HEADER HYDROLASE 12-DEC-11 3V2W TITLE CRYSTAL STRUCTURE OF A LIPID G PROTEIN-COUPLED RECEPTOR AT 3.35A COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPHINGOSINE 1-PHOSPHATE RECEPTOR 1, LYSOZYME CHIMERA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: S1P1,ENDOTHELIAL DIFFERENTIATION G-PROTEIN COUPLED RECEPTOR COMPND 5 1,SPHINGOSINE 1-PHOSPHATE RECEPTOR EDG-1,S1P RECEPTOR EDG-1,LYSIS COMPND 6 PROTEIN,LYSOZYME,MURAMIDASE; COMPND 7 EC: 3.2.1.17; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: S1PR1, CHEDG1, EDG1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS SPHINGOSINE, EDG RECEPTOR, LIPID RECEPTOR, MULTIPLE SCLEROSIS, KEYWDS 2 AUTOIMMUNITY, STRUCTURAL GENOMICS, PSI-BIOLOGY, GPCR NETWORK, GPCR, KEYWDS 3 MEMBRANE PROTEIN, G PROTEIN COUPLED RECEPTOR, MEMBRANE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR M.A.HANSON,C.B.ROTH,E.JO,M.T.GRIFFITH,F.L.SCOTT,G.REINHART,H.DESALE, AUTHOR 2 B.CLEMONS,S.M.CAHALAN,S.C.SCHUERER,M.G.SANNA,G.W.HAN,P.KUHN,H.ROSEN, AUTHOR 3 R.C.STEVENS,GPCR NETWORK (GPCR) REVDAT 4 29-JUL-20 3V2W 1 COMPND REMARK HETNAM LINK REVDAT 4 2 1 SITE REVDAT 3 21-JUN-17 3V2W 1 COMPND SOURCE SEQADV REVDAT 2 14-MAR-12 3V2W 1 JRNL REVDAT 1 15-FEB-12 3V2W 0 JRNL AUTH M.A.HANSON,C.B.ROTH,E.JO,M.T.GRIFFITH,F.L.SCOTT,G.REINHART, JRNL AUTH 2 H.DESALE,B.CLEMONS,S.M.CAHALAN,S.C.SCHUERER,M.G.SANNA, JRNL AUTH 3 G.W.HAN,P.KUHN,H.ROSEN,R.C.STEVENS JRNL TITL CRYSTAL STRUCTURE OF A LIPID G PROTEIN-COUPLED RECEPTOR. JRNL REF SCIENCE V. 335 851 2012 JRNL REFN ISSN 0036-8075 JRNL PMID 22344443 JRNL DOI 10.1126/SCIENCE.1215904 REMARK 2 REMARK 2 RESOLUTION. 3.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.65 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 8286 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) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.281 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.170 REMARK 3 FREE R VALUE TEST SET COUNT : 594 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 5 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.75 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2211 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2374 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2055 REMARK 3 BIN R VALUE (WORKING SET) : 0.2340 REMARK 3 BIN FREE R VALUE : 0.2829 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.06 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 221 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 : 3386 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 37 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 101.8 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.20690 REMARK 3 B22 (A**2) : 8.97860 REMARK 3 B33 (A**2) : -9.18560 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) : 0.704 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.887 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.823 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3494 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4767 ; 2.500 ; HARMONIC REMARK 3 TORSION ANGLES : 1554 ; 15.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 55 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 515 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3494 ; 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 : 499 ; 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 : 4286 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 0.91 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.45 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 1.49 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 17.8120 18.6984 13.8746 REMARK 3 T TENSOR REMARK 3 T11: 0.1160 T22: -0.0051 REMARK 3 T33: -0.2744 T12: 0.0379 REMARK 3 T13: -0.0389 T23: 0.0203 REMARK 3 L TENSOR REMARK 3 L11: 1.6847 L22: 0.0000 REMARK 3 L33: 0.2560 L12: -0.2612 REMARK 3 L13: 0.5199 L23: -0.3875 REMARK 3 S TENSOR REMARK 3 S11: 0.0302 S12: -0.2854 S13: -0.1822 REMARK 3 S21: -0.2237 S22: 0.0013 S23: 0.0164 REMARK 3 S31: 0.0158 S32: -0.0769 S33: -0.0315 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3V2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-11. REMARK 100 THE DEPOSITION ID IS D_1000069526. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-JAN-09; NULL REMARK 200 TEMPERATURE (KELVIN) : 100; NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 33 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; APS REMARK 200 BEAMLINE : 23-ID-B; 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL; NULL REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD; NULL REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8293 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.350 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : 0.18000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.8 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.78000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 7TM OF B2AR AND T4L REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRICINE, 34-36% PEG400, 80MM REMARK 280 SODIUM CITRATE AND 4% GLYCEROL, LUPUC CUBIC PHASE, TEMPERATURE REMARK 280 287K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 53.97000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.85000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.97000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.85000 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: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN REMARK 300 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 GLY A 2 REMARK 465 PRO A 3 REMARK 465 THR A 4 REMARK 465 SER A 5 REMARK 465 VAL A 6 REMARK 465 PRO A 7 REMARK 465 LEU A 8 REMARK 465 VAL A 9 REMARK 465 LYS A 10 REMARK 465 ALA A 11 REMARK 465 HIS A 12 REMARK 465 ARG A 13 REMARK 465 SER A 14 REMARK 465 SER A 15 REMARK 465 VAL A 16 REMARK 465 ASP A 40 REMARK 465 LYS A 41 REMARK 465 GLU A 42 REMARK 465 ASN A 43 REMARK 465 SER A 44 REMARK 465 ILE A 45 REMARK 465 LYS A 46 REMARK 465 MET A 149 REMARK 465 LYS A 150 REMARK 465 LEU A 151 REMARK 465 HIS A 152 REMARK 465 ASN A 153 REMARK 465 GLY A 154 REMARK 465 SER A 155 REMARK 465 MET A 326 REMARK 465 GLY A 327 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 LEU A 47 CG CD1 CD2 REMARK 470 GLU A 62 CG CD OE1 OE2 REMARK 470 LYS A 72 CG CD CE NZ REMARK 470 LYS A 74 CG CD CE NZ REMARK 470 LYS A 75 CG CD CE NZ REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 141 CG CD OE1 OE2 REMARK 470 MET A 180 CG SD CE REMARK 470 ARG A 223 CZ NH1 NH2 REMARK 470 ARG A 229 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 231 CG CD NE CZ NH1 NH2 REMARK 470 ARG A1014 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1016 CG CD CE NZ REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 GLU A1022 CG CD OE1 OE2 REMARK 470 TYR A1024 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A1035 CG CD CE NZ REMARK 470 GLU A1045 CG CD OE1 OE2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 ARG A1119 CG CD NE CZ NH1 NH2 REMARK 470 GLN A1122 CG CD OE1 NE2 REMARK 470 LYS A1135 CG CD CE NZ REMARK 470 ARG A1137 CG CD NE CZ NH1 NH2 REMARK 470 TYR A1139 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A1154 CG CD NE CZ NH1 NH2 REMARK 470 SER A 246 OG REMARK 470 VAL A 252 CG1 CG2 REMARK 470 LEU A 255 CG CD1 CD2 REMARK 470 VAL A 284 CG1 CG2 REMARK 470 LYS A 285 CG CD CE NZ REMARK 470 ARG A 319 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 324 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 19 35.01 -78.45 REMARK 500 ASN A 183 -156.13 -139.57 REMARK 500 GLN A1105 -65.06 -109.60 REMARK 500 GLN A1141 -71.10 -59.08 REMARK 500 ALA A1160 -18.88 -155.70 REMARK 500 THR A 286 -63.62 -95.44 REMARK 500 LEU A 313 -61.99 -95.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-110 RELATED DB: TARGETDB REMARK 900 RELATED ID: 3V2Y RELATED DB: PDB REMARK 900 2.8A RESOLUTION REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE AUTHORS STATE THAT THE SEQUENCE "NV" IS THE ORIGINAL SEQUENCE REMARK 999 FROM ENDOTHELIUM, AS OPPOSED TO KSL WHICH IS THE GENOMIC SEQUENCE. REMARK 999 THE UNIPROT RECORD WAS CHANGED TO THE GENOMIC SEQUENCE "KSL" AFTER REMARK 999 THE CLONE WAS CREATED AND THE CONSTRUCT WAS NOT CHANGED BECAUSE IT REMARK 999 WAS PERFORMING WELL. DBREF 3V2W A 2 231 UNP P21453 S1PR1_HUMAN 2 231 DBREF 3V2W A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 3V2W A 245 326 UNP P21453 S1PR1_HUMAN 244 326 SEQADV 3V2W MET A -17 UNP P21453 EXPRESSION TAG SEQADV 3V2W LYS A -16 UNP P21453 EXPRESSION TAG SEQADV 3V2W THR A -15 UNP P21453 EXPRESSION TAG SEQADV 3V2W ILE A -14 UNP P21453 EXPRESSION TAG SEQADV 3V2W ILE A -13 UNP P21453 EXPRESSION TAG SEQADV 3V2W ALA A -12 UNP P21453 EXPRESSION TAG SEQADV 3V2W LEU A -11 UNP P21453 EXPRESSION TAG SEQADV 3V2W SER A -10 UNP P21453 EXPRESSION TAG SEQADV 3V2W TYR A -9 UNP P21453 EXPRESSION TAG SEQADV 3V2W ILE A -8 UNP P21453 EXPRESSION TAG SEQADV 3V2W PHE A -7 UNP P21453 EXPRESSION TAG SEQADV 3V2W CYS A -6 UNP P21453 EXPRESSION TAG SEQADV 3V2W LEU A -5 UNP P21453 EXPRESSION TAG SEQADV 3V2W VAL A -4 UNP P21453 EXPRESSION TAG SEQADV 3V2W PHE A -3 UNP P21453 EXPRESSION TAG SEQADV 3V2W ALA A -2 UNP P21453 EXPRESSION TAG SEQADV 3V2W GLY A -1 UNP P21453 EXPRESSION TAG SEQADV 3V2W ALA A 0 UNP P21453 EXPRESSION TAG SEQADV 3V2W PRO A 1 UNP P21453 EXPRESSION TAG SEQADV 3V2W GLY A 1012 UNP P00720 ARG 12 CONFLICT SEQADV 3V2W THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 3V2W ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 3V2W ARG A 1137 UNP P00720 ILE 137 CONFLICT SEQADV 3V2W A UNP P21453 LYS 250 SEE REMARK 999 SEQADV 3V2W ASN A 251 UNP P21453 SER 251 SEE REMARK 999 SEQADV 3V2W VAL A 252 UNP P21453 LEU 252 SEE REMARK 999 SEQADV 3V2W GLY A 327 UNP P21453 EXPRESSION TAG SEQADV 3V2W ARG A 328 UNP P21453 EXPRESSION TAG SEQADV 3V2W PRO A 329 UNP P21453 EXPRESSION TAG SEQADV 3V2W LEU A 330 UNP P21453 EXPRESSION TAG SEQADV 3V2W GLU A 331 UNP P21453 EXPRESSION TAG SEQADV 3V2W VAL A 332 UNP P21453 EXPRESSION TAG SEQADV 3V2W LEU A 333 UNP P21453 EXPRESSION TAG SEQADV 3V2W PHE A 334 UNP P21453 EXPRESSION TAG SEQADV 3V2W GLN A 335 UNP P21453 EXPRESSION TAG SEQADV 3V2W GLY A 336 UNP P21453 EXPRESSION TAG SEQADV 3V2W PRO A 337 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 338 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 339 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 340 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 341 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 342 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 343 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 344 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 345 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 346 UNP P21453 EXPRESSION TAG SEQADV 3V2W HIS A 347 UNP P21453 EXPRESSION TAG SEQADV 3V2W ASP A 348 UNP P21453 EXPRESSION TAG SEQADV 3V2W TYR A 349 UNP P21453 EXPRESSION TAG SEQADV 3V2W LYS A 350 UNP P21453 EXPRESSION TAG SEQADV 3V2W ASP A 351 UNP P21453 EXPRESSION TAG SEQADV 3V2W ASP A 352 UNP P21453 EXPRESSION TAG SEQADV 3V2W ASP A 353 UNP P21453 EXPRESSION TAG SEQADV 3V2W ASP A 354 UNP P21453 EXPRESSION TAG SEQADV 3V2W LYS A 355 UNP P21453 EXPRESSION TAG SEQRES 1 A 520 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 520 VAL PHE ALA GLY ALA PRO GLY PRO THR SER VAL PRO LEU SEQRES 3 A 520 VAL LYS ALA HIS ARG SER SER VAL SER ASP TYR VAL ASN SEQRES 4 A 520 TYR ASP ILE ILE VAL ARG HIS TYR ASN TYR THR GLY LYS SEQRES 5 A 520 LEU ASN ILE SER ALA ASP LYS GLU ASN SER ILE LYS LEU SEQRES 6 A 520 THR SER VAL VAL PHE ILE LEU ILE CYS CYS PHE ILE ILE SEQRES 7 A 520 LEU GLU ASN ILE PHE VAL LEU LEU THR ILE TRP LYS THR SEQRES 8 A 520 LYS LYS PHE HIS ARG PRO MET TYR TYR PHE ILE GLY ASN SEQRES 9 A 520 LEU ALA LEU SER ASP LEU LEU ALA GLY VAL ALA TYR THR SEQRES 10 A 520 ALA ASN LEU LEU LEU SER GLY ALA THR THR TYR LYS LEU SEQRES 11 A 520 THR PRO ALA GLN TRP PHE LEU ARG GLU GLY SER MET PHE SEQRES 12 A 520 VAL ALA LEU SER ALA SER VAL PHE SER LEU LEU ALA ILE SEQRES 13 A 520 ALA ILE GLU ARG TYR ILE THR MET LEU LYS MET LYS LEU SEQRES 14 A 520 HIS ASN GLY SER ASN ASN PHE ARG LEU PHE LEU LEU ILE SEQRES 15 A 520 SER ALA CYS TRP VAL ILE SER LEU ILE LEU GLY GLY LEU SEQRES 16 A 520 PRO ILE MET GLY TRP ASN CYS ILE SER ALA LEU SER SER SEQRES 17 A 520 CYS SER THR VAL LEU PRO LEU TYR HIS LYS HIS TYR ILE SEQRES 18 A 520 LEU PHE CYS THR THR VAL PHE THR LEU LEU LEU LEU SER SEQRES 19 A 520 ILE VAL ILE LEU TYR CYS ARG ILE TYR SER LEU VAL ARG SEQRES 20 A 520 THR ARG ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY SEQRES 21 A 520 LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR SEQRES 22 A 520 THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER SEQRES 23 A 520 LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY SEQRES 24 A 520 ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU SEQRES 25 A 520 LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY SEQRES 26 A 520 ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER SEQRES 27 A 520 LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL SEQRES 28 A 520 PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SEQRES 29 A 520 SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA SEQRES 30 A 520 ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR SEQRES 31 A 520 PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR SEQRES 32 A 520 GLY THR TRP ASP ALA TYR ALA SER ARG SER SER GLU ASN SEQRES 33 A 520 VAL ALA LEU LEU LYS THR VAL ILE ILE VAL LEU SER VAL SEQRES 34 A 520 PHE ILE ALA CYS TRP ALA PRO LEU PHE ILE LEU LEU LEU SEQRES 35 A 520 LEU ASP VAL GLY CYS LYS VAL LYS THR CYS ASP ILE LEU SEQRES 36 A 520 PHE ARG ALA GLU TYR PHE LEU VAL LEU ALA VAL LEU ASN SEQRES 37 A 520 SER GLY THR ASN PRO ILE ILE TYR THR LEU THR ASN LYS SEQRES 38 A 520 GLU MET ARG ARG ALA PHE ILE ARG ILE MET GLY ARG PRO SEQRES 39 A 520 LEU GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS SEQRES 40 A 520 HIS HIS HIS HIS HIS ASP TYR LYS ASP ASP ASP ASP LYS MODRES 3V2W ASN A 30 ASN GLYCOSYLATION SITE HET ML5 A1201 23 HET NAG A1202 14 HETNAM ML5 {(3R)-3-AMINO-4-[(3-HEXYLPHENYL)AMINO]-4- HETNAM 2 ML5 OXOBUTYL}PHOSPHONIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE FORMUL 2 ML5 C16 H27 N2 O4 P FORMUL 3 NAG C8 H15 N O6 HELIX 1 1 TYR A 22 GLY A 33 1 12 HELIX 2 2 THR A 48 THR A 73 1 26 HELIX 3 3 LYS A 74 HIS A 77 5 4 HELIX 4 4 ARG A 78 LEU A 104 1 27 HELIX 5 5 ALA A 107 LEU A 112 5 6 HELIX 6 6 THR A 113 LEU A 147 1 35 HELIX 7 7 ARG A 159 LEU A 177 1 19 HELIX 8 8 ALA A 187 CYS A 191 5 5 HELIX 9 9 HIS A 199 GLU A 1011 1 43 HELIX 10 10 SER A 1038 ILE A 1050 1 13 HELIX 11 11 THR A 1059 GLY A 1077 1 19 HELIX 12 12 LEU A 1084 LEU A 1091 1 8 HELIX 13 13 ASP A 1092 PHE A 1104 1 13 HELIX 14 14 GLY A 1107 GLY A 1113 1 7 HELIX 15 15 PHE A 1114 GLN A 1123 1 10 HELIX 16 16 ARG A 1125 SER A 1136 1 12 HELIX 17 17 ARG A 1137 THR A 1142 1 6 HELIX 18 18 THR A 1142 GLY A 1156 1 15 HELIX 19 19 SER A 249 GLY A 281 1 33 HELIX 20 20 ASP A 288 ARG A 292 5 5 HELIX 21 21 ALA A 293 ASN A 303 1 11 HELIX 22 22 GLY A 305 ASN A 315 1 11 HELIX 23 23 ASN A 315 ARG A 324 1 10 SHEET 1 A 3 TYR A1018 LYS A1019 0 SHEET 2 A 3 TYR A1025 ILE A1027 -1 O THR A1026 N TYR A1018 SHEET 3 A 3 HIS A1031 THR A1034 -1 O HIS A1031 N ILE A1027 SSBOND 1 CYS A 184 CYS A 191 1555 1555 2.04 SSBOND 2 CYS A 282 CYS A 287 1555 1555 2.04 LINK ND2 ASN A 30 C1 NAG A1202 1555 1555 1.43 CRYST1 107.940 69.700 81.930 90.00 90.00 90.00 P 21 21 2 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 0.009264 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014347 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012206 0.00000 ATOM 1 N SER A 17 -5.253 34.350 -28.684 1.00 94.63 N ANISOU 1 N SER A 17 13994 13946 8017 262 -676 875 N ATOM 2 CA SER A 17 -5.912 34.028 -27.418 1.00 93.60 C ANISOU 2 CA SER A 17 13971 13583 8012 214 -706 820 C ATOM 3 C SER A 17 -4.953 34.110 -26.243 1.00 96.71 C ANISOU 3 C SER A 17 14391 13834 8520 224 -694 801 C ATOM 4 O SER A 17 -3.760 33.854 -26.414 1.00 96.88 O ANISOU 4 O SER A 17 14376 13926 8507 278 -669 792 O ATOM 5 CB SER A 17 -6.517 32.629 -27.466 1.00 97.78 C ANISOU 5 CB SER A 17 14619 14059 8476 231 -757 651 C ATOM 6 OG SER A 17 -7.520 32.541 -28.462 1.00109.71 O ANISOU 6 OG SER A 17 16116 15670 9899 211 -776 665 O ATOM 7 N ASP A 18 -5.486 34.428 -25.033 1.00 92.08 N ANISOU 7 N ASP A 18 13867 13056 8064 176 -713 792 N ATOM 8 CA ASP A 18 -4.722 34.517 -23.780 1.00 91.25 C ANISOU 8 CA ASP A 18 13792 12808 8071 182 -707 764 C ATOM 9 C ASP A 18 -3.787 33.349 -23.614 1.00 93.90 C ANISOU 9 C ASP A 18 14192 13139 8346 246 -712 626 C ATOM 10 O ASP A 18 -4.158 32.218 -23.937 1.00 94.10 O ANISOU 10 O ASP A 18 14285 13183 8284 271 -743 511 O ATOM 11 CB ASP A 18 -5.657 34.575 -22.546 1.00 92.71 C ANISOU 11 CB ASP A 18 14043 12810 8371 132 -736 746 C ATOM 12 CG ASP A 18 -6.346 35.905 -22.282 1.00107.93 C ANISOU 12 CG ASP A 18 15899 14693 10416 76 -727 881 C ATOM 13 OD1 ASP A 18 -5.805 36.941 -22.701 1.00109.71 O ANISOU 13 OD1 ASP A 18 16023 14980 10680 76 -699 990 O ATOM 14 OD2 ASP A 18 -7.329 35.922 -21.505 1.00114.72 O ANISOU 14 OD2 ASP A 18 16802 15442 11344 36 -752 875 O ATOM 15 N TYR A 19 -2.591 33.597 -23.064 1.00 88.92 N ANISOU 15 N TYR A 19 13541 12473 7772 271 -687 634 N ATOM 16 CA TYR A 19 -1.651 32.517 -22.800 1.00 88.20 C ANISOU 16 CA TYR A 19 13507 12369 7639 330 -688 512 C ATOM 17 C TYR A 19 -2.094 31.790 -21.513 1.00 88.73 C ANISOU 17 C TYR A 19 13677 12255 7780 312 -723 410 C ATOM 18 O TYR A 19 -1.287 31.284 -20.729 1.00 88.08 O ANISOU 18 O TYR A 19 13633 12104 7728 341 -721 340 O ATOM 19 CB TYR A 19 -0.212 33.032 -22.735 1.00 90.15 C ANISOU 19 CB TYR A 19 13685 12655 7912 361 -647 572 C ATOM 20 CG TYR A 19 0.517 32.919 -24.059 1.00 94.23 C ANISOU 20 CG TYR A 19 14128 13379 8297 419 -621 600 C ATOM 21 CD1 TYR A 19 -0.154 33.094 -25.267 1.00 97.42 C ANISOU 21 CD1 TYR A 19 14477 13935 8604 416 -622 652 C ATOM 22 CD2 TYR A 19 1.891 32.718 -24.103 1.00 95.75 C ANISOU 22 CD2 TYR A 19 14291 13628 8460 475 -593 592 C ATOM 23 CE1 TYR A 19 0.512 32.984 -26.488 1.00100.35 C ANISOU 23 CE1 TYR A 19 14768 14520 8839 476 -599 676 C ATOM 24 CE2 TYR A 19 2.568 32.595 -25.316 1.00 98.12 C ANISOU 24 CE2 TYR A 19 14515 14138 8628 536 -569 619 C ATOM 25 CZ TYR A 19 1.878 32.743 -26.509 1.00108.42 C ANISOU 25 CZ TYR A 19 15763 15602 9828 538 -572 661 C ATOM 26 OH TYR A 19 2.553 32.651 -27.707 1.00111.86 O ANISOU 26 OH TYR A 19 16112 16268 10123 604 -548 692 O ATOM 27 N VAL A 20 -3.424 31.722 -21.353 1.00 82.99 N ANISOU 27 N VAL A 20 12990 11466 7076 264 -757 409 N ATOM 28 CA VAL A 20 -4.166 31.005 -20.332 1.00 80.97 C ANISOU 28 CA VAL A 20 12821 11067 6876 243 -799 331 C ATOM 29 C VAL A 20 -5.297 30.238 -21.110 1.00 83.03 C ANISOU 29 C VAL A 20 13126 11366 7056 234 -844 281 C ATOM 30 O VAL A 20 -6.495 30.503 -20.936 1.00 82.06 O ANISOU 30 O VAL A 20 13021 11193 6966 184 -869 319 O ATOM 31 CB VAL A 20 -4.668 31.910 -19.159 1.00 83.55 C ANISOU 31 CB VAL A 20 13141 11272 7332 192 -799 396 C ATOM 32 CG1 VAL A 20 -5.395 31.086 -18.104 1.00 82.72 C ANISOU 32 CG1 VAL A 20 13116 11045 7270 177 -842 322 C ATOM 33 CG2 VAL A 20 -3.512 32.671 -18.509 1.00 82.93 C ANISOU 33 CG2 VAL A 20 13013 11165 7331 205 -762 437 C ATOM 34 N ASN A 21 -4.861 29.360 -22.059 1.00 78.39 N ANISOU 34 N ASN A 21 12546 10881 6358 287 -853 200 N ATOM 35 CA ASN A 21 -5.707 28.475 -22.872 1.00 77.81 C ANISOU 35 CA ASN A 21 12511 10854 6199 295 -903 124 C ATOM 36 C ASN A 21 -5.191 27.029 -22.742 1.00 80.60 C ANISOU 36 C ASN A 21 12931 11159 6533 349 -945 -30 C ATOM 37 O ASN A 21 -4.022 26.831 -22.413 1.00 80.29 O ANISOU 37 O ASN A 21 12891 11101 6515 388 -922 -66 O ATOM 38 CB ASN A 21 -5.774 28.912 -24.352 1.00 78.08 C ANISOU 38 CB ASN A 21 12474 11080 6112 315 -881 167 C ATOM 39 CG ASN A 21 -4.568 28.587 -25.213 1.00 94.75 C ANISOU 39 CG ASN A 21 14544 13336 8122 394 -855 114 C ATOM 40 OD1 ASN A 21 -4.706 28.180 -26.366 1.00 85.84 O ANISOU 40 OD1 ASN A 21 13388 12358 6870 433 -866 73 O ATOM 41 ND2 ASN A 21 -3.375 28.644 -24.659 1.00 86.74 N ANISOU 41 ND2 ASN A 21 13524 12284 7149 426 -826 103 N ATOM 42 N TYR A 22 -6.026 26.034 -23.072 1.00 76.03 N ANISOU 42 N TYR A 22 12404 10565 5918 352 -1011 -120 N ATOM 43 CA TYR A 22 -5.719 24.611 -22.897 1.00 75.23 C ANISOU 43 CA TYR A 22 12365 10395 5825 397 -1068 -267 C ATOM 44 C TYR A 22 -4.721 24.050 -23.957 1.00 76.83 C ANISOU 44 C TYR A 22 12544 10732 5915 484 -1063 -372 C ATOM 45 O TYR A 22 -4.278 22.908 -23.798 1.00 76.32 O ANISOU 45 O TYR A 22 12523 10610 5865 531 -1108 -500 O ATOM 46 CB TYR A 22 -7.021 23.793 -22.963 1.00 76.92 C ANISOU 46 CB TYR A 22 12635 10534 6058 364 -1153 -318 C ATOM 47 CG TYR A 22 -8.029 24.180 -21.898 1.00 78.35 C ANISOU 47 CG TYR A 22 12839 10588 6344 287 -1165 -224 C ATOM 48 CD1 TYR A 22 -8.024 23.567 -20.648 1.00 79.90 C ANISOU 48 CD1 TYR A 22 13078 10635 6646 273 -1201 -248 C ATOM 49 CD2 TYR A 22 -8.989 25.160 -22.140 1.00 79.02 C ANISOU 49 CD2 TYR A 22 12893 10711 6420 231 -1139 -104 C ATOM 50 CE1 TYR A 22 -8.934 23.935 -19.657 1.00 80.11 C ANISOU 50 CE1 TYR A 22 13114 10567 6756 210 -1211 -160 C ATOM 51 CE2 TYR A 22 -9.905 25.536 -21.157 1.00 79.23 C ANISOU 51 CE2 TYR A 22 12935 10632 6537 169 -1149 -22 C ATOM 52 CZ TYR A 22 -9.883 24.909 -19.921 1.00 86.92 C ANISOU 52 CZ TYR A 22 13952 11472 7604 161 -1186 -52 C ATOM 53 OH TYR A 22 -10.783 25.273 -18.947 1.00 88.04 O ANISOU 53 OH TYR A 22 14099 11529 7822 108 -1196 29 O ATOM 54 N ASP A 23 -4.333 24.839 -24.982 1.00 72.11 N ANISOU 54 N ASP A 23 11872 10314 5213 510 -1010 -314 N ATOM 55 CA ASP A 23 -3.427 24.349 -26.033 1.00 72.49 C ANISOU 55 CA ASP A 23 11885 10521 5137 601 -1004 -408 C ATOM 56 C ASP A 23 -1.945 24.355 -25.588 1.00 73.05 C ANISOU 56 C ASP A 23 11935 10599 5222 652 -955 -415 C ATOM 57 O ASP A 23 -1.175 23.518 -26.065 1.00 73.26 O ANISOU 57 O ASP A 23 11965 10692 5180 733 -969 -536 O ATOM 58 CB ASP A 23 -3.562 25.188 -27.315 1.00 75.77 C ANISOU 58 CB ASP A 23 12212 11151 5426 611 -968 -329 C ATOM 59 CG ASP A 23 -2.812 24.635 -28.524 1.00 90.85 C ANISOU 59 CG ASP A 23 14078 13258 7184 711 -969 -432 C ATOM 60 OD1 ASP A 23 -2.665 23.390 -28.618 1.00 92.54 O ANISOU 60 OD1 ASP A 23 14347 13434 7379 769 -1029 -605 O ATOM 61 OD2 ASP A 23 -2.475 25.431 -29.426 1.00 97.97 O ANISOU 61 OD2 ASP A 23 14883 14358 7984 733 -918 -342 O ATOM 62 N ILE A 24 -1.542 25.309 -24.721 1.00 66.69 N ANISOU 62 N ILE A 24 11105 9731 4502 608 -899 -289 N ATOM 63 CA ILE A 24 -0.164 25.436 -24.206 1.00 65.46 C ANISOU 63 CA ILE A 24 10929 9573 4372 645 -851 -278 C ATOM 64 C ILE A 24 0.254 24.119 -23.492 1.00 68.02 C ANISOU 64 C ILE A 24 11329 9767 4749 680 -894 -421 C ATOM 65 O ILE A 24 1.344 23.611 -23.761 1.00 68.23 O ANISOU 65 O ILE A 24 11345 9852 4728 753 -879 -491 O ATOM 66 CB ILE A 24 -0.050 26.669 -23.259 1.00 67.33 C ANISOU 66 CB ILE A 24 11133 9734 4716 581 -802 -127 C ATOM 67 CG1 ILE A 24 -0.194 27.968 -24.076 1.00 67.84 C ANISOU 67 CG1 ILE A 24 11100 9944 4732 561 -758 19 C ATOM 68 CG2 ILE A 24 1.282 26.672 -22.477 1.00 67.86 C ANISOU 68 CG2 ILE A 24 11195 9754 4835 610 -765 -127 C ATOM 69 CD1 ILE A 24 -0.280 29.219 -23.285 1.00 72.97 C ANISOU 69 CD1 ILE A 24 11710 10520 5494 497 -724 161 C ATOM 70 N ILE A 25 -0.632 23.563 -22.633 1.00 62.66 N ANISOU 70 N ILE A 25 10719 8921 4166 631 -950 -458 N ATOM 71 CA ILE A 25 -0.422 22.311 -21.896 1.00 61.59 C ANISOU 71 CA ILE A 25 10649 8650 4103 651 -1003 -575 C ATOM 72 C ILE A 25 -0.084 21.180 -22.881 1.00 65.16 C ANISOU 72 C ILE A 25 11113 9177 4468 736 -1050 -733 C ATOM 73 O ILE A 25 0.907 20.485 -22.677 1.00 64.55 O ANISOU 73 O ILE A 25 11046 9079 4401 793 -1050 -816 O ATOM 74 CB ILE A 25 -1.680 21.968 -21.045 1.00 64.10 C ANISOU 74 CB ILE A 25 11021 8809 4526 580 -1064 -564 C ATOM 75 CG1 ILE A 25 -2.137 23.162 -20.169 1.00 63.38 C ANISOU 75 CG1 ILE A 25 10911 8662 4509 504 -1021 -418 C ATOM 76 CG2 ILE A 25 -1.500 20.675 -20.226 1.00 65.25 C ANISOU 76 CG2 ILE A 25 11219 8811 4761 595 -1126 -667 C ATOM 77 CD1 ILE A 25 -1.120 23.695 -19.151 1.00 69.74 C ANISOU 77 CD1 ILE A 25 11698 9419 5381 504 -964 -367 C ATOM 78 N VAL A 26 -0.875 21.039 -23.970 1.00 61.91 N ANISOU 78 N VAL A 26 10694 8859 3969 747 -1088 -775 N ATOM 79 CA VAL A 26 -0.676 20.027 -25.018 1.00 62.55 C ANISOU 79 CA VAL A 26 10778 9030 3957 833 -1141 -937 C ATOM 80 C VAL A 26 0.702 20.241 -25.675 1.00 67.36 C ANISOU 80 C VAL A 26 11328 9810 4456 921 -1078 -955 C ATOM 81 O VAL A 26 1.497 19.308 -25.717 1.00 67.28 O ANISOU 81 O VAL A 26 11333 9795 4435 997 -1103 -1087 O ATOM 82 CB VAL A 26 -1.820 20.054 -26.071 1.00 66.56 C ANISOU 82 CB VAL A 26 11278 9631 4383 823 -1185 -958 C ATOM 83 CG1 VAL A 26 -1.545 19.085 -27.212 1.00 67.85 C ANISOU 83 CG1 VAL A 26 11431 9914 4433 923 -1237 -1133 C ATOM 84 CG2 VAL A 26 -3.172 19.749 -25.428 1.00 65.63 C ANISOU 84 CG2 VAL A 26 11220 9342 4374 741 -1255 -943 C ATOM 85 N ARG A 27 0.984 21.482 -26.120 1.00 64.89 N ANISOU 85 N ARG A 27 10942 9640 4074 907 -998 -813 N ATOM 86 CA ARG A 27 2.223 21.933 -26.773 1.00 66.01 C ANISOU 86 CA ARG A 27 11006 9966 4108 979 -930 -781 C ATOM 87 C ARG A 27 3.490 21.630 -25.920 1.00 70.25 C ANISOU 87 C ARG A 27 11560 10423 4710 1012 -901 -803 C ATOM 88 O ARG A 27 4.496 21.159 -26.461 1.00 70.54 O ANISOU 88 O ARG A 27 11569 10571 4661 1105 -889 -885 O ATOM 89 CB ARG A 27 2.121 23.454 -27.022 1.00 66.53 C ANISOU 89 CB ARG A 27 10991 10137 4150 926 -860 -581 C ATOM 90 CG ARG A 27 3.335 24.101 -27.687 1.00 79.21 C ANISOU 90 CG ARG A 27 12499 11940 5658 986 -789 -503 C ATOM 91 CD ARG A 27 3.224 25.618 -27.680 1.00 91.19 C ANISOU 91 CD ARG A 27 13936 13512 7200 919 -730 -290 C ATOM 92 NE ARG A 27 2.125 26.119 -28.509 1.00100.56 N ANISOU 92 NE ARG A 27 15080 14804 8325 885 -741 -231 N ATOM 93 CZ ARG A 27 1.749 27.394 -28.557 1.00113.11 C ANISOU 93 CZ ARG A 27 16600 16429 9948 818 -704 -52 C ATOM 94 NH1 ARG A 27 2.338 28.297 -27.781 1.00100.13 N ANISOU 94 NH1 ARG A 27 14925 14709 8409 776 -661 79 N ATOM 95 NH2 ARG A 27 0.750 27.767 -29.346 1.00 97.18 N ANISOU 95 NH2 ARG A 27 14543 14511 7869 790 -716 -3 N ATOM 96 N HIS A 28 3.438 21.940 -24.605 1.00 65.92 N ANISOU 96 N HIS A 28 11048 9694 4303 938 -886 -726 N ATOM 97 CA HIS A 28 4.552 21.769 -23.666 1.00 65.20 C ANISOU 97 CA HIS A 28 10971 9519 4285 954 -854 -725 C ATOM 98 C HIS A 28 4.685 20.306 -23.228 1.00 70.34 C ANISOU 98 C HIS A 28 11690 10046 4990 994 -919 -890 C ATOM 99 O HIS A 28 5.809 19.857 -23.003 1.00 70.11 O ANISOU 99 O HIS A 28 11658 10024 4958 1052 -899 -941 O ATOM 100 CB HIS A 28 4.375 22.686 -22.446 1.00 64.28 C ANISOU 100 CB HIS A 28 10861 9268 4295 862 -820 -588 C ATOM 101 CG HIS A 28 4.758 24.104 -22.748 1.00 67.12 C ANISOU 101 CG HIS A 28 11140 9739 4624 841 -750 -428 C ATOM 102 ND1 HIS A 28 4.019 24.888 -23.622 1.00 69.02 N ANISOU 102 ND1 HIS A 28 11328 10100 4798 819 -742 -348 N ATOM 103 CD2 HIS A 28 5.805 24.826 -22.300 1.00 67.91 C ANISOU 103 CD2 HIS A 28 11198 9845 4761 839 -691 -334 C ATOM 104 CE1 HIS A 28 4.653 26.045 -23.688 1.00 67.93 C ANISOU 104 CE1 HIS A 28 11113 10033 4663 806 -682 -205 C ATOM 105 NE2 HIS A 28 5.731 26.055 -22.907 1.00 67.76 N ANISOU 105 NE2 HIS A 28 11097 9943 4704 817 -652 -194 N ATOM 106 N TYR A 29 3.573 19.548 -23.161 1.00 67.97 N ANISOU 106 N TYR A 29 11445 9640 4741 966 -1000 -970 N ATOM 107 CA TYR A 29 3.646 18.116 -22.851 1.00 68.57 C ANISOU 107 CA TYR A 29 11575 9597 4883 1004 -1077 -1126 C ATOM 108 C TYR A 29 3.948 17.325 -24.143 1.00 74.00 C ANISOU 108 C TYR A 29 12246 10421 5449 1110 -1117 -1285 C ATOM 109 O TYR A 29 4.103 16.106 -24.095 1.00 74.33 O ANISOU 109 O TYR A 29 12323 10382 5537 1160 -1186 -1435 O ATOM 110 CB TYR A 29 2.364 17.606 -22.163 1.00 69.34 C ANISOU 110 CB TYR A 29 11727 9518 5100 930 -1157 -1136 C ATOM 111 CG TYR A 29 2.338 17.844 -20.665 1.00 69.57 C ANISOU 111 CG TYR A 29 11777 9387 5269 854 -1139 -1036 C ATOM 112 CD1 TYR A 29 2.711 16.842 -19.774 1.00 71.27 C ANISOU 112 CD1 TYR A 29 12024 9457 5599 859 -1182 -1099 C ATOM 113 CD2 TYR A 29 1.967 19.080 -20.139 1.00 69.15 C ANISOU 113 CD2 TYR A 29 11703 9336 5233 782 -1080 -881 C ATOM 114 CE1 TYR A 29 2.680 17.050 -18.397 1.00 70.69 C ANISOU 114 CE1 TYR A 29 11959 9258 5644 793 -1165 -1005 C ATOM 115 CE2 TYR A 29 1.942 19.303 -18.762 1.00 68.72 C ANISOU 115 CE2 TYR A 29 11661 9152 5297 721 -1066 -802 C ATOM 116 CZ TYR A 29 2.300 18.284 -17.896 1.00 75.35 C ANISOU 116 CZ TYR A 29 12530 9863 6238 727 -1107 -862 C ATOM 117 OH TYR A 29 2.285 18.492 -16.541 1.00 75.13 O ANISOU 117 OH TYR A 29 12503 9728 6316 672 -1092 -783 O ATOM 118 N ASN A 30 4.095 18.040 -25.273 1.00 71.28 N ANISOU 118 N ASN A 30 11841 10289 4953 1148 -1073 -1251 N ATOM 119 CA ASN A 30 4.445 17.483 -26.576 1.00 73.01 C ANISOU 119 CA ASN A 30 12026 10687 5027 1258 -1099 -1390 C ATOM 120 C ASN A 30 5.954 17.567 -26.782 1.00 77.97 C ANISOU 120 C ASN A 30 12606 11440 5579 1344 -1033 -1397 C ATOM 121 O ASN A 30 6.589 16.559 -27.104 1.00 78.37 O ANISOU 121 O ASN A 30 12664 11514 5599 1439 -1071 -1558 O ATOM 122 CB ASN A 30 3.690 18.237 -27.680 1.00 74.89 C ANISOU 122 CB ASN A 30 12212 11107 5137 1249 -1086 -1332 C ATOM 123 CG ASN A 30 3.880 17.755 -29.098 1.00 98.13 C ANISOU 123 CG ASN A 30 15108 14266 7912 1360 -1114 -1470 C ATOM 124 OD1 ASN A 30 4.358 16.645 -29.372 1.00 90.09 O ANISOU 124 OD1 ASN A 30 14108 13244 6876 1451 -1170 -1654 O ATOM 125 ND2 ASN A 30 3.456 18.592 -30.031 1.00 92.67 N ANISOU 125 ND2 ASN A 30 14347 13767 7095 1355 -1080 -1383 N ATOM 126 N TYR A 31 6.527 18.775 -26.566 1.00 74.59 N ANISOU 126 N TYR A 31 12125 11086 5130 1311 -940 -1219 N ATOM 127 CA TYR A 31 7.953 19.071 -26.718 1.00 75.22 C ANISOU 127 CA TYR A 31 12149 11293 5141 1379 -869 -1181 C ATOM 128 C TYR A 31 8.796 18.195 -25.774 1.00 80.46 C ANISOU 128 C TYR A 31 12865 11801 5906 1405 -881 -1266 C ATOM 129 O TYR A 31 9.894 17.788 -26.156 1.00 80.97 O ANISOU 129 O TYR A 31 12901 11968 5896 1502 -862 -1337 O ATOM 130 CB TYR A 31 8.224 20.567 -26.451 1.00 75.49 C ANISOU 130 CB TYR A 31 12122 11378 5182 1312 -782 -957 C ATOM 131 CG TYR A 31 9.657 20.991 -26.708 1.00 77.53 C ANISOU 131 CG TYR A 31 12310 11783 5367 1377 -710 -891 C ATOM 132 CD1 TYR A 31 10.062 21.420 -27.968 1.00 80.64 C ANISOU 132 CD1 TYR A 31 12605 12443 5593 1449 -676 -851 C ATOM 133 CD2 TYR A 31 10.600 20.993 -25.684 1.00 77.55 C ANISOU 133 CD2 TYR A 31 12335 11667 5465 1365 -676 -855 C ATOM 134 CE1 TYR A 31 11.378 21.810 -28.210 1.00 81.91 C ANISOU 134 CE1 TYR A 31 12693 12746 5684 1510 -612 -776 C ATOM 135 CE2 TYR A 31 11.919 21.373 -25.916 1.00 78.82 C ANISOU 135 CE2 TYR A 31 12430 11960 5559 1423 -612 -788 C ATOM 136 CZ TYR A 31 12.303 21.789 -27.179 1.00 87.76 C ANISOU 136 CZ TYR A 31 13464 13354 6526 1495 -581 -744 C ATOM 137 OH TYR A 31 13.603 22.171 -27.408 1.00 89.79 O ANISOU 137 OH TYR A 31 13649 13749 6718 1553 -521 -663 O ATOM 138 N THR A 32 8.292 17.919 -24.547 1.00 77.18 N ANISOU 138 N THR A 32 12518 11150 5656 1322 -912 -1252 N ATOM 139 CA THR A 32 8.989 17.068 -23.576 1.00 77.15 C ANISOU 139 CA THR A 32 12560 10989 5766 1334 -928 -1320 C ATOM 140 C THR A 32 8.898 15.618 -24.060 1.00 84.56 C ANISOU 140 C THR A 32 13531 11894 6703 1414 -1019 -1532 C ATOM 141 O THR A 32 9.927 14.968 -24.202 1.00 85.35 O ANISOU 141 O THR A 32 13624 12022 6783 1499 -1017 -1628 O ATOM 142 CB THR A 32 8.439 17.247 -22.148 1.00 79.93 C ANISOU 142 CB THR A 32 12959 11126 6286 1222 -934 -1230 C ATOM 143 OG1 THR A 32 7.054 16.907 -22.122 1.00 78.44 O ANISOU 143 OG1 THR A 32 12809 10844 6150 1169 -1009 -1263 O ATOM 144 CG2 THR A 32 8.646 18.658 -21.611 1.00 76.09 C ANISOU 144 CG2 THR A 32 12436 10662 5812 1153 -850 -1039 C ATOM 145 N GLY A 33 7.687 15.166 -24.392 1.00 82.67 N ANISOU 145 N GLY A 33 13321 11606 6482 1391 -1101 -1605 N ATOM 146 CA GLY A 33 7.452 13.828 -24.921 1.00 84.33 C ANISOU 146 CA GLY A 33 13560 11778 6704 1463 -1204 -1812 C ATOM 147 C GLY A 33 6.498 12.966 -24.121 1.00 89.88 C ANISOU 147 C GLY A 33 14325 12240 7585 1397 -1301 -1859 C ATOM 148 O GLY A 33 6.405 11.763 -24.382 1.00 90.62 O ANISOU 148 O GLY A 33 14441 12258 7734 1454 -1395 -2029 O ATOM 149 N LYS A 34 5.763 13.561 -23.151 1.00 86.64 N ANISOU 149 N LYS A 34 13937 11711 7272 1280 -1286 -1710 N ATOM 150 CA LYS A 34 4.809 12.807 -22.326 1.00 86.73 C ANISOU 150 CA LYS A 34 13996 11505 7452 1210 -1376 -1725 C ATOM 151 C LYS A 34 3.346 13.031 -22.827 1.00 91.85 C ANISOU 151 C LYS A 34 14660 12156 8083 1158 -1435 -1715 C ATOM 152 O LYS A 34 2.403 12.984 -22.027 1.00 90.90 O ANISOU 152 O LYS A 34 14569 11883 8087 1074 -1485 -1656 O ATOM 153 CB LYS A 34 4.936 13.202 -20.838 1.00 87.98 C ANISOU 153 CB LYS A 34 14165 11532 7732 1120 -1327 -1572 C ATOM 154 CG LYS A 34 4.407 12.111 -19.891 1.00106.03 C ANISOU 154 CG LYS A 34 16483 13602 10203 1078 -1419 -1604 C ATOM 155 CD LYS A 34 4.068 12.586 -18.473 1.00116.12 C ANISOU 155 CD LYS A 34 17764 14765 11590 973 -1389 -1441 C ATOM 156 CE LYS A 34 2.788 13.395 -18.419 1.00125.40 C ANISOU 156 CE LYS A 34 18949 15942 12757 894 -1402 -1347 C ATOM 157 NZ LYS A 34 2.414 13.752 -17.026 1.00132.19 N ANISOU 157 NZ LYS A 34 19807 16699 13720 803 -1380 -1203 N ATOM 158 N LEU A 35 3.162 13.258 -24.149 1.00 89.92 N ANISOU 158 N LEU A 35 14388 12094 7683 1211 -1430 -1769 N ATOM 159 CA LEU A 35 1.831 13.482 -24.731 1.00 90.26 C ANISOU 159 CA LEU A 35 14440 12163 7692 1168 -1479 -1760 C ATOM 160 C LEU A 35 1.209 12.142 -25.173 1.00 97.57 C ANISOU 160 C LEU A 35 15395 13001 8675 1208 -1618 -1945 C ATOM 161 O LEU A 35 0.104 11.799 -24.739 1.00 96.60 O ANISOU 161 O LEU A 35 15307 12732 8665 1136 -1695 -1925 O ATOM 162 CB LEU A 35 1.913 14.465 -25.922 1.00 90.46 C ANISOU 162 CB LEU A 35 14410 12437 7524 1204 -1409 -1720 C ATOM 163 CG LEU A 35 0.588 14.898 -26.565 1.00 94.72 C ANISOU 163 CG LEU A 35 14947 13034 8009 1155 -1440 -1684 C ATOM 164 CD1 LEU A 35 -0.239 15.743 -25.612 1.00 93.10 C ANISOU 164 CD1 LEU A 35 14760 12719 7894 1030 -1408 -1499 C ATOM 165 