HEADER TRANSPORT PROTEIN/INHIBITOR 30-MAR-15 4Z36 TITLE CRYSTAL STRUCTURE OF HUMAN LYSOPHOSPHATIDIC ACID RECEPTOR 1 IN COMPLEX TITLE 2 WITH ONO-3080573 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 78- COMPND 5 127; UNP RESIDUES 249-327; 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), NOVEL DISULFIDE BOND ENGINEERING, COMPOUND DESIGN, KEYWDS 5 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 4Z36 1 JRNL REVDAT 1 03-JUN-15 4Z36 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. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 3 NUMBER OF REFLECTIONS : 12660 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) : 0.273 REMARK 3 R VALUE (WORKING SET) : 0.272 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 625 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 : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.18 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.11 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2593 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2572 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2476 REMARK 3 BIN R VALUE (WORKING SET) : 0.2562 REMARK 3 BIN FREE R VALUE : 0.2793 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.51 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 117 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 : 3014 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 56 REMARK 3 SOLVENT ATOMS : 3 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 66.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 95.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 11.89450 REMARK 3 B22 (A**2) : -7.10170 REMARK 3 B33 (A**2) : -4.79280 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) : 0.684 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 4.569 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.426 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 2.352 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.429 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 : 0.885 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.848 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3141 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4267 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1445 ; 4.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 62 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 476 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3141 ; 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 : 419 ; 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 : 3662 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.87 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.58 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.61 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): -0.3047 -18.8188 30.2925 REMARK 3 T TENSOR REMARK 3 T11: -0.1899 T22: 0.1980 REMARK 3 T33: 0.1326 T12: -0.1437 REMARK 3 T13: -0.0055 T23: 0.0353 REMARK 3 L TENSOR REMARK 3 L11: 0.7166 L22: 0.8696 REMARK 3 L33: 0.3715 L12: -0.6523 REMARK 3 L13: 0.2160 L23: -0.7267 REMARK 3 S TENSOR REMARK 3 S11: -0.0088 S12: -0.0203 S13: -0.1395 REMARK 3 S21: -0.1020 S22: 0.1233 S23: -0.0956 REMARK 3 S31: -0.0382 S32: -0.0319 S33: -0.1145 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4Z36 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_1000208429. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-NOV-13; 30-NOV-13 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 : 12701 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 47.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.30 REMARK 200 R MERGE FOR SHELL (I) : 0.59000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89 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 17.17500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.98000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.96500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.98000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.17500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.96500 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 ASN A 20 REMARK 465 GLU A 21 REMARK 465 PRO A 22 REMARK 465 GLY A 1049 REMARK 465 SER A 1050 REMARK 465 GLY A 1051 REMARK 465 GLY A 1052 REMARK 465 SER 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 GLN A 23 CG CD OE1 NE2 REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2 REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 LEU A1106 CG CD1 CD2 REMARK 470 GLN A 286 CG CD OE1 NE2 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 95.78 -68.95 REMARK 500 MET A 153 -59.83 64.90 REMARK 500 ASP A 191 52.06 -143.41 REMARK 500 ASN A 194 38.69 -99.26 REMARK 500 GLN A 286 0.97 84.08 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 2001 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ON3 A 2000 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1WV A 2001 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-235 RELATED DB: TARGETTRACK REMARK 900 RELATED ID: 4Z34 RELATED DB: PDB REMARK 900 RELATED ID: 4Z35 RELATED DB: PDB DBREF 4Z36 A 2 232 UNP Q92633 LPAR1_HUMAN 2 232 DBREF 4Z36 A 1001 1042 UNP P0ABE7 C562_ECOLX 23 64 DBREF 4Z36 A 1056 1105 UNP P0ABE7 C562_ECOLX 78 127 DBREF 4Z36 A 248 326 UNP Q92633 LPAR1_HUMAN 249 327 SEQADV 4Z36 MET A -17 UNP Q92633 INITIATING METHIONINE SEQADV 4Z36 LYS A -16 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 THR A -15 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ILE A -14 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ILE A -13 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ALA A -12 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 LEU A -11 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 SER A -10 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 TYR A -9 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ILE A -8 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 PHE A -7 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 CYS A -6 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 LEU A -5 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 VAL A -4 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 PHE A -3 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ALA A -2 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 GLY A -1 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ALA A 0 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 PRO A 1 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 CYS A 204 UNP Q92633 ASP 204 ENGINEERED MUTATION SEQADV 4Z36 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4Z36 GLY A 1043 UNP P0ABE7 LINKER SEQADV 4Z36 GLY A 1049 UNP P0ABE7 LINKER SEQADV 4Z36 SER A 1050 UNP P0ABE7 LINKER SEQADV 4Z36 GLY A 1051 UNP P0ABE7 LINKER SEQADV 4Z36 GLY A 1052 UNP P0ABE7 LINKER SEQADV 4Z36 SER A 1053 UNP P0ABE7 LINKER SEQADV 4Z36 ASP A 1054 UNP P0ABE7 LINKER SEQADV 4Z36 SER A 1055 UNP P0ABE7 LINKER SEQADV 4Z36 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4Z36 LEU A 1106 UNP P0ABE7 LINKER SEQADV 4Z36 CYS A 282 UNP Q92633 VAL 283 CONFLICT SEQADV 4Z36 GLY A 327 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ARG A 328 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 PRO A 329 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 LEU A 330 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 GLU A 331 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 VAL A 332 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 LEU A 333 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 PHE A 334 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 GLN A 335 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 GLY A 336 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 PRO A 337 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 338 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 339 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 340 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 341 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 342 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 343 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 344 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 345 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 346 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 HIS A 347 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ASP A 348 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 TYR A 349 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 LYS A 350 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ASP A 351 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ASP A 352 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ASP A 353 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 ASP A 354 UNP Q92633 EXPRESSION TAG SEQADV 4Z36 LYS A 355 UNP Q92633 EXPRESSION TAG SEQRES 1 A 459 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 459 VAL PHE ALA GLY ALA PRO ALA ALA ILE SER THR SER ILE SEQRES 3 A 459 PRO VAL ILE SER GLN PRO GLN PHE THR ALA MET ASN GLU SEQRES 4 A 459 PRO GLN CYS PHE TYR ASN GLU SER ILE ALA PHE PHE TYR SEQRES 5 A 459 ASN ARG SER GLY LYS HIS LEU ALA THR GLU TRP ASN THR SEQRES 6 A 459 VAL SER LYS LEU VAL MET GLY LEU GLY ILE THR VAL CYS SEQRES 7 A 459 ILE PHE ILE MET LEU ALA ASN LEU LEU VAL MET VAL ALA SEQRES 8 A 459 ILE TYR VAL ASN ARG ARG PHE HIS PHE PRO ILE TYR TYR SEQRES 9 A 459 LEU MET ALA ASN LEU ALA ALA ALA ASP PHE PHE ALA GLY SEQRES 10 A 459 LEU ALA TYR PHE TYR LEU MET PHE ASN THR GLY PRO ASN SEQRES 11 A 459 THR ARG ARG LEU THR VAL SER THR TRP LEU LEU ARG GLN SEQRES 12 A 459 GLY LEU ILE ASP THR SER LEU THR ALA SER VAL ALA ASN SEQRES 13 A 459 LEU LEU ALA ILE ALA ILE GLU ARG HIS ILE THR VAL PHE SEQRES 14 A 459 ARG MET GLN LEU HIS THR ARG MET SER ASN ARG ARG VAL SEQRES 15 A 459 VAL VAL VAL ILE VAL VAL ILE TRP THR MET ALA ILE VAL SEQRES 16 A 459 MET GLY ALA ILE PRO SER VAL GLY TRP ASN CYS ILE CYS SEQRES 17 A 459 ASP ILE GLU ASN CYS SER ASN MET ALA PRO LEU TYR SER SEQRES 18 A 459 CYS SER TYR LEU VAL PHE TRP ALA ILE PHE ASN LEU VAL SEQRES 19 A 459 THR PHE VAL VAL MET VAL VAL LEU TYR ALA HIS ILE PHE SEQRES 20 A 459 GLY TYR VAL ALA ASP LEU GLU ASP ASN TRP GLU THR LEU SEQRES 21 A 459 ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA SEQRES 22 A 459 ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA SEQRES 23 A 459 ALA LEU ASP ALA GLN LYS GLY GLY SER GLY GLY SER ASP SEQRES 24 A 459 SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE SEQRES 25 A 459 LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN SEQRES 26 A 459 GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN SEQRES 27 A 459 LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SEQRES 28 A 459 ARG ASN ARG ASP THR MET MET SER LEU LEU LYS THR VAL SEQRES 29 A 459 VAL ILE VAL LEU GLY ALA PHE ILE ILE CYS TRP THR PRO SEQRES 30 A 459 GLY LEU VAL LEU LEU LEU LEU ASP CYS CYS CYS PRO GLN SEQRES 31 A 459 CYS ASP VAL LEU ALA TYR GLU LYS PHE PHE LEU LEU LEU SEQRES 32 A 459 ALA GLU PHE ASN SER ALA MET ASN PRO ILE ILE TYR SER SEQRES 33 A 459 TYR ARG ASP LYS GLU MET SER ALA THR PHE ARG GLN ILE SEQRES 34 A 459 LEU GLY ARG PRO LEU GLU VAL LEU PHE GLN GLY PRO HIS SEQRES 35 A 459 HIS HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP SEQRES 36 A 459 ASP ASP ASP LYS HET ON3 A2000 38 HET 1WV A2001 18 HETNAM ON3 1-(4-{[(2S,3R)-2-(2,3-DIHYDRO-1H-INDEN-2-YLOXY)-3-(3,5- HETNAM 2 ON3 DIMETHOXY-4-METHYLPHENYL)-3-HYDROXYPROPYL]OXY}PHENYL) HETNAM 3 ON3 CYCLOPROPANECARBOXYLIC ACID HETNAM 1WV (2S)-2,3-DIHYDROXYPROPYL (7Z)-TETRADEC-7-ENOATE HETSYN ON3 ONO-3080573 FORMUL 2 ON3 C31 H34 O7 FORMUL 3 1WV C17 H32 O4 FORMUL 4 HOH *3(H2 O) HELIX 1 AA1 SER A 29 SER A 37 1 9 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 ARG A 152 1 36 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 GLN A 1041 1 20 HELIX 12 AB3 PHE A 1061 GLY A 1082 1 22 HELIX 13 AB4 LYS A 1083 ASN A 1099 1 17 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 2.04 SSBOND 2 CYS A 188 CYS A 195 1555 1555 2.04 SSBOND 3 CYS A 204 CYS A 282 1555 1555 2.04 SSBOND 4 CYS A 284 CYS A 287 1555 1555 2.04 SITE 1 AC1 13 VAL A 52 THR A 109 GLN A 125 ILE A 128 SITE 2 AC1 13 ASP A 129 TRP A 210 TRP A 271 GLY A 274 SITE 3 AC1 13 LEU A 278 GLU A 293 LYS A 294 PHE A 296 SITE 4 AC1 13 LEU A 297 SITE 1 AC2 5 LEU A 51 LEU A 122 THR A 130 GLY A 179 SITE 2 AC2 5 SER A 183 CRYST1 34.350 111.930 153.960 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 0.029112 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008934 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006495 0.00000 ATOM 1 N GLN A 23 12.693 -31.022 68.655 1.00 93.87 N1+ ANISOU 1 N GLN A 23 9153 14922 11592 24 -393 1352 N1+ ATOM 2 CA GLN A 23 11.922 -30.429 67.567 1.00 92.89 C ANISOU 2 CA GLN A 23 9130 14662 11500 -8 -376 1274 C ATOM 3 C GLN A 23 12.678 -30.525 66.234 1.00 95.91 C ANISOU 3 C GLN A 23 9465 14935 12041 -207 -373 1252 C ATOM 4 O GLN A 23 12.077 -30.905 65.227 1.00 94.40 O ANISOU 4 O GLN A 23 9230 14673 11966 -229 -285 1264 O ATOM 5 CB GLN A 23 11.580 -28.965 67.880 1.00 95.05 C ANISOU 5 CB GLN A 23 9649 14879 11588 39 -496 1143 C ATOM 6 N CYS A 24 13.990 -30.188 66.235 1.00 93.02 N ANISOU 6 N CYS A 24 9107 14558 11678 -345 -473 1230 N ATOM 7 CA CYS A 24 14.860 -30.212 65.055 1.00 92.24 C ANISOU 7 CA CYS A 24 8963 14367 11716 -525 -476 1224 C ATOM 8 C CYS A 24 15.102 -31.669 64.610 1.00 96.53 C ANISOU 8 C CYS A 24 9295 14949 12433 -547 -334 1347 C ATOM 9 O CYS A 24 15.971 -32.361 65.149 1.00 96.48 O ANISOU 9 O CYS A 24 9160 15033 12465 -570 -321 1438 O ATOM 10 CB CYS A 24 16.169 -29.473 65.333 1.00 93.19 C ANISOU 10 CB CYS A 24 9136 14481 11790 -652 -625 1194 C ATOM 11 SG CYS A 24 17.335 -29.447 63.941 1.00 96.30 S ANISOU 11 SG CYS A 24 9467 14774 12350 -862 -629 1215 S ATOM 12 N PHE A 25 14.285 -32.117 63.628 1.00 92.99 N ANISOU 12 N PHE A 25 8819 14427 12086 -536 -230 1349 N ATOM 13 CA PHE A 25 14.258 -33.440 62.986 1.00 92.36 C ANISOU 13 CA PHE A 25 8575 14344 12173 -550 -94 1443 C ATOM 14 C PHE A 25 14.129 -34.592 64.011 1.00 97.20 C ANISOU 14 C PHE A 25 9032 15090 12810 -440 -15 1565 C ATOM 15 O PHE A 25 14.857 -35.588 63.939 1.00 96.66 O ANISOU 15 O PHE A 25 8815 15058 12853 -481 55 1660 O ATOM 16 CB PHE A 25 15.483 -33.662 62.080 1.00 93.92 C ANISOU 16 CB PHE A 25 8715 14486 12482 -702 -85 1465 C ATOM 17 CG PHE A 25 15.431 -32.903 60.777 1.00 94.94 C ANISOU 17 CG PHE A 25 8956 14477 12639 -797 -112 1374 C ATOM 18 CD1 PHE A 25 14.546 -33.277 59.770 1.00 97.16 C ANISOU 18 CD1 PHE A 25 9244 14675 12998 -781 -28 1354 C ATOM 19 CD2 PHE A 25 16.289 -31.838 60.540 1.00 97.53 C ANISOU 19 CD2 PHE A 25 9375 14759 12922 -905 -223 1317 C ATOM 20 CE1 PHE A 25 14.502 -32.578 58.562 1.00 97.61 C ANISOU 20 CE1 PHE A 25 9402 14612 13075 -863 -51 1273 C ATOM 21 CE2 PHE A 25 16.259 -31.152 59.324 1.00 99.89 C ANISOU 21 CE2 PHE A 25 9765 14935 13253 -987 -241 1244 C ATOM 22 CZ PHE A 25 15.362 -31.525 58.346 1.00 97.07 C ANISOU 22 CZ PHE A 25 9416 14504 12961 -961 -151 1221 C ATOM 23 N TYR A 26 13.164 -34.460 64.934 1.00 94.62 N ANISOU 23 N TYR A 26 8736 14833 12381 -291 -16 1572 N ATOM 24 CA TYR A 26 12.855 -35.477 65.940 1.00 94.92 C ANISOU 24 CA TYR A 26 8630 15001 12435 -162 62 1694 C ATOM 25 C TYR A 26 11.893 -36.503 65.339 1.00 98.44 C ANISOU 25 C TYR A 26 8969 15409 13026 -116 187 1766 C ATOM 26 O TYR A 26 11.259 -36.212 64.319 1.00 97.31 O ANISOU 26 O TYR A 26 8899 15150 12925 -156 195 1704 O ATOM 27 CB TYR A 26 12.244 -34.817 67.190 1.00 97.01 C ANISOU 27 CB TYR A 26 8986 15358 12516 -9 4 1676 C ATOM 28 CG TYR A 26 12.987 -35.105 68.477 1.00 99.69 C ANISOU 28 CG TYR A 26 9253 15845 12779 45 -25 1744 C ATOM 29 CD1 TYR A 26 12.704 -36.242 69.229 1.00101.80 C ANISOU 29 CD1 TYR A 26 9348 16233 13097 163 77 1882 C ATOM 30 CD2 TYR A 26 13.936 -34.215 68.971 1.00101.33 C ANISOU 30 CD2 TYR A 26 9567 16071 12862 -18 -162 1673 C ATOM 31 CE1 TYR A 26 13.372 -36.503 70.424 1.00103.57 C ANISOU 31 CE1 TYR A 26 9504 16602 13246 219 52 1949 C ATOM 32 CE2 TYR A 26 14.609 -34.465 70.166 1.00103.22 C ANISOU 32 CE2 TYR A 26 9745 16450 13024 30 -199 1736 C ATOM 33 CZ TYR A 26 14.324 -35.611 70.890 1.00110.77 C ANISOU 33 CZ TYR A 26 10527 17534 14027 152 -88 1873 C ATOM 34 OH TYR A 26 14.985 -35.861 72.068 1.00112.85 O ANISOU 34 OH TYR A 26 10726 17943 14210 203 -123 1939 O ATOM 35 N ASN A 27 11.756 -37.690 65.965 1.00 95.56 N ANISOU 35 N ASN A 27 8432 15138 12738 -33 279 1898 N ATOM 36 CA ASN A 27 10.831 -38.717 65.476 1.00 95.00 C ANISOU 36 CA ASN A 27 8252 15028 12814 10 386 1979 C ATOM 37 C ASN A 27 9.408 -38.395 65.995 1.00 99.21 C ANISOU 37 C ASN A 27 8827 15595 13272 165 391 1999 C ATOM 38 O ASN A 27 8.758 -39.222 66.643 1.00 99.04 O ANISOU 38 O ASN A 27 8676 15655 13301 285 464 2125 O ATOM 39 CB ASN A 27 11.300 -40.127 65.881 1.00 96.66 C ANISOU 39 CB ASN A 27 8257 15314 13155 29 483 2120 C ATOM 40 CG ASN A 27 10.634 -41.261 65.124 1.00122.58 C ANISOU 40 CG ASN A 27 11433 18519 16623 25 581 2192 C ATOM 41 OD1 ASN A 27 10.299 -41.156 63.936 1.00116.88 O ANISOU 41 OD1 ASN A 27 10781 17659 15968 -57 578 2124 O ATOM 42 ND2 ASN A 27 10.475 -42.396 65.788 1.00115.68 N ANISOU 42 ND2 ASN A 27 10385 17727 15839 107 665 2332 N ATOM 43 N GLU A 28 8.945 -37.163 65.702 1.00 95.83 N ANISOU 43 N GLU A 28 8580 15105 12725 164 315 1884 N ATOM 44 CA GLU A 28 7.639 -36.634 66.095 1.00 95.97 C ANISOU 44 CA GLU A 28 8669 15143 12651 307 315 1893 C ATOM 45 C GLU A 28 6.606 -36.868 65.005 1.00 98.82 C ANISOU 45 C GLU A 28 9025 15393 13128 280 358 1902 C ATOM 46 O GLU A 28 6.915 -36.729 63.818 1.00 97.71 O ANISOU 46 O GLU A 28 8935 15130 13060 137 340 1820 O ATOM 47 CB GLU A 28 7.728 -35.127 66.411 1.00 97.92 C ANISOU 47 CB GLU A 28 9128 15381 12696 327 207 1764 C ATOM 48 CG GLU A 28 8.505 -34.776 67.672 1.00109.94 C ANISOU 48 CG GLU A 28 10682 17021 14069 387 145 1757 C ATOM 49 CD GLU A 28 7.896 -35.176 69.005 1.00132.85 C ANISOU 49 CD GLU A 28 13513 20073 16890 593 193 1872 C ATOM 50 OE1 GLU A 28 8.675 -35.412 69.956 1.00129.96 O ANISOU 50 OE1 GLU A 28 13097 19818 16464 624 171 1907 O ATOM 51 OE2 GLU A 28 6.649 -35.248 69.105 1.00126.84 O1- ANISOU 51 OE2 GLU A 28 12743 19324 16125 726 252 1936 O1- ATOM 52 N SER A 29 5.370 -37.195 65.415 1.00 95.35 N ANISOU 52 N SER A 29 8525 15000 12703 421 411 2008 N ATOM 53 CA SER A 29 4.246 -37.421 64.507 1.00 94.50 C ANISOU 53 CA SER A 29 8403 14800 12704 410 443 2039 C ATOM 54 C SER A 29 3.737 -36.083 63.950 1.00 97.73 C ANISOU 54 C SER A 29 9006 15130 12996 395 381 1920 C ATOM 55 O SER A 29 4.173 -35.020 64.404 1.00 97.50 O ANISOU 55 O SER A 29 9120 15124 12802 416 316 1823 O ATOM 56 CB SER A 29 3.127 -38.172 65.226 1.00 98.63 C ANISOU 56 CB SER A 29 8785 15409 13281 571 516 2216 C ATOM 57 OG SER A 29 2.065 -38.494 64.343 1.00107.29 O ANISOU 57 OG SER A 29 9848 16414 14502 545 537 2265 O ATOM 58 N ILE A 30 2.807 -36.135 62.973 1.00 93.66 N ANISOU 58 N ILE A 30 8499 14519 12569 359 394 1929 N ATOM 59 CA ILE A 30 2.223 -34.949 62.345 1.00 93.23 C ANISOU 59 CA ILE A 30 8611 14387 12424 345 347 1832 C ATOM 60 C ILE A 30 1.374 -34.178 63.387 1.00 97.67 C ANISOU 60 C ILE A 30 9246 15042 12824 536 350 1877 C ATOM 61 O ILE A 30 1.245 -32.958 63.275 1.00 97.37 O ANISOU 61 O ILE A 30 9380 14966 12648 549 300 1774 O ATOM 62 CB ILE A 30 1.419 -35.349 61.067 1.00 95.68 C ANISOU 62 CB ILE A 30 8890 14583 12880 261 364 1852 C ATOM 63 CG1 ILE A 30 1.938 -34.624 59.813 1.00 95.44 C ANISOU 63 CG1 ILE A 30 8995 14424 12842 102 309 1694 C ATOM 64 CG2 ILE A 30 -0.105 -35.237 61.209 1.00 96.79 C ANISOU 64 CG2 ILE A 30 9010 14745 13020 385 392 1963 C ATOM 65 CD1 ILE A 30 3.290 -35.119 59.299 1.00102.34 C ANISOU 65 CD1 ILE A 30 9840 15252 13791 -40 301 1629 C ATOM 66 N ALA A 31 0.864 -34.887 64.420 1.00 94.73 N ANISOU 66 N ALA A 31 8742 14788 12461 691 411 2033 N ATOM 67 CA ALA A 31 0.062 -34.340 65.515 1.00 95.46 C ANISOU 67 CA ALA A 31 8881 14987 12402 903 433 2107 C ATOM 68 C ALA A 31 0.832 -33.282 66.318 1.00 99.81 C ANISOU 68 C ALA A 31 9602 15582 12737 953 368 1984 C ATOM 69 O ALA A 31 0.212 -32.350 66.821 1.00100.02 O ANISOU 69 O ALA A 31 9764 15638 12602 1092 359 1970 O ATOM 70 CB ALA A 31 -0.387 -35.460 66.439 1.00 96.75 C ANISOU 70 CB ALA A 31 8846 15274 12639 1044 514 2304 C ATOM 71 N PHE A 32 2.172 -33.421 66.420 1.00 96.21 N ANISOU 71 N PHE A 32 9146 15129 12281 839 320 1899 N ATOM 72 CA PHE A 32 3.058 -32.496 67.136 1.00 96.69 C ANISOU 72 CA PHE A 32 9360 15222 12157 852 235 1781 C ATOM 73 C PHE A 32 3.107 -31.124 66.440 1.00100.55 C ANISOU 73 C PHE A 32 10068 15592 12546 774 152 1617 C ATOM 74 O PHE A 32 3.029 -30.098 67.118 1.00100.90 O ANISOU 74 O PHE A 32 10281 15656 12400 874 98 1550 O ATOM 75 CB PHE A 32 4.477 -33.096 67.251 1.00 98.27 C ANISOU 75 CB PHE A 32 9474 15446 12419 723 205 1756 C ATOM 76 CG PHE A 32 5.521 -32.208 67.892 1.00100.48 C ANISOU 76 CG PHE A 32 9897 15747 12532 699 98 1638 C ATOM 77 CD1 PHE A 32 5.600 -32.085 69.275 1.00104.65 C ANISOU 77 CD1 PHE A 32 10450 16406 12905 858 82 1675 C ATOM 78 CD2 PHE A 32 6.450 -31.525 67.115 1.00102.20 C ANISOU 78 CD2 PHE A 32 10220 15858 12754 516 8 1500 C ATOM 79 CE1 PHE A 32 6.569 -31.269 69.867 1.00106.34 C ANISOU 79 CE1 PHE A 32 10805 16633 12966 826 -36 1564 C ATOM 80 CE2 PHE A 32 7.417 -30.709 67.708 1.00105.80 C ANISOU 80 CE2 PHE A 32 10802 16327 13069 482 -106 1402 C ATOM 81 CZ PHE A 32 7.472 -30.588 69.080 1.00105.05 C ANISOU 81 CZ PHE A 32 10742 16355 12819 632 -134 1430 C ATOM 82 N PHE A 33 3.242 -31.114 65.101 1.00 96.34 N ANISOU 82 N PHE A 33 9535 14933 12138 601 142 1554 N ATOM 83 CA PHE A 33 3.325 -29.895 64.293 1.00 96.05 C ANISOU 83 CA PHE A 33 9682 14777 12037 509 70 1408 C ATOM 84 C PHE A 33 1.951 -29.232 64.129 1.00100.21 C ANISOU 84 C PHE A 33 10299 15278 12498 628 102 1431 C ATOM 85 O PHE A 33 1.859 -28.006 64.213 1.00100.27 O ANISOU 85 O PHE A 33 10497 15242 12359 660 45 1330 O ATOM 86 CB PHE A 33 3.928 -30.200 62.909 1.00 96.83 C ANISOU 86 CB PHE A 33 9735 14762 12294 299 61 1352 C ATOM 87 CG PHE A 33 5.311 -30.807 62.932 1.00 98.31 C ANISOU 87 CG PHE A 33 9837 14965 12553 176 38 1338 C ATOM 88 CD1 PHE A 33 6.441 -30.001 63.009 1.00101.80 C ANISOU 88 CD1 PHE A 33 10386 15377 12915 83 -59 1227 C ATOM 89 CD2 PHE A 33 5.485 -32.184 62.851 1.00100.18 C ANISOU 89 CD2 PHE A 33 9882 15239 12944 152 111 1444 C ATOM 90 CE1 PHE A 33 7.721 -30.564 63.028 1.00102.68 C ANISOU 90 CE1 PHE A 33 10408 15510 13097 -28 -77 1236 C ATOM 91 CE2 PHE A 33 6.765 -32.746 62.869 1.00102.96 C ANISOU 91 CE2 PHE A 33 10152 15607 13360 47 101 1444 C ATOM 92 CZ PHE A 33 7.874 -31.932 62.958 1.00101.37 C ANISOU 92 CZ PHE A 33 10052 15387 13076 -41 9 1345 C ATOM 93 N TYR A 34 0.897 -30.038 63.883 1.00 96.51 N ANISOU 93 N TYR A 34 9694 14831 12143 689 190 1569 N ATOM 94 CA TYR A 34 -0.478 -29.577 63.673 1.00 96.50 C ANISOU 94 CA TYR A 34 9741 14815 12109 799 232 1628 C ATOM 95 C TYR A 34 -1.118 -29.006 64.952 1.00101.69 C ANISOU 95 C TYR A 34 10483 15575 12579 1035 255 1686 C ATOM 96 O TYR A 34 -1.987 -28.141 64.840 1.00101.57 O ANISOU 96 O TYR A 34 10589 15532 12472 1126 266 1682 O ATOM 97 CB TYR A 34 -1.349 -30.722 63.127 1.00 97.16 C ANISOU 97 CB TYR A 34 9634 14900 12384 790 307 1781 C ATOM 98 CG TYR A 34 -1.341 -30.833 61.617 1.00 97.87 C ANISOU 98 CG TYR A 34 9715 14858 12612 602 288 1719 C ATOM 99 CD1 TYR A 34 -0.295 -31.463 60.948 1.00 99.11 C ANISOU 99 CD1 TYR A 34 9813 14958 12888 427 263 1654 C ATOM 100 CD2 TYR A 34 -2.399 -30.343 60.857 1.00 98.44 C ANISOU 100 CD2 TYR A 34 9838 14869 12697 607 298 1738 C ATOM 101 CE1 TYR A 34 -0.285 -31.571 59.558 1.00 98.98 C ANISOU 101 CE1 TYR A 34 9800 14822 12985 270 248 1597 C ATOM 102 CE2 TYR A 34 -2.402 -30.449 59.467 1.00 98.47 C ANISOU 102 CE2 TYR A 34 9838 14756 12818 440 276 1680 C ATOM 103 CZ TYR A 34 -1.343 -31.065 58.821 1.00104.95 C ANISOU 103 CZ TYR A 34 10612 15520 13746 276 251 1606 C ATOM 104 OH TYR A 34 -1.342 -31.174 57.451 1.00104.89 O ANISOU 104 OH TYR A 34 10613 15399 13841 126 232 1549 O ATOM 105 N ASN A 35 -0.706 -29.479 66.149 1.00 99.12 N ANISOU 105 N ASN A 35 10100 15369 12194 1144 266 1743 N ATOM 106 CA ASN A 35 -1.256 -29.002 67.424 1.00100.34 C ANISOU 106 CA ASN A 35 10338 15630 12158 1387 291 1802 C ATOM 107 C ASN A 35 -0.640 -27.658 67.834 1.00104.97 C ANISOU 107 C ASN A 35 11177 16177 12528 1403 193 1626 C ATOM 108 O ASN A 35 -1.351 -26.823 68.399 1.00105.51 O ANISOU 108 O ASN A 35 11396 16268 12426 1582 206 1630 O ATOM 109 CB ASN A 35 -1.050 -30.033 68.539 1.00102.39 C ANISOU 109 CB ASN A 35 10436 16036 12430 1502 340 1934 C ATOM 110 CG ASN A 35 -1.727 -29.698 69.847 1.00130.28 C ANISOU 110 CG ASN A 35 14032 19694 15776 1778 385 2025 C ATOM 111 OD1 ASN A 35 -1.074 -29.361 70.840 1.00126.42 O ANISOU 111 OD1 ASN A 35 13638 19272 15124 1859 338 1965 O ATOM 112 ND2 ASN A 35 -3.051 -29.790 69.883 1.00123.07 N ANISOU 112 ND2 ASN A 35 13066 18816 14880 1933 475 2180 N ATOM 113 N ARG A 36 0.672 -27.458 67.568 1.00101.22 N ANISOU 113 N ARG A 36 10752 15643 12063 1221 95 1482 N ATOM 114 CA ARG A 36 1.406 -26.229 67.899 1.00101.80 C ANISOU 114 CA ARG A 36 11057 15664 11959 1198 -22 1312 C ATOM 115 C ARG A 36 0.831 -25.017 67.156 1.00105.60 C ANISOU 115 C ARG A 36 11725 16023 12377 1183 -47 1216 C ATOM 116 O ARG A 36 0.659 -23.959 67.764 1.00106.25 O ANISOU 116 O ARG A 36 12015 16091 12263 1303 -94 1142 O ATOM 117 CB ARG A 36 2.901 -26.378 67.585 1.00101.71 C ANISOU 117 CB ARG A 36 11019 15609 12017 981 -118 1210 C ATOM 118 CG ARG A 36 3.679 -27.126 68.662 1.00112.88 C ANISOU 118 CG ARG A 36 12334 17150 13407 1022 -131 1264 C ATOM 119 CD ARG A 36 5.178 -27.103 68.415 1.00122.68 C ANISOU 119 CD ARG A 36 13570 18348 14696 815 -235 1168 C ATOM 120 NE ARG A 36 5.733 -25.746 68.456 1.00132.19 N ANISOU 120 NE ARG A 36 15008 19463 15757 758 -373 1006 N ATOM 121 CZ ARG A 36 6.210 -25.157 69.549 1.00148.32 C ANISOU 121 CZ ARG A 36 17189 21549 17616 835 -471 945 C ATOM 122 NH1 ARG A 36 6.691 -23.923 69.487 1.00136.59 N ANISOU 122 NH1 ARG A 36 15919 19961 16018 767 -606 797 N ATOM 123 NH2 ARG A 36 6.209 -25.797 70.712 1.00136.32 N1+ ANISOU 123 NH2 ARG A 36 15596 20174 16024 981 -440 1034 N1+ ATOM 124 N SER A 37 0.523 -25.181 65.856 1.00101.04 N ANISOU 124 N SER A 37 11076 15355 11959 1044 -16 1220 N ATOM 125 CA SER A 37 -0.070 -24.140 65.017 1.00100.69 C ANISOU 125 CA SER A 37 11177 15198 11882 1019 -27 1147 C ATOM 126 C SER A 37 -1.598 -24.212 65.084 1.00104.85 C ANISOU 126 C SER A 37 11673 15770 12395 1199 83 1288 C ATOM 127 O SER A 37 -2.148 -25.247 65.467 1.00104.30 O ANISOU 127 O SER A 37 11427 15800 12402 1291 167 1450 O ATOM 128 CB SER A 37 0.408 -24.282 63.574 1.00102.88 C ANISOU 128 CB SER A 37 11394 15365 12333 781 -51 1083 C ATOM 129 OG SER A 37 1.816 -24.142 63.476 1.00111.44 O ANISOU 129 OG SER A 37 12505 16406 13430 619 -149 968 O ATOM 130 N GLY A 38 -2.266 -23.121 64.711 1.00101.88 N ANISOU 130 N GLY A 38 11460 15321 11930 1247 83 1239 N ATOM 131 CA GLY A 38 -3.724 -23.041 64.698 1.00102.05 C ANISOU 131 CA GLY A 38 11465 15377 11933 1415 186 1379 C ATOM 132 C GLY A 38 -4.321 -23.789 63.523 1.00104.80 C ANISOU 132 C GLY A 38 11634 15694 12493 1297 240 1473 C ATOM 133 O GLY A 38 -4.898 -23.173 62.623 1.00104.00 O ANISOU 133 O GLY A 38 11594 15511 12412 1251 249 1451 O ATOM 134 N LYS A 39 -4.173 -25.129 63.525 1.00100.84 N ANISOU 134 N LYS A 39 10914 15252 12150 1245 272 1578 N ATOM 135 CA LYS A 39 -4.651 -26.012 62.462 1.00 99.65 C ANISOU 135 CA LYS A 39 10585 15066 12209 1124 310 1668 C ATOM 136 C LYS A 39 -5.355 -27.243 63.047 1.00103.98 C ANISOU 136 C LYS A 39 10923 15728 12858 1239 390 1881 C ATOM 137 O LYS A 39 -4.912 -27.797 64.055 1.00103.99 O ANISOU 137 O LYS A 39 10861 15824 12829 1321 402 1925 O ATOM 138 CB LYS A 39 -3.475 -26.439 61.560 1.00100.99 C ANISOU 138 CB LYS A 39 10709 15153 12511 879 245 1545 C ATOM 139 CG LYS A 39 -3.862 -27.058 60.212 1.00113.55 C ANISOU 139 CG LYS A 39 12185 16668 14292 728 259 1581 C ATOM 140 CD LYS A 39 -4.444 -26.048 59.216 1.00122.98 C ANISOU 140 CD LYS A 39 13502 17767 15458 681 246 1519 C ATOM 141 CE LYS A 39 -4.692 -26.641 57.850 1.00132.47 C ANISOU 141 CE LYS A 39 14606 18891 16837 520 245 1534 C ATOM 142 NZ LYS A 39 -5.781 -27.656 57.854 1.00141.39 N1+ ANISOU 142 NZ LYS A 39 15562 20070 18090 580 303 1726 N1+ ATOM 143 N HIS A 40 -6.451 -27.661 62.391 1.00100.47 N ANISOU 143 N HIS A 40 10366 15270 12537 1239 441 2018 N ATOM 144 CA HIS A 40 -7.285 -28.803 62.769 1.00100.63 C ANISOU 144 CA HIS A 40 10174 15379 12683 1333 511 2243 C ATOM 145 C HIS A 40 -6.726 -30.125 62.229 1.00103.38 C ANISOU 145 C HIS A 40 10341 15698 13243 1161 492 2260 C ATOM 146 O HIS A 40 -6.162 -30.159 61.133 1.00101.99 O ANISOU 146 O HIS A 40 10188 15411 13152 960 438 2135 O ATOM 147 CB HIS A 40 -8.723 -28.602 62.256 1.00101.69 C ANISOU 147 CB HIS A 40 10274 15503 12862 1398 559 2390 C ATOM 148 CG HIS A 40 -8.811 -28.314 60.787 1.00104.26 C ANISOU 148 CG HIS A 40 10637 15697 13279 1202 512 2298 C ATOM 149 ND1 HIS A 40 -8.762 -27.018 60.303 1.00105.96 N ANISOU 149 ND1 HIS A 40 11051 15840 13369 1178 484 2158 N ATOM 150 CD2 HIS A 40 -8.930 -29.166 59.742 1.00105.29 C ANISOU 150 CD2 HIS A 40 10637 15759 13607 1031 486 2328 C ATOM 151 CE1 HIS A 40 -8.858 -27.122 58.987 1.00104.53 C ANISOU 151 CE1 HIS A 40 10845 15559 13313 998 448 2113 C ATOM 152 NE2 HIS A 40 -8.960 -28.395 58.603 1.00104.47 N ANISOU 152 NE2 HIS A 40 10650 15549 13496 905 445 2207 N ATOM 153 N LEU A 41 -6.911 -31.212 63.000 1.00100.19 N ANISOU 153 N LEU A 41 9756 15391 12921 1250 541 2423 N ATOM 154 CA LEU A 41 -6.488 -32.566 62.640 1.00 99.36 C ANISOU 154 CA LEU A 41 9467 15266 13020 1118 536 2469 C ATOM 155 C LEU A 41 -7.559 -33.562 63.095 1.00103.64 C ANISOU 155 C LEU A 41 9801 15887 13689 1237 601 2725 C ATOM 156 O LEU A 41 -7.843 -33.664 64.292 1.00104.03 O ANISOU 156 O LEU A 41 9799 16064 13662 1435 659 2851 O ATOM 157 CB LEU A 41 -5.107 -32.900 63.247 1.00 99.32 C ANISOU 157 CB LEU A 41 9461 15297 12979 1078 514 2369 C ATOM 158 CG LEU A 41 -4.419 -34.182 62.751 1.00103.34 C ANISOU 158 CG LEU A 41 9816 15764 13685 918 506 2374 C ATOM 159 CD1 LEU A 41 -3.791 -33.984 61.373 1.00102.51 C ANISOU 159 CD1 LEU A 41 9792 15513 13644 696 444 2206 C ATOM 160 CD2 LEU A 41 -3.346 -34.624 63.720 1.00106.04 C ANISOU 160 CD2 LEU A 41 10111 16191 13986 951 514 2356 C ATOM 161 N ALA A 42 -8.173 -34.266 62.129 1.00 99.78 N ANISOU 161 N ALA A 42 9196 15322 13395 1120 587 2806 N ATOM 162 CA ALA A 42 -9.242 -35.234 62.373 1.00100.19 C ANISOU 162 CA ALA A 42 9040 15424 13603 1199 630 3059 C ATOM 163 C ALA A 42 -8.696 -36.644 62.618 1.00103.77 C ANISOU 163 C ALA A 42 9310 15891 14225 1140 637 3125 C ATOM 164 O ALA A 42 -7.629 -36.998 62.111 1.00102.58 O ANISOU 164 O ALA A 42 9186 15667 14123 979 596 2971 O ATOM 165 CB ALA A 42 -10.203 -35.253 61.194 1.00100.72 C ANISOU 165 CB ALA A 42 9082 15393 13795 1093 594 3115 C ATOM 166 N THR A 43 -9.448 -37.444 63.396 1.00101.04 N ANISOU 166 N THR A 43 8775 15642 13973 1279 693 3366 N ATOM 167 CA THR A 43 -9.124 -38.834 63.740 1.00100.91 C ANISOU 167 CA THR A 43 8560 15649 14132 1252 711 3473 C ATOM 168 C THR A 43 -10.219 -39.780 63.224 1.00104.81 C ANISOU 168 C THR A 43 8869 16094 14861 1208 698 3682 C ATOM 169 O THR A 43 -9.942 -40.952 62.960 1.00104.25 O ANISOU 169 O THR A 43 8662 15968 14979 1101 679 3723 O ATOM 170 CB THR A 43 -8.932 -38.994 65.258 1.00110.23 C ANISOU 170 CB THR A 43 9668 16999 15216 1465 789 3584 C ATOM 171 OG1 THR A 43 -10.091 -38.512 65.940 1.00110.95 O ANISOU 171 OG1 THR A 43 9736 17194 15227 1682 847 3771 O ATOM 172 CG2 THR A 43 -7.685 -38.282 65.774 1.00108.77 C ANISOU 172 CG2 THR A 43 9648 16852 14827 1477 781 3376 C ATOM 173 N GLU A 44 -11.456 -39.263 63.084 1.00101.65 N ANISOU 173 N GLU A 44 8465 15709 14449 1291 705 3818 N ATOM 174 CA GLU A 44 -12.631 -40.002 62.613 1.00101.88 C ANISOU 174 CA GLU A 44 8322 15697 14690 1257 681 4039 C ATOM 175 C GLU A 44 -12.922 -39.689 61.133 1.00104.52 C ANISOU 175 C GLU A 44 8754 15875 15084 1057 590 3926 C ATOM 176 O GLU A 44 -12.500 -38.642 60.631 1.00103.35 O ANISOU 176 O GLU A 44 8807 15682 14778 1006 570 3721 O ATOM 177 CB GLU A 44 -13.866 -39.678 63.493 1.00104.50 C ANISOU 177 CB GLU A 44 8563 16166 14978 1496 756 4306 C ATOM 178 CG GLU A 44 -14.495 -38.293 63.319 1.00115.53 C ANISOU 178 CG GLU A 44 10126 17580 16191 1584 772 4275 C ATOM 179 CD GLU A 44 -13.672 -37.072 63.694 1.00135.96 C ANISOU 179 CD GLU A 44 12952 20199 18506 1653 796 4044 C ATOM 180 OE1 GLU A 44 -12.995 -37.100 64.747 1.00131.99 O ANISOU 180 OE1 GLU A 44 12461 19796 17892 1777 846 4017 O ATOM 181 OE2 GLU A 44 -13.743 -36.066 62.952 1.00128.97 O1- ANISOU 181 OE2 GLU A 44 12242 19242 17519 1586 762 3901 O1- ATOM 182 N TRP A 45 -13.649 -40.592 60.444 1.00100.96 N ANISOU 182 N TRP A 45 8162 15340 14860 946 531 4065 N ATOM 183 CA TRP A 45 -14.032 -40.391 59.047 1.00100.12 C ANISOU 183 CA TRP A 45 8133 15089 14819 762 436 3982 C ATOM 184 C TRP A 45 -15.249 -39.467 58.988 1.00103.56 C ANISOU 184 C TRP A 45 8591 15573 15183 863 451 4117 C ATOM 185 O TRP A 45 -16.376 -39.878 59.282 1.00104.09 O ANISOU 185 O TRP A 45 8489 15689 15370 945 460 4388 O ATOM 186 CB TRP A 45 -14.288 -41.721 58.318 1.00 99.16 C ANISOU 186 CB TRP A 45 7869 14846 14961 596 351 4064 C ATOM 187 CG TRP A 45 -13.097 -42.218 57.554 1.00 99.26 C ANISOU 187 CG TRP A 45 7972 14730 15011 411 299 3827 C ATOM 188 CD1 TRP A 45 -12.266 -43.240 57.905 1.00102.10 C ANISOU 188 CD1 TRP A 45 8252 15077 15465 380 315 3806 C ATOM 189 CD2 TRP A 45 -12.577 -41.677 56.332 1.00 98.22 C ANISOU 189 CD2 TRP A 45 8031 14475 14814 246 235 3584 C ATOM 190 NE1 TRP A 45 -11.273 -43.387 56.964 1.00100.74 N ANISOU 190 NE1 TRP A 45 8210 14775 15290 209 267 3570 N ATOM 191 CE2 TRP A 45 -11.436 -42.436 55.990 1.00101.63 C ANISOU 191 CE2 TRP A 45 8490 14821 15305 127 217 3431 C ATOM 192 CE3 TRP A 45 -12.962 -40.618 55.491 1.00 99.14 C ANISOU 192 CE3 TRP A 45 8295 14547 14826 196 197 3488 C ATOM 193 CZ2 TRP A 45 -10.681 -42.176 54.840 1.00100.13 C ANISOU 193 CZ2 TRP A 45 8469 14506 15071 -33 164 3193 C ATOM 194 CZ3 TRP A 45 -12.215 -40.363 54.351 1.00 99.76 C ANISOU 194 CZ3 TRP A 45 8536 14503 14866 32 140 3249 C ATOM 195 CH2 TRP A 45 -11.089 -41.135 54.036 1.00 99.93 C ANISOU 195 CH2 TRP A 45 8581 14443 14945 -77 125 3106 C ATOM 196 N ASN A 46 -14.992 -38.197 58.648 1.00 98.81 N ANISOU 196 N ASN A 46 8197 14962 14385 866 458 3935 N ATOM 197 CA ASN A 46 -15.980 -37.124 58.566 1.00 98.62 C ANISOU 197 CA ASN A 46 8237 14980 14253 967 484 4020 C ATOM 198 C ASN A 46 -16.855 -37.262 57.304 1.00101.21 C ANISOU 198 C ASN A 46 8534 15199 14723 808 393 4081 C ATOM 199 O ASN A 46 -16.473 -37.963 56.365 1.00100.19 O ANISOU 199 O ASN A 46 8399 14943 14728 605 302 3977 O ATOM 200 CB ASN A 46 -15.255 -35.781 58.575 1.00 99.08 C ANISOU 200 CB ASN A 46 8537 15045 14065 1000 513 3780 C ATOM 201 CG ASN A 46 -16.081 -34.650 59.105 1.00123.57 C ANISOU 201 CG ASN A 46 11709 18241 17001 1199 587 3882 C ATOM 202 OD1 ASN A 46 -16.984 -34.147 58.435 1.00118.43 O ANISOU 202 OD1 ASN A 46 11076 17559 16362 1178 569 3955 O ATOM 203 ND2 ASN A 46 -15.773 -34.216 60.317 1.00116.24 N ANISOU 203 ND2 ASN A 46 10830 17428 15907 1399 670 3888 N ATOM 204 N THR A 47 -18.028 -36.596 57.295 1.00 97.60 N ANISOU 204 N THR A 47 8059 14794 14232 908 418 4253 N ATOM 205 CA THR A 47 -18.988 -36.628 56.185 1.00 97.28 C ANISOU 205 CA THR A 47 7979 14670 14312 778 334 4344 C ATOM 206 C THR A 47 -18.466 -35.791 54.997 1.00 99.14 C ANISOU 206 C THR A 47 8427 14794 14446 619 277 4069 C ATOM 207 O THR A 47 -18.557 -36.252 53.857 1.00 98.44 O ANISOU 207 O THR A 47 8334 14584 14485 421 171 4016 O ATOM 208 CB THR A 47 -20.375 -36.144 56.657 1.00106.30 C ANISOU 208 CB THR A 47 9028 15922 15441 957 395 4637 C ATOM 209 OG1 THR A 47 -20.729 -36.824 57.864 1.00106.86 O ANISOU 209 OG1 THR A 47 8914 16111 15579 1134 466 4882 O ATOM 210 CG2 THR A 47 -21.469 -36.364 55.612 1.00105.14 C ANISOU 210 CG2 THR A 47 8792 15700 15455 823 299 4788 C ATOM 211 N VAL A 48 -17.926 -34.577 55.258 1.00 94.43 N ANISOU 211 N VAL A 48 8020 14237 13623 706 343 3899 N ATOM 212 CA VAL A 48 -17.398 -33.693 54.206 1.00 92.95 C ANISOU 212 CA VAL A 48 8031 13954 13331 573 300 3647 C ATOM 213 C VAL A 48 -16.055 -34.233 53.672 1.00 94.93 C ANISOU 213 C VAL A 48 8351 14103 13616 400 242 3398 C ATOM 214 O VAL A 48 -15.733 -33.981 52.509 1.00 93.84 O ANISOU 214 O VAL A 48 8320 13858 13479 237 175 3231 O ATOM 215 CB VAL A 48 -17.263 -32.199 54.622 1.00 96.75 C ANISOU 215 CB VAL A 48 8695 14496 13571 716 381 3550 C ATOM 216 CG1 VAL A 48 -18.628 -31.547 54.809 1.00 97.47 C ANISOU 216 CG1 VAL A 48 8748 14661 13624 861 435 3776 C ATOM 217 CG2 VAL A 48 -16.383 -32.012 55.859 1.00 96.58 C ANISOU 217 CG2 VAL A 48 8730 14556 13410 861 455 3471 C ATOM 218 N SER A 49 -15.287 -34.970 54.511 1.00 90.72 N ANISOU 218 N SER A 49 7754 13608 13108 442 271 3385 N ATOM 219 CA SER A 49 -13.993 -35.553 54.139 1.00 89.36 C ANISOU 219 CA SER A 49 7629 13353 12971 300 232 3179 C ATOM 220 C SER A 49 -14.166 -36.651 53.085 1.00 92.19 C ANISOU 220 C SER A 49 7907 13586 13534 112 133 3193 C ATOM 221 O SER A 49 -13.304 -36.802 52.221 1.00 91.00 O ANISOU 221 O SER A 49 7855 13331 13392 -38 84 2994 O ATOM 222 CB SER A 49 -13.271 -36.109 55.362 1.00 93.15 C ANISOU 222 CB SER A 49 8038 13918 13438 406 293 3201 C ATOM 223 OG SER A 49 -13.908 -37.268 55.875 1.00103.07 O ANISOU 223 OG SER A 49 9083 15212 14868 451 297 3433 O ATOM 224 N LYS A 50 -15.280 -37.408 53.161 1.00 88.86 N ANISOU 224 N LYS A 50 7312 13173 13277 126 102 3436 N ATOM 225 CA LYS A 50 -15.617 -38.480 52.221 1.00 88.57 C ANISOU 225 CA LYS A 50 7195 13013 13446 -46 -7 3479 C ATOM 226 C LYS A 50 -16.034 -37.906 50.866 1.00 91.06 C ANISOU 226 C LYS A 50 7623 13231 13743 -181 -89 3390 C ATOM 227 O LYS A 50 -15.703 -38.491 49.833 1.00 90.30 O ANISOU 227 O LYS A 50 7571 13003 13734 -352 -181 3274 O ATOM 228 CB LYS A 50 -16.740 -39.370 52.782 1.00 92.41 C ANISOU 228 CB LYS A 50 7454 13544 14114 16 -22 3788 C ATOM 229 CG LYS A 50 -16.310 -40.274 53.930 1.00108.45 C ANISOU 229 CG LYS A 50 9346 15644 16217 113 38 3883 C ATOM 230 CD LYS A 50 -17.491 -41.032 54.517 1.00120.66 C ANISOU 230 CD LYS A 50 10659 17246 17940 192 30 4213 C ATOM 231 CE LYS A 50 -17.087 -41.882 55.694 1.00133.02 C ANISOU 231 CE LYS A 50 12079 18892 19571 303 100 4320 C ATOM 232 NZ LYS A 50 -18.253 -42.587 56.289 1.00143.83 N1+ ANISOU 232 NZ LYS A 50 13208 20322 21117 391 98 4662 N1+ ATOM 233 N LEU A 51 -16.757 -36.765 50.870 1.00 87.03 N ANISOU 233 N LEU A 51 7165 12785 13116 -97 -54 3446 N ATOM 234 CA LEU A 51 -17.237 -36.116 49.650 1.00 86.38 C ANISOU 234 CA LEU A 51 7182 12631 13007 -207 -120 3383 C ATOM 235 C LEU A 51 -16.120 -35.328 48.952 1.00 88.46 C ANISOU 235 C LEU A 51 7656 12835 13120 -285 -115 3084 C ATOM 236 O LEU A 51 -16.086 -35.323 47.722 1.00 87.73 O ANISOU 236 O LEU A 51 7642 12637 13055 -436 -197 2974 O ATOM 237 CB LEU A 51 -18.425 -35.189 49.941 1.00 87.04 C ANISOU 237 CB LEU A 51 7236 12811 13023 -79 -73 3570 C ATOM 238 CG LEU A 51 -19.331 -34.906 48.743 1.00 92.07 C ANISOU 238 CG LEU A 51 7889 13383 13711 -197 -161 3616 C ATOM 239 CD1 LEU A 51 -20.566 -35.792 48.766 1.00 93.53 C ANISOU 239 CD1 LEU A 51 7869 13571 14096 -216 -232 3909 C ATOM 240 CD2 LEU A 51 -19.735 -33.454 48.698 1.00 94.31 C ANISOU 240 CD2 LEU A 51 8282 13732 13821 -100 -91 3607 C ATOM 241 N VAL A 52 -15.215 -34.669 49.720 1.00 84.00 N ANISOU 241 N VAL A 52 7182 12336 12400 -182 -24 2961 N ATOM 242 CA VAL A 52 -14.100 -33.895 49.151 1.00 82.63 C ANISOU 242 CA VAL A 52 7195 12110 12090 -249 -17 2695 C ATOM 243 C VAL A 52 -13.084 -34.887 48.516 1.00 85.34 C ANISOU 243 C VAL A 52 7553 12345 12526 -399 -74 2548 C ATOM 244 O VAL A 52 -12.452 -34.547 47.514 1.00 84.20 O ANISOU 244 O VAL A 52 7540 12118 12336 -511 -108 2362 O ATOM 245 CB VAL A 52 -13.444 -32.910 50.170 1.00 86.31 C ANISOU 245 CB VAL A 52 7754 12670 12372 -104 78 2616 C ATOM 246 CG1 VAL A 52 -12.593 -33.624 51.219 1.00 86.13 C ANISOU 246 CG1 VAL A 52 7667 12696 12363 -43 119 2609 C ATOM 247 CG2 VAL A 52 -12.639 -31.825 49.460 1.00 85.33 C ANISOU 247 CG2 VAL A 52 7821 12493 12109 -169 75 2384 C ATOM 248 N MET A 53 -12.983 -36.118 49.068 1.00 81.84 N ANISOU 248 N MET A 53 6974 11904 12218 -395 -81 2644 N ATOM 249 CA MET A 53 -12.136 -37.189 48.542 1.00 81.23 C ANISOU 249 CA MET A 53 6897 11723 12245 -520 -128 2538 C ATOM 250 C MET A 53 -12.808 -37.787 47.302 1.00 85.09 C ANISOU 250 C MET A 53 7379 12089 12863 -667 -242 2560 C ATOM 251 O MET A 53 -12.136 -38.015 46.296 1.00 84.28 O ANISOU 251 O MET A 53 7381 11877 12764 -790 -290 2392 O ATOM 252 CB MET A 53 -11.876 -38.265 49.616 1.00 83.94 C ANISOU 252 CB MET A 53 7091 12114 12689 -454 -91 2651 C ATOM 253 CG MET A 53 -10.924 -39.359 49.172 1.00 87.38 C ANISOU 253 CG MET A 53 7531 12446 13222 -566 -123 2543 C ATOM 254 SD MET A 53 -10.755 -40.679 50.392 1.00 92.09 S ANISOU 254 SD MET A 53 7933 13096 13959 -490 -81 2701 S ATOM 255 CE MET A 53 -9.631 -41.752 49.540 1.00 88.52 C ANISOU 255 CE MET A 53 7539 12496 13599 -638 -121 2538 C ATOM 256 N GLY A 54 -14.123 -38.011 47.396 1.00 82.24 N ANISOU 256 N GLY A 54 6897 11750 12602 -647 -285 2774 N ATOM 257 CA GLY A 54 -14.955 -38.552 46.326 1.00 82.55 C ANISOU 257 CA GLY A 54 6913 11682 12771 -780 -409 2834 C ATOM 258 C GLY A 54 -14.951 -37.683 45.086 1.00 85.68 C ANISOU 258 C GLY A 54 7472 12017 13066 -872 -453 2680 C ATOM 259 O GLY A 54 -14.745 -38.189 43.980 1.00 85.16 O ANISOU 259 O GLY A 54 7478 11825 13055 -1012 -545 2572 O ATOM 260 N LEU A 55 -15.147 -36.362 45.272 1.00 81.86 N ANISOU 260 N LEU A 55 7053 11620 12428 -785 -384 2666 N ATOM 261 CA LEU A 55 -15.127 -35.371 44.194 1.00 81.20 C ANISOU 261 CA LEU A 55 7121 11498 12235 -851 -407 2528 C ATOM 262 C LEU A 55 -13.691 -35.175 43.691 1.00 84.02 C ANISOU 262 C LEU A 55 7631 11794 12498 -908 -384 2267 C ATOM 263 O LEU A 55 -13.484 -35.051 42.485 1.00 83.32 O ANISOU 263 O LEU A 55 7650 11616 12390 -1019 -443 2137 O ATOM 264 CB LEU A 55 -15.730 -34.032 44.675 1.00 81.19 C ANISOU 264 CB LEU A 55 7140 11608 12101 -724 -328 2601 C ATOM 265 CG LEU A 55 -15.956 -32.931 43.627 1.00 85.60 C ANISOU 265 CG LEU A 55 7828 12141 12555 -777 -345 2506 C ATOM 266 CD1 LEU A 55 -17.196 -33.210 42.783 1.00 86.60 C ANISOU 266 CD1 LEU A 55 7890 12227 12786 -864 -447 2649 C ATOM 267 CD2 LEU A 55 -16.106 -31.580 44.293 1.00 87.81 C ANISOU 267 CD2 LEU A 55 8162 12525 12678 -633 -240 2522 C ATOM 268 N GLY A 56 -12.730 -35.178 44.620 1.00 80.12 N ANISOU 268 N GLY A 56 7139 11354 11951 -829 -300 2207 N ATOM 269 CA GLY A 56 -11.304 -35.015 44.348 1.00 79.17 C ANISOU 269 CA GLY A 56 7139 11194 11749 -867 -267 1991 C ATOM 270 C GLY A 56 -10.726 -36.041 43.395 1.00 83.04 C ANISOU 270 C GLY A 56 7665 11556 12329 -996 -334 1888 C ATOM 271 O GLY A 56 -10.036 -35.670 42.443 1.00 82.10 O ANISOU 271 O GLY A 56 7678 11373 12142 -1066 -345 1721 O ATOM 272 N ILE A 57 -11.024 -37.337 43.632 1.00 80.31 N ANISOU 272 N ILE A 57 7205 11170 12139 -1022 -379 1996 N ATOM 273 CA ILE A 57 -10.567 -38.461 42.804 1.00 80.41 C ANISOU 273 CA ILE A 57 7251 11049 12251 -1135 -448 1916 C ATOM 274 C ILE A 57 -11.264 -38.394 41.425 1.00 84.76 C ANISOU 274 C ILE A 57 7883 11501 12820 -1247 -558 1882 C ATOM 275 O ILE A 57 -10.585 -38.533 40.409 1.00 84.09 O ANISOU 275 O ILE A 57 7928 11321 12703 -1325 -587 1721 O ATOM 276 CB ILE A 57 -10.796 -39.828 43.525 1.00 84.23 C ANISOU 276 CB ILE A 57 7583 11517 12905 -1125 -468 2059 C ATOM 277 CG1 ILE A 57 -9.882 -39.946 44.773 1.00 84.23 C ANISOU 277 CG1 ILE A 57 7521 11609 12873 -1022 -357 2061 C ATOM 278 CG2 ILE A 57 -10.574 -41.024 42.574 1.00 85.52 C ANISOU 278 CG2 ILE A 57 7790 11521 13184 -1247 -560 1994 C ATOM 279 CD1 ILE A 57 -10.264 -41.044 45.795 1.00 92.36 C ANISOU 279 CD1 ILE A 57 8367 12670 14054 -969 -351 2246 C ATOM 280 N THR A 58 -12.595 -38.138 41.398 1.00 82.11 N ANISOU 280 N THR A 58 7474 11196 12529 -1247 -614 2040 N ATOM 281 CA THR A 58 -13.416 -38.031 40.179 1.00 82.55 C ANISOU 281 CA THR A 58 7587 11174 12605 -1351 -727 2040 C ATOM 282 C THR A 58 -12.829 -36.961 39.228 1.00 85.99 C ANISOU 282 C THR A 58 8196 11597 12879 -1377 -701 1849 C ATOM 283 O THR A 58 -12.759 -37.201 38.020 1.00 85.77 O ANISOU 283 O THR A 58 8272 11464 12852 -1478 -783 1746 O ATOM 284 CB THR A 58 -14.884 -37.726 40.549 1.00 90.54 C ANISOU 284 CB THR A 58 8472 12258 13672 -1318 -761 2268 C ATOM 285 OG1 THR A 58 -15.348 -38.719 41.464 1.00 90.76 O ANISOU 285 OG1 THR A 58 8330 12303 13853 -1284 -777 2455 O ATOM 286 CG2 THR A 58 -15.813 -37.697 39.334 1.00 89.45 C ANISOU 286 CG2 THR A 58 8372 12044 13571 -1433 -892 2296 C ATOM 287 N VAL A 59 -12.383 -35.811 39.779 1.00 82.01 N ANISOU 287 N VAL A 59 7726 11195 12241 -1284 -591 1802 N ATOM 288 CA VAL A 59 -11.772 -34.720 39.012 1.00 81.27 C ANISOU 288 CA VAL A 59 7781 11098 12001 -1297 -555 1635 C ATOM 289 C VAL A 59 -10.365 -35.176 38.548 1.00 85.17 C ANISOU 289 C VAL A 59 8376 11516 12470 -1338 -535 1451 C ATOM 290 O VAL A 59 -10.038 -34.986 37.377 1.00 84.66 O ANISOU 290 O VAL A 59 8432 11381 12355 -1405 -568 1325 O ATOM 291 CB VAL A 59 -11.742 -33.382 39.813 1.00 84.58 C ANISOU 291 CB VAL A 59 8206 11637 12295 -1185 -453 1651 C ATOM 292 CG1 VAL A 59 -10.943 -32.301 39.090 1.00 83.68 C ANISOU 292 CG1 VAL A 59 8240 11512 12043 -1201 -413 1475 C ATOM 293 CG2 VAL A 59 -13.156 -32.879 40.094 1.00 84.90 C ANISOU 293 CG2 VAL A 59 8166 11746 12347 -1138 -466 1834 C ATOM 294 N CYS A 60 -9.575 -35.825 39.443 1.00 81.90 N ANISOU 294 N CYS A 60 7905 11119 12094 -1294 -479 1450 N ATOM 295 CA CYS A 60 -8.219 -36.331 39.170 1.00 81.54 C ANISOU 295 CA CYS A 60 7933 11015 12035 -1317 -445 1307 C ATOM 296 C CYS A 60 -8.205 -37.314 37.991 1.00 86.17 C ANISOU 296 C CYS A 60 8590 11461 12689 -1416 -534 1243 C ATOM 297 O CYS A 60 -7.311 -37.218 37.148 1.00 85.56 O ANISOU 297 O CYS A 60 8637 11327 12546 -1445 -518 1096 O ATOM 298 CB CYS A 60 -7.615 -36.976 40.414 1.00 81.81 C ANISOU 298 CB CYS A 60 7866 11098 12120 -1252 -380 1360 C ATOM 299 SG CYS A 60 -6.879 -35.802 41.577 1.00 84.91 S ANISOU 299 SG CYS A 60 8253 11628 12383 -1143 -265 1337 S ATOM 300 N ILE A 61 -9.177 -38.254 37.938 1.00 83.73 N ANISOU 300 N ILE A 61 8206 11095 12512 -1463 -630 1358 N ATOM 301 CA ILE A 61 -9.295 -39.254 36.867 1.00 84.47 C ANISOU 301 CA ILE A 61 8374 11043 12678 -1559 -737 1306 C ATOM 302 C ILE A 61 -9.577 -38.527 35.535 1.00 88.61 C ANISOU 302 C ILE A 61 9035 11525 13108 -1617 -794 1210 C ATOM 303 O ILE A 61 -8.966 -38.872 34.522 1.00 88.28 O ANISOU 303 O ILE A 61 9127 11384 13030 -1661 -821 1073 O ATOM 304 CB ILE A 61 -10.375 -40.340 37.200 1.00 88.67 C ANISOU 304 CB ILE A 61 8781 11526 13384 -1602 -841 1472 C ATOM 305 CG1 ILE A 61 -10.077 -41.106 38.529 1.00 89.14 C ANISOU 305 CG1 ILE A 61 8695 11630 13543 -1536 -777 1577 C ATOM 306 CG2 ILE A 61 -10.625 -41.318 36.035 1.00 90.46 C ANISOU 306 CG2 ILE A 61 9101 11586 13683 -1712 -978 1417 C ATOM 307 CD1 ILE A 61 -8.713 -41.917 38.650 1.00 96.30 C ANISOU 307 CD1 ILE A 61 9649 12482 14460 -1521 -711 1465 C ATOM 308 N PHE A 62 -10.452 -37.494 35.557 1.00 85.32 N ANISOU 308 N PHE A 62 8586 11190 12642 -1605 -801 1282 N ATOM 309 CA PHE A 62 -10.806 -36.690 34.382 1.00 85.28 C ANISOU 309 CA PHE A 62 8692 11166 12546 -1652 -847 1212 C ATOM 310 C PHE A 62 -9.587 -35.910 33.862 1.00 88.53 C ANISOU 310 C PHE A 62 9235 11588 12816 -1622 -756 1037 C ATOM 311 O PHE A 62 -9.414 -35.829 32.647 1.00 88.26 O ANISOU 311 O PHE A 62 9326 11484 12725 -1671 -800 929 O ATOM 312 CB PHE A 62 -11.970 -35.729 34.696 1.00 87.07 C ANISOU 312 CB PHE A 62 8838 11491 12754 -1628 -852 1349 C ATOM 313 CG PHE A 62 -12.434 -34.883 33.531 1.00 88.75 C ANISOU 313 CG PHE A 62 9146 11694 12879 -1675 -897 1298 C ATOM 314 CD1 PHE A 62 -13.264 -35.414 32.550 1.00 92.88 C ANISOU 314 CD1 PHE A 62 9699 12133 13458 -1773 -1038 1325 C ATOM 315 CD2 PHE A 62 -12.065 -33.547 33.431 1.00 90.09 C ANISOU 315 CD2 PHE A 62 9375 11941 12916 -1622 -805 1230 C ATOM 316 CE1 PHE A 62 -13.693 -34.629 31.474 1.00 93.92 C ANISOU 316 CE1 PHE A 62 9915 12265 13504 -1814 -1080 1283 C ATOM 317 CE2 PHE A 62 -12.496 -32.762 32.356 1.00 93.02 C ANISOU 317 CE2 PHE A 62 9826 12307 13209 -1662 -841 1190 C ATOM 318 CZ PHE A 62 -13.309 -33.308 31.386 1.00 92.07 C ANISOU 318 CZ PHE A 62 9732 12113 13139 -1755 -975 1218 C ATOM 319 N ILE A 63 -8.748 -35.356 34.772 1.00 84.48 N ANISOU 319 N ILE A 63 8690 11159 12249 -1542 -636 1016 N ATOM 320 CA ILE A 63 -7.526 -34.609 34.425 1.00 83.64 C ANISOU 320 CA ILE A 63 8686 11069 12026 -1513 -549 873 C ATOM 321 C ILE A 63 -6.546 -35.558 33.705 1.00 87.90 C ANISOU 321 C ILE A 63 9317 11502 12578 -1542 -555 760 C ATOM 322 O ILE A 63 -5.997 -35.198 32.664 1.00 87.29 O ANISOU 322 O ILE A 63 9362 11387 12419 -1556 -546 646 O ATOM 323 CB ILE A 63 -6.870 -33.940 35.677 1.00 86.03 C ANISOU 323 CB ILE A 63 8925 11477 12285 -1429 -440 892 C ATOM 324 CG1 ILE A 63 -7.819 -32.923 36.351 1.00 86.29 C ANISOU 324 CG1 ILE A 63 8893 11608 12284 -1381 -426 995 C ATOM 325 CG2 ILE A 63 -5.543 -33.264 35.312 1.00 86.18 C ANISOU 325 CG2 ILE A 63 9040 11501 12204 -1411 -364 757 C ATOM 326 CD1 ILE A 63 -7.434 -32.510 37.797 1.00 93.33 C ANISOU 326 CD1 ILE A 63 9711 12599 13150 -1289 -341 1043 C ATOM 327 N MET A 64 -6.377 -36.782 34.242 1.00 85.08 N ANISOU 327 N MET A 64 8901 11100 12326 -1545 -568 801 N ATOM 328 CA MET A 64 -5.492 -37.819 33.705 1.00 85.38 C ANISOU 328 CA MET A 64 9019 11033 12388 -1560 -567 713 C ATOM 329 C MET A 64 -6.024 -38.420 32.382 1.00 90.33 C ANISOU 329 C MET A 64 9762 11532 13027 -1632 -684 658 C ATOM 330 O MET A 64 -5.290 -39.164 31.728 1.00 90.34 O ANISOU 330 O MET A 64 9868 11437 13021 -1636 -684 566 O ATOM 331 CB MET A 64 -5.288 -38.936 34.743 1.00 87.95 C ANISOU 331 CB MET A 64 9236 11349 12832 -1540 -549 790 C ATOM 332 CG MET A 64 -4.381 -38.531 35.894 1.00 90.77 C ANISOU 332 CG MET A 64 9515 11814 13161 -1465 -428 808 C ATOM 333 SD MET A 64 -4.287 -39.746 37.235 1.00 95.25 S ANISOU 333 SD MET A 64 9929 12396 13866 -1432 -403 924 S ATOM 334 CE MET A 64 -3.365 -41.057 36.439 1.00 92.64 C ANISOU 334 CE MET A 64 9699 11921 13579 -1458 -404 831 C ATOM 335 N LEU A 65 -7.274 -38.094 31.985 1.00 87.35 N ANISOU 335 N LEU A 65 9372 11155 12662 -1684 -784 718 N ATOM 336 CA LEU A 65 -7.884 -38.582 30.744 1.00 88.20 C ANISOU 336 CA LEU A 65 9589 11146 12775 -1761 -914 673 C ATOM 337 C LEU A 65 -7.987 -37.472 29.686 1.00 91.78 C ANISOU 337 C LEU A 65 10149 11626 13097 -1768 -918 595 C ATOM 338 O LEU A 65 -7.667 -37.725 28.524 1.00 91.85 O ANISOU 338 O LEU A 65 10306 11547 13044 -1788 -958 482 O ATOM 339 CB LEU A 65 -9.280 -39.184 31.002 1.00 89.13 C ANISOU 339 CB LEU A 65 9608 11233 13025 -1829 -1048 817 C ATOM 340 CG LEU A 65 -9.339 -40.566 31.666 1.00 94.56 C ANISOU 340 CG LEU A 65 10218 11846 13865 -1847 -1092 889 C ATOM 341 CD1 LEU A 65 -10.719 -40.834 32.229 1.00 95.33 C ANISOU 341 CD1 LEU A 65 10165 11962 14093 -1894 -1193 1076 C ATOM 342 CD2 LEU A 65 -8.941 -41.679 30.698 1.00 98.06 C ANISOU 342 CD2 LEU A 65 10811 12120 14325 -1894 -1172 776 C ATOM 343 N ALA A 66 -8.437 -36.259 30.082 1.00 87.60 N ANISOU 343 N ALA A 66 9548 11215 12521 -1745 -873 657 N ATOM 344 CA ALA A 66 -8.608 -35.110 29.184 1.00 87.13 C ANISOU 344 CA ALA A 66 9567 11193 12344 -1748 -867 602 C ATOM 345 C ALA A 66 -7.260 -34.550 28.707 1.00 90.30 C ANISOU 345 C ALA A 66 10073 11606 12632 -1693 -758 467 C ATOM 346 O ALA A 66 -7.132 -34.225 27.525 1.00 90.08 O ANISOU 346 O ALA A 66 10165 11544 12518 -1705 -779 380 O ATOM 347 CB ALA A 66 -9.409 -34.016 29.872 1.00 87.29 C ANISOU 347 CB ALA A 66 9479 11333 12354 -1726 -836 715 C ATOM 348 N ASN A 67 -6.264 -34.441 29.613 1.00 86.12 N ANISOU 348 N ASN A 67 9493 11125 12102 -1633 -646 459 N ATOM 349 CA ASN A 67 -4.930 -33.933 29.279 1.00 85.40 C ANISOU 349 CA ASN A 67 9478 11050 11921 -1582 -542 356 C ATOM 350 C ASN A 67 -4.114 -34.989 28.525 1.00 89.95 C ANISOU 350 C ASN A 67 10164 11518 12494 -1577 -546 266 C ATOM 351 O ASN A 67 -3.205 -34.627 27.779 1.00 89.39 O ANISOU 351 O ASN A 67 10188 11439 12336 -1540 -485 180 O ATOM 352 CB ASN A 67 -4.183 -33.469 30.526 1.00 85.10 C ANISOU 352 CB ASN A 67 9346 11100 11889 -1527 -437 390 C ATOM 353 CG ASN A 67 -4.766 -32.217 31.126 1.00106.13 C ANISOU 353 CG ASN A 67 11942 13865 14519 -1511 -414 451 C ATOM 354 OD1 ASN A 67 -4.357 -31.096 30.805 1.00 99.60 O ANISOU 354 OD1 ASN A 67 11157 13080 13606 -1490 -363 405 O ATOM 355 ND2 ASN A 67 -5.765 -32.375 31.980 1.00 97.65 N ANISOU 355 ND2 ASN A 67 10764 12826 13510 -1515 -453 562 N ATOM 356 N LEU A 68 -4.441 -36.283 28.705 1.00 87.34 N ANISOU 356 N LEU A 68 9823 11104 12259 -1607 -616 292 N ATOM 357 CA LEU A 68 -3.774 -37.381 28.002 1.00 88.00 C ANISOU 357 CA LEU A 68 10024 11069 12342 -1598 -628 210 C ATOM 358 C LEU A 68 -4.273 -37.442 26.554 1.00 92.62 C ANISOU 358 C LEU A 68 10761 11570 12859 -1633 -726 133 C ATOM 359 O LEU A 68 -3.498 -37.759 25.653 1.00 92.54 O ANISOU 359 O LEU A 68 10892 11493 12777 -1594 -699 34 O ATOM 360 CB LEU A 68 -4.023 -38.718 28.727 1.00 88.67 C ANISOU 360 CB LEU A 68 10044 11085 12561 -1622 -677 270 C ATOM 361 CG LEU A 68 -3.184 -39.929 28.291 1.00 94.25 C ANISOU 361 CG LEU A 68 10859 11671 13282 -1597 -664 196 C ATOM 362 CD1 LEU A 68 -1.765 -39.857 28.849 1.00 93.80 C ANISOU 362 CD1 LEU A 68 10773 11668 13199 -1517 -510 181 C ATOM 363 CD2 LEU A 68 -3.829 -41.219 28.751 1.00 97.65 C ANISOU 363 CD2 LEU A 68 11240 12010 13853 -1646 -759 259 C ATOM 364 N LEU A 69 -5.565 -37.114 26.343 1.00 89.51 N ANISOU 364 N LEU A 69 10338 11188 12485 -1700 -835 187 N ATOM 365 CA LEU A 69 -6.237 -37.101 25.043 1.00 90.25 C ANISOU 365 CA LEU A 69 10557 11215 12518 -1746 -949 133 C ATOM 366 C LEU A 69 -5.670 -36.001 24.131 1.00 93.75 C ANISOU 366 C LEU A 69 11094 11712 12815 -1696 -874 50 C ATOM 367 O LEU A 69 -5.499 -36.244 22.935 1.00 94.12 O ANISOU 367 O LEU A 69 11296 11685 12780 -1687 -915 -44 O ATOM 368 CB LEU A 69 -7.755 -36.899 25.242 1.00 90.54 C ANISOU 368 CB LEU A 69 10501 11278 12624 -1829 -1071 246 C ATOM 369 CG LEU A 69 -8.675 -37.118 24.032 1.00 96.37 C ANISOU 369 CG LEU A 69 11347 11937 13333 -1903 -1229 218 C ATOM 370 CD1 LEU A 69 -8.855 -38.603 23.728 1.00 97.88 C ANISOU 370 CD1 LEU A 69 11619 11970 13601 -1954 -1357 189 C ATOM 371 CD2 LEU A 69 -10.037 -36.505 24.280 1.00 98.80 C ANISOU 371 CD2 LEU A 69 11537 12315 13687 -1967 -1307 350 C ATOM 372 N VAL A 70 -5.377 -34.807 24.691 1.00 89.15 N ANISOU 372 N VAL A 70 10420 11252 12199 -1659 -767 87 N ATOM 373 CA VAL A 70 -4.840 -33.672 23.932 1.00 88.52 C ANISOU 373 CA VAL A 70 10404 11230 11998 -1613 -691 27 C ATOM 374 C VAL A 70 -3.331 -33.920 23.628 1.00 92.21 C ANISOU 374 C VAL A 70 10954 11672 12410 -1531 -580 -55 C ATOM 375 O VAL A 70 -2.850 -33.456 22.594 1.00 91.89 O ANISOU 375 O VAL A 70 11018 11630 12266 -1488 -544 -122 O ATOM 376 CB VAL A 70 -5.108 -32.303 24.634 1.00 91.39 C ANISOU 376 CB VAL A 70 10651 11721 12354 -1606 -627 98 C ATOM 377 CG1 VAL A 70 -4.336 -32.147 25.941 1.00 90.34 C ANISOU 377 CG1 VAL A 70 10410 11647 12267 -1565 -525 138 C ATOM 378 CG2 VAL A 70 -4.848 -31.124 23.702 1.00 90.97 C ANISOU 378 CG2 VAL A 70 10662 11715 12186 -1576 -578 50 C ATOM 379 N MET A 71 -2.615 -34.684 24.490 1.00 88.71 N ANISOU 379 N MET A 71 10462 11208 12037 -1507 -526 -38 N ATOM 380 CA MET A 71 -1.197 -35.015 24.286 1.00 88.68 C ANISOU 380 CA MET A 71 10521 11181 11993 -1428 -418 -92 C ATOM 381 C MET A 71 -1.022 -35.989 23.113 1.00 94.08 C ANISOU 381 C MET A 71 11380 11741 12625 -1402 -465 -179 C ATOM 382 O MET A 71 -0.039 -35.881 22.377 1.00 93.85 O ANISOU 382 O MET A 71 11448 11702 12508 -1323 -382 -235 O ATOM 383 CB MET A 71 -0.563 -35.600 25.556 1.00 90.58 C ANISOU 383 CB MET A 71 10653 11437 12325 -1412 -354 -38 C ATOM 384 CG MET A 71 -0.104 -34.542 26.540 1.00 93.06 C ANISOU 384 CG MET A 71 10840 11874 12647 -1396 -265 18 C ATOM 385 SD MET A 71 0.938 -35.188 27.875 1.00 96.86 S ANISOU 385 SD MET A 71 11213 12380 13209 -1362 -174 71 S ATOM 386 CE MET A 71 -0.285 -35.980 28.908 1.00 93.66 C ANISOU 386 CE MET A 71 10700 11960 12926 -1422 -270 148 C ATOM 387 N VAL A 72 -1.979 -36.923 22.937 1.00 91.80 N ANISOU 387 N VAL A 72 11134 11357 12390 -1466 -600 -185 N ATOM 388 CA VAL A 72 -1.987 -37.902 21.844 1.00 93.11 C ANISOU 388 CA VAL A 72 11485 11387 12507 -1452 -675 -274 C ATOM 389 C VAL A 72 -2.396 -37.170 20.548 1.00 97.67 C ANISOU 389 C VAL A 72 12178 11972 12959 -1448 -724 -334 C ATOM 390 O VAL A 72 -1.818 -37.438 19.494 1.00 98.07 O ANISOU 390 O VAL A 72 12396 11962 12905 -1377 -704 -422 O ATOM 391 CB VAL A 72 -2.905 -39.124 22.162 1.00 97.92 C ANISOU 391 CB VAL A 72 12091 11883 13231 -1534 -820 -251 C ATOM 392 CG1 VAL A 72 -3.058 -40.055 20.959 1.00 99.34 C ANISOU 392 CG1 VAL A 72 12483 11911 13353 -1531 -927 -353 C ATOM 393 CG2 VAL A 72 -2.384 -39.905 23.366 1.00 97.42 C ANISOU 393 CG2 VAL A 72 11919 11811 13285 -1521 -758 -194 C ATOM 394 N ALA A 73 -3.358 -36.222 20.649 1.00 93.90 N ANISOU 394 N ALA A 73 11612 11577 12488 -1513 -776 -280 N ATOM 395 CA ALA A 73 -3.888 -35.412 19.543 1.00 94.11 C ANISOU 395 CA ALA A 73 11716 11631 12408 -1521 -824 -315 C ATOM 396 C ALA A 73 -2.788 -34.608 18.828 1.00 97.90 C ANISOU 396 C ALA A 73 12265 12168 12764 -1415 -688 -368 C ATOM 397 O ALA A 73 -2.794 -34.542 17.600 1.00 98.33 O ANISOU 397 O ALA A 73 12465 12189 12707 -1378 -718 -438 O ATOM 398 CB ALA A 73 -4.959 -34.463 20.060 1.00 94.07 C ANISOU 398 CB ALA A 73 11568 11725 12451 -1596 -866 -221 C ATOM 399 N ILE A 74 -1.853 -34.014 19.593 1.00 93.51 N ANISOU 399 N ILE A 74 11603 11695 12230 -1366 -546 -326 N ATOM 400 CA ILE A 74 -0.731 -33.219 19.077 1.00 93.07 C ANISOU 400 CA ILE A 74 11579 11700 12082 -1269 -410 -347 C ATOM 401 C ILE A 74 0.315 -34.168 18.440 1.00 98.07 C ANISOU 401 C ILE A 74 12356 12248 12658 -1171 -354 -412 C ATOM 402 O ILE A 74 0.923 -33.819 17.425 1.00 98.02 O ANISOU 402 O ILE A 74 12452 12250 12540 -1083 -292 -452 O ATOM 403 CB ILE A 74 -0.139 -32.339 20.227 1.00 94.83 C ANISOU 403 CB ILE A 74 11634 12029 12366 -1266 -300 -270 C ATOM 404 CG1 ILE A 74 -1.167 -31.262 20.667 1.00 94.48 C ANISOU 404 CG1 ILE A 74 11480 12068 12349 -1339 -345 -213 C ATOM 405 CG2 ILE A 74 1.201 -31.685 19.840 1.00 95.25 C ANISOU 405 CG2 ILE A 74 11704 12133 12354 -1170 -159 -273 C ATOM 406 CD1 ILE A 74 -0.949 -30.632 22.057 1.00100.99 C ANISOU 406 CD1 ILE A 74 12146 12975 13252 -1357 -283 -137 C ATOM 407 N TYR A 75 0.479 -35.372 19.019 1.00 95.28 N ANISOU 407 N TYR A 75 12011 11811 12379 -1180 -374 -416 N ATOM 408 CA TYR A 75 1.423 -36.405 18.587 1.00 96.20 C ANISOU 408 CA TYR A 75 12259 11836 12457 -1086 -319 -467 C ATOM 409 C TYR A 75 1.033 -37.033 17.227 1.00101.88 C ANISOU 409 C TYR A 75 13199 12444 13069 -1054 -413 -568 C ATOM 410 O TYR A 75 1.929 -37.290 16.420 1.00102.22 O ANISOU 410 O TYR A 75 13379 12451 13009 -933 -332 -616 O ATOM 411 CB TYR A 75 1.523 -37.500 19.673 1.00 97.40 C ANISOU 411 CB TYR A 75 12344 11929 12734 -1119 -329 -435 C ATOM 412 CG TYR A 75 2.254 -38.765 19.271 1.00100.41 C ANISOU 412 CG TYR A 75 12873 12190 13090 -1036 -298 -489 C ATOM 413 CD1 TYR A 75 3.645 -38.813 19.244 1.00102.38 C ANISOU 413 CD1 TYR A 75 13137 12463 13299 -918 -136 -471 C ATOM 414 CD2 TYR A 75 1.556 -39.937 18.991 1.00102.43 C ANISOU 414 CD2 TYR A 75 13244 12303 13373 -1077 -430 -545 C ATOM 415 CE1 TYR A 75 4.323 -39.981 18.894 1.00104.37 C ANISOU 415 CE1 TYR A 75 13527 12605 13525 -830 -95 -512 C ATOM 416 CE2 TYR A 75 2.222 -41.110 18.639 1.00104.57 C ANISOU 416 CE2 TYR A 75 13663 12451 13619 -995 -400 -598 C ATOM 417 CZ TYR A 75 3.606 -41.129 18.595 1.00111.98 C ANISOU 417 CZ TYR A 75 14621 13419 14506 -865 -226 -581 C ATOM 418 OH TYR A 75 4.266 -42.285 18.255 1.00114.08 O ANISOU 418 OH TYR A 75 15037 13565 14744 -772 -185 -625 O ATOM 419 N VAL A 76 -0.271 -37.297 16.981 1.00 99.20 N ANISOU 419 N VAL A 76 12895 12048 12749 -1155 -584 -594 N ATOM 420 CA VAL A 76 -0.720 -37.960 15.745 1.00100.70 C ANISOU 420 CA VAL A 76 13301 12119 12840 -1140 -702 -693 C ATOM 421 C VAL A 76 -0.992 -36.956 14.598 1.00104.77 C ANISOU 421 C VAL A 76 13891 12698 13219 -1109 -713 -727 C ATOM 422 O VAL A 76 -0.714 -37.295 13.446 1.00105.57 O ANISOU 422 O VAL A 76 14191 12733 13188 -1022 -725 -813 O ATOM 423 CB VAL A 76 -1.953 -38.891 15.939 1.00105.49 C ANISOU 423 CB VAL A 76 13930 12612 13538 -1267 -902 -703 C ATOM 424 CG1 VAL A 76 -1.587 -40.138 16.740 1.00105.62 C ANISOU 424 CG1 VAL A 76 13937 12529 13665 -1269 -897 -694 C ATOM 425 CG2 VAL A 76 -3.150 -38.167 16.561 1.00104.40 C ANISOU 425 CG2 VAL A 76 13616 12559 13492 -1398 -990 -614 C ATOM 426 N ASN A 77 -1.542 -35.759 14.892 1.00100.27 N ANISOU 426 N ASN A 77 13172 12251 12674 -1172 -709 -659 N ATOM 427 CA ASN A 77 -1.873 -34.770 13.861 1.00100.29 C ANISOU 427 CA ASN A 77 13225 12321 12559 -1151 -719 -679 C ATOM 428 C ASN A 77 -0.615 -34.047 13.368 1.00103.88 C ANISOU 428 C ASN A 77 13702 12851 12916 -1010 -541 -679 C ATOM 429 O ASN A 77 0.202 -33.593 14.172 1.00102.31 O ANISOU 429 O ASN A 77 13370 12724 12777 -981 -409 -614 O ATOM 430 CB ASN A 77 -2.904 -33.770 14.377 1.00100.49 C ANISOU 430 CB ASN A 77 13083 12446 12652 -1262 -770 -597 C ATOM 431 CG ASN A 77 -3.587 -32.967 13.298 1.00126.46 C ANISOU 431 CG ASN A 77 16430 15784 15837 -1270 -828 -615 C ATOM 432 OD1 ASN A 77 -3.006 -32.059 12.694 1.00121.13 O ANISOU 432 OD1 ASN A 77 15767 15187 15068 -1185 -721 -618 O ATOM 433 ND2 ASN A 77 -4.856 -33.258 13.060 1.00119.81 N ANISOU 433 ND2 ASN A 77 15609 14898 15013 -1376 -1001 -613 N ATOM 434 N ARG A 78 -0.485 -33.941 12.031 1.00101.61 N ANISOU 434 N ARG A 78 13582 12549 12478 -922 -545 -746 N ATOM 435 CA ARG A 78 0.634 -33.330 11.308 1.00101.55 C ANISOU 435 CA ARG A 78 13621 12604 12359 -771 -388 -743 C ATOM 436 C ARG A 78 0.723 -31.807 11.540 1.00103.85 C ANISOU 436 C ARG A 78 13741 13044 12672 -785 -298 -657 C ATOM 437 O ARG A 78 1.830 -31.288 11.702 1.00102.79 O ANISOU 437 O ARG A 78 13542 12975 12539 -699 -145 -604 O ATOM 438 CB ARG A 78 0.491 -33.620 9.800 1.00103.77 C ANISOU 438 CB ARG A 78 14131 12831 12467 -681 -443 -836 C ATOM 439 CG ARG A 78 1.708 -33.257 8.954 1.00115.24 C ANISOU 439 CG ARG A 78 15665 14330 13793 -495 -278 -832 C ATOM 440 CD ARG A 78 1.417 -33.421 7.476 1.00127.10 C ANISOU 440 CD ARG A 78 17387 15792 15113 -407 -342 -921 C ATOM 441 NE ARG A 78 2.545 -32.996 6.646 1.00136.63 N ANISOU 441 NE ARG A 78 18659 17057 16195 -215 -175 -899 N ATOM 442 CZ ARG A 78 2.538 -32.986 5.316 1.00152.40 C ANISOU 442 CZ ARG A 78 20842 19046 18015 -95 -186 -959 C ATOM 443 NH1 ARG A 78 1.460 -33.376 4.647 1.00140.83 N ANISOU 443 NH1 ARG A 78 19523 17512 16473 -156 -366 -1054 N ATOM 444 NH2 ARG A 78 3.608 -32.583 4.645 1.00139.60 N1+ ANISOU 444 NH2 ARG A 78 19261 17490 16293 89 -19 -916 N1+ ATOM 445 N ARG A 79 -0.429 -31.102 11.544 1.00 99.87 N ANISOU 445 N ARG A 79 13167 12591 12190 -892 -395 -637 N ATOM 446 CA ARG A 79 -0.510 -29.644 11.701 1.00 98.52 C ANISOU 446 CA ARG A 79 12849 12548 12035 -911 -326 -561 C ATOM 447 C ARG A 79 -0.113 -29.173 13.121 1.00100.57 C ANISOU 447 C ARG A 79 12916 12864 12432 -960 -247 -478 C ATOM 448 O ARG A 79 0.188 -27.989 13.293 1.00 99.16 O ANISOU 448 O ARG A 79 12629 12781 12267 -949 -161 -418 O ATOM 449 CB ARG A 79 -1.932 -29.151 11.373 1.00 99.15 C ANISOU 449 CB ARG A 79 12912 12656 12105 -1013 -457 -556 C ATOM 450 CG ARG A 79 -1.987 -27.711 10.858 1.00109.50 C ANISOU 450 CG ARG A 79 14156 14083 13364 -986 -388 -508 C ATOM 451 CD ARG A 79 -3.403 -27.164 10.781 1.00119.60 C ANISOU 451 CD ARG A 79 15382 15402 14658 -1096 -503 -478 C ATOM 452 NE ARG A 79 -3.977 -26.912 12.106 1.00127.46 N ANISOU 452 NE ARG A 79 16214 16423 15792 -1204 -524 -404 N ATOM 453 CZ ARG A 79 -3.882 -25.759 12.763 1.00140.97 C ANISOU 453 CZ ARG A 79 17780 18225 17558 -1216 -437 -329 C ATOM 454 NH1 ARG A 79 -3.233 -24.732 12.228 1.00128.22 N ANISOU 454 NH1 ARG A 79 16149 16681 15887 -1140 -325 -312 N ATOM 455 NH2 ARG A 79 -4.435 -25.625 13.961 1.00127.22 N1+ ANISOU 455 NH2 ARG A 79 15910 16499 15928 -1300 -461 -267 N1+ ATOM 456 N PHE A 80 -0.102 -30.077 14.123 1.00 96.82 N ANISOU 456 N PHE A 80 12402 12329 12057 -1011 -279 -475 N ATOM 457 CA PHE A 80 0.248 -29.701 15.494 1.00 95.33 C ANISOU 457 CA PHE A 80 12041 12193 11988 -1054 -214 -400 C ATOM 458 C PHE A 80 1.725 -30.031 15.833 1.00 98.73 C ANISOU 458 C PHE A 80 12461 12617 12433 -963 -81 -383 C ATOM 459 O PHE A 80 2.075 -30.122 17.012 1.00 97.51 O ANISOU 459 O PHE A 80 12191 12480 12379 -998 -46 -335 O ATOM 460 CB PHE A 80 -0.706 -30.363 16.509 1.00 96.93 C ANISOU 460 CB PHE A 80 12174 12353 12300 -1168 -324 -382 C ATOM 461 CG PHE A 80 -2.157 -29.951 16.377 1.00 98.52 C ANISOU 461 CG PHE A 80 12347 12575 12510 -1263 -446 -364 C ATOM 462 CD1 PHE A 80 -2.511 -28.611 16.263 1.00100.98 C ANISOU 462 CD1 PHE A 80 12583 12985 12800 -1277 -415 -318 C ATOM 463 CD2 PHE A 80 -3.171 -30.897 16.430 1.00101.39 C ANISOU 463 CD2 PHE A 80 12748 12860 12916 -1343 -592 -377 C ATOM 464 CE1 PHE A 80 -3.849 -28.230 16.150 1.00101.91 C ANISOU 464 CE1 PHE A 80 12669 13127 12926 -1359 -518 -285 C ATOM 465 CE2 PHE A 80 -4.511 -30.516 16.318 1.00104.28 C ANISOU 465 CE2 PHE A 80 13074 13251 13297 -1433 -704 -338 C ATOM 466 CZ PHE A 80 -4.840 -29.185 16.180 1.00101.69 C ANISOU 466 CZ PHE A 80 12673 13027 12937 -1437 -662 -290 C ATOM 467 N HIS A 81 2.595 -30.143 14.808 1.00 95.76 N ANISOU 467 N HIS A 81 12201 12230 11955 -841 -3 -410 N ATOM 468 CA HIS A 81 4.025 -30.384 15.013 1.00 95.44 C ANISOU 468 CA HIS A 81 12147 12194 11923 -743 134 -372 C ATOM 469 C HIS A 81 4.785 -29.046 14.890 1.00 97.99 C ANISOU 469 C HIS A 81 12371 12623 12236 -696 248 -295 C ATOM 470 O HIS A 81 5.640 -28.880 14.015 1.00 98.06 O ANISOU 470 O HIS A 81 12444 12650 12166 -575 342 -279 O ATOM 471 CB HIS A 81 4.572 -31.450 14.040 1.00 97.69 C ANISOU 471 CB HIS A 81 12620 12391 12105 -621 159 -433 C ATOM 472 CG HIS A 81 4.073 -32.840 14.295 1.00101.76 C ANISOU 472 CG HIS A 81 13228 12788 12649 -661 60 -500 C ATOM 473 ND1 HIS A 81 3.431 -33.565 13.309 1.00104.81 N ANISOU 473 ND1 HIS A 81 13803 13080 12942 -642 -44 -595 N ATOM 474 CD2 HIS A 81 4.147 -33.599 15.414 1.00103.11 C ANISOU 474 CD2 HIS A 81 13326 12918 12935 -718 47 -479 C ATOM 475 CE1 HIS A 81 3.141 -34.735 13.854 1.00104.60 C ANISOU 475 CE1 HIS A 81 13811 12951 12982 -692 -119 -628 C ATOM 476 NE2 HIS A 81 3.546 -34.799 15.121 1.00103.92 N ANISOU 476 NE2 HIS A 81 13565 12896 13022 -737 -63 -558 N ATOM 477 N PHE A 82 4.445 -28.090 15.778 1.00 93.02 N ANISOU 477 N PHE A 82 11590 12063 11693 -790 236 -243 N ATOM 478 CA PHE A 82 5.037 -26.751 15.825 1.00 92.07 C ANISOU 478 CA PHE A 82 11363 12031 11586 -773 320 -169 C ATOM 479 C PHE A 82 5.445 -26.372 17.266 1.00 94.10 C ANISOU 479 C PHE A 82 11464 12325 11964 -841 345 -104 C ATOM 480 O PHE A 82 4.793 -26.830 18.208 1.00 93.19 O ANISOU 480 O PHE A 82 11308 12187 11915 -924 274 -120 O ATOM 481 CB PHE A 82 4.063 -25.711 15.246 1.00 93.75 C ANISOU 481 CB PHE A 82 11572 12292 11757 -812 269 -178 C ATOM 482 CG PHE A 82 3.990 -25.724 13.737 1.00 96.44 C ANISOU 482 CG PHE A 82 12047 12627 11969 -721 277 -218 C ATOM 483 CD1 PHE A 82 4.878 -24.975 12.975 1.00 99.91 C ANISOU 483 CD1 PHE A 82 12481 13122 12357 -619 386 -166 C ATOM 484 CD2 PHE A 82 3.033 -26.485 13.078 1.00 99.44 C ANISOU 484 CD2 PHE A 82 12557 12947 12278 -736 171 -300 C ATOM 485 CE1 PHE A 82 4.811 -24.988 11.578 1.00101.86 C ANISOU 485 CE1 PHE A 82 12855 13371 12475 -521 398 -198 C ATOM 486 CE2 PHE A 82 2.966 -26.498 11.681 1.00103.35 C ANISOU 486 CE2 PHE A 82 13188 13438 12640 -647 171 -342 C ATOM 487 CZ PHE A 82 3.856 -25.750 10.941 1.00101.69 C ANISOU 487 CZ PHE A 82 12975 13291 12372 -533 290 -292 C ATOM 488 N PRO A 83 6.499 -25.522 17.447 1.00 89.71 N ANISOU 488 N PRO A 83 10819 11827 11439 -807 440 -25 N ATOM 489 CA PRO A 83 6.971 -25.166 18.804 1.00 88.42 C ANISOU 489 CA PRO A 83 10519 11694 11382 -870 454 34 C ATOM 490 C PRO A 83 5.892 -24.727 19.804 1.00 90.56 C ANISOU 490 C PRO A 83 10721 11979 11709 -983 366 18 C ATOM 491 O PRO A 83 6.032 -25.032 20.989 1.00 89.75 O ANISOU 491 O PRO A 83 10546 11876 11680 -1030 352 37 O ATOM 492 CB PRO A 83 7.926 -23.987 18.553 1.00 90.15 C ANISOU 492 CB PRO A 83 10666 11973 11613 -833 536 117 C ATOM 493 CG PRO A 83 7.821 -23.662 17.089 1.00 95.37 C ANISOU 493 CG PRO A 83 11415 12644 12176 -752 567 104 C ATOM 494 CD PRO A 83 7.380 -24.919 16.429 1.00 91.72 C ANISOU 494 CD PRO A 83 11094 12118 11636 -704 535 24 C ATOM 495 N ILE A 84 4.839 -24.021 19.349 1.00 86.08 N ANISOU 495 N ILE A 84 10174 11429 11104 -1017 312 -8 N ATOM 496 CA ILE A 84 3.762 -23.539 20.220 1.00 84.72 C ANISOU 496 CA ILE A 84 9941 11275 10975 -1106 239 -10 C ATOM 497 C ILE A 84 2.894 -24.724 20.719 1.00 87.53 C ANISOU 497 C ILE A 84 10321 11582 11354 -1151 157 -47 C ATOM 498 O ILE A 84 2.552 -24.753 21.904 1.00 86.51 O ANISOU 498 O ILE A 84 10115 11463 11291 -1205 126 -25 O ATOM 499 CB ILE A 84 2.897 -22.423 19.534 1.00 87.71 C ANISOU 499 CB ILE A 84 10330 11690 11307 -1122 216 -11 C ATOM 500 CG1 ILE A 84 1.742 -21.904 20.436 1.00 87.45 C ANISOU 500 CG1 ILE A 84 10237 11679 11313 -1201 151 1 C ATOM 501 CG2 ILE A 84 2.386 -22.819 18.139 1.00 89.22 C ANISOU 501 CG2 ILE A 84 10633 11860 11405 -1082 190 -58 C ATOM 502 CD1 ILE A 84 2.153 -21.271 21.774 1.00 93.81 C ANISOU 502 CD1 ILE A 84 10945 12508 12189 -1233 171 43 C ATOM 503 N TYR A 85 2.571 -25.695 19.841 1.00 84.00 N ANISOU 503 N TYR A 85 9982 11080 10856 -1124 120 -99 N ATOM 504 CA TYR A 85 1.730 -26.840 20.193 1.00 83.65 C ANISOU 504 CA TYR A 85 9965 10977 10841 -1171 29 -130 C ATOM 505 C TYR A 85 2.479 -27.871 21.054 1.00 86.40 C ANISOU 505 C TYR A 85 10285 11289 11255 -1160 58 -120 C ATOM 506 O TYR A 85 1.828 -28.565 21.839 1.00 85.80 O ANISOU 506 O TYR A 85 10173 11185 11240 -1214 -7 -115 O ATOM 507 CB TYR A 85 1.154 -27.510 18.940 1.00 85.80 C ANISOU 507 CB TYR A 85 10376 11191 11035 -1152 -35 -193 C ATOM 508 CG TYR A 85 0.194 -26.618 18.184 1.00 87.57 C ANISOU 508 CG TYR A 85 10618 11452 11202 -1178 -83 -196 C ATOM 509 CD1 TYR A 85 -1.096 -26.390 18.655 1.00 89.20 C ANISOU 509 CD1 TYR A 85 10770 11675 11449 -1263 -172 -170 C ATOM 510 CD2 TYR A 85 0.575 -25.998 16.998 1.00 88.75 C ANISOU 510 CD2 TYR A 85 10835 11628 11259 -1110 -33 -213 C ATOM 511 CE1 TYR A 85 -1.982 -25.560 17.969 1.00 90.04 C ANISOU 511 CE1 TYR A 85 10886 11822 11504 -1286 -210 -160 C ATOM 512 CE2 TYR A 85 -0.304 -25.172 16.298 1.00 89.71 C ANISOU 512 CE2 TYR A 85 10968 11789 11328 -1132 -73 -210 C ATOM 513 CZ TYR A 85 -1.583 -24.957 16.787 1.00 96.70 C ANISOU 513 CZ TYR A 85 11798 12690 12255 -1223 -162 -184 C ATOM 514 OH TYR A 85 -2.454 -24.144 16.102 1.00 97.65 O ANISOU 514 OH TYR A 85 11923 12855 12326 -1244 -197 -170 O ATOM 515 N TYR A 86 3.825 -27.962 20.932 1.00 82.30 N ANISOU 515 N TYR A 86 9770 10774 10727 -1089 157 -103 N ATOM 516 CA TYR A 86 4.633 -28.876 21.753 1.00 81.75 C ANISOU 516 CA TYR A 86 9662 10679 10718 -1074 197 -80 C ATOM 517 C TYR A 86 4.656 -28.403 23.210 1.00 83.73 C ANISOU 517 C TYR A 86 9773 10986 11056 -1134 196 -25 C ATOM 518 O TYR A 86 4.663 -29.229 24.124 1.00 83.12 O ANISOU 518 O TYR A 86 9650 10889 11042 -1156 182 -12 O ATOM 519 CB TYR A 86 6.068 -29.012 21.216 1.00 83.43 C ANISOU 519 CB TYR A 86 9908 10894 10899 -977 310 -55 C ATOM 520 CG TYR A 86 6.214 -29.907 20.004 1.00 86.30 C ANISOU 520 CG TYR A 86 10424 11185 11179 -893 322 -110 C ATOM 521 CD1 TYR A 86 6.117 -31.291 20.118 1.00 88.86 C ANISOU 521 CD1 TYR A 86 10818 11426 11519 -883 293 -148 C ATOM 522 CD2 TYR A 86 6.554 -29.380 18.762 1.00 87.60 C ANISOU 522 CD2 TYR A 86 10669 11365 11249 -813 370 -117 C ATOM 523 CE1 TYR A 86 6.278 -32.122 19.010 1.00 90.80 C ANISOU 523 CE1 TYR A 86 11226 11594 11679 -798 300 -205 C ATOM 524 CE2 TYR A 86 6.717 -30.199 17.647 1.00 89.63 C ANISOU 524 CE2 TYR A 86 11085 11556 11414 -721 384 -170 C ATOM 525 CZ TYR A 86 6.583 -31.571 17.776 1.00 97.38 C ANISOU 525 CZ TYR A 86 12150 12445 12405 -713 346 -219 C ATOM 526 OH TYR A 86 6.758 -32.381 16.681 1.00 99.17 O ANISOU 526 OH TYR A 86 12553 12596 12532 -614 356 -278 O ATOM 527 N LEU A 87 4.647 -27.069 23.413 1.00 79.05 N ANISOU 527 N LEU A 87 9118 10458 10460 -1156 210 5 N ATOM 528 CA LEU A 87 4.625 -26.414 24.723 1.00 77.75 C ANISOU 528 CA LEU A 87 8842 10344 10357 -1206 202 49 C ATOM 529 C LEU A 87 3.262 -26.599 25.400 1.00 80.14 C ANISOU 529 C LEU A 87 9117 10644 10687 -1264 116 42 C ATOM 530 O LEU A 87 3.198 -26.651 26.630 1.00 79.33 O ANISOU 530 O LEU A 87 8936 10568 10640 -1290 105 75 O ATOM 531 CB LEU A 87 4.954 -24.919 24.572 1.00 77.54 C ANISOU 531 CB LEU A 87 8782 10369 10310 -1208 234 75 C ATOM 532 CG LEU A 87 6.374 -24.463 24.951 1.00 82.34 C ANISOU 532 CG LEU A 87 9328 11006 10951 -1188 303 130 C ATOM 533 CD1 LEU A 87 7.444 -25.108 24.071 1.00 83.26 C ANISOU 533 CD1 LEU A 87 9490 11101 11045 -1114 378 145 C ATOM 534 CD2 LEU A 87 6.498 -22.961 24.844 1.00 84.58 C ANISOU 534 CD2 LEU A 87 9582 11328 11228 -1204 312 155 C ATOM 535 N MET A 88 2.181 -26.708 24.596 1.00 76.02 N ANISOU 535 N MET A 88 8660 10097 10126 -1280 55 10 N ATOM 536 CA MET A 88 0.811 -26.934 25.071 1.00 75.28 C ANISOU 536 CA MET A 88 8541 10000 10062 -1332 -31 23 C ATOM 537 C MET A 88 0.666 -28.358 25.615 1.00 78.72 C ANISOU 537 C MET A 88 8966 10385 10560 -1345 -68 26 C ATOM 538 O MET A 88 -0.051 -28.566 26.596 1.00 77.97 O ANISOU 538 O MET A 88 8796 10305 10522 -1379 -111 70 O ATOM 539 CB MET A 88 -0.215 -26.681 23.954 1.00 77.90 C ANISOU 539 CB MET A 88 8943 10318 10337 -1349 -90 -2 C ATOM 540 CG MET A 88 -0.373 -25.223 23.593 1.00 81.06 C ANISOU 540 CG MET A 88 9334 10776 10691 -1346 -62 11 C ATOM 541 SD MET A 88 -1.606 -24.970 22.297 1.00 85.60 S ANISOU 541 SD MET A 88 9983 11344 11199 -1367 -133 -8 S ATOM 542 CE MET A 88 -1.488 -23.219 22.092 1.00 81.73 C ANISOU 542 CE MET A 88 9461 10926 10669 -1351 -70 17 C ATOM 543 N ALA A 89 1.356 -29.330 24.977 1.00 75.39 N ANISOU 543 N ALA A 89 8619 9900 10125 -1309 -48 -13 N ATOM 544 CA ALA A 89 1.373 -30.740 25.375 1.00 75.35 C ANISOU 544 CA ALA A 89 8618 9833 10180 -1313 -74 -15 C ATOM 545 C ALA A 89 2.126 -30.918 26.693 1.00 77.94 C ANISOU 545 C ALA A 89 8838 10199 10575 -1305 -17 36 C ATOM 546 O ALA A 89 1.753 -31.771 27.498 1.00 77.39 O ANISOU 546 O ALA A 89 8716 10110 10577 -1328 -52 65 O ATOM 547 CB ALA A 89 2.012 -31.587 24.285 1.00 76.97 C ANISOU 547 CB ALA A 89 8949 9960 10337 -1260 -53 -73 C ATOM 548 N ASN A 90 3.178 -30.097 26.911 1.00 73.76 N ANISOU 548 N ASN A 90 8272 9726 10026 -1275 65 54 N ATOM 549 CA ASN A 90 3.987 -30.099 28.131 1.00 72.92 C ANISOU 549 CA ASN A 90 8066 9666 9974 -1270 115 104 C ATOM 550 C ASN A 90 3.188 -29.486 29.284 1.00 75.83 C ANISOU 550 C ASN A 90 8345 10093 10375 -1311 72 143 C ATOM 551 O ASN A 90 3.354 -29.904 30.432 1.00 75.20 O ANISOU 551 O ASN A 90 8185 10038 10351 -1314 78 184 O ATOM 552 CB ASN A 90 5.301 -29.348 27.918 1.00 72.88 C ANISOU 552 CB ASN A 90 8053 9699 9941 -1235 198 120 C ATOM 553 CG ASN A 90 6.366 -29.698 28.928 1.00 92.82 C ANISOU 553 CG ASN A 90 10494 12253 12519 -1223 252 172 C ATOM 554 OD1 ASN A 90 6.703 -30.869 29.137 1.00 86.88 O ANISOU 554 OD1 ASN A 90 9739 11467 11805 -1202 273 183 O ATOM 555 ND2 ASN A 90 6.961 -28.686 29.539 1.00 83.88 N ANISOU 555 ND2 ASN A 90 9297 11183 11392 -1237 273 209 N ATOM 556 N LEU A 91 2.308 -28.508 28.967 1.00 71.85 N ANISOU 556 N LEU A 91 7858 9612 9831 -1333 33 135 N ATOM 557 CA LEU A 91 1.403 -27.855 29.916 1.00 71.07 C ANISOU 557 CA LEU A 91 7694 9565 9746 -1356 -4 175 C ATOM 558 C LEU A 91 0.353 -28.873 30.377 1.00 74.92 C ANISOU 558 C LEU A 91 8147 10030 10291 -1376 -67 208 C ATOM 559 O LEU A 91 -0.023 -28.881 31.550 1.00 74.23 O ANISOU 559 O LEU A 91 7978 9983 10241 -1374 -76 262 O ATOM 560 CB LEU A 91 0.750 -26.614 29.269 1.00 70.95 C ANISOU 560 CB LEU A 91 7715 9570 9670 -1366 -20 162 C ATOM 561 CG LEU A 91 -0.217 -25.773 30.120 1.00 75.34 C ANISOU 561 CG LEU A 91 8222 10178 10224 -1375 -47 206 C ATOM 562 CD1 LEU A 91 0.511 -25.025 31.232 1.00 75.09 C ANISOU 562 CD1 LEU A 91 8143 10195 10194 -1357 -9 223 C ATOM 563 CD2 LEU A 91 -0.961 -24.778 29.258 1.00 78.03 C ANISOU 563 CD2 LEU A 91 8609 10529 10510 -1384 -63 197 C ATOM 564 N ALA A 92 -0.084 -29.750 29.448 1.00 71.87 N ANISOU 564 N ALA A 92 7824 9573 9910 -1391 -113 180 N ATOM 565 CA ALA A 92 -1.026 -30.839 29.704 1.00 71.98 C ANISOU 565 CA ALA A 92 7813 9545 9992 -1419 -186 214 C ATOM 566 C ALA A 92 -0.347 -31.943 30.518 1.00 75.55 C ANISOU 566 C ALA A 92 8213 9977 10514 -1403 -156 235 C ATOM 567 O ALA A 92 -0.993 -32.562 31.365 1.00 75.14 O ANISOU 567 O ALA A 92 8084 9931 10537 -1415 -194 298 O ATOM 568 CB ALA A 92 -1.553 -31.394 28.391 1.00 73.45 C ANISOU 568 CB ALA A 92 8102 9649 10155 -1445 -252 166 C ATOM 569 N ALA A 93 0.966 -32.168 30.269 1.00 71.90 N ANISOU 569 N ALA A 93 7786 9500 10033 -1368 -84 197 N ATOM 570 CA ALA A 93 1.799 -33.141 30.983 1.00 71.69 C ANISOU 570 CA ALA A 93 7712 9461 10066 -1345 -37 220 C ATOM 571 C ALA A 93 2.007 -32.693 32.429 1.00 74.55 C ANISOU 571 C ALA A 93 7954 9913 10459 -1337 -7 283 C ATOM 572 O ALA A 93 2.069 -33.534 33.328 1.00 74.18 O ANISOU 572 O ALA A 93 7833 9871 10482 -1329 -1 331 O ATOM 573 CB ALA A 93 3.138 -33.307 30.279 1.00 72.68 C ANISOU 573 CB ALA A 93 7904 9558 10152 -1302 41 179 C ATOM 574 N ALA A 94 2.091 -31.361 32.645 1.00 70.25 N ANISOU 574 N ALA A 94 7397 9435 9859 -1335 9 283 N ATOM 575 CA ALA A 94 2.219 -30.729 33.959 1.00 69.41 C ANISOU 575 CA ALA A 94 7204 9411 9759 -1324 26 330 C ATOM 576 C ALA A 94 0.923 -30.909 34.750 1.00 72.65 C ANISOU 576 C ALA A 94 7552 9847 10206 -1326 -28 389 C ATOM 577 O ALA A 94 0.970 -31.137 35.960 1.00 71.99 O ANISOU 577 O ALA A 94 7383 9812 10156 -1304 -16 444 O ATOM 578 CB ALA A 94 2.551 -29.254 33.799 1.00 69.81 C ANISOU 578 CB ALA A 94 7283 9503 9739 -1324 43 305 C ATOM 579 N ASP A 95 -0.232 -30.837 34.049 1.00 69.10 N ANISOU 579 N ASP A 95 7139 9365 9750 -1351 -86 389 N ATOM 580 CA ASP A 95 -1.563 -31.052 34.618 1.00 68.88 C ANISOU 580 CA ASP A 95 7049 9357 9765 -1354 -141 465 C ATOM 581 C ASP A 95 -1.767 -32.542 34.896 1.00 72.70 C ANISOU 581 C ASP A 95 7482 9794 10346 -1364 -170 508 C ATOM 582 O ASP A 95 -2.407 -32.889 35.887 1.00 72.26 O ANISOU 582 O ASP A 95 7331 9775 10347 -1346 -186 596 O ATOM 583 CB ASP A 95 -2.661 -30.512 33.686 1.00 70.88 C ANISOU 583 CB ASP A 95 7355 9591 9985 -1384 -198 462 C ATOM 584 CG ASP A 95 -2.641 -29.007 33.477 1.00 80.69 C ANISOU 584 CG ASP A 95 8638 10881 11140 -1371 -170 435 C ATOM 585 OD1 ASP A 95 -2.423 -28.268 34.466 1.00 80.74 O ANISOU 585 OD1 ASP A 95 8604 10951 11121 -1334 -133 459 O ATOM 586 OD2 ASP A 95 -2.910 -28.565 32.340 1.00 87.07 O1- ANISOU 586 OD2 ASP A 95 9518 11660 11904 -1396 -190 393 O1- ATOM 587 N PHE A 96 -1.193 -33.418 34.037 1.00 69.29 N ANISOU 587 N PHE A 96 7116 9278 9933 -1383 -172 451 N ATOM 588 CA PHE A 96 -1.231 -34.878 34.190 1.00 69.45 C ANISOU 588 CA PHE A 96 7107 9232 10047 -1393 -196 478 C ATOM 589 C PHE A 96 -0.452 -35.271 35.451 1.00 72.61 C ANISOU 589 C PHE A 96 7410 9688 10492 -1353 -130 527 C ATOM 590 O PHE A 96 -0.879 -36.168 36.182 1.00 72.29 O ANISOU 590 O PHE A 96 7283 9643 10540 -1349 -151 600 O ATOM 591 CB PHE A 96 -0.664 -35.574 32.938 1.00 71.78 C ANISOU 591 CB PHE A 96 7523 9424 10328 -1406 -201 393 C ATOM 592 CG PHE A 96 -0.784 -37.081 32.932 1.00 74.04 C ANISOU 592 CG PHE A 96 7807 9618 10708 -1420 -239 410 C ATOM 593 CD1 PHE A 96 -1.952 -37.700 32.503 1.00 77.77 C ANISOU 593 CD1 PHE A 96 8296 10016 11236 -1471 -349 432 C ATOM 594 CD2 PHE A 96 0.283 -37.882 33.323 1.00 76.31 C ANISOU 594 CD2 PHE A 96 8077 9887 11030 -1385 -168 408 C ATOM 595 CE1 PHE A 96 -2.061 -39.094 32.493 1.00 79.46 C ANISOU 595 CE1 PHE A 96 8514 10131 11546 -1489 -394 447 C ATOM 596 CE2 PHE A 96 0.174 -39.276 33.311 1.00 79.87 C ANISOU 596 CE2 PHE A 96 8532 10245 11572 -1395 -200 423 C ATOM 597 CZ PHE A 96 -0.996 -39.873 32.894 1.00 78.62 C ANISOU 597 CZ PHE A 96 8396 10004 11472 -1448 -316 439 C ATOM 598 N PHE A 97 0.673 -34.568 35.712 1.00 68.52 N ANISOU 598 N PHE A 97 6898 9225 9914 -1324 -56 494 N ATOM 599 CA PHE A 97 1.508 -34.736 36.901 1.00 68.03 C ANISOU 599 CA PHE A 97 6746 9227 9874 -1288 4 537 C ATOM 600 C PHE A 97 0.759 -34.191 38.122 1.00 71.72 C ANISOU 600 C PHE A 97 7123 9785 10343 -1263 -12 611 C ATOM 601 O PHE A 97 0.875 -34.758 39.209 1.00 71.34 O ANISOU 601 O PHE A 97 6979 9781 10346 -1232 9 677 O ATOM 602 CB PHE A 97 2.869 -34.038 36.716 1.00 69.49 C ANISOU 602 CB PHE A 97 6968 9440 9994 -1276 71 488 C ATOM 603 CG PHE A 97 3.776 -34.061 37.925 1.00 70.76 C ANISOU 603 CG PHE A 97 7041 9676 10169 -1248 122 534 C ATOM 604 CD1 PHE A 97 4.557 -35.175 38.209 1.00 74.08 C ANISOU 604 CD1 PHE A 97 7417 10080 10650 -1232 169 563 C ATOM 605 CD2 PHE A 97 3.868 -32.959 38.767 1.00 72.45 C ANISOU 605 CD2 PHE A 97 7223 9974 10331 -1235 122 547 C ATOM 606 CE1 PHE A 97 5.393 -35.195 39.329 1.00 74.85 C ANISOU 606 CE1 PHE A 97 7427 10254 10760 -1209 213 612 C ATOM 607 CE2 PHE A 97 4.699 -32.982 39.888 1.00 75.18 C ANISOU 607 CE2 PHE A 97 7493 10388 10683 -1213 156 587 C ATOM 608 CZ PHE A 97 5.464 -34.095 40.156 1.00 73.54 C ANISOU 608 CZ PHE A 97 7230 10172 10538 -1202 201 623 C ATOM 609 N ALA A 98 -0.015 -33.095 37.932 1.00 68.19 N ANISOU 609 N ALA A 98 6708 9365 9834 -1267 -43 604 N ATOM 610 CA ALA A 98 -0.841 -32.477 38.974 1.00 67.93 C ANISOU 610 CA ALA A 98 6611 9413 9785 -1227 -55 676 C ATOM 611 C ALA A 98 -1.986 -33.414 39.361 1.00 72.28 C ANISOU 611 C ALA A 98 7080 9956 10427 -1221 -99 775 C ATOM 612 O ALA A 98 -2.320 -33.508 40.542 1.00 71.98 O ANISOU 612 O ALA A 98 6950 9988 10411 -1168 -86 861 O ATOM 613 CB ALA A 98 -1.382 -31.135 38.501 1.00 68.44 C ANISOU 613 CB ALA A 98 6744 9495 9766 -1231 -72 645 C ATOM 614 N GLY A 99 -2.525 -34.134 38.370 1.00 69.15 N ANISOU 614 N GLY A 99 6716 9472 10084 -1273 -153 766 N ATOM 615 CA GLY A 99 -3.580 -35.129 38.546 1.00 69.48 C ANISOU 615 CA GLY A 99 6684 9483 10232 -1287 -213 863 C ATOM 616 C GLY A 99 -3.137 -36.266 39.446 1.00 73.27 C ANISOU 616 C GLY A 99 7068 9968 10802 -1261 -184 921 C ATOM 617 O GLY A 99 -3.941 -36.799 40.214 1.00 73.10 O ANISOU 617 O GLY A 99 6938 9974 10861 -1238 -208 1039 O ATOM 618 N LEU A 100 -1.838 -36.620 39.368 1.00 69.50 N ANISOU 618 N LEU A 100 6623 9470 10314 -1259 -128 851 N ATOM 619 CA LEU A 100 -1.185 -37.636 40.193 1.00 69.42 C ANISOU 619 CA LEU A 100 6528 9471 10379 -1231 -84 897 C ATOM 620 C LEU A 100 -0.834 -37.060 41.566 1.00 72.56 C ANISOU 620 C LEU A 100 6840 9994 10737 -1164 -27 949 C ATOM 621 O LEU A 100 -0.879 -37.785 42.562 1.00 72.33 O ANISOU 621 O LEU A 100 6700 10006 10778 -1125 -7 1038 O ATOM 622 CB LEU A 100 0.087 -38.161 39.499 1.00 69.59 C ANISOU 622 CB LEU A 100 6625 9424 10394 -1249 -38 809 C ATOM 623 CG LEU A 100 -0.107 -39.055 38.273 1.00 75.01 C ANISOU 623 CG LEU A 100 7401 9974 11126 -1297 -87 758 C ATOM 624 CD1 LEU A 100 1.043 -38.899 37.298 1.00 75.08 C ANISOU 624 CD1 LEU A 100 7530 9935 11063 -1299 -38 651 C ATOM 625 CD2 LEU A 100 -0.281 -40.515 38.671 1.00 78.26 C ANISOU 625 CD2 LEU A 100 7741 10327 11667 -1299 -102 826 C ATOM 626 N ALA A 101 -0.482 -35.755 41.611 1.00 68.36 N ANISOU 626 N ALA A 101 6364 9519 10092 -1149 -6 894 N ATOM 627 CA ALA A 101 -0.112 -35.024 42.825 1.00 67.77 C ANISOU 627 CA ALA A 101 6242 9553 9955 -1089 33 922 C ATOM 628 C ALA A 101 -1.323 -34.807 43.743 1.00 71.57 C ANISOU 628 C ALA A 101 6647 10104 10441 -1027 13 1028 C ATOM 629 O ALA A 101 -1.198 -35.005 44.953 1.00 71.21 O ANISOU 629 O ALA A 101 6516 10139 10403 -962 44 1098 O ATOM 630 CB ALA A 101 0.516 -33.687 42.463 1.00 68.11 C ANISOU 630 CB ALA A 101 6382 9612 9884 -1101 44 830 C ATOM 631 N TYR A 102 -2.486 -34.409 43.175 1.00 68.07 N ANISOU 631 N TYR A 102 6233 9636 9993 -1041 -35 1051 N ATOM 632 CA TYR A 102 -3.714 -34.192 43.945 1.00 68.06 C ANISOU 632 CA TYR A 102 6159 9701 9999 -976 -48 1172 C ATOM 633 C TYR A 102 -4.343 -35.528 44.369 1.00 72.16 C ANISOU 633 C TYR A 102 6552 10211 10655 -966 -67 1299 C ATOM 634 O TYR A 102 -5.030 -35.569 45.388 1.00 72.00 O ANISOU 634 O TYR A 102 6435 10269 10652 -885 -54 1423 O ATOM 635 CB TYR A 102 -4.744 -33.349 43.166 1.00 69.27 C ANISOU 635 CB TYR A 102 6376 9834 10109 -996 -90 1172 C ATOM 636 CG TYR A 102 -4.361 -31.901 42.941 1.00 70.68 C ANISOU 636 CG TYR A 102 6664 10036 10156 -987 -70 1077 C ATOM 637 CD1 TYR A 102 -4.213 -31.023 44.012 1.00 72.60 C ANISOU 637 CD1 TYR A 102 6910 10365 10309 -901 -31 1090 C ATOM 638 CD2 TYR A 102 -4.272 -31.376 41.655 1.00 71.29 C ANISOU 638 CD2 TYR A 102 6844 10046 10197 -1057 -94 982 C ATOM 639 CE1 TYR A 102 -3.890 -29.682 43.810 1.00 73.21 C ANISOU 639 CE1 TYR A 102 7094 10451 10273 -897 -21 1004 C ATOM 640 CE2 TYR A 102 -3.950 -30.037 41.439 1.00 71.87 C ANISOU 640 CE2 TYR A 102 7010 10137 10161 -1049 -76 905 C ATOM 641 CZ TYR A 102 -3.764 -29.191 42.520 1.00 79.32 C ANISOU 641 CZ TYR A 102 7957 11156 11025 -973 -42 916 C ATOM 642 OH TYR A 102 -3.456 -27.869 42.312 1.00 80.20 O ANISOU 642 OH TYR A 102 8166 11272 11036 -969 -33 840 O ATOM 643 N PHE A 103 -4.105 -36.613 43.593 1.00 68.75 N ANISOU 643 N PHE A 103 6124 9679 10320 -1040 -98 1271 N ATOM 644 CA PHE A 103 -4.609 -37.965 43.869 1.00 69.04 C ANISOU 644 CA PHE A 103 6049 9680 10503 -1047 -126 1382 C ATOM 645 C PHE A 103 -4.000 -38.508 45.168 1.00 72.33 C ANISOU 645 C PHE A 103 6356 10176 10951 -974 -60 1448 C ATOM 646 O PHE A 103 -4.712 -39.106 45.977 1.00 72.29 O ANISOU 646 O PHE A 103 6222 10213 11031 -924 -63 1592 O ATOM 647 CB PHE A 103 -4.294 -38.906 42.692 1.00 71.17 C ANISOU 647 CB PHE A 103 6384 9811 10846 -1141 -171 1307 C ATOM 648 CG PHE A 103 -5.023 -40.228 42.697 1.00 73.52 C ANISOU 648 CG PHE A 103 6594 10039 11303 -1171 -231 1412 C ATOM 649 CD1 PHE A 103 -6.265 -40.358 42.087 1.00 77.15 C ANISOU 649 CD1 PHE A 103 7049 10441 11823 -1223 -328 1475 C ATOM 650 CD2 PHE A 103 -4.447 -41.357 43.269 1.00 75.96 C ANISOU 650 CD2 PHE A 103 6824 10331 11707 -1155 -197 1452 C ATOM 651 CE1 PHE A 103 -6.932 -41.586 42.075 1.00 78.95 C ANISOU 651 CE1 PHE A 103 7196 10593 12211 -1262 -399 1578 C ATOM 652 CE2 PHE A 103 -5.117 -42.584 43.261 1.00 79.64 C ANISOU 652 CE2 PHE A 103 7208 10720 12330 -1188 -259 1552 C ATOM 653 CZ PHE A 103 -6.354 -42.691 42.663 1.00 78.33 C ANISOU 653 CZ PHE A 103 7040 10492 12228 -1244 -365 1614 C ATOM 654 N TYR A 104 -2.687 -38.274 45.367 1.00 68.06 N ANISOU 654 N TYR A 104 5858 9660 10341 -966 -1 1354 N ATOM 655 CA TYR A 104 -1.933 -38.683 46.553 1.00 67.71 C ANISOU 655 CA TYR A 104 5722 9697 10308 -902 63 1402 C ATOM 656 C TYR A 104 -2.310 -37.790 47.749 1.00 71.16 C ANISOU 656 C TYR A 104 6116 10266 10656 -801 88 1468 C ATOM 657 O TYR A 104 -2.229 -38.236 48.894 1.00 70.95 O ANISOU 657 O TYR A 104 5980 10322 10656 -725 127 1561 O ATOM 658 CB TYR A 104 -0.420 -38.628 46.259 1.00 68.52 C ANISOU 658 CB TYR A 104 5892 9781 10361 -936 109 1286 C ATOM 659 CG TYR A 104 0.472 -39.130 47.375 1.00 70.27 C ANISOU 659 CG TYR A 104 6019 10081 10599 -883 172 1334 C ATOM 660 CD1 TYR A 104 0.538 -40.486 47.686 1.00 72.68 C ANISOU 660 CD1 TYR A 104 6221 10364 11032 -877 194 1414 C ATOM 661 CD2 TYR A 104 1.318 -38.264 48.059 1.00 70.69 C ANISOU 661 CD2 TYR A 104 6092 10224 10542 -848 206 1295 C ATOM 662 CE1 TYR A 104 1.372 -40.956 48.701 1.00 73.57 C ANISOU 662 CE1 TYR A 104 6240 10555 11160 -828 256 1464 C ATOM 663 CE2 TYR A 104 2.159 -38.722 49.072 1.00 71.66 C ANISOU 663 CE2 TYR A 104 6128 10424 10676 -805 257 1341 C ATOM 664 CZ TYR A 104 2.184 -40.070 49.388 1.00 79.45 C ANISOU 664 CZ TYR A 104 7003 11398 11788 -792 287 1428 C ATOM 665 OH TYR A 104 3.015 -40.526 50.384 1.00 80.58 O ANISOU 665 OH TYR A 104 7053 11624 11941 -748 342 1481 O ATOM 666 N LEU A 105 -2.747 -36.544 47.471 1.00 67.23 N ANISOU 666 N LEU A 105 5709 9786 10051 -792 69 1421 N ATOM 667 CA LEU A 105 -3.187 -35.567 48.468 1.00 67.03 C ANISOU 667 CA LEU A 105 5678 9869 9922 -689 89 1470 C ATOM 668 C LEU A 105 -4.565 -35.954 49.028 1.00 71.88 C ANISOU 668 C LEU A 105 6181 10527 10603 -615 80 1641 C ATOM 669 O LEU A 105 -4.739 -35.963 50.249 1.00 71.70 O ANISOU 669 O LEU A 105 6079 10607 10556 -504 119 1738 O ATOM 670 CB LEU A 105 -3.225 -34.156 47.840 1.00 66.65 C ANISOU 670 CB LEU A 105 5772 9805 9749 -710 70 1365 C ATOM 671 CG LEU A 105 -4.032 -33.073 48.567 1.00 71.52 C ANISOU 671 CG LEU A 105 6411 10503 10261 -607 80 1418 C ATOM 672 CD1 LEU A 105 -3.244 -32.453 49.704 1.00 71.69 C ANISOU 672 CD1 LEU A 105 6458 10609 10170 -528 114 1385 C ATOM 673 CD2 LEU A 105 -4.474 -32.006 47.607 1.00 73.82 C ANISOU 673 CD2 LEU A 105 6819 10746 10484 -648 52 1348 C ATOM 674 N MET A 106 -5.536 -36.260 48.134 1.00 69.08 N ANISOU 674 N MET A 106 5819 10098 10331 -675 26 1685 N ATOM 675 CA MET A 106 -6.913 -36.638 48.488 1.00 69.68 C ANISOU 675 CA MET A 106 5782 10204 10490 -622 4 1866 C ATOM 676 C MET A 106 -6.959 -37.990 49.207 1.00 73.94 C ANISOU 676 C MET A 106 6164 10759 11170 -594 17 1995 C ATOM 677 O MET A 106 -7.872 -38.225 49.998 1.00 74.02 O ANISOU 677 O MET A 106 6054 10841 11230 -505 28 2169 O ATOM 678 CB MET A 106 -7.822 -36.679 47.244 1.00 72.30 C ANISOU 678 CB MET A 106 6149 10440 10882 -717 -73 1874 C ATOM 679 CG MET A 106 -8.071 -35.319 46.610 1.00 75.75 C ANISOU 679 CG MET A 106 6715 10877 11190 -726 -81 1790 C ATOM 680 SD MET A 106 -8.935 -34.140 47.675 1.00 80.32 S ANISOU 680 SD MET A 106 7278 11587 11652 -570 -28 1904 S ATOM 681 CE MET A 106 -8.882 -32.701 46.649 1.00 76.51 C ANISOU 681 CE MET A 106 6969 11065 11036 -620 -42 1758 C ATOM 682 N PHE A 107 -5.977 -38.868 48.943 1.00 70.31 N ANISOU 682 N PHE A 107 5703 10237 10776 -662 21 1920 N ATOM 683 CA PHE A 107 -5.889 -40.177 49.585 1.00 70.63 C ANISOU 683 CA PHE A 107 5599 10282 10954 -641 38 2031 C ATOM 684 C PHE A 107 -5.346 -40.041 51.018 1.00 74.23 C ANISOU 684 C PHE A 107 5982 10876 11346 -517 119 2083 C ATOM 685 O PHE A 107 -5.537 -40.948 51.831 1.00 74.30 O ANISOU 685 O PHE A 107 5845 10931 11456 -460 145 2220 O ATOM 686 CB PHE A 107 -5.004 -41.121 48.757 1.00 72.43 C ANISOU 686 CB PHE A 107 5867 10389 11264 -749 22 1930 C ATOM 687 CG PHE A 107 -5.544 -42.527 48.646 1.00 74.82 C ANISOU 687 CG PHE A 107 6058 10614 11756 -788 -21 2044 C ATOM 688 CD1 PHE A 107 -6.386 -42.885 47.599 1.00 78.43 C ANISOU 688 CD1 PHE A 107 6547 10952 12302 -880 -116 2056 C ATOM 689 CD2 PHE A 107 -5.208 -43.495 49.585 1.00 77.38 C ANISOU 689 CD2 PHE A 107 6247 10981 12175 -734 28 2144 C ATOM 690 CE1 PHE A 107 -6.887 -44.186 47.496 1.00 80.22 C ANISOU 690 CE1 PHE A 107 6676 11091 12711 -924 -171 2162 C ATOM 691 CE2 PHE A 107 -5.710 -44.796 49.482 1.00 81.04 C ANISOU 691 CE2 PHE A 107 6605 11361 12824 -773 -15 2254 C ATOM 692 CZ PHE A 107 -6.545 -45.133 48.437 1.00 79.64 C ANISOU 692 CZ PHE A 107 6468 11055 12737 -870 -119 2261 C ATOM 693 N ASN A 108 -4.687 -38.899 51.324 1.00 70.00 N ANISOU 693 N ASN A 108 5549 10405 10643 -477 152 1976 N ATOM 694 CA ASN A 108 -4.097 -38.607 52.631 1.00 69.61 C ANISOU 694 CA ASN A 108 5463 10483 10503 -365 214 1998 C ATOM 695 C ASN A 108 -4.689 -37.314 53.251 1.00 73.01 C ANISOU 695 C ASN A 108 5954 11006 10781 -254 226 2018 C ATOM 696 O ASN A 108 -3.952 -36.519 53.844 1.00 72.26 O ANISOU 696 O ASN A 108 5933 10973 10548 -205 250 1937 O ATOM 697 CB ASN A 108 -2.574 -38.500 52.505 1.00 69.87 C ANISOU 697 CB ASN A 108 5570 10500 10477 -423 235 1850 C ATOM 698 CG ASN A 108 -1.901 -39.813 52.203 1.00 93.41 C ANISOU 698 CG ASN A 108 8481 13417 13594 -493 249 1854 C ATOM 699 OD1 ASN A 108 -1.639 -40.624 53.096 1.00 88.10 O ANISOU 699 OD1 ASN A 108 7685 12806 12983 -436 292 1948 O ATOM 700 ND2 ASN A 108 -1.590 -40.045 50.937 1.00 85.34 N ANISOU 700 ND2 ASN A 108 7541 12269 12616 -609 217 1754 N ATOM 701 N THR A 109 -6.024 -37.127 53.145 1.00 69.70 N ANISOU 701 N THR A 109 5500 10593 10389 -210 208 2135 N ATOM 702 CA THR A 109 -6.708 -35.960 53.718 1.00 69.62 C ANISOU 702 CA THR A 109 5546 10666 10239 -88 229 2175 C