -30.636 16.994 1.00 84.03 C ANISOU 455 CE2 PHE A 80 7223 12146 12560 -2154 -1258 -1115 C ATOM 456 CZ PHE A 80 -5.115 -29.309 16.840 1.00 81.52 C ANISOU 456 CZ PHE A 80 6867 11964 12140 -2153 -1214 -1047 C ATOM 457 N HIS A 81 2.343 -30.141 15.380 1.00 76.73 N ANISOU 457 N HIS A 81 6580 11262 11313 -1693 -771 -1735 N ATOM 458 CA HIS A 81 3.782 -30.381 15.558 1.00 76.66 C ANISOU 458 CA HIS A 81 6585 11227 11316 -1596 -680 -1800 C ATOM 459 C HIS A 81 4.558 -29.048 15.432 1.00 78.59 C ANISOU 459 C HIS A 81 6784 11597 11477 -1541 -570 -1769 C ATOM 460 O HIS A 81 5.441 -28.896 14.586 1.00 77.94 O ANISOU 460 O HIS A 81 6728 11535 11351 -1463 -494 -1837 O ATOM 461 CB HIS A 81 4.306 -31.446 14.571 1.00 79.18 C ANISOU 461 CB HIS A 81 7017 11468 11598 -1555 -695 -1950 C ATOM 462 CG HIS A 81 3.825 -32.840 14.845 1.00 83.93 C ANISOU 462 CG HIS A 81 7673 11923 12293 -1602 -802 -1987 C ATOM 463 ND1 HIS A 81 3.184 -33.581 13.873 1.00 87.31 N ANISOU 463 ND1 HIS A 81 8221 12284 12670 -1620 -877 -2106 N ATOM 464 CD2 HIS A 81 3.916 -33.587 15.972 1.00 85.70 C ANISOU 464 CD2 HIS A 81 7849 12057 12655 -1637 -850 -1916 C ATOM 465 CE1 HIS A 81 2.904 -34.748 14.433 1.00 87.46 C ANISOU 465 CE1 HIS A 81 8263 12167 12802 -1669 -970 -2105 C ATOM 466 NE2 HIS A 81 3.329 -34.800 15.694 1.00 86.88 N ANISOU 466 NE2 HIS A 81 8085 12079 12847 -1682 -955 -1987 N ATOM 467 N PHE A 82 4.203 -28.090 16.306 1.00 74.24 N ANISOU 467 N PHE A 82 6166 11131 10913 -1580 -563 -1656 N ATOM 468 CA PHE A 82 4.779 -26.745 16.379 1.00 73.33 C ANISOU 468 CA PHE A 82 6004 11125 10733 -1545 -475 -1603 C ATOM 469 C PHE A 82 5.237 -26.402 17.812 1.00 75.99 C ANISOU 469 C PHE A 82 6276 11441 11157 -1517 -433 -1520 C ATOM 470 O PHE A 82 4.590 -26.861 18.764 1.00 75.17 O ANISOU 470 O PHE A 82 6148 11259 11152 -1541 -481 -1475 O ATOM 471 CB PHE A 82 3.746 -25.713 15.924 1.00 74.95 C ANISOU 471 CB PHE A 82 6188 11426 10864 -1600 -495 -1531 C ATOM 472 CG PHE A 82 3.628 -25.421 14.453 1.00 77.38 C ANISOU 472 CG PHE A 82 6545 11807 11049 -1603 -492 -1602 C ATOM 473 CD1 PHE A 82 2.837 -26.209 13.634 1.00 81.84 C ANISOU 473 CD1 PHE A 82 7172 12337 11588 -1648 -576 -1670 C ATOM 474 CD2 PHE A 82 4.174 -24.255 13.919 1.00 79.24 C ANISOU 474 CD2 PHE A 82 6766 12147 11193 -1564 -411 -1594 C ATOM 475 CE1 PHE A 82 2.673 -25.892 12.279 1.00 83.44 C ANISOU 475 CE1 PHE A 82 7424 12613 11668 -1648 -574 -1736 C ATOM 476 CE2 PHE A 82 4.008 -23.938 12.569 1.00 82.67 C ANISOU 476 CE2 PHE A 82 7241 12657 11511 -1563 -405 -1653 C ATOM 477 CZ PHE A 82 3.262 -24.762 11.759 1.00 81.84 C ANISOU 477 CZ PHE A 82 7200 12521 11375 -1602 -485 -1725 C ATOM 478 N PRO A 83 6.304 -25.562 17.989 1.00 72.06 N ANISOU 478 N PRO A 83 5747 11008 10625 -1469 -350 -1495 N ATOM 479 CA PRO A 83 6.797 -25.244 19.347 1.00 71.09 C ANISOU 479 CA PRO A 83 5573 10860 10580 -1444 -318 -1424 C ATOM 480 C PRO A 83 5.728 -24.807 20.367 1.00 73.39 C ANISOU 480 C PRO A 83 5822 11140 10922 -1484 -357 -1311 C ATOM 481 O PRO A 83 5.885 -25.129 21.550 1.00 73.30 O ANISOU 481 O PRO A 83 5786 11057 11008 -1478 -376 -1278 O ATOM 482 CB PRO A 83 7.792 -24.094 19.110 1.00 72.39 C ANISOU 482 CB PRO A 83 5716 11112 10675 -1408 -240 -1405 C ATOM 483 CG PRO A 83 7.689 -23.741 17.646 1.00 77.15 C ANISOU 483 CG PRO A 83 6350 11796 11166 -1421 -231 -1441 C ATOM 484 CD PRO A 83 7.203 -24.977 16.974 1.00 73.71 C ANISOU 484 CD PRO A 83 5969 11311 10727 -1435 -284 -1531 C ATOM 485 N ILE A 84 4.657 -24.107 19.930 1.00 67.99 N ANISOU 485 N ILE A 84 5132 10528 10174 -1518 -365 -1248 N ATOM 486 CA ILE A 84 3.619 -23.649 20.853 1.00 66.63 C ANISOU 486 CA ILE A 84 4924 10363 10028 -1541 -388 -1128 C ATOM 487 C ILE A 84 2.717 -24.809 21.319 1.00 69.32 C ANISOU 487 C ILE A 84 5249 10631 10458 -1579 -464 -1095 C ATOM 488 O ILE A 84 2.359 -24.835 22.494 1.00 67.97 O ANISOU 488 O ILE A 84 5040 10446 10340 -1577 -474 -995 O ATOM 489 CB ILE A 84 2.773 -22.479 20.327 1.00 69.61 C ANISOU 489 CB ILE A 84 5305 10838 10306 -1561 -373 -1072 C ATOM 490 CG1 ILE A 84 2.406 -22.582 18.855 1.00 71.16 C ANISOU 490 CG1 ILE A 84 5529 11068 10442 -1602 -411 -1125 C ATOM 491 CG2 ILE A 84 3.482 -21.173 20.594 1.00 69.78 C ANISOU 491 CG2 ILE A 84 5331 10921 10259 -1525 -301 -1069 C ATOM 492 CD1 ILE A 84 1.131 -23.024 18.687 1.00 81.92 C ANISOU 492 CD1 ILE A 84 6873 12414 11837 -1657 -487 -1062 C ATOM 493 N TYR A 85 2.385 -25.769 20.436 1.00 66.41 N ANISOU 493 N TYR A 85 4913 10216 10104 -1612 -520 -1174 N ATOM 494 CA TYR A 85 1.539 -26.903 20.797 1.00 66.63 C ANISOU 494 CA TYR A 85 4927 10166 10222 -1659 -605 -1142 C ATOM 495 C TYR A 85 2.296 -27.933 21.650 1.00 69.23 C ANISOU 495 C TYR A 85 5240 10396 10667 -1630 -608 -1148 C ATOM 496 O TYR A 85 1.651 -28.634 22.432 1.00 68.97 O ANISOU 496 O TYR A 85 5167 10317 10722 -1654 -656 -1065 O ATOM 497 CB TYR A 85 0.941 -27.577 19.551 1.00 69.27 C ANISOU 497 CB TYR A 85 5316 10472 10532 -1710 -677 -1229 C ATOM 498 CG TYR A 85 -0.030 -26.693 18.800 1.00 71.52 C ANISOU 498 CG TYR A 85 5594 10838 10742 -1766 -714 -1176 C ATOM 499 CD1 TYR A 85 -1.318 -26.475 19.279 1.00 73.43 C ANISOU 499 CD1 TYR A 85 5782 11085 11031 -1818 -772 -1048 C ATOM 500 CD2 TYR A 85 0.332 -26.086 17.605 1.00 72.66 C ANISOU 500 CD2 TYR A 85 5782 11058 10769 -1766 -690 -1244 C ATOM 501 CE1 TYR A 85 -2.212 -25.656 18.594 1.00 74.41 C ANISOU 501 CE1 TYR A 85 5893 11292 11087 -1867 -803 -985 C ATOM 502 CE2 TYR A 85 -0.559 -25.277 16.904 1.00 73.83 C ANISOU 502 CE2 TYR A 85 5919 11286 10847 -1817 -723 -1188 C ATOM 503 CZ TYR A 85 -1.831 -25.063 17.402 1.00 81.91 C ANISOU 503 CZ TYR A 85 6887 12315 11920 -1868 -780 -1058 C ATOM 504 OH TYR A 85 -2.706 -24.265 16.706 1.00 83.72 O ANISOU 504 OH TYR A 85 7099 12629 12083 -1917 -811 -991 O ATOM 505 N TYR A 86 3.640 -28.023 21.527 1.00 64.61 N ANISOU 505 N TYR A 86 4680 9785 10084 -1576 -555 -1236 N ATOM 506 CA TYR A 86 4.453 -28.944 22.335 1.00 63.91 C ANISOU 506 CA TYR A 86 4575 9607 10103 -1541 -549 -1244 C ATOM 507 C TYR A 86 4.483 -28.476 23.794 1.00 63.93 C ANISOU 507 C TYR A 86 4512 9626 10152 -1520 -522 -1126 C ATOM 508 O TYR A 86 4.488 -29.305 24.705 1.00 63.15 O ANISOU 508 O TYR A 86 4384 9455 10156 -1507 -538 -1094 O ATOM 509 CB TYR A 86 5.879 -29.075 21.774 1.00 65.99 C ANISOU 509 CB TYR A 86 4873 9858 10344 -1479 -487 -1350 C ATOM 510 CG TYR A 86 6.009 -29.958 20.548 1.00 70.17 C ANISOU 510 CG TYR A 86 5479 10342 10842 -1482 -515 -1474 C ATOM 511 CD1 TYR A 86 5.906 -31.341 20.647 1.00 73.38 C ANISOU 511 CD1 TYR A 86 5919 10631 11331 -1502 -584 -1518 C ATOM 512 CD2 TYR A 86 6.348 -29.420 19.307 1.00 71.64 C ANISOU 512 CD2 TYR A 86 5708 10598 10914 -1458 -472 -1550 C ATOM 513 CE1 TYR A 86 6.054 -32.161 19.533 1.00 75.89 C ANISOU 513 CE1 TYR A 86 6326 10898 11612 -1501 -615 -1640 C ATOM 514 CE2 TYR A 86 6.506 -30.229 18.184 1.00 74.00 C ANISOU 514 CE2 TYR A 86 6089 10856 11171 -1449 -496 -1669 C ATOM 515 CZ TYR A 86 6.356 -31.600 18.303 1.00 83.60 C ANISOU 515 CZ TYR A 86 7351 11949 12463 -1470 -570 -1718 C ATOM 516 OH TYR A 86 6.519 -32.401 17.203 1.00 87.23 O ANISOU 516 OH TYR A 86 7910 12359 12875 -1457 -598 -1842 O ATOM 517 N LEU A 87 4.471 -27.145 24.002 1.00 58.00 N ANISOU 517 N LEU A 87 3746 8967 9323 -1515 -485 -1060 N ATOM 518 CA LEU A 87 4.447 -26.499 25.318 1.00 56.20 C ANISOU 518 CA LEU A 87 3477 8766 9112 -1492 -461 -949 C ATOM 519 C LEU A 87 3.082 -26.675 25.998 1.00 57.99 C ANISOU 519 C LEU A 87 3668 8980 9386 -1522 -515 -840 C ATOM 520 O LEU A 87 3.017 -26.717 27.229 1.00 57.68 O ANISOU 520 O LEU A 87 3591 8918 9408 -1498 -514 -754 O ATOM 521 CB LEU A 87 4.775 -25.007 25.177 1.00 55.62 C ANISOU 521 CB LEU A 87 3420 8787 8929 -1475 -406 -927 C ATOM 522 CG LEU A 87 6.204 -24.554 25.533 1.00 60.54 C ANISOU 522 CG LEU A 87 4050 9428 9524 -1435 -346 -972 C ATOM 523 CD1 LEU A 87 7.269 -25.189 24.625 1.00 61.63 C ANISOU 523 CD1 LEU A 87 4212 9552 9652 -1426 -329 -1090 C ATOM 524 CD2 LEU A 87 6.326 -23.059 25.416 1.00 62.41 C ANISOU 524 CD2 LEU A 87 4305 9748 9661 -1431 -308 -935 C ATOM 525 N MET A 88 1.995 -26.781 25.193 1.00 52.43 N ANISOU 525 N MET A 88 2973 8295 8655 -1574 -563 -836 N ATOM 526 CA MET A 88 0.625 -27.004 25.672 1.00 51.17 C ANISOU 526 CA MET A 88 2771 8132 8541 -1611 -621 -721 C ATOM 527 C MET A 88 0.477 -28.420 26.221 1.00 53.77 C ANISOU 527 C MET A 88 3073 8356 9002 -1630 -680 -716 C ATOM 528 O MET A 88 -0.245 -28.628 27.198 1.00 53.23 O ANISOU 528 O MET A 88 2948 8275 9000 -1634 -708 -595 O ATOM 529 CB MET A 88 -0.399 -26.766 24.552 1.00 53.66 C ANISOU 529 CB MET A 88 3100 8497 8791 -1670 -664 -721 C ATOM 530 CG MET A 88 -0.579 -25.318 24.202 1.00 56.23 C ANISOU 530 CG MET A 88 3439 8932 8994 -1651 -607 -689 C ATOM 531 SD MET A 88 -1.792 -25.075 22.886 1.00 60.48 S ANISOU 531 SD MET A 88 3991 9538 9450 -1718 -654 -690 S ATOM 532 CE MET A 88 -1.716 -23.321 22.732 1.00 56.21 C ANISOU 532 CE MET A 88 3463 9112 8782 -1672 -566 -643 C ATOM 533 N ALA A 89 1.179 -29.386 25.596 1.00 49.60 N ANISOU 533 N ALA A 89 2585 7751 8509 -1634 -695 -842 N ATOM 534 CA ALA A 89 1.199 -30.798 25.994 1.00 49.46 C ANISOU 534 CA ALA A 89 2557 7619 8617 -1646 -746 -858 C ATOM 535 C ALA A 89 1.952 -30.976 27.303 1.00 51.07 C ANISOU 535 C ALA A 89 2719 7797 8889 -1586 -699 -811 C ATOM 536 O ALA A 89 1.584 -31.825 28.114 1.00 50.82 O ANISOU 536 O ALA A 89 2644 7700 8967 -1593 -738 -745 O ATOM 537 CB ALA A 89 1.841 -31.642 24.904 1.00 51.07 C ANISOU 537 CB ALA A 89 2834 7754 8817 -1653 -763 -1014 C ATOM 538 N ASN A 90 3.002 -30.157 27.510 1.00 46.22 N ANISOU 538 N ASN A 90 2115 7235 8211 -1530 -619 -838 N ATOM 539 CA ASN A 90 3.816 -30.147 28.729 1.00 44.91 C ANISOU 539 CA ASN A 90 1913 7056 8094 -1475 -575 -794 C ATOM 540 C ASN A 90 3.012 -29.547 29.886 1.00 46.78 C ANISOU 540 C ASN A 90 2101 7341 8331 -1462 -574 -647 C ATOM 541 O ASN A 90 3.183 -29.967 31.032 1.00 46.46 O ANISOU 541 O ASN A 90 2018 7266 8367 -1433 -572 -578 O ATOM 542 CB ASN A 90 5.125 -29.375 28.516 1.00 43.20 C ANISOU 542 CB ASN A 90 1724 6883 7807 -1431 -503 -864 C ATOM 543 CG ASN A 90 6.198 -29.734 29.505 1.00 64.38 C ANISOU 543 CG ASN A 90 4377 9529 10555 -1382 -468 -855 C ATOM 544 OD1 ASN A 90 6.543 -30.904 29.695 1.00 59.09 O ANISOU 544 OD1 ASN A 90 3681 8779 9992 -1375 -493 -847 O ATOM 545 ND2 ASN A 90 6.794 -28.738 30.128 1.00 56.29 N ANISOU 545 ND2 ASN A 90 3355 8561 9470 -1349 -413 -857 N ATOM 546 N LEU A 91 2.125 -28.571 29.573 1.00 41.54 N ANISOU 546 N LEU A 91 1447 6757 7580 -1478 -571 -594 N ATOM 547 CA LEU A 91 1.224 -27.913 30.522 1.00 40.42 C ANISOU 547 CA LEU A 91 1270 6668 7420 -1456 -564 -450 C ATOM 548 C LEU A 91 0.176 -28.928 30.986 1.00 45.81 C ANISOU 548 C LEU A 91 1892 7304 8208 -1484 -628 -353 C ATOM 549 O LEU A 91 -0.201 -28.934 32.158 1.00 44.75 O ANISOU 549 O LEU A 91 1711 7180 8110 -1448 -621 -230 O ATOM 550 CB LEU A 91 0.577 -26.671 29.872 1.00 39.80 C ANISOU 550 CB LEU A 91 1221 6681 7220 -1464 -543 -428 C ATOM 551 CG LEU A 91 -0.395 -25.833 30.714 1.00 43.94 C ANISOU 551 CG LEU A 91 1719 7266 7709 -1432 -530 -277 C ATOM 552 CD1 LEU A 91 0.325 -25.092 31.825 1.00 43.07 C ANISOU 552 CD1 LEU A 91 1628 7177 7559 -1360 -473 -235 C ATOM 553 CD2 LEU A 91 -1.137 -24.845 29.846 1.00 46.99 C ANISOU 553 CD2 LEU A 91 2127 7729 7996 -1455 -524 -257 C ATOM 554 N ALA A 92 -0.256 -29.814 30.062 1.00 44.22 N ANISOU 554 N ALA A 92 1696 7051 8054 -1550 -693 -408 N ATOM 555 CA ALA A 92 -1.188 -30.906 30.325 1.00 45.07 C ANISOU 555 CA ALA A 92 1753 7098 8274 -1597 -771 -333 C ATOM 556 C ALA A 92 -0.503 -31.998 31.141 1.00 50.17 C ANISOU 556 C ALA A 92 2368 7654 9040 -1571 -777 -330 C ATOM 557 O ALA A 92 -1.146 -32.617 31.992 1.00 50.22 O ANISOU 557 O ALA A 92 2308 7637 9136 -1572 -809 -208 O ATOM 558 CB ALA A 92 -1.709 -31.470 29.021 1.00 46.60 C ANISOU 558 CB ALA A 92 1984 7250 8472 -1678 -844 -419 C ATOM 559 N ALA A 93 0.810 -32.223 30.887 1.00 47.42 N ANISOU 559 N ALA A 93 2062 7262 8692 -1542 -739 -455 N ATOM 560 CA ALA A 93 1.648 -33.189 31.601 1.00 47.77 C ANISOU 560 CA ALA A 93 2083 7227 8841 -1507 -731 -464 C ATOM 561 C ALA A 93 1.857 -32.736 33.040 1.00 52.27 C ANISOU 561 C ALA A 93 2604 7846 9408 -1442 -680 -355 C ATOM 562 O ALA A 93 1.908 -33.572 33.939 1.00 52.22 O ANISOU 562 O ALA A 93 2545 7792 9505 -1423 -694 -283 O ATOM 563 CB ALA A 93 2.984 -33.345 30.894 1.00 48.56 C ANISOU 563 CB ALA A 93 2240 7287 8923 -1486 -695 -617 C ATOM 564 N ALA A 94 1.935 -31.404 33.251 1.00 48.89 N ANISOU 564 N ALA A 94 2201 7513 8861 -1408 -624 -342 N ATOM 565 CA ALA A 94 2.069 -30.759 34.560 1.00 48.35 C ANISOU 565 CA ALA A 94 2113 7499 8760 -1343 -578 -246 C ATOM 566 C ALA A 94 0.776 -30.937 35.357 1.00 52.49 C ANISOU 566 C ALA A 94 2578 8044 9323 -1332 -602 -86 C ATOM 567 O ALA A 94 0.824 -31.169 36.564 1.00 51.24 O ANISOU 567 O ALA A 94 2385 7892 9193 -1277 -582 4 O ATOM 568 CB ALA A 94 2.400 -29.278 34.388 1.00 48.38 C ANISOU 568 CB ALA A 94 2174 7587 8623 -1321 -527 -276 C ATOM 569 N ASP A 95 -0.376 -30.861 34.665 1.00 50.36 N ANISOU 569 N ASP A 95 2294 7788 9051 -1383 -647 -45 N ATOM 570 CA ASP A 95 -1.707 -31.074 35.243 1.00 51.07 C ANISOU 570 CA ASP A 95 2316 7903 9183 -1382 -677 120 C ATOM 571 C ASP A 95 -1.909 -32.564 35.541 1.00 55.58 C ANISOU 571 C ASP A 95 2824 8382 9911 -1422 -743 158 C ATOM 572 O ASP A 95 -2.541 -32.903 36.541 1.00 55.21 O ANISOU 572 O ASP A 95 2706 8345 9928 -1394 -752 306 O ATOM 573 CB ASP A 95 -2.808 -30.548 34.303 1.00 53.51 C ANISOU 573 CB ASP A 95 2633 8275 9422 -1425 -698 156 C ATOM 574 CG ASP A 95 -2.812 -29.043 34.088 1.00 67.56 C ANISOU 574 CG ASP A 95 4467 10150 11053 -1377 -630 156 C ATOM 575 OD1 ASP A 95 -2.607 -28.298 35.076 1.00 68.35 O ANISOU 575 OD1 ASP A 95 4577 10286 11107 -1298 -575 214 O ATOM 576 OD2 ASP A 95 -3.079 -28.607 32.941 1.00 75.13 O1- ANISOU 576 OD2 ASP A 95 5461 11146 11939 -1419 -637 106 O1- ATOM 577 N PHE A 96 -1.338 -33.444 34.688 1.00 52.73 N ANISOU 577 N PHE A 96 2493 7931 9610 -1480 -787 29 N ATOM 578 CA PHE A 96 -1.374 -34.898 34.852 1.00 53.43 C ANISOU 578 CA PHE A 96 2539 7911 9850 -1518 -853 43 C ATOM 579 C PHE A 96 -0.595 -35.281 36.108 1.00 57.95 C ANISOU 579 C PHE A 96 3069 8460 10490 -1448 -812 93 C ATOM 580 O PHE A 96 -1.016 -36.170 36.850 1.00 57.87 O ANISOU 580 O PHE A 96 2983 8421 10584 -1446 -844 218 O ATOM 581 CB PHE A 96 -0.810 -35.606 33.603 1.00 55.69 C ANISOU 581 CB PHE A 96 2894 8104 10160 -1574 -893 -128 C ATOM 582 CG PHE A 96 -0.912 -37.115 33.616 1.00 58.22 C ANISOU 582 CG PHE A 96 3193 8296 10634 -1618 -968 -130 C ATOM 583 CD1 PHE A 96 0.164 -37.894 34.009 1.00 61.58 C ANISOU 583 CD1 PHE A 96 3615 8646 11138 -1574 -941 -174 C ATOM 584 CD2 PHE A 96 -2.087 -37.756 33.238 1.00 61.61 C ANISOU 584 CD2 PHE A 96 3606 8675 11127 -1706 -1068 -87 C ATOM 585 CE1 PHE A 96 0.066 -39.288 34.034 1.00 63.63 C ANISOU 585 CE1 PHE A 96 3858 8777 11540 -1611 -1009 -174 C ATOM 586 CE2 PHE A 96 -2.180 -39.148 33.260 1.00 65.57 C ANISOU 586 CE2 PHE A 96 4096 9046 11773 -1751 -1145 -89 C ATOM 587 CZ PHE A 96 -1.095 -39.905 33.636 1.00 63.66 C ANISOU 587 CZ PHE A 96 3854 8724 11608 -1701 -1113 -135 C ATOM 588 N PHE A 97 0.532 -34.585 36.347 1.00 54.51 N ANISOU 588 N PHE A 97 2677 8043 9989 -1393 -743 5 N ATOM 589 CA PHE A 97 1.376 -34.750 37.526 1.00 54.30 C ANISOU 589 CA PHE A 97 2620 8010 10003 -1324 -699 40 C ATOM 590 C PHE A 97 0.633 -34.204 38.756 1.00 58.98 C ANISOU 590 C PHE A 97 3160 8680 10570 -1268 -677 209 C ATOM 591 O PHE A 97 0.758 -34.776 39.844 1.00 58.60 O ANISOU 591 O PHE A 97 3049 8608 10608 -1233 -678 302 O ATOM 592 CB PHE A 97 2.733 -34.050 37.318 1.00 55.38 C ANISOU 592 CB PHE A 97 2818 8171 10054 -1288 -636 -79 C ATOM 593 CG PHE A 97 3.648 -34.068 38.515 1.00 56.47 C ANISOU 593 CG PHE A 97 2931 8328 10197 -1218 -590 -34 C ATOM 594 CD1 PHE A 97 4.429 -35.182 38.794 1.00 60.11 C ANISOU 594 CD1 PHE A 97 3357 8715 10767 -1202 -590 -51 C ATOM 595 CD2 PHE A 97 3.748 -32.961 39.351 1.00 57.96 C ANISOU 595 CD2 PHE A 97 3139 8605 10278 -1168 -548 22 C ATOM 596 CE1 PHE A 97 5.278 -35.196 39.902 1.00 60.86 C ANISOU 596 CE1 PHE A 97 3425 8833 10864 -1142 -552 -4 C ATOM 597 CE2 PHE A 97 4.590 -32.978 40.464 1.00 60.71 C ANISOU 597 CE2 PHE A 97 3472 8969 10624 -1109 -515 61 C ATOM 598 CZ PHE A 97 5.357 -34.092 40.727 1.00 59.29 C ANISOU 598 CZ PHE A 97 3248 8724 10555 -1098 -519 51 C ATOM 599 N ALA A 98 -0.137 -33.100 38.567 1.00 56.15 N ANISOU 599 N ALA A 98 2830 8414 10092 -1255 -653 250 N ATOM 600 CA ALA A 98 -0.947 -32.471 39.611 1.00 56.20 C ANISOU 600 CA ALA A 98 2801 8499 10053 -1190 -625 411 C ATOM 601 C ALA A 98 -2.088 -33.403 40.024 1.00 61.38 C ANISOU 601 C ALA A 98 3363 9135 10824 -1209 -677 561 C ATOM 602 O ALA A 98 -2.398 -33.501 41.214 1.00 61.52 O ANISOU 602 O ALA A 98 3324 9175 10876 -1146 -659 692 O ATOM 603 CB ALA A 98 -1.494 -31.135 39.131 1.00 56.58 C ANISOU 603 CB ALA A 98 2906 8637 9956 -1178 -593 416 C ATOM 604 N GLY A 99 -2.647 -34.120 39.042 1.00 58.21 N ANISOU 604 N GLY A 99 2945 8687 10485 -1299 -745 540 N ATOM 605 CA GLY A 99 -3.694 -35.114 39.241 1.00 58.73 C ANISOU 605 CA GLY A 99 2920 8721 10675 -1341 -813 676 C ATOM 606 C GLY A 99 -3.234 -36.245 40.142 1.00 62.86 C ANISOU 606 C GLY A 99 3382 9169 11335 -1321 -827 720 C ATOM 607 O GLY A 99 -4.022 -36.783 40.923 1.00 62.62 O ANISOU 607 O GLY A 99 3262 9158 11372 -1291 -836 893 O ATOM 608 N LEU A 100 -1.944 -36.596 40.044 1.00 59.61 N ANISOU 608 N LEU A 100 3015 8676 10958 -1329 -821 573 N ATOM 609 CA LEU A 100 -1.303 -37.619 40.859 1.00 59.93 C ANISOU 609 CA LEU A 100 3008 8643 11121 -1303 -824 593 C ATOM 610 C LEU A 100 -0.933 -37.041 42.230 1.00 63.04 C ANISOU 610 C LEU A 100 3376 9112 11463 -1198 -751 682 C ATOM 611 O LEU A 100 -0.950 -37.764 43.228 1.00 63.19 O ANISOU 611 O LEU A 100 3316 9118 11575 -1162 -755 806 O ATOM 612 CB LEU A 100 -0.056 -38.149 40.129 1.00 60.25 C ANISOU 612 CB LEU A 100 3112 8586 11192 -1330 -826 407 C ATOM 613 CG LEU A 100 0.473 -39.487 40.605 1.00 65.60 C ANISOU 613 CG LEU A 100 3746 9169 12009 -1313 -835 414 C ATOM 614 CD1 LEU A 100 0.810 -40.379 39.427 1.00 66.79 C ANISOU 614 CD1 LEU A 100 3937 9189 12253 -1384 -895 295 C ATOM 615 CD2 LEU A 100 1.667 -39.310 41.549 1.00 66.68 C ANISOU 615 CD2 LEU A 100 3899 9338 12100 -1233 -756 369 C ATOM 616 N ALA A 101 -0.585 -35.740 42.267 1.00 58.45 N ANISOU 616 N ALA A 101 2867 8609 10733 -1150 -688 620 N ATOM 617 CA ALA A 101 -0.186 -35.016 43.475 1.00 57.64 C ANISOU 617 CA ALA A 101 2769 8577 10556 -1053 -625 683 C ATOM 618 C ALA A 101 -1.379 -34.795 44.417 1.00 61.40 C ANISOU 618 C ALA A 101 3185 9127 11017 -996 -615 879 C ATOM 619 O ALA A 101 -1.248 -35.010 45.621 1.00 61.37 O ANISOU 619 O ALA A 101 3120 9130 11069 -935 -603 990 O ATOM 620 CB ALA A 101 0.435 -33.685 43.101 1.00 57.57 C ANISOU 620 CB ALA A 101 2860 8624 10391 -1032 -577 573 C ATOM 621 N TYR A 102 -2.541 -34.371 43.870 1.00 57.46 N ANISOU 621 N TYR A 102 2696 8688 10449 -1010 -620 932 N ATOM 622 CA TYR A 102 -3.753 -34.142 44.661 1.00 57.38 C ANISOU 622 CA TYR A 102 2626 8756 10418 -950 -605 1129 C ATOM 623 C TYR A 102 -4.389 -35.476 45.100 1.00 61.27 C ANISOU 623 C TYR A 102 2998 9210 11072 -962 -650 1275 C ATOM 624 O TYR A 102 -5.061 -35.513 46.130 1.00 61.43 O ANISOU 624 O TYR A 102 2960 9289 11093 -877 -620 1442 O ATOM 625 CB TYR A 102 -4.780 -33.291 43.887 1.00 58.84 C ANISOU 625 CB TYR A 102 2828 8998 10531 -984 -614 1160 C ATOM 626 CG TYR A 102 -4.389 -31.852 43.623 1.00 60.31 C ANISOU 626 CG TYR A 102 3122 9251 10542 -942 -556 1082 C ATOM 627 CD1 TYR A 102 -4.218 -30.951 44.670 1.00 62.42 C ANISOU 627 CD1 TYR A 102 3421 9601 10692 -827 -489 1177 C ATOM 628 CD2 TYR A 102 -4.322 -31.355 42.322 1.00 60.74 C ANISOU 628 CD2 TYR A 102 3247 9289 10543 -1015 -570 928 C ATOM 629 CE1 TYR A 102 -3.895 -29.619 44.433 1.00 63.45 C ANISOU 629 CE1 TYR A 102 3658 9785 10664 -791 -441 1111 C ATOM 630 CE2 TYR A 102 -4.000 -30.024 42.071 1.00 61.07 C ANISOU 630 CE2 TYR A 102 3382 9391 10430 -981 -520 868 C ATOM 631 CZ TYR A 102 -3.793 -29.158 43.130 1.00 69.75 C ANISOU 631 CZ TYR A 102 4517 10562 11422 -871 -457 960 C ATOM 632 OH TYR A 102 -3.487 -27.841 42.887 1.00 71.86 O ANISOU 632 OH TYR A 102 4885 10879 11541 -840 -412 900 O ATOM 633 N PHE A 103 -4.156 -36.563 44.336 1.00 57.36 N ANISOU 633 N PHE A 103 2470 8613 10712 -1065 -724 1215 N ATOM 634 CA PHE A 103 -4.666 -37.916 44.614 1.00 57.52 C ANISOU 634 CA PHE A 103 2379 8570 10905 -1099 -784 1336 C ATOM 635 C PHE A 103 -4.059 -38.452 45.922 1.00 59.94 C ANISOU 635 C PHE A 103 2642 8867 11264 -1017 -746 1393 C ATOM 636 O PHE A 103 -4.775 -39.021 46.753 1.00 60.04 O ANISOU 636 O PHE A 103 2557 8910 11346 -972 -747 1579 O ATOM 637 CB PHE A 103 -4.344 -38.862 43.436 1.00 59.85 C ANISOU 637 CB PHE A 103 2692 8740 11309 -1222 -868 1207 C ATOM 638 CG PHE A 103 -5.047 -40.195 43.458 1.00 62.53 C ANISOU 638 CG PHE A 103 2936 8988 11836 -1283 -949 1305 C ATOM 639 CD1 PHE A 103 -6.298 -40.343 42.883 1.00 66.60 C ANISOU 639 CD1 PHE A 103 3386 9504 12416 -1356 -1025 1430 C ATOM 640 CD2 PHE A 103 -4.441 -41.313 44.020 1.00 65.02 C ANISOU 640 CD2 PHE A 103 3232 9207 12266 -1277 -957 1267 C ATOM 641 CE1 PHE A 103 -6.951 -41.576 42.898 1.00 68.63 C ANISOU 641 CE1 PHE A 103 3558 9665 12853 -1425 -1112 1522 C ATOM 642 CE2 PHE A 103 -5.094 -42.546 44.035 1.00 68.98 C ANISOU 642 CE2 PHE A 103 3652 9613 12946 -1338 -1036 1355 C ATOM 643 CZ PHE A 103 -6.345 -42.670 43.470 1.00 67.90 C ANISOU 643 CZ PHE A 103 3452 9474 12874 -1415 -1117 1481 C ATOM 644 N TYR A 104 -2.742 -38.242 46.100 1.00 54.67 N ANISOU 644 N TYR A 104 2045 8170 10557 -993 -709 1244 N ATOM 645 CA TYR A 104 -1.991 -38.665 47.275 1.00 54.16 C ANISOU 645 CA TYR A 104 1949 8099 10531 -919 -673 1279 C ATOM 646 C TYR A 104 -2.347 -37.769 48.480 1.00 55.76 C ANISOU 646 C TYR A 104 2155 8420 10610 -798 -605 1400 C ATOM 647 O TYR A 104 -2.266 -38.216 49.632 1.00 55.13 O ANISOU 647 O TYR A 104 2020 8356 10573 -727 -583 1500 O ATOM 648 CB TYR A 104 -0.485 -38.632 46.950 1.00 55.44 C ANISOU 648 CB TYR A 104 2183 8201 10680 -936 -657 1088 C ATOM 649 CG TYR A 104 0.418 -39.137 48.049 1.00 57.94 C ANISOU 649 CG TYR A 104 2468 8512 11033 -867 -622 1116 C ATOM 650 CD1 TYR A 104 0.441 -40.487 48.399 1.00 60.95 C ANISOU 650 CD1 TYR A 104 2747 8842 11567 -859 -647 1228 C ATOM 651 CD2 TYR A 104 1.313 -38.285 48.686 1.00 58.23 C ANISOU 651 CD2 TYR A 104 2576 8593 10958 -817 -572 1031 C ATOM 652 CE1 TYR A 104 1.276 -40.957 49.410 1.00 62.28 C ANISOU 652 CE1 TYR A 104 2883 9012 11769 -795 -614 1258 C ATOM 653 CE2 TYR A 104 2.164 -38.744 49.686 1.00 59.35 C ANISOU 653 CE2 TYR A 104 2686 8733 11131 -759 -547 1060 C ATOM 654 CZ TYR A 104 2.143 -40.081 50.044 1.00 68.70 C ANISOU 654 CZ TYR A 104 3766 9874 12461 -745 -565 1174 C ATOM 655 OH TYR A 104 2.988 -40.529 51.024 1.00 71.38 O ANISOU 655 OH TYR A 104 4072 10220 12831 -686 -539 1209 O ATOM 656 N LEU A 105 -2.755 -36.513 48.198 1.00 50.69 N ANISOU 656 N LEU A 105 1584 7861 9817 -770 -572 1392 N ATOM 657 CA LEU A 105 -3.165 -35.524 49.196 1.00 49.77 C ANISOU 657 CA LEU A 105 1494 7850 9566 -650 -508 1498 C ATOM 658 C LEU A 105 -4.541 -35.883 49.790 1.00 54.41 C ANISOU 658 C LEU A 105 1982 8498 10192 -603 -508 1724 C ATOM 659 O LEU A 105 -4.708 -35.883 51.015 1.00 53.97 O ANISOU 659 O LEU A 105 1899 8508 10099 -491 -462 1861 O ATOM 660 CB LEU A 105 -3.189 -34.117 48.538 1.00 48.82 C ANISOU 660 CB LEU A 105 1500 7781 9268 -638 -472 1390 C ATOM 661 CG LEU A 105 -3.955 -33.001 49.252 1.00 53.22 C ANISOU 661 CG LEU A 105 2087 8441 9693 -559 -428 1510 C ATOM 662 CD1 LEU A 105 -3.156 -32.384 50.366 1.00 53.60 C ANISOU 662 CD1 LEU A 105 2172 8559 9635 -419 -367 1601 C ATOM 663 CD2 LEU A 105 -4.350 -31.921 48.290 1.00 54.49 C ANISOU 663 CD2 LEU A 105 2352 8619 9733 -597 -417 1385 C ATOM 664 N MET A 106 -5.512 -36.172 48.915 1.00 51.68 N ANISOU 664 N MET A 106 1583 8135 9917 -687 -559 1769 N ATOM 665 CA MET A 106 -6.881 -36.499 49.295 1.00 52.42 C ANISOU 665 CA MET A 106 1574 8292 10051 -658 -565 1992 C ATOM 666 C MET A 106 -6.964 -37.862 50.001 1.00 57.68 C ANISOU 666 C MET A 106 2106 8917 10893 -664 -604 2135 C ATOM 667 O MET A 106 -7.880 -38.065 50.798 1.00 57.90 O ANISOU 667 O MET A 106 2049 9021 10931 -582 -577 2347 O ATOM 668 CB MET A 106 -7.810 -36.475 48.071 1.00 55.03 C ANISOU 668 CB MET A 106 1894 8623 10393 -756 -616 1993 C ATOM 669 CG MET A 106 -8.022 -35.091 47.461 1.00 57.90 C ANISOU 669 CG MET A 106 2358 9065 10575 -719 -564 1943 C ATOM 670 SD MET A 106 -8.854 -33.909 48.535 1.00 61.85 S ANISOU 670 SD MET A 106 2872 9706 10922 -534 -461 2127 S ATOM 671 CE MET A 106 -8.815 -32.508 47.501 1.00 58.47 C ANISOU 671 CE MET A 106 2466 9352 10398 -555 -453 2172 C ATOM 672 N PHE A 107 -6.014 -38.771 49.737 1.00 55.11 N ANISOU 672 N PHE A 107 1763 8472 10705 -756 -663 2027 N ATOM 673 CA PHE A 107 -5.995 -40.079 50.380 1.00 56.66 C ANISOU 673 CA PHE A 107 1838 8611 11080 -771 -704 2149 C ATOM 674 C PHE A 107 -5.423 -39.951 51.809 1.00 62.89 C ANISOU 674 C PHE A 107 2602 9457 11838 -638 -635 2238 C ATOM 675 O PHE A 107 -5.640 -40.851 52.627 1.00 63.98 O ANISOU 675 O PHE A 107 2624 9625 12060 -590 -636 2439 O ATOM 676 CB PHE A 107 -5.204 -41.085 49.521 1.00 58.85 C ANISOU 676 CB PHE A 107 2128 8739 11492 -888 -775 1990 C ATOM 677 CG PHE A 107 -5.403 -42.557 49.852 1.00 61.53 C ANISOU 677 CG PHE A 107 2364 9000 12014 -899 -812 2081 C ATOM 678 CD1 PHE A 107 -6.608 -43.195 49.591 1.00 65.42 C ANISOU 678 CD1 PHE A 107 2740 9458 12660 -960 -885 2246 C ATOM 679 CD2 PHE A 107 -4.372 -43.304 50.423 1.00 64.36 C ANISOU 679 CD2 PHE A 107 2739 9316 12399 -855 -778 2003 C ATOM 680 CE1 PHE A 107 -6.792 -44.548 49.921 1.00 67.35 C ANISOU 680 CE1 PHE A 107 2889 9623 13079 -972 -922 2333 C ATOM 681 CE2 PHE A 107 -4.541 -44.668 50.708 1.00 68.02 C ANISOU 681 CE2 PHE A 107 3105 9705 13034 -863 -810 2089 C ATOM 682 CZ PHE A 107 -5.758 -45.275 50.475 1.00 66.74 C ANISOU 682 CZ PHE A 107 2832 9506 13023 -921 -881 2252 C ATOM 683 N ASN A 108 -4.762 -38.813 52.122 1.00 59.44 N ANISOU 683 N ASN A 108 2274 9040 11271 -580 -579 2099 N ATOM 684 CA ASN A 108 -4.151 -38.554 53.422 1.00 59.29 C ANISOU 684 CA ASN A 108 2257 9074 11198 -458 -519 2156 C ATOM 685 C ASN A 108 -4.715 -37.261 54.069 1.00 62.77 C ANISOU 685 C ASN A 108 2756 9644 11450 -330 -446 2244 C ATOM 686 O ASN A 108 -3.960 -36.482 54.649 1.00 61.33 O ANISOU 686 O ASN A 108 2690 9494 11119 -274 -402 2139 O ATOM 687 CB ASN A 108 -2.630 -38.479 53.262 1.00 60.40 C ANISOU 687 CB ASN A 108 2476 9153 11321 -478 -512 1962 C ATOM 688 CG ASN A 108 -1.985 -39.806 52.932 1.00 89.75 C ANISOU 688 CG ASN A 108 6131 12748 15223 -568 -567 1903 C ATOM 689 OD1 ASN A 108 -1.732 -40.637 53.813 1.00 87.88 O ANISOU 689 OD1 ASN A 108 5790 12486 15113 -546 -579 2024 O ATOM 690 ND2 ASN A 108 -1.673 -40.017 51.656 1.00 82.50 N ANISOU 690 ND2 ASN A 108 5280 11748 14320 -664 -599 1717 N ATOM 691 N THR A 109 -6.048 -37.063 54.001 1.00 60.59 N ANISOU 691 N THR A 109 2396 9440 11186 -282 -436 2451 N ATOM 692 CA THR A 109 -6.749 -35.898 54.583 1.00 60.73 C ANISOU 692 CA THR A 109 2455 9581 11037 -148 -363 2572 C ATOM 693 C THR A 109 -7.685 -36.355 55.735 1.00 65.35 C ANISOU 693 C THR A 109 2906 10240 11684 -44 -336 2840 C ATOM 694 O THR A 109 -8.190 -37.475 55.689 1.00 65.48 O ANISOU 694 O THR A 109 2783 10217 11878 -109 -389 2956 O ATOM 695 CB THR A 109 -7.549 -35.148 53.476 1.00 70.30 C ANISOU 695 CB THR A 109 3712 10824 12175 -193 -367 2552 C ATOM 696 OG1 THR A 109 -6.730 -34.912 52.336 1.00 70.69 O ANISOU 696 OG1 THR A 109 3857 10796 12206 -306 -403 2316 O ATOM 697 CG2 THR A 109 -8.164 -33.831 53.947 1.00 69.16 C ANISOU 697 CG2 THR A 109 3651 10796 11832 -50 -283 2628 C ATOM 698 N GLY A 110 -7.916 -35.481 56.724 1.00 61.65 N ANISOU 698 N GLY A 110 2488 9874 11063 119 -256 2935 N ATOM 699 CA GLY A 110 -8.790 -35.732 57.867 1.00 62.03 C ANISOU 699 CA GLY A 110 2427 10011 11130 249 -212 3190 C ATOM 700 C GLY A 110 -8.208 -36.684 58.895 1.00 65.15 C ANISOU 700 C GLY A 110 2756 10377 11622 278 -219 3224 C ATOM 701 O GLY A 110 -7.223 -36.340 59.552 1.00 63.71 O ANISOU 701 O GLY A 110 2672 10190 11343 332 -193 3110 O ATOM 702 N PRO A 111 -8.797 -37.896 59.060 1.00 62.44 N ANISOU 702 N PRO A 111 2242 10008 11474 236 -260 3382 N ATOM 703 CA PRO A 111 -8.258 -38.843 60.056 1.00 62.46 C ANISOU 703 CA PRO A 111 2174 9982 11577 265 -265 3423 C ATOM 704 C PRO A 111 -6.943 -39.501 59.578 1.00 65.71 C ANISOU 704 C PRO A 111 2608 10253 12103 121 -332 3209 C ATOM 705 O PRO A 111 -6.139 -39.923 60.413 1.00 65.98 O ANISOU 705 O PRO A 111 2558 10237 12274 106 -354 3243 O ATOM 706 CB PRO A 111 -9.396 -39.864 60.233 1.00 65.41 C ANISOU 706 CB PRO A 111 2354 10386 12114 276 -283 3694 C ATOM 707 CG PRO A 111 -10.185 -39.794 58.982 1.00 70.27 C ANISOU 707 CG PRO A 111 2938 11038 12721 235 -298 3783 C ATOM 708 CD PRO A 111 -9.992 -38.441 58.373 1.00 64.85 C ANISOU 708 CD PRO A 111 2410 10310 11921 158 -309 3541 C ATOM 709 N ASN A 112 -6.704 -39.550 58.247 1.00 60.86 N ANISOU 709 N ASN A 112 2112 9582 11431 25 -357 2992 N ATOM 710 CA ASN A 112 -5.506 -40.144 57.634 1.00 59.81 C ANISOU 710 CA ASN A 112 2024 9324 11377 -101 -410 2773 C ATOM 711 C ASN A 112 -4.274 -39.193 57.671 1.00 61.49 C ANISOU 711 C ASN A 112 2393 9546 11422 -68 -374 2579 C ATOM 712 O ASN A 112 -3.158 -39.615 57.351 1.00 60.19 O ANISOU 712 O ASN A 112 2259 9302 11309 -133 -398 2425 O ATOM 713 CB ASN A 112 -5.823 -40.538 56.191 1.00 60.74 C ANISOU 713 CB ASN A 112 2140 9363 11575 -249 -478 2687 C ATOM 714 CG ASN A 112 -6.723 -41.745 56.046 1.00 85.41 C ANISOU 714 CG ASN A 112 5118 12465 14869 -309 -534 2867 C ATOM 715 OD1 ASN A 112 -7.748 -41.905 56.719 1.00 82.30 O ANISOU 715 OD1 ASN A 112 4600 12074 14598 -274 -540 3037 O ATOM 716 ND2 ASN A 112 -6.366 -42.600 55.116 1.00 77.09 N ANISOU 716 ND2 ASN A 112 4075 11385 13832 -409 -583 2834 N ATOM 717 N THR A 113 -4.479 -37.934 58.104 1.00 57.55 N ANISOU 717 N THR A 113 1994 9145 10726 33 -317 2594 N ATOM 718 CA THR A 113 -3.427 -36.923 58.236 1.00 56.53 C ANISOU 718 CA THR A 113 2022 9035 10421 74 -286 2437 C ATOM 719 C THR A 113 -2.514 -37.279 59.407 1.00 61.08 C ANISOU 719 C THR A 113 2591 9631 10985 158 -265 2467 C ATOM 720 O THR A 113 -1.308 -37.036 59.337 1.00 60.88 O ANISOU 720 O THR A 113 2654 9577 10901 138 -271 2315 O ATOM 721 CB THR A 113 -4.027 -35.522 58.421 1.00 65.74 C ANISOU 721 CB THR A 113 3293 10293 11391 167 -234 2473 C ATOM 722 OG1 THR A 113 -5.084 -35.309 57.488 1.00 66.32 O ANISOU 722 OG1 THR A 113 3330 10368 11503 104 -251 2511 O ATOM 723 CG2 THR A 113 -2.995 -34.419 58.239 1.00 63.52 C ANISOU 723 CG2 THR A 113 3187 10009 10940 170 -221 2283 C ATOM 724 N ARG A 114 -3.095 -37.857 60.477 1.00 58.36 N ANISOU 724 N ARG A 114 2134 9338 10701 248 -243 2675 N ATOM 725 CA ARG A 114 -2.407 -38.288 61.696 1.00 58.63 C ANISOU 725 CA ARG A 114 2132 9402 10743 336 -223 2747 C ATOM 726 C ARG A 114 -1.431 -39.434 61.387 1.00 62.46 C ANISOU 726 C ARG A 114 2547 9782 11404 228 -272 2655 C ATOM 727 O ARG A 114 -0.373 -39.522 62.023 1.00 61.89 O ANISOU 727 O ARG A 114 2503 9708 11307 255 -268 2600 O ATOM 728 CB ARG A 114 -3.453 -38.725 62.734 1.00 60.38 C ANISOU 728 CB ARG A 114 2230 9706 11006 450 -187 3010 C ATOM 729 CG ARG A 114 -2.966 -38.807 64.171 1.00 74.05 C ANISOU 729 CG ARG A 114 3957 11511 12666 592 -145 3113 C ATOM 730 CD ARG A 114 -4.195 -38.905 65.045 1.00 88.53 C ANISOU 730 CD ARG A 114 5692 13448 14497 726 -95 3377 C ATOM 731 NE ARG A 114 -3.894 -38.929 66.472 1.00102.44 N ANISOU 731 NE ARG A 114 7433 15278 16211 861 -57 3485 N ATOM 732 CZ ARG A 114 -4.824 -38.909 67.424 1.00118.62 C ANISOU 732 CZ ARG A 114 9412 17434 18225 1012 -1 3717 C ATOM 733 NH1 ARG A 114 -6.111 -38.848 67.103 1.00104.77 N ANISOU 733 NH1 ARG A 114 7596 15733 16478 1049 26 3874 N ATOM 734 NH2 ARG A 114 -4.473 -38.946 68.699 1.00106.80 N1+ ANISOU 734 NH2 ARG A 114 7902 15996 16680 1130 30 3801 N1+ ATOM 735 N ARG A 115 -1.791 -40.288 60.390 1.00 59.20 N ANISOU 735 N ARG A 115 2050 9280 11164 105 -322 2637 N ATOM 736 CA ARG A 115 -1.010 -41.439 59.923 1.00 59.23 C ANISOU 736 CA ARG A 115 1990 9168 11345 0 -369 2552 C ATOM 737 C ARG A 115 0.304 -41.023 59.237 1.00 62.66 C ANISOU 737 C ARG A 115 2542 9546 11721 -70 -381 2316 C ATOM 738 O ARG A 115 1.253 -41.815 59.210 1.00 62.26 O ANISOU 738 O ARG A 115 2466 9443 11745 -91 -390 2257 O ATOM 739 CB ARG A 115 -1.839 -42.304 58.956 1.00 59.86 C ANISOU 739 CB ARG A 115 1976 9164 11604 -110 -425 2592 C ATOM 740 CG ARG A 115 -2.584 -43.404 59.674 1.00 73.17 C ANISOU 740 CG ARG A 115 3510 10885 13408 -62 -428 2841 C ATOM 741 CD ARG A 115 -3.420 -44.312 58.798 1.00 88.33 C ANISOU 741 CD ARG A 115 5327 12688 15546 -187 -502 2869 C ATOM 742 NE ARG A 115 -4.406 -45.043 59.611 1.00103.13 N ANISOU 742 NE ARG A 115 7046 14598 17539 -145 -509 3124 N ATOM 743 CZ ARG A 115 -4.154 -46.132 60.342 1.00119.93 C ANISOU 743 CZ ARG A 115 9066 16709 19791 -108 -507 3239 C ATOM 744 NH1 ARG A 115 -2.930 -46.646 60.378 1.00107.48 N ANISOU 744 NH1 ARG A 115 7520 15080 18237 -107 -497 3121 N ATOM 745 NH2 ARG A 115 -5.121 -46.701 61.049 1.00108.13 N1+ ANISOU 745 NH2 ARG A 115 7427 15254 18402 -70 -513 3483 N1+ ATOM 746 N LEU A 116 0.355 -39.796 58.689 1.00 58.56 N ANISOU 746 N LEU A 116 2141 9040 11070 -101 -378 2193 N ATOM 747 CA LEU A 116 1.527 -39.261 57.990 1.00 57.59 C ANISOU 747 CA LEU A 116 2128 8872 10882 -168 -388 1978 C ATOM 748 C LEU A 116 2.703 -38.977 58.934 1.00 61.57 C ANISOU 748 C LEU A 116 2689 9415 11289 -104 -366 1937 C ATOM 749 O LEU A 116 2.519 -38.447 60.039 1.00 61.31 O ANISOU 749 O LEU A 116 2705 9472 11118 1 -334 2015 O ATOM 750 CB LEU A 116 1.174 -37.963 57.237 1.00 56.90 C ANISOU 750 CB LEU A 116 2154 8812 10652 -192 -383 1886 C ATOM 751 CG LEU A 116 0.216 -38.056 56.046 1.00 61.35 C ANISOU 751 CG LEU A 116 2689 9333 11287 -279 -414 1878 C ATOM 752 CD1 LEU A 116 -0.426 -36.727 55.785 1.00 60.84 C ANISOU 752 CD1 LEU A 116 2732 9325 11060 -268 -394 1830 C ATOM 753 CD2 LEU A 116 0.922 -38.551 54.797 1.00 63.36 C ANISOU 753 CD2 LEU A 116 2934 9472 11669 -403 -460 1729 C ATOM 754 N THR A 117 3.913 -39.317 58.462 1.00 57.94 N ANISOU 754 N THR A 117 2229 8889 10898 -167 -384 1816 N ATOM 755 CA THR A 117 5.183 -39.080 59.152 1.00 57.64 C ANISOU 755 CA THR A 117 2237 8882 10783 -129 -374 1769 C ATOM 756 C THR A 117 5.744 -37.734 58.657 1.00 59.59 C ANISOU 756 C THR A 117 2632 9153 10857 -152 -375 1624 C ATOM 757 O THR A 117 5.139 -37.113 57.783 1.00 58.44 O ANISOU 757 O THR A 117 2541 8994 10669 -199 -379 1557 O ATOM 758 CB THR A 117 6.167 -40.262 58.939 1.00 69.85 C ANISOU 758 CB THR A 117 3705 10350 12483 -182 -389 1721 C ATOM 759 OG1 THR A 117 6.347 -40.493 57.542 1.00 71.18 O ANISOU 759 OG1 THR A 117 3910 10439 12696 -285 -408 1560 O ATOM 760 CG2 THR A 117 5.706 -41.558 59.607 1.00 69.60 C ANISOU 760 CG2 THR A 117 3530 10282 12632 -166 -392 1864 C ATOM 761 N VAL A 118 6.883 -37.280 59.215 1.00 55.52 N ANISOU 761 N VAL A 118 2179 8673 10244 -123 -376 1582 N ATOM 762 CA VAL A 118 7.526 -36.008 58.854 1.00 54.79 C ANISOU 762 CA VAL A 118 2226 8601 9991 -147 -387 1456 C ATOM 763 C VAL A 118 7.936 -36.046 57.356 1.00 57.37 C ANISOU 763 C VAL A 118 2569 8857 10372 -262 -402 1301 C ATOM 764 O VAL A 118 7.709 -35.069 56.638 1.00 56.10 O ANISOU 764 O VAL A 118 2504 8704 10108 -291 -403 1219 O ATOM 765 CB VAL A 118 8.735 -35.668 59.783 1.00 59.23 C ANISOU 765 CB VAL A 118 2826 9199 10479 -115 -401 1449 C ATOM 766 CG1 VAL A 118 9.398 -34.357 59.378 1.00 58.62 C ANISOU 766 CG1 VAL A 118 2883 9129 10260 -162 -425 1314 C ATOM 767 CG2 VAL A 118 8.311 -35.593 61.245 1.00 59.62 C ANISOU 767 CG2 VAL A 118 2885 9326 10443 8 -386 1593 C ATOM 768 N SER A 119 8.501 -37.184 56.895 1.00 53.74 N ANISOU 768 N SER A 119 2017 8328 10074 -319 -409 1268 N ATOM 769 CA SER A 119 8.950 -37.399 55.518 1.00 52.91 C ANISOU 769 CA SER A 119 1919 8151 10034 -414 -418 1130 C ATOM 770 C SER A 119 7.783 -37.461 54.521 1.00 55.47 C ANISOU 770 C SER A 119 2254 8445 10378 -455 -422 1105 C ATOM 771 O SER A 119 7.872 -36.836 53.464 1.00 54.94 O ANISOU 771 O SER A 119 2271 8379 10225 -500 -424 999 O ATOM 772 CB SER A 119 9.766 -38.683 55.421 1.00 57.06 C ANISOU 772 CB SER A 119 2341 8607 10731 -440 -419 1127 C ATOM 773 OG SER A 119 9.011 -39.817 55.817 1.00 65.99 O ANISOU 773 OG SER A 119 3372 9711 11991 -411 -418 1249 O ATOM 774 N THR A 120 6.700 -38.206 54.852 1.00 50.92 N ANISOU 774 N THR A 120 1589 7844 9912 -441 -425 1214 N ATOM 775 CA THR A 120 5.520 -38.378 53.989 1.00 50.08 C ANISOU 775 CA THR A 120 1471 7706 9850 -484 -439 1220 C ATOM 776 C THR A 120 4.689 -37.087 53.899 1.00 52.06 C ANISOU 776 C THR A 120 1806 8033 9942 -454 -427 1238 C ATOM 777 O THR A 120 4.036 -36.871 52.877 1.00 51.17 O ANISOU 777 O THR A 120 1715 7901 9824 -506 -439 1197 O ATOM 778 CB THR A 120 4.639 -39.541 54.448 1.00 58.32 C ANISOU 778 CB THR A 120 2394 8717 11048 -471 -453 1363 C ATOM 779 OG1 THR A 120 4.248 -39.342 55.805 1.00 57.99 O ANISOU 779 OG1 THR A 120 2318 8755 10961 -370 -430 1519 O ATOM 780 CG2 THR A 120 5.317 -40.899 54.279 1.00 57.36 C ANISOU 780 CG2 THR A 120 2198 8499 11099 -512 -469 1331 C ATOM 781 N TRP A 121 4.716 -36.239 54.947 1.00 47.69 N ANISOU 781 N TRP A 121 1307 7561 9252 -368 -403 1297 N ATOM 782 CA TRP A 121 4.013 -34.954 54.954 1.00 46.77 C ANISOU 782 CA TRP A 121 1289 7511 8970 -326 -385 1308 C ATOM 783 C TRP A 121 4.655 -34.018 53.939 1.00 48.11 C ANISOU 783 C TRP A 121 1568 7668 9041 -389 -392 1142 C ATOM 784 O TRP A 121 3.947 -33.363 53.174 1.00 47.87 O ANISOU 784 O TRP A 121 1596 7653 8939 -409 -387 1108 O ATOM 785 CB TRP A 121 4.031 -34.319 56.354 1.00 45.88 C ANISOU 785 CB TRP A 121 1218 7478 8735 -208 -360 1413 C ATOM 786 CG TRP A 121 