CD2 LEU A 35 0.840 15.695 -27.817 1.00 97.90 C ANISOU 165 CD2 LEU A 35 15281 13701 8217 1209 -1377 -1663 C ATOM 166 N ASN A 36 1.923 11.398 -26.037 1.00 97.49 N ANISOU 166 N ASN A 36 15367 13085 8589 1326 -1653 -2126 N ATOM 167 CA ASN A 36 1.487 10.099 -26.552 1.00 99.45 C ANISOU 167 CA ASN A 36 15636 13260 8891 1382 -1791 -2329 C ATOM 168 C ASN A 36 1.836 8.993 -25.557 1.00105.36 C ANISOU 168 C ASN A 36 16415 13782 9837 1381 -1864 -2393 C ATOM 169 O ASN A 36 1.065 8.044 -25.397 1.00105.76 O ANISOU 169 O ASN A 36 16491 13675 10020 1367 -1993 -2484 O ATOM 170 CB ASN A 36 2.132 9.826 -27.916 1.00101.32 C ANISOU 170 CB ASN A 36 15832 13711 8955 1519 -1797 -2503 C ATOM 171 CG ASN A 36 1.806 10.853 -28.982 1.00124.44 C ANISOU 171 CG ASN A 36 18714 16885 11683 1527 -1732 -2441 C ATOM 172 OD1 ASN A 36 0.813 11.590 -28.908 1.00117.11 O ANISOU 172 OD1 ASN A 36 17793 15950 10753 1434 -1719 -2312 O ATOM 173 ND2 ASN A 36 2.612 10.885 -30.031 1.00118.42 N ANISOU 173 ND2 ASN A 36 17895 16352 10746 1644 -1696 -2534 N ATOM 174 N ILE A 37 2.988 9.132 -24.874 1.00102.44 N ANISOU 174 N ILE A 37 16035 13393 9494 1393 -1785 -2335 N ATOM 175 CA ILE A 37 3.463 8.173 -23.877 1.00102.77 C ANISOU 175 CA ILE A 37 16093 13236 9717 1391 -1837 -2372 C ATOM 176 C ILE A 37 2.633 8.376 -22.576 1.00106.82 C ANISOU 176 C ILE A 37 16630 13566 10391 1257 -1848 -2201 C ATOM 177 O ILE A 37 3.001 9.185 -21.713 1.00105.23 O ANISOU 177 O ILE A 37 16423 13364 10197 1198 -1748 -2040 O ATOM 178 CB ILE A 37 5.007 8.331 -23.653 1.00105.68 C ANISOU 178 CB ILE A 37 16438 13679 10036 1456 -1740 -2368 C ATOM 179 CG1 ILE A 37 5.808 8.429 -24.991 1.00107.22 C ANISOU 179 CG1 ILE A 37 16597 14110 10033 1587 -1705 -2499 C ATOM 180 CG2 ILE A 37 5.577 7.263 -22.699 1.00106.61 C ANISOU 180 CG2 ILE A 37 16566 13601 10340 1461 -1792 -2415 C ATOM 181 CD1 ILE A 37 5.705 7.208 -25.989 1.00116.10 C ANISOU 181 CD1 ILE A 37 17718 15242 11151 1700 -1833 -2756 C ATOM 182 N SER A 38 1.484 7.664 -22.478 1.00104.48 N ANISOU 182 N SER A 38 16354 13126 10217 1212 -1972 -2237 N ATOM 183 CA SER A 38 0.572 7.727 -21.327 1.00103.47 C ANISOU 183 CA SER A 38 16240 12835 10240 1093 -2001 -2082 C ATOM 184 C SER A 38 0.039 6.326 -20.967 1.00108.63 C ANISOU 184 C SER A 38 16898 13278 11097 1085 -2159 -2168 C ATOM 185 O SER A 38 -0.370 5.571 -21.859 1.00109.77 O ANISOU 185 O SER A 38 17049 13408 11250 1136 -2269 -2327 O ATOM 186 CB SER A 38 -0.591 8.673 -21.611 1.00106.41 C ANISOU 186 CB SER A 38 16622 13275 10534 1020 -1978 -1970 C ATOM 187 OG SER A 38 -0.136 9.994 -21.856 1.00114.43 O ANISOU 187 OG SER A 38 17624 14463 11391 1016 -1838 -1868 O ATOM 188 N ALA A 39 0.055 5.985 -19.656 1.00104.27 N ANISOU 188 N ALA A 39 16336 12569 10714 1020 -2172 -2059 N ATOM 189 CA ALA A 39 -0.392 4.691 -19.126 1.00126.28 C ANISOU 189 CA ALA A 39 19112 15148 13722 1000 -2318 -2099 C ATOM 190 C ALA A 39 -1.915 4.591 -19.123 1.00139.46 C ANISOU 190 C ALA A 39 20790 16737 15462 921 -2416 -2037 C ATOM 191 O ALA A 39 -2.460 3.490 -19.144 1.00 97.32 O ANISOU 191 O ALA A 39 15442 11246 10287 918 -2565 -2106 O ATOM 192 CB ALA A 39 0.144 4.493 -17.717 1.00126.11 C ANISOU 192 CB ALA A 39 19063 15017 13837 952 -2286 -1973 C ATOM 193 N LEU A 47 -6.140 3.699 -11.369 1.00 81.95 N ANISOU 193 N LEU A 47 13249 8843 9046 351 -2641 -893 N ATOM 194 CA LEU A 47 -6.093 2.508 -10.518 1.00 82.39 C ANISOU 194 CA LEU A 47 13228 8751 9327 325 -2752 -827 C ATOM 195 C LEU A 47 -5.085 2.689 -9.376 1.00 85.14 C ANISOU 195 C LEU A 47 13527 9131 9690 322 -2653 -739 C ATOM 196 O LEU A 47 -5.389 2.345 -8.229 1.00 84.52 O ANISOU 196 O LEU A 47 13370 9010 9734 266 -2686 -575 O ATOM 197 CB LEU A 47 -5.734 1.263 -11.344 1.00 84.05 C ANISOU 197 CB LEU A 47 13441 8824 9670 384 -2887 -1009 C ATOM 198 N THR A 48 -3.887 3.222 -9.693 1.00 80.70 N ANISOU 198 N THR A 48 13006 8654 9002 384 -2535 -843 N ATOM 199 CA THR A 48 -2.825 3.467 -8.712 1.00 79.31 C ANISOU 199 CA THR A 48 12793 8519 8821 388 -2432 -777 C ATOM 200 C THR A 48 -3.117 4.732 -7.915 1.00 80.69 C ANISOU 200 C THR A 48 12960 8825 8875 338 -2311 -622 C ATOM 201 O THR A 48 -2.743 4.814 -6.748 1.00 79.53 O ANISOU 201 O THR A 48 12753 8697 8769 311 -2263 -505 O ATOM 202 CB THR A 48 -1.448 3.575 -9.399 1.00 87.29 C ANISOU 202 CB THR A 48 13850 9577 9739 474 -2353 -942 C ATOM 203 OG1 THR A 48 -1.471 4.640 -10.351 1.00 85.22 O ANISOU 203 OG1 THR A 48 13661 9446 9274 505 -2267 -1015 O ATOM 204 CG2 THR A 48 -1.021 2.275 -10.081 1.00 88.61 C ANISOU 204 CG2 THR A 48 14015 9617 10037 534 -2471 -1104 C ATOM 205 N SER A 49 -3.789 5.714 -8.550 1.00 76.07 N ANISOU 205 N SER A 49 12429 8331 8144 328 -2266 -625 N ATOM 206 CA SER A 49 -4.114 7.014 -7.971 1.00 74.17 C ANISOU 206 CA SER A 49 12187 8214 7780 290 -2156 -503 C ATOM 207 C SER A 49 -5.022 6.883 -6.737 1.00 77.00 C ANISOU 207 C SER A 49 12468 8553 8234 218 -2201 -315 C ATOM 208 O SER A 49 -4.604 7.296 -5.654 1.00 76.02 O ANISOU 208 O SER A 49 12295 8487 8102 202 -2128 -215 O ATOM 209 CB SER A 49 -4.786 7.910 -9.007 1.00 77.09 C ANISOU 209 CB SER A 49 12624 8665 8003 293 -2124 -548 C ATOM 210 OG SER A 49 -3.902 8.212 -10.074 1.00 84.59 O ANISOU 210 OG SER A 49 13630 9670 8838 360 -2064 -698 O ATOM 211 N VAL A 50 -6.225 6.275 -6.881 1.00 73.31 N ANISOU 211 N VAL A 50 11984 8011 7861 179 -2325 -266 N ATOM 212 CA VAL A 50 -7.221 6.120 -5.800 1.00 72.58 C ANISOU 212 CA VAL A 50 11811 7912 7855 112 -2379 -75 C ATOM 213 C VAL A 50 -6.572 5.531 -4.520 1.00 75.57 C ANISOU 213 C VAL A 50 12093 8268 8352 100 -2381 25 C ATOM 214 O VAL A 50 -7.063 5.797 -3.420 1.00 74.38 O ANISOU 214 O VAL A 50 11868 8182 8210 58 -2364 189 O ATOM 215 CB VAL A 50 -8.438 5.258 -6.218 1.00 77.45 C ANISOU 215 CB VAL A 50 12414 8422 8592 77 -2537 -47 C ATOM 216 CG1 VAL A 50 -9.303 5.992 -7.240 1.00 77.15 C ANISOU 216 CG1 VAL A 50 12454 8434 8426 73 -2527 -96 C ATOM 217 CG2 VAL A 50 -8.019 3.877 -6.731 1.00 78.58 C ANISOU 217 CG2 VAL A 50 12548 8408 8900 106 -2662 -160 C ATOM 218 N VAL A 51 -5.463 4.778 -4.671 1.00 72.47 N ANISOU 218 N VAL A 51 11698 7798 8041 141 -2397 -75 N ATOM 219 CA VAL A 51 -4.710 4.196 -3.559 1.00 72.22 C ANISOU 219 CA VAL A 51 11576 7742 8121 134 -2393 5 C ATOM 220 C VAL A 51 -3.989 5.334 -2.808 1.00 75.66 C ANISOU 220 C VAL A 51 12008 8325 8416 142 -2235 50 C ATOM 221 O VAL A 51 -4.159 5.448 -1.596 1.00 74.53 O ANISOU 221 O VAL A 51 11776 8239 8302 106 -2216 203 O ATOM 222 CB VAL A 51 -3.721 3.094 -4.037 1.00 76.69 C ANISOU 222 CB VAL A 51 12148 8182 8809 181 -2453 -130 C ATOM 223 CG1 VAL A 51 -2.925 2.517 -2.870 1.00 76.40 C ANISOU 223 CG1 VAL A 51 12014 8124 8890 171 -2443 -37 C ATOM 224 CG2 VAL A 51 -4.451 1.984 -4.787 1.00 77.74 C ANISOU 224 CG2 VAL A 51 12281 8163 9094 177 -2622 -186 C ATOM 225 N PHE A 52 -3.227 6.194 -3.538 1.00 72.54 N ANISOU 225 N PHE A 52 11701 7995 7866 189 -2125 -79 N ATOM 226 CA PHE A 52 -2.487 7.323 -2.954 1.00 71.43 C ANISOU 226 CA PHE A 52 11562 7982 7597 200 -1981 -53 C ATOM 227 C PHE A 52 -3.434 8.388 -2.422 1.00 72.77 C ANISOU 227 C PHE A 52 11716 8261 7673 162 -1936 61 C ATOM 228 O PHE A 52 -3.142 8.971 -1.381 1.00 71.40 O ANISOU 228 O PHE A 52 11489 8175 7465 151 -1864 147 O ATOM 229 CB PHE A 52 -1.518 7.962 -3.960 1.00 73.47 C ANISOU 229 CB PHE A 52 11911 8280 7724 259 -1889 -207 C ATOM 230 CG PHE A 52 -0.419 7.049 -4.443 1.00 76.37 C ANISOU 230 CG PHE A 52 12293 8567 8158 310 -1911 -328 C ATOM 231 CD1 PHE A 52 0.676 6.766 -3.635 1.00 79.71 C ANISOU 231 CD1 PHE A 52 12665 8987 8633 320 -1867 -301 C ATOM 232 CD2 PHE A 52 -0.426 6.554 -5.740 1.00 80.09 C ANISOU 232 CD2 PHE A 52 12827 8979 8624 354 -1967 -477 C ATOM 233 CE1 PHE A 52 1.691 5.917 -4.080 1.00 81.67 C ANISOU 233 CE1 PHE A 52 12924 9160 8945 370 -1887 -412 C ATOM 234 CE2 PHE A 52 0.603 5.728 -6.195 1.00 84.06 C ANISOU 234 CE2 PHE A 52 13340 9415 9183 411 -1987 -600 C ATOM 235 CZ PHE A 52 1.661 5.422 -5.364 1.00 82.07 C ANISOU 235 CZ PHE A 52 13039 9152 8993 418 -1946 -565 C ATOM 236 N ILE A 53 -4.571 8.626 -3.112 1.00 68.78 N ANISOU 236 N ILE A 53 11253 7752 7129 143 -1982 59 N ATOM 237 CA ILE A 53 -5.600 9.581 -2.681 1.00 67.89 C ANISOU 237 CA ILE A 53 11125 7734 6934 108 -1951 166 C ATOM 238 C ILE A 53 -6.008 9.244 -1.238 1.00 71.36 C ANISOU 238 C ILE A 53 11449 8206 7459 70 -1984 335 C ATOM 239 O ILE A 53 -6.129 10.144 -0.408 1.00 70.29 O ANISOU 239 O ILE A 53 11276 8186 7245 62 -1911 413 O ATOM 240 CB ILE A 53 -6.823 9.573 -3.653 1.00 71.51 C ANISOU 240 CB ILE A 53 11636 8160 7376 89 -2023 148 C ATOM 241 CG1 ILE A 53 -6.397 9.985 -5.088 1.00 72.15 C ANISOU 241 CG1 ILE A 53 11821 8240 7355 132 -1982 -16 C ATOM 242 CG2 ILE A 53 -7.950 10.488 -3.136 1.00 71.81 C ANISOU 242 CG2 ILE A 53 11650 8293 7342 52 -2000 271 C ATOM 243 CD1 ILE A 53 -7.496 9.903 -6.193 1.00 80.83 C ANISOU 243 CD1 ILE A 53 12974 9306 8432 119 -2055 -55 C ATOM 244 N LEU A 54 -6.141 7.938 -0.943 1.00 68.53 N ANISOU 244 N LEU A 54 11027 7748 7263 50 -2096 387 N ATOM 245 CA LEU A 54 -6.499 7.394 0.365 1.00 68.39 C ANISOU 245 CA LEU A 54 10882 7753 7350 13 -2147 561 C ATOM 246 C LEU A 54 -5.302 7.473 1.346 1.00 71.36 C ANISOU 246 C LEU A 54 11197 8189 7728 31 -2067 584 C ATOM 247 O LEU A 54 -5.519 7.716 2.532 1.00 70.43 O ANISOU 247 O LEU A 54 10981 8174 7606 11 -2047 721 O ATOM 248 CB LEU A 54 -6.962 5.933 0.182 1.00 69.65 C ANISOU 248 CB LEU A 54 10996 7766 7702 -12 -2304 598 C ATOM 249 CG LEU A 54 -7.536 5.194 1.386 1.00 74.90 C ANISOU 249 CG LEU A 54 11516 8440 8503 -59 -2389 800 C ATOM 250 CD1 LEU A 54 -8.824 5.854 1.883 1.00 74.62 C ANISOU 250 CD1 LEU A 54 11440 8517 8395 -92 -2393 942 C ATOM 251 CD2 LEU A 54 -7.825 3.756 1.027 1.00 79.13 C ANISOU 251 CD2 LEU A 54 12016 8804 9246 -79 -2547 811 C ATOM 252 N ILE A 55 -4.049 7.276 0.847 1.00 67.74 N ANISOU 252 N ILE A 55 10791 7676 7270 71 -2022 450 N ATOM 253 CA ILE A 55 -2.810 7.340 1.651 1.00 66.94 C ANISOU 253 CA ILE A 55 10644 7623 7168 89 -1942 457 C ATOM 254 C ILE A 55 -2.589 8.784 2.125 1.00 70.71 C ANISOU 254 C ILE A 55 11135 8252 7480 102 -1813 463 C ATOM 255 O ILE A 55 -2.117 8.986 3.239 1.00 69.85 O ANISOU 255 O ILE A 55 10947 8229 7365 99 -1762 539 O ATOM 256 CB ILE A 55 -1.568 6.805 0.864 1.00 70.04 C ANISOU 256 CB ILE A 55 11097 7917 7596 133 -1929 306 C ATOM 257 CG1 ILE A 55 -1.778 5.333 0.424 1.00 71.54 C ANISOU 257 CG1 ILE A 55 11266 7947 7969 127 -2070 288 C ATOM 258 CG2 ILE A 55 -0.278 6.941 1.697 1.00 69.63 C ANISOU 258 CG2 ILE A 55 11001 7922 7535 151 -1839 319 C ATOM 259 CD1 ILE A 55 -0.701 4.737 -0.532 1.00 78.02 C ANISOU 259 CD1 ILE A 55 12154 8665 8827 180 -2075 116 C ATOM 260 N CYS A 56 -2.950 9.777 1.293 1.00 68.27 N ANISOU 260 N CYS A 56 10918 7976 7045 115 -1766 387 N ATOM 261 CA CYS A 56 -2.821 11.197 1.627 1.00 68.01 C ANISOU 261 CA CYS A 56 10900 8070 6870 127 -1656 384 C ATOM 262 C CYS A 56 -3.792 11.569 2.754 1.00 72.32 C ANISOU 262 C CYS A 56 11352 8722 7402 98 -1668 531 C ATOM 263 O CYS A 56 -3.448 12.418 3.570 1.00 71.41 O ANISOU 263 O CYS A 56 11197 8719 7215 110 -1590 555 O ATOM 264 CB CYS A 56 -3.049 12.069 0.399 1.00 68.45 C ANISOU 264 CB CYS A 56 11066 8125 6817 144 -1618 280 C ATOM 265 SG CYS A 56 -1.842 11.817 -0.927 1.00 72.87 S ANISOU 265 SG CYS A 56 11725 8606 7357 191 -1588 109 S ATOM 266 N CYS A 57 -4.982 10.916 2.817 1.00 70.01 N ANISOU 266 N CYS A 57 11018 8400 7181 63 -1770 627 N ATOM 267 CA CYS A 57 -5.994 11.124 3.868 1.00 70.04 C ANISOU 267 CA CYS A 57 10920 8513 7179 38 -1796 782 C ATOM 268 C CYS A 57 -5.445 10.648 5.228 1.00 73.65 C ANISOU 268 C CYS A 57 11249 9042 7692 36 -1788 884 C ATOM 269 O CYS A 57 -5.828 11.189 6.269 1.00 72.28 O ANISOU 269 O CYS A 57 10991 9013 7461 37 -1758 977 O ATOM 270 CB CYS A 57 -7.300 10.412 3.522 1.00 71.23 C ANISOU 270 CB CYS A 57 11054 8601 7411 0 -1917 866 C ATOM 271 SG CYS A 57 -8.109 11.021 2.018 1.00 75.09 S ANISOU 271 SG CYS A 57 11680 9025 7827 -1 -1930 762 S ATOM 272 N PHE A 58 -4.556 9.629 5.207 1.00 71.24 N ANISOU 272 N PHE A 58 10925 8642 7500 35 -1818 866 N ATOM 273 CA PHE A 58 -3.871 9.113 6.393 1.00 71.41 C ANISOU 273 CA PHE A 58 10828 8720 7584 32 -1807 955 C ATOM 274 C PHE A 58 -2.824 10.130 6.846 1.00 74.12 C ANISOU 274 C PHE A 58 11189 9164 7809 68 -1679 882 C ATOM 275 O PHE A 58 -2.642 10.324 8.046 1.00 74.29 O ANISOU 275 O PHE A 58 11105 9317 7807 70 -1644 971 O ATOM 276 CB PHE A 58 -3.233 7.738 6.111 1.00 74.29 C ANISOU 276 CB PHE A 58 11178 8936 8113 23 -1879 943 C ATOM 277 CG PHE A 58 -2.616 7.058 7.314 1.00 76.70 C ANISOU 277 CG PHE A 58 11345 9288 8511 11 -1886 1061 C ATOM 278 CD1 PHE A 58 -3.343 6.139 8.063 1.00 81.05 C ANISOU 278 CD1 PHE A 58 11760 9841 9194 -29 -1991 1237 C ATOM 279 CD2 PHE A 58 -1.304 7.330 7.693 1.00 78.93 C ANISOU 279 CD2 PHE A 58 11625 9616 8751 37 -1790 1006 C ATOM 280 CE1 PHE A 58 -2.773 5.508 9.174 1.00 82.54 C ANISOU 280 CE1 PHE A 58 11808 10083 9471 -42 -1998 1360 C ATOM 281 CE2 PHE A 58 -0.740 6.711 8.813 1.00 82.34 C ANISOU 281 CE2 PHE A 58 11922 10100 9264 24 -1794 1121 C ATOM 282 CZ PHE A 58 -1.476 5.798 9.542 1.00 81.30 C ANISOU 282 CZ PHE A 58 11652 9975 9263 -16 -1897 1298 C ATOM 283 N ILE A 59 -2.149 10.791 5.873 1.00 69.05 N ANISOU 283 N ILE A 59 10674 8468 7092 97 -1611 724 N ATOM 284 CA ILE A 59 -1.146 11.835 6.118 1.00 67.53 C ANISOU 284 CA ILE A 59 10512 8353 6794 131 -1495 645 C ATOM 285 C ILE A 59 -1.867 13.080 6.675 1.00 69.87 C ANISOU 285 C ILE A 59 10785 8790 6974 137 -1450 677 C ATOM 286 O ILE A 59 -1.286 13.793 7.493 1.00 69.06 O ANISOU 286 O ILE A 59 10640 8792 6809 158 -1378 672 O ATOM 287 CB ILE A 59 -0.312 12.159 4.837 1.00 70.32 C ANISOU 287 CB ILE A 59 10998 8614 7105 159 -1447 485 C ATOM 288 CG1 ILE A 59 0.339 10.875 4.252 1.00 71.20 C ANISOU 288 CG1 ILE A 59 11130 8590 7333 162 -1499 442 C ATOM 289 CG2 ILE A 59 0.749 13.239 5.121 1.00 70.33 C ANISOU 289 CG2 ILE A 59 11021 8691 7009 190 -1333 419 C ATOM 290 CD1 ILE A 59 1.094 11.035 2.922 1.00 76.79 C ANISOU 290 CD1 ILE A 59 11959 9218 8000 198 -1464 286 C ATOM 291 N ILE A 60 -3.144 13.307 6.271 1.00 66.14 N ANISOU 291 N ILE A 60 10333 8319 6478 122 -1499 709 N ATOM 292 CA ILE A 60 -3.957 14.420 6.778 1.00 65.70 C ANISOU 292 CA ILE A 60 10250 8391 6321 130 -1468 742 C ATOM 293 C ILE A 60 -4.158 14.212 8.292 1.00 69.52 C ANISOU 293 C ILE A 60 10582 9017 6814 129 -1479 874 C ATOM 294 O ILE A 60 -3.714 15.055 9.073 1.00 68.62 O ANISOU 294 O ILE A 60 10427 9022 6624 157 -1410 854 O ATOM 295 CB ILE A 60 -5.326 14.591 6.019 1.00 69.12 C ANISOU 295 CB ILE A 60 10734 8794 6736 111 -1523 761 C ATOM 296 CG1 ILE A 60 -5.168 14.715 4.477 1.00 69.72 C ANISOU 296 CG1 ILE A 60 10949 8743 6799 113 -1517 636 C ATOM 297 CG2 ILE A 60 -6.163 15.748 6.580 1.00 69.36 C ANISOU 297 CG2 ILE A 60 10730 8960 6665 124 -1492 795 C ATOM 298 CD1 ILE A 60 -4.299 15.885 3.931 1.00 77.54 C ANISOU 298 CD1 ILE A 60 12020 9744 7698 146 -1416 509 C ATOM 299 N LEU A 61 -4.748 13.050 8.693 1.00 66.53 N ANISOU 299 N LEU A 61 10115 8627 6537 97 -1569 1007 N ATOM 300 CA LEU A 61 -5.011 12.693 10.093 1.00 66.67 C ANISOU 300 CA LEU A 61 9970 8791 6572 93 -1591 1157 C ATOM 301 C LEU A 61 -3.727 12.615 10.909 1.00 68.83 C ANISOU 301 C LEU A 61 10182 9118 6851 110 -1531 1144 C ATOM 302 O LEU A 61 -3.688 13.187 11.996 1.00 68.43 O ANISOU 302 O LEU A 61 10038 9237 6726 134 -1487 1185 O ATOM 303 CB LEU A 61 -5.759 11.354 10.219 1.00 68.04 C ANISOU 303 CB LEU A 61 10058 8918 6877 50 -1708 1311 C ATOM 304 CG LEU A 61 -7.212 11.300 9.727 1.00 74.11 C ANISOU 304 CG LEU A 61 10840 9672 7647 28 -1784 1378 C ATOM 305 CD1 LEU A 61 -7.766 9.885 9.841 1.00 75.61 C ANISOU 305 CD1 LEU A 61 10939 9795 7993 -17 -1908 1531 C ATOM 306 CD2 LEU A 61 -8.111 12.266 10.513 1.00 76.97 C ANISOU 306 CD2 LEU A 61 11134 10229 7884 51 -1754 1442 C ATOM 307 N GLU A 62 -2.675 11.935 10.389 1.00 64.21 N ANISOU 307 N GLU A 62 9649 8399 6349 103 -1526 1082 N ATOM 308 CA GLU A 62 -1.384 11.796 11.077 1.00 63.44 C ANISOU 308 CA GLU A 62 9502 8339 6265 117 -1468 1069 C ATOM 309 C GLU A 62 -0.873 13.174 11.553 1.00 67.10 C ANISOU 309 C GLU A 62 9978 8928 6590 157 -1365 985 C ATOM 310 O GLU A 62 -0.470 13.294 12.709 1.00 66.90 O ANISOU 310 O GLU A 62 9842 9038 6538 169 -1332 1039 O ATOM 311 CB GLU A 62 -0.341 11.117 10.173 1.00 64.64 C ANISOU 311 CB GLU A 62 9745 8317 6500 114 -1466 974 C ATOM 312 N ASN A 63 -0.992 14.222 10.700 1.00 63.31 N ANISOU 312 N ASN A 63 9618 8410 6024 177 -1323 863 N ATOM 313 CA ASN A 63 -0.561 15.586 11.021 1.00 62.50 C ANISOU 313 CA ASN A 63 9535 8403 5810 214 -1238 775 C ATOM 314 C ASN A 63 -1.668 16.385 11.756 1.00 67.27 C ANISOU 314 C ASN A 63 10069 9161 6331 231 -1246 824 C ATOM 315 O ASN A 63 -1.337 17.380 12.414 1.00 66.77 O ANISOU 315 O ASN A 63 9975 9209 6186 267 -1189 771 O ATOM 316 CB ASN A 63 -0.134 16.328 9.768 1.00 60.20 C ANISOU 316 CB ASN A 63 9393 7998 5482 226 -1193 632 C ATOM 317 CG ASN A 63 1.161 15.804 9.203 1.00 73.32 C ANISOU 317 CG ASN A 63 11114 9550 7197 226 -1165 568 C ATOM 318 OD1 ASN A 63 2.248 16.012 9.761 1.00 60.41 O ANISOU 318 OD1 ASN A 63 9455 7954 5545 244 -1104 536 O ATOM 319 ND2 ASN A 63 1.081 15.160 8.055 1.00 67.91 N ANISOU 319 ND2 ASN A 63 10503 8726 6572 210 -1209 543 N ATOM 320 N ILE A 64 -2.955 15.950 11.675 1.00 64.49 N ANISOU 320 N ILE A 64 9684 8820 6000 210 -1321 922 N ATOM 321 CA ILE A 64 -4.050 16.592 12.426 1.00 64.50 C ANISOU 321 CA ILE A 64 9604 8982 5923 230 -1334 985 C ATOM 322 C ILE A 64 -3.790 16.369 13.924 1.00 69.39 C ANISOU 322 C ILE A 64 10057 9785 6523 249 -1326 1077 C ATOM 323 O ILE A 64 -3.771 17.339 14.677 1.00 68.02 O ANISOU 323 O ILE A 64 9834 9758 6254 292 -1281 1036 O ATOM 324 CB ILE A 64 -5.474 16.109 12.003 1.00 67.75 C ANISOU 324 CB ILE A 64 10013 9366 6365 200 -1418 1083 C ATOM 325 CG1 ILE A 64 -5.851 16.654 10.602 1.00 67.47 C ANISOU 325 CG1 ILE A 64 10133 9193 6310 192 -1414 979 C ATOM 326 CG2 ILE A 64 -6.527 16.548 13.041 1.00 68.65 C ANISOU 326 CG2 ILE A 64 10002 9679 6403 224 -1437 1183 C ATOM 327 CD1 ILE A 64 -7.214 16.170 10.042 1.00 72.51 C ANISOU 327 CD1 ILE A 64 10786 9784 6981 159 -1497 1064 C ATOM 328 N PHE A 65 -3.522 15.103 14.334 1.00 68.24 N ANISOU 328 N PHE A 65 9825 9630 6473 218 -1370 1195 N ATOM 329 CA PHE A 65 -3.214 14.744 15.727 1.00 69.22 C ANISOU 329 CA PHE A 65 9779 9933 6590 230 -1365 1303 C ATOM 330 C PHE A 65 -1.961 15.478 16.238 1.00 72.84 C ANISOU 330 C PHE A 65 10238 10455 6984 267 -1275 1191 C ATOM 331 O PHE A 65 -1.923 15.821 17.420 1.00 72.86 O ANISOU 331 O PHE A 65 10113 10656 6914 301 -1253 1229 O ATOM 332 CB PHE A 65 -3.023 13.224 15.911 1.00 71.73 C ANISOU 332 CB PHE A 65 10014 10193 7046 184 -1428 1444 C ATOM 333 CG PHE A 65 -4.286 12.408 15.775 1.00 73.85 C ANISOU 333 CG PHE A 65 10231 10439 7391 148 -1531 1593 C ATOM 334 CD1 PHE A 65 -4.593 11.765 14.585 1.00 76.96 C ANISOU 334 CD1 PHE A 65 10735 10620 7885 110 -1590 1570 C ATOM 335 CD2 PHE A 65 -5.175 12.291 16.837 1.00 76.69 C ANISOU 335 CD2 PHE A 65 10425 10996 7719 154 -1573 1757 C ATOM 336 CE1 PHE A 65 -5.763 11.015 14.459 1.00 78.67 C ANISOU 336 CE1 PHE A 65 10902 10808 8181 74 -1693 1708 C ATOM 337 CE2 PHE A 65 -6.349 11.544 16.709 1.00 80.18 C ANISOU 337 CE2 PHE A 65 10812 11415 8236 118 -1673 1908 C ATOM 338 CZ PHE A 65 -6.633 10.908 15.523 1.00 78.37 C ANISOU 338 CZ PHE A 65 10699 10959 8119 76 -1735 1883 C ATOM 339 N VAL A 66 -0.957 15.740 15.358 1.00 67.94 N ANISOU 339 N VAL A 66 9753 9677 6385 264 -1226 1055 N ATOM 340 CA VAL A 66 0.256 16.476 15.747 1.00 66.91 C ANISOU 340 CA VAL A 66 9634 9588 6201 296 -1144 948 C ATOM 341 C VAL A 66 -0.155 17.902 16.154 1.00 70.07 C ANISOU 341 C VAL A 66 10026 10114 6481 345 -1110 865 C ATOM 342 O VAL A 66 0.261 18.380 17.208 1.00 69.69 O ANISOU 342 O VAL A 66 9882 10225 6372 381 -1076 853 O ATOM 343 CB VAL A 66 1.342 16.477 14.637 1.00 70.13 C ANISOU 343 CB VAL A 66 10189 9804 6653 284 -1103 829 C ATOM 344 CG1 VAL A 66 2.538 17.343 15.029 1.00 69.49 C ANISOU 344 CG1 VAL A 66 10120 9769 6516 316 -1022 724 C ATOM 345 CG2 VAL A 66 1.801 15.058 14.328 1.00 70.28 C ANISOU 345 CG2 VAL A 66 10203 9706 6793 244 -1139 900 C ATOM 346 N LEU A 67 -1.037 18.530 15.360 1.00 66.05 N ANISOU 346 N LEU A 67 9608 9543 5944 348 -1126 814 N ATOM 347 CA LEU A 67 -1.564 19.873 15.612 1.00 65.47 C ANISOU 347 CA LEU A 67 9534 9567 5774 395 -1105 734 C ATOM 348 C LEU A 67 -2.679 19.870 16.679 1.00 70.27 C ANISOU 348 C LEU A 67 9996 10381 6321 421 -1145 838 C ATOM 349 O LEU A 67 -3.011 20.930 17.226 1.00 69.84 O ANISOU 349 O LEU A 67 9901 10454 6180 473 -1127 773 O ATOM 350 CB LEU A 67 -2.105 20.453 14.304 1.00 64.84 C ANISOU 350 CB LEU A 67 9598 9341 5696 384 -1111 659 C ATOM 351 CG LEU A 67 -1.051 20.898 13.315 1.00 68.66 C ANISOU 351 CG LEU A 67 10216 9666 6207 376 -1062 537 C ATOM 352 CD1 LEU A 67 -1.618 21.006 11.933 1.00 68.85 C ANISOU 352 CD1 LEU A 67 10366 9546 6249 352 -1081 505 C ATOM 353 CD2 LEU A 67 -0.413 22.195 13.760 1.00 70.33 C ANISOU 353 CD2 LEU A 67 10421 9938 6364 421 -1007 422 C ATOM 354 N LEU A 68 -3.242 18.691 16.979 1.00 67.12 N ANISOU 354 N LEU A 68 9511 10019 5972 389 -1203 999 N ATOM 355 CA LEU A 68 -4.325 18.574 17.943 1.00 67.10 C ANISOU 355 CA LEU A 68 9361 10220 5915 412 -1246 1122 C ATOM 356 C LEU A 68 -3.760 18.294 19.331 1.00 72.05 C ANISOU 356 C LEU A 68 9819 11047 6508 438 -1229 1188 C ATOM 357 O LEU A 68 -4.283 18.828 20.303 1.00 72.03 O ANISOU 357 O LEU A 68 9698 11263 6408 491 -1228 1206 O ATOM 358 CB LEU A 68 -5.294 17.466 17.502 1.00 67.20 C ANISOU 358 CB LEU A 68 9360 10168 6006 360 -1327 1277 C ATOM 359 CG LEU A 68 -6.699 17.478 18.094 1.00 71.98 C ANISOU 359 CG LEU A 68 9853 10942 6555 379 -1380 1402 C ATOM 360 CD1 LEU A 68 -7.466 18.742 17.683 1.00 71.55 C ANISOU 360 CD1 LEU A 68 9881 10895 6411 416 -1363 1292 C ATOM 361 CD2 LEU A 68 -7.479 16.273 17.617 1.00 74.79 C ANISOU 361 CD2 LEU A 68 10195 11207 7013 319 -1466 1561 C ATOM 362 N THR A 69 -2.674 17.499 19.426 1.00 69.60 N ANISOU 362 N THR A 69 9496 10674 6275 406 -1212 1216 N ATOM 363 CA THR A 69 -2.043 17.171 20.710 1.00 70.84 C ANISOU 363 CA THR A 69 9491 11016 6408 425 -1192 1285 C ATOM 364 C THR A 69 -1.204 18.339 21.243 1.00 76.35 C ANISOU 364 C THR A 69 10193 11803 7013 481 -1120 1127 C ATOM 365 O THR A 69 -1.145 18.516 22.457 1.00 76.89 O ANISOU 365 O THR A 69 10110 12098 7008 523 -1108 1161 O ATOM 366 CB THR A 69 -1.163 15.921 20.617 1.00 81.88 C ANISOU 366 CB THR A 69 10873 12308 7930 370 -1202 1374 C ATOM 367 OG1 THR A 69 -0.211 16.097 19.569 1.00 82.99 O ANISOU 367 OG1 THR A 69 11184 12224 8124 350 -1161 1237 O ATOM 368 CG2 THR A 69 -1.970 14.650 20.388 1.00 82.02 C ANISOU 368 CG2 THR A 69 10837 12274 8055 317 -1288 1556 C ATOM 369 N ILE A 70 -0.555 19.123 20.361 1.00 73.23 N ANISOU 369 N ILE A 70 9961 11241 6624 485 -1077 959 N ATOM 370 CA ILE A 70 0.265 20.275 20.774 1.00 73.49 C ANISOU 370 CA ILE A 70 10003 11331 6587 535 -1017 804 C ATOM 371 C ILE A 70 -0.699 21.411 21.273 1.00 79.22 C ANISOU 371 C ILE A 70 10677 12219 7205 602 -1030 741 C ATOM 372 O ILE A 70 -0.329 22.188 22.162 1.00 78.55 O ANISOU 372 O ILE A 70 10512 12290 7044 660 -1004 659 O ATOM 373 CB ILE A 70 1.206 20.717 19.608 1.00 75.91 C ANISOU 373 CB ILE A 70 10492 11404 6949 513 -976 667 C ATOM 374 CG1 ILE A 70 2.290 19.612 19.377 1.00 76.45 C ANISOU 374 CG1 ILE A 70 10582 11358 7109 463 -959 723 C ATOM 375 CG2 ILE A 70 1.884 22.071 19.899 1.00 76.20 C ANISOU 375 CG2 ILE A 70 10548 11479 6925 565 -928 504 C ATOM 376 CD1 ILE A 70 3.284 19.796 18.168 1.00 84.16 C ANISOU 376 CD1 ILE A 70 11729 12106 8143 439 -920 615 C ATOM 377 N TRP A 71 -1.948 21.424 20.771 1.00 77.54 N ANISOU 377 N TRP A 71 10495 11981 6986 596 -1074 785 N ATOM 378 CA TRP A 71 -2.989 22.362 21.192 1.00 78.44 C ANISOU 378 CA TRP A 71 10557 12244 7004 657 -1093 744 C ATOM 379 C TRP A 71 -3.691 21.851 22.477 1.00 81.25 C ANISOU 379 C TRP A 71 10708 12877 7287 692 -1125 884 C ATOM 380 O TRP A 71 -4.263 22.657 23.215 1.00 81.02 O ANISOU 380 O TRP A 71 10591 13039 7155 765 -1129 831 O ATOM 381 CB TRP A 71 -4.008 22.570 20.048 1.00 77.86 C ANISOU 381 CB TRP A 71 10602 12026 6956 633 -1125 746 C ATOM 382 CG TRP A 71 -5.255 23.326 20.427 1.00 80.05 C ANISOU 382 CG TRP A 71 10817 12453 7144 688 -1154 740 C ATOM 383 CD1 TRP A 71 -5.349 24.651 20.738 1.00 83.26 C ANISOU 383 CD1 TRP A 71 11216 12941 7479 759 -1137 594 C ATOM 384 CD2 TRP A 71 -6.602 22.829 20.379 1.00 80.50 C ANISOU 384 CD2 TRP A 71 10832 12567 7188 676 -1209 879 C ATOM 385 NE1 TRP A 71 -6.663 24.988 20.985 1.00 83.38 N ANISOU 385 NE1 TRP A 71 11172 13081 7426 797 -1174 635 N ATOM 386 CE2 TRP A 71 -7.455 23.892 20.754 1.00 84.96 C ANISOU 386 CE2 TRP A 71 11354 13269 7658 745 -1217 814 C ATOM 387 CE3 TRP A 71 -7.173 21.578 20.075 1.00 82.05 C ANISOU 387 CE3 TRP A 71 11016 12710 7450 613 -1259 1055 C ATOM 388 CZ2 TRP A 71 -8.847 23.742 20.838 1.00 84.71 C ANISOU 388 CZ2 TRP A 71 11268 13332 7585 755 -1266 924 C ATOM 389 CZ3 TRP A 71 -8.550 21.432 20.156 1.00 83.99 C ANISOU 389 CZ3 TRP A 71 11207 13043 7661 618 -1312 1167 C ATOM 390 CH2 TRP A 71 -9.371 22.504 20.537 1.00 84.89 C ANISOU 390 CH2 TRP A 71 11280 13303 7670 689 -1312 1106 C ATOM 391 N LYS A 72 -3.615 20.532 22.755 1.00 77.02 N ANISOU 391 N LYS A 72 10089 12366 6808 644 -1152 1063 N ATOM 392 CA LYS A 72 -4.269 19.915 23.913 1.00 77.28 C ANISOU 392 CA LYS A 72 9917 12661 6785 667 -1189 1231 C ATOM 393 C LYS A 72 -3.292 19.650 25.095 1.00 80.59 C ANISOU 393 C LYS A 72 10189 13261 7172 690 -1156 1257 C ATOM 394 O LYS A 72 -3.766 19.292 26.179 1.00 81.14 O ANISOU 394 O LYS A 72 10066 13587 7175 721 -1180 1389 O ATOM 395 CB LYS A 72 -4.923 18.586 23.507 1.00 79.96 C ANISOU 395 CB LYS A 72 10232 12927 7221 597 -1252 1436 C ATOM 396 N THR A 73 -1.957 19.823 24.904 1.00 75.41 N ANISOU 396 N THR A 73 9611 12485 6554 676 -1102 1142 N ATOM 397 CA THR A 73 -0.981 19.575 25.980 1.00 74.97 C ANISOU 397 CA THR A 73 9423 12592 6471 693 -1068 1166 C ATOM 398 C THR A 73 -0.359 20.909 26.446 1.00 77.50 C ANISOU 398 C THR A 73 9752 12997 6696 766 -1021 960 C ATOM 399 O THR A 73 0.273 21.601 25.649 1.00 76.44 O ANISOU 399 O THR A 73 9778 12665 6600 758 -988 802 O ATOM 400 CB THR A 73 0.107 18.580 25.517 1.00 82.27 C ANISOU 400 CB THR A 73 10406 13330 7523 617 -1049 1221 C ATOM 401 OG1 THR A 73 -0.508 17.394 25.011 1.00 81.76 O ANISOU 401 OG1 THR A 73 10341 13162 7562 553 -1105 1392 O ATOM 402 CG2 THR A 73 1.089 18.215 26.629 1.00 81.62 C ANISOU 402 CG2 THR A 73 10178 13415 7419 627 -1015 1269 C ATOM 403 N LYS A 74 -0.520 21.234 27.754 1.00 73.94 N ANISOU 403 N LYS A 74 9119 12849 6127 838 -1021 966 N ATOM 404 CA LYS A 74 -0.014 22.451 28.405 1.00 73.51 C ANISOU 404 CA LYS A 74 9036 12919 5977 919 -989 774 C ATOM 405 C LYS A 74 1.524 22.511 28.397 1.00 76.48 C ANISOU 405 C LYS A 74 9465 13192 6402 895 -936 687 C ATOM 406 O LYS A 74 2.086 23.601 28.282 1.00 76.06 O ANISOU 406 O LYS A 74 9487 13083 6331 933 -912 495 O ATOM 407 CB LYS A 74 -0.518 22.532 29.850 1.00 77.01 C ANISOU 407 CB LYS A 74 9247 13732 6280 999 -1007 828 C ATOM 408 N LYS A 75 2.198 21.345 28.515 1.00 72.15 N ANISOU 408 N LYS A 75 8873 12616 5923 831 -922 833 N ATOM 409 CA LYS A 75 3.662 21.241 28.481 1.00 70.91 C ANISOU 409 CA LYS A 75 8763 12360 5820 800 -870 779 C ATOM 410 C LYS A 75 4.191 21.468 27.063 1.00 73.06 C ANISOU 410 C LYS A 75 9264 12298 6197 749 -850 679 C ATOM 411 O LYS A 75 5.369 21.794 26.901 1.00 71.65 O ANISOU 411 O LYS A 75 9154 12021 6047 741 -806 579 O ATOM 412 CB LYS A 75 4.117 19.867 28.998 1.00 73.49 C ANISOU 412 CB LYS A 75 8969 12756 6199 746 -866 980 C ATOM 413 N PHE A 76 3.307 21.290 26.039 1.00 69.66 N ANISOU 413 N PHE A 76 8945 11703 5820 716 -884 713 N ATOM 414 CA PHE A 76 3.605 21.440 24.605 1.00 68.64 C ANISOU 414 CA PHE A 76 9024 11273 5783 670 -872 636 C ATOM 415 C PHE A 76 3.277 22.854 24.089 1.00 72.46 C ANISOU 415 C PHE A 76 9614 11689 6230 715 -871 457 C ATOM 416 O PHE A 76 3.356 23.088 22.885 1.00 71.26 O ANISOU 416 O PHE A 76 9624 11310 6142 683 -865 397 O ATOM 417 CB PHE A 76 2.829 20.405 23.772 1.00 70.24 C ANISOU 417 CB PHE A 76 9280 11340 6067 609 -914 773 C ATOM 418 CG PHE A 76 3.282 18.962 23.864 1.00 72.08 C ANISOU 418 CG PHE A 76 9457 11542 6390 549 -922 935 C ATOM 419 CD1 PHE A 76 2.788 18.007 22.986 1.00 75.32 C ANISOU 419 CD1 PHE A 76 9928 11793 6898 491 -965 1040 C ATOM 420 CD2 PHE A 76 4.249 18.572 24.788 1.00 74.62 C ANISOU 420 CD2 PHE A 76 9666 11980 6706 549 -889 978 C ATOM 421 CE1 PHE A 76 3.214 16.679 23.061 1.00 76.61 C ANISOU 421 CE1 PHE A 76 10034 11912 7162 438 -982 1183 C ATOM 422 CE2 PHE A 76 4.676 17.244 24.860 1.00 77.64 C ANISOU 422 CE2 PHE A 76 9992 12324 7184 493 -899 1131 C ATOM 423 CZ PHE A 76 4.159 16.309 23.995 1.00 75.84 C ANISOU 423 CZ PHE A 76 9822 11932 7063 438 -948 1231 C ATOM 424 N HIS A 77 2.960 23.802 24.988 1.00 70.01 N ANISOU 424 N HIS A 77 9206 11575 5819 792 -879 370 N ATOM 425 CA HIS A 77 2.746 25.199 24.612 1.00 69.89 C ANISOU 425 CA HIS A 77 9273 11499 5781 840 -884 192 C ATOM 426 C HIS A 77 4.103 25.944 24.634 1.00 74.01 C ANISOU 426 C HIS A 77 9848 11944 6329 851 -844 46 C ATOM 427 O HIS A 77 4.156 27.164 24.811 1.00 73.75 O ANISOU 427 O HIS A 77 9823 11929 6269 907 -851 -111 O ATOM 428 CB HIS A 77 1.708 25.865 25.526 1.00 71.45 C ANISOU 428 CB HIS A 77 9341 11937 5868 923 -919 156 C ATOM 429 CG HIS A 77 0.298 25.617 25.099 1.00 75.07 C ANISOU 429 CG HIS A 77 9812 12397 6316 916 -961 245 C ATOM 430 ND1 HIS A 77 -0.430 26.587 24.434 1.00 76.89 N ANISOU 430 ND1 HIS A 77 10129 12543 6543 945 -982 139 N ATOM 431 CD2 HIS A 77 -0.450 24.494 25.184 1.00 77.17 C ANISOU 431 CD2 HIS A 77 10017 12716 6586 879 -988 434 C ATOM 432 CE1 HIS A 77 -1.609 26.041 24.179 1.00 76.46 C ANISOU 432 CE1 HIS A 77 10063 12508 6479 926 -1016 264 C ATOM 433 NE2 HIS A 77 -1.664 24.780 24.603 1.00 76.95 N ANISOU 433 NE2 HIS A 77 10040 12650 6548 886 -1024 443 N ATOM 434 N ARG A 78 5.192 25.191 24.402 1.00 70.87 N ANISOU 434 N ARG A 78 9487 11446 5993 795 -806 100 N ATOM 435 CA ARG A 78 6.561 25.688 24.370 1.00 70.96 C ANISOU 435 CA ARG A 78 9549 11374 6038 793 -766 -5 C ATOM 436 C ARG A 78 6.934 26.159 22.950 1.00 75.04 C ANISOU 436 C ARG A 78 10255 11617 6642 757 -754 -78 C ATOM 437 O ARG A 78 6.451 25.573 21.974 1.00 73.69 O ANISOU 437 O ARG A 78 10173 11308 6517 710 -763 -4 O ATOM 438 CB ARG A 78 7.532 24.597 24.854 1.00 71.72 C ANISOU 438 CB ARG A 78 9584 11509 6155 753 -731 102 C ATOM 439 N PRO A 79 7.818 27.192 22.827 1.00 72.68 N ANISOU 439 N PRO A 79 10007 11243 6366 777 -737 -216 N ATOM 440 CA PRO A 79 8.182 27.724 21.502 1.00 72.31 C ANISOU 440 CA PRO A 79 10120 10955 6397 746 -728 -275 C ATOM 441 C PRO A 79 8.524 26.653 20.453 1.00 77.13 C ANISOU 441 C PRO A 79 10835 11400 7070 675 -703 -170 C ATOM 442 O PRO A 79 7.968 26.734 19.358 1.00 77.04 O ANISOU 442 O PRO A 79 10928 11250 7093 652 -716 -164 O ATOM 443 CB PRO A 79 9.432 28.573 21.782 1.00 73.97 C ANISOU 443 CB PRO A 79 10335 11139 6632 766 -708 -390 C ATOM 444 CG PRO A 79 9.700 28.458 23.256 1.00 78.99 C ANISOU 444 CG PRO A 79 10816 12000 7197 807 -704 -396 C ATOM 445 CD PRO A 79 8.436 28.005 23.890 1.00 74.91 C ANISOU 445 CD PRO A 79 10194 11663 6604 834 -735 -327 C ATOM 446 N MET A 80 9.407 25.662 20.764 1.00 73.92 N ANISOU 446 N MET A 80 10399 11009 6680 644 -669 -91 N ATOM 447 CA MET A 80 9.826 24.642 19.781 1.00 73.61 C ANISOU 447 CA MET A 80 10454 10809 6706 584 -648 -7 C ATOM 448 C MET A 80 8.623 23.887 19.164 1.00 76.40 C ANISOU 448 C MET A 80 10836 11121 7073 558 -685 83 C ATOM 449 O MET A 80 8.618 23.646 17.953 1.00 75.66 O ANISOU 449 O MET A 80 10863 10856 7028 526 -684 88 O ATOM 450 CB MET A 80 10.788 23.609 20.395 1.00 76.39 C ANISOU 450 CB MET A 80 10740 11213 7073 560 -614 75 C ATOM 451 CG MET A 80 11.286 22.576 19.362 1.00 80.18 C ANISOU 451 CG MET A 80 11316 11520 7627 506 -597 146 C ATOM 452 SD MET A 80 12.125 21.111 20.012 1.00 85.02 S ANISOU 452 SD MET A 80 11842 12184 8278 471 -573 276 S ATOM 453 CE MET A 80 10.812 20.372 20.968 1.00 82.28 C ANISOU 453 CE MET A 80 11341 12024 7897 476 -625 397 C ATOM 454 N TYR A 81 7.624 23.518 19.988 1.00 72.34 N ANISOU 454 N TYR A 81 10207 10768 6512 574 -719 156 N ATOM 455 CA TYR A 81 6.452 22.765 19.533 1.00 71.60 C ANISOU 455 CA TYR A 81 10122 10648 6434 548 -762 256 C ATOM 456 C TYR A 81 5.622 23.553 18.511 1.00 73.47 C ANISOU 456 C TYR A 81 10470 10772 6672 552 -784 189 C ATOM 457 O TYR A 81 5.008 22.925 17.650 1.00 73.11 O ANISOU 457 O TYR A 81 10492 10622 6666 516 -809 250 O ATOM 458 CB TYR A 81 5.557 22.364 20.710 1.00 73.32 C ANISOU 458 CB TYR A 81 10178 11086 6593 571 -796 350 C ATOM 459 CG TYR A 81 6.176 21.312 21.603 1.00 74.86 C ANISOU 459 CG TYR A 81 10255 11387 6803 552 -783 464 C ATOM 460 CD1 TYR A 81 6.042 19.959 21.312 1.00 76.83 C ANISOU 460 CD1 TYR A 81 10493 11574 7125 499 -807 606 C ATOM 461 CD2 TYR A 81 6.887 21.668 22.744 1.00 75.73 C ANISOU 461 CD2 TYR A 81 10257 11656 6860 586 -753 430 C ATOM 462 CE1 TYR A 81 6.627 18.986 22.117 1.00 77.99 C ANISOU 462 CE1 TYR A 81 10523 11808 7300 478 -798 720 C ATOM 463 CE2 TYR A 81 7.471 20.703 23.561 1.00 76.94 C ANISOU 463 CE2 TYR A 81 10294 11910 7028 565 -739 544 C ATOM 464 CZ TYR A 81 7.338 19.361 23.243 1.00 85.01 C ANISOU 464 CZ TYR A 81 11305 12864 8131 510 -761 693 C ATOM 465 OH TYR A 81 7.903 18.397 24.041 1.00 87.46 O ANISOU 465 OH TYR A 81 11492 13268 8469 487 -751 816 O ATOM 466 N TYR A 82 5.622 24.905 18.577 1.00 68.41 N ANISOU 466 N TYR A 82 9848 10145 5999 595 -779 64 N ATOM 467 CA TYR A 82 4.888 25.721 17.608 1.00 67.27 C ANISOU 467 CA TYR A 82 9802 9892 5864 598 -799 4 C ATOM 468 C TYR A 82 5.496 25.589 16.219 1.00 69.58 C ANISOU 468 C TYR A 82 10239 9974 6222 555 -777 -10 C ATOM 469 O TYR A 82 4.757 25.619 15.237 1.00 69.21 O ANISOU 469 O TYR A 82 10274 9831 6193 535 -797 3 O ATOM 470 CB TYR A 82 4.846 27.197 18.012 1.00 68.56 C ANISOU 470 CB TYR A 82 9943 10109 5998 654 -804 -128 C ATOM 471 CG TYR A 82 4.106 27.469 19.301 1.00 70.94 C ANISOU 471 CG TYR A 82 10102 10630 6222 711 -832 -136 C ATOM 472 CD1 