ATOM 703 C THR A 109 -7.695 -36.419 54.818 1.00 73.85 C ANISOU 703 C THR A 109 5930 11309 10821 65 270 2399 C ATOM 704 O THR A 109 -8.143 -37.569 54.811 1.00 73.71 O ANISOU 704 O THR A 109 5765 11273 10969 45 261 2532 O ATOM 705 CB THR A 109 -7.395 -35.099 52.631 1.00 77.53 C ANISOU 705 CB THR A 109 6656 11597 11203 -150 186 2122 C ATOM 706 OG1 THR A 109 -7.757 -33.840 53.199 1.00 77.59 O ANISOU 706 OG1 THR A 109 6752 11680 11050 -32 216 2122 O ATOM 707 CG2 THR A 109 -8.624 -35.764 52.003 1.00 76.27 C ANISOU 707 CG2 THR A 109 6400 11387 11191 -192 143 2264 C ATOM 708 N GLY A 110 -7.997 -35.513 55.749 1.00 70.51 N ANISOU 708 N GLY A 110 5549 10991 10250 220 315 2439 N ATOM 709 CA GLY A 110 -8.904 -35.762 56.864 1.00 71.05 C ANISOU 709 CA GLY A 110 5492 11178 10327 397 368 2654 C ATOM 710 C GLY A 110 -8.296 -36.645 57.938 1.00 74.80 C ANISOU 710 C GLY A 110 5846 11736 10840 469 412 2720 C ATOM 711 O GLY A 110 -7.325 -36.236 58.582 1.00 74.11 O ANISOU 711 O GLY A 110 5833 11699 10625 511 433 2612 O ATOM 712 N PRO A 111 -8.830 -37.873 58.159 1.00 71.67 N ANISOU 712 N PRO A 111 5258 11352 10623 482 421 2903 N ATOM 713 CA PRO A 111 -8.250 -38.743 59.200 1.00 71.70 C ANISOU 713 CA PRO A 111 5134 11439 10668 557 470 2976 C ATOM 714 C PRO A 111 -6.937 -39.403 58.764 1.00 74.71 C ANISOU 714 C PRO A 111 5530 11746 11111 409 449 2826 C ATOM 715 O PRO A 111 -6.162 -39.820 59.626 1.00 74.53 O ANISOU 715 O PRO A 111 5449 11798 11069 464 492 2833 O ATOM 716 CB PRO A 111 -9.339 -39.789 59.440 1.00 74.25 C ANISOU 716 CB PRO A 111 5247 11784 11179 608 481 3230 C ATOM 717 CG PRO A 111 -10.091 -39.854 58.169 1.00 78.62 C ANISOU 717 CG PRO A 111 5817 12210 11844 470 406 3234 C ATOM 718 CD PRO A 111 -9.989 -38.513 57.499 1.00 73.62 C ANISOU 718 CD PRO A 111 5390 11537 11045 430 382 3060 C ATOM 719 N ASN A 112 -6.685 -39.490 57.439 1.00 70.34 N ANISOU 719 N ASN A 112 5054 11049 10624 230 388 2697 N ATOM 720 CA ASN A 112 -5.474 -40.086 56.866 1.00 69.38 C ANISOU 720 CA ASN A 112 4961 10843 10559 91 373 2557 C ATOM 721 C ASN A 112 -4.275 -39.112 56.920 1.00 72.17 C ANISOU 721 C ASN A 112 5472 11214 10737 70 378 2363 C ATOM 722 O ASN A 112 -3.149 -39.523 56.626 1.00 71.17 O ANISOU 722 O ASN A 112 5362 11042 10636 -21 380 2261 O ATOM 723 CB ASN A 112 -5.726 -40.539 55.423 1.00 69.56 C ANISOU 723 CB ASN A 112 5015 10706 10708 -73 306 2502 C ATOM 724 CG ASN A 112 -6.586 -41.775 55.291 1.00 91.51 C ANISOU 724 CG ASN A 112 7636 13439 13695 -94 282 2674 C ATOM 725 OD1 ASN A 112 -7.557 -41.985 56.028 1.00 87.43 O ANISOU 725 OD1 ASN A 112 6990 13001 13229 17 300 2869 O ATOM 726 ND2 ASN A 112 -6.269 -42.607 54.311 1.00 82.31 N ANISOU 726 ND2 ASN A 112 6482 12137 12656 -235 236 2611 N ATOM 727 N THR A 113 -4.514 -37.840 57.314 1.00 68.63 N ANISOU 727 N THR A 113 5134 10827 10115 158 381 2322 N ATOM 728 CA THR A 113 -3.481 -36.806 57.462 1.00 68.01 C ANISOU 728 CA THR A 113 5208 10766 9867 146 372 2153 C ATOM 729 C THR A 113 -2.586 -37.163 58.663 1.00 72.06 C ANISOU 729 C THR A 113 5658 11386 10337 222 412 2174 C ATOM 730 O THR A 113 -1.374 -36.949 58.607 1.00 71.42 O ANISOU 730 O THR A 113 5643 11293 10202 151 398 2047 O ATOM 731 CB THR A 113 -4.125 -35.410 57.608 1.00 76.12 C ANISOU 731 CB THR A 113 6369 11822 10731 231 362 2122 C ATOM 732 OG1 THR A 113 -5.119 -35.233 56.600 1.00 75.33 O ANISOU 732 OG1 THR A 113 6289 11641 10690 176 334 2146 O ATOM 733 CG2 THR A 113 -3.108 -34.274 57.521 1.00 74.48 C ANISOU 733 CG2 THR A 113 6335 11597 10367 187 331 1934 C ATOM 734 N ARG A 114 -3.191 -37.734 59.728 1.00 69.12 N ANISOU 734 N ARG A 114 5147 11121 9993 366 460 2348 N ATOM 735 CA ARG A 114 -2.531 -38.172 60.962 1.00 69.25 C ANISOU 735 CA ARG A 114 5080 11258 9975 463 504 2404 C ATOM 736 C ARG A 114 -1.569 -39.346 60.682 1.00 72.09 C ANISOU 736 C ARG A 114 5338 11575 10479 349 516 2391 C ATOM 737 O ARG A 114 -0.525 -39.444 61.330 1.00 71.69 O ANISOU 737 O ARG A 114 5276 11588 10373 360 533 2353 O ATOM 738 CB ARG A 114 -3.593 -38.573 62.001 1.00 71.09 C ANISOU 738 CB ARG A 114 5176 11607 10228 648 558 2617 C ATOM 739 CG ARG A 114 -3.068 -38.763 63.424 1.00 84.38 C ANISOU 739 CG ARG A 114 6795 13439 11826 791 606 2680 C ATOM 740 CD ARG A 114 -4.178 -39.081 64.415 1.00 98.54 C ANISOU 740 CD ARG A 114 8457 15353 13629 992 667 2902 C ATOM 741 NE ARG A 114 -4.837 -40.361 64.136 1.00110.31 N ANISOU 741 NE ARG A 114 9748 16813 15352 964 691 3075 N ATOM 742 CZ ARG A 114 -4.462 -41.531 64.648 1.00126.74 C ANISOU 742 CZ ARG A 114 11657 18941 17559 976 732 3180 C ATOM 743 NH1 ARG A 114 -3.426 -41.602 65.474 1.00115.46 N ANISOU 743 NH1 ARG A 114 10224 17601 16044 1019 758 3134 N ATOM 744 NH2 ARG A 114 -5.121 -42.639 64.335 1.00113.83 N1+ ANISOU 744 NH2 ARG A 114 9850 17259 16140 943 742 3336 N1+ ATOM 745 N ARG A 115 -1.919 -40.214 59.704 1.00 67.91 N ANISOU 745 N ARG A 115 4742 10933 10126 241 505 2423 N ATOM 746 CA ARG A 115 -1.134 -41.379 59.280 1.00 67.25 C ANISOU 746 CA ARG A 115 4576 10784 10191 134 519 2415 C ATOM 747 C ARG A 115 0.194 -40.987 58.610 1.00 69.89 C ANISOU 747 C ARG A 115 5036 11054 10465 8 498 2230 C ATOM 748 O ARG A 115 1.126 -41.795 58.603 1.00 69.54 O ANISOU 748 O ARG A 115 4930 10997 10494 -44 528 2224 O ATOM 749 CB ARG A 115 -1.947 -42.247 58.308 1.00 67.72 C ANISOU 749 CB ARG A 115 4573 10720 10436 51 494 2478 C ATOM 750 CG ARG A 115 -2.660 -43.415 58.970 1.00 79.72 C ANISOU 750 CG ARG A 115 5892 12284 12113 129 529 2687 C ATOM 751 CD ARG A 115 -3.389 -44.260 57.944 1.00 90.87 C ANISOU 751 CD ARG A 115 7260 13554 13714 25 482 2736 C ATOM 752 NE ARG A 115 -3.849 -45.532 58.504 1.00101.20 N ANISOU 752 NE ARG A 115 8368 14881 15201 74 510 2929 N ATOM 753 CZ ARG A 115 -3.175 -46.676 58.426 1.00116.05 C ANISOU 753 CZ ARG A 115 10169 16709 17214 17 533 2941 C ATOM 754 NH1 ARG A 115 -2.001 -46.723 57.806 1.00103.34 N ANISOU 754 NH1 ARG A 115 8663 15029 15573 -84 538 2777 N ATOM 755 NH2 ARG A 115 -3.671 -47.782 58.963 1.00103.49 N1+ ANISOU 755 NH2 ARG A 115 8393 15136 15792 66 556 3127 N1+ ATOM 756 N LEU A 116 0.272 -39.768 58.040 1.00 65.37 N ANISOU 756 N LEU A 116 4631 10441 9766 -36 451 2093 N ATOM 757 CA LEU A 116 1.459 -39.255 57.350 1.00 64.31 C ANISOU 757 CA LEU A 116 4618 10245 9573 -152 427 1930 C ATOM 758 C LEU A 116 2.617 -38.982 58.306 1.00 67.71 C ANISOU 758 C LEU A 116 5048 10775 9902 -118 441 1901 C ATOM 759 O LEU A 116 2.415 -38.451 59.401 1.00 67.70 O ANISOU 759 O LEU A 116 5049 10886 9788 0 442 1939 O ATOM 760 CB LEU A 116 1.136 -37.958 56.586 1.00 64.00 C ANISOU 760 CB LEU A 116 4747 10144 9426 -194 372 1811 C ATOM 761 CG LEU A 116 0.200 -38.050 55.383 1.00 68.41 C ANISOU 761 CG LEU A 116 5338 10587 10066 -262 343 1804 C ATOM 762 CD1 LEU A 116 -0.439 -36.714 55.105 1.00 68.41 C ANISOU 762 CD1 LEU A 116 5471 10578 9942 -241 305 1741 C ATOM 763 CD2 LEU A 116 0.928 -38.554 54.144 1.00 70.52 C ANISOU 763 CD2 LEU A 116 5645 10731 10418 -404 333 1712 C ATOM 764 N THR A 117 3.834 -39.333 57.865 1.00 63.52 N ANISOU 764 N THR A 117 4521 10203 9409 -219 450 1836 N ATOM 765 CA THR A 117 5.091 -39.096 58.579 1.00 63.22 C ANISOU 765 CA THR A 117 4484 10246 9292 -220 452 1805 C ATOM 766 C THR A 117 5.677 -37.762 58.084 1.00 66.37 C ANISOU 766 C THR A 117 5051 10603 9565 -292 388 1659 C ATOM 767 O THR A 117 5.093 -37.139 57.194 1.00 65.51 O ANISOU 767 O THR A 117 5045 10407 9440 -333 355 1589 O ATOM 768 CB THR A 117 6.062 -40.282 58.395 1.00 70.40 C ANISOU 768 CB THR A 117 5285 11137 10326 -282 507 1846 C ATOM 769 OG1 THR A 117 6.242 -40.543 57.003 1.00 68.94 O ANISOU 769 OG1 THR A 117 5157 10813 10226 -396 507 1777 O ATOM 770 CG2 THR A 117 5.597 -41.545 59.113 1.00 69.40 C ANISOU 770 CG2 THR A 117 4983 11069 10317 -199 570 2000 C ATOM 771 N VAL A 118 6.816 -37.323 58.661 1.00 62.92 N ANISOU 771 N VAL A 118 4637 10227 9043 -309 365 1621 N ATOM 772 CA VAL A 118 7.503 -36.069 58.311 1.00 62.56 C ANISOU 772 CA VAL A 118 4737 10145 8886 -382 294 1496 C ATOM 773 C VAL A 118 7.933 -36.108 56.823 1.00 65.53 C ANISOU 773 C VAL A 118 5164 10392 9341 -514 297 1424 C ATOM 774 O VAL A 118 7.730 -35.125 56.106 1.00 64.69 O ANISOU 774 O VAL A 118 5185 10216 9178 -560 249 1330 O ATOM 775 CB VAL A 118 8.712 -35.798 59.258 1.00 66.98 C ANISOU 775 CB VAL A 118 5285 10797 9366 -385 262 1494 C ATOM 776 CG1 VAL A 118 9.428 -34.495 58.903 1.00 66.85 C ANISOU 776 CG1 VAL A 118 5415 10735 9249 -470 175 1375 C ATOM 777 CG2 VAL A 118 8.275 -35.778 60.722 1.00 67.45 C ANISOU 777 CG2 VAL A 118 5305 10989 9335 -242 260 1563 C ATOM 778 N SER A 119 8.479 -37.254 56.367 1.00 61.89 N ANISOU 778 N SER A 119 4607 9901 9009 -562 358 1473 N ATOM 779 CA SER A 119 8.950 -37.465 54.996 1.00 61.28 C ANISOU 779 CA SER A 119 4573 9707 9006 -667 375 1418 C ATOM 780 C SER A 119 7.796 -37.512 53.979 1.00 64.86 C ANISOU 780 C SER A 119 5083 10057 9504 -679 370 1385 C ATOM 781 O SER A 119 7.914 -36.904 52.914 1.00 64.36 O ANISOU 781 O SER A 119 5126 9907 9422 -749 344 1297 O ATOM 782 CB SER A 119 9.763 -38.753 54.905 1.00 64.85 C ANISOU 782 CB SER A 119 4909 10156 9574 -690 450 1492 C ATOM 783 OG SER A 119 9.006 -39.881 55.312 1.00 73.67 O ANISOU 783 OG SER A 119 5913 11290 10786 -623 500 1587 O ATOM 784 N THR A 120 6.697 -38.234 54.300 1.00 61.19 N ANISOU 784 N THR A 120 4543 9603 9104 -611 392 1464 N ATOM 785 CA THR A 120 5.533 -38.392 53.415 1.00 60.65 C ANISOU 785 CA THR A 120 4510 9442 9093 -624 378 1455 C ATOM 786 C THR A 120 4.713 -37.093 53.315 1.00 64.06 C ANISOU 786 C THR A 120 5054 9873 9413 -603 321 1396 C ATOM 787 O THR A 120 4.075 -36.873 52.283 1.00 63.41 O ANISOU 787 O THR A 120 5041 9701 9350 -648 297 1350 O ATOM 788 CB THR A 120 4.634 -39.552 53.865 1.00 69.22 C ANISOU 788 CB THR A 120 5465 10543 10293 -561 410 1579 C ATOM 789 OG1 THR A 120 4.238 -39.352 55.220 1.00 69.69 O ANISOU 789 OG1 THR A 120 5454 10730 10293 -449 416 1662 O ATOM 790 CG2 THR A 120 5.301 -40.914 53.702 1.00 67.80 C ANISOU 790 CG2 THR A 120 5189 10329 10243 -592 467 1631 C ATOM 791 N TRP A 121 4.722 -36.245 54.372 1.00 60.57 N ANISOU 791 N TRP A 121 4634 9528 8850 -530 298 1398 N ATOM 792 CA TRP A 121 4.015 -34.956 54.374 1.00 60.24 C ANISOU 792 CA TRP A 121 4710 9487 8691 -496 250 1342 C ATOM 793 C TRP A 121 4.671 -34.014 53.373 1.00 63.35 C ANISOU 793 C TRP A 121 5235 9801 9035 -598 210 1215 C ATOM 794 O TRP A 121 3.972 -33.356 52.601 1.00 62.62 O ANISOU 794 O TRP A 121 5230 9645 8917 -619 185 1165 O ATOM 795 CB TRP A 121 4.004 -34.326 55.777 1.00 59.50 C ANISOU 795 CB TRP A 121 4625 9510 8471 -386 235 1368 C ATOM 796 CG TRP A 121 3.021 -33.202 55.942 1.00 60.62 C ANISOU 796 CG TRP A 121 4874 9660 8500 -314 203 1344 C ATOM 797 CD1 TRP A 121 1.765 -33.286 56.465 1.00 63.85 C ANISOU 797 CD1 TRP A 121 5245 10116 8898 -195 226 1440 C ATOM 798 CD2 TRP A 121 3.217 -31.825 55.588 1.00 60.41 C ANISOU 798 CD2 TRP A 121 5006 9589 8358 -348 148 1227 C ATOM 799 NE1 TRP A 121 1.169 -32.047 56.470 1.00 63.44 N ANISOU 799 NE1 TRP A 121 5325 10057 8723 -147 194 1389 N ATOM 800 CE2 TRP A 121 2.032 -31.133 55.925 1.00 64.60 C ANISOU 800 CE2 TRP A 121 5597 10143 8805 -242 145 1253 C ATOM 801 CE3 TRP A 121 4.279 -31.105 55.014 1.00 61.45 C ANISOU 801 CE3 TRP A 121 5230 9663 8453 -456 103 1114 C ATOM 802 CZ2 TRP A 121 1.879 -29.759 55.707 1.00 64.00 C ANISOU 802 CZ2 TRP A 121 5679 10029 8610 -241 99 1159 C ATOM 803 CZ3 TRP A 121 4.120 -29.748 54.785 1.00 62.97 C ANISOU 803 CZ3 TRP A 121 5571 9816 8537 -462 51 1024 C ATOM 804 CH2 TRP A 121 2.938 -29.086 55.141 1.00 63.88 C ANISOU 804 CH2 TRP A 121 5752 9951 8568 -355 50 1041 C ATOM 805 N LEU A 122 6.022 -33.971 53.382 1.00 59.63 N ANISOU 805 N LEU A 122 4767 9335 8555 -661 207 1175 N ATOM 806 CA LEU A 122 6.846 -33.164 52.481 1.00 59.09 C ANISOU 806 CA LEU A 122 4799 9198 8455 -759 175 1076 C ATOM 807 C LEU A 122 6.747 -33.684 51.044 1.00 62.37 C ANISOU 807 C LEU A 122 5228 9506 8963 -832 202 1050 C ATOM 808 O LEU A 122 6.978 -32.919 50.107 1.00 61.73 O ANISOU 808 O LEU A 122 5244 9358 8853 -895 177 971 O ATOM 809 CB LEU A 122 8.317 -33.156 52.943 1.00 59.38 C ANISOU 809 CB LEU A 122 4805 9279 8478 -801 168 1078 C ATOM 810 CG LEU A 122 8.645 -32.387 54.231 1.00 64.58 C ANISOU 810 CG LEU A 122 5487 10028 9021 -752 113 1074 C ATOM 811 CD1 LEU A 122 9.959 -32.854 54.822 1.00 65.06 C ANISOU 811 CD1 LEU A 122 5465 10151 9104 -784 120 1120 C ATOM 812 CD2 LEU A 122 8.680 -30.881 53.996 1.00 67.05 C ANISOU 812 CD2 LEU A 122 5948 10299 9227 -784 35 975 C ATOM 813 N LEU A 123 6.393 -34.977 50.874 1.00 58.78 N ANISOU 813 N LEU A 123 4683 9032 8620 -820 251 1117 N ATOM 814 CA LEU A 123 6.231 -35.615 49.571 1.00 58.37 C ANISOU 814 CA LEU A 123 4651 8872 8654 -878 271 1094 C ATOM 815 C LEU A 123 4.949 -35.113 48.888 1.00 62.14 C ANISOU 815 C LEU A 123 5202 9294 9114 -878 232 1061 C ATOM 816 O LEU A 123 5.041 -34.625 47.762 1.00 61.43 O ANISOU 816 O LEU A 123 5205 9127 9006 -938 216 984 O ATOM 817 CB LEU A 123 6.224 -37.154 49.700 1.00 58.59 C ANISOU 817 CB LEU A 123 4566 8889 8806 -862 324 1177 C ATOM 818 CG LEU A 123 6.151 -37.975 48.400 1.00 63.30 C ANISOU 818 CG LEU A 123 5194 9364 9492 -917 342 1151 C ATOM 819 CD1 LEU A 123 7.454 -37.894 47.609 1.00 63.51 C ANISOU 819 CD1 LEU A 123 5276 9347 9509 -974 374 1095 C ATOM 820 CD2 LEU A 123 5.833 -39.425 48.697 1.00 66.06 C ANISOU 820 CD2 LEU A 123 5436 9699 9966 -890 378 1241 C ATOM 821 N ARG A 124 3.773 -35.203 49.565 1.00 58.91 N ANISOU 821 N ARG A 124 4747 8929 8708 -806 221 1131 N ATOM 822 CA ARG A 124 2.496 -34.754 48.990 1.00 58.70 C ANISOU 822 CA ARG A 124 4773 8860 8669 -801 186 1125 C ATOM 823 C ARG A 124 2.499 -33.232 48.774 1.00 62.17 C ANISOU 823 C ARG A 124 5336 9301 8984 -808 151 1039 C ATOM 824 O ARG A 124 1.976 -32.770 47.761 1.00 61.61 O ANISOU 824 O ARG A 124 5342 9163 8905 -850 128 991 O ATOM 825 CB ARG A 124 1.269 -35.184 49.830 1.00 59.61 C ANISOU 825 CB ARG A 124 4796 9032 8819 -712 188 1245 C ATOM 826 CG ARG A 124 1.090 -34.555 51.214 1.00 70.66 C ANISOU 826 CG ARG A 124 6175 10549 10122 -603 195 1294 C ATOM 827 CD ARG A 124 -0.377 -34.605 51.605 1.00 80.62 C ANISOU 827 CD ARG A 124 7387 11846 11399 -517 193 1404 C ATOM 828 NE ARG A 124 -0.640 -34.055 52.937 1.00 90.21 N ANISOU 828 NE ARG A 124 8588 13175 12513 -388 208 1461 N ATOM 829 CZ ARG A 124 -0.930 -32.781 53.188 1.00105.14 C ANISOU 829 CZ ARG A 124 10588 15092 14268 -335 190 1416 C ATOM 830 NH1 ARG A 124 -0.965 -31.893 52.202 1.00 92.78 N ANISOU 830 NH1 ARG A 124 9143 13451 12658 -406 158 1315 N ATOM 831 NH2 ARG A 124 -1.170 -32.382 54.429 1.00 92.74 N1+ ANISOU 831 NH2 ARG A 124 9014 13623 12602 -204 206 1471 N1+ ATOM 832 N GLN A 125 3.121 -32.472 49.697 1.00 58.48 N ANISOU 832 N GLN A 125 4891 8905 8423 -772 144 1019 N ATOM 833 CA GLN A 125 3.222 -31.017 49.617 1.00 58.00 C ANISOU 833 CA GLN A 125 4951 8840 8246 -777 105 938 C ATOM 834 C GLN A 125 4.232 -30.611 48.533 1.00 60.98 C ANISOU 834 C GLN A 125 5399 9144 8627 -881 94 847 C ATOM 835 O GLN A 125 4.036 -29.593 47.870 1.00 60.50 O ANISOU 835 O GLN A 125 5437 9039 8512 -910 66 781 O ATOM 836 CB GLN A 125 3.613 -30.430 50.986 1.00 59.72 C ANISOU 836 CB GLN A 125 5178 9148 8365 -707 87 946 C ATOM 837 CG GLN A 125 3.309 -28.941 51.149 1.00 74.08 C ANISOU 837 CG GLN A 125 7127 10964 10056 -678 43 881 C ATOM 838 CD GLN A 125 1.841 -28.623 51.015 1.00 92.72 C ANISOU 838 CD GLN A 125 9516 13320 12393 -608 51 918 C ATOM 839 OE1 GLN A 125 1.018 -28.967 51.871 1.00 88.29 O ANISOU 839 OE1 GLN A 125 8899 12826 11821 -502 74 1010 O ATOM 840 NE2 GLN A 125 1.486 -27.955 49.931 1.00 84.40 N ANISOU 840 NE2 GLN A 125 8544 12192 11332 -662 36 861 N ATOM 841 N GLY A 126 5.275 -31.425 48.358 1.00 56.80 N ANISOU 841 N GLY A 126 4811 8605 8164 -927 123 857 N ATOM 842 CA GLY A 126 6.319 -31.215 47.360 1.00 56.12 C ANISOU 842 CA GLY A 126 4771 8458 8093 -1012 127 797 C ATOM 843 C GLY A 126 5.852 -31.442 45.936 1.00 58.67 C ANISOU 843 C GLY A 126 5142 8689 8460 -1055 138 762 C ATOM 844 O GLY A 126 6.197 -30.659 45.049 1.00 57.99 O ANISOU 844 O GLY A 126 5137 8554 8341 -1103 125 698 O ATOM 845 N LEU A 127 5.053 -32.513 45.711 1.00 54.55 N ANISOU 845 N LEU A 127 4571 8141 8015 -1037 157 806 N ATOM 846 CA LEU A 127 4.495 -32.882 44.400 1.00 54.00 C ANISOU 846 CA LEU A 127 4550 7980 7990 -1076 154 776 C ATOM 847 C LEU A 127 3.535 -31.806 43.872 1.00 57.51 C ANISOU 847 C LEU A 127 5079 8403 8370 -1080 112 734 C ATOM 848 O LEU A 127 3.453 -31.604 42.660 1.00 57.06 O ANISOU 848 O LEU A 127 5094 8276 8310 -1125 104 679 O ATOM 849 CB LEU A 127 3.761 -34.236 44.472 1.00 54.15 C ANISOU 849 CB LEU A 127 4492 7974 8107 -1058 163 844 C ATOM 850 CG LEU A 127 4.620 -35.498 44.628 1.00 58.90 C ANISOU 850 CG LEU A 127 5023 8564 8792 -1061 213 881 C ATOM 851 CD1 LEU A 127 3.818 -36.629 45.233 1.00 59.30 C ANISOU 851 CD1 LEU A 127 4973 8623 8936 -1024 214 972 C ATOM 852 CD2 LEU A 127 5.237 -35.931 43.307 1.00 61.27 C ANISOU 852 CD2 LEU A 127 5393 8768 9120 -1110 235 823 C ATOM 853 N ILE A 128 2.822 -31.120 44.786 1.00 53.76 N ANISOU 853 N ILE A 128 4597 7991 7838 -1025 90 763 N ATOM 854 CA ILE A 128 1.876 -30.045 44.479 1.00 53.30 C ANISOU 854 CA ILE A 128 4613 7925 7713 -1012 60 740 C ATOM 855 C ILE A 128 2.666 -28.770 44.099 1.00 56.61 C ANISOU 855 C ILE A 128 5128 8329 8052 -1048 47 654 C ATOM 856 O ILE A 128 2.289 -28.088 43.142 1.00 56.17 O ANISOU 856 O ILE A 128 5147 8226 7970 -1078 32 607 O ATOM 857 CB ILE A 128 0.904 -29.829 45.675 1.00 56.67 C ANISOU 857 CB ILE A 128 5000 8428 8105 -920 54 816 C ATOM 858 CG1 ILE A 128 -0.092 -31.012 45.771 1.00 57.41 C ANISOU 858 CG1 ILE A 128 4998 8522 8294 -894 59 916 C ATOM 859 CG2 ILE A 128 0.151 -28.497 45.569 1.00 57.31 C ANISOU 859 CG2 ILE A 128 5170 8512 8092 -891 32 790 C ATOM 860 CD1 ILE A 128 -0.861 -31.126 47.079 1.00 65.91 C ANISOU 860 CD1 ILE A 128 5998 9686 9357 -789 70 1023 C ATOM 861 N ASP A 129 3.763 -28.469 44.830 1.00 52.72 N ANISOU 861 N ASP A 129 4628 7875 7529 -1049 47 640 N ATOM 862 CA ASP A 129 4.625 -27.311 44.566 1.00 52.30 C ANISOU 862 CA ASP A 129 4652 7804 7417 -1091 23 573 C ATOM 863 C ASP A 129 5.380 -27.483 43.242 1.00 55.53 C ANISOU 863 C ASP A 129 5083 8147 7870 -1163 44 536 C ATOM 864 O ASP A 129 5.623 -26.493 42.550 1.00 54.97 O ANISOU 864 O ASP A 129 5083 8039 7761 -1198 28 485 O ATOM 865 CB ASP A 129 5.616 -27.089 45.721 1.00 54.42 C ANISOU 865 CB ASP A 129 4894 8129 7652 -1081 5 582 C ATOM 866 CG ASP A 129 4.990 -26.689 47.048 1.00 64.22 C ANISOU 866 CG ASP A 129 6143 9436 8821 -998 -20 607 C ATOM 867 OD1 ASP A 129 3.742 -26.631 47.128 1.00 64.58 O ANISOU 867 OD1 ASP A 129 6200 9490 8847 -938 -13 632 O ATOM 868 OD2 ASP A 129 5.747 -26.457 48.013 1.00 70.57 O1- ANISOU 868 OD2 ASP A 129 6940 10288 9586 -987 -46 608 O1- ATOM 869 N THR A 130 5.728 -28.740 42.890 1.00 51.72 N ANISOU 869 N THR A 130 4541 7647 7465 -1175 84 565 N ATOM 870 CA THR A 130 6.417 -29.098 41.647 1.00 51.26 C ANISOU 870 CA THR A 130 4506 7526 7444 -1221 115 540 C ATOM 871 C THR A 130 5.459 -28.893 40.462 1.00 54.17 C ANISOU 871 C THR A 130 4946 7834 7803 -1233 104 500 C ATOM 872 O THR A 130 5.851 -28.273 39.474 1.00 53.62 O ANISOU 872 O THR A 130 4939 7726 7710 -1263 109 456 O ATOM 873 CB THR A 130 6.944 -30.550 41.722 1.00 59.81 C ANISOU 873 CB THR A 130 5515 8604 8605 -1214 163 587 C ATOM 874 OG1 THR A 130 7.775 -30.694 42.873 1.00 60.20 O ANISOU 874 OG1 THR A 130 5491 8721 8660 -1202 172 633 O ATOM 875 CG2 THR A 130 7.725 -30.968 40.477 1.00 58.47 C ANISOU 875 CG2 THR A 130 5381 8371 8465 -1241 206 566 C ATOM 876 N SER A 131 4.206 -29.394 40.581 1.00 50.03 N ANISOU 876 N SER A 131 4405 7306 7299 -1208 87 525 N ATOM 877 CA SER A 131 3.162 -29.324 39.554 1.00 49.52 C ANISOU 877 CA SER A 131 4394 7189 7231 -1222 64 502 C ATOM 878 C SER A 131 2.758 -27.881 39.214 1.00 52.71 C ANISOU 878 C SER A 131 4872 7598 7559 -1227 41 463 C ATOM 879 O SER A 131 2.454 -27.607 38.051 1.00 52.15 O ANISOU 879 O SER A 131 4863 7479 7474 -1254 35 425 O ATOM 880 CB SER A 131 1.926 -30.101 39.993 1.00 53.03 C ANISOU 880 CB SER A 131 4785 7642 7722 -1195 41 564 C ATOM 881 OG SER A 131 1.325 -29.549 41.153 1.00 61.26 O ANISOU 881 OG SER A 131 5792 8755 8730 -1144 29 611 O ATOM 882 N LEU A 132 2.744 -26.974 40.218 1.00 48.92 N ANISOU 882 N LEU A 132 4391 7170 7025 -1197 28 471 N ATOM 883 CA LEU A 132 2.388 -25.565 40.029 1.00 48.46 C ANISOU 883 CA LEU A 132 4408 7112 6894 -1195 8 436 C ATOM 884 C LEU A 132 3.445 -24.866 39.165 1.00 52.07 C ANISOU 884 C LEU A 132 4918 7532 7336 -1245 16 380 C ATOM 885 O LEU A 132 3.105 -24.373 38.089 1.00 51.45 O ANISOU 885 O LEU A 132 4893 7414 7240 -1266 16 349 O ATOM 886 CB LEU A 132 2.212 -24.838 41.384 1.00 48.60 C ANISOU 886 CB LEU A 132 4427 7186 6853 -1141 -10 454 C ATOM 887 CG LEU A 132 2.045 -23.303 41.352 1.00 53.23 C ANISOU 887 CG LEU A 132 5103 7764 7359 -1134 -31 412 C ATOM 888 CD1 LEU A 132 0.749 -22.884 40.671 1.00 53.27 C ANISOU 888 CD1 LEU A 132 5146 7752 7342 -1117 -29 422 C ATOM 889 CD2 LEU A 132 2.100 -22.721 42.743 1.00 55.83 C ANISOU 889 CD2 LEU A 132 5449 8140 7625 -1076 -52 420 C ATOM 890 N THR A 133 4.722 -24.869 39.614 1.00 48.69 N ANISOU 890 N THR A 133 4463 7117 6920 -1263 23 379 N ATOM 891 CA THR A 133 5.853 -24.252 38.910 1.00 48.61 C ANISOU 891 CA THR A 133 4482 7079 6910 -1308 30 352 C ATOM 892 C THR A 133 6.102 -24.922 37.547 1.00 52.25 C ANISOU 892 C THR A 133 4953 7494 7407 -1326 71 344 C ATOM 893 O THR A 133 6.714 -24.296 36.683 1.00 51.85 O ANISOU 893 O THR A 133 4938 7416 7347 -1350 84 326 O ATOM 894 CB THR A 133 7.128 -24.260 39.760 1.00 57.75 C ANISOU 894 CB THR A 133 5593 8267 8083 -1325 23 377 C ATOM 895 OG1 THR A 133 7.172 -25.438 40.568 1.00 58.24 O ANISOU 895 OG1 THR A 133 5581 8367 8182 -1298 41 420 O ATOM 896 CG2 THR A 133 7.240 -23.025 40.635 1.00 56.62 C ANISOU 896 CG2 THR A 133 5488 8142 7885 -1327 -33 359 C ATOM 897 N ALA A 134 5.603 -26.162 37.342 1.00 48.69 N ANISOU 897 N ALA A 134 4477 7030 6995 -1310 89 358 N ATOM 898 CA ALA A 134 5.699 -26.860 36.059 1.00 48.56 C ANISOU 898 CA ALA A 134 4493 6959 6999 -1316 120 341 C ATOM 899 C ALA A 134 4.786 -26.182 35.037 1.00 52.41 C ANISOU 899 C ALA A 134 5053 7416 7444 -1324 99 301 C ATOM 900 O ALA A 134 5.189 -25.995 33.892 1.00 51.98 O ANISOU 900 O ALA A 134 5048 7328 7375 -1331 122 275 O ATOM 901 CB ALA A 134 5.333 -28.328 36.218 1.00 49.37 C ANISOU 901 CB ALA A 134 4558 7044 7155 -1301 128 364 C ATOM 902 N SER A 135 3.579 -25.769 35.476 1.00 49.12 N ANISOU 902 N SER A 135 4640 7018 7005 -1315 60 307 N ATOM 903 CA SER A 135 2.587 -25.070 34.658 1.00 49.04 C ANISOU 903 CA SER A 135 4688 6991 6955 -1321 39 285 C ATOM 904 C SER A 135 2.898 -23.570 34.572 1.00 53.20 C ANISOU 904 C SER A 135 5254 7529 7431 -1328 40 263 C ATOM 905 O SER A 135 2.619 -22.954 33.543 1.00 52.76 O ANISOU 905 O SER A 135 5250 7451 7346 -1338 43 238 O ATOM 906 CB SER A 135 1.185 -25.280 35.222 1.00 52.50 C ANISOU 906 CB SER A 135 5101 7449 7397 -1303 4 325 C ATOM 907 OG SER A 135 0.821 -26.650 35.205 1.00 61.38 O ANISOU 907 OG SER A 135 6188 8553 8580 -1305 -8 352 O ATOM 908 N VAL A 136 3.471 -22.990 35.652 1.00 49.98 N ANISOU 908 N VAL A 136 4825 7153 7015 -1322 33 273 N ATOM 909 CA VAL A 136 3.847 -21.573 35.746 1.00 49.99 C ANISOU 909 CA VAL A 136 4865 7153 6976 -1333 21 252 C ATOM 910 C VAL A 136 4.972 -21.286 34.727 1.00 54.59 C ANISOU 910 C VAL A 136 5460 7705 7575 -1365 47 240 C ATOM 911 O VAL A 136 4.851 -20.329 33.959 1.00 54.06 O ANISOU 911 O VAL A 136 5439 7619 7483 -1375 49 221 O ATOM 912 CB VAL A 136 4.237 -21.175 37.202 1.00 53.98 C ANISOU 912 CB VAL A 136 5352 7691 7466 -1320 -8 263 C ATOM 913 CG1 VAL A 136 5.013 -19.862 37.254 1.00 54.02 C ANISOU 913 CG1 VAL A 136 5398 7677 7449 -1348 -32 241 C ATOM 914 CG2 VAL A 136 3.004 -21.096 38.096 1.00 53.77 C ANISOU 914 CG2 VAL A 136 5333 7697 7402 -1268 -25 282 C ATOM 915 N ALA A 137 6.030 -22.132 34.698 1.00 51.83 N ANISOU 915 N ALA A 137 5067 7356 7269 -1373 74 260 N ATOM 916 CA ALA A 137 7.157 -22.000 33.766 1.00 52.04 C ANISOU 916 CA ALA A 137 5094 7362 7316 -1388 111 272 C ATOM 917 C ALA A 137 6.732 -22.321 32.328 1.00 56.53 C ANISOU 917 C ALA A 137 5710 7900 7869 -1371 144 250 C ATOM 918 O ALA A 137 7.298 -21.748 31.396 1.00 56.06 O ANISOU 918 O ALA A 137 5671 7826 7802 -1371 170 255 O ATOM 919 CB ALA A 137 8.303 -22.906 34.183 1.00 52.97 C ANISOU 919 CB ALA A 137 5150 7494 7483 -1389 139 315 C ATOM 920 N ASN A 138 5.738 -23.226 32.152 1.00 53.74 N ANISOU 920 N ASN A 138 5373 7536 7510 -1355 136 232 N ATOM 921 CA ASN A 138 5.200 -23.604 30.841 1.00 54.04 C ANISOU 921 CA ASN A 138 5468 7539 7524 -1341 148 204 C ATOM 922 C ASN A 138 4.460 -22.427 30.212 1.00 59.08 C ANISOU 922 C ASN A 138 6152 8179 8117 -1349 131 184 C ATOM 923 O ASN A 138 4.746 -22.087 29.066 1.00 58.74 O ANISOU 923 O ASN A 138 6149 8121 8050 -1339 158 173 O ATOM 924 CB ASN A 138 4.279 -24.823 30.940 1.00 54.08 C ANISOU 924 CB ASN A 138 5475 7526 7545 -1336 122 197 C ATOM 925 CG ASN A 138 4.939 -26.136 30.601 1.00 74.72 C ANISOU 925 CG ASN A 138 8093 10107 10190 -1317 154 198 C ATOM 926 OD1 ASN A 138 5.565 -26.299 29.548 1.00 69.09 O ANISOU 926 OD1 ASN A 138 7429 9365 9457 -1294 194 183 O ATOM 927 ND2 ASN A 138 4.733 -27.134 31.444 1.00 66.07 N ANISOU 927 ND2 ASN A 138 6951 9011 9141 -1317 140 218 N ATOM 928 N LEU A 139 3.550 -21.779 30.980 1.00 56.50 N ANISOU 928 N LEU A 139 5818 7874 7775 -1357 93 187 N ATOM 929 CA LEU A 139 2.781 -20.605 30.549 1.00 56.77 C ANISOU 929 CA LEU A 139 5891 7913 7766 -1360 81 178 C ATOM 930 C LEU A 139 3.704 -19.410 30.301 1.00 62.23 C ANISOU 930 C LEU A 139 6591 8601 8453 -1369 102 178 C ATOM 931 O LEU A 139 3.414 -18.592 29.426 1.00 61.80 O ANISOU 931 O LEU A 139 6572 8540 8371 -1368 112 170 O ATOM 932 CB LEU A 139 1.705 -20.235 31.584 1.00 56.64 C ANISOU 932 CB LEU A 139 5864 7922 7735 -1350 47 195 C ATOM 933 CG LEU A 139 0.463 -21.132 31.644 1.00 61.36 C ANISOU 933 CG LEU A 139 6449 8526 8339 -1342 21 217 C ATOM 934 CD1 LEU A 139 -0.224 -21.013 32.985 1.00 61.43 C ANISOU 934 CD1 LEU A 139 6425 8570 8347 -1316 1 256 C ATOM 935 CD2 LEU A 139 -0.515 -20.822 30.513 1.00 63.95 C ANISOU 935 CD2 LEU A 139 6818 8846 8635 -1349 10 215 C ATOM 936 N LEU A 140 4.818 -19.325 31.062 1.00 60.18 N ANISOU 936 N LEU A 140 6294 8345 8226 -1382 103 195 N ATOM 937 CA LEU A 140 5.846 -18.291 30.930 1.00 60.89 C ANISOU 937 CA LEU A 140 6379 8426 8332 -1402 109 211 C ATOM 938 C LEU A 140 6.586 -18.476 29.603 1.00 66.71 C ANISOU 938 C LEU A 140 7116 9150 9079 -1389 161 228 C ATOM 939 O LEU A 140 6.830 -17.493 28.904 1.00 66.43 O ANISOU 939 O LEU A 140 7095 9106 9040 -1393 174 240 O ATOM 940 CB LEU A 140 6.824 -18.344 32.125 1.00 61.09 C ANISOU 940 CB LEU A 140 6357 8460 8394 -1424 84 235 C ATOM 941 CG LEU A 140 7.895 -17.248 32.225 1.00 66.16 C ANISOU 941 CG LEU A 140 6986 9087 9066 -1459 66 262 C ATOM 942 CD1 LEU A 140 7.304 -15.932 32.711 1.00 66.33 C ANISOU 942 CD1 LEU A 140 7057 9090 9056 -1472 17 235 C ATOM 943 CD2 LEU A 140 9.000 -17.666 33.170 1.00 69.01 C ANISOU 943 CD2 LEU A 140 7290 9462 9470 -1484 45 299 C ATOM 944 N ALA A 141 6.909 -19.741 29.251 1.00 64.72 N ANISOU 944 N ALA A 141 6856 8897 8838 -1366 193 233 N ATOM 945 CA ALA A 141 7.587 -20.111 28.007 1.00 65.51 C ANISOU 945 CA ALA A 141 6971 8987 8934 -1331 251 251 C ATOM 946 C ALA A 141 6.677 -19.877 26.798 1.00 70.78 C ANISOU 946 C ALA A 141 7703 9644 9546 -1308 258 216 C ATOM 947 O ALA A 141 7.171 -19.484 25.741 1.00 70.68 O ANISOU 947 O ALA A 141 7706 9630 9518 -1279 301 235 O ATOM 948 CB ALA A 141 8.029 -21.564 28.060 1.00 66.43 C ANISOU 948 CB ALA A 141 7078 9096 9067 -1304 280 258 C ATOM 949 N ILE A 142 5.351 -20.105 26.963 1.00 68.18 N ANISOU 949 N ILE A 142 7405 9314 9189 -1319 215 176 N ATOM 950 CA ILE A 142 4.327 -19.894 25.930 1.00 68.62 C ANISOU 950 CA ILE A 142 7516 9365 9191 -1308 206 148 C ATOM 951 C ILE A 142 4.201 -18.376 25.677 1.00 73.67 C ANISOU 951 C ILE A 142 8156 10020 9818 -1317 212 162 C ATOM 952 O ILE A 142 4.099 -17.960 24.522 1.00 73.40 O ANISOU 952 O ILE A 142 8154 9988 9748 -1295 237 161 O ATOM 953 CB ILE A 142 2.969 -20.560 26.329 1.00 71.59 C ANISOU 953 CB ILE A 142 7906 9738 9557 -1325 151 126 C ATOM 954 CG1 ILE A 142 3.089 -22.104 26.330 1.00 72.34 C ANISOU 954 CG1 ILE A 142 8011 9805 9670 -1314 144 112 C ATOM 955 CG2 ILE A 142 1.826 -20.124 25.398 1.00 72.34 C ANISOU 955 CG2 ILE A 142 8047 9837 9601 -1325 130 112 C ATOM 956 CD1 ILE A 142 2.011 -22.871 27.143 1.00 79.76 C ANISOU 956 CD1 ILE A 142 8930 10742 10634 -1338 86 115 C ATOM 957 N ALA A 143 4.254 -17.561 26.757 1.00 71.04 N ANISOU 957 N ALA A 143 7790 9692 9509 -1346 188 175 N ATOM 958 CA ALA A 143 4.183 -16.096 26.700 1.00 71.29 C ANISOU 958 CA ALA A 143 7826 9724 9537 -1357 188 188 C ATOM 959 C ALA A 143 5.371 -15.510 25.926 1.00 76.63 C ANISOU 959 C ALA A 143 8484 10394 10240 -1350 229 224 C ATOM 960 O ALA A 143 5.193 -14.537 25.195 1.00 76.37 O ANISOU 960 O ALA A 143 8463 10362 10193 -1343 246 236 O ATOM 961 CB ALA A 143 4.135 -15.517 28.104 1.00 71.89 C ANISOU 961 CB ALA A 143 7888 9796 9631 -1382 147 188 C ATOM 962 N ILE A 144 6.569 -16.118 26.072 1.00 74.30 N ANISOU 962 N ILE A 144 8150 10095 9984 -1346 250 254 N ATOM 963 CA ILE A 144 7.796 -15.719 25.371 1.00 74.98 C ANISOU 963 CA ILE A 144 8203 10182 10106 -1331 295 315 C ATOM 964 C ILE A 144 7.676 -16.175 23.900 1.00 80.28 C ANISOU 964 C ILE A 144 8911 10863 10727 -1268 352 314 C ATOM 965 O ILE A 144 8.006 -15.400 23.001 1.00 80.10 O ANISOU 965 O ILE A 144 8882 10848 10704 -1244 389 353 O ATOM 966 CB ILE A 144 9.065 -16.282 26.085 1.00 78.30 C ANISOU 966 CB ILE A 144 8564 10602 10585 -1343 299 363 C ATOM 967 CG1 ILE A 144 9.210 -15.670 27.503 1.00 78.61 C ANISOU 967 CG1 ILE A 144 8575 10631 10664 -1405 230 362 C ATOM 968 CG2 ILE A 144 10.343 -16.034 25.259 1.00 79.67 C ANISOU 968 CG2 ILE A 144 8691 10781 10797 -1315 356 450 C ATOM 969 CD1 ILE A 144 10.088 -16.466 28.497 1.00 86.26 C ANISOU 969 CD1 ILE A 144 9492 11609 11676 -1425 216 391 C ATOM 970 N GLU A 145 7.165 -17.410 23.670 1.00 77.78 N ANISOU 970 N GLU A 145 8639 10544 10369 -1242 354 269 N ATOM 971 CA GLU A 145 6.938 -18.018 22.349 1.00 78.41 C ANISOU 971 CA GLU A 145 8780 10625 10387 -1180 392 250 C ATOM 972 C GLU A 145 6.013 -17.129 21.496 1.00 83.21 C ANISOU 972 C GLU A 145 9423 11247 10945 -1175 386 233 C ATOM 973 O GLU A 145 6.300 -16.918 20.316 1.00 83.19 O ANISOU 973 O GLU A 145 9445 11258 10906 -1120 434 253 O ATOM 974 CB GLU A 145 6.351 -19.442 22.511 1.00 79.79 C ANISOU 974 CB GLU A 145 9002 10778 10535 -1175 364 195 C ATOM 975 CG GLU A 145 5.779 -20.101 21.259 1.00 91.59 C ANISOU 975 CG GLU A 145 10587 12261 11954 -1126 370 152 C ATOM 976 CD GLU A 145 6.711 -20.384 20.094 1.00115.29 C ANISOU 976 CD GLU A 145 13629 15262 14916 -1039 444 177 C ATOM 977 OE1 GLU A 145 7.926 -20.589 20.321 1.00112.69 O ANISOU 977 OE1 GLU A 145 13257 14935 14626 -1008 499 233 O ATOM 978 OE2 GLU A 145 6.206 -20.459 18.950 1.00110.04 O1- ANISOU 978 OE2 GLU A 145 13040 14596 14175 -995 447 145 O1- ATOM 979 N ARG A 146 4.932 -16.592 22.099 1.00 80.13 N ANISOU 979 N ARG A 146 9034 10859 10552 -1224 333 206 N ATOM 980 CA ARG A 146 3.988 -15.716 21.401 1.00 80.28 C ANISOU 980 CA ARG A 146 9078 10895 10529 -1223 328 200 C ATOM 981 C ARG A 146 4.577 -14.313 21.205 1.00 85.23 C ANISOU 981 C ARG A 146 9664 11529 11188 -1223 362 251 C ATOM 982 O ARG A 146 4.236 -13.655 20.224 1.00 84.94 O ANISOU 982 O ARG A 146 9643 11512 11118 -1197 388 264 O ATOM 983 CB ARG A 146 2.635 -15.624 22.137 1.00 79.97 C ANISOU 983 CB ARG A 146 9049 10858 10478 -1265 270 172 C ATOM 984 CG ARG A 146 1.846 -16.941 22.264 1.00 89.66 C ANISOU 984 CG ARG A 146 10308 12076 11682 -1273 225 136 C ATOM 985 CD ARG A 146 1.636 -17.706 20.961 1.00 99.10 C ANISOU 985 CD ARG A 146 11567 13268 12820 -1238 227 109 C ATOM 986 NE ARG A 146 0.835 -16.972 19.981 1.00107.99 N ANISOU 986 NE ARG A 146 12720 14420 13893 -1229 226 114 N ATOM 987 CZ ARG A 146 0.567 -17.411 18.755 1.00123.07 C ANISOU 987 CZ ARG A 146 14693 16332 15737 -1196 222 90 C ATOM 988 NH1 ARG A 146 1.034 -18.585 18.345 1.00110.50 N ANISOU 988 NH1 ARG A 146 13154 14708 14122 -1164 219 56 N ATOM 989 NH2 ARG A 146 -0.167 -16.680 17.928 1.00110.56 N1+ ANISOU 989 NH2 ARG A 146 13124 14779 14105 -1190 221 102 N1+ ATOM 990 N HIS A 147 5.469 -13.868 22.116 1.00 82.57 N ANISOU 990 N HIS A 147 9276 11175 10921 -1254 356 283 N ATOM 991 CA HIS A 147 6.114 -12.552 22.050 1.00 83.05 C ANISOU 991 CA HIS A 147 9295 11228 11031 -1267 371 338 C ATOM 992 C HIS A 147 7.128 -12.480 20.893 1.00 88.61 C ANISOU 992 C HIS A 147 9971 11949 11746 -1213 438 404 C ATOM 993 O HIS A 147 7.375 -11.390 20.376 1.00 88.44 O ANISOU 993 O HIS A 147 9921 11931 11752 -1207 462 455 O ATOM 994 CB HIS A 147 6.806 -12.221 23.380 1.00 83.77 C ANISOU 994 CB HIS A 147 9346 11290 11192 -1322 327 354 C ATOM 995 CG HIS A 147 7.176 -10.778 23.525 1.00 87.41 C ANISOU 995 CG HIS A 147 9781 11726 11706 -1353 313 395 C ATOM 996 ND1 HIS A 147 8.424 -10.313 23.154 1.00 89.72 N ANISOU 996 ND1 HIS A 147 10013 12009 12067 -1355 335 476 N ATOM 997 CD2 HIS A 147 6.443 -9.740 23.989 1.00 88.97 C ANISOU 997 CD2 HIS A 147 10007 11900 11899 -1381 278 372 C ATOM 998 CE1 HIS A 147 8.413 -9.014 23.407 1.00 89.31 C ANISOU 998 CE1 HIS A 147 9954 11922 12056 -1393 303 495 C ATOM 999 NE2 HIS A 147 7.242 -8.624 23.910 1.00 89.22 N ANISOU 999 NE2 HIS A 147 10002 11899 11999 -1406 272 429 N ATOM 1000 N ILE A 148 7.701 -13.631 20.488 1.00 86.28 N ANISOU 1000 N ILE A 148 9687 11665 11432 -1165 473 409 N ATOM 1001 CA ILE A 148 8.675 -13.711 19.396 1.00 87.16 C ANISOU 1001 CA ILE A 148 9778 11797 11541 -1090 549 481 C ATOM 1002 C ILE A 148 7.929 -13.826 18.049 1.00 92.34 C ANISOU 1002 C ILE A 148 10502 12480 12104 -1022 584 451 C ATOM 1003 O ILE A 148 8.179 -13.012 17.160 1.00 92.32 O ANISOU 1003 O ILE A 148 10477 12502 12100 -980 631 509 O ATOM 1004 CB ILE A 148 9.685 -14.884 19.610 1.00 90.56 C ANISOU 1004 CB ILE A 148 10197 12224 11988 -1056 580 509 C ATOM 1005 CG1 ILE A 148 10.502 -14.687 20.912 1.00 90.90 C ANISOU 1005 CG1 ILE A 148 10163 12249 12126 -1126 542 552 C ATOM 1006 CG2 ILE A 148 10.624 -15.046 18.396 1.00 92.07 C ANISOU 1006 CG2 ILE A 148 10380 12442 12161 -953 672 591 C ATOM 1007 CD1 ILE A 148 11.155 -15.962 21.491 1.00 98.49 C ANISOU 1007 CD1 ILE A 148 11115 13206 13101 -1115 553 558 C ATOM 1008 N THR A 149 7.013 -14.818 17.917 1.00 89.59 N ANISOU 1008 N THR A 149 10232 12126 11681 -1015 553 367 N ATOM 1009 CA THR A 149 6.239 -15.127 16.700 1.00 90.12 C ANISOU 1009 CA THR A 149 10379 12214 11650 -959 564 327 C ATOM 1010 C THR A 149 5.398 -13.945 16.177 1.00 94.99 C ANISOU 1010 C THR A 149 10988 12857 12245 -972 559 335 C ATOM 1011 O THR A 149 5.178 -13.873 14.967 1.00 95.00 O ANISOU 1011 O THR A 149 11030 12889 12175 -908 592 338 O ATOM 1012 CB THR A 149 5.309 -16.328 16.919 1.00 97.84 C ANISOU 1012 CB THR A 149 11432 13167 12576 -980 502 239 C ATOM 1013 OG1 THR A 149 4.537 -16.130 18.102 1.00 96.84 O ANISOU 1013 OG1 THR A 149 11276 13026 12493 -1068 436 212 O ATOM 1014 CG2 THR A 149 6.061 -17.649 16.990 1.00 96.67 C ANISOU 1014 CG2 THR A 149 11319 12991 12422 -938 521 226 C ATOM 1015 N VAL A 150 4.926 -13.040 17.062 1.00 91.94 N ANISOU 1015 N VAL A 150 10558 12462 11913 -1047 521 338 N ATOM 1016 CA VAL A 150 4.132 -11.867 16.665 1.00 92.12 C ANISOU 1016 CA VAL A 150 10571 12507 11924 -1059 523 353 C ATOM 1017 C VAL A 150 5.063 -10.860 15.949 1.00 97.73 C ANISOU 1017 C VAL A 150 11225 13235 12672 -1014 592 439 C ATOM 1018 O VAL A 150 4.710 -10.368 14.873 1.00 97.60 O ANISOU 1018 O VAL A 150 11219 13257 12609 -967 629 461 O ATOM 1019 CB VAL A 150 3.371 -11.241 17.872 1.00 95.42 C ANISOU 1019 CB VAL A 150 10971 12902 12382 -1136 469 333 C ATOM 1020 CG1 VAL A 150 2.943 -9.797 17.605 1.00 95.19 C ANISOU 1020 CG1 VAL A 150 10918 12884 12367 -1144 488 372 C ATOM 1021 CG2 VAL A 150 2.160 -12.092 18.243 1.00 94.91 C ANISOU 1021 CG2 VAL A 150 10956 12837 12267 -1164 410 272 C ATOM 1022 N PHE A 151 6.261 -10.607 16.515 1.00 95.41 N ANISOU 1022 N PHE A 151 10868 12919 12466 -1028 606 496 N ATOM 1023 CA PHE A 151 7.254 -9.697 15.938 1.00 96.27 C ANISOU 1023 CA PHE A 151 10905 13038 12634 -992 664 600 C ATOM 1024 C PHE A 151 8.032 -10.366 14.778 1.00101.84 C ANISOU 1024 C PHE A 151 11618 13782 13293 -884 741 650 C ATOM 1025 O PHE A 151 8.703 -9.663 14.019 1.00101.95 O ANISOU 1025 O PHE A 151 11577 13823 13339 -829 802 747 O ATOM 1026 CB PHE A 151 8.222 -9.193 17.022 1.00 98.14 C ANISOU 1026 CB PHE A 151 11069 13231 12987 -1057 634 652 C ATOM 1027 CG PHE A 151 7.631 -8.133 17.925 1.00 99.36 C ANISOU 1027 CG PHE A 151 11219 13346 13189 -1140 573 627 C ATOM 1028 CD1 PHE A 151 6.923 -8.484 19.069 1.00101.88 C ANISOU 1028 CD1 PHE A 151 11582 13637 13491 -1199 506 544 C ATOM 1029 CD2 PHE A 151 7.784 -6.782 17.632 1.00101.87 C ANISOU 1029 CD2 PHE A 151 11491 13651 13566 -1151 586 691 C ATOM 1030 CE1 PHE A 151 6.375 -7.504 19.902 1.00102.56 C ANISOU 1030 CE1 PHE A 151 11678 13684 13606 -1257 458 522 C ATOM 1031 CE2 PHE A 151 7.236 -5.802 18.467 1.00104.47 C ANISOU 1031 CE2 PHE A 151 11832 13931 13930 -1219 532 664 C ATOM 1032 CZ PHE A 151 6.535 -6.170 19.596 1.00101.99 C ANISOU 1032 CZ PHE A 151 11575 13592 13587 -1266 470 577 C ATOM 1033 N ARG A 152 7.918 -11.706 14.628 1.00 99.25 N ANISOU 1033 N ARG A 152 11363 13456 12891 -845 739 589 N ATOM 1034 CA ARG A 152 8.558 -12.479 13.555 1.00100.20 C ANISOU 1034 CA ARG A 152 11521 13605 12944 -727 811 620 C ATOM 1035 C ARG A 152 7.519 -12.920 12.495 1.00105.14 C ANISOU 1035 C ARG A 152 12252 14256 13438 -671 808 545 C ATOM 1036 O ARG A 152 7.871 -13.629 11.548 1.00105.47 O ANISOU 1036 O ARG A 152 12358 14317 13398 -565 858 549 O ATOM 1037 CB ARG A 152 9.296 -13.699 14.130 1.00100.62 C ANISOU 1037 CB ARG A 152 11592 13631 13009 -716 814 610 C ATOM 1038 N MET A 153 6.244 -12.480 12.663 1.00101.74 N ANISOU 1038 N MET A 153 11843 13827 12986 -741 746 483 N ATOM 1039 CA MET A 153 5.065 -12.714 11.813 1.00101.94 C ANISOU 1039 CA MET A 153 11953 13877 12902 -720 717 418 C ATOM 1040 C MET A 153 4.640 -14.200 11.762 1.00106.45 C ANISOU 1040 C MET A 153 12633 14419 13395 -711 665 325 C ATOM 1041 O MET A 153 3.500 -14.492 12.128 1.00105.58 O ANISOU 1041 O MET A 153 12559 14294 13264 -782 585 258 O ATOM 1042 CB MET A 153 5.262 -12.177 10.380 1.00105.05 C ANISOU 1042 CB MET A 153 12355 14330 13231 -614 791 474 C ATOM 1043 CG MET A 153 4.898 -10.712 10.225 1.00108.54 C ANISOU 1043 CG MET A 153 12718 14804 13718 -642 810 534 C ATOM 1044 SD MET A 153 5.917 -9.564 11.187 1.00112.52 S ANISOU 1044 SD MET A 153 13087 15279 14385 -698 837 633 S ATOM 1045 CE MET A 153 5.148 -8.022 10.751 1.00109.09 C ANISOU 1045 CE MET A 153 12602 14877 13970 -718 853 677 C ATOM 1046 N GLN A 154 5.515 -15.122 11.299 1.00104.08 N ANISOU 1046 N GLN A 154 12385 14108 13052 -621 710 327 N ATOM 1047 CA GLN A 154 5.166 -16.544 11.177 1.00104.38 C ANISOU 1047 CA GLN A 154 12539 14105 13015 -605 661 237 C ATOM 1048 C GLN A 154 6.096 -17.441 12.033 1.00108.31 C ANISOU 1048 C GLN A 154 13025 14556 13571 -606 676 242 C ATOM 1049 O GLN A 154 7.063 -16.948 12.620 1.00107.63 O ANISOU 1049 O GLN A 154 12840 14478 13575 -612 727 322 O ATOM 1050 CB GLN A 154 5.212 -16.968 9.694 1.00106.84 C ANISOU 1050 CB GLN A 154 12964 14439 13193 -479 696 220 C ATOM 1051 CG GLN A 154 4.211 -18.067 9.307 1.00123.37 C ANISOU 1051 CG GLN A 154 15196 16491 15186 -491 602 108 C ATOM 1052 CD GLN A 154 2.761 -17.651 9.433 1.00142.79 C ANISOU 1052 CD GLN A 154 17648 18962 17642 -596 504 68 C ATOM 1053 OE1 GLN A 154 2.306 -16.675 8.824 1.00138.52 O ANISOU 1053 OE1 GLN A 154 17077 18479 17074 -588 519 102 O ATOM 1054 NE2 GLN A 154 1.993 -18.410 10.201 1.00134.57 N ANISOU 1054 NE2 GLN A 154 16632 17870 16628 -690 406 6 N ATOM 1055 N LEU A 155 5.775 -18.757 12.105 1.00105.22 N ANISOU 1055 N LEU A 155 12733 14115 13132 -604 626 161 N ATOM 1056 CA LEU A 155 6.480 -19.800 12.864 1.00105.08 C ANISOU 1056 CA LEU A 155 12721 14049 13157 -603 634 153 C ATOM 1057 C LEU A 155 7.939 -19.997 12.397 1.00109.71 C ANISOU 1057 C LEU A 155 13302 14649 13736 -480 749 234 C ATOM 1058 O LEU A 155 8.326 -19.525 11.324 1.00109.95 O ANISOU 1058 O LEU A 155 13351 14720 13706 -378 819 283 O ATOM 1059 CB LEU A 155 5.730 -21.155 12.773 1.00105.48 C ANISOU 1059 CB LEU A 155 12896 14037 13145 -613 554 49 C ATOM 1060 CG LEU A 155 4.352 -21.335 13.468 1.00109.57 C ANISOU 1060 CG LEU A 155 13411 14529 13690 -739 432 -16 C ATOM 1061 CD1 LEU A 155 4.338 -20.807 14.906 1.00108.68 C ANISOU 1061 CD1 LEU A 155 13169 14427 13698 -839 416 22 C ATOM 1062 CD2 LEU A 155 3.202 -20.789 12.632 1.00112.21 C ANISOU 1062 CD2 LEU A 155 13790 14893 13954 -757 375 -45 C ATOM 1063 N HIS A 156 8.735 -20.713 13.218 1.00106.16 N ANISOU 1063 N HIS A 156 12820 14167 13347 -484 772 257 N ATOM 1064 CA HIS A 156 10.158 -20.988 12.991 1.00106.59 C ANISOU 1064 CA HIS A 156 12852 14234 13413 -376 883 353 C ATOM 1065 C HIS A 156 10.381 -22.349 12.289 1.00110.99 C ANISOU 1065 C HIS A 156 13558 14746 13866 -259 916 304 C ATOM 1066 O HIS A 156 9.417 -23.064 12.002 1.00110.69 O ANISOU 1066 O HIS A 156 13642 14661 13754 -275 838 189 O ATOM 1067 CB HIS A 156 10.925 -20.957 14.326 1.00106.84 C ANISOU 1067 CB HIS A 156 12759 14261 13574 -451 889 418 C ATOM 1068 CG HIS A 156 10.303 -20.096 15.383 1.00109.20 C ANISOU 1068 CG HIS A 156 12962 14566 13961 -596 807 403 C ATOM 1069 ND1 HIS A 156 9.500 -20.638 16.371 1.00110.26 N ANISOU 1069 ND1 HIS A 156 13107 14664 14123 -694 718 321 N ATOM 1070 CD2 HIS A 156 10.369 -18.756 15.560 1.00110.59 C ANISOU 1070 CD2 HIS A 156 13042 14778 14199 -646 804 463 C ATOM 1071 CE1 HIS A 156 9.117 -19.619 17.122 1.00108.93 C ANISOU 1071 CE1 HIS A 156 12854 14512 14021 -790 671 332 C ATOM 1072 NE2 HIS A 156 9.612 -18.466 16.672 1.00109.44 N ANISOU 1072 NE2 HIS A 156 12858 14615 14108 -769 716 411 N ATOM 1073 N THR A 157 11.663 -22.695 12.019 1.00107.93 N ANISOU 1073 N THR A 157 13163 14371 13476 -139 1029 400 N ATOM 1074 CA THR A 157 12.090 -23.928 11.340 1.00108.65 C ANISOU 1074 CA THR A 157 13398 14419 13466 0 1086 374 C ATOM 1075 C THR A 157 12.285 -25.097 12.344 1.00111.54 C ANISOU 1075 C THR A 157 13774 14720 13886 -46 1063 339 C ATOM 1076 O THR A 157 11.858 -24.998 13.498 1.00110.07 O ANISOU 1076 O THR A 157 13499 14523 13798 -190 985 313 O ATOM 1077 CB THR A 157 13.385 -23.673 10.539 1.00118.16 C ANISOU 1077 CB THR A 157 14580 15675 14639 169 1235 517 C ATOM 1078 OG1 THR A 157 14.392 -23.156 11.411 1.00117.47 O ANISOU 1078 OG1 THR A 157 14316 15626 14690 125 1286 657 O ATOM 1079 CG2 THR A 157 13.175 -22.734 9.354 1.00117.26 C ANISOU 1079 CG2 THR A 157 14485 15621 14448 248 1268 547 C ATOM 1080 N ARG A 158 12.916 -26.207 11.878 1.00108.52 N ANISOU 1080 N ARG A 158 13505 14295 13431 88 1135 341 N ATOM 1081 CA ARG A 158 13.197 -27.439 12.628 1.00108.07 C ANISOU 1081 CA ARG A 158 13479 14173 13410 78 1134 316 C ATOM 1082 C ARG A 158 14.158 -27.188 13.814 1.00110.21 C ANISOU 1082 C ARG A 158 13566 14484 13824 19 1184 440 C ATOM 1083 O ARG A 158 14.061 -27.897 14.819 1.00109.24 O ANISOU 1083 O ARG A 158 13416 14322 13769 -60 1142 409 O ATOM 1084 CB ARG A 158 13.779 -28.518 11.678 1.00110.10 C ANISOU 1084 CB ARG A 158 13909 14381 13544 266 1224 309 C ATOM 1085 CG ARG A 158 14.208 -29.856 12.314 1.00121.66 C ANISOU 1085 CG ARG A 158 15419 15771 15036 286 1248 295 C ATOM 1086 CD ARG A 158 13.081 -30.624 12.989 1.00132.62 C ANISOU 1086 CD ARG A 158 16860 17075 16455 151 1105 154 C ATOM 1087 NE ARG A 158 13.595 -31.713 13.823 1.00142.58 N ANISOU 1087 NE ARG A 158 18110 18283 17780 151 1135 171 N ATOM 1088 CZ ARG A 158 12.850 -32.459 14.634 1.00156.83 C ANISOU 1088 CZ ARG A 158 19924 20021 19644 37 1032 85 C ATOM 1089 NH1 ARG A 158 11.544 -32.241 14.736 1.00143.81 N ANISOU 1089 NH1 ARG A 158 18291 18349 18000 -87 889 -19 N ATOM 1090 NH2 ARG A 158 13.406 -33.423 15.355 1.00143.99 N1+ ANISOU 1090 NH2 ARG A 158 18279 18353 18077 49 1075 115 N1+ ATOM 1091 N MET A 159 15.064 -26.188 13.704 1.00106.01 N ANISOU 1091 N MET A 159 12907 14029 13341 53 1265 585 N ATOM 1092 CA MET A 159 16.032 -25.834 14.752 1.00104.95 C ANISOU 1092 CA MET A 159 12596 13938 13343 -7 1301 718 C ATOM 1093 C MET A 159 15.312 -25.521 16.082 1.00106.30 C ANISOU 1093 C MET A 159 12674 14100 13617 -198 1177 654 C ATOM 1094 O MET A 159 15.760 -25.990 17.130 1.00105.53 O ANISOU 1094 O MET A 159 12501 13995 13600 -252 1174 688 O ATOM 1095 CB MET A 159 16.910 -24.642 14.310 1.00107.62 C ANISOU 1095 CB MET A 159 12814 14354 13721 42 1378 878 C ATOM 1096 CG MET A 159 17.986 -24.241 15.322 1.00111.04 C ANISOU 1096 CG MET A 159 13064 14828 14297 -22 1405 1031 C ATOM 1097 SD MET A 159 19.199 -25.537 15.685 1.00116.01 S ANISOU 1097 SD MET A 159 13687 15447 14947 77 1515 1135 S ATOM 1098 CE MET A 159 19.997 -24.832 17.105 1.00112.04 C ANISOU 1098 CE MET A 159 12959 14990 14622 -71 1476 1269 C ATOM 1099 N SER A 160 14.183 -24.779 16.024 1.00101.23 N ANISOU 1099 N SER A 160 12043 13459 12961 -289 1081 564 N ATOM 1100 CA SER A 160 13.380 -24.414 17.193 1.00 99.40 C ANISOU 1100 CA SER A 160 11739 13221 12808 -451 968 503 C ATOM 1101 C SER A 160 12.711 -25.633 17.836 1.00101.85 C ANISOU 1101 C SER A 160 12114 13469 13115 -497 904 400 C ATOM 1102 O SER A 160 12.539 -25.633 19.054 1.00100.65 O ANISOU 1102 O SER A 160 11877 13318 13047 -602 849 395 O ATOM 1103 CB SER A 160 12.323 -23.382 16.824 1.00102.39 C ANISOU 1103 CB SER A 160 12128 13617 13159 -511 898 443 C ATOM 1104 OG SER A 160 12.932 -22.122 16.598 1.00111.19 O ANISOU 1104 OG SER A 160 13144 14786 14316 -505 940 547 O ATOM 1105 N ASN A 161 12.355 -26.669 17.038 1.00 98.22 N ANISOU 1105 N ASN A 161 11806 12952 12560 -415 910 323 N ATOM 1106 CA ASN A 161 11.745 -27.909 17.540 1.00 97.53 C ANISOU 1106 CA ASN A 161 11789 12793 12475 -452 848 232 C ATOM 1107 C ASN A 161 12.742 -28.669 18.427 1.00100.08 C ANISOU 1107 C ASN A 161 12043 13110 12872 -438 910 304 C ATOM 1108 O ASN A 161 12.341 -29.248 19.438 1.00 99.12 O ANISOU 1108 O ASN A 161 11885 12962 12814 -521 850 269 O ATOM 1109 CB ASN A 161 11.253 -28.797 16.393 1.00 99.74 C ANISOU 1109 CB ASN A 161 12259 13004 12635 -362 836 138 C ATOM 1110 CG ASN A 161 10.122 -28.201 15.587 1.00123.81 C ANISOU 1110 CG ASN A 161 15379 16054 15609 -390 755 58 C ATOM 1111 OD1 ASN A 161 10.293 -27.814 14.427 1.00119.38 O ANISOU 1111 OD1 ASN A 161 14892 15513 14954 -292 801 66 O ATOM 1112 ND2 ASN A 161 8.936 -28.126 16.174 1.00114.86 N ANISOU 1112 ND2 ASN A 161 14224 14904 14515 -517 635 -9 N ATOM 1113 N ARG A 162 14.041 -28.628 18.061 1.00 96.20 N ANISOU 1113 N ARG A 162 11522 12652 12377 -331 1032 420 N ATOM 1114 CA ARG A 162 15.136 -29.229 18.827 1.00 95.67 C ANISOU 1114 CA ARG A 162 11374 12595 12382 -308 1106 519 C ATOM 1115 C ARG A 162 15.418 -28.382 20.070 1.00 97.31 C ANISOU 1115 C ARG A 162 11400 12864 12709 -433 1068 590 C ATOM 1116 O ARG A 162 15.805 -28.924 21.107 1.00 96.61 O ANISOU 1116 O ARG A 162 11236 12777 12694 -477 1069 626 O ATOM 1117 CB ARG A 162 16.400 -29.375 17.965 1.00 97.17 C ANISOU 1117 CB ARG A 162 11586 12807 12526 -146 1252 639 C ATOM 1118 CG ARG A 162 16.292 -30.449 16.883 1.00108.96 C ANISOU 1118 CG ARG A 162 13276 14228 13894 -1 1302 572 C ATOM 1119 CD ARG A 162 17.538 -30.532 16.019 1.00120.65 C ANISOU 1119 CD ARG A 162 14781 15740 15322 181 1459 705 C ATOM 1120 NE ARG A 162 17.673 -29.381 15.123 1.00129.99 N ANISOU 1120 NE ARG A 162 15944 16986 16462 231 1490 762 N ATOM 1121 CZ ARG A 162 18.677 -29.205 14.269 1.00145.50 C ANISOU 1121 CZ ARG A 162 17913 18992 18378 393 1624 894 C ATOM 1122 NH1 ARG A 162 19.651 -30.103 14.183 1.00133.91 N ANISOU 1122 NH1 ARG A 162 16475 17511 16893 526 1745 986 N ATOM 1123 NH2 ARG A 162 18.715 -28.129 13.494 1.00132.54 N1+ ANISOU 1123 NH2 ARG A 162 16243 17410 16708 431 1644 947 N1+ ATOM 1124 N ARG A 163 15.210 -27.050 19.959 1.00 92.43 N ANISOU 1124 N ARG A 163 10719 12293 12107 -489 1031 609 N ATOM 1125 CA ARG A 163 15.380 -26.085 21.049 1.00 90.99 C ANISOU 1125 CA ARG A 163 10389 12158 12025 -608 978 662 C ATOM 1126 C ARG A 163 14.255 -26.222 22.076 1.00 92.67 C ANISOU 1126 C ARG A 163 10595 12348 12266 -728 863 555 C ATOM 1127 O ARG A 163 14.490 -25.978 23.257 1.00 91.73 O ANISOU 1127 O ARG A 163 10372 12255 12227 -811 826 591 O ATOM 1128 CB ARG A 163 15.425 -24.643 20.515 1.00 91.34 C ANISOU 1128 CB ARG A 163 10389 12244 12072 -622 972 707 C ATOM 1129 CG ARG A 163 16.726 -24.265 19.819 1.00102.93 C ANISOU 1129 CG ARG A 163 11803 13754 13553 -525 1081 860 C ATOM 1130 CD ARG A 163 16.676 -22.838 19.312 1.00112.92 C ANISOU 1130 CD ARG A 163 13019 15054 14831 -545 1066 903 C ATOM 1131 NE ARG A 163 17.912 -22.456 18.628 1.00122.36 N ANISOU 1131 NE ARG A 163 14150 16292 16049 -449 1170 1070 N ATOM 1132 CZ ARG A 163 18.133 -21.263 18.083 1.00137.00 C ANISOU 1132 CZ ARG A 163 15946 18181 17928 -445 1180 1147 C ATOM 1133 NH1 ARG A 163 17.203 -20.317 18.136 1.00123.72 N ANISOU 1133 NH1 ARG A 163 14268 16492 16247 -532 1095 1065 N ATOM 1134 NH2 ARG A 163 19.287 -21.006 17.482 1.00125.14 N1+ ANISOU 1134 NH2 ARG A 163 14374 16719 16454 -349 1279 1318 N1+ ATOM 1135 N VAL A 164 13.038 -26.611 21.624 1.00 88.08 N ANISOU 1135 N VAL A 164 10126 11722 11620 -733 805 434 N ATOM 1136 CA VAL A 164 11.845 -26.811 22.459 1.00 86.66 C ANISOU 1136 CA VAL A 164 9945 11519 11462 -832 700 344 C ATOM 1137 C VAL A 164 12.116 -27.948 23.462 1.00 89.04 C ANISOU 1137 C VAL A 164 10212 11800 11819 -847 703 353 C ATOM 1138 O VAL A 164 11.760 -27.810 24.633 1.00 87.94 O ANISOU 1138 O VAL A 164 9993 11679 11739 -933 643 349 O ATOM 1139 CB VAL A 164 10.581 -27.064 21.585 1.00 90.78 C ANISOU 1139 CB VAL A 164 10594 11996 11904 -824 642 235 C ATOM 1140 CG1 VAL A 164 9.509 -27.867 22.320 1.00 90.22 C ANISOU 1140 CG1 VAL A 164 10540 11883 11858 -893 552 162 C ATOM 1141 CG2 VAL A 164 10.004 -25.748 21.084 1.00 90.30 C ANISOU 1141 CG2 VAL A 164 10528 11971 11813 -854 609 224 C ATOM 1142 N VAL A 165 12.793 -29.030 23.014 1.00 85.27 N ANISOU 1142 N VAL A 165 9791 11287 11319 -756 779 375 N ATOM 1143 CA VAL A 165 13.177 -30.184 23.842 1.00 84.69 C ANISOU 1143 CA VAL A 165 9687 11192 11299 -754 801 396 C ATOM 1144 C VAL A 165 14.041 -29.681 25.020 1.00 86.98 C ANISOU 1144 C VAL A 165 9820 11551 11677 -809 817 498 C ATOM 1145 O VAL A 165 13.806 -30.083 26.160 1.00 86.03 O ANISOU 1145 O VAL A 165 9635 11436 11615 -872 774 492 O ATOM 1146 CB VAL A 165 13.904 -31.282 23.008 1.00 89.64 C ANISOU 1146 CB VAL A 165 10413 11770 11878 -626 900 416 C ATOM 1147 CG1 VAL A 165 14.272 -32.491 23.869 1.00 89.57 C ANISOU 1147 CG1 VAL A 165 10370 11734 11927 -622 927 441 C ATOM 1148 CG2 VAL A 165 13.058 -31.722 21.815 1.00 90.02 C ANISOU 1148 CG2 VAL A 165 10633 11744 11826 -572 869 308 C ATOM 1149 N VAL A 166 14.986 -28.757 24.737 1.00 82.96 N ANISOU 1149 N VAL A 166 9249 11093 11178 -788 868 593 N ATOM 1150 CA VAL A 166 15.886 -28.122 25.709 1.00 82.15 C ANISOU 1150 CA VAL A 166 9003 11053 11158 -845 870 700 C ATOM 1151 C VAL A 166 15.054 -27.245 26.674 1.00 84.08 C ANISOU 1151 C VAL A 166 9197 11318 11434 -964 756 644 C ATOM 1152 O VAL A 166 15.298 -27.284 27.880 1.00 83.24 O ANISOU 1152 O VAL A 166 9002 11240 11386 -1025 721 675 O ATOM 1153 CB VAL A 166 17.002 -27.306 24.990 1.00 86.70 C ANISOU 1153 CB VAL A 166 9534 11668 11739 -792 942 821 C ATOM 1154 CG1 VAL A 166 17.923 -26.601 25.983 1.00 86.43 C ANISOU 1154 CG1 VAL A 166 9352 11691 11798 -866 923 936 C ATOM 1155 CG2 VAL A 166 17.814 -28.189 24.046 1.00 87.51 C ANISOU 1155 CG2 VAL A 166 9695 11755 11801 -653 1068 887 C ATOM 1156 N VAL A 167 14.062 -26.490 26.141 1.00 79.61 N ANISOU 1156 N VAL A 167 8690 10737 10820 -987 700 564 N ATOM 1157 CA VAL A 167 13.165 -25.611 26.910 1.00 78.28 C ANISOU 1157 CA VAL A 167 8495 10583 10666 -1080 602 510 C ATOM 1158 C VAL A 167 12.310 -26.474 27.872 1.00 80.75 C ANISOU 1158 C VAL A 167 8808 10880 10992 -1118 548 448 C ATOM 1159 O VAL A 167 12.188 -26.113 29.043 1.00 79.86 O ANISOU 1159 O VAL A 167 8628 10797 10919 -1181 494 456 O ATOM 1160 CB VAL A 167 12.291 -24.708 25.984 1.00 81.99 C ANISOU 1160 CB VAL A 167 9034 11042 11078 -1081 572 451 C ATOM 1161 CG1 VAL A 167 11.231 -23.938 26.769 1.00 81.10 C ANISOU 1161 CG1 VAL A 167 8906 10937 10970 -1163 480 394 C ATOM 1162 CG2 VAL A 167 13.156 -23.735 25.188 1.00 82.23 C ANISOU 1162 CG2 VAL A 167 9039 11095 11108 -1050 622 528 C ATOM 1163 N ILE A 168 11.776 -27.626 27.391 1.00 76.81 N ANISOU 1163 N ILE A 168 8387 10333 10465 -1075 560 395 N ATOM 1164 CA ILE A 168 10.970 -28.577 28.177 1.00 76.01 C ANISOU 1164 CA ILE A 168 8284 10209 10388 -1104 512 350 C ATOM 1165 C ILE A 168 11.798 -29.066 29.389 1.00 79.14 C ANISOU 1165 C ILE A 168 8578 10640 10852 -1118 536 420 C ATOM 1166 O ILE A 168 11.264 -29.115 30.500 1.00 78.29 O ANISOU 1166 O ILE A 168 8415 10554 10777 -1167 480 410 O ATOM 1167 CB ILE A 168 10.451 -29.755 27.290 1.00 79.58 C ANISOU 1167 CB ILE A 168 8845 10588 10803 -1052 521 291 C ATOM 1168 CG1 ILE A 168 9.318 -29.268 26.349 1.00 79.94 C ANISOU 1168 CG1 ILE A 168 8983 10606 10784 -1062 464 215 C ATOM 1169 CG2 ILE A 168 9.974 -30.957 28.136 1.00 80.18 C ANISOU 1169 CG2 ILE A 168 8901 10635 10930 -1072 491 277 C ATOM 1170 CD1 ILE A 168 8.910 -30.237 25.210 1.00 88.09 C ANISOU 1170 CD1 ILE A 168 10149 11562 11762 -1007 463 153 C ATOM 1171 N VAL A 169 13.099 -29.372 29.175 1.00 75.66 N ANISOU 1171 N VAL A 169 8107 10212 10429 -1069 620 500 N ATOM 1172 CA VAL A 169 14.037 -29.814 30.216 1.00 75.32 C ANISOU 1172 CA VAL A 169 7960 10208 10449 -1079 652 584 C ATOM 1173 C VAL A 169 14.160 -28.704 31.285 1.00 78.07 C ANISOU 1173 C VAL A 169 8217 10617 10828 -1158 586 612 C ATOM 1174 O VAL A 169 13.999 -29.002 32.466 1.00 77.35 O ANISOU 1174 O VAL A 169 8064 10554 10772 -1195 548 617 O ATOM 1175 CB VAL A 169 15.421 -30.224 29.626 1.00 80.05 C ANISOU 1175 CB VAL A 169 8545 10812 11057 -1004 762 683 C ATOM 1176 CG1 VAL A 169 16.469 -30.434 30.719 1.00 79.97 C ANISOU 1176 CG1 VAL A 169 8410 10860 11117 -1027 787 791 C ATOM 1177 CG2 VAL A 169 15.303 -31.475 28.762 1.00 80.45 C ANISOU 1177 CG2 VAL A 169 8699 10795 11072 -915 826 649 C ATOM 1178 N VAL A 170 14.376 -27.434 30.860 1.00 74.09 N ANISOU 1178 N VAL A 170 7714 10128 10309 -1181 566 625 N ATOM 1179 CA VAL A 170 14.510 -26.249 31.726 1.00 73.39 C ANISOU 1179 CA VAL A 170 7564 10079 10243 -1255 495 644 C ATOM 1180 C VAL A 170 13.237 -26.080 32.598 1.00 75.94 C ANISOU 1180 C VAL A 170 7904 10403 10546 -1298 410 559 C ATOM 1181 O VAL A 170 13.365 -25.855 33.803 1.00 75.31 O ANISOU 1181 O VAL A 170 7765 10358 10490 -1340 362 577 O ATOM 1182 CB VAL A 170 14.817 -24.963 30.897 1.00 77.53 C ANISOU 1182 CB VAL A 170 8104 10601 10754 -1264 491 666 C ATOM 1183 CG1 VAL A 170 14.748 -23.696 31.751 1.00 77.13 C ANISOU 1183 CG1 VAL A 170 8017 10570 10720 -1344 401 663 C ATOM 1184 CG2 VAL A 170 16.177 -25.062 30.210 1.00 78.11 C ANISOU 1184 CG2 VAL A 170 8135 10687 10857 -1218 575 781 C ATOM 1185 N ILE A 171 12.033 -26.224 31.992 1.00 71.69 N ANISOU 1185 N ILE A 171 7447 9829 9965 -1282 394 478 N ATOM 1186 CA ILE A 171 10.727 -26.098 32.661 1.00 70.73 C ANISOU 1186 CA ILE A 171 7342 9708 9824 -1309 324 415 C ATOM 1187 C ILE A 171 10.590 -27.170 33.768 1.00 73.91 C ANISOU 1187 C ILE A 171 7689 10129 10263 -1306 318 430 C ATOM 1188 O ILE A 171 10.244 -26.821 34.900 1.00 73.17 O ANISOU 1188 O ILE A 171 7556 10071 10173 -1332 267 430 O ATOM 1189 CB ILE A 171 9.555 -26.176 31.630 1.00 73.70 C ANISOU 1189 CB ILE A 171 7807 10041 10154 -1291 313 346 C ATOM 1190 CG1 ILE A 171 9.567 -24.950 30.686 1.00 74.17 C ANISOU 1190 CG1 ILE A 171 7911 10095 10175 -1294 313 333 C ATOM 1191 CG2 ILE A 171 8.187 -26.304 32.330 1.00 74.00 C ANISOU 1191 CG2 ILE A 171 7848 10083 10185 -1310 250 307 C ATOM 1192 CD1 ILE A 171 8.765 -25.110 29.380 1.00 81.75 C ANISOU 1192 CD1 ILE A 171 8961 11017 11086 -1265 320 281 C ATOM 1193 N TRP A 172 10.871 -28.451 33.445 1.00 70.35 N ANISOU 1193 N TRP A 172 7240 9653 9838 -1268 372 446 N ATOM 1194 CA TRP A 172 10.768 -29.556 34.401 1.00 69.93 C ANISOU 1194 CA TRP A 172 7130 9612 9829 -1261 375 469 C ATOM 1195 C TRP A 172 11.875 -29.502 35.463 1.00 73.74 C ANISOU 1195 C TRP A 172 7515 10155 10349 -1276 390 544 C ATOM 1196 O TRP A 172 11.597 -29.841 36.612 1.00 73.19 O ANISOU 1196 O TRP A 172 7387 10122 10301 -1285 362 558 O ATOM 1197 CB TRP A 172 10.778 -30.917 33.695 1.00 68.95 C ANISOU 1197 CB TRP A 172 7047 9430 9723 -1216 427 462 C ATOM 1198 CG TRP A 172 9.469 -31.253 33.041 1.00 69.79 C ANISOU 1198 CG TRP A 172 7234 9478 9806 -1214 383 391 C ATOM 1199 CD1 TRP A 172 9.189 -31.225 31.708 1.00 72.97 C ANISOU 1199 CD1 TRP A 172 7738 9824 10163 -1193 388 342 C ATOM 1200 CD2 TRP A 172 8.246 -31.610 33.702 1.00 69.33 C ANISOU 1200 CD2 TRP A 172 7156 9418 9771 -1237 319 373 C ATOM 1201 NE1 TRP A 172 7.875 -31.571 31.492 1.00 72.34 N ANISOU 1201 NE1 TRP A 172 7705 9703 10078 -1210 324 291 N ATOM 1202 CE2 TRP A 172 7.270 -31.806 32.699 1.00 73.38 C ANISOU 1202 CE2 TRP A 172 7758 9867 10257 -1238 282 316 C ATOM 1203 CE3 TRP A 172 7.879 -31.794 35.047 1.00 70.28 C ANISOU 1203 CE3 TRP A 172 7187 9586 9930 -1251 289 409 C ATOM 1204 CZ2 TRP A 172 5.954 -32.180 32.997 1.00 72.60 C ANISOU 1204 CZ2 TRP A 172 7654 9750 10181 -1260 213 305 C ATOM 1205 CZ3 TRP A 172 6.575 -32.161 35.341 1.00 71.61 C ANISOU 1205 CZ3 TRP A 172 7351 9741 10117 -1260 232 400 C ATOM 1206 CH2 TRP A 172 5.629 -32.352 34.324 1.00 72.42 C ANISOU 1206 CH2 TRP A 172 7534 9778 10204 -1269 193 353 C ATOM 1207 N THR A 173 13.105 -29.060 35.098 1.00 70.40 N ANISOU 1207 N THR A 173 7070 9746 9933 -1277 430 601 N ATOM 1208 CA THR A 173 14.233 -28.933 36.036 1.00 70.34 C ANISOU 1208 CA THR A 173 6965 9796 9964 -1301 433 685 C ATOM 1209 C THR A 173 13.887 -27.867 37.087 1.00 73.74 C ANISOU 1209 C THR A 173 7375 10266 10376 -1355 340 663 C ATOM 1210 O THR A 173 14.079 -28.116 38.278 1.00 73.38 O ANISOU 1210 O THR A 173 7264 10268 10349 -1369 314 694 O ATOM 1211 CB THR A 173 15.547 -28.620 35.293 1.00 78.77 C ANISOU 1211 CB THR A 173 8013 10867 11050 -1291 491 767 C ATOM 1212 OG1 THR A 173 15.777 -29.631 34.312 1.00 78.74 O ANISOU 1212 OG1 THR A 173 8049 10823 11047 -1221 583 780 O ATOM 1213 CG2 THR A 173 16.754 -28.540 36.225 1.00 77.59 C ANISOU 1213 CG2 THR A 173 7754 10778 10949 -1323 489 872 C ATOM 1214 N MET A 174 13.337 -26.711 36.645 1.00 69.86 N ANISOU 1214 N MET A 174 6948 9753 9844 -1378 292 609 N ATOM 1215 CA MET A 174 12.906 -25.609 37.510 1.00 69.42 C ANISOU 1215 CA MET A 174 6901 9718 9758 -1417 204 575 C ATOM 1216 C MET A 174 11.828 -26.101 38.487 1.00 71.90 C ANISOU 1216 C MET A 174 7213 10054 10053 -1397 173 538 C ATOM 1217 O MET A 174 11.906 -25.795 39.674 1.00 71.54 O ANISOU 1217 O MET A 174 7135 10050 9995 -1410 123 548 O ATOM 1218 CB MET A 174 12.387 -24.428 36.663 1.00 71.80 C ANISOU 1218 CB MET A 174 7280 9981 10020 -1431 177 524 C ATOM 1219 CG MET A 174 12.019 -23.196 37.472 1.00 75.69 C ANISOU 1219 CG MET A 174 7799 10481 10477 -1466 91 490 C ATOM 1220 SD MET A 174 11.268 -21.903 36.454 1.00 79.99 S ANISOU 1220 SD MET A 174 8435 10979 10979 -1474 71 431 S ATOM 1221 CE MET A 174 10.753 -20.765 37.717 1.00 76.78 C ANISOU 1221 CE MET A 174 8067 10580 10526 -1495 -23 391 C ATOM 1222 N ALA A 175 10.862 -26.901 37.986 1.00 67.44 N ANISOU 1222 N ALA A 175 6678 9460 9485 -1361 202 504 N ATOM 1223 CA ALA A 175 9.758 -27.478 38.755 1.00 66.66 C ANISOU 1223 CA ALA A 175 6567 9379 9383 -1336 180 489 C ATOM 1224 C ALA A 175 10.258 -28.417 39.860 1.00 69.99 C ANISOU 1224 C ALA A 175 6899 9850 9846 -1321 196 546 C ATOM 1225 O ALA A 175 9.773 -28.323 40.989 1.00 69.56 O ANISOU 1225 O ALA A 175 6815 9840 9774 -1307 158 552 O ATOM 1226 CB ALA A 175 8.818 -28.229 37.827 1.00 67.24 C ANISOU 1226 CB ALA A 175 6684 9401 9465 -1313 201 457 C ATOM 1227 N ILE A 176 11.232 -29.303 39.540 1.00 66.24 N ANISOU 1227 N ILE A 176 6380 9367 9419 -1315 259 594 N ATOM 1228 CA ILE A 176 11.823 -30.266 40.478 1.00 65.97 C ANISOU 1228 CA ILE A 176 6254 9381 9433 -1300 288 660 C ATOM 1229 C ILE A 176 12.594 -29.502 41.578 1.00 69.64 C ANISOU 1229 C ILE A 176 6667 9913 9881 -1330 242 697 C ATOM 1230 O ILE A 176 12.428 -29.831 42.752 1.00 69.21 O ANISOU 1230 O ILE A 176 6556 9913 9827 -1314 222 721 O ATOM 1231 CB ILE A 176 12.719 -31.313 39.740 1.00 69.34 C ANISOU 1231 CB ILE A 176 6659 9777 9910 -1280 376 708 C ATOM 1232 CG1 ILE A 176 11.858 -32.223 38.827 1.00 69.64 C ANISOU 1232 CG1 ILE A 176 6759 9741 9962 -1248 405 664 C ATOM 1233 CG2 ILE A 176 13.536 -32.172 40.731 1.00 70.31 C ANISOU 1233 CG2 ILE A 176 6676 9957 10083 -1268 413 792 C ATOM 1234 CD1 ILE A 176 12.616 -32.952 37.693 1.00 76.82 C ANISOU 1234 CD1 ILE A 176 7704 10594 10889 -1216 487 681 C ATOM 1235 N VAL A 177 13.390 -28.473 41.200 1.00 66.15 N ANISOU 1235 N VAL A 177 6247 9463 9423 -1373 218 702 N ATOM 1236 CA VAL A 177 14.187 -27.651 42.124 1.00 66.20 C ANISOU 1236 CA VAL A 177 6219 9518 9417 -1415 154 735 C ATOM 1237 C VAL A 177 13.242 -26.854 43.059 1.00 69.79 C ANISOU 1237 C VAL A 177 6721 9992 9805 -1410 70 673 C ATOM 1238 O VAL A 177 13.410 -26.942 44.276 1.00 69.51 O ANISOU 1238 O VAL A 177 6642 10014 9754 -1404 33 697 O ATOM 1239 CB VAL A 177 15.192 -26.723 41.376 1.00 70.45 C ANISOU 1239 CB VAL A 177 6769 10030 9967 -1466 142 764 C ATOM 1240 CG1 VAL A 177 15.828 -25.697 42.315 1.00 70.73 C ANISOU 1240 CG1 VAL A 177 6789 10098 9988 -1524 44 784 C ATOM 1241 CG2 VAL A 177 16.277 -27.541 40.680 1.00 70.59 C ANISOU 1241 CG2 VAL A 177 6725 10048 10046 -1455 232 853 C ATOM 1242 N MET A 178 12.240 -26.126 42.499 1.00 66.03 N ANISOU 1242 N MET A 178 6334 9471 9285 -1402 47 601 N ATOM 1243 CA MET A 178 11.264 -25.326 43.266 1.00 65.73 C ANISOU 1243 CA MET A 178 6355 9444 9176 -1381 -19 547 C ATOM 1244 C MET A 178 10.444 -26.190 44.238 1.00 68.99 C ANISOU 1244 C MET A 178 6726 9906 9579 -1318 -7 562 C ATOM 1245 O MET A 178 10.065 -25.709 45.308 1.00 68.75 O ANISOU 1245 O MET A 178 6716 9915 9491 -1288 -58 550 O ATOM 1246 CB MET A 178 10.309 -24.555 42.337 1.00 67.80 C ANISOU 1246 CB MET A 178 6708 9650 9402 -1376 -24 484 C ATOM 1247 CG MET A 178 10.964 -23.396 41.606 1.00 71.76 C ANISOU 1247 CG MET A 178 7258 10108 9900 -1431 -53 467 C ATOM 1248 SD MET A 178 11.452 -22.024 42.676 1.00 76.60 S ANISOU 1248 SD MET A 178 7913 10728 10464 -1468 -161 449 S ATOM 1249 CE MET A 178 12.536 -21.150 41.580 1.00 73.64 C ANISOU 1249 CE MET A 178 7544 10299 10135 -1542 -172 472 C ATOM 1250 N GLY A 179 10.199 -27.445 43.861 1.00 64.91 N ANISOU 1250 N GLY A 179 6157 9386 9120 -1293 60 592 N ATOM 1251 CA GLY A 179 9.476 -28.412 44.678 1.00 64.48 C ANISOU 1251 CA GLY A 179 6045 9374 9081 -1236 79 626 C ATOM 1252 C GLY A 179 10.371 -29.188 45.628 1.00 68.29 C ANISOU 1252 C GLY A 179 6429 9920 9599 -1229 97 693 C ATOM 1253 O GLY A 179 9.891 -30.081 46.332 1.00 67.86 O ANISOU 1253 O GLY A 179 6309 9906 9568 -1180 121 735 O ATOM 1254 N ALA A 180 11.680 -28.853 45.654 1.00 64.92 N ANISOU 1254 N ALA A 180 5982 9506 9181 -1279 87 717 N ATOM 1255 CA ALA A 180 12.685 -29.487 46.511 1.00 64.95 C ANISOU 1255 CA ALA A 180 5888 9574 9217 -1283 101 792 C ATOM 1256 C ALA A 180 13.292 -28.497 47.512 1.00 68.99 C ANISOU 1256 C ALA A 180 6410 10134 9668 -1311 13 791 C ATOM 1257 O ALA A 180 13.745 -28.934 48.567 1.00 68.88 O ANISOU 1257 O ALA A 180 6324 10193 9656 -1296 4 844 O ATOM 1258 CB ALA A 180 13.788 -30.102 45.667 1.00 65.82 C ANISOU 1258 CB ALA A 180 5950 9659 9398 -1316 168 845 C ATOM 1259 N ILE A 181 13.293 -27.176 47.194 1.00 65.47 N ANISOU 1259 N ILE A 181 6057 9646 9172 -1351 -56 733 N ATOM 1260 CA ILE A 181 13.829 -26.090 48.038 1.00 65.81 C ANISOU 1260 CA ILE A 181 6140 9710 9156 -1387 -160 717 C ATOM 1261 C ILE A 181 13.304 -26.219 49.510 1.00 69.65 C ANISOU 1261 C ILE A 181 6622 10270 9573 -1320 -199 714 C ATOM 1262 O ILE A 181 14.152 -26.207 50.407 1.00 69.70 O ANISOU 1262 O ILE A 181 6585 10330 9567 -1342 -248 754 O ATOM 1263 CB ILE A 181 13.530 -24.679 47.432 1.00 68.97 C ANISOU 1263 CB ILE A 181 6658 10037 9510 -1422 -223 641 C ATOM 1264 CG1 ILE A 181 14.362 -24.447 46.146 1.00 69.44 C ANISOU 1264 CG1 ILE A 181 6706 10041 9637 -1491 -196 667 C ATOM 1265 CG2 ILE A 181 13.792 -23.553 48.449 1.00 70.28 C ANISOU 1265 CG2 ILE A 181 6892 10211 9599 -1443 -343 607 C ATOM 1266 CD1 ILE A 181 13.898 -23.289 45.235 1.00 76.71 C ANISOU 1266 CD1 ILE A 181 7729 10885 10532 -1514 -224 599 C ATOM 1267 N PRO A 182 11.982 -26.395 49.809 1.00 65.81 N ANISOU 1267 N PRO A 182 6169 9794 9042 -1234 -176 683 N ATOM 1268 CA PRO A 182 11.578 -26.526 51.222 1.00 65.95 C ANISOU 1268 CA PRO A 182 6177 9891 8991 -1156 -205 697 C ATOM 1269 C PRO A 182 11.971 -27.874 51.837 1.00 69.65 C ANISOU 1269 C PRO A 182 6508 10437 9518 -1127 -146 786 C ATOM 1270 O PRO A 182 12.041 -27.984 53.062 1.00 69.52 O ANISOU 1270 O PRO A 182 6466 10499 9449 -1077 -176 813 O ATOM 1271 CB PRO A 182 10.058 -26.371 51.173 1.00 67.39 C ANISOU 1271 CB PRO A 182 6420 10059 9126 -1071 -182 662 C ATOM 1272 CG PRO A 182 9.680 -26.831 49.824 1.00 71.22 C ANISOU 1272 CG PRO A 182 6889 10480 9691 -1101 -115 660 C ATOM 1273 CD PRO A 182 10.803 -26.446 48.915 1.00 66.81 C ANISOU 1273 CD PRO A 182 6341 9867 9176 -1201 -128 646 C ATOM 1274 N SER A 183 12.232 -28.887 50.989 1.00 65.84 N ANISOU 1274 N SER A 183 5945 9932 9140 -1153 -61 832 N ATOM 1275 CA SER A 183 12.629 -30.231 51.405 1.00 65.72 C ANISOU 1275 CA SER A 183 5799 9975 9196 -1129 8 920 C ATOM 1276 C SER A 183 14.170 -30.365 51.459 1.00 70.35 C ANISOU 1276 C SER A 183 6318 10588 9825 -1201 3 979 C ATOM 1277 O SER A 183 14.678 -31.468 51.678 1.00 70.04 O ANISOU 1277 O SER A 183 6167 10592 9853 -1189 70 1060 O ATOM 1278 CB SER A 183 12.031 -31.268 50.459 1.00 68.64 C ANISOU 1278 CB SER A 183 6133 10293 9653 -1112 99 936 C ATOM 1279 OG SER A 183 12.239 -32.584 50.945 1.00 77.53 O ANISOU 1279 OG SER A 183 7139 11470 10850 -1076 166 1020 O ATOM 1280 N VAL A 184 14.908 -29.246 51.250 1.00 67.49 N ANISOU 1280 N VAL A 184 6018 10196 9428 -1275 -76 948 N ATOM 1281 CA VAL A 184 16.377 -29.192 51.316 1.00 67.89 C ANISOU 1281 CA VAL A 184 6005 10271 9518 -1352 -99 1018 C ATOM 1282 C VAL A 184 16.758 -28.014 52.266 1.00 72.86 C ANISOU 1282 C VAL A 184 6696 10927 10060 -1389 -237 986 C ATOM 1283 O VAL A 184 17.407 -27.046 51.857 1.00 72.74 O ANISOU 1283 O VAL A 184 6730 10863 10043 -1470 -311 971 O ATOM 1284 CB VAL A 184 17.091 -29.115 49.919 1.00 71.58 C ANISOU 1284 CB VAL A 184 6470 10666 10059 -1418 -53 1041 C ATOM 1285 CG1 VAL A 184 18.614 -29.178 50.063 1.00 72.05 C ANISOU 1285 CG1 VAL A 184 6440 10766 10171 -1486 -67 1146 C ATOM 1286 CG2 VAL A 184 16.628 -30.229 48.985 1.00 70.76 C ANISOU 1286 CG2 VAL A 184 6338 10525 10023 -1372 70 1053 C ATOM 1287 N GLY A 185 16.307 -28.108 53.518 1.00 70.07 N ANISOU 1287 N GLY A 185 6345 10645 9633 -1322 -274 978 N ATOM 1288 CA GLY A 185 16.622 -27.140 54.564 1.00 70.97 C ANISOU 1288 CA GLY A 185 6527 10789 9649 -1339 -408 945 C ATOM 1289 C GLY A 185 15.669 -25.993 54.849 1.00 75.42 C ANISOU 1289 C GLY A 185 7251 11308 10097 -1296 -488 833 C ATOM 1290 O GLY A 185 15.581 -25.571 56.006 1.00 75.53 O ANISOU 1290 O GLY A 185 7319 11368 10009 -1253 -572 807 O ATOM 1291 N TRP A 186 14.980 -25.440 53.824 1.00 72.08 N ANISOU 1291 N TRP A 186 6911 10795 9680 -1301 -467 767 N ATOM 1292 CA TRP A 186 14.093 -24.288 54.044 1.00 72.53 C ANISOU 1292 CA TRP A 186 7126 10805 9629 -1258 -536 666 C ATOM 1293 C TRP A 186 12.693 -24.736 54.538 1.00 77.84 C ANISOU 1293 C TRP A 186 7815 11519 10242 -1120 -471 653 C ATOM 1294 O TRP A 186 11.692 -24.607 53.828 1.00 76.74 O ANISOU 1294 O TRP A 186 7720 11331 10105 -1083 -419 619 O ATOM 1295 CB TRP A 186 13.973 -23.401 52.784 1.00 70.76 C ANISOU 1295 CB TRP A 186 6982 10471 9432 -1323 -546 609 C ATOM 1296 CG TRP A 186 13.534 -21.982 53.053 1.00 72.10 C ANISOU 1296 CG TRP A 186 7317 10581 9498 -1314 -648 514 C ATOM 1297 CD1 TRP A 186 13.066 -21.470 54.230 1.00 75.67 C ANISOU 1297 CD1 TRP A 186 7868 11060 9824 -1236 -718 466 C ATOM 1298 CD2 TRP A 186 13.526 -20.896 52.116 1.00 71.86 C ANISOU 1298 CD2 TRP A 186 7378 10448 9477 -1378 -686 458 C ATOM 1299 NE1 TRP A 186 12.771 -20.136 54.085 1.00 75.50 N ANISOU 1299 NE1 TRP A 186 8002 10952 9733 -1247 -799 380 N ATOM 1300 CE2 TRP A 186 13.042 -19.756 52.797 1.00 76.42 C ANISOU 1300 CE2 TRP A 186 8112 10989 9937 -1338 -782 375 C ATOM 1301 CE3 TRP A 186 13.886 -20.772 50.763 1.00 72.60 C ANISOU 1301 CE3 TRP A 186 7440 10479 9666 -1456 -646 473 C ATOM 1302 CZ2 TRP A 186 12.904 -18.512 52.171 1.00 75.91 C ANISOU 1302 CZ2 TRP A 186 8165 10822 9854 -1381 -838 307 C ATOM 1303 CZ3 TRP A 186 13.746 -19.540 50.143 1.00 74.21 C ANISOU 1303 CZ3 TRP A 186 7753 10591 9853 -1497 -701 412 C ATOM 1304 CH2 TRP A 186 13.262 -18.427 50.844 1.00 75.51 C ANISOU 1304 CH2 TRP A 186 8065 10716 9908 -1464 -796 330 C ATOM 1305 N ASN A 187 12.639 -25.201 55.794 1.00 76.37 N ANISOU 1305 N ASN A 187 7592 11427 9998 -1042 -481 689 N ATOM 1306 CA ASN A 187 11.425 -25.637 56.489 1.00 76.81 C ANISOU 1306 CA ASN A 187 7647 11542 9994 -898 -425 703 C ATOM 1307 C ASN A 187 11.544 -25.291 57.982 1.00 83.81 C ANISOU 1307 C ASN A 187 8586 12506 10752 -821 -504 696 C ATOM 1308 O ASN A 187 12.659 -25.127 58.483 1.00 84.11 O ANISOU 1308 O ASN A 187 8612 12569 10777 -889 -585 704 O ATOM 1309 CB ASN A 187 11.146 -27.135 56.265 1.00 76.56 C ANISOU 1309 CB ASN A 187 7456 11560 10073 -865 -303 796 C ATOM 1310 CG ASN A 187 12.312 -28.082 56.456 1.00 99.17 C ANISOU 1310 CG ASN A 187 10179 14479 13021 -923 -278 877 C ATOM 1311 OD1 ASN A 187 13.481 -27.690 56.557 1.00 94.35 O ANISOU 1311 OD1 ASN A 187 9569 13867 12411 -1012 -347 878 O ATOM 1312 ND2 ASN A 187 12.016 -29.372 56.476 1.00 90.83 N ANISOU 1312 ND2 ASN A 187 8995 13468 12048 -876 -177 958 N ATOM 1313 N CYS A 188 10.400 -25.162 58.685 1.00 82.24 N ANISOU 1313 N CYS A 188 8449 12346 10453 -676 -483 688 N ATOM 1314 CA CYS A 188 10.368 -24.772 60.099 1.00 83.98 C ANISOU 1314 CA CYS A 188 8745 12638 10526 -574 -552 674 C ATOM 1315 C CYS A 188 10.561 -25.995 61.046 1.00 89.20 C ANISOU 1315 C CYS A 188 9254 13431 11207 -502 -497 779 C ATOM 1316 O CYS A 188 10.110 -25.962 62.194 1.00 89.60 O ANISOU 1316 O CYS A 188 9341 13562 11140 -365 -508 794 O ATOM 1317 CB CYS A 188 9.076 -24.018 60.414 1.00 84.78 C ANISOU 1317 CB CYS A 188 8990 12723 10501 -433 -546 627 C ATOM 1318 SG CYS A 188 7.582 -25.047 60.445 1.00 88.11 S ANISOU 1318 SG CYS A 188 9303 13212 10962 -279 -394 731 S ATOM 1319 N ILE A 189 11.287 -27.032 60.587 1.00 86.01 N ANISOU 1319 N ILE A 189 8686 13049 10946 -589 -440 854 N ATOM 1320 CA ILE A 189 11.573 -28.246 61.359 1.00 86.31 C ANISOU 1320 CA ILE A 189 8564 13204 11027 -538 -380 962 C ATOM 1321 C ILE A 189 12.552 -27.917 62.521 1.00 92.13 C ANISOU 1321 C ILE A 189 9325 14015 11665 -546 -487 960 C ATOM 1322 O ILE A 189 12.337 -28.392 63.636 1.00 92.16 O ANISOU 1322 O ILE A 189 9283 14130 11604 -429 -469 1015 O ATOM 1323 CB ILE A 189 12.109 -29.378 60.430 1.00 88.63 C ANISOU 1323 CB ILE A 189 8694 13480 11500 -633 -287 1036 C ATOM 1324 CG1 ILE A 189 12.217 -30.742 61.143 1.00 89.11 C ANISOU 1324 CG1 ILE A 189 8580 13653 11622 -568 -202 1157 C ATOM 1325 CG2 ILE A 189 13.396 -28.999 59.702 1.00 89.47 C ANISOU 1325 CG2 ILE A 189 8806 13525 11666 -795 -344 1012 C ATOM 1326 CD1 ILE A 189 10.990 -31.622 61.016 1.00 96.14 C ANISOU 1326 CD1 ILE A 189 9394 14558 12575 -464 -91 1218 C ATOM 1327 N CYS A 190 13.591 -27.095 62.260 1.00 89.95 N ANISOU 1327 N CYS A 190 9120 13678 11379 -680 -601 902 N ATOM 1328 CA CYS A 190 14.585 -26.675 63.254 1.00 91.39 C ANISOU 1328 CA CYS A 190 9338 13913 11475 -715 -730 896 C ATOM 1329 C CYS A 190 14.374 -25.185 63.602 1.00 96.00 C ANISOU 1329 C CYS A 190 10149 14425 11903 -701 -872 770 C ATOM 1330 O CYS A 190 15.250 -24.539 64.187 1.00 96.74 O ANISOU 1330 O CYS A 190 10314 14517 11928 -767 -1016 736 O ATOM 1331 CB CYS A 190 16.002 -26.950 62.755 1.00 91.99 C ANISOU 1331 CB CYS A 190 9304 13978 11670 -883 -760 953 C ATOM 1332 SG CYS A 190 16.320 -28.688 62.349 1.00 95.10 S ANISOU 1332 SG CYS A 190 9448 14445 12240 -891 -590 1100 S ATOM 1333 N ASP A 191 13.182 -24.668 63.256 1.00 91.90 N ANISOU 1333 N ASP A 191 9743 13845 11331 -613 -832 706 N ATOM 1334 CA ASP A 191 12.703 -23.307 63.499 1.00 92.34 C ANISOU 1334 CA ASP A 191 10023 13822 11238 -568 -933 587 C ATOM 1335 C ASP A 191 11.198 -23.408 63.813 1.00 95.51 C ANISOU 1335 C ASP A 191 10474 14258 11557 -373 -834 592 C ATOM 1336 O ASP A 191 10.365 -22.734 63.201 1.00 94.68 O ANISOU 1336 O ASP A 191 10476 14069 11429 -344 -812 535 O ATOM 1337 CB ASP A 191 13.018 -22.412 62.277 1.00 93.79 C ANISOU 1337 CB ASP A 191 10283 13863 11492 -715 -985 516 C ATOM 1338 CG ASP A 191 12.874 -20.913 62.488 1.00104.36 C ANISOU 1338 CG ASP A 191 11854 15101 12697 -711 -1120 392 C ATOM 1339 OD1 ASP A 191 12.952 -20.462 63.654 1.00106.20 O ANISOU 1339 OD1 ASP A 191 12205 15368 12779 -636 -1219 350 O ATOM 1340 OD2 ASP A 191 12.742 -20.185 61.482 1.00109.36 O ANISOU 1340 OD2 ASP A 191 12555 15620 13378 -787 -1130 338 O ATOM 1341 N ILE A 192 10.873 -24.290 64.786 1.00 92.04 N ANISOU 1341 N ILE A 192 9943 13949 11078 -238 -769 676 N ATOM 1342 CA ILE A 192 9.540 -24.690 65.255 1.00 91.60 C ANISOU 1342 CA ILE A 192 9876 13962 10964 -40 -658 731 C ATOM 1343 C ILE A 192 8.664 -23.478 65.689 1.00 96.00 C ANISOU 1343 C ILE A 192 10663 14475 11337 94 -706 643 C ATOM 1344 O ILE A 192 7.437 -23.579 65.625 1.00 95.19 O ANISOU 1344 O ILE A 192 10568 14388 11214 232 -606 684 O ATOM 1345 CB ILE A 192 9.683 -25.738 66.406 1.00 95.14 C ANISOU 1345 CB ILE A 192 10190 14568 11392 67 -613 839 C ATOM 1346 CG1 ILE A 192 8.458 -26.666 66.542 1.00 95.07 C ANISOU 1346 CG1 ILE A 192 10061 14638 11426 226 -459 954 C ATOM 1347 CG2 ILE A 192 10.156 -25.156 67.749 1.00 97.42 C ANISOU 1347 CG2 ILE A 192 10605 14918 11490 144 -734 793 C ATOM 1348 CD1 ILE A 192 8.384 -27.812 65.515 1.00101.34 C ANISOU 1348 CD1 ILE A 192 10653 15415 12436 135 -346 1041 C ATOM 1349 N GLU A 193 9.280 -22.352 66.099 1.00 93.52 N ANISOU 1349 N GLU A 193 10537 14101 10897 55 -857 530 N ATOM 1350 CA GLU A 193 8.552 -21.152 66.516 1.00 94.20 C ANISOU 1350 CA GLU A 193 10863 14129 10801 180 -911 436 C ATOM 1351 C GLU A 193 8.030 -20.364 65.308 1.00 96.50 C ANISOU 1351 C GLU A 193 11239 14282 11144 113 -893 372 C ATOM 1352 O GLU A 193 7.007 -19.687 65.427 1.00 96.39 O ANISOU 1352 O GLU A 193 11369 14237 11019 252 -863 341 O ATOM 1353 CB GLU A 193 9.434 -20.246 67.392 1.00 97.31 C ANISOU 1353 CB GLU A 193 11437 14493 11043 153 -1094 333 C ATOM 1354 CG GLU A 193 9.674 -20.773 68.801 1.00109.91 C ANISOU 1354 CG GLU A 193 13012 16230 12519 279 -1119 381 C ATOM 1355 CD GLU A 193 8.475 -20.844 69.732 1.00133.13 C ANISOU 1355 CD GLU A 193 16027 19261 15298 551 -1031 420 C ATOM 1356 OE1 GLU A 193 7.572 -19.983 69.624 1.00128.96 O ANISOU 1356 OE1 GLU A 193 15674 18661 14666 660 -1016 362 O ATOM 1357 OE2 GLU A 193 8.463 -21.743 70.603 1.00128.69 O1- ANISOU 1357 OE2 GLU A 193 15345 18842 14708 661 -977 517 O1- ATOM 1358 N ASN A 194 8.726 -20.452 64.155 1.00 91.49 N ANISOU 1358 N ASN A 194 10515 13572 10675 -88 -906 362 N ATOM 1359 CA ASN A 194 8.354 -19.741 62.930 1.00 90.32 C ANISOU 1359 CA ASN A 194 10431 13298 10590 -167 -892 307 C ATOM 1360 C ASN A 194 7.591 -20.661 61.944 1.00 91.87 C ANISOU 1360 C ASN A 194 10459 13513 10935 -168 -735 396 C ATOM 1361 O ASN A 194 7.768 -20.549 60.727 1.00 90.47 O ANISOU 1361 O ASN A 194 10244 13253 10878 -299 -719 379 O ATOM 1362 CB ASN A 194 9.596 -19.136 62.264 1.00 91.52 C ANISOU 1362 CB ASN A 194 10607 13347 10818 -379 -1013 241 C ATOM 1363 CG ASN A 194 10.182 -17.961 63.012 1.00118.50 C ANISOU 1363 CG ASN A 194 14228 16701 14095 -396 -1188 136 C ATOM 1364 OD1 ASN A 194 9.521 -16.942 63.246 1.00114.24 O ANISOU 1364 OD1 ASN A 194 13890 16094 13423 -303 -1225 53 O ATOM 1365 ND2 ASN A 194 11.457 -18.054 63.356 1.00111.66 N ANISOU 1365 ND2 ASN A 194 13318 15847 13259 -521 -1303 139 N ATOM 1366 N CYS A 195 6.710 -21.535 62.475 1.00 87.74 N ANISOU 1366 N CYS A 195 9842 13096 10400 -15 -624 495 N ATOM 1367 CA CYS A 195 5.874 -22.425 61.664 1.00 86.08 C ANISOU 1367 CA CYS A 195 9481 12903 10323 -2 -489 587 C ATOM 1368 C CYS A 195 4.578 -21.714 61.289 1.00 89.63 C ANISOU 1368 C CYS A 195 10041 13303 10713 99 -440 574 C ATOM 1369 O CYS A 195 4.010 -20.992 62.114 1.00 90.16 O ANISOU 1369 O CYS A 195 10255 13384 10617 249 -459 550 O ATOM 1370 CB CYS A 195 5.594 -23.741 62.386 1.00 86.17 C ANISOU 1370 CB CYS A 195 9320 13046 10373 99 -401 716 C ATOM 1371 SG CYS A 195 6.979 -24.910 62.384 1.00 89.55 S ANISOU 1371 SG CYS A 195 9555 13527 10941 -42 -410 767 S ATOM 1372 N SER A 196 4.110 -21.921 60.046 1.00 84.95 N ANISOU 1372 N SER A 196 9381 12652 10246 22 -376 594 N ATOM 1373 CA SER A 196 2.882 -21.305 59.543 1.00 84.53 C ANISOU 1373 CA SER A 196 9409 12552 10157 100 -324 597 C ATOM 1374 C SER A 196 1.642 -22.071 60.013 1.00 88.46 C ANISOU 1374 C SER A 196 9813 13146 10654 269 -215 733 C ATOM 1375 O SER A 196 1.709 -23.282 60.237 1.00 87.64 O ANISOU 1375 O SER A 196 9536 13119 10643 274 -164 830 O ATOM 1376 CB SER A 196 2.905 -21.223 58.021 1.00 86.70 C ANISOU 1376 CB SER A 196 9648 12732 10564 -52 -308 568 C ATOM 1377 OG SER A 196 3.024 -22.500 57.418 1.00 93.72 O ANISOU 1377 OG SER A 196 10347 13648 11613 -128 -246 645 O ATOM 1378 N ASN A 197 0.513 -21.350 60.162 1.00 85.61 N ANISOU 1378 N ASN A 197 9561 12777 10190 409 -177 751 N ATOM 1379 CA ASN A 197 -0.770 -21.896 60.613 1.00 85.67 C ANISOU 1379 CA ASN A 197 9490 12873 10186 586 -73 898 C ATOM 1380 C ASN A 197 -1.392 -22.834 59.569 1.00 88.32 C ANISOU 1380 C ASN A 197 9649 13203 10707 510 0 998 C ATOM 1381 O ASN A 197 -2.035 -23.810 59.954 1.00 87.86 O ANISOU 1381 O ASN A 197 9445 13230 10707 600 71 1140 O ATOM 1382 CB ASN A 197 -1.753 -20.769 60.946 1.00 87.79 C ANISOU 1382 CB ASN A 197 9936 13125 10296 750 -52 894 C ATOM 1383 CG ASN A 197 -1.327 -19.880 62.092 1.00113.91 C ANISOU 1383 CG ASN A 197 13438 16440 13402 862 -121 806 C ATOM 1384 OD1 ASN A 197 -1.075 -20.335 63.215 1.00109.57 O ANISOU 1384 OD1 ASN A 197 12865 15986 12781 967 -125 845 O ATOM 1385 ND2 ASN A 197 -1.297 -18.578 61.849 1.00106.46 N ANISOU 1385 ND2 ASN A 197 12699 15395 12357 852 -177 688 N ATOM 1386 N MET A 198 -1.205 -22.543 58.264 1.00 84.01 N ANISOU 1386 N MET A 198 9116 12554 10250 350 -22 927 N ATOM 1387 CA MET A 198 -1.745 -23.352 57.166 1.00 82.87 C ANISOU 1387 CA MET A 198 8830 12386 10270 265 30 1000 C ATOM 1388 C MET A 198 -0.918 -24.636 56.997 1.00 86.32 C ANISOU 1388 C MET A 198 9104 12845 10850 154 29 1025 C ATOM 1389 O MET A 198 -1.473 -25.732 57.100 1.00 85.72 O ANISOU 1389 O MET A 198 8876 12823 10870 192 86 1149 O ATOM 1390 CB MET A 198 -1.776 -22.539 55.862 1.00 84.62 C ANISOU 1390 CB MET A 198 9138 12494 10519 143 5 910 C ATOM 1391 CG MET A 198 -2.654 -23.139 54.782 1.00 87.52 C ANISOU 1391 CG MET A 198 9399 12839 11018 93 55 990 C ATOM 1392 SD MET A 198 -3.918 -21.994 54.174 1.00 91.81 S ANISOU 1392 SD MET A 198 10054 13336 11492 156 84 1004 S ATOM 1393 CE MET A 198 -2.904 -20.777 53.360 1.00 88.22 C ANISOU 1393 CE MET A 198 9757 12766 10998 16 11 820 C ATOM 1394 N ALA A 199 0.399 -24.497 56.743 1.00 82.81 N ANISOU 1394 N ALA A 199 8688 12354 10422 19 -33 917 N ATOM 1395 CA ALA A 199 1.324 -25.619 56.587 1.00 82.20 C ANISOU 1395 CA ALA A 199 8472 12293 10468 -84 -31 935 C ATOM 1396 C ALA A 199 2.202 -25.737 57.850 1.00 86.87 C ANISOU 1396 C ALA A 199 9060 12962 10984 -36 -66 930 C ATOM 1397 O ALA A 199 3.099 -24.915 58.056 1.00 86.85 O ANISOU 1397 O ALA A 199 9168 12929 10902 -88 -144 829 O ATOM 1398 CB ALA A 199 2.169 -25.439 55.335 1.00 82.25 C ANISOU 1398 CB ALA A 199 8497 12199 10555 -263 -66 843 C ATOM 1399 N PRO A 200 1.929 -26.726 58.734 1.00 83.68 N ANISOU 1399 N PRO A 200 8532 12661 10602 66 -15 1044 N ATOM 1400 CA PRO A 200 2.675 -26.813 60.004 1.00 84.21 C ANISOU 1400 CA PRO A 200 8599 12815 10582 128 -48 1046 C ATOM 1401 C PRO A 200 4.148 -27.235 59.873 1.00 87.51 C ANISOU 1401 C PRO A 200 8959 13225 11068 -16 -92 1002 C ATOM 1402 O PRO A 200 4.890 -27.076 60.845 1.00 87.84 O ANISOU 1402 O PRO A 200 9027 13326 11024 12 -142 984 O ATOM 1403 CB PRO A 200 1.897 -27.870 60.796 1.00 86.23 C ANISOU 1403 CB PRO A 200 8709 13181 10873 271 35 1201 C ATOM 1404 CG PRO A 200 0.563 -27.972 60.122 1.00 90.32 C ANISOU 1404 CG PRO A 200 9198 13668 11452 314 95 1274 C ATOM 1405 CD PRO A 200 0.864 -27.746 58.682 1.00 85.00 C ANISOU 1405 CD PRO A 200 8555 12872 10868 138 68 1185 C ATOM 1406 N LEU A 201 4.580 -27.753 58.705 1.00 82.80 N ANISOU 1406 N LEU A 201 8287 12557 10616 -163 -74 991 N ATOM 1407 CA LEU A 201 5.969 -28.183 58.496 1.00 82.21 C ANISOU 1407 CA LEU A 201 8149 12474 10613 -294 -102 968 C ATOM 1408 C LEU A 201 6.756 -27.189 57.613 1.00 85.79 C ANISOU 1408 C LEU A 201 8716 12825 11057 -432 -174 854 C ATOM 1409 O LEU A 201 7.982 -27.297 57.529 1.00 85.36 O ANISOU 1409 O LEU A 201 8629 12764 11040 -535 -211 837 O ATOM 1410 CB LEU A 201 6.027 -29.594 57.879 1.00 81.48 C ANISOU 1410 CB LEU A 201 7888 12381 10691 -346 -21 1051 C ATOM 1411 CG LEU A 201 5.823 -30.781 58.830 1.00 86.30 C ANISOU 1411 CG LEU A 201 8346 13098 11344 -249 40 1174 C ATOM 1412 CD1 LEU A 201 4.344 -31.110 59.013 1.00 86.46 C ANISOU 1412 CD1 LEU A 201 8327 13146 11377 -124 98 1262 C ATOM 1413 CD2 LEU A 201 6.520 -32.014 58.298 1.00 88.09 C ANISOU 1413 CD2 LEU A 201 8431 13312 11728 -340 91 1225 C ATOM 1414 N TYR A 202 6.061 -26.221 56.980 1.00 82.23 N ANISOU 1414 N TYR A 202 8388 12296 10558 -430 -192 789 N ATOM 1415 CA TYR A 202 6.666 -25.200 56.116 1.00 81.93 C ANISOU 1415 CA TYR A 202 8458 12159 10513 -549 -256 688 C ATOM 1416 C TYR A 202 6.861 -23.882 56.870 1.00 86.80 C ANISOU 1416 C TYR A 202 9240 12762 10978 -514 -354 607 C ATOM 1417 O TYR A 202 5.984 -23.467 57.631 1.00 86.84 O ANISOU 1417 O TYR A 202 9325 12801 10869 -378 -351 609 O ATOM 1418 CB TYR A 202 5.797 -24.965 54.866 1.00 82.36 C ANISOU 1418 CB TYR A 202 8543 12132 10618 -576 -214 669 C ATOM 1419 CG TYR A 202 6.093 -25.857 53.675 1.00 83.18 C ANISOU 1419 CG TYR A 202 8541 12193 10869 -678 -161 694 C ATOM 1420 CD1 TYR A 202 6.334 -27.219 53.838 1.00 84.93 C ANISOU 1420 CD1 TYR A 202 8616 12466 11188 -678 -104 776 C ATOM 1421 CD2 TYR A 202 6.030 -25.360 52.377 1.00 83.39 C ANISOU 1421 CD2 TYR A 202 8622 12128 10936 -762 -162 640 C ATOM 1422 CE1 TYR A 202 6.578 -28.048 52.744 1.00 85.14 C ANISOU 1422 CE1 TYR A 202 8566 12443 11340 -760 -56 794 C ATOM 1423 CE2 TYR A 202 6.260 -26.182 51.274 1.00 83.64 C ANISOU 1423 CE2 TYR A 202 8574 12118 11087 -840 -113 660 C ATOM 1424 CZ TYR A 202 6.541 -27.524 51.463 1.00 90.92 C ANISOU 1424 CZ TYR A 202 9365 13083 12098 -838 -62 733 C ATOM 1425 OH TYR A 202 6.762 -28.340 50.380 1.00 91.35 O ANISOU 1425 OH TYR A 202 9361 13087 12261 -905 -14 747 O ATOM 1426 N SER A 203 8.013 -23.226 56.643 1.00 83.82 N ANISOU 1426 N SER A 203 8916 12330 10600 -635 -442 542 N ATOM 1427 CA SER A 203 8.378 -21.952 57.266 1.00 84.70 C ANISOU 1427 CA SER A 203 9193 12407 10584 -633 -559 456 C ATOM 1428 C SER A 203 7.596 -20.789 56.645 1.00 88.55 C ANISOU 1428 C SER A 203 9830 12800 11016 -616 -572 382 C ATOM 1429 O SER A 203 7.304 -20.822 55.446 1.00 87.29 O ANISOU 1429 O SER A 203 9639 12582 10945 -677 -520 381 O ATOM 1430 CB SER A 203 9.878 -21.709 57.125 1.00 88.65 C ANISOU 1430 CB SER A 203 9677 12875 11132 -784 -653 433 C ATOM 1431 OG SER A 203 10.293 -20.537 57.808 1.00 98.74 O ANISOU 1431 OG SER A 203 11111 14113 12291 -791 -786 354 O ATOM 1432 N CYS A 204 7.266 -19.761 57.464 1.00 86.07 N ANISOU 1432 N CYS A 204 9684 12469 10549 -527 -641 318 N ATOM 1433 CA CYS A 204 6.536 -18.560 57.034 1.00 86.05 C ANISOU 1433 CA CYS A 204 9843 12376 10476 -495 -657 247 C ATOM 1434 C CYS A 204 7.359 -17.765 56.017 1.00 88.47 C ANISOU 1434 C CYS A 204 10193 12570 10853 -661 -727 181 C ATOM 1435 O CYS A 204 6.786 -17.231 55.069 1.00 87.50 O ANISOU 1435 O CYS A 204 10113 12377 10756 -678 -691 157 O ATOM 1436 CB CYS A 204 6.148 -17.687 58.225 1.00 87.95 C ANISOU 1436 CB CYS A 204 10265 12621 10531 -358 -720 194 C ATOM 1437 SG CYS A 204 4.457 -17.948 58.829 1.00 92.11 S ANISOU 1437 SG CYS A 204 10814 13226 10956 -121 -599 266 S ATOM 1438 N SER A 205 8.697 -17.707 56.206 1.00 84.60 N ANISOU 1438 N SER A 205 9679 12067 10399 -781 -825 166 N ATOM 1439 CA SER A 205 9.641 -17.012 55.323 1.00 83.97 C ANISOU 1439 CA SER A 205 9616 11889 10399 -942 -899 128 C ATOM 1440 C SER A 205 9.629 -17.610 53.910 1.00 85.48 C ANISOU 1440 C SER A 205 9676 12064 10738 -1021 -799 176 C ATOM 1441 O SER A 205 9.814 -16.875 52.938 1.00 84.87 O ANISOU 1441 O SER A 205 9640 11899 10710 -1104 -819 142 O ATOM 1442 CB SER A 205 11.054 -17.065 55.898 1.00 88.12 C ANISOU 1442 CB SER A 205 10106 12429 10946 -1046 -1014 138 C ATOM 1443 OG SER A 205 11.504 -18.399 56.073 1.00 95.82 O ANISOU 1443 OG SER A 205 10903 13505 11999 -1057 -950 230 O ATOM 1444 N TYR A 206 9.394 -18.935 53.802 1.00 80.37 N ANISOU 1444 N TYR A 206 8879 11499 10160 -989 -695 254 N ATOM 1445 CA TYR A 206 9.318 -19.639 52.525 1.00 78.69 C ANISOU 1445 CA TYR A 206 8552 11272 10075 -1047 -599 298 C ATOM 1446 C TYR A 206 7.995 -19.331 51.820 1.00 81.24 C ANISOU 1446 C TYR A 206 8930 11558 10379 -982 -530 277 C ATOM 1447 O TYR A 206 8.016 -19.045 50.625 1.00 80.19 O ANISOU 1447 O TYR A 206 8797 11361 10311 -1053 -507 262 O ATOM 1448 CB TYR A 206 9.492 -21.163 52.710 1.00 79.29 C ANISOU 1448 CB TYR A 206 8462 11436 10226 -1030 -519 385 C ATOM 1449 CG TYR A 206 9.270 -21.960 51.440 1.00 79.83 C ANISOU 1449 CG TYR A 206 8436 11485 10412 -1070 -421 423 C ATOM 1450 CD1 TYR A 206 10.277 -22.086 50.486 1.00 81.55 C ANISOU 1450 CD1 TYR A 206 8597 11661 10727 -1184 -417 438 C ATOM 1451 CD2 TYR A 206 8.051 -22.583 51.188 1.00 79.92 C ANISOU 1451 CD2 TYR A 206 8416 11516 10436 -989 -336 451 C ATOM 1452 CE1 TYR A 206 10.071 -22.802 49.307 1.00 81.47 C ANISOU 1452 CE1 TYR A 206 8520 11627 10808 -1208 -329 464 C ATOM 1453 CE2 TYR A 206 7.831 -23.292 50.009 1.00 80.04 C ANISOU 1453 CE2 TYR A 206 8361 11501 10550 -1029 -262 476 C ATOM 1454 CZ TYR A 206 8.846 -23.404 49.074 1.00 87.07 C ANISOU 1454 CZ TYR A 206 9214 12348 11522 -1134 -258 476 C ATOM 1455 OH TYR A 206 8.635 -24.122 47.922 1.00 87.15 O ANISOU 1455 OH TYR A 206 9171 12326 11615 -1160 -186 495 O ATOM 1456 N LEU A 207 6.852 -19.418 52.547 1.00 77.49 N ANISOU 1456 N LEU A 207 8495 11131 9818 -845 -493 290 N ATOM 1457 CA LEU A 207 5.509 -19.186 51.999 1.00 76.60 C ANISOU 1457 CA LEU A 207 8423 10998 9685 -771 -425 294 C ATOM 1458 C LEU A 207 5.332 -17.755 51.488 1.00 80.21 C ANISOU 1458 C LEU A 207 9028 11360 10089 -795 -471 216 C ATOM 1459 O LEU A 207 4.659 -17.571 50.475 1.00 79.04 O ANISOU 1459 O LEU A 207 8882 11173 9977 -806 -418 218 O ATOM 1460 CB LEU A 207 4.405 -19.502 53.021 1.00 76.94 C ANISOU 1460 CB LEU A 207 8475 11118 9641 -608 -380 344 C ATOM 1461 CG LEU A 207 4.196 -20.973 53.420 1.00 81.28 C ANISOU 1461 CG LEU A 207 8866 11762 10255 -561 -312 442 C ATOM 1462 CD1 LEU A 207 2.997 -21.106 54.320 1.00 81.83 C ANISOU 1462 CD1 LEU A 207 8950 11902 10240 -391 -264 504 C ATOM 1463 CD2 LEU A 207 3.978 -21.872 52.205 1.00 82.72 C ANISOU 1463 CD2 LEU A 207 8927 11925 10576 -634 -243 486 C ATOM 1464 N VAL A 208 5.936 -16.756 52.170 1.00 77.54 N ANISOU 1464 N VAL A 208 8814 10982 9667 -805 -573 149 N ATOM 1465 CA VAL A 208 5.889 -15.345 51.759 1.00 77.69 C ANISOU 1465 CA VAL A 208 8982 10898 9640 -834 -630 73 C ATOM 1466 C VAL A 208 6.683 -15.212 50.442 1.00 80.87 C ANISOU 1466 C VAL A 208 9322 11236 10168 -987 -638 67 C ATOM 1467 O VAL A 208 6.204 -14.563 49.512 1.00 80.10 O ANISOU 1467 O VAL A 208 9270 11077 10087 -1004 -610 46 O ATOM 1468 CB VAL A 208 6.397 -14.383 52.875 1.00 82.91 C ANISOU 1468 CB VAL A 208 9797 11522 10184 -811 -753 2 C ATOM 1469 CG1 VAL A 208 6.596 -12.958 52.357 1.00 83.22 C ANISOU 1469 CG1 VAL A 208 9978 11436 10205 -874 -828 -76 C ATOM 1470 CG2 VAL A 208 5.446 -14.381 54.070 1.00 83.35 C ANISOU 1470 CG2 VAL A 208 9939 11636 10093 -631 -730 7 C ATOM 1471 N PHE A 209 7.852 -15.888 50.353 1.00 77.27 N ANISOU 1471 N PHE A 209 8753 10803 9801 -1086 -663 100 N ATOM 1472 CA PHE A 209 8.723 -15.915 49.174 1.00 76.66 C ANISOU 1472 CA PHE A 209 8600 10681 9845 -1217 -660 118 C ATOM 1473 C PHE A 209 8.047 -16.654 48.006 1.00 79.22 C ANISOU 1473 C PHE A 209 8838 11020 10243 -1209 -542 156 C ATOM 1474 O PHE A 209 8.096 -16.160 46.882 1.00 78.56 O ANISOU 1474 O PHE A 209 8764 10876 10207 -1266 -527 144 O ATOM 1475 CB PHE A 209 10.081 -16.570 49.517 1.00 78.77 C ANISOU 1475 CB PHE A 209 8762 10986 10180 -1301 -705 165 C ATOM 1476 CG PHE A 209 10.964 -16.927 48.339 1.00 79.90 C ANISOU 1476 CG PHE A 209 8798 11109 10453 -1409 -671 214 C ATOM 1477 CD1 PHE A 209 11.727 -15.957 47.700 1.00 83.42 C ANISOU 1477 CD1 PHE A 209 9277 11475 10943 -1507 -737 203 C ATOM 1478 CD2 PHE A 209 11.053 -18.240 47.888 1.00 81.32 C ANISOU 1478 CD2 PHE A 209 8843 11346 10708 -1406 -574 279 C ATOM 1479 CE1 PHE A 209 12.541 -16.288 46.612 1.00 84.00 C ANISOU 1479 CE1 PHE A 209 9248 11538 11131 -1589 -696 263 C ATOM 1480 CE2 PHE A 209 11.867 -18.570 46.800 1.00 83.82 C ANISOU 1480 CE2 PHE A 209 9074 11642 11130 -1487 -535 327 C ATOM 1481 CZ PHE A 209 12.608 -17.593 46.172 1.00 82.33 C ANISOU 1481 CZ PHE A 209 8915 11385 10980 -1573 -593 323 C ATOM 1482 N TRP A 210 7.439 -17.831 48.273 1.00 75.01 N ANISOU 1482 N TRP A 210 8220 10563 9719 -1140 -466 206 N ATOM 1483 CA TRP A 210 6.761 -18.681 47.288 1.00 73.83 C ANISOU 1483 CA TRP A 210 7989 10426 9637 -1131 -369 245 C ATOM 1484 C TRP A 210 5.547 -17.972 46.670 1.00 76.55 C ANISOU 1484 C TRP A 210 8414 10732 9941 -1084 -337 220 C ATOM 1485 O TRP A 210 5.373 -18.030 45.451 1.00 75.51 O ANISOU 1485 O TRP A 210 8257 10565 9866 -1129 -295 222 O ATOM 1486 CB TRP A 210 6.328 -20.005 47.941 1.00 72.48 C ANISOU 1486 CB TRP A 210 7720 10338 9481 -1062 -315 307 C ATOM 1487 CG TRP A 210 5.584 -20.944 47.037 1.00 72.81 C ANISOU 1487 CG TRP A 210 7685 10385 9593 -1054 -232 349 C ATOM 1488 CD1 TRP A 210 4.234 -21.124 46.975 1.00 75.50 C ANISOU 1488 CD1 TRP A 210 8031 10742 9912 -976 -188 375 C ATOM 1489 CD2 TRP A 210 6.154 -21.843 46.078 1.00 72.23 C ANISOU 1489 CD2 TRP A 210 7523 10299 9623 -1124 -190 373 C ATOM 1490 NE1 TRP A 210 3.926 -22.083 46.039 1.00 74.42 N ANISOU 1490 NE1 TRP A 210 7815 10597 9862 -1006 -135 410 N ATOM 1491 CE2 TRP A 210 5.086 -22.539 45.469 1.00 75.68 C ANISOU 1491 CE2 TRP A 210 7926 10736 10093 -1091 -132 402 C ATOM 1492 CE3 TRP A 210 7.468 -22.124 45.664 1.00 73.56 C ANISOU 1492 CE3 TRP A 210 7641 10453 9857 -1207 -195 381 C ATOM 1493 CZ2 TRP A 210 5.291 -23.504 44.476 1.00 74.59 C ANISOU 1493 CZ2 TRP A 210 7722 10576 10044 -1137 -87 422 C ATOM 1494 CZ3 TRP A 210 7.669 -23.083 44.684 1.00 74.63 C ANISOU 1494 CZ3 TRP A 210 7707 10573 10075 -1240 -134 409 C ATOM 1495 CH2 TRP A 210 6.590 -23.763 44.104 1.00 74.82 C ANISOU 1495 CH2 TRP A 210 7714 10589 10123 -1205 -83 422 C ATOM 1496 N ALA A 211 4.716 -17.315 47.507 1.00 72.89 N ANISOU 1496 N ALA A 211 8046 10276 9372 -987 -354 202 N ATOM 1497 CA ALA A 211 3.518 -16.604 47.061 1.00 72.27 C ANISOU 1497 CA ALA A 211 8045 10168 9245 -928 -318 192 C ATOM 1498 C ALA A 211 3.870 -15.354 46.252 1.00 75.47 C ANISOU 1498 C ALA A 211 8540 10485 9651 -997 -356 132 C ATOM 1499 O ALA A 211 3.217 -15.104 45.241 1.00 74.66 O ANISOU 1499 O ALA A 211 8442 10356 9571 -1005 -309 137 O ATOM 1500 CB ALA A 211 2.653 -16.223 48.251 1.00 73.62 C ANISOU 1500 CB ALA A 211 8300 10374 9297 -791 -321 199 C ATOM 1501 N ILE A 212 4.905 -14.589 46.672 1.00 71.98 N ANISOU 1501 N ILE A 212 8162 9996 9192 -1053 -445 82 N ATOM 1502 CA ILE A 212 5.316 -13.369 45.970 1.00 71.77 C ANISOU 1502 CA ILE A 212 8215 9877 9177 -1124 -490 33 C ATOM 1503 C ILE A 212 6.063 -13.738 44.662 1.00 74.45 C ANISOU 1503 C ILE A 212 8452 10200 9638 -1235 -463 59 C ATOM 1504 O ILE A 212 6.067 -12.929 43.736 1.00 73.92 O ANISOU 1504 O ILE A 212 8420 10071 9596 -1277 -461 42 O ATOM 1505 CB ILE A 212 6.148 -12.409 46.881 1.00 