3.044 -33.209 56.527 1.00 46.91 C ANISOU 786 CG TRP A 121 1434 7674 8717 -144 -333 1464 C ATOM 787 CD1 TRP A 121 1.796 -33.305 57.065 1.00 50.32 C ANISOU 787 CD1 TRP A 121 1815 8151 9154 -76 -308 1616 C ATOM 788 CD2 TRP A 121 3.206 -31.834 56.137 1.00 46.21 C ANISOU 788 CD2 TRP A 121 1491 7609 8456 -139 -327 1369 C ATOM 789 NE1 TRP A 121 1.177 -32.075 57.056 1.00 49.71 N ANISOU 789 NE1 TRP A 121 1846 8128 8914 -21 -280 1623 N ATOM 790 CE2 TRP A 121 2.013 -31.157 56.478 1.00 50.56 C ANISOU 790 CE2 TRP A 121 2080 8219 8912 -60 -292 1468 C ATOM 791 CE3 TRP A 121 4.244 -31.106 55.531 1.00 46.81 C ANISOU 791 CE3 TRP A 121 1667 7663 8454 -195 -347 1218 C ATOM 792 CZ2 TRP A 121 1.822 -29.792 56.233 1.00 49.48 C ANISOU 792 CZ2 TRP A 121 2086 8112 8602 -31 -276 1414 C ATOM 793 CZ3 TRP A 121 4.050 -29.752 55.284 1.00 47.83 C ANISOU 793 CZ3 TRP A 121 1933 7821 8418 -175 -338 1166 C ATOM 794 CH2 TRP A 121 2.857 -29.107 55.644 1.00 48.70 C ANISOU 794 CH2 TRP A 121 2088 7983 8433 -92 -302 1260 C ATOM 795 N LEU A 122 6.002 -33.969 53.928 1.00 42.49 N ANISOU 795 N LEU A 122 879 6935 8331 -419 -403 1049 N ATOM 796 CA LEU A 122 6.808 -33.160 53.009 1.00 41.11 C ANISOU 796 CA LEU A 122 795 6750 8075 -481 -412 901 C ATOM 797 C LEU A 122 6.708 -33.692 51.581 1.00 45.46 C ANISOU 797 C LEU A 122 1316 7236 8720 -573 -421 799 C ATOM 798 O LEU A 122 6.911 -32.925 50.639 1.00 45.37 O ANISOU 798 O LEU A 122 1374 7220 8643 -624 -424 683 O ATOM 799 CB LEU A 122 8.280 -33.125 53.455 1.00 40.59 C ANISOU 799 CB LEU A 122 744 6688 7989 -481 -424 862 C ATOM 800 CG LEU A 122 8.578 -32.348 54.733 1.00 44.45 C ANISOU 800 CG LEU A 122 1307 7241 8339 -402 -427 928 C ATOM 801 CD1 LEU A 122 9.888 -32.778 55.324 1.00 45.07 C ANISOU 801 CD1 LEU A 122 1351 7323 8449 -393 -444 943 C ATOM 802 CD2 LEU A 122 8.561 -30.848 54.487 1.00 45.18 C ANISOU 802 CD2 LEU A 122 1544 7363 8261 -408 -433 857 C ATOM 803 N LEU A 123 6.386 -34.992 51.424 1.00 41.80 N ANISOU 803 N LEU A 123 755 6722 8405 -591 -429 846 N ATOM 804 CA LEU A 123 6.216 -35.636 50.128 1.00 41.54 C ANISOU 804 CA LEU A 123 702 6620 8459 -672 -444 757 C ATOM 805 C LEU A 123 4.921 -35.143 49.468 1.00 45.35 C ANISOU 805 C LEU A 123 1209 7124 8899 -687 -450 784 C ATOM 806 O LEU A 123 4.994 -34.647 48.346 1.00 44.19 O ANISOU 806 O LEU A 123 1125 6974 8689 -738 -453 680 O ATOM 807 CB LEU A 123 6.225 -37.174 50.264 1.00 42.26 C ANISOU 807 CB LEU A 123 691 6633 8734 -691 -459 786 C ATOM 808 CG LEU A 123 6.136 -37.997 48.967 1.00 47.52 C ANISOU 808 CG LEU A 123 1344 7212 9501 -770 -484 698 C ATOM 809 CD1 LEU A 123 7.424 -37.911 48.155 1.00 47.00 C ANISOU 809 CD1 LEU A 123 1349 7126 9383 -817 -474 535 C ATOM 810 CD2 LEU A 123 5.808 -39.454 49.264 1.00 51.97 C ANISOU 810 CD2 LEU A 123 1816 7691 10241 -777 -501 742 C ATOM 811 N ARG A 124 3.752 -35.242 50.164 1.00 42.55 N ANISOU 811 N ARG A 124 800 6798 8571 -640 -451 934 N ATOM 812 CA ARG A 124 2.463 -34.802 49.616 1.00 42.42 C ANISOU 812 CA ARG A 124 787 6808 8522 -652 -457 986 C ATOM 813 C ARG A 124 2.449 -33.281 49.387 1.00 44.88 C ANISOU 813 C ARG A 124 1210 7189 8651 -625 -430 947 C ATOM 814 O ARG A 124 1.894 -32.831 48.394 1.00 43.90 O ANISOU 814 O ARG A 124 1116 7075 8490 -666 -435 916 O ATOM 815 CB ARG A 124 1.261 -35.234 50.491 1.00 43.86 C ANISOU 815 CB ARG A 124 878 7019 8769 -598 -458 1177 C ATOM 816 CG ARG A 124 1.088 -34.589 51.864 1.00 55.59 C ANISOU 816 CG ARG A 124 2376 8591 10153 -478 -418 1307 C ATOM 817 CD ARG A 124 -0.379 -34.641 52.252 1.00 65.76 C ANISOU 817 CD ARG A 124 3599 9928 11460 -437 -412 1481 C ATOM 818 NE ARG A 124 -0.652 -34.090 53.578 1.00 77.73 N ANISOU 818 NE ARG A 124 5114 11526 12892 -307 -369 1628 N ATOM 819 CZ ARG A 124 -0.939 -32.817 53.826 1.00 96.47 C ANISOU 819 CZ ARG A 124 7579 13977 15096 -224 -327 1661 C ATOM 820 NH1 ARG A 124 -0.934 -31.925 52.843 1.00 84.57 N ANISOU 820 NH1 ARG A 124 6165 12478 13490 -263 -323 1560 N ATOM 821 NH2 ARG A 124 -1.203 -32.421 55.062 1.00 87.12 N1+ ANISOU 821 NH2 ARG A 124 6399 12864 13839 -97 -287 1796 N1+ ATOM 822 N GLN A 125 3.094 -32.511 50.270 1.00 40.61 N ANISOU 822 N GLN A 125 737 6695 7999 -559 -405 948 N ATOM 823 CA GLN A 125 3.167 -31.060 50.156 1.00 39.85 C ANISOU 823 CA GLN A 125 760 6652 7729 -531 -383 906 C ATOM 824 C GLN A 125 4.166 -30.657 49.049 1.00 43.10 C ANISOU 824 C GLN A 125 1234 7030 8110 -613 -395 734 C ATOM 825 O GLN A 125 3.948 -29.659 48.361 1.00 42.70 O ANISOU 825 O GLN A 125 1261 7003 7962 -633 -387 677 O ATOM 826 CB GLN A 125 3.564 -30.450 51.509 1.00 41.32 C ANISOU 826 CB GLN A 125 1003 6891 7806 -430 -362 976 C ATOM 827 CG GLN A 125 3.260 -28.961 51.649 1.00 57.69 C ANISOU 827 CG GLN A 125 3207 9017 9696 -379 -339 967 C ATOM 828 CD GLN A 125 1.788 -28.660 51.579 1.00 80.00 C ANISOU 828 CD GLN A 125 6027 11885 12486 -339 -313 1064 C ATOM 829 OE1 GLN A 125 0.992 -29.077 52.437 1.00 78.38 O ANISOU 829 OE1 GLN A 125 5762 11717 12303 -261 -293 1215 O ATOM 830 NE2 GLN A 125 1.399 -27.932 50.548 1.00 69.54 N ANISOU 830 NE2 GLN A 125 4756 10561 11105 -389 -310 989 N ATOM 831 N GLY A 126 5.223 -31.451 48.881 1.00 39.02 N ANISOU 831 N GLY A 126 760 6424 7644 -642 -405 665 N ATOM 832 CA GLY A 126 6.255 -31.226 47.877 1.00 38.36 C ANISOU 832 CA GLY A 126 774 6281 7521 -699 -407 519 C ATOM 833 C GLY A 126 5.779 -31.449 46.461 1.00 40.73 C ANISOU 833 C GLY A 126 925 6615 7937 -797 -427 439 C ATOM 834 O GLY A 126 6.103 -30.653 45.578 1.00 40.08 O ANISOU 834 O GLY A 126 910 6544 7774 -835 -422 343 O ATOM 835 N LEU A 127 4.992 -32.526 46.243 1.00 38.32 N ANISOU 835 N LEU A 127 902 6085 7572 -744 -416 485 N ATOM 836 CA LEU A 127 4.437 -32.891 44.938 1.00 38.57 C ANISOU 836 CA LEU A 127 987 6044 7624 -794 -431 422 C ATOM 837 C LEU A 127 3.468 -31.827 44.411 1.00 41.87 C ANISOU 837 C LEU A 127 1222 6630 8056 -854 -446 431 C ATOM 838 O LEU A 127 3.388 -31.627 43.196 1.00 41.14 O ANISOU 838 O LEU A 127 1264 6474 7892 -885 -446 339 O ATOM 839 CB LEU A 127 3.718 -34.247 45.024 1.00 39.47 C ANISOU 839 CB LEU A 127 1027 6087 7883 -807 -461 494 C ATOM 840 CG LEU A 127 4.582 -35.508 45.203 1.00 43.43 C ANISOU 840 CG LEU A 127 1208 6636 8658 -879 -494 457 C ATOM 841 CD1 LEU A 127 3.776 -36.631 45.832 1.00 44.60 C ANISOU 841 CD1 LEU A 127 1281 6730 8934 -871 -523 578 C ATOM 842 CD2 LEU A 127 5.213 -35.962 43.885 1.00 44.80 C ANISOU 842 CD2 LEU A 127 1274 6810 8936 -975 -516 302 C ATOM 843 N ILE A 128 2.752 -31.145 45.327 1.00 40.75 N ANISOU 843 N ILE A 128 1243 6479 7762 -758 -416 551 N ATOM 844 CA ILE A 128 1.803 -30.076 45.022 1.00 41.22 C ANISOU 844 CA ILE A 128 1318 6616 7727 -749 -403 594 C ATOM 845 C ILE A 128 2.581 -28.808 44.638 1.00 43.42 C ANISOU 845 C ILE A 128 1398 7076 8024 -815 -405 486 C ATOM 846 O ILE A 128 2.198 -28.140 43.673 1.00 43.23 O ANISOU 846 O ILE A 128 1417 7078 7930 -842 -399 453 O ATOM 847 CB ILE A 128 0.836 -29.862 46.220 1.00 44.38 C ANISOU 847 CB ILE A 128 1437 7197 8229 -706 -402 763 C ATOM 848 CG1 ILE A 128 -0.216 -30.977 46.194 1.00 46.31 C ANISOU 848 CG1 ILE A 128 1554 7465 8575 -728 -424 881 C ATOM 849 CG2 ILE A 128 0.087 -28.527 46.124 1.00 44.86 C ANISOU 849 CG2 ILE A 128 1558 7348 8138 -640 -365 788 C ATOM 850 CD1 ILE A 128 -0.315 -31.988 47.162 1.00 60.28 C ANISOU 850 CD1 ILE A 128 3207 9168 10528 -787 -471 897 C ATOM 851 N ASP A 129 3.680 -28.500 45.373 1.00 39.18 N ANISOU 851 N ASP A 129 902 6537 7449 -792 -396 442 N ATOM 852 CA ASP A 129 4.534 -27.339 45.112 1.00 38.00 C ANISOU 852 CA ASP A 129 850 6407 7180 -804 -386 349 C ATOM 853 C ASP A 129 5.272 -27.497 43.779 1.00 40.98 C ANISOU 853 C ASP A 129 1223 6749 7597 -889 -397 215 C ATOM 854 O ASP A 129 5.496 -26.503 43.087 1.00 40.35 O ANISOU 854 O ASP A 129 1210 6692 7431 -918 -388 145 O ATOM 855 CB ASP A 129 5.525 -27.125 46.260 1.00 39.60 C ANISOU 855 CB ASP A 129 1089 6615 7341 -762 -387 358 C ATOM 856 CG ASP A 129 4.896 -26.683 47.569 1.00 48.89 C ANISOU 856 CG ASP A 129 2317 7837 8423 -667 -373 469 C ATOM 857 OD1 ASP A 129 3.655 -26.712 47.677 1.00 51.01 O1- ANISOU 857 OD1 ASP A 129 2546 8127 8707 -618 -358 577 O1- ATOM 858 OD2 ASP A 129 5.641 -26.321 48.485 1.00 53.09 O ANISOU 858 OD2 ASP A 129 2928 8380 8862 -639 -378 455 O ATOM 859 N THR A 130 5.624 -28.750 43.421 1.00 37.23 N ANISOU 859 N THR A 130 672 6219 7254 -923 -412 184 N ATOM 860 CA THR A 130 6.307 -29.109 42.175 1.00 37.01 C ANISOU 860 CA THR A 130 637 6151 7274 -989 -418 63 C ATOM 861 C THR A 130 5.339 -28.917 40.998 1.00 40.74 C ANISOU 861 C THR A 130 1124 6632 7724 -1029 -426 39 C ATOM 862 O THR A 130 5.735 -28.327 39.996 1.00 40.45 O ANISOU 862 O THR A 130 1129 6601 7639 -1071 -420 -59 O ATOM 863 CB THR A 130 6.848 -30.558 42.256 1.00 43.57 C ANISOU 863 CB THR A 130 1390 6913 8252 -1000 -432 51 C ATOM 864 OG1 THR A 130 7.687 -30.686 43.405 1.00 43.31 O ANISOU 864 OG1 THR A 130 1333 6883 8240 -957 -425 99 O ATOM 865 CG2 THR A 130 7.633 -30.972 41.016 1.00 41.05 C ANISOU 865 CG2 THR A 130 1076 6551 7970 -1050 -429 -77 C ATOM 866 N SER A 131 4.083 -29.388 41.139 1.00 37.06 N ANISOU 866 N SER A 131 619 6172 7289 -1015 -440 142 N ATOM 867 CA SER A 131 3.048 -29.316 40.111 1.00 37.24 C ANISOU 867 CA SER A 131 649 6204 7297 -1053 -456 147 C ATOM 868 C SER A 131 2.644 -27.871 39.766 1.00 40.86 C ANISOU 868 C SER A 131 1175 6737 7611 -1041 -429 146 C ATOM 869 O SER A 131 2.323 -27.611 38.603 1.00 40.92 O ANISOU 869 O SER A 131 1205 6755 7587 -1090 -436 86 O ATOM 870 CB SER A 131 1.808 -30.091 40.548 1.00 41.16 C ANISOU 870 CB SER A 131 1063 6697 7879 -1043 -482 281 C ATOM 871 OG SER A 131 1.186 -29.528 41.692 1.00 49.29 O ANISOU 871 OG SER A 131 2096 7790 8843 -967 -455 412 O ATOM 872 N LEU A 132 2.630 -26.949 40.762 1.00 36.24 N ANISOU 872 N LEU A 132 636 6198 6936 -972 -400 212 N ATOM 873 CA LEU A 132 2.252 -25.538 40.577 1.00 35.21 C ANISOU 873 CA LEU A 132 589 6127 6663 -947 -372 218 C ATOM 874 C LEU A 132 3.281 -24.845 39.693 1.00 38.83 C ANISOU 874 C LEU A 132 1108 6583 7062 -998 -366 83 C ATOM 875 O LEU A 132 2.920 -24.366 38.615 1.00 38.82 O ANISOU 875 O LEU A 132 1126 6604 7020 -1037 -363 42 O ATOM 876 CB LEU A 132 2.160 -24.861 41.960 1.00 34.88 C ANISOU 876 CB LEU A 132 601 6117 6536 -858 -347 303 C ATOM 877 CG LEU A 132 1.358 -23.595 42.230 1.00 39.17 C ANISOU 877 CG LEU A 132 1207 6720 6956 -794 -314 388 C ATOM 878 CD1 LEU A 132 1.408 -23.289 43.683 1.00 39.24 C ANISOU 878 CD1 LEU A 132 1301 6743 6864 -710 -294 429 C ATOM 879 CD2 LEU A 132 1.879 -22.389 41.532 1.00 40.57 C ANISOU 879 CD2 LEU A 132 1445 6922 7049 -837 -303 315 C ATOM 880 N THR A 133 4.566 -24.835 40.129 1.00 34.37 N ANISOU 880 N THR A 133 609 5974 6474 -987 -362 23 N ATOM 881 CA THR A 133 5.691 -24.221 39.415 1.00 33.48 C ANISOU 881 CA THR A 133 623 5827 6272 -1007 -349 -87 C ATOM 882 C THR A 133 5.929 -24.897 38.062 1.00 35.63 C ANISOU 882 C THR A 133 808 6093 6636 -1082 -361 -184 C ATOM 883 O THR A 133 6.526 -24.268 37.191 1.00 35.75 O ANISOU 883 O THR A 133 868 6119 6597 -1111 -349 -266 O ATOM 884 CB THR A 133 6.971 -24.219 40.252 1.00 42.67 C ANISOU 884 CB THR A 133 1680 7036 7494 -1031 -366 -107 C ATOM 885 OG1 THR A 133 7.025 -25.403 41.042 1.00 43.58 O ANISOU 885 OG1 THR A 133 1734 7122 7702 -1000 -377 -51 O ATOM 886 CG2 THR A 133 7.067 -22.993 41.144 1.00 40.93 C ANISOU 886 CG2 THR A 133 1557 6848 7147 -998 -362 -78 C ATOM 887 N ALA A 134 5.450 -26.151 37.875 1.00 32.29 N ANISOU 887 N ALA A 134 714 5441 6112 -975 -340 -162 N ATOM 888 CA ALA A 134 5.544 -26.854 36.594 1.00 31.93 C ANISOU 888 CA ALA A 134 701 5340 6092 -1005 -344 -253 C ATOM 889 C ALA A 134 4.617 -26.184 35.589 1.00 34.67 C ANISOU 889 C ALA A 134 879 5821 6472 -1097 -367 -269 C ATOM 890 O ALA A 134 4.997 -26.016 34.436 1.00 33.40 O ANISOU 890 O ALA A 134 762 5650 6278 -1124 -361 -363 O ATOM 891 CB ALA A 134 5.193 -28.318 36.758 1.00 32.94 C ANISOU 891 CB ALA A 134 733 5414 6368 -1023 -377 -233 C ATOM 892 N SER A 135 3.407 -25.784 36.037 1.00 32.85 N ANISOU 892 N SER A 135 841 5543 6096 -1014 -347 -161 N ATOM 893 CA SER A 135 2.398 -25.101 35.225 1.00 32.92 C ANISOU 893 CA SER A 135 901 5589 6016 -1024 -341 -148 C ATOM 894 C SER A 135 2.700 -23.607 35.121 1.00 36.54 C ANISOU 894 C SER A 135 1288 6166 6428 -1059 -322 -189 C ATOM 895 O SER A 135 2.408 -23.005 34.088 1.00 36.70 O ANISOU 895 O SER A 135 1359 6196 6390 -1087 -313 -263 O ATOM 896 CB SER A 135 1.005 -25.311 35.811 1.00 35.15 C ANISOU 896 CB SER A 135 999 5971 6385 -1048 -367 -11 C ATOM 897 OG SER A 135 0.648 -26.683 35.806 1.00 41.26 O ANISOU 897 OG SER A 135 1307 6885 7485 -1200 -451 18 O ATOM 898 N VAL A 136 3.285 -23.013 36.186 1.00 33.31 N ANISOU 898 N VAL A 136 1135 5669 5852 -944 -283 -137 N ATOM 899 CA VAL A 136 3.643 -21.590 36.263 1.00 32.80 C ANISOU 899 CA VAL A 136 1156 5638 5668 -931 -258 -161 C ATOM 900 C VAL A 136 4.758 -21.309 35.243 1.00 35.67 C ANISOU 900 C VAL A 136 1299 6110 6145 -1051 -275 -284 C ATOM 901 O VAL A 136 4.630 -20.361 34.469 1.00 35.16 O ANISOU 901 O VAL A 136 1294 6070 5994 -1063 -258 -315 O ATOM 902 CB VAL A 136 4.025 -21.176 37.714 1.00 35.96 C ANISOU 902 CB VAL A 136 1382 6136 6144 -949 -275 -119 C ATOM 903 CG1 VAL A 136 4.820 -19.872 37.761 1.00 35.58 C ANISOU 903 CG1 VAL A 136 1424 6121 5972 -938 -257 -127 C ATOM 904 CG2 VAL A 136 2.789 -21.067 38.589 1.00 36.08 C ANISOU 904 CG2 VAL A 136 1366 6156 6185 -894 -277 0 C ATOM 905 N ALA A 137 5.811 -22.152 35.213 1.00 33.49 N ANISOU 905 N ALA A 137 1124 5731 5869 -1019 -269 -336 N ATOM 906 CA ALA A 137 6.934 -22.015 34.281 1.00 33.34 C ANISOU 906 CA ALA A 137 1100 5714 5854 -1054 -259 -436 C ATOM 907 C ALA A 137 6.514 -22.347 32.850 1.00 36.62 C ANISOU 907 C ALA A 137 1198 6282 6432 -1194 -290 -508 C ATOM 908 O ALA A 137 7.066 -21.767 31.915 1.00 35.81 O ANISOU 908 O ALA A 137 1170 6193 6244 -1199 -266 -565 O ATOM 909 CB ALA A 137 8.084 -22.907 34.701 1.00 34.14 C ANISOU 909 CB ALA A 137 1129 5780 6063 -1059 -269 -463 C ATOM 910 N ASN A 138 5.531 -23.268 32.681 1.00 35.16 N ANISOU 910 N ASN A 138 1083 6021 6257 -1165 -300 -489 N ATOM 911 CA ASN A 138 4.981 -23.657 31.375 1.00 35.65 C ANISOU 911 CA ASN A 138 1074 6117 6357 -1225 -319 -548 C ATOM 912 C ASN A 138 4.242 -22.486 30.743 1.00 40.79 C ANISOU 912 C ASN A 138 1507 6950 7042 -1329 -339 -530 C ATOM 913 O ASN A 138 4.520 -22.158 29.590 1.00 40.24 O ANISOU 913 O ASN A 138 1456 6909 6924 -1359 -331 -600 O ATOM 914 CB ASN A 138 4.062 -24.867 31.491 1.00 35.05 C ANISOU 914 CB ASN A 138 1023 5955 6340 -1211 -349 -518 C ATOM 915 CG ASN A 138 4.727 -26.183 31.164 1.00 53.48 C ANISOU 915 CG ASN A 138 3025 8399 8897 -1370 -413 -631 C ATOM 916 OD1 ASN A 138 5.352 -26.347 30.106 1.00 42.68 O ANISOU 916 OD1 ASN A 138 1756 7027 7431 -1373 -404 -685 O ATOM 917 ND2 ASN A 138 4.492 -27.199 32.001 1.00 49.28 N ANISOU 917 ND2 ASN A 138 2551 7755 8419 -1329 -415 -652 N ATOM 918 N LEU A 139 3.345 -21.829 31.512 1.00 39.49 N ANISOU 918 N LEU A 139 1354 6812 6839 -1297 -334 -424 N ATOM 919 CA LEU A 139 2.593 -20.648 31.074 1.00 40.42 C ANISOU 919 CA LEU A 139 1509 6992 6857 -1291 -315 -377 C ATOM 920 C LEU A 139 3.529 -19.465 30.821 1.00 46.49 C ANISOU 920 C LEU A 139 2337 7792 7533 -1290 -281 -427 C ATOM 921 O LEU A 139 3.254 -18.663 29.932 1.00 46.72 O ANISOU 921 O LEU A 139 2391 7870 7491 -1309 -267 -445 O ATOM 922 CB LEU A 139 1.527 -20.257 32.111 1.00 40.59 C ANISOU 922 CB LEU A 139 1534 7028 6860 -1237 -308 -246 C ATOM 923 CG LEU A 139 0.291 -21.151 32.192 1.00 46.20 C ANISOU 923 CG LEU A 139 2179 7730 7646 -1242 -339 -165 C ATOM 924 CD1 LEU A 139 -0.390 -21.013 33.528 1.00 46.34 C ANISOU 924 CD1 LEU A 139 2183 7737 7686 -1176 -332 -51 C ATOM 925 CD2 LEU A 139 -0.689 -20.854 31.047 1.00 49.74 C ANISOU 925 CD2 LEU A 139 2620 8235 8045 -1264 -342 -118 C ATOM 926 N LEU A 140 4.645 -19.378 31.585 1.00 44.16 N ANISOU 926 N LEU A 140 2061 7471 7244 -1273 -274 -446 N ATOM 927 CA LEU A 140 5.672 -18.337 31.443 1.00 44.56 C ANISOU 927 CA LEU A 140 2163 7544 7225 -1281 -254 -487 C ATOM 928 C LEU A 140 6.412 -18.533 30.127 1.00 51.05 C ANISOU 928 C LEU A 140 2962 8380 8057 -1323 -247 -585 C ATOM 929 O LEU A 140 6.677 -17.560 29.428 1.00 50.82 O ANISOU 929 O LEU A 140 2963 8390 7955 -1339 -226 -611 O ATOM 930 CB LEU A 140 6.647 -18.377 32.640 1.00 44.49 C ANISOU 930 CB LEU A 140 2171 7500 7234 -1259 -263 -470 C ATOM 931 CG LEU A 140 7.738 -17.290 32.743 1.00 48.90 C ANISOU 931 CG LEU A 140 2774 8069 7735 -1277 -257 -500 C ATOM 932 CD1 LEU A 140 7.163 -15.965 33.212 1.00 48.60 C ANISOU 932 CD1 LEU A 140 2823 8053 7589 -1259 -248 -452 C ATOM 933 CD2 LEU A 140 8.829 -17.719 33.712 1.00 51.59 C ANISOU 933 CD2 LEU A 140 3105 8373 8124 -1271 -279 -493 C ATOM 934 N ALA A 141 6.710 -19.799 29.777 1.00 49.62 N ANISOU 934 N ALA A 141 2727 8163 7962 -1336 -261 -636 N ATOM 935 CA ALA A 141 7.395 -20.180 28.538 1.00 50.56 C ANISOU 935 CA ALA A 141 2830 8291 8090 -1362 -251 -731 C ATOM 936 C ALA A 141 6.493 -19.956 27.329 1.00 56.59 C ANISOU 936 C ALA A 141 3607 9098 8796 -1387 -251 -752 C ATOM 937 O ALA A 141 6.996 -19.587 26.271 1.00 56.54 O ANISOU 937 O ALA A 141 3616 9135 8730 -1401 -227 -804 O ATOM 938 CB ALA A 141 7.835 -21.633 28.601 1.00 51.72 C ANISOU 938 CB ALA A 141 2933 8378 8341 -1359 -267 -776 C ATOM 939 N ILE A 142 5.166 -20.176 27.486 1.00 54.20 N ANISOU 939 N ILE A 142 3294 8791 8509 -1393 -278 -699 N ATOM 940 CA ILE A 142 4.153 -19.977 26.438 1.00 54.78 C ANISOU 940 CA ILE A 142 3373 8908 8533 -1421 -288 -696 C ATOM 941 C ILE A 142 4.040 -18.466 26.163 1.00 59.63 C ANISOU 941 C ILE A 142 4028 9592 9037 -1416 -251 -671 C ATOM 942 O ILE A 142 3.932 -18.060 25.003 1.00 59.57 O ANISOU 942 O ILE A 142 4029 9632 8973 -1440 -244 -709 O ATOM 943 CB ILE A 142 2.786 -20.629 26.835 1.00 58.14 C ANISOU 943 CB ILE A 142 3768 9316 9005 -1424 -325 -608 C ATOM 944 CG1 ILE A 142 2.900 -22.171 26.853 1.00 59.27 C ANISOU 944 CG1 ILE A 142 3874 9391 9255 -1449 -373 -650 C ATOM 945 CG2 ILE A 142 1.660 -20.190 25.894 1.00 58.65 C ANISOU 945 CG2 ILE A 142 3837 9445 9002 -1444 -330 -556 C ATOM 946 CD1 ILE A 142 1.813 -22.923 27.669 1.00 66.71 C ANISOU 946 CD1 ILE A 142 4773 10297 10278 -1444 -410 -548 C ATOM 947 N ALA A 143 4.102 -17.647 27.234 1.00 56.57 N ANISOU 947 N ALA A 143 3671 9205 8619 -1382 -231 -610 N ATOM 948 CA ALA A 143 4.035 -16.186 27.170 1.00 56.59 C ANISOU 948 CA ALA A 143 3724 9254 8522 -1371 -199 -578 C ATOM 949 C ALA A 143 5.227 -15.607 26.393 1.00 62.11 C ANISOU 949 C ALA A 143 4436 9978 9186 -1392 -177 -654 C ATOM 950 O ALA A 143 5.053 -14.643 25.646 1.00 61.83 O ANISOU 950 O ALA A 143 4416 9997 9079 -1407 -157 -664 O ATOM 951 CB ALA A 143 3.986 -15.602 28.570 1.00 56.98 C ANISOU 951 CB ALA A 143 3817 9279 8554 -1327 -193 -502 C ATOM 952 N ILE A 144 6.423 -16.216 26.552 1.00 60.00 N ANISOU 952 N ILE A 144 4153 9675 8969 -1392 -180 -696 N ATOM 953 CA ILE A 144 7.651 -15.825 25.858 1.00 60.51 C ANISOU 953 CA ILE A 144 4215 9764 9011 -1408 -158 -750 C ATOM 954 C ILE A 144 7.534 -16.290 24.398 1.00 67.29 C ANISOU 954 C ILE A 144 5047 10659 9861 -1425 -146 -827 C ATOM 955 O ILE A 144 7.888 -15.536 23.490 1.00 67.27 O ANISOU 955 O ILE A 144 5053 10711 9795 -1436 -119 -848 O ATOM 956 CB ILE A 144 8.915 -16.386 26.586 1.00 63.40 C ANISOU 956 CB ILE A 144 4560 10086 9445 -1401 -167 -760 C ATOM 957 CG1 ILE A 144 9.057 -15.762 27.995 1.00 63.40 C ANISOU 957 CG1 ILE A 144 4601 10054 9435 -1386 -185 -686 C ATOM 958 CG2 ILE A 144 10.195 -16.163 25.768 1.00 64.35 C ANISOU 958 CG2 ILE A 144 4660 10239 9553 -1415 -143 -803 C ATOM 959 CD1 ILE A 144 9.939 -16.540 29.006 1.00 72.22 C ANISOU 959 CD1 ILE A 144 5692 11120 10629 -1375 -206 -677 C ATOM 960 N GLU A 145 6.979 -17.504 24.180 1.00 65.56 N ANISOU 960 N GLU A 145 4801 10409 9699 -1427 -168 -865 N ATOM 961 CA GLU A 145 6.789 -18.107 22.856 1.00 66.60 C ANISOU 961 CA GLU A 145 4922 10562 9820 -1440 -166 -947 C ATOM 962 C GLU A 145 5.860 -17.254 21.973 1.00 71.57 C ANISOU 962 C GLU A 145 5571 11255 10368 -1462 -166 -935 C ATOM 963 O GLU A 145 6.146 -17.067 20.785 1.00 71.31 O ANISOU 963 O GLU A 145 5540 11258 10296 -1471 -158 -1001 O ATOM 964 CB GLU A 145 6.267 -19.547 22.963 1.00 68.58 C ANISOU 964 CB GLU A 145 5153 10746 10157 -1441 -202 -987 C ATOM 965 CG GLU A 145 6.914 -20.441 21.905 1.00 81.27 C ANISOU 965 CG GLU A 145 6756 12338 11784 -1427 -189 -1086 C ATOM 966 CD GLU A 145 8.417 -20.699 21.989 1.00107.72 C ANISOU 966 CD GLU A 145 10087 15689 15154 -1396 -148 -1101 C ATOM 967 OE1 GLU A 145 8.989 -20.592 23.100 1.00102.64 O ANISOU 967 OE1 GLU A 145 9425 15010 14565 -1386 -152 -1050 O ATOM 968 OE2 GLU A 145 9.021 -21.020 20.938 1.00106.12 O1- ANISOU 968 OE2 GLU A 145 9885 15524 14911 -1379 -112 -1159 O1- ATOM 969 N ARG A 146 4.791 -16.694 22.565 1.00 69.11 N ANISOU 969 N ARG A 146 5275 10959 10026 -1463 -172 -848 N ATOM 970 CA ARG A 146 3.861 -15.821 21.846 1.00 69.56 C ANISOU 970 CA ARG A 146 5345 11082 10004 -1479 -166 -817 C ATOM 971 C ARG A 146 4.475 -14.427 21.629 1.00 75.02 C ANISOU 971 C ARG A 146 6063 11825 10615 -1471 -122 -796 C ATOM 972 O ARG A 146 4.163 -13.779 20.626 1.00 74.72 O ANISOU 972 O ARG A 146 6032 11853 10507 -1484 -104 -802 O ATOM 973 CB ARG A 146 2.506 -15.702 22.585 1.00 69.01 C ANISOU 973 CB ARG A 146 5270 11006 9943 -1477 -190 -721 C ATOM 974 CG ARG A 146 1.705 -17.007 22.738 1.00 78.63 C ANISOU 974 CG ARG A 146 6455 12183 11238 -1500 -244 -728 C ATOM 975 CD ARG A 146 1.499 -17.800 21.454 1.00 88.23 C ANISOU 975 CD ARG A 146 7665 13411 12448 -1539 -272 -818 C ATOM 976 NE ARG A 146 0.688 -17.100 20.461 1.00 98.70 N ANISOU 976 NE ARG A 146 8997 14816 13687 -1562 -269 -800 N ATOM 977 CZ ARG A 146 0.405 -17.598 19.263 1.00113.95 C ANISOU 977 CZ ARG A 146 10938 16781 15577 -1590 -281 -880 C ATOM 978 NH1 ARG A 146 0.871 -18.786 18.904 1.00100.98 N ANISOU 978 NH1 ARG A 146 9306 15096 13965 -1589 -292 -987 N ATOM 979 NH2 ARG A 146 -0.326 -16.901 18.408 1.00101.49 N1+ ANISOU 979 NH2 ARG A 146 9361 15280 13920 -1611 -279 -850 N1+ ATOM 980 N HIS A 147 5.363 -13.986 22.554 1.00 72.73 N ANISOU 980 N HIS A 147 5791 11504 10340 -1453 -109 -773 N ATOM 981 CA HIS A 147 6.049 -12.689 22.495 1.00 73.19 C ANISOU 981 CA HIS A 147 5878 11592 10337 -1452 -79 -751 C ATOM 982 C HIS A 147 7.105 -12.662 21.373 1.00 79.41 C ANISOU 982 C HIS A 147 6640 12424 11109 -1465 -55 -820 C ATOM 983 O HIS A 147 7.441 -11.581 20.889 1.00 79.20 O ANISOU 983 O HIS A 147 6626 12449 11018 -1473 -28 -806 O ATOM 984 CB HIS A 147 6.705 -12.353 23.841 1.00 73.76 C ANISOU 984 CB HIS A 147 5978 11608 10439 -1438 -89 -710 C ATOM 985 CG HIS A 147 7.113 -10.921 23.972 1.00 77.09 C ANISOU 985 CG HIS A 147 6434 12044 10811 -1447 -74 -688 C ATOM 986 ND1 HIS A 147 8.400 -10.503 23.662 1.00 79.00 N ANISOU 986 ND1 HIS A 147 6647 12291 11078 -1464 -69 -723 N ATOM 987 CD2 HIS A 147 6.384 -9.854 24.377 1.00 78.64 C ANISOU 987 CD2 HIS A 147 6691 12249 10940 -1441 -64 -630 C ATOM 988 CE1 HIS A 147 8.412 -9.201 23.893 1.00 78.41 C ANISOU 988 CE1 HIS A 147 6612 12227 10955 -1478 -64 -682 C ATOM 989 NE2 HIS A 147 7.218 -8.765 24.321 1.00 78.52 N ANISOU 989 NE2 HIS A 147 6687 12238 10911 -1464 -62 -631 N ATOM 990 N ILE A 148 7.610 -13.839 20.951 1.00 77.79 N ANISOU 990 N ILE A 148 6400 12197 10961 -1461 -61 -890 N ATOM 991 CA ILE A 148 8.601 -13.965 19.875 1.00 78.85 C ANISOU 991 CA ILE A 148 6507 12372 11080 -1457 -32 -955 C ATOM 992 C ILE A 148 7.860 -14.020 18.512 1.00 84.64 C ANISOU 992 C ILE A 148 7245 13164 11752 -1464 -27 -998 C ATOM 993 O ILE A 148 8.202 -13.235 17.625 1.00 84.58 O ANISOU 993 O ILE A 148 7227 13218 11691 -1458 7 -1030 O ATOM 994 CB ILE A 148 9.544 -15.190 20.107 1.00 82.44 C ANISOU 994 CB ILE A 148 6932 12776 11617 -1436 -36 -1007 C ATOM 995 CG1 ILE A 148 10.403 -14.977 21.385 1.00 82.48 C ANISOU 995 CG1 ILE A 148 6929 12732 11678 -1434 -47 -954 C ATOM 996 CG2 ILE A 148 10.426 -15.500 18.880 1.00 84.13 C ANISOU 996 CG2 ILE A 148 7121 13037 11809 -1414 3 -1070 C ATOM 997 CD1 ILE A 148 11.031 -16.257 21.993 1.00 89.41 C ANISOU 997 CD1 ILE A 148 7779 13543 12650 -1414 -62 -982 C ATOM 998 N THR A 149 6.831 -14.901 18.362 1.00 82.36 N ANISOU 998 N THR A 149 6966 12858 11468 -1479 -62 -990 N ATOM 999 CA THR A 149 6.045 -15.056 17.116 1.00 83.00 C ANISOU 999 CA THR A 149 7052 12990 11492 -1496 -72 -1022 C ATOM 1000 C THR A 149 5.381 -13.764 16.589 1.00 88.23 C ANISOU 1000 C THR A 149 7726 13728 12068 -1506 -47 -958 C ATOM 1001 O THR A 149 5.171 -13.636 15.378 1.00 88.09 O ANISOU 1001 O THR A 149 7709 13778 11985 -1516 -38 -986 O ATOM 1002 CB THR A 149 4.901 -16.085 17.241 1.00 88.98 C ANISOU 1002 CB THR A 149 7810 13701 12298 -1517 -129 -1021 C ATOM 1003 OG1 THR A 149 4.550 -16.421 18.582 1.00 87.19 O ANISOU 1003 OG1 THR A 149 7573 13391 12165 -1504 -149 -1047 O ATOM 1004 CG2 THR A 149 5.076 -17.282 16.324 1.00 88.29 C ANISOU 1004 CG2 THR A 149 7731 13645 12171 -1539 -156 -1087 C ATOM 1005 N VAL A 150 4.984 -12.860 17.512 1.00 85.60 N ANISOU 1005 N VAL A 150 7410 13382 11732 -1499 -35 -875 N ATOM 1006 CA VAL A 150 4.298 -11.603 17.210 1.00 85.93 C ANISOU 1006 CA VAL A 150 7471 13483 11695 -1501 -6 -809 C ATOM 1007 C VAL A 150 5.321 -10.551 16.702 1.00 91.78 C ANISOU 1007 C VAL A 150 8212 14258 12403 -1497 34 -819 C ATOM 1008 O VAL A 150 4.901 -9.644 15.990 1.00 91.54 O ANISOU 1008 O VAL A 150 8193 14283 12305 -1500 62 -779 O ATOM 1009 CB VAL A 150 3.476 -11.103 18.431 1.00 89.38 C ANISOU 1009 CB VAL A 150 7941 13887 12133 -1487 -12 -713 C ATOM 1010 CG1 VAL A 150 4.360 -10.542 19.547 1.00 88.89 C ANISOU 1010 CG1 VAL A 150 7911 13771 12093 -1471 -4 -685 C ATOM 1011 CG2 VAL A 150 2.395 -10.099 18.031 1.00 89.09 C ANISOU 1011 CG2 VAL A 150 7920 13916 12015 -1485 12 -645 C ATOM 1012 N PHE A 151 6.636 -10.661 17.032 1.00 89.73 N ANISOU 1012 N PHE A 151 7932 13968 12194 -1490 36 -866 N ATOM 1013 CA PHE A 151 7.648 -9.734 16.515 1.00 90.41 C ANISOU 1013 CA PHE A 151 8001 14088 12263 -1488 69 -866 C ATOM 1014 C PHE A 151 8.088 -10.156 15.084 1.00 96.39 C ANISOU 1014 C PHE A 151 8732 14931 12960 -1480 102 -916 C ATOM 1015 O PHE A 151 8.983 -9.527 14.511 1.00 96.39 O ANISOU 1015 O PHE A 151 8714 14983 12925 -1478 136 -896 O ATOM 1016 CB PHE A 151 8.860 -9.603 17.449 1.00 92.36 C ANISOU 1016 CB PHE A 151 8225 14281 12586 -1479 62 -887 C ATOM 1017 N ARG A 152 7.439 -11.181 14.499 1.00 94.11 N ANISOU 1017 N ARG A 152 8443 14655 12660 -1477 86 -976 N ATOM 1018 CA ARG A 152 7.610 -11.650 13.122 1.00 95.00 C ANISOU 1018 CA ARG A 152 8545 14844 12706 -1467 107 -1034 C ATOM 1019 C ARG A 152 6.198 -11.999 12.618 1.00100.31 C ANISOU 1019 C ARG A 152 9237 15522 13353 -1487 67 -1059 C ATOM 1020 O ARG A 152 5.238 -11.309 12.976 1.00 99.34 O ANISOU 1020 O ARG A 152 9126 15389 13229 -1509 45 -994 O ATOM 1021 CB ARG A 152 8.608 -12.832 13.058 1.00 95.80 C ANISOU 1021 CB ARG A 152 8626 14940 12832 -1430 128 -1109 C ATOM 1022 N MET A 153 6.055 -13.080 11.865 1.00 98.63 N ANISOU 1022 N MET A 153 9032 15325 13118 -1478 54 -1147 N ATOM 1023 CA MET A 153 4.758 -13.602 11.453 1.00 99.26 C ANISOU 1023 CA MET A 153 9132 15407 13177 -1507 1 -1175 C ATOM 1024 C MET A 153 4.568 -14.962 12.151 1.00104.65 C ANISOU 1024 C MET A 153 9828 15988 13948 -1514 -53 -1221 C ATOM 1025 O MET A 153 3.579 -15.160 12.858 1.00103.86 O ANISOU 1025 O MET A 153 9726 15845 13893 -1545 -97 -1170 O ATOM 1026 CB MET A 153 4.653 -13.694 9.927 1.00102.42 C ANISOU 1026 CB MET A 153 9545 15884 13484 -1497 10 -1244 C ATOM 1027 N GLN A 154 5.510 -15.900 11.923 1.00102.84 N ANISOU 1027 N GLN A 154 9610 15721 13744 -1479 -44 -1309 N ATOM 1028 CA GLN A 154 5.579 -17.248 12.517 1.00103.37 C ANISOU 1028 CA GLN A 154 9692 15686 13897 -1477 -89 -1361 C ATOM 1029 C GLN A 154 7.015 -17.581 12.913 1.00107.89 C ANISOU 1029 C GLN A 154 10255 16224 14515 -1422 -43 -1401 C ATOM 1030 O GLN A 154 7.951 -17.072 12.290 1.00107.67 O ANISOU 1030 O GLN A 154 10223 16255 14432 -1380 11 -1434 O ATOM 1031 CB GLN A 154 5.045 -18.341 11.576 1.00105.74 C ANISOU 1031 CB GLN A 154 10037 15968 14171 -1496 -147 -1447 C ATOM 1032 CG GLN A 154 3.532 -18.472 11.571 1.00121.98 C ANISOU 1032 CG GLN A 154 12095 18028 16222 -1563 -217 -1396 C ATOM 1033 CD GLN A 154 2.845 -17.483 10.663 1.00141.86 C ANISOU 1033 CD GLN A 154 14612 20656 18633 -1583 -207 -1368 C ATOM 1034 OE1 GLN A 154 3.209 -17.304 9.495 1.00138.13 O ANISOU 1034 OE1 GLN A 154 14162 20245 18076 -1558 -181 -1432 O ATOM 1035 NE2 GLN A 154 1.775 -16.881 11.157 1.00133.22 N ANISOU 1035 NE2 GLN A 154 13490 19591 17537 -1624 -227 -1266 N ATOM 1036 N LEU A 155 7.201 -18.440 13.930 1.00104.84 N ANISOU 1036 N LEU A 155 9857 15747 14229 -1420 -63 -1390 N ATOM 1037 CA LEU A 155 8.534 -18.861 14.377 1.00105.08 C ANISOU 1037 CA LEU A 155 9871 15741 14316 -1370 -24 -1413 C ATOM 1038 C LEU A 155 8.624 -20.381 14.372 1.00110.28 C ANISOU 1038 C LEU A 155 10557 16304 15041 -1354 -60 -1489 C ATOM 1039 O LEU A 155 8.280 -21.029 15.366 1.00109.31 O ANISOU 1039 O LEU A 155 10426 16103 15005 -1376 -102 -1461 O ATOM 1040 CB LEU A 155 8.869 -18.300 15.770 1.00104.28 C ANISOU 1040 CB LEU A 155 9728 15620 14273 -1379 -11 -1322 C ATOM 1041 N HIS A 156 9.073 -20.958 13.243 1.00108.69 N ANISOU 1041 N HIS A 156 10394 16108 14795 -1309 -43 -1585 N ATOM 1042 CA HIS A 156 9.229 -22.401 13.105 1.00109.75 C ANISOU 1042 CA HIS A 156 10573 16147 14979 -1284 -74 -1671 C ATOM 1043 C HIS A 156 10.282 -22.776 12.050 1.00114.62 C ANISOU 1043 C HIS A 156 11218 16783 15551 -1197 -10 -1749 C ATOM 1044 O HIS A 156 10.187 -22.405 10.879 1.00114.70 O ANISOU 1044 O HIS A 156 11258 16867 15456 -1173 15 -1793 O ATOM 1045 CB HIS A 156 7.891 -23.087 12.762 1.00111.19 C ANISOU 1045 CB HIS A 156 10812 16291 15144 -1340 -160 -1718 C ATOM 1046 CG HIS A 156 7.970 -24.582 12.676 1.00115.76 C ANISOU 1046 CG HIS A 156 11456 16766 15763 -1318 -200 -1816 C ATOM 1047 ND1 HIS A 156 8.027 -25.230 11.457 1.00118.76 N ANISOU 1047 ND1 HIS A 156 11915 17150 16060 -1283 -204 -1925 N ATOM 1048 CD2 HIS A 156 8.022 -25.507 13.664 1.00117.70 C ANISOU 1048 CD2 HIS A 156 11701 16898 16120 -1321 -236 -1820 C ATOM 1049 CE1 HIS A 156 8.093 -26.521 11.737 1.00119.01 C ANISOU 1049 CE1 HIS A 156 12001 17064 16155 -1268 -246 -1995 C ATOM 1050 NE2 HIS A 156 8.092 -26.737 13.053 1.00118.74 N ANISOU 1050 NE2 HIS A 156 11917 16957 16242 -1291 -265 -1932 N ATOM 1051 N THR A 157 11.309 -23.472 12.529 1.00111.40 N ANISOU 1051 N THR A 157 10797 16312 15218 -1144 19 -1761 N ATOM 1052 CA THR A 157 12.418 -24.205 11.902 1.00112.10 C ANISOU 1052 CA THR A 157 10907 16406 15280 -1044 87 -1823 C ATOM 1053 C THR A 157 12.571 -25.460 12.783 1.00115.80 C ANISOU 1053 C THR A 157 11401 16751 15845 -1010 70 -1869 C ATOM 1054 O THR A 157 12.022 -25.471 13.897 1.00114.84 O ANISOU 1054 O THR A 157 11270 16550 15813 -1068 8 -1841 O ATOM 1055 CB THR A 157 13.723 -23.370 11.768 1.00120.78 C ANISOU 1055 CB THR A 157 11927 17598 16365 -1000 175 -1745 C ATOM 1056 OG1 THR A 157 14.142 -22.931 13.059 1.00119.47 O ANISOU 1056 OG1 THR A 157 11690 17422 16281 -1052 161 -1643 O ATOM 1057 CG2 THR A 157 13.603 -22.193 10.809 1.00119.58 C ANISOU 1057 CG2 THR A 157 11769 17570 16095 -993 213 -1734 C ATOM 1058 N ARG A 158 13.319 -26.485 12.338 1.00112.92 N ANISOU 1058 N ARG A 158 11071 16373 15461 -909 130 -1932 N ATOM 1059 CA ARG A 158 13.514 -27.718 13.118 1.00113.09 C ANISOU 1059 CA ARG A 158 11122 16279 15569 -859 129 -1975 C ATOM 1060 C ARG A 158 14.365 -27.480 14.382 1.00115.05 C ANISOU 1060 C ARG A 158 11271 16513 15929 -866 152 -1871 C ATOM 1061 O ARG A 158 14.206 -28.196 15.380 1.00114.51 O ANISOU 1061 O ARG A 158 11203 16343 15962 -886 109 -1868 O ATOM 1062 CB ARG A 158 14.173 -28.802 12.250 1.00114.88 C ANISOU 1062 CB ARG A 158 11408 16509 15731 -733 203 -2056 C ATOM 1063 N MET A 159 15.263 -26.461 14.335 1.00109.98 N ANISOU 1063 N MET A 159 10545 15976 15268 -856 213 -1781 N ATOM 1064 CA MET A 159 16.153 -26.129 15.451 1.00108.40 C ANISOU 1064 CA MET A 159 10250 15780 15156 -870 231 -1674 C ATOM 1065 C MET A 159 15.338 -25.721 16.694 1.00108.44 C ANISOU 1065 C MET A 159 10231 15756 15215 -975 154 -1613 C ATOM 1066 O MET A 159 15.742 -26.099 17.782 1.00107.49 O ANISOU 1066 O MET A 159 10058 15600 15184 -991 145 -1546 O ATOM 1067 CB MET A 159 17.201 -25.058 15.084 1.00110.78 C ANISOU 1067 CB MET A 159 10477 16201 15413 -838 306 -1594 C ATOM 1068 CG MET A 159 16.696 -23.632 14.905 1.00114.00 C ANISOU 1068 CG MET A 159 10876 16704 15734 -896 296 -1562 C ATOM 1069 SD MET A 159 18.022 -22.455 14.514 1.00118.50 S ANISOU 1069 SD MET A 159 11363 17412 16251 -856 381 -1471 S ATOM 1070 CE MET A 159 18.513 -23.019 12.857 1.00116.70 C ANISOU 1070 CE MET A 159 11190 17224 15927 -733 457 -1565 C ATOM 1071 N SER A 160 14.179 -25.033 16.534 1.00102.46 N ANISOU 1071 N SER A 160 9511 15017 14400 -1040 103 -1631 N ATOM 1072 CA SER A 160 13.300 -24.633 17.645 1.00100.20 C ANISOU 1072 CA SER A 160 9209 14710 14150 -1127 36 -1570 C ATOM 1073 C SER A 160 12.638 -25.845 18.310 1.00101.57 C ANISOU 1073 C SER A 160 9403 14767 14422 -1146 -24 -1590 C ATOM 1074 O SER A 160 12.437 -25.813 19.523 1.00100.58 O ANISOU 1074 O SER A 160 9238 14612 14366 -1185 -54 -1515 O ATOM 1075 CB SER A 160 12.227 -23.659 17.171 1.00103.28 C ANISOU 1075 CB SER A 160 9633 15159 14451 -1179 6 -1579 C ATOM 1076 OG SER A 160 12.801 -22.407 16.836 1.00110.82 O ANISOU 1076 OG SER A 160 10555 16221 15331 -1175 55 -1534 O ATOM 1077 N ASN A 161 12.310 -26.902 17.521 1.00 96.64 N ANISOU 1077 N ASN A 161 8844 14073 13801 -1116 -43 -1687 N ATOM 1078 CA ASN A 161 11.729 -28.157 18.013 1.00 95.49 C ANISOU 1078 CA ASN A 161 8726 13805 13751 -1133 -104 -1713 C ATOM 1079 C ASN A 161 12.710 -28.851 18.980 1.00 96.22 C ANISOU 1079 C ASN A 161 8769 13843 13948 -1087 -71 -1675 C ATOM 1080 O ASN A 161 12.282 -29.392 20.004 1.00 95.68 O ANISOU 1080 O ASN A 161 8682 13697 13974 -1119 -119 -1639 O ATOM 1081 CB ASN A 161 11.367 -29.088 16.843 1.00 97.29 C ANISOU 1081 CB ASN A 161 9051 13969 13945 -1111 -134 -1834 C ATOM 1082 CG ASN A 161 10.204 -28.637 15.994 1.00121.12 C ANISOU 1082 CG ASN A 161 12120 17007 16893 -1181 -204 -1865 C ATOM 1083 OD1 ASN A 161 10.342 -27.947 14.975 1.00115.75 O ANISOU 1083 OD1 ASN A 161 11420 16430 16131 -1209 -190 -1832 O ATOM 1084 ND2 ASN A 161 9.060 -29.208 16.279 1.00113.56 N ANISOU 1084 ND2 ASN A 161 11230 15950 15967 -1212 -283 -1929 N ATOM 1085 N ARG A 162 14.028 -28.800 18.661 1.00 90.36 N ANISOU 1085 N ARG A 162 7998 13147 13188 -1012 12 -1671 N ATOM 1086 CA ARG A 162 15.115 -29.346 19.482 1.00 88.84 C ANISOU 1086 CA ARG A 162 7749 12920 13087 -964 50 -1623 C ATOM 1087 C ARG A 162 15.343 -28.457 20.695 1.00 88.31 C ANISOU 1087 C ARG A 162 7599 12894 13059 -1016 40 -1505 C ATOM 1088 O ARG A 162 15.708 -28.967 21.752 1.00 87.66 O ANISOU 1088 O ARG A 162 7476 12759 13072 -1014 29 -1456 O ATOM 1089 CB ARG A 162 16.412 -29.499 18.677 1.00 89.76 C ANISOU 1089 CB ARG A 162 7856 13085 13165 -865 143 -1643 C ATOM 1090 N ARG A 163 15.127 -27.128 20.539 1.00 81.70 N ANISOU 1090 N ARG A 163 6746 12149 12146 -1059 41 -1462 N ATOM 1091 CA ARG A 163 15.246 -26.130 21.604 1.00 79.35 C ANISOU 1091 CA ARG A 163 6393 11890 11866 -1108 26 -1358 C ATOM 1092 C ARG A 163 14.107 -26.278 22.613 1.00 79.58 C ANISOU 1092 C ARG A 163 6433 11863 11941 -1168 -46 -1326 C ATOM 1093 O ARG A 163 14.327 -26.019 23.794 1.00 78.74 O ANISOU 1093 O ARG A 163 6288 11753 11878 -1190 -62 -1246 O ATOM 1094 CB ARG A 163 15.257 -24.697 21.039 1.00 79.55 C ANISOU 1094 CB ARG A 163 6411 12019 11794 -1134 47 -1326 C ATOM 1095 CG ARG A 163 16.566 -24.252 20.375 1.00 91.85 C ANISOU 1095 CG ARG A 163 7932 13651 13317 -1081 119 -1314 C ATOM 1096 CD ARG A 163 16.430 -22.828 19.834 1.00103.41 C ANISOU 1096 CD ARG A 163 9385 15211 14697 -1117 130 -1269 C ATOM 1097 NE ARG A 163 17.627 -22.330 19.148 1.00113.77 N ANISOU 1097 NE ARG A 163 10691 16597 15938 -1065 194 -1298 N ATOM 1098 CZ ARG A 163 17.696 -21.157 18.523 1.00128.88 C ANISOU 1098 CZ ARG A 163 12592 18602 17776 -1084 214 -1263 C ATOM 1099 NH1 ARG A 163 16.637 -20.354 18.477 1.00114.70 N ANISOU 1099 NH1 ARG A 163 10794 16824 15963 -1155 175 -1202 N ATOM 1100 NH2 ARG A 163 18.822 -20.778 17.928 1.00118.52 N1+ ANISOU 1100 NH2 ARG A 163 11270 17361 16402 -1026 277 -1284 N1+ ATOM 1101 N VAL A 164 12.899 -26.694 22.151 1.00 73.73 N ANISOU 1101 N VAL A 164 5745 11083 11188 -1193 -90 -1382 N ATOM 1102 CA VAL A 164 11.697 -26.896 22.970 1.00 71.99 C ANISOU 1102 CA VAL A 164 5528 10812 11013 -1246 -158 -1343 C ATOM 1103 C VAL A 164 11.967 -28.009 23.996 1.00 73.40 C ANISOU 1103 C VAL A 164 5679 10900 11312 -1226 -175 -1323 C ATOM 1104 O VAL A 164 11.590 -27.857 25.160 1.00 72.46 O ANISOU 1104 O VAL A 164 5526 10763 11242 -1251 -204 -1243 O ATOM 1105 CB VAL A 164 10.453 -27.181 22.082 1.00 76.38 C ANISOU 1105 CB VAL A 164 6140 11353 11526 -1282 -206 -1404 C ATOM 1106 CG1 VAL A 164 9.374 -27.967 22.816 1.00 76.24 C ANISOU 1106 CG1 VAL A 164 6123 11252 11591 -1322 -280 -1378 C ATOM 1107 CG2 VAL A 164 9.879 -25.879 21.548 1.00 75.71 C ANISOU 1107 CG2 VAL A 164 6065 11364 11338 -1318 -204 -1379 C ATOM 1108 N VAL A 165 12.663 -29.085 23.573 1.00 68.94 N ANISOU 1108 N VAL A 165 5127 10279 10786 -1173 -149 -1389 N ATOM 1109 CA VAL A 165 13.052 -30.224 24.419 1.00 68.32 C ANISOU 1109 CA VAL A 165 5023 10111 10823 -1144 -154 -1376 C ATOM 1110 C VAL A 165 13.894 -29.700 25.597 1.00 68.38 C ANISOU 1110 C VAL A 165 4958 10154 10870 -1134 -128 -1277 C ATOM 1111 O VAL A 165 13.656 -30.103 26.737 1.00 68.20 O ANISOU 1111 O VAL A 165 4902 10081 10929 -1146 -160 -1218 O ATOM 1112 CB VAL A 165 13.801 -31.330 23.615 1.00 73.78 C ANISOU 1112 CB VAL A 165 5753 10748 11531 -1073 -116 -1467 C ATOM 1113 CG1 VAL A 165 14.169 -32.527 24.494 1.00 73.99 C ANISOU 1113 CG1 VAL A 165 5752 10682 11680 -1037 -115 -1447 C ATOM 1114 CG2 VAL A 165 12.974 -31.793 22.419 1.00 74.50 C ANISOU 1114 CG2 VAL A 165 5933 10795 11576 -1086 -155 -1570 C ATOM 1115 N VAL A 166 14.825 -28.762 25.316 1.00 61.45 N ANISOU 1115 N VAL A 166 4054 9362 9932 -1117 -78 -1253 N ATOM 1116 CA VAL A 166 15.700 -28.108 26.296 1.00 59.33 C ANISOU 1116 CA VAL A 166 3723 9132 9687 -1119 -63 -1160 C ATOM 1117 C VAL A 166 14.844 -27.226 27.231 1.00 59.53 C ANISOU 1117 C VAL A 166 3749 9170 9698 -1177 -115 -1089 C ATOM 1118 O VAL A 166 15.067 -27.248 28.440 1.00 59.23 O ANISOU 1118 O VAL A 166 3677 9105 9722 -1180 -135 -1022 O ATOM 1119 CB VAL A 166 16.835 -27.298 25.608 1.00 63.10 C ANISOU 1119 CB VAL A 166 4176 9698 10099 -1098 -7 -1148 C ATOM 1120 CG1 VAL A 166 17.724 -26.598 26.631 1.00 62.28 C ANISOU 1120 CG1 VAL A 166 4014 9633 10017 -1115 -9 -1047 C ATOM 1121 CG2 VAL A 166 17.673 -28.196 24.700 1.00 63.93 C ANISOU 1121 CG2 VAL A 166 4279 9795 10216 -1023 53 -1206 C ATOM 1122 N VAL A 167 13.857 -26.488 26.677 1.00 53.14 N ANISOU 1122 N VAL A 167 2980 8403 8806 -1215 -132 -1101 N ATOM 1123 CA VAL A 167 12.947 -25.612 27.427 1.00 51.25 C ANISOU 1123 CA VAL A 167 2752 8183 8538 -1257 -171 -1034 C ATOM 1124 C VAL A 167 12.096 -26.472 28.397 1.00 53.59 C ANISOU 1124 C VAL A 167 3037 8407 8919 -1262 -215 -998 C ATOM 1125 O VAL A 167 11.973 -26.101 29.562 1.00 52.88 O ANISOU 1125 O VAL A 167 2926 8315 8850 -1264 -231 -920 O ATOM 1126 CB VAL A 167 12.071 -24.738 26.486 1.00 54.86 C ANISOU 1126 CB VAL A 167 3254 8693 8897 -1289 -177 -1060 C ATOM 1127 CG1 VAL A 167 11.015 -23.960 27.262 1.00 54.09 C ANISOU 1127 CG1 VAL A 167 3171 8598 8781 -1321 -217 -993 C ATOM 1128 CG2 VAL A 167 12.927 -23.772 25.674 1.00 54.49 C ANISOU 1128 CG2 VAL A 167 3209 8726 8767 -1289 -136 -1061 C ATOM 1129 N ILE A 168 11.567 -27.630 27.933 1.00 49.32 N ANISOU 1129 N ILE A 168 2510 7804 8426 -1262 -238 -1053 N ATOM 1130 CA ILE A 168 10.771 -28.583 28.731 1.00 48.38 C ANISOU 1130 CA ILE A 168 2374 7609 8398 -1272 -285 -1018 C ATOM 1131 C ILE A 168 11.608 -29.060 29.935 1.00 51.00 C ANISOU 1131 C ILE A 168 2657 7908 8815 -1239 -274 -961 C ATOM 1132 O ILE A 168 11.075 -29.104 31.043 1.00 50.35 O ANISOU 1132 O ILE A 168 2548 7808 8773 -1245 -303 -881 O ATOM 1133 CB ILE A 168 10.270 -29.770 27.847 1.00 52.04 C ANISOU 1133 CB ILE A 168 2869 8000 8904 -1278 -313 -1100 C ATOM 1134 CG1 ILE A 168 9.131 -29.308 26.898 1.00 52.13 C ANISOU 1134 CG1 ILE A 168 2924 8042 8841 -1326 -348 -1127 C ATOM 1135 CG2 ILE A 168 9.806 -30.968 28.702 1.00 52.99 C ANISOU 1135 CG2 ILE A 168 2962 8023 9147 -1278 -355 -1067 C ATOM 1136 CD1 ILE A 168 8.741 -30.282 25.776 1.00 59.24 C ANISOU 1136 CD1 ILE A 168 3878 8882 9750 -1338 -380 -1229 C ATOM 1137 N VAL A 169 12.917 -29.352 29.724 1.00 46.92 N ANISOU 1137 N VAL A 169 2121 7388 8318 -1201 -230 -995 N ATOM 1138 CA VAL A 169 13.864 -29.772 30.769 1.00 46.31 C ANISOU 1138 CA VAL A 169 1991 7287 8319 -1168 -216 -942 C ATOM 1139 C VAL A 169 13.979 -28.647 31.822 1.00 48.75 C ANISOU 1139 C VAL A 169 2280 7654 8590 -1182 -223 -851 C ATOM 1140 O VAL A 169 13.828 -28.940 33.002 1.00 48.10 O ANISOU 1140 O VAL A 169 2165 7544 8566 -1174 -244 -782 O ATOM 1141 CB VAL A 169 15.250 -30.173 30.180 1.00 50.61 C ANISOU 1141 CB VAL A 169 2518 7831 8880 -1120 -160 -991 C ATOM 1142 CG1 VAL A 169 16.317 -30.331 31.264 1.00 50.34 C ANISOU 1142 CG1 VAL A 169 2420 7806 8901 -1093 -141 -918 C ATOM 1143 CG2 VAL A 169 15.144 -31.449 29.362 1.00 51.28 C ANISOU 1143 CG2 VAL A 169 2631 7831 9021 -1091 -157 -1073 C ATOM 1144 N VAL A 170 14.175 -27.377 31.391 1.00 44.37 N ANISOU 1144 N VAL A 170 1750 7172 7934 -1203 -211 -851 N ATOM 1145 CA VAL A 170 14.289 -26.186 32.256 1.00 43.37 C ANISOU 1145 CA VAL A 170 1629 7096 7756 -1220 -224 -776 C ATOM 1146 C VAL A 170 13.022 -26.029 33.130 1.00 46.53 C ANISOU 1146 C VAL A 170 2047 7478 8156 -1228 -263 -713 C ATOM 1147 O VAL A 170 13.153 -25.795 34.331 1.00 45.61 O ANISOU 1147 O VAL A 170 1915 7356 8057 -1217 -280 -642 O ATOM 1148 CB VAL A 170 14.567 -24.898 31.424 1.00 47.02 C ANISOU 1148 CB VAL A 170 2126 7628 8110 -1245 -207 -797 C ATOM 1149 CG1 VAL A 170 14.466 -23.624 32.275 1.00 46.13 C ANISOU 1149 CG1 VAL A 170 2040 7551 7935 -1266 -230 -725 C ATOM 1150 CG2 VAL A 170 15.928 -24.974 30.736 1.00 47.49 C ANISOU 1150 CG2 VAL A 170 2157 7716 8170 -1229 -164 -837 C ATOM 1151 N ILE A 171 11.824 -26.192 32.530 1.00 43.39 N ANISOU 1151 N ILE A 171 1677 7074 7737 -1244 -278 -733 N ATOM 1152 CA ILE A 171 10.517 -26.088 33.195 1.00 43.14 C ANISOU 1152 CA ILE A 171 1655 7034 7702 -1247 -310 -666 C ATOM 1153 C ILE A 171 10.396 -27.161 34.303 1.00 47.36 C ANISOU 1153 C ILE A 171 2142 7513 8340 -1222 -329 -607 C ATOM 1154 O ILE A 171 10.042 -26.828 35.428 1.00 46.25 O ANISOU 1154 O ILE A 171 2002 7385 8188 -1204 -341 -523 O ATOM 1155 CB ILE A 171 9.346 -26.189 32.161 1.00 46.45 C ANISOU 1155 CB ILE A 171 2095 7451 8105 -1274 -326 -700 C ATOM 1156 CG1 ILE A 171 9.345 -24.970 31.204 1.00 46.90 C ANISOU 1156 CG1 ILE A 171 2196 7570 8054 -1297 -305 -750 C ATOM 1157 CG2 ILE A 171 7.987 -26.314 32.860 1.00 46.69 C ANISOU 1157 CG2 ILE A 171 2119 7478 8145 -1274 -356 -611 C ATOM 1158 CD1 ILE A 171 8.547 -25.145 29.911 1.00 54.65 C ANISOU 1158 CD1 ILE A 171 3195 8547 9024 -1325 -318 -813 C ATOM 1159 N TRP A 172 10.686 -28.432 33.983 1.00 45.15 N ANISOU 1159 N TRP A 172 1826 7170 8157 -1216 -330 -650 N ATOM 1160 CA TRP A 172 10.603 -29.537 34.940 1.00 45.71 C ANISOU 1160 CA TRP A 172 1847 7182 8337 -1193 -347 -596 C ATOM 1161 C TRP A 172 11.719 -29.468 35.987 1.00 51.10 C ANISOU 1161 C TRP A 172 2499 7878 9038 -1163 -332 -550 C ATOM 1162 O TRP A 172 11.454 -29.821 37.129 1.00 50.83 O ANISOU 1162 O TRP A 172 2438 7833 9043 -1142 -348 -468 O ATOM 1163 CB TRP A 172 10.622 -30.904 34.242 1.00 45.28 C ANISOU 1163 CB TRP A 172 1777 7050 8379 -1194 -354 -661 C ATOM 1164 CG TRP A 172 9.318 -31.259 33.596 1.00 46.66 C ANISOU 1164 CG TRP A 172 1972 7194 8563 -1229 -393 -681 C ATOM 1165 CD1 TRP A 172 9.034 -31.250 32.264 1.00 50.08 C ANISOU 1165 CD1 TRP A 172 2449 7617 8961 -1255 -397 -774 C ATOM 1166 CD2 TRP A 172 8.098 -31.611 34.264 1.00 46.58 C ANISOU 1166 CD2 TRP A 172 1938 7166 8593 -1245 -436 -595 C ATOM 1167 NE1 TRP A 172 7.718 -31.597 32.056 1.00 49.84 N ANISOU 1167 NE1 TRP A 172 2426 7560 8951 -1295 -449 -755 N ATOM 1168 CE2 TRP A 172 7.117 -31.818 33.268 1.00 50.97 C ANISOU 1168 CE2 TRP A 172 2522 7699 9144 -1290 -473 -640 C ATOM 1169 CE3 TRP A 172 7.738 -31.770 35.612 1.00 47.52 C ANISOU 1169 CE3 TRP A 172 2014 7291 8752 -1223 -449 -477 C ATOM 1170 CZ2 TRP A 172 5.801 -32.191 33.576 1.00 50.43 C ANISOU 1170 CZ2 TRP A 172 2431 7615 9117 -1320 -524 -563 C ATOM 1171 CZ3 TRP A 172 6.436 -32.131 35.916 1.00 49.13 C ANISOU 1171 CZ3 TRP A 172 2194 7481 8992 -1242 -491 -400 C ATOM 1172 CH2 TRP A 172 5.482 -32.335 34.907 1.00 50.21 C ANISOU 1172 CH2 TRP A 172 2351 7596 9132 -1294 -530 -439 C ATOM 1173 N THR A 173 12.944 -29.023 35.617 1.00 48.66 N ANISOU 1173 N THR A 173 2193 7597 8699 -1161 -302 -595 N ATOM 1174 CA THR A 173 14.076 -28.894 36.542 1.00 48.81 C ANISOU 1174 CA THR A 173 2179 7636 8731 -1144 -292 -551 C ATOM 1175 C THR A 173 13.736 -27.843 37.588 1.00 52.96 C ANISOU 1175 C THR A 173 2732 8202 9189 -1146 -318 -471 C ATOM 1176 O THR A 173 13.937 -28.101 38.772 1.00 52.75 O ANISOU 1176 O THR A 173 2674 8162 9205 -1123 -332 -403 O ATOM 1177 CB THR A 173 15.384 -28.563 35.793 1.00 57.96 C ANISOU 1177 CB THR A 173 3338 8832 9854 -1150 -258 -604 C ATOM 1178 OG1 THR A 173 15.616 -29.564 34.806 1.00 58.16 O ANISOU 1178 OG1 THR A 173 3351 8816 9930 -1133 -230 -679 O ATOM 1179 CG2 THR A 173 16.602 -28.490 36.712 1.00 57.67 C ANISOU 1179 CG2 THR A 173 3257 8818 9836 -1140 -254 -549 C ATOM 1180 N MET A 174 13.170 -26.692 37.160 1.00 49.71 N ANISOU 1180 N MET A 174 2382 7836 8670 -1169 -323 -478 N ATOM 1181 CA MET A 174 12.804 -25.612 38.069 1.00 49.55 C ANISOU 1181 CA MET A 174 2410 7847 8571 -1164 -346 -410 C ATOM 1182 C MET A 174 11.647 -26.061 38.993 1.00 51.33 C ANISOU 1182 C MET A 174 2634 8052 8818 -1131 -362 -341 C ATOM 1183 O MET A 174 11.682 -25.750 40.173 1.00 50.46 O ANISOU 1183 O MET A 174 2549 7954 8670 -1105 -378 -271 O ATOM 1184 CB MET A 174 12.513 -24.286 37.342 1.00 52.22 C ANISOU 1184 CB MET A 174 2820 8231 8791 -1191 -343 -435 C ATOM 1185 CG MET A 174 11.314 -24.205 36.452 1.00 56.83 C ANISOU 1185 CG MET A 174 3424 8822 9348 -1203 -330 -477 C ATOM 1186 SD MET A 174 11.570 -22.838 35.283 1.00 61.82 S ANISOU 1186 SD MET A 174 4116 9509 9864 -1239 -315 -526 S ATOM 1187 CE MET A 174 11.268 -21.389 36.365 1.00 58.20 C ANISOU 1187 CE MET A 174 3743 9071 9300 -1223 -336 -449 C ATOM 1188 N ALA A 175 10.724 -26.889 38.495 1.00 46.99 N ANISOU 1188 N ALA A 175 2053 7469 8331 -1132 -360 -356 N ATOM 1189 CA ALA A 175 9.611 -27.458 39.260 1.00 46.32 C ANISOU 1189 CA ALA A 175 1946 7365 8288 -1105 -376 -278 C ATOM 1190 C ALA A 175 10.112 -28.392 40.371 1.00 49.52 C ANISOU 1190 C ALA A 175 2292 7736 8787 -1074 -383 -223 C ATOM 1191 O ALA A 175 9.626 -28.295 41.495 1.00 49.42 O ANISOU 1191 O ALA A 175 2272 7731 8775 -1036 -394 -132 O ATOM 1192 CB ALA A 175 8.675 -28.216 38.331 1.00 47.22 C ANISOU 1192 CB ALA A 175 2040 7450 8452 -1130 -384 -308 C ATOM 1193 N ILE A 176 11.098 -29.267 40.063 1.00 45.40 N ANISOU 1193 N ILE A 176 1728 7183 8340 -1082 -373 -273 N ATOM 1194 CA ILE A 176 11.697 -30.232 41.001 1.00 45.12 C ANISOU 1194 CA ILE A 176 1628 7114 8400 -1053 -375 -226 C ATOM 1195 C ILE A 176 12.450 -29.457 42.101 1.00 47.43 C ANISOU 1195 C ILE A 176 1938 7450 8633 -1030 -386 -160 C ATOM 1196 O ILE A 176 12.278 -29.768 43.279 1.00 46.76 O ANISOU 1196 O ILE A 176 1836 7365 8568 -993 -399 -75 O ATOM 1197 CB ILE A 176 12.611 -31.269 40.261 1.00 48.79 C ANISOU 1197 CB ILE A 176 2052 7541 8946 -1060 -353 -296 C ATOM 1198 CG1 ILE A 176 11.759 -32.188 39.354 1.00 50.11 C ANISOU 1198 CG1 ILE A 176 2214 7649 9178 -1075 -353 -361 C ATOM 1199 CG2 ILE A 176 13.447 -32.107 41.245 1.00 49.48 C ANISOU 1199 CG2 ILE A 176 2073 7605 9124 -1027 -351 -239 C ATOM 1200 CD1 ILE A 176 12.543 -32.932 38.232 1.00 60.33 C ANISOU 1200 CD1 ILE A 176 3508 8917 10496 -1080 -322 -459 C ATOM 1201 N VAL A 177 13.248 -28.433 41.714 1.00 43.43 N ANISOU 1201 N VAL A 177 1469 6980 8050 -1054 -384 -196 N ATOM 1202 CA VAL A 177 14.042 -27.585 42.622 1.00 42.66 C ANISOU 1202 CA VAL A 177 1403 6919 7888 -1047 -407 -146 C ATOM 1203 C VAL A 177 13.096 -26.783 43.552 1.00 46.68 C ANISOU 1203 C VAL A 177 1977 7448 8310 -1014 -426 -80 C ATOM 1204 O VAL A 177 13.285 -26.844 44.767 1.00 45.85 O ANISOU 1204 O VAL A 177 1866 7347 8207 -977 -443 -8 O ATOM 1205 CB VAL A 177 15.026 -26.665 41.843 1.00 45.89 C ANISOU 1205 CB VAL A 177 1848 7362 8225 -1092 -410 -196 C ATOM 1206 CG1 VAL A 177 15.656 -25.613 42.745 1.00 45.77 C ANISOU 1206 CG1 VAL A 177 1847 7371 8172 -1097 -446 -143 C ATOM 1207 CG2 VAL A 177 16.116 -27.490 41.163 1.00 46.00 C ANISOU 1207 CG2 VAL A 177 1805 7364 8309 -1112 -377 -263 C ATOM 1208 N MET A 178 12.076 -26.075 42.997 1.00 43.91 N ANISOU 1208 N MET A 178 1687 7113 7882 -1020 -418 -100 N ATOM 1209 CA MET A 178 11.100 -25.282 43.769 1.00 43.84 C ANISOU 1209 CA MET A 178 1748 7127 7782 -977 -425 -35 C ATOM 1210 C MET A 178 10.287 -26.145 44.739 1.00 47.57 C ANISOU 1210 C MET A 178 2169 7587 8319 -920 -422 55 C ATOM 1211 O MET A 178 9.882 -25.652 45.794 1.00 47.18 O ANISOU 1211 O MET A 178 2163 7558 8204 -864 -429 131 O ATOM 1212 CB MET A 178 10.141 -24.512 42.846 1.00 46.06 C ANISOU 1212 CB MET A 178 2082 7426 7992 -992 -408 -69 C ATOM 1213 CG MET A 178 10.790 -23.341 42.132 1.00 49.83 C ANISOU 1213 CG MET A 178 2632 7926 8373 -1033 -413 -130 C ATOM 1214 SD MET A 178 11.300 -21.975 43.208 1.00 54.27 S ANISOU 1214 SD MET A 178 3302 8504 8815 -1010 -447 -85 S ATOM 1215 CE MET A 178 13.080 -22.225 43.257 1.00 51.07 C ANISOU 1215 CE MET A 178 2856 8093 8456 -1069 -474 -126 C ATOM 1216 N GLY A 179 10.072 -27.409 44.372 1.00 43.76 N ANISOU 1216 N GLY A 179 1598 7068 7959 -931 -414 49 N ATOM 1217 CA GLY A 179 9.361 -28.390 45.184 1.00 43.45 C ANISOU 1217 CA GLY A 179 1491 7010 8006 -888 -415 138 C ATOM 1218 C GLY A 179 10.272 -29.148 46.135 1.00 46.99 C ANISOU 1218 C GLY A 179 1873 7434 8547 -874 -422 163 C ATOM 1219 O GLY A 179 9.823 -30.063 46.830 1.00 46.71 O ANISOU 1219 O GLY A 179 1758 7361 8630 -862 -421 203 O ATOM 1220 N ALA A 180 11.565 -28.777 46.165 1.00 43.40 N ANISOU 1220 N ALA A 180 1448 6999 8043 -879 -432 145 N ATOM 1221 CA ALA A 180 12.576 -29.380 47.029 1.00 43.37 C ANISOU 1221 CA ALA A 180 1383 6984 8111 -868 -441 174 C ATOM 1222 C ALA A 180 13.166 -28.360 48.011 1.00 47.95 C ANISOU 1222 C ALA A 180 2025 7604 8588 -858 -468 202 C ATOM 1223 O ALA A 180 13.612 -28.772 49.077 1.00 47.69 O ANISOU 1223 O ALA A 180 1948 7574 8600 -844 -482 244 O ATOM 1224 CB ALA A 180 13.680 -30.000 46.194 1.00 44.19 C ANISOU 1224 CB ALA A 180 1431 7054 8303 -913 -427 96 C ATOM 1225 N ILE A 181 13.132 -27.039 47.680 1.00 45.15 N ANISOU 1225 N ILE A 181 1779 7279 8098 -865 -481 180 N ATOM 1226 CA ILE A 181 13.667 -25.933 48.505 1.00 45.27 C ANISOU 1226 CA ILE A 181 1879 7321 7999 -861 -520 200 C ATOM 1227 C ILE A 181 13.155 -26.068 49.988 1.00 49.71 C ANISOU 1227 C ILE A 181 2435 7895 8556 -789 -533 299 C ATOM 1228 O ILE A 181 13.991 -26.049 50.894 1.00 49.84 O ANISOU 1228 O ILE A 181 2433 7919 8585 -798 -564 321 O ATOM 1229 CB ILE A 181 13.352 -24.530 47.884 1.00 48.03 C ANISOU 1229 CB ILE A 181 2358 7687 8205 -868 -528 167 C ATOM 1230 CG1 ILE A 181 14.152 -24.271 46.556 1.00 48.74 C ANISOU 1230 CG1 ILE A 181 2451 7773 8295 -934 -511 76 C ATOM 1231 CG2 ILE A 181 13.561 -23.388 48.888 1.00 48.13 C ANISOU 1231 CG2 ILE A 181 2475 7714 8098 -864 -579 186 C ATOM 1232 CD1 ILE A 181 15.845 -24.083 46.561 1.00 61.97 C ANISOU 1232 CD1 ILE A 181 4100 9450 9997 -1005 -529 20 C ATOM 1233 N PRO A 182 11.848 -26.278 50.281 1.00 46.58 N ANISOU 1233 N PRO A 182 2039 7506 8155 -718 -510 369 N ATOM 1234 CA PRO A 182 11.444 -26.418 51.691 1.00 46.91 C ANISOU 1234 CA PRO A 182 2065 7565 8195 -645 -519 469 C ATOM 1235 C PRO A 182 11.864 -27.753 52.307 1.00 51.22 C ANISOU 1235 C PRO A 182 2487 8094 8881 -656 -521 495 C ATOM 1236 O PRO A 182 11.965 -27.849 53.528 1.00 50.89 O ANISOU 1236 O PRO A 182 2446 8070 8820 -638 -550 537 O ATOM 1237 CB PRO A 182 9.921 -26.308 51.635 1.00 48.75 C ANISOU 1237 CB PRO A 182 2286 7808 8430 -576 -482 542 C ATOM 1238 CG PRO A 182 9.561 -26.786 50.292 1.00 53.07 C ANISOU 1238 CG PRO A 182 2797 8330 9037 -631 -459 479 C ATOM 1239 CD PRO A 182 10.673 -26.357 49.387 1.00 48.38 C ANISOU 1239 CD PRO A 182 2273 7732 8376 -700 -476 373 C ATOM 1240 N SER A 183 12.148 -28.764 51.465 1.00 48.03 N ANISOU 1240 N SER A 183 1984 7654 8612 -689 -494 466 N ATOM 1241 CA SER A 183 12.588 -30.086 51.907 1.00 48.23 C ANISOU 1241 CA SER A 183 1891 7650 8783 -698 -487 483 C ATOM 1242 C SER A 183 14.128 -30.198 51.933 1.00 52.20 C ANISOU 1242 C SER A 183 2385 8160 9288 -746 -509 441 C ATOM 1243 O SER A 183 14.649 -31.304 52.125 1.00 52.65 O ANISOU 1243 O SER A 183 2357 8211 9438 -737 -508 481 O ATOM 1244 CB SER A 183 11.998 -31.166 51.012 1.00 52.26 C ANISOU 1244 CB SER A 183 2332 8109 9415 -727 -458 440 C ATOM 1245 OG SER A 183 10.753 -31.607 51.519 1.00 64.48 O ANISOU 1245 OG SER A 183 3875 9653 10971 -693 -446 494 O ATOM 1246 N VAL A 184 14.850 -29.060 51.763 1.00 47.77 N ANISOU 1246 N VAL A 184 1906 7616 8628 -795 -529 373 N ATOM 1247 CA VAL A 184 16.324 -29.024 51.798 1.00 47.27 C ANISOU 1247 CA VAL A 184 1836 7569 8557 -846 -557 348 C ATOM 1248 C VAL A 184 16.776 -28.009 52.911 1.00 50.86 C ANISOU 1248 C VAL A 184 2354 8059 8911 -825 -611 412 C ATOM 1249 O VAL A 184 17.829 -27.389 52.806 1.00 50.33 O ANISOU 1249 O VAL A 184 2249 8010 8867 -850 -642 438 O ATOM 1250 CB VAL A 184 16.938 -28.723 50.382 1.00 50.75 C ANISOU 1250 CB VAL A 184 2324 8011 8949 -914 -557 256 C ATOM 1251 CG1 VAL A 184 18.441 -28.457 50.409 1.00 50.91 C ANISOU 1251 CG1 VAL A 184 2346 8057 8940 -968 -598 253 C ATOM 1252 CG2 VAL A 184 16.627 -29.845 49.409 1.00 50.47 C ANISOU 1252 CG2 VAL A 184 2219 7940 9018 -930 -507 194 C ATOM 1253 N GLY A 185 16.057 -27.952 54.022 1.00 47.47 N ANISOU 1253 N GLY A 185 2018 7642 8376 -773 -621 444 N ATOM 1254 CA GLY A 185 16.424 -27.053 55.113 1.00 47.82 C ANISOU 1254 CA GLY A 185 2142 7715 8312 -739 -672 500 C ATOM 1255 C GLY A 185 15.496 -25.885 55.390 1.00 52.16 C ANISOU 1255 C GLY A 185 2849 8274 8696 -703 -693 495 C ATOM 1256 O GLY A 185 15.407 -25.456 56.545 1.00 51.95 O ANISOU 1256 O GLY A 185 2904 8265 8570 -669 -739 538 O ATOM 1257 N TRP A 186 14.806 -25.334 54.355 1.00 49.07 N ANISOU 1257 N TRP A 186 2509 7869 8265 -707 -660 445 N ATOM 1258 CA TRP A 186 13.902 -24.187 54.551 1.00 49.16 C ANISOU 1258 CA TRP A 186 2674 7887 8117 -664 -671 443 C ATOM 1259 C TRP A 186 12.500 -24.656 55.036 1.00 55.55 C ANISOU 1259 C TRP A 186 3477 8710 8921 -562 -617 514 C ATOM 1260 O TRP A 186 11.500 -24.538 54.319 1.00 54.46 O ANISOU 1260 O TRP A 186 3342 8568 8784 -553 -575 498 O ATOM 1261 CB TRP A 186 13.782 -23.315 53.281 1.00 47.04 C ANISOU 1261 CB TRP A 186 2480 7603 7790 -729 -675 355 C ATOM 1262 CG TRP A 186 13.322 -21.902 53.533 1.00 47.67 C ANISOU 1262 CG TRP A 186 2736 7681 7697 -697 -703 348 C ATOM 1263 CD1 TRP A 186 12.844 -21.387 54.703 1.00 50.97 C ANISOU 1263 CD1 TRP A 186 3263 8103 8000 -631 -740 397 C ATOM 1264 CD2 TRP A 186 13.298 -20.826 52.585 1.00 47.09 C ANISOU 1264 CD2 TRP A 186 2759 7593 7541 -729 -700 286 C ATOM 1265 NE1 TRP A 186 12.542 -20.056 54.549 1.00 50.22 N ANISOU 1265 NE1 TRP A 186 3334 7992 7755 -615 -758 367 N ATOM 1266 CE2 TRP A 186 12.809 -19.684 53.257 1.00 51.02 C ANISOU 1266 CE2 TRP A 186 3427 8081 7877 -677 -734 301 C ATOM 1267 CE3 TRP A 186 13.661 -20.708 51.232 1.00 47.88 C ANISOU 1267 CE3 TRP A 186 2822 7686 7684 -795 -672 218 C ATOM 1268 CZ2 TRP A 186 12.653 -18.446 52.619 1.00 50.09 C ANISOU 1268 CZ2 TRP A 186 3441 7944 7649 -690 -740 253 C ATOM 1269 CZ3 TRP A 186 13.500 -19.484 50.599 1.00 49.09 C ANISOU 1269 CZ3 TRP A 186 3096 7829 7727 -807 -676 176 C ATOM 1270 CH2 TRP A 186 13.012 -18.367 51.292 1.00 49.95 C ANISOU 1270 CH2 TRP A 186 3371 7925 7684 -756 -709 194 C ATOM 1271 N ASN A 187 12.445 -25.142 56.292 1.00 55.20 N ANISOU 1271 N ASN A 187 3417 8685 8870 -486 -622 602 N ATOM 1272 CA ASN A 187 11.233 -25.599 56.971 1.00 56.54 C ANISOU 1272 CA ASN A 187 3566 8879 9036 -377 -577 701 C ATOM 1273 C ASN A 187 11.334 -25.335 58.483 1.00 64.46 C ANISOU 1273 C ASN A 187 4625 9912 9956 -297 -605 777 C ATOM 1274 O ASN A 187 12.437 -25.277 59.029 1.00 64.81 O ANISOU 1274 O ASN A 187 4691 9952 9981 -342 -663 752 O ATOM 1275 CB ASN A 187 10.967 -27.085 56.691 1.00 57.83 C ANISOU 1275 CB ASN A 187 3557 9033 9381 -387 -535 738 C ATOM 1276 CG ASN A 187 12.131 -28.035 56.884 1.00 85.81 C ANISOU 1276 CG ASN A 187 6986 12566 13054 -431 -555 741 C ATOM 1277 OD1 ASN A 187 13.301 -27.642 57.016 1.00 84.04 O ANISOU 1277 OD1 ASN A 187 6787 12340 12806 -483 -600 699 O ATOM 1278 ND2 ASN A 187 11.838 -29.328 56.845 1.00 77.60 N ANISOU 1278 ND2 ASN A 187 5812 11513 12159 -416 -523 795 N ATOM 1279 N CYS A 188 10.184 -25.184 59.158 1.00 63.64 N ANISOU 1279 N CYS A 188 4540 9839 9800 -177 -568 875 N ATOM 1280 CA CYS A 188 10.132 -24.887 60.593 1.00 65.48 C ANISOU 1280 CA CYS A 188 4828 10105 9948 -89 -591 952 C ATOM 1281 C CYS A 188 10.179 -26.186 61.463 1.00 72.44 C ANISOU 1281 C CYS A 188 5538 11007 10979 -59 -567 1047 C ATOM 1282 O CYS A 188 9.712 -26.177 62.607 1.00 72.57 O ANISOU 1282 O CYS A 188 5535 11062 10974 54 -532 1160 O ATOM 1283 CB CYS A 188 8.887 -24.055 60.897 1.00 66.33 C ANISOU 1283 CB CYS A 188 5076 10239 9887 40 -562 1008 C ATOM 1284 SG CYS A 188 7.324 -24.978 60.869 1.00 70.20 S ANISOU 1284 SG CYS A 188 5479 10760 10435 128 -467 1109 S ATOM 1285 N ILE A 189 10.791 -27.271 60.926 1.00 70.95 N ANISOU 1285 N ILE A 189 5224 10792 10942 -159 -584 1005 N ATOM 1286 CA ILE A 189 10.906 -28.603 61.531 1.00 72.14 C ANISOU 1286 CA ILE A 189 5209 10948 11251 -148 -565 1081 C ATOM 1287 C ILE A 189 11.650 -28.521 62.868 1.00 78.88 C ANISOU 1287 C ILE A 189 6086 11843 12044 -85 -599 1155 C ATOM 1288 O ILE A 189 11.136 -29.035 63.860 1.00 79.41 O ANISOU 1288 O ILE A 189 6060 11936 12175 -11 -570 1264 O ATOM 1289 CB ILE A 189 11.580 -29.602 60.541 1.00 75.15 C ANISOU 1289 CB ILE A 189 5469 11285 11801 -260 -569 1012 C ATOM 1290 CG1 ILE A 189 11.444 -31.069 60.986 1.00 75.95 C ANISOU 1290 CG1 ILE A 189 5400 11377 12081 -237 -533 1096 C ATOM 1291 CG2 ILE A 189 13.019 -29.178 60.099 1.00 76.21 C ANISOU 1291 CG2 ILE A 189 5631 11414 11910 -342 -628 943 C ATOM 1292 CD1 ILE A 189 12.255 -32.051 60.186 1.00 84.61 C ANISOU 1292 CD1 ILE A 189 6379 12420 13351 -327 -523 1034 C ATOM 1293 N CYS A 190 12.832 -27.893 62.904 1.00 76.92 N ANISOU 1293 N CYS A 190 5960 11598 11669 -117 -664 1099 N ATOM 1294 CA CYS A 190 13.577 -27.733 64.149 1.00 78.40 C ANISOU 1294 CA CYS A 190 6200 11821 11766 -67 -712 1155 C ATOM 1295 C CYS A 190 13.776 -26.213 64.381 1.00 81.20 C ANISOU 1295 C CYS A 190 6764 12168 11919 -77 -777 1085 C ATOM 1296 O CYS A 190 14.763 -25.763 64.956 1.00 81.21 O ANISOU 1296 O CYS A 190 6815 12164 11877 -147 -856 1045 O ATOM 1297 CB CYS A 190 14.881 -28.533 64.160 1.00 79.85 C ANISOU 1297 CB CYS A 190 6253 12008 12077 -135 -744 1169 C ATOM 1298 SG CYS A 190 14.856 -30.035 65.212 1.00 85.06 S ANISOU 1298 SG CYS A 190 6814 12725 12781 -29 -730 1319 S ATOM 1299 N ASP A 191 12.749 -25.449 63.943 1.00 76.32 N ANISOU 1299 N ASP A 191 6268 11546 11186 -9 -743 1074 N ATOM 1300 CA ASP A 191 12.485 -24.014 64.141 1.00 75.59 C ANISOU 1300 CA ASP A 191 6393 11436 10893 13 -783 1017 C ATOM 1301 C ASP A 191 10.954 -23.878 64.375 1.00 77.91 C ANISOU 1301 C ASP A 191 6759 11752 11091 157 -709 1082 C ATOM 1302 O ASP A 191 10.257 -23.075 63.747 1.00 76.92 O ANISOU 1302 O ASP A 191 6751 11604 10871 168 -693 1032 O ATOM 1303 CB ASP A 191 13.007 -23.161 62.977 1.00 76.77 C ANISOU 1303 CB ASP A 191 6585 11534 11049 -118 -817 895 C ATOM 1304 N ILE A 192 10.461 -24.728 65.306 1.00 74.06 N ANISOU 1304 N ILE A 192 6191 11315 10632 272 -662 1205 N ATOM 1305 CA ILE A 192 9.082 -24.959 65.758 1.00 73.74 C ANISOU 1305 CA ILE A 192 6155 11320 10544 426 -580 1318 C ATOM 1306 C ILE A 192 8.360 -23.632 66.140 1.00 77.87 C ANISOU 1306 C ILE A 192 6896 11839 10851 523 -567 1300 C ATOM 1307 O ILE A 192 7.135 -23.587 66.065 1.00 76.97 O ANISOU 1307 O ILE A 192 6773 11745 10728 602 -491 1356 O ATOM 1308 CB ILE A 192 9.087 -25.961 66.966 1.00 77.33 C ANISOU 1308 CB ILE A 192 6540 11834 11009 533 -568 1447 C ATOM 1309 CG1 ILE A 192 9.827 -27.281 66.657 1.00 77.41 C ANISOU 1309 CG1 ILE A 192 6335 11844 11235 446 -575 1473 C ATOM 1310 CG2 ILE A 192 7.684 -26.260 67.492 1.00 78.33 C ANISOU 1310 CG2 ILE A 192 6650 12017 11095 700 -478 1587 C ATOM 1311 CD1 ILE A 192 11.141 -27.511 67.451 1.00 84.91 C ANISOU 1311 CD1 ILE A 192 7292 12791 12177 380 -659 1439 C ATOM 1312 N GLU A 193 9.097 -22.576 66.543 1.00 75.39 N ANISOU 1312 N GLU A 193 6777 11499 10368 523 -642 1231 N ATOM 1313 CA GLU A 193 8.510 -21.285 66.917 1.00 75.82 C ANISOU 1313 CA GLU A 193 7057 11538 10212 622 -632 1209 C ATOM 1314 C GLU A 193 8.048 -20.480 65.696 1.00 78.25 C ANISOU 1314 C GLU A 193 7396 11802 10532 552 -607 1128 C ATOM 1315 O GLU A 193 7.102 -19.700 65.803 1.00 77.89 O ANISOU 1315 O GLU A 193 7439 11768 10389 661 -541 1165 O ATOM 1316 CB GLU A 193 9.500 -20.440 67.722 1.00 78.21 C ANISOU 1316 CB GLU A 193 7570 11808 10340 617 -734 1143 C ATOM 1317 CG GLU A 193 9.734 -20.923 69.141 1.00 92.00 C ANISOU 1317 CG GLU A 193 9353 13605 11997 744 -744 1237 C ATOM 1318 CD GLU A 193 10.182 -19.836 70.101 1.00117.32 C ANISOU 1318 CD GLU A 193 12773 16780 15022 747 -854 1180 C ATOM 1319 OE1 GLU A 193 10.856 -18.873 69.663 1.00113.09 O ANISOU 1319 OE1 GLU A 193 12360 16175 14433 630 -940 1063 O ATOM 1320 OE2 GLU A 193 9.849 -19.950 71.303 1.00113.24 O1- ANISOU 1320 OE2 GLU A 193 12300 16310 14416 865 -859 1258 O1- ATOM 1321 N ASN A 194 8.720 -20.653 64.547 1.00 73.40 N ANISOU 1321 N ASN A 194 6698 11147 10044 380 -651 1031 N ATOM 1322 CA ASN A 194 8.415 -19.926 63.315 1.00 72.12 C ANISOU 1322 CA ASN A 194 6546 10946 9910 294 -635 947 C ATOM 1323 C ASN A 194 7.492 -20.735 62.376 1.00 73.22 C ANISOU 1323 C ASN A 194 6506 11113 10199 298 -546 1001 C ATOM 1324 O ASN A 194 7.605 -20.593 61.158 1.00 72.01 O ANISOU 1324 O ASN A 194 6319 10933 10107 204 -537 930 O ATOM 1325 CB ASN A 194 9.730 -19.560 62.595 1.00 75.03 C ANISOU 1325 CB ASN A 194 6889 11268 10351 116 -718 833 C ATOM 1326 CG ASN A 194 10.492 -18.438 63.247 1.00109.96 C ANISOU 1326 CG ASN A 194 11524 15640 14617 75 -806 747 C ATOM 1327 OD1 ASN A 194 9.989 -17.319 63.409 1.00106.23 O ANISOU 1327 OD1 ASN A 194 11229 15143 13990 146 -795 730 O ATOM 1328 ND2 ASN A 194 11.744 -18.698 63.580 1.00104.91 N ANISOU 1328 ND2 ASN A 194 10863 14978 14020 -50 -897 694 N ATOM 1329 N CYS A 195 6.562 -21.542 62.925 1.00 68.55 N ANISOU 1329 N CYS A 195 5806 10577 9663 403 -485 1130 N ATOM 1330 CA CYS A 195 5.654 -22.362 62.110 1.00 67.37 C ANISOU 1330 CA CYS A 195 5489 10452 9656 404 -412 1196 C ATOM 1331 C CYS A 195 4.367 -21.623 61.747 1.00 70.72 C ANISOU 1331 C CYS A 195 5999 10896 9976 500 -346 1239 C ATOM 1332 O CYS A 195 3.793 -20.912 62.580 1.00 71.08 O ANISOU 1332 O CYS A 195 6191 10965 9853 639 -322 1293 O ATOM 1333 CB CYS A 195 5.330 -23.673 62.815 1.00 67.82 C ANISOU 1333 CB CYS A 195 5387 10557 9826 469 -380 1328 C ATOM 1334 SG CYS A 195 6.684 -24.874 62.802 1.00 71.23 S ANISOU 1334 SG CYS A 195 5630 10962 10470 331 -429 1291 S ATOM 1335 N SER A 196 3.892 -21.853 60.508 1.00 66.04 N ANISOU 1335 N SER A 196 5313 10296 9483 431 -314 1221 N ATOM 1336 CA SER A 196 2.662 -21.255 59.992 1.00 65.92 C ANISOU 1336 CA SER A 196 5348 10305 9393 509 -247 1274 C ATOM 1337 C SER A 196 1.415 -22.037 60.436 1.00 69.93 C ANISOU 1337 C SER A 196 5730 10879 9960 621 -178 1447 C ATOM 1338 O SER A 196 1.504 -23.242 60.665 1.00 69.56 O ANISOU 1338 O SER A 196 5534 10847 10050 602 -186 1507 O ATOM 1339 CB SER A 196 2.707 -21.173 58.472 1.00 69.04 C ANISOU 1339 CB SER A 196 5699 10669 9863 383 -250 1183 C ATOM 1340 OG SER A 196 2.810 -22.455 57.876 1.00 77.50 O ANISOU 1340 OG SER A 196 6574 11737 11136 285 -254 1189 O ATOM 1341 N ASN A 197 0.258 -21.345 60.545 1.00 66.48 N ANISOU 1341 N ASN A 197 5351 10484 9424 739 -110 1537 N ATOM 1342 CA ASN A 197 -1.031 -21.922 60.957 1.00 66.58 C ANISOU 1342 CA ASN A 197 5249 10570 9477 859 -39 1725 C ATOM 1343 C ASN A 197 -1.607 -22.865 59.897 1.00 69.68 C ANISOU 1343 C ASN A 197 5443 10967 10066 755 -30 1762 C ATOM 1344 O ASN A 197 -2.241 -23.854 60.253 1.00 69.30 O ANISOU 1344 O ASN A 197 5231 10948 10150 766 -20 1877 O ATOM 1345 CB ASN A 197 -2.053 -20.810 61.258 1.00 67.07 C ANISOU 1345 CB ASN A 197 5451 10679 9354 1030 34 1816 C ATOM 1346 CG ASN A 197 -1.696 -19.949 62.447 1.00 85.23 C ANISOU 1346 CG ASN A 197 7976 12962 11445 1135 20 1767 C ATOM 1347 OD1 ASN A 197 -1.533 -20.430 63.569 1.00 78.77 O ANISOU 1347 OD1 ASN A 197 7185 12183 10562 1261 36 1857 O ATOM 1348 ND2 ASN A 197 -1.597 -18.646 62.242 1.00 75.99 N ANISOU 1348 ND2 ASN A 197 6976 11731 10166 1082 -15 1625 N ATOM 1349 N MET A 198 -1.393 -22.558 58.612 1.00 65.67 N ANISOU 1349 N MET A 198 4952 10425 9573 651 -40 1663 N ATOM 1350 CA MET A 198 -1.914 -23.361 57.505 1.00 65.03 C ANISOU 1350 CA MET A 198 4713 10342 9653 546 -40 1678 C ATOM 1351 C MET A 198 -1.068 -24.633 57.333 1.00 68.69 C ANISOU 1351 C MET A 198 5048 10751 10300 398 -102 1594 C ATOM 1352 O MET A 198 -1.607 -25.740 57.359 1.00 68.48 O ANISOU 1352 O MET A 198 4860 10728 10432 348 -104 1662 O ATOM 1353 CB MET A 198 -1.943 -22.525 56.221 1.00 66.85 C ANISOU 1353 CB MET A 198 5027 10555 9816 491 -33 1588 C ATOM 1354 CG MET A 198 -2.825 -23.098 55.150 1.00 70.22 C ANISOU 1354 CG MET A 198 5319 11003 10357 431 -16 1648 C ATOM 1355 SD MET A 198 -4.072 -21.926 54.560 1.00 74.21 S ANISOU 1355 SD MET A 198 5930 11546 10720 488 41 1673 S ATOM 1356 CE MET A 198 -3.043 -20.696 53.801 1.00 70.12 C ANISOU 1356 CE MET A 198 5564 10954 10125 378 -7 1446 C ATOM 1357 N ALA A 199 0.252 -24.477 57.164 1.00 64.90 N ANISOU 1357 N ALA A 199 4641 10219 9798 328 -154 1451 N ATOM 1358 CA ALA A 199 1.167 -25.608 57.027 1.00 64.33 C ANISOU 1358 CA ALA A 199 4463 10097 9882 204 -207 1370 C ATOM 1359 C ALA A 199 2.027 -25.724 58.299 1.00 68.36 C ANISOU 1359 C ALA A 199 4992 10612 10369 258 -229 1393 C ATOM 1360 O ALA A 199 2.898 -24.873 58.521 1.00 67.78 O ANISOU 1360 O ALA A 199 5043 10517 10193 247 -264 1301 O ATOM 1361 CB ALA A 199 2.027 -25.437 55.787 1.00 64.36 C ANISOU 1361 CB ALA A 199 4519 10046 9890 71 -247 1195 C ATOM 1362 N PRO A 200 1.752 -26.716 59.192 1.00 65.26 N ANISOU 1362 N PRO A 200 4477 10251 10066 322 -210 1530 N ATOM 1363 CA PRO A 200 2.487 -26.776 60.468 1.00 65.68 C ANISOU 1363 CA PRO A 200 4548 10325 10084 396 -222 1579 C ATOM 1364 C PRO A 200 3.955 -27.185 60.344 1.00 69.89 C ANISOU 1364 C PRO A 200 5051 10809 10693 294 -282 1473 C ATOM 1365 O PRO A 200 4.678 -26.999 61.319 1.00 70.62 O ANISOU 1365 O PRO A 200 5153 10922 10756 352 -296 1518 O ATOM 1366 CB PRO A 200 1.723 -27.822 61.278 1.00 67.90 C ANISOU 1366 CB PRO A 200 4675 10651 10474 471 -183 1758 C ATOM 1367 CG PRO A 200 0.416 -27.986 60.573 1.00 72.20 C ANISOU 1367 CG PRO A 200 5187 11221 11026 489 -141 1828 C ATOM 1368 CD PRO A 200 0.717 -27.764 59.138 1.00 66.89 C ANISOU 1368 CD PRO A 200 4534 10486 10396 342 -175 1668 C ATOM 1369 N LEU A 201 4.402 -27.723 59.186 1.00 65.10 N ANISOU 1369 N LEU A 201 4415 10146 10176 152 -316 1340 N ATOM 1370 CA LEU A 201 5.799 -28.132 58.988 1.00 64.07 C ANISOU 1370 CA LEU A 201 4255 9972 10116 55 -367 1243 C ATOM 1371 C LEU A 201 6.561 -27.153 58.069 1.00 67.09 C ANISOU 1371 C LEU A 201 4743 10316 10430 -43 -403 1086 C ATOM 1372 O LEU A 201 7.779 -27.274 57.950 1.00 66.56 O ANISOU 1372 O LEU A 201 4677 10225 10389 -114 -447 1010 O ATOM 1373 CB LEU A 201 5.902 -29.558 58.424 1.00 63.75 C ANISOU 1373 CB LEU A 201 4036 9897 10290 -19 -369 1254 C ATOM 1374 CG LEU A 201 5.731 -30.711 59.403 1.00 68.49 C ANISOU 1374 CG LEU A 201 4514 10521 10989 50 -353 1395 C ATOM 1375 CD1 LEU A 201 4.268 -31.065 59.593 1.00 68.79 C ANISOU 1375 CD1 LEU A 201 4476 10586 11075 110 -310 1526 C ATOM 1376 CD2 LEU A 201 6.457 -31.939 58.901 1.00 70.49 C ANISOU 1376 CD2 LEU A 201 4638 10723 11423 -36 -375 1361 C ATOM 1377 N TYR A 202 5.865 -26.176 57.451 1.00 63.20 N ANISOU 1377 N TYR A 202 4337 9825 9850 -43 -382 1049 N ATOM 1378 CA TYR A 202 6.481 -25.161 56.582 1.00 62.27 C ANISOU 1378 CA TYR A 202 4325 9676 9659 -127 -411 915 C ATOM 1379 C TYR A 202 6.681 -23.848 57.336 1.00 65.36 C ANISOU 1379 C TYR A 202 4900 10077 9858 -68 -435 897 C ATOM 1380 O TYR A 202 5.807 -23.435 58.104 1.00 65.46 O ANISOU 1380 O TYR A 202 4986 10125 9763 56 -405 987 O ATOM 1381 CB TYR A 202 5.625 -24.925 55.326 1.00 63.08 C ANISOU 1381 CB TYR A 202 4421 9774 9772 -160 -378 886 C ATOM 1382 CG TYR A 202 5.934 -25.818 54.140 1.00 64.59 C ANISOU 1382 CG TYR A 202 4482 9931 10127 -269 -382 828 C ATOM 1383 CD1 TYR A 202 6.197 -27.175 54.312 1.00 66.62 C ANISOU 1383 CD1 TYR A 202 4613 10164 10534 -310 -398 833 C ATOM 1384 CD2 TYR A 202 5.879 -25.324 52.844 1.00 65.17 C ANISOU 1384 CD2 TYR A 202 4563 9996 10203 -325 -367 770 C ATOM 1385 CE1 TYR A 202 6.471 -28.002 53.225 1.00 67.36 C ANISOU 1385 CE1 TYR A 202 4605 10218 10770 -401 -400 775 C ATOM 1386 CE2 TYR A 202 6.126 -26.148 51.747 1.00 65.91 C ANISOU 1386 CE2 TYR A 202 4553 10056 10436 -419 -373 711 C ATOM 1387 CZ TYR A 202 6.429 -27.484 51.944 1.00 73.65 C ANISOU 1387 CZ TYR A 202 5421 11005 11558 -455 -390 710 C ATOM 1388 OH TYR A 202 6.665 -28.301 50.867 1.00 74.74 O ANISOU 1388 OH TYR A 202 5473 11100 11825 -539 -396 647 O ATOM 1389 N SER A 203 7.821 -23.180 57.086 1.00 60.95 N ANISOU 1389 N SER A 203 4420 9484 9252 -155 -490 787 N ATOM 1390 CA SER A 203 8.184 -21.912 57.724 1.00 60.81 C ANISOU 1390 CA SER A 203 4590 9459 9057 -121 -531 756 C ATOM 1391 C SER A 203 7.404 -20.740 57.114 1.00 63.72 C ANISOU 1391 C SER A 203 5088 9818 9303 -97 -505 722 C ATOM 1392 O SER A 203 7.085 -20.771 55.921 1.00 62.58 O ANISOU 1392 O SER A 203 4890 9666 9221 -160 -479 678 O ATOM 1393 CB SER A 203 9.688 -21.663 57.615 1.00 64.13 C ANISOU 1393 CB SER A 203 5032 9847 9488 -233 -609 667 C ATOM 1394 OG SER A 203 10.091 -21.105 56.377 1.00 71.70 O ANISOU 1394 OG SER A 203 5920 10781 10542 -353 -612 580 O ATOM 1395 N ASP A 204 7.101 -19.712 57.944 1.00 60.40 N ANISOU 1395 N ASP A 204 4844 9399 8705 2 -512 746 N ATOM 1396 CA ASP A 204 6.375 -18.499 57.536 1.00 60.08 C ANISOU 1396 CA ASP A 204 4955 9347 8525 50 -486 725 C ATOM 1397 C ASP A 204 7.179 -17.709 56.497 1.00 63.28 C ANISOU 1397 C ASP A 204 5406 9706 8932 -84 -529 601 C ATOM 1398 O ASP A 204 6.597 -17.155 55.564 1.00 62.20 O ANISOU 1398 O ASP A 204 5267 9569 8795 -100 -488 579 O ATOM 1399 CB ASP A 204 6.077 -17.590 58.747 1.00 62.59 C ANISOU 1399 CB ASP A 204 5473 9660 8647 177 -500 759 C ATOM 1400 CG ASP A 204 5.308 -18.197 59.897 1.00 71.25 C ANISOU 1400 CG ASP A 204 6550 10813 9707 341 -437 897 C ATOM 1401 OD1 ASP A 204 4.094 -18.405 59.749 1.00 70.35 O ANISOU 1401 OD1 ASP A 204 6336 10743 9652 396 -359 979 O ATOM 1402 OD2 ASP A 204 5.890 -18.327 60.991 1.00 78.81 O1- ANISOU 1402 OD2 ASP A 204 7603 11775 10565 421 -467 928 O1- ATOM 1403 N SER A 205 8.524 -17.656 56.673 1.00 60.27 N ANISOU 1403 N SER A 205 5049 9292 8561 -182 -612 529 N ATOM 1404 CA SER A 205 9.467 -16.964 55.782 1.00 59.56 C ANISOU 1404 CA SER A 205 4986 9162 8483 -316 -662 424 C ATOM 1405 C SER A 205 9.444 -17.562 54.371 1.00 62.55 C ANISOU 1405 C SER A 205 5198 9553 9013 -401 -620 391 C ATOM 1406 O SER A 205 9.654 -16.837 53.401 1.00 61.78 O ANISOU 1406 O SER A 205 5130 9437 8904 -471 -623 322 O ATOM 1407 CB SER A 205 10.882 -17.028 56.350 1.00 62.45 C ANISOU 1407 CB SER A 205 5366 9503 8857 -401 -756 386 C ATOM 1408 OG SER A 205 11.341 -18.358 56.530 1.00 68.38 O ANISOU 1408 OG SER A 205 5953 10283 9745 -419 -755 426 O ATOM 1409 N TYR A 206 9.184 -18.883 54.266 1.00 58.88 N ANISOU 1409 N TYR A 206 4565 9117 8688 -392 -584 440 N ATOM 1410 CA TYR A 206 9.110 -19.592 52.993 1.00 58.03 C ANISOU 1410 CA TYR A 206 4310 9016 8722 -462 -547 410 C ATOM 1411 C TYR A 206 7.793 -19.291 52.294 1.00 62.96 C ANISOU 1411 C TYR A 206 4950 9660 9312 -408 -483 439 C ATOM 1412 O TYR A 206 7.821 -19.014 51.095 1.00 62.28 O ANISOU 1412 O TYR A 206 4834 9568 9261 -477 -468 380 O ATOM 1413 CB TYR A 206 9.292 -21.109 53.176 1.00 58.59 C ANISOU 1413 CB TYR A 206 4210 9100 8954 -471 -535 452 C ATOM 1414 CG TYR A 206 9.087 -21.900 51.904 1.00 58.97 C ANISOU 1414 CG TYR A 206 4127 9142 9138 -542 -503 412 C ATOM 1415 CD1 TYR A 206 10.101 -22.010 50.958 1.00 60.48 C ANISOU 1415 CD1 TYR A 206 4287 9312 9379 -649 -526 317 C ATOM 1416 CD2 TYR A 206 7.883 -22.543 51.651 1.00 59.36 C ANISOU 1416 CD2 TYR A 206 4089 9207 9258 -501 -454 471 C ATOM 1417 CE1 TYR A 206 9.911 -22.724 49.776 1.00 60.26 C ANISOU 1417 CE1 TYR A 206 4159 9277 9459 -705 -497 272 C ATOM 1418 CE2 TYR A 206 7.679 -23.252 50.471 1.00 59.74 C ANISOU 1418 CE2 TYR A 206 4035 9242 9421 -569 -435 427 C ATOM 1419 CZ TYR A 206 8.698 -23.346 49.539 1.00 65.93 C ANISOU 1419 CZ TYR A 206 4803 10003 10244 -667 -456 322 C ATOM 1420 OH TYR A 206 8.508 -24.058 48.380 1.00 66.03 O ANISOU 1420 OH TYR A 206 4729 10001 10358 -727 -438 272 O ATOM 1421 N LEU A 207 6.650 -19.363 53.025 1.00 60.66 N ANISOU 1421 N LEU A 207 4705 9396 8948 -281 -444 538 N ATOM 1422 CA LEU A 207 5.309 -19.139 52.476 1.00 60.75 C ANISOU 1422 CA LEU A 207 4726 9435 8919 -215 -379 592 C ATOM 1423 C LEU A 207 5.123 -17.709 51.969 1.00 65.57 C ANISOU 1423 C LEU A 207 5475 10027 9411 -234 -379 526 C ATOM 1424 O LEU A 207 4.459 -17.532 50.950 1.00 64.58 O ANISOU 1424 O LEU A 207 5305 9914 9316 -266 -345 513 O ATOM 1425 CB LEU A 207 4.207 -19.468 53.493 1.00 61.39 C ANISOU 1425 CB LEU A 207 4841 9555 8929 -62 -335 723 C ATOM 1426 CG LEU A 207 4.025 -20.944 53.902 1.00 66.58 C ANISOU 1426 CG LEU A 207 5350 10243 9704 -20 -317 824 C ATOM 1427 CD1 LEU A 207 2.821 -21.092 54.778 1.00 67.11 C ANISOU 1427 CD1 LEU A 207 5437 10361 9700 129 -255 964 C ATOM 1428 CD2 LEU A 207 3.845 -21.859 52.684 1.00 69.40 C ANISOU 1428 CD2 LEU A 207 5529 10598 10242 -114 -310 812 C ATOM 1429 N VAL A 208 5.732 -16.703 52.642 1.00 63.87 N ANISOU 1429 N VAL A 208 5426 9779 9063 -220 -423 485 N ATOM 1430 CA VAL A 208 5.690 -15.291 52.221 1.00 64.34 C ANISOU 1430 CA VAL A 208 5633 9809 9005 -239 -432 423 C ATOM 1431 C VAL A 208 6.473 -15.165 50.903 1.00 69.21 C ANISOU 1431 C VAL A 208 6178 10409 9711 -387 -458 322 C ATOM 1432 O VAL A 208 6.000 -14.507 49.980 1.00 68.23 O ANISOU 1432 O VAL A 208 6086 10285 9552 -407 -431 293 O ATOM 1433 CB VAL A 208 6.216 -14.327 53.325 1.00 68.88 C ANISOU 1433 CB VAL A 208 6409 10338 9425 -200 -489 399 C ATOM 1434 CG1 VAL A 208 6.438 -12.909 52.797 1.00 68.72 C ANISOU 1434 CG1 VAL A 208 6546 10280 9285 -212 -494 344 C ATOM 1435 CG2 VAL A 208 5.267 -14.305 54.510 1.00 69.35 C ANISOU 1435 CG2 VAL A 208 6543 10418 9389 -44 -462 497 C ATOM 1436 N PHE A 209 7.640 -15.841 50.815 1.00 67.31 N ANISOU 1436 N PHE A 209 5833 10159 9584 -481 -504 279 N ATOM 1437 CA PHE A 209 8.510 -15.878 49.636 1.00 67.64 C ANISOU 1437 CA PHE A 209 5796 10191 9714 -610 -524 193 C ATOM 1438 C PHE A 209 7.837 -16.617 48.475 1.00 71.77 C ANISOU 1438 C PHE A 209 6190 10743 10335 -629 -466 193 C ATOM 1439 O PHE A 209 7.880 -16.119 47.354 1.00 71.40 O ANISOU 1439 O PHE A 209 6161 10699 10268 -672 -449 146 O ATOM 1440 CB PHE