TYR A 82 2.715 27.500 19.334 1.00 73.17 C ANISOU 472 CD1 TYR A 82 10354 10985 6464 728 -872 -97 C ATOM 473 CD2 TYR A 82 4.789 27.833 20.455 1.00 72.11 C ANISOU 473 CD2 TYR A 82 10147 10920 6333 755 -819 -197 C ATOM 474 CE1 TYR A 82 2.025 27.787 20.511 1.00 74.83 C ANISOU 474 CE1 TYR A 82 10427 11414 6593 789 -898 -108 C ATOM 475 CE2 TYR A 82 4.113 28.129 21.637 1.00 73.65 C ANISOU 475 CE2 TYR A 82 10203 11337 6444 818 -846 -217 C ATOM 476 CZ TYR A 82 2.729 28.110 21.659 1.00 81.23 C ANISOU 476 CZ TYR A 82 11130 12375 7360 837 -885 -172 C ATOM 477 OH TYR A 82 2.055 28.414 22.818 1.00 82.59 O ANISOU 477 OH TYR A 82 11158 12782 7440 907 -911 -191 O ATOM 478 N PHE A 83 6.835 25.421 16.135 1.00 65.18 N ANISOU 478 N PHE A 83 9710 9357 5698 542 -735 -31 N ATOM 479 CA PHE A 83 7.547 25.266 14.860 1.00 64.34 C ANISOU 479 CA PHE A 83 9730 9073 5645 509 -710 -42 C ATOM 480 C PHE A 83 7.374 23.838 14.314 1.00 67.05 C ANISOU 480 C PHE A 83 10104 9353 6020 467 -720 56 C ATOM 481 O PHE A 83 7.353 23.653 13.097 1.00 65.84 O ANISOU 481 O PHE A 83 10055 9065 5897 445 -720 51 O ATOM 482 CB PHE A 83 9.040 25.602 15.005 1.00 66.09 C ANISOU 482 CB PHE A 83 9962 9264 5887 514 -664 -94 C ATOM 483 CG PHE A 83 9.357 26.936 15.644 1.00 67.93 C ANISOU 483 CG PHE A 83 10149 9560 6104 555 -663 -192 C ATOM 484 CD1 PHE A 83 9.093 28.126 14.975 1.00 71.28 C ANISOU 484 CD1 PHE A 83 10626 9911 6545 570 -679 -269 C ATOM 485 CD2 PHE A 83 10.033 26.999 16.855 1.00 70.42 C ANISOU 485 CD2 PHE A 83 10366 9995 6396 577 -647 -210 C ATOM 486 CE1 PHE A 83 9.419 29.357 15.549 1.00 72.50 C ANISOU 486 CE1 PHE A 83 10733 10109 6703 610 -689 -367 C ATOM 487 CE2 PHE A 83 10.364 28.230 17.426 1.00 73.58 C ANISOU 487 CE2 PHE A 83 10722 10447 6789 619 -655 -315 C ATOM 488 CZ PHE A 83 10.058 29.400 16.769 1.00 71.80 C ANISOU 488 CZ PHE A 83 10550 10140 6592 636 -679 -396 C ATOM 489 N ILE A 84 7.247 22.839 15.222 1.00 63.92 N ANISOU 489 N ILE A 84 9608 9057 5621 459 -732 144 N ATOM 490 CA ILE A 84 6.994 21.416 14.920 1.00 63.86 C ANISOU 490 CA ILE A 84 9600 9001 5661 422 -757 248 C ATOM 491 C ILE A 84 5.579 21.277 14.304 1.00 67.48 C ANISOU 491 C ILE A 84 10092 9427 6119 410 -811 283 C ATOM 492 O ILE A 84 5.380 20.505 13.356 1.00 66.50 O ANISOU 492 O ILE A 84 10040 9182 6044 380 -833 314 O ATOM 493 CB ILE A 84 7.165 20.558 16.218 1.00 67.35 C ANISOU 493 CB ILE A 84 9899 9585 6105 419 -762 345 C ATOM 494 CG1 ILE A 84 8.647 20.562 16.674 1.00 67.79 C ANISOU 494 CG1 ILE A 84 9932 9659 6167 424 -707 314 C ATOM 495 CG2 ILE A 84 6.651 19.116 16.033 1.00 68.16 C ANISOU 495 CG2 ILE A 84 9979 9644 6275 379 -807 467 C ATOM 496 CD1 ILE A 84 8.958 19.806 17.938 1.00 75.90 C ANISOU 496 CD1 ILE A 84 10811 10836 7189 423 -704 404 C ATOM 497 N GLY A 85 4.635 22.043 14.856 1.00 64.17 N ANISOU 497 N GLY A 85 9618 9119 5644 438 -832 272 N ATOM 498 CA GLY A 85 3.251 22.102 14.409 1.00 63.76 C ANISOU 498 CA GLY A 85 9587 9060 5580 432 -880 303 C ATOM 499 C GLY A 85 3.118 22.772 13.058 1.00 66.85 C ANISOU 499 C GLY A 85 10114 9304 5980 424 -874 227 C ATOM 500 O GLY A 85 2.388 22.274 12.200 1.00 66.98 O ANISOU 500 O GLY A 85 10190 9237 6021 397 -907 265 O ATOM 501 N ASN A 86 3.854 23.895 12.839 1.00 61.97 N ANISOU 501 N ASN A 86 9540 8654 5350 447 -834 123 N ATOM 502 CA ASN A 86 3.851 24.623 11.559 1.00 60.77 C ANISOU 502 CA ASN A 86 9504 8374 5210 440 -824 58 C ATOM 503 C ASN A 86 4.378 23.721 10.433 1.00 63.14 C ANISOU 503 C ASN A 86 9896 8540 5553 406 -816 78 C ATOM 504 O ASN A 86 3.897 23.804 9.299 1.00 62.67 O ANISOU 504 O ASN A 86 9921 8392 5499 392 -830 68 O ATOM 505 CB ASN A 86 4.679 25.905 11.646 1.00 60.10 C ANISOU 505 CB ASN A 86 9431 8283 5123 468 -789 -38 C ATOM 506 CG ASN A 86 4.582 26.761 10.405 1.00 79.63 C ANISOU 506 CG ASN A 86 12000 10643 7612 462 -785 -88 C ATOM 507 OD1 ASN A 86 3.498 26.992 9.858 1.00 68.46 O ANISOU 507 OD1 ASN A 86 10610 9214 6186 458 -814 -79 O ATOM 508 ND2 ASN A 86 5.701 27.321 9.983 1.00 74.59 N ANISOU 508 ND2 ASN A 86 11408 9933 7001 463 -748 -134 N ATOM 509 N LEU A 87 5.359 22.848 10.772 1.00 58.16 N ANISOU 509 N LEU A 87 9244 7903 4951 398 -795 105 N ATOM 510 CA LEU A 87 5.944 21.841 9.888 1.00 56.97 C ANISOU 510 CA LEU A 87 9162 7640 4844 374 -791 120 C ATOM 511 C LEU A 87 4.878 20.823 9.526 1.00 59.91 C ANISOU 511 C LEU A 87 9541 7979 5244 349 -850 188 C ATOM 512 O LEU A 87 4.784 20.432 8.363 1.00 59.54 O ANISOU 512 O LEU A 87 9581 7826 5217 336 -864 170 O ATOM 513 CB LEU A 87 7.160 21.181 10.579 1.00 56.81 C ANISOU 513 CB LEU A 87 9093 7641 4851 374 -759 140 C ATOM 514 CG LEU A 87 7.876 20.034 9.866 1.00 61.30 C ANISOU 514 CG LEU A 87 9713 8105 5473 357 -757 156 C ATOM 515 CD1 LEU A 87 9.338 20.040 10.176 1.00 61.32 C ANISOU 515 CD1 LEU A 87 9709 8105 5484 367 -701 131 C ATOM 516 CD2 LEU A 87 7.246 18.682 10.194 1.00 64.11 C ANISOU 516 CD2 LEU A 87 10011 8465 5882 333 -812 248 C ATOM 517 N ALA A 88 4.061 20.409 10.522 1.00 55.82 N ANISOU 517 N ALA A 88 8923 7560 4725 344 -889 267 N ATOM 518 CA ALA A 88 2.958 19.473 10.316 1.00 55.44 C ANISOU 518 CA ALA A 88 8863 7490 4711 318 -956 349 C ATOM 519 C ALA A 88 1.859 20.128 9.483 1.00 57.17 C ANISOU 519 C ALA A 88 9147 7677 4896 316 -980 324 C ATOM 520 O ALA A 88 1.243 19.449 8.672 1.00 56.68 O ANISOU 520 O ALA A 88 9134 7535 4868 292 -1026 351 O ATOM 521 CB ALA A 88 2.406 18.995 11.651 1.00 56.57 C ANISOU 521 CB ALA A 88 8868 7770 4857 316 -988 454 C ATOM 522 N LEU A 89 1.655 21.456 9.642 1.00 52.53 N ANISOU 522 N LEU A 89 8563 7146 4251 342 -952 266 N ATOM 523 CA LEU A 89 0.678 22.221 8.862 1.00 52.14 C ANISOU 523 CA LEU A 89 8573 7067 4171 341 -969 239 C ATOM 524 C LEU A 89 1.131 22.301 7.401 1.00 57.96 C ANISOU 524 C LEU A 89 9430 7669 4923 329 -951 180 C ATOM 525 O LEU A 89 0.297 22.239 6.497 1.00 58.28 O ANISOU 525 O LEU A 89 9528 7655 4960 312 -982 187 O ATOM 526 CB LEU A 89 0.475 23.632 9.454 1.00 51.53 C ANISOU 526 CB LEU A 89 8458 7077 4043 376 -946 187 C ATOM 527 CG LEU A 89 -0.595 24.521 8.797 1.00 55.16 C ANISOU 527 CG LEU A 89 8963 7519 4477 378 -963 164 C ATOM 528 CD1 LEU A 89 -1.986 23.912 8.926 1.00 55.21 C ANISOU 528 CD1 LEU A 89 8939 7566 4474 362 -1020 252 C ATOM 529 CD2 LEU A 89 -0.603 25.891 9.411 1.00 56.99 C ANISOU 529 CD2 LEU A 89 9151 7823 4678 418 -943 98 C ATOM 530 N SER A 90 2.456 22.406 7.178 1.00 54.81 N ANISOU 530 N SER A 90 9062 7227 4535 339 -903 126 N ATOM 531 CA SER A 90 3.058 22.429 5.845 1.00 54.62 C ANISOU 531 CA SER A 90 9137 7098 4517 335 -881 75 C ATOM 532 C SER A 90 2.821 21.095 5.142 1.00 59.29 C ANISOU 532 C SER A 90 9768 7615 5145 314 -924 103 C ATOM 533 O SER A 90 2.321 21.070 4.015 1.00 58.95 O ANISOU 533 O SER A 90 9794 7511 5092 306 -944 83 O ATOM 534 CB SER A 90 4.550 22.732 5.941 1.00 57.82 C ANISOU 534 CB SER A 90 9549 7493 4927 353 -823 28 C ATOM 535 OG SER A 90 4.791 23.949 6.625 1.00 66.80 O ANISOU 535 OG SER A 90 10644 8692 6045 373 -794 -3 O ATOM 536 N ASP A 91 3.123 19.983 5.853 1.00 56.61 N ANISOU 536 N ASP A 91 9372 7283 4852 306 -944 151 N ATOM 537 CA ASP A 91 2.953 18.605 5.383 1.00 56.97 C ANISOU 537 CA ASP A 91 9435 7253 4958 287 -998 181 C ATOM 538 C ASP A 91 1.461 18.208 5.338 1.00 59.88 C ANISOU 538 C ASP A 91 9786 7625 5341 263 -1071 245 C ATOM 539 O ASP A 91 1.117 17.270 4.615 1.00 59.89 O ANISOU 539 O ASP A 91 9822 7543 5392 248 -1126 253 O ATOM 540 CB ASP A 91 3.736 17.623 6.278 1.00 59.37 C ANISOU 540 CB ASP A 91 9666 7569 5322 284 -999 227 C ATOM 541 CG ASP A 91 5.259 17.709 6.162 1.00 72.10 C ANISOU 541 CG ASP A 91 11303 9159 6932 305 -934 169 C ATOM 542 OD1 ASP A 91 5.754 18.368 5.207 1.00 72.27 O ANISOU 542 OD1 ASP A 91 11405 9142 6913 322 -895 93 O ATOM 543 OD2 ASP A 91 5.954 17.044 6.966 1.00 79.01 O ANISOU 543 OD2 ASP A 91 12113 10056 7850 302 -926 208 O ATOM 544 N LEU A 92 0.584 18.922 6.087 1.00 55.02 N ANISOU 544 N LEU A 92 9115 7105 4685 263 -1076 288 N ATOM 545 CA LEU A 92 -0.863 18.689 6.075 1.00 54.55 C ANISOU 545 CA LEU A 92 9036 7062 4629 243 -1141 357 C ATOM 546 C LEU A 92 -1.440 19.267 4.795 1.00 57.70 C ANISOU 546 C LEU A 92 9533 7398 4992 238 -1144 303 C ATOM 547 O LEU A 92 -2.224 18.599 4.126 1.00 57.33 O ANISOU 547 O LEU A 92 9518 7292 4973 216 -1203 329 O ATOM 548 CB LEU A 92 -1.534 19.293 7.329 1.00 54.62 C ANISOU 548 CB LEU A 92 8944 7211 4596 254 -1141 418 C ATOM 549 CG LEU A 92 -3.050 19.088 7.522 1.00 60.02 C ANISOU 549 CG LEU A 92 9586 7941 5277 236 -1207 509 C ATOM 550 CD1 LEU A 92 -3.418 19.091 8.988 1.00 60.74 C ANISOU 550 CD1 LEU A 92 9544 8187 5348 250 -1217 596 C ATOM 551 CD2 LEU A 92 -3.888 20.100 6.726 1.00 61.99 C ANISOU 551 CD2 LEU A 92 9907 8175 5472 238 -1203 467 C ATOM 552 N LEU A 93 -1.036 20.502 4.441 1.00 54.15 N ANISOU 552 N LEU A 93 9126 6961 4488 259 -1084 231 N ATOM 553 CA LEU A 93 -1.487 21.160 3.217 1.00 54.19 C ANISOU 553 CA LEU A 93 9215 6919 4457 255 -1079 186 C ATOM 554 C LEU A 93 -0.830 20.495 2.003 1.00 58.63 C ANISOU 554 C LEU A 93 9855 7384 5036 254 -1080 132 C ATOM 555 O LEU A 93 -1.400 20.542 0.912 1.00 59.13 O ANISOU 555 O LEU A 93 9980 7406 5082 245 -1102 113 O ATOM 556 CB LEU A 93 -1.201 22.674 3.242 1.00 54.09 C ANISOU 556 CB LEU A 93 9207 6946 4398 276 -1020 137 C ATOM 557 CG LEU A 93 -1.912 23.499 4.350 1.00 59.05 C ANISOU 557 CG LEU A 93 9760 7674 5003 289 -1022 166 C ATOM 558 CD1 LEU A 93 -1.452 24.943 4.340 1.00 59.15 C ANISOU 558 CD1 LEU A 93 9778 7705 4994 312 -972 104 C ATOM 559 CD2 LEU A 93 -3.436 23.434 4.231 1.00 61.62 C ANISOU 559 CD2 LEU A 93 10079 8020 5312 271 -1074 224 C ATOM 560 N ALA A 94 0.335 19.822 2.204 1.00 54.21 N ANISOU 560 N ALA A 94 9289 6798 4511 266 -1061 109 N ATOM 561 CA ALA A 94 1.021 19.055 1.157 1.00 53.50 C ANISOU 561 CA ALA A 94 9263 6626 4440 275 -1066 52 C ATOM 562 C ALA A 94 0.180 17.850 0.760 1.00 56.02 C ANISOU 562 C ALA A 94 9591 6882 4812 254 -1152 77 C ATOM 563 O ALA A 94 -0.005 17.607 -0.429 1.00 55.81 O ANISOU 563 O ALA A 94 9631 6801 4773 258 -1175 26 O ATOM 564 CB ALA A 94 2.399 18.616 1.632 1.00 54.21 C ANISOU 564 CB ALA A 94 9330 6708 4559 294 -1028 31 C ATOM 565 N GLY A 95 -0.377 17.160 1.765 1.00 51.71 N ANISOU 565 N GLY A 95 8971 6353 4325 233 -1202 161 N ATOM 566 CA GLY A 95 -1.276 16.020 1.596 1.00 51.63 C ANISOU 566 CA GLY A 95 8949 6284 4385 208 -1296 210 C ATOM 567 C GLY A 95 -2.563 16.415 0.901 1.00 54.86 C ANISOU 567 C GLY A 95 9397 6689 4757 190 -1334 221 C ATOM 568 O GLY A 95 -3.172 15.596 0.211 1.00 54.73 O ANISOU 568 O GLY A 95 9410 6600 4786 175 -1407 219 O ATOM 569 N VAL A 96 -2.980 17.687 1.076 1.00 50.87 N ANISOU 569 N VAL A 96 8892 6262 4176 192 -1286 231 N ATOM 570 CA VAL A 96 -4.143 18.270 0.403 1.00 50.61 C ANISOU 570 CA VAL A 96 8898 6235 4097 177 -1307 241 C ATOM 571 C VAL A 96 -3.758 18.542 -1.047 1.00 54.79 C ANISOU 571 C VAL A 96 9520 6714 4584 190 -1283 146 C ATOM 572 O VAL A 96 -4.323 17.940 -1.959 1.00 55.08 O ANISOU 572 O VAL A 96 9601 6693 4633 179 -1339 127 O ATOM 573 CB VAL A 96 -4.679 19.553 1.109 1.00 53.88 C ANISOU 573 CB VAL A 96 9273 6747 4451 180 -1266 278 C ATOM 574 CG1 VAL A 96 -5.823 20.182 0.319 1.00 53.51 C ANISOU 574 CG1 VAL A 96 9270 6700 4359 164 -1283 286 C ATOM 575 CG2 VAL A 96 -5.110 19.269 2.541 1.00 53.81 C ANISOU 575 CG2 VAL A 96 9162 6814 4468 175 -1293 373 C ATOM 576 N ALA A 97 -2.745 19.412 -1.244 1.00 50.83 N ANISOU 576 N ALA A 97 9039 6239 4036 217 -1203 88 N ATOM 577 CA ALA A 97 -2.220 19.825 -2.547 1.00 50.91 C ANISOU 577 CA ALA A 97 9119 6229 3996 236 -1168 10 C ATOM 578 C ALA A 97 -1.846 18.625 -3.433 1.00 55.23 C ANISOU 578 C ALA A 97 9708 6705 4570 249 -1210 -52 C ATOM 579 O ALA A 97 -1.849 18.764 -4.659 1.00 54.69 O ANISOU 579 O ALA A 97 9695 6631 4454 262 -1205 -109 O ATOM 580 CB ALA A 97 -0.997 20.708 -2.354 1.00 51.34 C ANISOU 580 CB ALA A 97 9166 6321 4021 262 -1085 -23 C ATOM 581 N TYR A 98 -1.527 17.458 -2.826 1.00 52.30 N ANISOU 581 N TYR A 98 9305 6287 4278 248 -1254 -40 N ATOM 582 CA TYR A 98 -1.164 16.298 -3.616 1.00 53.13 C ANISOU 582 CA TYR A 98 9446 6317 4424 265 -1303 -109 C ATOM 583 C TYR A 98 -2.412 15.450 -3.902 1.00 57.84 C ANISOU 583 C TYR A 98 10048 6857 5073 237 -1405 -83 C ATOM 584 O TYR A 98 -2.435 14.785 -4.938 1.00 58.47 O ANISOU 584 O TYR A 98 10173 6882 5160 253 -1451 -160 O ATOM 585 CB TYR A 98 -0.062 15.452 -2.963 1.00 55.00 C ANISOU 585 CB TYR A 98 9649 6518 4732 282 -1300 -121 C ATOM 586 CG TYR A 98 0.515 14.434 -3.926 1.00 58.47 C ANISOU 586 CG TYR A 98 10129 6884 5201 315 -1339 -218 C ATOM 587 CD1 TYR A 98 1.363 14.824 -4.959 1.00 60.83 C ANISOU 587 CD1 TYR A 98 10482 7208 5422 359 -1285 -311 C ATOM 588 CD2 TYR A 98 0.185 13.086 -3.827 1.00 60.16 C ANISOU 588 CD2 TYR A 98 10323 7009 5526 305 -1435 -216 C ATOM 589 CE1 TYR A 98 1.858 13.901 -5.877 1.00 62.70 C ANISOU 589 CE1 TYR A 98 10753 7392 5676 399 -1324 -412 C ATOM 590 CE2 TYR A 98 0.713 12.146 -4.712 1.00 62.07 C ANISOU 590 CE2 TYR A 98 10601 7180 5803 343 -1479 -321 C ATOM 591 CZ TYR A 98 1.540 12.561 -5.744 1.00 70.79 C ANISOU 591 CZ TYR A 98 11761 8321 6815 393 -1421 -425 C ATOM 592 OH TYR A 98 2.048 11.649 -6.636 1.00 74.45 O ANISOU 592 OH TYR A 98 12256 8730 7302 440 -1466 -540 O ATOM 593 N THR A 99 -3.466 15.504 -3.043 1.00 54.01 N ANISOU 593 N THR A 99 9513 6391 4619 198 -1443 21 N ATOM 594 CA THR A 99 -4.728 14.797 -3.341 1.00 54.28 C ANISOU 594 CA THR A 99 9549 6375 4701 167 -1542 60 C ATOM 595 C THR A 99 -5.355 15.469 -4.573 1.00 58.32 C ANISOU 595 C THR A 99 10129 6903 5125 167 -1533 12 C ATOM 596 O THR A 99 -5.818 14.775 -5.484 1.00 59.04 O ANISOU 596 O THR A 99 10260 6936 5237 166 -1602 -36 O ATOM 597 CB THR A 99 -5.670 14.771 -2.130 1.00 60.54 C ANISOU 597 CB THR A 99 10263 7204 5536 130 -1579 195 C ATOM 598 OG1 THR A 99 -5.047 14.023 -1.095 1.00 62.04 O ANISOU 598 OG1 THR A 99 10382 7377 5812 130 -1598 241 O ATOM 599 CG2 THR A 99 -7.018 14.131 -2.447 1.00 58.01 C ANISOU 599 CG2 THR A 99 9944 6839 5260 95 -1680 251 C ATOM 600 N ALA A 100 -5.292 16.824 -4.620 1.00 53.02 N ANISOU 600 N ALA A 100 9470 6314 4364 172 -1449 20 N ATOM 601 CA ALA A 100 -5.757 17.636 -5.740 1.00 51.93 C ANISOU 601 CA ALA A 100 9385 6207 4139 172 -1424 -14 C ATOM 602 C ALA A 100 -4.897 17.380 -6.966 1.00 54.42 C ANISOU 602 C ALA A 100 9754 6506 4418 211 -1409 -127 C ATOM 603 O ALA A 100 -5.436 17.293 -8.062 1.00 54.29 O ANISOU 603 O ALA A 100 9778 6483 4366 211 -1444 -168 O ATOM 604 CB ALA A 100 -5.731 19.108 -5.367 1.00 51.99 C ANISOU 604 CB ALA A 100 9375 6294 4083 171 -1341 23 C ATOM 605 N ASN A 101 -3.567 17.200 -6.773 1.00 50.38 N ANISOU 605 N ASN A 101 9236 5994 3913 246 -1362 -177 N ATOM 606 CA ASN A 101 -2.620 16.888 -7.846 1.00 50.79 C ANISOU 606 CA ASN A 101 9327 6042 3927 293 -1346 -285 C ATOM 607 C ASN A 101 -3.017 15.568 -8.518 1.00 56.68 C ANISOU 607 C ASN A 101 10097 6712 4725 301 -1445 -349 C ATOM 608 O ASN A 101 -3.169 15.547 -9.734 1.00 57.62 O ANISOU 608 O ASN A 101 10258 6850 4785 322 -1460 -421 O ATOM 609 CB ASN A 101 -1.182 16.829 -7.319 1.00 50.07 C ANISOU 609 CB ASN A 101 9216 5955 3852 325 -1288 -310 C ATOM 610 CG ASN A 101 -0.134 16.522 -8.365 1.00 66.85 C ANISOU 610 CG ASN A 101 11376 8091 5935 381 -1267 -417 C ATOM 611 OD1 ASN A 101 0.192 15.359 -8.638 1.00 59.04 O ANISOU 611 OD1 ASN A 101 10396 7040 4996 406 -1323 -486 O ATOM 612 ND2 ASN A 101 0.458 17.564 -8.929 1.00 58.05 N ANISOU 612 ND2 ASN A 101 10272 7056 4730 403 -1188 -428 N ATOM 613 N LEU A 102 -3.262 14.498 -7.724 1.00 53.09 N ANISOU 613 N LEU A 102 9610 6176 4386 282 -1520 -317 N ATOM 614 CA LEU A 102 -3.694 13.183 -8.223 1.00 53.61 C ANISOU 614 CA LEU A 102 9687 6149 4533 284 -1633 -370 C ATOM 615 C LEU A 102 -5.016 13.286 -9.002 1.00 58.32 C ANISOU 615 C LEU A 102 10314 6747 5099 258 -1690 -363 C ATOM 616 O LEU A 102 -5.147 12.673 -10.066 1.00 58.87 O ANISOU 616 O LEU A 102 10420 6785 5162 283 -1748 -461 O ATOM 617 CB LEU A 102 -3.853 12.186 -7.059 1.00 53.52 C ANISOU 617 CB LEU A 102 9615 6056 4664 256 -1703 -295 C ATOM 618 CG LEU A 102 -2.575 11.774 -6.334 1.00 57.82 C ANISOU 618 CG LEU A 102 10124 6579 5264 281 -1670 -308 C ATOM 619 CD1 LEU A 102 -2.878 11.170 -4.988 1.00 57.75 C ANISOU 619 CD1 LEU A 102 10036 6534 5374 240 -1716 -188 C ATOM 620 CD2 LEU A 102 -1.697 10.873 -7.197 1.00 60.85 C ANISOU 620 CD2 LEU A 102 10539 6900 5681 335 -1705 -445 C ATOM 621 N LEU A 103 -5.975 14.086 -8.489 1.00 54.40 N ANISOU 621 N LEU A 103 9800 6294 4577 211 -1673 -251 N ATOM 622 CA LEU A 103 -7.277 14.302 -9.125 1.00 54.55 C ANISOU 622 CA LEU A 103 9842 6321 4563 180 -1719 -223 C ATOM 623 C LEU A 103 -7.146 15.135 -10.415 1.00 59.84 C ANISOU 623 C LEU A 103 10563 7068 5106 205 -1662 -296 C ATOM 624 O LEU A 103 -7.982 14.995 -11.314 1.00 60.37 O ANISOU 624 O LEU A 103 10659 7134 5143 193 -1713 -317 O ATOM 625 CB LEU A 103 -8.257 15.003 -8.157 1.00 53.57 C ANISOU 625 CB LEU A 103 9679 6235 4440 130 -1706 -82 C ATOM 626 CG LEU A 103 -8.711 14.222 -6.914 1.00 57.63 C ANISOU 626 CG LEU A 103 10128 6698 5069 98 -1775 21 C ATOM 627 CD1 LEU A 103 -9.485 15.105 -5.981 1.00 56.95 C ANISOU 627 CD1 LEU A 103 9999 6684 4954 65 -1741 146 C ATOM 628 CD2 LEU A 103 -9.543 13.003 -7.284 1.00 60.27 C ANISOU 628 CD2 LEU A 103 10463 6936 5500 76 -1907 23 C ATOM 629 N LEU A 104 -6.096 15.981 -10.511 1.00 56.18 N ANISOU 629 N LEU A 104 10102 6674 4569 239 -1561 -327 N ATOM 630 CA LEU A 104 -5.885 16.853 -11.668 1.00 56.20 C ANISOU 630 CA LEU A 104 10135 6766 4453 263 -1501 -374 C ATOM 631 C LEU A 104 -4.599 16.457 -12.461 1.00 62.46 C ANISOU 631 C LEU A 104 10946 7582 5206 329 -1477 -495 C ATOM 632 O LEU A 104 -4.051 17.292 -13.180 1.00 61.91 O ANISOU 632 O LEU A 104 10880 7604 5039 356 -1404 -515 O ATOM 633 CB LEU A 104 -5.799 18.327 -11.211 1.00 55.04 C ANISOU 633 CB LEU A 104 9966 6695 4252 245 -1404 -289 C ATOM 634 CG LEU A 104 -7.031 18.911 -10.489 1.00 58.43 C ANISOU 634 CG LEU A 104 10374 7123 4702 190 -1415 -176 C ATOM 635 CD1 LEU A 104 -6.700 20.216 -9.825 1.00 57.65 C ANISOU 635 CD1 LEU A 104 10244 7083 4576 185 -1327 -115 C ATOM 636 CD2 LEU A 104 -8.228 19.052 -11.415 1.00 60.48 C ANISOU 636 CD2 LEU A 104 10660 7400 4920 163 -1457 -162 C ATOM 637 N SER A 105 -4.179 15.172 -12.392 1.00 61.52 N ANISOU 637 N SER A 105 10829 7380 5163 356 -1546 -574 N ATOM 638 CA SER A 105 -3.017 14.648 -13.136 1.00 62.92 C ANISOU 638 CA SER A 105 11021 7575 5310 427 -1536 -700 C ATOM 639 C SER A 105 -3.443 13.684 -14.266 1.00 69.03 C ANISOU 639 C SER A 105 11824 8326 6078 460 -1630 -821 C ATOM 640 O SER A 105 -4.622 13.332 -14.380 1.00 68.91 O ANISOU 640 O SER A 105 11819 8266 6098 422 -1709 -801 O ATOM 641 CB SER A 105 -2.041 13.924 -12.205 1.00 67.06 C ANISOU 641 CB SER A 105 11522 8025 5931 444 -1541 -712 C ATOM 642 OG SER A 105 -1.373 14.798 -11.311 1.00 75.81 O ANISOU 642 OG SER A 105 12603 9171 7031 430 -1449 -629 O ATOM 643 N GLY A 106 -2.462 13.272 -15.076 1.00 66.91 N ANISOU 643 N GLY A 106 11565 8092 5765 534 -1623 -947 N ATOM 644 CA GLY A 106 -2.635 12.312 -16.161 1.00 68.16 C ANISOU 644 CA GLY A 106 11745 8238 5914 585 -1711 -1093 C ATOM 645 C GLY A 106 -3.504 12.799 -17.296 1.00 72.84 C ANISOU 645 C GLY A 106 12355 8920 6399 582 -1723 -1113 C ATOM 646 O GLY A 106 -3.096 13.683 -18.052 1.00 72.69 O ANISOU 646 O GLY A 106 12333 9042 6244 613 -1643 -1120 O ATOM 647 N ALA A 107 -4.704 12.206 -17.433 1.00 69.69 N ANISOU 647 N ALA A 107 11970 8444 6065 543 -1827 -1114 N ATOM 648 CA ALA A 107 -5.659 12.553 -18.488 1.00 69.75 C ANISOU 648 CA ALA A 107 11995 8526 5982 533 -1852 -1131 C ATOM 649 C ALA A 107 -6.303 13.916 -18.223 1.00 72.26 C ANISOU 649 C ALA A 107 12304 8920 6230 470 -1766 -977 C ATOM 650 O ALA A 107 -6.564 14.659 -19.172 1.00 72.58 O ANISOU 650 O ALA A 107 12345 9086 6145 480 -1721 -978 O ATOM 651 CB ALA A 107 -6.732 11.481 -18.596 1.00 71.19 C ANISOU 651 CB ALA A 107 12191 8587 6271 506 -1995 -1169 C ATOM 652 N THR A 108 -6.528 14.256 -16.934 1.00 66.67 N ANISOU 652 N THR A 108 11582 8145 5604 409 -1742 -844 N ATOM 653 CA THR A 108 -7.152 15.518 -16.517 1.00 64.89 C ANISOU 653 CA THR A 108 11345 7975 5336 351 -1669 -701 C ATOM 654 C THR A 108 -6.147 16.697 -16.620 1.00 66.31 C ANISOU 654 C THR A 108 11506 8268 5421 377 -1543 -673 C ATOM 655 O THR A 108 -6.579 17.846 -16.575 1.00 65.18 O ANISOU 655 O THR A 108 11350 8191 5227 342 -1482 -576 O ATOM 656 CB THR A 108 -7.714 15.408 -15.081 1.00 73.69 C ANISOU 656 CB THR A 108 12441 8991 6566 290 -1692 -582 C ATOM 657 OG1 THR A 108 -6.682 14.955 -14.211 1.00 73.12 O ANISOU 657 OG1 THR A 108 12350 8865 6566 313 -1677 -597 O ATOM 658 CG2 THR A 108 -8.896 14.444 -14.981 1.00 73.48 C ANISOU 658 CG2 THR A 108 12423 8865 6632 252 -1816 -570 C ATOM 659 N THR A 109 -4.826 16.418 -16.797 1.00 61.96 N ANISOU 659 N THR A 109 10949 7742 4852 440 -1509 -755 N ATOM 660 CA THR A 109 -3.774 17.451 -16.940 1.00 60.82 C ANISOU 660 CA THR A 109 10780 7703 4624 470 -1397 -728 C ATOM 661 C THR A 109 -4.115 18.407 -18.095 1.00 63.31 C ANISOU 661 C THR A 109 11084 8157 4815 473 -1354 -704 C ATOM 662 O THR A 109 -3.871 19.615 -18.010 1.00 62.14 O ANISOU 662 O THR A 109 10906 8079 4624 456 -1270 -612 O ATOM 663 CB THR A 109 -2.390 16.782 -17.182 1.00 68.46 C ANISOU 663 CB THR A 109 11746 8685 5581 547 -1387 -840 C ATOM 664 OG1 THR A 109 -2.102 15.853 -16.138 1.00 67.93 O ANISOU 664 OG1 THR A 109 11683 8487 5638 541 -1431 -856 O ATOM 665 CG2 THR A 109 -1.246 17.792 -17.311 1.00 65.96 C ANISOU 665 CG2 THR A 109 11399 8477 5184 578 -1278 -804 C ATOM 666 N TYR A 110 -4.711 17.851 -19.152 1.00 59.57 N ANISOU 666 N TYR A 110 10627 7717 4290 492 -1417 -785 N ATOM 667 CA TYR A 110 -5.045 18.565 -20.368 1.00 59.26 C ANISOU 667 CA TYR A 110 10570 7821 4125 502 -1387 -775 C ATOM 668 C TYR A 110 -6.394 19.304 -20.223 1.00 61.62 C ANISOU 668 C TYR A 110 10869 8109 4433 423 -1391 -658 C ATOM 669 O TYR A 110 -6.694 20.143 -21.078 1.00 61.45 O ANISOU 669 O TYR A 110 10822 8209 4317 417 -1351 -612 O ATOM 670 CB TYR A 110 -5.075 17.586 -21.558 1.00 61.36 C ANISOU 670 CB TYR A 110 10849 8136 4328 565 -1459 -929 C ATOM 671 CG TYR A 110 -3.778 16.818 -21.683 1.00 63.19 C ANISOU 671 CG TYR A 110 11080 8375 4556 648 -1461 -1053 C ATOM 672 CD1 TYR A 110 -2.643 17.412 -22.228 1.00 65.32 C ANISOU 672 CD1 TYR A 110 11311 8788 4719 708 -1377 -1060 C ATOM 673 CD2 TYR A 110 -3.666 15.517 -21.203 1.00 64.27 C ANISOU 673 CD2 TYR A 110 11246 8371 4804 666 -1547 -1151 C ATOM 674 CE1 TYR A 110 -1.425 16.734 -22.282 1.00 66.55 C ANISOU 674 CE1 TYR A 110 11464 8953 4871 786 -1375 -1167 C ATOM 675 CE2 TYR A 110 -2.455 14.825 -21.260 1.00 65.71 C ANISOU 675 CE2 TYR A 110 11424 8552 4992 743 -1548 -1261 C ATOM 676 CZ TYR A 110 -1.337 15.437 -21.804 1.00 72.48 C ANISOU 676 CZ TYR A 110 12249 9559 5732 805 -1459 -1273 C ATOM 677 OH TYR A 110 -0.140 14.767 -21.862 1.00 72.91 O ANISOU 677 OH TYR A 110 12298 9618 5786 884 -1457 -1379 O ATOM 678 N LYS A 111 -7.170 19.065 -19.125 1.00 56.37 N ANISOU 678 N LYS A 111 10224 7314 3880 364 -1434 -596 N ATOM 679 CA LYS A 111 -8.417 19.819 -18.938 1.00 55.35 C ANISOU 679 CA LYS A 111 10092 7182 3755 294 -1432 -480 C ATOM 680 C LYS A 111 -8.130 21.006 -17.969 1.00 56.61 C ANISOU 680 C LYS A 111 10221 7342 3945 261 -1347 -359 C ATOM 681 O LYS A 111 -9.041 21.546 -17.330 1.00 55.33 O ANISOU 681 O LYS A 111 10055 7143 3826 205 -1349 -261 O ATOM 682 CB LYS A 111 -9.607 18.939 -18.455 1.00 58.54 C ANISOU 682 CB LYS A 111 10527 7469 4249 249 -1535 -472 C ATOM 683 CG LYS A 111 -9.582 18.463 -16.995 1.00 78.99 C ANISOU 683 CG LYS A 111 13115 9933 6964 223 -1561 -425 C ATOM 684 CD LYS A 111 -10.895 17.775 -16.599 1.00 89.42 C ANISOU 684 CD LYS A 111 14451 11161 8364 171 -1660 -382 C ATOM 685 CE LYS A 111 -10.970 17.463 -15.123 1.00 96.98 C ANISOU 685 CE LYS A 111 15389 12026 9435 141 -1678 -305 C ATOM 686 NZ LYS A 111 -12.250 16.798 -14.763 1.00104.32 N ANISOU 686 NZ LYS A 111 16321 12876 10440 92 -1777 -246 N ATOM 687 N LEU A 112 -6.859 21.439 -17.926 1.00 52.43 N ANISOU 687 N LEU A 112 9667 6864 3391 301 -1275 -370 N ATOM 688 CA LEU A 112 -6.413 22.556 -17.092 1.00 51.06 C ANISOU 688 CA LEU A 112 9459 6692 3249 281 -1199 -274 C ATOM 689 C LEU A 112 -5.830 23.683 -17.937 1.00 53.77 C ANISOU 689 C LEU A 112 9758 7160 3512 298 -1122 -231 C ATOM 690 O LEU A 112 -5.221 23.427 -18.978 1.00 54.13 O ANISOU 690 O LEU A 112 9794 7297 3474 348 -1112 -294 O ATOM 691 CB LEU A 112 -5.355 22.084 -16.066 1.00 50.66 C ANISOU 691 CB LEU A 112 9409 6573 3267 306 -1186 -306 C ATOM 692 CG LEU A 112 -5.793 21.046 -15.026 1.00 54.62 C ANISOU 692 CG LEU A 112 9933 6951 3867 285 -1254 -320 C ATOM 693 CD1 LEU A 112 -4.610 20.507 -14.273 1.00 54.35 C ANISOU 693 CD1 LEU A 112 9894 6873 3885 318 -1239 -362 C ATOM 694 CD2 LEU A 112 -6.830 21.613 -14.068 1.00 55.98 C ANISOU 694 CD2 LEU A 112 10093 7084 4094 225 -1260 -214 C ATOM 695 N THR A 113 -6.018 24.928 -17.484 1.00 48.55 N ANISOU 695 N THR A 113 9062 6506 2878 259 -1073 -123 N ATOM 696 CA THR A 113 -5.440 26.108 -18.127 1.00 48.18 C ANISOU 696 CA THR A 113 8959 6562 2786 268 -1003 -57 C ATOM 697 C THR A 113 -3.982 26.267 -17.615 1.00 51.47 C ANISOU 697 C THR A 113 9354 6975 3228 307 -955 -73 C ATOM 698 O THR A 113 -3.684 25.730 -16.537 1.00 50.99 O ANISOU 698 O THR A 113 9319 6818 3235 309 -971 -108 O ATOM 699 CB THR A 113 -6.312 27.356 -17.861 1.00 54.47 C ANISOU 699 CB THR A 113 9722 7352 3621 212 -981 61 C ATOM 700 OG1 THR A 113 -6.408 27.596 -16.455 1.00 51.13 O ANISOU 700 OG1 THR A 113 9305 6825 3295 188 -983 87 O ATOM 701 CG2 THR A 113 -7.696 27.246 -18.464 1.00 53.41 C ANISOU 701 CG2 THR A 113 9604 7238 3453 175 -1021 85 C ATOM 702 N PRO A 114 -3.059 26.982 -18.336 1.00 46.79 N ANISOU 702 N PRO A 114 8709 6486 2584 337 -900 -39 N ATOM 703 CA PRO A 114 -1.681 27.146 -17.823 1.00 45.78 C ANISOU 703 CA PRO A 114 8560 6351 2483 371 -857 -46 C ATOM 704 C PRO A 114 -1.656 27.712 -16.401 1.00 47.78 C ANISOU 704 C PRO A 114 8808 6497 2847 336 -844 2 C ATOM 705 O PRO A 114 -0.861 27.252 -15.591 1.00 47.28 O ANISOU 705 O PRO A 114 8760 6378 2826 356 -838 -40 O ATOM 706 CB PRO A 114 -1.048 28.131 -18.812 1.00 47.83 C ANISOU 706 CB PRO A 114 8747 6745 2682 391 -804 27 C ATOM 707 CG PRO A 114 -1.816 27.964 -20.043 1.00 52.97 C ANISOU 707 CG PRO A 114 9391 7495 3241 392 -824 24 C ATOM 708 CD PRO A 114 -3.222 27.674 -19.625 1.00 48.30 C ANISOU 708 CD PRO A 114 8848 6813 2692 340 -874 19 C ATOM 709 N ALA A 115 -2.562 28.666 -16.090 1.00 43.02 N ANISOU 709 N ALA A 115 8182 5871 2292 286 -843 85 N ATOM 710 CA ALA A 115 -2.698 29.278 -14.772 1.00 41.78 C ANISOU 710 CA ALA A 115 8014 5626 2235 256 -838 123 C ATOM 711 C ALA A 115 -3.089 28.236 -13.730 1.00 46.38 C ANISOU 711 C ALA A 115 8648 6119 2857 251 -880 63 C ATOM 712 O ALA A 115 -2.450 28.165 -12.673 1.00 46.37 O ANISOU 712 O ALA A 115 8640 6064 2913 259 -869 49 O ATOM 713 CB ALA A 115 -3.728 30.387 -14.819 1.00 42.17 C ANISOU 713 CB ALA A 115 8030 5677 2317 211 -838 210 C ATOM 714 N GLN A 116 -4.104 27.387 -14.051 1.00 42.79 N ANISOU 714 N GLN A 116 8236 5651 2373 238 -932 31 N ATOM 715 CA GLN A 116 -4.559 26.294 -13.181 1.00 42.31 C ANISOU 715 CA GLN A 116 8214 5507 2352 230 -985 -13 C ATOM 716 C GLN A 116 -3.415 25.304 -12.931 1.00 46.55 C ANISOU 716 C GLN A 116 8769 6021 2897 272 -985 -91 C ATOM 717 O GLN A 116 -3.272 24.808 -11.812 1.00 45.81 O ANISOU 717 O GLN A 116 8679 5862 2866 269 -1000 -101 O ATOM 718 CB GLN A 116 -5.779 25.571 -13.781 1.00 43.94 C ANISOU 718 CB GLN A 116 8459 5708 2529 209 -1047 -28 C ATOM 719 CG GLN A 116 -7.078 26.382 -13.701 1.00 58.33 C ANISOU 719 CG GLN A 116 10269 7533 4362 161 -1056 54 C ATOM 720 CD GLN A 116 -8.260 25.703 -14.360 1.00 78.19 C ANISOU 720 CD GLN A 116 12820 10046 6844 138 -1117 46 C ATOM 721 OE1 GLN A 116 -8.139 25.004 -15.376 1.00 74.54 O ANISOU 721 OE1 GLN A 116 12380 9616 6324 160 -1141 -17 O ATOM 722 NE2 GLN A 116 -9.451 25.996 -13.860 1.00 69.81 N ANISOU 722 NE2 GLN A 116 11756 8955 5811 96 -1143 111 N ATOM 723 N TRP A 117 -2.569 25.074 -13.963 1.00 43.47 N ANISOU 723 N TRP A 117 8381 5695 2441 315 -966 -140 N ATOM 724 CA TRP A 117 -1.392 24.208 -13.910 1.00 43.13 C ANISOU 724 CA TRP A 117 8351 5643 2394 364 -961 -217 C ATOM 725 C TRP A 117 -0.348 24.797 -12.938 1.00 45.52 C ANISOU 725 C TRP A 117 8622 5927 2746 370 -907 -185 C ATOM 726 O TRP A 117 0.072 24.104 -12.013 1.00 44.52 O ANISOU 726 O TRP A 117 8506 5737 2674 377 -919 -216 O ATOM 727 CB TRP A 117 -0.808 24.044 -15.321 1.00 42.67 C ANISOU 727 CB TRP A 117 8290 5685 2237 412 -947 -266 C ATOM 728 CG TRP A 117 0.159 22.912 -15.459 1.00 44.16 C ANISOU 728 CG TRP A 117 8500 5867 2413 469 -959 -367 C ATOM 729 CD1 TRP A 117 -0.103 21.675 -15.970 1.00 47.88 C ANISOU 729 CD1 TRP A 117 9007 6319 2866 498 -1022 -468 C ATOM 730 CD2 TRP A 117 1.527 22.890 -15.032 1.00 43.74 C ANISOU 730 CD2 TRP A 117 8429 5816 2373 505 -913 -379 C ATOM 731 NE1 TRP A 117 1.029 20.898 -15.932 1.00 47.88 N ANISOU 731 NE1 TRP A 117 9012 6313 2866 554 -1016 -546 N ATOM 732 CE2 TRP A 117 2.040 21.611 -15.338 1.00 48.65 C ANISOU 732 CE2 TRP A 117 9079 6425 2980 557 -947 -489 C ATOM 733 CE3 TRP A 117 2.380 23.835 -14.445 1.00 44.09 C ANISOU 733 CE3 TRP A 117 8436 5873 2445 500 -850 -310 C ATOM 734 CZ2 TRP A 117 3.365 21.250 -15.060 1.00 47.80 C ANISOU 734 CZ2 TRP A 117 8964 6319 2880 603 -914 -525 C ATOM 735 CZ3 TRP A 117 3.683 23.471 -14.166 1.00 45.39 C ANISOU 735 CZ3 TRP A 117 8594 6039 2615 542 -819 -343 C ATOM 736 CH2 TRP A 117 4.166 22.196 -14.476 1.00 46.65 C ANISOU 736 CH2 TRP A 117 8782 6189 2753 593 -848 -447 C ATOM 737 N PHE A 118 0.042 26.088 -13.125 1.00 41.76 N ANISOU 737 N PHE A 118 8100 5504 2260 365 -853 -116 N ATOM 738 CA PHE A 118 0.994 26.771 -12.237 1.00 41.19 C ANISOU 738 CA PHE A 118 7993 5414 2242 369 -808 -83 C ATOM 739 C PHE A 118 0.470 26.849 -10.815 1.00 45.71 C ANISOU 739 C PHE A 118 8564 5906 2897 337 -826 -67 C ATOM 740 O PHE A 118 1.248 27.088 -9.887 1.00 45.26 O ANISOU 740 O PHE A 118 8486 5823 2888 344 -802 -65 O ATOM 741 CB PHE A 118 1.329 28.189 -12.719 1.00 42.77 C ANISOU 741 CB PHE A 118 8137 5674 2438 363 -763 -3 C ATOM 742 CG PHE A 118 2.104 28.260 -14.003 1.00 44.79 C ANISOU 742 CG PHE A 118 8371 6033 2613 401 -734 3 C ATOM 743 CD1 PHE A 118 3.417 27.814 -14.064 1.00 48.21 C ANISOU 743 CD1 PHE A 118 8801 6493 3021 448 -707 -35 C ATOM 744 CD2 PHE A 118 1.589 28.925 -15.103 1.00 47.35 C ANISOU 744 CD2 PHE A 118 8663 6440 2888 390 -728 61 C ATOM 745 CE1 PHE A 118 4.147 27.906 -15.247 1.00 49.92 C ANISOU 745 CE1 PHE A 118 8987 6825 3153 490 -679 -24 C ATOM 746 CE2 PHE A 118 2.318 29.016 -16.288 1.00 51.03 C ANISOU 746 CE2 PHE A 118 9094 7026 3270 430 -700 76 C ATOM 747 CZ PHE A 118 3.590 28.501 -16.354 1.00 49.40 C ANISOU 747 CZ PHE A 118 8886 6852 3031 482 -676 32 C ATOM 748 N LEU A 119 -0.850 26.667 -10.648 1.00 42.34 N ANISOU 748 N LEU A 119 8154 5452 2481 303 -870 -53 N ATOM 749 CA LEU A 119 -1.513 26.672 -9.352 1.00 41.64 C ANISOU 749 CA LEU A 119 8057 5308 2456 276 -894 -32 C ATOM 750 C LEU A 119 -1.552 25.227 -8.814 1.00 45.41 C ANISOU 750 C LEU A 119 8563 5736 2953 282 -939 -80 C ATOM 751 O LEU A 119 -1.447 25.017 -7.602 1.00 44.10 O ANISOU 751 O LEU A 119 8378 5538 2841 277 -945 -72 O ATOM 752 CB LEU A 119 -2.918 27.288 -9.516 1.00 41.50 C ANISOU 752 CB LEU A 119 8034 5296 2437 239 -918 20 C ATOM 753 CG LEU A 119 -3.657 27.808 -8.275 1.00 45.63 C ANISOU 753 CG LEU A 119 8528 5792 3016 216 -930 59 C ATOM 754 CD1 LEU A 119 -4.733 28.785 -8.672 1.00 45.84 C ANISOU 754 CD1 LEU A 119 8538 5838 3039 188 -933 115 C ATOM 755 CD2 LEU A 119 -4.227 26.682 -7.402 1.00 47.79 C ANISOU 755 CD2 LEU A 119 8815 6029 3312 207 -980 48 C ATOM 756 N ARG A 120 -1.631 24.236 -9.730 1.00 42.92 N ANISOU 756 N ARG A 120 8287 5420 2600 297 -972 -131 N ATOM 757 CA ARG A 120 -1.651 22.810 -9.393 1.00 43.38 C ANISOU 757 CA ARG A 120 8369 5421 2691 305 -1027 -180 C ATOM 758 C ARG A 120 -0.287 22.349 -8.846 1.00 48.90 C ANISOU 758 C ARG A 120 9057 6102 3419 338 -998 -218 C ATOM 759 O ARG A 120 -0.239 21.469 -7.979 1.00 48.70 O ANISOU 759 O ARG A 120 9027 6024 3454 333 -1032 -225 O ATOM 760 CB ARG A 120 -2.028 21.965 -10.629 1.00 43.17 C ANISOU 760 CB ARG A 120 8383 5399 2621 319 -1074 -240 C ATOM 761 CG ARG A 120 -2.270 20.493 -10.307 1.00 49.90 C ANISOU 761 CG ARG A 120 9255 6174 3531 321 -1150 -286 C ATOM 762 CD ARG A 120 -2.319 19.610 -11.527 1.00 55.31 C ANISOU 762 CD ARG A 120 9977 6860 4179 351 -1198 -375 C ATOM 763 NE ARG A 120 -1.021 19.539 -12.195 1.00 62.27 N ANISOU 763 NE ARG A 120 10861 7790 5008 409 -1154 -446 N ATOM 764 CZ ARG A 120 -0.751 18.749 -13.229 1.00 76.34 C ANISOU 764 CZ ARG A 120 12668 9587 6751 454 -1189 -545 C ATOM 765 NH1 ARG A 120 -1.680 17.931 -13.709 1.00 61.39 N ANISOU 765 NH1 ARG A 120 10799 7651 4875 447 -1273 -590 N ATOM 766 NH2 ARG A 120 0.457 18.746 -13.771 1.00 65.01 N ANISOU 766 NH2 ARG A 120 11228 8212 5261 512 -1143 -602 N ATOM 767 N GLU A 121 0.816 22.925 -9.374 1.00 46.19 N ANISOU 767 N GLU A 121 8706 5809 3035 369 -938 -232 N ATOM 768 CA GLU A 121 2.175 22.549 -8.975 1.00 46.33 C ANISOU 768 CA GLU A 121 8714 5817 3071 403 -906 -265 C ATOM 769 C GLU A 121 2.776 23.556 -8.002 1.00 51.08 C ANISOU 769 C GLU A 121 9274 6429 3704 393 -852 -214 C ATOM 770 O GLU A 121 3.609 23.171 -7.182 1.00 51.06 O ANISOU 770 O GLU A 121 9257 6404 3739 406 -836 -225 O ATOM 771 CB GLU A 121 3.091 22.412 -10.195 1.00 48.25 C ANISOU 771 CB GLU A 121 8973 6116 3244 453 -880 -319 C ATOM 772 CG GLU A 121 2.644 21.315 -11.152 1.00 61.30 C ANISOU 772 CG GLU A 121 10664 7762 4865 474 -939 -394 C ATOM 773 CD GLU A 121 2.578 19.912 -10.574 1.00 84.68 C ANISOU 773 CD GLU A 121 13643 10634 7899 475 -1003 -445 C ATOM 774 OE1 GLU A 121 3.461 19.554 -9.761 1.00 79.76 O ANISOU 774 OE1 GLU A 121 13004 9972 7330 482 -988 -444 O ATOM 775 OE2 GLU A 121 1.686 19.143 -10.998 1.00 81.48 O ANISOU 775 OE2 GLU A 121 13263 10197 7498 470 -1072 -484 O ATOM 776 N GLY A 122 2.345 24.816 -8.085 1.00 47.76 N ANISOU 776 N GLY A 122 8830 6039 3276 372 -831 -160 N ATOM 777 CA GLY A 122 2.813 25.888 -7.209 1.00 46.90 C ANISOU 