75.94 C ANISOU 1505 CB ILE A 212 8851 10351 9652 -1151 -610 -22 C ATOM 1506 CG1 ILE A 212 6.009 -10.929 46.461 1.00 76.84 C ANISOU 1506 CG1 ILE A 212 9096 10362 9738 -1170 -653 -77 C ATOM 1507 CG2 ILE A 212 7.615 -12.827 47.058 1.00 76.95 C ANISOU 1507 CG2 ILE A 212 8897 10485 9854 -1259 -679 -4 C ATOM 1508 CD1 ILE A 212 4.706 -10.234 46.907 1.00 84.09 C ANISOU 1508 CD1 ILE A 212 10148 11265 10535 -1038 -621 -106 C ATOM 1509 N PHE A 213 6.658 -14.953 44.581 1.00 70.24 N ANISOU 1509 N PHE A 213 7794 9719 9174 -1269 -435 106 N ATOM 1510 CA PHE A 213 7.375 -15.429 43.393 1.00 69.42 C ANISOU 1510 CA PHE A 213 7597 9606 9173 -1352 -398 139 C ATOM 1511 C PHE A 213 6.389 -15.800 42.278 1.00 71.75 C ANISOU 1511 C PHE A 213 7871 9905 9487 -1324 -311 151 C ATOM 1512 O PHE A 213 6.621 -15.436 41.126 1.00 71.15 O ANISOU 1512 O PHE A 213 7790 9789 9455 -1372 -291 150 O ATOM 1513 CB PHE A 213 8.279 -16.631 43.735 1.00 71.24 C ANISOU 1513 CB PHE A 213 7714 9891 9463 -1381 -390 188 C ATOM 1514 CG PHE A 213 9.084 -17.191 42.583 1.00 72.62 C ANISOU 1514 CG PHE A 213 7799 10057 9734 -1448 -343 231 C ATOM 1515 CD1 PHE A 213 10.255 -16.570 42.164 1.00 76.22 C ANISOU 1515 CD1 PHE A 213 8244 10473 10244 -1531 -387 249 C ATOM 1516 CD2 PHE A 213 8.691 -18.361 41.944 1.00 74.29 C ANISOU 1516 CD2 PHE A 213 7941 10300 9984 -1423 -259 260 C ATOM 1517 CE1 PHE A 213 11.000 -17.090 41.102 1.00 76.97 C ANISOU 1517 CE1 PHE A 213 8258 10567 10421 -1573 -332 302 C ATOM 1518 CE2 PHE A 213 9.438 -18.882 40.883 1.00 77.01 C ANISOU 1518 CE2 PHE A 213 8222 10635 10405 -1467 -211 297 C ATOM 1519 CZ PHE A 213 10.586 -18.242 40.468 1.00 75.51 C ANISOU 1519 CZ PHE A 213 8020 10413 10259 -1535 -241 321 C ATOM 1520 N ASN A 214 5.306 -16.526 42.617 1.00 67.28 N ANISOU 1520 N ASN A 214 7286 9388 8889 -1246 -265 170 N ATOM 1521 CA ASN A 214 4.289 -16.953 41.654 1.00 66.16 C ANISOU 1521 CA ASN A 214 7121 9252 8765 -1223 -198 189 C ATOM 1522 C ASN A 214 3.399 -15.782 41.215 1.00 69.51 C ANISOU 1522 C ASN A 214 7637 9638 9135 -1195 -193 164 C ATOM 1523 O ASN A 214 2.939 -15.778 40.072 1.00 68.74 O ANISOU 1523 O ASN A 214 7530 9525 9064 -1212 -153 171 O ATOM 1524 CB ASN A 214 3.433 -18.078 42.232 1.00 66.04 C ANISOU 1524 CB ASN A 214 7049 9299 8746 -1155 -162 235 C ATOM 1525 CG ASN A 214 4.169 -19.390 42.363 1.00 85.55 C ANISOU 1525 CG ASN A 214 9417 11802 11285 -1183 -147 268 C ATOM 1526 OD1 ASN A 214 4.526 -20.037 41.372 1.00 78.01 O ANISOU 1526 OD1 ASN A 214 8414 10831 10396 -1231 -115 277 O ATOM 1527 ND2 ASN A 214 4.382 -19.829 43.593 1.00 77.64 N ANISOU 1527 ND2 ASN A 214 8387 10849 10265 -1145 -165 289 N ATOM 1528 N LEU A 215 3.164 -14.794 42.105 1.00 66.11 N ANISOU 1528 N LEU A 215 7301 9190 8627 -1148 -234 136 N ATOM 1529 CA LEU A 215 2.333 -13.629 41.793 1.00 65.88 C ANISOU 1529 CA LEU A 215 7369 9121 8542 -1110 -225 116 C ATOM 1530 C LEU A 215 3.071 -12.627 40.900 1.00 69.64 C ANISOU 1530 C LEU A 215 7882 9525 9054 -1191 -251 80 C ATOM 1531 O LEU A 215 2.435 -12.048 40.019 1.00 68.90 O ANISOU 1531 O LEU A 215 7816 9408 8957 -1186 -215 81 O ATOM 1532 CB LEU A 215 1.834 -12.925 43.065 1.00 66.56 C ANISOU 1532 CB LEU A 215 7560 9207 8523 -1017 -254 98 C ATOM 1533 CG LEU A 215 0.627 -13.561 43.769 1.00 71.07 C ANISOU 1533 CG LEU A 215 8114 9848 9041 -901 -205 155 C ATOM 1534 CD1 LEU A 215 0.477 -13.025 45.174 1.00 71.98 C ANISOU 1534 CD1 LEU A 215 8330 9969 9048 -804 -240 136 C ATOM 1535 CD2 LEU A 215 -0.663 -13.343 42.986 1.00 73.16 C ANISOU 1535 CD2 LEU A 215 8382 10119 9297 -858 -139 199 C ATOM 1536 N VAL A 216 4.397 -12.428 41.106 1.00 66.59 N ANISOU 1536 N VAL A 216 7486 9107 8708 -1265 -313 61 N ATOM 1537 CA VAL A 216 5.192 -11.498 40.291 1.00 66.70 C ANISOU 1537 CA VAL A 216 7519 9053 8772 -1345 -344 46 C ATOM 1538 C VAL A 216 5.352 -12.093 38.867 1.00 69.97 C ANISOU 1538 C VAL A 216 7841 9482 9261 -1387 -277 82 C ATOM 1539 O VAL A 216 5.469 -11.330 37.906 1.00 69.54 O ANISOU 1539 O VAL A 216 7802 9386 9236 -1420 -266 81 O ATOM 1540 CB VAL A 216 6.557 -11.109 40.941 1.00 71.35 C ANISOU 1540 CB VAL A 216 8116 9604 9391 -1416 -440 34 C ATOM 1541 CG1 VAL A 216 7.597 -12.226 40.845 1.00 70.95 C ANISOU 1541 CG1 VAL A 216 7943 9598 9416 -1471 -434 81 C ATOM 1542 CG2 VAL A 216 7.101 -9.807 40.359 1.00 71.71 C ANISOU 1542 CG2 VAL A 216 8213 9563 9472 -1480 -488 19 C ATOM 1543 N THR A 217 5.305 -13.442 38.740 1.00 66.12 N ANISOU 1543 N THR A 217 7268 9054 8803 -1378 -232 112 N ATOM 1544 CA THR A 217 5.390 -14.143 37.457 1.00 65.52 C ANISOU 1544 CA THR A 217 7123 8990 8782 -1402 -171 139 C ATOM 1545 C THR A 217 4.081 -13.902 36.688 1.00 69.10 C ANISOU 1545 C THR A 217 7610 9445 9199 -1360 -124 136 C ATOM 1546 O THR A 217 4.126 -13.709 35.474 1.00 68.57 O ANISOU 1546 O THR A 217 7533 9362 9158 -1384 -91 142 O ATOM 1547 CB THR A 217 5.701 -15.638 37.653 1.00 73.60 C ANISOU 1547 CB THR A 217 8062 10063 9841 -1399 -145 169 C ATOM 1548 OG1 THR A 217 6.827 -15.774 38.520 1.00 74.07 O ANISOU 1548 OG1 THR A 217 8091 10128 9924 -1432 -192 180 O ATOM 1549 CG2 THR A 217 6.002 -16.353 36.337 1.00 71.86 C ANISOU 1549 CG2 THR A 217 7789 9842 9672 -1422 -89 190 C ATOM 1550 N PHE A 218 2.932 -13.867 37.401 1.00 65.61 N ANISOU 1550 N PHE A 218 7206 9026 8695 -1294 -120 135 N ATOM 1551 CA PHE A 218 1.619 -13.604 36.803 1.00 65.18 C ANISOU 1551 CA PHE A 218 7179 8979 8606 -1251 -80 149 C ATOM 1552 C PHE A 218 1.537 -12.174 36.264 1.00 69.16 C ANISOU 1552 C PHE A 218 7754 9433 9089 -1260 -81 129 C ATOM 1553 O PHE A 218 0.945 -11.964 35.208 1.00 68.34 O ANISOU 1553 O PHE A 218 7648 9330 8988 -1261 -42 143 O ATOM 1554 CB PHE A 218 0.474 -13.843 37.809 1.00 67.07 C ANISOU 1554 CB PHE A 218 7437 9260 8788 -1168 -73 176 C ATOM 1555 CG PHE A 218 0.269 -15.247 38.339 1.00 68.48 C ANISOU 1555 CG PHE A 218 7538 9491 8989 -1147 -66 213 C ATOM 1556 CD1 PHE A 218 0.711 -16.354 37.622 1.00 71.26 C ANISOU 1556 CD1 PHE A 218 7815 9852 9409 -1197 -52 222 C ATOM 1557 CD2 PHE A 218 -0.438 -15.465 39.515 1.00 70.91 C ANISOU 1557 CD2 PHE A 218 7852 9840 9250 -1068 -67 246 C ATOM 1558 CE1 PHE A 218 0.510 -17.648 38.108 1.00 72.04 C ANISOU 1558 CE1 PHE A 218 7844 9990 9537 -1179 -47 258 C ATOM 1559 CE2 PHE A 218 -0.656 -16.761 39.990 1.00 73.56 C ANISOU 1559 CE2 PHE A 218 8106 10225 9619 -1047 -58 292 C ATOM 1560 CZ PHE A 218 -0.178 -17.844 39.285 1.00 71.29 C ANISOU 1560 CZ PHE A 218 7743 9937 9408 -1108 -51 296 C ATOM 1561 N VAL A 219 2.146 -11.204 36.983 1.00 66.37 N ANISOU 1561 N VAL A 219 7465 9034 8717 -1268 -131 97 N ATOM 1562 CA VAL A 219 2.165 -9.781 36.623 1.00 66.61 C ANISOU 1562 CA VAL A 219 7570 9002 8735 -1279 -143 76 C ATOM 1563 C VAL A 219 3.011 -9.581 35.347 1.00 70.52 C ANISOU 1563 C VAL A 219 8016 9473 9307 -1352 -131 87 C ATOM 1564 O VAL A 219 2.509 -8.973 34.400 1.00 69.96 O ANISOU 1564 O VAL A 219 7957 9388 9234 -1347 -92 97 O ATOM 1565 CB VAL A 219 2.659 -8.882 37.796 1.00 71.28 C ANISOU 1565 CB VAL A 219 8254 9539 9291 -1274 -218 35 C ATOM 1566 CG1 VAL A 219 2.844 -7.428 37.359 1.00 71.61 C ANISOU 1566 CG1 VAL A 219 8371 9499 9339 -1299 -240 14 C ATOM 1567 CG2 VAL A 219 1.706 -8.957 38.986 1.00 71.30 C ANISOU 1567 CG2 VAL A 219 8322 9569 9200 -1175 -216 30 C ATOM 1568 N VAL A 220 4.261 -10.115 35.307 1.00 67.32 N ANISOU 1568 N VAL A 220 7546 9067 8965 -1412 -158 96 N ATOM 1569 CA VAL A 220 5.161 -9.971 34.148 1.00 67.24 C ANISOU 1569 CA VAL A 220 7481 9040 9028 -1468 -140 125 C ATOM 1570 C VAL A 220 4.576 -10.704 32.916 1.00 70.52 C ANISOU 1570 C VAL A 220 7851 9498 9444 -1446 -64 145 C ATOM 1571 O VAL A 220 4.830 -10.263 31.794 1.00 70.20 O ANISOU 1571 O VAL A 220 7794 9445 9433 -1462 -33 166 O ATOM 1572 CB VAL A 220 6.642 -10.387 34.397 1.00 71.51 C ANISOU 1572 CB VAL A 220 7957 9576 9638 -1528 -179 152 C ATOM 1573 CG1 VAL A 220 7.318 -9.466 35.409 1.00 72.07 C ANISOU 1573 CG1 VAL A 220 8077 9590 9717 -1567 -273 136 C ATOM 1574 CG2 VAL A 220 6.785 -11.852 34.805 1.00 70.98 C ANISOU 1574 CG2 VAL A 220 7829 9566 9573 -1514 -161 163 C ATOM 1575 N MET A 221 3.775 -11.779 33.123 1.00 66.54 N ANISOU 1575 N MET A 221 7331 9043 8908 -1408 -39 143 N ATOM 1576 CA MET A 221 3.120 -12.502 32.029 1.00 65.96 C ANISOU 1576 CA MET A 221 7230 9002 8829 -1391 13 157 C ATOM 1577 C MET A 221 2.001 -11.647 31.429 1.00 69.90 C ANISOU 1577 C MET A 221 7774 9497 9286 -1364 38 159 C ATOM 1578 O MET A 221 1.862 -11.620 30.209 1.00 69.36 O ANISOU 1578 O MET A 221 7694 9436 9222 -1368 74 171 O ATOM 1579 CB MET A 221 2.579 -13.867 32.478 1.00 67.96 C ANISOU 1579 CB MET A 221 7452 9296 9073 -1367 17 161 C ATOM 1580 CG MET A 221 3.629 -14.960 32.448 1.00 71.58 C ANISOU 1580 CG MET A 221 7852 9763 9580 -1392 21 169 C ATOM 1581 SD MET A 221 2.991 -16.635 32.720 1.00 75.41 S ANISOU 1581 SD MET A 221 8298 10285 10069 -1368 29 178 S ATOM 1582 CE MET A 221 2.620 -16.578 34.462 1.00 72.18 C ANISOU 1582 CE MET A 221 7891 9898 9636 -1338 -9 183 C ATOM 1583 N VAL A 222 1.239 -10.918 32.280 1.00 66.69 N ANISOU 1583 N VAL A 222 7424 9082 8833 -1329 23 152 N ATOM 1584 CA VAL A 222 0.160 -10.012 31.859 1.00 66.58 C ANISOU 1584 CA VAL A 222 7456 9065 8776 -1294 52 166 C ATOM 1585 C VAL A 222 0.778 -8.881 31.007 1.00 70.66 C ANISOU 1585 C VAL A 222 7988 9538 9323 -1326 61 163 C ATOM 1586 O VAL A 222 0.246 -8.575 29.939 1.00 70.00 O ANISOU 1586 O VAL A 222 7899 9468 9232 -1319 103 184 O ATOM 1587 CB VAL A 222 -0.660 -9.477 33.073 1.00 70.80 C ANISOU 1587 CB VAL A 222 8055 9594 9249 -1234 39 166 C ATOM 1588 CG1 VAL A 222 -1.496 -8.248 32.712 1.00 70.83 C ANISOU 1588 CG1 VAL A 222 8119 9578 9214 -1198 71 181 C ATOM 1589 CG2 VAL A 222 -1.553 -10.570 33.654 1.00 70.39 C ANISOU 1589 CG2 VAL A 222 7972 9600 9172 -1190 46 197 C ATOM 1590 N VAL A 223 1.932 -8.326 31.454 1.00 67.78 N ANISOU 1590 N VAL A 223 7634 9123 8998 -1364 19 146 N ATOM 1591 CA VAL A 223 2.693 -7.261 30.781 1.00 68.12 C ANISOU 1591 CA VAL A 223 7677 9115 9088 -1402 15 157 C ATOM 1592 C VAL A 223 3.118 -7.740 29.371 1.00 72.11 C ANISOU 1592 C VAL A 223 8112 9653 9634 -1419 64 191 C ATOM 1593 O VAL A 223 3.012 -6.964 28.418 1.00 71.80 O ANISOU 1593 O VAL A 223 8071 9604 9606 -1417 98 214 O ATOM 1594 CB VAL A 223 3.915 -6.803 31.637 1.00 72.62 C ANISOU 1594 CB VAL A 223 8259 9627 9705 -1451 -59 145 C ATOM 1595 CG1 VAL A 223 4.833 -5.852 30.869 1.00 72.90 C ANISOU 1595 CG1 VAL A 223 8271 9612 9815 -1500 -68 177 C ATOM 1596 CG2 VAL A 223 3.460 -6.154 32.942 1.00 72.84 C ANISOU 1596 CG2 VAL A 223 8384 9614 9677 -1423 -110 103 C ATOM 1597 N LEU A 224 3.552 -9.017 29.245 1.00 68.68 N ANISOU 1597 N LEU A 224 7624 9256 9214 -1426 72 195 N ATOM 1598 CA LEU A 224 3.973 -9.627 27.978 1.00 68.50 C ANISOU 1598 CA LEU A 224 7550 9263 9213 -1424 119 222 C ATOM 1599 C LEU A 224 2.837 -9.621 26.945 1.00 72.46 C ANISOU 1599 C LEU A 224 8068 9797 9664 -1389 165 224 C ATOM 1600 O LEU A 224 3.063 -9.164 25.825 1.00 72.14 O ANISOU 1600 O LEU A 224 8013 9761 9635 -1383 203 250 O ATOM 1601 CB LEU A 224 4.483 -11.066 28.188 1.00 68.37 C ANISOU 1601 CB LEU A 224 7493 9274 9208 -1426 119 219 C ATOM 1602 CG LEU A 224 5.908 -11.219 28.724 1.00 73.43 C ANISOU 1602 CG LEU A 224 8090 9897 9912 -1462 92 243 C ATOM 1603 CD1 LEU A 224 6.064 -12.514 29.490 1.00 73.37 C ANISOU 1603 CD1 LEU A 224 8060 9914 9903 -1460 79 231 C ATOM 1604 CD2 LEU A 224 6.940 -11.129 27.605 1.00 76.29 C ANISOU 1604 CD2 LEU A 224 8404 10260 10323 -1465 134 298 C ATOM 1605 N TYR A 225 1.622 -10.089 27.322 1.00 69.10 N ANISOU 1605 N TYR A 225 7669 9399 9188 -1365 160 207 N ATOM 1606 CA TYR A 225 0.464 -10.119 26.420 1.00 68.93 C ANISOU 1606 CA TYR A 225 7659 9412 9120 -1340 191 219 C ATOM 1607 C TYR A 225 -0.083 -8.707 26.177 1.00 73.73 C ANISOU 1607 C TYR A 225 8297 10005 9712 -1326 212 239 C ATOM 1608 O TYR A 225 -0.515 -8.425 25.060 1.00 73.32 O ANISOU 1608 O TYR A 225 8240 9978 9642 -1314 248 260 O ATOM 1609 CB TYR A 225 -0.652 -11.041 26.942 1.00 69.67 C ANISOU 1609 CB TYR A 225 7757 9537 9178 -1324 171 218 C ATOM 1610 CG TYR A 225 -0.242 -12.495 27.046 1.00 71.07 C ANISOU 1610 CG TYR A 225 7905 9724 9373 -1335 153 202 C ATOM 1611 CD1 TYR A 225 -0.166 -13.304 25.915 1.00 72.99 C ANISOU 1611 CD1 TYR A 225 8141 9980 9610 -1336 166 197 C ATOM 1612 CD2 TYR A 225 0.030 -13.074 28.280 1.00 71.70 C ANISOU 1612 CD2 TYR A 225 7972 9799 9471 -1338 123 192 C ATOM 1613 CE1 TYR A 225 0.215 -14.643 26.007 1.00 73.57 C ANISOU 1613 CE1 TYR A 225 8200 10053 9701 -1342 151 180 C ATOM 1614 CE2 TYR A 225 0.419 -14.408 28.384 1.00 72.46 C ANISOU 1614 CE2 TYR A 225 8039 9902 9591 -1347 112 183 C ATOM 1615 CZ TYR A 225 0.501 -15.192 27.247 1.00 79.53 C ANISOU 1615 CZ TYR A 225 8932 10802 10484 -1349 126 176 C ATOM 1616 OH TYR A 225 0.877 -16.508 27.361 1.00 80.14 O ANISOU 1616 OH TYR A 225 8991 10876 10583 -1353 116 166 O ATOM 1617 N ALA A 226 -0.034 -7.816 27.198 1.00 71.09 N ANISOU 1617 N ALA A 226 7999 9629 9381 -1325 190 230 N ATOM 1618 CA ALA A 226 -0.482 -6.419 27.083 1.00 71.49 C ANISOU 1618 CA ALA A 226 8091 9651 9420 -1308 210 246 C ATOM 1619 C ALA A 226 0.369 -5.660 26.059 1.00 76.54 C ANISOU 1619 C ALA A 226 8704 10269 10111 -1331 234 267 C ATOM 1620 O ALA A 226 -0.147 -4.787 25.360 1.00 76.23 O ANISOU 1620 O ALA A 226 8673 10230 10060 -1313 273 295 O ATOM 1621 CB ALA A 226 -0.418 -5.725 28.435 1.00 72.51 C ANISOU 1621 CB ALA A 226 8283 9727 9542 -1299 171 222 C ATOM 1622 N HIS A 227 1.665 -6.022 25.960 1.00 74.04 N ANISOU 1622 N HIS A 227 8344 9935 9851 -1366 215 267 N ATOM 1623 CA HIS A 227 2.615 -5.459 25.003 1.00 74.60 C ANISOU 1623 CA HIS A 227 8371 9992 9981 -1382 238 308 C ATOM 1624 C HIS A 227 2.296 -5.968 23.593 1.00 79.08 C ANISOU 1624 C HIS A 227 8906 10622 10519 -1350 298 332 C ATOM 1625 O HIS A 227 2.493 -5.233 22.626 1.00 78.96 O ANISOU 1625 O HIS A 227 8866 10610 10523 -1338 339 373 O ATOM 1626 CB HIS A 227 4.058 -5.814 25.402 1.00 75.66 C ANISOU 1626 CB HIS A 227 8463 10099 10183 -1422 201 319 C ATOM 1627 CG HIS A 227 5.102 -5.163 24.549 1.00 79.55 C ANISOU 1627 CG HIS A 227 8900 10575 10751 -1437 222 383 C ATOM 1628 ND1 HIS A 227 5.631 -5.803 23.443 1.00 81.34 N ANISOU 1628 ND1 HIS A 227 9071 10850 10987 -1410 275 425 N ATOM 1629 CD2 HIS A 227 5.678 -3.944 24.667 1.00 81.86 C ANISOU 1629 CD2 HIS A 227 9187 10805 11112 -1470 194 417 C ATOM 1630 CE1 HIS A 227 6.511 -4.960 22.928 1.00 81.30 C ANISOU 1630 CE1 HIS A 227 9016 10819 11057 -1422 286 495 C ATOM 1631 NE2 HIS A 227 6.573 -3.828 23.629 1.00 81.98 N ANISOU 1631 NE2 HIS A 227 9126 10836 11188 -1465 234 494 N ATOM 1632 N ILE A 228 1.791 -7.219 23.484 1.00 75.82 N ANISOU 1632 N ILE A 228 8495 10254 10057 -1335 299 307 N ATOM 1633 CA ILE A 228 1.411 -7.852 22.216 1.00 75.85 C ANISOU 1633 CA ILE A 228 8490 10312 10019 -1304 338 316 C ATOM 1634 C ILE A 228 0.098 -7.219 21.718 1.00 80.19 C ANISOU 1634 C ILE A 228 9063 10889 10517 -1284 360 330 C ATOM 1635 O ILE A 228 0.077 -6.700 20.602 1.00 79.94 O ANISOU 1635 O ILE A 228 9016 10881 10476 -1261 403 362 O ATOM 1636 CB ILE A 228 1.310 -9.404 22.346 1.00 78.79 C ANISOU 1636 CB ILE A 228 8867 10706 10362 -1302 316 281 C ATOM 1637 CG1 ILE A 228 2.693 -10.030 22.647 1.00 79.39 C ANISOU 1637 CG1 ILE A 228 8913 10763 10489 -1313 310 283 C ATOM 1638 CG2 ILE A 228 0.690 -10.033 21.083 1.00 79.65 C ANISOU 1638 CG2 ILE A 228 8990 10859 10412 -1272 337 279 C ATOM 1639 CD1 ILE A 228 2.659 -11.439 23.289 1.00 86.60 C ANISOU 1639 CD1 ILE A 228 9832 11681 11393 -1319 279 247 C ATOM 1640 N PHE A 229 -0.976 -7.246 22.548 1.00 77.00 N ANISOU 1640 N PHE A 229 8688 10487 10080 -1284 336 318 N ATOM 1641 CA PHE A 229 -2.294 -6.689 22.214 1.00 77.00 C ANISOU 1641 CA PHE A 229 8706 10518 10034 -1263 358 348 C ATOM 1642 C PHE A 229 -2.223 -5.189 21.913 1.00 81.59 C ANISOU 1642 C PHE A 229 9291 11076 10635 -1251 399 381 C ATOM 1643 O PHE A 229 -2.911 -4.730 21.002 1.00 81.23 O ANISOU 1643 O PHE A 229 9236 11068 10559 -1230 438 418 O ATOM 1644 CB PHE A 229 -3.318 -6.941 23.332 1.00 78.66 C ANISOU 1644 CB PHE A 229 8941 10732 10215 -1255 330 349 C ATOM 1645 CG PHE A 229 -3.868 -8.347 23.378 1.00 80.10 C ANISOU 1645 CG PHE A 229 9112 10950 10374 -1263 294 341 C ATOM 1646 CD1 PHE A 229 -4.804 -8.777 22.443 1.00 83.35 C ANISOU 1646 CD1 PHE A 229 9512 11409 10746 -1261 293 369 C ATOM 1647 CD2 PHE A 229 -3.491 -9.225 24.385 1.00 82.19 C ANISOU 1647 CD2 PHE A 229 9373 11196 10658 -1275 255 311 C ATOM 1648 CE1 PHE A 229 -5.316 -10.077 22.490 1.00 84.26 C ANISOU 1648 CE1 PHE A 229 9619 11545 10849 -1277 246 365 C ATOM 1649 CE2 PHE A 229 -4.007 -10.522 24.434 1.00 84.94 C ANISOU 1649 CE2 PHE A 229 9706 11570 10995 -1284 219 310 C ATOM 1650 CZ PHE A 229 -4.917 -10.940 23.487 1.00 83.16 C ANISOU 1650 CZ PHE A 229 9475 11382 10738 -1288 211 336 C ATOM 1651 N GLY A 230 -1.390 -4.462 22.660 1.00 78.78 N ANISOU 1651 N GLY A 230 8946 10655 10331 -1267 384 370 N ATOM 1652 CA GLY A 230 -1.171 -3.030 22.480 1.00 79.18 C ANISOU 1652 CA GLY A 230 9004 10663 10417 -1264 410 399 C ATOM 1653 C GLY A 230 -0.546 -2.708 21.136 1.00 83.80 C ANISOU 1653 C GLY A 230 9535 11269 11035 -1259 454 440 C ATOM 1654 O GLY A 230 -0.979 -1.770 20.463 1.00 83.51 O ANISOU 1654 O GLY A 230 9492 11242 10997 -1238 500 482 O ATOM 1655 N TYR A 231 0.455 -3.516 20.726 1.00 80.87 N ANISOU 1655 N TYR A 231 9124 10913 10690 -1269 447 437 N ATOM 1656 CA TYR A 231 1.176 -3.398 19.455 1.00 81.20 C ANISOU 1656 CA TYR A 231 9112 10984 10757 -1248 494 485 C ATOM 1657 C TYR A 231 0.267 -3.777 18.274 1.00 85.41 C ANISOU 1657 C TYR A 231 9646 11595 11211 -1206 536 496 C ATOM 1658 O TYR A 231 0.347 -3.130 17.227 1.00 85.34 O ANISOU 1658 O TYR A 231 9605 11613 11206 -1174 588 546 O ATOM 1659 CB TYR A 231 2.442 -4.276 19.478 1.00 82.53 C ANISOU 1659 CB TYR A 231 9247 11148 10963 -1257 478 484 C ATOM 1660 CG TYR A 231 3.210 -4.341 18.175 1.00 84.74 C ANISOU 1660 CG TYR A 231 9475 11466 11256 -1215 534 542 C ATOM 1661 CD1 TYR A 231 3.933 -3.245 17.712 1.00 87.25 C ANISOU 1661 CD1 TYR A 231 9740 11764 11649 -1210 565 617 C ATOM 1662 CD2 TYR A 231 3.277 -5.522 17.442 1.00 85.49 C ANISOU 1662 CD2 TYR A 231 9577 11614 11291 -1173 555 527 C ATOM 1663 CE1 TYR A 231 4.654 -3.304 16.521 1.00 88.56 C ANISOU 1663 CE1 TYR A 231 9851 11973 11826 -1156 625 686 C ATOM 1664 CE2 TYR A 231 4.011 -5.600 16.259 1.00 86.88 C ANISOU 1664 CE2 TYR A 231 9717 11828 11467 -1115 614 584 C ATOM 1665 CZ TYR A 231 4.693 -4.485 15.798 1.00 94.78 C ANISOU 1665 CZ TYR A 231 10654 12818 12539 -1102 653 669 C ATOM 1666 OH TYR A 231 5.411 -4.553 14.629 1.00 96.25 O ANISOU 1666 OH TYR A 231 10798 13050 12723 -1030 720 740 O ATOM 1667 N VAL A 232 -0.592 -4.811 18.445 1.00 81.88 N ANISOU 1667 N VAL A 232 9232 11181 10696 -1206 508 454 N ATOM 1668 CA VAL A 232 -1.545 -5.273 17.424 1.00 81.80 C ANISOU 1668 CA VAL A 232 9231 11239 10609 -1178 524 461 C ATOM 1669 C VAL A 232 -2.605 -4.170 17.221 1.00 86.01 C ANISOU 1669 C VAL A 232 9764 11792 11123 -1168 556 504 C ATOM 1670 O VAL A 232 -2.903 -3.827 16.075 1.00 85.76 O ANISOU 1670 O VAL A 232 9715 11811 11059 -1138 597 542 O ATOM 1671 CB VAL A 232 -2.172 -6.655 17.778 1.00 85.46 C ANISOU 1671 CB VAL A 232 9727 11719 11023 -1194 469 414 C ATOM 1672 CG1 VAL A 232 -3.353 -6.999 16.869 1.00 85.35 C ANISOU 1672 CG1 VAL A 232 9729 11766 10935 -1182 463 427 C ATOM 1673 CG2 VAL A 232 -1.123 -7.763 17.717 1.00 85.35 C ANISOU 1673 CG2 VAL A 232 9716 11692 11021 -1192 452 377 C ATOM 1674 N ALA A1001 -3.118 -3.584 18.331 1.00 82.73 N ANISOU 1674 N ALA A1001 9372 11337 10725 -1184 542 504 N ATOM 1675 CA ALA A1001 -4.095 -2.488 18.308 1.00 82.79 C ANISOU 1675 CA ALA A1001 9387 11353 10717 -1166 580 551 C ATOM 1676 C ALA A1001 -3.502 -1.240 17.650 1.00 87.39 C ANISOU 1676 C ALA A1001 9940 11917 11349 -1150 635 595 C ATOM 1677 O ALA A1001 -4.221 -0.532 16.943 1.00 87.12 O ANISOU 1677 O ALA A1001 9891 11921 11291 -1123 685 647 O ATOM 1678 CB ALA A1001 -4.564 -2.164 19.718 1.00 83.41 C ANISOU 1678 CB ALA A1001 9510 11382 10800 -1171 557 539 C ATOM 1679 N ASP A1002 -2.186 -0.991 17.862 1.00 84.47 N ANISOU 1679 N ASP A1002 9554 11490 11053 -1167 624 585 N ATOM 1680 CA ASP A1002 -1.452 0.127 17.264 1.00 84.92 C ANISOU 1680 CA ASP A1002 9569 11520 11178 -1158 667 638 C ATOM 1681 C ASP A1002 -1.328 -0.067 15.752 1.00 89.19 C ANISOU 1681 C ASP A1002 10056 12139 11691 -1117 720 683 C ATOM 1682 O ASP A1002 -1.448 0.905 15.009 1.00 89.07 O ANISOU 1682 O ASP A1002 10007 12141 11695 -1090 776 744 O ATOM 1683 CB ASP A1002 -0.062 0.299 17.904 1.00 87.07 C ANISOU 1683 CB ASP A1002 9827 11714 11542 -1195 627 629 C ATOM 1684 CG ASP A1002 -0.055 1.044 19.228 1.00 97.27 C ANISOU 1684 CG ASP A1002 11174 12911 12874 -1229 581 600 C ATOM 1685 OD1 ASP A1002 -0.772 2.065 19.342 1.00 97.90 O ANISOU 1685 OD1 ASP A1002 11285 12963 12949 -1213 607 619 O ATOM 1686 OD2 ASP A1002 0.726 0.655 20.122 1.00103.34 O1- ANISOU 1686 OD2 ASP A1002 11957 13629 13680 -1267 519 563 O1- ATOM 1687 N LEU A1003 -1.119 -1.321 15.297 1.00 85.78 N ANISOU 1687 N LEU A1003 9626 11757 11211 -1105 704 653 N ATOM 1688 CA LEU A1003 -1.028 -1.648 13.873 1.00 85.97 C ANISOU 1688 CA LEU A1003 9623 11857 11186 -1053 748 684 C ATOM 1689 C LEU A1003 -2.408 -1.614 13.217 1.00 89.92 C ANISOU 1689 C LEU A1003 10140 12428 11600 -1034 763 696 C ATOM 1690 O LEU A1003 -2.515 -1.203 12.062 1.00 89.81 O ANISOU 1690 O LEU A1003 10094 12472 11557 -988 816 747 O ATOM 1691 CB LEU A1003 -0.379 -3.025 13.644 1.00 86.05 C ANISOU 1691 CB LEU A1003 9650 11885 11162 -1040 722 641 C ATOM 1692 CG LEU A1003 1.130 -3.151 13.871 1.00 91.03 C ANISOU 1692 CG LEU A1003 10245 12473 11870 -1038 726 659 C ATOM 1693 CD1 LEU A1003 1.552 -4.599 13.811 1.00 91.18 C ANISOU 1693 CD1 LEU A1003 10296 12506 11843 -1023 701 610 C ATOM 1694 CD2 LEU A1003 1.926 -2.353 12.841 1.00 94.16 C ANISOU 1694 CD2 LEU A1003 10574 12893 12309 -985 796 749 C ATOM 1695 N GLU A1004 -3.456 -2.046 13.953 1.00 86.34 N ANISOU 1695 N GLU A1004 9727 11972 11105 -1067 718 662 N ATOM 1696 CA GLU A1004 -4.837 -2.077 13.468 1.00 86.29 C ANISOU 1696 CA GLU A1004 9730 12032 11024 -1059 719 687 C ATOM 1697 C GLU A1004 -5.420 -0.665 13.331 1.00 90.42 C ANISOU 1697 C GLU A1004 10225 12562 11567 -1042 782 759 C ATOM 1698 O GLU A1004 -6.168 -0.432 12.381 1.00 90.17 O ANISOU 1698 O GLU A1004 10174 12603 11484 -1017 813 807 O ATOM 1699 CB GLU A1004 -5.735 -2.933 14.374 1.00 87.36 C ANISOU 1699 CB GLU A1004 9905 12161 11128 -1097 653 653 C ATOM 1700 CG GLU A1004 -5.580 -4.428 14.135 1.00 98.22 C ANISOU 1700 CG GLU A1004 11308 13552 12460 -1110 591 595 C ATOM 1701 CD GLU A1004 -6.496 -5.349 14.919 1.00118.55 C ANISOU 1701 CD GLU A1004 13909 16124 15012 -1149 520 575 C ATOM 1702 OE1 GLU A1004 -6.865 -5.006 16.066 1.00112.79 O ANISOU 1702 OE1 GLU A1004 13180 15361 14314 -1164 516 587 O ATOM 1703 OE2 GLU A1004 -6.807 -6.445 14.400 1.00112.34 O1- ANISOU 1703 OE2 GLU A1004 13144 15364 14175 -1160 466 549 O1- ATOM 1704 N ASP A1005 -5.081 0.273 14.252 1.00 87.04 N ANISOU 1704 N ASP A1005 9802 12058 11213 -1054 798 765 N ATOM 1705 CA ASP A1005 -5.579 1.652 14.166 1.00 87.14 C ANISOU 1705 CA ASP A1005 9799 12061 11250 -1033 860 831 C ATOM 1706 C ASP A1005 -4.845 2.403 13.042 1.00 91.34 C ANISOU 1706 C ASP A1005 10270 12613 11822 -1000 922 886 C ATOM 1707 O ASP A1005 -5.441 3.281 12.418 1.00 91.00 O ANISOU 1707 O ASP A1005 10198 12607 11772 -970 983 953 O ATOM 1708 CB ASP A1005 -5.493 2.413 15.509 1.00 89.03 C ANISOU 1708 CB ASP A1005 10083 12201 11545 -1050 849 815 C ATOM 1709 CG ASP A1005 -4.116 2.647 16.109 1.00 99.77 C ANISOU 1709 CG ASP A1005 11447 13467 12993 -1078 817 777 C ATOM 1710 OD1 ASP A1005 -3.257 3.238 15.418 1.00100.79 O ANISOU 1710 OD1 ASP A1005 11526 13585 13184 -1071 848 816 O ATOM 1711 OD2 ASP A1005 -3.952 2.398 17.321 1.00105.57 O1- ANISOU 1711 OD2 ASP A1005 12234 14138 13740 -1104 764 724 O1- ATOM 1712 N ASN A1006 -3.568 2.041 12.775 1.00 88.22 N ANISOU 1712 N ASN A1006 9850 12198 11471 -1000 910 868 N ATOM 1713 CA ASN A1006 -2.768 2.616 11.689 1.00 88.63 C ANISOU 1713 CA ASN A1006 9835 12277 11564 -958 969 934 C ATOM 1714 C ASN A1006 -3.296 2.117 10.342 1.00 92.99 C ANISOU 1714 C ASN A1006 10370 12944 12019 -906 1002 959 C ATOM 1715 O ASN A1006 -3.316 2.879 9.375 1.00 92.98 O ANISOU 1715 O ASN A1006 10315 12991 12022 -859 1070 1033 O ATOM 1716 CB ASN A1006 -1.277 2.287 11.849 1.00 89.34 C ANISOU 1716 CB ASN A1006 9900 12319 11726 -966 948 925 C ATOM 1717 CG ASN A1006 -0.542 3.065 12.925 1.00111.61 C ANISOU 1717 CG ASN A1006 12719 15025 14661 -1015 918 926 C ATOM 1718 OD1 ASN A1006 0.480 2.610 13.450 1.00105.65 O ANISOU 1718 OD1 ASN A1006 11961 14223 13958 -1044 873 904 O ATOM 1719 ND2 ASN A1006 -1.017 4.257 13.273 1.00103.68 N ANISOU 1719 ND2 ASN A1006 11722 13971 13699 -1026 938 955 N ATOM 1720 N TRP A1007 -3.749 0.842 10.296 1.00 89.54 N ANISOU 1720 N TRP A1007 9982 12547 11493 -915 947 897 N ATOM 1721 CA TRP A1007 -4.357 0.204 9.124 1.00 89.71 C ANISOU 1721 CA TRP A1007 10013 12667 11407 -877 950 901 C ATOM 1722 C TRP A1007 -5.728 0.832 8.860 1.00 93.58 C ANISOU 1722 C TRP A1007 10491 13210 11853 -879 972 953 C ATOM 1723 O TRP A1007 -6.119 0.989 7.701 1.00 93.46 O ANISOU 1723 O TRP A1007 10453 13281 11777 -835 1007 999 O ATOM 1724 CB TRP A1007 -4.474 -1.318 9.339 1.00 88.34 C ANISOU 1724 CB TRP A1007 9904 12494 11166 -900 868 817 C ATOM 1725 CG TRP A1007 -5.104 -2.066 8.200 1.00 89.72 C ANISOU 1725 CG TRP A1007 10111 12755 11226 -869 846 808 C ATOM 1726 CD1 TRP A1007 -6.419 -2.402 8.068 1.00 92.64 C ANISOU 1726 CD1 TRP A1007 10504 13169 11525 -900 797 809 C ATOM 1727 CD2 TRP A1007 -4.438 -2.588 7.042 1.00 90.15 C ANISOU 1727 CD2 TRP A1007 10181 12855 11217 -799 864 800 C ATOM 1728 NE1 TRP A1007 -6.618 -3.090 6.894 1.00 92.66 N ANISOU 1728 NE1 TRP A1007 10542 13238 11426 -863 772 794 N ATOM 1729 CE2 TRP A1007 -5.418 -3.220 6.244 1.00 94.43 C ANISOU 1729 CE2 TRP A1007 10770 13465 11645 -794 816 784 C ATOM 1730 CE3 TRP A1007 -3.105 -2.579 6.596 1.00 91.78 C ANISOU 1730 CE3 TRP A1007 10367 13053 11450 -734 916 816 C ATOM 1731 CZ2 TRP A1007 -5.107 -3.839 5.027 1.00 94.44 C ANISOU 1731 CZ2 TRP A1007 10815 13520 11548 -721 816 766 C ATOM 1732 CZ3 TRP A1007 -2.799 -3.192 5.390 1.00 93.92 C ANISOU 1732 CZ3 TRP A1007 10675 13386 11626 -652 930 810 C ATOM 1733 CH2 TRP A1007 -3.792 -3.812 4.620 1.00 94.91 C ANISOU 1733 CH2 TRP A1007 10863 13572 11627 -643 879 777 C ATOM 1734 N GLU A1008 -6.446 1.195 9.946 1.00 89.86 N ANISOU 1734 N GLU A1008 10038 12693 11411 -923 955 952 N ATOM 1735 CA GLU A1008 -7.756 1.850 9.916 1.00 89.70 C ANISOU 1735 CA GLU A1008 10006 12716 11362 -923 984 1017 C ATOM 1736 C GLU A1008 -7.609 3.270 9.356 1.00 93.85 C ANISOU 1736 C GLU A1008 10474 13249 11936 -882 1079 1100 C ATOM 1737 O GLU A1008 -8.435 3.689 8.548 1.00 93.64 O ANISOU 1737 O GLU A1008 10413 13303 11861 -855 1122 1170 O ATOM 1738 CB GLU A1008 -8.375 1.870 11.328 1.00 90.69 C ANISOU 1738 CB GLU A1008 10171 12778 11508 -962 952 999 C ATOM 1739 CG GLU A1008 -9.840 2.275 11.373 1.00101.12 C ANISOU 1739 CG GLU A1008 11484 14151 12787 -958 974 1074 C ATOM 1740 CD GLU A1008 -10.447 2.330 12.762 1.00120.07 C ANISOU 1740 CD GLU A1008 13925 16494 15201 -974 956 1072 C ATOM 1741 OE1 GLU A1008 -9.962 3.128 13.597 1.00113.03 O ANISOU 1741 OE1 GLU A1008 13059 15516 14371 -964 985 1058 O ATOM 1742 OE2 GLU A1008 -11.438 1.603 13.002 1.00113.68 O1- ANISOU 1742 OE2 GLU A1008 13122 15728 14341 -992 911 1092 O1- ATOM 1743 N THR A1009 -6.541 3.990 9.770 1.00 90.47 N ANISOU 1743 N THR A1009 10030 12738 11607 -879 1106 1099 N ATOM 1744 CA THR A1009 -6.219 5.351 9.325 1.00 90.65 C ANISOU 1744 CA THR A1009 9995 12746 11701 -846 1189 1179 C ATOM 1745 C THR A1009 -5.804 5.319 7.840 1.00 94.87 C ANISOU 1745 C THR A1009 10465 13374 12207 -788 1237 1231 C ATOM 1746 O THR A1009 -6.160 6.228 7.091 1.00 94.74 O ANISOU 1746 O THR A1009 10394 13407 12197 -747 1312 1317 O ATOM 1747 CB THR A1009 -5.117 5.958 10.223 1.00 98.56 C ANISOU 1747 CB THR A1009 11003 13623 12823 -873 1177 1160 C ATOM 1748 OG1 THR A1009 -5.482 5.805 11.596 1.00 97.69 O ANISOU 1748 OG1 THR A1009 10968 13434 12717 -917 1122 1098 O ATOM 1749 CG2 THR A1009 -4.858 7.437 9.935 1.00 97.64 C ANISOU 1749 CG2 THR A1009 10833 13466 12798 -849 1250 1244 C ATOM 1750 N LEU A1010 -5.079 4.263 7.423 1.00 91.49 N ANISOU 1750 N LEU A1010 10049 12972 11741 -774 1199 1184 N ATOM 1751 CA LEU A1010 -4.599 4.081 6.051 1.00 91.83 C ANISOU 1751 CA LEU A1010 10049 13102 11739 -702 1243 1225 C ATOM 1752 C LEU A1010 -5.748 3.753 5.079 1.00 95.90 C ANISOU 1752 C LEU A1010 10575 13735 12128 -673 1246 1244 C ATOM 1753 O LEU A1010 -5.692 4.176 3.925 1.00 95.96 O ANISOU 1753 O LEU A1010 10532 13824 12105 -605 1310 1313 O ATOM 1754 CB LEU A1010 -3.542 2.960 6.010 1.00 91.95 C ANISOU 1754 CB LEU A1010 10095 13102 11739 -689 1200 1164 C ATOM 1755 CG LEU A1010 -2.603 2.927 4.798 1.00 97.37 C ANISOU 1755 CG LEU A1010 10734 13851 12412 -596 1260 1221 C ATOM 1756 CD1 LEU A1010 -1.466 3.935 4.950 1.00 97.84 C ANISOU 1756 CD1 LEU A1010 10708 13851 12615 -582 1315 1303 C ATOM 1757 CD2 LEU A1010 -2.010 1.546 4.617 1.00100.03 C ANISOU 1757 CD2 LEU A1010 11133 14197 12678 -570 1213 1149 C ATOM 1758 N ASN A1011 -6.773 3.003 5.537 1.00 92.16 N ANISOU 1758 N ASN A1011 10162 13272 11585 -725 1174 1191 N ATOM 1759 CA ASN A1011 -7.913 2.600 4.706 1.00 92.23 C ANISOU 1759 CA ASN A1011 10182 13384 11476 -716 1152 1210 C ATOM 1760 C ASN A1011 -9.013 3.671 4.635 1.00 96.02 C ANISOU 1760 C ASN A1011 10613 13906 11964 -719 1208 1305 C ATOM 1761 O ASN A1011 -9.595 3.847 3.563 1.00 96.04 O ANISOU 1761 O ASN A1011 10584 14011 11894 -682 1235 1364 O ATOM 1762 CB ASN A1011 -8.520 1.288 5.209 1.00 92.92 C ANISOU 1762 CB ASN A1011 10347 13461 11499 -775 1040 1129 C ATOM 1763 CG ASN A1011 -7.879 0.046 4.635 1.00116.08 C ANISOU 1763 CG ASN A1011 13339 16406 14360 -752 982 1051 C ATOM 1764 OD1 ASN A1011 -6.662 -0.160 4.710 1.00110.46 O ANISOU 1764 OD1 ASN A1011 12634 15649 13689 -721 1000 1016 O ATOM 1765 ND2 ASN A1011 -8.699 -0.832 4.077 1.00108.11 N ANISOU 1765 ND2 ASN A1011 12379 15454 13244 -766 906 1025 N ATOM 1766 N ASP A1012 -9.315 4.360 5.758 1.00 92.09 N ANISOU 1766 N ASP A1012 10113 13333 11544 -756 1226 1321 N ATOM 1767 CA ASP A1012 -10.367 5.383 5.811 1.00 91.93 C ANISOU 1767 CA ASP A1012 10055 13342 11533 -751 1289 1416 C ATOM 1768 C ASP A1012 -9.976 6.653 5.042 1.00 95.87 C ANISOU 1768 C ASP A1012 10477 13863 12084 -692 1398 1505 C ATOM 1769 O ASP A1012 -10.815 7.189 4.317 1.00 95.72 O ANISOU 1769 O ASP A1012 10412 13934 12025 -663 1451 1594 O ATOM 1770 CB ASP A1012 -10.726 5.746 7.263 1.00 93.41 C ANISOU 1770 CB ASP A1012 10280 13432 11780 -790 1282 1404 C ATOM 1771 CG ASP A1012 -11.443 4.655 8.043 1.00103.35 C ANISOU 1771 CG ASP A1012 11596 14685 12988 -841 1190 1354 C ATOM 1772 OD1 ASP A1012 -12.264 3.926 7.436 1.00104.07 O ANISOU 1772 OD1 ASP A1012 11682 14865 12993 -855 1144 1374 O ATOM 1773 OD2 ASP A1012 -11.234 4.571 9.271 1.00108.85 O1- ANISOU 1773 OD2 ASP A1012 12339 15289 13731 -867 1163 1305 O1- ATOM 1774 N ASN A1013 -8.718 7.125 5.190 1.00 92.24 N ANISOU 1774 N ASN A1013 9999 13328 11722 -674 1428 1492 N ATOM 1775 CA ASN A1013 -8.220 8.329 4.514 1.00 92.38 C ANISOU 1775 CA ASN A1013 9934 13353 11812 -620 1527 1584 C ATOM 1776 C ASN A1013 -8.022 8.100 3.006 1.00 96.59 C ANISOU 1776 C ASN A1013 10413 14013 12274 -550 1563 1631 C ATOM 1777 O ASN A1013 -8.027 9.072 2.248 1.00 96.60 O ANISOU 1777 O ASN A1013 10336 14063 12307 -496 1653 1732 O ATOM 1778 CB ASN A1013 -6.917 8.815 5.145 1.00 92.79 C ANISOU 1778 CB ASN A1013 9977 13282 11995 -632 1530 1566 C ATOM 1779 CG ASN A1013 -7.113 9.502 6.473 1.00114.49 C ANISOU 1779 CG ASN A1013 12772 15905 14824 -681 1519 1546 C ATOM 1780 OD1 ASN A1013 -7.157 10.733 6.559 1.00108.64 O ANISOU 1780 OD1 ASN A1013 12000 15116 14164 -667 1584 1614 O ATOM 1781 ND2 ASN A1013 -7.246 8.727 7.540 1.00106.03 N ANISOU 1781 ND2 ASN A1013 11782 14776 13728 -734 1438 1453 N ATOM 1782 N LEU A1014 -7.866 6.829 2.575 1.00 93.05 N ANISOU 1782 N LEU A1014 10013 13616 11727 -544 1494 1561 N ATOM 1783 CA LEU A1014 -7.705 6.452 1.166 1.00 93.41 C ANISOU 1783 CA LEU A1014 10034 13779 11677 -468 1515 1589 C ATOM 1784 C LEU A1014 -9.023 6.672 0.408 1.00 97.51 C ANISOU 1784 C LEU A1014 10532 14416 12101 -456 1532 1653 C ATOM 1785 O LEU A1014 -8.997 7.049 -0.764 1.00 97.63 O ANISOU 1785 O LEU A1014 10492 14531 12071 -380 1594 1726 O ATOM 1786 CB LEU A1014 -7.248 4.985 1.055 1.00 93.45 C ANISOU 1786 CB LEU A1014 10124 13787 11597 -468 1425 1483 C ATOM 1787 CG LEU A1014 -6.581 4.562 -0.257 1.00 98.85 C ANISOU 1787 CG LEU A1014 10803 14558 12198 -366 1452 1496 C ATOM 1788 CD1 LEU A1014 -5.397 3.655 0.006 1.00 99.01 C ANISOU 1788 CD1 LEU A1014 10874 14516 12228 -349 1415 1421 C ATOM 1789 CD2 LEU A1014 -7.569 3.886 -1.198 1.00101.70 C ANISOU 1789 CD2 LEU A1014 11214 15031 12397 -347 1403 1481 C ATOM 1790 N LYS A1015 -10.165 6.444 1.088 1.00 93.75 N ANISOU 1790 N LYS A1015 10093 13931 11595 -527 1478 1638 N ATOM 1791 CA LYS A1015 -11.513 6.620 0.540 1.00 93.87 C ANISOU 1791 CA LYS A1015 10084 14052 11529 -532 1483 1712 C ATOM 1792 C LYS A1015 -11.865 8.110 0.405 1.00 98.08 C ANISOU 1792 C LYS A1015 10528 14604 12134 -498 1605 1837 C ATOM 1793 O LYS A1015 -12.684 8.462 -0.445 1.00 98.08 O ANISOU 1793 O LYS A1015 10477 14717 12071 -470 1643 1926 O ATOM 1794 CB LYS A1015 -12.557 5.906 1.414 1.00 95.98 C ANISOU 1794 CB LYS A1015 10410 14296 11762 -617 1389 1675 C ATOM 1795 CG LYS A1015 -12.474 4.378 1.357 1.00110.42 C ANISOU 1795 CG LYS A1015 12324 16125 13506 -653 1260 1566 C ATOM 1796 CD LYS A1015 -13.505 3.681 2.253 1.00120.46 C ANISOU 1796 CD LYS A1015 13638 17372 14760 -738 1166 1547 C ATOM 1797 CE LYS A1015 -13.121 3.644 3.716 1.00130.79 C ANISOU 1797 CE LYS A1015 14978 18553 16161 -778 1156 1492 C ATOM 1798 NZ LYS A1015 -14.148 2.951 4.537 1.00139.50 N1+ ANISOU 1798 NZ LYS A1015 16113 19645 17246 -848 1071 1491 N1+ ATOM 1799 N VAL A1016 -11.246 8.975 1.243 1.00 94.51 N ANISOU 1799 N VAL A1016 10059 14038 11814 -503 1661 1845 N ATOM 1800 CA VAL A1016 -11.440 10.434 1.250 1.00 94.61 C ANISOU 1800 CA VAL A1016 9998 14034 11913 -472 1776 1955 C ATOM 1801 C VAL A1016 -10.862 11.022 -0.056 1.00 99.35 C ANISOU 1801 C VAL A1016 10508 14719 12522 -388 1861 2037 C ATOM 1802 O VAL A1016 -11.486 11.899 -0.659 1.00 99.21 O ANISOU 1802 O VAL A1016 10417 14774 12503 -349 1948 2150 O ATOM 1803 CB VAL A1016 -10.817 11.097 2.518 1.00 98.20 C ANISOU 1803 CB VAL A1016 10483 14325 12504 -504 1789 1922 C ATOM 1804 CG1 VAL A1016 -11.021 12.612 2.524 1.00 98.33 C ANISOU 1804 CG1 VAL A1016 10439 14310 12613 -471 1902 2031 C ATOM 1805 CG2 VAL A1016 -11.381 10.487 3.799 1.00 97.47 C ANISOU 1805 CG2 VAL A1016 10482 14160 12393 -571 1710 1845 C ATOM 1806 N ILE A1017 -9.689 10.512 -0.495 1.00 96.42 N ANISOU 1806 N ILE A1017 10137 14344 12154 -352 1841 1991 N ATOM 1807 CA ILE A1017 -8.998 10.937 -1.721 1.00 97.07 C ANISOU 1807 CA ILE A1017 10135 14508 12241 -257 1921 2072 C ATOM 1808 C ILE A1017 -9.824 10.505 -2.950 1.00101.87 C ANISOU 1808 C ILE A1017 10733 15283 12691 -208 1920 2108 C ATOM 1809 O ILE A1017 -9.921 11.272 -3.910 1.00102.02 O ANISOU 1809 O ILE A1017 10662 15396 12706 -134 2012 2219 O ATOM 1810 CB ILE A1017 -7.538 10.392 -1.783 1.00100.30 C ANISOU 1810 CB ILE A1017 10555 14868 12687 -225 1897 2020 C ATOM 1811 CG1 ILE A1017 -6.774 10.678 -0.468 1.00100.29 C ANISOU 1811 CG1 ILE A1017 10575 14699 12833 -292 1869 1974 C ATOM 1812 CG2 ILE A1017 -6.782 10.974 -2.992 1.00101.78 C ANISOU 1812 CG2 ILE A1017 10639 15137 12897 -112 1996 2131 C ATOM 1813 CD1 ILE A1017 -5.513 9.849 -0.232 1.00107.70 C ANISOU 1813 CD1 ILE A1017 11546 15580 13795 -290 1815 1904 C ATOM 1814 N GLU A1018 -10.444 9.302 -2.896 1.00 98.64 N ANISOU 1814 N GLU A1018 10415 14908 12157 -253 1809 2018 N ATOM 1815 CA GLU A1018 -11.289 8.741 -3.963 1.00 99.19 C ANISOU 1815 CA GLU A1018 10499 15122 12068 -226 1772 2035 C ATOM 1816 C GLU A1018 -12.476 9.664 -4.285 1.00103.71 C ANISOU 1816 C GLU A1018 10994 15780 12632 -228 1838 2160 C ATOM 1817 O GLU A1018 -12.878 9.753 -5.447 1.00103.98 O ANISOU 1817 O GLU A1018 10987 15949 12570 -170 1864 2227 O ATOM 1818 CB GLU A1018 -11.801 7.342 -3.584 1.00100.36 C ANISOU 1818 CB GLU A1018 10762 15256 12115 -301 1625 1918 C ATOM 1819 CG GLU A1018 -10.728 6.266 -3.606 1.00110.86 C ANISOU 1819 CG GLU A1018 12175 16536 13411 -278 1560 1800 C ATOM 1820 CD GLU A1018 -11.220 4.870 -3.278 1.00131.01 C ANISOU 1820 CD GLU A1018 14841 19067 15868 -350 1413 1686 C ATOM 1821 OE1 GLU A1018 -10.865 4.358 -2.192 1.00124.89 O ANISOU 1821 OE1 GLU A1018 14118 18180 15155 -412 1359 1604 O ATOM 1822 OE2 GLU A1018 -11.960 4.288 -4.103 1.00125.49 O1- ANISOU 1822 OE2 GLU A1018 14181 18463 15035 -346 1346 1683 O1- ATOM 1823 N LYS A1019 -13.013 10.359 -3.261 1.00100.07 N ANISOU 1823 N LYS A1019 10514 15240 12267 -287 1870 2196 N ATOM 1824 CA LYS A1019 -14.112 11.317 -3.394 1.00100.19 C ANISOU 1824 CA LYS A1019 10457 15318 12292 -286 1948 2325 C ATOM 1825 C LYS A1019 -13.591 12.606 -4.049 1.00104.79 C ANISOU 1825 C LYS A1019 10930 15927 12958 -200 2091 2438 C ATOM 1826 O LYS A1019 -12.537 13.111 -3.652 1.00104.14 O ANISOU 1826 O LYS A1019 10832 15740 12997 -182 2135 2423 O ATOM 1827 CB LYS A1019 -14.737 11.603 -2.013 1.00102.11 C ANISOU 1827 CB LYS A1019 10734 15453 12608 -359 1941 2322 C ATOM 1828 CG LYS A1019 -15.998 12.461 -2.050 1.00116.96 C ANISOU 1828 CG LYS A1019 12553 17399 14488 -356 2018 2460 C ATOM 1829 CD LYS A1019 -16.474 12.815 -0.650 1.00126.27 C ANISOU 1829 CD LYS A1019 13776 18460 15740 -402 2028 2460 C ATOM 1830 CE LYS A1019 -17.679 13.721 -0.677 1.00136.59 C ANISOU 1830 CE LYS A1019 15023 19828 17048 -383 2122 2611 C ATOM 1831 NZ LYS A1019 -18.116 14.094 0.693 1.00144.88 N1+ ANISOU 1831 NZ LYS A1019 16128 20761 18160 -407 2143 2615 N1+ ATOM 1832 N ALA A1020 -14.326 13.121 -5.059 1.00102.23 N ANISOU 1832 N ALA A1020 10525 15744 12573 -151 2158 2558 N ATOM 1833 CA ALA A1020 -13.975 14.338 -5.799 1.00102.63 C ANISOU 1833 CA ALA A1020 10459 15842 12695 -63 2299 2685 C ATOM 1834 C ALA A1020 -14.063 15.574 -4.887 1.00106.24 C ANISOU 1834 C ALA A1020 10878 16181 13308 -83 2392 2750 C ATOM 1835 O ALA A1020 -15.158 16.064 -4.592 1.00105.84 O ANISOU 1835 O ALA A1020 10811 16150 13252 -106 2430 2825 O ATOM 1836 CB ALA A1020 -14.880 14.498 -7.014 1.00104.05 C ANISOU 1836 CB ALA A1020 10568 16207 12758 -14 2336 2795 C ATOM 1837 N ASP A1021 -12.893 16.038 -4.409 1.00102.57 N ANISOU 1837 N ASP A1021 10407 15585 12979 -72 2421 2721 N ATOM 1838 CA ASP A1021 -12.761 17.181 -3.502 1.00102.20 C ANISOU 1838 CA ASP A1021 10347 15395 13088 -91 2490 2760 C ATOM 1839 C ASP A1021 -11.605 18.108 -3.927 1.00106.31 C ANISOU 1839 C ASP A1021 10775 15869 13748 -30 2575 2830 C ATOM 1840 O ASP A1021 -10.911 17.825 -4.907 1.00106.32 O ANISOU 1840 O ASP A1021 10718 15957 13720 34 2587 2854 O ATOM 1841 CB ASP A1021 -12.540 16.687 -2.057 1.00103.41 C ANISOU 1841 CB ASP A1021 10621 15386 13282 -176 2395 2628 C ATOM 1842 CG ASP A1021 -13.678 15.866 -1.483 1.00113.06 C ANISOU 1842 CG ASP A1021 11926 16637 14394 -236 2317 2577 C ATOM 1843 OD1 ASP A1021 -14.769 16.437 -1.257 1.00113.70 O ANISOU 1843 OD1 ASP A1021 11994 16741 14464 -238 2372 2660 O ATOM 1844 OD2 ASP A1021 -13.465 14.666 -1.214 1.00118.42 O1- ANISOU 1844 OD2 ASP A1021 12681 17309 15006 -280 2202 2461 O1- ATOM 1845 N ASN A1022 -11.404 19.212 -3.177 1.00102.67 N ANISOU 1845 N ASN A1022 10304 15266 13439 -47 2632 2868 N ATOM 1846 CA ASN A1022 -10.353 20.208 -3.409 1.00102.88 C ANISOU 1846 CA ASN A1022 10243 15219 13630 -7 2702 2946 C ATOM 1847 C ASN A1022 -8.962 19.663 -3.012 1.00105.98 C ANISOU 1847 C ASN A1022 10666 15508 14094 -35 2617 2857 C ATOM 1848 O ASN A1022 -8.866 18.589 -2.414 1.00104.89 O ANISOU 1848 O ASN A1022 10629 15339 13883 -89 2509 2726 O ATOM 1849 CB ASN A1022 -10.665 21.506 -2.644 1.00104.37 C ANISOU 1849 CB ASN A1022 10435 15269 13952 -27 2771 3003 C ATOM 1850 CG ASN A1022 -10.930 21.322 -1.167 1.00128.77 C ANISOU 1850 CG ASN A1022 13670 18203 17055 -109 2692 2885 C ATOM 1851 OD1 ASN A1022 -10.024 21.060 -0.371 1.00123.06 O ANISOU 1851 OD1 ASN A1022 13012 17342 16404 -160 2607 2788 O ATOM 1852 ND2 ASN A1022 -12.181 21.488 -0.766 1.00121.09 N ANISOU 1852 ND2 ASN A1022 12746 17249 16012 -115 2723 2904 N ATOM 1853 N ALA A1023 -7.893 20.417 -3.352 1.00102.75 N ANISOU 1853 N ALA A1023 10161 15048 13833 4 2668 2941 N ATOM 1854 CA ALA A1023 -6.491 20.075 -3.087 1.00102.49 C ANISOU 1854 CA ALA A1023 10124 14923 13893 -13 2604 2900 C ATOM 1855 C ALA A1023 -6.176 19.976 -1.584 1.00105.33 C ANISOU 1855 C ALA A1023 10603 15087 14330 -120 2501 2779 C ATOM 1856 O ALA A1023 -5.368 19.128 -1.201 1.00104.61 O ANISOU 1856 O ALA A1023 10558 14952 14236 -154 2411 2691 O ATOM 1857 CB ALA A1023 -5.577 21.106 -3.729 1.00104.12 C ANISOU 1857 CB ALA A1023 10185 15112 14263 47 2688 3052 C ATOM 1858 N ALA A1024 -6.804 20.831 -0.744 1.00101.46 N ANISOU 1858 N ALA A1024 10166 14481 13903 -165 2518 2776 N ATOM 1859 CA ALA A1024 -6.598 20.864 0.710 1.00100.79 C ANISOU 1859 CA ALA A1024 10206 14207 13883 -255 2426 2664 C ATOM 1860 C ALA A1024 -7.105 19.583 1.393 1.00103.16 C ANISOU 1860 C ALA A1024 10633 14529 14036 -304 2330 2517 C ATOM 1861 O ALA A1024 -6.519 19.160 2.392 1.00102.40 O ANISOU 1861 O ALA A1024 10621 14310 13975 -370 2231 2412 O ATOM 1862 CB ALA A1024 -7.290 22.076 1.311 1.00101.84 C ANISOU 1862 CB ALA A1024 10377 14229 14088 -266 2483 2704 C ATOM 1863 N GLN A1025 -8.181 18.971 0.854 1.00 98.96 N ANISOU 1863 N GLN A1025 10106 14151 13344 -274 2353 2519 N ATOM 1864 CA GLN A1025 -8.771 17.731 1.371 1.00 97.85 C ANISOU 1864 CA GLN A1025 10070 14047 13063 -317 2264 2400 C ATOM 1865 C GLN A1025 -7.864 16.525 1.096 1.00100.90 C ANISOU 1865 C GLN A1025 10463 14471 13403 -324 2181 2322 C ATOM 1866 O GLN A1025 -7.796 15.615 1.924 1.00 99.91 O ANISOU 1866 O GLN A1025 10434 14293 13235 -381 2083 2203 O ATOM 1867 CB GLN A1025 -10.161 17.487 0.756 1.00 99.10 C ANISOU 1867 CB GLN A1025 10214 14361 13078 -286 2308 2449 C ATOM 1868 CG GLN A1025 -11.276 18.380 1.304 1.00115.03 C ANISOU 1868 CG GLN A1025 12258 16341 15107 -286 2375 2507 C ATOM 1869 CD GLN A1025 -11.750 17.963 2.676 1.00134.12 C ANISOU 1869 CD GLN A1025 14808 18657 17496 -345 2301 2407 C ATOM 1870 OE1 GLN A1025 -11.415 18.585 3.690 1.00130.01 O ANISOU 1870 OE1 GLN A1025 14354 17974 17069 -368 2293 2371 O ATOM 1871 NE2 GLN A1025 -12.550 16.907 2.739 1.00125.72 N ANISOU 1871 NE2 GLN A1025 13785 17684 16301 -368 2243 2365 N ATOM 1872 N VAL A1026 -7.177 16.524 -0.067 1.00 97.47 N ANISOU 1872 N VAL A1026 9928 14130 12977 -256 2227 2396 N ATOM 1873 CA VAL A1026 -6.266 15.457 -0.504 1.00 97.08 C ANISOU 1873 CA VAL A1026 9878 14128 12880 -235 2172 2346 C ATOM 1874 C VAL A1026 -4.994 15.484 0.372 1.00100.49 C ANISOU 1874 C VAL A1026 10328 14403 13449 -286 2111 2301 C ATOM 1875 O VAL A1026 -4.534 14.423 0.799 1.00 99.65 O ANISOU 1875 O VAL A1026 10290 14275 13299 -318 2025 2199 O ATOM 1876 CB VAL A1026 -5.930 15.565 -2.023 1.00101.67 C ANISOU 1876 CB VAL A1026 10346 14859 13425 -125 2255 2457 C ATOM 1877 CG1 VAL A1026 -5.055 14.402 -2.490 1.00101.55 C ANISOU 1877 CG1 VAL A1026 10349 14896 13338 -85 2205 2405 C ATOM 1878 CG2 VAL A1026 -7.199 15.636 -2.870 1.00101.58 C ANISOU 1878 CG2 VAL A1026 10312 15000 13283 -81 2310 2510 C ATOM 1879 N LYS A1027 -4.453 16.694 0.651 1.00 97.19 N ANISOU 1879 N LYS A1027 9851 13876 13201 -296 2151 2380 N ATOM 1880 CA LYS A1027 -3.251 16.910 1.470 1.00 97.03 C ANISOU 1880 CA LYS A1027 9837 13698 13333 -354 2087 2359 C ATOM 1881 C LYS A1027 -3.437 16.412 2.907 1.00 99.66 C ANISOU 1881 C LYS A1027 10310 13907 13648 -449 1979 2213 C ATOM 1882 O LYS A1027 -2.536 15.764 3.439 1.00 99.02 O ANISOU 1882 O LYS A1027 10260 13764 13600 -491 1896 2150 O ATOM 1883 CB LYS A1027 -2.860 18.397 1.500 1.00100.40 C ANISOU 1883 CB LYS A1027 10183 14022 13943 -355 2142 2475 C ATOM 1884 CG LYS A1027 -2.304 18.943 0.194 1.00116.47 C ANISOU 1884 CG LYS A1027 12058 16153 16043 -263 2240 2638 C ATOM 1885 CD LYS A1027 -1.969 20.418 0.338 1.00128.36 C ANISOU 1885 CD LYS A1027 13490 17537 17745 -278 2283 2750 C ATOM 1886 CE LYS A1027 -1.521 21.034 -0.960 1.00141.58 C ANISOU 1886 CE LYS A1027 14993 19312 19490 -180 2392 2929 C ATOM 1887 NZ LYS A1027 -1.159 22.466 -0.793 1.00152.40 N1+ ANISOU 1887 NZ LYS A1027 16287 20549 21068 -202 2424 3044 N1+ ATOM 1888 N ASP A1028 -4.600 16.716 3.526 1.00 95.51 N ANISOU 1888 N ASP A1028 9865 13353 13070 -476 1985 2172 N ATOM 1889 CA ASP A1028 -4.946 16.339 4.901 1.00 94.63 C ANISOU 1889 CA ASP A1028 9890 13133 12931 -549 1897 2046 C ATOM 1890 C ASP A1028 -5.030 14.814 5.067 1.00 97.12 C ANISOU 1890 C ASP A1028 10267 13518 13118 -569 1820 1938 C ATOM 1891 O ASP A1028 -4.622 14.298 6.108 1.00 96.38 O ANISOU 1891 O ASP A1028 10254 13327 13038 -629 1729 1840 O ATOM 1892 CB ASP A1028 -6.280 16.987 5.315 1.00 96.45 C ANISOU 1892 CB ASP A1028 10179 13350 13116 -542 1947 2057 C ATOM 1893 CG ASP A1028 -6.670 16.773 6.768 1.00106.69 C ANISOU 1893 CG ASP A1028 11618 14531 14390 -598 1873 1946 C ATOM 1894 OD1 ASP A1028 -5.890 17.177 7.660 1.00107.58 O ANISOU 1894 OD1 ASP A1028 11782 14486 14606 -646 1812 1901 O ATOM 1895 OD2 ASP A1028 -7.777 16.249 7.012 1.00112.15 O1- ANISOU 1895 OD2 ASP A1028 12366 15288 14959 -592 1874 1915 O1- ATOM 1896 N ALA A1029 -5.550 14.103 4.048 1.00 93.02 N ANISOU 1896 N ALA A1029 9713 13160 12472 -518 1850 1957 N ATOM 1897 CA ALA A1029 -5.694 12.647 4.063 1.00 92.08 C ANISOU 1897 CA ALA A1029 9652 13107 12225 -532 1776 1861 C ATOM 1898 C ALA A1029 -4.344 11.941 3.877 1.00 95.47 C ANISOU 1898 C ALA A1029 10061 13524 12689 -526 1732 1833 C ATOM 1899 O ALA A1029 -4.109 10.920 4.524 1.00 94.56 O ANISOU 1899 O ALA A1029 10019 13377 12533 -569 1648 1730 O ATOM 1900 CB ALA A1029 -6.664 12.206 2.980 1.00 92.80 C ANISOU 1900 CB ALA A1029 9720 13365 12176 -480 1814 1897 C ATOM 1901 N LEU A1030 -3.465 12.482 3.005 1.00 92.31 N ANISOU 1901 N LEU A1030 9556 13151 12366 -468 1794 1935 N ATOM 1902 CA LEU A1030 -2.139 11.918 2.725 1.00 92.27 C ANISOU 1902 CA LEU A1030 9513 13144 