A 209 9.867 -16.535 49.973 1.00 70.03 C ANISOU 1440 CB PHE A 209 6014 10482 10112 -684 -578 167 C ATOM 1441 CG PHE A 209 10.746 -16.898 48.791 1.00 71.82 C ANISOU 1441 CG PHE A 209 6141 10707 10439 -800 -586 93 C ATOM 1442 CD1 PHE A 209 11.523 -15.932 48.154 1.00 75.35 C ANISOU 1442 CD1 PHE A 209 6658 11137 10837 -878 -626 31 C ATOM 1443 CD2 PHE A 209 10.835 -18.213 48.346 1.00 74.05 C ANISOU 1443 CD2 PHE A 209 6265 11006 10865 -827 -555 89 C ATOM 1444 CE1 PHE A 209 12.342 -16.268 47.069 1.00 76.12 C ANISOU 1444 CE1 PHE A 209 6659 11241 11021 -973 -627 -26 C ATOM 1445 CE2 PHE A 209 11.651 -18.547 47.261 1.00 76.87 C ANISOU 1445 CE2 PHE A 209 6541 11362 11303 -918 -556 21 C ATOM 1446 CZ PHE A 209 12.400 -17.572 46.629 1.00 75.04 C ANISOU 1446 CZ PHE A 209 6372 11123 11017 -987 -589 -33 C ATOM 1447 N TRP A 210 7.234 -17.797 48.742 1.00 68.47 N ANISOU 1447 N TRP A 210 5644 10345 10026 -602 -441 246 N ATOM 1448 CA TRP A 210 6.551 -18.650 47.761 1.00 67.89 C ANISOU 1448 CA TRP A 210 5443 10292 10060 -623 -400 255 C ATOM 1449 C TRP A 210 5.334 -17.943 47.148 1.00 70.00 C ANISOU 1449 C TRP A 210 5755 10586 10256 -580 -353 287 C ATOM 1450 O TRP A 210 5.158 -18.005 45.929 1.00 69.15 O ANISOU 1450 O TRP A 210 5584 10489 10202 -636 -335 252 O ATOM 1451 CB TRP A 210 6.120 -19.973 48.416 1.00 67.16 C ANISOU 1451 CB TRP A 210 5239 10209 10069 -577 -388 335 C ATOM 1452 CG TRP A 210 5.379 -20.915 47.518 1.00 68.31 C ANISOU 1452 CG TRP A 210 5259 10366 10330 -600 -359 355 C ATOM 1453 CD1 TRP A 210 4.029 -21.104 47.458 1.00 71.51 C ANISOU 1453 CD1 TRP A 210 5621 10800 10750 -534 -324 457 C ATOM 1454 CD2 TRP A 210 5.952 -21.815 46.562 1.00 68.11 C ANISOU 1454 CD2 TRP A 210 5138 10320 10419 -695 -368 277 C ATOM 1455 NE1 TRP A 210 3.727 -22.077 46.532 1.00 71.04 N ANISOU 1455 NE1 TRP A 210 5446 10735 10813 -594 -321 445 N ATOM 1456 CE2 TRP A 210 4.891 -22.529 45.964 1.00 72.18 C ANISOU 1456 CE2 TRP A 210 5564 10846 11016 -689 -346 329 C ATOM 1457 CE3 TRP A 210 7.270 -22.089 46.151 1.00 69.36 C ANISOU 1457 CE3 TRP A 210 5280 10455 10618 -781 -392 174 C ATOM 1458 CZ2 TRP A 210 5.102 -23.495 44.977 1.00 71.40 C ANISOU 1458 CZ2 TRP A 210 5374 10724 11029 -766 -354 268 C ATOM 1459 CZ3 TRP A 210 7.481 -23.051 45.177 1.00 70.77 C ANISOU 1459 CZ3 TRP A 210 5366 10618 10906 -845 -387 118 C ATOM 1460 CH2 TRP A 210 6.408 -23.747 44.606 1.00 71.45 C ANISOU 1460 CH2 TRP A 210 5379 10705 11065 -838 -371 159 C ATOM 1461 N ALA A 211 4.509 -17.277 47.982 1.00 65.82 N ANISOU 1461 N ALA A 211 5339 10068 9601 -478 -332 356 N ATOM 1462 CA ALA A 211 3.315 -16.557 47.536 1.00 65.35 C ANISOU 1462 CA ALA A 211 5330 10039 9463 -422 -281 402 C ATOM 1463 C ALA A 211 3.675 -15.322 46.714 1.00 68.68 C ANISOU 1463 C ALA A 211 5846 10444 9807 -478 -289 317 C ATOM 1464 O ALA A 211 3.038 -15.093 45.685 1.00 68.42 O ANISOU 1464 O ALA A 211 5753 10429 9815 -534 -269 287 O ATOM 1465 CB ALA A 211 2.459 -16.151 48.724 1.00 66.57 C ANISOU 1465 CB ALA A 211 5580 10210 9503 -279 -249 508 C ATOM 1466 N ILE A 212 4.691 -14.537 47.147 1.00 64.61 N ANISOU 1466 N ILE A 212 5476 9891 9183 -470 -324 278 N ATOM 1467 CA ILE A 212 5.098 -13.326 46.435 1.00 63.96 C ANISOU 1467 CA ILE A 212 5497 9785 9020 -521 -337 206 C ATOM 1468 C ILE A 212 5.864 -13.702 45.132 1.00 67.55 C ANISOU 1468 C ILE A 212 5848 10241 9578 -654 -358 116 C ATOM 1469 O ILE A 212 5.864 -12.900 44.195 1.00 66.83 O ANISOU 1469 O ILE A 212 5775 10159 9458 -689 -339 82 O ATOM 1470 CB ILE A 212 5.908 -12.361 47.344 1.00 67.38 C ANISOU 1470 CB ILE A 212 6105 10166 9333 -502 -390 181 C ATOM 1471 CG1 ILE A 212 5.747 -10.886 46.925 1.00 67.73 C ANISOU 1471 CG1 ILE A 212 6296 10185 9254 -495 -382 154 C ATOM 1472 CG2 ILE A 212 7.387 -12.767 47.530 1.00 68.58 C ANISOU 1472 CG2 ILE A 212 6229 10285 9544 -599 -468 118 C ATOM 1473 CD1 ILE A 212 4.440 -10.208 47.349 1.00 73.29 C ANISOU 1473 CD1 ILE A 212 7109 10903 9836 -353 -318 236 C ATOM 1474 N PHE A 213 6.472 -14.918 45.061 1.00 64.27 N ANISOU 1474 N PHE A 213 5319 9819 9280 -717 -390 86 N ATOM 1475 CA PHE A 213 7.204 -15.395 43.882 1.00 63.76 C ANISOU 1475 CA PHE A 213 5153 9758 9315 -825 -402 7 C ATOM 1476 C PHE A 213 6.229 -15.771 42.772 1.00 66.42 C ANISOU 1476 C PHE A 213 5405 10130 9700 -835 -353 7 C ATOM 1477 O PHE A 213 6.470 -15.407 41.622 1.00 66.61 O ANISOU 1477 O PHE A 213 5426 10165 9719 -896 -347 -52 O ATOM 1478 CB PHE A 213 8.109 -16.591 44.225 1.00 65.87 C ANISOU 1478 CB PHE A 213 5316 10014 9699 -863 -433 -6 C ATOM 1479 CG PHE A 213 8.907 -17.159 43.071 1.00 67.56 C ANISOU 1479 CG PHE A 213 5410 10234 10025 -949 -430 -73 C ATOM 1480 CD1 PHE A 213 10.097 -16.563 42.666 1.00 70.87 C ANISOU 1480 CD1 PHE A 213 5833 10645 10449 -1027 -461 -137 C ATOM 1481 CD2 PHE A 213 8.494 -18.318 42.420 1.00 69.90 C ANISOU 1481 CD2 PHE A 213 5593 10543 10424 -948 -400 -67 C ATOM 1482 CE1 PHE A 213 10.850 -17.104 41.618 1.00 71.76 C ANISOU 1482 CE1 PHE A 213 5840 10768 10658 -1090 -450 -193 C ATOM 1483 CE2 PHE A 213 9.245 -18.854 41.371 1.00 72.73 C ANISOU 1483 CE2 PHE A 213 5858 10900 10875 -1016 -396 -134 C ATOM 1484 CZ PHE A 213 10.422 -18.246 40.982 1.00 70.81 C ANISOU 1484 CZ PHE A 213 5622 10654 10628 -1080 -416 -197 C ATOM 1485 N ASN A 214 5.140 -16.497 43.113 1.00 61.05 N ANISOU 1485 N ASN A 214 4658 9471 9067 -777 -324 80 N ATOM 1486 CA ASN A 214 4.135 -16.936 42.152 1.00 59.88 C ANISOU 1486 CA ASN A 214 4427 9355 8970 -790 -290 95 C ATOM 1487 C ASN A 214 3.245 -15.777 41.699 1.00 62.63 C ANISOU 1487 C ASN A 214 4856 9733 9207 -751 -253 127 C ATOM 1488 O ASN A 214 2.797 -15.781 40.552 1.00 62.10 O ANISOU 1488 O ASN A 214 4748 9691 9156 -796 -236 100 O ATOM 1489 CB ASN A 214 3.283 -18.063 42.717 1.00 59.73 C ANISOU 1489 CB ASN A 214 4310 9346 9039 -746 -280 178 C ATOM 1490 CG ASN A 214 4.020 -19.372 42.857 1.00 78.07 C ANISOU 1490 CG ASN A 214 6526 11639 11496 -799 -309 139 C ATOM 1491 OD1 ASN A 214 4.436 -20.001 41.874 1.00 70.27 O ANISOU 1491 OD1 ASN A 214 5510 10635 10557 -877 -327 45 O ATOM 1492 ND2 ASN A 214 4.185 -19.826 44.088 1.00 70.72 N ANISOU 1492 ND2 ASN A 214 5532 10705 10632 -753 -309 217 N ATOM 1493 N LEU A 215 2.995 -14.786 42.580 1.00 58.57 N ANISOU 1493 N LEU A 215 4464 9213 8576 -667 -240 180 N ATOM 1494 CA LEU A 215 2.161 -13.624 42.254 1.00 58.07 C ANISOU 1494 CA LEU A 215 4490 9174 8400 -617 -199 216 C ATOM 1495 C LEU A 215 2.903 -12.632 41.361 1.00 60.75 C ANISOU 1495 C LEU A 215 4897 9497 8688 -689 -214 125 C ATOM 1496 O LEU A 215 2.272 -12.065 40.473 1.00 60.72 O ANISOU 1496 O LEU A 215 4904 9523 8643 -692 -180 131 O ATOM 1497 CB LEU A 215 1.651 -12.909 43.514 1.00 58.54 C ANISOU 1497 CB LEU A 215 4674 9226 8343 -491 -178 300 C ATOM 1498 CG LEU A 215 0.440 -13.543 44.218 1.00 63.39 C ANISOU 1498 CG LEU A 215 5230 9875 8982 -392 -144 424 C ATOM 1499 CD1 LEU A 215 0.296 -13.019 45.624 1.00 63.78 C ANISOU 1499 CD1 LEU A 215 5418 9909 8907 -265 -128 488 C ATOM 1500 CD2 LEU A 215 -0.850 -13.311 43.438 1.00 66.54 C ANISOU 1500 CD2 LEU A 215 5553 10333 9397 -368 -92 505 C ATOM 1501 N VAL A 216 4.221 -12.422 41.575 1.00 55.88 N ANISOU 1501 N VAL A 216 4318 8838 8076 -748 -265 51 N ATOM 1502 CA VAL A 216 5.024 -11.503 40.747 1.00 55.26 C ANISOU 1502 CA VAL A 216 4291 8744 7961 -824 -285 -26 C ATOM 1503 C VAL A 216 5.172 -12.116 39.333 1.00 58.55 C ANISOU 1503 C VAL A 216 4587 9198 8460 -902 -268 -77 C ATOM 1504 O VAL A 216 5.258 -11.366 38.361 1.00 58.11 O ANISOU 1504 O VAL A 216 4560 9164 8358 -926 -247 -98 O ATOM 1505 CB VAL A 216 6.396 -11.126 41.391 1.00 59.04 C ANISOU 1505 CB VAL A 216 4820 9174 8441 -876 -351 -77 C ATOM 1506 CG1 VAL A 216 7.585 -11.404 40.470 1.00 58.51 C ANISOU 1506 CG1 VAL A 216 4717 9107 8408 -985 -375 -155 C ATOM 1507 CG2 VAL A 216 6.404 -9.674 41.871 1.00 59.27 C ANISOU 1507 CG2 VAL A 216 5022 9157 8341 -814 -374 -49 C ATOM 1508 N THR A 217 5.146 -13.469 39.225 1.00 54.66 N ANISOU 1508 N THR A 217 3968 8715 8086 -935 -276 -93 N ATOM 1509 CA THR A 217 5.229 -14.185 37.948 1.00 54.20 C ANISOU 1509 CA THR A 217 3803 8684 8106 -1003 -266 -148 C ATOM 1510 C THR A 217 3.923 -13.957 37.169 1.00 57.69 C ANISOU 1510 C THR A 217 4227 9171 8520 -979 -225 -105 C ATOM 1511 O THR A 217 3.975 -13.794 35.951 1.00 57.06 O ANISOU 1511 O THR A 217 4118 9120 8442 -1031 -214 -153 O ATOM 1512 CB THR A 217 5.546 -15.689 38.120 1.00 62.92 C ANISOU 1512 CB THR A 217 4793 9776 9338 -1030 -284 -168 C ATOM 1513 OG1 THR A 217 5.503 -16.094 39.474 1.00 63.60 O ANISOU 1513 OG1 THR A 217 4856 9857 9452 -965 -279 -87 O ATOM 1514 CG2 THR A 217 6.898 -16.116 37.488 1.00 61.42 C ANISOU 1514 CG2 THR A 217 4596 9555 9187 -1074 -320 -220 C ATOM 1515 N PHE A 218 2.765 -13.912 37.874 1.00 54.06 N ANISOU 1515 N PHE A 218 3785 8724 8029 -897 -201 -8 N ATOM 1516 CA PHE A 218 1.457 -13.657 37.263 1.00 53.74 C ANISOU 1516 CA PHE A 218 3725 8733 7959 -868 -163 56 C ATOM 1517 C PHE A 218 1.384 -12.235 36.704 1.00 57.40 C ANISOU 1517 C PHE A 218 4283 9215 8312 -865 -136 43 C ATOM 1518 O PHE A 218 0.809 -12.033 35.636 1.00 56.79 O ANISOU 1518 O PHE A 218 4169 9180 8227 -895 -116 39 O ATOM 1519 CB PHE A 218 0.309 -13.875 38.267 1.00 55.74 C ANISOU 1519 CB PHE A 218 3981 9002 8197 -768 -138 182 C ATOM 1520 CG PHE A 218 0.099 -15.264 38.822 1.00 57.37 C ANISOU 1520 CG PHE A 218 4083 9199 8515 -764 -158 223 C ATOM 1521 CD1 PHE A 218 0.542 -16.385 38.129 1.00 60.28 C ANISOU 1521 CD1 PHE A 218 4353 9551 9002 -849 -193 151 C ATOM 1522 CD2 PHE A 218 -0.621 -15.454 39.997 1.00 59.80 C ANISOU 1522 CD2 PHE A 218 4392 9518 8810 -667 -138 342 C ATOM 1523 CE1 PHE A 218 0.333 -17.668 38.640 1.00 61.26 C ANISOU 1523 CE1 PHE A 218 4384 9658 9233 -845 -213 192 C ATOM 1524 CE2 PHE A 218 -0.842 -16.737 40.501 1.00 62.65 C ANISOU 1524 CE2 PHE A 218 4650 9873 9281 -665 -157 391 C ATOM 1525 CZ PHE A 218 -0.362 -17.838 39.822 1.00 60.51 C ANISOU 1525 CZ PHE A 218 4285 9576 9132 -757 -196 314 C ATOM 1526 N VAL A 219 1.972 -11.258 37.428 1.00 54.11 N ANISOU 1526 N VAL A 219 3988 8761 7812 -833 -143 35 N ATOM 1527 CA VAL A 219 1.996 -9.840 37.059 1.00 54.03 C ANISOU 1527 CA VAL A 219 4088 8748 7694 -825 -125 24 C ATOM 1528 C VAL A 219 2.862 -9.649 35.791 1.00 57.14 C ANISOU 1528 C VAL A 219 4445 9149 8117 -930 -144 -73 C ATOM 1529 O VAL A 219 2.368 -9.054 34.834 1.00 56.73 O ANISOU 1529 O VAL A 219 4394 9135 8025 -944 -114 -73 O ATOM 1530 CB VAL A 219 2.471 -8.934 38.236 1.00 58.55 C ANISOU 1530 CB VAL A 219 4809 9261 8177 -766 -144 38 C ATOM 1531 CG1 VAL A 219 2.678 -7.483 37.789 1.00 58.64 C ANISOU 1531 CG1 VAL A 219 4943 9248 8088 -778 -142 10 C ATOM 1532 CG2 VAL A 219 1.490 -8.995 39.406 1.00 58.67 C ANISOU 1532 CG2 VAL A 219 4871 9281 8141 -642 -110 144 C ATOM 1533 N VAL A 220 4.116 -10.181 35.766 1.00 52.99 N ANISOU 1533 N VAL A 220 3879 8595 7659 -998 -188 -146 N ATOM 1534 CA VAL A 220 5.020 -10.048 34.610 1.00 52.53 C ANISOU 1534 CA VAL A 220 3781 8549 7629 -1088 -201 -228 C ATOM 1535 C VAL A 220 4.440 -10.793 33.377 1.00 55.18 C ANISOU 1535 C VAL A 220 4007 8940 8017 -1121 -175 -251 C ATOM 1536 O VAL A 220 4.696 -10.359 32.253 1.00 54.60 O ANISOU 1536 O VAL A 220 3923 8898 7927 -1169 -164 -295 O ATOM 1537 CB VAL A 220 6.499 -10.458 34.871 1.00 56.84 C ANISOU 1537 CB VAL A 220 4299 9059 8238 -1145 -249 -285 C ATOM 1538 CG1 VAL A 220 7.164 -9.527 35.887 1.00 57.02 C ANISOU 1538 CG1 VAL A 220 4437 9026 8201 -1128 -288 -265 C ATOM 1539 CG2 VAL A 220 6.642 -11.919 35.286 1.00 56.64 C ANISOU 1539 CG2 VAL A 220 4166 9032 8323 -1152 -259 -297 C ATOM 1540 N MET A 221 3.640 -11.865 33.586 1.00 51.00 N ANISOU 1540 N MET A 221 3405 8423 7549 -1097 -170 -217 N ATOM 1541 CA MET A 221 2.983 -12.591 32.495 1.00 50.58 C ANISOU 1541 CA MET A 221 3262 8415 7543 -1130 -158 -231 C ATOM 1542 C MET A 221 1.866 -11.739 31.883 1.00 53.94 C ANISOU 1542 C MET A 221 3717 8890 7888 -1103 -122 -174 C ATOM 1543 O MET A 221 1.725 -11.729 30.664 1.00 53.66 O ANISOU 1543 O MET A 221 3634 8899 7857 -1145 -114 -203 O ATOM 1544 CB MET A 221 2.431 -13.946 32.954 1.00 53.04 C ANISOU 1544 CB MET A 221 3492 8714 7946 -1117 -175 -199 C ATOM 1545 CG MET A 221 3.474 -15.041 32.947 1.00 56.72 C ANISOU 1545 CG MET A 221 3895 9147 8511 -1164 -205 -275 C ATOM 1546 SD MET A 221 2.821 -16.707 33.217 1.00 61.22 S ANISOU 1546 SD MET A 221 4370 9698 9192 -1155 -226 -233 S ATOM 1547 CE MET A 221 2.432 -16.643 34.943 1.00 57.89 C ANISOU 1547 CE MET A 221 3981 9235 8780 -1089 -234 -166 C ATOM 1548 N VAL A 222 1.112 -10.997 32.723 1.00 49.60 N ANISOU 1548 N VAL A 222 3249 8335 7262 -1026 -98 -89 N ATOM 1549 CA VAL A 222 0.034 -10.098 32.293 1.00 49.00 C ANISOU 1549 CA VAL A 222 3210 8305 7101 -982 -54 -18 C ATOM 1550 C VAL A 222 0.662 -8.972 31.443 1.00 51.71 C ANISOU 1550 C VAL A 222 3617 8654 7377 -1018 -43 -73 C ATOM 1551 O VAL A 222 0.148 -8.678 30.367 1.00 51.37 O ANISOU 1551 O VAL A 222 3542 8665 7310 -1044 -21 -73 O ATOM 1552 CB VAL A 222 -0.795 -9.564 33.501 1.00 53.13 C ANISOU 1552 CB VAL A 222 3809 8817 7561 -872 -25 92 C ATOM 1553 CG1 VAL A 222 -1.625 -8.334 33.137 1.00 53.20 C ANISOU 1553 CG1 VAL A 222 3911 8849 7453 -816 24 149 C ATOM 1554 CG2 VAL A 222 -1.697 -10.654 34.071 1.00 53.03 C ANISOU 1554 CG2 VAL A 222 3707 8832 7609 -837 -21 180 C ATOM 1555 N VAL A 223 1.821 -8.420 31.890 1.00 47.24 N ANISOU 1555 N VAL A 223 3129 8034 6788 -1029 -66 -118 N ATOM 1556 CA VAL A 223 2.591 -7.371 31.204 1.00 46.48 C ANISOU 1556 CA VAL A 223 3094 7931 6637 -1069 -67 -164 C ATOM 1557 C VAL A 223 3.015 -7.872 29.801 1.00 50.80 C ANISOU 1557 C VAL A 223 3542 8524 7237 -1154 -71 -239 C ATOM 1558 O VAL A 223 2.908 -7.108 28.843 1.00 50.42 O ANISOU 1558 O VAL A 223 3507 8508 7141 -1180 -51 -252 O ATOM 1559 CB VAL A 223 3.811 -6.910 32.061 1.00 49.77 C ANISOU 1559 CB VAL A 223 3600 8273 7037 -1077 -109 -190 C ATOM 1560 CG1 VAL A 223 4.724 -5.958 31.293 1.00 49.45 C ANISOU 1560 CG1 VAL A 223 3606 8223 6961 -1135 -122 -234 C ATOM 1561 CG2 VAL A 223 3.349 -6.258 33.365 1.00 49.71 C ANISOU 1561 CG2 VAL A 223 3713 8220 6954 -983 -102 -121 C ATOM 1562 N LEU A 224 3.453 -9.146 29.685 1.00 48.00 N ANISOU 1562 N LEU A 224 3092 8171 6975 -1188 -94 -283 N ATOM 1563 CA LEU A 224 3.869 -9.769 28.422 1.00 48.32 C ANISOU 1563 CA LEU A 224 3044 8249 7068 -1253 -98 -358 C ATOM 1564 C LEU A 224 2.741 -9.763 27.386 1.00 53.90 C ANISOU 1564 C LEU A 224 3709 9023 7748 -1259 -71 -342 C ATOM 1565 O LEU A 224 2.984 -9.353 26.255 1.00 53.62 O ANISOU 1565 O LEU A 224 3659 9029 7685 -1297 -57 -384 O ATOM 1566 CB LEU A 224 4.359 -11.208 28.648 1.00 48.35 C ANISOU 1566 CB LEU A 224 2973 8225 7174 -1270 -127 -397 C ATOM 1567 CG LEU A 224 5.776 -11.342 29.205 1.00 53.04 C ANISOU 1567 CG LEU A 224 3520 8813 7821 -1322 -143 -480 C ATOM 1568 CD1 LEU A 224 5.929 -12.662 29.975 1.00 53.18 C ANISOU 1568 CD1 LEU A 224 3514 8776 7916 -1316 -173 -489 C ATOM 1569 CD2 LEU A 224 6.834 -11.220 28.093 1.00 55.97 C ANISOU 1569 CD2 LEU A 224 3818 9228 8219 -1355 -133 -537 C ATOM 1570 N TYR A 225 1.521 -10.205 27.768 1.00 51.69 N ANISOU 1570 N TYR A 225 3407 8758 7475 -1222 -64 -273 N ATOM 1571 CA TYR A 225 0.364 -10.235 26.867 1.00 52.36 C ANISOU 1571 CA TYR A 225 3446 8909 7539 -1230 -48 -240 C ATOM 1572 C TYR A 225 -0.179 -8.826 26.616 1.00 57.89 C ANISOU 1572 C TYR A 225 4206 9651 8139 -1201 -6 -184 C ATOM 1573 O TYR A 225 -0.623 -8.547 25.498 1.00 57.55 O ANISOU 1573 O TYR A 225 4128 9671 8069 -1230 8 -187 O ATOM 1574 CB TYR A 225 -0.759 -11.143 27.392 1.00 53.86 C ANISOU 1574 CB TYR A 225 3588 9103 7773 -1201 -59 -161 C ATOM 1575 CG TYR A 225 -0.361 -12.600 27.503 1.00 56.00 C ANISOU 1575 CG TYR A 225 3785 9342 8151 -1240 -104 -213 C ATOM 1576 CD1 TYR A 225 -0.282 -13.412 26.373 1.00 58.17 C ANISOU 1576 CD1 TYR A 225 4003 9636 8463 -1305 -128 -293 C ATOM 1577 CD2 TYR A 225 -0.100 -13.176 28.740 1.00 56.78 C ANISOU 1577 CD2 TYR A 225 3875 9390 8310 -1207 -122 -178 C ATOM 1578 CE1 TYR A 225 0.087 -14.754 26.473 1.00 58.57 C ANISOU 1578 CE1 TYR A 225 3998 9646 8609 -1337 -169 -344 C ATOM 1579 CE2 TYR A 225 0.272 -14.514 28.851 1.00 57.74 C ANISOU 1579 CE2 TYR A 225 3930 9476 8534 -1242 -162 -223 C ATOM 1580 CZ TYR A 225 0.354 -15.302 27.717 1.00 63.50 C ANISOU 1580 CZ TYR A 225 4611 10216 9301 -1306 -186 -306 C ATOM 1581 OH TYR A 225 0.718 -16.618 27.839 1.00 62.62 O ANISOU 1581 OH TYR A 225 4445 10058 9287 -1335 -226 -353 O ATOM 1582 N ALA A 226 -0.125 -7.933 27.638 1.00 55.81 N ANISOU 1582 N ALA A 226 4037 9351 7819 -1141 15 -130 N ATOM 1583 CA ALA A 226 -0.563 -6.535 27.517 1.00 56.47 C ANISOU 1583 CA ALA A 226 4196 9456 7803 -1101 58 -74 C ATOM 1584 C ALA A 226 0.294 -5.783 26.500 1.00 61.92 C ANISOU 1584 C ALA A 226 4896 10167 8466 -1159 62 -142 C ATOM 1585 O ALA A 226 -0.221 -4.902 25.809 1.00 61.53 O ANISOU 1585 O ALA A 226 4849 10171 8358 -1156 96 -110 O ATOM 1586 CB ALA A 226 -0.500 -5.839 28.861 1.00 57.34 C ANISOU 1586 CB ALA A 226 4424 9503 7861 -1026 68 -25 C ATOM 1587 N HIS A 227 1.595 -6.158 26.398 1.00 59.61 N ANISOU 1587 N HIS A 227 4598 9836 8217 -1210 28 -227 N ATOM 1588 CA HIS A 227 2.549 -5.605 25.437 1.00 60.08 C ANISOU 1588 CA HIS A 227 4651 9915 8263 -1266 29 -286 C ATOM 1589 C HIS A 227 2.212 -6.102 24.023 1.00 64.97 C ANISOU 1589 C HIS A 227 5179 10615 8891 -1306 42 -321 C ATOM 1590 O HIS A 227 2.410 -5.364 23.055 1.00 64.79 O ANISOU 1590 O HIS A 227 5158 10641 8818 -1325 67 -323 O ATOM 1591 CB HIS A 227 3.995 -5.984 25.818 1.00 60.94 C ANISOU 1591 CB HIS A 227 4752 9972 8429 -1307 -11 -353 C ATOM 1592 CG HIS A 227 5.045 -5.335 24.964 1.00 64.46 C ANISOU 1592 CG HIS A 227 5186 10441 8865 -1360 -10 -395 C ATOM 1593 ND1 HIS A 227 5.546 -5.959 23.835 1.00 66.29 N ANISOU 1593 ND1 HIS A 227 5327 10726 9135 -1403 -6 -458 N ATOM 1594 CD2 HIS A 227 5.635 -4.124 25.091 1.00 66.37 C ANISOU 1594 CD2 HIS A 227 5498 10661 9059 -1373 -11 -376 C ATOM 1595 CE1 HIS A 227 6.428 -5.117 23.320 1.00 65.92 C ANISOU 1595 CE1 HIS A 227 5287 10695 9064 -1435 0 -467 C ATOM 1596 NE2 HIS A 227 6.515 -3.999 24.038 1.00 66.30 N ANISOU 1596 NE2 HIS A 227 5428 10697 9066 -1425 -7 -417 N ATOM 1597 N ILE A 228 1.702 -7.352 23.914 1.00 62.03 N ANISOU 1597 N ILE A 228 4732 10254 8581 -1319 22 -345 N ATOM 1598 CA ILE A 228 1.315 -7.976 22.648 1.00 62.36 C ANISOU 1598 CA ILE A 228 4697 10362 8636 -1358 19 -386 C ATOM 1599 C ILE A 228 0.004 -7.333 22.152 1.00 67.42 C ANISOU 1599 C ILE A 228 5338 11069 9211 -1338 48 -307 C ATOM 1600 O ILE A 228 -0.022 -6.797 21.041 1.00 67.29 O ANISOU 1600 O ILE A 228 5298 11117 9153 -1366 64 -328 O ATOM 1601 CB ILE A 228 1.205 -9.531 22.781 1.00 65.56 C ANISOU 1601 CB ILE A 228 5040 10741 9129 -1375 -21 -427 C ATOM 1602 CG1 ILE A 228 2.594 -10.169 23.069 1.00 65.91 C ANISOU 1602 CG1 ILE A 228 5080 10726 9237 -1390 -42 -499 C ATOM 1603 CG2 ILE A 228 0.598 -10.151 21.504 1.00 66.84 C ANISOU 1603 CG2 ILE A 228 5140 10960 9297 -1416 -34 -470 C ATOM 1604 CD1 ILE A 228 2.565 -11.575 23.697 1.00 73.80 C ANISOU 1604 CD1 ILE A 228 6038 11674 10329 -1390 -78 -520 C ATOM 1605 N PHE A 229 -1.065 -7.370 22.982 1.00 64.73 N ANISOU 1605 N PHE A 229 5023 10716 8854 -1285 59 -211 N ATOM 1606 CA PHE A 229 -2.382 -6.813 22.658 1.00 65.16 C ANISOU 1606 CA PHE A 229 5074 10836 8847 -1257 93 -116 C ATOM 1607 C PHE A 229 -2.314 -5.309 22.376 1.00 69.20 C ANISOU 1607 C PHE A 229 5653 11368 9274 -1237 138 -93 C ATOM 1608 O PHE A 229 -3.014 -4.836 21.484 1.00 68.70 O ANISOU 1608 O PHE A 229 5563 11377 9162 -1250 162 -69 O ATOM 1609 CB PHE A 229 -3.403 -7.079 23.777 1.00 67.25 C ANISOU 1609 CB PHE A 229 5349 11087 9115 -1191 102 -4 C ATOM 1610 CG PHE A 229 -3.960 -8.482 23.811 1.00 69.26 C ANISOU 1610 CG PHE A 229 5518 11353 9447 -1217 59 12 C ATOM 1611 CD1 PHE A 229 -4.911 -8.893 22.887 1.00 72.86 C ANISOU 1611 CD1 PHE A 229 5901 11882 9900 -1252 47 50 C ATOM 1612 CD2 PHE A 229 -3.575 -9.375 24.801 1.00 71.57 C ANISOU 1612 CD2 PHE A 229 5800 11579 9814 -1208 27 -5 C ATOM 1613 CE1 PHE A 229 -5.437 -10.187 22.930 1.00 74.10 C ANISOU 1613 CE1 PHE A 229 5982 12040 10133 -1286 -5 67 C ATOM 1614 CE2 PHE A 229 -4.099 -10.666 24.842 1.00 74.66 C ANISOU 1614 CE2 PHE A 229 6111 11973 10282 -1236 -17 14 C ATOM 1615 CZ PHE A 229 -5.032 -11.062 23.911 1.00 73.05 C ANISOU 1615 CZ PHE A 229 5841 11835 10078 -1277 -36 50 C ATOM 1616 N GLY A 230 -1.470 -4.594 23.120 1.00 66.11 N ANISOU 1616 N GLY A 230 5345 10906 8866 -1211 144 -103 N ATOM 1617 CA GLY A 230 -1.246 -3.161 22.957 1.00 66.22 C ANISOU 1617 CA GLY A 230 5440 10912 8808 -1194 177 -84 C ATOM 1618 C GLY A 230 -0.626 -2.819 21.620 1.00 70.58 C ANISOU 1618 C GLY A 230 5954 11517 9346 -1254 183 -141 C ATOM 1619 O GLY A 230 -1.048 -1.858 20.974 1.00 69.95 O ANISOU 1619 O GLY A 230 5895 11483 9201 -1242 222 -95 O ATOM 1620 N TYR A 231 0.361 -3.632 21.191 1.00 67.71 N ANISOU 1620 N TYR A 231 5533 11153 9041 -1312 150 -234 N ATOM 1621 CA TYR A 231 1.052 -3.478 19.913 1.00 68.04 C ANISOU 1621 CA TYR A 231 5530 11250 9071 -1362 158 -290 C ATOM 1622 C TYR A 231 0.111 -3.844 18.743 1.00 72.83 C ANISOU 1622 C TYR A 231 6070 11955 9647 -1375 175 -281 C ATOM 1623 O TYR A 231 0.133 -3.149 17.728 1.00 72.56 O ANISOU 1623 O TYR A 231 6031 11981 9558 -1384 205 -267 O ATOM 1624 CB TYR A 231 2.345 -4.324 19.882 1.00 69.36 C ANISOU 1624 CB TYR A 231 5655 11392 9307 -1404 124 -382 C ATOM 1625 CG TYR A 231 3.038 -4.382 18.532 1.00 71.73 C ANISOU 1625 CG TYR A 231 5889 11765 9599 -1444 135 -442 C ATOM 1626 CD1 TYR A 231 3.668 -3.259 17.996 1.00 74.00 C ANISOU 1626 CD1 TYR A 231 6186 12092 9837 -1456 164 -425 C ATOM 1627 CD2 TYR A 231 3.100 -5.569 17.811 1.00 72.83 C ANISOU 1627 CD2 TYR A 231 5962 11930 9779 -1464 116 -514 C ATOM 1628 CE1 TYR A 231 4.296 -3.308 16.748 1.00 75.62 C ANISOU 1628 CE1 TYR A 231 6330 12374 10028 -1481 180 -473 C ATOM 1629 CE2 TYR A 231 3.756 -5.638 16.581 1.00 74.16 C ANISOU 1629 CE2 TYR A 231 6082 12167 9930 -1487 130 -571 C ATOM 1630 CZ TYR A 231 4.335 -4.502 16.043 1.00 82.03 C ANISOU 1630 CZ TYR A 231 7082 13213 10872 -1493 165 -548 C ATOM 1631 OH TYR A 231 4.933 -4.582 14.808 1.00 83.52 O ANISOU 1631 OH TYR A 231 7221 13477 11036 -1506 184 -596 O ATOM 1632 N VAL A 232 -0.724 -4.903 18.897 1.00 69.86 N ANISOU 1632 N VAL A 232 5644 11593 9306 -1379 150 -282 N ATOM 1633 CA VAL A 232 -1.688 -5.350 17.879 1.00 70.21 C ANISOU 1633 CA VAL A 232 5627 11725 9326 -1400 148 -271 C ATOM 1634 C VAL A 232 -2.728 -4.227 17.697 1.00 74.46 C ANISOU 1634 C VAL A 232 6189 12312 9792 -1362 192 -157 C ATOM 1635 O VAL A 232 -3.083 -3.914 16.558 1.00 74.12 O ANISOU 1635 O VAL A 232 6109 12354 9698 -1380 208 -142 O ATOM 1636 CB VAL A 232 -2.321 -6.737 18.223 1.00 74.57 C ANISOU 1636 CB VAL A 232 6128 12262 9942 -1419 99 -288 C ATOM 1637 CG1 VAL A 232 -3.491 -7.085 17.300 1.00 74.85 C ANISOU 1637 CG1 VAL A 232 6109 12382 9949 -1444 86 -251 C ATOM 1638 CG2 VAL A 232 -1.271 -7.848 18.168 1.00 74.50 C ANISOU 1638 CG2 VAL A 232 6095 12214 9996 -1454 63 -406 C ATOM 1639 N ALA A1001 -3.130 -3.570 18.813 1.00 71.34 N ANISOU 1639 N ALA A1001 5857 11864 9385 -1302 214 -77 N ATOM 1640 CA ALA A1001 -4.072 -2.447 18.827 1.00 71.38 C ANISOU 1640 CA ALA A1001 5899 11903 9318 -1246 265 39 C ATOM 1641 C ALA A1001 -3.543 -1.280 17.997 1.00 75.68 C ANISOU 1641 C ALA A1001 6469 12484 9800 -1254 303 36 C ATOM 1642 O ALA A1001 -4.293 -0.735 17.192 1.00 75.62 O ANISOU 1642 O ALA A1001 6434 12558 9740 -1248 335 98 O ATOM 1643 CB ALA A1001 -4.335 -1.995 20.254 1.00 71.98 C ANISOU 1643 CB ALA A1001 6061 11900 9387 -1171 283 105 C ATOM 1644 N ASP A1002 -2.246 -0.931 18.159 1.00 72.29 N ANISOU 1644 N ASP A1002 6083 12000 9383 -1275 296 -32 N ATOM 1645 CA ASP A1002 -1.594 0.155 17.424 1.00 72.28 C ANISOU 1645 CA ASP A1002 6103 12024 9335 -1290 326 -36 C ATOM 1646 C ASP A1002 -1.443 -0.182 15.938 1.00 75.97 C ANISOU 1646 C ASP A1002 6480 12593 9793 -1343 325 -85 C ATOM 1647 O ASP A1002 -1.499 0.733 15.117 1.00 75.70 O ANISOU 1647 O ASP A1002 6441 12618 9703 -1343 362 -50 O ATOM 1648 CB ASP A1002 -0.222 0.486 18.031 1.00 74.23 C ANISOU 1648 CB ASP A1002 6411 12184 9610 -1307 305 -87 C ATOM 1649 CG ASP A1002 -0.278 1.339 19.287 1.00 85.73 C ANISOU 1649 CG ASP A1002 7985 13539 11050 -1253 307 -36 C ATOM 1650 OD1 ASP A1002 -0.928 0.915 20.268 1.00 86.20 O1- ANISOU 1650 OD1 ASP A1002 8067 13568 11119 -1206 303 -1 O1- ATOM 1651 OD2 ASP A1002 0.365 2.411 19.303 1.00 92.36 O ANISOU 1651 OD2 ASP A1002 8897 14327 11869 -1258 308 -31 O ATOM 1652 N LEU A1003 -1.268 -1.479 15.592 1.00 72.49 N ANISOU 1652 N LEU A1003 5972 12168 9402 -1382 283 -164 N ATOM 1653 CA LEU A1003 -1.142 -1.925 14.199 1.00 72.69 C ANISOU 1653 CA LEU A1003 5924 12283 9410 -1425 277 -222 C ATOM 1654 C LEU A1003 -2.462 -1.770 13.457 1.00 76.51 C ANISOU 1654 C LEU A1003 6371 12861 9839 -1422 292 -154 C ATOM 1655 O LEU A1003 -2.497 -1.167 12.385 1.00 76.15 O ANISOU 1655 O LEU A1003 6303 12895 9736 -1432 321 -141 O ATOM 1656 CB LEU A1003 -0.677 -3.389 14.097 1.00 72.89 C ANISOU 1656 CB LEU A1003 5907 12290 9500 -1458 226 -321 C ATOM 1657 CG LEU A1003 0.712 -3.766 14.599 1.00 77.64 C ANISOU 1657 CG LEU A1003 6518 12823 10157 -1469 210 -399 C ATOM 1658 CD1 LEU A1003 0.859 -5.269 14.624 1.00 78.05 C ANISOU 1658 CD1 LEU A1003 6535 12850 10271 -1489 164 -479 C ATOM 1659 CD2 LEU A1003 1.824 -3.123 13.763 1.00 80.20 C ANISOU 1659 CD2 LEU A1003 6827 13195 10452 -1484 238 -434 C ATOM 1660 N GLU A1004 -3.545 -2.312 14.041 1.00 73.12 N ANISOU 1660 N GLU A1004 5930 12424 9428 -1409 271 -100 N ATOM 1661 CA GLU A1004 -4.900 -2.273 13.495 1.00 73.37 C ANISOU 1661 CA GLU A1004 5918 12542 9418 -1408 276 -14 C ATOM 1662 C GLU A1004 -5.410 -0.833 13.407 1.00 76.63 C ANISOU 1662 C GLU A1004 6364 12992 9759 -1361 344 93 C ATOM 1663 O GLU A1004 -6.124 -0.518 12.458 1.00 76.39 O ANISOU 1663 O GLU A1004 6291 13059 9675 -1371 360 142 O ATOM 1664 CB GLU A1004 -5.847 -3.131 14.343 1.00 75.00 C ANISOU 1664 CB GLU A1004 6106 12718 9671 -1397 242 42 C ATOM 1665 CG GLU A1004 -5.522 -4.617 14.300 1.00 87.48 C ANISOU 1665 CG GLU A1004 7653 14258 11326 -1446 172 -57 C ATOM 1666 CD GLU A1004 -6.226 -5.468 15.338 1.00113.76 C ANISOU 1666 CD GLU A1004 10969 17536 14717 -1432 138 -2 C ATOM 1667 OE1 GLU A1004 -6.199 -5.101 16.536 1.00112.77 O ANISOU 1667 OE1 GLU A1004 10893 17348 14606 -1375 166 51 O ATOM 1668 OE2 GLU A1004 -6.755 -6.538 14.961 1.00110.16 O1- ANISOU 1668 OE2 GLU A1004 10458 17100 14297 -1480 79 -14 O1- ATOM 1669 N ASP A1005 -5.019 0.038 14.373 1.00 72.63 N ANISOU 1669 N ASP A1005 5940 12405 9251 -1309 378 125 N ATOM 1670 CA ASP A1005 -5.357 1.468 14.422 1.00 72.35 C ANISOU 1670 CA ASP A1005 5963 12376 9152 -1256 443 217 C ATOM 1671 C ASP A1005 -4.699 2.200 13.247 1.00 76.15 C ANISOU 1671 C ASP A1005 6429 12913 9594 -1288 466 182 C ATOM 1672 O ASP A1005 -5.363 2.986 12.572 1.00 75.73 O ANISOU 1672 O ASP A1005 6363 12931 9479 -1269 510 260 O ATOM 1673 CB ASP A1005 -4.923 2.087 15.772 1.00 73.91 C ANISOU 1673 CB ASP A1005 6269 12453 9361 -1201 456 234 C ATOM 1674 CG ASP A1005 -4.692 3.592 15.777 1.00 84.04 C ANISOU 1674 CG ASP A1005 7639 13703 10589 -1162 506 280 C ATOM 1675 OD1 ASP A1005 -5.643 4.342 15.458 1.00 85.18 O ANISOU 1675 OD1 ASP A1005 7789 13903 10674 -1119 559 379 O ATOM 1676 OD2 ASP A1005 -3.570 4.019 16.131 1.00 88.82 O1- ANISOU 1676 OD2 ASP A1005 8310 14222 11215 -1174 489 225 O1- ATOM 1677 N ASN A1006 -3.399 1.934 13.006 1.00 72.75 N ANISOU 1677 N ASN A1006 5992 12453 9198 -1333 438 76 N ATOM 1678 CA ASN A1006 -2.642 2.539 11.914 1.00 72.81 C ANISOU 1678 CA ASN A1006 5976 12515 9175 -1362 460 46 C ATOM 1679 C ASN A1006 -3.103 1.963 10.567 1.00 77.68 C ANISOU 1679 C ASN A1006 6503 13257 9756 -1395 454 26 C ATOM 1680 O ASN A1006 -3.058 2.674 9.561 1.00 77.34 O ANISOU 1680 O ASN A1006 6435 13293 9658 -1399 490 54 O ATOM 1681 CB ASN A1006 -1.143 2.345 12.122 1.00 72.30 C ANISOU 1681 CB ASN A1006 5922 12388 9161 -1393 433 -45 C ATOM 1682 CG ASN A1006 -0.577 3.126 13.293 1.00 89.29 C ANISOU 1682 CG ASN A1006 8168 14423 11336 -1371 434 -21 C ATOM 1683 OD1 ASN A1006 -1.026 4.232 13.630 1.00 80.94 O ANISOU 1683 OD1 ASN A1006 7177 13337 10238 -1333 468 60 O ATOM 1684 ND2 ASN A1006 0.447 2.574 13.926 1.00 80.28 N ANISOU 1684 ND2 ASN A1006 7037 13208 10256 -1394 393 -91 N ATOM 1685 N TRP A1007 -3.592 0.700 10.561 1.00 74.86 N ANISOU 1685 N TRP A1007 6102 12914 9426 -1420 406 -17 N ATOM 1686 CA TRP A1007 -4.145 0.053 9.367 1.00 75.26 C ANISOU 1686 CA TRP A1007 6082 13071 9442 -1456 383 -39 C ATOM 1687 C TRP A1007 -5.565 0.577 9.119 1.00 78.23 C ANISOU 1687 C TRP A1007 6436 13524 9765 -1438 407 84 C ATOM 1688 O TRP A1007 -6.022 0.584 7.975 1.00 78.39 O ANISOU 1688 O TRP A1007 6404 13651 9732 -1464 405 95 O ATOM 1689 CB TRP A1007 -4.133 -1.478 9.493 1.00 74.46 C ANISOU 1689 CB TRP A1007 5955 12941 9395 -1492 314 -126 C ATOM 1690 CG TRP A1007 -4.397 -2.182 8.195 1.00 76.39 C ANISOU 1690 CG TRP A1007 6146 13277 9600 -1536 279 -184 C ATOM 1691 CD1 TRP A1007 -5.591 -2.674 7.757 1.00 79.71 C ANISOU 1691 CD1 TRP A1007 6527 13761 9998 -1565 239 -145 C ATOM 1692 CD2 TRP A1007 -3.451 -2.423 7.141 1.00 76.66 C ANISOU 1692 CD2 TRP A1007 6166 13354 9608 -1553 279 -285 C ATOM 1693 NE1 TRP A1007 -5.446 -3.227 6.504 1.00 79.89 N ANISOU 1693 NE1 TRP A1007 6522 13855 9978 -1603 207 -227 N ATOM 1694 CE2 TRP A1007 -4.143 -3.084 6.100 1.00 81.30 C ANISOU 1694 CE2 TRP A1007 6717 14024 10149 -1589 237 -314 C ATOM 1695 CE3 TRP A1007 -2.079 -2.157 6.980 1.00 77.92 C ANISOU 1695 CE3 TRP A1007 6338 13490 9776 -1539 310 -348 C ATOM 1696 CZ2 TRP A1007 -3.510 -3.483 4.915 1.00 81.14 C ANISOU 1696 CZ2 TRP A1007 6685 14062 10084 -1601 229 -412 C ATOM 1697 CZ3 TRP A1007 -1.453 -2.553 5.806 1.00 79.97 C ANISOU 1697 CZ3 TRP A1007 6573 13815 9996 -1549 309 -432 C ATOM 1698 CH2 TRP A1007 -2.165 -3.209 4.790 1.00 81.24 C ANISOU 1698 CH2 TRP A1007 6709 14056 10103 -1574 271 -468 C ATOM 1699 N GLU A1008 -6.254 1.029 10.193 1.00 73.50 N ANISOU 1699 N GLU A1008 5878 12873 9177 -1389 431 183 N ATOM 1700 CA GLU A1008 -7.591 1.624 10.119 1.00 73.15 C ANISOU 1700 CA GLU A1008 5815 12894 9085 -1354 466 323 C ATOM 1701 C GLU A1008 -7.455 3.027 9.524 1.00 76.18 C ANISOU 1701 C GLU A1008 6219 13324 9403 -1325 535 381 C ATOM 1702 O GLU A1008 -8.200 3.370 8.606 1.00 76.00 O ANISOU 1702 O GLU A1008 6143 13410 9323 -1330 556 448 O ATOM 1703 CB GLU A1008 -8.267 1.648 11.508 1.00 74.30 C ANISOU 1703 CB GLU A1008 6005 12964 9260 -1295 478 409 C ATOM 1704 CG GLU A1008 -9.765 1.918 11.491 1.00 85.39 C ANISOU 1704 CG GLU A1008 7370 14444 10630 -1260 502 560 C ATOM 1705 CD GLU A1008 -10.505 1.613 12.783 1.00108.39 C ANISOU 1705 CD GLU A1008 10305 17299 13579 -1205 503 643 C ATOM 1706 OE1 GLU A1008 -10.053 2.060 13.862 1.00104.96 O ANISOU 1706 OE1 GLU A1008 9960 16764 13157 -1145 532 640 O ATOM 1707 OE2 GLU A1008 -11.565 0.951 12.707 1.00102.69 O1- ANISOU 1707 OE2 GLU A1008 9510 16636 12871 -1220 473 720 O1- ATOM 1708 N THR A1009 -6.447 3.804 10.003 1.00 71.83 N ANISOU 1708 N THR A1009 5741 12689 8862 -1300 565 352 N ATOM 1709 CA THR A1009 -6.108 5.159 9.544 1.00 71.41 C ANISOU 1709 CA THR A1009 5718 12653 8760 -1277 625 398 C ATOM 1710 C THR A1009 -5.731 5.116 8.053 1.00 74.85 C ANISOU 1710 C THR A1009 6078 13203 9160 -1326 623 354 C ATOM 1711 O THR A1009 -6.045 6.044 7.309 1.00 74.48 O ANISOU 1711 O THR A1009 6009 13236 9055 -1312 670 429 O ATOM 1712 CB THR A1009 -4.957 5.752 10.401 1.00 78.39 C ANISOU 1712 CB THR A1009 6694 13412 9679 -1263 629 358 C ATOM 1713 OG1 THR A1009 -5.164 5.472 11.787 1.00 76.75 O ANISOU 1713 OG1 THR A1009 6556 13099 9505 -1223 615 372 O ATOM 1714 CG2 THR A1009 -4.785 7.257 10.205 1.00 77.17 C ANISOU 1714 CG2 THR A1009 6591 13250 9481 -1232 687 427 C ATOM 1715 N LEU A1010 -5.072 4.021 7.633 1.00 71.22 N ANISOU 1715 N LEU A1010 5579 12749 8732 -1378 571 234 N ATOM 1716 CA LEU A1010 -4.635 3.763 6.267 1.00 71.35 C ANISOU 1716 CA LEU A1010 5531 12866 8713 -1418 562 171 C ATOM 1717 C LEU A1010 -5.843 3.627 5.329 1.00 75.96 C ANISOU 1717 C LEU A1010 6050 13578 9234 -1431 559 227 C ATOM 1718 O LEU A1010 -5.963 4.406 4.385 1.00 75.81 O ANISOU 1718 O LEU A1010 5999 13653 9153 -1428 598 271 O ATOM 1719 CB LEU A1010 -3.779 2.483 6.243 1.00 71.35 C ANISOU 1719 CB LEU A1010 5518 12828 8763 -1455 505 36 C ATOM 1720 CG LEU A1010 -3.031 2.175 4.952 1.00 76.56 C ANISOU 1720 CG LEU A1010 6130 13571 9388 -1481 500 -47 C ATOM 1721 CD1 LEU A1010 -1.548 2.433 5.116 1.00 76.56 C ANISOU 1721 CD1 LEU A1010 6148 13516 9425 -1477 517 -101 C ATOM 1722 CD2 LEU A1010 -3.260 0.738 4.526 1.00 79.46 C ANISOU 1722 CD2 LEU A1010 6469 13962 9760 -1515 436 -138 C ATOM 1723 N ASN A1011 -6.745 2.668 5.615 1.00 73.01 N ANISOU 1723 N ASN A1011 5655 13208 8878 -1449 509 237 N ATOM 1724 CA ASN A1011 -7.925 2.370 4.803 1.00 73.58 C ANISOU 1724 CA ASN A1011 5663 13396 8899 -1475 485 294 C ATOM 1725 C ASN A1011 -9.002 3.462 4.860 1.00 77.54 C ANISOU 1725 C ASN A1011 6153 13956 9354 -1432 546 455 C ATOM 1726 O ASN A1011 -9.678 3.666 3.850 1.00 77.65 O ANISOU 1726 O ASN A1011 6109 14091 9304 -1450 550 507 O ATOM 1727 CB ASN A1011 -8.542 1.043 5.222 1.00 75.31 C ANISOU 1727 CB ASN A1011 5862 13588 9164 -1513 407 269 C ATOM 1728 CG ASN A1011 -7.740 -0.145 4.761 1.00101.28 C ANISOU 1728 CG ASN A1011 9148 16858 12476 -1563 340 114 C ATOM 1729 OD1 ASN A1011 -7.971 -0.696 3.681 1.00 97.07 O ANISOU 1729 OD1 ASN A1011 8578 16407 11897 -1607 296 70 O ATOM 1730 ND2 ASN A1011 -6.764 -0.550 5.554 1.00 92.85 N ANISOU 1730 ND2 ASN A1011 8125 15680 11475 -1552 332 29 N ATOM 1731 N ASP A1012 -9.181 4.145 6.010 1.00 73.68 N ANISOU 1731 N ASP A1012 5721 13383 8890 -1371 592 535 N ATOM 1732 CA ASP A1012 -10.208 5.183 6.136 1.00 73.78 C ANISOU 1732 CA ASP A1012 5736 13441 8858 -1313 659 695 C ATOM 1733 C ASP A1012 -9.827 6.455 5.362 1.00 77.18 C ANISOU 1733 C ASP A1012 6174 13918 9233 -1292 726 726 C ATOM 1734 O ASP A1012 -10.680 6.991 4.652 1.00 77.17 O ANISOU 1734 O ASP A1012 6127 14020 9173 -1276 765 835 O ATOM 1735 CB ASP A1012 -10.509 5.520 7.608 1.00 75.62 C ANISOU 1735 CB ASP A1012 6045 13563 9125 -1241 693 766 C ATOM 1736 CG ASP A1012 -11.561 4.635 8.275 1.00 87.91 C ANISOU 1736 CG ASP A1012 7571 15118 10714 -1235 656 829 C ATOM 1737 OD1 ASP A1012 -11.972 3.620 7.658 1.00 88.69 O ANISOU 1737 OD1 ASP A1012 7597 15274 10829 -1304 584 788 O ATOM 1738 OD2 ASP A1012 -11.979 4.962 9.408 1.00 94.51 O1- ANISOU 1738 OD2 ASP A1012 8458 15893 11557 -1159 697 921 O1- ATOM 1739 N ASN A1013 -8.563 6.916 5.461 1.00 73.09 N ANISOU 1739 N ASN A1013 5705 13329 8735 -1295 739 641 N ATOM 1740 CA ASN A1013 -8.108 8.115 4.751 1.00 72.89 C ANISOU 1740 CA ASN A1013 5686 13339 8669 -1279 797 672 C ATOM 1741 C ASN A1013 -7.874 7.838 3.256 1.00 77.04 C ANISOU 1741 C ASN A1013 6127 13999 9147 -1328 784 627 C ATOM 1742 O ASN A1013 -7.783 8.792 2.481 1.00 76.80 O ANISOU 1742 O ASN A1013 6078 14033 9071 -1315 836 681 O ATOM 1743 CB ASN A1013 -6.861 8.702 5.389 1.00 72.70 C ANISOU 1743 CB ASN A1013 5742 13191 8689 -1269 808 616 C ATOM 1744 CG ASN A1013 -7.188 9.507 6.617 1.00 92.00 C ANISOU 1744 CG ASN A1013 8287 15523 11147 -1203 845 696 C ATOM 1745 OD1 ASN A1013 -7.477 8.966 7.692 1.00 85.03 O ANISOU 1745 OD1 ASN A1013 7446 14563 10297 -1181 821 692 O ATOM 1746 ND2 ASN A1013 -7.202 10.822 6.470 1.00 83.06 N ANISOU 1746 ND2 ASN A1013 7195 14382 9980 -1164 906 778 N ATOM 1747 N LEU A1014 -7.815 6.551 2.850 1.00 73.81 N ANISOU 1747 N LEU A1014 5670 13631 8742 -1381 715 533 N ATOM 1748 CA LEU A1014 -7.701 6.147 1.446 1.00 74.24 C ANISOU 1748 CA LEU A1014 5655 13814 8739 -1422 695 485 C ATOM 1749 C LEU A1014 -8.972 6.537 0.699 1.00 78.99 C ANISOU 1749 C LEU A1014 6198 14545 9270 -1419 714 606 C ATOM 1750 O LEU A1014 -8.896 7.071 -0.406 1.00 78.73 O ANISOU 1750 O LEU A1014 6122 14619 9173 -1420 746 631 O ATOM 1751 CB LEU A1014 -7.453 4.634 1.329 1.00 74.43 C ANISOU 1751 CB LEU A1014 5664 13829 8785 -1473 610 355 C ATOM 1752 CG LEU A1014 -6.027 4.182 1.033 1.00 79.17 C ANISOU 1752 CG LEU A1014 6282 14390 9410 -1484 597 219 C ATOM 1753 CD1 LEU A1014 -5.841 2.725 1.401 1.00 79.40 C ANISOU 1753 CD1 LEU A1014 6323 14358 9485 -1518 519 103 C ATOM 1754 CD2 LEU A1014 -5.666 4.403 -0.428 1.00 82.19 C ANISOU 1754 CD2 LEU A1014 6617 14895 9715 -1490 619 192 C ATOM 1755 N LYS A1015 -10.136 6.308 1.345 1.00 76.33 N ANISOU 1755 N LYS A1015 5856 14199 8947 -1410 699 693 N ATOM 1756 CA LYS A1015 -11.482 6.631 0.858 1.00 77.11 C ANISOU 1756 CA LYS A1015 5895 14413 8991 -1404 714 834 C ATOM 1757 C LYS A1015 -11.671 8.147 0.721 1.00 81.83 C ANISOU 1757 C LYS A1015 6502 15039 9549 -1340 814 960 C ATOM 1758 O LYS A1015 -12.386 8.600 -0.175 1.00 81.91 O ANISOU 1758 O LYS A1015 6450 15178 9495 -1340 839 1054 O ATOM 1759 CB LYS A1015 -12.549 6.068 1.818 1.00 79.91 C ANISOU 1759 CB LYS A1015 6246 14729 9386 -1397 683 911 C ATOM 1760 CG LYS A1015 -12.478 4.566 2.090 1.00 97.21 C ANISOU 1760 CG LYS A1015 8432 16876 11629 -1459 582 804 C ATOM 1761 CD LYS A1015 -13.445 4.171 3.208 1.00107.98 C ANISOU 1761 CD LYS A1015 9794 18192 13044 -1440 564 902 C ATOM 1762 CE LYS A1015 -13.325 2.721 3.608 1.00117.98 C ANISOU 1762 CE LYS A1015 11056 19398 14371 -1500 465 802 C ATOM 1763 NZ LYS A1015 -14.214 2.390 4.752 1.00126.15 N1+ ANISOU 1763 NZ LYS A1015 12083 20390 15460 -1475 453 910 N1+ ATOM 1764 N VAL A1016 -11.034 8.918 1.631 1.00 78.45 N ANISOU 1764 N VAL A1016 6158 14488 9162 -1287 866 964 N ATOM 1765 CA VAL A1016 -11.066 10.385 1.708 1.00 78.42 C ANISOU 1765 CA VAL A1016 6192 14472 9133 -1221 958 1072 C ATOM 1766 C VAL A1016 -10.363 10.984 0.465 1.00 82.72 C ANISOU 1766 C VAL A1016 6697 15098 9634 -1242 985 1046 C ATOM 1767 O VAL A1016 -10.920 11.888 -0.166 1.00 82.70 O ANISOU 1767 O VAL A1016 6662 15181 9578 -1212 1045 1159 O ATOM 1768 CB VAL A1016 -10.430 10.891 3.043 1.00 81.76 C ANISOU 1768 CB VAL A1016 6731 14721 