777 CA GLY A 122 8678 5935 3208 364 -792 -119 C ATOM 778 C GLY A 122 2.514 25.639 -5.745 1.00 49.55 C ANISOU 778 C GLY A 122 8991 6233 3603 347 -811 -111 C ATOM 779 O GLY A 122 3.295 26.034 -4.877 1.00 48.41 O ANISOU 779 O GLY A 122 8813 6088 3492 355 -781 -107 O ATOM 780 N SER A 123 1.393 24.940 -5.473 1.00 46.36 N ANISOU 780 N SER A 123 8600 5805 3209 326 -863 -106 N ATOM 781 CA SER A 123 0.950 24.577 -4.130 1.00 46.27 C ANISOU 781 CA SER A 123 8558 5779 3246 310 -890 -86 C ATOM 782 C SER A 123 1.920 23.560 -3.470 1.00 51.50 C ANISOU 782 C SER A 123 9210 6418 3939 328 -887 -111 C ATOM 783 O SER A 123 2.025 23.538 -2.243 1.00 50.50 O ANISOU 783 O SER A 123 9038 6299 3849 323 -886 -89 O ATOM 784 CB SER A 123 -0.464 24.004 -4.176 1.00 49.66 C ANISOU 784 CB SER A 123 9000 6192 3677 284 -951 -61 C ATOM 785 OG SER A 123 -0.547 22.858 -5.005 1.00 59.73 O ANISOU 785 OG SER A 123 10319 7435 4942 288 -990 -96 O ATOM 786 N MET A 124 2.642 22.750 -4.282 1.00 49.61 N ANISOU 786 N MET A 124 9008 6159 3684 351 -884 -157 N ATOM 787 CA MET A 124 3.627 21.772 -3.792 1.00 49.99 C ANISOU 787 CA MET A 124 9048 6180 3766 370 -880 -184 C ATOM 788 C MET A 124 4.911 22.483 -3.347 1.00 55.60 C ANISOU 788 C MET A 124 9733 6919 4475 389 -814 -183 C ATOM 789 O MET A 124 5.481 22.127 -2.312 1.00 55.15 O ANISOU 789 O MET A 124 9640 6855 4458 390 -804 -174 O ATOM 790 CB MET A 124 3.953 20.710 -4.863 1.00 52.75 C ANISOU 790 CB MET A 124 9444 6501 4099 397 -905 -246 C ATOM 791 CG MET A 124 2.750 19.909 -5.344 1.00 56.61 C ANISOU 791 CG MET A 124 9958 6952 4598 381 -980 -256 C ATOM 792 SD MET A 124 1.880 18.961 -4.070 1.00 60.70 S ANISOU 792 SD MET A 124 10436 7420 5207 344 -1050 -202 S ATOM 793 CE MET A 124 3.157 17.817 -3.557 1.00 57.63 C ANISOU 793 CE MET A 124 10027 6988 4881 369 -1047 -233 C ATOM 794 N PHE A 125 5.366 23.481 -4.141 1.00 53.51 N ANISOU 794 N PHE A 125 9477 6687 4168 403 -772 -185 N ATOM 795 CA PHE A 125 6.558 24.290 -3.867 1.00 53.85 C ANISOU 795 CA PHE A 125 9493 6754 4213 419 -715 -175 C ATOM 796 C PHE A 125 6.354 25.157 -2.631 1.00 56.75 C ANISOU 796 C PHE A 125 9810 7130 4623 399 -708 -144 C ATOM 797 O PHE A 125 7.295 25.317 -1.856 1.00 56.59 O ANISOU 797 O PHE A 125 9759 7116 4627 409 -677 -143 O ATOM 798 CB PHE A 125 6.912 25.170 -5.072 1.00 56.64 C ANISOU 798 CB PHE A 125 9856 7144 4518 434 -684 -166 C ATOM 799 CG PHE A 125 7.562 24.445 -6.228 1.00 59.60 C ANISOU 799 CG PHE A 125 10266 7539 4839 470 -676 -205 C ATOM 800 CD1 PHE A 125 8.912 24.619 -6.507 1.00 63.54 C ANISOU 800 CD1 PHE A 125 10754 8070 5318 503 -628 -204 C ATOM 801 CD2 PHE A 125 6.836 23.554 -7.012 1.00 62.56 C ANISOU 801 CD2 PHE A 125 10680 7905 5184 477 -719 -246 C ATOM 802 CE1 PHE A 125 9.508 23.964 -7.589 1.00 65.28 C ANISOU 802 CE1 PHE A 125 10999 8324 5478 546 -620 -244 C ATOM 803 CE2 PHE A 125 7.441 22.876 -8.071 1.00 66.15 C ANISOU 803 CE2 PHE A 125 11161 8387 5585 520 -716 -298 C ATOM 804 CZ PHE A 125 8.772 23.087 -8.356 1.00 64.55 C ANISOU 804 CZ PHE A 125 10946 8228 5354 557 -664 -298 C ATOM 805 N VAL A 126 5.127 25.699 -2.432 1.00 52.19 N ANISOU 805 N VAL A 126 9221 6557 4051 375 -738 -121 N ATOM 806 CA VAL A 126 4.781 26.501 -1.248 1.00 50.97 C ANISOU 806 CA VAL A 126 9014 6420 3931 365 -741 -104 C ATOM 807 C VAL A 126 4.806 25.570 -0.006 1.00 54.26 C ANISOU 807 C VAL A 126 9398 6845 4374 363 -756 -103 C ATOM 808 O VAL A 126 5.339 25.961 1.039 1.00 53.48 O ANISOU 808 O VAL A 126 9250 6771 4298 371 -737 -105 O ATOM 809 CB VAL A 126 3.421 27.234 -1.413 1.00 54.11 C ANISOU 809 CB VAL A 126 9407 6827 4324 345 -771 -81 C ATOM 810 CG1 VAL A 126 3.005 27.944 -0.123 1.00 53.50 C ANISOU 810 CG1 VAL A 126 9271 6778 4279 344 -781 -76 C ATOM 811 CG2 VAL A 126 3.475 28.225 -2.573 1.00 53.90 C ANISOU 811 CG2 VAL A 126 9396 6799 4283 344 -753 -70 C ATOM 812 N ALA A 127 4.296 24.320 -0.157 1.00 50.64 N ANISOU 812 N ALA A 127 8961 6365 3916 354 -794 -97 N ATOM 813 CA ALA A 127 4.286 23.302 0.901 1.00 50.11 C ANISOU 813 CA ALA A 127 8854 6303 3882 349 -816 -78 C ATOM 814 C ALA A 127 5.702 22.815 1.205 1.00 53.21 C ANISOU 814 C ALA A 127 9237 6687 4293 367 -779 -96 C ATOM 815 O ALA A 127 5.966 22.432 2.342 1.00 52.65 O ANISOU 815 O ALA A 127 9111 6643 4251 365 -778 -75 O ATOM 816 CB ALA A 127 3.406 22.130 0.504 1.00 51.16 C ANISOU 816 CB ALA A 127 9010 6400 4029 333 -876 -62 C ATOM 817 N LEU A 128 6.613 22.837 0.199 1.00 49.46 N ANISOU 817 N LEU A 128 8810 6186 3797 387 -748 -131 N ATOM 818 CA LEU A 128 8.017 22.471 0.395 1.00 49.21 C ANISOU 818 CA LEU A 128 8772 6148 3776 407 -707 -147 C ATOM 819 C LEU A 128 8.768 23.609 1.076 1.00 54.19 C ANISOU 819 C LEU A 128 9364 6816 4409 413 -661 -141 C ATOM 820 O LEU A 128 9.449 23.371 2.077 1.00 53.60 O ANISOU 820 O LEU A 128 9247 6759 4361 416 -642 -133 O ATOM 821 CB LEU A 128 8.710 22.099 -0.930 1.00 49.39 C ANISOU 821 CB LEU A 128 8852 6146 3767 433 -691 -185 C ATOM 822 CG LEU A 128 10.252 21.932 -0.878 1.00 53.97 C ANISOU 822 CG LEU A 128 9429 6730 4348 461 -641 -199 C ATOM 823 CD1 LEU A 128 10.680 20.823 0.080 1.00 54.14 C ANISOU 823 CD1 LEU A 128 9418 6730 4421 457 -650 -192 C ATOM 824 CD2 LEU A 128 10.822 21.679 -2.245 1.00 56.99 C ANISOU 824 CD2 LEU A 128 9861 7110 4685 494 -628 -237 C ATOM 825 N SER A 129 8.666 24.837 0.515 1.00 51.80 N ANISOU 825 N SER A 129 9070 6523 4087 415 -646 -142 N ATOM 826 CA SER A 129 9.334 26.039 1.020 1.00 52.02 C ANISOU 826 CA SER A 129 9060 6572 4133 420 -614 -140 C ATOM 827 C SER A 129 9.056 26.222 2.515 1.00 56.39 C ANISOU 827 C SER A 129 9549 7160 4715 414 -626 -138 C ATOM 828 O SER A 129 10.005 26.341 3.289 1.00 55.57 O ANISOU 828 O SER A 129 9409 7074 4630 423 -599 -144 O ATOM 829 CB SER A 129 8.884 27.269 0.236 1.00 56.27 C ANISOU 829 CB SER A 129 9607 7108 4665 417 -617 -131 C ATOM 830 OG SER A 129 9.563 28.439 0.660 1.00 66.71 O ANISOU 830 OG SER A 129 10888 8436 6022 422 -597 -128 O ATOM 831 N ALA A 130 7.766 26.140 2.923 1.00 53.67 N ANISOU 831 N ALA A 130 9188 6836 4369 401 -667 -128 N ATOM 832 CA ALA A 130 7.319 26.254 4.313 1.00 53.58 C ANISOU 832 CA ALA A 130 9107 6882 4370 401 -684 -122 C ATOM 833 C ALA A 130 7.927 25.141 5.198 1.00 58.67 C ANISOU 833 C ALA A 130 9715 7551 5026 401 -676 -104 C ATOM 834 O ALA A 130 8.377 25.439 6.308 1.00 58.40 O ANISOU 834 O ALA A 130 9618 7572 5002 411 -662 -110 O ATOM 835 CB ALA A 130 5.805 26.198 4.374 1.00 54.21 C ANISOU 835 CB ALA A 130 9180 6982 4437 388 -730 -102 C ATOM 836 N SER A 131 7.982 23.883 4.688 1.00 55.75 N ANISOU 836 N SER A 131 9381 7141 4662 392 -688 -86 N ATOM 837 CA SER A 131 8.551 22.729 5.401 1.00 55.96 C ANISOU 837 CA SER A 131 9372 7177 4716 389 -686 -60 C ATOM 838 C SER A 131 10.037 22.928 5.719 1.00 60.05 C ANISOU 838 C SER A 131 9875 7700 5239 404 -633 -77 C ATOM 839 O SER A 131 10.460 22.618 6.833 1.00 59.39 O ANISOU 839 O SER A 131 9726 7666 5172 403 -623 -56 O ATOM 840 CB SER A 131 8.386 21.448 4.586 1.00 60.68 C ANISOU 840 CB SER A 131 10016 7707 5331 381 -715 -51 C ATOM 841 OG SER A 131 7.028 21.095 4.383 1.00 71.84 O ANISOU 841 OG SER A 131 11435 9113 6748 364 -772 -26 O ATOM 842 N VAL A 132 10.824 23.435 4.738 1.00 57.33 N ANISOU 842 N VAL A 132 9587 7314 4881 417 -599 -107 N ATOM 843 CA VAL A 132 12.272 23.670 4.862 1.00 57.30 C ANISOU 843 CA VAL A 132 9578 7310 4883 432 -549 -117 C ATOM 844 C VAL A 132 12.532 24.753 5.937 1.00 61.79 C ANISOU 844 C VAL A 132 10083 7934 5461 435 -535 -126 C ATOM 845 O VAL A 132 13.347 24.518 6.832 1.00 60.94 O ANISOU 845 O VAL A 132 9930 7860 5366 437 -512 -118 O ATOM 846 CB VAL A 132 12.913 24.056 3.496 1.00 61.21 C ANISOU 846 CB VAL A 132 10138 7763 5355 447 -523 -135 C ATOM 847 CG1 VAL A 132 14.379 24.458 3.651 1.00 60.95 C ANISOU 847 CG1 VAL A 132 10093 7737 5328 462 -473 -133 C ATOM 848 CG2 VAL A 132 12.780 22.917 2.492 1.00 61.32 C ANISOU 848 CG2 VAL A 132 10208 7735 5356 455 -537 -144 C ATOM 849 N PHE A 133 11.818 25.905 5.877 1.00 59.36 N ANISOU 849 N PHE A 133 9768 7637 5149 436 -554 -145 N ATOM 850 CA PHE A 133 12.003 26.980 6.857 1.00 59.54 C ANISOU 850 CA PHE A 133 9728 7706 5188 446 -553 -170 C ATOM 851 C PHE A 133 11.479 26.559 8.234 1.00 62.82 C ANISOU 851 C PHE A 133 10066 8206 5597 447 -571 -164 C ATOM 852 O PHE A 133 11.903 27.140 9.234 1.00 62.32 O ANISOU 852 O PHE A 133 9940 8199 5541 461 -564 -190 O ATOM 853 CB PHE A 133 11.336 28.291 6.420 1.00 61.92 C ANISOU 853 CB PHE A 133 10035 7991 5501 450 -576 -196 C ATOM 854 CG PHE A 133 11.924 28.888 5.162 1.00 64.44 C ANISOU 854 CG PHE A 133 10408 8246 5831 449 -559 -188 C ATOM 855 CD1 PHE A 133 13.192 29.460 5.172 1.00 68.07 C ANISOU 855 CD1 PHE A 133 10858 8688 6316 457 -528 -187 C ATOM 856 CD2 PHE A 133 11.169 28.983 4.000 1.00 67.65 C ANISOU 856 CD2 PHE A 133 10861 8620 6223 440 -576 -175 C ATOM 857 CE1 PHE A 133 13.733 30.023 4.012 1.00 69.47 C ANISOU 857 CE1 PHE A 133 11070 8822 6503 457 -515 -163 C ATOM 858 CE2 PHE A 133 11.707 29.552 2.840 1.00 70.99 C ANISOU 858 CE2 PHE A 133 11317 9004 6650 441 -560 -156 C ATOM 859 CZ PHE A 133 12.985 30.069 2.854 1.00 69.18 C ANISOU 859 CZ PHE A 133 11075 8765 6447 451 -530 -146 C ATOM 860 N SER A 134 10.602 25.534 8.296 1.00 59.14 N ANISOU 860 N SER A 134 9597 7755 5118 434 -599 -127 N ATOM 861 CA SER A 134 10.115 25.006 9.571 1.00 58.87 C ANISOU 861 CA SER A 134 9477 7815 5076 434 -618 -98 C ATOM 862 C SER A 134 11.244 24.263 10.280 1.00 62.50 C ANISOU 862 C SER A 134 9895 8302 5549 433 -586 -75 C ATOM 863 O SER A 134 11.466 24.494 11.464 1.00 61.39 O ANISOU 863 O SER A 134 9672 8255 5400 444 -580 -78 O ATOM 864 CB SER A 134 8.906 24.105 9.366 1.00 62.07 C ANISOU 864 CB SER A 134 9887 8220 5478 417 -661 -48 C ATOM 865 OG SER A 134 7.809 24.836 8.846 1.00 69.51 O ANISOU 865 OG SER A 134 10859 9149 6403 418 -690 -66 O ATOM 866 N LEU A 135 12.008 23.441 9.526 1.00 60.02 N ANISOU 866 N LEU A 135 9638 7912 5256 422 -563 -57 N ATOM 867 CA LEU A 135 13.187 22.713 10.009 1.00 60.29 C ANISOU 867 CA LEU A 135 9645 7954 5310 420 -528 -33 C ATOM 868 C LEU A 135 14.258 23.697 10.489 1.00 66.27 C ANISOU 868 C LEU A 135 10379 8739 6061 435 -488 -71 C ATOM 869 O LEU A 135 14.845 23.478 11.549 1.00 65.96 O ANISOU 869 O LEU A 135 10267 8769 6024 436 -470 -55 O ATOM 870 CB LEU A 135 13.742 21.799 8.907 1.00 60.16 C ANISOU 870 CB LEU A 135 9704 7841 5313 415 -516 -25 C ATOM 871 CG LEU A 135 12.874 20.599 8.530 1.00 64.79 C ANISOU 871 CG LEU A 135 10304 8388 5924 401 -562 10 C ATOM 872 CD1 LEU A 135 13.252 20.062 7.185 1.00 65.11 C ANISOU 872 CD1 LEU A 135 10434 8332 5972 408 -559 -16 C ATOM 873 CD2 LEU A 135 12.920 19.510 9.603 1.00 67.34 C ANISOU 873 CD2 LEU A 135 10541 8758 6287 385 -577 76 C ATOM 874 N LEU A 136 14.469 24.808 9.728 1.00 64.22 N ANISOU 874 N LEU A 136 10172 8429 5798 446 -480 -115 N ATOM 875 CA LEU A 136 15.361 25.928 10.069 1.00 64.64 C ANISOU 875 CA LEU A 136 10204 8494 5861 459 -458 -153 C ATOM 876 C LEU A 136 14.978 26.521 11.422 1.00 69.93 C ANISOU 876 C LEU A 136 10782 9264 6524 472 -479 -183 C ATOM 877 O LEU A 136 15.834 26.675 12.294 1.00 69.51 O ANISOU 877 O LEU A 136 10674 9261 6475 479 -458 -195 O ATOM 878 CB LEU A 136 15.295 27.019 8.965 1.00 64.83 C ANISOU 878 CB LEU A 136 10289 8448 5896 464 -464 -180 C ATOM 879 CG LEU A 136 15.912 28.415 9.271 1.00 69.77 C ANISOU 879 CG LEU A 136 10884 9072 6554 477 -464 -220 C ATOM 880 CD1 LEU A 136 17.426 28.351 9.447 1.00 70.02 C ANISOU 880 CD1 LEU A 136 10907 9096 6600 478 -423 -206 C ATOM 881 CD2 LEU A 136 15.577 29.415 8.176 1.00 72.04 C ANISOU 881 CD2 LEU A 136 11218 9293 6863 478 -482 -227 C ATOM 882 N ALA A 137 13.675 26.839 11.588 1.00 67.50 N ANISOU 882 N ALA A 137 10454 8993 6200 477 -520 -196 N ATOM 883 CA ALA A 137 13.098 27.410 12.801 1.00 67.57 C ANISOU 883 CA ALA A 137 10371 9113 6190 500 -547 -232 C ATOM 884 C ALA A 137 13.219 26.441 13.983 1.00 71.28 C ANISOU 884 C ALA A 137 10753 9694 6636 498 -539 -187 C ATOM 885 O ALA A 137 13.364 26.905 15.108 1.00 70.95 O ANISOU 885 O ALA A 137 10624 9760 6575 522 -543 -222 O ATOM 886 CB ALA A 137 11.642 27.771 12.569 1.00 68.37 C ANISOU 886 CB ALA A 137 10477 9226 6276 506 -591 -243 C ATOM 887 N ILE A 138 13.185 25.106 13.729 1.00 67.85 N ANISOU 887 N ILE A 138 10334 9239 6206 473 -530 -111 N ATOM 888 CA ILE A 138 13.334 24.092 14.784 1.00 68.07 C ANISOU 888 CA ILE A 138 10269 9368 6226 466 -524 -48 C ATOM 889 C ILE A 138 14.824 23.976 15.143 1.00 71.88 C ANISOU 889 C ILE A 138 10736 9852 6724 464 -476 -49 C ATOM 890 O ILE A 138 15.154 23.914 16.328 1.00 71.68 O ANISOU 890 O ILE A 138 10611 9946 6678 473 -467 -39 O ATOM 891 CB ILE A 138 12.724 22.703 14.404 1.00 71.45 C ANISOU 891 CB ILE A 138 10707 9764 6675 438 -545 40 C ATOM 892 CG1 ILE A 138 11.211 22.819 14.087 1.00 72.00 C ANISOU 892 CG1 ILE A 138 10790 9837 6730 438 -596 48 C ATOM 893 CG2 ILE A 138 12.941 21.693 15.543 1.00 72.61 C ANISOU 893 CG2 ILE A 138 10741 10020 6828 428 -543 120 C ATOM 894 CD1 ILE A 138 10.529 21.540 13.563 1.00 78.28 C ANISOU 894 CD1 ILE A 138 11603 10579 7559 409 -631 129 C ATOM 895 N ALA A 139 15.715 23.966 14.124 1.00 68.07 N ANISOU 895 N ALA A 139 10345 9248 6269 453 -445 -57 N ATOM 896 CA ALA A 139 17.168 23.878 14.315 1.00 67.70 C ANISOU 896 CA ALA A 139 10295 9190 6237 451 -397 -52 C ATOM 897 C ALA A 139 17.717 25.108 15.043 1.00 72.31 C ANISOU 897 C ALA A 139 10832 9831 6811 472 -390 -117 C ATOM 898 O ALA A 139 18.616 24.961 15.870 1.00 72.14 O ANISOU 898 O ALA A 139 10750 9875 6787 472 -363 -106 O ATOM 899 CB ALA A 139 17.865 23.725 12.980 1.00 68.18 C ANISOU 899 CB ALA A 139 10462 9120 6321 444 -371 -51 C ATOM 900 N ILE A 140 17.172 26.314 14.757 1.00 69.16 N ANISOU 900 N ILE A 140 10457 9408 6413 490 -420 -185 N ATOM 901 CA ILE A 140 17.631 27.544 15.406 1.00 69.02 C ANISOU 901 CA ILE A 140 10393 9430 6403 514 -428 -259 C ATOM 902 C ILE A 140 17.003 27.621 16.840 1.00 73.62 C ANISOU 902 C ILE A 140 10855 10173 6943 538 -454 -286 C ATOM 903 O ILE A 140 17.628 28.195 17.728 1.00 73.34 O ANISOU 903 O ILE A 140 10753 10209 6904 558 -452 -335 O ATOM 904 CB ILE A 140 17.323 28.819 14.547 1.00 71.89 C ANISOU 904 CB ILE A 140 10815 9701 6801 525 -458 -318 C ATOM 905 CG1 ILE A 140 18.283 29.991 14.841 1.00 72.46 C ANISOU 905 CG1 ILE A 140 10861 9755 6914 540 -463 -379 C ATOM 906 CG2 ILE A 140 15.843 29.235 14.523 1.00 72.31 C ANISOU 906 CG2 ILE A 140 10858 9778 6837 539 -506 -351 C ATOM 907 CD1 ILE A 140 19.779 29.758 14.438 1.00 78.83 C ANISOU 907 CD1 ILE A 140 11705 10502 7747 522 -416 -337 C ATOM 908 N GLU A 141 15.814 26.983 17.071 1.00 70.53 N ANISOU 908 N GLU A 141 10432 9848 6518 538 -478 -248 N ATOM 909 CA GLU A 141 15.140 26.947 18.383 1.00 70.75 C ANISOU 909 CA GLU A 141 10336 10051 6494 565 -503 -256 C ATOM 910 C GLU A 141 15.798 25.907 19.312 1.00 75.67 C ANISOU 910 C GLU A 141 10874 10781 7098 552 -471 -180 C ATOM 911 O GLU A 141 15.344 25.720 20.447 1.00 75.85 O ANISOU 911 O GLU A 141 10780 10967 7072 570 -487 -158 O ATOM 912 CB GLU A 141 13.642 26.645 18.237 1.00 72.11 C ANISOU 912 CB GLU A 141 10503 10256 6641 569 -543 -227 C ATOM 913 N ARG A 142 16.858 25.230 18.823 1.00 72.42 N ANISOU 913 N ARG A 142 10513 10281 6723 521 -428 -133 N ATOM 914 CA ARG A 142 17.664 24.283 19.594 1.00 72.43 C ANISOU 914 CA ARG A 142 10440 10358 6720 503 -392 -59 C ATOM 915 C ARG A 142 18.902 24.977 20.123 1.00 78.02 C ANISOU 915 C ARG A 142 11123 11092 7428 515 -363 -114 C ATOM 916 O ARG A 142 19.217 24.857 21.304 1.00 78.22 O ANISOU 916 O ARG A 142 11035 11266 7419 527 -355 -108 O ATOM 917 CB ARG A 142 18.060 23.041 18.761 1.00 70.65 C ANISOU 917 CB ARG A 142 10283 10018 6543 464 -366 31 C ATOM 918 CG ARG A 142 16.948 22.045 18.402 1.00 75.91 C ANISOU 918 CG ARG A 142 10954 10666 7223 446 -400 105 C ATOM 919 CD ARG A 142 16.418 21.232 19.574 1.00 78.35 C ANISOU 919 CD ARG A 142 11124 11133 7514 441 -417 193 C ATOM 920 NE ARG A 142 15.636 22.036 20.512 1.00 81.68 N ANISOU 920 NE ARG A 142 11452 11714 7870 477 -446 151 N ATOM 921 CZ ARG A 142 15.100 21.564 21.630 1.00 96.83 C ANISOU 921 CZ ARG A 142 13230 13809 9752 485 -464 221 C ATOM 922 NH1 ARG A 142 15.257 20.288 21.964 1.00 82.93 N ANISOU 922 NH1 ARG A 142 11403 12080 8027 452 -458 347 N ATOM 923 NH2 ARG A 142 14.394 22.359 22.420 1.00 87.26 N ANISOU 923 NH2 ARG A 142 11936 12749 8471 527 -491 169 N ATOM 924 N TYR A 143 19.584 25.741 19.254 1.00 75.46 N ANISOU 924 N TYR A 143 10898 10632 7143 513 -351 -166 N ATOM 925 CA TYR A 143 20.812 26.462 19.576 1.00 76.02 C ANISOU 925 CA TYR A 143 10959 10695 7229 520 -329 -213 C ATOM 926 C TYR A 143 20.589 27.474 20.729 1.00 81.46 C ANISOU 926 C TYR A 143 11549 11514 7887 561 -365 -310 C ATOM 927 O TYR A 143 21.542 27.810 21.435 1.00 81.48 O ANISOU 927 O TYR A 143 11503 11565 7891 568 -351 -342 O ATOM 928 CB TYR A 143 21.326 27.187 18.317 1.00 77.15 C ANISOU 928 CB TYR A 143 11221 10670 7424 513 -326 -242 C ATOM 929 CG TYR A 143 22.712 27.770 18.464 1.00 79.50 C ANISOU 929 CG TYR A 143 11519 10935 7750 512 -302 -263 C ATOM 930 CD1 TYR A 143 23.841 27.010 18.179 1.00 81.47 C ANISOU 930 CD1 TYR A 143 11798 11145 8011 486 -247 -190 C ATOM 931 CD2 TYR A 143 22.897 29.093 18.853 1.00 80.95 C ANISOU 931 CD2 TYR A 143 11677 11120 7959 537 -338 -356 C ATOM 932 CE1 TYR A 143 25.124 27.537 18.322 1.00 83.13 C ANISOU 932 CE1 TYR A 143 12007 11330 8247 484 -226 -199 C ATOM 933 CE2 TYR A 143 24.174 29.630 19.008 1.00 82.32 C ANISOU 933 CE2 TYR A 143 11848 11262 8169 533 -324 -369 C ATOM 934 CZ TYR A 143 25.286 28.850 18.738 1.00 91.04 C ANISOU 934 CZ TYR A 143 12980 12336 9275 505 -265 -286 C ATOM 935 OH TYR A 143 26.548 29.380 18.878 1.00 93.48 O ANISOU 935 OH TYR A 143 13284 12614 9619 501 -252 -290 O ATOM 936 N ILE A 144 19.337 27.914 20.943 1.00 78.82 N ANISOU 936 N ILE A 144 11180 11245 7524 590 -412 -358 N ATOM 937 CA ILE A 144 19.015 28.909 21.965 1.00 79.77 C ANISOU 937 CA ILE A 144 11205 11491 7613 640 -454 -466 C ATOM 938 C ILE A 144 18.728 28.205 23.330 1.00 86.55 C ANISOU 938 C ILE A 144 11920 12572 8393 658 -449 -429 C ATOM 939 O ILE A 144 18.715 28.895 24.355 1.00 86.87 O ANISOU 939 O ILE A 144 11861 12751 8394 704 -475 -518 O ATOM 940 CB ILE A 144 17.814 29.785 21.498 1.00 82.80 C ANISOU 940 CB ILE A 144 11622 11832 8007 669 -509 -542 C ATOM 941 CG1 ILE A 144 18.092 30.372 20.089 1.00 82.82 C ANISOU 941 CG1 ILE A 144 11758 11623 8087 645 -511 -550 C ATOM 942 CG2 ILE A 144 17.508 30.913 22.509 1.00 83.95 C ANISOU 942 CG2 ILE A 144 11673 12095 8131 730 -560 -676 C ATOM 943 CD1 ILE A 144 16.925 31.097 19.410 1.00 90.94 C ANISOU 943 CD1 ILE A 144 12832 12587 9135 662 -559 -598 C ATOM 944 N THR A 145 18.560 26.850 23.364 1.00 84.56 N ANISOU 944 N THR A 145 11647 12358 8124 624 -419 -299 N ATOM 945 CA THR A 145 18.313 26.133 24.639 1.00 85.41 C ANISOU 945 CA THR A 145 11603 12685 8164 636 -415 -238 C ATOM 946 C THR A 145 19.520 26.307 25.582 1.00 91.80 C ANISOU 946 C THR A 145 12333 13594 8955 643 -385 -262 C ATOM 947 O THR A 145 19.340 26.720 26.734 1.00 92.18 O ANISOU 947 O THR A 145 12251 13838 8936 688 -404 -314 O ATOM 948 CB THR A 145 17.997 24.638 24.434 1.00 88.80 C ANISOU 948 CB THR A 145 12023 13113 8605 592 -397 -81 C ATOM 949 OG1 THR A 145 19.129 23.960 23.872 1.00 85.08 O ANISOU 949 OG1 THR A 145 11620 12513 8192 545 -348 -16 O ATOM 950 CG2 THR A 145 16.738 24.410 23.609 1.00 85.99 C ANISOU 950 CG2 THR A 145 11732 12679 8263 586 -433 -55 C ATOM 951 N MET A 146 20.744 26.043 25.069 1.00 89.05 N ANISOU 951 N MET A 146 12060 13114 8662 604 -341 -230 N ATOM 952 CA MET A 146 21.994 26.209 25.816 1.00 89.30 C ANISOU 952 CA MET A 146 12034 13209 8686 604 -310 -247 C ATOM 953 C MET A 146 22.314 27.725 25.988 1.00 93.62 C ANISOU 953 C MET A 146 12589 13741 9243 647 -347 -406 C ATOM 954 O MET A 146 22.610 28.158 27.105 1.00 93.80 O ANISOU 954 O MET A 146 12497 13926 9216 683 -361 -473 O ATOM 955 CB MET A 146 23.164 25.459 25.125 1.00 91.15 C ANISOU 955 CB MET A 146 12352 13302 8980 550 -252 -156 C ATOM 956 CG MET A 146 23.388 25.843 23.654 1.00 94.47 C ANISOU 956 CG MET A 146 12934 13490 9468 533 -251 -177 C ATOM 957 SD MET A 146 24.785 25.029 22.830 1.00 98.30 S ANISOU 957 SD MET A 146 13513 13828 10011 484 -185 -81 S ATOM 958 CE MET A 146 26.162 25.682 23.769 1.00 95.33 C ANISOU 958 CE MET A 146 13073 13520 9628 490 -162 -126 C ATOM 959 N LEU A 147 22.194 28.523 24.898 1.00 89.75 N ANISOU 959 N LEU A 147 12221 13062 8816 645 -370 -465 N ATOM 960 CA LEU A 147 22.464 29.963 24.889 1.00 89.74 C ANISOU 960 CA LEU A 147 12236 13007 8855 679 -416 -604 C ATOM 961 C LEU A 147 21.161 30.743 25.208 1.00 93.79 C ANISOU 961 C LEU A 147 12703 13595 9339 734 -482 -710 C ATOM 962 O LEU A 147 20.496 31.259 24.303 1.00 93.28 O ANISOU 962 O LEU A 147 12722 13403 9318 736 -512 -737 O ATOM 963 CB LEU A 147 23.058 30.373 23.513 1.00 89.33 C ANISOU 963 CB LEU A 147 12328 12721 8894 646 -408 -591 C ATOM 964 CG LEU A 147 23.528 31.832 23.323 1.00 94.53 C ANISOU 964 CG LEU A 147 13009 13283 9626 668 -457 -706 C ATOM 965 CD1 LEU A 147 24.681 32.182 24.265 1.00 95.27 C ANISOU 965 CD1 LEU A 147 13029 13447 9723 677 -454 -750 C ATOM 966 CD2 LEU A 147 23.964 32.072 21.895 1.00 96.43 C ANISOU 966 CD2 LEU A 147 13379 13313 9946 633 -447 -658 C ATOM 967 N LYS A 148 20.787 30.790 26.502 1.00 90.35 N ANISOU 967 N LYS A 148 12127 13379 8824 782 -502 -762 N ATOM 968 CA LYS A 148 19.578 31.485 26.944 1.00106.49 C ANISOU 968 CA LYS A 148 14109 15527 10826 845 -564 -866 C ATOM 969 C LYS A 148 19.927 32.459 28.069 1.00137.15 C ANISOU 969 C LYS A 148 17881 19545 14683 909 -608 -1019 C ATOM 970 O LYS A 148 20.872 33.235 27.938 1.00 99.32 O ANISOU 970 O LYS A 148 13124 14650 9964 908 -623 -1095 O ATOM 971 CB LYS A 148 18.510 30.473 27.393 1.00108.53 C ANISOU 971 CB LYS A 148 14290 15952 10995 850 -552 -768 C ATOM 972 CG LYS A 148 17.156 31.095 27.716 1.00117.74 C ANISOU 972 CG LYS A 148 15400 17223 12112 914 -611 -854 C ATOM 973 CD LYS A 148 16.143 30.038 28.116 1.00124.86 C ANISOU 973 CD LYS A 148 16223 18286 12930 913 -600 -732 C ATOM 974 CE LYS A 148 14.793 30.636 28.422 1.00132.81 C ANISOU 974 CE LYS A 148 17174 19407 13882 979 -656 -809 C ATOM 975 NZ LYS A 148 13.801 29.593 28.799 1.00139.37 N ANISOU 975 NZ LYS A 148 17920 20399 14635 975 -649 -672 N ATOM 976 N ASN A 156 8.904 36.618 24.182 1.00109.26 N ANISOU 976 N ASN A 156 14576 15744 11195 1155 -984 -1349 N ATOM 977 CA ASN A 156 9.305 35.837 23.013 1.00107.78 C ANISOU 977 CA ASN A 156 14516 15374 11059 1061 -932 -1207 C ATOM 978 C ASN A 156 8.188 34.836 22.637 1.00108.79 C ANISOU 978 C ASN A 156 14673 15538 11124 1028 -909 -1066 C ATOM 979 O ASN A 156 8.451 33.644 22.455 1.00107.89 O ANISOU 979 O ASN A 156 14590 15416 10987 971 -860 -933 O ATOM 980 CB ASN A 156 10.650 35.109 23.271 1.00109.78 C ANISOU 980 CB ASN A 156 14768 15631 11312 1021 -881 -1151 C ATOM 981 CG ASN A 156 10.696 34.189 24.483 1.00136.37 C ANISOU 981 CG ASN A 156 18018 19232 14565 1039 -853 -1096 C ATOM 982 OD1 ASN A 156 9.819 34.198 25.359 1.00131.84 O ANISOU 982 OD1 ASN A 156 17336 18857 13901 1098 -879 -1123 O ATOM 983 ND2 ASN A 156 11.761 33.404 24.579 1.00128.39 N ANISOU 983 ND2 ASN A 156 17016 18210 13556 992 -802 -1014 N ATOM 984 N ASN A 157 6.945 35.343 22.499 1.00103.43 N ANISOU 984 N ASN A 157 13982 14893 10425 1065 -949 -1098 N ATOM 985 CA ASN A 157 5.774 34.529 22.160 1.00101.89 C ANISOU 985 CA ASN A 157 13806 14734 10173 1040 -939 -972 C ATOM 986 C ASN A 157 5.025 35.140 20.968 1.00102.28 C ANISOU 986 C ASN A 157 13958 14613 10290 1020 -962 -979 C ATOM 987 O ASN A 157 4.612 34.398 20.077 1.00100.89 O ANISOU 987 O ASN A 157 13864 14350 10118 960 -939 -859 O ATOM 988 CB ASN A 157 4.848 34.385 23.371 1.00104.50 C ANISOU 988 CB ASN A 157 13995 15326 10385 1109 -963 -979 C ATOM 989 CG ASN A 157 5.488 33.704 24.569 1.00132.30 C ANISOU 989 CG ASN A 157 17396 19044 13828 1128 -940 -954 C ATOM 990 OD1 ASN A 157 6.367 32.838 24.443 1.00126.50 O ANISOU 990 OD1 ASN A 157 16691 18261 13114 1071 -894 -870 O ATOM 991 ND2 ASN A 157 5.005 34.028 25.765 1.00125.78 N ANISOU 991 ND2 ASN A 157 16426 18459 12905 1212 -970 -1017 N ATOM 992 N PHE A 158 4.864 36.484 20.942 1.00 97.24 N ANISOU 992 N PHE A 158 13311 13925 9711 1069 -1010 -1119 N ATOM 993 CA PHE A 158 4.233 37.201 19.825 1.00 95.85 C ANISOU 993 CA PHE A 158 13222 13583 9614 1051 -1035 -1130 C ATOM 994 C PHE A 158 5.113 37.141 18.590 1.00 96.86 C ANISOU 994 C PHE A 158 13470 13493 9838 974 -1004 -1071 C ATOM 995 O PHE A 158 4.616 36.885 17.491 1.00 95.88 O ANISOU 995 O PHE A 158 13437 13257 9736 924 -990 -985 O ATOM 996 CB PHE A 158 3.943 38.670 20.196 1.00 98.38 C ANISOU 996 CB PHE A 158 13486 13903 9990 1126 -1102 -1298 C ATOM 997 CG PHE A 158 3.718 39.589 19.011 1.00 99.71 C ANISOU 997 CG PHE A 158 13742 13861 10283 1099 -1128 -1317 C ATOM 998 CD1 PHE A 158 2.480 39.653 18.382 1.00102.61 C ANISOU 998 CD1 PHE A 158 14147 14199 10642 1091 -1140 -1270 C ATOM 999 CD2 PHE A 158 4.740 40.411 18.543 1.00101.82 C ANISOU 999 CD2 PHE A 158 14044 13965 10678 1081 -1143 -1374 C ATOM 1000 CE1 PHE A 158 2.279 40.496 17.283 1.00103.41 C ANISOU 1000 CE1 PHE A 158 14319 14114 10858 1063 -1162 -1276 C ATOM 1001 CE2 PHE A 158 4.536 41.255 17.447 1.00104.53 C ANISOU 1001 CE2 PHE A 158 14453 14124 11141 1053 -1170 -1373 C ATOM 1002 CZ PHE A 158 3.308 41.294 16.825 1.00102.51 C ANISOU 1002 CZ PHE A 158 14231 13844 10872 1044 -1177 -1324 C ATOM 1003 N ARG A 159 6.426 37.393 18.779 1.00 91.76 N ANISOU 1003 N ARG A 159 12821 12798 9244 968 -993 -1116 N ATOM 1004 CA ARG A 159 7.442 37.400 17.728 1.00 90.20 C ANISOU 1004 CA ARG A 159 12722 12417 9135 905 -964 -1064 C ATOM 1005 C ARG A 159 7.535 36.018 17.043 1.00 91.42 C ANISOU 1005 C ARG A 159 12950 12545 9239 838 -903 -913 C ATOM 1006 O ARG A 159 8.060 35.935 15.936 1.00 90.74 O ANISOU 1006 O ARG A 159 12957 12311 9209 786 -878 -854 O ATOM 1007 CB ARG A 159 8.812 37.815 18.302 1.00 90.67 C ANISOU 1007 CB ARG A 159 12743 12464 9244 918 -966 -1137 C ATOM 1008 CG ARG A 159 9.400 36.867 19.351 1.00102.58 C ANISOU 1008 CG ARG A 159 14186 14125 10663 925 -928 -1113 C ATOM 1009 CD ARG A 159 10.629 37.449 20.027 1.00115.80 C ANISOU 1009 CD ARG A 159 15811 15803 12386 948 -941 -1206 C ATOM 1010 NE ARG A 159 10.288 38.616 20.848 1.00127.94 N ANISOU 1010 NE ARG A 159 17255 17413 13944 1027 -1011 -1368 N ATOM 1011 CZ ARG A 159 11.155 39.288 21.599 1.00142.78 C ANISOU 1011 CZ ARG A 159 19069 19317 15864 1065 -1043 -1482 C ATOM 1012 NH1 ARG A 159 12.426 38.911 21.658 1.00131.03 N ANISOU 1012 NH1 ARG A 159 17599 17791 14398 1027 -1006 -1442 N ATOM 1013 NH2 ARG A 159 10.754 40.332 22.310 1.00129.14 N ANISOU 1013 NH2 ARG A 159 17255 17656 14157 1144 -1114 -1640 N ATOM 1014 N LEU A 160 6.993 34.955 17.682 1.00 86.24 N ANISOU 1014 N LEU A 160 12248 12036 8483 842 -885 -849 N ATOM 1015 CA LEU A 160 6.981 33.604 17.115 1.00 84.69 C ANISOU 1015 CA LEU A 160 12110 11816 8251 784 -841 -711 C ATOM 1016 C LEU A 160 5.900 33.494 16.023 1.00 86.86 C ANISOU 1016 C LEU A 160 12464 12005 8533 754 -852 -651 C ATOM 1017 O LEU A 160 6.210 33.058 14.910 1.00 86.06 O ANISOU 1017 O LEU A 160 12459 11775 8465 702 -825 -584 O ATOM 1018 CB LEU A 160 6.764 32.531 18.199 1.00 84.67 C ANISOU 1018 CB LEU A 160 12016 11996 8158 796 -828 -652 C ATOM 1019 CG LEU A 160 7.773 32.457 19.352 1.00 89.30 C ANISOU 1019 CG LEU A 160 12510 12700 8719 824 -814 -694 C ATOM 1020 CD1 LEU A 160 7.395 31.355 20.311 1.00 89.65 C ANISOU 1020 CD1 LEU A 160 12457 12930 8676 831 -804 -608 C ATOM 1021 CD2 LEU A 160 9.195 32.226 18.854 1.00 90.72 C ANISOU 1021 CD2 LEU A 160 12755 12757 8957 781 -772 -676 C ATOM 1022 N PHE A 161 4.646 33.938 16.321 1.00 82.22 N ANISOU 1022 N PHE A 161 11833 11494 7913 792 -892 -681 N ATOM 1023 CA PHE A 161 3.545 33.931 15.344 1.00 80.97 C ANISOU 1023 CA PHE A 161 11742 11263 7760 767 -906 -628 C ATOM 1024 C PHE A 161 3.738 35.096 14.343 1.00 79.71 C ANISOU 1024 C PHE A 161 11652 10939 7695 756 -918 -680 C ATOM 1025 O PHE A 161 2.824 35.449 13.590 1.00 79.37 O ANISOU 1025 O PHE A 161 11657 10833 7668 741 -935 -657 O ATOM 1026 CB PHE A 161 2.164 33.999 16.032 1.00 83.86 C ANISOU 1026 CB PHE A 161 12032 11771 8058 812 -943 -634 C ATOM 1027 CG PHE A 161 1.825 32.793 16.886 1.00 86.24 C ANISOU 1027 CG PHE A 161 12261 12235 8271 815 -935 -546 C ATOM 1028 CD1 PHE A 161 1.343 31.623 16.309 1.00 89.42 C ANISOU 1028 CD1 PHE A 161 12711 12611 8654 763 -926 -416 C ATOM 1029 CD2 PHE A 161 1.919 32.853 18.273 1.00 89.28 C ANISOU 1029 CD2 PHE A 161 12520 12808 8595 873 -945 -591 C ATOM 1030 CE1 PHE A 161 1.028 30.510 17.101 1.00 90.44 C ANISOU 1030 CE1 PHE A 161 12760 12884 8719 762 -927 -320 C ATOM 1031 CE2 PHE A 161 1.586 31.743 19.064 1.00 92.09 C ANISOU 1031 CE2 PHE A 161 12792 13325 8872 874 -940 -491 C ATOM 1032 CZ PHE A 161 1.139 30.583 18.472 1.00 89.67 C ANISOU 1032 CZ PHE A 161 12532 12977 8561 816 -933 -351 C ATOM 1033 N LEU A 162 4.954 35.662 14.345 1.00 71.94 N ANISOU 1033 N LEU A 162 10668 9889 6775 759 -912 -741 N ATOM 1034 CA LEU A 162 5.446 36.682 13.438 1.00 69.57 C ANISOU 1034 CA LEU A 162 10420 9434 6579 743 -923 -772 C ATOM 1035 C LEU A 162 6.487 36.034 12.534 1.00 70.47 C ANISOU 1035 C LEU A 162 10615 9448 6713 686 -874 -690 C ATOM 1036 O LEU A 162 6.589 36.384 11.364 1.00 69.55 O ANISOU 1036 O LEU A 162 10566 9211 6648 653 -870 -651 O ATOM 1037 CB LEU A 162 6.008 37.871 14.227 1.00 69.62 C ANISOU 1037 CB LEU A 162 10352 9447 6652 793 -963 -898 C ATOM 1038 CG LEU A 162 6.302 39.133 13.447 1.00 73.71 C ANISOU 1038 CG LEU A 162 10895 9814 7298 787 -996 -937 C ATOM 1039 CD1 LEU A 162 5.012 39.832 13.053 1.00 73.98 C ANISOU 1039 CD1 LEU A 162 10927 9825 7357 803 -1038 -957 C ATOM 1040 CD2 LEU A 162 7.096 40.089 14.285 1.00 76.29 C ANISOU 1040 CD2 LEU A 162 11148 10141 7699 831 -1037 -1056 C ATOM 1041 N LEU A 163 7.234 35.042 13.081 1.00 65.71 N ANISOU 1041 N LEU A 163 9998 8906 6062 678 -837 -659 N ATOM 1042 CA LEU A 163 8.203 34.225 12.341 1.00 64.63 C ANISOU 1042 CA LEU A 163 9931 8696 5929 631 -789 -582 C ATOM 1043 C LEU A 163 7.476 33.224 11.464 1.00 67.63 C ANISOU 1043 C LEU A 163 10380 9050 6266 594 -772 -490 C ATOM 1044 O LEU A 163 7.876 32.996 10.323 1.00 67.33 O ANISOU 1044 O LEU A 163 10420 8913 6249 560 -749 -442 O ATOM 1045 CB LEU A 163 9.182 33.485 13.282 1.00 64.50 C ANISOU 1045 CB LEU A 163 9868 8760 5879 637 -758 -578 C ATOM 1046 CG LEU A 163 10.198 34.315 14.068 1.00 69.42 C ANISOU 1046 CG LEU A 163 10433 9397 6547 666 -767 -661 C ATOM 1047 CD1 LEU A 163 10.976 33.444 15.027 1.00 69.43 C ANISOU 1047 CD1 LEU A 163 10377 9508 6497 672 -737 -648 C ATOM 1048 CD2 LEU A 163 11.162 35.052 13.142 1.00 72.02 C ANISOU 1048 CD2 LEU A 163 10819 9584 6962 642 -758 -656 C ATOM 1049 N ILE A 164 6.400 32.621 12.010 1.00 63.06 N ANISOU 1049 N ILE A 164 9767 8567 5626 604 -789 -466 N ATOM 1050 CA ILE A 164 5.547 31.656 11.320 1.00 61.92 C ANISOU 1050 CA ILE A 164 9675 8407 5445 571 -788 -383 C ATOM 1051 C ILE A 164 4.818 32.384 10.162 1.00 64.84 C ANISOU 1051 C ILE A 164 10109 8682 5846 557 -806 -382 C ATOM 1052 O ILE A 164 4.732 31.832 9.062 1.00 64.56 O ANISOU 1052 O ILE A 164 10150 8571 5808 520 -792 -325 O ATOM 1053 CB ILE A 164 4.568 30.983 12.329 1.00 65.01 C ANISOU 1053 CB ILE A 164 9992 8937 5771 589 -810 -352 C ATOM 1054 CG1 ILE A 164 5.370 30.176 13.397 1.00 65.19 C ANISOU 1054 CG1 ILE A 164 9946 9057 5767 596 -789 -333 C ATOM 1055 CG2 ILE A 164 3.555 30.075 11.602 1.00 65.92 C ANISOU 1055 CG2 ILE A 164 10157 9026 5862 554 -823 -265 C ATOM 1056 CD1 ILE A 164 4.557 29.544 14.555 1.00 70.61 C ANISOU 1056 CD1 ILE A 164 10530 9910 6389 618 -811 -290 C ATOM 1057 N SER A 165 4.354 33.636 10.392 1.00 60.50 N ANISOU 1057 N SER A 165 9523 8135 5329 587 -838 -449 N ATOM 1058 CA SER A 165 3.688 34.439 9.358 1.00 59.63 C ANISOU 1058 CA SER A 165 9459 7938 5260 574 -857 -445 C ATOM 1059 C SER A 165 4.680 34.821 8.255 1.00 62.09 C ANISOU 1059 C SER A 165 9829 8130 5632 546 -833 -428 C ATOM 1060 O SER A 165 4.339 34.725 7.078 1.00 61.77 O ANISOU 1060 O SER A 165 9853 8025 5593 514 -825 -374 O ATOM 1061 CB SER A 165 3.054 35.690 9.956 1.00 63.18 C ANISOU 1061 CB SER A 165 9845 8418 5745 618 -901 -526 C ATOM 1062 OG SER A 165 2.032 35.360 10.883 1.00 71.28 O ANISOU 1062 OG SER A 165 10812 9569 6702 649 -923 -534 O ATOM 1063 N ALA A 166 5.919 35.196 8.634 1.00 57.30 N ANISOU 1063 N ALA A 166 9195 7507 5070 558 -821 -468 N ATOM 1064 CA ALA A 166 6.982 35.542 7.689 1.00 56.42 C ANISOU 1064 CA ALA A 166 9124 7298 5014 535 -799 -441 C ATOM 1065 C ALA A 166 7.309 34.359 6.781 1.00 58.36 C ANISOU 1065 C ALA A 166 9445 7520 5208 500 -757 -363 C ATOM 1066 O ALA A 166 7.374 34.532 5.568 1.00 58.01 O ANISOU 1066 O ALA A 166 9451 7410 5179 477 -748 -318 O ATOM 1067 CB ALA A 166 8.227 35.984 8.440 1.00 57.34 C ANISOU 1067 CB ALA A 166 9192 7418 5175 554 -795 -491 C ATOM 1068 N CYS A 167 7.435 33.147 7.378 1.00 53.49 N ANISOU 1068 N CYS A 167 8829 6965 4531 499 -736 -347 N ATOM 1069 CA CYS A 167 7.739 31.859 6.735 1.00 52.30 C ANISOU 1069 CA CYS A 167 8737 6799 4335 474 -704 -288 C ATOM 1070 C CYS A 167 6.789 31.590 5.553 1.00 55.47 C ANISOU 1070 C CYS A 167 9201 7161 4713 451 -714 -246 C ATOM 1071 O CYS A 167 7.270 31.296 4.457 1.00 55.28 O ANISOU 1071 O CYS A 167 9234 7086 4684 435 -692 -214 O ATOM 1072 CB CYS A 167 7.655 30.729 7.760 1.00 52.08 C ANISOU 1072 CB CYS A 167 8674 6852 4263 479 -700 -278 C ATOM 1073 SG CYS A 167 7.830 29.068 7.059 1.00 55.52 S ANISOU 1073 SG CYS A 167 9172 7261 4663 450 -679 -212 S ATOM 1074 N TRP A 168 5.458 31.674 5.778 1.00 51.11 N ANISOU 1074 N TRP A 168 8634 6643 4141 452 -748 -245 N ATOM 1075 CA TRP A 168 4.462 31.406 4.742 1.00 50.61 C ANISOU 1075 CA TRP A 168 8625 6550 4054 429 -762 -204 C ATOM 1076 C TRP A 168 4.404 32.530 3.693 1.00 55.17 C ANISOU 1076 C TRP A 168 9227 7066 4670 421 -764 -201 C ATOM 1077 O TRP A 168 4.052 32.248 2.547 1.00 55.07 O ANISOU 1077 O TRP A 168 9269 7020 4635 400 -760 -162 O ATOM 1078 CB TRP A 168 3.075 31.199 5.345 1.00 49.11 C ANISOU 1078 CB TRP A 168 8406 