12402 -444 1772 1943 C ATOM 1903 C LEU A1030 -1.176 12.107 3.907 1.00 95.80 C ANISOU 1903 C LEU A1030 9983 13431 12987 -524 1700 1908 C ATOM 1904 O LEU A1030 -0.364 11.216 4.165 1.00 95.25 O ANISOU 1904 O LEU A1030 9934 13344 12912 -537 1642 1858 O ATOM 1905 CB LEU A1030 -1.527 12.539 1.455 1.00 93.14 C ANISOU 1905 CB LEU A1030 9493 13335 12562 -347 1870 2089 C ATOM 1906 CG LEU A1030 -2.119 12.108 0.107 1.00 98.00 C ANISOU 1906 CG LEU A1030 10084 14127 13026 -248 1933 2125 C ATOM 1907 CD1 LEU A1030 -1.777 13.108 -0.975 1.00 99.00 C ANISOU 1907 CD1 LEU A1030 10073 14320 13221 -156 2044 2287 C ATOM 1908 CD2 LEU A1030 -1.645 10.718 -0.301 1.00100.36 C ANISOU 1908 CD2 LEU A1030 10433 14493 13207 -204 1891 2059 C ATOM 1909 N THR A1031 -1.266 13.256 4.616 1.00 92.31 N ANISOU 1909 N THR A1031 9541 12868 12663 -574 1699 1933 N ATOM 1910 CA THR A1031 -0.425 13.584 5.778 1.00 92.14 C ANISOU 1910 CA THR A1031 9551 12683 12776 -657 1618 1900 C ATOM 1911 C THR A1031 -0.744 12.613 6.933 1.00 94.92 C ANISOU 1911 C THR A1031 10033 12987 13047 -723 1521 1750 C ATOM 1912 O THR A1031 0.176 12.179 7.631 1.00 94.48 O ANISOU 1912 O THR A1031 9998 12854 13048 -774 1442 1706 O ATOM 1913 CB THR A1031 -0.617 15.061 6.187 1.00100.64 C ANISOU 1913 CB THR A1031 10619 13642 13977 -686 1640 1955 C ATOM 1914 OG1 THR A1031 -0.434 15.893 5.041 1.00100.60 O ANISOU 1914 OG1 THR A1031 10486 13698 14039 -618 1739 2101 O ATOM 1915 CG2 THR A1031 0.348 15.506 7.285 1.00 99.82 C ANISOU 1915 CG2 THR A1031 10546 13359 14021 -772 1545 1932 C ATOM 1916 N LYS A1032 -2.036 12.259 7.107 1.00 90.65 N ANISOU 1916 N LYS A1032 9568 12499 12376 -719 1528 1685 N ATOM 1917 CA LYS A1032 -2.502 11.323 8.135 1.00 89.66 C ANISOU 1917 CA LYS A1032 9555 12344 12166 -770 1447 1559 C ATOM 1918 C LYS A1032 -2.046 9.891 7.821 1.00 92.88 C ANISOU 1918 C LYS A1032 9968 12828 12495 -760 1405 1504 C ATOM 1919 O LYS A1032 -1.792 9.124 8.752 1.00 92.07 O ANISOU 1919 O LYS A1032 9933 12669 12379 -811 1324 1412 O ATOM 1920 CB LYS A1032 -4.030 11.377 8.285 1.00 91.80 C ANISOU 1920 CB LYS A1032 9885 12664 12331 -758 1475 1538 C ATOM 1921 CG LYS A1032 -4.522 12.609 9.036 1.00106.55 C ANISOU 1921 CG LYS A1032 11796 14425 14264 -773 1499 1558 C ATOM 1922 CD LYS A1032 -6.040 12.619 9.180 1.00116.32 C ANISOU 1922 CD LYS A1032 13084 15720 15393 -751 1537 1559 C ATOM 1923 CE LYS A1032 -6.555 13.824 9.935 1.00127.66 C ANISOU 1923 CE LYS A1032 14576 17048 16879 -748 1572 1581 C ATOM 1924 NZ LYS A1032 -6.197 13.785 11.380 1.00136.92 N1+ ANISOU 1924 NZ LYS A1032 15862 18077 18086 -797 1486 1485 N1+ ATOM 1925 N MET A1033 -1.928 9.540 6.521 1.00 89.43 N ANISOU 1925 N MET A1033 9463 12514 12000 -688 1461 1562 N ATOM 1926 CA MET A1033 -1.466 8.220 6.078 1.00 88.99 C ANISOU 1926 CA MET A1033 9421 12529 11862 -660 1431 1517 C ATOM 1927 C MET A1033 0.043 8.071 6.272 1.00 92.77 C ANISOU 1927 C MET A1033 9857 12947 12445 -667 1407 1541 C ATOM 1928 O MET A1033 0.504 6.975 6.591 1.00 92.02 O ANISOU 1928 O MET A1033 9805 12849 12309 -680 1353 1473 O ATOM 1929 CB MET A1033 -1.822 7.954 4.607 1.00 91.64 C ANISOU 1929 CB MET A1033 9714 13013 12093 -568 1499 1572 C ATOM 1930 CG MET A1033 -3.290 7.655 4.373 1.00 94.95 C ANISOU 1930 CG MET A1033 10184 13511 12380 -569 1496 1536 C ATOM 1931 SD MET A1033 -3.595 6.615 2.918 1.00 99.43 S ANISOU 1931 SD MET A1033 10762 14239 12780 -484 1509 1533 S ATOM 1932 CE MET A1033 -3.036 7.687 1.606 1.00 96.97 C ANISOU 1932 CE MET A1033 10325 14002 12518 -379 1630 1684 C ATOM 1933 N ARG A1034 0.806 9.168 6.065 1.00 89.78 N ANISOU 1933 N ARG A1034 9387 12521 12206 -657 1448 1650 N ATOM 1934 CA ARG A1034 2.264 9.203 6.211 1.00 90.05 C ANISOU 1934 CA ARG A1034 9357 12496 12364 -666 1426 1709 C ATOM 1935 C ARG A1034 2.662 9.044 7.684 1.00 93.49 C ANISOU 1935 C ARG A1034 9859 12796 12867 -771 1320 1625 C ATOM 1936 O ARG A1034 3.608 8.313 7.979 1.00 93.12 O ANISOU 1936 O ARG A1034 9807 12731 12846 -786 1275 1613 O ATOM 1937 CB ARG A1034 2.836 10.510 5.638 1.00 91.14 C ANISOU 1937 CB ARG A1034 9373 12611 12645 -638 1489 1861 C ATOM 1938 CG ARG A1034 4.318 10.427 5.281 1.00101.97 C ANISOU 1938 CG ARG A1034 10642 13978 14126 -608 1497 1971 C ATOM 1939 CD ARG A1034 4.917 11.790 4.988 1.00113.22 C ANISOU 1939 CD ARG A1034 11945 15347 15727 -607 1534 2124 C ATOM 1940 NE ARG A1034 5.236 12.526 6.213 1.00122.90 N ANISOU 1940 NE ARG A1034 13199 16402 17095 -726 1440 2100 N ATOM 1941 CZ ARG A1034 6.425 12.512 6.810 1.00138.41 C ANISOU 1941 CZ ARG A1034 15124 18275 19189 -787 1365 2142 C ATOM 1942 NH1 ARG A1034 7.426 11.805 6.298 1.00126.44 N ANISOU 1942 NH1 ARG A1034 13531 16826 17686 -733 1385 2221 N ATOM 1943 NH2 ARG A1034 6.624 13.210 7.920 1.00125.63 N1+ ANISOU 1943 NH2 ARG A1034 13548 16498 17687 -897 1269 2109 N1+ ATOM 1944 N ALA A1035 1.933 9.722 8.598 1.00 89.72 N ANISOU 1944 N ALA A1035 9450 12230 12411 -835 1285 1570 N ATOM 1945 CA ALA A1035 2.163 9.676 10.045 1.00 89.33 C ANISOU 1945 CA ALA A1035 9481 12051 12410 -927 1183 1482 C ATOM 1946 C ALA A1035 1.833 8.292 10.617 1.00 92.48 C ANISOU 1946 C ALA A1035 9967 12483 12688 -945 1128 1361 C ATOM 1947 O ALA A1035 2.517 7.837 11.534 1.00 91.96 O ANISOU 1947 O ALA A1035 9934 12346 12662 -1002 1049 1310 O ATOM 1948 CB ALA A1035 1.330 10.741 10.741 1.00 90.10 C ANISOU 1948 CB ALA A1035 9643 12058 12532 -962 1176 1458 C ATOM 1949 N ALA A1036 0.797 7.625 10.067 1.00 88.62 N ANISOU 1949 N ALA A1036 9511 12102 12059 -899 1166 1322 N ATOM 1950 CA ALA A1036 0.364 6.290 10.483 1.00 87.82 C ANISOU 1950 CA ALA A1036 9486 12038 11844 -912 1116 1218 C ATOM 1951 C ALA A1036 1.340 5.209 10.000 1.00 91.86 C ANISOU 1951 C ALA A1036 9968 12598 12337 -882 1108 1219 C ATOM 1952 O ALA A1036 1.527 4.209 10.695 1.00 91.03 O ANISOU 1952 O ALA A1036 9917 12473 12199 -916 1045 1139 O ATOM 1953 CB ALA A1036 -1.032 6.003 9.955 1.00 88.18 C ANISOU 1953 CB ALA A1036 9566 12178 11759 -877 1151 1197 C ATOM 1954 N ALA A1037 1.955 5.412 8.815 1.00 89.06 N ANISOU 1954 N ALA A1037 9528 12309 12003 -810 1177 1317 N ATOM 1955 CA ALA A1037 2.915 4.484 8.210 1.00 89.20 C ANISOU 1955 CA ALA A1037 9515 12378 11997 -755 1191 1341 C ATOM 1956 C ALA A1037 4.247 4.467 8.972 1.00 93.41 C ANISOU 1956 C ALA A1037 10011 12823 12656 -803 1144 1370 C ATOM 1957 O ALA A1037 4.871 3.409 9.072 1.00 92.86 O ANISOU 1957 O ALA A1037 9959 12768 12556 -790 1122 1342 O ATOM 1958 CB ALA A1037 3.153 4.853 6.756 1.00 90.58 C ANISOU 1958 CB ALA A1037 9609 12650 12159 -650 1288 1454 C ATOM 1959 N LEU A1038 4.675 5.632 9.508 1.00 90.50 N ANISOU 1959 N LEU A1038 9596 12361 12429 -859 1123 1428 N ATOM 1960 CA LEU A1038 5.914 5.778 10.282 1.00 90.83 C ANISOU 1960 CA LEU A1038 9596 12308 12605 -921 1061 1468 C ATOM 1961 C LEU A1038 5.794 5.097 11.651 1.00 94.48 C ANISOU 1961 C LEU A1038 10155 12701 13043 -1005 962 1342 C ATOM 1962 O LEU A1038 6.799 4.632 12.189 1.00 94.23 O ANISOU 1962 O LEU A1038 10102 12629 13071 -1040 912 1353 O ATOM 1963 CB LEU A1038 6.284 7.262 10.462 1.00 91.56 C ANISOU 1963 CB LEU A1038 9625 12309 12855 -966 1051 1560 C ATOM 1964 CG LEU A1038 6.774 8.013 9.216 1.00 97.05 C ANISOU 1964 CG LEU A1038 10192 13057 13624 -890 1142 1721 C ATOM 1965 CD1 LEU A1038 6.621 9.509 9.389 1.00 97.71 C ANISOU 1965 CD1 LEU A1038 10242 13051 13832 -934 1136 1781 C ATOM 1966 CD2 LEU A1038 8.219 7.657 8.873 1.00100.20 C ANISOU 1966 CD2 LEU A1038 10487 13473 14111 -860 1149 1842 C ATOM 1967 N ASP A1039 4.569 5.044 12.207 1.00 90.74 N ANISOU 1967 N ASP A1039 9778 12217 12482 -1031 939 1234 N ATOM 1968 CA ASP A1039 4.273 4.399 13.488 1.00 90.16 C ANISOU 1968 CA ASP A1039 9798 12089 12369 -1095 855 1117 C ATOM 1969 C ASP A1039 4.066 2.889 13.300 1.00 93.69 C ANISOU 1969 C ASP A1039 10283 12617 12699 -1062 856 1050 C ATOM 1970 O ASP A1039 4.195 2.131 14.263 1.00 92.97 O ANISOU 1970 O ASP A1039 10243 12491 12592 -1107 791 975 O ATOM 1971 CB ASP A1039 3.029 5.035 14.138 1.00 91.71 C ANISOU 1971 CB ASP A1039 10077 12244 12524 -1121 841 1053 C ATOM 1972 CG ASP A1039 3.192 6.479 14.590 1.00102.78 C ANISOU 1972 CG ASP A1039 11477 13538 14038 -1161 822 1093 C ATOM 1973 OD1 ASP A1039 4.053 7.192 14.021 1.00104.07 O1- ANISOU 1973 OD1 ASP A1039 11552 13680 14312 -1158 842 1196 O1- ATOM 1974 OD2 ASP A1039 2.435 6.908 15.485 1.00108.63 O ANISOU 1974 OD2 ASP A1039 12306 14215 14753 -1188 789 1029 O ATOM 1975 N ALA A1040 3.756 2.460 12.058 1.00 90.38 N ANISOU 1975 N ALA A1040 9842 12301 12196 -982 927 1078 N ATOM 1976 CA ALA A1040 3.524 1.062 11.691 1.00 89.93 C ANISOU 1976 CA ALA A1040 9831 12316 12023 -942 928 1017 C ATOM 1977 C ALA A1040 4.837 0.282 11.538 1.00 94.34 C ANISOU 1977 C ALA A1040 10351 12880 12612 -915 931 1052 C ATOM 1978 O ALA A1040 4.860 -0.918 11.818 1.00 93.60 O ANISOU 1978 O ALA A1040 10311 12799 12455 -914 901 982 O ATOM 1979 CB ALA A1040 2.730 0.990 10.397 1.00 90.76 C ANISOU 1979 CB ALA A1040 9937 12522 12024 -865 993 1035 C ATOM 1980 N GLN A1041 5.923 0.956 11.096 1.00 91.75 N ANISOU 1980 N GLN A1041 9929 12543 12389 -889 970 1172 N ATOM 1981 CA GLN A1041 7.241 0.337 10.892 1.00 92.13 C ANISOU 1981 CA GLN A1041 9924 12602 12479 -851 987 1241 C ATOM 1982 C GLN A1041 8.057 0.278 12.213 1.00 96.04 C ANISOU 1982 C GLN A1041 10408 13005 13080 -947 904 1232 C ATOM 1983 O GLN A1041 9.182 -0.231 12.213 1.00 96.02 O ANISOU 1983 O GLN A1041 10355 13004 13124 -928 910 1297 O ATOM 1984 CB GLN A1041 8.039 1.062 9.786 1.00 94.37 C ANISOU 1984 CB GLN A1041 10098 12929 12832 -771 1071 1398 C ATOM 1985 CG GLN A1041 8.286 2.554 10.011 1.00110.26 C ANISOU 1985 CG GLN A1041 12029 14874 14990 -826 1060 1488 C ATOM 1986 CD GLN A1041 9.044 3.176 8.865 1.00130.68 C ANISOU 1986 CD GLN A1041 14497 17512 17645 -738 1147 1656 C ATOM 1987 OE1 GLN A1041 10.268 3.331 8.911 1.00126.72 O ANISOU 1987 OE1 GLN A1041 13901 16986 17261 -738 1147 1778 O ATOM 1988 NE2 GLN A1041 8.332 3.552 7.811 1.00123.23 N ANISOU 1988 NE2 GLN A1041 13547 16646 16630 -659 1224 1679 N ATOM 1989 N LYS A1042 7.476 0.767 13.329 1.00 92.20 N ANISOU 1989 N LYS A1042 9972 12440 12619 -1040 828 1155 N ATOM 1990 CA LYS A1042 8.099 0.755 14.656 1.00 91.99 C ANISOU 1990 CA LYS A1042 9953 12324 12675 -1133 736 1129 C ATOM 1991 C LYS A1042 7.588 -0.440 15.467 1.00 94.91 C ANISOU 1991 C LYS A1042 10412 12699 12951 -1156 689 1003 C ATOM 1992 O LYS A1042 6.376 -0.645 15.569 1.00 93.86 O ANISOU 1992 O LYS A1042 10354 12585 12722 -1152 688 914 O ATOM 1993 CB LYS A1042 7.834 2.074 15.405 1.00 94.72 C ANISOU 1993 CB LYS A1042 10312 12573 13104 -1210 679 1125 C ATOM 1994 CG LYS A1042 8.534 3.285 14.802 1.00110.03 C ANISOU 1994 CG LYS A1042 12152 14481 15172 -1208 704 1261 C ATOM 1995 CD LYS A1042 8.176 4.561 15.546 1.00120.43 C ANISOU 1995 CD LYS A1042 13506 15690 16562 -1281 642 1241 C ATOM 1996 CE LYS A1042 8.833 5.769 14.930 1.00132.55 C ANISOU 1996 CE LYS A1042 14940 17187 18235 -1283 663 1380 C ATOM 1997 NZ LYS A1042 8.471 7.017 15.650 1.00142.22 N1+ ANISOU 1997 NZ LYS A1042 16217 18291 19529 -1352 599 1354 N1+ ATOM 1998 N GLY A1043 8.523 -1.214 16.018 1.00 91.44 N ANISOU 1998 N GLY A1043 9954 12244 12545 -1179 655 1011 N ATOM 1999 CA GLY A1043 8.237 -2.402 16.817 1.00119.46 C ANISOU 1999 CA GLY A1043 13570 15796 16024 -1200 612 909 C ATOM 2000 C GLY A1043 7.656 -2.092 18.181 1.00142.29 C ANISOU 2000 C GLY A1043 16526 18617 18920 -1281 526 821 C ATOM 2001 O GLY A1043 8.265 -1.373 18.974 1.00102.43 O ANISOU 2001 O GLY A1043 11459 13494 13965 -1347 463 846 O ATOM 2002 N MET A1058 17.719 -9.970 13.233 1.00140.75 N1+ ANISOU 2002 N MET A1058 15903 18826 18749 -511 1166 1713 N1+ ATOM 2003 CA MET A1058 16.287 -10.214 13.407 1.00139.49 C ANISOU 2003 CA MET A1058 15874 18643 18483 -558 1108 1504 C ATOM 2004 C MET A1058 15.528 -10.005 12.085 1.00143.29 C ANISOU 2004 C MET A1058 16423 19169 18849 -451 1171 1470 C ATOM 2005 O MET A1058 15.957 -9.211 11.243 1.00143.49 O ANISOU 2005 O MET A1058 16376 19234 18911 -382 1234 1599 O ATOM 2006 CB MET A1058 15.694 -9.325 14.525 1.00141.06 C ANISOU 2006 CB MET A1058 16054 18782 18762 -725 985 1429 C ATOM 2007 CG MET A1058 15.919 -7.824 14.336 1.00145.09 C ANISOU 2007 CG MET A1058 16465 19280 19382 -768 968 1533 C ATOM 2008 SD MET A1058 15.180 -6.799 15.635 1.00148.52 S ANISOU 2008 SD MET A1058 16909 19631 19890 -946 827 1431 S ATOM 2009 CE MET A1058 16.318 -7.095 16.983 1.00145.45 C ANISOU 2009 CE MET A1058 16449 19198 19619 -1045 749 1493 C ATOM 2010 N LYS A1059 14.401 -10.727 11.915 1.00139.15 N ANISOU 2010 N LYS A1059 16036 18642 18193 -440 1148 1302 N ATOM 2011 CA LYS A1059 13.546 -10.661 10.728 1.00139.03 C ANISOU 2011 CA LYS A1059 16104 18668 18052 -351 1188 1247 C ATOM 2012 C LYS A1059 12.801 -9.320 10.694 1.00142.21 C ANISOU 2012 C LYS A1059 16464 19069 18500 -426 1147 1239 C ATOM 2013 O LYS A1059 12.042 -9.009 11.617 1.00140.88 O ANISOU 2013 O LYS A1059 16310 18856 18364 -552 1056 1144 O ATOM 2014 CB LYS A1059 12.559 -11.852 10.706 1.00141.14 C ANISOU 2014 CB LYS A1059 16525 18920 18183 -343 1150 1075 C ATOM 2015 CG LYS A1059 11.683 -11.965 9.451 1.00155.91 C ANISOU 2015 CG LYS A1059 18499 20831 19908 -249 1178 1011 C ATOM 2016 CD LYS A1059 12.415 -12.562 8.248 1.00167.00 C ANISOU 2016 CD LYS A1059 19951 22283 21218 -64 1288 1083 C ATOM 2017 CE LYS A1059 11.508 -12.680 7.049 1.00178.21 C ANISOU 2017 CE LYS A1059 21486 23740 22484 24 1299 1008 C ATOM 2018 NZ LYS A1059 12.209 -13.282 5.886 1.00188.61 N1+ ANISOU 2018 NZ LYS A1059 22870 25101 23692 220 1407 1072 N1+ ATOM 2019 N ASP A1060 13.046 -8.524 9.638 1.00139.26 N ANISOU 2019 N ASP A1060 16035 18746 18130 -338 1221 1348 N ATOM 2020 CA ASP A1060 12.430 -7.211 9.446 1.00138.73 C ANISOU 2020 CA ASP A1060 15920 18683 18109 -389 1202 1363 C ATOM 2021 C ASP A1060 11.935 -7.052 8.011 1.00142.56 C ANISOU 2021 C ASP A1060 16446 19242 18478 -261 1278 1375 C ATOM 2022 O ASP A1060 12.724 -7.168 7.069 1.00142.98 O ANISOU 2022 O ASP A1060 16468 19351 18508 -122 1375 1493 O ATOM 2023 CB ASP A1060 13.419 -6.081 9.795 1.00141.05 C ANISOU 2023 CB ASP A1060 16061 18955 18578 -437 1204 1524 C ATOM 2024 CG ASP A1060 13.910 -6.086 11.229 1.00150.91 C ANISOU 2024 CG ASP A1060 17267 20128 19942 -572 1114 1517 C ATOM 2025 OD1 ASP A1060 13.081 -5.877 12.142 1.00150.54 O ANISOU 2025 OD1 ASP A1060 17269 20030 19901 -689 1022 1394 O ATOM 2026 OD2 ASP A1060 15.131 -6.247 11.435 1.00157.68 O1- ANISOU 2026 OD2 ASP A1060 18039 20984 20888 -558 1136 1645 O1- ATOM 2027 N PHE A1061 10.626 -6.796 7.849 1.00138.24 N ANISOU 2027 N PHE A1061 15968 18700 17857 -302 1234 1261 N ATOM 2028 CA PHE A1061 10.011 -6.586 6.540 1.00138.33 C ANISOU 2028 CA PHE A1061 16021 18783 17754 -197 1291 1263 C ATOM 2029 C PHE A1061 9.625 -5.098 6.404 1.00141.49 C ANISOU 2029 C PHE A1061 16330 19193 18237 -244 1295 1327 C ATOM 2030 O PHE A1061 8.586 -4.759 5.832 1.00140.81 O ANISOU 2030 O PHE A1061 16286 19144 18073 -236 1293 1275 O ATOM 2031 CB PHE A1061 8.807 -7.530 6.341 1.00139.77 C ANISOU 2031 CB PHE A1061 16355 18971 17782 -201 1237 1096 C ATOM 2032 CG PHE A1061 8.537 -7.907 4.901 1.00142.20 C ANISOU 2032 CG PHE A1061 16743 19352 17933 -53 1297 1093 C ATOM 2033 CD1 PHE A1061 9.274 -8.908 4.277 1.00146.19 C ANISOU 2033 CD1 PHE A1061 17316 19878 18350 84 1357 1110 C ATOM 2034 CD2 PHE A1061 7.525 -7.285 4.180 1.00144.38 C ANISOU 2034 CD2 PHE A1061 17037 19678 18143 -45 1293 1070 C ATOM 2035 CE1 PHE A1061 9.020 -9.262 2.948 1.00147.99 C ANISOU 2035 CE1 PHE A1061 17639 20171 18420 230 1407 1099 C ATOM 2036 CE2 PHE A1061 7.272 -7.640 2.851 1.00148.05 C ANISOU 2036 CE2 PHE A1061 17584 20214 18455 93 1340 1063 C ATOM 2037 CZ PHE A1061 8.019 -8.627 2.245 1.00147.04 C ANISOU 2037 CZ PHE A1061 17535 20102 18234 231 1393 1072 C ATOM 2038 N ARG A1062 10.500 -4.211 6.925 1.00137.86 N ANISOU 2038 N ARG A1062 15742 18697 17941 -295 1299 1448 N ATOM 2039 CA ARG A1062 10.341 -2.755 6.888 1.00137.51 C ANISOU 2039 CA ARG A1062 15602 18643 18004 -343 1302 1526 C ATOM 2040 C ARG A1062 10.585 -2.214 5.474 1.00141.72 C ANISOU 2040 C ARG A1062 16074 19263 18509 -202 1410 1655 C ATOM 2041 O ARG A1062 10.088 -1.137 5.140 1.00141.24 O ANISOU 2041 O ARG A1062 15963 19215 18485 -217 1425 1693 O ATOM 2042 CB ARG A1062 11.295 -2.084 7.887 1.00137.98 C ANISOU 2042 CB ARG A1062 15554 18625 18249 -443 1257 1617 C ATOM 2043 N HIS A1063 11.329 -2.978 4.640 1.00138.71 N ANISOU 2043 N HIS A1063 15704 18945 18056 -55 1492 1724 N ATOM 2044 CA HIS A1063 11.646 -2.642 3.249 1.00139.33 C ANISOU 2044 CA HIS A1063 15736 19118 18086 110 1607 1852 C ATOM 2045 C HIS A1063 10.436 -2.877 2.314 1.00142.42 C ANISOU 2045 C HIS A1063 16241 19577 18296 177 1621 1744 C ATOM 2046 O HIS A1063 10.533 -2.617 1.112 1.00142.78 O ANISOU 2046 O HIS A1063 16266 19710 18275 320 1712 1832 O ATOM 2047 CB HIS A1063 12.862 -3.445 2.763 1.00141.12 C ANISOU 2047 CB HIS A1063 15948 19384 18286 255 1692 1963 C ATOM 2048 CG HIS A1063 14.168 -2.901 3.252 1.00145.04 C ANISOU 2048 CG HIS A1063 16285 19848 18974 228 1710 2147 C ATOM 2049 ND1 HIS A1063 14.868 -1.953 2.528 1.00147.76 N ANISOU 2049 ND1 HIS A1063 16484 20242 19416 312 1794 2355 N ATOM 2050 CD2 HIS A1063 14.857 -3.187 4.380 1.00146.52 C ANISOU 2050 CD2 HIS A1063 16437 19962 19272 124 1648 2158 C ATOM 2051 CE1 HIS A1063 15.957 -1.694 3.234 1.00147.51 C ANISOU 2051 CE1 HIS A1063 16331 20160 19556 250 1773 2488 C ATOM 2052 NE2 HIS A1063 15.994 -2.413 4.357 1.00147.13 N ANISOU 2052 NE2 HIS A1063 16346 20039 19519 135 1685 2374 N ATOM 2053 N GLY A1064 9.320 -3.335 2.881 1.00137.57 N ANISOU 2053 N GLY A1064 15737 18924 17608 74 1528 1567 N ATOM 2054 CA GLY A1064 8.069 -3.571 2.170 1.00137.00 C ANISOU 2054 CA GLY A1064 15771 18904 17378 103 1512 1459 C ATOM 2055 C GLY A1064 7.049 -2.479 2.427 1.00139.60 C ANISOU 2055 C GLY A1064 16058 19224 17758 -2 1474 1439 C ATOM 2056 O GLY A1064 6.303 -2.101 1.519 1.00139.36 O ANISOU 2056 O GLY A1064 16042 19265 17643 53 1504 1443 O ATOM 2057 N PHE A1065 7.017 -1.961 3.674 1.00134.97 N ANISOU 2057 N PHE A1065 15424 18550 17307 -148 1408 1420 N ATOM 2058 CA PHE A1065 6.111 -0.898 4.115 1.00133.95 C ANISOU 2058 CA PHE A1065 15262 18394 17240 -251 1373 1402 C ATOM 2059 C PHE A1065 6.647 0.500 3.766 1.00137.57 C ANISOU 2059 C PHE A1065 15581 18859 17830 -230 1439 1559 C ATOM 2060 O PHE A1065 5.847 1.429 3.637 1.00136.84 O ANISOU 2060 O PHE A1065 15463 18775 17755 -263 1445 1568 O ATOM 2061 CB PHE A1065 5.862 -0.988 5.631 1.00134.92 C ANISOU 2061 CB PHE A1065 15412 18413 17437 -402 1274 1310 C ATOM 2062 CG PHE A1065 5.056 -2.185 6.079 1.00135.93 C ANISOU 2062 CG PHE A1065 15666 18530 17451 -444 1199 1159 C ATOM 2063 CD1 PHE A1065 3.668 -2.128 6.137 1.00138.54 C ANISOU 2063 CD1 PHE A1065 16056 18874 17708 -493 1156 1075 C ATOM 2064 CD2 PHE A1065 5.686 -3.359 6.475 1.00138.14 C ANISOU 2064 CD2 PHE A1065 15996 18782 17707 -436 1173 1111 C ATOM 2065 CE1 PHE A1065 2.924 -3.234 6.561 1.00139.00 C ANISOU 2065 CE1 PHE A1065 16218 18919 17676 -537 1081 952 C ATOM 2066 CE2 PHE A1065 4.941 -4.464 6.899 1.00140.47 C ANISOU 2066 CE2 PHE A1065 16401 19060 17910 -478 1101 978 C ATOM 2067 CZ PHE A1065 3.565 -4.394 6.940 1.00138.08 C ANISOU 2067 CZ PHE A1065 16152 18770 17541 -530 1051 902 C ATOM 2068 N ASP A1066 7.986 0.652 3.615 1.00134.38 N ANISOU 2068 N ASP A1066 15083 18451 17526 -175 1489 1693 N ATOM 2069 CA ASP A1066 8.618 1.937 3.288 1.00134.62 C ANISOU 2069 CA ASP A1066 14967 18481 17701 -155 1546 1863 C ATOM 2070 C ASP A1066 8.334 2.350 1.829 1.00138.42 C ANISOU 2070 C ASP A1066 15412 19077 18103 -14 1650 1949 C ATOM 2071 O ASP A1066 8.449 3.535 1.506 1.00138.34 O ANISOU 2071 O ASP A1066 15289 19073 18199 -8 1695 2070 O ATOM 2072 CB ASP A1066 10.139 1.912 3.559 1.00137.21 C ANISOU 2072 CB ASP A1066 15194 18774 18164 -139 1562 2000 C ATOM 2073 CG ASP A1066 10.983 0.907 2.785 1.00148.38 C ANISOU 2073 CG ASP A1066 16619 20265 19496 12 1638 2064 C ATOM 2074 OD1 ASP A1066 10.454 0.279 1.840 1.00149.16 O ANISOU 2074 OD1 ASP A1066 16804 20449 19421 128 1689 2011 O ATOM 2075 OD2 ASP A1066 12.181 0.767 3.110 1.00154.82 O1- ANISOU 2075 OD2 ASP A1066 17358 21052 20417 19 1647 2175 O1- ATOM 2076 N ILE A1067 7.965 1.376 0.961 1.00134.68 N ANISOU 2076 N ILE A1067 15038 18692 17444 98 1683 1887 N ATOM 2077 CA ILE A1067 7.608 1.604 -0.447 1.00134.95 C ANISOU 2077 CA ILE A1067 15065 18844 17366 242 1772 1947 C ATOM 2078 C ILE A1067 6.324 2.448 -0.480 1.00137.56 C ANISOU 2078 C ILE A1067 15396 19185 17685 169 1750 1899 C ATOM 2079 O ILE A1067 6.235 3.397 -1.262 1.00137.57 O ANISOU 2079 O ILE A1067 15306 19247 17716 232 1825 2013 O ATOM 2080 CB ILE A1067 7.456 0.271 -1.247 1.00138.52 C ANISOU 2080 CB ILE A1067 15655 19369 17606 367 1788 1863 C ATOM 2081 CG1 ILE A1067 8.668 -0.675 -1.037 1.00139.46 C ANISOU 2081 CG1 ILE A1067 15793 19463 17733 431 1806 1894 C ATOM 2082 CG2 ILE A1067 7.212 0.547 -2.746 1.00140.16 C ANISOU 2082 CG2 ILE A1067 15855 19705 17694 532 1883 1939 C ATOM 2083 CD1 ILE A1067 8.451 -2.152 -1.479 1.00147.13 C ANISOU 2083 CD1 ILE A1067 16937 20463 18502 519 1791 1769 C ATOM 2084 N LEU A1068 5.358 2.119 0.409 1.00132.65 N ANISOU 2084 N LEU A1068 14868 18503 17030 38 1651 1746 N ATOM 2085 CA LEU A1068 4.082 2.820 0.568 1.00131.62 C ANISOU 2085 CA LEU A1068 14749 18373 16889 -42 1623 1697 C ATOM 2086 C LEU A1068 4.303 4.254 1.059 1.00134.66 C ANISOU 2086 C LEU A1068 15012 18694 17458 -110 1643 1797 C ATOM 2087 O LEU A1068 3.585 5.153 0.623 1.00134.24 O ANISOU 2087 O LEU A1068 14918 18679 17409 -104 1682 1841 O ATOM 2088 CB LEU A1068 3.148 2.071 1.538 1.00130.74 C ANISOU 2088 CB LEU A1068 14756 18204 16716 -160 1514 1530 C ATOM 2089 CG LEU A1068 2.500 0.785 1.017 1.00135.50 C ANISOU 2089 CG LEU A1068 15489 18864 17130 -117 1475 1417 C ATOM 2090 CD1 LEU A1068 3.301 -0.442 1.427 1.00135.73 C ANISOU 2090 CD1 LEU A1068 15586 18850 17135 -105 1438 1355 C ATOM 2091 CD2 LEU A1068 1.088 0.645 1.546 1.00137.16 C ANISOU 2091 CD2 LEU A1068 15771 19060 17285 -221 1394 1310 C ATOM 2092 N VAL A1069 5.308 4.464 1.944 1.00130.62 N ANISOU 2092 N VAL A1069 14448 18085 17098 -173 1612 1838 N ATOM 2093 CA VAL A1069 5.688 5.774 2.498 1.00130.28 C ANISOU 2093 CA VAL A1069 14300 17956 17244 -247 1611 1932 C ATOM 2094 C VAL A1069 6.168 6.676 1.342 1.00134.29 C ANISOU 2094 C VAL A1069 14675 18536 17813 -136 1719 2112 C ATOM 2095 O VAL A1069 5.757 7.835 1.260 1.00133.93 O ANISOU 2095 O VAL A1069 14567 18474 17848 -163 1745 2172 O ATOM 2096 CB VAL A1069 6.758 5.654 3.625 1.00134.21 C ANISOU 2096 CB VAL A1069 14775 18339 17880 -334 1540 1941 C ATOM 2097 CG1 VAL A1069 7.075 7.015 4.245 1.00134.28 C ANISOU 2097 CG1 VAL A1069 14696 18242 18081 -423 1515 2023 C ATOM 2098 CG2 VAL A1069 6.322 4.670 4.708 1.00133.13 C ANISOU 2098 CG2 VAL A1069 14765 18145 17673 -425 1443 1770 C ATOM 2099 N GLY A1070 6.992 6.111 0.456 1.00130.95 N ANISOU 2099 N GLY A1070 14216 18197 17344 -4 1787 2198 N ATOM 2100 CA GLY A1070 7.526 6.788 -0.721 1.00131.48 C ANISOU 2100 CA GLY A1070 14156 18351 17450 129 1900 2382 C ATOM 2101 C GLY A1070 6.462 7.138 -1.743 1.00134.50 C ANISOU 2101 C GLY A1070 14552 18843 17711 206 1964 2378 C ATOM 2102 O GLY A1070 6.513 8.218 -2.337 1.00134.60 O ANISOU 2102 O GLY A1070 14446 18889 17807 251 2037 2516 O ATOM 2103 N GLN A1071 5.481 6.229 -1.940 1.00129.88 N ANISOU 2103 N GLN A1071 14106 18310 16931 215 1930 2226 N ATOM 2104 CA GLN A1071 4.360 6.402 -2.872 1.00129.42 C ANISOU 2104 CA GLN A1071 14079 18361 16735 276 1971 2206 C ATOM 2105 C GLN A1071 3.416 7.518 -2.404 1.00132.01 C ANISOU 2105 C GLN A1071 14370 18643 17144 168 1955 2201 C ATOM 2106 O GLN A1071 2.890 8.252 -3.242 1.00131.90 O ANISOU 2106 O GLN A1071 14296 18712 17107 229 2027 2279 O ATOM 2107 CB GLN A1071 3.579 5.090 -3.049 1.00130.40 C ANISOU 2107 CB GLN A1071 14367 18530 16647 288 1911 2042 C ATOM 2108 CG GLN A1071 4.291 4.066 -3.930 1.00146.34 C ANISOU 2108 CG GLN A1071 16438 20626 18537 442 1952 2055 C ATOM 2109 CD GLN A1071 3.535 2.765 -4.035 1.00165.51 C ANISOU 2109 CD GLN A1071 19040 23076 20769 440 1875 1885 C ATOM 2110 OE1 GLN A1071 3.365 2.029 -3.055 1.00160.44 O ANISOU 2110 OE1 GLN A1071 18484 22348 20129 331 1780 1759 O ATOM 2111 NE2 GLN A1071 3.106 2.427 -5.241 1.00158.33 N ANISOU 2111 NE2 GLN A1071 18189 22282 19687 565 1910 1881 N ATOM 2112 N ILE A1072 3.216 7.651 -1.073 1.00127.25 N ANISOU 2112 N ILE A1072 13806 17912 16632 17 1868 2115 N ATOM 2113 CA ILE A1072 2.375 8.689 -0.461 1.00126.32 C ANISOU 2113 CA ILE A1072 13672 17730 16593 -83 1851 2106 C ATOM 2114 C ILE A1072 3.112 10.043 -0.575 1.00130.25 C ANISOU 2114 C ILE A1072 14023 18182 17284 -74 1912 2270 C ATOM 2115 O ILE A1072 2.479 11.044 -0.922 1.00129.91 O ANISOU 2115 O ILE A1072 13926 18161 17274 -68 1966 2333 O ATOM 2116 CB ILE A1072 1.992 8.320 1.009 1.00128.48 C ANISOU 2116 CB ILE A1072 14048 17882 16888 -227 1739 1962 C ATOM 2117 CG1 ILE A1072 1.001 7.126 1.029 1.00128.27 C ANISOU 2117 CG1 ILE A1072 14153 17908 16676 -239 1682 1817 C ATOM 2118 CG2 ILE A1072 1.395 9.521 1.770 1.00128.92 C ANISOU 2118 CG2 ILE A1072 14086 17845 17053 -319 1728 1972 C ATOM 2119 CD1 ILE A1072 0.883 6.363 2.371 1.00134.72 C ANISOU 2119 CD1 ILE A1072 15070 18625 17494 -351 1574 1680 C ATOM 2120 N ASP A1073 4.444 10.057 -0.322 1.00126.90 N ANISOU 2120 N ASP A1073 13530 17699 16989 -72 1905 2351 N ATOM 2121 CA ASP A1073 5.299 11.248 -0.414 1.00127.34 C ANISOU 2121 CA ASP A1073 13436 17700 17246 -69 1947 2522 C ATOM 2122 C ASP A1073 5.304 11.828 -1.835 1.00131.59 C ANISOU 2122 C ASP A1073 13860 18370 17769 75 2074 2679 C ATOM 2123 O ASP A1073 5.259 13.050 -1.985 1.00131.49 O ANISOU 2123 O ASP A1073 13746 18328 17887 64 2117 2790 O ATOM 2124 CB ASP A1073 6.739 10.934 0.030 1.00129.64 C ANISOU 2124 CB ASP A1073 13673 17924 17660 -84 1909 2590 C ATOM 2125 CG ASP A1073 6.974 11.033 1.526 1.00138.89 C ANISOU 2125 CG ASP A1073 14898 18932 18944 -246 1787 2504 C ATOM 2126 OD1 ASP A1073 6.684 12.104 2.105 1.00139.32 O ANISOU 2126 OD1 ASP A1073 14935 18883 19118 -335 1755 2513 O ATOM 2127 OD2 ASP A1073 7.530 10.075 2.103 1.00144.54 O1- ANISOU 2127 OD2 ASP A1073 15667 19617 19634 -275 1725 2439 O1- ATOM 2128 N ASP A1074 5.337 10.956 -2.867 1.00128.22 N ANISOU 2128 N ASP A1074 13456 18085 17178 212 2132 2685 N ATOM 2129 CA ASP A1074 5.307 11.357 -4.277 1.00128.76 C ANISOU 2129 CA ASP A1074 13432 18297 17195 370 2255 2824 C ATOM 2130 C ASP A1074 3.913 11.868 -4.663 1.00131.86 C ANISOU 2130 C ASP A1074 13853 18751 17498 361 2282 2779 C ATOM 2131 O ASP A1074 3.805 12.762 -5.504 1.00132.02 O ANISOU 2131 O ASP A1074 13761 18844 17557 440 2377 2917 O ATOM 2132 CB ASP A1074 5.729 10.195 -5.193 1.00131.11 C ANISOU 2132 CB ASP A1074 13777 18718 17321 525 2299 2824 C ATOM 2133 CG ASP A1074 7.182 9.768 -5.060 1.00141.48 C ANISOU 2133 CG ASP A1074 15035 20000 18721 574 2307 2918 C ATOM 2134 OD1 ASP A1074 8.052 10.653 -4.886 1.00142.51 O ANISOU 2134 OD1 ASP A1074 15017 20072 19057 557 2333 3081 O ATOM 2135 OD2 ASP A1074 7.457 8.556 -5.190 1.00147.36 O1- ANISOU 2135 OD2 ASP A1074 15879 20781 19329 636 2293 2843 O1- ATOM 2136 N ALA A1075 2.855 11.308 -4.039 1.00127.21 N ANISOU 2136 N ALA A1075 13404 18135 16794 267 2200 2601 N ATOM 2137 CA ALA A1075 1.463 11.712 -4.256 1.00126.49 C ANISOU 2137 CA ALA A1075 13347 18095 16618 243 2213 2557 C ATOM 2138 C ALA A1075 1.179 13.055 -3.577 1.00129.96 C ANISOU 2138 C ALA A1075 13720 18428 17230 147 2220 2610 C ATOM 2139 O ALA A1075 0.352 13.825 -4.070 1.00129.61 O ANISOU 2139 O ALA A1075 13633 18442 17172 170 2283 2665 O ATOM 2140 CB ALA A1075 0.516 10.645 -3.730 1.00126.34 C ANISOU 2140 CB ALA A1075 13489 18073 16441 170 2116 2370 C ATOM 2141 N LEU A1076 1.871 13.330 -2.448 1.00126.20 N ANISOU 2141 N LEU A1076 13242 17795 16914 43 2154 2594 N ATOM 2142 CA LEU A1076 1.762 14.567 -1.670 1.00125.95 C ANISOU 2142 CA LEU A1076 13170 17629 17055 -52 2143 2632 C ATOM 2143 C LEU A1076 2.356 15.747 -2.454 1.00130.73 C ANISOU 2143 C LEU A1076 13608 18254 17810 19 2241 2833 C ATOM 2144 O LEU A1076 1.815 16.852 -2.389 1.00130.37 O ANISOU 2144 O LEU A1076 13521 18167 17848 -9 2278 2885 O ATOM 2145 CB LEU A1076 2.475 14.401 -0.310 1.00125.73 C ANISOU 2145 CB LEU A1076 13196 17432 17142 -174 2031 2558 C ATOM 2146 CG LEU A1076 2.314 15.525 0.727 1.00130.42 C ANISOU 2146 CG LEU A1076 13801 17862 17892 -287 1987 2553 C ATOM 2147 CD1 LEU A1076 0.950 15.466 1.407 1.00129.74 C ANISOU 2147 CD1 LEU A1076 13845 17751 17700 -349 1955 2416 C ATOM 2148 CD2 LEU A1076 3.394 15.438 1.784 1.00133.05 C ANISOU 2148 CD2 LEU A1076 14147 18044 18360 -381 1883 2530 C ATOM 2149 N LYS A1077 3.459 15.500 -3.199 1.00128.07 N ANISOU 2149 N LYS A1077 13171 17981 17508 118 2287 2953 N ATOM 2150 CA LYS A1077 4.153 16.492 -4.030 1.00128.96 C ANISOU 2150 CA LYS A1077 13106 18127 17765 204 2384 3168 C ATOM 2151 C LYS A1077 3.266 16.958 -5.191 1.00132.93 C ANISOU 2151 C LYS A1077 13556 18780 18171 313 2499 3239 C ATOM 2152 O LYS A1077 3.322 18.131 -5.563 1.00133.10 O ANISOU 2152 O LYS A1077 13451 18793 18328 336 2571 3385 O ATOM 2153 CB LYS A1077 5.475 15.924 -4.576 1.00132.31 C ANISOU 2153 CB LYS A1077 13448 18606 18216 305 2412 3282 C ATOM 2154 CG LYS A1077 6.564 15.758 -3.523 1.00147.06 C ANISOU 2154 CG LYS A1077 15314 20325 20238 202 2313 3279 C ATOM 2155 CD LYS A1077 7.806 15.098 -4.102 1.00158.13 C ANISOU 2155 CD LYS A1077 16637 21797 21647 316 2352 3400 C ATOM 2156 CE LYS A1077 8.869 14.876 -3.055 1.00169.16 C ANISOU 2156 CE LYS A1077 18027 23055 23190 209 2249 3404 C ATOM 2157 NZ LYS A1077 10.066 14.201 -3.622 1.00179.06 N1+ ANISOU 2157 NZ LYS A1077 19202 24385 24446 330 2297 3537 N1+ ATOM 2158 N LEU A1078 2.447 16.040 -5.750 1.00128.99 N ANISOU 2158 N LEU A1078 13154 18415 17441 374 2510 3137 N ATOM 2159 CA LEU A1078 1.513 16.310 -6.849 1.00128.99 C ANISOU 2159 CA LEU A1078 13124 18572 17314 473 2603 3185 C ATOM 2160 C LEU A1078 0.372 17.226 -6.390 1.00132.24 C ANISOU 2160 C LEU A1078 13550 18931 17766 382 2606 3159 C ATOM 2161 O LEU A1078 -0.087 18.062 -7.169 1.00132.22 O ANISOU 2161 O LEU A1078 13451 19011 17776 449 2705 3275 O ATOM 2162 CB LEU A1078 0.937 14.995 -7.411 1.00128.77 C ANISOU 2162 CB LEU A1078 13221 18676 17029 538 2579 3062 C ATOM 2163 CG LEU A1078 1.907 14.071 -8.160 1.00134.22 C ANISOU 2163 CG LEU A1078 13911 19454 17632 673 2603 3097 C ATOM 2164 CD1 LEU A1078 1.413 12.640 -8.146 1.00133.91 C ANISOU 2164 CD1 LEU A1078 14046 19460 17372 673 2523 2917 C ATOM 2165 CD2 LEU A1078 2.141 14.543 -9.591 1.00137.85 C ANISOU 2165 CD2 LEU A1078 14245 20073 18060 854 2736 3274 C ATOM 2166 N ALA A1079 -0.073 17.068 -5.127 1.00127.92 N ANISOU 2166 N ALA A1079 13120 18249 17236 240 2506 3015 N ATOM 2167 CA ALA A1079 -1.141 17.865 -4.519 1.00127.29 C ANISOU 2167 CA ALA A1079 13076 18100 17188 155 2505 2981 C ATOM 2168 C ALA A1079 -0.665 19.288 -4.199 1.00131.71 C ANISOU 2168 C ALA A1079 13532 18534 17980 121 2543 3105 C ATOM 2169 O ALA A1079 -1.463 20.224 -4.281 1.00131.31 O ANISOU 2169 O ALA A1079 13452 18479 17962 116 2604 3155 O ATOM 2170 CB ALA A1079 -1.642 17.188 -3.254 1.00127.06 C ANISOU 2170 CB ALA A1079 13208 17967 17104 32 2388 2797 C ATOM 2171 N ASN A1080 0.627 19.446 -3.836 1.00128.83 N ANISOU 2171 N ASN A1080 13109 18061 17778 96 2504 3160 N ATOM 2172 CA ASN A1080 1.247 20.734 -3.503 1.00129.42 C ANISOU 2172 CA ASN A1080 13085 17997 18093 52 2515 3282 C ATOM 2173 C ASN A1080 1.384 21.630 -4.740 1.00134.35 C ANISOU 2173 C ASN A1080 13533 18725 18789 169 2650 3487 C ATOM 2174 O ASN A1080 1.307 22.854 -4.613 1.00134.40 O ANISOU 2174 O ASN A1080 13470 18642 18955 141 2686 3581 O ATOM 2175 CB ASN A1080 2.619 20.525 -2.855 1.00130.44 C ANISOU 2175 CB ASN A1080 13193 18001 18368 -8 2425 3297 C ATOM 2176 CG ASN A1080 2.577 19.866 -1.495 1.00151.22 C ANISOU 2176 CG ASN A1080 15987 20502 20970 -135 2288 3110 C ATOM 2177 OD1 ASN A1080 1.830 20.268 -0.593 1.00144.91 O ANISOU 2177 OD1 ASN A1080 15291 19592 20174 -225 2242 3010 O ATOM 2178 ND2 ASN A1080 3.426 18.870 -1.298 1.00142.53 N ANISOU 2178 ND2 ASN A1080 14906 19406 19843 -139 2226 3071 N ATOM 2179 N GLU A1081 1.585 21.021 -5.926 1.00131.37 N ANISOU 2179 N GLU A1081 13087 18534 18292 307 2725 3558 N ATOM 2180 CA GLU A1081 1.721 21.721 -7.208 1.00132.19 C ANISOU 2180 CA GLU A1081 13023 18769 18435 444 2861 3757 C ATOM 2181 C GLU A1081 0.380 22.308 -7.665 1.00135.91 C ANISOU 2181 C GLU A1081 13496 19326 18820 470 2942 3764 C ATOM 2182 O GLU A1081 0.344 23.430 -8.172 1.00136.13 O ANISOU 2182 O GLU A1081 13390 19364 18970 514 3037 3921 O ATOM 2183 CB GLU A1081 2.273 20.776 -8.291 1.00134.00 C ANISOU 2183 CB GLU A1081 13211 19176 18526 595 2911 3810 C ATOM 2184 CG GLU A1081 3.721 20.365 -8.087 1.00145.15 C ANISOU 2184 CG GLU A1081 14573 20530 20046 607 2870 3872 C ATOM 2185 CD GLU A1081 4.241 19.323 -9.059 1.00166.11 C ANISOU 2185 CD GLU A1081 17220 23351 22542 766 2918 3906 C ATOM 2186 OE1 GLU A1081 4.723 18.267 -8.589 1.00160.65 O ANISOU 2186 OE1 GLU A1081 16627 22628 21783 740 2839 3800 O ATOM 2187 OE2 GLU A1081 4.165 19.555 -10.288 1.00161.29 O1- ANISOU 2187 OE2 GLU A1081 16510 22902 21869 922 3037 4040 O1- ATOM 2188 N GLY A1082 -0.693 21.539 -7.481 1.00131.71 N ANISOU 2188 N GLY A1082 13105 18853 18084 441 2904 3604 N ATOM 2189 CA GLY A1082 -2.050 21.914 -7.865 1.00131.31 C ANISOU 2189 CA GLY A1082 13069 18895 17926 459 2968 3602 C ATOM 2190 C GLY A1082 -2.799 20.816 -8.594 1.00134.90 C ANISOU 2190 C GLY A1082 13599 19535 18123 525 2965 3522 C ATOM 2191 O GLY A1082 -4.016 20.913 -8.775 1.00134.07 O ANISOU 2191 O GLY A1082 13530 19505 17906 518 2990 3496 O ATOM 2192 N LYS A1083 -2.073 19.761 -9.019 1.00131.81 N ANISOU 2192 N LYS A1083 13234 19214 17636 591 2932 3488 N ATOM 2193 CA LYS A1083 -2.616 18.606 -9.737 1.00131.58 C ANISOU 2193 CA LYS A1083 13291 19344 17357 660 2911 3402 C ATOM 2194 C LYS A1083 -3.391 17.710 -8.759 1.00134.59 C ANISOU 2194 C LYS A1083 13850 19658 17629 533 2785 3200 C ATOM 2195 O LYS A1083 -2.795 16.889 -8.054 1.00133.71 O ANISOU 2195 O LYS A1083 13827 19458 17518 479 2692 3090 O ATOM 2196 CB LYS A1083 -1.491 17.824 -10.449 1.00134.80 C ANISOU 2196 CB LYS A1083 13679 19827 17711 782 2922 3438 C ATOM 2197 CG LYS A1083 -0.748 18.625 -11.515 1.00150.48 C ANISOU 2197 CG LYS A1083 15483 21904 19788 930 3054 3656 C ATOM 2198 CD LYS A1083 0.459 17.870 -12.050 1.00161.15 C ANISOU 2198 CD LYS A1083 16818 23309 21104 1053 3067 3701 C ATOM 2199 CE LYS A1083 1.235 18.689 -13.051 1.00173.10 C ANISOU 2199 CE LYS A1083 18137 24910 22722 1206 3203 3938 C ATOM 2200 NZ LYS A1083 2.432 17.963 -13.546 1.00183.15 N1+ ANISOU 2200 NZ LYS A1083 19392 26235 23962 1340 3225 4001 N1+ ATOM 2201 N VAL A1084 -4.720 17.906 -8.696 1.00131.02 N ANISOU 2201 N VAL A1084 13439 19249 17094 488 2786 3167 N ATOM 2202 CA VAL A1084 -5.623 17.168 -7.804 1.00130.04 C ANISOU 2202 CA VAL A1084 13464 19073 16872 373 2678 3005 C ATOM 2203 C VAL A1084 -5.913 15.781 -8.408 1.00134.01 C ANISOU 2203 C VAL A1084 14066 19700 17154 414 2610 2905 C ATOM 2204 O VAL A1084 -5.816 14.782 -7.693 1.00132.96 O ANISOU 2204 O VAL A1084 14053 19497 16969 344 2501 2763 O ATOM 2205 CB VAL A1084 -6.935 17.956 -7.507 1.00133.71 C ANISOU 2205 CB VAL A1084 13923 19537 17342 317 2714 3034 C ATOM 2206 CG1 VAL A1084 -7.809 17.225 -6.489 1.00132.64 C ANISOU 2206 CG1 VAL A1084 13932 19341 17125 202 2605 2886 C ATOM 2207 CG2 VAL A1084 -6.635 19.374 -7.023 1.00133.75 C ANISOU 2207 CG2 VAL A1084 13839 19418 17561 293 2789 3137 C ATOM 2208 N LYS A1085 -6.253 15.729 -9.717 1.00131.44 N ANISOU 2208 N LYS A1085 13693 19552 16698 528 2670 2980 N ATOM 2209 CA LYS A1085 -6.574 14.502 -10.460 1.00131.58 C ANISOU 2209 CA LYS A1085 13808 19693 16492 581 2606 2896 C ATOM 2210 C LYS A1085 -5.386 13.528 -10.495 1.00135.64 C ANISOU 2210 C LYS A1085 14386 20175 16976 634 2560 2827 C ATOM 2211 O LYS A1085 -5.599 12.317 -10.409 1.00134.96 O ANISOU 2211 O LYS A1085 14435 20096 16746 610 2456 2690 O ATOM 2212 CB LYS A1085 -7.027 14.831 -11.892 1.00135.11 C ANISOU 2212 CB LYS A1085 14179 20333 16823 709 2692 3011 C ATOM 2213 CG LYS A1085 -8.405 15.483 -11.958 1.00150.45 C ANISOU 2213 CG LYS A1085 16085 22338 18740 656 2718 3063 C ATOM 2214 CD LYS A1085 -8.815 15.813 -13.383 1.00162.13 C ANISOU 2214 CD LYS A1085 17484 24015 20104 784 2801 3183 C ATOM 2215 CE LYS A1085 -10.194 16.421 -13.441 1.00173.64 C ANISOU 2215 CE LYS A1085 18901 25540 21535 729 2826 3244 C ATOM 2216 NZ LYS A1085 -10.604 16.722 -14.837 1.00184.54 N1+ ANISOU 2216 NZ LYS A1085 20200 27121 22795 852 2903 3363 N1+ ATOM 2217 N GLU A1086 -4.147 14.054 -10.603 1.00132.73 N ANISOU 2217 N GLU A1086 13916 19767 16750 704 2636 2929 N ATOM 2218 CA GLU A1086 -2.918 13.253 -10.611 1.00132.90 C ANISOU 2218 CA GLU A1086 13975 19755 16766 764 2611 2897 C ATOM 2219 C GLU A1086 -2.630 12.684 -9.218 1.00135.70 C ANISOU 2219 C GLU A1086 14426 19940 17196 622 2500 2760 C ATOM 2220 O GLU A1086 -2.114 11.570 -9.114 1.00135.24 O ANISOU 2220 O GLU A1086 14465 19865 17055 639 2435 2665 O ATOM 2221 CB GLU A1086 -1.720 14.077 -11.108 1.00135.16 C ANISOU 2221 CB GLU A1086 14102 20051 17203 875 2728 3079 C ATOM 2222 CG GLU A1086 -1.583 14.136 -12.624 1.00147.36 C ANISOU 2222 CG GLU A1086 15579 21782 18628 1068 2831 3200 C ATOM 2223 CD GLU A1086 -2.643 14.902 -13.395 1.00169.14 C ANISOU 2223 CD GLU A1086 18270 24666 21330 1104 2901 3280 C ATOM 2224 OE1 GLU A1086 -3.059 15.988 -12.930 1.00163.25 O ANISOU 2224 OE1 GLU A1086 17434 23859 20734 1021 2938 3346 O ATOM 2225 OE2 GLU A1086 -3.023 14.435 -14.493 1.00164.52 O1- ANISOU 2225 OE2 GLU A1086 17721 24241 20547 1223 2921 3284 O1- ATOM 2226 N ALA A1087 -2.972 13.445 -8.155 1.00131.48 N ANISOU 2226 N ALA A1087 13868 19279 16808 491 2480 2752 N ATOM 2227 CA ALA A1087 -2.794 13.038 -6.757 1.00130.39 C ANISOU 2227 CA ALA A1087 13818 18979 16745 354 2377 2627 C ATOM 2228 C ALA A1087 -3.780 11.925 -6.383 1.00133.36 C ANISOU 2228 C ALA A1087 14347 19369 16956 282 2268 2464 C ATOM 2229 O ALA A1087 -3.434 11.045 -5.593 1.00132.40 O ANISOU 2229 O ALA A1087 14319 19160 16825 219 2177 2346 O ATOM 2230 CB ALA A1087 -2.975 14.233 -5.835 1.00130.78 C ANISOU 2230 CB ALA A1087 13812 18900 16978 255 2393 2670 C ATOM 2231 N GLN A1088 -4.998 11.962 -6.963 1.00129.89 N ANISOU 2231 N GLN A1088 13922 19038 16391 292 2276 2468 N ATOM 2232 CA GLN A1088 -6.051 10.965 -6.749 1.00129.23 C ANISOU 2232 CA GLN A1088 13966 18983 16153 224 2171 2340 C ATOM 2233 C GLN A1088 -5.705 9.656 -7.465 1.00133.48 C ANISOU 2233 C GLN A1088 14599 19594 16524 298 2114 2261 C ATOM 2234 O GLN A1088 -6.004 8.579 -6.945 1.00132.58 O ANISOU 2234 O GLN A1088 14607 19437 16330 229 2002 2127 O ATOM 2235 CB GLN A1088 -7.416 11.494 -7.225 1.00130.67 C ANISOU 2235 CB GLN A1088 14116 19266 16264 215 2201 2399 C ATOM 2236 CG GLN A1088 -7.989 12.606 -6.351 1.00145.69 C ANISOU 2236 CG GLN A1088 15965 21084 18305 132 2241 2452 C ATOM 2237 CD GLN A1088 -9.284 13.147 -6.899 1.00165.52 C ANISOU 2237 CD GLN A1088 18433 23709 20749 137 2286 2533 C ATOM 2238 OE1 GLN A1088 -10.376 12.703 -6.532 1.00160.76 O ANISOU 2238 OE1 GLN A1088 17896 23121 20065 63 2216 2482 O ATOM 2239 NE2 GLN A1088 -9.192 14.129 -7.782 1.00158.62 N ANISOU 2239 NE2 GLN A1088 17437 22918 19912 227 2405 2674 N ATOM 2240 N ALA A1089 -5.069 9.756 -8.652 1.00131.00 N ANISOU 2240 N ALA A1089 14230 19385 16157 446 2194 2347 N ATOM 2241 CA ALA A1089 -4.643 8.615 -9.466 1.00131.49 C ANISOU 2241 CA ALA A1089 14387 19521 16052 550 2160 2287 C ATOM 2242 C ALA A1089 -3.441 7.902 -8.834 1.00135.12 C ANISOU 2242 C ALA A1089 14898 19873 16570 550 2127 2224 C ATOM 2243 O ALA A1089 -3.357 6.675 -8.910 1.00134.78 O ANISOU 2243 O ALA A1089 14986 19829 16396 565 2046 2108 O ATOM 2244 CB ALA A1089 -4.297 9.076 -10.873 1.00133.36 C ANISOU 2244 CB ALA A1089 14542 19904 16225 724 2273 2419 C ATOM 2245 N ALA A1090 -2.520 8.672 -8.212 1.00131.47 N ANISOU 2245 N ALA A1090 14331 19318 16305 531 2184 2304 N ATOM 2246 CA ALA A1090 -1.327 8.153 -7.537 1.00131.15 C ANISOU 2246 CA ALA A1090 14312 19172 16348 520 2158 2271 C ATOM 2247 C ALA A1090 -1.704 7.420 -6.245 1.00134.01 C ANISOU 2247 C ALA A1090 14785 19411 16720 366 2033 2113 C ATOM 2248 O ALA A1090 -1.072 6.418 -5.906 1.00133.44 O ANISOU 2248 O ALA A1090 14795 19290 16615 367 1978 2031 O ATOM 2249 CB ALA A1090 -0.360 9.286 -7.235 1.00132.06 C ANISOU 2249 CB ALA A1090 14274 19221 16681 526 2240 2414 C ATOM 2250 N ALA A1091 -2.743 7.915 -5.540 1.00129.97 N ANISOU 2250 N ALA A1091 14276 18856 16250 244 1994 2080 N ATOM 2251 CA ALA A1091 -3.260 7.325 -4.302 1.00128.94 C ANISOU 2251 CA ALA A1091 14242 18621 16128 103 1883 1947 C ATOM 2252 C ALA A1091 -4.081 6.062 -4.593 1.00133.07 C ANISOU 2252 C ALA A1091 14898 19200 16462 92 1788 1827 C ATOM 2253 O ALA A1091 -4.256 5.228 -3.703 1.00131.94 O ANISOU 2253 O ALA A1091 14847 18978 16307 2 1690 1711 O ATOM 2254 CB ALA A1091 -4.108 8.341 -3.555 1.00129.09 C ANISOU 2254 CB ALA A1091 14217 18586 16246 4 1891 1975 C ATOM 2255 N GLU A1092 -4.579 5.923 -5.839 1.00130.76 N ANISOU 2255 N GLU A1092 14617 19043 16025 184 1812 1858 N ATOM 2256 CA GLU A1092 -5.353 4.764 -6.287 1.00131.04 C ANISOU 2256 CA GLU A1092 14780 19135 15873 180 1712 1754 C ATOM 2257 C GLU A1092 -4.420 3.564 -6.515 1.00135.67 C ANISOU 2257 C GLU A1092 15470 19701 16377 251 1674 1671 C ATOM 2258 O GLU A1092 -4.857 2.419 -6.389 1.00135.15 O ANISOU 2258 O GLU A1092 15534 19616 16201 209 1562 1549 O ATOM 2259 CB GLU A1092 -6.138 5.101 -7.566 1.00133.24 C ANISOU 2259 CB GLU A1092 15036 19564 16024 257 1748 1822 C ATOM 2260 CG GLU A1092 -7.375 4.240 -7.786 1.00144.42 C ANISOU 2260 CG GLU A1092 16562 21026 17284 196 1624 1734 C ATOM 2261 CD GLU A1092 -8.514 4.417 -6.796 1.00164.89 C ANISOU 2261 CD GLU A1092 19147 23568 19936 41 1558 1715 C ATOM 2262 OE1 GLU A1092 -8.794 5.571 -6.399 1.00158.96 O ANISOU 2262 OE1 GLU A1092 18288 22807 19305 8 1636 1809 O ATOM 2263 OE2 GLU A1092 -9.155 3.399 -6.450 1.00159.40 O1- ANISOU 2263 OE2 GLU A1092 18556 22843 19164 -40 1429 1614 O1- ATOM 2264 N GLN A1093 -3.134 3.834 -6.835 1.00133.06 N ANISOU 2264 N GLN A1093 15079 19369 16107 361 1767 1747 N ATOM 2265 CA GLN A1093 -2.097 2.819 -7.048 1.00133.55 C ANISOU 2265 CA GLN A1093 15223 19413 16108 450 1759 1698 C ATOM 2266 C GLN A1093 -1.657 2.226 -5.697 1.00136.81 C ANISOU 2266 C GLN A1093 15679 19683 16619 336 1686 1607 C ATOM 2267 O GLN A1093 -1.196 1.084 -5.650 1.00136.58 O ANISOU 2267 O GLN A1093 15758 19622 16513 365 1636 1519 O ATOM 2268 CB GLN A1093 -0.897 3.424 -7.801 1.00135.78 C ANISOU 2268 CB GLN A1093 15401 19748 16441 607 1895 1844 C ATOM 2269 CG GLN A1093 -0.001 2.389 -8.480 1.00153.58 C ANISOU 2269 CG GLN A1093 17749 22033 18570 757 1911 1819 C ATOM 2270 CD GLN A1093 1.169 3.025 -9.186 1.00175.90 C ANISOU 2270 CD GLN A1093 20456 24918 21458 918 2053 1989 C ATOM 2271 OE1 GLN A1093 2.266 3.148 -8.632 1.00171.88 O ANISOU 2271 OE1 GLN A1093 19878 24339 21088 922 2092 2053 O ATOM 2272 NE2 GLN A1093 0.967 3.428 -10.432 1.00169.58 N ANISOU 2272 NE2 GLN A1093 19625 24252 20554 1059 2130 2075 N ATOM 2273 N LEU A1094 -1.818 3.005 -4.603 1.00132.68 N ANISOU 2273 N LEU A1094 15078 19075 16260 210 1681 1627 N ATOM 2274 CA LEU A1094 -1.496 2.610 -3.228 1.00131.76 C ANISOU 2274 CA LEU A1094 14990 18826 16245 93 1612 1549 C ATOM 2275 C LEU A1094 -2.475 1.526 -2.749 1.00135.44 C ANISOU 2275 C LEU A1094 15588 19266 16609 1 1485 1404 C ATOM 2276 O LEU A1094 -2.094 0.670 -1.949 1.00134.56 O ANISOU 2276 O LEU A1094 15543 19070 16514 -51 1420 1317 O ATOM 2277 CB LEU A1094 -1.549 3.855 -2.306 1.00131.17 C ANISOU 2277 CB LEU A1094 14808 18676 16352 -2 1640 1613 C ATOM 2278 CG LEU A1094 -0.757 3.878 -0.973 1.00135.29 C ANISOU 2278 CG LEU A1094 15317 19062 17025 -91 1605 1587 C ATOM 2279 CD1 LEU A1094 -1.498 3.196 0.171 1.00134.60 C ANISOU 2279 CD1 LEU A1094 15323 18898 16919 -217 1495 1456 C ATOM 2280 CD2 LEU A1094 0.691 3.429 -1.133 1.00138.35 C ANISOU 2280 CD2 LEU A1094 15686 19432 17450 -14 1637 1623 C ATOM 2281 N LYS A1095 -3.727 1.559 -3.262 1.00132.47 N ANISOU 2281 N LYS A1095 15240 18962 16129 -19 1450 1391 N ATOM 2282 CA LYS A1095 -4.795 0.602 -2.953 1.00132.18 C ANISOU 2282 CA LYS A1095 15313 18914 15997 -108 1325 1280 C ATOM 2283 C LYS A1095 -4.445 -0.794 -3.498 1.00137.12 C ANISOU 2283 C LYS A1095 16072 19545 16480 -45 1259 1183 C ATOM 2284 O LYS A1095 -4.729 -1.789 -2.835 1.00136.32 O ANISOU 2284 O LYS A1095 16063 19377 16357 -125 1155 1078 O ATOM 2285 CB LYS A1095 -6.135 1.094 -3.532 1.00134.88 C ANISOU 2285 CB LYS A1095 15633 19348 16268 -130 1313 1324 C ATOM 2286 CG LYS A1095 -7.361 0.353 -3.009 1.00148.87 C ANISOU 2286 CG LYS A1095 17480 21098 17984 -248 1184 1246 C ATOM 2287 CD LYS A1095 -8.642 0.880 -3.635 1.00159.30 C ANISOU 2287 CD LYS A1095 18765 22521 19241 -266 1177 1314 C ATOM 2288 CE LYS A1095 -9.859 0.147 -3.128 1.00170.09 C ANISOU 2288 CE LYS A1095 20193 23870 20563 -384 1045 1260 C ATOM 2289 NZ LYS A1095 -11.107 0.662 -3.748 1.00179.62 N1+ ANISOU 2289 NZ LYS A1095 21354 25181 21710 -404 1038 1344 N1+ ATOM 2290 N THR A1096 -3.819 -0.862 -4.691 1.00135.03 N ANISOU 2290 N THR A1096 15824 19360 16123 104 1325 1222 N ATOM 2291 CA THR A1096 -3.409 -2.125 -5.318 1.00135.85 C ANISOU 2291 CA THR A1096 16069 19468 16078 192 1278 1136 C ATOM 2292 C THR A1096 -2.140 -2.679 -4.643 1.00139.80 C ANISOU 2292 C THR A1096 16586 19876 16654 214 1300 1108 C ATOM 2293 O THR A1096 -1.894 -3.886 -4.712 1.00139.76 O ANISOU 2293 O THR A1096 16713 19835 16555 243 1238 1011 O ATOM 2294 CB THR A1096 -3.195 -1.954 -6.833 1.00145.35 C ANISOU 2294 CB THR A1096 17289 20794 17143 363 1350 1196 C ATOM 2295 OG1 THR A1096 -2.249 -0.911 -7.071 1.00145.22 O ANISOU 2295 OG1 THR A1096 17134 20813 17232 456 1495 1335 O ATOM 2296 CG2 THR A1096 -4.492 -1.671 -7.586 1.00144.26 C ANISOU 2296 CG2 THR A1096 17163 20753 16897 342 1303 1205 C ATOM 2297 N THR A1097 -1.348 -1.801 -3.989 1.00136.03 N ANISOU 2297 N THR A1097 15979 19358 16347 198 1383 1198 N ATOM 2298 CA THR A1097 -0.109 -2.157 -3.290 1.00135.75 C ANISOU 2298 CA THR A1097 15931 19240 16407 208 1409 1199 C ATOM 2299 C THR A1097 -0.440 -2.877 -1.965 1.00138.79 C ANISOU 2299 C THR A1097 16373 19516 16845 59 1299 1085 C ATOM 2300 O THR A1097 0.187 -3.894 -1.661 1.00138.42 O ANISOU 2300 O THR A1097 16404 19414 16775 75 1268 1019 O ATOM 2301 CB THR A1097 0.759 -0.901 -3.059 1.00143.86 C ANISOU 2301 CB THR A1097 16795 20261 17606 226 1517 1343 C ATOM 2302 OG1 THR A1097 0.865 -0.164 -4.279 1.00144.47 O ANISOU 2302 OG1 THR A1097 16806 20447 17639 356 1616 1458 O ATOM 2303 CG2 THR A1097 2.157 -1.231 -2.538 1.00142.57 C ANISOU 2303 CG2 THR A1097 16604 20030 17535 257 1550 1376 C ATOM 2304 N ARG A1098 -1.416 -2.353 -1.188 1.00134.63 N ANISOU 2304 N ARG A1098 15808 18960 16386 -75 1248 1069 N ATOM 2305 CA ARG A1098 -1.831 -2.932 0.097 1.00133.63 C ANISOU 2305 CA ARG A1098 15723 18738 16310 -211 1149 976 C ATOM 2306 C ARG A1098 -2.657 -4.221 -0.112 1.00137.79 C ANISOU 2306 C ARG A1098 16388 19267 16699 -238 1035 860 C ATOM 2307 O ARG A1098 -2.680 -5.071 0.781 1.00136.88 O ANISOU 2307 O ARG A1098 16329 19073 16607 -313 958 778 O ATOM 2308 CB ARG A1098 -2.610 -1.912 0.963 1.00133.16 C ANISOU 2308 CB ARG A1098 15582 18653 16361 -323 1143 1011 C ATOM 2309 CG ARG A1098 -3.871 -1.301 0.341 1.00144.01 C ANISOU 2309 CG ARG A1098 16935 20108 17673 -335 1143 1050 C ATOM 2310 CD ARG A1098 -5.148 -1.955 0.841 1.00153.91 C ANISOU 2310 CD ARG A1098 18257 21349 18875 -438 1030 977 C ATOM 2311 NE ARG A1098 -6.340 -1.352 0.243 1.00162.73 N ANISOU 2311 NE ARG A1098 19343 22549 19938 -450 1031 1034 N ATOM 2312 CZ ARG A1098 -7.588 -1.734 0.503 1.00176.58 C ANISOU 2312 CZ ARG A1098 21131 24313 21647 -534 942 1009 C ATOM 2313 NH1 ARG A1098 -7.823 -2.726 1.354 1.00163.66 N ANISOU 2313 NH1 ARG A1098 19561 22606 20017 -612 842 925 N ATOM 2314 NH2 ARG A1098 -8.609 -1.128 -0.087 1.00163.36 N1+ ANISOU 2314 NH2 ARG A1098 19416 22723 19928 -538 952 1079 N1+ ATOM 2315 N ASN A1099 -3.312 -4.367 -1.286 1.00135.22 N ANISOU 2315 N ASN A1099 16116 19027 16233 -178 1019 858 N ATOM 2316 CA ASN A1099 -4.120 -5.542 -1.638 1.00135.52 C ANISOU 2316 CA ASN A1099 16292 19066 16135 -203 897 755 C ATOM 2317 C ASN A1099 -3.240 -6.714 -2.134 1.00140.06 C ANISOU 2317 C ASN A1099 16992 19614 16610 -100 885 682 C ATOM 2318 O ASN A1099 -3.769 -7.780 -2.458 1.00140.12 O ANISOU 2318 O ASN A1099 17134 19605 16502 -112 778 587 O ATOM 2319 CB ASN A1099 -5.173 -5.182 -2.697 1.00137.34 C ANISOU 2319 CB ASN A1099 16532 19399 16253 -183 874 787 C ATOM 2320 CG ASN A1099 -6.367 -4.414 -2.172 1.00161.34 C ANISOU 2320 CG ASN A1099 19486 22457 19358 -301 847 837 C ATOM 2321 OD1 ASN A1099 -6.851 -4.628 -1.052 1.00155.26 O ANISOU 2321 OD1 ASN A1099 18706 21618 18669 -420 783 806 O ATOM 2322 ND2 ASN A1099 -6.908 -3.535 -3.001 1.00153.96 N ANISOU 2322 ND2 ASN A1099 18491 21622 18384 -263 896 921 N ATOM 2323 N ALA A1100 -1.906 -6.518 -2.174 1.00136.75 N ANISOU 2323 N ALA A1100 16532 19185 16241 -1 993 734 N ATOM 2324 CA ALA A1100 -0.935 -7.534 -2.586 1.00137.36 C ANISOU 2324 CA ALA A1100 16716 19237 16237 115 1010 688 C ATOM 2325 C ALA A1100 -0.368 -8.277 -1.371 1.00140.38 C ANISOU 2325 C ALA A1100 17115 19511 16714 41 974 631 C ATOM 2326 O ALA A1100 -0.049 -9.463 -1.475 1.00140.47 O ANISOU 2326 O ALA A1100 17253 19476 16644 84 931 548 O ATOM 2327 CB ALA A1100 0.192 -6.889 -3.378 1.00138.78 C ANISOU 2327 CB ALA A1100 16830 19483 16418 278 1156 805 C ATOM 2328 N TYR A1101 -0.247 -7.577 -0.224 1.00135.74 N ANISOU 2328 N TYR A1101 16404 18879 16292 -65 990 674 N ATOM 2329 CA TYR A1101 0.274 -8.120 1.034 1.00134.78 C ANISOU 2329 CA TYR A1101 16276 18661 16274 -144 959 633 C ATOM 2330 C TYR A1101 -0.868 -8.508 1.999 1.00137.40 C ANISOU 2330 C TYR A1101 16633 18939 16633 -299 837 551 C ATOM 2331 O TYR A1101 -0.597 -8.995 3.101 1.00136.28 O ANISOU 2331 O TYR A1101 16489 18721 16572 -372 800 511 O ATOM 2332 CB TYR A1101 1.216 -7.101 1.708 1.00135.53 C ANISOU 2332 CB TYR A1101 16226 18738 16532 -156 1047 737 C ATOM 2333 CG TYR A1101 2.455 -6.774 0.902 1.00138.21 C ANISOU 2333 CG TYR A1101 16520 19123 16871 -7 1167 841 C ATOM 2334 CD1 TYR A1101 3.604 -7.553 1.005 1.00140.63 C ANISOU 2334 CD1 TYR A1101 16858 19395 17180 66 1202 847 C ATOM 2335 CD2 TYR A1101 2.492 -5.665 0.061 1.00139.41 C ANISOU 2335 CD2 TYR A1101 16586 19355 17029 65 1252 950 C ATOM 2336 CE1 TYR A1101 4.751 -7.252 0.271 1.00142.36 C ANISOU 2336 CE1 TYR A1101 17025 19661 17403 212 1319 965 C ATOM 2337 CE2 TYR A1101 3.632 -5.354 -0.678 1.00141.18 C ANISOU 2337 CE2 TYR A1101 16755 19626 17260 209 1366 1066 C ATOM 2338 CZ TYR A1101 4.761 -6.150 -0.569 1.00149.19 C ANISOU 2338 CZ TYR A1101 17802 20608 18276 284 1400 1077 C ATOM 2339 OH TYR A1101 5.889 -5.846 -1.292 1.00151.21 O ANISOU 2339 OH TYR A1101 17994 20915 18542 435 1519 1213 O ATOM 2340 N ILE A1102 -2.138 -8.322 1.571 1.00133.77 N ANISOU 2340 N ILE A1102 16195 18525 16107 -344 776 537 N ATOM 2341 CA ILE A1102 -3.335 -8.637 2.362 1.00132.84 C ANISOU 2341 CA ILE A1102 16090 18371 16011 -481 663 487 C ATOM 2342 C ILE A1102 -3.542 -10.177 2.432 1.00136.57 C ANISOU 2342 C ILE A1102 16698 18783 16408 -504 551 375 C ATOM 2343 O ILE A1102 -4.246 -10.656 3.322 1.00135.59 O ANISOU 2343 O ILE A1102 16580 18608 16329 -616 460 336 O ATOM 2344 CB ILE A1102 -4.585 -7.893 1.790 1.00136.10 C ANISOU 2344 CB ILE A1102 16470 18862 16380 -513 642 533 C ATOM 2345 CG1 ILE A1102 -5.666 -7.665 2.874 1.00135.72 C ANISOU 2345 CG1 ILE A1102 16370 18785 16411 -650 577 542 C ATOM 2346 CG2 ILE A1102 -5.148 -8.548 0.511 1.00137.96 C ANISOU 2346 CG2 ILE A1102 16818 19151 16451 -459 577 491 C ATOM 2347 CD1 ILE A1102 -6.658 -6.512 2.605 1.00143.25 C ANISOU 2347 CD1 ILE A1102 17241 19812 17373 -677 605 630 C ATOM 2348 N GLN A1103 -2.923 -10.936 1.505 1.00133.73 N ANISOU 2348 N GLN A1103 16448 18428 15936 -392 560 332 N ATOM 2349 CA GLN A1103 -3.016 -12.398 1.442 1.00133.95 C ANISOU 2349 CA GLN A1103 16622 18389 15884 -396 458 223 C ATOM 2350 C GLN A1103 -1.806 -13.071 2.107 1.00136.88 C ANISOU 2350 C GLN A1103 17010 18687 16312 -360 503 197 C ATOM 2351 O GLN A1103 -1.884 -14.249 2.463 1.00136.63 O ANISOU 2351 O GLN A1103 17073 18579 16260 -393 419 113 O ATOM 2352 CB GLN A1103 -3.133 -12.871 -0.019 1.00136.76 C ANISOU 2352 CB GLN A1103 17115 18787 16062 -284 433 183 C ATOM 2353 CG GLN A1103 -4.443 -12.483 -0.702 1.00154.46 C ANISOU 2353 CG GLN A1103 19363 21095 18228 -333 355 194 C ATOM 2354 CD GLN A1103 -4.489 -12.936 -2.140 1.00177.62 C ANISOU 2354 CD GLN A1103 22441 24070 20977 -215 327 151 C ATOM 2355 OE1 GLN A1103 -4.525 -14.134 -2.445 1.00174.65 O ANISOU 2355 OE1 GLN A1103 22226 23630 20503 -196 232 49 O ATOM 2356 NE2 GLN A1103 -4.526 -11.983 -3.059 1.00170.82 N ANISOU 2356 NE2 GLN A1103 21532 23315 20059 -132 406 226 N ATOM 2357 N LYS A1104 -0.698 -12.322 2.273 1.00132.53 N ANISOU 2357 N LYS A1104 16362 18156 15838 -295 631 279 N ATOM 2358 CA LYS A1104 0.553 -12.814 2.849 1.00131.92 C ANISOU 2358 CA LYS A1104 16279 18024 15822 -253 688 283 C ATOM 2359 C LYS A1104 0.639 -12.565 4.369 1.00133.56 C ANISOU 2359 C LYS A1104 16381 18177 16189 -379 673 297 C ATOM 2360 O LYS A1104 1.256 -13.373 5.067 1.00132.96 O ANISOU 2360 O LYS A1104 16329 18038 16153 -390 663 263 O ATOM 2361 CB LYS A1104 1.748 -12.145 2.143 1.00135.09 C ANISOU 2361 CB LYS A1104 16626 18482 16222 -110 830 385 C ATOM 2362 CG LYS A1104 3.079 -12.875 2.312 1.00151.00 C ANISOU 2362 CG LYS A1104 18669 20454 18249 -20 895 397 C ATOM 2363 CD LYS A1104 4.206 -12.161 1.582 1.00162.45 C ANISOU 2363 CD LYS A1104 20049 21970 19706 125 1037 525 C ATOM 2364 CE LYS A1104 5.530 -12.860 1.769 1.00175.25 C ANISOU 2364 CE LYS A1104 21686 23555 21346 217 1108 560 C ATOM 2365 NZ LYS A1104 6.631 -12.148 1.069 1.00186.18 N1+ ANISOU 2365 NZ LYS A1104 22986 25007 22747 362 1248 710 N1+ ATOM 2366 N TYR A1105 0.044 -11.464 4.880 1.00128.55 N ANISOU 2366 N TYR A1105 15637 17567 15638 -464 674 348 N ATOM 2367 CA TYR A1105 0.134 -11.133 6.306 1.00126.93 C ANISOU 2367 CA TYR A1105 15344 17313 15572 -569 662 361 C ATOM 2368 C TYR A1105 -1.236 -10.952 6.981 1.00129.04 C ANISOU 2368 C TYR A1105 15594 17571 15863 -690 574 337 C ATOM 2369 O TYR A1105 -1.404 -11.423 8.107 1.00127.99 O ANISOU 2369 O TYR A1105 15454 17382 15794 -771 520 302 O ATOM 2370 CB TYR A1105 0.969 -9.856 6.511 1.00127.88 C ANISOU 2370 CB TYR A1105 15340 17452 15795 -549 760 464 C ATOM 2371 CG TYR A1105 2.398 -9.983 6.029 1.00130.30 C ANISOU 2371 CG TYR A1105 15635 17766 16107 -436 851 518 C ATOM 2372 CD1 TYR A1105 3.379 -10.552 6.836 1.00132.14 C ANISOU 2372 CD1 TYR A1105 15855 17943 16409 -445 860 518 C ATOM 2373 CD2 TYR A1105 2.773 -9.527 4.769 1.00131.88 C ANISOU 2373 CD2 TYR A1105 15831 18035 16243 -314 932 585 C ATOM 2374 CE1 TYR A1105 4.695 -10.679 6.395 1.00133.60 C ANISOU 2374 CE1 TYR A1105 16020 18139 16602 -336 948 589 C ATOM 2375 CE2 TYR A1105 4.087 -9.646 4.318 1.00133.46 C ANISOU 2375 CE2 TYR A1105 16012 18247 16448 -197 1024 656 C ATOM 2376 CZ TYR A1105 5.045 -10.223 5.135 1.00140.57 C ANISOU 2376 CZ TYR A1105 16897 19090 17421 -209 1032 662 C ATOM 2377 OH TYR A1105 6.341 -10.344 4.697 1.00141.96 O ANISOU 2377 OH TYR A1105 17046 19284 17607 -90 1127 752 O ATOM 2378 N LEU A1106 -2.192 -10.261 6.324 1.00124.91 N ANISOU 2378 N LEU A1106 15057 17109 15293 -697 567 367 N ATOM 2379 CA LEU A1106 -3.519 -9.997 6.892 1.00123.81 C ANISOU 2379 CA LEU A1106 14891 16974 15177 -799 497 371 C ATOM 2380 C LEU A1106 -4.397 -11.264 6.956 1.00126.85 C ANISOU 2380 C LEU A1106 15366 17330 15503 -855 372 297 C ATOM 2381 O LEU A1106 -5.298 -11.324 7.794 1.00125.94 O ANISOU 2381 O LEU A1106 15221 17196 15434 -946 309 303 O ATOM 2382 CB LEU A1106 -4.244 -8.905 6.102 1.00124.07 C ANISOU 2382 CB LEU A1106 14878 17086 15175 -782 533 439 C ATOM 2383 N ARG A 248 -4.139 -12.263 6.088 1.00123.38 N1+ ANISOU 2383 N ARG A 248 15036 16880 14964 -797 336 236 N1+ ATOM 2384 CA ARG A 248 -4.890 -13.524 6.079 1.00123.22 C ANISOU 2384 CA ARG A 248 15112 16815 14890 -851 206 163 C ATOM 2385 C ARG A 248 -4.276 -14.545 7.051 1.00125.51 C ANISOU 2385 C ARG A 248 15429 17018 15240 -876 179 107 C ATOM 2386 O ARG A 248 -4.967 -15.474 7.473 1.00125.15 O ANISOU 2386 O ARG A 248 15426 16923 15200 -950 70 64 O ATOM 2387 CB ARG A 248 -4.964 -14.120 4.665 1.00125.04 C ANISOU 2387 CB ARG A 248 15469 17066 14973 -775 166 114 C ATOM 2388 CG ARG A 248 -6.042 -13.490 3.794 1.00136.89 C ANISOU 2388 CG ARG A 248 16962 18646 16404 -789 131 155 C ATOM 2389 CD ARG A 248 -6.208 -14.231 2.482 1.00148.98 C ANISOU 2389 CD ARG A 248 18639 20188 17781 -724 63 92 C ATOM 2390 NE ARG A 248 -7.273 -13.654 1.660 1.00159.46 N ANISOU 2390 NE ARG A 248 19954 21595 19038 -745 19 137 N ATOM 2391 CZ ARG A 248 -7.643 -14.118 0.470 1.00175.83 C ANISOU 2391 CZ ARG A 248 22147 23693 20967 -701 -56 93 C ATOM 2392 NH1 ARG A 248 -7.037 -15.176 -0.056 1.00164.43 N ANISOU 2392 NH1 ARG A 248 20858 22191 19428 -625 -93 -3 N ATOM 2393 NH2 ARG A 248 -8.621 -13.528 -0.203 1.00162.98 N1+ ANISOU 2393 NH2 ARG A 248 20492 22146 19286 -727 -95 146 N1+ ATOM 2394 N ASN A 249 -2.988 -14.364 7.408 1.00120.78 N ANISOU 2394 N ASN A 249 14796 16402 14693 -819 277 119 N ATOM 2395 CA ASN A 249 -2.254 -15.250 8.314 1.00119.82 C ANISOU 2395 CA ASN A 249 14689 16208 14631 -832 270 80 C ATOM 2396 C ASN A 249 -2.295 -14.758 9.773 1.00121.10 C ANISOU 2396 C ASN A 249 14741 16351 14922 -917 279 116 C ATOM 2397 O ASN A 249 -2.052 -15.561 10.678 1.00120.35 O ANISOU 2397 O ASN A 249 14651 16199 14879 -954 245 83 O ATOM 2398 CB ASN A 249 -0.803 -15.397 7.858 1.00121.47 C ANISOU 2398 CB ASN A 249 14922 16412 14819 -717 369 86 C ATOM 2399 CG ASN A 249 -0.655 -16.179 6.578 1.00147.94 C ANISOU 2399 CG ASN A 249 18413 19765 18034 -617 358 34 C ATOM 2400 OD1 ASN A 249 -0.633 -17.414 6.575 1.00143.59 O ANISOU 2400 OD1 ASN A 249 17967 19149 17440 -611 295 -40 O ATOM 2401 ND2 ASN A 249 -0.552 -15.477 5.460 1.00140.78 N ANISOU 2401 ND2 ASN A 249 17513 18926 17050 -530 417 73 N ATOM 2402 N ARG A 250 -2.602 -13.461 10.006 1.00115.98 N ANISOU 2402 N ARG A 250 14000 15746 14320 -941 323 182 N ATOM 2403 CA ARG A 250 -2.668 -12.894 11.360 1.00114.35 C ANISOU 2403 CA ARG A 250 13707 15520 14221 -1008 331 214 C ATOM 2404 C ARG A 250 -3.945 -13.353 12.096 1.00116.44 C ANISOU 2404 C ARG A 250 13971 15769 14501 -1096 235 203 C ATOM 2405 O ARG A 250 -3.944 -13.396 13.328 1.00115.43 O ANISOU 2405 O ARG A 250 13801 15610 14449 -1143 224 208 O ATOM 2406 CB ARG A 250 -2.571 -11.351 11.354 1.00114.42 C ANISOU 2406 CB ARG A 250 13633 15568 14272 -998 408 287 C ATOM 2407 CG ARG A 250 -3.717 -10.606 10.663 1.00125.31 C ANISOU 2407 CG ARG A 250 15001 17007 15603 -1006 401 327 C ATOM 2408 CD ARG A 250 -3.701 -9.113 10.948 1.00134.97 C ANISOU 2408 CD ARG A 250 16142 18252 16888 -1008 472 398 C ATOM 2409 NE ARG A 250 -2.578 -8.426 10.306 1.00144.32 N ANISOU 2409 NE ARG A 250 17295 19452 18088 -937 561 436 N ATOM 2410 CZ ARG A 250 -2.327 -7.125 10.421 1.00158.69 C ANISOU 2410 CZ ARG A 250 19045 21280 19970 -931 626 500 C ATOM 2411 NH1 ARG A 250 -3.116 -6.351 11.158 1.00145.67 N ANISOU 2411 NH1 ARG A 250 17363 19622 18363 -984 618 526 N ATOM 2412 NH2 ARG A 250 -1.285 -6.587 9.802 1.00145.85 N1+ ANISOU 2412 NH2 ARG A 250 17382 19667 18367 -867 701 547 N1+ ATOM 2413 N ASP A 251 -5.017 -13.697 11.345 1.00112.26 N ANISOU 2413 N ASP A 251 13488 15265 13901 -1115 165 197 N ATOM 2414 CA ASP A 251 -6.295 -14.166 11.892 1.00111.34 C ANISOU 2414 CA ASP A 251 13363 15141 13801 -1196 67 210 C ATOM 2415 C ASP A 251 -6.138 -15.540 12.549 1.00113.43 C ANISOU 2415 C ASP A 251 13668 15335 14094 -1229 -5 155 C ATOM 2416 O ASP A 251 -6.761 -15.791 13.581 1.00112.59 O ANISOU 2416 O ASP A 251 13518 15212 14051 -1290 -51 180 O ATOM 2417 CB ASP A 251 -7.375 -14.217 10.800 1.00113.91 C ANISOU 2417 CB ASP A 251 13726 15509 14043 -1210 1 226 C ATOM 2418 CG ASP A 251 -7.775 -12.859 10.256 1.00123.93 C ANISOU 2418 CG ASP A 251 14941 16854 15292 -1187 67 297 C ATOM 2419 OD1 ASP A 251 -8.224 -12.006 11.055 1.00123.77 O ANISOU 2419 OD1 ASP A 251 14841 16852 15333 -1216 102 362 O ATOM 2420 OD2 ASP A 251 -7.694 -12.668 9.025 1.00130.67 O1- ANISOU 2420 OD2 ASP A 251 15837 17750 16063 -1137 81 291 O1- ATOM 2421 N THR A 252 -5.295 -16.415 11.962 1.00109.03 N ANISOU 2421 N THR A 252 13194 14740 13492 -1180 -7 86 N ATOM 2422 CA THR A 252 -5.001 -17.754 12.488 1.00108.25 C ANISOU 2422 CA THR A 252 13143 14568 13419 -1200 -65 31 C ATOM 2423 C THR A 252 -4.090 -17.638 13.716 1.00109.50 C ANISOU 2423 C THR A 252 13233 14704 13668 -1198 1 41 C ATOM 2424 O THR A 252 -4.176 -18.468 14.622 1.00108.81 O ANISOU 2424 O THR A 252 13136 14570 13635 -1240 -46 26 O ATOM 2425 CB THR A 252 -4.374 -18.651 11.409 1.00117.00 C ANISOU 2425 CB THR A 252 14374 15641 14438 -1132 -76 -42 C ATOM 2426 OG1 THR A 252 -3.211 -18.016 10.876 1.00116.73 O ANISOU 2426 OG1 THR A 252 14339 15637 14375 -1036 41 -34 O ATOM 2427 CG2 THR A 252 -5.348 -18.995 10.286 1.00116.29 C ANISOU 2427 CG2 THR A 252 14372 15559 14254 -1144 -174 -66 C ATOM 2428 N MET A 253 -3.226 -16.599 13.741 1.00104.34 N ANISOU 2428 N MET A 253 12530 14081 13033 -1152 104 72 N ATOM 2429 CA MET A 253 -2.303 -16.306 14.839 1.00102.85 C ANISOU 2429 CA MET A 253 12276 13876 12928 -1154 162 89 C ATOM 2430 C MET A 253 -3.052 -15.752 16.053 1.00104.20 C ANISOU 2430 C MET A 253 12372 14054 13165 -1218 139 129 C ATOM 2431 O MET A 253 -2.793 -16.197 17.171 1.00103.32 O ANISOU 2431 O MET A 253 12232 13912 13113 -1245 126 123 O ATOM 2432 CB MET A 253 -1.215 -15.315 14.390 1.00105.22 C ANISOU 2432 CB MET A 253 12545 14203 13232 -1091 263 123 C ATOM 2433 CG MET A 253 -0.032 -15.969 13.711 1.00109.50 C ANISOU 2433 CG MET A 253 13137 14728 13740 -1013 310 101 C ATOM 2434 SD MET A 253 1.050 -16.841 14.873 1.00113.46 S ANISOU 2434 SD MET A 253 13616 15176 14319 -1022 322 88 S ATOM 2435 CE MET A 253 2.385 -17.269 13.798 1.00110.99 C ANISOU 2435 CE MET A 253 13357 14862 13953 -906 405 95 C ATOM 2436 N MET A 254 -3.980 -14.793 15.834 1.00 99.30 N ANISOU 2436 N MET A 254 11724 13478 12529 -1235 140 175 N ATOM 2437 CA MET A 254 -4.778 -14.162 16.892 1.00 97.95 C ANISOU 2437 CA MET A 254 11493 13318 12405 -1276 131 223 C ATOM 2438 C MET A 254 -5.803 -15.139 17.491 1.00 99.93 C ANISOU 2438 C MET A 254 11743 13555 12671 -1327 42 230 C ATOM 2439 O MET A 254 -6.160 -14.986 18.661 1.00 99.06 O ANISOU 2439 O MET A 254 11587 13442 12611 -1348 37 264 O ATOM 2440 CB MET A 254 -5.490 -12.903 16.379 1.00100.35 C ANISOU 2440 CB MET A 254 11773 13674 12683 -1268 165 279 C ATOM 2441 CG MET A 254 -4.564 -11.709 16.226 1.00103.96 C ANISOU 2441 CG MET A 254 12203 14137 13159 -1229 254 295 C ATOM 2442 SD MET A 254 -5.414 -10.163 15.812 1.00108.25 S ANISOU 2442 SD MET A 254 12712 14732 13687 -1219 302 368 S ATOM 2443 CE MET A 254 -5.819 -10.454 14.090 1.00105.64 C ANISOU 2443 CE MET A 254 12419 14454 13265 -1193 289 367 C ATOM 2444 N SER A 255 -6.266 -16.135 16.700 1.00 95.53 N ANISOU 2444 N SER A 255 11239 12985 12071 -1343 -31 203 N ATOM 2445 CA SER A 255 -7.211 -17.167 17.144 1.00 94.78 C ANISOU 2445 CA SER A 255 11142 12867 12001 -1398 -130 218 C ATOM 2446 C SER A 255 -6.550 -18.079 18.182 1.00 96.49 C ANISOU 2446 C SER A 255 11349 13033 12279 -1404 -138 186 C ATOM 2447 O SER A 255 -7.197 -18.472 19.154 1.00 95.83 O ANISOU 2447 O SER A 255 11218 12943 12249 -1439 -180 227 O ATOM 2448 CB SER A 255 -7.714 -17.985 15.957 1.00 99.17 C ANISOU 2448 CB SER A 255 11773 13409 12496 -1415 -216 187 C ATOM 2449 OG SER A 255 -8.666 -18.959 16.354 1.00108.09 O ANISOU 2449 OG SER A 255 12895 14511 13663 -1479 -324 212 O ATOM 2450 N LEU A 256 -5.255 -18.392 17.975 1.00 91.66 N ANISOU 2450 N LEU A 256 10775 12391 11660 -1363 -90 124 N ATOM 2451 CA LEU A 256 -4.447 -19.216 18.872 1.00 90.54 C ANISOU 2451 CA LEU A 256 10623 12204 11572 -1361 -84 96 C ATOM 2452 C LEU A 256 -3.941 -18.374 20.051 1.00 91.97 C ANISOU 2452 C LEU A 256 10732 12404 11807 -1355 -20 128 C ATOM 2453 O LEU A 256 -3.794 -18.905 21.152 1.00 91.22 O ANISOU 2453 O LEU A 256 10601 12291 11766 -1370 -33 133 O ATOM 2454 CB LEU A 256 -3.269 -19.845 18.101 1.00 91.01 C ANISOU 2454 CB LEU A 256 10753 12229 11597 -1311 -51 34 C ATOM 2455 CG LEU A 256 -2.507 -20.988 18.786 1.00 95.75 C ANISOU 2455 CG LEU A 256 11360 12777 12244 -1307 -54 3 C ATOM 2456 CD1 LEU A 256 -3.349 -22.258 18.856 1.00 96.40 C ANISOU 2456 CD1 LEU A 256 11477 12810 12340 -1351 -156 -14 C ATOM 2457 CD2 LEU A 256 -1.218 -21.287 18.053 1.00 98.69 C ANISOU 2457 CD2 LEU A 256 11791 13128 12578 -1237 11 -36 C ATOM 2458 N LEU A 257 -3.690 -17.064 19.817 1.00 87.03 N ANISOU 2458 N LEU A 257 10088 11813 11165 -1332 42 149 N ATOM 2459 CA LEU A 257 -3.223 -16.109 20.827 1.00 85.71 C ANISOU 2459 CA LEU A 257 9870 11655 11041 -1327 92 174 C ATOM 2460 C LEU A 257 -4.292 -15.898 21.907 1.00 87.51 C ANISOU 2460 C LEU A 257 10058 11898 11293 -1351 61 221 C ATOM 2461 O LEU A 257 -3.958 -15.922 23.091 1.00 86.71 O ANISOU 2461 O LEU A 257 9927 11785 11232 -1351 66 225 O ATOM 2462 CB LEU A 257 -2.849 -14.763 20.170 1.00 85.82 C ANISOU 2462 CB LEU A 257 9881 11693 11034 -1300 155 191 C ATOM 2463 CG LEU A 257 -2.146 -13.719 21.049 1.00 90.30 C ANISOU 2463 CG LEU A 257 10412 12252 11647 -1296 199 209 C ATOM 2464 CD1 LEU A 257 -0.646 -13.974 21.120 1.00 90.58 C ANISOU 2464 CD1 LEU A 257 10439 12262 11717 -1282 230 189 C ATOM 2465 CD2 LEU A 257 -2.379 -12.323 20.514 1.00 92.90 C ANISOU 2465 CD2 LEU A 257 10734 12603 11960 -1282 242 243 C ATOM 2466 N LYS A 258 -5.568 -15.708 21.496 1.00 82.88 N ANISOU 2466 N LYS A 258 9470 11341 10679 -1365 29 264 N ATOM 2467 CA LYS A 258 -6.713 -15.508 22.393 1.00 81.87 C ANISOU 2467 CA LYS A 258 9302 11237 10569 -1374 7 332 C ATOM 2468 C LYS A 258 -6.966 -16.746 23.258 1.00 83.94 C ANISOU 2468 C LYS A 258 9540 11479 10876 -1395 -50 341 C ATOM 2469 O LYS A 258 -7.278 -16.597 24.439 1.00 83.11 O ANISOU 2469 O LYS A 258 9395 11385 10798 -1381 -43 384 O ATOM 2470 CB LYS A 258 -7.983 -15.153 21.599 1.00 84.75 C ANISOU 2470 CB LYS A 258 9664 11642 10897 -1387 -17 392 C ATOM 2471 CG LYS A 258 -8.085 -13.686 21.179 1.00 99.28 C ANISOU 2471 CG LYS A 258 11505 13514 12704 -1358 50 419 C ATOM 2472 CD LYS A 258 -8.587 -12.778 22.312 1.00109.05 C ANISOU 2472 CD LYS A 258 12712 14766 13955 -1331 89 480 C ATOM 2473 CE LYS A 258 -8.751 -11.334 21.896 1.00120.15 C ANISOU 2473 CE LYS A 258 14125 16194 15332 -1302 155 510 C ATOM 2474 NZ LYS A 258 -9.879 -11.142 20.945 1.00129.95 N1+ ANISOU 2474 NZ LYS A 258 15352 17485 16537 -1312 142 576 N1+ ATOM 2475 N THR A 259 -6.805 -17.957 22.674 1.00 79.65 N ANISOU 2475 N THR A 259 9023 10903 10337 -1420 -104 302 N ATOM 2476 CA THR A 259 -6.973 -19.258 23.338 1.00 79.01 C ANISOU 2476 CA THR A 259 8922 10792 10308 -1444 -162 308 C ATOM 2477 C THR A 259 -5.977 -19.379 24.507 1.00 81.16 C ANISOU 2477 C THR A 259 9166 11051 10619 -1421 -119 285 C ATOM 2478 O THR A 259 -6.362 -19.812 25.593 1.00 80.55 O ANISOU 2478 O THR A 259 9040 10979 10585 -1421 -139 328 O ATOM 2479 CB THR A 259 -6.794 -20.395 22.309 1.00 87.30 C ANISOU 2479 CB THR A 259 10032 11796 11344 -1468 -221 252 C ATOM 2480 OG1 THR A 259 -7.680 -20.179 21.209 1.00 87.34 O ANISOU 2480 OG1 THR A 259 10067 11817 11302 -1490 -267 270 O ATOM 2481 CG2 THR A 259 -7.041 -21.781 22.901 1.00 86.20 C ANISOU 2481 CG2 THR A 259 9874 11614 11265 -1499 -290 261 C ATOM 2482 N VAL A 260 -4.715 -18.961 24.277 1.00 76.64 N ANISOU 2482 N VAL A 260 8620 10466 10032 -1398 -62 228 N ATOM 2483 CA VAL A 260 -3.605 -18.966 25.235 1.00 75.64 C ANISOU 2483 CA VAL A 260 8471 10328 9939 -1382 -23 207 C ATOM 2484 C VAL A 260 -3.924 -18.024 26.425 1.00 77.97 C ANISOU 2484 C VAL A 260 8729 10652 10242 -1365 -3 249 C ATOM 2485 O VAL A 260 -3.691 -18.404 27.576 1.00 77.38 O ANISOU 2485 O VAL A 260 8623 10578 10200 -1357 -7 259 O ATOM 2486 CB VAL A 260 -2.287 -18.574 24.507 1.00 79.57 C ANISOU 2486 CB VAL A 260 9001 10812 10420 -1363 31 161 C ATOM 2487 CG1 VAL A 260 -1.227 -18.050 25.466 1.00 79.11 C ANISOU 2487 CG1 VAL A 260 8911 10753 10394 -1353 70 159 C ATOM 2488 CG2 VAL A 260 -1.743 -19.741 23.689 1.00 79.78 C ANISOU 2488 CG2 VAL A 260 9069 10804 10441 -1358 21 119 C ATOM 2489 N VAL A 261 -4.476 -16.823 26.140 1.00 73.49 N ANISOU 2489 N VAL A 261 8175 10110 9640 -1353 20 275 N ATOM 2490 CA VAL A 261 -4.842 -15.804 27.136 1.00 72.63 C ANISOU 2490 CA VAL A 261 8054 10020 9522 -1324 44 312 C ATOM 2491 C VAL A 261 -5.997 -16.333 28.025 1.00 75.33 C ANISOU 2491 C VAL A 261 8358 10388 9876 -1310 13 381 C ATOM 2492 O VAL A 261 -6.014 -16.031 29.218 1.00 74.78 O ANISOU 2492 O VAL A 261 8278 10328 9807 -1275 26 402 O ATOM 2493 CB VAL A 261 -5.191 -14.444 26.460 1.00 76.53 C ANISOU 2493 CB VAL A 261 8576 10528 9976 -1311 81 328 C ATOM 2494 CG1 VAL A 261 -5.667 -13.403 27.474 1.00 76.30 C ANISOU 2494 CG1 VAL A 261 8553 10509 9930 -1271 106 366 C ATOM 2495 CG2 VAL A 261 -3.995 -13.903 25.684 1.00 76.35 C ANISOU 2495 CG2 VAL A 261 8576 10481 9953 -1319 114 277 C ATOM 2496 N ILE A 262 -6.922 -17.142 27.460 1.00 71.19 N ANISOU 2496 N ILE A 262 7815 9873 9362 -1335 -33 421 N ATOM 2497 CA ILE A 262 -8.045 -17.742 28.199 1.00 70.79 C ANISOU 2497 CA ILE A 262 7711 9847 9338 -1326 -69 509 C ATOM 2498 C ILE A 262 -7.482 -18.791 29.190 1.00 73.53 C ANISOU 2498 C ILE A 262 8024 10178 9735 -1324 -87 496 C ATOM 2499 O ILE A 262 -7.930 -18.833 30.339 1.00 73.14 O ANISOU 2499 O ILE A 262 7934 10156 9699 -1283 -81 558 O ATOM 2500 CB ILE A 262 -9.120 -18.332 27.233 1.00 74.34 C ANISOU 2500 CB ILE A 262 8146 10303 9796 -1369 -130 560 C ATOM 2501 CG1 ILE A 262 -9.803 -17.196 26.431 1.00 74.83 C ANISOU 2501 CG1 ILE A 262 8228 10397 9808 -1363 -105 596 C ATOM 2502 CG2 ILE A 262 -10.180 -19.160 27.991 1.00 75.45 C ANISOU 2502 CG2 ILE A 262 8215 10463 9988 -1370 -180 665 C ATOM 2503 CD1 ILE A 262 -10.483 -17.615 25.128 1.00 82.29 C ANISOU 2503 CD1 ILE A 262 9181 11342 10742 -1415 -166 611 C ATOM 2504 N VAL A 263 -6.479 -19.590 28.756 1.00 69.17 N ANISOU 2504 N VAL A 263 7491 9586 9206 -1355 -100 420 N ATOM 2505 CA VAL A 263 -5.803 -20.607 29.579 1.00 68.50 C ANISOU 2505 CA VAL A 263 7375 9483 9169 -1354 -109 404 C ATOM 2506 C VAL A 263 -5.072 -19.896 30.742 1.00 71.15 C ANISOU 2506 C VAL A 263 7705 9837 9493 -1313 -62 392 C ATOM 2507 O VAL A 263 -5.180 -20.332 31.891 1.00 70.62 O ANISOU 2507 O VAL A 263 7593 9789 9450 -1286 -67 429 O ATOM 2508 CB VAL A 263 -4.839 -21.497 28.735 1.00 72.44 C ANISOU 2508 CB VAL A 263 7907 9932 9684 -1387 -119 329 C ATOM 2509 CG1 VAL A 263 -4.018 -22.440 29.614 1.00 72.17 C ANISOU 2509 CG1 VAL A 263 7839 9882 9699 -1380 -114 315 C ATOM 2510 CG2 VAL A 263 -5.602 -22.293 27.681 1.00 72.70 C ANISOU 2510 CG2 VAL A 263 7963 9937 9724 -1426 -182 334 C ATOM 2511 N LEU A 264 -4.372 -18.784 30.435 1.00 67.03 N ANISOU 2511 N LEU A 264 7228 9309 8932 -1308 -24 344 N ATOM 2512 CA LEU A 264 -3.632 -17.974 31.406 1.00 66.44 C ANISOU 2512 CA LEU A 264 7164 9239 8842 -1280 3 325 C ATOM 2513 C LEU A 264 -4.586 -17.216 32.339 1.00 69.86 C ANISOU 2513 C LEU A 264 7600 9704 9240 -1225 12 382 C ATOM 2514 O LEU A 264 -4.303 -17.103 33.532 1.00 69.46 O ANISOU 2514 O LEU A 264 7546 9665 9182 -1189 15 385 O ATOM 2515 CB LEU A 264 -2.711 -16.985 30.678 1.00 66.40 C ANISOU 2515 CB LEU A 264 7204 9209 8817 -1297 31 272 C ATOM 2516 CG LEU A 264 -1.554 -16.439 31.500 1.00 71.00 C ANISOU 2516 CG LEU A 264 7795 9776 9404 -1293 39 240 C ATOM 2517 CD1 LEU A 264 -0.243 -16.993 31.003 1.00 71.13 C ANISOU 2517 CD1 LEU A 264 7798 9771 9459 -1327 47 205 C ATOM 2518 CD2 LEU A 264 -1.530 -14.928 31.467 1.00 73.52 C ANISOU 2518 CD2 LEU A 264 8163 10083 9690 -1282 55 231 C ATOM 2519 N GLY A 265 -5.689 -16.708 31.782 1.00 66.10 N ANISOU 2519 N GLY A 265 7133 9245 8737 -1214 18 430 N ATOM 2520 CA GLY A 265 -6.718 -15.966 32.504 1.00 65.90 C ANISOU 2520 CA GLY A 265 7114 9253 8672 -1150 38 501 C ATOM 2521 C GLY A 265 -7.388 -16.796 33.577 1.00 69.47 C ANISOU 2521 C GLY A 265 7510 9741 9146 -1107 24 578 C ATOM 2522 O GLY A 265 -7.502 -16.349 34.720 1.00 69.04 O ANISOU 2522 O GLY A 265 7470 9707 9057 -1037 46 603 O ATOM 2523 N ALA A 266 -7.795 -18.032 33.217 1.00 66.00 N ANISOU 2523 N ALA A 266 7009 9305 8763 -1146 -16 616 N ATOM 2524 CA ALA A 266 -8.424 -18.997 34.122 1.00 65.92 C ANISOU 2524 CA ALA A 266 6925 9325 8794 -1115 -36 702 C ATOM 2525 C ALA A 266 -7.447 -19.441 35.216 1.00 69.57 C ANISOU 2525 C ALA A 266 7377 9788 9270 -1091 -29 661 C ATOM 2526 O ALA A 266 -7.875 -19.698 36.342 1.00 69.44 O ANISOU 2526 O ALA A 266 7319 9810 9256 -1026 -20 733 O ATOM 2527 CB ALA A 266 -8.918 -20.204 33.340 1.00 66.78 C ANISOU 2527 CB ALA A 266 6983 9419 8972 -1180 -94 737 C ATOM 2528 N PHE A 267 -6.137 -19.507 34.882 1.00 65.60 N ANISOU 2528 N PHE A 267 6906 9245 8773 -1138 -30 557 N ATOM 2529 CA PHE A 267 -5.052 -19.889 35.789 1.00 65.22 C ANISOU 2529 CA PHE A 267 6847 9195 8739 -1129 -26 515 C ATOM 2530 C PHE A 267 -4.858 -18.830 36.881 1.00 68.94 C ANISOU 2530 C PHE A 267 7363 9687 9145 -1063 -3 508 C ATOM 2531 O PHE A 267 -4.665 -19.195 38.038 1.00 68.64 O ANISOU 2531 O PHE A 267 7298 9677 9105 -1017 -3 529 O ATOM 2532 CB PHE A 267 -3.741 -20.098 35.004 1.00 66.82 C ANISOU 2532 CB PHE A 267 7074 9353 8964 -1194 -28 424 C ATOM 2533 CG PHE A 267 -2.643 -20.827 35.745 1.00 68.32 C ANISOU 2533 CG PHE A 267 7230 9541 9187 -1200 -28 399 C ATOM 2534 CD1 PHE A 267 -2.523 -22.209 35.660 1.00 71.42 C ANISOU 2534 CD1 PHE A 267 7568 9925 9644 -1222 -42 414 C ATOM 2535 CD2 PHE A 267 -1.700 -20.129 36.490 1.00 70.50 C ANISOU 2535 CD2 PHE A 267 7532 9821 9434 -1186 -20 361 C ATOM 2536 CE1 PHE A 267 -1.501 -22.884 36.335 1.00 72.37 C ANISOU 2536 CE1 PHE A 267 7652 10048 9796 -1224 -34 399 C ATOM 2537 CE2 PHE A 267 -0.678 -20.805 37.166 1.00 73.33 C ANISOU 2537 CE2 PHE A 267 7853 10185 9825 -1195 -22 348 C ATOM 2538 CZ PHE A 267 -0.584 -22.176 37.082 1.00 71.43 C ANISOU 2538 CZ PHE A 267 7551 9944 9646 -1211 -23 369 C ATOM 2539 N ILE A 268 -4.919 -17.529 36.519 1.00 65.29 N ANISOU 2539 N ILE A 268 6974 9208 8627 -1054 15 479 N ATOM 2540 CA ILE A 268 -4.744 -16.410 37.454 1.00 65.22 C ANISOU 2540 CA ILE A 268 7033 9200 8548 -992 28 460 C ATOM 2541 C ILE A 268 -5.957 -16.330 38.409 1.00 69.40 C ANISOU 2541 C ILE A 268 7555 9780 9036 -888 50 556 C ATOM 2542 O ILE A 268 -5.760 -16.334 39.622 1.00 69.18 O ANISOU 2542 O ILE A 268 7540 9774 8973 -823 50 562 O ATOM 2543 CB ILE A 268 -4.501 -15.062 36.699 1.00 68.26 C ANISOU 2543 CB ILE A 268 7497 9541 8896 -1014 40 407 C ATOM 2544 CG1 ILE A 268 -3.143 -15.091 35.948 1.00 68.49 C ANISOU 2544 CG1 ILE A 268 7529 9526 8967 -1100 23 328 C ATOM 2545 CG2 ILE A 268 -4.569 -13.853 37.658 1.00 69.21 C ANISOU 2545 CG2 ILE A 268 7706 9651 8939 -941 49 395 C ATOM 2546 CD1 ILE A 268 -2.925 -13.983 34.889 1.00 75.93 C ANISOU 2546 CD1 ILE A 268 8523 10430 9898 -1134 37 292 C ATOM 2547 N ILE A 269 -7.191 -16.294 37.860 1.00 66.06 N ANISOU 2547 N ILE A 269 7106 9379 8613 -870 68 639 N ATOM 2548 CA ILE A 269 -8.468 -16.169 38.584 1.00 66.28 C ANISOU 2548 CA ILE A 269 7116 9460 8606 -766 98 759 C ATOM 2549 C ILE A 269 -8.628 -17.267 39.683 1.00 70.15 C ANISOU 2549 C ILE A 269 7528 9999 9128 -714 91 829 C ATOM 2550 O ILE A 269 -9.199 -16.967 40.735 1.00 70.14 O ANISOU 2550 O ILE A 269 7539 10040 9070 -599 123 900 O ATOM 2551 CB ILE A 269 -9.656 -16.192 37.562 1.00 69.44 C ANISOU 2551 CB ILE A 269 7475 9877 9032 -788 105 848 C ATOM 2552 CG1 ILE A 269 -9.676 -14.879 36.731 1.00 69.82 C ANISOU 2552 CG1 ILE A 269 7606 9893 9029 -801 131 802 C ATOM 2553 CG2 ILE A 269 -11.027 -16.417 38.239 1.00 70.59 C ANISOU 2553 CG2 ILE A 269 7562 10088 9172 -691 131 1010 C ATOM 2554 CD1 ILE A 269 -10.526 -14.897 35.433 1.00 76.88 C ANISOU 2554 CD1 ILE A 269 8463 10795 9951 -854 126 857 C ATOM 2555 N CYS A 270 -8.109 -18.493 39.467 1.00 66.39 N ANISOU 2555 N CYS A 270 6977 9514 8734 -787 54 811 N ATOM 2556 CA CYS A 270 -8.273 -19.579 40.437 1.00 66.49 C ANISOU 2556 CA CYS A 270 6903 9571 8790 -743 49 886 C ATOM 2557 C CYS A 270 -7.070 -19.717 41.401 1.00 70.26 C ANISOU 2557 C CYS A 270 7400 10048 9246 -728 44 809 C ATOM 2558 O CYS A 270 -7.284 -20.113 42.549 1.00 70.23 O ANISOU 2558 O CYS A 270 7357 10096 9231 -643 58 875 O ATOM 2559 CB CYS A 270 -8.537 -20.899 39.721 1.00 66.79 C ANISOU 2559 CB CYS A 270 6845 9597 8936 -824 10 927 C ATOM 2560 SG CYS A 270 -7.079 -21.620 38.927 1.00 70.29 S ANISOU 2560 SG CYS A 270 7296 9974 9435 -944 -24 792 S ATOM 2561 N TRP A 271 -5.826 -19.459 40.939 1.00 66.24 N ANISOU 2561 N TRP A 271 6942 9490 8738 -807 25 687 N ATOM 2562 CA TRP A 271 -4.626 -19.628 41.772 1.00 65.90 C ANISOU 2562 CA TRP A 271 6907 9447 8685 -808 12 624 C ATOM 2563 C TRP A 271 -4.329 -18.425 42.685 1.00 70.29 C ANISOU 2563 C TRP A 271 7565 10005 9137 -738 14 581 C ATOM 2564 O TRP A 271 -3.769 -18.637 43.763 1.00 70.16 O ANISOU 2564 O TRP A 271 7546 10014 9096 -697 2 572 O ATOM 2565 CB TRP A 271 -3.387 -19.914 40.917 1.00 64.10 C ANISOU 2565 CB TRP A 271 6678 9167 8509 -919 -10 533 C ATOM 2566 CG TRP A 271 -3.252 -21.351 40.510 1.00 64.74 C ANISOU 2566 CG TRP A 271 6667 9246 8683 -971 -18 558 C ATOM 2567 CD1 TRP A 271 -3.544 -21.892 39.293 1.00 67.44 C ANISOU 2567 CD1 TRP A 271 6989 9554 9081 -1035 -26 558 C ATOM 2568 CD2 TRP A 271 -2.796 -22.434 41.332 1.00 64.58 C ANISOU 2568 CD2 TRP A 271 6572 9255 8710 -958 -20 586 C ATOM 2569 NE1 TRP A 271 -3.290 -23.243 39.301 1.00 66.81 N ANISOU 2569 NE1 TRP A 271 6835 9470 9079 -1064 -36 579 N ATOM 2570 CE2 TRP A 271 -2.829 -23.604 40.540 1.00 68.29 C ANISOU 2570 CE2 TRP A 271 6981 9698 9267 -1018 -28 600 C ATOM 2571 CE3 TRP A 271 -2.355 -22.530 42.663 1.00 66.03 C ANISOU 2571 CE3 TRP A 271 6738 9485 8866 -900 -17 600 C ATOM 2572 CZ2 TRP A 271 -2.438 -24.854 41.034 1.00 67.62 C ANISOU 2572 CZ2 TRP A 271 6815 9626 9251 -1022 -27 632 C ATOM 2573 CZ3 TRP A 271 -1.962 -23.767 43.149 1.00 67.48 C ANISOU 2573 CZ3 TRP A 271 6830 9692 9116 -904 -14 635 C ATOM 2574 CH2 TRP A 271 -2.010 -24.912 42.342 1.00 67.93 C ANISOU 2574 CH2 TRP A 271 6824 9718 9268 -964 -16 653 C ATOM 2575 N THR A 272 -4.671 -17.185 42.262 1.00 67.01 N ANISOU 2575 N THR A 272 7242 9556 8661 -724 24 554 N ATOM 2576 CA THR A 272 -4.424 -15.957 43.037 1.00 67.35 C ANISOU 2576 CA THR A 272 7404 9581 8604 -659 18 505 C ATOM 2577 C THR A 272 -5.140 -16.011 44.423 1.00 71.90 C ANISOU 2577 C THR A 272 7994 10219 9105 -514 42 579 C ATOM 2578 O THR A 272 -4.446 -15.742 45.405 1.00 71.86 O ANISOU 2578 O THR A 272 8047 10214 9042 -477 14 529 O ATOM 2579 CB THR A 272 -4.826 -14.694 42.244 1.00 75.51 C ANISOU 2579 CB THR A 272 8527 10566 9597 -665 34 479 C ATOM 2580 OG1 THR A 272 -4.159 -14.707 40.981 1.00 75.14 O ANISOU 2580 OG1 THR A 272 8460 10474 9618 -786 17 422 O ATOM 2581 CG2 THR A 272 -4.492 -13.395 42.976 1.00 74.54 C ANISOU 2581 CG2 THR A 272 8543 10403 9376 -607 18 416 C ATOM 2582 N PRO A 273 -6.450 -16.381 44.573 1.00 68.67 N ANISOU 2582 N PRO A 273 7529 9867 8696 -427 89 704 N ATOM 2583 CA PRO A 273 -7.055 -16.397 45.923 1.00 69.19 C ANISOU 2583 CA PRO A 273 7608 9996 8684 -272 119 785 C ATOM 2584 C PRO A 273 -6.360 -17.357 46.897 1.00 73.14 C ANISOU 2584 C PRO A 273 8045 10539 9205 -259 96 784 C ATOM 2585 O PRO A 273 -6.311 -17.069 48.092 1.00 73.33 O ANISOU 2585 O PRO A 273 8129 10597 9136 -144 102 790 O ATOM 2586 CB PRO A 273 -8.500 -16.838 45.666 1.00 71.00 C ANISOU 2586 CB PRO A 273 7749 10279 8949 -212 169 941 C ATOM 2587 CG PRO A 273 -8.482 -17.488 44.334 1.00 74.73 C ANISOU 2587 CG PRO A 273 8135 10721 9538 -355 145 936 C ATOM 2588 CD PRO A 273 -7.456 -16.740 43.552 1.00 69.88 C ANISOU 2588 CD PRO A 273 7608 10030 8915 -460 113 789 C ATOM 2589 N GLY A 274 -5.817 -18.458 46.377 1.00 69.12 N ANISOU 2589 N GLY A 274 7426 10028 8809 -369 73 776 N ATOM 2590 CA GLY A 274 -5.086 -19.444 47.163 1.00 68.92 C ANISOU 2590 CA GLY A 274 7327 10040 8819 -372 55 778 C ATOM 2591 C GLY A 274 -3.707 -18.968 47.577 1.00 72.76 C ANISOU 2591 C GLY A 274 7890 10494 9261 -417 7 656 C ATOM 2592 O GLY A 274 -3.237 -19.306 48.667 1.00 72.59 O ANISOU 2592 O GLY A 274 7857 10516 9206 -364 -6 660 O ATOM 2593 N LEU A 275 -3.045 -18.179 46.704 1.00 69.07 N ANISOU 2593 N LEU A 275 7496 9951 8796 -516 -24 556 N ATOM 2594 CA LEU A 275 -1.715 -17.616 46.955 1.00 69.04 C ANISOU 2594 CA LEU A 275 7564 9904 8764 -577 -81 450 C ATOM 2595 C LEU A 275 -1.808 -16.388 47.869 1.00 73.82 C ANISOU 2595 C LEU A 275 8317 10494 9236 -483 -105 408 C ATOM 2596 O LEU A 275 -0.878 -16.141 48.639 1.00 73.82 O ANISOU 2596 O LEU A 275 8368 10486 9193 -490 -161 349 O ATOM 2597 CB LEU A 275 -1.003 -17.259 45.641 1.00 68.62 C ANISOU 2597 CB LEU A 275 7521 9777 8774 -713 -102 380 C ATOM 2598 CG LEU A 275 -0.487 -18.440 44.809 1.00 72.71 C ANISOU 2598 CG LEU A 275 7920 10296 9411 -811 -93 393 C ATOM 2599 CD1 LEU A 275 -0.305 -18.047 43.366 1.00 72.49 C ANISOU 2599 CD1 LEU A 275 7908 10206 9428 -903 -90 352 C ATOM 2600 CD2 LEU A 275 0.814 -19.004 45.372 1.00 75.33 C ANISOU 2600 CD2 LEU A 275 8208 10640 9773 -858 -127 367 C ATOM 2601 N VAL A 276 -2.932 -15.635 47.799 1.00 70.83 N ANISOU 2601 N VAL A 276 8010 10111 8791 -391 -64 444 N ATOM 2602 CA VAL A 276 -3.203 -14.471 48.656 1.00 71.65 C ANISOU 2602 CA VAL A 276 8272 10195 8756 -276 -74 412 C ATOM 2603 C VAL A 276 -3.494 -15.005 50.078 1.00 76.47 C ANISOU 2603 C VAL A 276 8872 10889 9293 -135 -59 473 C ATOM 2604 O VAL A 276 -3.084 -14.385 51.062 1.00 76.77 O ANISOU 2604 O VAL A 276 9031 10915 9222 -67 -102 416 O ATOM 2605 CB VAL A 276 -4.343 -13.572 48.083 1.00 75.62 C ANISOU 2605 CB VAL A 276 8845 10671 9215 -214 -19 447 C ATOM 2606 CG1 VAL A 276 -4.853 -12.559 49.109 1.00 76.48 C ANISOU 2606 CG1 VAL A 276 9114 10773 9170 -53 -7 443 C ATOM 2607 CG2 VAL A 276 -3.886 -12.851 46.817 1.00 74.97 C ANISOU 2607 CG2 VAL A 276 8797 10504 9186 -345 -42 372 C ATOM 2608 N LEU A 277 -4.137 -16.194 50.163 1.00 73.06 N ANISOU 2608 N LEU A 277 8294 10538 8928 -98 -6 590 N ATOM 2609 CA LEU A 277 -4.459 -16.908 51.404 1.00 73.59 C ANISOU 2609 CA LEU A 277 8311 10698 8953 34 20 675 C ATOM 2610 C LEU A 277 -3.171 -17.276 52.162 1.00 78.16 C ANISOU 2610 C LEU A 277 8886 11289 9524 -11 -45 603 C ATOM 2611 O LEU A 277 -3.157 -17.230 53.394 1.00 78.44 O ANISOU 2611 O LEU A 277 8970 11375 9458 112 -51 617 O ATOM 2612 CB LEU A 277 -5.280 -18.173 51.079 1.00 73.14 C ANISOU 2612 CB LEU A 277 8073 10707 9009 39 76 815 C ATOM 2613 CG LEU A 277 -6.031 -18.856 52.226 1.00 78.40 C ANISOU 2613 CG LEU A 277 8668 11477 9643 202 127 952 C ATOM 2614 CD1 LEU A 277 -7.312 -18.113 52.565 1.00 79.24 C ANISOU 2614 CD1 LEU A 277 8846 11612 9650 369 191 1046 C ATOM 2615 CD2 LEU A 277 -6.392 -20.279 51.854 1.00 80.37 C ANISOU 2615 CD2 LEU A 277 8723 11771 10043 151 151 1065 C ATOM 2616 N LEU A 278 -2.092 -17.616 51.417 1.00 74.63 N ANISOU 2616 N LEU A 278 8383 10795 9177 -179 -92 533 N ATOM 2617 CA LEU A 278 -0.766 -17.946 51.954 1.00 74.83 C ANISOU 2617 CA LEU A 278 8391 10826 9214 -248 -157 473 C ATOM 2618 C LEU A 278 -0.115 -16.707 52.572 1.00 80.39 C ANISOU 2618 C LEU A 278 9270 11477 9799 -234 -236 367 C ATOM 2619 O LEU A 278 0.562 -16.820 53.596 1.00 80.56 O ANISOU 2619 O LEU A 278 9315 11531 9763 -205 -287 343 O ATOM 2620 CB LEU A 278 0.147 -18.534 50.860 1.00 74.01 C ANISOU 2620 CB LEU A 278 8190 10682 9250 -422 -175 441 C ATOM 2621 CG LEU A 278 -0.167 -19.953 50.374 1.00 77.97 C ANISOU 2621 CG LEU A 278 8522 11228 9876 -453 -119 529 C ATOM 2622 CD1 LEU A 278 0.416 -20.197 49.001 1.00 77.36 C ANISOU 2622 CD1 LEU A 278 8398 11087 9908 -602 -124 489 C ATOM 2623 CD2 LEU A 278 0.341 -21.006 51.350 1.00 80.62 C ANISOU 2623 CD2 LEU A 278 8759 11639 10234 -423 -119 576 C ATOM 2624 N LEU A 279 -0.330 -15.527 51.950 1.00 77.78 N ANISOU 2624 N LEU A 279 9063 11061 9430 -255 -251 305 N ATOM 2625 CA LEU A 279 0.184 -14.239 52.423 1.00 78.85 C ANISOU 2625 CA LEU A 279 9381 11122 9457 -246 -333 202 C ATOM 2626 C LEU A 279 -0.556 -13.800 53.688 1.00 84.63 C ANISOU 2626 C LEU A 279 10238 11892 10027 -51 -320 219 C ATOM 2627 O LEU A 279 0.081 -13.333 54.631 1.00 85.12 O ANISOU 2627 O LEU A 279 10414 11937 9991 -21 -401 150 O ATOM 2628 CB LEU A 279 0.061 -13.155 51.334 1.00 78.73 C ANISOU 2628 CB LEU A 279 9450 11005 9461 -317 -340 146 C ATOM 2629 CG LEU A 279 0.922 -13.309 50.076 1.00 82.62 C ANISOU 2629 CG LEU A 279 9855 11446 10093 -500 -364 116 C ATOM 2630 CD1 LEU A 279 0.409 -12.422 48.962 1.00 82.48 C ANISOU 2630 CD1 LEU A 279 9890 11356 10092 -532 -335 98 C ATOM 2631 CD2 LEU A 279 2.390 -13.001 50.356 1.00 85.66 C ANISOU 2631 CD2 LEU A 279 10272 11782 10494 -611 -475 40 C ATOM 2632 N LEU A 280 -1.895 -13.980 53.714 1.00 81.86 N ANISOU 2632 N LEU A 280 9863 11594 9645 84 -219 319 N ATOM 2633 CA LEU A 280 -2.764 -13.630 54.844 1.00 83.11 C ANISOU 2633 CA LEU A 280 10129 11801 9650 298 -179 365 C ATOM 2634 C LEU A 280 -2.562 -14.589 56.037 1.00 88.45 C ANISOU 2634 C LEU A 280 10731 12583 10291 387 -178 421 C ATOM 2635 O LEU A 280 -3.007 -14.287 57.146 1.00 89.07 O ANISOU 2635 O LEU A 280 10915 12705 10223 567 -163 443 O ATOM 2636 CB LEU A 280 -4.248 -13.635 54.414 1.00 82.95 C ANISOU 2636 CB LEU A 280 10070 11815 9631 407 -64 487 C ATOM 2637 CG LEU A 280 -4.706 -12.558 53.415 1.00 87.50 C ANISOU 2637 CG LEU A 280 10739 12302 10207 371 -46 451 C ATOM 2638 CD1 LEU A 280 -6.029 -12.933 52.784 1.00 87.17 C ANISOU 2638 CD1 LEU A 280 10590 12311 10219 427 61 594 C ATOM 2639 CD2 LEU A 280 -4.815 -11.186 54.068 1.00 91.22 C ANISOU 2639 CD2 LEU A 280 11447 12704 10508 489 -71 375 C ATOM 2640 N ASP A 281 -1.891 -15.733 55.807 1.00 85.07 N ANISOU 2640 N ASP A 281 10129 12199 9994 269 -189 447 N ATOM 2641 CA ASP A 281 -1.611 -16.744 56.824 1.00 85.51 C ANISOU 2641 CA ASP A 281 10088 12357 10043 332 -185 507 C ATOM 2642 C ASP A 281 -0.468 -16.309 57.754 1.00 91.01 C ANISOU 2642 C ASP A 281 10899 13039 10643 318 -295 401 C ATOM 2643 O ASP A 281 -0.534 -16.583 58.953 1.00 91.44 O ANISOU 2643 O ASP A 281 10974 13173 10598 454 -293 435 O ATOM 2644 CB ASP A 281 -1.261 -18.085 56.155 1.00 86.27 C ANISOU 2644 CB ASP A 281 9966 12492 10322 202 -159 568 C ATOM 2645 CG ASP A 281 -1.134 -19.253 57.113 1.00 96.96 C ANISOU 2645 CG ASP A 281 11192 13958 11692 272 -134 656 C ATOM 2646 OD1 ASP A 281 -2.119 -19.547 57.824 1.00 98.08 O1- ANISOU 2646 OD1 ASP A 281 11306 14181 11777 444 -65 766 O1- ATOM 2647 OD2 ASP A 281 -0.080 -19.919 57.095 1.00102.56 O ANISOU 2647 OD2 ASP A 281 11811 14676 12480 157 -175 630 O ATOM 2648 N CYS A 282 0.576 -15.650 57.206 1.00 88.04 N ANISOU 2648 N CYS A 282 10591 12562 10298 155 -392 283 N ATOM 2649 CA CYS A 282 1.743 -15.217 57.979 1.00 89.01 C ANISOU 2649 CA CYS A 282 10814 12657 10349 110 -517 186 C ATOM 2650 C CYS A 282 1.772 -13.682 58.190 1.00 95.32 C ANISOU 2650 C CYS A 282 11859 13345 11012 142 -600 71 C ATOM 2651 O CYS A 282 2.385 -13.236 59.162 1.00 96.06 O ANISOU 2651 O CYS A 282 12080 13425 10992 174 -702 1 O ATOM 2652 CB CYS A 282 3.034 -15.693 57.315 1.00 88.42 C ANISOU 2652 CB CYS A 282 10618 12555 10421 -102 -579 158 C ATOM 2653 SG CYS A 282 3.233 -17.497 57.264 1.00 91.12 S ANISOU 2653 SG CYS A 282 10698 13017 10907 -137 -500 277 S ATOM 2654 N CYS A 283 1.138 -12.882 57.302 1.00 92.73 N ANISOU 2654 N CYS A 283 11602 12935 10696 133 -563 51 N ATOM 2655 CA CYS A 283 1.177 -11.415 57.401 1.00 94.19 C ANISOU 2655 CA CYS A 283 12019 13000 10769 154 -639 -58 C ATOM 2656 C CYS A 283 -0.154 -10.815 57.925 1.00100.14 C ANISOU 2656 C CYS A 283 12917 13764 11366 380 -557 -26 C ATOM 2657 O CYS A 283 -0.239 -9.591 58.074 1.00100.63 O ANISOU 2657 O CYS A 283 13190 13724 11320 424 -608 -113 O ATOM 2658 CB CYS A 283 1.558 -10.800 56.057 1.00 93.85 C ANISOU 2658 CB CYS A 283 11967 12847 10844 -21 -666 -108 C ATOM 2659 SG CYS A 283 3.165 -11.346 55.420 1.00 97.06 S ANISOU 2659 SG CYS A 283 12222 13232 11423 -270 -759 -135 S ATOM 2660 N CYS A 284 -1.161 -11.657 58.234 1.00 97.48 N ANISOU 2660 N CYS A 284 12473 13547 11020 526 -433 105 N ATOM 2661 CA CYS A 284 -2.456 -11.206 58.757 1.00 98.60 C ANISOU 2661 CA CYS A 284 12726 13717 11019 757 -338 169 C ATOM 2662 C CYS A 284 -2.900 -12.141 59.927 1.00103.26 C ANISOU 2662 C CYS A 284 13245 14452 11536 938 -277 279 C ATOM 2663 O CYS A 284 -3.828 -12.943 59.773 1.00102.20 O ANISOU 2663 O CYS A 284 12957 14413 11463 1016 -159 428 O ATOM 2664 CB CYS A 284 -3.492 -11.138 57.631 1.00 98.23 C ANISOU 2664 CB CYS A 284 12601 13661 11059 751 -227 254 C ATOM 2665 SG CYS A 284 -5.177 -10.661 58.128 1.00103.15 S ANISOU 2665 SG CYS A 284 13324 14333 11535 1033 -88 376 S ATOM 2666 N PRO A 285 -2.275 -12.016 61.127 1.00101.28 N ANISOU 2666 N PRO A 285 13111 14220 11153 1012 -360 215 N ATOM 2667 CA PRO A 285 -2.684 -12.865 62.256 1.00101.71 C ANISOU 2667 CA PRO A 285 13098 14416 11130 1195 -299 324 C ATOM 2668 C PRO A 285 -3.750 -12.173 63.124 1.00107.09 C ANISOU 2668 C PRO A 285 13966 15120 11603 1476 -228 366 C ATOM 2669 O PRO A 285 -3.507 -11.075 63.630 1.00108.02 O ANISOU 2669 O PRO A 285 14335 15149 11559 1541 -306 244 O ATOM 2670 CB PRO A 285 -1.367 -13.083 63.021 1.00104.04 C ANISOU 2670 CB PRO A 285 13420 14719 11393 1115 -433 229 C ATOM 2671 CG PRO A 285 -0.416 -11.993 62.526 1.00108.77 C ANISOU 2671 CG PRO A 285 14176 15161 11993 941 -576 60 C ATOM 2672 CD PRO A 285 -1.148 -11.146 61.517 1.00103.88 C ANISOU 2672 CD PRO A 285 13626 14444 11400 928 -521 49 C ATOM 2673 N GLN A 286 -4.948 -12.802 63.251 1.00103.43 N ANISOU 2673 N GLN A 286 13381 14769 11151 1642 -79 548 N ATOM 2674 CA GLN A 286 -6.129 -12.379 64.038 1.00104.47 C ANISOU 2674 CA GLN A 286 13635 14954 11105 1935 27 647 C ATOM 2675 C GLN A 286 -7.055 -11.365 63.295 1.00108.06 C ANISOU 2675 C GLN A 286 14204 15323 11531 1987 96 661 C ATOM 2676 O GLN A 286 -8.081 -10.980 63.867 1.00108.66 O ANISOU 2676 O GLN A 286 14379 15441 11464 2236 197 759 O ATOM 2677 CB GLN A 286 -5.739 -11.788 65.410 1.00107.70 C ANISOU 2677 CB GLN A 286 14284 15362 11277 2109 -43 554 C ATOM 2678 N CYS A 287 -6.744 -10.976 62.038 1.00103.30 N ANISOU 2678 N CYS A 287 13575 14612 11062 1768 54 583 N ATOM 2679 CA CYS A 287 -7.611 -10.047 61.295 1.00103.03 C ANISOU 2679 CA CYS A 287 13634 14504 11010 1810 123 604 C ATOM 2680 C CYS A 287 -8.819 -10.803 60.700 1.00105.92 C ANISOU 2680 C CYS A 287 13781 14969 11495 1857 268 817 C ATOM 2681 O CYS A 287 -9.932 -10.272 60.732 1.00106.11 O ANISOU 2681 O CYS A 287 13874 15006 11438 2033 374 921 O ATOM 2682 CB CYS A 287 -6.857 -9.264 60.218 1.00102.58 C ANISOU 2682 CB CYS A 287 13642 14296 11038 1577 27 447 C ATOM 2683 SG CYS A 287 -5.136 -9.773 59.959 1.00105.54 S ANISOU 2683 SG CYS A 287 13928 14627 11544 1293 -137 302 S ATOM 2684 N ASP A 288 -8.602 -12.033 60.172 1.00101.05 N ANISOU 2684 N ASP A 288 12906 14417 11069 1704 268 887 N ATOM 2685 CA ASP A 288 -9.654 -12.885 59.597 1.00 99.98 C ANISOU 2685 CA ASP A 288 12548 14370 11070 1720 378 1088 C ATOM 2686 C ASP A 288 -9.235 -14.368 59.611 1.00102.29 C ANISOU 2686 C ASP A 288 12597 14749 11519 1612 362 1154 C ATOM 2687 O ASP A 288 -8.052 -14.682 59.455 1.00101.14 O ANISOU 2687 O ASP A 288 12424 14564 11439 1436 263 1025 O ATOM 2688 CB ASP A 288 -10.011 -12.447 58.163 1.00100.93 C ANISOU 2688 CB ASP A 288 12635 14410 11304 1571 393 1080 C ATOM 2689 CG ASP A 288 -11.311 -13.032 57.642 1.00110.63 C ANISOU 2689 CG ASP A 288 13685 15718 12631 1626 506 1297 C ATOM 2690 OD1 ASP A 288 -12.381 -12.694 58.199 1.00112.13 O ANISOU 2690 OD1 ASP A 288 13926 15965 12715 1851 607 1437 O ATOM 2691 OD2 ASP A 288 -11.264 -13.791 56.653 1.00115.17 O1- ANISOU 2691 OD2 ASP A 288 14076 16294 13389 1444 490 1329 O1- ATOM 2692 N VAL A 289 -10.221 -15.269 59.794 1.00 98.38 N ANISOU 2692 N VAL A 289 11924 14369 11089 1721 460 1365 N ATOM 2693 CA VAL A 289 -10.030 -16.726 59.852 1.00 97.21 C ANISOU 2693 CA VAL A 289 11536 14306 11095 1647 460 1460 C ATOM 2694 C VAL A 289 -9.869 -17.284 58.424 1.00 98.91 C ANISOU 2694 C VAL A 289 11595 14465 11521 1398 429 1446 C ATOM 2695 O VAL A 289 -10.549 -16.822 57.504 1.00 98.08 O ANISOU 2695 O VAL A 289 11496 14313 11457 1359 460 1479 O ATOM 2696 CB VAL A 289 -11.192 -17.442 60.607 1.00101.77 C ANISOU 2696 CB VAL A 289 11981 15021 11667 1865 573 1707 C ATOM 2697 CG1 VAL A 289 -10.808 -18.871 60.991 1.00101.12 C ANISOU 2697 CG1 VAL A 289 11685 15025 11710 1818 562 1784 C ATOM 2698 CG2 VAL A 289 -11.620 -16.663 61.848 1.00103.21 C ANISOU 2698 CG2 VAL A 289 12348 15251 11617 2148 628 1739 C ATOM 2699 N LEU A 290 -8.986 -18.290 58.253 1.00 94.14 N ANISOU 2699 N LEU A 290 10854 13869 11046 1240 371 1403 N ATOM 2700 CA LEU A 290 -8.724 -18.944 56.968 1.00 92.36 C ANISOU 2700 CA LEU A 290 10487 13591 11012 1014 339 1384 C ATOM 2701 C LEU A 290 -9.630 -20.189 56.822 1.00 94.96 C ANISOU 2701 C LEU A 290 10592 14002 11488 1036 399 1589 C ATOM 2702 O LEU A 290 -9.143 -21.317 56.689 1.00 93.81 O ANISOU 2702 O LEU A 290 10295 13874 11475 930 373 1604 O ATOM 2703 CB LEU A 290 -7.221 -19.316 56.814 1.00 91.83 C ANISOU 2703 CB LEU A 290 10409 13479 11004 834 246 1227 C ATOM 2704 CG LEU A 290 -6.129 -18.208 56.879 1.00 96.93 C ANISOU 2704 CG LEU A 290 11252 14035 11542 768 161 1026 C ATOM 2705 CD1 LEU A 290 -6.502 -16.964 56.073 1.00 97.11 C ANISOU 2705 CD1 LEU A 290 11418 13963 11517 743 160 959 C ATOM 2706 CD2 LEU A 290 -5.750 -17.852 58.314 1.00100.85 C ANISOU 2706 CD2 LEU A 290 11871 14577 11870 920 137 989 C ATOM 2707 N ALA A 291 -10.960 -19.963 56.857 1.00 91.44 N ANISOU 2707 N ALA A 291 10124 13600 11018 1177 478 1754 N ATOM 2708 CA ALA A 291 -11.988 -21.003 56.752 1.00 90.88 C ANISOU 2708 CA ALA A 291 9844 13603 11082 1214 532 1977 C ATOM 2709 C ALA A 291 -12.107 -21.535 55.320 1.00 92.63 C ANISOU 2709 C ALA A 291 9952 13758 11487 1000 491 1975 C ATOM 2710 O ALA A 291 -12.225 -22.748 55.134 1.00 91.91 O ANISOU 2710 O ALA A 291 9678 13692 11550 929 479 2071 O ATOM 2711 CB ALA A 291 -13.331 -20.459 57.217 1.00 92.64 C ANISOU 2711 CB ALA A 291 10092 13892 11214 1435 627 2160 C ATOM 2712 N TYR A 292 -12.068 -20.634 54.316 1.00 87.83 N ANISOU 2712 N TYR A 292 9452 13060 10858 899 467 1866 N ATOM 2713 CA TYR A 292 -12.157 -20.974 52.892 1.00 86.27 C ANISOU 2713 CA TYR A 292 9179 12794 10807 703 425 1845 C ATOM 2714 C TYR A 292 -10.797 -21.513 52.406 1.00 88.19 C ANISOU 2714 C TYR A 292 9409 12973 11128 512 347 1673 C ATOM 2715 O TYR A 292 -10.085 -20.863 51.635 1.00 87.17 O ANISOU 2715 O TYR A 292 9382 12758 10980 391 303 1512 O ATOM 2716 CB TYR A 292 -12.639 -19.769 52.047 1.00 87.37 C ANISOU 2716 CB TYR A 292 9438 12872 10885 686 438 1804 C ATOM 2717 CG TYR A 292 -12.287 -18.405 52.607 1.00 89.54 C ANISOU 2717 CG TYR A 292 9927 13119 10976 791 454 1687 C ATOM 2718 CD1 TYR A 292 -11.026 -17.851 52.408 1.00 91.05 C ANISOU 2718 CD1 TYR A 292 10243 13228 11122 680 388 1472 C ATOM 2719 CD2 TYR A 292 -13.229 -17.650 53.300 1.00 91.31 C ANISOU 2719 CD2 TYR A 292 10231 13392 11071 1000 534 1798 C ATOM 2720 CE1 TYR A 292 -10.701 -16.592 52.910 1.00 92.39 C ANISOU 2720 CE1 TYR A 292 10616 13358 11131 766 386 1362 C ATOM 2721 CE2 TYR A 292 -12.915 -16.390 53.808 1.00 92.84 C ANISOU 2721 CE2 TYR A 292 10639 13545 11090 1100 543 1682 C ATOM 2722 CZ TYR A 292 -11.649 -15.864 53.609 1.00 99.73 C ANISOU 2722 CZ TYR A 292 11637 14328 11928 976 462 1460 C ATOM 2723 OH TYR A 292 -11.333 -14.621 54.101 1.00101.22 O ANISOU 2723 OH TYR A 292 12043 14463 11953 1063 455 1345 O ATOM 2724 N GLU A 293 -10.451 -22.722 52.879 1.00 83.92 N ANISOU 2724 N GLU A 293 8734 12476 10677 496 336 1724 N ATOM 2725 CA GLU A 293 -9.205 -23.420 52.569 1.00 82.61 C ANISOU 2725 CA GLU A 293 8532 12265 10591 341 277 1598 C ATOM 2726 C GLU A 293 -9.464 -24.556 51.572 1.00 84.74 C ANISOU 2726 C GLU A 293 8653 12501 11043 201 251 1657 C ATOM 2727 O GLU A 293 -8.698 -24.720 50.621 1.00 83.52 O ANISOU 2727 O GLU A 293 8516 12268 10950 40 203 1533 O ATOM 2728 CB GLU A 293 -8.579 -23.962 53.865 1.00 84.38 C ANISOU 2728 CB GLU A 293 8719 12562 10778 429 286 1610 C ATOM 2729 CG GLU A 293 -7.067 -24.079 53.826 1.00 94.14 C ANISOU 2729 CG GLU A 293 9997 13755 12017 308 230 1442 C ATOM 2730 CD GLU A 293 -6.468 -24.776 55.032 1.00113.52 C ANISOU 2730 CD GLU A 293 12389 16289 14456 380 236 1471 C ATOM 2731 OE1 GLU A 293 -5.888 -24.078 55.895 1.00107.22 O ANISOU 2731 OE1 GLU A 293 11706 15513 13518 456 222 1394 O ATOM 2732 OE2 GLU A 293 -6.589 -26.019 55.121 1.00106.28 O1- ANISOU 2732 OE2 GLU A 293 11308 15409 13666 363 252 1574 O1- ATOM 2733 N LYS A 294 -10.551 -25.328 51.793 1.00 80.88 N ANISOU 2733 N LYS A 294 8022 12068 10640 268 280 1852 N ATOM 2734 CA LYS A 294 -10.974 -26.455 50.953 1.00 79.97 C ANISOU 2734 CA LYS A 294 7764 11919 10702 150 244 1934 C ATOM 2735 C LYS A 294 -11.491 -25.977 49.594 1.00 82.20 C ANISOU 2735 C LYS A 294 8091 12127 11014 42 213 1904 C ATOM 2736 O LYS A 294 -11.303 -26.671 48.594 1.00 81.16 O ANISOU 2736 O LYS A 294 7913 11926 10997 -108 158 1865 O ATOM 2737 CB LYS A 294 -12.070 -27.280 51.655 1.00 83.35 C ANISOU 2737 CB LYS A 294 8028 12430 11211 264 279 2173 C ATOM 2738 CG LYS A 294 -11.642 -27.953 52.956 1.00 99.04 C ANISOU 2738 CG LYS A 294 9939 14498 13193 371 312 2229 C ATOM 2739 CD LYS A 294 -12.824 -28.661 53.617 1.00110.40 C ANISOU 2739 CD LYS A 294 11211 16023 14713 498 352 2488 C ATOM 2740 CE LYS A 294 -12.493 -29.278 54.957 1.00122.67 C ANISOU 2740 CE LYS A 294 12684 17672 16253 628 396 2564 C ATOM 2741 NZ LYS A 294 -11.633 -30.485 54.831 1.00131.63 N1+ ANISOU 2741 NZ LYS A 294 13721 18771 17521 503 355 2513 N1+ ATOM 2742 N PHE A 295 -12.153 -24.800 49.569 1.00 78.30 N ANISOU 2742 N PHE A 295 7692 11649 10411 126 249 1927 N ATOM 2743 CA PHE A 295 -12.742 -24.189 48.375 1.00 77.58 C ANISOU 2743 CA PHE A 295 7646 11502 10328 48 230 1915 C ATOM 2744 C PHE A 295 -11.669 -23.745 47.372 1.00 79.81 C ANISOU 2744 C PHE A 295 8041 11692 10593 -103 184 1699 C ATOM 2745 O PHE A 295 -11.789 -24.067 46.189 1.00 78.87 O ANISOU 2745 O PHE A 295 7896 11512 10558 -236 138 1675 O ATOM 2746 CB PHE A 295 -13.626 -22.987 48.752 1.00 79.96 C ANISOU 2746 CB PHE A 295 8028 11850 10504 198 295 1995 C ATOM 2747 CG PHE A 295 -14.809 -23.309 49.634 1.00 82.42 C ANISOU 2747 CG PHE A 295 8231 12259 10827 363 352 2235 C ATOM 2748 CD1 PHE A 295 -16.010 -23.744 49.085 1.00 85.83 C ANISOU 2748 CD1 PHE A 295 8538 12708 11367 344 344 2423 C ATOM 2749 CD2 PHE A 295 -14.735 -23.143 51.012 1.00 85.19 C ANISOU 2749 CD2 PHE A 295 8605 12688 11077 545 413 2284 C ATOM 2750 CE1 PHE A 295 -17.108 -24.031 49.901 1.00 87.69 C ANISOU 2750 CE1 PHE A 295 8659 13039 11622 502 400 2669 C ATOM 2751 CE2 PHE A 295 -15.834 -23.428 51.828 1.00 88.95 C ANISOU 2751 CE2 PHE A 295 8975 13261 11559 715 476 2522 C ATOM 2752 CZ PHE A 295 -17.014 -23.865 51.266 1.00 87.36 C ANISOU 2752 CZ PHE A 295 8638 13078 11477 693 472 2720 C ATOM 2753 N PHE A 296 -10.630 -23.014 47.841 1.00 75.76 N ANISOU 2753 N PHE A 296 7648 11165 9970 -82 193 1551 N ATOM 2754 CA PHE A 296 -9.535 -22.513 47.000 1.00 74.70 C ANISOU 2754 CA PHE A 296 7616 10949 9818 -211 154 1361 C ATOM 2755 C PHE A 296 -8.658 -23.654 46.467 1.00 77.05 C ANISOU 2755 C PHE A 296 7840 11204 10232 -348 108 1296 C ATOM 2756 O PHE A 296 -8.061 -23.506 45.398 1.00 76.03 O ANISOU 2756 O PHE A 296 7759 11004 10127 -470 76 1184 O ATOM 2757 CB PHE A 296 -8.659 -21.500 47.763 1.00 76.76 C ANISOU 2757 CB PHE A 296 8013 11207 9945 -151 163 1241 C ATOM 2758 CG PHE A 296 -9.279 -20.165 48.128 1.00 78.99 C ANISOU 2758 CG PHE A 296 8418 11501 10093 -30 202 1255 C ATOM 2759 CD1 PHE A 296 -10.432 -19.713 47.493 1.00 82.28 C ANISOU 2759 CD1 PHE A 296 8833 11919 10511 -5 232 1346 C ATOM 2760 CD2 PHE A 296 -8.669 -19.330 49.055 1.00 81.71 C ANISOU 2760 CD2 PHE A 296 8889 11848 10309 54 205 1171 C ATOM 2761 CE1 PHE A 296 -10.994 -18.477 47.825 1.00 83.82 C ANISOU 2761 CE1 PHE A 296 9146 12120 10580 116 279 1362 C ATOM 2762 CE2 PHE A 296 -9.222 -18.087 49.374 1.00 85.18 C ANISOU 2762 CE2 PHE A 296 9460 12283 10620 171 241 1175 C ATOM 2763 CZ PHE A 296 -10.383 -17.671 48.760 1.00 83.39 C ANISOU 2763 CZ PHE A 296 9227 12061 10396 206 284 1273 C ATOM 2764 N LEU A 297 -8.584 -24.780 47.208 1.00 73.10 N ANISOU 2764 N LEU A 297 7227 10747 9800 -318 110 1374 N ATOM 2765 CA LEU A 297 -7.823 -25.975 46.835 1.00 72.17 C ANISOU 2765 CA LEU A 297 7032 10592 9796 -427 77 1334 C ATOM 2766 C LEU A 297 -8.459 -26.633 45.603 1.00 74.97 C ANISOU 2766 C LEU A 297 7332 10889 10264 -532 37 1373 C ATOM 2767 O LEU A 297 -7.752 -26.936 44.640 1.00 74.02 O ANISOU 2767 O LEU A 297 7241 10696 10187 -651 4 1267 O ATOM 2768 CB LEU A 297 -7.777 -26.966 48.027 1.00 72.58 C ANISOU 2768 CB LEU A 297 6970 10714 9894 -348 98 1433 C ATOM 2769 CG LEU A 297 -6.542 -27.884 48.216 1.00 77.07 C ANISOU 2769 CG LEU A 297 7495 11267 10523 -414 85 1363 C ATOM 2770 CD1 LEU A 297 -6.354 -28.874 47.074 1.00 76.94 C ANISOU 2770 CD1 LEU A 297 7429 11169 10635 -550 47 1337 C ATOM 2771 CD2 LEU A 297 -5.279 -27.099 48.538 1.00 79.44 C ANISOU 2771 CD2 LEU A 297 7902 11562 10720 -423 85 1220 C ATOM 2772 N LEU A 298 -9.794 -26.830 45.636 1.00 71.40 N ANISOU 2772 N LEU A 298 6804 10468 9855 -483 38 1531 N ATOM 2773 CA LEU A 298 -10.579 -27.426 44.551 1.00 71.01 C ANISOU 2773 CA LEU A 298 6699 10368 9912 -577 -14 1592 C ATOM 2774 C LEU A 298 -10.645 -26.492 43.340 1.00 74.06 C ANISOU 2774 C LEU A 298 7195 10701 10244 -650 -33 1497 C ATOM 2775 O LEU A 298 -10.666 -26.974 42.208 1.00 73.46 O ANISOU 2775 O LEU A 298 7119 10556 10236 -766 -88 1458 O ATOM 2776 CB LEU A 298 -12.002 -27.766 45.032 1.00 71.74 C ANISOU 2776 CB LEU A 298 6674 10522 10062 -495 -9 1811 C ATOM 2777 CG LEU A 298 -12.141 -28.913 46.042 1.00 76.83 C ANISOU 2777 CG LEU A 298 7178 11215 10799 -436 -1 1942 C ATOM 2778 CD1 LEU A 298 -13.413 -28.777 46.847 1.00 77.79 C ANISOU 2778 CD1 LEU A 298 7207 11426 10922 -298 38 2161 C ATOM 2779 CD2 LEU A 298 -12.088 -30.274 45.358 1.00 79.29 C ANISOU 2779 CD2 LEU A 298 7404 11451 11270 -563 -74 1955 C ATOM 2780 N LEU A 299 -10.662 -25.163 43.583 1.00 70.24 N ANISOU 2780 N LEU A 299 6809 10244 9635 -579 12 1459 N ATOM 2781 CA LEU A 299 -10.711 -24.111 42.560 1.00 69.67 C ANISOU 2781 CA LEU A 299 6842 10130 9501 -630 8 1375 C ATOM 2782 C LEU A 299 -9.474 -24.178 41.648 1.00 72.68 C ANISOU 2782 C LEU A 299 7291 10435 9890 -750 -22 1200 C ATOM 2783 O LEU A 299 -9.607 -24.036 40.432 1.00 72.08 O ANISOU 2783 O LEU A 299 7249 10308 9830 -836 -53 1156 O ATOM 2784 CB LEU A 299 -10.814 -22.729 43.239 1.00 69.89 C ANISOU 2784 CB LEU A 299 6965 10198 9393 -514 67 1364 C ATOM 2785 CG LEU A 299 -11.177 -21.520 42.366 1.00 74.54 C ANISOU 2785 CG LEU A 299 7648 10758 9914 -532 79 1324 C ATOM 2786 CD1 LEU A 299 -12.637 -21.563 41.924 1.00 75.22 C ANISOU 2786 CD1 LEU A 299 7667 10873 10039 -514 79 1486 C ATOM 2787 CD2 LEU A 299 -10.931 -20.227 43.117 1.00 77.09 C ANISOU 2787 CD2 LEU A 299 8088 11099 10105 -427 130 1275 C ATOM 2788 N ALA A 300 -8.287 -24.424 42.237 1.00 68.82 N ANISOU 2788 N ALA A 300 6817 9943 9390 -751 -13 1113 N ATOM 2789 CA ALA A 300 -7.018 -24.552 41.519 1.00 68.08 C ANISOU 2789 CA ALA A 300 6773 9786 9306 -849 -31 970 C ATOM 2790 C ALA A 300 -6.897 -25.926 40.845 1.00 71.67 C ANISOU 2790 C ALA A 300 7162 10194 9876 -935 -71 976 C ATOM 2791 O ALA A 300 -6.245 -26.038 39.806 1.00 70.90 O ANISOU 2791 O ALA A 300 7114 10035 9792 -1020 -89 879 O ATOM 2792 CB ALA A 300 -5.856 -24.335 42.474 1.00 68.69 C ANISOU 2792 CB ALA A 300 6879 9884 9336 -815 -9 901 C ATOM 2793 N GLU A 301 -7.526 -26.962 41.441 1.00 68.58 N ANISOU 2793 N GLU A 301 6663 9830 9565 -906 -83 1093 N ATOM 2794 CA GLU A 301 -7.530 -28.343 40.949 1.00 68.54 C ANISOU 2794 CA GLU A 301 6592 9773 9678 -979 -127 1114 C ATOM 2795 C GLU A 301 -8.333 -28.464 39.644 1.00 72.43 C ANISOU 2795 C GLU A 301 7105 10208 10208 -1058 -185 1125 C ATOM 2796 O GLU A 301 -7.923 -29.202 38.746 1.00 71.80 O ANISOU 2796 O GLU A 301 7049 10053 10180 -1142 -226 1059 O ATOM 2797 CB GLU A 301 -8.109 -29.287 42.020 1.00 70.37 C ANISOU 2797 CB GLU A 301 6695 10054 9989 -917 -125 1258 C ATOM 2798 CG GLU A 301 -7.943 -30.770 41.711 1.00 80.98 C ANISOU 2798 CG GLU A 301 7970 11338 11461 -986 -169 1276 C ATOM 2799 CD GLU A 301 -8.640 -31.749 42.638 1.00101.16 C ANISOU 2799 CD GLU A 301 10384 13933 14118 -935 -175 1436 C ATOM 2800 OE1 GLU A 301 -9.337 -31.304 43.579 1.00 96.46 O ANISOU 2800 OE1 GLU A 301 9735 13424 13492 -833 -141 1553 O ATOM 2801 OE2 GLU A 301 -8.501 -32.972 42.408 1.00 94.10 O ANISOU 2801 OE2 GLU A 301 9436 12981 13336 -993 -214 1452 O ATOM 2802 N PHE A 302 -9.471 -27.741 39.548 1.00 69.43 N ANISOU 2802 N PHE A 302 6721 9863 9798 -1025 -189 1212 N ATOM 2803 CA PHE A 302 -10.360 -27.742 38.383 1.00 69.64 C ANISOU 2803 CA PHE A 302 6759 9848 9851 -1095 -249 1242 C ATOM 2804 C PHE A 302 -9.693 -27.134 37.141 1.00 73.37 C ANISOU 2804 C PHE A 302 7351 10264 10261 -1165 -255 1092 C ATOM 2805 O PHE A 302 -10.055 -27.515 36.027 1.00 73.18 O ANISOU 2805 O PHE A 302 7349 10185 10271 -1244 -318 1078 O ATOM 2806 CB PHE A 302 -11.666 -26.991 38.689 1.00 71.78 C ANISOU 2806 CB PHE A 302 6994 10185 10095 -1028 -235 1384 C ATOM 2807 CG PHE A 302 -12.812 -27.886 39.102 1.00 74.04 C ANISOU 2807 CG PHE A 302 7147 10495 10489 -1015 -278 1572 C ATOM 2808 CD1 PHE A 302 -13.020 -28.206 40.438 1.00 77.37 C ANISOU 2808 CD1 PHE A 302 7476 10984 10936 -913 -236 1688 C ATOM 2809 CD2 PHE A 302 -13.688 -28.403 38.155 1.00 76.67 C ANISOU 2809 CD2 PHE A 302 7446 10783 10901 -1103 -366 1640 C ATOM 2810 CE1 PHE A 302 -14.079 -29.035 40.820 1.00 79.01 C ANISOU 2810 CE1 PHE A 302 7548 11217 11256 -897 -274 1881 C ATOM 2811 CE2 PHE A 302 -14.747 -29.233 38.538 1.00 80.27 C ANISOU 2811 CE2 PHE A 302 7770 11256 11472 -1099 -416 1829 C ATOM 2812 CZ PHE A 302 -14.936 -29.541 39.868 1.00 78.59 C ANISOU 2812 CZ PHE A 302 7455 11113 11293 -995 -366 1954 C ATOM 2813 N ASN A 303 -8.715 -26.217 37.330 1.00 69.58 N ANISOU 2813 N ASN A 303 6947 9798 9693 -1135 -196 986 N ATOM 2814 CA ASN A 303 -7.976 -25.552 36.249 1.00 69.16 C ANISOU 2814 CA ASN A 303 6996 9700 9581 -1188 -190 855 C ATOM 2815 C ASN A 303 -7.171 -26.553 35.410 1.00 73.42 C ANISOU 2815 C ASN A 303 7561 10166 10170 -1263 -223 770 C ATOM 2816 O ASN A 303 -7.038 -26.358 34.200 1.00 72.97 O ANISOU 2816 O ASN A 303 7573 10064 10088 -1315 -243 701 O ATOM 2817 CB ASN A 303 -7.043 -24.487 36.810 1.00 69.35 C ANISOU 2817 CB ASN A 303 7078 9750 9522 -1141 -130 780 C ATOM 2818 CG ASN A 303 -6.429 -23.610 35.749 1.00 91.57 C ANISOU 2818 CG ASN A 303 9985 12528 12279 -1183 -118 675 C ATOM 2819 OD1 ASN A 303 -7.036 -22.645 35.277 1.00 85.94 O ANISOU 2819 OD1 ASN A 303 9312 11825 11516 -1175 -111 686 O ATOM 2820 ND2 ASN A 303 -5.226 -23.953 35.323 1.00 83.34 N ANISOU 2820 ND2 ASN A 303 8974 11445 11247 -1225 -113 582 N ATOM 2821 N SER A 304 -6.644 -27.619 36.052 1.00 70.44 N ANISOU 2821 N SER A 304 7129 9777 9856 -1260 -223 778 N ATOM 2822 CA SER A 304 -5.875 -28.686 35.404 1.00 70.57 C ANISOU 2822 CA SER A 304 7168 9721 9923 -1315 -245 709 C ATOM 2823 C SER A 304 -6.748 -29.464 34.403 1.00 75.51 C ANISOU 2823 C SER A 304 7804 10283 10604 -1379 -328 734 C ATOM 2824 O SER A 304 -6.219 -30.088 33.482 1.00 75.23 O ANISOU 2824 O SER A 304 7832 10174 10579 -1425 -352 655 O ATOM 2825 CB SER A 304 -5.293 -29.633 36.449 1.00 74.10 C ANISOU 2825 CB SER A 304 7542 10180 10432 -1288 -223 737 C ATOM 2826 OG SER A 304 -4.432 -28.947 37.343 1.00 82.18 O ANISOU 2826 OG SER A 304 8564 11259 11401 -1236 -160 710 O ATOM 2827 N ALA A 305 -8.083 -29.398 34.583 1.00 72.92 N ANISOU 2827 N ALA A 305 7416 9983 10307 -1377 -373 850 N ATOM 2828 CA ALA A 305 -9.094 -30.017 33.728 1.00 73.65 C ANISOU 2828 CA ALA A 305 7505 10022 10456 -1444 -469 899 C ATOM 2829 C ALA A 305 -9.695 -28.998 32.747 1.00 77.96 C ANISOU 2829 C ALA A 305 8113 10578 10928 -1467 -487 885 C ATOM 2830 O ALA A 305 -10.234 -29.397 31.714 1.00 78.05 O ANISOU 2830 O ALA A 305 8162 10535 10960 -1534 -570 880 O ATOM 2831 CB ALA A 305 -10.195 -30.620 34.585 1.00 74.90 C ANISOU 2831 CB ALA A 305 7537 10211 10710 -1429 -510 1065 C ATOM 2832 N MET A 306 -9.607 -27.690 33.078 1.00 74.37 N ANISOU 2832 N MET A 306 7676 10193 10390 -1410 -413 880 N ATOM 2833 CA MET A 306 -10.136 -26.582 32.276 1.00 74.32 C ANISOU 2833 CA MET A 306 7721 10207 10310 -1418 -411 875 C ATOM 2834 C MET A 306 -9.393 -26.400 30.951 1.00 79.04 C ANISOU 2834 C MET A 306 8429 10750 10853 -1465 -418 739 C ATOM 2835 O MET A 306 -10.033 -26.046 29.963 1.00 78.94 O ANISOU 2835 O MET A 306 8454 10730 10812 -1502 -459 744 O ATOM 2836 CB MET A 306 -10.080 -25.260 33.056 1.00 76.09 C ANISOU 2836 CB MET A 306 7946 10505 10460 -1338 -324 893 C ATOM 2837 CG MET A 306 -11.186 -25.100 34.066 1.00 79.93 C ANISOU 2837 CG MET A 306 8342 11059 10969 -1275 -314 1050 C ATOM 2838 SD MET A 306 -11.036 -23.552 34.983 1.00 83.64 S ANISOU 2838 SD MET A 306 8846 11599 11334 -1167 -213 1052 S ATOM 2839 CE MET A 306 -12.409 -23.709 36.091 1.00 80.87 C ANISOU 2839 CE MET A 306 8384 11322 11020 -1082 -205 1257 C ATOM 2840 N ASN A 307 -8.056 -26.611 30.932 1.00 75.97 N ANISOU 2840 N ASN A 307 8088 10330 10447 -1458 -374 630 N ATOM 2841 CA ASN A 307 -7.210 -26.439 29.743 1.00 76.05 C ANISOU 2841 CA ASN A 307 8199 10294 10401 -1482 -363 511 C ATOM 2842 C ASN A 307 -7.707 -27.298 28.542 1.00 81.10 C ANISOU 2842 C ASN A 307 8891 10865 11059 -1544 -455 491 C ATOM 2843 O ASN A 307 -8.000 -26.677 27.520 1.00 80.69 O ANISOU 2843 O ASN A 307 8898 10813 10946 -1561 -470 463 O ATOM 2844 CB ASN A 307 -5.733 -26.735 30.048 1.00 77.08 C ANISOU 2844 CB ASN A 307 8351 10405 10530 -1458 -303 430 C ATOM 2845 CG ASN A 307 -5.052 -25.743 30.971 1.00101.45 C ANISOU 2845 CG ASN A 307 11415 13549 13582 -1409 -225 426 C ATOM 2846 OD1 ASN A 307 -5.671 -24.842 31.555 1.00 96.38 O ANISOU 2846 OD1 ASN A 307 10745 12960 12914 -1379 -209 480 O ATOM 2847 ND2 ASN A 307 -3.745 -25.891 31.124 1.00 93.22 N ANISOU 2847 ND2 ASN A 307 10390 12493 12536 -1396 -178 364 N ATOM 2848 N PRO A 308 -7.900 -28.652 28.615 1.00 78.81 N ANISOU 2848 N PRO A 308 8584 10513 10847 -1578 -524 508 N ATOM 2849 CA PRO A 308 -8.397 -29.384 27.429 1.00 79.71 C ANISOU 2849 CA PRO A 308 8769 10549 10967 -1640 -627 479 C ATOM 2850 C PRO A 308 -9.821 -28.989 27.014 1.00 84.90 C ANISOU 2850 C PRO A 308 9398 11232 11627 -1684 -707 570 C ATOM 2851 O PRO A 308 -10.177 -29.170 25.849 1.00 85.14 O ANISOU 2851 O PRO A 308 9507 11216 11627 -1731 -784 531 O ATOM 2852 CB PRO A 308 -8.358 -30.851 27.872 1.00 81.92 C ANISOU 2852 CB PRO A 308 9020 10759 11347 -1665 -683 498 C ATOM 2853 CG PRO A 308 -7.407 -30.886 29.011 1.00 85.61 C ANISOU 2853 CG PRO A 308 9431 11263 11835 -1608 -586 495 C ATOM 2854 CD PRO A 308 -7.627 -29.593 29.721 1.00 80.41 C ANISOU 2854 CD PRO A 308 8712 10706 11135 -1564 -517 549 C ATOM 2855 N ILE A 309 -10.623 -28.444 27.954 1.00 81.82 N ANISOU 2855 N ILE A 309 8900 10918 11269 -1661 -687 694 N ATOM 2856 CA ILE A 309 -11.992 -27.974 27.713 1.00 82.32 C ANISOU 2856 CA ILE A 309 8916 11022 11339 -1690 -744 811 C ATOM 2857 C ILE A 309 -11.920 -26.677 26.868 1.00 86.68 C ANISOU 2857 C ILE A 309 9537 11616 11782 -1674 -695 759 C ATOM 2858 O ILE A 309 -12.733 -26.505 25.956 1.00 86.68 O ANISOU 2858 O ILE A 309 9559 11614 11762 -1721 -765 789 O ATOM 2859 CB ILE A 309 -12.764 -27.791 29.062 1.00 85.29 C ANISOU 2859 CB ILE A 309 9158 11472 11776 -1645 -715 969 C ATOM 2860 CG1 ILE A 309 -13.017 -29.167 29.740 1.00 86.25 C ANISOU 2860 CG1 ILE A 309 9200 11550 12020 -1671 -783 1043 C ATOM 2861 CG2 ILE A 309 -14.084 -27.015 28.883 1.00 86.32 C ANISOU 2861 CG2 ILE A 309 9236 11666 11895 -1649 -739 1103 C ATOM 2862 CD1 ILE A 309 -13.555 -29.139 31.207 1.00 93.20 C ANISOU 2862 CD1 ILE A 309 9944 12506 12963 -1604 -738 1198 C ATOM 2863 N ILE A 310 -10.922 -25.804 27.146 1.00 83.31 N ANISOU 2863 N ILE A 310 9142 11223 11290 -1612 -582 683 N ATOM 2864 CA ILE A 310 -10.693 -24.537 26.435 1.00 83.21 C ANISOU 2864 CA ILE A 310 9187 11246 11182 -1590 -522 633 C ATOM 2865 C ILE A 310 -10.292 -24.832 24.971 1.00 88.73 C ANISOU 2865 C ILE A 310 9993 11889 11831 -1629 -566 528 C ATOM 2866 O ILE A 310 -10.877 -24.241 24.061 1.00 88.53 O ANISOU 2866 O ILE A 310 9998 11884 11756 -1648 -590 540 O ATOM 2867 CB ILE A 310 -9.642 -23.643 27.170 1.00 85.48 C ANISOU 2867 CB ILE A 310 9480 11569 11430 -1523 -406 581 C ATOM 2868 CG1 ILE A 310 -10.213 -23.122 28.514 1.00 85.66 C ANISOU 2868 CG1 ILE A 310 9419 11654 11474 -1471 -364 687 C ATOM 2869 CG2 ILE A 310 -9.184 -22.460 26.291 1.00 85.88 C ANISOU 2869 CG2 ILE A 310 9599 11636 11395 -1507 -350 515 C ATOM 2870 CD1 ILE A 310 -9.169 -22.665 29.561 1.00 92.66 C ANISOU 2870 CD1 ILE A 310 10304 12559 12344 -1411 -280 641 C ATOM 2871 N TYR A 311 -9.335 -25.763 24.750 1.00 86.49 N ANISOU 2871 N TYR A 311 9768 11538 11559 -1632 -574 434 N ATOM 2872 CA TYR A 311 -8.862 -26.145 23.411 1.00 87.35 C ANISOU 2872 CA TYR A 311 9993 11587 11610 -1647 -608 331 C ATOM 2873 C TYR A 311 -9.951 -26.858 22.585 1.00 93.48 C ANISOU 2873 C TYR A 311 10802 12318 12400 -1718 -747 359 C ATOM 2874 O TYR A 311 -9.861 -26.876 21.355 1.00 93.51 O ANISOU 2874 O TYR A 311 10908 12290 12332 -1728 -783 289 O ATOM 2875 CB TYR A 311 -7.619 -27.058 23.493 1.00 88.57 C ANISOU 2875 CB TYR A 311 10199 11676 11776 -1622 -578 242 C ATOM 2876 CG TYR A 311 -6.425 -26.481 24.226 1.00 89.45 C ANISOU 2876 CG TYR A 311 10283 11825 11879 -1562 -457 214 C ATOM 2877 CD1 TYR A 311 -5.792 -25.327 23.771 1.00 91.00 C ANISOU 2877 CD1 TYR A 311 10510 12064 12004 -1523 -375 177 C ATOM 2878 CD2 TYR A 311 -5.848 -27.158 25.296 1.00 89.94 C ANISOU 2878 CD2 TYR A 311 10292 11874 12006 -1548 -429 224 C ATOM 2879 CE1 TYR A 311 -4.675 -24.808 24.425 1.00 91.18 C ANISOU 2879 CE1 TYR A 311 10505 12113 12026 -1480 -280 158 C ATOM 2880 CE2 TYR A 311 -4.731 -26.650 25.958 1.00 90.18 C ANISOU 2880 CE2 TYR A 311 10298 11938 12028 -1501 -331 202 C ATOM 2881 CZ TYR A 311 -4.144 -25.476 25.516 1.00 97.31 C ANISOU 2881 CZ TYR A 311 11231 12879 12865 -1471 -262 170 C ATOM 2882 OH TYR A 311 -3.038 -24.978 26.160 1.00 97.97 O ANISOU 2882 OH TYR A 311 11287 12988 12949 -1435 -181 157 O ATOM 2883 N SER A 312 -10.963 -27.443 23.256 1.00 91.54 N ANISOU 2883 N SER A 312 10469 12066 12244 -1765 -827 468 N ATOM 2884 CA SER A 312 -12.054 -28.182 22.620 1.00 92.98 C ANISOU 2884 CA SER A 312 10664 12200 12463 -1846 -978 517 C ATOM 2885 C SER A 312 -13.048 -27.263 21.886 1.00 98.48 C ANISOU 2885 C SER A 312 11353 12956 13108 -1873 -1012 581 C ATOM 2886 O SER A 312 -13.535 -27.655 20.823 1.00 98.88 O ANISOU 2886 O SER A 312 11477 12962 13133 -1931 -1125 558 O ATOM 2887 CB SER A 312 -12.804 -29.018 23.652 1.00 96.75 C ANISOU 2887 CB SER A 312 11029 12662 13069 -1883 -1045 639 C ATOM 2888 OG SER A 312 -13.745 -29.884 23.040 1.00106.39 O ANISOU 2888 OG SER A 312 12265 13816 14342 -1973 -1208 685 O ATOM 2889 N TYR A 313 -13.363 -26.069 22.439 1.00 95.61 N ANISOU 2889 N TYR A 313 10909 12690 12727 -1831 -920 661 N ATOM 2890 CA TYR A 313 -14.332 -25.166 21.808 1.00 96.33 C ANISOU 2890 CA TYR A 313 10981 12845 12774 -1850 -940 738 C ATOM 2891 C TYR A 313 -13.644 -24.011 21.039 1.00101.21 C ANISOU 2891 C TYR A 313 11672 13503 13279 -1798 -841 647 C ATOM 2892 O TYR A 313 -14.307 -23.370 20.220 1.00101.12 O ANISOU 2892 O TYR A 313 11671 13532 13216 -1817 -865 683 O ATOM 2893 CB TYR A 313 -15.339 -24.605 22.840 1.00 97.37 C ANISOU 2893 CB TYR A 313 10977 13057 12964 -1833 -910 912 C ATOM 2894 CG TYR A 313 -14.846 -23.473 23.718 1.00 98.25 C ANISOU 2894 CG TYR A 313 11053 13237 13040 -1741 -757 917 C ATOM 2895 CD1 TYR A 313 -14.182 -23.730 24.914 1.00 99.68 C ANISOU 2895 CD1 TYR A 313 11198 13413 13261 -1691 -693 903 C ATOM 2896 CD2 TYR A 313 -15.134 -22.147 23.406 1.00 98.77 C ANISOU 2896 CD2 TYR A 313 11119 13372 13036 -1705 -684 947 C ATOM 2897 CE1 TYR A 313 -13.762 -22.693 25.747 1.00 99.66 C ANISOU 2897 CE1 TYR A 313 11176 13467 13224 -1610 -569 906 C ATOM 2898 CE2 TYR A 313 -14.709 -21.101 24.225 1.00 98.91 C ANISOU 2898 CE2 TYR A 313 11118 13439 13023 -1623 -556 949 C ATOM 2899 CZ TYR A 313 -14.025 -21.379 25.396 1.00105.77 C ANISOU 2899 CZ TYR A 313 11964 14296 13927 -1577 -504 926 C ATOM 2900 OH TYR A 313 -13.611 -20.353 26.211 1.00105.94 O ANISOU 2900 OH TYR A 313 11981 14358 13913 -1499 -393 922 O ATOM 2901 N ARG A 314 -12.344 -23.748 21.290 1.00 98.24 N ANISOU 2901 N ARG A 314 11338 13118 12870 -1735 -734 543 N ATOM 2902 CA ARG A 314 -11.621 -22.667 20.614 1.00 98.18 C ANISOU 2902 CA ARG A 314 11387 13145 12771 -1685 -639 470 C ATOM 2903 C ARG A 314 -10.897 -23.163 19.355 1.00104.04 C ANISOU 2903 C ARG A 314 12254 13833 13446 -1684 -668 348 C ATOM 2904 O ARG A 314 -11.086 -22.572 18.290 1.00103.95 O ANISOU 2904 O ARG A 314 12291 13848 13358 -1680 -671 331 O ATOM 2905 CB ARG A 314 -10.626 -21.975 21.561 1.00 97.41 C ANISOU 2905 CB ARG A 314 11260 13073 12677 -1618 -510 444 C ATOM 2906 CG ARG A 314 -11.256 -20.884 22.426 1.00107.53 C ANISOU 2906 CG ARG A 314 12458 14427 13971 -1589 -448 546 C ATOM 2907 CD ARG A 314 -11.465 -19.588 21.659 1.00118.09 C ANISOU 2907 CD ARG A 314 13815 15816 15238 -1568 -395 556 C ATOM 2908 NE ARG A 314 -12.306 -18.644 22.396 1.00127.16 N ANISOU 2908 NE ARG A 314 14892 17026 16395 -1540 -350 668 N ATOM 2909 CZ ARG A 314 -12.619 -17.424 21.970 1.00141.68 C ANISOU 2909 CZ ARG A 314 16733 18915 18185 -1515 -292 701 C ATOM 2910 NH1 ARG A 314 -12.160 -16.980 20.805 1.00129.08 N ANISOU 2910 NH1 ARG A 314 15196 17319 16530 -1515 -274 633 N ATOM 2911 NH2 ARG A 314 -13.390 -16.636 22.706 1.00128.74 N1+ ANISOU 2911 NH2 ARG A 314 15037 17325 16552 -1479 -246 807 N1+ ATOM 2912 N ASP A 315 -10.076 -24.227 19.467 1.00101.89 N ANISOU 2912 N ASP A 315 12034 13485 13194 -1678 -684 268 N ATOM 2913 CA ASP A 315 -9.337 -24.767 18.324 1.00102.85 C ANISOU 2913 CA ASP A 315 12287 13549 13244 -1657 -702 154 C ATOM 2914 C ASP A 315 -10.268 -25.631 17.468 1.00109.06 C ANISOU 2914 C ASP A 315 13141 14279 14019 -1724 -858 151 C ATOM 2915 O ASP A 315 -10.908 -26.554 17.980 1.00108.97 O ANISOU 2915 O ASP A 315 13096 14219 14090 -1786 -958 197 O ATOM 2916 CB ASP A 315 -8.101 -25.558 18.783 1.00104.55 C ANISOU 2916 CB ASP A 315 12536 13705 13484 -1616 -651 80 C ATOM 2917 CG ASP A 315 -7.051 -25.757 17.705 1.00114.99 C ANISOU 2917 CG ASP A 315 13985 14989 14716 -1554 -611 -27 C ATOM 2918 OD1 ASP A 315 -7.319 -26.514 16.745 1.00116.61 O1- ANISOU 2918 OD1 ASP A 315 14301 15134 14874 -1568 -703 -80 O1- ATOM 2919 OD2 ASP A 315 -5.947 -25.190 17.842 1.00120.01 O ANISOU 2919 OD2 ASP A 315 14614 15655 15332 -1488 -492 -52 O ATOM 2920 N LYS A 316 -10.349 -25.306 16.166 1.00107.26 N ANISOU 2920 N LYS A 316 13005 14059 13689 -1713 -883 103 N ATOM 2921 CA LYS A 316 -11.205 -25.978 15.183 1.00108.85 C ANISOU 2921 CA LYS A 316 13291 14211 13856 -1775 -1039 91 C ATOM 2922 C LYS A 316 -10.629 -27.335 14.756 1.00114.74 C ANISOU 2922 C LYS A 316 14173 14837 14585 -1770 -1112 -19 C ATOM 2923 O LYS A 316 -11.376 -28.312 14.679 1.00115.21 O ANISOU 2923 O LYS A 316 14262 14821 14690 -1848 -1263 -6 O ATOM 2924 CB LYS A 316 -11.407 -25.086 13.943 1.00111.79 C ANISOU 2924 CB LYS A 316 13720 14643 14112 -1751 -1029 74 C ATOM 2925 CG LYS A 316 -12.122 -23.769 14.231 1.00126.34 C ANISOU 2925 CG LYS A 316 15438 16597 15967 -1760 -970 188 C ATOM 2926 CD LYS A 316 -12.249 -22.907 12.988 1.00137.55 C ANISOU 2926 CD LYS A 316 16911 18077 17275 -1730 -951 173 C ATOM 2927 CE LYS A 316 -12.946 -21.605 13.290 1.00149.19 C ANISOU 2927 CE LYS A 316 18265 19656 18765 -1734 -884 290 C ATOM 2928 NZ LYS A 316 -13.060 -20.749 12.081 1.00159.71 N1+ ANISOU 2928 NZ LYS A 316 19638 21051 19991 -1702 -859 282 N1+ ATOM 2929 N GLU A 317 -9.312 -27.386 14.470 1.00112.08 N ANISOU 2929 N GLU A 317 13920 14480 14185 -1676 -1005 -118 N ATOM 2930 CA GLU A 317 -8.597 -28.584 14.019 1.00113.26 C ANISOU 2930 CA GLU A 317 14214 14519 14301 -1641 -1042 -225 C ATOM 2931 C GLU A 317 -8.482 -29.632 15.141 1.00117.95 C ANISOU 2931 C GLU A 317 14759 15041 15017 -1678 -1070 -208 C ATOM 2932 O GLU A 317 -8.607 -30.826 14.864 1.00118.60 O ANISOU 2932 O GLU A 317 14940 15011 15111 -1707 -1180 -260 O ATOM 2933 CB GLU A 317 -7.194 -28.195 13.508 1.00114.42 C ANISOU 2933 CB GLU A 317 14436 14685 14354 -1516 -892 -302 C ATOM 2934 CG GLU A 317 -6.451 -29.289 12.751 1.00126.66 C ANISOU 2934 CG GLU A 317 16165 16130 15830 -1451 -915 -414 C ATOM 2935 CD GLU A 317 -6.967 -29.624 11.364 1.00149.48 C ANISOU 2935 CD GLU A 317 19222 18973 18601 -1449 -1034 -484 C ATOM 2936 OE1 GLU A 317 -7.133 -28.692 10.544 1.00144.93 O ANISOU 2936 OE1 GLU A 317 18659 18475 17932 -1416 -1006 -477 O ATOM 2937 OE2 GLU A 317 -7.146 -30.830 11.078 1.00145.18 O1- ANISOU 2937 OE2 GLU A 317 18803 18309 18049 -1472 -1154 -548 O1- ATOM 2938 N MET A 318 -8.243 -29.186 16.391 1.00114.04 N ANISOU 2938 N MET A 318 14116 14605 14610 -1674 -973 -136 N ATOM 2939 CA MET A 318 -8.070 -30.048 17.564 1.00113.96 C ANISOU 2939 CA MET A 318 14035 14547 14716 -1696 -976 -107 C ATOM 2940 C MET A 318 -9.374 -30.742 17.970 1.00119.16 C ANISOU 2940 C MET A 318 14635 15165 15475 -1802 -1131 -24 C ATOM 2941 O MET A 318 -9.324 -31.897 18.394 1.00119.24 O ANISOU 2941 O MET A 318 14657 15087 15563 -1830 -1192 -32 O ATOM 2942 CB MET A 318 -7.531 -29.232 18.744 1.00114.92 C ANISOU 2942 CB MET A 318 14020 14757 14888 -1659 -837 -48 C ATOM 2943 CG MET A 318 -6.562 -29.996 19.618 1.00118.25 C ANISOU 2943 CG MET A 318 14421 15138 15372 -1624 -774 -70 C ATOM 2944 SD MET A 318 -5.746 -28.948 20.850 1.00120.93 S ANISOU 2944 SD MET A 318 14626 15579 15743 -1573 -614 -20 S ATOM 2945 CE MET A 318 -4.611 -28.027 19.814 1.00117.47 C ANISOU 2945 CE MET A 318 14273 15175 15184 -1488 -501 -93 C ATOM 2946 N SER A 319 -10.527 -30.047 17.833 1.00116.30 N ANISOU 2946 N SER A 319 14203 14867 15118 -1860 -1192 66 N ATOM 2947 CA SER A 319 -11.865 -30.547 18.179 1.00117.01 C ANISOU 2947 CA SER A 319 14215 14936 15308 -1962 -1338 178 C ATOM 2948 C SER A 319 -12.229 -31.815 17.386 1.00123.07 C ANISOU 2948 C SER A 319 15108 15570 16081 -2028 -1514 121 C ATOM 2949 O SER A 319 -12.863 -32.715 17.942 1.00123.19 O ANISOU 2949 O SER A 319 15068 15523 16214 -2101 -1625 191 O ATOM 2950 CB SER A 319 -12.914 -29.466 17.935 1.00120.42 C ANISOU 2950 CB SER A 319 14570 15467 15718 -1995 -1357 281 C ATOM 2951 OG SER A 319 -14.198 -29.869 18.382 1.00129.82 O ANISOU 2951 OG SER A 319 15658 16652 17015 -2087 -1483 420 O ATOM 2952 N ALA A 320 -11.821 -31.885 16.104 1.00120.95 N ANISOU 2952 N ALA A 320 15012 15257 15686 -1997 -1542 -2 N ATOM 2953 CA ALA A 320 -12.071 -33.028 15.223 1.00122.70 C ANISOU 2953 CA ALA A 320 15394 15343 15884 -2046 -1711 -81 C ATOM 2954 C ALA A 320 -11.083 -34.174 15.490 1.00127.70 C ANISOU 2954 C ALA A 320 16118 15860 16542 -1999 -1686 -176 C ATOM 2955 O ALA A 320 -11.415 -35.333 15.233 1.00128.54 O ANISOU 2955 O ALA A 320 16316 15835 16688 -2058 -1837 -209 O ATOM 2956 CB ALA A 320 -11.980 -32.592 13.769 1.00124.15 C ANISOU 2956 CB ALA A 320 15735 15533 15905 -2009 -1736 -176 C ATOM 2957 N THR A 321 -9.877 -33.846 16.003 1.00123.86 N ANISOU 2957 N THR A 321 15606 15420 16036 -1897 -1500 -213 N ATOM 2958 CA THR A 321 -8.807 -34.805 16.301 1.00124.20 C ANISOU 2958 CA THR A 321 15721 15373 16096 -1835 -1442 -290 C ATOM 2959 C THR A 321 -9.169 -35.663 17.533 1.00128.88 C ANISOU 2959 C THR A 321 16191 15919 16858 -1901 -1490 -205 C ATOM 2960 O THR A 321 -8.824 -36.846 17.552 1.00129.24 O ANISOU 2960 O THR A 321 16322 15842 16941 -1900 -1539 -260 O ATOM 2961 CB THR A 321 -7.464 -34.071 16.505 1.00131.06 C ANISOU 2961 CB THR A 321 16574 16323 16901 -1714 -1231 -327 C ATOM 2962 OG1 THR A 321 -7.301 -33.082 15.487 1.00130.69 O ANISOU 2962 OG1 THR A 321 16595 16344 16719 -1661 -1183 -368 O ATOM 2963 CG2 THR A 321 -6.262 -35.014 16.486 1.00130.11 C ANISOU 2963 CG2 THR A 321 16561 16112 16763 -1632 -1163 -414 C ATOM 2964 N PHE A 322 -9.862 -35.079 18.542 1.00125.31 N ANISOU 2964 N PHE A 322 15545 15565 16504 -1949 -1474 -68 N ATOM 2965 CA PHE A 322 -10.266 -35.782 19.770 1.00125.42 C ANISOU 2965 CA PHE A 322 15420 15557 16679 -2000 -1509 36 C ATOM 2966 C PHE A 322 -11.208 -36.963 19.479 1.00131.84 C ANISOU 2966 C PHE A 322 16277 16238 17578 -2106 -1717 61 C ATOM 2967 O PHE A 322 -11.098 -37.999 20.138 1.00131.74 O ANISOU 2967 O PHE A 322 16234 16144 17677 -2126 -1750 83 O ATOM 2968 CB PHE A 322 -10.944 -34.830 20.776 1.00126.14 C ANISOU 2968 CB PHE A 322 15309 15782 16835 -2017 -1455 185 C ATOM 2969 CG PHE A 322 -10.121 -33.665 21.282 1.00126.23 C ANISOU 2969 CG PHE A 322 15259 15916 16786 -1927 -1266 178 C ATOM 2970 CD1 PHE A 322 -8.899 -33.875 21.913 1.00128.68 C ANISOU 2970 CD1 PHE A 322 15564 16226 17102 -1853 -1139 128 C ATOM 2971 CD2 PHE A 322 -10.619 -32.369 21.229 1.00127.75 C ANISOU 2971 CD2 PHE A 322 15386 16223 16931 -1921 -1222 238 C ATOM 2972 CE1 PHE A 322 -8.152 -32.800 22.404 1.00128.37 C ANISOU 2972 CE1 PHE A 322 15467 16292 17015 -1781 -983 128 C ATOM 2973 CE2 PHE A 322 -9.872 -31.294 21.721 1.00129.35 C ANISOU 2973 CE2 PHE A 322 15538 16523 17085 -1844 -1062 231 C ATOM 2974 CZ PHE A 322 -8.646 -31.517 22.309 1.00126.86 C ANISOU 2974 CZ PHE A 322 15223 16201 16775 -1779 -950 176 C ATOM 2975 N ARG A 323 -12.121 -36.803 18.499 1.00130.19 N ANISOU 2975 N ARG A 323 16136 16008 17323 -2176 -1862 63 N ATOM 2976 CA ARG A 323 -13.088 -37.831 18.095 1.00132.05 C ANISOU 2976 CA ARG A 323 16423 16115 17635 -2292 -2087 90 C ATOM 2977 C ARG A 323 -12.409 -38.984 17.341 1.00138.11 C ANISOU 2977 C ARG A 323 17409 16713 18352 -2271 -2155 -68 C ATOM 2978 O ARG A 323 -12.899 -40.114 17.395 1.00138.97 O ANISOU 2978 O ARG A 323 17550 16688 18564 -2353 -2315 -51 O ATOM 2979 CB ARG A 323 -14.199 -37.228 17.218 1.00133.07 C ANISOU 2979 CB ARG A 323 16566 16282 17713 -2369 -2218 138 C ATOM 2980 CG ARG A 323 -15.100 -36.225 17.938 1.00142.92 C ANISOU 2980 CG ARG A 323 17599 17679 19026 -2401 -2180 319 C ATOM 2981 CD ARG A 323 -16.293 -35.805 17.094 1.00154.92 C ANISOU 2981 CD ARG A 323 19123 19224 20517 -2491 -2330 388 C ATOM 2982 NE ARG A 323 -15.904 -35.039 15.907 1.00164.14 N ANISOU 2982 NE ARG A 323 20433 20429 21503 -2438 -2289 267 N ATOM 2983 CZ ARG A 323 -16.753 -34.606 14.980 1.00179.67 C ANISOU 2983 CZ ARG A 323 22435 22422 23408 -2500 -2404 296 C ATOM 2984 NH1 ARG A 323 -18.052 -34.858 15.088 1.00168.34 N ANISOU 2984 NH1 ARG A 323 20902 20979 22081 -2623 -2574 449 N ATOM 2985 NH2 ARG A 323 -16.309 -33.919 13.936 1.00166.80 N1+ ANISOU 2985 NH2 ARG A 323 20933 20833 21612 -2436 -2350 184 N1+ ATOM 2986 N GLN A 324 -11.296 -38.694 16.637 1.00135.15 N ANISOU 2986 N GLN A 324 17187 16342 17823 -2157 -2035 -213 N ATOM 2987 CA GLN A 324 -10.524 -39.659 15.847 1.00136.54 C ANISOU 2987 CA GLN A 324 17593 16370 17918 -2102 -2065 -370 C ATOM 2988 C GLN A 324 -9.793 -40.671 16.753 1.00140.81 C ANISOU 2988 C GLN A 324 18108 16830 18564 -2069 -2002 -375 C ATOM 2989 O GLN A 324 -9.646 -41.833 16.367 1.00141.78 O ANISOU 2989 O GLN A 324 18384 16789 18696 -2078 -2102 -455 O ATOM 2990 CB GLN A 324 -9.518 -38.915 14.950 1.00137.61 C ANISOU 2990 CB GLN A 324 17863 16563 17862 -1970 -1922 -488 C ATOM 2991 CG GLN A 324 -8.960 -39.744 13.797 1.00156.90 C ANISOU 2991 CG GLN A 324 20578 18860 20177 -1906 -1979 -649 C ATOM 2992 CD GLN A 324 -8.084 -38.913 12.895 1.00178.33 C ANISOU 2992 CD GLN A 324 23403 21650 22703 -1770 -1837 -737 C ATOM 2993 OE1 GLN A 324 -8.555 -38.273 11.949 1.00174.69 O ANISOU 2993 OE1 GLN A 324 23009 21232 22132 -1777 -1895 -761 O ATOM 2994 NE2 GLN A 324 -6.789 -38.905 13.167 1.00170.78 N ANISOU 2994 NE2 GLN A 324 22461 20717 21712 -1643 -1647 -775 N ATOM 2995 N ILE A 325 -9.344 -40.230 17.948 1.00136.16 N ANISOU 2995 N ILE A 325 17331 16353 18051 -2030 -1841 -289 N ATOM 2996 CA ILE A 325 -8.627 -41.060 18.927 1.00135.84 C ANISOU 2996 CA ILE A 325 17234 16266 18113 -1994 -1760 -275 C ATOM 2997 C ILE A 325 -9.608 -42.055 19.584 1.00140.94 C ANISOU 2997 C ILE A 325 17788 16820 18941 -2111 -1922 -172 C ATOM 2998 O ILE A 325 -9.271 -43.233 19.727 1.00141.34 O ANISOU 2998 O ILE A 325 17909 16737 19058 -2110 -1961 -211 O ATOM 2999 CB ILE A 325 -7.899 -40.182 19.993 1.00137.03 C ANISOU 2999 CB ILE A 325 17211 16576 18279 -1920 -1550 -209 C ATOM 3000 CG1 ILE A 325 -7.040 -39.078 19.331 1.00136.71 C ANISOU 3000 CG1 ILE A 325 17239 16630 18073 -1819 -1405 -286 C ATOM 3001 CG2 ILE A 325 -7.047 -41.045 20.945 1.00137.48 C ANISOU 3001 CG2 ILE A 325 17219 16591 18426 -1873 -1458 -200 C ATOM 3002 CD1 ILE A 325 -6.825 -37.827 20.183 1.00142.58 C ANISOU 3002 CD1 ILE A 325 17805 17545 18825 -1788 -1259 -203 C ATOM 3003 N LEU A 326 -10.812 -41.574 19.970 1.00137.65 N ANISOU 3003 N LEU A 326 17213 16477 18609 -2207 -2012 -32 N ATOM 3004 CA LEU A 326 -11.873 -42.356 20.622 1.00138.40 C ANISOU 3004 CA LEU A 326 17184 16511 18890 -2322 -2167 105 C ATOM 3005 C LEU A 326 -12.375 -43.507 19.731 1.00144.60 C ANISOU 3005 C LEU A 326 18142 17098 19703 -2410 -2392 40 C ATOM 3006 O LEU A 326 -12.633 -44.599 20.240 1.00145.08 O ANISOU 3006 O LEU A 326 18166 17046 19913 -2468 -2486 93 O ATOM 3007 CB LEU A 326 -13.058 -41.447 21.007 1.00137.94 C ANISOU 3007 CB LEU A 326 16941 16584 18887 -2390 -2209 272 C ATOM 3008 CG LEU A 326 -12.803 -40.377 22.078 1.00140.79 C ANISOU 3008 CG LEU A 326 17113 17129 19250 -2316 -2016 365 C ATOM 3009 CD1 LEU A 326 -13.800 -39.243 21.961 1.00140.57 C ANISOU 3009 CD1 LEU A 326 16987 17226 19197 -2353 -2040 474 C ATOM 3010 CD2 LEU A 326 -12.826 -40.968 23.483 1.00142.88 C ANISOU 3010 CD2 LEU A 326 17201 17408 19679 -2312 -1973 490 C ATOM 3011 N GLY A 327 -12.500 -43.248 18.429 1.00142.08 N ANISOU 3011 N GLY A 327 18009 16737 19238 -2418 -2478 -72 N ATOM 3012 CA GLY A 327 -12.955 -44.226 17.447 1.00174.70 C ANISOU 3012 CA GLY A 327 22338 20678 23360 -2497 -2702 -154 C ATOM 3013 C GLY A 327 -11.826 -45.044 16.855 1.00204.32 C ANISOU 3013 C GLY A 327 26332 24289 27013 -2401 -2659 -339 C ATOM 3014 O GLY A 327 -10.981 -45.568 17.583 1.00165.09 O ANISOU 3014 O GLY A 327 21331 19296 22099 -2330 -2532 -350 O TER 3015 GLY A 327 HETATM 3016 C1 ON3 A2000 -0.867 -25.698 49.741 1.00 61.53 C ANISOU 3016 C1 ON3 A2000 5841 9281 8258 -528 24 861 C HETATM 3017 C2 ON3 A2000 -1.404 -26.000 48.473 1.00 60.87 C ANISOU 3017 C2 ON3 A2000 5737 9135 8254 -601 30 867 C HETATM 3018 C3 ON3 A2000 -0.854 -25.392 47.311 1.00 60.48 C ANISOU 3018 C3 ON3 A2000 5765 9007 8206 -704 8 767 C HETATM 3019 C4 ON3 A2000 0.251 -24.481 47.390 1.00 60.48 C ANISOU 3019 C4 ON3 A2000 5853 8985 8142 -745 -22 669 C HETATM 3020 C5 ON3 A2000 0.781 -24.212 48.705 1.00 61.10 C ANISOU 3020 C5 ON3 A2000 5949 9120 8148 -682 -39 666 C HETATM 3021 C6 ON3 A2000 0.212 -24.811 49.858 1.00 61.60 C ANISOU 3021 C6 ON3 A2000 5945 9264 8195 -571 -15 756 C HETATM 3022 C9 ON3 A2000 0.782 -23.847 46.135 1.00 59.91 C ANISOU 3022 C9 ON3 A2000 5849 8835 8082 -846 -39 584 C HETATM 3023 C13 ON3 A2000 -2.745 -26.058 45.943 1.00 59.92 C ANISOU 3023 C13 ON3 A2000 5635 8894 8237 -724 21 867 C HETATM 3024 O17 ON3 A2000 -1.377 -25.678 46.033 1.00 60.11 O ANISOU 3024 O17 ON3 A2000 5710 8903 8228 -771 10 768 O HETATM 3025 O18 ON3 A2000 1.863 -23.357 48.762 1.00 61.18 O ANISOU 3025 O18 ON3 A2000 6039 9100 8108 -735 -85 578 O HETATM 3026 C19 ON3 A2000 3.152 -23.882 49.055 1.00 61.15 C ANISOU 3026 C19 ON3 A2000 5982 9110 8143 -794 -102 565 C HETATM 3027 C23 ON3 A2000 -1.509 -26.392 50.932 1.00 62.61 C ANISOU 3027 C23 ON3 A2000 5888 9508 8394 -404 56 981 C HETATM 3028 O25 ON3 A2000 -0.558 -26.746 51.902 1.00 63.16 O ANISOU 3028 O25 ON3 A2000 5923 9630 8443 -384 50 973 O HETATM 3029 C27 ON3 A2000 -2.683 -25.607 51.626 1.00 63.48 C ANISOU 3029 C27 ON3 A2000 6054 9667 8399 -258 76 1045 C HETATM 3030 O29 ON3 A2000 -3.566 -25.022 50.680 1.00 63.39 O ANISOU 3030 O29 ON3 A2000 6092 9605 8388 -278 80 1047 O HETATM 3031 C30 ON3 A2000 -3.888 -23.640 50.738 1.00 63.58 C ANISOU 3031 C30 ON3 A2000 6257 9612 8288 -224 75 998 C HETATM 3032 C31 ON3 A2000 -5.168 -23.486 49.857 1.00 63.44 C ANISOU 3032 C31 ON3 A2000 6226 9571 8307 -221 99 1070 C HETATM 3033 C32 ON3 A2000 -2.837 -22.700 50.059 1.00 63.30 C ANISOU 3033 C32 ON3 A2000 6340 9495 8215 -335 28 843 C HETATM 3034 C38 ON3 A2000 -4.603 -23.150 48.516 1.00 62.80 C ANISOU 3034 C38 ON3 A2000 6195 9399 8266 -369 66 959 C HETATM 3035 C39 ON3 A2000 -3.269 -22.690 48.639 1.00 62.69 C ANISOU 3035 C39 ON3 A2000 6253 9353 8211 -429 31 834 C HETATM 3036 C40 ON3 A2000 -2.525 -22.310 47.518 1.00 62.03 C ANISOU 3036 C40 ON3 A2000 6219 9193 8158 -556 3 731 C HETATM 3037 C41 ON3 A2000 -3.137 -22.399 46.246 1.00 61.51 C ANISOU 3037 C41 ON3 A2000 6138 9081 8153 -620 11 742 C HETATM 3038 C42 ON3 A2000 -4.460 -22.858 46.115 1.00 61.97 C ANISOU 3038 C42 ON3 A2000 6131 9167 8249 -570 36 856 C HETATM 3039 C43 ON3 A2000 -5.211 -23.240 47.259 1.00 62.55 C ANISOU 3039 C43 ON3 A2000 6146 9319 8303 -445 64 973 C HETATM 3040 C48 ON3 A2000 -3.394 -26.452 52.730 1.00 64.16 C ANISOU 3040 C48 ON3 A2000 6025 9852 8503 -126 119 1194 C HETATM 3041 O51 ON3 A2000 -4.803 -26.340 52.682 1.00 65.00 O ANISOU 3041 O51 ON3 A2000 6108 9981 8610 -37 153 1310 O HETATM 3042 C52 ON3 A2000 -7.369 -29.555 51.690 1.00 66.54 C ANISOU 3042 C52 ON3 A2000 5876 10184 9224 -79 182 1720 C HETATM 3043 C53 ON3 A2000 -7.763 -28.198 51.614 1.00 66.37 C ANISOU 3043 C53 ON3 A2000 5985 10164 9069 -22 191 1679 C HETATM 3044 C54 ON3 A2000 -6.875 -27.156 51.939 1.00 65.95 C ANISOU 3044 C54 ON3 A2000 6076 10106 8875 -7 187 1534 C HETATM 3045 C55 ON3 A2000 -5.563 -27.468 52.360 1.00 65.50 C ANISOU 3045 C55 ON3 A2000 6025 10053 8811 -51 171 1438 C HETATM 3046 C56 ON3 A2000 -5.139 -28.827 52.446 1.00 65.62 C ANISOU 3046 C56 ON3 A2000 5902 10076 8953 -102 172 1485 C HETATM 3047 C57 ON3 A2000 -6.041 -29.851 52.111 1.00 65.89 C ANISOU 3047 C57 ON3 A2000 5803 10106 9126 -114 179 1620 C HETATM 3048 C62 ON3 A2000 -8.319 -30.653 51.365 1.00 67.55 C ANISOU 3048 C62 ON3 A2000 5855 10302 9508 -101 173 1876 C HETATM 3049 C63 ON3 A2000 -8.926 -30.818 49.972 1.00 67.26 C ANISOU 3049 C63 ON3 A2000 5819 10173 9563 -226 122 1874 C HETATM 3050 C64 ON3 A2000 -7.885 -31.797 50.449 1.00 67.14 C ANISOU 3050 C64 ON3 A2000 5740 10162 9609 -254 127 1838 C HETATM 3051 C69 ON3 A2000 -9.237 -31.026 52.572 1.00 69.21 C ANISOU 3051 C69 ON3 A2000 5944 10623 9729 67 221 2082 C HETATM 3052 O70 ON3 A2000 -10.476 -31.098 52.370 1.00 69.85 O ANISOU 3052 O70 ON3 A2000 5958 10716 9865 105 223 2235 O HETATM 3053 O71 ON3 A2000 -8.671 -31.227 53.673 1.00 69.76 O1- ANISOU 3053 O71 ON3 A2000 5987 10767 9752 158 256 2092 O1- HETATM 3054 C10 1WV A2001 8.927 -36.261 39.708 1.00 62.28 C ANISOU 3054 C10 1WV A2001 5751 8703 9211 -1172 397 686 C HETATM 3055 C13 1WV A2001 9.985 -35.673 43.449 1.00 63.48 C ANISOU 3055 C13 1WV A2001 5627 9129 9361 -1145 394 846 C HETATM 3056 C17 1WV A2001 9.203 -34.164 46.385 1.00 64.31 C ANISOU 3056 C17 1WV A2001 5637 9442 9355 -1094 285 891 C HETATM 3057 C20 1WV A2001 9.848 -34.761 48.770 1.00 64.79 C ANISOU 3057 C20 1WV A2001 5525 9673 9417 -1026 297 1013 C HETATM 3058 C07 1WV A2001 10.605 -39.762 39.020 1.00 63.50 C ANISOU 3058 C07 1WV A2001 5887 8713 9526 -1086 587 775 C HETATM 3059 C08 1WV A2001 9.642 -38.720 39.622 1.00 62.92 C ANISOU 3059 C08 1WV A2001 5785 8702 9419 -1122 499 754 C HETATM 3060 C09 1WV A2001 9.827 -37.309 39.016 1.00 62.65 C ANISOU 3060 C09 1WV A2001 5822 8688 9295 -1147 475 700 C HETATM 3061 C11 1WV A2001 9.555 -35.577 40.941 1.00 62.44 C ANISOU 3061 C11 1WV A2001 5683 8832 9210 -1174 397 734 C HETATM 3062 C12 1WV A2001 9.215 -36.295 42.265 1.00 62.95 C ANISOU 3062 C12 1WV A2001 5636 8957 9327 -1147 396 802 C HETATM 3063 C14 1WV A2001 9.400 -34.368 43.978 1.00 63.87 C ANISOU 3063 C14 1WV A2001 5706 9229 9333 -1152 322 812 C HETATM 3064 O15 1WV A2001 8.552 -33.648 43.458 1.00 64.07 O ANISOU 3064 O15 1WV A2001 5807 9220 9316 -1163 279 756 O HETATM 3065 O16 1WV A2001 9.956 -34.018 45.181 1.00 64.09 O ANISOU 3065 O16 1WV A2001 5670 9347 9335 -1142 309 853 O HETATM 3066 C18 1WV A2001 10.200 -33.874 47.538 1.00 64.79 C ANISOU 3066 C18 1WV A2001 5636 9597 9385 -1090 277 934 C HETATM 3067 O19 1WV A2001 10.040 -32.565 48.008 1.00 65.08 O ANISOU 3067 O19 1WV A2001 5735 9667 9328 -1093 207 889 O HETATM 3068 O21 1WV A2001 10.756 -34.552 49.803 1.00 64.91 O ANISOU 3068 O21 1WV A2001 5486 9778 9400 -1022 286 1053 O HETATM 3069 C1 1WV A2001 10.197 -40.198 37.632 1.00 63.77 C ANISOU 3069 C1 1WV A2001 6063 8622 9545 -1076 576 700 C HETATM 3070 C2 1WV A2001 10.936 -40.108 36.505 1.00 64.00 C ANISOU 3070 C2 1WV A2001 6194 8600 9522 -1047 629 668 C HETATM 3071 C3 1WV A2001 12.320 -39.553 36.387 1.00 63.93 C ANISOU 3071 C3 1WV A2001 6166 8651 9475 -1021 712 716 C HETATM 3072 O HOH A2101 -3.464 -26.107 37.190 1.00 69.30 O ANISOU 3072 O HOH A2101 7076 9676 9580 -1203 -92 584 O HETATM 3073 O HOH A2102 -4.232 -31.822 54.852 1.00 77.76 O ANISOU 3073 O HOH A2102 7081 11794 10671 21 241 1714 O HETATM 3074 O HOH A2103 -3.665 -28.731 55.399 1.00 50.41 O ANISOU 3074 O HOH A2103 3984 8337 6831 115 202 1479 O CONECT 11 1332 CONECT 1318 1371 CONECT 1332 11 CONECT 1371 1318 CONECT 1437 2653 CONECT 2653 1437 CONECT 2665 2683 CONECT 2683 2665 CONECT 3016 3017 3021 3027 CONECT 3017 3016 3018 CONECT 3018 3017 3019 3024 CONECT 3019 3018 3020 3022 CONECT 3020 3019 3021 3025 CONECT 3021 3016 3020 CONECT 3022 3019 CONECT 3023 3024 CONECT 3024 3018 3023 CONECT 3025 3020 3026 CONECT 3026 3025 CONECT 3027 3016 3028 3029 CONECT 3028 3027 CONECT 3029 3027 3030 3040 CONECT 3030 3029 3031 CONECT 3031 3030 3032 3033 CONECT 3032 3031 3034 CONECT 3033 3031 3035 CONECT 3034 3032 3035 3039 CONECT 3035 3033 3034 3036 CONECT 3036 3035 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3039 CONECT 3039 3034 3038 CONECT 3040 3029 3041 CONECT 3041 3040 3045 CONECT 3042 3043 3047 3048 CONECT 3043 3042 3044 CONECT 3044 3043 3045 CONECT 3045 3041 3044 3046 CONECT 3046 3045 3047 CONECT 3047 3042 3046 CONECT 3048 3042 3049 3050 3051 CONECT 3049 3048 3050 CONECT 3050 3048 3049 CONECT 3051 3048 3052 3053 CONECT 3052 3051 CONECT 3053 3051 CONECT 3054 3060 3061 CONECT 3055 3062 3063 CONECT 3056 3065 3066 CONECT 3057 3066 3068 CONECT 3058 3059 3069 CONECT 3059 3058 3060 CONECT 3060 3054 3059 CONECT 3061 3054 3062 CONECT 3062 3055 3061 CONECT 3063 3055 3064 3065 CONECT 3064 3063 CONECT 3065 3056 3063 CONECT 3066 3056 3057 3067 CONECT 3067 3066 CONECT 3068 3057 CONECT 3069 3058 3070 CONECT 3070 3069 3071 CONECT 3071 3070 MASTER 369 0 2 16 0 0 6 6 3073 1 64 36 END