9613 -1169 984 1060 C ATOM 1769 CG1 VAL A1016 -10.349 12.416 3.097 1.00 81.70 C ANISOU 1769 CG1 VAL A1016 6782 14680 9581 -1106 1069 1156 C ATOM 1770 CG2 VAL A1016 -11.187 10.357 4.257 1.00 81.36 C ANISOU 1770 CG2 VAL A1016 6715 14604 9594 -1135 968 1103 C ATOM 1771 N ILE A1017 -9.160 10.465 0.116 1.00 79.16 N ANISOU 1771 N ILE A1017 6245 14628 9206 -1288 944 906 N ATOM 1772 CA ILE A1017 -8.352 10.919 -1.025 1.00 79.31 C ANISOU 1772 CA ILE A1017 6222 14726 9187 -1303 968 877 C ATOM 1773 C ILE A1017 -9.100 10.627 -2.334 1.00 83.79 C ANISOU 1773 C ILE A1017 6696 15470 9671 -1329 957 910 C ATOM 1774 O ILE A1017 -9.219 11.524 -3.167 1.00 83.53 O ANISOU 1774 O ILE A1017 6624 15528 9585 -1308 1014 997 O ATOM 1775 CB ILE A1017 -6.929 10.283 -1.012 1.00 82.26 C ANISOU 1775 CB ILE A1017 6612 15041 9603 -1337 928 729 C ATOM 1776 CG1 ILE A1017 -6.145 10.735 0.244 1.00 82.23 C ANISOU 1776 CG1 ILE A1017 6699 14866 9678 -1316 937 712 C ATOM 1777 CG2 ILE A1017 -6.147 10.647 -2.285 1.00 83.47 C ANISOU 1777 CG2 ILE A1017 6707 15297 9709 -1345 957 713 C ATOM 1778 CD1 ILE A1017 -5.018 9.811 0.714 1.00 89.44 C ANISOU 1778 CD1 ILE A1017 7634 15697 10652 -1349 882 573 C ATOM 1779 N GLU A1018 -9.638 9.402 -2.482 1.00 81.09 N ANISOU 1779 N GLU A1018 6322 15171 9318 -1374 881 850 N ATOM 1780 CA GLU A1018 -10.396 8.937 -3.650 1.00 82.09 C ANISOU 1780 CA GLU A1018 6369 15455 9365 -1412 846 868 C ATOM 1781 C GLU A1018 -11.511 9.922 -4.063 1.00 86.87 C ANISOU 1781 C GLU A1018 6926 16164 9916 -1382 904 1042 C ATOM 1782 O GLU A1018 -11.721 10.120 -5.264 1.00 87.04 O ANISOU 1782 O GLU A1018 6882 16329 9860 -1398 909 1072 O ATOM 1783 CB GLU A1018 -11.008 7.558 -3.371 1.00 83.72 C ANISOU 1783 CB GLU A1018 6569 15651 9589 -1464 749 807 C ATOM 1784 CG GLU A1018 -9.995 6.427 -3.426 1.00 95.84 C ANISOU 1784 CG GLU A1018 8134 17132 11149 -1500 685 627 C ATOM 1785 CD GLU A1018 -10.399 5.121 -2.765 1.00121.23 C ANISOU 1785 CD GLU A1018 11369 20278 14415 -1544 593 559 C ATOM 1786 OE1 GLU A1018 -9.492 4.419 -2.261 1.00120.05 O ANISOU 1786 OE1 GLU A1018 11269 20020 14326 -1547 568 441 O ATOM 1787 OE2 GLU A1018 -11.611 4.804 -2.732 1.00115.90 O1- ANISOU 1787 OE2 GLU A1018 10656 19658 13723 -1576 546 631 O1- ATOM 1788 N LYS A1019 -12.194 10.553 -3.074 1.00 83.27 N ANISOU 1788 N LYS A1019 6505 15638 9497 -1331 952 1159 N ATOM 1789 CA LYS A1019 -13.266 11.530 -3.297 1.00 83.46 C ANISOU 1789 CA LYS A1019 6492 15744 9476 -1286 1020 1338 C ATOM 1790 C LYS A1019 -12.706 12.781 -3.993 1.00 87.42 C ANISOU 1790 C LYS A1019 6988 16288 9942 -1250 1102 1384 C ATOM 1791 O LYS A1019 -11.788 13.417 -3.467 1.00 86.34 O ANISOU 1791 O LYS A1019 6920 16038 9849 -1219 1142 1352 O ATOM 1792 CB LYS A1019 -13.946 11.901 -1.964 1.00 85.67 C ANISOU 1792 CB LYS A1019 6829 15918 9802 -1223 1060 1441 C ATOM 1793 CG LYS A1019 -15.231 12.709 -2.122 1.00100.60 C ANISOU 1793 CG LYS A1019 8674 17902 11646 -1170 1126 1638 C ATOM 1794 CD LYS A1019 -15.756 13.216 -0.782 1.00110.06 C ANISOU 1794 CD LYS A1019 9948 18988 12882 -1082 1187 1741 C ATOM 1795 CE LYS A1019 -17.097 13.911 -0.890 1.00120.29 C ANISOU 1795 CE LYS A1019 11193 20380 14130 -1020 1257 1948 C ATOM 1796 NZ LYS A1019 -17.026 15.184 -1.660 1.00128.95 N1+ ANISOU 1796 NZ LYS A1019 12269 21552 15173 -987 1337 2028 N1+ ATOM 1797 N ALA A1020 -13.249 13.103 -5.192 1.00 84.89 N ANISOU 1797 N ALA A1020 6581 16131 9541 -1261 1120 1461 N ATOM 1798 CA ALA A1020 -12.855 14.248 -6.020 1.00 85.04 C ANISOU 1798 CA ALA A1020 6573 16220 9518 -1230 1196 1524 C ATOM 1799 C ALA A1020 -13.183 15.574 -5.317 1.00 89.02 C ANISOU 1799 C ALA A1020 7126 16653 10044 -1150 1293 1669 C ATOM 1800 O ALA A1020 -14.296 16.100 -5.445 1.00 89.27 O ANISOU 1800 O ALA A1020 7120 16759 10041 -1114 1335 1819 O ATOM 1801 CB ALA A1020 -13.543 14.182 -7.376 1.00 86.52 C ANISOU 1801 CB ALA A1020 6656 16606 9611 -1260 1184 1581 C ATOM 1802 N ASP A1021 -12.203 16.090 -4.553 1.00 84.66 N ANISOU 1802 N ASP A1021 6664 15952 9552 -1121 1324 1624 N ATOM 1803 CA ASP A1021 -12.310 17.336 -3.791 1.00 84.04 C ANISOU 1803 CA ASP A1021 6664 15769 9499 -1045 1406 1733 C ATOM 1804 C ASP A1021 -11.188 18.319 -4.200 1.00 86.83 C ANISOU 1804 C ASP A1021 7040 16086 9866 -1039 1450 1725 C ATOM 1805 O ASP A1021 -10.670 18.233 -5.321 1.00 86.77 O ANISOU 1805 O ASP A1021 6951 16197 9821 -1074 1447 1700 O ATOM 1806 CB ASP A1021 -12.257 17.041 -2.276 1.00 85.28 C ANISOU 1806 CB ASP A1021 6932 15748 9722 -1018 1387 1692 C ATOM 1807 CG ASP A1021 -13.285 16.047 -1.768 1.00 94.78 C ANISOU 1807 CG ASP A1021 8114 16973 10925 -1023 1342 1706 C ATOM 1808 OD1 ASP A1021 -14.497 16.334 -1.881 1.00 96.11 O ANISOU 1808 OD1 ASP A1021 8241 17222 11054 -981 1383 1851 O ATOM 1809 OD2 ASP A1021 -12.877 15.017 -1.192 1.00 99.22 O1- ANISOU 1809 OD2 ASP A1021 8701 17466 11533 -1065 1269 1583 O1- ATOM 1810 N ASN A1022 -10.835 19.256 -3.297 1.00 81.99 N ANISOU 1810 N ASN A1022 6538 15310 9303 -993 1488 1750 N ATOM 1811 CA ASN A1022 -9.790 20.257 -3.507 1.00 81.31 C ANISOU 1811 CA ASN A1022 6487 15162 9246 -992 1521 1754 C ATOM 1812 C ASN A1022 -8.417 19.691 -3.119 1.00 82.36 C ANISOU 1812 C ASN A1022 6657 15194 9443 -1049 1453 1602 C ATOM 1813 O ASN A1022 -8.342 18.608 -2.534 1.00 81.12 O ANISOU 1813 O ASN A1022 6512 15000 9309 -1078 1389 1498 O ATOM 1814 CB ASN A1022 -10.101 21.535 -2.715 1.00 83.67 C ANISOU 1814 CB ASN A1022 6898 15330 9561 -916 1589 1865 C ATOM 1815 CG ASN A1022 -10.324 21.317 -1.239 1.00109.42 C ANISOU 1815 CG ASN A1022 10287 18423 12863 -879 1569 1834 C ATOM 1816 OD1 ASN A1022 -9.383 21.280 -0.444 1.00104.63 O ANISOU 1816 OD1 ASN A1022 9773 17667 12316 -900 1528 1745 O ATOM 1817 ND2 ASN A1022 -11.579 21.172 -0.846 1.00101.53 N ANISOU 1817 ND2 ASN A1022 9294 17451 11830 -821 1598 1915 N ATOM 1818 N ALA A1023 -7.338 20.425 -3.461 1.00 77.73 N ANISOU 1818 N ALA A1023 6079 14567 8888 -1065 1466 1599 N ATOM 1819 CA ALA A1023 -5.949 20.045 -3.185 1.00 76.62 C ANISOU 1819 CA ALA A1023 5958 14342 8810 -1119 1409 1481 C ATOM 1820 C ALA A1023 -5.654 19.971 -1.677 1.00 78.02 C ANISOU 1820 C ALA A1023 6269 14319 9056 -1114 1369 1426 C ATOM 1821 O ALA A1023 -4.913 19.082 -1.258 1.00 77.24 O ANISOU 1821 O ALA A1023 6178 14171 9000 -1157 1305 1307 O ATOM 1822 CB ALA A1023 -4.998 21.030 -3.845 1.00 77.83 C ANISOU 1822 CB ALA A1023 6083 14505 8984 -1133 1438 1529 C ATOM 1823 N ALA A1024 -6.234 20.892 -0.874 1.00 73.07 N ANISOU 1823 N ALA A1024 5752 13576 8435 -1057 1408 1512 N ATOM 1824 CA ALA A1024 -6.043 20.966 0.581 1.00 71.76 C ANISOU 1824 CA ALA A1024 5730 13216 8320 -1040 1375 1471 C ATOM 1825 C ALA A1024 -6.649 19.759 1.302 1.00 72.38 C ANISOU 1825 C ALA A1024 5817 13290 8396 -1033 1336 1402 C ATOM 1826 O ALA A1024 -6.129 19.346 2.340 1.00 71.29 O ANISOU 1826 O ALA A1024 5752 13027 8308 -1052 1280 1313 O ATOM 1827 CB ALA A1024 -6.657 22.247 1.122 1.00 72.98 C ANISOU 1827 CB ALA A1024 6002 13267 8460 -964 1436 1588 C ATOM 1828 N GLN A1025 -7.736 19.200 0.744 1.00 67.40 N ANISOU 1828 N GLN A1025 5102 12798 7707 -1012 1360 1448 N ATOM 1829 CA GLN A1025 -8.461 18.040 1.263 1.00 66.16 C ANISOU 1829 CA GLN A1025 4929 12665 7544 -1009 1324 1407 C ATOM 1830 C GLN A1025 -7.618 16.764 1.169 1.00 67.37 C ANISOU 1830 C GLN A1025 5032 12831 7733 -1085 1242 1256 C ATOM 1831 O GLN A1025 -7.765 15.869 1.999 1.00 66.10 O ANISOU 1831 O GLN A1025 4899 12616 7600 -1091 1195 1193 O ATOM 1832 CB GLN A1025 -9.765 17.858 0.465 1.00 68.05 C ANISOU 1832 CB GLN A1025 5067 13075 7714 -987 1362 1506 C ATOM 1833 CG GLN A1025 -10.854 17.044 1.174 1.00 87.31 C ANISOU 1833 CG GLN A1025 7505 15524 10144 -961 1345 1531 C ATOM 1834 CD GLN A1025 -11.803 17.874 2.014 1.00107.19 C ANISOU 1834 CD GLN A1025 10093 17997 12637 -861 1418 1676 C ATOM 1835 OE1 GLN A1025 -12.053 19.059 1.752 1.00102.94 O ANISOU 1835 OE1 GLN A1025 9593 17444 12074 -806 1491 1776 O ATOM 1836 NE2 GLN A1025 -12.415 17.240 3.006 1.00 98.20 N ANISOU 1836 NE2 GLN A1025 8968 16842 11503 -830 1404 1701 N ATOM 1837 N VAL A1026 -6.758 16.682 0.143 1.00 63.07 N ANISOU 1837 N VAL A1026 4414 12361 7188 -1136 1230 1205 N ATOM 1838 CA VAL A1026 -5.901 15.529 -0.144 1.00 62.35 C ANISOU 1838 CA VAL A1026 4270 12297 7121 -1198 1164 1069 C ATOM 1839 C VAL A1026 -4.600 15.595 0.699 1.00 65.49 C ANISOU 1839 C VAL A1026 4746 12540 7598 -1222 1126 992 C ATOM 1840 O VAL A1026 -4.114 14.545 1.134 1.00 65.16 O ANISOU 1840 O VAL A1026 4706 12457 7593 -1253 1068 883 O ATOM 1841 CB VAL A1026 -5.591 15.449 -1.670 1.00 66.68 C ANISOU 1841 CB VAL A1026 4705 13010 7622 -1227 1177 1063 C ATOM 1842 CG1 VAL A1026 -4.793 14.196 -2.021 1.00 66.42 C ANISOU 1842 CG1 VAL A1026 4624 13010 7602 -1275 1117 924 C ATOM 1843 CG2 VAL A1026 -6.871 15.509 -2.502 1.00 66.82 C ANISOU 1843 CG2 VAL A1026 4648 13182 7557 -1208 1210 1149 C ATOM 1844 N LYS A1027 -4.047 16.814 0.923 1.00 60.95 N ANISOU 1844 N LYS A1027 4231 11878 7048 -1210 1155 1053 N ATOM 1845 CA LYS A1027 -2.803 17.050 1.669 1.00 59.72 C ANISOU 1845 CA LYS A1027 4147 11577 6966 -1241 1114 1001 C ATOM 1846 C LYS A1027 -2.878 16.512 3.104 1.00 61.57 C ANISOU 1846 C LYS A1027 4484 11668 7242 -1232 1066 939 C ATOM 1847 O LYS A1027 -2.020 15.717 3.481 1.00 60.19 O ANISOU 1847 O LYS A1027 4304 11449 7116 -1274 1009 839 O ATOM 1848 CB LYS A1027 -2.442 18.545 1.703 1.00 62.52 C ANISOU 1848 CB LYS A1027 4565 11854 7336 -1229 1148 1096 C ATOM 1849 CG LYS A1027 -1.978 19.116 0.370 1.00 76.20 C ANISOU 1849 CG LYS A1027 6194 13707 9050 -1250 1184 1152 C ATOM 1850 CD LYS A1027 -1.421 20.524 0.539 1.00 86.68 C ANISOU 1850 CD LYS A1027 7591 14928 10414 -1253 1199 1237 C ATOM 1851 CE LYS A1027 -0.997 21.134 -0.775 1.00 96.84 C ANISOU 1851 CE LYS A1027 8770 16338 11687 -1270 1239 1308 C ATOM 1852 NZ LYS A1027 -0.260 22.412 -0.584 1.00104.90 N1+ ANISOU 1852 NZ LYS A1027 9854 17243 12762 -1290 1237 1385 N1+ ATOM 1853 N ASP A1028 -3.912 16.917 3.884 1.00 57.88 N ANISOU 1853 N ASP A1028 4104 11136 6751 -1170 1095 1003 N ATOM 1854 CA ASP A1028 -4.104 16.507 5.283 1.00 57.05 C ANISOU 1854 CA ASP A1028 4103 10898 6675 -1146 1059 961 C ATOM 1855 C ASP A1028 -4.377 15.000 5.411 1.00 58.73 C ANISOU 1855 C ASP A1028 4251 11167 6898 -1169 1014 873 C ATOM 1856 O ASP A1028 -3.961 14.396 6.403 1.00 58.52 O ANISOU 1856 O ASP A1028 4274 11040 6921 -1187 961 793 O ATOM 1857 CB ASP A1028 -5.239 17.300 5.955 1.00 59.30 C ANISOU 1857 CB ASP A1028 4487 11125 6918 -1058 1114 1065 C ATOM 1858 CG ASP A1028 -6.634 16.959 5.475 1.00 71.87 C ANISOU 1858 CG ASP A1028 6005 12850 8452 -1014 1160 1137 C ATOM 1859 OD1 ASP A1028 -6.983 17.351 4.343 1.00 73.17 O1- ANISOU 1859 OD1 ASP A1028 6085 13141 8574 -1013 1205 1206 O1- ATOM 1860 OD2 ASP A1028 -7.379 16.305 6.237 1.00 78.61 O ANISOU 1860 OD2 ASP A1028 6878 13685 9304 -982 1147 1131 O ATOM 1861 N ALA A1029 -5.074 14.403 4.424 1.00 53.20 N ANISOU 1861 N ALA A1029 3443 10620 6152 -1173 1031 889 N ATOM 1862 CA ALA A1029 -5.365 12.973 4.418 1.00 51.98 C ANISOU 1862 CA ALA A1029 3227 10518 6005 -1201 981 810 C ATOM 1863 C ALA A1029 -4.080 12.184 4.186 1.00 54.44 C ANISOU 1863 C ALA A1029 3501 10821 6364 -1264 926 683 C ATOM 1864 O ALA A1029 -3.836 11.214 4.900 1.00 53.20 O ANISOU 1864 O ALA A1029 3363 10601 6250 -1281 874 600 O ATOM 1865 CB ALA A1029 -6.403 12.644 3.360 1.00 52.96 C ANISOU 1865 CB ALA A1029 3249 10806 6066 -1201 1001 860 C ATOM 1866 N LEU A1030 -3.228 12.649 3.243 1.00 50.90 N ANISOU 1866 N LEU A1030 3003 10428 5908 -1291 941 678 N ATOM 1867 CA LEU A1030 -1.929 12.049 2.935 1.00 50.44 C ANISOU 1867 CA LEU A1030 2904 10371 5891 -1339 902 579 C ATOM 1868 C LEU A1030 -0.925 12.286 4.073 1.00 53.11 C ANISOU 1868 C LEU A1030 3329 10548 6304 -1353 867 547 C ATOM 1869 O LEU A1030 0.001 11.487 4.229 1.00 52.27 O ANISOU 1869 O LEU A1030 3202 10415 6244 -1388 823 458 O ATOM 1870 CB LEU A1030 -1.362 12.584 1.613 1.00 51.12 C ANISOU 1870 CB LEU A1030 2907 10572 5943 -1353 937 606 C ATOM 1871 CG LEU A1030 -1.829 11.895 0.330 1.00 56.31 C ANISOU 1871 CG LEU A1030 3463 11400 6534 -1359 943 577 C ATOM 1872 CD1 LEU A1030 -1.439 12.706 -0.889 1.00 57.05 C ANISOU 1872 CD1 LEU A1030 3486 11607 6584 -1357 993 635 C ATOM 1873 CD2 LEU A1030 -1.250 10.487 0.205 1.00 58.81 C ANISOU 1873 CD2 LEU A1030 3748 11726 6870 -1387 889 445 C ATOM 1874 N THR A1031 -1.107 13.370 4.868 1.00 49.12 N ANISOU 1874 N THR A1031 2924 9933 5807 -1325 885 622 N ATOM 1875 CA THR A1031 -0.261 13.660 6.035 1.00 48.42 C ANISOU 1875 CA THR A1031 2938 9679 5780 -1339 843 599 C ATOM 1876 C THR A1031 -0.632 12.649 7.127 1.00 50.64 C ANISOU 1876 C THR A1031 3273 9888 6082 -1321 805 540 C ATOM 1877 O THR A1031 0.250 12.143 7.821 1.00 49.97 O ANISOU 1877 O THR A1031 3227 9705 6053 -1348 752 474 O ATOM 1878 CB THR A1031 -0.397 15.126 6.499 1.00 56.41 C ANISOU 1878 CB THR A1031 4054 10595 6784 -1311 871 694 C ATOM 1879 OG1 THR A1031 -0.371 15.996 5.368 1.00 56.83 O ANISOU 1879 OG1 THR A1031 4044 10746 6802 -1312 922 770 O ATOM 1880 CG2 THR A1031 0.703 15.536 7.482 1.00 53.93 C ANISOU 1880 CG2 THR A1031 3830 10126 6534 -1349 814 671 C ATOM 1881 N LYS A1032 -1.942 12.327 7.236 1.00 46.02 N ANISOU 1881 N LYS A1032 2679 9356 5452 -1276 832 574 N ATOM 1882 CA LYS A1032 -2.470 11.325 8.161 1.00 45.01 C ANISOU 1882 CA LYS A1032 2579 9183 5339 -1255 803 537 C ATOM 1883 C LYS A1032 -2.068 9.917 7.699 1.00 48.33 C ANISOU 1883 C LYS A1032 2906 9670 5788 -1304 756 432 C ATOM 1884 O LYS A1032 -1.942 9.024 8.534 1.00 47.50 O ANISOU 1884 O LYS A1032 2824 9501 5723 -1307 713 374 O ATOM 1885 CB LYS A1032 -3.995 11.438 8.293 1.00 47.26 C ANISOU 1885 CB LYS A1032 2874 9513 5570 -1192 849 631 C ATOM 1886 CG LYS A1032 -4.473 12.483 9.289 1.00 59.01 C ANISOU 1886 CG LYS A1032 4497 10878 7046 -1120 876 702 C ATOM 1887 CD LYS A1032 -5.966 12.318 9.533 1.00 69.53 C ANISOU 1887 CD LYS A1032 5819 12266 8331 -1051 919 795 C ATOM 1888 CE LYS A1032 -6.466 13.089 10.726 1.00 79.85 C ANISOU 1888 CE LYS A1032 7263 13454 9624 -964 946 858 C ATOM 1889 NZ LYS A1032 -7.882 12.760 11.034 1.00 87.94 N1+ ANISOU 1889 NZ LYS A1032 8260 14547 10608 -893 990 960 N1+ ATOM 1890 N MET A1033 -1.874 9.724 6.371 1.00 45.20 N ANISOU 1890 N MET A1033 2409 9398 5365 -1336 766 410 N ATOM 1891 CA MET A1033 -1.442 8.463 5.751 1.00 44.98 C ANISOU 1891 CA MET A1033 2300 9438 5351 -1376 727 307 C ATOM 1892 C MET A1033 0.019 8.165 6.097 1.00 48.69 C ANISOU 1892 C MET A1033 2781 9831 5888 -1409 690 227 C ATOM 1893 O MET A1033 0.343 7.031 6.453 1.00 47.88 O ANISOU 1893 O MET A1033 2668 9698 5824 -1425 646 141 O ATOM 1894 CB MET A1033 -1.603 8.513 4.215 1.00 47.87 C ANISOU 1894 CB MET A1033 2572 9961 5655 -1388 756 315 C ATOM 1895 CG MET A1033 -3.030 8.429 3.709 1.00 51.99 C ANISOU 1895 CG MET A1033 3056 10585 6111 -1370 776 378 C ATOM 1896 SD MET A1033 -3.701 6.756 3.518 1.00 56.54 S ANISOU 1896 SD MET A1033 3588 11211 6682 -1394 716 307 S ATOM 1897 CE MET A1033 -2.696 6.145 2.186 1.00 53.68 C ANISOU 1897 CE MET A1033 3162 10926 6307 -1431 690 183 C ATOM 1898 N ARG A1034 0.896 9.194 5.976 1.00 45.66 N ANISOU 1898 N ARG A1034 2412 9418 5518 -1421 707 264 N ATOM 1899 CA ARG A1034 2.338 9.127 6.230 1.00 45.60 C ANISOU 1899 CA ARG A1034 2403 9350 5574 -1456 674 217 C ATOM 1900 C ARG A1034 2.638 8.897 7.711 1.00 48.66 C ANISOU 1900 C ARG A1034 2880 9588 6021 -1460 626 188 C ATOM 1901 O ARG A1034 3.413 7.998 8.028 1.00 47.82 O ANISOU 1901 O ARG A1034 2752 9453 5964 -1483 585 110 O ATOM 1902 CB ARG A1034 3.036 10.412 5.748 1.00 47.42 C ANISOU 1902 CB ARG A1034 2627 9584 5805 -1471 700 292 C ATOM 1903 CG ARG A1034 4.493 10.209 5.339 1.00 60.56 C ANISOU 1903 CG ARG A1034 4232 11259 7519 -1510 679 259 C ATOM 1904 CD ARG A1034 5.132 11.484 4.810 1.00 74.66 C ANISOU 1904 CD ARG A1034 5993 13068 9306 -1528 705 347 C ATOM 1905 NE ARG A1034 5.633 12.352 5.881 1.00 86.50 N ANISOU 1905 NE ARG A1034 7586 14421 10859 -1556 668 397 N ATOM 1906 CZ ARG A1034 6.915 12.468 6.223 1.00 98.67 C ANISOU 1906 CZ ARG A1034 9121 15901 12469 -1603 623 399 C ATOM 1907 NH1 ARG A1034 7.848 11.777 5.580 1.00 84.05 N ANISOU 1907 NH1 ARG A1034 7165 14126 10642 -1619 620 360 N ATOM 1908 NH2 ARG A1034 7.274 13.284 7.205 1.00 84.83 N1+ ANISOU 1908 NH2 ARG A1034 7466 14008 10757 -1634 579 444 N1+ ATOM 1909 N ALA A1035 2.026 9.699 8.609 1.00 45.56 N ANISOU 1909 N ALA A1035 2589 9101 5620 -1433 631 250 N ATOM 1910 CA ALA A1035 2.203 9.619 10.065 1.00 45.28 C ANISOU 1910 CA ALA A1035 2656 8921 5626 -1426 588 232 C ATOM 1911 C ALA A1035 1.808 8.242 10.617 1.00 48.27 C ANISOU 1911 C ALA A1035 3016 9298 6027 -1417 559 160 C ATOM 1912 O ALA A1035 2.491 7.742 11.509 1.00 47.38 O ANISOU 1912 O ALA A1035 2936 9097 5969 -1434 511 108 O ATOM 1913 CB ALA A1035 1.386 10.701 10.753 1.00 46.20 C ANISOU 1913 CB ALA A1035 2888 8960 5704 -1376 614 315 C ATOM 1914 N ALA A1036 0.730 7.630 10.072 1.00 44.65 N ANISOU 1914 N ALA A1036 2498 8938 5528 -1396 583 160 N ATOM 1915 CA ALA A1036 0.238 6.309 10.478 1.00 44.32 C ANISOU 1915 CA ALA A1036 2429 8903 5508 -1393 552 101 C ATOM 1916 C ALA A1036 1.166 5.190 9.997 1.00 48.72 C ANISOU 1916 C ALA A1036 2913 9490 6108 -1436 517 -2 C ATOM 1917 O ALA A1036 1.252 4.152 10.653 1.00 47.85 O ANISOU 1917 O ALA A1036 2808 9328 6045 -1442 477 -62 O ATOM 1918 CB ALA A1036 -1.164 6.081 9.942 1.00 45.21 C ANISOU 1918 CB ALA A1036 2496 9115 5565 -1370 579 145 C ATOM 1919 N ALA A1037 1.859 5.403 8.861 1.00 46.52 N ANISOU 1919 N ALA A1037 2569 9293 5813 -1459 535 -16 N ATOM 1920 CA ALA A1037 2.801 4.437 8.289 1.00 46.86 C ANISOU 1920 CA ALA A1037 2545 9374 5886 -1485 515 -104 C ATOM 1921 C ALA A1037 4.114 4.385 9.093 1.00 51.36 C ANISOU 1921 C ALA A1037 3139 9845 6529 -1507 482 -131 C ATOM 1922 O ALA A1037 4.629 3.294 9.345 1.00 50.40 O ANISOU 1922 O ALA A1037 2989 9708 6452 -1516 453 -207 O ATOM 1923 CB ALA A1037 3.088 4.786 6.837 1.00 48.09 C ANISOU 1923 CB ALA A1037 2627 9655 5991 -1488 554 -95 C ATOM 1924 N LEU A1038 4.641 5.561 9.498 1.00 49.31 N ANISOU 1924 N LEU A1038 2932 9522 6283 -1517 484 -65 N ATOM 1925 CA LEU A1038 5.886 5.698 10.263 1.00 49.93 C ANISOU 1925 CA LEU A1038 3037 9506 6428 -1549 444 -70 C ATOM 1926 C LEU A1038 5.696 5.261 11.724 1.00 56.11 C ANISOU 1926 C LEU A1038 3900 10167 7250 -1542 398 -96 C ATOM 1927 O LEU A1038 6.669 4.865 12.370 1.00 55.31 O ANISOU 1927 O LEU A1038 3804 10001 7210 -1568 356 -127 O ATOM 1928 CB LEU A1038 6.412 7.146 10.204 1.00 50.19 C ANISOU 1928 CB LEU A1038 3107 9507 6458 -1570 451 16 C ATOM 1929 CG LEU A1038 6.813 7.697 8.823 1.00 54.90 C ANISOU 1929 CG LEU A1038 3617 10218 7026 -1580 494 56 C ATOM 1930 CD1 LEU A1038 6.942 9.205 8.856 1.00 55.16 C ANISOU 1930 CD1 LEU A1038 3703 10213 7043 -1591 506 153 C ATOM 1931 CD2 LEU A1038 8.102 7.068 8.313 1.00 57.59 C ANISOU 1931 CD2 LEU A1038 3869 10597 7413 -1608 482 29 C ATOM 1932 N ASP A1039 4.455 5.338 12.242 1.00 55.23 N ANISOU 1932 N ASP A1039 3849 10033 7104 -1504 409 -73 N ATOM 1933 CA ASP A1039 4.125 4.903 13.603 1.00 56.06 C ANISOU 1933 CA ASP A1039 4028 10037 7237 -1484 374 -89 C ATOM 1934 C ASP A1039 4.070 3.376 13.659 1.00 61.29 C ANISOU 1934 C ASP A1039 4627 10723 7938 -1487 352 -169 C ATOM 1935 O ASP A1039 4.564 2.783 14.620 1.00 61.09 O ANISOU 1935 O ASP A1039 4629 10618 7965 -1492 311 -205 O ATOM 1936 CB ASP A1039 2.797 5.517 14.087 1.00 58.27 C ANISOU 1936 CB ASP A1039 4382 10297 7462 -1430 403 -23 C ATOM 1937 CG ASP A1039 2.861 6.977 14.514 1.00 72.77 C ANISOU 1937 CG ASP A1039 6325 12057 9266 -1411 415 52 C ATOM 1938 OD1 ASP A1039 3.973 7.565 14.486 1.00 74.09 O ANISOU 1938 OD1 ASP A1039 6519 12170 9461 -1452 387 54 O ATOM 1939 OD2 ASP A1039 1.803 7.534 14.877 1.00 80.39 O1- ANISOU 1939 OD2 ASP A1039 7351 13015 10180 -1355 451 114 O1- ATOM 1940 N ALA A1040 3.502 2.745 12.603 1.00 58.54 N ANISOU 1940 N ALA A1040 4199 10482 7560 -1485 376 -197 N ATOM 1941 CA ALA A1040 3.389 1.291 12.443 1.00 58.53 C ANISOU 1941 CA ALA A1040 4143 10510 7587 -1489 354 -275 C ATOM 1942 C ALA A1040 4.759 0.643 12.148 1.00 62.55 C ANISOU 1942 C ALA A1040 4600 11022 8145 -1514 337 -345 C ATOM 1943 O ALA A1040 4.877 -0.584 12.243 1.00 61.64 O ANISOU 1943 O ALA A1040 4455 10900 8066 -1515 313 -416 O ATOM 1944 CB ALA A1040 2.409 0.968 11.325 1.00 59.55 C ANISOU 1944 CB ALA A1040 4217 10749 7658 -1483 377 -277 C ATOM 1945 N GLN A1041 5.783 1.474 11.795 1.00 59.89 N ANISOU 1945 N GLN A1041 4251 10691 7812 -1533 349 -318 N ATOM 1946 CA GLN A1041 7.170 1.075 11.505 1.00 60.10 C ANISOU 1946 CA GLN A1041 4223 10728 7885 -1552 340 -357 C ATOM 1947 C GLN A1041 7.862 0.598 12.792 1.00 63.35 C ANISOU 1947 C GLN A1041 4668 11029 8372 -1565 292 -379 C ATOM 1948 O GLN A1041 8.701 -0.304 12.729 1.00 63.01 O ANISOU 1948 O GLN A1041 4576 10989 8375 -1568 280 -433 O ATOM 1949 CB GLN A1041 7.948 2.241 10.857 1.00 61.95 C ANISOU 1949 CB GLN A1041 4432 10999 8106 -1572 364 -294 C ATOM 1950 CG GLN A1041 9.270 1.856 10.180 1.00 79.92 C ANISOU 1950 CG GLN A1041 6624 13331 10412 -1579 374 -316 C ATOM 1951 CD GLN A1041 10.469 1.932 11.099 1.00103.45 C ANISOU 1951 CD GLN A1041 9609 16227 13470 -1611 332 -298 C ATOM 1952 OE1 GLN A1041 11.067 0.916 11.470 1.00100.52 O ANISOU 1952 OE1 GLN A1041 9219 15826 13149 -1606 311 -352 O ATOM 1953 NE2 GLN A1041 10.873 3.142 11.457 1.00 96.40 N ANISOU 1953 NE2 GLN A1041 8742 15295 12590 -1647 316 -218 N ATOM 1954 N LYS A1042 7.491 1.189 13.955 1.00 59.17 N ANISOU 1954 N LYS A1042 4226 10406 7851 -1566 265 -336 N ATOM 1955 CA LYS A1042 8.006 0.824 15.280 1.00 58.43 C ANISOU 1955 CA LYS A1042 4179 10204 7817 -1575 215 -349 C ATOM 1956 C LYS A1042 7.463 -0.578 15.666 1.00 61.31 C ANISOU 1956 C LYS A1042 4528 10557 8211 -1552 202 -412 C ATOM 1957 O LYS A1042 6.539 -0.709 16.479 1.00 60.05 O ANISOU 1957 O LYS A1042 4426 10342 8048 -1529 187 -399 O ATOM 1958 CB LYS A1042 7.639 1.893 16.334 1.00 60.43 C ANISOU 1958 CB LYS A1042 4546 10366 8050 -1570 196 -286 C ATOM 1959 CG LYS A1042 8.222 3.278 16.072 1.00 69.32 C ANISOU 1959 CG LYS A1042 5705 11478 9157 -1600 195 -222 C ATOM 1960 CD LYS A1042 7.819 4.248 17.171 1.00 75.72 C ANISOU 1960 CD LYS A1042 6649 12179 9943 -1587 169 -173 C ATOM 1961 CE LYS A1042 8.325 5.645 16.921 1.00 81.98 C ANISOU 1961 CE LYS A1042 7491 12936 10721 -1622 157 -110 C ATOM 1962 NZ LYS A1042 7.978 6.560 18.038 1.00 88.23 N1+ ANISOU 1962 NZ LYS A1042 8435 13607 11483 -1602 127 -73 N1+ ATOM 1963 N ALA A1043 8.043 -1.619 15.032 1.00 57.78 N ANISOU 1963 N ALA A1043 4002 10160 7791 -1554 208 -477 N ATOM 1964 CA ALA A1043 7.690 -3.026 15.193 1.00 75.73 C ANISOU 1964 CA ALA A1043 6252 12423 10098 -1538 192 -543 C ATOM 1965 C ALA A1043 8.427 -3.657 16.376 1.00 99.68 C ANISOU 1965 C ALA A1043 9289 15375 13210 -1545 154 -566 C ATOM 1966 O ALA A1043 9.646 -3.544 16.487 1.00 61.42 O ANISOU 1966 O ALA A1043 4407 10530 8398 -1562 151 -568 O ATOM 1967 CB ALA A1043 8.004 -3.788 13.913 1.00 76.76 C ANISOU 1967 CB ALA A1043 6313 12643 10208 -1529 218 -605 C ATOM 1968 N MET A1058 10.830 -12.365 8.195 1.00137.08 N1+ ANISOU 1968 N MET A1058 13801 20468 17814 -1268 305 -1257 N1+ ATOM 1969 CA MET A1058 10.785 -11.100 8.928 1.00136.07 C ANISOU 1969 CA MET A1058 13647 20343 17710 -1316 303 -1152 C ATOM 1970 C MET A1058 11.277 -9.940 8.038 1.00139.69 C ANISOU 1970 C MET A1058 14066 20910 18100 -1304 358 -1091 C ATOM 1971 O MET A1058 10.737 -8.836 8.138 1.00138.82 O ANISOU 1971 O MET A1058 13956 20824 17967 -1345 353 -1022 O ATOM 1972 CB MET A1058 11.621 -11.195 10.224 1.00138.07 C ANISOU 1972 CB MET A1058 13879 20516 18066 -1326 292 -1109 C ATOM 1973 CG MET A1058 11.406 -10.033 11.188 1.00141.01 C ANISOU 1973 CG MET A1058 14252 20859 18465 -1380 269 -1016 C ATOM 1974 SD MET A1058 12.269 -10.233 12.768 1.00144.84 S ANISOU 1974 SD MET A1058 14728 21243 19063 -1397 240 -975 S ATOM 1975 CE MET A1058 12.087 -8.593 13.441 1.00140.84 C ANISOU 1975 CE MET A1058 14241 20727 18545 -1450 223 -869 C ATOM 1976 N LYS A1059 12.285 -10.199 7.170 1.00136.51 N ANISOU 1976 N LYS A1059 13631 20572 17664 -1242 413 -1112 N ATOM 1977 CA LYS A1059 12.891 -9.234 6.238 1.00136.39 C ANISOU 1977 CA LYS A1059 13565 20669 17586 -1218 472 -1051 C ATOM 1978 C LYS A1059 11.853 -8.693 5.228 1.00139.70 C ANISOU 1978 C LYS A1059 14007 21168 17904 -1230 474 -1057 C ATOM 1979 O LYS A1059 11.823 -7.487 4.980 1.00139.04 O ANISOU 1979 O LYS A1059 13894 21141 17795 -1256 494 -973 O ATOM 1980 CB LYS A1059 14.070 -9.898 5.490 1.00139.71 C ANISOU 1980 CB LYS A1059 13954 21142 17986 -1131 532 -1083 C ATOM 1981 CG LYS A1059 14.869 -8.972 4.573 1.00151.61 C ANISOU 1981 CG LYS A1059 15396 22773 19435 -1094 601 -1008 C ATOM 1982 CD LYS A1059 15.892 -9.751 3.757 1.00160.93 C ANISOU 1982 CD LYS A1059 16553 24011 20581 -989 667 -1045 C ATOM 1983 CE LYS A1059 16.610 -8.883 2.754 1.00169.97 C ANISOU 1983 CE LYS A1059 17626 25289 21666 -943 740 -961 C ATOM 1984 NZ LYS A1059 17.568 -9.668 1.934 1.00178.68 N1+ ANISOU 1984 NZ LYS A1059 18709 26453 22729 -826 813 -989 N1+ ATOM 1985 N ASP A1060 11.011 -9.590 4.666 1.00136.00 N ANISOU 1985 N ASP A1060 13592 20701 17381 -1215 449 -1154 N ATOM 1986 CA ASP A1060 9.968 -9.291 3.674 1.00135.59 C ANISOU 1986 CA ASP A1060 13565 20726 17229 -1227 442 -1172 C ATOM 1987 C ASP A1060 8.914 -8.299 4.206 1.00137.00 C ANISOU 1987 C ASP A1060 13745 20895 17415 -1299 409 -1094 C ATOM 1988 O ASP A1060 8.470 -7.429 3.453 1.00136.47 O ANISOU 1988 O ASP A1060 13662 20917 17275 -1306 432 -1049 O ATOM 1989 CB ASP A1060 9.276 -10.587 3.197 1.00138.14 C ANISOU 1989 CB ASP A1060 13954 21021 17510 -1213 397 -1292 C ATOM 1990 CG ASP A1060 8.913 -11.586 4.288 1.00148.25 C ANISOU 1990 CG ASP A1060 15273 22171 18883 -1242 333 -1341 C ATOM 1991 OD1 ASP A1060 8.073 -11.246 5.154 1.00148.01 O ANISOU 1991 OD1 ASP A1060 15246 22089 18903 -1306 287 -1294 O ATOM 1992 OD2 ASP A1060 9.424 -12.727 4.241 1.00154.66 O1- ANISOU 1992 OD2 ASP A1060 16115 22937 19713 -1196 333 -1424 O1- ATOM 1993 N PHE A1061 8.530 -8.424 5.490 1.00131.79 N ANISOU 1993 N PHE A1061 13103 20131 16841 -1344 363 -1074 N ATOM 1994 CA PHE A1061 7.539 -7.549 6.121 1.00130.32 C ANISOU 1994 CA PHE A1061 12926 19926 16663 -1397 338 -995 C ATOM 1995 C PHE A1061 8.195 -6.251 6.632 1.00131.96 C ANISOU 1995 C PHE A1061 13105 20134 16902 -1409 371 -894 C ATOM 1996 O PHE A1061 7.523 -5.218 6.674 1.00131.15 O ANISOU 1996 O PHE A1061 13007 20052 16772 -1435 374 -821 O ATOM 1997 CB PHE A1061 6.810 -8.286 7.262 1.00131.70 C ANISOU 1997 CB PHE A1061 13137 19995 16908 -1430 275 -1013 C ATOM 1998 CG PHE A1061 5.640 -7.548 7.875 1.00132.67 C ANISOU 1998 CG PHE A1061 13276 20102 17031 -1471 252 -934 C ATOM 1999 CD1 PHE A1061 4.485 -7.304 7.138 1.00135.91 C ANISOU 1999 CD1 PHE A1061 13689 20583 17367 -1487 244 -914 C ATOM 2000 CD2 PHE A1061 5.671 -7.146 9.205 1.00134.12 C ANISOU 2000 CD2 PHE A1061 13473 20201 17285 -1486 237 -877 C ATOM 2001 CE1 PHE A1061 3.403 -6.625 7.708 1.00136.25 C ANISOU 2001 CE1 PHE A1061 13743 20616 17409 -1514 231 -829 C ATOM 2002 CE2 PHE A1061 4.582 -6.483 9.778 1.00136.39 C ANISOU 2002 CE2 PHE A1061 13782 20474 17565 -1507 224 -801 C ATOM 2003 CZ PHE A1061 3.458 -6.221 9.024 1.00134.61 C ANISOU 2003 CZ PHE A1061 13554 20323 17269 -1518 225 -774 C ATOM 2004 N ARG A1062 9.500 -6.299 6.995 1.00127.24 N ANISOU 2004 N ARG A1062 12476 19512 16358 -1389 392 -886 N ATOM 2005 CA ARG A1062 10.274 -5.144 7.472 1.00126.12 C ANISOU 2005 CA ARG A1062 12306 19363 16251 -1408 410 -790 C ATOM 2006 C ARG A1062 10.451 -4.123 6.335 1.00128.67 C ANISOU 2006 C ARG A1062 12590 19799 16501 -1396 462 -734 C ATOM 2007 O ARG A1062 10.303 -2.921 6.568 1.00127.83 O ANISOU 2007 O ARG A1062 12484 19692 16395 -1428 465 -647 O ATOM 2008 CB ARG A1062 11.646 -5.596 8.030 1.00126.51 C ANISOU 2008 CB ARG A1062 12323 19368 16378 -1393 414 -791 C ATOM 2009 CG ARG A1062 12.511 -4.496 8.670 1.00136.31 C ANISOU 2009 CG ARG A1062 13538 20583 17668 -1428 412 -688 C ATOM 2010 CD ARG A1062 12.022 -4.049 10.041 1.00144.87 C ANISOU 2010 CD ARG A1062 14681 21565 18799 -1477 360 -650 C ATOM 2011 NE ARG A1062 12.896 -3.033 10.636 1.00152.43 N ANISOU 2011 NE ARG A1062 15627 22489 19800 -1515 347 -560 N ATOM 2012 CZ ARG A1062 12.743 -1.720 10.483 1.00165.31 C ANISOU 2012 CZ ARG A1062 17271 24137 21402 -1544 351 -482 C ATOM 2013 NH1 ARG A1062 11.749 -1.241 9.744 1.00152.92 N ANISOU 2013 NH1 ARG A1062 15720 22625 19760 -1535 377 -478 N ATOM 2014 NH2 ARG A1062 13.585 -0.877 11.064 1.00150.49 N1+ ANISOU 2014 NH2 ARG A1062 15392 22217 19571 -1585 326 -403 N1+ ATOM 2015 N HIS A1063 10.743 -4.608 5.110 1.00124.71 N ANISOU 2015 N HIS A1063 12060 19390 15934 -1347 500 -783 N ATOM 2016 CA HIS A1063 10.910 -3.779 3.916 1.00124.42 C ANISOU 2016 CA HIS A1063 11981 19474 15819 -1325 553 -734 C ATOM 2017 C HIS A1063 9.560 -3.251 3.407 1.00125.95 C ANISOU 2017 C HIS A1063 12203 19714 15937 -1348 545 -723 C ATOM 2018 O HIS A1063 9.519 -2.182 2.803 1.00125.56 O ANISOU 2018 O HIS A1063 12124 19740 15843 -1351 580 -648 O ATOM 2019 CB HIS A1063 11.621 -4.562 2.800 1.00126.31 C ANISOU 2019 CB HIS A1063 12190 19798 16003 -1252 600 -792 C ATOM 2020 CG HIS A1063 13.106 -4.655 2.971 1.00130.22 C ANISOU 2020 CG HIS A1063 12628 20294 16556 -1218 634 -755 C ATOM 2021 ND1 HIS A1063 13.951 -3.673 2.483 1.00132.41 N ANISOU 2021 ND1 HIS A1063 12833 20649 16828 -1209 682 -651 N ATOM 2022 CD2 HIS A1063 13.852 -5.622 3.552 1.00132.14 C ANISOU 2022 CD2 HIS A1063 12870 20474 16863 -1193 627 -799 C ATOM 2023 CE1 HIS A1063 15.176 -4.067 2.792 1.00132.20 C ANISOU 2023 CE1 HIS A1063 12760 20607 16862 -1181 700 -630 C ATOM 2024 NE2 HIS A1063 15.166 -5.234 3.436 1.00132.38 N ANISOU 2024 NE2 HIS A1063 12824 20546 16927 -1167 670 -718 N ATOM 2025 N GLY A1064 8.485 -3.997 3.669 1.00120.64 N ANISOU 2025 N GLY A1064 11582 18997 15258 -1365 498 -787 N ATOM 2026 CA GLY A1064 7.122 -3.672 3.257 1.00119.51 C ANISOU 2026 CA GLY A1064 11462 18896 15051 -1389 481 -773 C ATOM 2027 C GLY A1064 6.574 -2.330 3.707 1.00120.70 C ANISOU 2027 C GLY A1064 11613 19044 15204 -1422 491 -663 C ATOM 2028 O GLY A1064 5.797 -1.717 2.971 1.00120.24 O ANISOU 2028 O GLY A1064 11543 19071 15072 -1424 512 -622 O ATOM 2029 N PHE A1065 6.969 -1.861 4.913 1.00115.23 N ANISOU 2029 N PHE A1065 10938 18252 14591 -1446 476 -613 N ATOM 2030 CA PHE A1065 6.511 -0.588 5.484 1.00113.80 C ANISOU 2030 CA PHE A1065 10780 18042 14417 -1472 482 -513 C ATOM 2031 C PHE A1065 7.075 0.630 4.734 1.00115.56 C ANISOU 2031 C PHE A1065 10962 18341 14605 -1468 531 -433 C ATOM 2032 O PHE A1065 6.302 1.529 4.406 1.00114.99 O ANISOU 2032 O PHE A1065 10897 18309 14484 -1474 550 -369 O ATOM 2033 CB PHE A1065 6.873 -0.470 6.978 1.00115.14 C ANISOU 2033 CB PHE A1065 10990 18082 14674 -1493 448 -490 C ATOM 2034 CG PHE A1065 6.049 -1.308 7.931 1.00116.32 C ANISOU 2034 CG PHE A1065 11186 18149 14860 -1500 401 -531 C ATOM 2035 CD1 PHE A1065 4.768 -0.911 8.304 1.00118.98 C ANISOU 2035 CD1 PHE A1065 11563 18468 15174 -1506 391 -484 C ATOM 2036 CD2 PHE A1065 6.578 -2.454 8.510 1.00118.52 C ANISOU 2036 CD2 PHE A1065 11465 18367 15201 -1496 370 -604 C ATOM 2037 CE1 PHE A1065 4.014 -1.674 9.202 1.00119.49 C ANISOU 2037 CE1 PHE A1065 11661 18463 15275 -1508 350 -507 C ATOM 2038 CE2 PHE A1065 5.826 -3.213 9.413 1.00120.89 C ANISOU 2038 CE2 PHE A1065 11802 18592 15540 -1503 327 -631 C ATOM 2039 CZ PHE A1065 4.548 -2.819 9.751 1.00118.55 C ANISOU 2039 CZ PHE A1065 11540 18284 15220 -1509 317 -580 C ATOM 2040 N ASP A1066 8.406 0.662 4.468 1.00110.58 N ANISOU 2040 N ASP A1066 10284 17730 14002 -1457 553 -428 N ATOM 2041 CA ASP A1066 9.078 1.788 3.800 1.00109.83 C ANISOU 2041 CA ASP A1066 10139 17703 13887 -1456 596 -340 C ATOM 2042 C ASP A1066 8.638 1.949 2.331 1.00110.97 C ANISOU 2042 C ASP A1066 10242 17989 13931 -1424 643 -338 C ATOM 2043 O ASP A1066 8.721 3.062 1.809 1.00110.78 O ANISOU 2043 O ASP A1066 10190 18021 13879 -1428 678 -250 O ATOM 2044 CB ASP A1066 10.613 1.672 3.880 1.00112.36 C ANISOU 2044 CB ASP A1066 10406 18019 14265 -1449 606 -325 C ATOM 2045 CG ASP A1066 11.217 0.417 3.282 1.00125.26 C ANISOU 2045 CG ASP A1066 12003 19707 15885 -1398 625 -411 C ATOM 2046 OD1 ASP A1066 11.209 0.287 2.038 1.00126.99 O ANISOU 2046 OD1 ASP A1066 12186 20041 16022 -1354 669 -430 O ATOM 2047 OD2 ASP A1066 11.766 -0.399 4.051 1.00131.65 O1- ANISOU 2047 OD2 ASP A1066 12820 20442 16760 -1397 598 -455 O1- ATOM 2048 N ILE A1067 8.175 0.860 1.674 1.00105.18 N ANISOU 2048 N ILE A1067 9512 17310 13144 -1392 641 -433 N ATOM 2049 CA ILE A1067 7.682 0.899 0.289 1.00104.37 C ANISOU 2049 CA ILE A1067 9381 17340 12935 -1361 675 -445 C ATOM 2050 C ILE A1067 6.396 1.753 0.267 1.00105.05 C ANISOU 2050 C ILE A1067 9489 17446 12980 -1390 673 -379 C ATOM 2051 O ILE A1067 6.218 2.580 -0.630 1.00104.82 O ANISOU 2051 O ILE A1067 9422 17518 12887 -1378 715 -317 O ATOM 2052 CB ILE A1067 7.465 -0.536 -0.291 1.00107.94 C ANISOU 2052 CB ILE A1067 9854 17816 13340 -1330 654 -571 C ATOM 2053 CG1 ILE A1067 8.778 -1.361 -0.259 1.00108.76 C ANISOU 2053 CG1 ILE A1067 9940 17904 13482 -1287 669 -628 C ATOM 2054 CG2 ILE A1067 6.892 -0.485 -1.723 1.00109.48 C ANISOU 2054 CG2 ILE A1067 10036 18147 13415 -1302 677 -588 C ATOM 2055 CD1 ILE A1067 8.614 -2.908 -0.351 1.00115.86 C ANISOU 2055 CD1 ILE A1067 10885 18768 14368 -1261 633 -761 C ATOM 2056 N LEU A1068 5.541 1.579 1.294 1.00 98.95 N ANISOU 2056 N LEU A1068 8771 16577 12247 -1422 628 -382 N ATOM 2057 CA LEU A1068 4.283 2.304 1.471 1.00 97.42 C ANISOU 2057 CA LEU A1068 8602 16387 12024 -1442 626 -314 C ATOM 2058 C LEU A1068 4.518 3.775 1.824 1.00 98.35 C ANISOU 2058 C LEU A1068 8723 16480 12164 -1452 658 -199 C ATOM 2059 O LEU A1068 3.753 4.619 1.366 1.00 98.07 O ANISOU 2059 O LEU A1068 8681 16504 12076 -1450 687 -126 O ATOM 2060 CB LEU A1068 3.429 1.637 2.562 1.00 96.95 C ANISOU 2060 CB LEU A1068 8600 16228 12009 -1463 572 -343 C ATOM 2061 CG LEU A1068 2.362 0.634 2.102 1.00102.00 C ANISOU 2061 CG LEU A1068 9244 16907 12604 -1468 533 -408 C ATOM 2062 CD1 LEU A1068 2.976 -0.661 1.581 1.00102.78 C ANISOU 2062 CD1 LEU A1068 9333 17025 12695 -1453 514 -526 C ATOM 2063 CD2 LEU A1068 1.414 0.304 3.235 1.00103.97 C ANISOU 2063 CD2 LEU A1068 9538 17060 12905 -1489 487 -400 C ATOM 2064 N VAL A1069 5.565 4.084 2.623 1.00 92.60 N ANISOU 2064 N VAL A1069 8007 15662 11514 -1465 649 -181 N ATOM 2065 CA VAL A1069 5.915 5.453 3.043 1.00 91.43 C ANISOU 2065 CA VAL A1069 7874 15465 11399 -1484 664 -79 C ATOM 2066 C VAL A1069 6.314 6.281 1.798 1.00 93.82 C ANISOU 2066 C VAL A1069 8108 15888 11653 -1471 718 -12 C ATOM 2067 O VAL A1069 5.886 7.431 1.666 1.00 93.25 O ANISOU 2067 O VAL A1069 8046 15824 11560 -1477 743 80 O ATOM 2068 CB VAL A1069 7.030 5.473 4.136 1.00 95.13 C ANISOU 2068 CB VAL A1069 8367 15815 11962 -1509 628 -81 C ATOM 2069 CG1 VAL A1069 7.423 6.900 4.521 1.00 94.99 C ANISOU 2069 CG1 VAL A1069 8374 15742 11976 -1537 630 23 C ATOM 2070 CG2 VAL A1069 6.610 4.693 5.379 1.00 94.33 C ANISOU 2070 CG2 VAL A1069 8335 15601 11906 -1517 577 -139 C ATOM 2071 N GLY A1070 7.098 5.671 0.906 1.00 89.55 N ANISOU 2071 N GLY A1070 7499 15438 11088 -1447 740 -55 N ATOM 2072 CA GLY A1070 7.576 6.282 -0.330 1.00 89.29 C ANISOU 2072 CA GLY A1070 7390 15534 11003 -1423 795 3 C ATOM 2073 C GLY A1070 6.475 6.634 -1.308 1.00 91.24 C ANISOU 2073 C GLY A1070 7624 15892 11152 -1404 827 24 C ATOM 2074 O GLY A1070 6.503 7.717 -1.897 1.00 90.94 O ANISOU 2074 O GLY A1070 7548 15921 11085 -1401 869 118 O ATOM 2075 N GLN A1071 5.489 5.726 -1.472 1.00 86.29 N ANISOU 2075 N GLN A1071 7026 15283 10476 -1397 802 -57 N ATOM 2076 CA GLN A1071 4.335 5.911 -2.360 1.00 85.83 C ANISOU 2076 CA GLN A1071 6958 15329 10324 -1386 818 -39 C ATOM 2077 C GLN A1071 3.425 7.035 -1.851 1.00 88.66 C ANISOU 2077 C GLN A1071 7349 15648 10691 -1407 827 63 C ATOM 2078 O GLN A1071 2.845 7.757 -2.663 1.00 88.51 O ANISOU 2078 O GLN A1071 7298 15727 10605 -1396 865 132 O ATOM 2079 CB GLN A1071 3.533 4.610 -2.512 1.00 87.07 C ANISOU 2079 CB GLN A1071 7142 15497 10442 -1386 772 -146 C ATOM 2080 CG GLN A1071 4.248 3.536 -3.327 1.00100.14 C ANISOU 2080 CG GLN A1071 8774 17219 12054 -1352 772 -248 C ATOM 2081 CD GLN A1071 3.425 2.281 -3.485 1.00116.24 C ANISOU 2081 CD GLN A1071 10852 19263 14051 -1359 717 -349 C ATOM 2082 OE1 GLN A1071 3.104 1.585 -2.514 1.00110.98 O ANISOU 2082 OE1 GLN A1071 10233 18490 13445 -1386 665 -397 O ATOM 2083 NE2 GLN A1071 3.114 1.933 -4.725 1.00106.92 N ANISOU 2083 NE2 GLN A1071 9654 18205 12765 -1336 724 -385 N ATOM 2084 N ILE A1072 3.318 7.188 -0.511 1.00 84.11 N ANISOU 2084 N ILE A1072 6839 14929 10191 -1429 795 74 N ATOM 2085 CA ILE A1072 2.526 8.234 0.148 1.00 83.27 C ANISOU 2085 CA ILE A1072 6782 14762 10093 -1435 805 169 C ATOM 2086 C ILE A1072 3.261 9.586 -0.002 1.00 87.53 C ANISOU 2086 C ILE A1072 7308 15299 10651 -1438 845 269 C ATOM 2087 O ILE A1072 2.644 10.562 -0.431 1.00 87.44 O ANISOU 2087 O ILE A1072 7286 15345 10594 -1426 886 357 O ATOM 2088 CB ILE A1072 2.226 7.883 1.649 1.00 85.36 C ANISOU 2088 CB ILE A1072 7133 14875 10427 -1448 759 145 C ATOM 2089 CG1 ILE A1072 1.262 6.677 1.763 1.00 85.34 C ANISOU 2089 CG1 ILE A1072 7139 14883 10404 -1446 723 76 C ATOM 2090 CG2 ILE A1072 1.663 9.094 2.416 1.00 85.54 C ANISOU 2090 CG2 ILE A1072 7222 14817 10461 -1441 777 248 C ATOM 2091 CD1 ILE A1072 1.196 6.003 3.161 1.00 90.74 C ANISOU 2091 CD1 ILE A1072 7890 15428 11158 -1455 674 36 C ATOM 2092 N ASP A1073 4.571 9.631 0.335 1.00 84.02 N ANISOU 2092 N ASP A1073 6858 14791 10275 -1457 830 263 N ATOM 2093 CA ASP A1073 5.390 10.847 0.289 1.00 84.06 C ANISOU 2093 CA ASP A1073 6850 14774 10315 -1473 851 360 C ATOM 2094 C ASP A1073 5.517 11.421 -1.129 1.00 89.08 C ANISOU 2094 C ASP A1073 7395 15562 10888 -1453 910 425 C ATOM 2095 O ASP A1073 5.564 12.644 -1.269 1.00 88.81 O ANISOU 2095 O ASP A1073 7361 15522 10860 -1461 936 531 O ATOM 2096 CB ASP A1073 6.787 10.595 0.863 1.00 85.63 