6419 3834 433 -799 -196 C ATOM 1079 CG TRP A 168 2.926 29.872 6.021 1.00 49.80 C ANISOU 1079 CG TRP A 168 8477 6562 3883 429 -803 -163 C ATOM 1080 CD1 TRP A 168 3.096 29.602 7.345 1.00 52.73 C ANISOU 1080 CD1 TRP A 168 8775 7018 4243 450 -806 -174 C ATOM 1081 CD2 TRP A 168 2.662 28.615 5.385 1.00 49.57 C ANISOU 1081 CD2 TRP A 168 8499 6505 3831 402 -809 -112 C ATOM 1082 NE1 TRP A 168 2.912 28.260 7.582 1.00 52.11 N ANISOU 1082 NE1 TRP A 168 8693 6967 4141 434 -814 -118 N ATOM 1083 CE2 TRP A 168 2.643 27.630 6.395 1.00 53.48 C ANISOU 1083 CE2 TRP A 168 8943 7063 4313 405 -819 -84 C ATOM 1084 CE3 TRP A 168 2.426 28.224 4.053 1.00 50.95 C ANISOU 1084 CE3 TRP A 168 8750 6611 3997 378 -811 -89 C ATOM 1085 CZ2 TRP A 168 2.390 26.278 6.120 1.00 52.97 C ANISOU 1085 CZ2 TRP A 168 8902 6978 4244 382 -838 -31 C ATOM 1086 CZ3 TRP A 168 2.176 26.886 3.781 1.00 52.51 C ANISOU 1086 CZ3 TRP A 168 8975 6793 4181 360 -829 -53 C ATOM 1087 CH2 TRP A 168 2.155 25.930 4.805 1.00 53.19 C ANISOU 1087 CH2 TRP A 168 9011 6927 4272 360 -845 -23 C ATOM 1088 N VAL A 169 4.767 33.776 4.056 1.00 51.80 N ANISOU 1088 N VAL A 169 8753 6624 4305 439 -774 -238 N ATOM 1089 CA VAL A 169 4.779 34.879 3.089 1.00 51.65 C ANISOU 1089 CA VAL A 169 8740 6543 4343 429 -781 -221 C ATOM 1090 C VAL A 169 5.956 34.646 2.121 1.00 53.71 C ANISOU 1090 C VAL A 169 9038 6765 4604 415 -743 -180 C ATOM 1091 O VAL A 169 5.750 34.706 0.913 1.00 53.08 O ANISOU 1091 O VAL A 169 8994 6662 4513 397 -737 -132 O ATOM 1092 CB VAL A 169 4.831 36.272 3.768 1.00 56.56 C ANISOU 1092 CB VAL A 169 9292 7148 5050 452 -813 -274 C ATOM 1093 CG1 VAL A 169 5.069 37.383 2.747 1.00 56.99 C ANISOU 1093 CG1 VAL A 169 9341 7129 5185 437 -822 -239 C ATOM 1094 CG2 VAL A 169 3.552 36.542 4.557 1.00 56.50 C ANISOU 1094 CG2 VAL A 169 9247 7188 5032 473 -851 -316 C ATOM 1095 N ILE A 170 7.146 34.288 2.657 1.00 49.63 N ANISOU 1095 N ILE A 170 8511 6257 4090 426 -718 -196 N ATOM 1096 CA ILE A 170 8.371 33.969 1.898 1.00 49.60 C ANISOU 1096 CA ILE A 170 8537 6232 4079 421 -680 -159 C ATOM 1097 C ILE A 170 8.132 32.719 1.007 1.00 53.11 C ANISOU 1097 C ILE A 170 9048 6688 4443 410 -660 -128 C ATOM 1098 O ILE A 170 8.673 32.638 -0.102 1.00 52.35 O ANISOU 1098 O ILE A 170 8982 6580 4329 407 -637 -90 O ATOM 1099 CB ILE A 170 9.565 33.746 2.878 1.00 52.92 C ANISOU 1099 CB ILE A 170 8926 6666 4514 437 -660 -188 C ATOM 1100 CG1 ILE A 170 9.788 34.993 3.780 1.00 53.84 C ANISOU 1100 CG1 ILE A 170 8973 6770 4715 453 -690 -235 C ATOM 1101 CG2 ILE A 170 10.862 33.373 2.115 1.00 53.74 C ANISOU 1101 CG2 ILE A 170 9060 6754 4606 435 -618 -146 C ATOM 1102 CD1 ILE A 170 10.770 34.790 5.002 1.00 63.34 C ANISOU 1102 CD1 ILE A 170 10135 8004 5929 471 -678 -278 C ATOM 1103 N SER A 171 7.318 31.761 1.499 1.00 49.77 N ANISOU 1103 N SER A 171 8641 6294 3977 407 -673 -143 N ATOM 1104 CA SER A 171 6.965 30.534 0.782 1.00 49.66 C ANISOU 1104 CA SER A 171 8684 6282 3904 397 -670 -124 C ATOM 1105 C SER A 171 6.100 30.850 -0.449 1.00 53.70 C ANISOU 1105 C SER A 171 9229 6779 4395 382 -684 -96 C ATOM 1106 O SER A 171 6.447 30.423 -1.552 1.00 53.27 O ANISOU 1106 O SER A 171 9216 6719 4304 382 -668 -78 O ATOM 1107 CB SER A 171 6.235 29.564 1.709 1.00 53.20 C ANISOU 1107 CB SER A 171 9122 6760 4330 394 -692 -134 C ATOM 1108 OG SER A 171 7.056 29.191 2.804 1.00 60.85 O ANISOU 1108 OG SER A 171 10053 7755 5313 407 -677 -152 O ATOM 1109 N LEU A 172 5.003 31.631 -0.263 1.00 50.52 N ANISOU 1109 N LEU A 172 8803 6378 4015 373 -714 -93 N ATOM 1110 CA LEU A 172 4.083 32.066 -1.329 1.00 50.83 C ANISOU 1110 CA LEU A 172 8863 6406 4042 356 -730 -61 C ATOM 1111 C LEU A 172 4.811 32.849 -2.436 1.00 55.43 C ANISOU 1111 C LEU A 172 9442 6974 4643 354 -708 -24 C ATOM 1112 O LEU A 172 4.460 32.706 -3.610 1.00 55.88 O ANISOU 1112 O LEU A 172 9529 7041 4663 343 -706 10 O ATOM 1113 CB LEU A 172 2.953 32.941 -0.756 1.00 50.95 C ANISOU 1113 CB LEU A 172 8841 6426 4093 352 -763 -67 C ATOM 1114 CG LEU A 172 1.884 32.251 0.097 1.00 55.81 C ANISOU 1114 CG LEU A 172 9455 7074 4677 351 -792 -79 C ATOM 1115 CD1 LEU A 172 1.108 33.256 0.924 1.00 56.26 C ANISOU 1115 CD1 LEU A 172 9453 7149 4772 365 -819 -103 C ATOM 1116 CD2 LEU A 172 0.951 31.392 -0.751 1.00 58.16 C ANISOU 1116 CD2 LEU A 172 9806 7371 4922 328 -808 -45 C ATOM 1117 N ILE A 173 5.813 33.675 -2.059 1.00 51.04 N ANISOU 1117 N ILE A 173 8844 6403 4146 366 -695 -25 N ATOM 1118 CA ILE A 173 6.614 34.474 -2.984 1.00 50.61 C ANISOU 1118 CA ILE A 173 8767 6339 4122 364 -678 27 C ATOM 1119 C ILE A 173 7.472 33.537 -3.866 1.00 56.40 C ANISOU 1119 C ILE A 173 9542 7105 4784 375 -642 46 C ATOM 1120 O ILE A 173 7.430 33.685 -5.086 1.00 56.22 O ANISOU 1120 O ILE A 173 9526 7107 4728 372 -633 94 O ATOM 1121 CB ILE A 173 7.479 35.496 -2.209 1.00 53.11 C ANISOU 1121 CB ILE A 173 9021 6624 4533 374 -684 20 C ATOM 1122 CG1 ILE A 173 6.561 36.549 -1.528 1.00 53.22 C ANISOU 1122 CG1 ILE A 173 8989 6609 4624 370 -729 -8 C ATOM 1123 CG2 ILE A 173 8.488 36.175 -3.146 1.00 53.99 C ANISOU 1123 CG2 ILE A 173 9104 6731 4680 372 -669 91 C ATOM 1124 CD1 ILE A 173 7.246 37.566 -0.567 1.00 58.16 C ANISOU 1124 CD1 ILE A 173 9547 7197 5354 385 -751 -42 C ATOM 1125 N LEU A 174 8.202 32.561 -3.266 1.00 54.39 N ANISOU 1125 N LEU A 174 9309 6855 4501 392 -622 8 N ATOM 1126 CA LEU A 174 9.058 31.620 -4.014 1.00 55.05 C ANISOU 1126 CA LEU A 174 9429 6966 4520 410 -589 13 C ATOM 1127 C LEU A 174 8.239 30.660 -4.881 1.00 59.14 C ANISOU 1127 C LEU A 174 10001 7507 4963 410 -600 0 C ATOM 1128 O LEU A 174 8.581 30.465 -6.046 1.00 59.30 O ANISOU 1128 O LEU A 174 10036 7564 4930 424 -583 21 O ATOM 1129 CB LEU A 174 9.960 30.795 -3.082 1.00 55.18 C ANISOU 1129 CB LEU A 174 9452 6978 4537 426 -570 -26 C ATOM 1130 CG LEU A 174 11.069 31.564 -2.369 1.00 60.83 C ANISOU 1130 CG LEU A 174 10119 7680 5315 432 -554 -15 C ATOM 1131 CD1 LEU A 174 11.764 30.688 -1.340 1.00 61.23 C ANISOU 1131 CD1 LEU A 174 10172 7729 5362 442 -537 -54 C ATOM 1132 CD2 LEU A 174 12.087 32.140 -3.368 1.00 64.16 C ANISOU 1132 CD2 LEU A 174 10522 8119 5736 443 -528 44 C ATOM 1133 N GLY A 175 7.181 30.078 -4.314 1.00 55.18 N ANISOU 1133 N GLY A 175 9522 6987 4456 396 -630 -32 N ATOM 1134 CA GLY A 175 6.310 29.139 -5.016 1.00 54.91 C ANISOU 1134 CA GLY A 175 9537 6962 4365 392 -653 -47 C ATOM 1135 C GLY A 175 5.444 29.779 -6.082 1.00 58.43 C ANISOU 1135 C GLY A 175 9984 7428 4788 376 -665 -11 C ATOM 1136 O GLY A 175 5.016 29.101 -7.018 1.00 58.26 O ANISOU 1136 O GLY A 175 10000 7429 4706 380 -676 -21 O ATOM 1137 N GLY A 176 5.192 31.080 -5.932 1.00 54.60 N ANISOU 1137 N GLY A 176 9454 6935 4355 360 -668 28 N ATOM 1138 CA GLY A 176 4.371 31.866 -6.845 1.00 54.57 C ANISOU 1138 CA GLY A 176 9438 6948 4347 341 -680 76 C ATOM 1139 C GLY A 176 5.109 32.522 -7.997 1.00 58.87 C ANISOU 1139 C GLY A 176 9953 7537 4877 350 -654 133 C ATOM 1140 O GLY A 176 4.464 32.960 -8.952 1.00 59.13 O ANISOU 1140 O GLY A 176 9978 7603 4886 336 -661 178 O ATOM 1141 N LEU A 177 6.470 32.576 -7.941 1.00 54.96 N ANISOU 1141 N LEU A 177 9436 7053 4394 373 -624 143 N ATOM 1142 CA LEU A 177 7.326 33.162 -8.995 1.00 54.89 C ANISOU 1142 CA LEU A 177 9386 7100 4370 386 -598 212 C ATOM 1143 C LEU A 177 6.944 32.663 -10.411 1.00 57.85 C ANISOU 1143 C LEU A 177 9782 7555 4644 397 -593 227 C ATOM 1144 O LEU A 177 6.908 33.506 -11.311 1.00 57.32 O ANISOU 1144 O LEU A 177 9664 7538 4577 389 -588 307 O ATOM 1145 CB LEU A 177 8.823 32.867 -8.763 1.00 55.11 C ANISOU 1145 CB LEU A 177 9406 7139 4393 416 -565 206 C ATOM 1146 CG LEU A 177 9.496 33.417 -7.509 1.00 59.30 C ANISOU 1146 CG LEU A 177 9906 7609 5017 411 -565 197 C ATOM 1147 CD1 LEU A 177 10.904 32.864 -7.366 1.00 59.54 C ANISOU 1147 CD1 LEU A 177 9941 7658 5023 442 -530 188 C ATOM 1148 CD2 LEU A 177 9.513 34.935 -7.501 1.00 61.83 C ANISOU 1148 CD2 LEU A 177 10152 7904 5437 391 -582 268 C ATOM 1149 N PRO A 178 6.646 31.342 -10.652 1.00 54.13 N ANISOU 1149 N PRO A 178 9376 7101 4092 415 -599 155 N ATOM 1150 CA PRO A 178 6.280 30.918 -12.016 1.00 54.64 C ANISOU 1150 CA PRO A 178 9453 7248 4059 431 -600 157 C ATOM 1151 C PRO A 178 4.902 31.446 -12.444 1.00 59.10 C ANISOU 1151 C PRO A 178 10013 7817 4626 394 -627 192 C ATOM 1152 O PRO A 178 4.715 31.758 -13.624 1.00 59.06 O ANISOU 1152 O PRO A 178 9981 7896 4561 398 -621 239 O ATOM 1153 CB PRO A 178 6.275 29.392 -11.921 1.00 56.28 C ANISOU 1153 CB PRO A 178 9730 7442 4211 458 -613 57 C ATOM 1154 CG PRO A 178 6.003 29.101 -10.508 1.00 59.82 C ANISOU 1154 CG PRO A 178 10202 7795 4733 436 -632 20 C ATOM 1155 CD PRO A 178 6.675 30.180 -9.735 1.00 55.08 C ANISOU 1155 CD PRO A 178 9550 7168 4211 424 -609 70 C ATOM 1156 N ILE A 179 3.951 31.567 -11.487 1.00 55.61 N ANISOU 1156 N ILE A 179 9589 7295 4246 360 -655 175 N ATOM 1157 CA ILE A 179 2.604 32.099 -11.745 1.00 55.74 C ANISOU 1157 CA ILE A 179 9601 7306 4273 324 -682 210 C ATOM 1158 C ILE A 179 2.741 33.591 -12.087 1.00 60.62 C ANISOU 1158 C ILE A 179 10140 7939 4952 305 -670 307 C ATOM 1159 O ILE A 179 2.102 34.081 -13.020 1.00 60.53 O ANISOU 1159 O ILE A 179 10103 7975 4919 286 -675 366 O ATOM 1160 CB ILE A 179 1.641 31.857 -10.537 1.00 58.37 C ANISOU 1160 CB ILE A 179 9966 7559 4654 300 -715 169 C ATOM 1161 CG1 ILE A 179 1.884 30.475 -9.853 1.00 59.20 C ANISOU 1161 CG1 ILE A 179 10124 7632 4738 320 -726 88 C ATOM 1162 CG2 ILE A 179 0.166 32.077 -10.949 1.00 58.39 C ANISOU 1162 CG2 ILE A 179 9980 7566 4640 267 -745 194 C ATOM 1163 CD1 ILE A 179 1.140 30.216 -8.482 1.00 67.78 C ANISOU 1163 CD1 ILE A 179 11222 8655 5875 301 -757 60 C ATOM 1164 N MET A 180 3.651 34.284 -11.364 1.00 57.62 N ANISOU 1164 N MET A 180 9718 7523 4653 310 -657 327 N ATOM 1165 CA MET A 180 3.963 35.701 -11.531 1.00 57.59 C ANISOU 1165 CA MET A 180 9631 7514 4738 294 -656 419 C ATOM 1166 C MET A 180 4.846 35.949 -12.777 1.00 61.67 C ANISOU 1166 C MET A 180 10095 8127 5209 312 -627 500 C ATOM 1167 O MET A 180 5.302 37.075 -12.966 1.00 61.83 O ANISOU 1167 O MET A 180 10035 8148 5311 301 -628 591 O ATOM 1168 CB MET A 180 4.668 36.246 -10.278 1.00 59.65 C ANISOU 1168 CB MET A 180 9864 7694 5105 297 -661 397 C ATOM 1169 N GLY A 181 5.074 34.919 -13.602 1.00 58.09 N ANISOU 1169 N GLY A 181 9679 7760 4633 342 -608 470 N ATOM 1170 CA GLY A 181 5.791 35.080 -14.865 1.00 58.70 C ANISOU 1170 CA GLY A 181 9701 7960 4643 367 -582 546 C ATOM 1171 C GLY A 181 7.092 34.344 -15.125 1.00 62.78 C ANISOU 1171 C GLY A 181 10228 8541 5085 419 -550 516 C ATOM 1172 O GLY A 181 7.493 34.239 -16.288 1.00 63.33 O ANISOU 1172 O GLY A 181 10260 8739 5063 450 -531 560 O ATOM 1173 N TRP A 182 7.791 33.862 -14.084 1.00 58.56 N ANISOU 1173 N TRP A 182 9732 7931 4585 433 -544 448 N ATOM 1174 CA TRP A 182 9.077 33.199 -14.321 1.00 58.41 C ANISOU 1174 CA TRP A 182 9719 7973 4502 484 -513 426 C ATOM 1175 C TRP A 182 8.828 31.727 -14.709 1.00 60.56 C ANISOU 1175 C TRP A 182 10068 8281 4660 521 -515 314 C ATOM 1176 O TRP A 182 8.946 30.813 -13.887 1.00 59.93 O ANISOU 1176 O TRP A 182 10052 8129 4591 530 -523 221 O ATOM 1177 CB TRP A 182 10.012 33.327 -13.102 1.00 56.92 C ANISOU 1177 CB TRP A 182 9532 7697 4399 484 -503 410 C ATOM 1178 CG TRP A 182 11.395 32.762 -13.302 1.00 58.30 C ANISOU 1178 CG TRP A 182 9704 7929 4516 534 -469 401 C ATOM 1179 CD1 TRP A 182 12.071 32.641 -14.484 1.00 61.93 C ANISOU 1179 CD1 TRP A 182 10128 8524 4880 577 -443 447 C ATOM 1180 CD2 TRP A 182 12.352 32.495 -12.269 1.00 57.84 C ANISOU 1180 CD2 TRP A 182 9661 7808 4506 543 -454 368 C ATOM 1181 NE1 TRP A 182 13.340 32.165 -14.256 1.00 61.46 N ANISOU 1181 NE1 TRP A 182 10072 8483 4797 618 -414 430 N ATOM 1182 CE2 TRP A 182 13.548 32.088 -12.902 1.00 62.27 C ANISOU 1182 CE2 TRP A 182 10207 8461 4992 594 -419 386 C ATOM 1183 CE3 TRP A 182 12.312 32.546 -10.864 1.00 58.42 C ANISOU 1183 CE3 TRP A 182 9758 7767 4674 517 -467 323 C ATOM 1184 CZ2 TRP A 182 14.688 31.718 -12.178 1.00 61.43 C ANISOU 1184 CZ2 TRP A 182 10111 8325 4906 615 -396 364 C ATOM 1185 CZ3 TRP A 182 13.429 32.148 -10.148 1.00 59.71 C ANISOU 1185 CZ3 TRP A 182 9929 7905 4852 537 -444 298 C ATOM 1186 CH2 TRP A 182 14.600 31.741 -10.802 1.00 60.85 C ANISOU 1186 CH2 TRP A 182 10062 8132 4926 583 -409 320 C ATOM 1187 N ASN A 183 8.504 31.526 -15.994 1.00 56.27 N ANISOU 1187 N ASN A 183 9510 7857 4014 544 -514 327 N ATOM 1188 CA ASN A 183 8.205 30.229 -16.596 1.00 55.91 C ANISOU 1188 CA ASN A 183 9525 7859 3859 585 -526 219 C ATOM 1189 C ASN A 183 8.844 30.139 -18.010 1.00 60.81 C ANISOU 1189 C ASN A 183 10094 8658 4355 643 -502 249 C ATOM 1190 O ASN A 183 9.826 30.844 -18.270 1.00 60.85 O ANISOU 1190 O ASN A 183 10026 8734 4362 659 -470 344 O ATOM 1191 CB ASN A 183 6.690 30.013 -16.643 1.00 54.36 C ANISOU 1191 CB ASN A 183 9372 7617 3663 547 -567 181 C ATOM 1192 CG ASN A 183 5.894 31.109 -17.317 1.00 69.75 C ANISOU 1192 CG ASN A 183 11263 9619 5618 508 -571 284 C ATOM 1193 OD1 ASN A 183 6.216 31.583 -18.413 1.00 66.63 O ANISOU 1193 OD1 ASN A 183 10802 9359 5157 529 -551 357 O ATOM 1194 ND2 ASN A 183 4.784 31.480 -16.706 1.00 57.79 N ANISOU 1194 ND2 ASN A 183 9769 8010 4178 454 -598 293 N ATOM 1195 N CYS A 184 8.304 29.274 -18.910 1.00 57.51 N ANISOU 1195 N CYS A 184 9706 8316 3828 677 -522 168 N ATOM 1196 CA CYS A 184 8.895 29.048 -20.232 1.00 58.12 C ANISOU 1196 CA CYS A 184 9733 8579 3769 745 -502 172 C ATOM 1197 C CYS A 184 7.817 28.949 -21.329 1.00 62.46 C ANISOU 1197 C CYS A 184 10275 9227 4230 746 -528 157 C ATOM 1198 O CYS A 184 8.095 28.371 -22.381 1.00 63.02 O ANISOU 1198 O CYS A 184 10328 9445 4171 813 -526 103 O ATOM 1199 CB CYS A 184 9.728 27.770 -20.192 1.00 58.65 C ANISOU 1199 CB CYS A 184 9850 8655 3778 816 -501 43 C ATOM 1200 SG CYS A 184 8.760 26.260 -19.898 1.00 62.43 S ANISOU 1200 SG CYS A 184 10441 9021 4258 821 -563 -139 S ATOM 1201 N ILE A 185 6.626 29.540 -21.118 1.00 58.72 N ANISOU 1201 N ILE A 185 9806 8685 3819 676 -550 206 N ATOM 1202 CA ILE A 185 5.469 29.418 -22.023 1.00 59.29 C ANISOU 1202 CA ILE A 185 9880 8828 3820 665 -577 191 C ATOM 1203 C ILE A 185 5.880 29.759 -23.524 1.00 65.38 C ANISOU 1203 C ILE A 185 10554 9835 4452 718 -552 255 C ATOM 1204 O ILE A 185 5.271 29.207 -24.454 1.00 66.22 O ANISOU 1204 O ILE A 185 10668 10041 4451 746 -575 188 O ATOM 1205 CB ILE A 185 4.281 30.296 -21.549 1.00 61.66 C ANISOU 1205 CB ILE A 185 10178 9031 4220 580 -594 273 C ATOM 1206 CG1 ILE A 185 3.919 29.976 -20.085 1.00 61.34 C ANISOU 1206 CG1 ILE A 185 10219 8790 4297 539 -619 211 C ATOM 1207 CG2 ILE A 185 3.068 30.071 -22.429 1.00 62.85 C ANISOU 1207 CG2 ILE A 185 10334 9250 4296 566 -622 258 C ATOM 1208 CD1 ILE A 185 2.804 30.858 -19.459 1.00 71.61 C ANISOU 1208 CD1 ILE A 185 11516 9991 5700 462 -635 284 C ATOM 1209 N SER A 186 6.928 30.580 -23.750 1.00 62.01 N ANISOU 1209 N SER A 186 10033 9504 4023 736 -509 378 N ATOM 1210 CA SER A 186 7.396 30.838 -25.121 1.00 62.98 C ANISOU 1210 CA SER A 186 10052 9868 4008 792 -484 446 C ATOM 1211 C SER A 186 8.746 30.154 -25.373 1.00 66.93 C ANISOU 1211 C SER A 186 10542 10467 4421 883 -460 387 C ATOM 1212 O SER A 186 9.101 29.906 -26.531 1.00 67.90 O ANISOU 1212 O SER A 186 10601 10803 4396 955 -447 383 O ATOM 1213 CB SER A 186 7.509 32.333 -25.405 1.00 66.74 C ANISOU 1213 CB SER A 186 10403 10416 4537 747 -459 657 C ATOM 1214 OG SER A 186 7.949 32.564 -26.735 1.00 76.65 O ANISOU 1214 OG SER A 186 11546 11924 5654 803 -436 736 O ATOM 1215 N ALA A 187 9.496 29.858 -24.290 1.00 61.71 N ANISOU 1215 N ALA A 187 9937 9662 3847 882 -452 344 N ATOM 1216 CA ALA A 187 10.811 29.230 -24.378 1.00 61.50 C ANISOU 1216 CA ALA A 187 9906 9705 3755 963 -427 292 C ATOM 1217 C ALA A 187 10.709 27.711 -24.175 1.00 63.92 C ANISOU 1217 C ALA A 187 10322 9942 4024 1012 -459 83 C ATOM 1218 O ALA A 187 11.075 27.199 -23.111 1.00 62.85 O ANISOU 1218 O ALA A 187 10257 9648 3976 1002 -463 17 O ATOM 1219 CB ALA A 187 11.756 29.842 -23.348 1.00 61.55 C ANISOU 1219 CB ALA A 187 9897 9605 3883 933 -399 383 C ATOM 1220 N LEU A 188 10.233 26.988 -25.216 1.00 59.91 N ANISOU 1220 N LEU A 188 9818 9558 3386 1068 -485 -21 N ATOM 1221 CA LEU A 188 10.124 25.524 -25.194 1.00 59.23 C ANISOU 1221 CA LEU A 188 9822 9420 3263 1124 -529 -225 C ATOM 1222 C LEU A 188 11.494 24.892 -24.935 1.00 63.64 C ANISOU 1222 C LEU A 188 10387 9992 3800 1198 -505 -286 C ATOM 1223 O LEU A 188 11.595 23.959 -24.137 1.00 62.92 O ANISOU 1223 O LEU A 188 10381 9745 3780 1202 -531 -405 O ATOM 1224 CB LEU A 188 9.528 24.990 -26.509 1.00 59.96 C ANISOU 1224 CB LEU A 188 9894 9679 3208 1183 -561 -317 C ATOM 1225 CG LEU A 188 8.053 25.286 -26.771 1.00 63.54 C ANISOU 1225 CG LEU A 188 10362 10100 3679 1113 -597 -296 C ATOM 1226 CD1 LEU A 188 7.692 24.964 -28.180 1.00 64.96 C ANISOU 1226 CD1 LEU A 188 10490 10497 3696 1177 -614 -348 C ATOM 1227 CD2 LEU A 188 7.150 24.522 -25.818 1.00 64.17 C ANISOU 1227 CD2 LEU A 188 10559 9947 3873 1062 -655 -410 C ATOM 1228 N SER A 189 12.553 25.479 -25.536 1.00 60.89 N ANISOU 1228 N SER A 189 9942 9826 3368 1250 -454 -184 N ATOM 1229 CA SER A 189 13.960 25.076 -25.404 1.00 61.14 C ANISOU 1229 CA SER A 189 9959 9906 3366 1324 -421 -206 C ATOM 1230 C SER A 189 14.458 25.111 -23.941 1.00 63.96 C ANISOU 1230 C SER A 189 10376 10047 3879 1268 -408 -186 C ATOM 1231 O SER A 189 15.437 24.435 -23.609 1.00 63.25 O ANISOU 1231 O SER A 189 10313 9936 3786 1322 -396 -258 O ATOM 1232 CB SER A 189 14.837 26.001 -26.240 1.00 65.26 C ANISOU 1232 CB SER A 189 10349 10656 3791 1364 -368 -43 C ATOM 1233 OG SER A 189 14.698 27.346 -25.813 1.00 72.92 O ANISOU 1233 OG SER A 189 11265 11574 4867 1272 -346 151 O ATOM 1234 N SER A 190 13.790 25.904 -23.086 1.00 59.95 N ANISOU 1234 N SER A 190 9884 9390 3505 1165 -411 -91 N ATOM 1235 CA SER A 190 14.154 26.092 -21.686 1.00 58.81 C ANISOU 1235 CA SER A 190 9783 9055 3507 1106 -400 -61 C ATOM 1236 C SER A 190 13.162 25.418 -20.719 1.00 62.51 C ANISOU 1236 C SER A 190 10355 9318 4080 1050 -447 -168 C ATOM 1237 O SER A 190 13.293 25.595 -19.503 1.00 61.32 O ANISOU 1237 O SER A 190 10237 9013 4051 996 -442 -144 O ATOM 1238 CB SER A 190 14.214 27.582 -21.375 1.00 61.95 C ANISOU 1238 CB SER A 190 10110 9441 3988 1035 -373 127 C ATOM 1239 OG SER A 190 15.148 28.277 -22.184 1.00 73.40 O ANISOU 1239 OG SER A 190 11453 11073 5363 1077 -333 254 O ATOM 1240 N CYS A 191 12.183 24.646 -21.239 1.00 59.95 N ANISOU 1240 N CYS A 191 10073 8996 3707 1063 -496 -280 N ATOM 1241 CA CYS A 191 11.179 23.994 -20.391 1.00 59.27 C ANISOU 1241 CA CYS A 191 10075 8726 3720 1010 -548 -367 C ATOM 1242 C CYS A 191 11.732 22.713 -19.779 1.00 62.47 C ANISOU 1242 C CYS A 191 10541 9033 4161 1050 -569 -498 C ATOM 1243 O CYS A 191 12.367 21.914 -20.473 1.00 63.67 O ANISOU 1243 O CYS A 191 10691 9275 4226 1136 -574 -596 O ATOM 1244 CB CYS A 191 9.902 23.705 -21.171 1.00 60.20 C ANISOU 1244 CB CYS A 191 10210 8878 3785 1003 -598 -424 C ATOM 1245 SG CYS A 191 8.963 25.184 -21.624 1.00 64.03 S ANISOU 1245 SG CYS A 191 10632 9428 4267 931 -582 -264 S ATOM 1246 N SER A 192 11.448 22.513 -18.474 1.00 56.51 N ANISOU 1246 N SER A 192 9836 8097 3537 988 -585 -501 N ATOM 1247 CA SER A 192 11.810 21.319 -17.706 1.00 55.72 C ANISOU 1247 CA SER A 192 9790 7878 3503 1007 -612 -606 C ATOM 1248 C SER A 192 11.024 20.099 -18.209 1.00 59.77 C ANISOU 1248 C SER A 192 10351 8362 3999 1039 -687 -752 C ATOM 1249 O SER A 192 9.894 20.263 -18.665 1.00 60.18 O ANISOU 1249 O SER A 192 10411 8425 4031 1010 -723 -754 O ATOM 1250 CB SER A 192 11.545 21.555 -16.226 1.00 57.82 C ANISOU 1250 CB SER A 192 10080 7982 3905 927 -612 -552 C ATOM 1251 OG SER A 192 11.772 20.386 -15.458 1.00 66.46 O ANISOU 1251 OG SER A 192 11218 8961 5074 936 -645 -641 O ATOM 1252 N THR A 193 11.620 18.886 -18.148 1.00 55.52 N ANISOU 1252 N THR A 193 9840 7783 3473 1098 -714 -873 N ATOM 1253 CA THR A 193 10.989 17.651 -18.646 1.00 55.55 C ANISOU 1253 CA THR A 193 9883 7750 3475 1137 -797 -1025 C ATOM 1254 C THR A 193 10.001 17.081 -17.611 1.00 57.52 C ANISOU 1254 C THR A 193 10180 7808 3868 1064 -861 -1038 C ATOM 1255 O THR A 193 8.929 16.604 -17.992 1.00 57.57 O ANISOU 1255 O THR A 193 10211 7778 3884 1052 -931 -1101 O ATOM 1256 CB THR A 193 12.059 16.602 -18.993 1.00 65.00 C ANISOU 1256 CB THR A 193 11079 8980 4637 1237 -806 -1151 C ATOM 1257 OG1 THR A 193 13.125 17.213 -19.724 1.00 65.86 O ANISOU 1257 OG1 THR A 193 11135 9269 4620 1301 -735 -1108 O ATOM 1258 CG2 THR A 193 11.493 15.401 -19.757 1.00 64.92 C ANISOU 1258 CG2 THR A 193 11097 8959 4610 1296 -897 -1324 C ATOM 1259 N VAL A 194 10.374 17.109 -16.318 1.00 52.08 N ANISOU 1259 N VAL A 194 9497 7007 3287 1016 -838 -976 N ATOM 1260 CA VAL A 194 9.548 16.594 -15.227 1.00 50.76 C ANISOU 1260 CA VAL A 194 9357 6675 3253 948 -893 -968 C ATOM 1261 C VAL A 194 8.379 17.616 -14.962 1.00 53.91 C ANISOU 1261 C VAL A 194 9754 7066 3664 866 -889 -862 C ATOM 1262 O VAL A 194 7.276 17.186 -14.609 1.00 53.08 O ANISOU 1262 O VAL A 194 9672 6868 3628 820 -953 -870 O ATOM 1263 CB VAL A 194 10.407 16.293 -13.964 1.00 53.61 C ANISOU 1263 CB VAL A 194 9712 6944 3711 933 -866 -936 C ATOM 1264 CG1 VAL A 194 11.344 17.440 -13.605 1.00 52.69 C ANISOU 1264 CG1 VAL A 194 9562 6898 3560 923 -772 -829 C ATOM 1265 CG2 VAL A 194 9.557 15.866 -12.776 1.00 52.82 C ANISOU 1265 CG2 VAL A 194 9623 6700 3744 860 -917 -902 C ATOM 1266 N LEU A 195 8.612 18.938 -15.204 1.00 50.56 N ANISOU 1266 N LEU A 195 9296 6741 3174 852 -820 -763 N ATOM 1267 CA LEU A 195 7.605 20.019 -15.095 1.00 49.92 C ANISOU 1267 CA LEU A 195 9204 6666 3096 784 -812 -664 C ATOM 1268 C LEU A 195 7.595 20.840 -16.415 1.00 55.22 C ANISOU 1268 C LEU A 195 9842 7493 3645 812 -781 -635 C ATOM 1269 O LEU A 195 8.374 21.784 -16.558 1.00 54.26 O ANISOU 1269 O LEU A 195 9676 7454 3486 820 -717 -554 O ATOM 1270 CB LEU A 195 7.829 20.937 -13.870 1.00 48.75 C ANISOU 1270 CB LEU A 195 9034 6467 3023 727 -765 -554 C ATOM 1271 CG LEU A 195 7.591 20.367 -12.460 1.00 52.51 C ANISOU 1271 CG LEU A 195 9527 6810 3617 685 -793 -552 C ATOM 1272 CD1 LEU A 195 8.770 19.542 -11.972 1.00 52.51 C ANISOU 1272 CD1 LEU A 195 9527 6775 3650 724 -780 -600 C ATOM 1273 CD2 LEU A 195 7.462 21.487 -11.470 1.00 54.76 C ANISOU 1273 CD2 LEU A 195 9782 7072 3951 629 -756 -449 C ATOM 1274 N PRO A 196 6.712 20.478 -17.383 1.00 53.76 N ANISOU 1274 N PRO A 196 9673 7352 3402 825 -831 -695 N ATOM 1275 CA PRO A 196 6.771 21.083 -18.728 1.00 55.02 C ANISOU 1275 CA PRO A 196 9792 7682 3433 863 -805 -678 C ATOM 1276 C PRO A 196 6.500 22.598 -18.816 1.00 60.80 C ANISOU 1276 C PRO A 196 10474 8477 4152 812 -754 -529 C ATOM 1277 O PRO A 196 6.845 23.175 -19.852 1.00 61.26 O ANISOU 1277 O PRO A 196 10479 8690 4107 847 -721 -490 O ATOM 1278 CB PRO A 196 5.653 20.363 -19.470 1.00 57.30 C ANISOU 1278 CB PRO A 196 10113 7970 3690 869 -879 -769 C ATOM 1279 CG PRO A 196 5.613 19.036 -18.839 1.00 61.58 C ANISOU 1279 CG PRO A 196 10704 8374 4318 881 -943 -879 C ATOM 1280 CD PRO A 196 5.789 19.326 -17.380 1.00 55.79 C ANISOU 1280 CD PRO A 196 9978 7516 3703 821 -918 -796 C ATOM 1281 N LEU A 197 5.897 23.242 -17.800 1.00 57.71 N ANISOU 1281 N LEU A 197 10089 7979 3859 735 -750 -445 N ATOM 1282 CA LEU A 197 5.649 24.692 -17.886 1.00 57.63 C ANISOU 1282 CA LEU A 197 10025 8018 3852 689 -709 -310 C ATOM 1283 C LEU A 197 6.666 25.487 -17.039 1.00 63.06 C ANISOU 1283 C LEU A 197 10678 8678 4605 676 -656 -227 C ATOM 1284 O LEU A 197 6.799 26.697 -17.230 1.00 62.83 O ANISOU 1284 O LEU A 197 10590 8700 4581 653 -621 -115 O ATOM 1285 CB LEU A 197 4.218 25.075 -17.467 1.00 56.80 C ANISOU 1285 CB LEU A 197 9940 7834 3806 616 -743 -268 C ATOM 1286 CG LEU A 197 3.109 24.976 -18.529 1.00 61.47 C ANISOU 1286 CG LEU A 197 10536 8494 4327 609 -779 -283 C ATOM 1287 CD1 LEU A 197 2.805 23.526 -18.920 1.00 62.24 C ANISOU 1287 CD1 LEU A 197 10686 8574 4386 650 -840 -423 C ATOM 1288 CD2 LEU A 197 1.850 25.621 -18.023 1.00 62.38 C ANISOU 1288 CD2 LEU A 197 10659 8535 4509 534 -798 -212 C ATOM 1289 N TYR A 198 7.395 24.807 -16.137 1.00 60.64 N ANISOU 1289 N TYR A 198 10399 8290 4350 692 -653 -278 N ATOM 1290 CA TYR A 198 8.418 25.420 -15.285 1.00 60.29 C ANISOU 1290 CA TYR A 198 10325 8215 4366 683 -607 -214 C ATOM 1291 C TYR A 198 9.733 25.588 -16.057 1.00 64.20 C ANISOU 1291 C TYR A 198 10775 8834 4785 745 -560 -191 C ATOM 1292 O TYR A 198 10.127 24.707 -16.831 1.00 63.98 O ANISOU 1292 O TYR A 198 10759 8880 4671 809 -567 -272 O ATOM 1293 CB TYR A 198 8.640 24.572 -14.011 1.00 61.22 C ANISOU 1293 CB TYR A 198 10486 8205 4568 673 -623 -272 C ATOM 1294 CG TYR A 198 7.693 24.874 -12.862 1.00 62.37 C ANISOU 1294 CG TYR A 198 10645 8242 4809 605 -649 -243 C ATOM 1295 CD1 TYR A 198 8.179 25.179 -11.598 1.00 63.85 C ANISOU 1295 CD1 TYR A 198 10823 8357 5081 582 -631 -217 C ATOM 1296 CD2 TYR A 198 6.323 24.987 -13.071 1.00 63.11 C ANISOU 1296 CD2 TYR A 198 10752 8323 4903 567 -686 -232 C ATOM 1297 CE1 TYR A 198 7.319 25.487 -10.543 1.00 64.29 C ANISOU 1297 CE1 TYR A 198 10881 8334 5211 529 -655 -192 C ATOM 1298 CE2 TYR A 198 5.454 25.319 -12.030 1.00 63.38 C ANISOU 1298 CE2 TYR A 198 10791 8273 5016 512 -708 -199 C ATOM 1299 CZ TYR A 198 5.956 25.559 -10.764 1.00 70.30 C ANISOU 1299 CZ TYR A 198 11656 9086 5970 496 -693 -182 C ATOM 1300 OH TYR A 198 5.109 25.891 -9.735 1.00 70.68 O ANISOU 1300 OH TYR A 198 11699 9071 6084 451 -715 -155 O ATOM 1301 N HIS A 199 10.394 26.738 -15.852 1.00 60.68 N ANISOU 1301 N HIS A 199 10271 8412 4373 727 -518 -79 N ATOM 1302 CA HIS A 199 11.670 27.064 -16.492 1.00 61.15 C ANISOU 1302 CA HIS A 199 10272 8590 4370 778 -473 -26 C ATOM 1303 C HIS A 199 12.811 26.354 -15.773 1.00 64.53 C ANISOU 1303 C HIS A 199 10725 8971 4823 811 -453 -76 C ATOM 1304 O HIS A 199 12.784 26.269 -14.539 1.00 64.31 O ANISOU 1304 O HIS A 199 10726 8816 4894 771 -458 -85 O ATOM 1305 CB HIS A 199 11.888 28.583 -16.481 1.00 61.89 C ANISOU 1305 CB HIS A 199 10288 8714 4515 739 -447 124 C ATOM 1306 CG HIS A 199 12.854 29.064 -17.514 1.00 66.30 C ANISOU 1306 CG HIS A 199 10766 9432 4992 787 -411 210 C ATOM 1307 ND1 HIS A 199 12.417 29.707 -18.660 1.00 68.93 N ANISOU 1307 ND1 HIS A 199 11034 9895 5260 789 -411 288 N ATOM 1308 CD2 HIS A 199 14.194 28.924 -17.579 1.00 68.39 C ANISOU 1308 CD2 HIS A 199 11002 9758 5224 837 -376 230 C ATOM 1309 CE1 HIS A 199 13.508 29.992 -19.350 1.00 69.01 C ANISOU 1309 CE1 HIS A 199 10970 10044 5205 839 -377 364 C ATOM 1310 NE2 HIS A 199 14.599 29.520 -18.753 1.00 69.10 N ANISOU 1310 NE2 HIS A 199 11004 10022 5230 871 -355 330 N ATOM 1311 N LYS A 200 13.819 25.854 -16.521 1.00 59.94 N ANISOU 1311 N LYS A 200 10127 8499 4148 887 -429 -107 N ATOM 1312 CA LYS A 200 14.962 25.149 -15.923 1.00 58.66 C ANISOU 1312 CA LYS A 200 9984 8302 4001 924 -407 -152 C ATOM 1313 C LYS A 200 15.709 26.063 -14.926 1.00 61.69 C ANISOU 1313 C LYS A 200 10334 8629 4478 882 -372 -48 C ATOM 1314 O LYS A 200 16.158 25.568 -13.893 1.00 61.04 O ANISOU 1314 O LYS A 200 10284 8451 4459 874 -367 -86 O ATOM 1315 CB LYS A 200 15.924 24.628 -16.994 1.00 60.97 C ANISOU 1315 CB LYS A 200 10250 8746 4169 1017 -384 -186 C ATOM 1316 CG LYS A 200 15.326 23.523 -17.847 1.00 67.91 C ANISOU 1316 CG LYS A 200 11168 9671 4964 1071 -426 -323 C ATOM 1317 CD LYS A 200 16.274 23.095 -18.948 1.00 78.15 C ANISOU 1317 CD LYS A 200 12426 11142 6126 1173 -404 -360 C ATOM 1318 CE LYS A 200 15.666 22.024 -19.821 1.00 86.51 C ANISOU 1318 CE LYS A 200 13516 12252 7101 1232 -454 -510 C ATOM 1319 NZ LYS A 200 16.561 21.651 -20.945 1.00 93.63 N ANISOU 1319 NZ LYS A 200 14371 13347 7858 1342 -434 -554 N ATOM 1320 N HIS A 201 15.766 27.395 -15.194 1.00 57.73 N ANISOU 1320 N HIS A 201 9764 8177 3995 852 -356 82 N ATOM 1321 CA HIS A 201 16.404 28.369 -14.300 1.00 56.94 C ANISOU 1321 CA HIS A 201 9624 8016 3995 811 -336 180 C ATOM 1322 C HIS A 201 15.653 28.492 -12.967 1.00 60.13 C ANISOU 1322 C HIS A 201 10069 8262 4517 744 -362 148 C ATOM 1323 O HIS A 201 16.281 28.794 -11.955 1.00 59.63 O ANISOU 1323 O HIS A 201 9996 8129 4533 723 -349 173 O ATOM 1324 CB HIS A 201 16.516 29.759 -14.946 1.00 58.16 C ANISOU 1324 CB HIS A 201 9687 8252 4158 792 -326 327 C ATOM 1325 CG HIS A 201 17.483 29.828 -16.086 1.00 62.51 C ANISOU 1325 CG HIS A 201 10173 8973 4606 855 -294 394 C ATOM 1326 ND1 HIS A 201 17.053 29.887 -17.392 1.00 65.08 N ANISOU 1326 ND1 HIS A 201 10463 9444 4821 890 -297 411 N ATOM 1327 CD2 HIS A 201 18.834 29.819 -16.074 1.00 64.61 C ANISOU 1327 CD2 HIS A 201 10401 9290 4856 892 -260 447 C ATOM 1328 CE1 HIS A 201 18.146 29.920 -18.134 1.00 65.32 C ANISOU 1328 CE1 HIS A 201 10429 9621 4770 949 -264 476 C ATOM 1329 NE2 HIS A 201 19.243 29.879 -17.384 1.00 65.37 N ANISOU 1329 NE2 HIS A 201 10434 9574 4831 953 -241 502 N ATOM 1330 N TYR A 202 14.326 28.282 -12.956 1.00 56.40 N ANISOU 1330 N TYR A 202 9635 7743 4053 714 -400 97 N ATOM 1331 CA TYR A 202 13.562 28.348 -11.711 1.00 55.44 C ANISOU 1331 CA TYR A 202 9544 7491 4029 659 -427 69 C ATOM 1332 C TYR A 202 13.856 27.109 -10.863 1.00 59.43 C ANISOU 1332 C TYR A 202 10104 7927 4549 673 -431 -26 C ATOM 1333 O TYR A 202 14.072 27.251 -9.661 1.00 58.79 O ANISOU 1333 O TYR A 202 10022 7768 4547 645 -428 -23 O ATOM 1334 CB TYR A 202 12.050 28.497 -11.976 1.00 56.57 C ANISOU 1334 CB TYR A 202 9706 7615 4174 623 -466 56 C ATOM 1335 CG TYR A 202 11.188 28.433 -10.729 1.00 57.63 C ANISOU 1335 CG TYR A 202 9871 7634 4393 575 -497 22 C ATOM 1336 CD1 TYR A 202 10.990 29.558 -9.932 1.00 58.94 C ANISOU 1336 CD1 TYR A 202 9998 7746 4650 533 -500 77 C ATOM 1337 CD2 TYR A 202 10.529 27.262 -10.374 1.00 58.23 C ANISOU 1337 CD2 TYR A 202 10004 7659 4460 574 -529 -65 C ATOM 1338 CE1 TYR A 202 10.190 29.504 -8.791 1.00 58.46 C ANISOU 1338 CE1 TYR A 202 9956 7601 4653 498 -528 43 C ATOM 1339 CE2 TYR A 202 9.733 27.196 -9.233 1.00 58.35 C ANISOU 1339 CE2 TYR A 202 10035 7588 4546 533 -558 -82 C ATOM 1340 CZ TYR A 202 9.544 28.325 -8.459 1.00 64.97 C ANISOU 1340 CZ TYR A 202 10835 8392 5458 498 -555 -30 C ATOM 1341 OH TYR A 202 8.738 28.246 -7.350 1.00 66.12 O ANISOU 1341 OH TYR A 202 10988 8473 5660 466 -583 -50 O ATOM 1342 N ILE A 203 13.884 25.907 -11.486 1.00 56.33 N ANISOU 1342 N ILE A 203 9752 7566 4084 719 -441 -110 N ATOM 1343 CA ILE A 203 14.147 24.642 -10.791 1.00 56.07 C ANISOU 1343 CA ILE A 203 9764 7464 4074 735 -453 -197 C ATOM 1344 C ILE A 203 15.611 24.635 -10.297 1.00 60.88 C ANISOU 1344 C ILE A 203 10352 8080 4700 759 -407 -171 C ATOM 1345 O ILE A 203 15.845 24.228 -9.158 1.00 60.09 O ANISOU 1345 O ILE A 203 10262 7899 4669 737 -407 -188 O ATOM 1346 CB ILE A 203 13.816 23.415 -11.691 1.00 59.60 C ANISOU 1346 CB ILE A 203 10252 7941 4451 784 -484 -297 C ATOM 1347 CG1 ILE A 203 12.265 23.252 -11.763 1.00 59.63 C ANISOU 1347 CG1 ILE A 203 10287 7899 4472 745 -540 -328 C ATOM 1348 CG2 ILE A 203 14.472 22.121 -11.162 1.00 59.95 C ANISOU 1348 CG2 ILE A 203 10327 7929 4522 816 -491 -378 C ATOM 1349 CD1 ILE A 203 11.707 22.092 -12.564 1.00 65.20 C ANISOU 1349 CD1 ILE A 203 11033 8613 5130 782 -589 -432 C ATOM 1350 N LEU A 204 16.562 25.158 -11.103 1.00 58.71 N ANISOU 1350 N LEU A 204 10037 7906 4364 798 -368 -116 N ATOM 1351 CA LEU A 204 17.982 25.259 -10.724 1.00 58.89 C ANISOU 1351 CA LEU A 204 10033 7945 4397 821 -323 -76 C ATOM 1352 C LEU A 204 18.152 26.133 -9.469 1.00 61.27 C ANISOU 1352 C LEU A 204 10309 8167 4803 763 -315 -12 C ATOM 1353 O LEU A 204 18.976 25.815 -8.615 1.00 60.53 O ANISOU 1353 O LEU A 204 10217 8034 4749 764 -294 -17 O ATOM 1354 CB LEU A 204 18.814 25.835 -11.891 1.00 60.05 C ANISOU 1354 CB LEU A 204 10127 8231 4458 869 -290 -3 C ATOM 1355 CG LEU A 204 20.333 26.017 -11.682 1.00 65.38 C ANISOU 1355 CG LEU A 204 10765 8943 5132 897 -243 58 C ATOM 1356 CD1 LEU A 204 21.022 24.694 -11.352 1.00 65.96 C ANISOU 1356 CD1 LEU A 204 10882 8992 5189 941 -230 -33 C ATOM 1357 CD2 LEU A 204 20.974 26.627 -12.910 1.00 68.82 C ANISOU 1357 CD2 LEU A 204 11137 9532 5480 943 -217 146 C ATOM 1358 N PHE A 205 17.346 27.207 -9.359 1.00 57.17 N ANISOU 1358 N PHE A 205 9764 7629 4330 715 -335 42 N ATOM 1359 CA PHE A 205 17.325 28.151 -8.242 1.00 56.09 C ANISOU 1359 CA PHE A 205 9597 7421 4295 665 -339 88 C ATOM 1360 C PHE A 205 16.789 27.475 -6.966 1.00 58.91 C ANISOU 1360 C PHE A 205 9990 7685 4708 636 -360 17 C ATOM 1361 O PHE A 205 17.481 27.485 -5.950 1.00 57.36 O ANISOU 1361 O PHE A 205 9781 7451 4561 628 -344 19 O ATOM 1362 CB PHE A 205 16.465 29.377 -8.617 1.00 57.75 C ANISOU 1362 CB PHE A 205 9769 7636 4536 629 -363 151 C ATOM 1363 CG PHE A 205 16.216 30.395 -7.527 1.00 58.55 C ANISOU 1363 CG PHE A 205 9838 7659 4749 581 -382 179 C ATOM 1364 CD1 PHE A 205 17.185 31.334 -7.197 1.00 61.45 C ANISOU 1364 CD1 PHE A 205 10149 8020 5180 575 -370 250 C ATOM 1365 CD2 PHE A 205 14.973 30.486 -6.913 1.00 60.04 C ANISOU 1365 CD2 PHE A 205 10047 7788 4979 546 -418 136 C ATOM 1366 CE1 PHE A 205 16.942 32.297 -6.213 1.00 61.92 C ANISOU 1366 CE1 PHE A 205 10173 8006 5346 537 -396 260 C ATOM 1367 CE2 PHE A 205 14.725 31.457 -5.939 1.00 62.36 C ANISOU 1367 CE2 PHE A 205 10304 8022 5370 512 -439 150 C ATOM 1368 CZ PHE A 205 15.710 32.356 -5.597 1.00 60.57 C ANISOU 1368 CZ PHE A 205 10023 7783 5209 509 -430 205 C ATOM 1369 N CYS A 206 15.579 26.875 -7.033 1.00 56.38 N ANISOU 1369 N CYS A 206 9708 7338 4377 623 -397 -38 N ATOM 1370 CA CYS A 206 14.909 26.202 -5.913 1.00 56.63 C ANISOU 1370 CA CYS A 206 9763 7296 4458 595 -424 -91 C ATOM 1371 C CYS A 206 15.787 25.083 -5.353 1.00 61.98 C ANISOU 1371 C CYS A 206 10456 7952 5141 617 -407 -131 C ATOM 1372 O CYS A 206 16.002 25.028 -4.139 1.00 61.18 O ANISOU 1372 O CYS A 206 10337 7810 5097 595 -404 -130 O ATOM 1373 CB CYS A 206 13.555 25.658 -6.349 1.00 57.24 C ANISOU 1373 CB CYS A 206 9877 7361 4512 585 -468 -133 C ATOM 1374 SG CYS A 206 12.382 26.935 -6.856 1.00 61.28 S ANISOU 1374 SG CYS A 206 10368 7889 5026 552 -490 -83 S ATOM 1375 N THR A 207 16.306 24.212 -6.236 1.00 59.66 N ANISOU 1375 N THR A 207 10189 7693 4786 665 -397 -167 N ATOM 1376 CA THR A 207 17.188 23.109 -5.872 1.00 59.78 C ANISOU 1376 CA THR A 207 10216 7689 4807 693 -382 -207 C ATOM 1377 C THR A 207 18.383 23.657 -5.062 1.00 64.87 C ANISOU 1377 C THR A 207 10825 8336 5488 687 -336 -154 C ATOM 1378 O THR A 207 18.625 23.171 -3.958 1.00 64.49 O ANISOU 1378 O THR A 207 10768 8240 5493 668 -335 -164 O ATOM 1379 CB THR A 207 17.633 22.374 -7.143 1.00 66.53 C ANISOU 1379 CB THR A 207 11096 8600 5582 756 -376 -254 C ATOM 1380 OG1 THR A 207 16.469 21.899 -7.816 1.00 64.26 O ANISOU 1380 OG1 THR A 207 10840 8308 5268 758 -425 -308 O ATOM 1381 CG2 THR A 207 18.575 21.211 -6.862 1.00 66.52 C ANISOU 1381 CG2 THR A 207 11107 8577 5591 792 -364 -302 C ATOM 1382 N THR A 208 19.062 24.714 -5.579 1.00 62.08 N ANISOU 1382 N THR A 208 10440 8038 5108 698 -305 -90 N ATOM 1383 CA THR A 208 20.236 25.364 -4.971 1.00 61.73 C ANISOU 1383 CA THR A 208 10356 8000 5097 694 -266 -30 C ATOM 1384 C THR A 208 19.887 25.994 -3.600 1.00 64.62 C ANISOU 1384 C THR A 208 10695 8307 5549 642 -281 -16 C ATOM 1385 O THR A 208 20.563 25.687 -2.618 1.00 63.98 O ANISOU 1385 O THR A 208 10600 8203 5505 634 -262 -18 O ATOM 1386 CB THR A 208 20.794 26.434 -5.928 1.00 70.31 C ANISOU 1386 CB THR A 208 11407 9159 6147 713 -245 48 C ATOM 1387 OG1 THR A 208 21.234 25.775 -7.116 1.00 72.26 O ANISOU 1387 OG1 THR A 208 11672 9483 6302 771 -229 30 O ATOM 1388 CG2 THR A 208 21.959 27.218 -5.334 1.00 68.05 C ANISOU 1388 CG2 THR A 208 11075 8874 5907 704 -216 121 C ATOM 1389 N VAL A 209 18.853 26.864 -3.537 1.00 60.27 N ANISOU 1389 N VAL A 209 10132 7741 5027 609 -314 -6 N ATOM 1390 CA VAL A 209 18.458 27.552 -2.301 1.00 59.02 C ANISOU 1390 CA VAL A 209 9941 7539 4944 570 -332 -4 C ATOM 1391 C VAL A 209 18.123 26.514 -1.204 1.00 62.51 C ANISOU 1391 C VAL A 209 10394 7950 5406 558 -342 -56 C ATOM 1392 O VAL A 209 18.738 26.571 -0.140 1.00 61.83 O ANISOU 1392 O VAL A 209 10278 7857 5359 548 -328 -51 O ATOM 1393 CB VAL A 209 17.271 28.537 -2.511 1.00 62.36 C ANISOU 1393 CB VAL A 209 10351 7952 5393 543 -370 7 C ATOM 1394 CG1 VAL A 209 16.811 29.144 -1.186 1.00 61.54 C ANISOU 1394 CG1 VAL A 209 10211 7812 5361 513 -395 -11 C ATOM 1395 CG2 VAL A 209 17.640 29.642 -3.499 1.00 62.52 C ANISOU 1395 CG2 VAL A 209 10341 8002 5412 549 -364 76 C ATOM 1396 N PHE A 210 17.202 25.555 -1.474 1.00 59.32 N ANISOU 1396 N PHE A 210 10027 7534 4977 559 -369 -97 N ATOM 1397 CA PHE A 210 16.766 24.575 -0.472 1.00 58.88 C ANISOU 1397 CA PHE A 210 9970 7451 4950 544 -388 -128 C ATOM 1398 C PHE A 210 17.912 23.623 -0.036 1.00 63.01 C ANISOU 1398 C PHE A 210 10489 7971 5481 561 -357 -132 C ATOM 1399 O PHE A 210 17.994 23.346 1.160 1.00 62.47 O ANISOU 1399 O PHE A 210 10385 7896 5453 542 -357 -128 O ATOM 1400 CB PHE A 210 15.579 23.740 -0.956 1.00 60.73 C ANISOU 1400 CB PHE A 210 10241 7666 5168 541 -432 -162 C ATOM 1401 CG PHE A 210 14.332 24.535 -1.272 1.00 62.12 C ANISOU 1401 CG PHE A 210 10420 7844 5340 519 -466 -156 C ATOM 1402 CD1 PHE A 210 13.731 25.331 -0.301 1.00 64.91 C ANISOU 1402 CD1 PHE A 210 10733 8198 5732 492 -480 -142 C ATOM 1403 CD2 PHE A 210 13.652 24.343 -2.467 1.00 64.52 C ANISOU 1403 CD2 PHE A 210 10763 8150 5600 529 -488 -173 C ATOM 1404 CE1 PHE A 210 12.561 26.041 -0.580 1.00 65.68 C ANISOU 1404 CE1 PHE A 210 10832 8296 5828 474 -512 -137 C ATOM 1405 CE2 PHE A 210 12.468 25.035 -2.738 1.00 67.26 C ANISOU 1405 CE2 PHE A 210 11112 8500 5945 506 -519 -162 C ATOM 1406 CZ PHE A 210 11.925 25.872 -1.789 1.00 64.91 C ANISOU 1406 CZ PHE A 210 10776 8198 5690 478 -530 -143 C ATOM 1407 N THR A 211 18.799 23.153 -0.956 1.00 59.89 N ANISOU 1407 N THR A 211 10122 7589 5045 600 -330 -138 N ATOM 1408 CA THR A 211 19.934 22.303 -0.534 1.00 59.76 C ANISOU 1408 CA THR A 211 10099 7568 5040 618 -297 -139 C ATOM 1409 C THR A 211 20.908 23.106 0.348 1.00 63.85 C ANISOU 1409 C THR A 211 10572 8102 5586 604 -259 -93 C ATOM 1410 O THR A 211 21.414 22.553 1.325 1.00 63.92 O ANISOU 1410 O THR A 211 10556 8103 5629 595 -245 -88 O ATOM 1411 CB THR A 211 20.701 21.664 -1.703 1.00 67.25 C ANISOU 1411 CB THR A 211 11081 8537 5934 671 -277 -161 C ATOM 1412 OG1 THR A 211 21.084 22.673 -2.633 1.00 68.48 O ANISOU 1412 OG1 THR A 211 11235 8745 6038 690 -254 -126 O ATOM 1413 CG2 THR A 211 19.921 20.573 -2.399 1.00 65.48 C ANISOU 1413 CG2 THR A 211 10896 8287 5695 691 -319 -225 C ATOM 1414 N LEU A 212 21.144 24.408 0.033 1.00 59.52 N ANISOU 1414 N LEU A 212 10007 7577 5031 601 -249 -56 N ATOM 1415 CA LEU A 212 22.030 25.258 0.842 1.00 58.58 C ANISOU 1415 CA LEU A 212 9842 7465 4949 587 -224 -16 C ATOM 1416 C LEU A 212 21.448 25.446 2.240 1.00 61.71 C ANISOU 1416 C LEU A 212 10200 7850 5398 552 -246 -34 C ATOM 1417 O LEU A 212 22.201 25.427 3.215 1.00 61.27 O ANISOU 1417 O LEU A 212 10108 7802 5369 544 -225 -22 O ATOM 1418 CB LEU A 212 22.291 26.622 0.185 1.00 58.54 C ANISOU 1418 CB LEU A 212 9820 7477 4947 588 -223 31 C ATOM 1419 CG LEU A 212 23.142 26.604 -1.086 1.00 63.50 C ANISOU 1419 CG LEU A 212 10462 8145 5519 626 -194 72 C ATOM 1420 CD1 LEU A 212 23.134 27.949 -1.760 1.00 64.04 C ANISOU 1420 CD1 LEU A 212 10500 8232 5601 621 -205 133 C ATOM 1421 CD2 LEU A 212 24.568 26.130 -0.815 1.00 65.47 C ANISOU 1421 CD2 LEU A 212 10703 8412 5760 648 -148 98 C ATOM 1422 N LEU A 213 20.112 25.563 2.345 1.00 57.73 N ANISOU 1422 N LEU A 213 9699 7336 4901 534 -289 -61 N ATOM 1423 CA LEU A 213 19.452 25.660 3.639 1.00 57.20 C ANISOU 1423 CA LEU A 213 9588 7276 4869 509 -313 -79 C ATOM 1424 C LEU A 213 19.578 24.327 4.365 1.00 61.53 C ANISOU 1424 C LEU A 213 10126 7830 5423 506 -306 -83 C ATOM 1425 O LEU A 213 20.037 24.321 5.500 1.00 60.98 O ANISOU 1425 O LEU A 213 10004 7787 5377 495 -294 -75 O ATOM 1426 CB LEU A 213 17.978 26.087 3.517 1.00 57.13 C ANISOU 1426 CB LEU A 213 9583 7262 4861 496 -360 -100 C ATOM 1427 CG LEU A 213 17.703 27.495 2.974 1.00 61.87 C ANISOU 1427 CG LEU A 213 10179 7854 5475 493 -374 -92 C ATOM 1428 CD1 LEU A 213 16.223 27.702 2.736 1.00 62.10 C ANISOU 1428 CD1 LEU A 213 10220 7877 5499 482 -417 -110 C ATOM 1429 CD2 LEU A 213 18.257 28.579 3.893 1.00 63.67 C ANISOU 1429 CD2 LEU A 213 10349 8088 5754 488 -375 -92 C ATOM 1430 N LEU A 214 19.290 23.193 3.675 1.00 58.81 N ANISOU 1430 N LEU A 214 9824 7461 5061 517 -315 -94 N ATOM 1431 CA LEU A 214 19.404 21.848 4.263 1.00 59.04 C ANISOU 1431 CA LEU A 214 9837 7480 5113 514 -318 -91 C ATOM 1432 C LEU A 214 20.855 21.524 4.651 1.00 63.99 C ANISOU 1432 C LEU A 214 10446 8117 5751 524 -269 -68 C ATOM 1433 O LEU A 214 21.064 20.767 5.600 1.00 63.58 O ANISOU 1433 O LEU A 214 10352 8073 5732 511 -265 -50 O ATOM 1434 CB LEU A 214 18.871 20.750 3.328 1.00 59.34 C ANISOU 1434 CB LEU A 214 9926 7477 5145 528 -348 -117 C ATOM 1435 CG LEU A 214 17.354 20.725 3.077 1.00 63.81 C ANISOU 1435 CG LEU A 214 10506 8030 5710 512 -404 -132 C ATOM 1436 CD1 LEU A 214 16.989 19.598 2.150 1.00 64.40 C ANISOU 1436 CD1 LEU A 214 10629 8058 5783 530 -437 -166 C ATOM 1437 CD2 LEU A 214 16.570 20.573 4.373 1.00 65.63 C ANISOU 1437 CD2 LEU A 214 10674 8283 5980 480 -433 -106 C ATOM 1438 N LEU A 215 21.843 22.114 3.952 1.00 61.30 N ANISOU 1438 N LEU A 215 10128 7781 5383 546 -231 -59 N ATOM 1439 CA LEU A 215 23.260 21.953 4.287 1.00 61.25 C ANISOU 1439 CA LEU A 215 10103 7787 5381 556 -182 -31 C ATOM 1440 C LEU A 215 23.548 22.674 5.607 1.00 65.12 C ANISOU 1440 C LEU A 215 10529 8311 5901 529 -172 -10 C ATOM 1441 O LEU A 215 24.031 22.056 6.554 1.00 64.09 O ANISOU 1441 O LEU A 215 10358 8199 5795 518 -154 8 O ATOM 1442 CB LEU A 215 24.158 22.486 3.144 1.00 61.37 C ANISOU 1442 CB LEU A 215 10153 7810 5355 589 -150 -15 C ATOM 1443 CG LEU A 215 25.677 22.431 3.351 1.00 65.71 C ANISOU 1443 CG LEU A 215 10686 8377 5903 603 -97 24 C ATOM 1444 CD1 LEU A 215 26.171 20.999 3.503 1.00 65.85 C ANISOU 1444 CD1 LEU A 215 10711 8381 5930 619 -79 16 C ATOM 1445 CD2 LEU A 215 26.393 23.090 2.202 1.00 68.55 C ANISOU 1445 CD2 LEU A 215 11068 8758 6218 634 -74 53 C ATOM 1446 N SER A 216 23.146 23.957 5.680 1.00 62.51 N ANISOU 1446 N SER A 216 10186 7992 5575 520 -190 -16 N ATOM 1447 CA SER A 216 23.296 24.851 6.829 1.00 62.72 C ANISOU 1447 CA SER A 216 10150 8049 5630 502 -194 -17 C ATOM 1448 C SER A 216 22.643 24.283 8.099 1.00 67.10 C ANISOU 1448 C SER A 216 10650 8646 6200 483 -212 -29 C ATOM 1449 O SER A 216 23.148 24.523 9.195 1.00 66.40 O ANISOU 1449 O SER A 216 10502 8602 6127 474 -200 -24 O ATOM 1450 CB SER A 216 22.671 26.206 6.513 1.00 66.80 C ANISOU 1450 CB SER A 216 10666 8556 6159 499 -229 -37 C ATOM 1451 OG SER A 216 23.220 26.763 5.329 1.00 76.45 O ANISOU 1451 OG SER A 216 11925 9751 7371 514 -216 -9 O ATOM 1452 N ILE A 217 21.528 23.535 7.944 1.00 64.36 N ANISOU 1452 N ILE A 217 10316 8291 5847 478 -244 -39 N ATOM 1453 CA ILE A 217 20.776 22.935 9.054 1.00 64.29 C ANISOU 1453 CA ILE A 217 10246 8331 5851 461 -268 -32 C ATOM 1454 C ILE A 217 21.548 21.714 9.582 1.00 68.08 C ANISOU 1454 C ILE A 217 10697 8821 6351 455 -240 8 C ATOM 1455 O ILE A 217 21.621 21.540 10.797 1.00 67.91 O ANISOU 1455 O ILE A 217 10597 8866 6341 442 -237 30 O ATOM 1456 CB ILE A 217 19.315 22.557 8.635 1.00 67.67 C ANISOU 1456 CB ILE A 217 10695 8742 6274 455 -318 -43 C ATOM 1457 CG1 ILE A 217 18.587 23.691 7.865 1.00 68.17 C ANISOU 1457 CG1 ILE A 217 10797 8785 6320 461 -343 -78 C ATOM 1458 CG2 ILE A 217 18.482 22.061 9.808 1.00 68.36 C ANISOU 1458 CG2 ILE A 217 10706 8893 6373 439 -348 -21 C ATOM 1459 CD1 ILE A 217 18.529 25.073 8.538 1.00 75.32 C ANISOU 1459 CD1 ILE A 217 11656 9730 7233 463 -350 -104 C ATOM 1460 N VAL A 218 22.136 20.888 8.678 1.00 64.42 N ANISOU 1460 N VAL A 218 10288 8298 5890 469 -221 17 N ATOM 1461 CA VAL A 218 22.934 19.708 9.055 1.00 64.20 C ANISOU 1461 CA VAL A 218 10236 8265 5892 466 -195 54 C ATOM 1462 C VAL A 218 24.181 20.182 9.851 1.00 68.42 C ANISOU 1462 C VAL A 218 10726 8846 6424 463 -146 78 C ATOM 1463 O VAL A 218 24.440 19.653 10.938 1.00 68.08 O ANISOU 1463 O VAL A 218 10610 8852 6405 445 -135 115 O ATOM 1464 CB VAL A 218 23.322 18.835 7.824 1.00 67.89 C ANISOU 1464 CB VAL A 218 10774 8660 6361 493 -189 40 C ATOM 1465 CG1 VAL A 218 24.378 17.787 8.174 1.00 67.60 C ANISOU 1465 CG1 VAL A 218 10713 8614 6359 497 -155 73 C ATOM 1466 CG2 VAL A 218 22.090 18.167 7.224 1.00 67.90 C ANISOU 1466 CG2 VAL A 218 10805 8618 6378 493 -247 16 C ATOM 1467 N ILE A 219 24.884 21.228 9.349 1.00 64.88 N ANISOU 1467 N ILE A 219 10312 8389 5951 477 -120 64 N ATOM 1468 CA ILE A 219 26.072 21.826 9.989 1.00 64.59 C ANISOU 1468 CA ILE A 219 10238 8387 5916 473 -80 85 C ATOM 1469 C ILE A 219 25.670 22.469 11.353 1.00 68.47 C ANISOU 1469 C ILE A 219 10647 8954 6415 454 -99 74 C ATOM 1470 O ILE A 219 26.490 22.510 12.273 1.00 67.72 O ANISOU 1470 O ILE A 219 10495 8910 6328 444 -71 96 O ATOM 1471 CB ILE A 219 26.746 22.870 9.037 1.00 67.69 C ANISOU 1471 CB ILE A 219 10681 8749 6290 492 -64 81 C ATOM 1472 CG1 ILE A 219 27.078 22.234 7.663 1.00 68.42 C ANISOU 1472 CG1 ILE A 219 10846 8793 6359 521 -48 88 C ATOM 1473 CG2 ILE A 219 28.012 23.490 9.674 1.00 68.27 C ANISOU 1473 CG2 ILE A 219 10716 8850 6374 487 -29 110 C ATOM 1474 CD1 ILE A 219 27.573 23.202 6.570 1.00 76.50 C ANISOU 1474 CD1 ILE A 219 11909 9801 7356 543 -37 99 C ATOM 1475 N LEU A 220 24.408 22.924 11.487 1.00 65.50 N ANISOU 1475 N LEU A 220 10259 8595 6033 451 -146 38 N ATOM 1476 CA LEU A 220 23.938 23.544 12.720 1.00 65.63 C ANISOU 1476 CA LEU A 220 10194 8695 6047 444 -169 15 C ATOM 1477 C LEU A 220 23.680 22.483 13.807 1.00 71.92 C ANISOU 1477 C LEU A 220 10910 9570 6847 429 -169 55 C ATOM 1478 O LEU A 220 24.087 22.716 14.943 1.00 72.21 O ANISOU 1478 O LEU A 220 10865 9693 6877 425 -157 59 O ATOM 1479 CB LEU A 220 22.669 24.380 12.479 1.00 65.47 C ANISOU 1479 CB LEU A 220 10185 8673 6019 451 -220 -36 C ATOM 1480 CG LEU A 220 22.135 25.207 13.662 1.00 69.96 C ANISOU 1480 CG LEU A 220 10669 9332 6580 456 -250 -79 C ATOM 1481 CD1 LEU A 220 23.201 26.136 14.230 1.00 70.14 C ANISOU 1481 CD1 LEU A 220 10655 9379 6618 462 -234 -105 C ATOM 1482 CD2 LEU A 220 20.925 26.018 13.251 1.00 72.44 C ANISOU 1482 CD2 LEU A 220 11003 9628 6891 466 -299 -128 C ATOM 1483 N TYR A 221 23.037 21.328 13.476 1.00 69.66 N ANISOU 1483 N TYR A 221 10637 9256 6574 421 -185 89 N ATOM 1484 CA TYR A 221 22.761 20.289 14.478 1.00 70.36 C ANISOU 1484 CA TYR A 221 10637 9418 6681 403 -192 148 C ATOM 1485 C TYR A 221 24.045 19.663 15.016 1.00 75.88 C ANISOU 1485 C TYR A 221 11294 10138 7400 393 -142 199 C ATOM 1486 O TYR A 221 24.091 19.341 16.205 1.00 75.34 O ANISOU 1486 O TYR A 221 11122 10173 7332 379 -138 241 O ATOM 1487 CB TYR A 221 21.855 19.177 13.949 1.00 72.15 C ANISOU 1487 CB TYR A 221 10884 9593 6939 394 -229 179 C ATOM 1488 CG TYR A 221 20.407 19.586 13.796 1.00 74.97 C ANISOU 1488 CG TYR A 221 11245 9962 7276 396 -283 153 C ATOM 1489 CD1 TYR A 221 19.610 19.829 14.913 1.00 77.24 C ANISOU 1489 CD1 TYR A 221 11435 10367 7544 392 -310 169 C ATOM 1490 CD2 TYR A 221 19.790 19.576 12.550 1.00 76.12 C ANISOU 1490 CD2 TYR A 221 11484 10013 7423 404 -309 120 C ATOM 1491 CE1 TYR A 221 18.265 20.170 14.782 1.00 78.69 C ANISOU 1491 CE1 TYR A 221 11622 10568 7710 396 -359 151 C ATOM 1492 CE2 TYR A 221 18.439 19.894 12.408 1.00 77.33 C ANISOU 1492 CE2 TYR A 221 11641 10177 7562 403 -358 104 C ATOM 1493 CZ TYR A 221 17.680 20.194 13.526 1.00 86.33 C ANISOU 1493 CZ TYR A 221 12689 11429 8684 399 -383 121 C ATOM 1494 OH TYR A 221 16.355 20.533 13.371 1.00 88.40 O ANISOU 1494 OH TYR A 221 12956 11706 8928 401 -430 107 O ATOM 1495 N CYS A 222 25.084 19.498 14.160 1.00 73.90 N ANISOU 1495 N CYS A 222 11116 9802 7159 401 -105 199 N ATOM 1496 CA CYS A 222 26.387 18.947 14.568 1.00 74.28 C ANISOU 1496 CA CYS A 222 11134 9862 7226 394 -53 248 C ATOM 1497 C CYS A 222 27.050 19.893 15.567 1.00 78.38 C ANISOU 1497 C CYS A 222 11594 10470 7719 390 -28 239 C ATOM 1498 O CYS A 222 27.601 19.427 16.566 1.00 78.13 O ANISOU 1498 O CYS A 222 11479 10512 7696 374 -3 288 O ATOM 1499 CB CYS A 222 27.283 18.700 13.359 1.00 74.74 C ANISOU 1499 CB CYS A 222 11287 9820 7292 413 -22 242 C ATOM 1500 SG CYS A 222 26.621 17.490 12.190 1.00 79.04 S ANISOU 1500 SG CYS A 222 11896 10264 7871 425 -56 237 S ATOM 1501 N ARG A 223 26.964 21.224 15.310 1.00 74.76 N ANISOU 1501 N ARG A 223 11168 10002 7234 405 -41 176 N ATOM 1502 CA ARG A 223 27.459 22.266 16.206 1.00 74.54 C ANISOU 1502 CA ARG A 223 11085 10047 7190 406 -35 147 C ATOM 1503 C ARG A 223 26.733 22.194 17.537 1.00 79.37 C ANISOU 1503 C ARG A 223 11582 10790 7783 400 -59 146 C ATOM 1504 O ARG A 223 27.394 22.101 18.563 1.00 79.22 O ANISOU 1504 O ARG A 223 11483 10859 7757 391 -33 172 O ATOM 1505 CB ARG A 223 27.308 23.667 15.581 1.00 74.03 C ANISOU 1505 CB ARG A 223 11073 9933 7122 423 -63 78 C ATOM 1506 CG ARG A 223 28.477 24.110 14.692 1.00 82.33 C ANISOU 1506 CG ARG A 223 12189 10906 8187 429 -32 91 C ATOM 1507 CD ARG A 223 29.623 24.797 15.451 1.00 90.66 C ANISOU 1507 CD ARG A 223 13192 12005 9251 425 -15 87 C ATOM 1508 NE ARG A 223 30.273 23.946 16.445 1.00 99.17 N ANISOU 1508 NE ARG A 223 14199 13161 10321 409 23 134 N ATOM 1509 N ILE A 224 25.385 22.142 17.521 1.00 76.52 N ANISOU 1509 N ILE A 224 11210 10452 7412 405 -105 126 N ATOM 1510 CA ILE A 224 24.562 22.061 18.734 1.00 76.90 C ANISOU 1510 CA ILE A 224 11143 10642 7433 406 -132 131 C ATOM 1511 C ILE A 224 24.880 20.742 19.497 1.00 82.53 C ANISOU 1511 C ILE A 224 11771 11425 8161 382 -107 231 C ATOM 1512 O ILE A 224 25.072 20.794 20.709 1.00 82.44 O ANISOU 1512 O ILE A 224 11647 11553 8124 381 -98 249 O ATOM 1513 CB ILE A 224 23.043 22.178 18.398 1.00 79.74 C ANISOU 1513 CB ILE A 224 11517 10999 7781 416 -187 105 C ATOM 1514 CG1 ILE A 224 22.744 23.535 17.714 1.00 79.66 C ANISOU 1514 CG1 ILE A 224 11579 10923 7764 438 -213 11 C ATOM 1515 CG2 ILE A 224 22.179 22.018 19.666 1.00 80.68 C ANISOU 1515 CG2 ILE A 224 11506 11285 7865 422 -215 124 C ATOM 1516 CD1 ILE A 224 21.390 23.662 17.126 1.00 84.22 C ANISOU 1516 CD1 ILE A 224 12195 11468 8336 445 -259 -10 C ATOM 1517 N TYR A 225 25.000 19.601 18.792 1.00 80.18 N ANISOU 1517 N TYR A 225 11521 11034 7910 365 -96 293 N ATOM 1518 CA TYR A 225 25.275 18.299 19.413 1.00 81.06 C ANISOU 1518 CA TYR A 225 11551 11189 8059 340 -80 395 C ATOM 1519 C TYR A 225 26.619 18.304 20.211 1.00 86.31 C ANISOU 1519 C TYR A 225 12155 11921 8717 331 -24 427 C ATOM 1520 O TYR A 225 26.619 17.935 21.389 1.00 85.92 O ANISOU 1520 O TYR A 225 11978 12009 8658 318 -19 486 O ATOM 1521 CB TYR A 225 25.307 17.190 18.337 1.00 82.65 C ANISOU 1521 CB TYR A 225 11832 11248 8325 332 -83 431 C ATOM 1522 CG TYR A 225 25.620 15.806 18.868 1.00 85.40 C ANISOU 1522 CG TYR A 225 12097 11615 8735 305 -74 538 C ATOM 1523 CD1 TYR A 225 26.904 15.274 18.771 1.00 87.54 C ANISOU 1523 CD1 TYR A 225 12376 11847 9039 298 -22 574 C ATOM 1524 CD2 TYR A 225 24.639 15.036 19.488 1.00 86.69 C ANISOU 1524 CD2 TYR A 225 12165 11840 8932 287 -119 611 C ATOM 1525 CE1 TYR A 225 27.204 14.007 19.272 1.00 89.13 C ANISOU 1525 CE1 TYR A 225 12492 12061 9310 272 -16 676 C ATOM 1526 CE2 TYR A 225 24.927 13.768 19.995 1.00 88.14 C ANISOU 1526 CE2 TYR A 225 12257 12040 9191 260 -118 723 C ATOM 1527 CZ TYR A 225 26.212 13.257 19.885 1.00 96.15 C ANISOU 1527 CZ TYR A 225 13282 13007 10242 252 -66 752 C ATOM 1528 OH TYR A 225 26.505 12.009 20.383 1.00 97.17 O ANISOU 1528 OH TYR A 225 13316 13147 10458 224 -67 865 O ATOM 1529 N SER A 226 27.736 18.722 19.573 1.00 83.68 N ANISOU 1529 N SER A 226 11906 11501 8386 337 15 395 N ATOM 1530 CA SER A 226 29.086 18.705 20.159 1.00 83.61 C ANISOU 1530 CA SER A 226 11858 11533 8376 327 70 428 C ATOM 1531 C SER A 226 29.307 19.809 21.226 1.00 86.90 C ANISOU 1531 C SER A 226 12195 12081 8740 335 69 380 C ATOM 1532 O SER A 226 30.039 19.566 22.189 1.00 86.02 O ANISOU 1532 O SER A 226 11992 12070 8621 321 101 428 O ATOM 1533 CB SER A 226 30.137 18.873 19.065 1.00 87.32 C ANISOU 1533 CB SER A 226 12444 11873 8860 336 106 410 C ATOM 1534 OG SER A 226 29.986 20.103 18.372 1.00 96.59 O ANISOU 1534 OG SER A 226 13694 12996 10009 358 84 326 O ATOM 1535 N LEU A 227 28.733 21.019 21.031 1.00 83.51 N ANISOU 1535 N LEU A 227 11801 11648 8283 359 31 284 N ATOM 1536 CA LEU A 227 28.907 22.140 21.968 1.00 83.44 C ANISOU 1536 CA LEU A 227 11721 11749 8234 376 17 215 C ATOM 1537 C LEU A 227 28.117 21.888 23.259 1.00 87.00 C ANISOU 1537 C LEU A 227 12031 12383 8643 380 -5 230 C ATOM 1538 O LEU A 227 28.595 22.266 24.329 1.00 87.04 O ANISOU 1538 O LEU A 227 11939 12519 8613 387 4 213 O ATOM 1539 CB LEU A 227 28.496 23.491 21.344 1.00 83.59 C ANISOU 1539 CB LEU A 227 11811 11697 8251 402 -26 107 C ATOM 1540 CG LEU A 227 29.292 23.958 20.096 1.00 88.39 C ANISOU 1540 CG LEU A 227 12544 12143 8896 402 -10 96 C ATOM 1541 CD1 LEU A 227 28.657 25.174 19.460 1.00 88.69 C ANISOU 1541 CD1 LEU A 227 12636 12120 8944 425 -62 6 C ATOM 1542 CD2 LEU A 227 30.761 24.213 20.407 1.00 91.60 C ANISOU 1542 CD2 LEU A 227 12942 12548 9315 392 32 119 C ATOM 1543 N VAL A 228 26.935 21.224 23.168 1.00 82.89 N ANISOU 1543 N VAL A 228 11490 11880 8123 378 -35 269 N ATOM 1544 CA VAL A 228 26.132 20.846 24.344 1.00 82.79 C ANISOU 1544 CA VAL A 228 11332 12054 8071 383 -57 309 C ATOM 1545 C VAL A 228 26.890 19.716 25.084 1.00 85.85 C ANISOU 1545 C VAL A 228 11621 12523 8476 351 -13 431 C ATOM 1546 O VAL A 228 26.916 19.714 26.317 1.00 85.69 O ANISOU 1546 O VAL A 228 11460 12690 8407 356 -10 456 O ATOM 1547 CB VAL A 228 24.660 20.453 23.991 1.00 86.73 C ANISOU 1547 CB VAL A 228 11837 12544 8574 387 -107 330 C ATOM 1548 CG1 VAL A 228 23.944 19.781 25.164 1.00 87.02 C ANISOU 1548 CG1 VAL A 228 11710 12774 8578 385 -125 415 C ATOM 1549 CG2 VAL A 228 23.866 21.662 23.512 1.00 86.45 C ANISOU 1549 CG2 VAL A 228 11869 12466 8511 421 -151 210 C ATOM 1550 N ARG A 229 27.570 18.814 24.326 1.00 81.34 N ANISOU 1550 N ARG A 229 11121 11814 7971 321 21 502 N ATOM 1551 CA ARG A 229 28.381 17.721 24.883 1.00 80.80 C ANISOU 1551 CA ARG A 229 10972 11790 7938 289 64 621 C ATOM 1552 C ARG A 229 29.459 18.280 25.830 1.00 83.30 C ANISOU 1552 C ARG A 229 11216 12223 8209 290 105 605 C ATOM 1553 O ARG A 229 29.755 17.658 26.852 1.00 83.20 O ANISOU 1553 O ARG A 229 11070 12353 8188 271 127 694 O ATOM 1554 CB ARG A 229 29.028 16.893 23.759 1.00 80.68 C ANISOU 1554 CB ARG A 229 11068 11587 8001 270 91 663 C ATOM 1555 N THR A 230 29.994 19.484 25.510 1.00 78.14 N ANISOU 1555 N THR A 230 10644 11515 7529 312 108 495 N ATOM 1556 CA THR A 230 30.995 20.205 26.304 1.00 77.03 C ANISOU 1556 CA THR A 230 10451 11465 7351 317 134 456 C ATOM 1557 C THR A 230 30.279 21.018 27.409 1.00 79.49 C ANISOU 1557 C THR A 230 10645 11968 7588 350 93 381 C ATOM 1558 O THR A 230 30.745 21.038 28.549 1.00 79.11 O ANISOU 1558 O THR A 230 10471 12090 7498 349 111 403 O ATOM 1559 CB THR A 230 31.850 21.101 25.381 1.00 81.67 C ANISOU 1559 CB THR A 230 11175 11895 7961 325 144 380 C ATOM 1560 OG1 THR A 230 32.400 20.301 24.337 1.00 79.77 O ANISOU 1560 OG1 THR A 230 11034 11498 7776 304 181 448 O ATOM 1561 CG2 THR A 230 32.980 21.811 26.119 1.00 80.15 C ANISOU 1561 CG2 THR A 230 10935 11772 7744 327 166 345 C ATOM 1562 N ARG A 231 29.143 21.662 27.069 1.00 75.35 N ANISOU 1562 N ARG A 231 10159 11424 7047 382 37 292 N ATOM 1563 CA ARG A 231 28.348 22.483 27.992 1.00 75.54 C ANISOU 1563 CA ARG A 231 10083 11619 7000 425 -10 202 C ATOM 1564 C ARG A 231 27.823 21.662 29.176 1.00 79.61 C ANISOU 1564 C ARG A 231 10424 12361 7463 424 -8 293 C ATOM 1565 O ARG A 231 27.751 22.190 30.288 1.00 79.98 O ANISOU 1565 O ARG A 231 10348 12603 7439 456 -22 240 O ATOM 1566 CB ARG A 231 27.166 23.129 27.260 1.00 75.72 C ANISOU 1566 CB ARG A 231 10184 11562 7026 453 -66 119 C ATOM 1567 N ASN A1002 27.457 20.380 28.937 1.00 75.21 N ANISOU 1567 N ASN A1002 9850 11782 6946 390 4 430 N ATOM 1568 CA ASN A1002 26.957 19.462 29.965 1.00 74.85 C ANISOU 1568 CA ASN A1002 9631 11939 6871 380 2 551 C ATOM 1569 C ASN A1002 28.057 19.131 30.971 1.00 76.61 C ANISOU 1569 C ASN A1002 9736 12302 7073 362 52 617 C ATOM 1570 O ASN A1002 27.787 19.054 32.168 1.00 76.41 O ANISOU 1570 O ASN A1002 9539 12517 6975 378 46 651 O ATOM 1571 CB ASN A1002 26.413 18.176 29.333 1.00 75.90 C ANISOU 1571 CB ASN A1002 9785 11973 7081 343 -5 684 C ATOM 1572 CG ASN A1002 25.166 18.348 28.492 1.00 95.88 C ANISOU 1572 CG ASN A1002 12403 14401 9626 359 -58 640 C ATOM 1573 OD1 ASN A1002 24.456 19.362 28.559 1.00 89.31 O ANISOU 1573 OD1 ASN A1002 11588 13611 8735 401 -95 525 O ATOM 1574 ND2 ASN A1002 24.835 17.318 27.729 1.00 86.64 N ANISOU 1574 ND2 ASN A1002 11281 13101 8537 326 -68 734 N ATOM 1575 N ILE A1003 29.296 18.968 30.486 1.00 71.63 N ANISOU 1575 N ILE A1003 9191 11530 6497 330 102 636 N ATOM 1576 CA ILE A1003 30.462 18.692 31.325 1.00 71.25 C ANISOU 1576 CA ILE A1003 9047 11589 6435 308 154 699 C ATOM 1577 C ILE A1003 30.774 19.954 32.155 1.00 75.60 C ANISOU 1577 C ILE A1003 9542 12284 6899 349 142 565 C ATOM 1578 O ILE A1003 31.124 19.838 33.331 1.00 75.68 O ANISOU 1578 O ILE A1003 9397 12507 6850 352 160 603 O ATOM 1579 CB ILE A1003 31.672 18.231 30.448 1.00 73.48 C ANISOU 1579 CB ILE A1003 9452 11666 6800 268 207 747 C ATOM 1580 CG1 ILE A1003 31.313 16.939 29.668 1.00 73.34 C ANISOU 1580 CG1 ILE A1003 9478 11515 6874 234 209 866 C ATOM 1581 CG2 ILE A1003 32.942 18.031 31.293 1.00 74.37 C ANISOU 1581 CG2 ILE A1003 9474 11884 6898 244 264 808 C ATOM 1582 CD1 ILE A1003 32.368 16.388 28.708 1.00 78.29 C ANISOU 1582 CD1 ILE A1003 10224 11941 7583 205 255 908 C ATOM 1583 N PHE A1004 30.585 21.153 31.553 1.00 72.11 N ANISOU 1583 N PHE A1004 9216 11730 6451 384 106 409 N ATOM 1584 CA PHE A1004 30.847 22.449 32.188 1.00 72.26 C ANISOU 1584 CA PHE A1004 9199 11844 6411 428 79 260 C ATOM 1585 C PHE A1004 29.865 22.729 33.340 1.00 75.97 C ANISOU 1585 C PHE A1004 9505 12577 6784 478 36 213 C ATOM 1586 O PHE A1004 30.266 23.353 34.324 1.00 76.11 O ANISOU 1586 O PHE A1004 9417 12765 6735 508 30 141 O ATOM 1587 CB PHE A1004 30.771 23.588 31.154 1.00 73.95 C ANISOU 1587 CB PHE A1004 9573 11856 6668 451 39 120 C ATOM 1588 CG PHE A1004 30.939 24.978 31.726 1.00 76.33 C ANISOU 1588 CG PHE A1004 9842 12229 6933 500 -7 -46 C ATOM 1589 CD1 PHE A1004 32.184 25.426 32.160 1.00 79.62 C ANISOU 1589 CD1 PHE A1004 10240 12656 7354 492 13 -77 C ATOM 1590 CD2 PHE A1004 29.871 25.864 31.765 1.00 79.37 C ANISOU 1590 CD2 PHE A1004 10220 12647 7289 554 -75 -177 C ATOM 1591 CE1 PHE A1004 32.340 26.714 32.679 1.00 81.08 C ANISOU 1591 CE1 PHE A1004 10393 12894 7520 538 -40 -240 C ATOM 1592 CE2 PHE A1004 30.031 27.157 32.275 1.00 82.91 C ANISOU 1592 CE2 PHE A1004 10637 13146 7720 604 -127 -343 C ATOM 1593 CZ PHE A1004 31.266 27.572 32.729 1.00 80.98 C ANISOU 1593 CZ PHE A1004 10369 12913 7486 596 -113 -376 C ATOM 1594 N GLU A1005 28.602 22.283 33.219 1.00 71.69 N ANISOU 1594 N GLU A1005 8937 12074 6228 491 5 252 N ATOM 1595 CA GLU A1005 27.592 22.499 34.256 1.00 71.73 C ANISOU 1595 CA GLU A1005 8783 12337 6134 543 -36 220 C ATOM 1596 C GLU A1005 27.653 21.398 35.333 1.00 74.86 C ANISOU 1596 C GLU A1005 8989 12970 6486 522 -3 386 C ATOM 1597 O GLU A1005 27.341 21.681 36.492 1.00 75.18 O ANISOU 1597 O GLU A1005 8861 13280 6422 568 -21 356 O ATOM 1598 CB GLU A1005 26.179 22.569 33.652 1.00 73.04 C ANISOU 1598 CB GLU A1005 8999 12449 6303 567 -87 197 C ATOM 1599 CG GLU A1005 25.914 23.833 32.840 1.00 84.20 C ANISOU 1599 CG GLU A1005 10555 13697 7740 603 -132 19 C ATOM 1600 CD GLU A1005 25.919 25.149 33.603 1.00110.71 C ANISOU 1600 CD GLU A1005 13845 17192 11029 672 -176 -161 C ATOM 1601 OE1 GLU A1005 25.564 25.150 34.805 1.00111.73 O ANISOU 1601 OE1 GLU A1005 13801 17592 11058 717 -192 -171 O ATOM 1602 OE2 GLU A1005 26.183 26.195 32.969 1.00105.35 O ANISOU 1602 OE2 GLU A1005 13280 16350 10398 687 -202 -296 O ATOM 1603 N MET A1006 28.063 20.163 34.963 1.00 70.07 N ANISOU 1603 N MET A1006 8397 12269 5957 456 42 559 N ATOM 1604 CA MET A1006 28.170 19.031 35.897 1.00 69.88 C ANISOU 1604 CA MET A1006 8190 12446 5915 426 72 740 C ATOM 1605 C MET A1006 29.181 19.336 37.007 1.00 74.28 C ANISOU 1605 C MET A1006 8622 13200 6400 435 107 720 C ATOM 1606 O MET A1006 28.863 19.200 38.191 1.00 74.42 O ANISOU 1606 O MET A1006 8443 13509 6324 463 99 759 O ATOM 1607 CB MET A1006 28.585 17.753 35.144 1.00 71.41 C ANISOU 1607 CB MET A1006 8447 12453 6233 354 109 906 C ATOM 1608 CG MET A1006 28.536 16.508 35.991 1.00 75.09 C ANISOU 1608 CG MET A1006 8722 13100 6710 318 129 1113 C ATOM 1609 SD MET A1006 29.328 15.114 35.176 1.00 78.34 S ANISOU 1609 SD MET A1006 9205 13279 7280 237 173 1283 S ATOM 1610 CE MET A1006 28.882 13.825 36.254 1.00 75.84 C ANISOU 1610 CE MET A1006 8636 13202 6977 206 168 1518 C ATOM 1611 N LEU A1007 30.392 19.761 36.609 1.00 70.71 N ANISOU 1611 N LEU A1007 8282 12595 5991 414 142 659 N ATOM 1612 CA LEU A1007 31.484 20.092 37.514 1.00 71.02 C ANISOU 1612 CA LEU A1007 8231 12776 5976 416 176 633 C ATOM 1613 C LEU A1007 31.301 21.510 38.116 1.00 76.35 C ANISOU 1613 C LEU A1007 8873 13580 6556 491 126 422 C ATOM 1614 O LEU A1007 31.884 21.786 39.165 1.00 76.72 O ANISOU 1614 O LEU A1007 8789 13833 6527 511 137 391 O ATOM 1615 CB LEU A1007 32.832 19.975 36.785 1.00 70.18 C ANISOU 1615 CB LEU A1007 8264 12442 5959 364 229 656 C ATOM 1616 CG LEU A1007 33.326 18.533 36.569 1.00 74.05 C ANISOU 1616 CG LEU A1007 8738 12866 6533 295 286 864 C ATOM 1617 CD1 LEU A1007 34.391 18.462 35.521 1.00 73.28 C ANISOU 1617 CD1 LEU A1007 8818 12498 6528 256 326 866 C ATOM 1618 CD2 LEU A1007 33.806 17.906 37.873 1.00 76.30 C ANISOU 1618 CD2 LEU A1007 8813 13413 6766 275 325 990 C ATOM 1619 N ARG A1008 30.424 22.360 37.527 1.00 73.09 N ANISOU 1619 N ARG A1008 8559 13066 6145 537 66 280 N ATOM 1620 CA ARG A1008 30.094 23.683 38.090 1.00 73.60 C ANISOU 1620 CA ARG A1008 8583 13251 6130 616 6 74 C ATOM 1621 C ARG A1008 29.361 23.516 39.448 1.00 79.31 C ANISOU 1621 C ARG A1008 9076 14338 6721 670 -14 89 C ATOM 1622 O ARG A1008 29.296 24.452 40.247 1.00 80.37 O ANISOU 1622 O ARG A1008 9124 14646 6769 740 -56 -71 O ATOM 1623 CB ARG A1008 29.225 24.486 37.100 1.00 73.05 C ANISOU 1623 CB ARG A1008 8665 12986 6106 647 -52 -54 C ATOM 1624 CG ARG A1008 29.048 25.965 37.455 1.00 83.37 C ANISOU 1624 CG ARG A1008 9967 14338 7371 724 -121 -284 C ATOM 1625 CD ARG A1008 27.656 26.475 37.119 1.00 91.90 C ANISOU 1625 CD ARG A1008 11068 15420 8431 779 -184 -373 C ATOM 1626 NE ARG A1008 26.652 25.890 38.013 1.00100.25 N ANISOU 1626 NE ARG A1008 11942 16771 9375 817 -193 -310 N ATOM 1627 CZ ARG A1008 25.345 26.115 37.931 1.00113.51 C ANISOU 1627 CZ ARG A1008 13599 18517 11013 867 -241 -352 C ATOM 1628 NH1 ARG A1008 24.858 26.898 36.977 1.00101.28 N ANISOU 1628 NH1 ARG A1008 12201 16751 9529 881 -284 -457 N ATOM 1629 NH2 ARG A1008 24.512 25.543 38.790 1.00 99.17 N ANISOU 1629 NH2 ARG A1008 11603 16988 9091 901 -247 -276 N ATOM 1630 N ILE A1009 28.800 22.308 39.680 1.00 75.45 N ANISOU 1630 N ILE A1009 8483 13964 6222 638 12 285 N ATOM 1631 CA ILE A1009 28.054 21.918 40.882 1.00 75.68 C ANISOU 1631 CA ILE A1009 8280 14343 6133 678 -1 357 C ATOM 1632 C ILE A1009 28.968 21.112 41.835 1.00 78.60 C ANISOU 1632 C ILE A1009 8485 14909 6470 639 59 506 C ATOM 1633 O ILE A1009 29.099 21.468 43.009 1.00 79.08 O ANISOU 1633 O ILE A1009 8375 15258 6412 689 53 450 O ATOM 1634 CB ILE A1009 26.793 21.089 40.468 1.00 78.52 C ANISOU 1634 CB ILE A1009 8627 14689 6520 664 -20 497 C ATOM 1635 CG1 ILE A1009 25.912 21.868 39.449 1.00 78.38 C ANISOU 1635 CG1 ILE A1009 8780 14462 6538 696 -75 355 C ATOM 1636 CG2 ILE A1009 25.989 20.637 41.704 1.00 79.91 C ANISOU 1636 CG2 ILE A1009 8547 15242 6574 704 -35 598 C ATOM 1637 CD1 ILE A1009 24.772 21.065 38.783 1.00 84.34 C ANISOU 1637 CD1 ILE A1009 9570 15129 7347 670 -94 486 C ATOM 1638 N ASP A1010 29.590 20.030 41.315 1.00 73.27 N ANISOU 1638 N ASP A1010 7858 14077 5902 552 114 692 N ATOM 1639 CA ASP A1010 30.429 19.086 42.057 1.00 72.63 C ANISOU 1639 CA ASP A1010 7634 14141 5822 501 174 870 C ATOM 1640 C ASP A1010 31.765 19.709 42.536 1.00 75.15 C ANISOU 1640 C ASP A1010 7952 14493 6108 501 208 773 C ATOM 1641 O ASP A1010 32.347 19.198 43.493 1.00 75.19 O ANISOU 1641 O ASP A1010 7788 14718 6063 483 248 882 O ATOM 1642 CB ASP A1010 30.731 17.858 41.181 1.00 73.50 C ANISOU 1642 CB ASP A1010 7834 14014 6080 413 215 1061 C ATOM 1643 CG ASP A1010 29.515 16.998 40.861 1.00 80.48 C ANISOU 1643 CG ASP A1010 8679 14892 7008 400 182 1199 C ATOM 1644 OD1 ASP A1010 28.400 17.346 41.316 1.00 81.57 O ANISOU 1644 OD1 ASP A1010 8719 15218 7055 458 132 1158 O ATOM 1645 OD2 ASP A1010 29.686 15.955 40.201 1.00 83.44 O ANISOU 1645 OD2 ASP A1010 9109 15085 7508 334 204 1351 O ATOM 1646 N GLU A1011 32.243 20.784 41.890 1.00 70.26 N ANISOU 1646 N GLU A1011 7510 13666 5520 521 188 582 N ATOM 1647 CA GLU A1011 33.491 21.445 42.287 1.00 69.76 C ANISOU 1647 CA GLU A1011 7456 13614 5437 522 208 484 C ATOM 1648 C GLU A1011 33.230 22.904 42.680 1.00 73.31 C ANISOU 1648 C GLU A1011 7902 14147 5807 610 138 229 C ATOM 1649 O GLU A1011 33.935 23.442 43.536 1.00 73.61 O ANISOU 1649 O GLU A1011 7848 14344 5778 637 137 141 O ATOM 1650 CB GLU A1011 34.545 21.377 41.163 1.00 70.15 C ANISOU 1650 CB GLU A1011 7712 13325 5617 458 248 504 C ATOM 1651 CG GLU A1011 35.087 19.983 40.861 1.00 80.80 C ANISOU 1651 CG GLU A1011 9059 14592 7048 374 320 736 C ATOM 1652 CD GLU A1011 35.998 19.333 41.893 1.00106.91 C ANISOU 1652 CD GLU A1011 12196 18108 10316 339 379 867 C ATOM 1653 OE1 GLU A1011 36.468 20.034 42.819 1.00108.15 O ANISOU 1653 OE1 GLU A1011 12255 18457 10380 374 372 767 O ATOM 1654 OE2 GLU A1011 36.316 18.134 41.716 1.00100.98 O ANISOU 1654 OE2 GLU A1011 11420 17310 9638 274 431 1067 O ATOM 1655 N GLY A1012 32.229 23.523 42.054 1.00 68.95 N ANISOU 1655 N GLY A1012 7446 13483 5269 654 78 112 N ATOM 1656 CA GLY A1012 31.836 24.898 42.331 1.00 69.17 C ANISOU 1656 CA GLY A1012 7476 13565 5240 742 2 -133 C ATOM 1657 C GLY A1012 32.736 25.941 41.705 1.00 72.34 C ANISOU 1657 C GLY A1012 8039 13720 5725 737 -20 -287 C ATOM 1658 O GLY A1012 33.942 25.956 41.966 1.00 71.53 O ANISOU 1658 O GLY A1012 7934 13603 5643 701 17 -265 O ATOM 1659 N LEU A1013 32.139 26.840 40.893 1.00 69.03 N ANISOU 1659 N LEU A1013 7754 13115 5360 774 -84 -440 N ATOM 1660 CA LEU A1013 32.831 27.932 40.197 1.00 68.87 C ANISOU 1660 CA LEU A1013 7887 12846 5435 773 -120 -584 C ATOM 1661 C LEU A1013 33.262 29.038 41.176 1.00 74.95 C ANISOU 1661 C LEU A1013 8555 13776 6149 841 -179 -782 C ATOM 1662 O LEU A1013 32.562 29.294 42.154 1.00 75.83 O ANISOU 1662 O LEU A1013 8507 14159 6145 916 -217 -873 O ATOM 1663 CB LEU A1013 31.907 28.522 39.110 1.00 68.38 C ANISOU 1663 CB LEU A1013 7979 12553 5450 793 -175 -671 C ATOM 1664 CG LEU A1013 32.452 29.680 38.244 1.00 72.65 C ANISOU 1664 CG LEU A1013 8680 12815 6109 788 -220 -800 C ATOM 1665 CD1 LEU A1013 33.646 29.242 37.404 1.00 71.80 C ANISOU 1665 CD1 LEU A1013 8697 12488 6094 702 -153 -661 C ATOM 1666 CD2 LEU A1013 31.386 30.207 37.329 1.00 75.29 C ANISOU 1666 CD2 LEU A1013 9128 12976 6501 815 -276 -882 C ATOM 1667 N ARG A1014 34.413 29.696 40.897 1.00 71.66 N ANISOU 1667 N ARG A1014 8225 13189 5815 816 -189 -849 N ATOM 1668 CA ARG A1014 34.949 30.793 41.706 1.00 72.50 C ANISOU 1668 CA ARG A1014 8256 13392 5899 873 -254 -1045 C ATOM 1669 C ARG A1014 35.819 31.728 40.860 1.00 76.84 C ANISOU 1669 C ARG A1014 8968 13635 6594 846 -292 -1125 C ATOM 1670 O ARG A1014 36.620 31.260 40.054 1.00 75.49 O ANISOU 1670 O ARG A1014 8912 13268 6504 767 -232 -982 O ATOM 1671 CB ARG A1014 35.760 30.252 42.891 1.00 72.70 C ANISOU 1671 CB ARG A1014 8115 13682 5825 862 -203 -979 C ATOM 1672 N LEU A1015 35.667 33.048 41.046 1.00 74.99 N ANISOU 1672 N LEU A1015 8732 13362 6397 914 -397 -1352 N ATOM 1673 CA LEU A1015 36.469 34.028 40.307 1.00 74.95 C ANISOU 1673 CA LEU A1015 8861 13075 6543 892 -449 -1428 C ATOM 1674 C LEU A1015 37.611 34.580 41.185 1.00 80.81 C ANISOU 1674 C LEU A1015 9517 13903 7283 904 -483 -1527 C ATOM 1675 O LEU A1015 38.584 35.100 40.641 1.00 80.08 O ANISOU 1675 O LEU A1015 9521 13591 7314 868 -509 -1539 O ATOM 1676 CB LEU A1015 35.611 35.185 39.771 1.00 75.24 C ANISOU 1676 CB LEU A1015 8968 12956 