C ANISOU 2096 CB ASP A1073 7043 14895 10600 -1502 814 339 C ATOM 2097 CG ASP A1073 7.259 11.692 1.797 1.00 93.20 C ANISOU 2097 CG ASP A1073 8064 15720 11628 -1542 787 419 C ATOM 2098 OD1 ASP A1073 7.034 12.884 1.481 1.00 93.43 O ANISOU 2098 OD1 ASP A1073 8101 15758 11640 -1545 815 516 O ATOM 2099 OD2 ASP A1073 7.873 11.363 2.831 1.00 98.48 O1- ANISOU 2099 OD2 ASP A1073 8777 16274 12366 -1571 733 385 O1- ATOM 2100 N ASP A1074 5.560 10.560 -2.166 1.00 86.49 N ANISOU 2100 N ASP A1074 6996 15367 10500 -1424 930 364 N ATOM 2101 CA ASP A1074 5.640 11.003 -3.563 1.00 87.23 C ANISOU 2101 CA ASP A1074 7003 15619 10521 -1395 988 420 C ATOM 2102 C ASP A1074 4.274 11.509 -4.053 1.00 90.98 C ANISOU 2102 C ASP A1074 7485 16165 10918 -1382 1015 469 C ATOM 2103 O ASP A1074 4.233 12.401 -4.901 1.00 91.08 O ANISOU 2103 O ASP A1074 7443 16275 10887 -1367 1065 558 O ATOM 2104 CB ASP A1074 6.168 9.887 -4.480 1.00 89.76 C ANISOU 2104 CB ASP A1074 7262 16053 10790 -1358 999 334 C ATOM 2105 CG ASP A1074 7.681 9.705 -4.473 1.00102.20 C ANISOU 2105 CG ASP A1074 8784 17627 12421 -1352 1007 342 C ATOM 2106 OD1 ASP A1074 8.343 10.212 -3.535 1.00102.78 O ANISOU 2106 OD1 ASP A1074 8877 17586 12590 -1392 982 393 O ATOM 2107 OD2 ASP A1074 8.203 9.051 -5.402 1.00109.38 O1- ANISOU 2107 OD2 ASP A1074 9634 18649 13276 -1305 1036 300 O1- ATOM 2108 N ALA A1075 3.166 10.956 -3.507 1.00 86.76 N ANISOU 2108 N ALA A1075 7012 15584 10368 -1386 984 422 N ATOM 2109 CA ALA A1075 1.797 11.377 -3.826 1.00 86.36 C ANISOU 2109 CA ALA A1075 6969 15592 10252 -1375 1005 477 C ATOM 2110 C ALA A1075 1.503 12.754 -3.220 1.00 89.94 C ANISOU 2110 C ALA A1075 7468 15962 10741 -1379 1031 596 C ATOM 2111 O ALA A1075 0.744 13.533 -3.799 1.00 89.78 O ANISOU 2111 O ALA A1075 7428 16017 10669 -1361 1075 686 O ATOM 2112 CB ALA A1075 0.797 10.353 -3.315 1.00 86.62 C ANISOU 2112 CB ALA A1075 7047 15594 10272 -1382 958 402 C ATOM 2113 N LEU A1076 2.122 13.046 -2.055 1.00 85.92 N ANISOU 2113 N LEU A1076 7028 15297 10321 -1401 1001 597 N ATOM 2114 CA LEU A1076 2.013 14.308 -1.322 1.00 85.46 C ANISOU 2114 CA LEU A1076 7040 15127 10303 -1405 1013 694 C ATOM 2115 C LEU A1076 2.659 15.439 -2.126 1.00 90.05 C ANISOU 2115 C LEU A1076 7566 15765 10886 -1409 1055 794 C ATOM 2116 O LEU A1076 2.121 16.545 -2.157 1.00 89.58 O ANISOU 2116 O LEU A1076 7533 15691 10812 -1396 1091 895 O ATOM 2117 CB LEU A1076 2.683 14.160 0.060 1.00 85.00 C ANISOU 2117 CB LEU A1076 7069 14894 10334 -1433 956 650 C ATOM 2118 CG LEU A1076 2.572 15.329 1.042 1.00 89.59 C ANISOU 2118 CG LEU A1076 7757 15326 10955 -1437 951 727 C ATOM 2119 CD1 LEU A1076 1.200 15.373 1.701 1.00 89.38 C ANISOU 2119 CD1 LEU A1076 7811 15258 10891 -1396 965 747 C ATOM 2120 CD2 LEU A1076 3.627 15.218 2.120 1.00 92.06 C ANISOU 2120 CD2 LEU A1076 8134 15490 11354 -1476 887 684 C ATOM 2121 N LYS A1077 3.796 15.142 -2.792 1.00 87.43 N ANISOU 2121 N LYS A1077 7151 15498 10568 -1422 1055 772 N ATOM 2122 CA LYS A1077 4.559 16.069 -3.636 1.00 88.21 C ANISOU 2122 CA LYS A1077 7176 15666 10674 -1426 1094 870 C ATOM 2123 C LYS A1077 3.732 16.509 -4.852 1.00 93.04 C ANISOU 2123 C LYS A1077 7722 16435 11195 -1390 1158 937 C ATOM 2124 O LYS A1077 3.804 17.674 -5.245 1.00 93.10 O ANISOU 2124 O LYS A1077 7708 16458 11207 -1390 1196 1053 O ATOM 2125 CB LYS A1077 5.882 15.428 -4.091 1.00 91.29 C ANISOU 2125 CB LYS A1077 7483 16113 11090 -1433 1085 828 C ATOM 2126 CG LYS A1077 6.883 15.227 -2.958 1.00109.25 C ANISOU 2126 CG LYS A1077 9806 18237 13466 -1476 1023 796 C ATOM 2127 CD LYS A1077 8.115 14.444 -3.398 1.00121.45 C ANISOU 2127 CD LYS A1077 11263 19848 15035 -1473 1020 761 C ATOM 2128 CE LYS A1077 9.074 14.217 -2.252 1.00132.65 C ANISOU 2128 CE LYS A1077 12723 21122 16555 -1520 956 738 C ATOM 2129 NZ LYS A1077 10.267 13.436 -2.672 1.00142.46 N1+ ANISOU 2129 NZ LYS A1077 13875 22433 17820 -1509 960 713 N1+ ATOM 2130 N LEU A1078 2.936 15.583 -5.426 1.00 89.89 N ANISOU 2130 N LEU A1078 7295 16147 10712 -1362 1166 868 N ATOM 2131 CA LEU A1078 2.053 15.837 -6.569 1.00 90.32 C ANISOU 2131 CA LEU A1078 7289 16360 10668 -1330 1217 921 C ATOM 2132 C LEU A1078 0.943 16.808 -6.175 1.00 95.00 C ANISOU 2132 C LEU A1078 7938 16905 11253 -1322 1240 1015 C ATOM 2133 O LEU A1078 0.620 17.710 -6.948 1.00 95.04 O ANISOU 2133 O LEU A1078 7896 16996 11218 -1303 1295 1121 O ATOM 2134 CB LEU A1078 1.445 14.520 -7.095 1.00 90.35 C ANISOU 2134 CB LEU A1078 7270 16468 10592 -1314 1197 813 C ATOM 2135 CG LEU A1078 2.415 13.439 -7.585 1.00 95.44 C ANISOU 2135 CG LEU A1078 7870 17171 11224 -1305 1179 709 C ATOM 2136 CD1 LEU A1078 1.778 12.066 -7.530 1.00 95.20 C ANISOU 2136 CD1 LEU A1078 7871 17151 11151 -1305 1130 581 C ATOM 2137 CD2 LEU A1078 2.944 13.743 -8.982 1.00 99.23 C ANISOU 2137 CD2 LEU A1078 8250 17820 11634 -1270 1235 757 C ATOM 2138 N ALA A1079 0.383 16.626 -4.956 1.00 91.71 N ANISOU 2138 N ALA A1079 7621 16352 10875 -1329 1204 982 N ATOM 2139 CA ALA A1079 -0.686 17.440 -4.371 1.00 91.67 C ANISOU 2139 CA ALA A1079 7687 16280 10864 -1309 1227 1066 C ATOM 2140 C ALA A1079 -0.201 18.855 -4.018 1.00 96.37 C ANISOU 2140 C ALA A1079 8331 16770 11514 -1312 1251 1170 C ATOM 2141 O ALA A1079 -0.976 19.808 -4.133 1.00 95.92 O ANISOU 2141 O ALA A1079 8300 16713 11432 -1281 1298 1274 O ATOM 2142 CB ALA A1079 -1.234 16.760 -3.127 1.00 91.80 C ANISOU 2142 CB ALA A1079 7795 16177 10909 -1309 1181 997 C ATOM 2143 N ASN A1080 1.071 18.986 -3.584 1.00 93.62 N ANISOU 2143 N ASN A1080 7998 16331 11244 -1349 1216 1149 N ATOM 2144 CA ASN A1080 1.679 20.272 -3.233 1.00 94.06 C ANISOU 2144 CA ASN A1080 8102 16275 11362 -1368 1220 1243 C ATOM 2145 C ASN A1080 1.915 21.119 -4.487 1.00 99.48 C ANISOU 2145 C ASN A1080 8687 17089 12021 -1360 1277 1350 C ATOM 2146 O ASN A1080 1.909 22.349 -4.398 1.00 99.54 O ANISOU 2146 O ASN A1080 8733 17032 12054 -1361 1300 1458 O ATOM 2147 CB ASN A1080 2.991 20.067 -2.469 1.00 94.34 C ANISOU 2147 CB ASN A1080 8171 16184 11489 -1420 1153 1192 C ATOM 2148 CG ASN A1080 2.846 19.452 -1.092 1.00112.35 C ANISOU 2148 CG ASN A1080 10565 18317 13806 -1428 1094 1101 C ATOM 2149 OD1 ASN A1080 1.750 19.119 -0.623 1.00104.44 O ANISOU 2149 OD1 ASN A1080 9624 17292 12765 -1392 1103 1078 O ATOM 2150 ND2 ASN A1080 3.967 19.274 -0.413 1.00103.93 N ANISOU 2150 ND2 ASN A1080 9521 17152 12816 -1476 1033 1056 N ATOM 2151 N GLU A1081 2.109 20.458 -5.649 1.00 96.80 N ANISOU 2151 N GLU A1081 8223 16930 11626 -1350 1301 1323 N ATOM 2152 CA GLU A1081 2.312 21.101 -6.948 1.00 97.68 C ANISOU 2152 CA GLU A1081 8225 17192 11698 -1334 1360 1420 C ATOM 2153 C GLU A1081 0.991 21.705 -7.450 1.00102.21 C ANISOU 2153 C GLU A1081 8794 17847 12195 -1291 1419 1502 C ATOM 2154 O GLU A1081 0.987 22.815 -7.986 1.00102.39 O ANISOU 2154 O GLU A1081 8788 17899 12218 -1281 1467 1625 O ATOM 2155 CB GLU A1081 2.872 20.086 -7.966 1.00 99.44 C ANISOU 2155 CB GLU A1081 8332 17580 11871 -1323 1366 1354 C ATOM 2156 CG GLU A1081 3.322 20.706 -9.285 1.00112.52 C ANISOU 2156 CG GLU A1081 9868 19392 13491 -1303 1426 1457 C ATOM 2157 CD GLU A1081 3.788 19.762 -10.381 1.00136.51 C ANISOU 2157 CD GLU A1081 12801 22610 16459 -1273 1445 1400 C ATOM 2158 OE1 GLU A1081 4.269 18.650 -10.061 1.00131.57 O ANISOU 2158 OE1 GLU A1081 12184 21961 15843 -1278 1404 1283 O ATOM 2159 OE2 GLU A1081 3.717 20.161 -11.566 1.00132.73 O1- ANISOU 2159 OE2 GLU A1081 12230 22291 15912 -1239 1502 1476 O1- ATOM 2160 N GLY A1082 -0.102 20.966 -7.259 1.00 98.65 N ANISOU 2160 N GLY A1082 8368 17431 11684 -1270 1413 1440 N ATOM 2161 CA GLY A1082 -1.444 21.351 -7.681 1.00 98.69 C ANISOU 2161 CA GLY A1082 8363 17522 11614 -1230 1462 1515 C ATOM 2162 C GLY A1082 -2.164 20.247 -8.431 1.00102.73 C ANISOU 2162 C GLY A1082 8805 18196 12031 -1219 1456 1449 C ATOM 2163 O GLY A1082 -3.362 20.362 -8.708 1.00102.27 O ANISOU 2163 O GLY A1082 8733 18217 11909 -1193 1485 1507 O ATOM 2164 N LYS A1083 -1.426 19.168 -8.766 1.00 99.59 N ANISOU 2164 N LYS A1083 8367 17848 11625 -1238 1416 1332 N ATOM 2165 CA LYS A1083 -1.931 17.997 -9.481 1.00 99.67 C ANISOU 2165 CA LYS A1083 8325 17997 11546 -1233 1394 1248 C ATOM 2166 C LYS A1083 -2.752 17.137 -8.520 1.00102.80 C ANISOU 2166 C LYS A1083 8797 18311 11953 -1246 1340 1170 C ATOM 2167 O LYS A1083 -2.215 16.245 -7.856 1.00101.92 O ANISOU 2167 O LYS A1083 8721 18122 11880 -1268 1285 1053 O ATOM 2168 CB LYS A1083 -0.775 17.192 -10.116 1.00102.68 C ANISOU 2168 CB LYS A1083 8652 18446 11916 -1237 1376 1154 C ATOM 2169 CG LYS A1083 -0.041 17.912 -11.247 1.00117.43 C ANISOU 2169 CG LYS A1083 10426 20434 13758 -1215 1434 1238 C ATOM 2170 CD LYS A1083 1.106 17.069 -11.790 1.00126.40 C ANISOU 2170 CD LYS A1083 11511 21632 14881 -1205 1422 1151 C ATOM 2171 CE LYS A1083 1.808 17.722 -12.953 1.00135.52 C ANISOU 2171 CE LYS A1083 12565 22922 16006 -1174 1484 1244 C ATOM 2172 NZ LYS A1083 2.897 16.860 -13.482 1.00143.54 N1+ ANISOU 2172 NZ LYS A1083 13532 24002 17004 -1149 1481 1168 N1+ ATOM 2173 N VAL A1084 -4.053 17.444 -8.419 1.00 99.52 N ANISOU 2173 N VAL A1084 8398 17910 11503 -1230 1359 1249 N ATOM 2174 CA VAL A1084 -4.989 16.734 -7.543 1.00 99.17 C ANISOU 2174 CA VAL A1084 8413 17799 11467 -1236 1316 1211 C ATOM 2175 C VAL A1084 -5.262 15.345 -8.150 1.00103.83 C ANISOU 2175 C VAL A1084 8959 18497 11994 -1261 1259 1105 C ATOM 2176 O VAL A1084 -5.463 14.384 -7.407 1.00102.81 O ANISOU 2176 O VAL A1084 8877 18295 11893 -1281 1201 1024 O ATOM 2177 CB VAL A1084 -6.300 17.543 -7.296 1.00103.29 C ANISOU 2177 CB VAL A1084 8954 18324 11967 -1202 1362 1347 C ATOM 2178 CG1 VAL A1084 -7.143 16.915 -6.187 1.00102.59 C ANISOU 2178 CG1 VAL A1084 8937 18136 11908 -1200 1325 1324 C ATOM 2179 CG2 VAL A1084 -5.999 19.002 -6.958 1.00103.26 C ANISOU 2179 CG2 VAL A1084 8991 18239 12006 -1172 1426 1460 C ATOM 2180 N LYS A1085 -5.216 15.243 -9.499 1.00101.84 N ANISOU 2180 N LYS A1085 8624 18414 11657 -1258 1273 1105 N ATOM 2181 CA LYS A1085 -5.435 14.009 -10.260 1.00102.38 C ANISOU 2181 CA LYS A1085 8659 18590 11650 -1279 1216 1002 C ATOM 2182 C LYS A1085 -4.365 12.957 -9.934 1.00106.71 C ANISOU 2182 C LYS A1085 9243 19061 12242 -1295 1165 849 C ATOM 2183 O LYS A1085 -4.714 11.830 -9.581 1.00106.20 O ANISOU 2183 O LYS A1085 9213 18958 12180 -1321 1097 753 O ATOM 2184 CB LYS A1085 -5.444 14.302 -11.775 1.00105.79 C ANISOU 2184 CB LYS A1085 9004 19216 11975 -1262 1251 1044 C ATOM 2185 CG LYS A1085 -5.720 13.069 -12.644 1.00118.98 C ANISOU 2185 CG LYS A1085 10655 21001 13551 -1281 1186 937 C ATOM 2186 CD LYS A1085 -5.632 13.347 -14.141 1.00128.01 C ANISOU 2186 CD LYS A1085 11721 22341 14577 -1258 1218 972 C ATOM 2187 CE LYS A1085 -4.228 13.330 -14.698 1.00135.79 C ANISOU 2187 CE LYS A1085 12682 23367 15545 -1223 1249 913 C ATOM 2188 NZ LYS A1085 -4.191 13.704 -16.137 1.00144.46 N1+ ANISOU 2188 NZ LYS A1085 13707 24662 16520 -1192 1282 953 N1+ ATOM 2189 N GLU A1086 -3.076 13.332 -10.057 1.00103.80 N ANISOU 2189 N GLU A1086 8862 18668 11911 -1278 1199 838 N ATOM 2190 CA GLU A1086 -1.919 12.463 -9.819 1.00103.79 C ANISOU 2190 CA GLU A1086 8881 18604 11950 -1283 1165 713 C ATOM 2191 C GLU A1086 -1.840 11.995 -8.358 1.00106.97 C ANISOU 2191 C GLU A1086 9366 18825 12452 -1309 1116 653 C ATOM 2192 O GLU A1086 -1.366 10.884 -8.108 1.00106.55 O ANISOU 2192 O GLU A1086 9338 18732 12414 -1320 1065 530 O ATOM 2193 CB GLU A1086 -0.621 13.185 -10.212 1.00105.55 C ANISOU 2193 CB GLU A1086 9060 18841 12203 -1260 1218 757 C ATOM 2194 CG GLU A1086 -0.289 13.127 -11.698 1.00117.66 C ANISOU 2194 CG GLU A1086 10512 20558 13636 -1225 1255 761 C ATOM 2195 CD GLU A1086 -1.209 13.814 -12.695 1.00142.23 C ANISOU 2195 CD GLU A1086 13569 23820 16651 -1209 1293 858 C ATOM 2196 OE1 GLU A1086 -1.994 14.706 -12.295 1.00138.50 O ANISOU 2196 OE1 GLU A1086 13101 23316 16206 -1217 1322 973 O ATOM 2197 OE2 GLU A1086 -1.108 13.480 -13.898 1.00138.70 O1- ANISOU 2197 OE2 GLU A1086 13077 23525 16097 -1185 1296 820 O1- ATOM 2198 N ALA A1087 -2.315 12.829 -7.408 1.00102.83 N ANISOU 2198 N ALA A1087 8889 18193 11990 -1313 1132 739 N ATOM 2199 CA ALA A1087 -2.349 12.517 -5.977 1.00101.80 C ANISOU 2199 CA ALA A1087 8841 17892 11945 -1330 1091 698 C ATOM 2200 C ALA A1087 -3.370 11.407 -5.687 1.00105.17 C ANISOU 2200 C ALA A1087 9290 18322 12348 -1346 1034 638 C ATOM 2201 O ALA A1087 -3.123 10.555 -4.831 1.00104.28 O ANISOU 2201 O ALA A1087 9227 18104 12292 -1363 983 551 O ATOM 2202 CB ALA A1087 -2.684 13.767 -5.179 1.00102.23 C ANISOU 2202 CB ALA A1087 8948 17845 12048 -1317 1128 812 C ATOM 2203 N GLN A1088 -4.502 11.415 -6.420 1.00101.87 N ANISOU 2203 N GLN A1088 8829 18028 11848 -1345 1040 691 N ATOM 2204 CA GLN A1088 -5.576 10.423 -6.313 1.00101.60 C ANISOU 2204 CA GLN A1088 8799 18018 11786 -1369 980 658 C ATOM 2205 C GLN A1088 -5.228 9.157 -7.116 1.00105.69 C ANISOU 2205 C GLN A1088 9296 18609 12253 -1393 921 524 C ATOM 2206 O GLN A1088 -5.681 8.067 -6.758 1.00105.23 O ANISOU 2206 O GLN A1088 9262 18517 12203 -1423 851 453 O ATOM 2207 CB GLN A1088 -6.915 11.012 -6.795 1.00103.29 C ANISOU 2207 CB GLN A1088 8971 18340 11935 -1361 1007 788 C ATOM 2208 CG GLN A1088 -7.452 12.128 -5.905 1.00117.56 C ANISOU 2208 CG GLN A1088 10817 20063 13789 -1329 1060 917 C ATOM 2209 CD GLN A1088 -8.732 12.722 -6.433 1.00136.53 C ANISOU 2209 CD GLN A1088 13168 22583 16124 -1311 1099 1059 C ATOM 2210 OE1 GLN A1088 -8.736 13.523 -7.374 1.00132.33 O ANISOU 2210 OE1 GLN A1088 12585 22152 15541 -1293 1154 1130 O ATOM 2211 NE2 GLN A1088 -9.846 12.375 -5.809 1.00128.75 N ANISOU 2211 NE2 GLN A1088 12189 21589 15141 -1314 1076 1114 N ATOM 2212 N ALA A1089 -4.431 9.309 -8.201 1.00102.46 N ANISOU 2212 N ALA A1089 8844 18296 11789 -1374 951 495 N ATOM 2213 CA ALA A1089 -3.984 8.214 -9.069 1.00102.70 C ANISOU 2213 CA ALA A1089 8866 18397 11758 -1378 907 368 C ATOM 2214 C ALA A1089 -2.943 7.350 -8.360 1.00105.98 C ANISOU 2214 C ALA A1089 9331 18689 12249 -1379 876 247 C ATOM 2215 O ALA A1089 -2.974 6.126 -8.492 1.00105.74 O ANISOU 2215 O ALA A1089 9330 18644 12202 -1396 810 132 O ATOM 2216 CB ALA A1089 -3.412 8.766 -10.365 1.00104.16 C ANISOU 2216 CB ALA A1089 8991 18727 11859 -1341 963 393 C ATOM 2217 N ALA A1090 -2.035 7.991 -7.595 1.00101.98 N ANISOU 2217 N ALA A1090 8835 18086 11827 -1364 917 277 N ATOM 2218 CA ALA A1090 -0.997 7.321 -6.809 1.00101.38 C ANISOU 2218 CA ALA A1090 8799 17887 11833 -1365 893 185 C ATOM 2219 C ALA A1090 -1.599 6.676 -5.545 1.00104.40 C ANISOU 2219 C ALA A1090 9245 18137 12287 -1397 833 150 C ATOM 2220 O ALA A1090 -0.986 5.777 -4.963 1.00103.77 O ANISOU 2220 O ALA A1090 9199 17965 12263 -1404 795 53 O ATOM 2221 CB ALA A1090 0.094 8.310 -6.434 1.00101.91 C ANISOU 2221 CB ALA A1090 8854 17898 11967 -1349 946 250 C ATOM 2222 N ALA A1091 -2.799 7.137 -5.128 1.00100.33 N ANISOU 2222 N ALA A1091 8738 17615 11768 -1411 830 236 N ATOM 2223 CA ALA A1091 -3.535 6.597 -3.985 1.00 99.39 C ANISOU 2223 CA ALA A1091 8667 17390 11705 -1434 780 228 C ATOM 2224 C ALA A1091 -4.104 5.223 -4.326 1.00103.12 C ANISOU 2224 C ALA A1091 9141 17897 12144 -1465 704 132 C ATOM 2225 O ALA A1091 -4.105 4.336 -3.475 1.00102.44 O ANISOU 2225 O ALA A1091 9096 17709 12119 -1484 650 64 O ATOM 2226 CB ALA A1091 -4.650 7.544 -3.583 1.00 99.97 C ANISOU 2226 CB ALA A1091 8741 17469 11772 -1426 811 366 C ATOM 2227 N GLU A1092 -4.562 5.039 -5.582 1.00100.11 N ANISOU 2227 N GLU A1092 8718 17656 11662 -1472 694 125 N ATOM 2228 CA GLU A1092 -5.078 3.760 -6.071 1.00100.46 C ANISOU 2228 CA GLU A1092 8772 17737 11661 -1506 611 31 C ATOM 2229 C GLU A1092 -3.914 2.791 -6.308 1.00104.17 C ANISOU 2229 C GLU A1092 9273 18173 12136 -1492 589 -118 C ATOM 2230 O GLU A1092 -4.115 1.577 -6.257 1.00104.08 O ANISOU 2230 O GLU A1092 9296 18124 12124 -1519 513 -219 O ATOM 2231 CB GLU A1092 -5.925 3.941 -7.342 1.00102.81 C ANISOU 2231 CB GLU A1092 9024 18196 11843 -1519 602 77 C ATOM 2232 CG GLU A1092 -7.288 4.571 -7.093 1.00115.46 C ANISOU 2232 CG GLU A1092 10595 19834 13442 -1541 602 219 C ATOM 2233 CD GLU A1092 -8.247 3.736 -6.265 1.00142.52 C ANISOU 2233 CD GLU A1092 14045 23180 16925 -1586 525 220 C ATOM 2234 OE1 GLU A1092 -8.895 2.830 -6.838 1.00142.93 O ANISOU 2234 OE1 GLU A1092 14092 23282 16932 -1635 440 178 O ATOM 2235 OE2 GLU A1092 -8.346 3.982 -5.042 1.00137.36 O1- ANISOU 2235 OE2 GLU A1092 13417 22413 16361 -1573 546 264 O1- ATOM 2236 N GLN A1093 -2.696 3.335 -6.540 1.00100.36 N ANISOU 2236 N GLN A1093 8777 17696 11662 -1447 656 -125 N ATOM 2237 CA GLN A1093 -1.449 2.579 -6.699 1.00100.31 C ANISOU 2237 CA GLN A1093 8790 17656 11666 -1419 654 -243 C ATOM 2238 C GLN A1093 -1.061 1.998 -5.330 1.00103.32 C ANISOU 2238 C GLN A1093 9219 17874 12164 -1435 619 -294 C ATOM 2239 O GLN A1093 -0.541 0.884 -5.260 1.00103.16 O ANISOU 2239 O GLN A1093 9233 17806 12156 -1432 577 -411 O ATOM 2240 CB GLN A1093 -0.341 3.484 -7.283 1.00101.85 C ANISOU 2240 CB GLN A1093 8940 17910 11846 -1368 739 -200 C ATOM 2241 CG GLN A1093 1.033 2.824 -7.488 1.00118.61 C ANISOU 2241 CG GLN A1093 11071 20020 13976 -1325 752 -300 C ATOM 2242 CD GLN A1093 1.116 1.898 -8.679 1.00139.61 C ANISOU 2242 CD GLN A1093 13743 22779 16522 -1294 732 -401 C ATOM 2243 OE1 GLN A1093 0.758 2.252 -9.809 1.00136.38 O ANISOU 2243 OE1 GLN A1093 13306 22504 16007 -1281 748 -370 O ATOM 2244 NE2 GLN A1093 1.681 0.719 -8.468 1.00131.70 N ANISOU 2244 NE2 GLN A1093 12787 21715 15536 -1274 700 -523 N ATOM 2245 N LEU A1094 -1.357 2.751 -4.244 1.00 98.91 N ANISOU 2245 N LEU A1094 8667 17230 11685 -1449 636 -205 N ATOM 2246 CA LEU A1094 -1.125 2.354 -2.852 1.00 97.92 C ANISOU 2246 CA LEU A1094 8586 16952 11666 -1464 606 -231 C ATOM 2247 C LEU A1094 -2.131 1.259 -2.456 1.00101.74 C ANISOU 2247 C LEU A1094 9099 17396 12161 -1501 526 -279 C ATOM 2248 O LEU A1094 -1.795 0.379 -1.663 1.00101.02 O ANISOU 2248 O LEU A1094 9044 17203 12138 -1511 484 -356 O ATOM 2249 CB LEU A1094 -1.243 3.593 -1.924 1.00 97.23 C ANISOU 2249 CB LEU A1094 8508 16800 11636 -1461 647 -113 C ATOM 2250 CG LEU A1094 -0.657 3.557 -0.486 1.00101.17 C ANISOU 2250 CG LEU A1094 9055 17142 12242 -1463 635 -122 C ATOM 2251 CD1 LEU A1094 -1.589 2.894 0.520 1.00100.96 C ANISOU 2251 CD1 LEU A1094 9067 17034 12259 -1485 581 -131 C ATOM 2252 CD2 LEU A1094 0.774 3.031 -0.437 1.00103.63 C ANISOU 2252 CD2 LEU A1094 9367 17410 12598 -1452 636 -205 C ATOM 2253 N LYS A1095 -3.352 1.310 -3.033 1.00 98.64 N ANISOU 2253 N LYS A1095 8686 17090 11704 -1526 503 -226 N ATOM 2254 CA LYS A1095 -4.430 0.346 -2.800 1.00 98.61 C ANISOU 2254 CA LYS A1095 8695 17067 11704 -1571 420 -246 C ATOM 2255 C LYS A1095 -4.039 -1.037 -3.355 1.00103.89 C ANISOU 2255 C LYS A1095 9395 17731 12349 -1585 354 -395 C ATOM 2256 O LYS A1095 -4.331 -2.047 -2.717 1.00103.28 O ANISOU 2256 O LYS A1095 9349 17562 12329 -1615 287 -451 O ATOM 2257 CB LYS A1095 -5.740 0.846 -3.433 1.00100.99 C ANISOU 2257 CB LYS A1095 8955 17484 11932 -1594 414 -140 C ATOM 2258 CG LYS A1095 -6.998 0.152 -2.926 1.00109.71 C ANISOU 2258 CG LYS A1095 10059 18563 13062 -1644 337 -102 C ATOM 2259 CD LYS A1095 -8.240 0.751 -3.564 1.00116.61 C ANISOU 2259 CD LYS A1095 10880 19561 13866 -1663 339 24 C ATOM 2260 CE LYS A1095 -9.507 0.099 -3.074 1.00124.07 C ANISOU 2260 CE LYS A1095 11810 20487 14843 -1712 267 91 C ATOM 2261 NZ LYS A1095 -10.710 0.723 -3.679 1.00132.13 N1+ ANISOU 2261 NZ LYS A1095 12770 21638 15795 -1729 272 228 N1+ ATOM 2262 N THR A1096 -3.345 -1.073 -4.513 1.00101.89 N ANISOU 2262 N THR A1096 9135 17568 12011 -1556 378 -457 N ATOM 2263 CA THR A1096 -2.886 -2.308 -5.168 1.00102.80 C ANISOU 2263 CA THR A1096 9292 17682 12084 -1551 327 -602 C ATOM 2264 C THR A1096 -1.658 -2.905 -4.448 1.00107.03 C ANISOU 2264 C THR A1096 9861 18103 12702 -1517 342 -690 C ATOM 2265 O THR A1096 -1.352 -4.082 -4.652 1.00106.83 O ANISOU 2265 O THR A1096 9884 18041 12667 -1512 294 -811 O ATOM 2266 CB THR A1096 -2.568 -2.060 -6.654 1.00111.63 C ANISOU 2266 CB THR A1096 10396 18943 13074 -1514 359 -629 C ATOM 2267 OG1 THR A1096 -1.539 -1.076 -6.771 1.00110.68 O ANISOU 2267 OG1 THR A1096 10238 18859 12957 -1457 458 -582 O ATOM 2268 CG2 THR A1096 -3.798 -1.647 -7.465 1.00110.55 C ANISOU 2268 CG2 THR A1096 10229 18928 12848 -1552 331 -553 C ATOM 2269 N THR A1097 -0.960 -2.097 -3.618 1.00103.84 N ANISOU 2269 N THR A1097 9436 17641 12377 -1495 404 -626 N ATOM 2270 CA THR A1097 0.218 -2.521 -2.851 1.00103.78 C ANISOU 2270 CA THR A1097 9449 17528 12454 -1468 419 -687 C ATOM 2271 C THR A1097 -0.232 -3.120 -1.507 1.00107.76 C ANISOU 2271 C THR A1097 9984 17898 13062 -1506 364 -690 C ATOM 2272 O THR A1097 0.299 -4.159 -1.107 1.00107.31 O ANISOU 2272 O THR A1097 9960 17756 13056 -1501 332 -782 O ATOM 2273 CB THR A1097 1.207 -1.348 -2.656 1.00112.25 C ANISOU 2273 CB THR A1097 10484 18610 13555 -1432 503 -613 C ATOM 2274 OG1 THR A1097 1.436 -0.697 -3.908 1.00113.43 O ANISOU 2274 OG1 THR A1097 10595 18895 13608 -1398 555 -588 O ATOM 2275 CG2 THR A1097 2.546 -1.793 -2.065 1.00110.53 C ANISOU 2275 CG2 THR A1097 10277 18305 13414 -1404 517 -671 C ATOM 2276 N ARG A1098 -1.204 -2.475 -0.819 1.00104.52 N ANISOU 2276 N ARG A1098 9563 17472 12679 -1537 358 -584 N ATOM 2277 CA ARG A1098 -1.718 -2.943 0.473 1.00104.15 C ANISOU 2277 CA ARG A1098 9539 17308 12723 -1565 313 -568 C ATOM 2278 C ARG A1098 -2.560 -4.219 0.291 1.00109.52 C ANISOU 2278 C ARG A1098 10240 17975 13398 -1608 222 -631 C ATOM 2279 O ARG A1098 -2.606 -5.031 1.213 1.00108.66 O ANISOU 2279 O ARG A1098 10154 17761 13370 -1626 176 -660 O ATOM 2280 CB ARG A1098 -2.512 -1.846 1.223 1.00104.03 C ANISOU 2280 CB ARG A1098 9511 17286 12729 -1569 343 -428 C ATOM 2281 CG ARG A1098 -3.763 -1.303 0.528 1.00116.24 C ANISOU 2281 CG ARG A1098 11025 18939 14201 -1589 340 -338 C ATOM 2282 CD ARG A1098 -5.050 -1.896 1.078 1.00127.52 C ANISOU 2282 CD ARG A1098 12453 20340 15658 -1629 272 -298 C ATOM 2283 NE ARG A1098 -6.231 -1.382 0.382 1.00136.36 N ANISOU 2283 NE ARG A1098 13533 21571 16708 -1648 270 -197 N ATOM 2284 CZ ARG A1098 -7.484 -1.736 0.660 1.00150.06 C ANISOU 2284 CZ ARG A1098 15248 23313 18454 -1684 217 -125 C ATOM 2285 NH1 ARG A1098 -7.734 -2.608 1.627 1.00136.70 N ANISOU 2285 NH1 ARG A1098 13575 21522 16844 -1704 162 -145 N ATOM 2286 NH2 ARG A1098 -8.491 -1.216 -0.025 1.00137.13 N1+ ANISOU 2286 NH2 ARG A1098 13566 21787 16751 -1700 219 -24 N1+ ATOM 2287 N ASN A1099 -3.198 -4.401 -0.889 1.00107.89 N ANISOU 2287 N ASN A1099 10025 17871 13097 -1629 190 -650 N ATOM 2288 CA ASN A1099 -4.000 -5.588 -1.205 1.00108.93 C ANISOU 2288 CA ASN A1099 10181 17994 13214 -1680 90 -709 C ATOM 2289 C ASN A1099 -3.101 -6.805 -1.476 1.00114.47 C ANISOU 2289 C ASN A1099 10937 18639 13919 -1665 54 -866 C ATOM 2290 O ASN A1099 -3.552 -7.939 -1.311 1.00114.21 O ANISOU 2290 O ASN A1099 10940 18544 13913 -1707 -35 -927 O ATOM 2291 CB ASN A1099 -4.931 -5.338 -2.405 1.00111.33 C ANISOU 2291 CB ASN A1099 10462 18430 13411 -1711 62 -669 C ATOM 2292 CG ASN A1099 -6.200 -4.550 -2.115 1.00139.14 C ANISOU 2292 CG ASN A1099 13931 21999 16936 -1740 69 -511 C ATOM 2293 OD1 ASN A1099 -6.732 -3.858 -2.989 1.00134.97 O ANISOU 2293 OD1 ASN A1099 13367 21590 16324 -1741 93 -440 O ATOM 2294 ND2 ASN A1099 -6.745 -4.658 -0.907 1.00131.46 N ANISOU 2294 ND2 ASN A1099 12953 20940 16056 -1757 50 -445 N ATOM 2295 N ALA A1100 -1.839 -6.568 -1.888 1.00112.55 N ANISOU 2295 N ALA A1100 10700 18415 13649 -1602 123 -923 N ATOM 2296 CA ALA A1100 -0.855 -7.621 -2.161 1.00113.66 C ANISOU 2296 CA ALA A1100 10892 18507 13787 -1566 110 -1062 C ATOM 2297 C ALA A1100 -0.301 -8.199 -0.855 1.00118.47 C ANISOU 2297 C ALA A1100 11517 18974 14521 -1564 100 -1089 C ATOM 2298 O ALA A1100 -0.150 -9.417 -0.742 1.00118.37 O ANISOU 2298 O ALA A1100 11555 18883 14538 -1572 39 -1187 O ATOM 2299 CB ALA A1100 0.277 -7.074 -3.019 1.00114.75 C ANISOU 2299 CB ALA A1100 11016 18726 13857 -1492 197 -1085 C ATOM 2300 N TYR A1101 -0.010 -7.321 0.130 1.00115.48 N ANISOU 2300 N TYR A1101 11101 18560 14215 -1554 155 -999 N ATOM 2301 CA TYR A1101 0.510 -7.678 1.454 1.00115.25 C ANISOU 2301 CA TYR A1101 11080 18406 14303 -1551 153 -1003 C ATOM 2302 C TYR A1101 -0.605 -8.204 2.379 1.00119.23 C ANISOU 2302 C TYR A1101 11594 18834 14875 -1606 79 -968 C ATOM 2303 O TYR A1101 -0.304 -8.878 3.370 1.00118.42 O ANISOU 2303 O TYR A1101 11509 18623 14862 -1609 53 -1000 O ATOM 2304 CB TYR A1101 1.205 -6.468 2.103 1.00115.99 C ANISOU 2304 CB TYR A1101 11140 18495 14435 -1525 229 -913 C ATOM 2305 CG TYR A1101 2.636 -6.257 1.653 1.00118.50 C ANISOU 2305 CG TYR A1101 11444 18839 14740 -1470 293 -949 C ATOM 2306 CD1 TYR A1101 2.926 -5.588 0.467 1.00121.05 C ANISOU 2306 CD1 TYR A1101 11740 19282 14970 -1440 346 -932 C ATOM 2307 CD2 TYR A1101 3.703 -6.683 2.440 1.00119.17 C ANISOU 2307 CD2 TYR A1101 11534 18836 14908 -1448 305 -983 C ATOM 2308 CE1 TYR A1101 4.242 -5.377 0.058 1.00122.25 C ANISOU 2308 CE1 TYR A1101 11868 19467 15114 -1386 408 -947 C ATOM 2309 CE2 TYR A1101 5.023 -6.474 2.044 1.00120.44 C ANISOU 2309 CE2 TYR A1101 11672 19029 15062 -1397 365 -997 C ATOM 2310 CZ TYR A1101 5.289 -5.818 0.853 1.00128.91 C ANISOU 2310 CZ TYR A1101 12713 20222 16043 -1366 417 -975 C ATOM 2311 OH TYR A1101 6.590 -5.607 0.463 1.00131.01 O ANISOU 2311 OH TYR A1101 12946 20527 16306 -1313 479 -973 O ATOM 2312 N ILE A1102 -1.885 -7.908 2.049 1.00116.13 N ANISOU 2312 N ILE A1102 11182 18503 14439 -1649 47 -892 N ATOM 2313 CA ILE A1102 -3.055 -8.356 2.809 1.00115.81 C ANISOU 2313 CA ILE A1102 11136 18412 14455 -1701 -22 -835 C ATOM 2314 C ILE A1102 -3.275 -9.863 2.532 1.00120.87 C ANISOU 2314 C ILE A1102 11816 18998 15111 -1739 -118 -942 C ATOM 2315 O ILE A1102 -3.898 -10.540 3.339 1.00120.13 O ANISOU 2315 O ILE A1102 11723 18825 15094 -1776 -179 -921 O ATOM 2316 CB ILE A1102 -4.300 -7.468 2.478 1.00118.90 C ANISOU 2316 CB ILE A1102 11486 18901 14790 -1729 -21 -708 C ATOM 2317 CG1 ILE A1102 -4.858 -6.695 3.703 1.00118.45 C ANISOU 2317 CG1 ILE A1102 11404 18807 14795 -1723 8 -572 C ATOM 2318 CG2 ILE A1102 -5.376 -8.124 1.591 1.00120.66 C ANISOU 2318 CG2 ILE A1102 11707 19187 14953 -1789 -108 -721 C ATOM 2319 CD1 ILE A1102 -5.516 -7.505 4.845 1.00125.95 C ANISOU 2319 CD1 ILE A1102 12353 19666 15835 -1756 -59 -541 C ATOM 2320 N GLN A1103 -2.740 -10.380 1.412 1.00119.01 N ANISOU 2320 N GLN A1103 11618 18800 14800 -1723 -129 -1054 N ATOM 2321 CA GLN A1103 -2.836 -11.794 1.038 1.00120.16 C ANISOU 2321 CA GLN A1103 11822 18889 14943 -1750 -218 -1173 C ATOM 2322 C GLN A1103 -1.779 -12.634 1.771 1.00124.54 C ANISOU 2322 C GLN A1103 12413 19324 15583 -1712 -209 -1262 C ATOM 2323 O GLN A1103 -2.034 -13.799 2.085 1.00124.75 O ANISOU 2323 O GLN A1103 12480 19259 15661 -1745 -291 -1324 O ATOM 2324 CB GLN A1103 -2.670 -11.969 -0.484 1.00122.66 C ANISOU 2324 CB GLN A1103 12179 19297 15130 -1734 -226 -1259 C ATOM 2325 CG GLN A1103 -3.792 -11.364 -1.323 1.00138.36 C ANISOU 2325 CG GLN A1103 14139 21400 17030 -1785 -263 -1185 C ATOM 2326 CD GLN A1103 -3.494 -11.462 -2.798 1.00158.33 C ANISOU 2326 CD GLN A1103 16713 24022 19425 -1759 -264 -1273 C ATOM 2327 OE1 GLN A1103 -3.643 -12.519 -3.422 1.00154.90 O ANISOU 2327 OE1 GLN A1103 16349 23559 18946 -1784 -351 -1378 O ATOM 2328 NE2 GLN A1103 -3.077 -10.355 -3.392 1.00150.03 N ANISOU 2328 NE2 GLN A1103 15623 23080 18301 -1706 -170 -1230 N ATOM 2329 N LYS A1104 -0.593 -12.037 2.032 1.00120.69 N ANISOU 2329 N LYS A1104 11909 18836 15112 -1646 -115 -1263 N ATOM 2330 CA LYS A1104 0.559 -12.679 2.673 1.00120.36 C ANISOU 2330 CA LYS A1104 11889 18697 15144 -1600 -92 -1335 C ATOM 2331 C LYS A1104 0.462 -12.671 4.212 1.00122.92 C ANISOU 2331 C LYS A1104 12187 18923 15593 -1618 -96 -1267 C ATOM 2332 O LYS A1104 0.953 -13.612 4.840 1.00122.41 O ANISOU 2332 O LYS A1104 12146 18760 15605 -1604 -114 -1327 O ATOM 2333 CB LYS A1104 1.859 -11.979 2.232 1.00122.91 C ANISOU 2333 CB LYS A1104 12197 19078 15426 -1525 8 -1350 C ATOM 2334 CG LYS A1104 3.078 -12.897 2.151 1.00138.31 C ANISOU 2334 CG LYS A1104 14185 20967 17401 -1464 28 -1457 C ATOM 2335 CD LYS A1104 3.953 -12.839 3.402 1.00147.81 C ANISOU 2335 CD LYS A1104 15355 22092 18714 -1442 70 -1419 C ATOM 2336 CE LYS A1104 5.117 -13.801 3.345 1.00159.88 C ANISOU 2336 CE LYS A1104 16915 23558 20275 -1382 87 -1515 C ATOM 2337 NZ LYS A1104 4.683 -15.221 3.456 1.00169.93 N1+ ANISOU 2337 NZ LYS A1104 18249 24729 21589 -1407 4 -1601 N1+ ATOM 2338 N TYR A1105 -0.141 -11.622 4.818 1.00118.46 N ANISOU 2338 N TYR A1105 11578 18385 15044 -1641 -78 -1143 N ATOM 2339 CA TYR A1105 -0.252 -11.534 6.276 1.00117.25 C ANISOU 2339 CA TYR A1105 11408 18146 14994 -1648 -78 -1074 C ATOM 2340 C TYR A1105 -1.641 -11.961 6.773 1.00120.40 C ANISOU 2340 C TYR A1105 11798 18514 15436 -1705 -155 -1012 C ATOM 2341 O TYR A1105 -1.706 -12.679 7.773 1.00119.81 O ANISOU 2341 O TYR A1105 11728 18341 15453 -1714 -190 -1016 O ATOM 2342 CB TYR A1105 0.079 -10.128 6.790 1.00117.71 C ANISOU 2342 CB TYR A1105 11438 18238 15051 -1620 -1 -976 C ATOM 2343 CG TYR A1105 0.975 -10.148 8.011 1.00119.21 C ANISOU 2343 CG TYR A1105 11629 18336 15328 -1593 26 -972 C ATOM 2344 CD1 TYR A1105 2.361 -10.156 7.884 1.00121.51 C ANISOU 2344 CD1 TYR A1105 11923 18617 15627 -1553 70 -1033 C ATOM 2345 CD2 TYR A1105 0.437 -10.176 9.295 1.00119.37 C ANISOU 2345 CD2 TYR A1105 11649 18284 15422 -1604 7 -902 C ATOM 2346 CE1 TYR A1105 3.193 -10.179 9.004 1.00122.00 C ANISOU 2346 CE1 TYR A1105 11984 18599 15771 -1534 87 -1023 C ATOM 2347 CE2 TYR A1105 1.257 -10.196 10.423 1.00119.79 C ANISOU 2347 CE2 TYR A1105 11709 18256 15551 -1580 25 -900 C ATOM 2348 CZ TYR A1105 2.636 -10.198 10.273 1.00127.38 C ANISOU 2348 CZ TYR A1105 12671 19208 16521 -1550 62 -961 C ATOM 2349 OH TYR A1105 3.450 -10.219 11.380 1.00127.38 O ANISOU 2349 OH TYR A1105 12673 19132 16595 -1533 74 -952 O ATOM 2350 N LEU A1106 -2.741 -11.539 6.095 1.00116.62 N ANISOU 2350 N LEU A1106 11299 18119 14894 -1743 -179 -945 N ATOM 2351 CA LEU A1106 -4.097 -11.946 6.495 1.00116.27 C ANISOU 2351 CA LEU A1106 11231 18058 14888 -1799 -253 -864 C ATOM 2352 C LEU A1106 -4.316 -13.415 6.140 1.00120.03 C ANISOU 2352 C LEU A1106 11740 18471 15395 -1848 -356 -957 C ATOM 2353 O LEU A1106 -3.561 -13.987 5.346 1.00120.25 O ANISOU 2353 O LEU A1106 11815 18492 15381 -1837 -368 -1083 O ATOM 2354 CB LEU A1106 -5.199 -11.070 5.897 1.00116.53 C ANISOU 2354 CB LEU A1106 11227 18205 14845 -1825 -251 -758 C ATOM 2355 N ARG A 248 -5.324 -14.029 6.777 1.00115.94 N ANISOU 2355 N ARG A 248 11199 17901 14952 -1898 -428 -889 N ATOM 2356 CA ARG A 248 -5.653 -15.457 6.765 1.00116.37 C ANISOU 2356 CA ARG A 248 11280 17874 15061 -1955 -538 -951 C ATOM 2357 C ARG A 248 -4.639 -16.184 7.646 1.00118.94 C ANISOU 2357 C ARG A 248 11638 18078 15477 -1918 -527 -1036 C ATOM 2358 O ARG A 248 -4.999 -17.197 8.246 1.00118.74 O ANISOU 2358 O ARG A 248 11618 17961 15536 -1956 -603 -1047 O ATOM 2359 CB ARG A 248 -5.757 -16.090 5.361 1.00118.53 C ANISOU 2359 CB ARG A 248 11603 18184 15249 -1997 -609 -1052 C ATOM 2360 CG ARG A 248 -6.987 -15.639 4.542 1.00131.63 C ANISOU 2360 CG ARG A 248 13227 19957 16831 -2055 -651 -962 C ATOM 2361 CD ARG A 248 -8.338 -16.245 4.974 1.00144.15 C ANISOU 2361 CD ARG A 248 14781 21512 18480 -2145 -769 -877 C ATOM 2362 NE ARG A 248 -9.454 -15.893 4.080 1.00155.01 N ANISOU 2362 NE ARG A 248 16126 22996 19774 -2208 -824 -803 N ATOM 2363 CZ ARG A 248 -10.460 -15.075 4.393 1.00169.89 C ANISOU 2363 CZ ARG A 248 17930 24971 21649 -2217 -795 -635 C ATOM 2364 NH1 ARG A 248 -10.514 -14.502 5.591 1.00156.86 N ANISOU 2364 NH1 ARG A 248 16232 23310 20058 -2162 -711 -528 N ATOM 2365 NH2 ARG A 248 -11.420 -14.826 3.512 1.00157.30 N1+ ANISOU 2365 NH2 ARG A 248 16308 23480 19981 -2277 -850 -570 N1+ ATOM 2366 N ASN A 249 -3.416 -15.619 7.806 1.00114.28 N ANISOU 2366 N ASN A 249 11061 17489 14872 -1846 -433 -1085 N ATOM 2367 CA ASN A 249 -2.379 -16.177 8.671 1.00113.49 C ANISOU 2367 CA ASN A 249 10982 17291 14849 -1801 -405 -1152 C ATOM 2368 C ASN A 249 -2.389 -15.528 10.081 1.00115.35 C ANISOU 2368 C ASN A 249 11178 17506 15146 -1769 -345 -1051 C ATOM 2369 O ASN A 249 -2.091 -16.223 11.055 1.00114.49 O ANISOU 2369 O ASN A 249 11071 17306 15123 -1748 -343 -1069 O ATOM 2370 CB ASN A 249 -1.012 -16.043 8.027 1.00114.97 C ANISOU 2370 CB ASN A 249 11209 17499 14977 -1745 -348 -1268 C ATOM 2371 CG ASN A 249 -0.842 -16.974 6.853 1.00139.58 C ANISOU 2371 CG ASN A 249 14386 20618 18031 -1761 -406 -1386 C ATOM 2372 OD1 ASN A 249 -0.503 -18.150 7.009 1.00135.09 O ANISOU 2372 OD1 ASN A 249 13856 19962 17512 -1794 -488 -1445 O ATOM 2373 ND2 ASN A 249 -1.102 -16.479 5.650 1.00131.45 N ANISOU 2373 ND2 ASN A 249 13371 19684 16888 -1734 -365 -1424 N ATOM 2374 N ARG A 250 -2.745 -14.232 10.198 1.00110.79 N ANISOU 2374 N ARG A 250 10567 17008 14519 -1761 -297 -943 N ATOM 2375 CA ARG A 250 -2.786 -13.544 11.498 1.00109.35 C ANISOU 2375 CA ARG A 250 10363 16808 14378 -1727 -244 -841 C ATOM 2376 C ARG A 250 -4.047 -13.946 12.299 1.00112.39 C ANISOU 2376 C ARG A 250 10715 17167 14819 -1757 -295 -731 C ATOM 2377 O ARG A 250 -4.028 -13.891 13.529 1.00111.25 O ANISOU 2377 O ARG A 250 10564 16965 14740 -1729 -277 -674 O ATOM 2378 CB ARG A 250 -2.710 -12.008 11.330 1.00109.12 C ANISOU 2378 CB ARG A 250 10328 16865 14269 -1695 -165 -779 C ATOM 2379 CG ARG A 250 -3.878 -11.355 10.581 1.00119.56 C ANISOU 2379 CG ARG A 250 11625 18288 15516 -1722 -173 -695 C ATOM 2380 CD ARG A 250 -3.835 -9.839 10.663 1.00128.38 C ANISOU 2380 CD ARG A 250 12735 19463 16581 -1684 -94 -598 C ATOM 2381 NE ARG A 250 -2.780 -9.269 9.822 1.00135.65 N ANISOU 2381 NE ARG A 250 13670 20429 17440 -1658 -35 -655 N ATOM 2382 CZ ARG A 250 -2.568 -7.964 9.658 1.00147.92 C ANISOU 2382 CZ ARG A 250 15224 22038 18942 -1630 31 -587 C ATOM 2383 NH1 ARG A 250 -3.338 -7.077 10.273 1.00134.70 N ANISOU 2383 NH1 ARG A 250 13544 20377 17260 -1616 52 -464 N ATOM 2384 NH2 ARG A 250 -1.585 -7.541 8.874 1.00133.63 N1+ ANISOU 2384 NH2 ARG A 250 13419 20268 17086 -1611 78 -635 N1+ ATOM 2385 N ASP A 251 -5.128 -14.346 11.595 1.00109.21 N ANISOU 2385 N ASP A 251 10293 16809 14393 -1814 -361 -700 N ATOM 2386 CA ASP A 251 -6.396 -14.782 12.185 1.00108.98 C ANISOU 2386 CA ASP A 251 10220 16771 14417 -1851 -419 -580 C ATOM 2387 C ASP A 251 -6.222 -16.099 12.926 1.00111.31 C ANISOU 2387 C ASP A 251 10518 16955 14821 -1876 -489 -621 C ATOM 2388 O ASP A 251 -6.853 -16.287 13.957 1.00110.81 O ANISOU 2388 O ASP A 251 10412 16867 14823 -1893 -526 -513 O ATOM 2389 CB ASP A 251 -7.482 -14.930 11.112 1.00111.96 C ANISOU 2389 CB ASP A 251 10571 17235 14733 -1913 -476 -532 C ATOM 2390 CG ASP A 251 -7.861 -13.628 10.439 1.00124.79 C ANISOU 2390 CG ASP A 251 12184 18975 16256 -1886 -405 -470 C ATOM 2391 OD1 ASP A 251 -7.157 -13.227 9.485 1.00125.77 O1- ANISOU 2391 OD1 ASP A 251 12342 19132 16313 -1861 -358 -561 O1- ATOM 2392 OD2 ASP A 251 -8.847 -13.004 10.875 1.00131.57 O ANISOU 2392 OD2 ASP A 251 12997 19893 17103 -1886 -394 -323 O ATOM 2393 N THR A 252 -5.371 -17.008 12.397 1.00106.65 N ANISOU 2393 N THR A 252 9975 16301 14248 -1873 -503 -768 N ATOM 2394 CA THR A 252 -5.057 -18.305 13.001 1.00105.97 C ANISOU 2394 CA THR A 252 9901 16099 14265 -1887 -559 -824 C ATOM 2395 C THR A 252 -4.172 -18.085 14.217 1.00107.33 C ANISOU 2395 C THR A 252 10071 16217 14494 -1821 -489 -812 C ATOM 2396 O THR A 252 -4.275 -18.847 15.175 1.00106.54 O ANISOU 2396 O THR A 252 9957 16034 14491 -1822 -521 -792 O ATOM 2397 CB THR A 252 -4.394 -19.271 11.994 1.00113.77 C ANISOU 2397 CB THR A 252 10949 17044 15236 -1907 -606 -984 C ATOM 2398 OG1 THR A 252 -3.235 -18.662 11.419 1.00113.26 O ANISOU 2398 OG1 THR A 252 10917 17020 15095 -1851 -526 -1071 O ATOM 2399 CG2 THR A 252 -5.342 -19.725 10.892 1.00113.12 C ANISOU 2399 CG2 THR A 252 10878 16993 15111 -1985 -703 -995 C ATOM 2400 N MET A 253 -3.314 -17.038 14.182 1.00102.44 N ANISOU 2400 N MET A 253 9463 15644 13814 -1766 -399 -816 N ATOM 2401 CA MET A 253 -2.404 -16.663 15.269 1.00101.05 C ANISOU 2401 CA MET A 253 9292 15427 13677 -1708 -336 -800 C ATOM 2402 C MET A 253 -3.168 -16.044 16.445 1.00103.03 C ANISOU 2402 C MET A 253 9516 15691 13940 -1686 -312 -654 C ATOM 2403 O MET A 253 -2.927 -16.427 17.589 1.00102.14 O ANISOU 2403 O MET A 253 9406 15521 13883 -1649 -291 -626 O ATOM 2404 CB MET A 253 -1.316 -15.688 14.775 1.00103.12 C ANISOU 2404 CB MET A 253 9580 15730 13872 -1669 -261 -860 C ATOM 2405 CG MET A 253 -0.131 -16.381 14.131 1.00107.52 C ANISOU 2405 CG MET A 253 10165 16273 14416 -1667 -266 -998 C ATOM 2406 SD MET A 253 0.861 -17.426 15.249 1.00112.13 S ANISOU 2406 SD MET A 253 10760 16734 15109 -1654 -297 -1082 S ATOM 2407 CE MET A 253 0.907 -18.976 14.251 1.00110.02 C ANISOU 2407 CE MET A 253 10519 16440 14841 -1708 -390 -1161 C ATOM 2408 N MET A 254 -4.098 -15.112 16.163 1.00 98.58 N ANISOU 2408 N MET A 254 8930 15207 13318 -1701 -311 -559 N ATOM 2409 CA MET A 254 -4.902 -14.418 17.179 1.00 97.45 C ANISOU 2409 CA MET A 254 8764 15088 13173 -1669 -283 -407 C ATOM 2410 C MET A 254 -5.942 -15.358 17.837 1.00 98.86 C ANISOU 2410 C MET A 254 8899 15219 13442 -1692 -347 -333 C ATOM 2411 O MET A 254 -6.291 -15.157 19.008 1.00 97.73 O ANISOU 2411 O MET A 254 8749 15043 13340 -1645 -323 -249 O ATOM 2412 CB MET A 254 -5.597 -13.187 16.572 1.00100.21 C ANISOU 2412 CB MET A 254 9099 15545 13431 -1674 -258 -323 C ATOM 2413 CG MET A 254 -4.644 -12.011 16.348 1.00103.90 C ANISOU 2413 CG MET A 254 9604 16062 13812 -1643 -186 -365 C ATOM 2414 SD MET A 254 -5.425 -10.480 15.737 1.00108.58 S ANISOU 2414 SD MET A 254 10181 16774 14301 -1630 -139 -244 S ATOM 2415 CE MET A 254 -5.754 -10.918 14.025 1.00106.18 C ANISOU 2415 CE MET A 254 9836 16539 13970 -1714 -218 -275 C ATOM 2416 N SER A 255 -6.411 -16.385 17.089 1.00 94.35 N ANISOU 2416 N SER A 255 8304 14643 12901 -1764 -433 -363 N ATOM 2417 CA SER A 255 -7.364 -17.397 17.568 1.00 93.72 C ANISOU 2417 CA SER A 255 8178 14516 