6664 950 -554 -1603 C ATOM 1677 CG LEU A1015 34.532 34.833 38.739 1.00 79.00 C ANISOU 1677 CG LEU A1015 9551 13302 7165 935 -534 -1521 C ATOM 1678 CD1 LEU A1015 33.760 36.066 38.331 1.00 79.73 C ANISOU 1678 CD1 LEU A1015 9698 13249 7346 993 -643 -1703 C ATOM 1679 CD2 LEU A1015 35.130 34.183 37.498 1.00 79.84 C ANISOU 1679 CD2 LEU A1015 9813 13169 7354 839 -454 -1317 C ATOM 1680 N LYS A1016 37.497 34.453 42.529 1.00 79.10 N ANISOU 1680 N LYS A1016 9116 14012 6927 955 -482 -1587 N ATOM 1681 CA LYS A1016 38.520 34.884 43.492 1.00 80.03 C ANISOU 1681 CA LYS A1016 9130 14259 7019 971 -509 -1681 C ATOM 1682 C LYS A1016 39.177 33.661 44.130 1.00 84.03 C ANISOU 1682 C LYS A1016 9542 14965 7422 914 -396 -1486 C ATOM 1683 O LYS A1016 38.469 32.711 44.471 1.00 84.05 O ANISOU 1683 O LYS A1016 9458 15163 7313 916 -334 -1372 O ATOM 1684 CB LYS A1016 37.912 35.799 44.566 1.00 84.30 C ANISOU 1684 CB LYS A1016 9519 15029 7481 1089 -615 -1940 C ATOM 1685 N ILE A1017 40.525 33.666 44.263 1.00 80.22 N ANISOU 1685 N ILE A1017 9072 14426 6983 861 -370 -1436 N ATOM 1686 CA ILE A1017 41.296 32.542 44.822 1.00 79.82 C ANISOU 1686 CA ILE A1017 8937 14541 6851 799 -261 -1243 C ATOM 1687 C ILE A1017 40.771 32.183 46.223 1.00 85.68 C ANISOU 1687 C ILE A1017 9451 15690 7412 862 -254 -1286 C ATOM 1688 O ILE A1017 40.675 33.052 47.095 1.00 86.53 O ANISOU 1688 O ILE A1017 9447 15967 7466 944 -339 -1498 O ATOM 1689 CB ILE A1017 42.829 32.836 44.872 1.00 82.73 C ANISOU 1689 CB ILE A1017 9340 14802 7290 746 -253 -1222 C ATOM 1690 CG1 ILE A1017 43.393 33.130 43.462 1.00 81.84 C ANISOU 1690 CG1 ILE A1017 9443 14305 7349 682 -253 -1151 C ATOM 1691 CG2 ILE A1017 43.603 31.678 45.552 1.00 83.35 C ANISOU 1691 CG2 ILE A1017 9313 15079 7277 686 -141 -1028 C ATOM 1692 CD1 ILE A1017 44.890 33.504 43.411 1.00 86.19 C ANISOU 1692 CD1 ILE A1017 10037 14728 7983 630 -254 -1124 C ATOM 1693 N TYR A1018 40.418 30.899 46.411 1.00 82.63 N ANISOU 1693 N TYR A1018 8992 15462 6940 826 -158 -1080 N ATOM 1694 CA TYR A1018 39.953 30.348 47.681 1.00 83.84 C ANISOU 1694 CA TYR A1018 8918 16016 6922 872 -135 -1058 C ATOM 1695 C TYR A1018 40.834 29.159 48.055 1.00 87.24 C ANISOU 1695 C TYR A1018 9273 16558 7315 788 -22 -818 C ATOM 1696 O TYR A1018 41.735 28.809 47.292 1.00 85.59 O ANISOU 1696 O TYR A1018 9201 16105 7215 702 34 -686 O ATOM 1697 CB TYR A1018 38.458 29.948 47.608 1.00 85.73 C ANISOU 1697 CB TYR A1018 9112 16366 7095 918 -141 -1033 C ATOM 1698 CG TYR A1018 38.152 28.709 46.790 1.00 87.31 C ANISOU 1698 CG TYR A1018 9393 16439 7344 836 -53 -777 C ATOM 1699 CD1 TYR A1018 38.001 27.465 47.400 1.00 89.45 C ANISOU 1699 CD1 TYR A1018 9514 16948 7526 804 26 -568 C ATOM 1700 CD2 TYR A1018 37.960 28.786 45.414 1.00 87.54 C ANISOU 1700 CD2 TYR A1018 9636 16116 7508 796 -57 -748 C ATOM 1701 CE1 TYR A1018 37.706 26.322 46.656 1.00 89.70 C ANISOU 1701 CE1 TYR A1018 9613 16852 7617 731 95 -341 C ATOM 1702 CE2 TYR A1018 37.660 27.650 44.658 1.00 87.76 C ANISOU 1702 CE2 TYR A1018 9735 16029 7582 728 15 -530 C ATOM 1703 CZ TYR A1018 37.532 26.419 45.284 1.00 96.07 C ANISOU 1703 CZ TYR A1018 10640 17305 8557 696 88 -332 C ATOM 1704 OH TYR A1018 37.234 25.298 44.541 1.00 96.30 O ANISOU 1704 OH TYR A1018 10734 17208 8647 630 148 -125 O ATOM 1705 N LYS A1019 40.577 28.536 49.215 1.00 85.10 N ANISOU 1705 N LYS A1019 8781 16659 6892 815 12 -755 N ATOM 1706 CA LYS A1019 41.309 27.351 49.662 1.00 84.93 C ANISOU 1706 CA LYS A1019 8661 16777 6833 737 118 -513 C ATOM 1707 C LYS A1019 40.350 26.164 49.762 1.00 89.33 C ANISOU 1707 C LYS A1019 9118 17490 7332 723 173 -313 C ATOM 1708 O LYS A1019 39.202 26.345 50.179 1.00 89.64 O ANISOU 1708 O LYS A1019 9055 17726 7279 801 125 -394 O ATOM 1709 CB LYS A1019 42.012 27.610 51.006 1.00 88.47 C ANISOU 1709 CB LYS A1019 8912 17541 7160 770 113 -584 C ATOM 1710 N ASP A1020 40.805 24.954 49.371 1.00 85.25 N ANISOU 1710 N ASP A1020 8630 16885 6878 625 269 -52 N ATOM 1711 CA ASP A1020 39.956 23.763 49.445 1.00 85.00 C ANISOU 1711 CA ASP A1020 8500 16978 6818 603 316 157 C ATOM 1712 C ASP A1020 39.887 23.246 50.907 1.00 91.45 C ANISOU 1712 C ASP A1020 9027 18243 7476 628 342 244 C ATOM 1713 O ASP A1020 40.559 23.787 51.795 1.00 91.49 O ANISOU 1713 O ASP A1020 8921 18447 7395 660 331 141 O ATOM 1714 CB ASP A1020 40.449 22.644 48.490 1.00 85.02 C ANISOU 1714 CB ASP A1020 8630 16716 6957 494 398 396 C ATOM 1715 CG ASP A1020 41.764 21.958 48.846 1.00 89.42 C ANISOU 1715 CG ASP A1020 9131 17312 7534 416 482 563 C ATOM 1716 OD1 ASP A1020 42.617 22.601 49.497 1.00 89.58 O ANISOU 1716 OD1 ASP A1020 9094 17443 7499 431 475 462 O ATOM 1717 OD2 ASP A1020 41.963 20.801 48.417 1.00 92.41 O ANISOU 1717 OD2 ASP A1020 9530 17589 7993 339 551 789 O ATOM 1718 N THR A1021 39.083 22.187 51.136 1.00 89.19 N ANISOU 1718 N THR A1021 8614 18117 7158 613 375 442 N ATOM 1719 CA THR A1021 38.894 21.543 52.441 1.00 90.34 C ANISOU 1719 CA THR A1021 8469 18693 7161 631 403 574 C ATOM 1720 C THR A1021 40.225 20.965 52.977 1.00 94.81 C ANISOU 1720 C THR A1021 8947 19344 7731 557 483 726 C ATOM 1721 O THR A1021 40.397 20.879 54.195 1.00 95.63 O ANISOU 1721 O THR A1021 8816 19822 7697 587 495 751 O ATOM 1722 CB THR A1021 37.836 20.437 52.337 1.00 98.08 C ANISOU 1722 CB THR A1021 9364 19749 8155 610 421 792 C ATOM 1723 OG1 THR A1021 38.254 19.477 51.364 1.00 95.35 O ANISOU 1723 OG1 THR A1021 9159 19094 7976 504 481 995 O ATOM 1724 CG2 THR A1021 36.456 20.980 51.968 1.00 97.59 C ANISOU 1724 CG2 THR A1021 9356 19656 8066 689 343 653 C ATOM 1725 N GLU A1022 41.156 20.583 52.071 1.00 90.67 N ANISOU 1725 N GLU A1022 8606 18485 7359 464 537 826 N ATOM 1726 CA GLU A1022 42.477 20.041 52.423 1.00 90.53 C ANISOU 1726 CA GLU A1022 8535 18498 7364 387 616 973 C ATOM 1727 C GLU A1022 43.414 21.161 52.918 1.00 94.78 C ANISOU 1727 C GLU A1022 9084 19084 7842 422 589 764 C ATOM 1728 O GLU A1022 44.185 20.942 53.860 1.00 94.76 O ANISOU 1728 O GLU A1022 8918 19323 7762 405 629 828 O ATOM 1729 CB GLU A1022 43.109 19.311 51.224 1.00 90.56 C ANISOU 1729 CB GLU A1022 8737 18121 7549 286 677 1135 C ATOM 1730 N GLY A1023 43.337 22.336 52.280 1.00 90.96 N ANISOU 1730 N GLY A1023 8787 18370 7402 468 516 521 N ATOM 1731 CA GLY A1023 44.136 23.501 52.646 1.00 90.81 C ANISOU 1731 CA GLY A1023 8794 18357 7352 506 469 302 C ATOM 1732 C GLY A1023 44.698 24.313 51.495 1.00 92.18 C ANISOU 1732 C GLY A1023 9236 18118 7669 486 434 173 C ATOM 1733 O GLY A1023 44.700 25.548 51.557 1.00 92.22 O ANISOU 1733 O GLY A1023 9288 18089 7664 552 347 -75 O ATOM 1734 N TYR A1024 45.197 23.624 50.442 1.00 86.14 N ANISOU 1734 N TYR A1024 8640 17046 7044 398 497 343 N ATOM 1735 CA TYR A1024 45.839 24.227 49.265 1.00 84.43 C ANISOU 1735 CA TYR A1024 8673 16438 6968 367 479 272 C ATOM 1736 C TYR A1024 44.893 25.203 48.522 1.00 86.43 C ANISOU 1736 C TYR A1024 9064 16512 7264 434 383 67 C ATOM 1737 O TYR A1024 43.673 25.019 48.534 1.00 85.80 O ANISOU 1737 O TYR A1024 8938 16520 7142 477 358 56 O ATOM 1738 CB TYR A1024 46.305 23.129 48.305 1.00 84.38 C ANISOU 1738 CB TYR A1024 8793 16187 7082 272 567 508 C ATOM 1739 N TYR A1025 45.475 26.256 47.898 1.00 81.56 N ANISOU 1739 N TYR A1025 8606 15649 6736 441 326 -87 N ATOM 1740 CA TYR A1025 44.724 27.298 47.185 1.00 80.80 C ANISOU 1740 CA TYR A1025 8640 15362 6697 500 230 -285 C ATOM 1741 C TYR A1025 44.211 26.800 45.826 1.00 81.21 C ANISOU 1741 C TYR A1025 8874 15124 6858 460 256 -177 C ATOM 1742 O TYR A1025 44.944 26.144 45.082 1.00 79.98 O ANISOU 1742 O TYR A1025 8829 14772 6787 383 327 -13 O ATOM 1743 CB TYR A1025 45.579 28.550 46.981 1.00 82.45 C ANISOU 1743 CB TYR A1025 8944 15400 6982 513 157 -461 C ATOM 1744 CG TYR A1025 45.942 29.258 48.267 1.00 85.77 C ANISOU 1744 CG TYR A1025 9197 16088 7305 569 104 -622 C ATOM 1745 CD1 TYR A1025 47.141 28.989 48.919 1.00 87.86 C ANISOU 1745 CD1 TYR A1025 9385 16456 7542 521 156 -539 C ATOM 1746 CD2 TYR A1025 45.094 30.211 48.825 1.00 87.89 C ANISOU 1746 CD2 TYR A1025 9380 16504 7509 673 -1 -865 C ATOM 1747 CE1 TYR A1025 47.484 29.645 50.100 1.00 90.25 C ANISOU 1747 CE1 TYR A1025 9531 17008 7752 574 103 -695 C ATOM 1748 CE2 TYR A1025 45.423 30.867 50.011 1.00 90.19 C ANISOU 1748 CE2 TYR A1025 9512 17049 7708 732 -57 -1030 C ATOM 1749 CZ TYR A1025 46.621 30.583 50.645 1.00 98.61 C ANISOU 1749 CZ TYR A1025 10504 18218 8745 682 -5 -946 C ATOM 1750 OH TYR A1025 46.951 31.227 51.814 1.00101.93 O ANISOU 1750 OH TYR A1025 10764 18895 9071 743 -63 -1115 O ATOM 1751 N THR A1026 42.953 27.158 45.500 1.00 75.82 N ANISOU 1751 N THR A1026 8222 14417 6169 518 196 -281 N ATOM 1752 CA THR A1026 42.244 26.727 44.291 1.00 73.79 C ANISOU 1752 CA THR A1026 8117 13923 5996 493 210 -199 C ATOM 1753 C THR A1026 41.544 27.952 43.617 1.00 75.56 C ANISOU 1753 C THR A1026 8463 13967 6279 553 108 -409 C ATOM 1754 O THR A1026 41.407 29.001 44.249 1.00 76.30 O ANISOU 1754 O THR A1026 8491 14165 6334 622 26 -613 O ATOM 1755 CB THR A1026 41.236 25.626 44.712 1.00 81.83 C ANISOU 1755 CB THR A1026 9007 15150 6935 496 251 -61 C ATOM 1756 OG1 THR A1026 41.918 24.619 45.466 1.00 80.89 O ANISOU 1756 OG1 THR A1026 8749 15219 6767 445 333 121 O ATOM 1757 CG2 THR A1026 40.518 24.983 43.543 1.00 80.07 C ANISOU 1757 CG2 THR A1026 8921 14706 6796 464 271 46 C ATOM 1758 N ILE A1027 41.134 27.812 42.328 1.00 69.36 N ANISOU 1758 N ILE A1027 7850 12912 5591 527 112 -359 N ATOM 1759 CA ILE A1027 40.429 28.843 41.542 1.00 68.37 C ANISOU 1759 CA ILE A1027 7847 12595 5534 573 25 -522 C ATOM 1760 C ILE A1027 39.434 28.162 40.570 1.00 70.45 C ANISOU 1760 C ILE A1027 8208 12727 5833 555 50 -420 C ATOM 1761 O ILE A1027 39.642 27.008 40.188 1.00 69.63 O ANISOU 1761 O ILE A1027 8129 12582 5744 494 132 -226 O ATOM 1762 CB ILE A1027 41.430 29.768 40.771 1.00 70.98 C ANISOU 1762 CB ILE A1027 8325 12654 5989 550 -11 -590 C ATOM 1763 CG1 ILE A1027 40.760 31.041 40.194 1.00 71.34 C ANISOU 1763 CG1 ILE A1027 8459 12540 6108 607 -119 -784 C ATOM 1764 CG2 ILE A1027 42.198 29.009 39.681 1.00 70.68 C ANISOU 1764 CG2 ILE A1027 8432 12383 6039 467 70 -397 C ATOM 1765 CD1 ILE A1027 40.183 31.991 41.181 1.00 77.74 C ANISOU 1765 CD1 ILE A1027 9142 13542 6854 697 -214 -1005 C ATOM 1766 N GLY A1028 38.386 28.893 40.179 1.00 65.97 N ANISOU 1766 N GLY A1028 7693 12090 5283 610 -25 -557 N ATOM 1767 CA GLY A1028 37.363 28.429 39.244 1.00 64.47 C ANISOU 1767 CA GLY A1028 7598 11770 5127 601 -18 -491 C ATOM 1768 C GLY A1028 36.712 27.117 39.620 1.00 66.76 C ANISOU 1768 C GLY A1028 7786 12238 5342 585 40 -331 C ATOM 1769 O GLY A1028 36.381 26.889 40.786 1.00 66.56 O ANISOU 1769 O GLY A1028 7581 12504 5205 622 37 -342 O ATOM 1770 N ILE A1029 36.567 26.233 38.627 1.00 62.20 N ANISOU 1770 N ILE A1029 7315 11488 4828 529 91 -177 N ATOM 1771 CA ILE A1029 35.965 24.917 38.796 1.00 61.67 C ANISOU 1771 CA ILE A1029 7167 11540 4725 503 141 -4 C ATOM 1772 C ILE A1029 37.083 23.923 39.232 1.00 66.24 C ANISOU 1772 C ILE A1029 7676 12187 5304 440 225 168 C ATOM 1773 O ILE A1029 37.677 23.226 38.401 1.00 65.28 O ANISOU 1773 O ILE A1029 7662 11874 5267 379 279 295 O ATOM 1774 CB ILE A1029 35.224 24.476 37.494 1.00 63.52 C ANISOU 1774 CB ILE A1029 7548 11549 5037 481 141 60 C ATOM 1775 CG1 ILE A1029 34.178 25.535 37.072 1.00 63.64 C ANISOU 1775 CG1 ILE A1029 7625 11506 5051 542 59 -109 C ATOM 1776 CG2 ILE A1029 34.574 23.099 37.667 1.00 64.34 C ANISOU 1776 CG2 ILE A1029 7562 11760 5123 450 182 245 C ATOM 1777 CD1 ILE A1029 33.400 25.223 35.822 1.00 70.55 C ANISOU 1777 CD1 ILE A1029 8638 12174 5993 525 52 -62 C ATOM 1778 N GLY A1030 37.370 23.930 40.537 1.00 63.79 N ANISOU 1778 N GLY A1030 7185 12154 4898 460 232 159 N ATOM 1779 CA GLY A1030 38.341 23.057 41.191 1.00 63.89 C ANISOU 1779 CA GLY A1030 7092 12288 4893 407 307 317 C ATOM 1780 C GLY A1030 39.756 23.008 40.636 1.00 67.87 C ANISOU 1780 C GLY A1030 7715 12590 5482 348 357 370 C ATOM 1781 O GLY A1030 40.433 21.986 40.790 1.00 67.03 O ANISOU 1781 O GLY A1030 7562 12511 5394 290 430 545 O ATOM 1782 N HIS A1031 40.237 24.110 40.014 1.00 64.92 N ANISOU 1782 N HIS A1031 7484 12020 5163 363 316 227 N ATOM 1783 CA HIS A1031 41.601 24.160 39.474 1.00 64.45 C ANISOU 1783 CA HIS A1031 7534 11775 5180 311 359 278 C ATOM 1784 C HIS A1031 42.591 24.497 40.585 1.00 70.06 C ANISOU 1784 C HIS A1031 8122 12666 5832 311 369 249 C ATOM 1785 O HIS A1031 42.626 25.632 41.068 1.00 69.83 O ANISOU 1785 O HIS A1031 8062 12698 5772 360 301 70 O ATOM 1786 CB HIS A1031 41.732 25.171 38.310 1.00 64.63 C ANISOU 1786 CB HIS A1031 7749 11514 5293 323 309 165 C ATOM 1787 CG HIS A1031 43.119 25.257 37.729 1.00 67.29 C ANISOU 1787 CG HIS A1031 8190 11672 5704 274 349 225 C ATOM 1788 ND1 HIS A1031 43.538 24.398 36.729 1.00 68.07 N ANISOU 1788 ND1 HIS A1031 8402 11590 5871 224 415 376 N ATOM 1789 CD2 HIS A1031 44.129 26.109 38.021 1.00 69.06 C ANISOU 1789 CD2 HIS A1031 8416 11880 5943 274 327 151 C ATOM 1790 CE1 HIS A1031 44.784 24.745 36.453 1.00 67.10 C ANISOU 1790 CE1 HIS A1031 8343 11357 5794 196 435 397 C ATOM 1791 NE2 HIS A1031 45.183 25.770 37.201 1.00 68.03 N ANISOU 1791 NE2 HIS A1031 8399 11564 5887 221 383 270 N ATOM 1792 N LEU A1032 43.408 23.508 40.972 1.00 68.08 N ANISOU 1792 N LEU A1032 7799 12496 5573 254 452 421 N ATOM 1793 CA LEU A1032 44.444 23.683 41.983 1.00 69.07 C ANISOU 1793 CA LEU A1032 7809 12789 5645 243 474 422 C ATOM 1794 C LEU A1032 45.606 24.494 41.382 1.00 74.65 C ANISOU 1794 C LEU A1032 8655 13279 6429 223 464 364 C ATOM 1795 O LEU A1032 46.113 24.154 40.303 1.00 73.32 O ANISOU 1795 O LEU A1032 8639 12866 6353 180 502 455 O ATOM 1796 CB LEU A1032 44.924 22.313 42.515 1.00 68.90 C ANISOU 1796 CB LEU A1032 7668 12910 5602 184 568 644 C ATOM 1797 CG LEU A1032 45.838 22.331 43.751 1.00 73.90 C ANISOU 1797 CG LEU A1032 8135 13788 6155 173 596 663 C ATOM 1798 CD1 LEU A1032 45.063 22.750 44.991 1.00 74.98 C ANISOU 1798 CD1 LEU A1032 8078 14249 6161 240 545 553 C ATOM 1799 CD2 LEU A1032 46.431 20.963 44.002 1.00 75.70 C ANISOU 1799 CD2 LEU A1032 8282 14084 6398 103 695 903 C ATOM 1800 N LEU A1033 45.990 25.584 42.065 1.00 73.28 N ANISOU 1800 N LEU A1033 8426 13198 6220 258 407 209 N ATOM 1801 CA LEU A1033 47.059 26.485 41.635 1.00 73.60 C ANISOU 1801 CA LEU A1033 8574 13053 6336 244 379 144 C ATOM 1802 C LEU A1033 48.420 26.043 42.205 1.00 80.22 C ANISOU 1802 C LEU A1033 9350 13970 7160 188 449 265 C ATOM 1803 O LEU A1033 49.404 25.981 41.456 1.00 79.20 O ANISOU 1803 O LEU A1033 9341 13639 7112 141 485 351 O ATOM 1804 CB LEU A1033 46.733 27.924 42.077 1.00 74.21 C ANISOU 1804 CB LEU A1033 8622 13172 6401 314 263 -101 C ATOM 1805 CG LEU A1033 45.520 28.571 41.411 1.00 78.18 C ANISOU 1805 CG LEU A1033 9206 13561 6940 369 184 -236 C ATOM 1806 CD1 LEU A1033 45.065 29.789 42.168 1.00 79.24 C ANISOU 1806 CD1 LEU A1033 9254 13818 7036 449 74 -475 C ATOM 1807 CD2 LEU A1033 45.792 28.885 39.948 1.00 79.15 C ANISOU 1807 CD2 LEU A1033 9532 13347 7193 340 175 -205 C ATOM 1808 N THR A1034 48.471 25.741 43.528 1.00 79.29 N ANISOU 1808 N THR A1034 9038 14156 6934 197 470 277 N ATOM 1809 CA THR A1034 49.673 25.286 44.240 1.00 80.00 C ANISOU 1809 CA THR A1034 9037 14367 6992 147 538 393 C ATOM 1810 C THR A1034 49.294 24.593 45.556 1.00 86.04 C ANISOU 1810 C THR A1034 9575 15488 7630 157 572 449 C ATOM 1811 O THR A1034 48.235 24.870 46.129 1.00 86.52 O ANISOU 1811 O THR A1034 9531 15733 7610 221 518 336 O ATOM 1812 CB THR A1034 50.660 26.462 44.525 1.00 90.56 C ANISOU 1812 CB THR A1034 10391 15667 8350 156 479 258 C ATOM 1813 OG1 THR A1034 51.854 25.935 45.105 1.00 91.91 O ANISOU 1813 OG1 THR A1034 10488 15939 8497 100 554 393 O ATOM 1814 CG2 THR A1034 50.072 27.547 45.446 1.00 89.62 C ANISOU 1814 CG2 THR A1034 10158 15735 8158 239 373 18 C ATOM 1815 N LYS A1035 50.186 23.720 46.044 1.00 83.45 N ANISOU 1815 N LYS A1035 9161 15264 7282 97 661 627 N ATOM 1816 CA LYS A1035 50.022 23.052 47.332 1.00 84.47 C ANISOU 1816 CA LYS A1035 9057 15744 7293 98 700 707 C ATOM 1817 C LYS A1035 50.582 23.951 48.446 1.00 89.88 C ANISOU 1817 C LYS A1035 9620 16642 7889 133 653 557 C ATOM 1818 O LYS A1035 50.206 23.801 49.613 1.00 90.33 O ANISOU 1818 O LYS A1035 9471 17031 7821 169 648 534 O ATOM 1819 CB LYS A1035 50.705 21.676 47.320 1.00 86.54 C ANISOU 1819 CB LYS A1035 9279 16016 7587 14 814 975 C ATOM 1820 N SER A1036 51.460 24.918 48.054 1.00 86.47 N ANISOU 1820 N SER A1036 9313 16018 7526 128 613 451 N ATOM 1821 CA SER A1036 52.126 25.899 48.918 1.00 87.18 C ANISOU 1821 CA SER A1036 9323 16235 7565 157 554 292 C ATOM 1822 C SER A1036 51.096 26.718 49.728 1.00 92.58 C ANISOU 1822 C SER A1036 9883 17146 8149 258 454 58 C ATOM 1823 O SER A1036 50.040 27.064 49.190 1.00 92.38 O ANISOU 1823 O SER A1036 9927 17027 8147 308 396 -45 O ATOM 1824 CB SER A1036 52.997 26.832 48.078 1.00 89.95 C ANISOU 1824 CB SER A1036 9861 16275 8041 139 507 215 C ATOM 1825 OG SER A1036 53.722 27.753 48.876 1.00 98.78 O ANISOU 1825 OG SER A1036 10908 17494 9131 162 444 70 O ATOM 1826 N PRO A1037 51.380 27.028 51.022 1.00 90.16 N ANISOU 1826 N PRO A1037 9387 17146 7725 293 432 -30 N ATOM 1827 CA PRO A1037 50.397 27.767 51.837 1.00 90.90 C ANISOU 1827 CA PRO A1037 9346 17484 7709 399 336 -258 C ATOM 1828 C PRO A1037 50.492 29.294 51.662 1.00 93.83 C ANISOU 1828 C PRO A1037 9807 17699 8145 462 203 -539 C ATOM 1829 O PRO A1037 49.908 30.040 52.460 1.00 94.61 O ANISOU 1829 O PRO A1037 9789 18000 8159 557 113 -759 O ATOM 1830 CB PRO A1037 50.755 27.370 53.278 1.00 93.81 C ANISOU 1830 CB PRO A1037 9467 18252 7923 408 373 -222 C ATOM 1831 CG PRO A1037 52.045 26.582 53.194 1.00 97.68 C ANISOU 1831 CG PRO A1037 9977 18678 8459 300 483 19 C ATOM 1832 CD PRO A1037 52.576 26.680 51.814 1.00 92.09 C ANISOU 1832 CD PRO A1037 9522 17547 7922 240 494 77 C ATOM 1833 N SER A1038 51.175 29.758 50.600 1.00 88.21 N ANISOU 1833 N SER A1038 9296 16630 7589 414 186 -531 N ATOM 1834 CA SER A1038 51.312 31.179 50.298 1.00 87.80 C ANISOU 1834 CA SER A1038 9338 16388 7634 462 56 -767 C ATOM 1835 C SER A1038 50.304 31.595 49.245 1.00 89.33 C ANISOU 1835 C SER A1038 9677 16350 7915 496 -1 -845 C ATOM 1836 O SER A1038 50.179 30.928 48.218 1.00 87.50 O ANISOU 1836 O SER A1038 9576 15920 7750 441 68 -674 O ATOM 1837 CB SER A1038 52.728 31.492 49.831 1.00 90.87 C ANISOU 1837 CB SER A1038 9845 16538 8143 390 62 -701 C ATOM 1838 OG SER A1038 52.883 32.848 49.441 1.00 99.64 O ANISOU 1838 OG SER A1038 11050 17436 9374 428 -69 -906 O ATOM 1839 N LEU A1039 49.577 32.692 49.508 1.00 86.25 N ANISOU 1839 N LEU A1039 9258 15988 7526 590 -128 -1107 N ATOM 1840 CA LEU A1039 48.571 33.240 48.594 1.00 85.76 C ANISOU 1840 CA LEU A1039 9318 15718 7547 631 -196 -1208 C ATOM 1841 C LEU A1039 49.239 33.826 47.343 1.00 89.07 C ANISOU 1841 C LEU A1039 9948 15737 8158 579 -229 -1181 C ATOM 1842 O LEU A1039 48.721 33.654 46.235 1.00 88.14 O ANISOU 1842 O LEU A1039 9971 15401 8115 559 -212 -1106 O ATOM 1843 CB LEU A1039 47.721 34.318 49.304 1.00 87.07 C ANISOU 1843 CB LEU A1039 9381 16037 7667 750 -330 -1507 C ATOM 1844 CG LEU A1039 46.627 35.017 48.476 1.00 91.34 C ANISOU 1844 CG LEU A1039 10032 16380 8294 804 -415 -1640 C ATOM 1845 CD1 LEU A1039 45.583 34.024 47.959 1.00 90.35 C ANISOU 1845 CD1 LEU A1039 9939 16275 8116 790 -332 -1485 C ATOM 1846 CD2 LEU A1039 45.962 36.108 49.279 1.00 95.63 C ANISOU 1846 CD2 LEU A1039 10460 17081 8795 924 -551 -1944 C ATOM 1847 N ASN A1040 50.391 34.504 47.525 1.00 85.35 N ANISOU 1847 N ASN A1040 9490 15179 7761 558 -279 -1235 N ATOM 1848 CA ASN A1040 51.150 35.126 46.438 1.00 84.19 C ANISOU 1848 CA ASN A1040 9518 14676 7796 509 -319 -1202 C ATOM 1849 C ASN A1040 51.803 34.046 45.565 1.00 85.75 C ANISOU 1849 C ASN A1040 9833 14724 8025 410 -185 -914 C ATOM 1850 O ASN A1040 52.023 34.286 44.377 1.00 84.09 O ANISOU 1850 O ASN A1040 9784 14220 7946 374 -194 -846 O ATOM 1851 CB ASN A1040 52.189 36.093 46.996 1.00 85.15 C ANISOU 1851 CB ASN A1040 9595 14777 7980 515 -411 -1330 C ATOM 1852 CG ASN A1040 51.570 37.273 47.724 1.00108.76 C ANISOU 1852 CG ASN A1040 12485 17873 10968 620 -563 -1638 C ATOM 1853 OD1 ASN A1040 50.494 37.781 47.371 1.00101.62 O ANISOU 1853 OD1 ASN A1040 11619 16880 10109 680 -641 -1775 O ATOM 1854 ND2 ASN A1040 52.265 37.779 48.719 1.00102.75 N ANISOU 1854 ND2 ASN A1040 11591 17293 10158 647 -613 -1760 N ATOM 1855 N ALA A1041 52.047 32.843 46.136 1.00 82.00 N ANISOU 1855 N ALA A1041 9268 14458 7430 370 -62 -743 N ATOM 1856 CA ALA A1041 52.557 31.686 45.395 1.00 80.57 C ANISOU 1856 CA ALA A1041 9179 14166 7268 284 70 -475 C ATOM 1857 C ALA A1041 51.469 31.139 44.486 1.00 83.41 C ANISOU 1857 C ALA A1041 9629 14423 7641 291 102 -413 C ATOM 1858 O ALA A1041 51.759 30.650 43.393 1.00 81.85 O ANISOU 1858 O ALA A1041 9574 14002 7521 239 159 -259 O ATOM 1859 CB ALA A1041 53.050 30.614 46.352 1.00 81.36 C ANISOU 1859 CB ALA A1041 9136 14529 7246 245 177 -327 C ATOM 1860 N ALA A1042 50.207 31.245 44.939 1.00 80.72 N ANISOU 1860 N ALA A1042 9199 14250 7219 361 60 -540 N ATOM 1861 CA ALA A1042 49.032 30.863 44.168 1.00 80.23 C ANISOU 1861 CA ALA A1042 9210 14107 7166 378 71 -513 C ATOM 1862 C ALA A1042 48.760 31.908 43.089 1.00 85.00 C ANISOU 1862 C ALA A1042 9972 14419 7905 400 -22 -628 C ATOM 1863 O ALA A1042 48.474 31.541 41.943 1.00 83.89 O ANISOU 1863 O ALA A1042 9970 14072 7831 370 13 -524 O ATOM 1864 CB ALA A1042 47.829 30.700 45.083 1.00 81.62 C ANISOU 1864 CB ALA A1042 9228 14573 7210 448 49 -611 C ATOM 1865 N LYS A1043 48.906 33.217 43.444 1.00 82.46 N ANISOU 1865 N LYS A1043 9625 14074 7632 450 -143 -840 N ATOM 1866 CA LYS A1043 48.733 34.338 42.513 1.00 82.09 C ANISOU 1866 CA LYS A1043 9707 13753 7732 471 -248 -956 C ATOM 1867 C LYS A1043 49.808 34.287 41.428 1.00 84.85 C ANISOU 1867 C LYS A1043 10207 13826 8205 394 -210 -793 C ATOM 1868 O LYS A1043 49.525 34.640 40.287 1.00 83.87 O ANISOU 1868 O LYS A1043 10216 13463 8186 388 -241 -779 O ATOM 1869 CB LYS A1043 48.753 35.699 43.231 1.00 85.71 C ANISOU 1869 CB LYS A1043 10084 14255 8226 540 -391 -1213 C ATOM 1870 CG LYS A1043 47.514 35.949 44.087 1.00 96.89 C ANISOU 1870 CG LYS A1043 11370 15909 9534 635 -448 -1405 C ATOM 1871 CD LYS A1043 47.469 37.349 44.666 1.00105.96 C ANISOU 1871 CD LYS A1043 12451 17073 10738 713 -603 -1681 C ATOM 1872 CE LYS A1043 46.186 37.573 45.430 1.00116.71 C ANISOU 1872 CE LYS A1043 13688 18669 11985 814 -656 -1868 C ATOM 1873 NZ LYS A1043 46.096 38.954 45.972 1.00127.49 N ANISOU 1873 NZ LYS A1043 14984 20047 13409 901 -815 -2157 N ATOM 1874 N SER A1044 51.015 33.792 41.766 1.00 81.29 N ANISOU 1874 N SER A1044 9730 13422 7733 335 -138 -657 N ATOM 1875 CA SER A1044 52.101 33.607 40.802 1.00 80.30 C ANISOU 1875 CA SER A1044 9734 13070 7705 263 -88 -480 C ATOM 1876 C SER A1044 51.675 32.627 39.718 1.00 82.67 C ANISOU 1876 C SER A1044 10149 13256 8006 231 6 -309 C ATOM 1877 O SER A1044 51.810 32.932 38.533 1.00 82.04 O ANISOU 1877 O SER A1044 10207 12932 8031 214 -10 -259 O ATOM 1878 CB SER A1044 53.364 33.112 41.502 1.00 84.19 C ANISOU 1878 CB SER A1044 10158 13677 8151 211 -19 -365 C ATOM 1879 OG SER A1044 54.444 32.980 40.593 1.00 92.77 O ANISOU 1879 OG SER A1044 11366 14554 9330 147 26 -197 O ATOM 1880 N GLU A1045 51.100 31.474 40.137 1.00 78.36 N ANISOU 1880 N GLU A1045 9535 12893 7346 227 96 -226 N ATOM 1881 CA GLU A1045 50.623 30.411 39.257 1.00 77.00 C ANISOU 1881 CA GLU A1045 9448 12642 7167 199 184 -70 C ATOM 1882 C GLU A1045 49.425 30.885 38.408 1.00 80.60 C ANISOU 1882 C GLU A1045 9994 12958 7671 242 120 -165 C ATOM 1883 O GLU A1045 49.411 30.637 37.201 1.00 79.12 O ANISOU 1883 O GLU A1045 9943 12570 7549 217 150 -67 O ATOM 1884 CB GLU A1045 50.232 29.169 40.075 1.00 78.20 C ANISOU 1884 CB GLU A1045 9476 13041 7196 191 271 21 C ATOM 1885 N LEU A1046 48.450 31.593 39.024 1.00 78.06 N ANISOU 1885 N LEU A1046 9595 12746 7318 309 30 -359 N ATOM 1886 CA LEU A1046 47.250 32.072 38.328 1.00 77.91 C ANISOU 1886 CA LEU A1046 9646 12615 7339 353 -34 -458 C ATOM 1887 C LEU A1046 47.602 33.131 37.274 1.00 82.33 C ANISOU 1887 C LEU A1046 10338 12898 8045 348 -109 -500 C ATOM 1888 O LEU A1046 47.143 33.005 36.139 1.00 81.51 O ANISOU 1888 O LEU A1046 10353 12621 7995 338 -96 -437 O ATOM 1889 CB LEU A1046 46.218 32.647 39.317 1.00 78.89 C ANISOU 1889 CB LEU A1046 9644 12936 7394 431 -116 -662 C ATOM 1890 CG LEU A1046 44.869 33.095 38.721 1.00 83.55 C ANISOU 1890 CG LEU A1046 10289 13443 8012 481 -180 -769 C ATOM 1891 CD1 LEU A1046 44.097 31.917 38.138 1.00 82.82 C ANISOU 1891 CD1 LEU A1046 10244 13352 7873 459 -94 -623 C ATOM 1892 CD2 LEU A1046 44.018 33.759 39.763 1.00 87.40 C ANISOU 1892 CD2 LEU A1046 10644 14134 8432 564 -266 -979 C ATOM 1893 N ASP A1047 48.421 34.154 37.635 1.00 79.87 N ANISOU 1893 N ASP A1047 9997 12546 7803 355 -190 -597 N ATOM 1894 CA ASP A1047 48.830 35.233 36.716 1.00 79.74 C ANISOU 1894 CA ASP A1047 10084 12272 7941 349 -274 -628 C ATOM 1895 C ASP A1047 49.706 34.693 35.574 1.00 81.59 C ANISOU 1895 C ASP A1047 10445 12326 8231 282 -193 -410 C ATOM 1896 O ASP A1047 49.982 35.422 34.620 1.00 80.65 O ANISOU 1896 O ASP A1047 10417 11991 8233 271 -247 -392 O ATOM 1897 CB ASP A1047 49.588 36.353 37.463 1.00 82.87 C ANISOU 1897 CB ASP A1047 10406 12679 8404 365 -379 -765 C ATOM 1898 CG ASP A1047 48.785 37.120 38.508 1.00 95.68 C ANISOU 1898 CG ASP A1047 11906 14455 9993 445 -485 -1013 C ATOM 1899 OD1 ASP A1047 47.569 36.854 38.642 1.00 96.11 O ANISOU 1899 OD1 ASP A1047 11934 14609 9973 490 -480 -1081 O ATOM 1900 OD2 ASP A1047 49.374 37.995 39.184 1.00102.93 O ANISOU 1900 OD2 ASP A1047 12752 15394 10961 465 -576 -1141 O ATOM 1901 N LYS A1048 50.124 33.420 35.665 1.00 77.48 N ANISOU 1901 N LYS A1048 9919 11897 7621 240 -67 -245 N ATOM 1902 CA LYS A1048 50.930 32.785 34.635 1.00 76.70 C ANISOU 1902 CA LYS A1048 9932 11654 7558 185 18 -44 C ATOM 1903 C LYS A1048 50.060 31.784 33.842 1.00 79.53 C ANISOU 1903 C LYS A1048 10362 11980 7875 184 91 43 C ATOM 1904 O LYS A1048 50.285 31.601 32.643 1.00 78.42 O ANISOU 1904 O LYS A1048 10340 11667 7788 164 120 151 O ATOM 1905 CB LYS A1048 52.166 32.099 35.254 1.00 79.60 C ANISOU 1905 CB LYS A1048 10245 12126 7874 137 104 84 C ATOM 1906 CG LYS A1048 53.251 31.722 34.235 1.00101.41 C ANISOU 1906 CG LYS A1048 13114 14726 10691 87 170 274 C ATOM 1907 CD LYS A1048 53.838 32.965 33.522 1.00114.03 C ANISOU 1907 CD LYS A1048 14777 16128 12421 85 75 249 C ATOM 1908 CE LYS A1048 54.835 32.634 32.439 1.00122.55 C ANISOU 1908 CE LYS A1048 15960 17057 13548 44 136 441 C ATOM 1909 NZ LYS A1048 55.355 33.860 31.774 1.00128.95 N ANISOU 1909 NZ LYS A1048 16816 17691 14490 42 37 431 N ATOM 1910 N ALA A1049 49.049 31.175 34.502 1.00 76.03 N ANISOU 1910 N ALA A1049 9844 11707 7338 210 113 -6 N ATOM 1911 CA ALA A1049 48.122 30.232 33.863 1.00 75.18 C ANISOU 1911 CA ALA A1049 9790 11581 7195 212 168 63 C ATOM 1912 C ALA A1049 47.103 30.961 32.975 1.00 79.44 C ANISOU 1912 C ALA A1049 10414 11975 7796 248 92 -34 C ATOM 1913 O ALA A1049 46.526 30.342 32.081 1.00 78.49 O ANISOU 1913 O ALA A1049 10377 11767 7677 243 130 37 O ATOM 1914 CB ALA A1049 47.393 29.415 34.918 1.00 76.02 C ANISOU 1914 CB ALA A1049 9770 11924 7190 226 205 50 C ATOM 1915 N ILE A1050 46.878 32.268 33.229 1.00 77.05 N ANISOU 1915 N ILE A1050 10083 11644 7548 286 -20 -200 N ATOM 1916 CA ILE A1050 45.928 33.109 32.487 1.00 77.05 C ANISOU 1916 CA ILE A1050 10147 11511 7617 323 -105 -304 C ATOM 1917 C ILE A1050 46.708 34.139 31.636 1.00 81.39 C ANISOU 1917 C ILE A1050 10775 11847 8303 309 -171 -297 C ATOM 1918 O ILE A1050 46.248 34.511 30.553 1.00 80.81 O ANISOU 1918 O ILE A1050 10791 11614 8300 316 -206 -294 O ATOM 1919 CB ILE A1050 44.932 33.799 33.468 1.00 80.93 C ANISOU 1919 CB ILE A1050 10532 12146 8071 385 -191 -506 C ATOM 1920 CG1 ILE A1050 44.208 32.772 34.396 1.00 81.20 C ANISOU 1920 CG1 ILE A1050 10465 12423 7965 399 -127 -494 C ATOM 1921 CG2 ILE A1050 43.937 34.716 32.747 1.00 82.09 C ANISOU 1921 CG2 ILE A1050 10738 12157 8294 425 -281 -618 C ATOM 1922 CD1 ILE A1050 43.346 31.624 33.699 1.00 86.91 C ANISOU 1922 CD1 ILE A1050 11250 13130 8642 384 -49 -373 C ATOM 1923 N GLY A1051 47.876 34.559 32.124 1.00 78.51 N ANISOU 1923 N GLY A1051 10371 11485 7973 286 -185 -279 N ATOM 1924 CA GLY A1051 48.748 35.496 31.421 1.00 78.62 C ANISOU 1924 CA GLY A1051 10442 11310 8119 266 -246 -247 C ATOM 1925 C GLY A1051 48.773 36.882 32.022 1.00 83.45 C ANISOU 1925 C GLY A1051 10986 11897 8826 299 -386 -424 C ATOM 1926 O GLY A1051 49.841 37.383 32.387 1.00 83.52 O ANISOU 1926 O GLY A1051 10958 11883 8892 279 -422 -417 O ATOM 1927 N ARG A1052 47.595 37.512 32.125 1.00 80.20 N ANISOU 1927 N ARG A1052 10552 11483 8436 352 -469 -587 N ATOM 1928 CA ARG A1052 47.452 38.858 32.680 1.00 81.02 C ANISOU 1928 CA ARG A1052 10587 11558 8640 395 -614 -782 C ATOM 1929 C ARG A1052 47.601 38.845 34.220 1.00 85.94 C ANISOU 1929 C ARG A1052 11073 12405 9175 425 -631 -916 C ATOM 1930 O ARG A1052 47.440 37.795 34.853 1.00 85.12 O ANISOU 1930 O ARG A1052 10923 12497 8923 421 -533 -872 O ATOM 1931 CB ARG A1052 46.091 39.460 32.284 1.00 80.58 C ANISOU 1931 CB ARG A1052 10549 11440 8627 446 -691 -913 C ATOM 1932 CG ARG A1052 44.896 38.717 32.861 1.00 88.62 C ANISOU 1932 CG ARG A1052 11524 12649 9497 486 -641 -982 C ATOM 1933 CD ARG A1052 43.596 39.402 32.530 1.00 98.29 C ANISOU 1933 CD ARG A1052 12757 13819 10771 540 -729 -1126 C ATOM 1934 NE ARG A1052 42.492 38.831 33.297 1.00106.91 N ANISOU 1934 NE ARG A1052 13780 15121 11718 586 -696 -1210 N ATOM 1935 CZ ARG A1052 42.117 39.263 34.498 1.00120.75 C ANISOU 1935 CZ ARG A1052 15409 17053 13417 647 -757 -1393 C ATOM 1936 NH1 ARG A1052 42.753 40.274 35.078 1.00107.57 N ANISOU 1936 NH1 ARG A1052 13673 15366 11831 670 -858 -1526 N ATOM 1937 NH2 ARG A1052 41.106 38.687 35.129 1.00107.83 N ANISOU 1937 NH2 ARG A1052 13708 15618 11644 688 -722 -1444 N ATOM 1938 N ASN A1053 47.892 40.018 34.814 1.00 83.59 N ANISOU 1938 N ASN A1053 10704 12080 8974 456 -761 -1079 N ATOM 1939 CA ASN A1053 48.007 40.170 36.266 1.00 84.19 C ANISOU 1939 CA ASN A1053 10643 12370 8975 495 -796 -1235 C ATOM 1940 C ASN A1053 46.586 40.238 36.857 1.00 88.84 C ANISOU 1940 C ASN A1053 11162 13115 9477 573 -831 -1416 C ATOM 1941 O ASN A1053 46.000 41.320 36.977 1.00 89.68 O ANISOU 1941 O ASN A1053 11239 13162 9674 631 -960 -1606 O ATOM 1942 CB ASN A1053 48.856 41.405 36.625 1.00 84.60 C ANISOU 1942 CB ASN A1053 10647 12324 9175 503 -931 -1348 C ATOM 1943 CG ASN A1053 50.263 41.405 36.055 1.00 99.34 C ANISOU 1943 CG ASN A1053 12576 14038 11131 427 -905 -1161 C ATOM 1944 OD1 ASN A1053 50.637 40.580 35.208 1.00 90.81 O ANISOU 1944 OD1 ASN A1053 11591 12891 10023 372 -793 -946 O ATOM 1945 ND2 ASN A1053 51.061 42.372 36.474 1.00 90.48 N ANISOU 1945 ND2 ASN A1053 11400 12850 10128 428 -1016 -1243 N ATOM 1946 N THR A1054 46.015 39.058 37.153 1.00 84.31 N ANISOU 1946 N THR A1054 10566 12731 8738 573 -716 -1344 N ATOM 1947 CA THR A1054 44.639 38.888 37.631 1.00 84.14 C ANISOU 1947 CA THR A1054 10482 12877 8613 639 -725 -1466 C ATOM 1948 C THR A1054 44.435 39.401 39.066 1.00 88.11 C ANISOU 1948 C THR A1054 10822 13612 9043 713 -800 -1683 C ATOM 1949 O THR A1054 43.338 39.867 39.377 1.00 88.00 O ANISOU 1949 O THR A1054 10756 13672 9007 788 -871 -1854 O ATOM 1950 CB THR A1054 44.241 37.407 37.578 1.00 92.57 C ANISOU 1950 CB THR A1054 11559 14080 9533 608 -581 -1297 C ATOM 1951 OG1 THR A1054 45.116 36.647 38.414 1.00 91.19 O ANISOU 1951 OG1 THR A1054 11304 14084 9261 576 -500 -1209 O ATOM 1952 CG2 THR A1054 44.247 36.844 36.156 1.00 90.53 C ANISOU 1952 CG2 THR A1054 11455 13612 9330 550 -509 -1106 C ATOM 1953 N ASN A1055 45.468 39.268 39.943 1.00 84.62 N ANISOU 1953 N ASN A1055 10296 13302 8554 696 -781 -1674 N ATOM 1954 CA ASN A1055 45.460 39.644 41.375 1.00 85.43 C ANISOU 1954 CA ASN A1055 10232 13660 8569 763 -840 -1865 C ATOM 1955 C ASN A1055 44.443 38.745 42.145 1.00 87.65 C ANISOU 1955 C ASN A1055 10408 14245 8652 807 -767 -1871 C ATOM 1956 O ASN A1055 43.998 39.079 43.246 1.00 87.92 O ANISOU 1956 O ASN A1055 10296 14515 8593 886 -823 -2053 O ATOM 1957 CB ASN A1055 45.146 41.154 41.568 1.00 89.06 C ANISOU 1957 CB ASN A1055 10655 14030 9154 840 -1017 -2132 C ATOM 1958 CG ASN A1055 45.284 41.685 42.987 1.00120.99 C ANISOU 1958 CG ASN A1055 14528 18315 13126 917 -1098 -2356 C ATOM 1959 OD1 ASN A1055 45.955 41.099 43.852 1.00115.66 O ANISOU 1959 OD1 ASN A1055 13761 17850 12335 901 -1035 -2310 O ATOM 1960 ND2 ASN A1055 44.700 42.850 43.238 1.00116.73 N ANISOU 1960 ND2 ASN A1055 13942 17745 12664 1004 -1245 -2609 N ATOM 1961 N GLY A1056 44.134 37.590 41.563 1.00 82.33 N ANISOU 1961 N GLY A1056 9799 13566 7917 755 -645 -1665 N ATOM 1962 CA GLY A1056 43.196 36.638 42.134 1.00 81.74 C ANISOU 1962 CA GLY A1056 9634 13749 7676 783 -572 -1626 C ATOM 1963 C GLY A1056 41.816 36.696 41.513 1.00 84.97 C ANISOU 1963 C GLY A1056 10099 14095 8092 822 -596 -1665 C ATOM 1964 O GLY A1056 41.037 35.761 41.687 1.00 84.18 O ANISOU 1964 O GLY A1056 9963 14143 7880 823 -521 -1569 O ATOM 1965 N VAL A1057 41.504 37.794 40.781 1.00 81.49 N ANISOU 1965 N VAL A1057 9742 13430 7790 851 -703 -1797 N ATOM 1966 CA VAL A1057 40.205 38.016 40.126 1.00 80.87 C ANISOU 1966 CA VAL A1057 9724 13264 7738 889 -739 -1850 C ATOM 1967 C VAL A1057 40.335 37.697 38.616 1.00 83.25 C ANISOU 1967 C VAL A1057 10206 13279 8145 811 -685 -1666 C ATOM 1968 O VAL A1057 41.069 38.383 37.897 1.00 82.77 O ANISOU 1968 O VAL A1057 10238 12981 8232 777 -729 -1653 O ATOM 1969 CB VAL A1057 39.675 39.465 40.361 1.00 85.80 C ANISOU 1969 CB VAL A1057 10315 13833 8452 975 -895 -2117 C ATOM 1970 CG1 VAL A1057 38.362 39.710 39.617 1.00 85.40 C ANISOU 1970 CG1 VAL A1057 10330 13683 8434 1010 -929 -2160 C ATOM 1971 CG2 VAL A1057 39.509 39.760 41.850 1.00 86.92 C ANISOU 1971 CG2 VAL A1057 10272 14275 8479 1063 -952 -2315 C ATOM 1972 N ILE A1058 39.607 36.658 38.149 1.00 78.39 N ANISOU 1972 N ILE A1058 9633 12695 7456 788 -596 -1525 N ATOM 1973 CA ILE A1058 39.605 36.225 36.743 1.00 76.58 C ANISOU 1973 CA ILE A1058 9565 12227 7304 724 -541 -1358 C ATOM 1974 C ILE A1058 38.226 36.569 