12915 -1805 -512 -297 C ATOM 2418 C SER A 255 -6.727 -18.258 18.658 1.00 94.73 C ANISOU 2418 C SER A 255 8316 14535 13141 -1783 -521 -348 C ATOM 2419 O SER A 255 -7.403 -18.647 19.618 1.00 94.32 O ANISOU 2419 O SER A 255 8222 14447 13166 -1776 -545 -250 O ATOM 2420 CB SER A 255 -7.845 -18.280 16.416 1.00 98.33 C ANISOU 2420 CB SER A 255 8755 15107 13500 -1896 -610 -349 C ATOM 2421 OG SER A 255 -8.734 -19.303 16.843 1.00107.78 O ANISOU 2421 OG SER A 255 9910 16243 14797 -1948 -700 -295 O ATOM 2422 N LEU A 256 -5.427 -18.574 18.483 1.00 88.90 N ANISOU 2422 N LEU A 256 7627 13751 12400 -1769 -500 -493 N ATOM 2423 CA LEU A 256 -4.638 -19.367 19.418 1.00 87.33 C ANISOU 2423 CA LEU A 256 7442 13455 12286 -1744 -500 -556 C ATOM 2424 C LEU A 256 -4.141 -18.483 20.557 1.00 87.88 C ANISOU 2424 C LEU A 256 7512 13519 12361 -1672 -430 -481 C ATOM 2425 O LEU A 256 -4.002 -18.971 21.674 1.00 87.43 O ANISOU 2425 O LEU A 256 7434 13401 12386 -1653 -443 -437 O ATOM 2426 CB LEU A 256 -3.466 -20.035 18.689 1.00 87.46 C ANISOU 2426 CB LEU A 256 7508 13445 12277 -1742 -488 -719 C ATOM 2427 CG LEU A 256 -2.747 -21.157 19.432 1.00 92.23 C ANISOU 2427 CG LEU A 256 8129 13949 12965 -1724 -496 -809 C ATOM 2428 CD1 LEU A 256 -3.601 -22.421 19.485 1.00 93.07 C ANISOU 2428 CD1 LEU A 256 8215 13976 13173 -1771 -584 -797 C ATOM 2429 CD2 LEU A 256 -1.446 -21.458 18.764 1.00 95.13 C ANISOU 2429 CD2 LEU A 256 8544 14317 13285 -1714 -475 -953 C ATOM 2430 N LEU A 257 -3.888 -17.188 20.279 1.00 82.01 N ANISOU 2430 N LEU A 257 6794 12838 11527 -1632 -359 -460 N ATOM 2431 CA LEU A 257 -3.419 -16.207 21.262 1.00 80.29 C ANISOU 2431 CA LEU A 257 6597 12616 11292 -1564 -295 -394 C ATOM 2432 C LEU A 257 -4.495 -15.967 22.341 1.00 81.39 C ANISOU 2432 C LEU A 257 6704 12773 11446 -1536 -296 -237 C ATOM 2433 O LEU A 257 -4.169 -15.965 23.530 1.00 80.30 O ANISOU 2433 O LEU A 257 6579 12601 11330 -1479 -267 -181 O ATOM 2434 CB LEU A 257 -3.036 -14.888 20.564 1.00 80.14 C ANISOU 2434 CB LEU A 257 6620 12658 11171 -1540 -231 -411 C ATOM 2435 CG LEU A 257 -2.319 -13.820 21.408 1.00 84.52 C ANISOU 2435 CG LEU A 257 7222 13188 11705 -1480 -174 -391 C ATOM 2436 CD1 LEU A 257 -0.815 -14.090 21.521 1.00 84.59 C ANISOU 2436 CD1 LEU A 257 7248 13139 11754 -1481 -173 -502 C ATOM 2437 CD2 LEU A 257 -2.547 -12.433 20.826 1.00 87.04 C ANISOU 2437 CD2 LEU A 257 7577 13572 11923 -1458 -120 -357 C ATOM 2438 N LYS A 258 -5.769 -15.812 21.919 1.00 76.74 N ANISOU 2438 N LYS A 258 6073 12243 10842 -1573 -329 -160 N ATOM 2439 CA LYS A 258 -6.912 -15.610 22.818 1.00 75.95 C ANISOU 2439 CA LYS A 258 5925 12174 10759 -1550 -333 7 C ATOM 2440 C LYS A 258 -7.141 -16.843 23.724 1.00 77.58 C ANISOU 2440 C LYS A 258 6095 12304 11077 -1547 -375 39 C ATOM 2441 O LYS A 258 -7.486 -16.686 24.893 1.00 76.77 O ANISOU 2441 O LYS A 258 5993 12190 10986 -1478 -337 133 O ATOM 2442 CB LYS A 258 -8.201 -15.290 22.021 1.00 79.32 C ANISOU 2442 CB LYS A 258 6300 12676 11161 -1612 -379 71 C ATOM 2443 CG LYS A 258 -8.800 -16.477 21.271 1.00 95.71 C ANISOU 2443 CG LYS A 258 8298 14773 13295 -1619 -419 242 C ATOM 2444 CD LYS A 258 -10.259 -16.308 20.844 1.00105.81 C ANISOU 2444 CD LYS A 258 9520 16128 14556 -1695 -480 309 C ATOM 2445 CE LYS A 258 -10.602 -17.136 19.615 1.00115.34 C ANISOU 2445 CE LYS A 258 10728 17300 15796 -1801 -578 182 C ATOM 2446 NZ LYS A 258 -10.314 -18.594 19.759 1.00122.95 N1+ ANISOU 2446 NZ LYS A 258 11673 18162 16879 -1839 -652 149 N1+ ATOM 2447 N THR A 259 -6.969 -18.061 23.161 1.00 72.72 N ANISOU 2447 N THR A 259 5459 11632 10539 -1617 -451 -48 N ATOM 2448 CA THR A 259 -7.148 -19.343 23.847 1.00 71.89 C ANISOU 2448 CA THR A 259 5318 11447 10551 -1628 -501 -30 C ATOM 2449 C THR A 259 -6.147 -19.455 25.007 1.00 72.34 C ANISOU 2449 C THR A 259 5409 11443 10632 -1559 -451 -66 C ATOM 2450 O THR A 259 -6.528 -19.883 26.096 1.00 71.56 O ANISOU 2450 O THR A 259 5279 11317 10592 -1520 -450 27 O ATOM 2451 CB THR A 259 -6.998 -20.496 22.839 1.00 81.49 C ANISOU 2451 CB THR A 259 6533 12605 11826 -1714 -587 -148 C ATOM 2452 OG1 THR A 259 -7.901 -20.278 21.746 1.00 83.06 O ANISOU 2452 OG1 THR A 259 6721 12865 11972 -1778 -630 -144 O ATOM 2453 CG2 THR A 259 -7.255 -21.880 23.463 1.00 80.88 C ANISOU 2453 CG2 THR A 259 6406 12449 11877 -1743 -657 -104 C ATOM 2454 N VAL A 260 -4.893 -19.020 24.771 1.00 66.74 N ANISOU 2454 N VAL A 260 4760 10722 9875 -1544 -410 -191 N ATOM 2455 CA VAL A 260 -3.779 -19.012 25.721 1.00 65.20 C ANISOU 2455 CA VAL A 260 4603 10476 9694 -1494 -369 -245 C ATOM 2456 C VAL A 260 -4.097 -18.072 26.905 1.00 66.47 C ANISOU 2456 C VAL A 260 4783 10657 9816 -1412 -314 -128 C ATOM 2457 O VAL A 260 -3.860 -18.450 28.060 1.00 66.13 O ANISOU 2457 O VAL A 260 4741 10562 9823 -1373 -309 -110 O ATOM 2458 CB VAL A 260 -2.467 -18.614 24.983 1.00 68.97 C ANISOU 2458 CB VAL A 260 5132 10965 10110 -1504 -339 -379 C ATOM 2459 CG1 VAL A 260 -1.408 -18.086 25.935 1.00 68.21 C ANISOU 2459 CG1 VAL A 260 5082 10854 9981 -1449 -283 -394 C ATOM 2460 CG2 VAL A 260 -1.917 -19.785 24.178 1.00 69.28 C ANISOU 2460 CG2 VAL A 260 5166 10952 10206 -1552 -383 -507 C ATOM 2461 N VAL A 261 -4.659 -16.878 26.615 1.00 60.93 N ANISOU 2461 N VAL A 261 4100 10027 9023 -1384 -273 -49 N ATOM 2462 CA VAL A 261 -4.993 -15.880 27.631 1.00 59.45 C ANISOU 2462 CA VAL A 261 3952 9858 8780 -1296 -216 57 C ATOM 2463 C VAL A 261 -6.166 -16.384 28.512 1.00 61.31 C ANISOU 2463 C VAL A 261 4131 10103 9061 -1258 -226 212 C ATOM 2464 O VAL A 261 -6.191 -16.061 29.702 1.00 61.04 O ANISOU 2464 O VAL A 261 4127 10059 9006 -1175 -187 289 O ATOM 2465 CB VAL A 261 -5.255 -14.453 27.069 1.00 63.28 C ANISOU 2465 CB VAL A 261 4490 10409 9146 -1268 -160 85 C ATOM 2466 CG1 VAL A 261 -4.027 -13.913 26.348 1.00 62.77 C ANISOU 2466 CG1 VAL A 261 4479 10334 9038 -1295 -144 -49 C ATOM 2467 CG2 VAL A 261 -6.491 -14.343 26.201 1.00 63.61 C ANISOU 2467 CG2 VAL A 261 4480 10528 9159 -1299 -171 161 C ATOM 2468 N ILE A 262 -7.077 -17.215 27.948 1.00 55.89 N ANISOU 2468 N ILE A 262 3365 9437 8434 -1316 -281 261 N ATOM 2469 CA ILE A 262 -8.197 -17.806 28.688 1.00 55.09 C ANISOU 2469 CA ILE A 262 3192 9350 8390 -1290 -299 422 C ATOM 2470 C ILE A 262 -7.640 -18.846 29.682 1.00 55.79 C ANISOU 2470 C ILE A 262 3263 9359 8577 -1275 -323 407 C ATOM 2471 O ILE A 262 -8.097 -18.887 30.829 1.00 55.02 O ANISOU 2471 O ILE A 262 3150 9266 8490 -1199 -296 528 O ATOM 2472 CB ILE A 262 -9.278 -18.400 27.730 1.00 59.29 C ANISOU 2472 CB ILE A 262 3641 9922 8963 -1374 -366 481 C ATOM 2473 CG1 ILE A 262 -9.954 -17.265 26.925 1.00 59.78 C ANISOU 2473 CG1 ILE A 262 3718 10073 8923 -1383 -337 507 C ATOM 2474 CG2 ILE A 262 -10.346 -19.240 28.485 1.00 61.07 C ANISOU 2474 CG2 ILE A 262 3778 10163 9263 -1352 -390 665 C ATOM 2475 CD1 ILE A 262 -10.669 -17.687 25.656 1.00 67.97 C ANISOU 2475 CD1 ILE A 262 4698 11143 9984 -1488 -414 501 C ATOM 2476 N VAL A 263 -6.642 -19.649 29.248 1.00 50.46 N ANISOU 2476 N VAL A 263 2593 8615 7966 -1338 -368 262 N ATOM 2477 CA VAL A 263 -5.957 -20.662 30.072 1.00 49.24 C ANISOU 2477 CA VAL A 263 2422 8379 7909 -1331 -392 227 C ATOM 2478 C VAL A 263 -5.226 -19.946 31.232 1.00 50.25 C ANISOU 2478 C VAL A 263 2609 8495 7988 -1238 -329 240 C ATOM 2479 O VAL A 263 -5.326 -20.382 32.384 1.00 49.35 O ANISOU 2479 O VAL A 263 2470 8360 7920 -1185 -325 327 O ATOM 2480 CB VAL A 263 -5.001 -21.563 29.239 1.00 53.05 C ANISOU 2480 CB VAL A 263 2915 8797 8446 -1406 -437 58 C ATOM 2481 CG1 VAL A 263 -4.180 -22.492 30.130 1.00 52.79 C ANISOU 2481 CG1 VAL A 263 2871 8682 8506 -1390 -450 20 C ATOM 2482 CG2 VAL A 263 -5.776 -22.375 28.214 1.00 53.62 C ANISOU 2482 CG2 VAL A 263 2941 8867 8565 -1496 -512 46 C ATOM 2483 N LEU A 264 -4.540 -18.832 30.925 1.00 45.51 N ANISOU 2483 N LEU A 264 2089 7910 7293 -1220 -284 162 N ATOM 2484 CA LEU A 264 -3.810 -18.015 31.898 1.00 44.77 C ANISOU 2484 CA LEU A 264 2069 7802 7141 -1143 -236 168 C ATOM 2485 C LEU A 264 -4.770 -17.248 32.820 1.00 48.67 C ANISOU 2485 C LEU A 264 2585 8346 7562 -1051 -188 322 C ATOM 2486 O LEU A 264 -4.495 -17.127 34.015 1.00 47.95 O ANISOU 2486 O LEU A 264 2540 8235 7443 -973 -160 366 O ATOM 2487 CB LEU A 264 -2.880 -17.031 31.173 1.00 44.33 C ANISOU 2487 CB LEU A 264 2089 7745 7011 -1161 -212 48 C ATOM 2488 CG LEU A 264 -1.730 -16.468 31.996 1.00 48.34 C ANISOU 2488 CG LEU A 264 2639 8194 7534 -1146 -211 -26 C ATOM 2489 CD1 LEU A 264 -0.414 -17.034 31.532 1.00 48.13 C ANISOU 2489 CD1 LEU A 264 2598 8141 7548 -1217 -235 -165 C ATOM 2490 CD2 LEU A 264 -1.700 -14.969 31.938 1.00 50.46 C ANISOU 2490 CD2 LEU A 264 3006 8470 7698 -1087 -170 -7 C ATOM 2491 N GLY A 265 -5.867 -16.740 32.250 1.00 45.84 N ANISOU 2491 N GLY A 265 2193 8053 7171 -1058 -180 405 N ATOM 2492 CA GLY A 265 -6.895 -15.998 32.973 1.00 46.10 C ANISOU 2492 CA GLY A 265 2235 8143 7138 -966 -130 567 C ATOM 2493 C GLY A 265 -7.557 -16.823 34.053 1.00 51.33 C ANISOU 2493 C GLY A 265 2825 8800 7877 -922 -143 695 C ATOM 2494 O GLY A 265 -7.695 -16.365 35.190 1.00 50.87 O ANISOU 2494 O GLY A 265 2808 8747 7775 -816 -96 786 O ATOM 2495 N ALA A 266 -7.944 -18.062 33.700 1.00 49.22 N ANISOU 2495 N ALA A 266 2459 8515 7727 -1003 -210 696 N ATOM 2496 CA ALA A 266 -8.578 -19.026 34.606 1.00 50.09 C ANISOU 2496 CA ALA A 266 2480 8616 7937 -986 -238 817 C ATOM 2497 C ALA A 266 -7.617 -19.464 35.709 1.00 54.76 C ANISOU 2497 C ALA A 266 3098 9141 8569 -940 -234 780 C ATOM 2498 O ALA A 266 -8.055 -19.724 36.833 1.00 54.86 O ANISOU 2498 O ALA A 266 3068 9162 8616 -871 -222 911 O ATOM 2499 CB ALA A 266 -9.058 -20.236 33.825 1.00 51.35 C ANISOU 2499 CB ALA A 266 2543 8754 8211 -1104 -324 799 C ATOM 2500 N PHE A 267 -6.308 -19.527 35.381 1.00 51.29 N ANISOU 2500 N PHE A 267 2721 8643 8123 -974 -242 613 N ATOM 2501 CA PHE A 267 -5.227 -19.904 36.291 1.00 51.03 C ANISOU 2501 CA PHE A 267 2712 8549 8127 -941 -243 567 C ATOM 2502 C PHE A 267 -5.032 -18.842 37.373 1.00 54.89 C ANISOU 2502 C PHE A 267 3283 9057 8514 -821 -182 639 C ATOM 2503 O PHE A 267 -4.828 -19.199 38.527 1.00 54.27 O ANISOU 2503 O PHE A 267 3180 8974 8464 -752 -173 737 O ATOM 2504 CB PHE A 267 -3.914 -20.119 35.506 1.00 52.45 C ANISOU 2504 CB PHE A 267 2935 8674 8320 -1010 -265 383 C ATOM 2505 CG PHE A 267 -2.815 -20.837 36.258 1.00 53.88 C ANISOU 2505 CG PHE A 267 3117 8790 8565 -999 -279 329 C ATOM 2506 CD1 PHE A 267 -2.696 -22.222 36.195 1.00 57.42 C ANISOU 2506 CD1 PHE A 267 3482 9192 9144 -1037 -325 332 C ATOM 2507 CD2 PHE A 267 -1.872 -20.125 36.993 1.00 56.01 C ANISOU 2507 CD2 PHE A 267 3473 9043 8767 -961 -253 271 C ATOM 2508 CE1 PHE A 267 -1.674 -22.886 36.884 1.00 58.59 C ANISOU 2508 CE1 PHE A 267 3627 9284 9352 -1026 -335 286 C ATOM 2509 CE2 PHE A 267 -0.847 -20.786 37.678 1.00 58.90 C ANISOU 2509 CE2 PHE A 267 3832 9354 9191 -958 -271 225 C ATOM 2510 CZ PHE A 267 -0.750 -22.160 37.614 1.00 57.39 C ANISOU 2510 CZ PHE A 267 3553 9123 9129 -987 -307 234 C ATOM 2511 N ILE A 268 -5.108 -17.546 37.010 1.00 52.31 N ANISOU 2511 N ILE A 268 3057 8753 8066 -794 -141 598 N ATOM 2512 CA ILE A 268 -4.933 -16.425 37.947 1.00 52.89 C ANISOU 2512 CA ILE A 268 3240 8834 8022 -683 -87 644 C ATOM 2513 C ILE A 268 -6.155 -16.335 38.898 1.00 58.68 C ANISOU 2513 C ILE A 268 3947 9623 8725 -573 -43 836 C ATOM 2514 O ILE A 268 -5.969 -16.335 40.112 1.00 58.45 O ANISOU 2514 O ILE A 268 3970 9585 8655 -472 -15 897 O ATOM 2515 CB ILE A 268 -4.677 -15.086 37.186 1.00 55.92 C ANISOU 2515 CB ILE A 268 3727 9228 8293 -694 -60 565 C ATOM 2516 CG1 ILE A 268 -3.306 -15.122 36.453 1.00 56.26 C ANISOU 2516 CG1 ILE A 268 3807 9213 8357 -774 -96 397 C ATOM 2517 CG2 ILE A 268 -4.742 -13.870 38.139 1.00 56.76 C ANISOU 2517 CG2 ILE A 268 3955 9347 8262 -572 0 639 C ATOM 2518 CD1 ILE A 268 -3.071 -14.031 35.381 1.00 65.45 C ANISOU 2518 CD1 ILE A 268 5030 10387 9451 -825 -86 303 C ATOM 2519 N ILE A 269 -7.381 -16.301 38.340 1.00 56.61 N ANISOU 2519 N ILE A 269 3599 9421 8488 -591 -40 936 N ATOM 2520 CA ILE A 269 -8.663 -16.182 39.056 1.00 57.41 C ANISOU 2520 CA ILE A 269 3659 9587 8567 -487 4 1137 C ATOM 2521 C ILE A 269 -8.821 -17.271 40.163 1.00 62.08 C ANISOU 2521 C ILE A 269 4186 10160 9241 -439 -9 1223 C ATOM 2522 O ILE A 269 -9.390 -16.962 41.215 1.00 62.42 O ANISOU 2522 O ILE A 269 4279 10224 9213 -308 45 1326 O ATOM 2523 CB ILE A 269 -9.853 -16.222 38.031 1.00 60.91 C ANISOU 2523 CB ILE A 269 3999 10102 9044 -538 -6 1237 C ATOM 2524 CG1 ILE A 269 -9.877 -14.914 37.191 1.00 61.36 C ANISOU 2524 CG1 ILE A 269 4129 10195 8991 -546 29 1191 C ATOM 2525 CG2 ILE A 269 -11.225 -16.449 38.707 1.00 61.89 C ANISOU 2525 CG2 ILE A 269 4044 10296 9175 -438 31 1469 C ATOM 2526 CD1 ILE A 269 -10.737 -14.950 35.887 1.00 70.69 C ANISOU 2526 CD1 ILE A 269 5215 11441 10204 -627 4 1248 C ATOM 2527 N CYS A 270 -8.298 -18.497 39.958 1.00 58.23 N ANISOU 2527 N CYS A 270 3597 9633 8895 -537 -78 1183 N ATOM 2528 CA CYS A 270 -8.468 -19.570 40.944 1.00 58.27 C ANISOU 2528 CA CYS A 270 3527 9625 8989 -495 -92 1281 C ATOM 2529 C CYS A 270 -7.268 -19.690 41.911 1.00 60.03 C ANISOU 2529 C CYS A 270 3814 9779 9214 -470 -98 1180 C ATOM 2530 O CYS A 270 -7.481 -20.083 43.058 1.00 59.92 O ANISOU 2530 O CYS A 270 3762 9766 9239 -401 -91 1277 O ATOM 2531 CB CYS A 270 -8.736 -20.904 40.255 1.00 59.27 C ANISOU 2531 CB CYS A 270 3510 9738 9272 -604 -165 1312 C ATOM 2532 SG CYS A 270 -7.294 -21.620 39.432 1.00 62.97 S ANISOU 2532 SG CYS A 270 3977 10125 9825 -769 -244 1087 S ATOM 2533 N TRP A 271 -6.023 -19.432 41.451 1.00 54.44 N ANISOU 2533 N TRP A 271 3200 9022 8464 -521 -110 1002 N ATOM 2534 CA TRP A 271 -4.825 -19.598 42.284 1.00 53.05 C ANISOU 2534 CA TRP A 271 3077 8785 8295 -513 -125 908 C ATOM 2535 C TRP A 271 -4.533 -18.392 43.184 1.00 55.80 C ANISOU 2535 C TRP A 271 3571 9133 8496 -410 -80 902 C ATOM 2536 O TRP A 271 -3.986 -18.595 44.268 1.00 55.55 O ANISOU 2536 O TRP A 271 3572 9072 8463 -363 -85 898 O ATOM 2537 CB TRP A 271 -3.596 -19.886 41.425 1.00 51.14 C ANISOU 2537 CB TRP A 271 2833 8485 8112 -636 -174 729 C ATOM 2538 CG TRP A 271 -3.460 -21.327 41.030 1.00 52.26 C ANISOU 2538 CG TRP A 271 2855 8589 8412 -716 -228 714 C ATOM 2539 CD1 TRP A 271 -3.764 -21.879 39.821 1.00 55.23 C ANISOU 2539 CD1 TRP A 271 3157 8961 8868 -811 -268 687 C ATOM 2540 CD2 TRP A 271 -2.979 -22.401 41.852 1.00 52.17 C ANISOU 2540 CD2 TRP A 271 2792 8535 8496 -704 -251 731 C ATOM 2541 NE1 TRP A 271 -3.501 -23.230 39.835 1.00 54.82 N ANISOU 2541 NE1 TRP A 271 3018 8857 8956 -860 -316 678 N ATOM 2542 CE2 TRP A 271 -3.005 -23.575 41.066 1.00 56.24 C ANISOU 2542 CE2 TRP A 271 3204 9014 9151 -795 -304 708 C ATOM 2543 CE3 TRP A 271 -2.470 -22.477 43.161 1.00 53.32 C ANISOU 2543 CE3 TRP A 271 2972 8667 8620 -625 -235 762 C ATOM 2544 CZ2 TRP A 271 -2.586 -24.819 41.562 1.00 55.74 C ANISOU 2544 CZ2 TRP A 271 3070 8899 9210 -807 -336 718 C ATOM 2545 CZ3 TRP A 271 -2.074 -23.710 43.655 1.00 54.83 C ANISOU 2545 CZ3 TRP A 271 3085 8818 8932 -638 -266 776 C ATOM 2546 CH2 TRP A 271 -2.101 -24.856 42.851 1.00 55.70 C ANISOU 2546 CH2 TRP A 271 3090 8889 9184 -727 -313 755 C ATOM 2547 N THR A 272 -4.887 -17.157 42.753 1.00 51.51 N ANISOU 2547 N THR A 272 3120 8621 7830 -375 -39 902 N ATOM 2548 CA THR A 272 -4.657 -15.918 43.515 1.00 50.96 C ANISOU 2548 CA THR A 272 3210 8542 7612 -277 0 893 C ATOM 2549 C THR A 272 -5.369 -15.964 44.902 1.00 55.14 C ANISOU 2549 C THR A 272 3764 9101 8084 -124 47 1048 C ATOM 2550 O THR A 272 -4.677 -15.651 45.874 1.00 54.59 O ANISOU 2550 O THR A 272 3808 8997 7935 -57 50 1019 O ATOM 2551 CB THR A 272 -5.068 -14.668 42.715 1.00 56.43 C ANISOU 2551 CB THR A 272 3987 9259 8197 -275 35 870 C ATOM 2552 OG1 THR A 272 -4.390 -14.687 41.457 1.00 55.03 O ANISOU 2552 OG1 THR A 272 3784 9055 8069 -409 -8 729 O ATOM 2553 CG2 THR A 272 -4.731 -13.363 43.432 1.00 54.65 C ANISOU 2553 CG2 THR A 272 3940 9008 7816 -178 68 855 C ATOM 2554 N PRO A 273 -6.675 -16.364 45.065 1.00 52.29 N ANISOU 2554 N PRO A 273 3303 8805 7761 -64 79 1216 N ATOM 2555 CA PRO A 273 -7.280 -16.368 46.422 1.00 52.73 C ANISOU 2555 CA PRO A 273 3386 8895 7755 96 131 1367 C ATOM 2556 C PRO A 273 -6.566 -17.308 47.395 1.00 55.70 C ANISOU 2556 C PRO A 273 3724 9236 8202 107 97 1365 C ATOM 2557 O PRO A 273 -6.509 -17.016 48.588 1.00 55.45 O ANISOU 2557 O PRO A 273 3769 9214 8087 237 131 1435 O ATOM 2558 CB PRO A 273 -8.723 -16.829 46.182 1.00 55.13 C ANISOU 2558 CB PRO A 273 3561 9281 8107 129 165 1549 C ATOM 2559 CG PRO A 273 -8.696 -17.500 44.857 1.00 59.40 C ANISOU 2559 CG PRO A 273 3973 9809 8790 -36 100 1483 C ATOM 2560 CD PRO A 273 -7.673 -16.764 44.051 1.00 54.16 C ANISOU 2560 CD PRO A 273 3400 9089 8088 -133 70 1285 C ATOM 2561 N GLY A 274 -6.017 -18.401 46.870 1.00 51.49 N ANISOU 2561 N GLY A 274 3081 8665 7817 -23 32 1287 N ATOM 2562 CA GLY A 274 -5.271 -19.373 47.654 1.00 51.39 C ANISOU 2562 CA GLY A 274 3021 8617 7888 -27 -3 1278 C ATOM 2563 C GLY A 274 -3.894 -18.888 48.059 1.00 55.00 C ANISOU 2563 C GLY A 274 3607 9016 8273 -28 -25 1146 C ATOM 2564 O GLY A 274 -3.420 -19.228 49.143 1.00 54.41 O ANISOU 2564 O GLY A 274 3543 8930 8202 29 -33 1173 O ATOM 2565 N LEU A 275 -3.245 -18.088 47.191 1.00 51.64 N ANISOU 2565 N LEU A 275 3278 8559 7784 -94 -40 1009 N ATOM 2566 CA LEU A 275 -1.920 -17.513 47.437 1.00 51.32 C ANISOU 2566 CA LEU A 275 3361 8462 7677 -118 -72 880 C ATOM 2567 C LEU A 275 -2.019 -16.276 48.342 1.00 54.99 C ANISOU 2567 C LEU A 275 3999 8928 7966 11 -37 915 C ATOM 2568 O LEU A 275 -1.089 -16.018 49.111 1.00 54.55 O ANISOU 2568 O LEU A 275 4031 8835 7862 36 -66 872 O ATOM 2569 CB LEU A 275 -1.217 -17.165 46.117 1.00 51.01 C ANISOU 2569 CB LEU A 275 3339 8391 7651 -247 -104 732 C ATOM 2570 CG LEU A 275 -0.702 -18.357 45.293 1.00 55.70 C ANISOU 2570 CG LEU A 275 3796 8963 8403 -377 -149 656 C ATOM 2571 CD1 LEU A 275 -0.503 -17.971 43.853 1.00 55.63 C ANISOU 2571 CD1 LEU A 275 3785 8954 8397 -473 -155 562 C ATOM 2572 CD2 LEU A 275 0.601 -18.934 45.865 1.00 58.18 C ANISOU 2572 CD2 LEU A 275 4109 9227 8770 -421 -196 574 C ATOM 2573 N VAL A 276 -3.147 -15.531 48.272 1.00 51.66 N ANISOU 2573 N VAL A 276 3632 8549 7448 95 23 996 N ATOM 2574 CA VAL A 276 -3.414 -14.362 49.126 1.00 51.94 C ANISOU 2574 CA VAL A 276 3846 8583 7306 236 67 1040 C ATOM 2575 C VAL A 276 -3.699 -14.888 50.552 1.00 56.64 C ANISOU 2575 C VAL A 276 4441 9202 7878 368 89 1157 C ATOM 2576 O VAL A 276 -3.304 -14.258 51.537 1.00 56.77 O ANISOU 2576 O VAL A 276 4613 9190 7766 463 91 1149 O ATOM 2577 CB VAL A 276 -4.552 -13.468 48.551 1.00 55.84 C ANISOU 2577 CB VAL A 276 4379 9122 7715 300 135 1113 C ATOM 2578 CG1 VAL A 276 -5.050 -12.440 49.570 1.00 56.42 C ANISOU 2578 CG1 VAL A 276 4636 9196 7605 474 192 1180 C ATOM 2579 CG2 VAL A 276 -4.095 -12.766 47.272 1.00 54.94 C ANISOU 2579 CG2 VAL A 276 4286 8982 7606 175 110 987 C ATOM 2580 N LEU A 277 -4.320 -16.082 50.638 1.00 53.38 N ANISOU 2580 N LEU A 277 3853 8834 7597 363 96 1259 N ATOM 2581 CA LEU A 277 -4.632 -16.798 51.881 1.00 53.96 C ANISOU 2581 CA LEU A 277 3882 8939 7681 474 116 1385 C ATOM 2582 C LEU A 277 -3.342 -17.165 52.632 1.00 57.70 C ANISOU 2582 C LEU A 277 4406 9357 8161 446 56 1292 C ATOM 2583 O LEU A 277 -3.325 -17.126 53.863 1.00 57.64 O ANISOU 2583 O LEU A 277 4499 9353 8049 570 72 1341 O ATOM 2584 CB LEU A 277 -5.448 -18.065 51.565 1.00 54.13 C ANISOU 2584 CB LEU A 277 3688 9008 7872 432 118 1497 C ATOM 2585 CG LEU A 277 -6.169 -18.759 52.717 1.00 59.88 C ANISOU 2585 CG LEU A 277 4340 9793 8617 562 158 1680 C ATOM 2586 CD1 LEU A 277 -7.455 -18.016 53.119 1.00 60.96 C ANISOU 2586 CD1 LEU A 277 4529 10004 8630 728 248 1843 C ATOM 2587 CD2 LEU A 277 -6.493 -20.190 52.350 1.00 62.55 C ANISOU 2587 CD2 LEU A 277 4467 10149 9149 475 129 1750 C ATOM 2588 N LEU A 278 -2.259 -17.487 51.884 1.00 53.69 N ANISOU 2588 N LEU A 278 3835 8799 7767 287 -13 1158 N ATOM 2589 CA LEU A 278 -0.939 -17.814 52.434 1.00 53.25 C ANISOU 2589 CA LEU A 278 3805 8692 7735 235 -76 1065 C ATOM 2590 C LEU A 278 -0.301 -16.572 53.057 1.00 58.46 C ANISOU 2590 C LEU A 278 4676 9313 8222 290 -93 999 C ATOM 2591 O LEU A 278 0.363 -16.680 54.090 1.00 58.33 O ANISOU 2591 O LEU A 278 4719 9280 8162 338 -121 1002 O ATOM 2592 CB LEU A 278 -0.021 -18.398 51.346 1.00 52.34 C ANISOU 2592 CB LEU A 278 3597 8536 7756 59 -133 934 C ATOM 2593 CG LEU A 278 -0.329 -19.812 50.855 1.00 56.56 C ANISOU 2593 CG LEU A 278 3934 9085 8472 -9 -138 976 C ATOM 2594 CD1 LEU A 278 0.270 -20.049 49.498 1.00 55.97 C ANISOU 2594 CD1 LEU A 278 3804 8981 8482 -155 -168 855 C ATOM 2595 CD2 LEU A 278 0.198 -20.863 51.810 1.00 59.50 C ANISOU 2595 CD2 LEU A 278 4223 9444 8939 -7 -167 1002 C ATOM 2596 N LEU A 279 -0.537 -15.387 52.445 1.00 55.75 N ANISOU 2596 N LEU A 279 4451 8954 7778 285 -77 946 N ATOM 2597 CA LEU A 279 -0.029 -14.097 52.923 1.00 56.28 C ANISOU 2597 CA LEU A 279 4736 8973 7676 332 -96 882 C ATOM 2598 C LEU A 279 -0.791 -13.657 54.191 1.00 62.73 C ANISOU 2598 C LEU A 279 5678 9816 8342 527 -39 999 C ATOM 2599 O LEU A 279 -0.170 -13.182 55.145 1.00 62.84 O ANISOU 2599 O LEU A 279 5869 9784 8222 584 -70 958 O ATOM 2600 CB LEU A 279 -0.137 -13.023 51.817 1.00 55.82 C ANISOU 2600 CB LEU A 279 4749 8891 7569 270 -90 806 C ATOM 2601 CG LEU A 279 0.723 -13.220 50.558 1.00 59.35 C ANISOU 2601 CG LEU A 279 5096 9314 8140 88 -140 687 C ATOM 2602 CD1 LEU A 279 0.233 -12.359 49.416 1.00 59.02 C ANISOU 2602 CD1 LEU A 279 5098 9274 8054 56 -112 652 C ATOM 2603 CD2 LEU A 279 2.191 -12.938 50.835 1.00 62.22 C ANISOU 2603 CD2 LEU A 279 5518 9615 8508 -5 -226 572 C ATOM 2604 N LEU A 280 -2.128 -13.864 54.211 1.00 60.63 N ANISOU 2604 N LEU A 280 5320 9623 8094 632 41 1148 N ATOM 2605 CA LEU A 280 -3.005 -13.533 55.341 1.00 61.97 C ANISOU 2605 CA LEU A 280 5586 9833 8126 836 111 1283 C ATOM 2606 C LEU A 280 -2.811 -14.512 56.524 1.00 68.90 C ANISOU 2606 C LEU A 280 6386 10743 9050 901 105 1368 C ATOM 2607 O LEU A 280 -3.266 -14.232 57.636 1.00 69.01 O ANISOU 2607 O LEU A 280 6464 10799 8958 1078 163 1491 O ATOM 2608 CB LEU A 280 -4.484 -13.534 54.897 1.00 61.95 C ANISOU 2608 CB LEU A 280 5518 9904 8117 921 204 1420 C ATOM 2609 CG LEU A 280 -4.930 -12.449 53.904 1.00 65.85 C ANISOU 2609 CG LEU A 280 6109 10378 8534 897 228 1364 C ATOM 2610 CD1 LEU A 280 -6.229 -12.821 53.233 1.00 65.86 C ANISOU 2610 CD1 LEU A 280 5975 10458 8590 923 300 1494 C ATOM 2611 CD2 LEU A 280 -5.069 -11.093 54.578 1.00 68.56 C ANISOU 2611 CD2 LEU A 280 6709 10678 8662 1034 253 1345 C ATOM 2612 N ASP A 281 -2.128 -15.648 56.280 1.00 67.57 N ANISOU 2612 N ASP A 281 6084 10554 9037 764 37 1305 N ATOM 2613 CA ASP A 281 -1.841 -16.673 57.284 1.00 68.96 C ANISOU 2613 CA ASP A 281 6168 10750 9281 793 18 1365 C ATOM 2614 C ASP A 281 -0.709 -16.243 58.229 1.00 76.33 C ANISOU 2614 C ASP A 281 7253 11626 10124 785 -54 1263 C ATOM 2615 O ASP A 281 -0.764 -16.560 59.418 1.00 76.49 O ANISOU 2615 O ASP A 281 7276 11666 10120 867 -59 1325 O ATOM 2616 CB ASP A 281 -1.463 -18.005 56.597 1.00 70.06 C ANISOU 2616 CB ASP A 281 6079 10896 9646 646 -14 1355 C ATOM 2617 CG ASP A 281 -1.315 -19.192 57.535 1.00 79.76 C ANISOU 2617 CG ASP A 281 7199 12134 10973 648 -42 1401 C ATOM 2618 OD1 ASP A 281 -2.299 -19.543 58.202 1.00 81.06 O1- ANISOU 2618 OD1 ASP A 281 7371 12348 11081 795 1 1533 O1- ATOM 2619 OD2 ASP A 281 -0.236 -19.810 57.544 1.00 84.29 O ANISOU 2619 OD2 ASP A 281 7676 12669 11680 508 -101 1312 O ATOM 2620 N VAL A 282 0.302 -15.531 57.706 1.00 75.02 N ANISOU 2620 N VAL A 282 7211 11390 9902 686 -111 1115 N ATOM 2621 CA VAL A 282 1.480 -15.113 58.470 1.00 76.39 C ANISOU 2621 CA VAL A 282 7531 11500 9992 648 -196 1010 C ATOM 2622 C VAL A 282 1.470 -13.585 58.748 1.00 84.16 C ANISOU 2622 C VAL A 282 8779 12443 10754 756 -191 984 C ATOM 2623 O VAL A 282 2.068 -13.165 59.737 1.00 84.41 O ANISOU 2623 O VAL A 282 8956 12447 10669 820 -235 970 O ATOM 2624 CB VAL A 282 2.784 -15.537 57.726 1.00 79.61 C ANISOU 2624 CB VAL A 282 7878 11856 10515 443 -278 866 C ATOM 2625 CG1 VAL A 282 2.746 -17.017 57.347 1.00 78.92 C ANISOU 2625 CG1 VAL A 282 7563 11794 10628 351 -291 883 C ATOM 2626 CG2 VAL A 282 2.991 -14.694 56.476 1.00 78.91 C ANISOU 2626 CG2 VAL A 282 7805 11746 10430 365 -262 799 C ATOM 2627 N CYS A 283 0.830 -12.764 57.880 1.00 83.48 N ANISOU 2627 N CYS A 283 8758 12351 10609 777 -142 978 N ATOM 2628 CA CYS A 283 0.836 -11.299 58.022 1.00 85.54 C ANISOU 2628 CA CYS A 283 9274 12561 10668 871 -137 945 C ATOM 2629 C CYS A 283 -0.507 -10.764 58.589 1.00 92.57 C ANISOU 2629 C CYS A 283 10239 13505 11429 1093 -28 1088 C ATOM 2630 O CYS A 283 -0.608 -9.565 58.867 1.00 92.86 O ANISOU 2630 O CYS A 283 10509 13497 11276 1211 -21 1075 O ATOM 2631 CB CYS A 283 1.171 -10.637 56.685 1.00 85.71 C ANISOU 2631 CB CYS A 283 9339 12532 10694 754 -157 842 C ATOM 2632 SG CYS A 283 1.569 -8.869 56.795 1.00 90.67 S ANISOU 2632 SG CYS A 283 10296 13064 11092 820 -187 764 S ATOM 2633 N CYS A 284 -1.510 -11.641 58.796 1.00 91.12 N ANISOU 2633 N CYS A 284 9865 13413 11343 1153 54 1227 N ATOM 2634 CA CYS A 284 -2.807 -11.228 59.328 1.00 92.78 C ANISOU 2634 CA CYS A 284 10130 13686 11438 1367 165 1383 C ATOM 2635 C CYS A 284 -3.248 -12.192 60.482 1.00 97.32 C ANISOU 2635 C CYS A 284 10590 14341 12046 1489 207 1535 C ATOM 2636 O CYS A 284 -4.156 -13.008 60.299 1.00 96.60 O ANISOU 2636 O CYS A 284 10316 14335 12053 1530 278 1678 O ATOM 2637 CB CYS A 284 -3.839 -11.146 58.200 1.00 93.34 C ANISOU 2637 CB CYS A 284 10108 13804 11555 1365 242 1449 C ATOM 2638 SG CYS A 284 -5.531 -10.706 58.705 1.00 98.75 S ANISOU 2638 SG CYS A 284 10948 14536 12038 1626 374 1599 S ATOM 2639 N PRO A 285 -2.644 -12.075 61.691 1.00 94.98 N ANISOU 2639 N PRO A 285 10422 14022 11644 1570 169 1520 N ATOM 2640 CA PRO A 285 -3.072 -12.931 62.806 1.00 95.56 C ANISOU 2640 CA PRO A 285 10413 14176 11718 1716 220 1676 C ATOM 2641 C PRO A 285 -4.134 -12.228 63.678 1.00100.63 C ANISOU 2641 C PRO A 285 11222 14858 12153 1971 323 1801 C ATOM 2642 O PRO A 285 -3.898 -11.108 64.150 1.00100.77 O ANISOU 2642 O PRO A 285 11479 14809 11998 2028 318 1720 O ATOM 2643 CB PRO A 285 -1.765 -13.175 63.572 1.00 97.52 C ANISOU 2643 CB PRO A 285 10721 14376 11956 1657 118 1582 C ATOM 2644 CG PRO A 285 -0.804 -12.061 63.105 1.00101.94 C ANISOU 2644 CG PRO A 285 11497 14827 12410 1566 31 1401 C ATOM 2645 CD PRO A 285 -1.527 -11.204 62.106 1.00 96.99 C ANISOU 2645 CD PRO A 285 10904 14179 11770 1534 74 1370 C ATOM 2646 N GLN A 286 -5.313 -12.876 63.863 1.00 97.64 N ANISOU 2646 N GLN A 286 10725 14585 11789 2130 417 2000 N ATOM 2647 CA GLN A 286 -6.491 -12.432 64.648 1.00 98.71 C ANISOU 2647 CA GLN A 286 10998 14776 11731 2397 531 2148 C ATOM 2648 C GLN A 286 -7.475 -11.543 63.847 1.00102.30 C ANISOU 2648 C GLN A 286 11506 15241 12123 2456 615 2190 C ATOM 2649 O GLN A 286 -8.552 -11.244 64.373 1.00102.56 O ANISOU 2649 O GLN A 286 11615 15335 12017 2681 727 2340 O ATOM 2650 CB GLN A 286 -6.117 -11.668 65.953 1.00101.21 C ANISOU 2650 CB GLN A 286 11611 15032 11813 2534 503 2075 C ATOM 2651 CG GLN A 286 -5.394 -12.477 67.021 1.00117.30 C ANISOU 2651 CG GLN A 286 13626 17075 13867 2527 435 2063 C ATOM 2652 CD GLN A 286 -4.789 -11.542 68.037 1.00138.11 C ANISOU 2652 CD GLN A 286 16575 19631 16269 2624 382 1958 C ATOM 2653 OE1 GLN A 286 -3.691 -11.009 67.852 1.00133.26 O ANISOU 2653 OE1 GLN A 286 16097 18909 15628 2476 270 1772 O ATOM 2654 NE2 GLN A 286 -5.477 -11.339 69.147 1.00132.27 N ANISOU 2654 NE2 GLN A 286 15961 18944 15352 2873 458 2079 N ATOM 2655 N CYS A 287 -7.131 -11.110 62.615 1.00 98.04 N ANISOU 2655 N CYS A 287 10924 14647 11680 2265 567 2068 N ATOM 2656 CA CYS A 287 -8.025 -10.242 61.839 1.00 97.99 C ANISOU 2656 CA CYS A 287 10953 14650 11627 2301 639 2102 C ATOM 2657 C CYS A 287 -9.152 -11.071 61.154 1.00101.30 C ANISOU 2657 C CYS A 287 11088 15162 12238 2228 686 2233 C ATOM 2658 O CYS A 287 -10.285 -10.595 61.060 1.00101.26 O ANISOU 2658 O CYS A 287 11070 15218 12184 2342 785 2364 O ATOM 2659 CB CYS A 287 -7.265 -9.380 60.823 1.00 97.73 C ANISOU 2659 CB CYS A 287 11079 14502 11551 2161 565 1897 C ATOM 2660 SG CYS A 287 -5.524 -9.840 60.554 1.00100.43 S ANISOU 2660 SG CYS A 287 11367 14753 12038 1883 402 1682 S ATOM 2661 N ASP A 288 -8.836 -12.295 60.682 1.00 96.88 N ANISOU 2661 N ASP A 288 10309 14609 11891 2042 613 2199 N ATOM 2662 CA ASP A 288 -9.754 -13.184 59.963 1.00 96.06 C ANISOU 2662 CA ASP A 288 9940 14579 11978 1954 636 2312 C ATOM 2663 C ASP A 288 -9.345 -14.654 60.138 1.00 98.48 C ANISOU 2663 C ASP A 288 10034 14915 12470 1866 586 2356 C ATOM 2664 O ASP A 288 -8.152 -14.966 60.124 1.00 97.24 O ANISOU 2664 O ASP A 288 9883 14690 12373 1739 494 2211 O ATOM 2665 CB ASP A 288 -9.745 -12.790 58.475 1.00 96.99 C ANISOU 2665 CB ASP A 288 10020 14648 12182 1758 589 2178 C ATOM 2666 CG ASP A 288 -10.749 -13.496 57.611 1.00106.06 C ANISOU 2666 CG ASP A 288 10936 15874 13489 1691 621 2303 C ATOM 2667 OD1 ASP A 288 -11.963 -13.230 57.772 1.00106.98 O ANISOU 2667 OD1 ASP A 288 11044 16064 13539 1824 715 2461 O ATOM 2668 OD2 ASP A 288 -10.323 -14.271 56.729 1.00110.35 O1- ANISOU 2668 OD2 ASP A 288 11308 16403 14217 1506 549 2244 O1- ATOM 2669 N VAL A 289 -10.339 -15.554 60.283 1.00 94.77 N ANISOU 2669 N VAL A 289 9372 14546 12090 1938 649 2569 N ATOM 2670 CA VAL A 289 -10.103 -17.004 60.435 1.00 93.95 C ANISOU 2670 CA VAL A 289 9044 14477 12176 1865 612 2648 C ATOM 2671 C VAL A 289 -9.855 -17.610 59.042 1.00 95.81 C ANISOU 2671 C VAL A 289 9105 14683 12615 1632 544 2570 C ATOM 2672 O VAL A 289 -10.506 -17.170 58.089 1.00 95.58 O ANISOU 2672 O VAL A 289 8990 14696 12630 1607 579 2649 O ATOM 2673 CB VAL A 289 -11.261 -17.743 61.169 1.00 98.72 C ANISOU 2673 CB VAL A 289 9518 15200 12790 2043 703 2921 C ATOM 2674 CG1 VAL A 289 -10.831 -19.145 61.612 1.00 98.39 C ANISOU 2674 CG1 VAL A 289 9261 15178 12944 1960 654 2988 C ATOM 2675 CG2 VAL A 289 -11.768 -16.951 62.368 1.00 99.61 C ANISOU 2675 CG2 VAL A 289 9825 15347 12676 2297 784 3000 C ATOM 2676 N LEU A 290 -8.951 -18.609 58.912 1.00 90.30 N ANISOU 2676 N LEU A 290 8359 13914 12036 1465 449 2419 N ATOM 2677 CA LEU A 290 -8.671 -19.221 57.608 1.00 88.48 C ANISOU 2677 CA LEU A 290 7987 13643 11989 1247 379 2321 C ATOM 2678 C LEU A 290 -9.521 -20.495 57.452 1.00 90.89 C ANISOU 2678 C LEU A 290 8049 13993 12491 1201 367 2464 C ATOM 2679 O LEU A 290 -8.998 -21.605 57.304 1.00 89.82 O ANISOU 2679 O LEU A 290 7832 13822 12474 1120 308 2417 O ATOM 2680 CB LEU A 290 -7.171 -19.492 57.426 1.00 87.72 C ANISOU 2680 CB LEU A 290 7971 13446 11912 1099 288 2088 C ATOM 2681 CG LEU A 290 -6.304 -18.227 57.374 1.00 92.47 C ANISOU 2681 CG LEU A 290 8810 13992 12332 1122 284 1944 C ATOM 2682 CD1 LEU A 290 -5.577 -17.997 58.670 1.00 93.33 C ANISOU 2682 CD1 LEU A 290 9083 14077 12303 1232 273 1914 C ATOM 2683 CD2 LEU A 290 -5.388 -18.245 56.220 1.00 94.12 C ANISOU 2683 CD2 LEU A 290 9026 14124 12611 926 207 1747 C ATOM 2684 N ALA A 291 -10.859 -20.311 57.491 1.00 87.23 N ANISOU 2684 N ALA A 291 7473 13610 12059 1259 424 2651 N ATOM 2685 CA ALA A 291 -11.849 -21.381 57.360 1.00 86.95 C ANISOU 2685 CA ALA A 291 7205 13625 12206 1223 414 2822 C ATOM 2686 C ALA A 291 -11.974 -21.826 55.920 1.00 88.52 C ANISOU 2686 C ALA A 291 7278 13826 12530 1075 382 2828 C ATOM 2687 O ALA A 291 -12.067 -23.026 55.683 1.00 88.36 O ANISOU 2687 O ALA A 291 7071 13807 12694 974 334 2900 O ATOM 2688 CB ALA A 291 -13.203 -20.923 57.879 1.00 88.92 C ANISOU 2688 CB ALA A 291 7416 13982 12388 1434 507 3077 C ATOM 2689 N TYR A 292 -11.976 -20.870 54.959 1.00 82.85 N ANISOU 2689 N TYR A 292 6665 13101 11713 1057 402 2749 N ATOM 2690 CA TYR A 292 -12.094 -21.175 53.538 1.00 81.46 C ANISOU 2690 CA TYR A 292 6387 12926 11638 912 367 2736 C ATOM 2691 C TYR A 292 -10.748 -21.634 53.005 1.00 81.42 C ANISOU 2691 C TYR A 292 6383 12817 11737 702 268 2496 C ATOM 2692 O TYR A 292 -10.118 -20.930 52.207 1.00 80.46 O ANISOU 2692 O TYR A 292 6233 12678 11660 578 235 2423 O ATOM 2693 CB TYR A 292 -12.650 -19.994 52.712 1.00 83.09 C ANISOU 2693 CB TYR A 292 6684 13180 11705 984 434 2775 C ATOM 2694 CG TYR A 292 -12.400 -18.628 53.299 1.00 85.12 C ANISOU 2694 CG TYR A 292 7176 13420 11744 1115 494 2690 C ATOM 2695 CD1 TYR A 292 -11.167 -18.001 53.146 1.00 86.49 C ANISOU 2695 CD1 TYR A 292 7500 13498 11866 1046 444 2458 C ATOM 2696 CD2 TYR A 292 -13.404 -17.946 53.974 1.00 86.68 C ANISOU 2696 CD2 TYR A 292 7449 13693 11792 1295 596 2838 C ATOM 2697 CE1 TYR A 292 -10.934 -16.738 53.677 1.00 87.71 C ANISOU 2697 CE1 TYR A 292 7877 13625 11824 1152 485 2378 C ATOM 2698 CE2 TYR A 292 -13.187 -16.678 54.500 1.00 87.76 C ANISOU 2698 CE2 TYR A 292 7818 13801 11728 1412 646 2752 C ATOM 2699 CZ TYR A 292 -11.947 -16.082 54.356 1.00 95.21 C ANISOU 2699 CZ TYR A 292 8912 14641 12624 1335 585 2520 C ATOM 2700 OH TYR A 292 -11.738 -14.825 54.857 1.00 96.59 O ANISOU 2700 OH TYR A 292 9321 14777 12601 1443 623 2439 O ATOM 2701 N GLU A 293 -10.303 -22.829 53.456 1.00 75.40 N ANISOU 2701 N GLU A 293 5641 11991 11016 669 223 2390 N ATOM 2702 CA GLU A 293 -9.053 -23.389 52.970 1.00 72.98 C ANISOU 2702 CA GLU A 293 5324 11591 10814 494 137 2185 C ATOM 2703 C GLU A 293 -9.360 -24.606 52.087 1.00 73.62 C ANISOU 2703 C GLU A 293 5221 11656 11094 345 76 2213 C ATOM 2704 O GLU A 293 -8.645 -24.772 51.115 1.00 72.36 O ANISOU 2704 O GLU A 293 5064 11442 10987 200 23 2061 O ATOM 2705 CB GLU A 293 -7.944 -23.664 54.015 1.00 74.21 C ANISOU 2705 CB GLU A 293 5516 11704 10979 519 113 2124 C ATOM 2706 CG GLU A 293 -8.200 -24.307 55.362 1.00 85.43 C ANISOU 2706 CG GLU A 293 6830 13175 12457 624 138 2312 C ATOM 2707 CD GLU A 293 -6.895 -24.850 55.936 1.00104.86 C ANISOU 2707 CD GLU A 293 9280 15590 14973 612 99 2254 C ATOM 2708 OE1 GLU A 293 -6.109 -24.073 56.529 1.00101.77 O ANISOU 2708 OE1 GLU A 293 9037 15177 14453 670 105 2161 O ATOM 2709 OE2 GLU A 293 -6.652 -26.065 55.765 1.00 96.33 O1- ANISOU 2709 OE2 GLU A 293 8041 14496 14064 549 62 2315 O1- ATOM 2710 N LYS A 294 -10.458 -25.364 52.335 1.00 68.52 N ANISOU 2710 N LYS A 294 4422 11061 10551 385 83 2416 N ATOM 2711 CA LYS A 294 -10.920 -26.502 51.527 1.00 67.23 C ANISOU 2711 CA LYS A 294 4080 10884 10581 257 19 2482 C ATOM 2712 C LYS A 294 -11.501 -26.008 50.190 1.00 68.22 C ANISOU 2712 C LYS A 294 4178 11037 10706 183 10 2498 C ATOM 2713 O LYS A 294 -11.332 -26.677 49.176 1.00 67.60 O ANISOU 2713 O LYS A 294 4002 10916 10766 33 -65 2461 O ATOM 2714 CB LYS A 294 -11.949 -27.366 52.294 1.00 70.38 C ANISOU 2714 CB LYS A 294 4330 11341 11071 338 35 2723 C ATOM 2715 CG LYS A 294 -12.902 -26.620 53.265 1.00 82.59 C ANISOU 2715 CG LYS A 294 5889 13003 12490 530 133 2940 C ATOM 2716 CD LYS A 294 -13.417 -27.514 54.417 1.00 91.57 C ANISOU 2716 CD LYS A 294 6860 14200 13732 604 146 3190 C ATOM 2717 CE LYS A 294 -12.388 -27.770 55.502 1.00101.41 C ANISOU 2717 CE LYS A 294 8111 15421 14998 667 147 3181 C ATOM 2718 NZ LYS A 294 -12.919 -28.680 56.548 1.00111.13 N1+ ANISOU 2718 NZ LYS A 294 9158 16702 16364 707 146 3419 N1+ ATOM 2719 N PHE A 295 -12.165 -24.840 50.193 1.00 62.90 N ANISOU 2719 N PHE A 295 3595 10432 9874 290 83 2553 N ATOM 2720 CA PHE A 295 -12.794 -24.230 49.020 1.00 61.96 C ANISOU 2720 CA PHE A 295 3457 10347 9737 230 81 2572 C ATOM 2721 C PHE A 295 -11.751 -23.730 47.992 1.00 62.62 C ANISOU 2721 C PHE A 295 3645 10354 9792 102 38 2318 C ATOM 2722 O PHE A 295 -11.878 -24.032 46.800 1.00 61.69 O ANISOU 2722 O PHE A 295 3466 10222 9752 -32 -16 2274 O ATOM 2723 CB PHE A 295 -13.712 -23.067 49.448 1.00 64.33 C ANISOU 2723 CB PHE A 295 3812 10749 9882 399 183 2735 C ATOM 2724 CG PHE A 295 -14.857 -23.444 50.365 1.00 66.83 C ANISOU 2724 CG PHE A 295 3975 11161 10258 488 216 3021 C ATOM 2725 CD1 PHE A 295 -16.060 -23.913 49.848 1.00 69.80 C ANISOU 2725 CD1 PHE A 295 4203 11584 10733 404 182 3154 C ATOM 2726 CD2 PHE A 295 -14.742 -23.307 51.741 1.00 69.77 C ANISOU 2726 CD2 PHE A 295 4346 11579 10587 655 278 3164 C ATOM 2727 CE1 PHE A 295 -17.116 -24.253 50.698 1.00 71.69 C ANISOU 2727 CE1 PHE A 295 4288 11914 11035 479 207 3434 C ATOM 2728 CE2 PHE A 295 -15.801 -23.647 52.590 1.00 73.49 C ANISOU 2728 CE2 PHE A 295 4662 12144 11116 741 312 3443 C ATOM 2729 CZ PHE A 295 -16.979 -24.114 52.063 1.00 71.72 C ANISOU 2729 CZ PHE A 295 4285 11966 10999 650 275 3580 C ATOM 2730 N PHE A 296 -10.723 -22.995 48.453 1.00 57.47 N ANISOU 2730 N PHE A 296 3144 9654 9040 135 55 2157 N ATOM 2731 CA PHE A 296 -9.663 -22.467 47.589 1.00 56.29 C ANISOU 2731 CA PHE A 296 3088 9435 8864 20 16 1925 C ATOM 2732 C PHE A 296 -8.751 -23.582 47.040 1.00 58.51 C ANISOU 2732 C PHE A 296 3292 9633 9304 -132 -70 1797 C ATOM 2733 O PHE A 296 -8.153 -23.402 45.974 1.00 57.65 O ANISOU 2733 O PHE A 296 3201 9483 9223 -255 -113 1649 O ATOM 2734 CB PHE A 296 -8.803 -21.427 48.329 1.00 57.93 C ANISOU 2734 CB PHE A 296 3477 9616 8917 101 54 1810 C ATOM 2735 CG PHE A 296 -9.449 -20.113 48.706 1.00 60.12 C ANISOU 2735 CG PHE A 296 3864 9958 9022 261 140 1913 C ATOM 2736 CD1 PHE A 296 -10.617 -19.687 48.084 1.00 63.48 C ANISOU 2736 CD1 PHE A 296 4302 10432 9386 266 175 1959 C ATOM 2737 CD2 PHE A 296 -8.850 -19.265 49.632 1.00 62.79 C ANISOU 2737 CD2 PHE A 296 4303 10304 9251 410 187 1957 C ATOM 2738 CE1 PHE A 296 -11.209 -18.469 48.438 1.00 64.92 C ANISOU 2738 CE1 PHE A 296 4592 10669 9405 425 262 2057 C ATOM 2739 CE2 PHE A 296 -9.434 -18.040 49.971 1.00 66.17 C ANISOU 2739 CE2 PHE A 296 4849 10783 9509 570 269 2048 C ATOM 2740 CZ PHE A 296 -10.610 -17.653 49.375 1.00 64.36 C ANISOU 2740 CZ PHE A 296 4629 10599 9224 579 309 2097 C ATOM 2741 N LEU A 297 -8.651 -24.723 47.760 1.00 53.90 N ANISOU 2741 N LEU A 297 2631 9028 8822 -115 -91 1857 N ATOM 2742 CA LEU A 297 -7.848 -25.887 47.384 1.00 52.76 C ANISOU 2742 CA LEU A 297 2410 8802 8835 -235 -165 1760 C ATOM 2743 C LEU A 297 -8.500 -26.585 46.192 1.00 56.37 C ANISOU 2743 C LEU A 297 2751 9243 9424 -367 -228 1779 C ATOM 2744 O LEU A 297 -7.800 -26.886 45.226 1.00 55.56 O ANISOU 2744 O LEU A 297 2648 9068 9396 -491 -287 1623 O ATOM 2745 CB LEU A 297 -7.706 -26.827 48.596 1.00 52.87 C ANISOU 2745 CB LEU A 297 2356 8813 8917 -161 -160 1869 C ATOM 2746 CG LEU A 297 -6.591 -27.887 48.678 1.00 56.93 C ANISOU 2746 CG LEU A 297 2785 9247 9600 -253 -225 1806 C ATOM 2747 CD1 LEU A 297 -7.147 -29.248 48.482 1.00 57.65 C ANISOU 2747 CD1 LEU A 297 2718 9331 9854 -320 -275 1933 C ATOM 2748 CD2 LEU A 297 -5.465 -27.667 47.702 1.00 58.39 C ANISOU 2748 CD2 LEU A 297 3038 9350 9797 -362 -265 1576 C ATOM 2749 N LEU A 298 -9.838 -26.781 46.235 1.00 53.26 N ANISOU 2749 N LEU A 298 2263 8918 9053 -335 -218 1974 N ATOM 2750 CA LEU A 298 -10.626 -27.399 45.168 1.00 53.38 C ANISOU 2750 CA LEU A 298 2173 8924 9185 -461 -287 2011 C ATOM 2751 C LEU A 298 -10.713 -26.484 43.954 1.00 56.58 C ANISOU 2751 C LEU A 298 2652 9343 9503 -524 -288 1901 C ATOM 2752 O LEU A 298 -10.730 -26.983 42.831 1.00 56.05 O ANISOU 2752 O LEU A 298 2560 9223 9512 -661 -359 1796 O ATOM 2753 CB LEU A 298 -12.041 -27.755 45.656 1.00 54.36 C ANISOU 2753 CB LEU A 298 2162 9125 9366 -409 -280 2276 C ATOM 2754 CG LEU A 298 -12.149 -28.875 46.691 1.00 59.69 C ANISOU 2754 CG LEU A 298 2711 9767 10201 -419 -322 2387 C ATOM 2755 CD1 LEU A 298 -13.433 -28.769 47.465 1.00 61.00 C ANISOU 2755 CD1 LEU A 298 2792 10032 10353 -282 -265 2653 C ATOM 2756 CD2 LEU A 298 -12.044 -30.234 46.052 1.00 62.17 C ANISOU 2756 CD2 LEU A 298 2922 10009 10690 -590 -434 2367 C ATOM 2757 N LEU A 299 -10.749 -25.153 44.180 1.00 52.76 N ANISOU 2757 N LEU A 299 2269 8925 8855 -420 -209 1918 N ATOM 2758 CA LEU A 299 -10.819 -24.119 43.140 1.00 52.19 C ANISOU 2758 CA LEU A 299 2276 8874 8678 -456 -194 1827 C ATOM 2759 C LEU A 299 -9.583 -24.180 42.223 1.00 55.73 C ANISOU 2759 C LEU A 299 2801 9239 9137 -569 -238 1578 C ATOM 2760 O LEU A 299 -9.720 -24.065 41.004 1.00 55.34 O ANISOU 2760 O LEU A 299 2743 9180 9105 -676 -280 1498 O ATOM 2761 CB LEU A 299 -10.942 -22.727 43.798 1.00 52.01 C ANISOU 2761 CB LEU A 299 2369 8916 8477 -303 -95 1879 C ATOM 2762 CG LEU A 299 -11.324 -21.535 42.909 1.00 56.19 C ANISOU 2762 CG LEU A 299 3001 9469 8880 -312 -64 1792 C ATOM 2763 CD1 LEU A 299 -12.770 -21.621 42.454 1.00 57.36 C ANISOU 2763 CD1 LEU A 299 3061 9687 9047 -356 -73 1913 C ATOM 2764 CD2 LEU A 299 -11.106 -20.227 43.649 1.00 57.77 C ANISOU 2764 CD2 LEU A 299 3340 9698 8911 -161 24 1810 C ATOM 2765 N ALA A 300 -8.392 -24.397 42.810 1.00 51.79 N ANISOU 2765 N ALA A 300 2369 8685 8625 -543 -230 1467 N ATOM 2766 CA ALA A 300 -7.128 -24.531 42.086 1.00 50.97 C ANISOU 2766 CA ALA A 300 2327 8506 8534 -635 -265 1251 C ATOM 2767 C ALA A 300 -6.989 -25.918 41.440 1.00 55.82 C ANISOU 2767 C ALA A 300 2847 9052 9312 -759 -346 1195 C ATOM 2768 O ALA A 300 -6.328 -26.049 40.406 1.00 55.58 O ANISOU 2768 O ALA A 300 2846 8974 9296 -855 -382 1036 O ATOM 2769 CB ALA A 300 -5.973 -24.286 43.035 1.00 51.22 C ANISOU 2769 CB ALA A 300 2442 8506 8513 -567 -237 1181 C ATOM 2770 N GLU A 301 -7.589 -26.942 42.061 1.00 53.09 N ANISOU 2770 N GLU A 301 2389 8699 9085 -754 -376 1330 N ATOM 2771 CA GLU A 301 -7.571 -28.327 41.588 1.00 53.50 C ANISOU 2771 CA GLU A 301 2352 8675 9299 -865 -458 1298 C ATOM 2772 C GLU A 301 -8.394 -28.472 40.299 1.00 57.70 C ANISOU 2772 C GLU A 301 2849 9214 9860 -972 -514 1294 C ATOM 2773 O GLU A 301 -7.997 -29.223 39.412 1.00 57.31 O ANISOU 2773 O GLU A 301 2794 9090 9892 -1082 -580 1171 O ATOM 2774 CB GLU A 301 -8.117 -29.260 42.683 1.00 55.64 C ANISOU 2774 CB GLU A 301 2512 8944 9684 -824 -472 1469 C ATOM 2775 CG GLU A 301 -7.957 -30.743 42.391 1.00 68.01 C ANISOU 2775 CG GLU A 301 3996 10419 11427 -931 -559 1442 C ATOM 2776 CD GLU A 301 -8.626 -31.703 43.357 1.00 93.89 C ANISOU 2776 CD GLU A 301 7162 13689 14823 -890 -572 1611 C ATOM 2777 OE1 GLU A 301 -9.243 -31.244 44.346 1.00 95.18 O ANISOU 2777 OE1 GLU A 301 7336 13891 14938 -774 -510 1681 O ATOM 2778 OE2 GLU A 301 -8.527 -32.928 43.120 1.00 88.77 O1- ANISOU 2778 OE2 GLU A 301 6420 12992 14317 -977 -650 1671 O1- ATOM 2779 N PHE A 302 -9.541 -27.761 40.211 1.00 54.38 N ANISOU 2779 N PHE A 302 2413 8885 9364 -934 -484 1425 N ATOM 2780 CA PHE A 302 -10.469 -27.773 39.069 1.00 54.60 C ANISOU 2780 CA PHE A 302 2402 8939 9405 -1027 -534 1449 C ATOM 2781 C PHE A 302 -9.813 -27.192 37.807 1.00 57.32 C ANISOU 2781 C PHE A 302 2843 9262 9673 -1097 -541 1248 C ATOM 2782 O PHE A 302 -10.200 -27.567 36.701 1.00 57.77 O ANISOU 2782 O PHE A 302 2876 9316 9759 -1198 -602 1223 O ATOM 2783 CB PHE A 302 -11.783 -26.994 39.355 1.00 56.92 C ANISOU 2783 CB PHE A 302 2653 9346 9626 -952 -487 1655 C ATOM 2784 CG PHE A 302 -12.730 -27.353 40.492 1.00 59.42 C ANISOU 2784 CG PHE A 302 2861 9705 10012 -876 -475 1886 C ATOM 2785 CD1 PHE A 302 -13.040 -28.682 40.783 1.00 63.12 C ANISOU 2785 CD1 PHE A 302 3227 10112 10645 -941 -551 1939 C ATOM 2786 CD2 PHE A 302 -13.394 -26.357 41.200 1.00 62.12 C ANISOU 2786 CD2 PHE A 302 3199 10149 10254 -739 -388 2061 C ATOM 2787 CE1 PHE A 302 -13.984 -29.004 41.765 1.00 64.75 C ANISOU 2787 CE1 PHE A 302 3322 10361 10918 -870 -539 2165 C ATOM 2788 CE2 PHE A 302 -14.297 -26.682 42.219 1.00 65.70 C ANISOU 2788 CE2 PHE A 302 3545 10650 10767 -659 -372 2287 C ATOM 2789 CZ PHE A 302 -14.572 -28.003 42.507 1.00 64.18 C ANISOU 2789 CZ PHE A 302 3243 10399 10742 -728 -448 2341 C ATOM 2790 N ASN A 303 -8.841 -26.268 37.971 1.00 52.31 N ANISOU 2790 N ASN A 303 2316 8615 8943 -1047 -484 1111 N ATOM 2791 CA ASN A 303 -8.127 -25.613 36.870 1.00 51.63 C ANISOU 2791 CA ASN A 303 2319 8514 8785 -1104 -484 927 C ATOM 2792 C ASN A 303 -7.310 -26.609 36.046 1.00 55.50 C ANISOU 2792 C ASN A 303 2798 8913 9375 -1217 -559 780 C ATOM 2793 O ASN A 303 -7.208 -26.446 34.829 1.00 55.37 O ANISOU 2793 O ASN A 303 2806 8895 9338 -1296 -592 687 O ATOM 2794 CB ASN A 303 -7.229 -24.510 37.391 1.00 51.96 C ANISOU 2794 CB ASN A 303 2468 8556 8717 -1030 -415 831 C ATOM 2795 CG ASN A 303 -6.566 -23.655 36.340 1.00 75.89 C ANISOU 2795 CG ASN A 303 5581 11586 11668 -1081 -408 669 C ATOM 2796 OD1 ASN A 303 -5.392 -23.361 36.463 1.00 71.23 O ANISOU 2796 OD1 ASN A 303 5021 10935 11108 -1132 -430 517 O ATOM 2797 ND2 ASN A 303 -7.265 -23.257 35.277 1.00 69.06 N ANISOU 2797 ND2 ASN A 303 4742 10791 10705 -1071 -380 708 N ATOM 2798 N SER A 304 -6.769 -27.648 36.695 1.00 52.23 N ANISOU 2798 N SER A 304 2352 8427 9068 -1218 -584 764 N ATOM 2799 CA SER A 304 -6.008 -28.710 36.038 1.00 52.68 C ANISOU 2799 CA SER A 304 2403 8386 9229 -1308 -650 633 C ATOM 2800 C SER A 304 -6.891 -29.518 35.068 1.00 57.41 C ANISOU 2800 C SER A 304 2938 8962 9912 -1410 -740 679 C ATOM 2801 O SER A 304 -6.371 -30.157 34.155 1.00 57.48 O ANISOU 2801 O SER A 304 2954 8884 10003 -1489 -805 572 O ATOM 2802 CB SER A 304 -5.393 -29.635 37.084 1.00 56.84 C ANISOU 2802 CB SER A 304 2899 8846 9854 -1273 -650 639 C ATOM 2803 OG SER A 304 -4.505 -28.939 37.946 1.00 65.35 O ANISOU 2803 OG SER A 304 4043 9928 10859 -1204 -586 561 O ATOM 2804 N ALA A 305 -8.223 -29.447 35.251 1.00 54.48 N ANISOU 2804 N ALA A 305 2515 8672 9513 -1407 -745 837 N ATOM 2805 CA ALA A 305 -9.243 -30.091 34.419 1.00 55.35 C ANISOU 2805 CA ALA A 305 2557 8778 9694 -1506 -836 914 C ATOM 2806 C ALA A 305 -9.859 -29.092 33.417 1.00 58.87 C ANISOU 2806 C ALA A 305 3030 9308 10031 -1537 -832 915 C ATOM 2807 O ALA A 305 -10.409 -29.505 32.396 1.00 59.26 O ANISOU 2807 O ALA A 305 3053 9342 10119 -1641 -918 913 O ATOM 2808 CB ALA A 305 -10.337 -30.684 35.301 1.00 56.75 C ANISOU 2808 CB ALA A 305 2618 8985 9960 -1479 -855 1144 C ATOM 2809 N MET A 306 -9.766 -27.781 33.723 1.00 54.09 N ANISOU 2809 N MET A 306 2477 8786 9290 -1449 -737 926 N ATOM 2810 CA MET A 306 -10.316 -26.677 32.929 1.00 53.49 C ANISOU 2810 CA MET A 306 2426 8796 9100 -1459 -716 939 C ATOM 2811 C MET A 306 -9.587 -26.487 31.604 1.00 56.67 C ANISOU 2811 C MET A 306 2909 9168 9456 -1538 -743 737 C ATOM 2812 O MET A 306 -10.241 -26.145 30.614 1.00 56.29 O ANISOU 2812 O MET A 306 2855 9168 9367 -1598 -776 747 O ATOM 2813 CB MET A 306 -10.276 -25.358 33.721 1.00 55.18 C ANISOU 2813 CB MET A 306 2691 9090 9185 -1333 -603 993 C ATOM 2814 CG MET A 306 -11.455 -25.206 34.662 1.00 59.61 C ANISOU 2814 CG MET A 306 3178 9729 9743 -1249 -566 1228 C ATOM 2815 SD MET A 306 -11.326 -24.234 36.196 1.00 63.72 S ANISOU 2815 SD MET A 306 3743 10265 10201 -1083 -461 1293 S ATOM 2816 CE MET A 306 -10.746 -22.710 35.599 1.00 59.58 C ANISOU 2816 CE MET A 306 3367 9758 9513 -1038 -385 1133 C ATOM 2817 N ASN A 307 -8.243 -26.693 31.580 1.00 52.47 N ANISOU 2817 N ASN A 307 2448 8566 8923 -1529 -723 563 N ATOM 2818 CA ASN A 307 -7.395 -26.527 30.391 1.00 51.87 C ANISOU 2818 CA ASN A 307 2452 8462 8795 -1579 -730 366 C ATOM 2819 C ASN A 307 -7.905 -27.393 29.189 1.00 56.51 C ANISOU 2819 C ASN A 307 3028 9008 9436 -1699 -835 308 C ATOM 2820 O ASN A 307 -8.197 -26.785 28.157 1.00 56.04 O ANISOU 2820 O ASN A 307 3005 8996 9290 -1734 -837 251 O ATOM 2821 CB ASN A 307 -5.926 -26.825 30.692 1.00 52.86 C ANISOU 2821 CB ASN A 307 2630 8515 8940 -1545 -698 229 C ATOM 2822 CG ASN A 307 -5.246 -25.807 31.571 1.00 83.21 C ANISOU 2822 CG ASN A 307 6508 12401 12707 -1441 -606 261 C ATOM 2823 OD1 ASN A 307 -5.870 -24.907 32.149 1.00 76.91 O ANISOU 2823 OD1 ASN A 307 5740 11683 11801 -1397 -552 310 O ATOM 2824 ND2 ASN A 307 -3.937 -25.953 31.713 1.00 78.48 N ANISOU 2824 ND2 ASN A 307 5912 11747 12161 -1398 -588 236 N ATOM 2825 N PRO A 308 -8.095 -28.748 29.269 1.00 53.97 N ANISOU 2825 N PRO A 308 2659 8601 9245 -1763 -924 327 N ATOM 2826 CA PRO A 308 -8.595 -29.488 28.087 1.00 54.87 C ANISOU 2826 CA PRO A 308 2782 8675 9392 -1879 -1031 268 C ATOM 2827 C PRO A 308 -10.021 -29.091 27.672 1.00 60.99 C ANISOU 2827 C PRO A 308 3501 9542 10132 -1928 -1071 411 C ATOM 2828 O PRO A 308 -10.384 -29.274 26.509 1.00 61.51 O ANISOU 2828 O PRO A 308 3596 9611 10164 -2011 -1136 345 O ATOM 2829 CB PRO A 308 -8.551 -30.958 28.532 1.00 57.26 C ANISOU 2829 CB PRO A 308 3046 8861 9850 -1926 -1115 283 C ATOM 2830 CG PRO A 308 -7.608 -30.989 29.688 1.00 61.10 C ANISOU 2830 CG PRO A 308 3518 9322 10376 -1832 -1041 303 C ATOM 2831 CD PRO A 308 -7.821 -29.680 30.383 1.00 55.73 C ANISOU 2831 CD PRO A 308 2827 8756 9591 -1737 -939 399 C ATOM 2832 N ILE A 309 -10.822 -28.544 28.612 1.00 58.09 N ANISOU 2832 N ILE A 309 3052 9251 9766 -1870 -1030 612 N ATOM 2833 CA ILE A 309 -12.198 -28.083 28.372 1.00 58.44 C ANISOU 2833 CA ILE A 309 3026 9397 9780 -1895 -1052 787 C ATOM 2834 C ILE A 309 -12.135 -26.791 27.523 1.00 61.66 C ANISOU 2834 C ILE A 309 3495 9895 10037 -1877 -992 724 C ATOM 2835 O ILE A 309 -12.956 -26.633 26.619 1.00 61.20 O ANISOU 2835 O ILE A 309 3415 9889 9948 -1950 -1047 764 O ATOM 2836 CB ILE A 309 -12.963 -27.904 29.729 1.00 61.58 C ANISOU 2836 CB ILE A 309 3332 9855 10211 -1805 -998 1013 C ATOM 2837 CG1 ILE A 309 -13.202 -29.289 30.409 1.00 62.99 C ANISOU 2837 CG1 ILE A 309 3423 9956 10553 -1854 -1084 1113 C ATOM 2838 CG2 ILE A 309 -14.285 -27.130 29.570 1.00 62.44 C ANISOU 2838 CG2 ILE A 309 3383 10097 10243 -1779 -965 1196 C ATOM 2839 CD1 ILE A 309 -13.716 -29.285 31.878 1.00 70.71 C ANISOU 2839 CD1 ILE A 309 4317 10974 11575 -1749 -1024 1312 C ATOM 2840 N ILE A 310 -11.132 -25.910 27.782 1.00 58.01 N ANISOU 2840 N ILE A 310 3109 9449 9484 -1786 -886 626 N ATOM 2841 CA ILE A 310 -10.905 -24.650 27.058 1.00 57.67 C ANISOU 2841 CA ILE A 310 3130 9482 9301 -1761 -822 559 C ATOM 2842 C ILE A 310 -10.512 -24.953 25.594 1.00 62.95 C ANISOU 2842 C ILE A 310 3858 10114 9947 -1855 -886 379 C ATOM 2843 O ILE A 310 -11.104 -24.370 24.686 1.00 62.31 O ANISOU 2843 O ILE A 310 3781 10104 9790 -1895 -899 388 O ATOM 2844 CB ILE A 310 -9.848 -23.747 27.775 1.00 59.77 C ANISOU 2844 CB ILE A 310 3463 9758 9488 -1647 -705 504 C ATOM 2845 CG1 ILE A 310 -10.405 -23.222 29.123 1.00 60.06 C ANISOU 2845 CG1 ILE A 310 3455 9835 9528 -1544 -643 684 C ATOM 2846 CG2 ILE A 310 -9.394 -22.562 26.879 1.00 60.00 C ANISOU 2846 CG2 ILE A 310 3560 9858 9380 -1630 -646 432 C ATOM 2847 CD1 ILE A 310 -9.352 -22.731 30.142 1.00 67.43 C ANISOU 2847 CD1 ILE A 310 4456 10744 10420 -1439 -555 632 C ATOM 2848 N TYR A 311 -9.556 -25.884 25.372 1.00 61.30 N ANISOU 2848 N TYR A 311 3694 9797 9802 -1887 -925 226 N ATOM 2849 CA TYR A 311 -9.089 -26.271 24.032 1.00 62.43 C ANISOU 2849 CA TYR A 311 3903 9897 9920 -1962 -983 52 C ATOM 2850 C TYR A 311 -10.181 -26.997 23.216 1.00 70.62 C ANISOU 2850 C TYR A 311 4904 10929 11000 -2076 -1107 104 C ATOM 2851 O TYR A 311 -10.101 -27.030 21.986 1.00 70.55 O ANISOU 2851 O TYR A 311 4951 10920 10936 -2138 -1155 -9 O ATOM 2852 CB TYR A 311 -7.838 -27.173 24.112 1.00 63.28 C ANISOU 2852 CB TYR A 311 4067 9886 10091 -1957 -992 -108 C ATOM 2853 CG TYR A 311 -6.650 -26.590 24.849 1.00 63.62 C ANISOU 2853 CG TYR A 311 4137 9919 10117 -1857 -889 -154 C ATOM 2854 CD1 TYR A 311 -6.022 -25.432 24.397 1.00 64.58 C ANISOU 2854 CD1 TYR A 311 4297 10119 10123 -1795 -795 -181 C ATOM 2855 CD2 TYR A 311 -6.066 -27.267 25.917 1.00 64.27 C ANISOU 2855 CD2 TYR A 311 4213 9908 10299 -1833 -893 -184 C ATOM 2856 CE1 TYR A 311 -4.913 -24.908 25.052 1.00 64.19 C ANISOU 2856 CE1 TYR A 311 4275 10055 10057 -1715 -714 -221 C ATOM 2857 CE2 TYR A 311 -4.953 -26.758 26.578 1.00 64.19 C ANISOU 2857 CE2 TYR A 311 4227 9890 10272 -1749 -807 -224 C ATOM 2858 CZ TYR A 311 -4.379 -25.578 26.141 1.00 70.32 C ANISOU 2858 CZ TYR A 311 5040 10744 10932 -1694 -722 -242 C ATOM 2859 OH TYR A 311 -3.275 -25.089 26.794 1.00 70.53 O ANISOU 2859 OH TYR A 311 5092 10761 10945 -1622 -650 -277 O ATOM 2860 N SER A 312 -11.184 -27.580 23.895 1.00 70.37 N ANISOU 2860 N SER A 312 4779 10893 11065 -2106 -1164 279 N ATOM 2861 CA SER A 312 -12.266 -28.328 23.265 1.00 72.76 C ANISOU 2861 CA SER A 312 5033 11188 11426 -2224 -1296 360 C ATOM 2862 C SER A 312 -13.264 -27.409 22.535 1.00 79.91 C ANISOU 2862 C SER A 312 5908 12220 12232 -2253 -1298 452 C ATOM 2863 O SER A 312 -13.752 -27.798 21.478 1.00 80.30 O ANISOU 2863 O SER A 312 5968 12265 12277 -2360 -1404 423 O ATOM 2864 CB SER A 312 -13.000 -29.168 24.306 1.00 77.03 C ANISOU 2864 CB SER A 312 5469 11697 12103 -2239 -1348 543 C ATOM 2865 OG SER A 312 -13.941 -30.026 23.679 1.00 87.19 O ANISOU 2865 OG SER A 312 6710 12953 13464 -2368 -1494 613 O ATOM 2866 N TYR A 313 -13.580 -26.213 23.084 1.00 78.47 N ANISOU 2866 N TYR A 313 5696 12150 11971 -2158 -1184 560 N ATOM 2867 CA TYR A 313 -14.551 -25.317 22.445 1.00 80.01 C ANISOU 2867 CA TYR A 313 5856 12469 12074 -2176 -1176 664 C ATOM 2868 C TYR A 313 -13.864 -24.158 21.678 1.00 85.44 C ANISOU 2868 C TYR A 313 6629 13217 12616 -2122 -1081 535 C ATOM 2869 O TYR A 313 -14.527 -23.516 20.858 1.00 85.45 O ANISOU 2869 O TYR A 313 6629 13298 12541 -2168 -1103 549 O ATOM 2870 CB TYR A 313 -15.567 -24.762 23.471 1.00 81.78 C ANISOU 2870 CB TYR A 313 5973 12785 12314 -2113 -1127 919 C ATOM 2871 CG TYR A 313 -15.078 -23.636 24.358 1.00 83.31 C ANISOU 2871 CG TYR A 313 6190 13039 12425 -1966 -974 958 C ATOM 2872 CD1 TYR A 313 -14.413 -23.900 25.554 1.00 84.77 C ANISOU 2872 CD1 TYR A 313 6410 13158 12642 -1879 -909 908 C ATOM 2873 CD2 TYR A 313 -15.370 -22.309 24.055 1.00 84.10 C ANISOU 2873 CD2 TYR A 313 6275 13261 12418 -1912 -900 1065 C ATOM 2874 CE1 TYR A 313 -13.997 -22.866 26.396 1.00 84.82 C ANISOU 2874 CE1 TYR A 313 6449 13212 12568 -1749 -780 945 C ATOM 2875 CE2 TYR A 313 -14.947 -21.266 24.880 1.00 84.20 C ANISOU 2875 CE2 TYR A 313 6323 13318 12352 -1775 -765 1103 C ATOM 2876 CZ TYR A 313 -14.258 -21.550 26.050 1.00 90.36 C ANISOU 2876 CZ TYR A 313 7148 14024 13159 -1696 -710 1039 C ATOM 2877 OH TYR A 313 -13.841 -20.528 26.869 1.00 88.94 O ANISOU 2877 OH TYR A 313 7017 13879 12897 -1566 -589 1071 O ATOM 2878 N ARG A 314 -12.559 -23.891 21.931 1.00 82.72 N ANISOU 2878 N ARG A 314 6354 12838 12237 -2031 -983 418 N ATOM 2879 CA ARG A 314 -11.847 -22.809 21.242 1.00 82.69 C ANISOU 2879 CA ARG A 314 6425 12888 12105 -1983 -896 307 C ATOM 2880 C ARG A 314 -11.135 -23.300 19.978 1.00 88.50 C ANISOU 2880 C ARG A 314 7244 13571 12812 -2041 -940 93 C ATOM 2881 O ARG A 314 -11.338 -22.711 18.913 1.00 88.12 O ANISOU 2881 O ARG A 314 7241 13584 12656 -2032 -898 19 O ATOM 2882 CB ARG A 314 -10.836 -22.110 22.161 1.00 82.62 C ANISOU 2882 CB ARG A 314 6453 12876 12064 -1862 -774 296 C ATOM 2883 CG ARG A 314 -11.439 -21.053 23.069 1.00 95.55 C ANISOU 2883 CG ARG A 314 8038 14589 13678 -1777 -702 495 C ATOM 2884 CD ARG A 314 -11.764 -19.705 22.416 1.00108.09 C ANISOU 2884 CD ARG A 314 9619 16295 15154 -1760 -656 578 C ATOM 2885 NE ARG A 314 -12.589 -18.964 23.377 1.00116.88 N ANISOU 2885 NE ARG A 314 10696 17473 16241 -1661 -578 767 N ATOM 2886 CZ ARG A 314 -13.584 -18.129 23.095 1.00128.80 C ANISOU 2886 CZ ARG A 314 12193 19085 17659 -1620 -521 877 C ATOM 2887 NH1 ARG A 314 -13.853 -17.807 21.839 1.00116.01 N ANISOU 2887 NH1 ARG A 314 10588 17520 15969 -1677 -537 821 N ATOM 2888 NH2 ARG A 314 -14.288 -17.574 24.075 1.00112.76 N1+ ANISOU 2888 NH2 ARG A 314 10138 17103 15604 -1516 -446 1046 N1+ ATOM 2889 N ASP A 315 -10.311 -24.368 20.088 1.00 86.46 N ANISOU 2889 N ASP A 315 7006 13199 12645 -2093 -1020 -3 N ATOM 2890 CA ASP A 315 -9.566 -24.923 18.950 1.00 87.11 C ANISOU 2890 CA ASP A 315 7175 13224 12699 -2137 -1063 -203 C ATOM 2891 C ASP A 315 -10.484 -25.786 18.096 1.00 93.54 C ANISOU 2891 C ASP A 315 7983 14017 13542 -2258 -1204 -198 C ATOM 2892 O ASP A 315 -11.121 -26.710 18.605 1.00 94.13 O ANISOU 2892 O ASP A 315 8003 14035 13725 -2314 -1292 -106 O ATOM 2893 CB ASP A 315 -8.332 -25.716 19.405 1.00 88.69 C ANISOU 2893 CB ASP A 315 7423 13306 12967 -2100 -1047 -332 C ATOM 2894 CG ASP A 315 -7.027 -24.954 19.264 1.00 97.19 C ANISOU 2894 CG ASP A 315 8563 14395 13971 -2016 -937 -455 C ATOM 2895 OD1 ASP A 315 -6.849 -23.937 19.977 1.00 96.86 O ANISOU 2895 OD1 ASP A 315 8509 14439 13853 -1957 -848 -396 O ATOM 2896 OD2 ASP A 315 -6.175 -25.386 18.465 1.00102.38 O1- ANISOU 2896 OD2 ASP A 315 9279 14971 14649 -2006 -940 -602 O1- ATOM 2897 N LYS A 316 -10.549 -25.462 16.795 1.00 91.08 N ANISOU 2897 N LYS A 316 7724 13753 13130 -2298 -1227 -289 N ATOM 2898 CA LYS A 316 -11.405 -26.112 15.806 1.00 92.38 C ANISOU 2898 CA LYS A 316 7900 13907 13295 -2416 -1366 -299 C ATOM 2899 C LYS A 316 -10.833 -27.471 15.351 1.00 97.74 C ANISOU 2899 C LYS A 316 8669 14444 14024 -2460 -1452 -472 C ATOM 2900 O LYS A 316 -11.591 -28.433 15.260 1.00 98.25 O ANISOU 2900 O LYS A 316 8727 14437 14165 -2558 -1586 -444 O ATOM 2901 CB LYS A 316 -11.613 -25.179 14.594 1.00 94.80 C ANISOU 2901 CB LYS A 316 8232 14329 13461 -2434 -1352 -327 C ATOM 2902 CG LYS A 316 -12.492 -23.949 14.881 1.00105.75 C ANISOU 2902 CG LYS A 316 9529 15856 14796 -2408 -1290 -140 C ATOM 2903 CD LYS A 316 -11.723 -22.692 15.333 1.00112.31 C ANISOU 2903 CD LYS A 316 10368 16746 15558 -2285 -1129 -144 C ATOM 2904 CE LYS A 316 -12.649 -21.550 15.675 1.00119.94 C ANISOU 2904 CE LYS A 316 11258 17839 16476 -2252 -1068 43 C ATOM 2905 NZ LYS A 316 -11.909 -20.397 16.242 1.00126.00 N1+ ANISOU 2905 NZ LYS A 316 12046 18643 17186 -2134 -922 41 N1+ ATOM 2906 N GLU A 317 -9.518 -27.548 15.067 1.00 94.60 N ANISOU 2906 N GLU A 317 8356 14003 13584 -2386 -1375 -644 N ATOM 2907 CA GLU A 317 -8.828 -28.767 14.622 1.00 95.56 C ANISOU 2907 CA GLU A 317 8576 13994 13736 -2399 -1429 -820 C ATOM 2908 C GLU A 317 -8.724 -29.819 15.748 1.00100.59 C ANISOU 2908 C GLU A 317 9188 14507 14526 -2399 -1464 -788 C ATOM 2909 O GLU A 317 -8.818 -31.018 15.469 1.00101.42 O ANISOU 2909 O GLU A 317 9355 14490 14691 -2453 -1564 -874 O ATOM 2910 CB GLU A 317 -7.422 -28.412 14.124 1.00 96.23 C ANISOU 2910 CB GLU A 317 8741 14095 13728 -2303 -1316 -982 C ATOM 2911 CG GLU A 317 -6.678 -29.558 13.461 1.00107.31 C ANISOU 2911 CG GLU A 317 10255 15377 15141 -2289 -1347 -1170 C ATOM 2912 CD GLU A 317 -7.044 -29.789 12.013 1.00130.53 C ANISOU 2912 CD GLU A 317 13288 18270 18036 -2370 -1471 -1272 C ATOM 2913 OE1 GLU A 317 -6.998 -28.812 11.232 1.00126.48 O ANISOU 2913 OE1 GLU A 317 12863 17787 17408 -2333 -1439 -1409 O ATOM 2914 OE2 GLU A 317 -7.279 -30.963 11.647 1.00126.24 O1- ANISOU 2914 OE2 GLU A 317 12735 17656 17573 -2468 -1605 -1218 O1- ATOM 2915 N MET A 318 -8.523 -29.364 17.003 1.00 96.76 N ANISOU 2915 N MET A 318 8617 14047 14099 -2337 -1382 -664 N ATOM 2916 CA MET A 318 -8.362 -30.219 18.182 1.00 96.90 C ANISOU 2916 CA MET A 318 8597 13963 14259 -2325 -1400 -614 C ATOM 2917 C MET A 318 -9.689 -30.902 18.566 1.00103.54 C ANISOU 2917 C MET A 318 9374 14762 15205 -2432 -1537 -480 C ATOM 2918 O MET A 318 -9.663 -32.061 18.984 1.00103.47 O ANISOU 2918 O MET A 318 9371 14629 15312 -2462 -1605 -495 O ATOM 2919 CB MET A 318 -7.816 -29.393 19.363 1.00 97.66 C ANISOU 2919 CB MET A 318 8623 14115 14367 -2227 -1276 -511 C ATOM 2920 CG MET A 318 -6.931 -30.183 20.327 1.00100.72 C ANISOU 2920 CG MET A 318 9003 14399 14867 -2178 -1253 -528 C ATOM 2921 SD MET A 318 -5.112 -29.960 20.363 1.00103.69 S ANISOU 2921 SD MET A 318 9462 14740 15197 -2076 -1140 -711 S ATOM 2922 CE MET A 318 -4.928 -28.169 20.439 1.00 98.73 C ANISOU 2922 CE MET A 318 8790 14244 14480 -1988 -1006 -621 C ATOM 2923 N SER A 319 -10.837 -30.193 18.397 1.00102.04 N ANISOU 2923 N SER A 319 9120 14674 14975 -2490 -1578 -343 N ATOM 2924 CA SER A 319 -12.198 -30.675 18.691 1.00103.70 C ANISOU 2924 CA SER A 319 9251 14871 15277 -2598 -1710 -184 C ATOM 2925 C SER A 319 -12.574 -31.901 17.831 1.00111.10 C ANISOU 2925 C SER A 319 10269 15683 16262 -2712 -1869 -293 C ATOM 2926 O SER A 319 -13.358 -32.734 18.280 1.00111.66 O ANISOU 2926 O SER A 319 10293 15673 16461 -2790 -1980 -199 O ATOM 2927 CB SER A 319 -13.228 -29.574 18.464 1.00107.09 C ANISOU 2927 CB SER A 319 9609 15450 15630 -2631 -1712 -34 C ATOM 2928 OG SER A 319 -13.005 -28.418 19.249 1.00114.60 O ANISOU 2928 OG SER A 319 10491 16511 16541 -2526 -1574 86 O ATOM 2929 N ALA A 320 -12.034 -32.001 16.595 1.00109.54 N ANISOU 2929 N ALA A 320 10196 15466 15960 -2719 -1881 -488 N ATOM 2930 CA ALA A 320 -12.268 -33.133 15.687 1.00111.63 C ANISOU 2930 CA ALA A 320 10570 15610 16233 -2813 -2025 -625 C ATOM 2931 C ALA A 320 -11.321 -34.328 15.977 1.00117.23 C ANISOU 2931 C ALA A 320 11336 16145 17059 -2798 -2055 -718 C ATOM 2932 O ALA A 320 -11.656 -35.478 15.660 1.00118.27 O ANISOU 2932 O ALA A 320 11506 16156 17274 -2900 -2206 -729 O ATOM 2933 CB ALA A 320 -12.120 -32.691 14.242 1.00112.48 C ANISOU 2933 CB ALA A 320 10799 15756 16182 -2785 -1992 -811 C ATOM 2934 N THR A 321 -10.180 -34.056 16.629 1.00113.68 N ANISOU 2934 N THR A 321 10888 15678 16629 -2679 -1923 -768 N ATOM 2935 CA THR A 321 -9.169 -35.050 16.995 1.00114.46 C ANISOU 2935 CA THR A 321 11025 15619 16847 -2659 -1944 -835 C ATOM 2936 C THR A 321 -9.713 -35.872 18.210 1.00120.27 C ANISOU 2936 C THR A 321 11657 16290 17749 -2730 -2036 -658 C ATOM 2937 O THR A 321 -9.461 -37.064 18.299 1.00120.74 O ANISOU 2937 O THR A 321 11764 16197 17916 -2788 -2143 -700 O ATOM 2938 CB THR A 321 -7.810 -34.312 17.249 1.00121.28 C ANISOU 2938 CB THR A 321 11892 16492 17698 -2518 -1779 -900 C ATOM 2939 OG1 THR A 321 -7.565 -33.322 16.227 1.00119.83 O ANISOU 2939 OG1 THR A 321 11744 16425 17363 -2449 -1671 -979 O ATOM 2940 CG2 THR A 321 -6.605 -35.270 17.291 1.00120.70 C ANISOU 2940 CG2 THR A 321 11920 16258 17683 -2486 -1793 -1058 C ATOM 2941 N PHE A 322 -10.505 -35.223 19.095 1.00117.51 N ANISOU 2941 N PHE A 322 11169 16058 17421 -2721 -1992 -455 N ATOM 2942 CA PHE A 322 -11.150 -35.802 20.278 1.00118.37 C ANISOU 2942 CA PHE A 322 11159 16134 17683 -2760 -2048 -261 C ATOM 2943 C PHE A 322 -12.183 -36.899 19.933 1.00125.48 C ANISOU 2943 C PHE A 322 12054 16952 18670 -2916 -2243 -198 C ATOM 2944 O PHE A 322 -12.313 -37.858 20.684 1.00125.78 O ANISOU 2944 O PHE A 322 12060 16875 18856 -2961 -2323 -137 O ATOM 2945 CB PHE A 322 -11.849 -34.707 21.089 1.00119.15 C ANISOU 2945 CB PHE A 322 11120 16392 17761 -2708 -1955 -54 C ATOM 2946 CG PHE A 322 -11.018 -34.068 22.175 1.00119.21 C ANISOU 2946 CG PHE A 322 11113 16445 17738 -2562 -1785 -69 C ATOM 2947 CD1 PHE A 322 -9.784 -33.483 21.893 1.00121.51 C ANISOU 2947 CD1 PHE A 322 11493 16768 17906 -2481 -1679 -238 C ATOM 2948 CD2 PHE A 322 -11.479 -34.026 23.484 1.00120.97 C ANISOU 2948 CD2 PHE A 322 11230 16681 18053 -2507 -1736 91 C ATOM 2949 CE1 PHE A 322 -8.994 -32.939 22.920 1.00121.10 C ANISOU 2949 CE1 PHE A 322 11429 16755 17830 -2359 -1536 -247 C ATOM 2950 CE2 PHE A 322 -10.704 -33.452 24.496 1.00122.49 C ANISOU 2950 CE2 PHE A 322 11417 16912 18212 -2379 -1591 74 C ATOM 2951 CZ PHE A 322 -9.478 -32.899 24.200 1.00119.75 C ANISOU 2951 CZ PHE A 322 11161 16591 17746 -2310 -1495 -95 C ATOM 2952 N ARG A 323 -12.922 -36.751 18.814 1.00123.94 N ANISOU 2952 N ARG A 323 11890 16814 18387 -3002 -2324 -209 N ATOM 2953 CA ARG A 323 -13.910 -37.730 18.330 1.00126.20 C ANISOU 2953 CA ARG A 323 12183 17024 18743 -3163 -2525 -155 C ATOM 2954 C ARG A 323 -13.220 -39.021 17.825 1.00133.15 C ANISOU 2954 C ARG A 323 13208 17703 19679 -3198 -2618 -347 C ATOM 2955 O ARG A 323 -13.798 -40.111 17.889 1.00134.39 O ANISOU 2955 O ARG A 323 13358 17737 19969 -3304 -2766 -288 O ATOM 2956 CB ARG A 323 -14.781 -37.125 17.193 1.00126.63 C ANISOU 2956 CB ARG A 323 12263 17181 18669 -3239 -2587 -162 C ATOM 2957 CG ARG A 323 -15.736 -36.020 17.626 1.00136.75 C ANISOU 2957 CG ARG A 323 13390 18576 19992 -3329 -2659 100 C ATOM 2958 CD ARG A 323 -16.730 -35.691 16.510 1.00146.94 C ANISOU 2958 CD ARG A 323 14718 19948 21163 -3421 -2746 83 C ATOM 2959 NE ARG A 323 -16.198 -34.700 15.579 1.00153.30 N ANISOU 2959 NE ARG A 323 15523 20913 21812 -3317 -2590 49 N ATOM 2960 CZ ARG A 323 -16.735 -34.391 14.392 1.00167.23 C ANISOU 2960 CZ ARG A 323 17360 22745 23435 -3350 -2614 -44 C ATOM 2961 NH1 ARG A 323 -17.788 -35.067 13.938 1.00155.53 N ANISOU 2961 NH1 ARG A 323 15965 21187 21943 -3484 -2792 -120 N ATOM 2962 NH2 ARG A 323 -16.172 -33.471 13.623 1.00152.91 N1+ ANISOU 2962 NH2 ARG A 323 15536 21073 21490 -3250 -2465 -62 N1+ ATOM 2963 N GLN A 324 -11.985 -38.871 17.324 1.00130.34 N ANISOU 2963 N GLN A 324 12986 17317 19221 -3106 -2528 -569 N ATOM 2964 CA GLN A 324 -11.143 -39.944 16.773 1.00131.76 C ANISOU 2964 CA GLN A 324 13321 17311 19429 -3107 -2586 -769 C ATOM 2965 C GLN A 324 -10.599 -40.879 17.866 1.00136.27 C ANISOU 2965 C GLN A 324 13854 17757 20167 -3075 -2576 -727 C ATOM 2966 O GLN A 324 -10.263 -42.031 17.564 1.00137.35 O ANISOU 2966 O GLN A 324 14075 17718 20392 -3138 -2697 -797 O ATOM 2967 CB GLN A 324 -9.962 -39.342 15.971 1.00132.61 C ANISOU 2967 CB GLN A 324 13558 17441 19387 -2988 -2460 -990 C ATOM 2968 CG GLN A 324 -10.383 -38.593 14.702 1.00152.61 C ANISOU 2968 CG GLN A 324 16182 20045 21759 -3031 -2505 -1088 C ATOM 2969 CD GLN A 324 -11.307 -39.397 13.813 1.00178.16 C ANISOU 2969 CD GLN A 324 19462 23204 25027 -3200 -2722 -1060 C ATOM 2970 OE1 GLN A 324 -11.002 -40.507 13.373 1.00176.07 O ANISOU 2970 OE1 GLN A 324 19272 22765 24864 -3264 -2846 -1109 O ATOM 2971 NE2 GLN A 324 -12.488 -38.860 13.588 1.00171.65 N ANISOU 2971 NE2 GLN A 324 18593 22509 24118 -3275 -2773 -978 N ATOM 2972 N ILE A 325 -10.464 -40.371 19.116 1.00131.67 N ANISOU 2972 N ILE A 325 13151 17258 19621 -2974 -2434 -616 N ATOM 2973 CA ILE A 325 -9.952 -41.130 20.250 1.00131.50 C ANISOU 2973 CA ILE A 325 13095 17130 19738 -2919 -2397 -592 C ATOM 2974 C ILE A 325 -10.956 -42.174 20.712 1.00137.22 C ANISOU 2974 C ILE A 325 13756 17736 20648 -3029 -2546 -451 C ATOM 2975 O ILE A 325 -10.521 -43.231 21.145 1.00137.31 O ANISOU 2975 O ILE A 325 13821 17589 20762 -3019 -2577 -520 O ATOM 2976 CB ILE A 325 -9.514 -40.229 21.433 1.00132.72 C ANISOU 2976 CB ILE A 325 13132 17410 19885 -2791 -2220 -489 C ATOM 2977 CG1 ILE A 325 -8.271 -40.785 22.116 1.00132.85 C ANISOU 2977 CG1 ILE A 325 13152 17319 20006 -2708 -2156 -528 C ATOM 2978 CG2 ILE A 325 -10.618 -39.890 22.436 1.00133.16 C ANISOU 2978 CG2 ILE A 325 13020 17582 19994 -2832 -2237 -231 C ATOM 2979 CD1 ILE A 325 -7.111 -40.041 21.823 1.00139.42 C ANISOU 2979 CD1 ILE A 325 14040 18192 20741 -2566 -1990 -671 C ATOM 2980 N LEU A 326 -12.286 -41.897 20.638 1.00134.80 N ANISOU 2980 N LEU A 326 13328 17503 20386 -3129 -2636 -245 N ATOM 2981 CA LEU A 326 -13.341 -42.825 21.066 1.00135.94 C ANISOU 2981 CA LEU A 326 13376 17560 20714 -3230 -2768 -66 C ATOM 2982 C LEU A 326 -13.334 -44.131 20.235 1.00141.34 C ANISOU 2982 C LEU A 326 14195 18024 21485 -3332 -2936 -193 C ATOM 2983 O LEU A 326 -13.557 -45.215 20.786 1.00141.67 O ANISOU 2983 O LEU A 326 14187 17948 21692 -3371 -3005 -104 O ATOM 2984 CB LEU A 326 -14.727 -42.170 20.993 1.00136.61 C ANISOU 2984 CB LEU A 326 13327 17767 20812 -3338 -2858 166 C ATOM 2985 CG LEU A 326 -15.022 -41.059 22.015 1.00140.01 C ANISOU 2985 CG LEU A 326 13595 18399 21203 -3248 -2716 363 C ATOM 2986 CD1 LEU A 326 -16.250 -40.298 21.608 1.00140.74 C ANISOU 2986 CD1 LEU A 326 13604 18623 21249 -3344 -2793 526 C ATOM 2987 CD2 LEU A 326 -15.242 -41.632 23.440 1.00142.42 C ANISOU 2987 CD2 LEU A 326 13760 18696 21657 -3197 -2670 550 C ATOM 2988 N GLY A 327 -13.070 -44.010 18.932 1.00138.38 N ANISOU 2988 N GLY A 327 13987 17594 20996 -3372 -3001 -392 N ATOM 2989 CA GLY A 327 -12.993 -45.137 18.007 1.00166.01 C ANISOU 2989 CA GLY A 327 17650 20881 24546 -3460 -3160 -541 C ATOM 2990 C GLY A 327 -11.609 -45.746 17.918 1.00181.39 C ANISOU 2990 C GLY A 327 19793 22749 26379 -3356 -3081 -823 C ATOM 2991 O GLY A 327 -10.981 -46.043 18.937 1.00136.75 O ANISOU 2991 O GLY A 327 14154 17055 20750 -3227 -2949 -895 O TER 2992 GLY A 327 HETATM 2993 O5 ON7 A2001 -8.538 -28.661 53.158 1.00 57.59 O ANISOU 2993 O5 ON7 A2001 2716 9532 9634 203 -74 2425 O HETATM 2994 C28 ON7 A2001 -7.476 -29.205 52.843 1.00 57.42 C ANISOU 2994 C28 ON7 A2001 2702 9424 9691 96 -129 2262 C HETATM 2995 O4 ON7 A2001 -7.451 -30.351 52.064 1.00 58.00 O ANISOU 2995 O4 ON7 A2001 2653 9432 9952 -43 -202 2242 O HETATM 2996 C29 ON7 A2001 -8.634 -30.958 51.620 1.00 58.56 C ANISOU 2996 C29 ON7 A2001 2586 9528 10137 -80 -227 2405 C HETATM 2997 C25 ON7 A2001 -6.126 -28.784 53.145 1.00 56.22 C ANISOU 2997 C25 ON7 A2001 2679 9225 9458 93 -132 2078 C HETATM 2998 C24 ON7 A2001 -4.980 -29.564 53.542 1.00 57.22 C ANISOU 2998 C24 ON7 A2001 2789 9284 9667 47 -170 1983 C HETATM 2999 C30 ON7 A2001 -4.871 -31.028 53.759 1.00 61.22 C ANISOU 2999 C30 ON7 A2001 3151 9743 10368 -14 -215 2030 C HETATM 3000 C31 ON7 A2001 -4.850 -31.453 55.282 1.00 64.92 C ANISOU 3000 C31 ON7 A2001 3559 10254 10854 108 -185 2190 C HETATM 3001 O7 ON7 A2001 -5.416 -32.537 55.557 1.00 66.60 O ANISOU 3001 O7 ON7 A2001 3625 10451 11228 79 -213 2305 O HETATM 3002 O6 ON7 A2001 -4.272 -30.707 56.118 1.00 65.70 O ANISOU 3002 O6 ON7 A2001 3761 10396 10804 225 -141 2192 O HETATM 3003 C23 ON7 A2001 -3.937 -28.664 53.693 1.00 54.18 C ANISOU 3003 C23 ON7 A2001 2553 8883 9149 65 -159 1835 C HETATM 3004 C26 ON7 A2001 -5.744 -27.457 53.068 1.00 53.93 C ANISOU 3004 C26 ON7 A2001 2553 8949 8988 140 -97 1977 C HETATM 3005 N1 ON7 A2001 -4.414 -27.383 53.409 1.00 51.90 N ANISOU 3005 N1 ON7 A2001 2378 8640 8702 119 -118 1829 N HETATM 3006 C13 ON7 A2001 -3.670 -26.134 53.514 1.00 48.88 C ANISOU 3006 C13 ON7 A2001 2172 8250 8150 152 -103 1702 C HETATM 3007 C8 ON7 A2001 -3.003 -25.572 52.228 1.00 45.75 C ANISOU 3007 C8 ON7 A2001 1846 7802 7734 26 -135 1511 C HETATM 3008 C6 ON7 A2001 -2.015 -26.601 51.510 1.00 43.44 C ANISOU 3008 C6 ON7 A2001 1467 7432 7604 -124 -198 1386 C HETATM 3009 O2 ON7 A2001 -1.001 -27.045 52.382 1.00 41.53 O ANISOU 3009 O2 ON7 A2001 1214 7162 7404 -114 -217 1361 O HETATM 3010 C3 ON7 A2001 -1.342 -25.966 50.303 1.00 42.96 C ANISOU 3010 C3 ON7 A2001 1483 7331 7508 -229 -221 1205 C HETATM 3011 C2 ON7 A2001 -1.807 -26.320 49.027 1.00 43.01 C ANISOU 3011 C2 ON7 A2001 1421 7316 7602 -332 -245 1165 C HETATM 3012 C5 ON7 A2001 -0.293 -25.050 50.454 1.00 42.97 C ANISOU 3012 C5 ON7 A2001 1615 7314 7396 -227 -225 1086 C HETATM 3013 C7 ON7 A2001 0.303 -24.477 49.308 1.00 42.84 C ANISOU 3013 C7 ON7 A2001 1651 7264 7364 -329 -247 931 C HETATM 3014 O3 ON7 A2001 1.337 -23.560 49.438 1.00 44.06 O ANISOU 3014 O3 ON7 A2001 1927 7401 7414 -336 -257 826 O HETATM 3015 C11 ON7 A2001 2.623 -24.082 49.797 1.00 44.38 C ANISOU 3015 C11 ON7 A2001 1952 7403 7508 -371 -293 763 C HETATM 3016 C9 ON7 A2001 -0.143 -24.796 47.993 1.00 41.84 C ANISOU 3016 C9 ON7 A2001 1455 7122 7321 -426 -263 886 C HETATM 3017 C10 ON7 A2001 0.474 -24.174 46.791 1.00 40.74 C ANISOU 3017 C10 ON7 A2001 1367 6954 7158 -522 -280 730 C HETATM 3018 C1 ON7 A2001 -1.229 -25.736 47.883 1.00 42.26 C ANISOU 3018 C1 ON7 A2001 1387 7190 7482 -426 -264 1004 C HETATM 3019 O1 ON7 A2001 -1.659 -26.020 46.591 1.00 41.12 O ANISOU 3019 O1 ON7 A2001 1188 7027 7410 -524 -290 958 O HETATM 3020 C4 ON7 A2001 -3.005 -25.853 46.248 1.00 39.88 C ANISOU 3020 C4 ON7 A2001 978 6916 7260 -511 -279 1077 C HETATM 3021 C12 ON7 A2001 -4.033 -24.989 51.226 1.00 44.98 C ANISOU 3021 C12 ON7 A2001 1761 7740 7590 14 -110 1539 C HETATM 3022 C14 ON7 A2001 -4.223 -23.445 51.197 1.00 44.41 C ANISOU 3022 C14 ON7 A2001 1857 7695 7322 86 -67 1500 C HETATM 3023 C16 ON7 A2001 -2.991 -22.647 50.662 1.00 43.72 C ANISOU 3023 C16 ON7 A2001 1885 7548 7179 -1 -101 1297 C HETATM 3024 C18 ON7 A2001 -3.234 -22.517 49.196 1.00 43.31 C ANISOU 3024 C18 ON7 A2001 1792 7486 7177 -113 -117 1229 C HETATM 3025 C19 ON7 A2001 -2.336 -22.167 48.187 1.00 42.59 C ANISOU 3025 C19 ON7 A2001 1730 7346 7107 -235 -155 1060 C HETATM 3026 C20 ON7 A2001 -2.766 -22.209 46.841 1.00 42.08 C ANISOU 3026 C20 ON7 A2001 1608 7284 7097 -327 -168 1026 C HETATM 3027 C21 ON7 A2001 -4.072 -22.598 46.529 1.00 43.27 C ANISOU 3027 C21 ON7 A2001 1674 7483 7283 -306 -150 1162 C HETATM 3028 C22 ON7 A2001 -4.993 -22.945 47.560 1.00 44.65 C ANISOU 3028 C22 ON7 A2001 1812 7711 7440 -184 -111 1344 C HETATM 3029 C17 ON7 A2001 -4.558 -22.882 48.893 1.00 44.19 C ANISOU 3029 C17 ON7 A2001 1815 7652 7323 -83 -90 1373 C HETATM 3030 C15 ON7 A2001 -5.324 -23.128 50.154 1.00 44.74 C ANISOU 3030 C15 ON7 A2001 1871 7777 7352 66 -43 1552 C HETATM 3031 C10 1WV A2002 10.697 -37.914 40.594 1.00 63.06 C ANISOU 3031 C10 1WV A2002 3645 8920 11394 -1031 -428 -245 C HETATM 3032 C13 1WV A2002 8.977 -35.350 42.907 1.00 63.50 C ANISOU 3032 C13 1WV A2002 3692 9188 11248 -994 -446 13 C HETATM 3033 C17 1WV A2002 9.241 -34.243 46.208 1.00 60.22 C ANISOU 3033 C17 1WV A2002 3244 8912 10724 -867 -432 265 C HETATM 3034 C20 1WV A2002 9.554 -34.604 48.709 1.00 56.61 C ANISOU 3034 C20 1WV A2002 2709 8493 10306 -768 -429 441 C HETATM 3035 C07 1WV A2002 10.949 -41.225 38.540 1.00 65.17 C ANISOU 3035 C07 1WV A2002 3955 8872 11935 -1047 -468 -427 C HETATM 3036 C08 1WV A2002 11.392 -39.945 39.282 1.00 64.06 C ANISOU 3036 C08 1WV A2002 3789 8862 11690 -1025 -427 -375 C HETATM 3037 C09 1WV A2002 10.200 -39.173 39.885 1.00 63.80 C ANISOU 3037 C09 1WV A2002 3739 8899 11603 -1053 -462 -280 C HETATM 3038 C11 1WV A2002 9.554 -37.148 41.259 1.00 62.97 C ANISOU 3038 C11 1WV A2002 3629 8975 11323 -1040 -453 -149 C HETATM 3039 C12 1WV A2002 10.107 -35.993 42.094 1.00 62.95 C ANISOU 3039 C12 1WV A2002 3631 9068 11219 -1009 -426 -103 C HETATM 3040 C14 1WV A2002 9.523 -34.244 43.780 1.00 63.58 C ANISOU 3040 C14 1WV A2002 3725 9281 11151 -959 -428 59 C HETATM 3041 O15 1WV A2002 9.657 -33.065 43.457 1.00 63.89 O ANISOU 3041 O15 1WV A2002 3830 9377 11070 -969 -419 21 O HETATM 3042 O16 1WV A2002 9.906 -34.703 45.026 1.00 62.49 O ANISOU 3042 O16 1WV A2002 3532 9145 11068 -913 -427 151 O HETATM 3043 C18 1WV A2002 10.291 -34.327 47.362 1.00 57.82 C ANISOU 3043 C18 1WV A2002 2926 8639 10406 -828 -424 303 C HETATM 3044 O19 1WV A2002 10.904 -33.083 47.580 1.00 56.64 O ANISOU 3044 O19 1WV A2002 2854 8555 10111 -820 -424 295 O HETATM 3045 O21 1WV A2002 10.457 -34.865 49.733 1.00 55.23 O ANISOU 3045 O21 1WV A2002 2538 8363 10084 -728 -428 489 O HETATM 3046 C1 1WV A2002 10.237 -40.922 37.242 1.00 65.38 C ANISOU 3046 C1 1WV A2002 4062 8888 11893 -1101 -504 -517 C HETATM 3047 C2 1WV A2002 9.444 -41.748 36.526 1.00 66.68 C ANISOU 3047 C2 1WV A2002 4268 8954 12113 -1146 -564 -563 C HETATM 3048 C3 1WV A2002 9.092 -43.165 36.853 1.00 68.04 C ANISOU 3048 C3 1WV A2002 4423 8992 12438 -1155 -612 -537 C CONECT 36 1298 CONECT 1284 1334 CONECT 1298 36 CONECT 1334 1284 CONECT 2638 2660 CONECT 2660 2638 CONECT 2993 2994 CONECT 2994 2993 2995 2997 CONECT 2995 2994 2996 CONECT 2996 2995 CONECT 2997 2994 2998 3004 CONECT 2998 2997 2999 3003 CONECT 2999 2998 3000 CONECT 3000 2999 3001 3002 CONECT 3001 3000 CONECT 3002 3000 CONECT 3003 2998 3005 CONECT 3004 2997 3005 CONECT 3005 3003 3004 3006 CONECT 3006 3005 3007 CONECT 3007 3006 3008 3021 CONECT 3008 3007 3009 3010 CONECT 3009 3008 CONECT 3010 3008 3011 3012 CONECT 3011 3010 3018 CONECT 3012 3010 3013 CONECT 3013 3012 3014 3016 CONECT 3014 3013 3015 CONECT 3015 3014 CONECT 3016 3013 3017 3018 CONECT 3017 3016 CONECT 3018 3011 3016 3019 CONECT 3019 3018 3020 CONECT 3020 3019 CONECT 3021 3007 3022 CONECT 3022 3021 3023 3030 CONECT 3023 3022 3024 CONECT 3024 3023 3025 3029 CONECT 3025 3024 3026 CONECT 3026 3025 3027 CONECT 3027 3026 3028 CONECT 3028 3027 3029 CONECT 3029 3024 3028 3030 CONECT 3030 3022 3029 CONECT 3031 3037 3038 CONECT 3032 3039 3040 CONECT 3033 3042 3043 CONECT 3034 3043 3045 CONECT 3035 3036 3046 CONECT 3036 3035 3037 CONECT 3037 3031 3036 CONECT 3038 3031 3039 CONECT 3039 3032 3038 CONECT 3040 3032 3041 3042 CONECT 3041 3040 CONECT 3042 3033 3040 CONECT 3043 3033 3034 3044 CONECT 3044 3043 CONECT 3045 3034 CONECT 3046 3035 3047 CONECT 3047 3046 3048 CONECT 3048 3047 MASTER 388 0 2 16 0 0 6 6 3047 1 62 36 END