36.105 1.00 80.31 C ANISOU 1974 C ILE A1058 10090 12623 7800 766 -589 -1429 C ATOM 1975 O ILE A1058 37.430 37.293 36.709 1.00 80.74 O ANISOU 1975 O ILE A1058 10065 12778 7835 842 -674 -1614 O ATOM 1976 CB ILE A1058 39.961 34.709 36.585 1.00 78.30 C ANISOU 1976 CB ILE A1058 9805 12507 7441 657 -401 -1126 C ATOM 1977 CG1 ILE A1058 38.955 33.790 37.326 1.00 78.42 C ANISOU 1977 CG1 ILE A1058 9712 12776 7306 685 -353 -1102 C ATOM 1978 CG2 ILE A1058 41.410 34.439 37.019 1.00 78.77 C ANISOU 1978 CG2 ILE A1058 9835 12595 7500 608 -354 -1041 C ATOM 1979 CD1 ILE A1058 39.172 32.318 37.140 1.00 82.21 C ANISOU 1979 CD1 ILE A1058 10208 13298 7730 621 -230 -878 C ATOM 1980 N THR A1059 37.982 36.083 34.873 1.00 75.97 N ANISOU 1980 N THR A1059 9674 11896 7297 717 -537 -1286 N ATOM 1981 CA THR A1059 36.755 36.317 34.101 1.00 75.77 C ANISOU 1981 CA THR A1059 9716 11772 7300 742 -570 -1320 C ATOM 1982 C THR A1059 35.956 34.986 34.024 1.00 78.71 C ANISOU 1982 C THR A1059 10088 12261 7558 725 -476 -1187 C ATOM 1983 O THR A1059 36.462 33.950 34.465 1.00 77.71 O ANISOU 1983 O THR A1059 9920 12251 7354 688 -389 -1059 O ATOM 1984 CB THR A1059 37.151 36.875 32.696 1.00 86.30 C ANISOU 1984 CB THR A1059 11197 12805 8786 699 -593 -1258 C ATOM 1985 OG1 THR A1059 38.094 37.939 32.843 1.00 86.91 O ANISOU 1985 OG1 THR A1059 11261 12785 8977 703 -673 -1344 O ATOM 1986 CG2 THR A1059 35.959 37.350 31.864 1.00 86.34 C ANISOU 1986 CG2 THR A1059 11272 12690 8843 725 -641 -1306 C ATOM 1987 N LYS A1060 34.713 35.022 33.479 1.00 75.38 N ANISOU 1987 N LYS A1060 9706 11806 7131 752 -498 -1214 N ATOM 1988 CA LYS A1060 33.864 33.839 33.279 1.00 74.57 C ANISOU 1988 CA LYS A1060 9609 11783 6940 735 -425 -1090 C ATOM 1989 C LYS A1060 34.519 32.941 32.230 1.00 78.08 C ANISOU 1989 C LYS A1060 10176 12063 7428 657 -339 -896 C ATOM 1990 O LYS A1060 34.641 31.734 32.456 1.00 77.64 O ANISOU 1990 O LYS A1060 10091 12105 7303 623 -257 -759 O ATOM 1991 CB LYS A1060 32.425 34.255 32.869 1.00 76.77 C ANISOU 1991 CB LYS A1060 9911 12039 7221 782 -481 -1175 C ATOM 1992 CG LYS A1060 31.364 33.126 32.794 1.00 86.13 C ANISOU 1992 CG LYS A1060 11083 13328 8315 775 -425 -1066 C ATOM 1993 CD LYS A1060 31.470 32.188 31.576 1.00 92.31 C ANISOU 1993 CD LYS A1060 12000 13935 9139 706 -354 -888 C ATOM 1994 CE LYS A1060 30.410 31.114 31.586 1.00 97.84 C ANISOU 1994 CE LYS A1060 12675 14737 9762 702 -314 -792 C ATOM 1995 NZ LYS A1060 30.526 30.217 30.408 1.00102.59 N ANISOU 1995 NZ LYS A1060 13404 15164 10411 641 -255 -639 N ATOM 1996 N ASP A1061 34.964 33.537 31.094 1.00 74.18 N ANISOU 1996 N ASP A1061 9809 11326 7050 632 -362 -882 N ATOM 1997 CA ASP A1061 35.643 32.805 30.025 1.00 73.09 C ANISOU 1997 CA ASP A1061 9789 11030 6953 568 -288 -713 C ATOM 1998 C ASP A1061 36.993 32.284 30.507 1.00 76.44 C ANISOU 1998 C ASP A1061 10181 11502 7360 528 -225 -620 C ATOM 1999 O ASP A1061 37.264 31.099 30.339 1.00 75.66 O ANISOU 1999 O ASP A1061 10100 11427 7220 488 -139 -475 O ATOM 2000 CB ASP A1061 35.828 33.674 28.767 1.00 74.74 C ANISOU 2000 CB ASP A1061 10118 10996 7283 558 -333 -722 C ATOM 2001 CG ASP A1061 34.551 34.019 28.020 1.00 82.12 C ANISOU 2001 CG ASP A1061 11108 11853 8242 583 -378 -773 C ATOM 2002 OD1 ASP A1061 34.650 34.509 26.876 1.00 81.86 O ANISOU 2002 OD1 ASP A1061 11174 11630 8299 567 -400 -745 O ATOM 2003 OD2 ASP A1061 33.450 33.736 28.553 1.00 86.74 O ANISOU 2003 OD2 ASP A1061 11632 12573 8750 617 -386 -826 O ATOM 2004 N GLU A1062 37.801 33.135 31.175 1.00 73.17 N ANISOU 2004 N GLU A1062 9710 11111 6979 540 -272 -706 N ATOM 2005 CA GLU A1062 39.120 32.748 31.702 1.00 72.82 C ANISOU 2005 CA GLU A1062 9629 11120 6921 502 -218 -625 C ATOM 2006 C GLU A1062 39.004 31.532 32.653 1.00 77.12 C ANISOU 2006 C GLU A1062 10069 11889 7343 493 -141 -548 C ATOM 2007 O GLU A1062 39.902 30.693 32.658 1.00 76.48 O ANISOU 2007 O GLU A1062 9996 11813 7248 445 -61 -407 O ATOM 2008 CB GLU A1062 39.799 33.922 32.421 1.00 74.80 C ANISOU 2008 CB GLU A1062 9813 11387 7220 527 -298 -759 C ATOM 2009 CG GLU A1062 40.158 35.059 31.475 1.00 83.42 C ANISOU 2009 CG GLU A1062 10998 12244 8455 523 -373 -798 C ATOM 2010 CD GLU A1062 40.793 36.294 32.084 1.00 99.68 C ANISOU 2010 CD GLU A1062 12995 14286 10592 547 -471 -936 C ATOM 2011 OE1 GLU A1062 40.949 36.348 33.326 1.00 91.70 O ANISOU 2011 OE1 GLU A1062 11864 13463 9514 576 -487 -1029 O ATOM 2012 OE2 GLU A1062 41.140 37.215 31.309 1.00 91.90 O ANISOU 2012 OE2 GLU A1062 12075 13102 9740 539 -538 -950 O ATOM 2013 N ALA A1063 37.883 31.407 33.395 1.00 74.24 N ANISOU 2013 N ALA A1063 9606 11707 6896 540 -166 -627 N ATOM 2014 CA ALA A1063 37.624 30.265 34.281 1.00 74.08 C ANISOU 2014 CA ALA A1063 9470 11914 6764 534 -102 -543 C ATOM 2015 C ALA A1063 37.274 29.017 33.471 1.00 76.81 C ANISOU 2015 C ALA A1063 9888 12186 7109 490 -27 -373 C ATOM 2016 O ALA A1063 37.757 27.927 33.776 1.00 76.04 O ANISOU 2016 O ALA A1063 9750 12162 6978 449 49 -232 O ATOM 2017 CB ALA A1063 36.493 30.596 35.245 1.00 75.61 C ANISOU 2017 CB ALA A1063 9537 12321 6873 603 -159 -675 C ATOM 2018 N GLU A1064 36.434 29.196 32.436 1.00 72.83 N ANISOU 2018 N GLU A1064 9489 11534 6649 499 -55 -391 N ATOM 2019 CA GLU A1064 35.937 28.163 31.527 1.00 71.71 C ANISOU 2019 CA GLU A1064 9429 11300 6518 467 -5 -262 C ATOM 2020 C GLU A1064 37.077 27.611 30.659 1.00 73.84 C ANISOU 2020 C GLU A1064 9804 11403 6849 412 60 -131 C ATOM 2021 O GLU A1064 37.154 26.399 30.455 1.00 73.05 O ANISOU 2021 O GLU A1064 9711 11307 6737 378 126 4 O ATOM 2022 CB GLU A1064 34.822 28.768 30.652 1.00 73.08 C ANISOU 2022 CB GLU A1064 9688 11350 6728 497 -65 -343 C ATOM 2023 CG GLU A1064 34.142 27.808 29.693 1.00 84.15 C ANISOU 2023 CG GLU A1064 11175 12658 8142 472 -29 -235 C ATOM 2024 CD GLU A1064 33.018 28.421 28.877 1.00109.82 C ANISOU 2024 CD GLU A1064 14504 15800 11422 501 -88 -314 C ATOM 2025 OE1 GLU A1064 32.894 29.668 28.859 1.00108.50 O ANISOU 2025 OE1 GLU A1064 14347 15588 11289 535 -155 -445 O ATOM 2026 OE2 GLU A1064 32.268 27.647 28.239 1.00105.04 O ANISOU 2026 OE2 GLU A1064 13947 15150 10814 488 -69 -242 O ATOM 2027 N LYS A1065 37.956 28.500 30.155 1.00 69.49 N ANISOU 2027 N LYS A1065 9328 10709 6366 406 38 -171 N ATOM 2028 CA LYS A1065 39.096 28.134 29.315 1.00 68.39 C ANISOU 2028 CA LYS A1065 9286 10419 6281 362 94 -54 C ATOM 2029 C LYS A1065 40.172 27.449 30.153 1.00 71.61 C ANISOU 2029 C LYS A1065 9615 10940 6653 330 160 38 C ATOM 2030 O LYS A1065 40.906 26.619 29.622 1.00 71.31 O ANISOU 2030 O LYS A1065 9631 10831 6632 292 229 169 O ATOM 2031 CB LYS A1065 39.677 29.357 28.579 1.00 71.04 C ANISOU 2031 CB LYS A1065 9706 10585 6702 367 41 -113 C ATOM 2032 CG LYS A1065 38.918 29.789 27.295 1.00 85.56 C ANISOU 2032 CG LYS A1065 11660 12253 8596 380 3 -137 C ATOM 2033 CD LYS A1065 37.460 30.241 27.484 1.00 93.60 C ANISOU 2033 CD LYS A1065 12650 13320 9594 422 -61 -254 C ATOM 2034 CE LYS A1065 36.786 30.654 26.203 1.00101.66 C ANISOU 2034 CE LYS A1065 13781 14174 10670 430 -94 -264 C ATOM 2035 NZ LYS A1065 35.386 31.086 26.447 1.00109.53 N ANISOU 2035 NZ LYS A1065 14746 15225 11645 470 -154 -374 N ATOM 2036 N LEU A1066 40.244 27.758 31.459 1.00 67.61 N ANISOU 2036 N LEU A1066 8976 10619 6094 347 139 -31 N ATOM 2037 CA LEU A1066 41.179 27.105 32.380 1.00 66.91 C ANISOU 2037 CA LEU A1066 8791 10671 5962 317 200 55 C ATOM 2038 C LEU A1066 40.617 25.733 32.782 1.00 69.41 C ANISOU 2038 C LEU A1066 9032 11122 6221 301 258 166 C ATOM 2039 O LEU A1066 41.378 24.808 33.048 1.00 68.63 O ANISOU 2039 O LEU A1066 8893 11070 6111 261 330 297 O ATOM 2040 CB LEU A1066 41.428 28.002 33.615 1.00 67.69 C ANISOU 2040 CB LEU A1066 8768 10930 6021 347 148 -72 C ATOM 2041 CG LEU A1066 42.485 27.569 34.641 1.00 72.46 C ANISOU 2041 CG LEU A1066 9261 11692 6578 320 201 -5 C ATOM 2042 CD1 LEU A1066 43.891 27.567 34.034 1.00 72.21 C ANISOU 2042 CD1 LEU A1066 9317 11508 6612 272 245 90 C ATOM 2043 CD2 LEU A1066 42.476 28.502 35.830 1.00 75.35 C ANISOU 2043 CD2 LEU A1066 9502 12233 6896 363 135 -160 C ATOM 2044 N PHE A1067 39.274 25.612 32.795 1.00 65.50 N ANISOU 2044 N PHE A1067 8512 10681 5695 332 222 121 N ATOM 2045 CA PHE A1067 38.530 24.397 33.125 1.00 64.86 C ANISOU 2045 CA PHE A1067 8352 10721 5571 321 257 224 C ATOM 2046 C PHE A1067 38.745 23.305 32.075 1.00 66.87 C ANISOU 2046 C PHE A1067 8707 10814 5885 278 315 368 C ATOM 2047 O PHE A1067 39.053 22.173 32.444 1.00 66.65 O ANISOU 2047 O PHE A1067 8609 10863 5851 245 371 501 O ATOM 2048 CB PHE A1067 37.031 24.714 33.251 1.00 67.00 C ANISOU 2048 CB PHE A1067 8590 11063 5804 369 194 131 C ATOM 2049 CG PHE A1067 36.102 23.527 33.195 1.00 68.45 C ANISOU 2049 CG PHE A1067 8734 11302 5973 356 216 243 C ATOM 2050 CD1 PHE A1067 35.950 22.690 34.292 1.00 72.13 C ANISOU 2050 CD1 PHE A1067 9033 11995 6377 347 243 335 C ATOM 2051 CD2 PHE A1067 35.313 23.295 32.076 1.00 70.13 C ANISOU 2051 CD2 PHE A1067 9064 11348 6234 354 200 256 C ATOM 2052 CE1 PHE A1067 35.071 21.608 34.249 1.00 72.97 C ANISOU 2052 CE1 PHE A1067 9093 12147 6485 333 253 450 C ATOM 2053 CE2 PHE A1067 34.434 22.213 32.034 1.00 73.05 C ANISOU 2053 CE2 PHE A1067 9393 11761 6601 342 210 358 C ATOM 2054 CZ PHE A1067 34.310 21.381 33.126 1.00 71.58 C ANISOU 2054 CZ PHE A1067 9041 11791 6366 331 234 457 C ATOM 2055 N ASN A1068 38.568 23.634 30.778 1.00 61.85 N ANISOU 2055 N ASN A1068 8228 9964 5311 282 297 339 N ATOM 2056 CA ASN A1068 38.729 22.690 29.664 1.00 60.58 C ANISOU 2056 CA ASN A1068 8172 9641 5204 253 343 450 C ATOM 2057 C ASN A1068 40.101 22.010 29.704 1.00 64.11 C ANISOU 2057 C ASN A1068 8618 10067 5673 213 417 568 C ATOM 2058 O ASN A1068 40.213 20.850 29.312 1.00 63.55 O ANISOU 2058 O ASN A1068 8564 9950 5633 187 463 683 O ATOM 2059 CB ASN A1068 38.545 23.403 28.326 1.00 58.41 C ANISOU 2059 CB ASN A1068 8054 9160 4978 270 309 386 C ATOM 2060 CG ASN A1068 37.197 24.048 28.133 1.00 73.64 C ANISOU 2060 CG ASN A1068 9998 11087 6895 307 238 275 C ATOM 2061 OD1 ASN A1068 37.096 25.132 27.557 1.00 68.65 O ANISOU 2061 OD1 ASN A1068 9441 10351 6291 329 191 182 O ATOM 2062 ND2 ASN A1068 36.137 23.444 28.664 1.00 63.15 N ANISOU 2062 ND2 ASN A1068 8584 9882 5527 316 225 287 N ATOM 2063 N GLN A1069 41.134 22.735 30.196 1.00 60.28 N ANISOU 2063 N GLN A1069 8110 9615 5179 208 423 538 N ATOM 2064 CA GLN A1069 42.504 22.237 30.347 1.00 59.58 C ANISOU 2064 CA GLN A1069 8013 9521 5106 171 492 645 C ATOM 2065 C GLN A1069 42.534 21.075 31.331 1.00 62.69 C ANISOU 2065 C GLN A1069 8269 10082 5470 143 541 758 C ATOM 2066 O GLN A1069 43.181 20.061 31.065 1.00 61.90 O ANISOU 2066 O GLN A1069 8182 9932 5405 110 604 885 O ATOM 2067 CB GLN A1069 43.452 23.359 30.814 1.00 61.17 C ANISOU 2067 CB GLN A1069 8197 9746 5298 174 473 578 C ATOM 2068 CG GLN A1069 43.583 24.536 29.843 1.00 73.97 C ANISOU 2068 CG GLN A1069 9942 11195 6969 195 420 488 C ATOM 2069 CD GLN A1069 44.502 25.631 30.349 1.00 93.33 C ANISOU 2069 CD GLN A1069 12366 13666 9430 196 389 424 C ATOM 2070 OE1 GLN A1069 45.090 25.555 31.441 1.00 88.20 O ANISOU 2070 OE1 GLN A1069 11607 13162 8742 182 410 439 O ATOM 2071 NE2 GLN A1069 44.647 26.684 29.557 1.00 86.44 N ANISOU 2071 NE2 GLN A1069 11583 12646 8614 212 334 356 N ATOM 2072 N ASP A1070 41.797 21.207 32.449 1.00 59.54 N ANISOU 2072 N ASP A1070 7730 9884 5008 160 510 714 N ATOM 2073 CA ASP A1070 41.700 20.158 33.456 1.00 59.90 C ANISOU 2073 CA ASP A1070 7620 10117 5022 136 549 828 C ATOM 2074 C ASP A1070 40.788 19.035 32.954 1.00 63.16 C ANISOU 2074 C ASP A1070 8041 10482 5474 127 551 915 C ATOM 2075 O ASP A1070 40.881 17.920 33.457 1.00 63.42 O ANISOU 2075 O ASP A1070 7971 10606 5521 95 590 1050 O ATOM 2076 CB ASP A1070 41.201 20.709 34.801 1.00 62.86 C ANISOU 2076 CB ASP A1070 7832 10746 5307 164 512 752 C ATOM 2077 CG ASP A1070 42.125 21.723 35.448 1.00 77.21 C ANISOU 2077 CG ASP A1070 9614 12634 7087 172 505 670 C ATOM 2078 OD1 ASP A1070 42.532 22.684 34.756 1.00 77.98 O ANISOU 2078 OD1 ASP A1070 9832 12576 7220 187 473 569 O ATOM 2079 OD2 ASP A1070 42.364 21.612 36.674 1.00 85.12 O ANISOU 2079 OD2 ASP A1070 10458 13858 8024 167 524 699 O ATOM 2080 N VAL A1071 39.934 19.315 31.947 1.00 58.67 N ANISOU 2080 N VAL A1071 7593 9764 4934 152 507 844 N ATOM 2081 CA VAL A1071 39.081 18.294 31.326 1.00 57.88 C ANISOU 2081 CA VAL A1071 7519 9589 4883 144 502 917 C ATOM 2082 C VAL A1071 39.972 17.491 30.376 1.00 60.71 C ANISOU 2082 C VAL A1071 7981 9767 5320 115 556 1010 C ATOM 2083 O VAL A1071 40.015 16.268 30.474 1.00 60.23 O ANISOU 2083 O VAL A1071 7863 9715 5305 86 586 1135 O ATOM 2084 CB VAL A1071 37.825 18.890 30.625 1.00 61.33 C ANISOU 2084 CB VAL A1071 8039 9948 5316 182 435 808 C ATOM 2085 CG1 VAL A1071 37.000 17.805 29.941 1.00 60.80 C ANISOU 2085 CG1 VAL A1071 8002 9793 5305 170 427 885 C ATOM 2086 CG2 VAL A1071 36.963 19.654 31.617 1.00 61.66 C ANISOU 2086 CG2 VAL A1071 7968 10182 5277 217 383 715 C ATOM 2087 N ASP A1072 40.739 18.199 29.516 1.00 56.74 N ANISOU 2087 N ASP A1072 7615 9112 4832 124 565 952 N ATOM 2088 CA ASP A1072 41.709 17.638 28.575 1.00 56.12 C ANISOU 2088 CA ASP A1072 7639 8872 4811 108 616 1022 C ATOM 2089 C ASP A1072 42.684 16.708 29.303 1.00 58.67 C ANISOU 2089 C ASP A1072 7863 9277 5151 69 682 1156 C ATOM 2090 O ASP A1072 42.851 15.563 28.888 1.00 58.14 O ANISOU 2090 O ASP A1072 7806 9137 5145 52 713 1253 O ATOM 2091 CB ASP A1072 42.471 18.777 27.868 1.00 58.18 C ANISOU 2091 CB ASP A1072 8021 9018 5065 125 613 946 C ATOM 2092 CG ASP A1072 43.549 18.323 26.902 1.00 72.43 C ANISOU 2092 CG ASP A1072 9926 10680 6915 117 667 1017 C ATOM 2093 OD1 ASP A1072 44.729 18.665 27.131 1.00 73.13 O ANISOU 2093 OD1 ASP A1072 10013 10779 6994 103 702 1046 O ATOM 2094 OD2 ASP A1072 43.222 17.571 25.954 1.00 80.71 O ANISOU 2094 OD2 ASP A1072 11047 11614 8005 125 673 1048 O ATOM 2095 N ALA A1073 43.271 17.184 30.425 1.00 54.51 N ANISOU 2095 N ALA A1073 7232 8908 4572 56 698 1157 N ATOM 2096 CA ALA A1073 44.197 16.418 31.261 1.00 54.23 C ANISOU 2096 CA ALA A1073 7085 8977 4541 16 761 1283 C ATOM 2097 C ALA A1073 43.498 15.198 31.901 1.00 58.22 C ANISOU 2097 C ALA A1073 7452 9596 5073 -7 765 1396 C ATOM 2098 O ALA A1073 44.127 14.144 32.027 1.00 57.97 O ANISOU 2098 O ALA A1073 7370 9562 5095 -41 817 1529 O ATOM 2099 CB ALA A1073 44.783 17.309 32.342 1.00 55.17 C ANISOU 2099 CB ALA A1073 7116 9257 4590 13 763 1238 C ATOM 2100 N ALA A1074 42.201 15.336 32.287 1.00 54.56 N ANISOU 2100 N ALA A1074 6924 9229 4579 13 708 1350 N ATOM 2101 CA ALA A1074 41.416 14.236 32.864 1.00 54.48 C ANISOU 2101 CA ALA A1074 6774 9328 4597 -7 700 1465 C ATOM 2102 C ALA A1074 41.128 13.186 31.806 1.00 58.17 C ANISOU 2102 C ALA A1074 7327 9604 5172 -16 697 1529 C ATOM 2103 O ALA A1074 41.311 12.000 32.069 1.00 58.49 O ANISOU 2103 O ALA A1074 7279 9660 5284 -50 722 1670 O ATOM 2104 CB ALA A1074 40.114 14.755 33.464 1.00 55.46 C ANISOU 2104 CB ALA A1074 6814 9607 4653 24 637 1394 C ATOM 2105 N VAL A1075 40.722 13.631 30.593 1.00 53.70 N ANISOU 2105 N VAL A1075 6928 8856 4622 16 663 1423 N ATOM 2106 CA VAL A1075 40.430 12.783 29.439 1.00 53.19 C ANISOU 2106 CA VAL A1075 6964 8598 4650 18 651 1450 C ATOM 2107 C VAL A1075 41.707 12.044 29.032 1.00 57.84 C ANISOU 2107 C VAL A1075 7594 9078 5304 -2 713 1533 C ATOM 2108 O VAL A1075 41.655 10.826 28.869 1.00 57.75 O ANISOU 2108 O VAL A1075 7546 9011 5387 -21 717 1632 O ATOM 2109 CB VAL A1075 39.836 13.602 28.262 1.00 56.69 C ANISOU 2109 CB VAL A1075 7573 8893 5075 60 606 1310 C ATOM 2110 CG1 VAL A1075 39.816 12.801 26.962 1.00 56.49 C ANISOU 2110 CG1 VAL A1075 7664 8664 5135 69 601 1323 C ATOM 2111 CG2 VAL A1075 38.441 14.107 28.599 1.00 56.66 C ANISOU 2111 CG2 VAL A1075 7522 8983 5022 80 541 1241 C ATOM 2112 N ARG A1076 42.855 12.758 28.916 1.00 55.13 N ANISOU 2112 N ARG A1076 7317 8711 4919 2 759 1499 N ATOM 2113 CA ARG A1076 44.143 12.133 28.566 1.00 55.47 C ANISOU 2113 CA ARG A1076 7397 8666 5013 -14 823 1580 C ATOM 2114 C ARG A1076 44.552 11.101 29.627 1.00 61.62 C ANISOU 2114 C ARG A1076 8009 9566 5836 -60 861 1732 C ATOM 2115 O ARG A1076 45.067 10.048 29.265 1.00 61.68 O ANISOU 2115 O ARG A1076 8020 9480 5934 -73 889 1821 O ATOM 2116 CB ARG A1076 45.264 13.168 28.385 1.00 54.84 C ANISOU 2116 CB ARG A1076 7397 8565 4873 -4 860 1529 C ATOM 2117 CG ARG A1076 45.120 14.030 27.139 1.00 60.69 C ANISOU 2117 CG ARG A1076 8309 9157 5595 38 831 1411 C ATOM 2118 CD ARG A1076 46.226 15.057 27.054 1.00 64.34 C ANISOU 2118 CD ARG A1076 8828 9609 6010 42 860 1381 C ATOM 2119 NE ARG A1076 46.065 15.937 25.898 1.00 67.11 N ANISOU 2119 NE ARG A1076 9322 9832 6344 81 826 1282 N ATOM 2120 CZ ARG A1076 46.630 15.731 24.713 1.00 79.84 C ANISOU 2120 CZ ARG A1076 11052 11304 7979 105 848 1292 C ATOM 2121 NH1 ARG A1076 47.421 14.682 24.520 1.00 65.38 N ANISOU 2121 NH1 ARG A1076 9220 9431 6190 97 903 1387 N ATOM 2122 NH2 ARG A1076 46.423 16.581 23.718 1.00 66.81 N ANISOU 2122 NH2 ARG A1076 9514 9561 6310 139 815 1211 N ATOM 2123 N GLY A1077 44.243 11.380 30.898 1.00 59.28 N ANISOU 2123 N GLY A1077 7563 9480 5482 -80 856 1759 N ATOM 2124 CA GLY A1077 44.512 10.484 32.021 1.00 60.01 C ANISOU 2124 CA GLY A1077 7470 9726 5605 -125 888 1911 C ATOM 2125 C GLY A1077 43.727 9.181 31.997 1.00 65.86 C ANISOU 2125 C GLY A1077 8129 10440 6454 -143 858 2020 C ATOM 2126 O GLY A1077 44.038 8.251 32.748 1.00 66.18 O ANISOU 2126 O GLY A1077 8024 10567 6556 -184 885 2171 O ATOM 2127 N ILE A1078 42.698 9.113 31.139 1.00 63.35 N ANISOU 2127 N ILE A1078 7899 10002 6170 -115 796 1949 N ATOM 2128 CA ILE A1078 41.841 7.942 30.933 1.00 64.05 C ANISOU 2128 CA ILE A1078 7932 10031 6375 -127 750 2033 C ATOM 2129 C ILE A1078 42.344 7.175 29.684 1.00 68.77 C ANISOU 2129 C ILE A1078 8664 10384 7082 -115 759 2029 C ATOM 2130 O ILE A1078 42.354 5.943 29.679 1.00 68.74 O ANISOU 2130 O ILE A1078 8589 10323 7206 -139 752 2143 O ATOM 2131 CB ILE A1078 40.343 8.387 30.804 1.00 67.22 C ANISOU 2131 CB ILE A1078 8342 10460 6739 -101 673 1952 C ATOM 2132 CG1 ILE A1078 39.849 9.086 32.103 1.00 67.58 C ANISOU 2132 CG1 ILE A1078 8239 10768 6670 -104 663 1953 C ATOM 2133 CG2 ILE A1078 39.433 7.207 30.444 1.00 68.68 C ANISOU 2133 CG2 ILE A1078 8484 10557 7053 -113 615 2033 C ATOM 2134 CD1 ILE A1078 38.418 9.701 32.043 1.00 72.77 C ANISOU 2134 CD1 ILE A1078 8906 11473 7269 -71 591 1860 C ATOM 2135 N LEU A1079 42.806 7.915 28.656 1.00 65.74 N ANISOU 2135 N LEU A1079 8463 9866 6650 -76 773 1901 N ATOM 2136 CA LEU A1079 43.299 7.366 27.386 1.00 65.98 C ANISOU 2136 CA LEU A1079 8633 9683 6753 -49 782 1870 C ATOM 2137 C LEU A1079 44.773 6.879 27.491 1.00 71.20 C ANISOU 2137 C LEU A1079 9280 10323 7450 -66 859 1956 C ATOM 2138 O LEU A1079 45.339 6.437 26.486 1.00 70.38 O ANISOU 2138 O LEU A1079 9283 10059 7397 -38 874 1933 O ATOM 2139 CB LEU A1079 43.183 8.429 26.272 1.00 65.52 C ANISOU 2139 CB LEU A1079 8758 9523 6613 1 770 1712 C ATOM 2140 CG LEU A1079 41.775 8.982 25.977 1.00 70.06 C ANISOU 2140 CG LEU A1079 9373 10093 7151 24 697 1613 C ATOM 2141 CD1 LEU A1079 41.837 10.155 25.020 1.00 69.50 C ANISOU 2141 CD1 LEU A1079 9460 9952 6994 66 695 1475 C ATOM 2142 CD2 LEU A1079 40.830 7.897 25.455 1.00 73.22 C ANISOU 2142 CD2 LEU A1079 9778 10380 7660 31 637 1628 C ATOM 2143 N ARG A1080 45.374 6.943 28.701 1.00 69.39 N ANISOU 2143 N ARG A1080 8913 10261 7190 -109 905 2055 N ATOM 2144 CA ARG A1080 46.742 6.471 28.966 1.00 70.06 C ANISOU 2144 CA ARG A1080 8962 10350 7307 -133 979 2154 C ATOM 2145 C ARG A1080 46.750 5.392 30.082 1.00 77.00 C ANISOU 2145 C ARG A1080 9636 11349 8272 -188 989 2328 C ATOM 2146 O ARG A1080 47.826 5.030 30.572 1.00 76.92 O ANISOU 2146 O ARG A1080 9557 11391 8276 -219 1054 2428 O ATOM 2147 CB ARG A1080 47.693 7.632 29.348 1.00 69.53 C ANISOU 2147 CB ARG A1080 8929 10373 7116 -134 1035 2116 C ATOM 2148 CG ARG A1080 47.227 8.454 30.546 1.00 79.35 C ANISOU 2148 CG ARG A1080 10059 11829 8261 -154 1021 2102 C ATOM 2149 CD ARG A1080 48.271 9.394 31.112 1.00 87.00 C ANISOU 2149 CD ARG A1080 11024 12899 9134 -165 1073 2089 C ATOM 2150 NE ARG A1080 49.263 8.669 31.909 1.00 94.13 N ANISOU 2150 NE ARG A1080 11806 13888 10072 -210 1138 2238 N ATOM 2151 CZ ARG A1080 50.186 9.251 32.667 1.00106.51 C ANISOU 2151 CZ ARG A1080 13323 15577 11568 -233 1187 2263 C ATOM 2152 NH1 ARG A1080 50.245 10.575 32.756 1.00 91.27 N ANISOU 2152 NH1 ARG A1080 11451 13694 9534 -212 1171 2144 N ATOM 2153 NH2 ARG A1080 51.039 8.514 33.366 1.00 94.04 N ANISOU 2153 NH2 ARG A1080 11629 14076 10027 -276 1246 2408 N ATOM 2154 N ASN A1081 45.561 4.881 30.472 1.00 75.64 N ANISOU 2154 N ASN A1081 9359 11221 8159 -202 925 2373 N ATOM 2155 CA ASN A1081 45.443 3.855 31.512 1.00 76.91 C ANISOU 2155 CA ASN A1081 9309 11501 8413 -256 923 2553 C ATOM 2156 C ASN A1081 44.573 2.692 30.972 1.00 83.82 C ANISOU 2156 C ASN A1081 10159 12238 9450 -256 849 2599 C ATOM 2157 O ASN A1081 43.470 2.922 30.458 1.00 83.46 O ANISOU 2157 O ASN A1081 10173 12142 9395 -229 781 2512 O ATOM 2158 CB ASN A1081 44.869 4.467 32.807 1.00 76.38 C ANISOU 2158 CB ASN A1081 9086 11698 8238 -279 917 2589 C ATOM 2159 CG ASN A1081 44.916 3.589 34.046 1.00 95.55 C ANISOU 2159 CG ASN A1081 11273 14302 10730 -336 930 2790 C ATOM 2160 OD1 ASN A1081 44.750 2.362 34.006 1.00 87.97 O ANISOU 2160 OD1 ASN A1081 10227 13270 9928 -363 903 2918 O ATOM 2161 ND2 ASN A1081 45.043 4.226 35.199 1.00 87.71 N ANISOU 2161 ND2 ASN A1081 10155 13553 9616 -354 962 2823 N ATOM 2162 N ALA A1082 45.112 1.446 31.054 1.00 82.23 N ANISOU 2162 N ALA A1082 9874 11963 9406 -285 859 2734 N ATOM 2163 CA ALA A1082 44.496 0.205 30.552 1.00 83.11 C ANISOU 2163 CA ALA A1082 9953 11919 9707 -287 786 2789 C ATOM 2164 C ALA A1082 43.266 -0.228 31.394 1.00 88.64 C ANISOU 2164 C ALA A1082 10466 12751 10463 -325 715 2906 C ATOM 2165 O ALA A1082 42.518 -1.111 30.963 1.00 88.76 O ANISOU 2165 O ALA A1082 10454 12640 10630 -327 635 2941 O ATOM 2166 CB ALA A1082 45.526 -0.916 30.546 1.00 84.18 C ANISOU 2166 CB ALA A1082 10032 11959 9995 -310 819 2906 C ATOM 2167 N LYS A1083 43.066 0.377 32.580 1.00 85.71 N ANISOU 2167 N LYS A1083 9961 12635 9972 -353 739 2968 N ATOM 2168 CA LYS A1083 41.924 0.082 33.447 1.00 86.33 C ANISOU 2168 CA LYS A1083 9850 12877 10075 -383 678 3085 C ATOM 2169 C LYS A1083 40.836 1.159 33.294 1.00 89.85 C ANISOU 2169 C LYS A1083 10372 13390 10376 -344 636 2942 C ATOM 2170 O LYS A1083 39.745 1.008 33.847 1.00 89.96 O ANISOU 2170 O LYS A1083 10256 13525 10397 -356 576 3013 O ATOM 2171 CB LYS A1083 42.377 -0.022 34.914 1.00 89.45 C ANISOU 2171 CB LYS A1083 10018 13540 10430 -434 729 3258 C ATOM 2172 N LEU A1084 41.130 2.233 32.530 1.00 85.60 N ANISOU 2172 N LEU A1084 10040 12770 9713 -296 664 2748 N ATOM 2173 CA LEU A1084 40.205 3.347 32.323 1.00 85.07 C ANISOU 2173 CA LEU A1084 10060 12754 9511 -256 630 2599 C ATOM 2174 C LEU A1084 39.759 3.469 30.857 1.00 89.37 C ANISOU 2174 C LEU A1084 10819 13053 10086 -210 586 2444 C ATOM 2175 O LEU A1084 38.584 3.746 30.621 1.00 88.84 O ANISOU 2175 O LEU A1084 10777 12986 9992 -190 522 2382 O ATOM 2176 CB LEU A1084 40.845 4.678 32.763 1.00 84.47 C ANISOU 2176 CB LEU A1084 10025 12819 9252 -239 693 2501 C ATOM 2177 CG LEU A1084 41.235 4.841 34.238 1.00 89.50 C ANISOU 2177 CG LEU A1084 10459 13732 9814 -274 736 2616 C ATOM 2178 CD1 LEU A1084 41.930 6.172 34.465 1.00 89.02 C ANISOU 2178 CD1 LEU A1084 10471 13761 9591 -251 790 2490 C ATOM 2179 CD2 LEU A1084 40.021 4.726 35.163 1.00 92.73 C ANISOU 2179 CD2 LEU A1084 10685 14352 10197 -283 680 2696 C ATOM 2180 N LYS A1085 40.692 3.306 29.880 1.00 86.46 N ANISOU 2180 N LYS A1085 10598 12490 9761 -190 621 2381 N ATOM 2181 CA LYS A1085 40.401 3.442 28.441 1.00 86.32 C ANISOU 2181 CA LYS A1085 10782 12255 9762 -140 586 2232 C ATOM 2182 C LYS A1085 39.276 2.464 27.979 1.00 91.72 C ANISOU 2182 C LYS A1085 11439 12823 10589 -141 491 2262 C ATOM 2183 O LYS A1085 38.353 2.932 27.308 1.00 90.60 O ANISOU 2183 O LYS A1085 11400 12617 10406 -108 440 2148 O ATOM 2184 CB LYS A1085 41.660 3.212 27.574 1.00 88.44 C ANISOU 2184 CB LYS A1085 11179 12361 10065 -117 640 2189 C ATOM 2185 CG LYS A1085 41.442 3.594 26.099 1.00 99.76 C ANISOU 2185 CG LYS A1085 12822 13612 11472 -57 615 2020 C ATOM 2186 CD LYS A1085 42.464 3.010 25.118 1.00108.13 C ANISOU 2186 CD LYS A1085 13986 14494 12604 -25 644 1990 C ATOM 2187 CE LYS A1085 42.291 1.518 24.920 1.00119.61 C ANISOU 2187 CE LYS A1085 15374 15822 14250 -33 588 2064 C ATOM 2188 NZ LYS A1085 43.215 0.982 23.889 1.00129.72 N ANISOU 2188 NZ LYS A1085 16763 16929 15595 11 609 2010 N ATOM 2189 N PRO A1086 39.316 1.130 28.294 1.00 90.29 N ANISOU 2189 N PRO A1086 11121 12604 10581 -178 461 2415 N ATOM 2190 CA PRO A1086 38.234 0.239 27.827 1.00 91.22 C ANISOU 2190 CA PRO A1086 11214 12599 10845 -179 359 2439 C ATOM 2191 C PRO A1086 36.886 0.609 28.446 1.00 96.07 C ANISOU 2191 C PRO A1086 11733 13365 11404 -193 302 2473 C ATOM 2192 O PRO A1086 35.860 0.505 27.769 1.00 95.80 O ANISOU 2192 O PRO A1086 11763 13231 11407 -172 225 2408 O ATOM 2193 CB PRO A1086 38.690 -1.153 28.286 1.00 93.75 C ANISOU 2193 CB PRO A1086 11378 12880 11363 -223 345 2616 C ATOM 2194 CG PRO A1086 40.143 -1.016 28.566 1.00 97.66 C ANISOU 2194 CG PRO A1086 11875 13415 11815 -231 446 2644 C ATOM 2195 CD PRO A1086 40.313 0.370 29.074 1.00 92.25 C ANISOU 2195 CD PRO A1086 11226 12913 10912 -222 511 2575 C ATOM 2196 N VAL A1087 36.901 1.069 29.724 1.00 92.78 N ANISOU 2196 N VAL A1087 11162 13198 10890 -223 339 2568 N ATOM 2197 CA VAL A1087 35.718 1.535 30.451 1.00 92.77 C ANISOU 2197 CA VAL A1087 11054 13387 10807 -229 296 2601 C ATOM 2198 C VAL A1087 35.137 2.742 29.689 1.00 97.31 C ANISOU 2198 C VAL A1087 11814 13920 11240 -177 285 2398 C ATOM 2199 O VAL A1087 33.963 2.715 29.335 1.00 97.17 O ANISOU 2199 O VAL A1087 11813 13865 11240 -165 211 2370 O ATOM 2200 CB VAL A1087 36.044 1.868 31.939 1.00 96.42 C ANISOU 2200 CB VAL A1087 11325 14140 11170 -260 350 2719 C ATOM 2201 CG1 VAL A1087 34.837 2.467 32.658 1.00 96.28 C ANISOU 2201 CG1 VAL A1087 11207 14336 11039 -251 309 2726 C ATOM 2202 CG2 VAL A1087 36.552 0.638 32.684 1.00 96.96 C ANISOU 2202 CG2 VAL A1087 11194 14257 11389 -317 355 2939 C ATOM 2203 N TYR A1088 35.992 3.743 29.355 1.00 93.90 N ANISOU 2203 N TYR A1088 11522 13472 10682 -147 355 2263 N ATOM 2204 CA TYR A1088 35.628 4.963 28.619 1.00 93.22 C ANISOU 2204 CA TYR A1088 11612 13341 10468 -99 353 2074 C ATOM 2205 C TYR A1088 35.090 4.635 27.216 1.00 96.37 C ANISOU 2205 C TYR A1088 12167 13503 10944 -69 296 1979 C ATOM 2206 O TYR A1088 34.113 5.245 26.788 1.00 95.90 O ANISOU 2206 O TYR A1088 12176 13433 10829 -44 249 1888 O ATOM 2207 CB TYR A1088 36.849 5.899 28.501 1.00 94.18 C ANISOU 2207 CB TYR A1088 11837 13468 10481 -80 436 1981 C ATOM 2208 CG TYR A1088 36.561 7.244 27.859 1.00 95.92 C ANISOU 2208 CG TYR A1088 12215 13658 10573 -35 434 1802 C ATOM 2209 CD1 TYR A1088 36.149 8.331 28.626 1.00 97.93 C ANISOU 2209 CD1 TYR A1088 12420 14093 10695 -25 436 1752 C ATOM 2210 CD2 TYR A1088 36.756 7.445 26.494 1.00 96.29 C ANISOU 2210 CD2 TYR A1088 12453 13501 10630 1 431 1684 C ATOM 2211 CE1 TYR A1088 35.892 9.572 28.043 1.00 98.24 C ANISOU 2211 CE1 TYR A1088 12597 14095 10634 15 428 1591 C ATOM 2212 CE2 TYR A1088 36.497 8.680 25.899 1.00 96.57 C ANISOU 2212 CE2 TYR A1088 12623 13512 10559 39 427 1535 C ATOM 2213 CZ TYR A1088 36.067 9.742 26.679 1.00103.56 C ANISOU 2213 CZ TYR A1088 13455 14562 11329 44 424 1491 C ATOM 2214 OH TYR A1088 35.816 10.964 26.102 1.00103.84 O ANISOU 2214 OH TYR A1088 13615 14563 11277 80 414 1349 O ATOM 2215 N ASP A1089 35.728 3.689 26.503 1.00 92.51 N ANISOU 2215 N ASP A1089 11734 12833 10581 -68 299 1994 N ATOM 2216 CA ASP A1089 35.316 3.303 25.154 1.00 92.30 C ANISOU 2216 CA ASP A1089 11853 12588 10630 -33 244 1895 C ATOM 2217 C ASP A1089 33.979 2.537 25.169 1.00 94.88 C ANISOU 2217 C ASP A1089 12098 12880 11070 -50 143 1960 C ATOM 2218 O ASP A1089 33.268 2.538 24.163 1.00 94.20 O ANISOU 2218 O ASP A1089 12128 12655 11009 -20 86 1860 O ATOM 2219 CB ASP A1089 36.404 2.445 24.485 1.00 94.99 C ANISOU 2219 CB ASP A1089 12253 12762 11076 -21 272 1895 C ATOM 2220 CG ASP A1089 37.732 3.156 24.249 1.00108.62 C ANISOU 2220 CG ASP A1089 14082 14492 12695 2 366 1826 C ATOM 2221 OD1 ASP A1089 37.878 4.322 24.698 1.00108.80 O ANISOU 2221 OD1 ASP A1089 14120 14649 12571 3 409 1785 O ATOM 2222 OD2 ASP A1089 38.631 2.543 23.632 1.00116.57 O ANISOU 2222 OD2 ASP A1089 15149 15371 13771 21 391 1814 O ATOM 2223 N SER A1090 33.630 1.909 26.306 1.00 91.01 N ANISOU 2223 N SER A1090 11405 12528 10648 -98 119 2131 N ATOM 2224 CA SER A1090 32.383 1.159 26.451 1.00 91.10 C ANISOU 2224 CA SER A1090 11314 12527 10774 -120 19 2223 C ATOM 2225 C SER A1090 31.238 2.056 26.970 1.00 93.28 C ANISOU 2225 C SER A1090 11548 12975 10918 -116 -6 2208 C ATOM 2226 O SER A1090 30.073 1.756 26.700 1.00 93.71 O ANISOU 2226 O SER A1090 11587 12988 11030 -117 -91 2223 O ATOM 2227 CB SER A1090 32.575 -0.029 27.389 1.00 95.86 C ANISOU 2227 CB SER A1090 11702 13186 11535 -175 -1 2437 C ATOM 2228 OG SER A1090 32.988 0.351 28.692 1.00104.49 O ANISOU 2228 OG SER A1090 12641 14523 12536 -204 62 2547 O ATOM 2229 N LEU A1091 31.567 3.145 27.704 1.00 87.39 N ANISOU 2229 N LEU A1091 10781 12421 10000 -108 62 2175 N ATOM 2230 CA LEU A1091 30.581 4.086 28.262 1.00 86.11 C ANISOU 2230 CA LEU A1091 10576 12440 9701 -95 43 2146 C ATOM 2231 C LEU A1091 29.941 4.965 27.184 1.00 86.63 C ANISOU 2231 C LEU A1091 10836 12390 9689 -49 18 1961 C ATOM 2232 O LEU A1091 30.549 5.214 26.137 1.00 85.39 O ANISOU 2232 O LEU A1091 10855 12062 9530 -22 44 1837 O ATOM 2233 CB LEU A1091 31.234 5.013 29.321 1.00 85.98 C ANISOU 2233 CB LEU A1091 10486 12652 9530 -93 120 2142 C ATOM 2234 CG LEU A1091 31.829 4.400 30.594 1.00 91.42 C ANISOU 2234 CG LEU A1091 10961 13522 10250 -136 155 2323 C ATOM 2235 CD1 LEU A1091 32.680 5.409 31.342 1.00 91.04 C ANISOU 2235 CD1 LEU A1091 10897 13647 10047 -124 237 2269 C ATOM 2236 CD2 LEU A1091 30.762 3.798 31.493 1.00 95.44 C ANISOU 2236 CD2 LEU A1091 11257 14202 10803 -163 92 2492 C ATOM 2237 N ASP A1092 28.723 5.466 27.466 1.00 81.26 N ANISOU 2237 N ASP A1092 10117 11819 8938 -38 -30 1949 N ATOM 2238 CA ASP A1092 28.025 6.425 26.605 1.00 79.47 C ANISOU 2238 CA ASP A1092 10053 11519 8623 4 -52 1784 C ATOM 2239 C ASP A1092 28.471 7.840 26.994 1.00 80.15 C ANISOU 2239 C ASP A1092 10182 11733 8538 33 12 1671 C ATOM 2240 O ASP A1092 29.063 8.003 28.061 1.00 79.97 O ANISOU 2240 O ASP A1092 10038 11884 8463 20 58 1733 O ATOM 2241 CB ASP A1092 26.492 6.257 26.697 1.00 81.58 C ANISOU 2241 CB ASP A1092 10258 11832 8905 2 -137 1828 C ATOM 2242 CG ASP A1092 25.908 6.393 28.093 1.00 90.35 C ANISOU 2242 CG ASP A1092 11164 13215 9949 -10 -147 1945 C ATOM 2243 OD1 ASP A1092 26.460 5.777 29.031 1.00 91.07 O ANISOU 2243 OD1 ASP A1092 11091 13428 10082 -42 -124 2090 O ATOM 2244 OD2 ASP A1092 24.820 6.994 28.223 1.00 95.38 O ANISOU 2244 OD2 ASP A1092 11794 13943 10504 13 -186 1907 O ATOM 2245 N ALA A1093 28.182 8.854 26.150 1.00 73.87 N ANISOU 2245 N ALA A1093 9550 10856 7662 71 9 1509 N ATOM 2246 CA ALA A1093 28.572 10.266 26.334 1.00 72.11 C ANISOU 2246 CA ALA A1093 9387 10713 7298 102 55 1383 C ATOM 2247 C ALA A1093 28.280 10.808 27.774 1.00 73.28 C ANISOU 2247 C ALA A1093 9367 11132 7346 104 61 1424 C ATOM 2248 O ALA A1093 29.093 11.573 28.304 1.00 72.08 O ANISOU 2248 O ALA A1093 9203 11074 7110 115 112 1372 O ATOM 2249 CB ALA A1093 27.842 11.136 25.323 1.00 72.44 C ANISOU 2249 CB ALA A1093 9586 10647 7290 138 24 1237 C ATOM 2250 N VAL A1094 27.139 10.412 28.385 1.00 68.48 N ANISOU 2250 N VAL A1094 8626 10650 6744 97 6 1514 N ATOM 2251 CA VAL A1094 26.716 10.852 29.725 1.00 67.72 C ANISOU 2251 CA VAL A1094 8354 10830 6545 108 4 1557 C ATOM 2252 C VAL A1094 27.605 10.179 30.806 1.00 70.24 C ANISOU 2252 C VAL A1094 8503 11299 6886 74 49 1700 C ATOM 2253 O VAL A1094 28.022 10.846 31.757 1.00 69.41 O ANISOU 2253 O VAL A1094 8308 11392 6674 90 85 1678 O ATOM 2254 CB VAL A1094 25.210 10.551 29.967 1.00 71.91 C ANISOU 2254 CB VAL A1094 8790 11452 7080 113 -71 1628 C ATOM 2255 CG1 VAL A1094 24.748 11.095 31.316 1.00 72.01 C ANISOU 2255 CG1 VAL A1094 8628 11769 6965 139 -74 1651 C ATOM 2256 CG2 VAL A1094 24.348 11.127 28.846 1.00 71.38 C ANISOU 2256 CG2 VAL A1094 8893 11221 7006 140 -115 1500 C ATOM 2257 N ARG A1095 27.884 8.866 30.655 1.00 66.27 N ANISOU 2257 N ARG A1095 7954 10701 6526 30 43 1843 N ATOM 2258 CA ARG A1095 28.719 8.129 31.601 1.00 65.99 C ANISOU 2258 CA ARG A1095 7754 10788 6531 -8 83 1996 C ATOM 2259 C ARG A1095 30.199 8.349 31.291 1.00 68.41 C ANISOU 2259 C ARG A1095 8165 10991 6838 -13 159 1932 C ATOM 2260 O ARG A1095 31.011 8.261 32.215 1.00 67.83 O ANISOU 2260 O ARG A1095 7971 11065 6737 -32 210 2008 O ATOM 2261 CB ARG A1095 28.395 6.638 31.625 1.00 66.83 C ANISOU 2261 CB ARG A1095 7749 10839 6805 -54 37 2186 C ATOM 2262 CG ARG A1095 27.068 6.322 32.304 1.00 75.70 C ANISOU 2262 CG ARG A1095 8703 12136 7925 -58 -33 2305 C ATOM 2263 CD ARG A1095 26.853 4.832 32.370 1.00 82.85 C ANISOU 2263 CD ARG A1095 9482 12981 9016 -109 -84 2509 C ATOM 2264 NE ARG A1095 25.605 4.471 33.040 1.00 90.50 N ANISOU 2264 NE ARG A1095 10271 14124 9991 -117 -154 2651 N ATOM 2265 CZ ARG A1095 24.446 4.278 32.419 1.00102.88 C ANISOU 2265 CZ ARG A1095 11885 15594 11610 -110 -234 2646 C ATOM 2266 NH1 ARG A1095 24.353 4.439 31.104 1.00 86.19 N ANISOU 2266 NH1 ARG A1095 9994 13215 9540 -94 -253 2496 N ATOM 2267 NH2 ARG A1095 23.364 3.945 33.111 1.00 90.69 N ANISOU 2267 NH2 ARG A1095 10161 14229 10067 -118 -296 2794 N ATOM 2268 N ARG A1096 30.557 8.670 30.019 1.00 64.51 N ANISOU 2268 N ARG A1096 7885 10260 6366 6 168 1797 N ATOM 2269 CA ARG A1096 31.938 9.043 29.686 1.00 64.18 C ANISOU 2269 CA ARG A1096 7949 10132 6306 8 240 1729 C ATOM 2270 C ARG A1096 32.305 10.301 30.457 1.00 69.75 C ANISOU 2270 C ARG A1096 8626 11013 6862 32 277 1642 C ATOM 2271 O ARG A1096 33.362 10.344 31.086 1.00 70.29 O ANISOU 2271 O ARG A1096 8633 11168 6906 16 335 1682 O ATOM 2272 CB ARG A1096 32.182 9.241 28.178 1.00 62.72 C ANISOU 2272 CB ARG A1096 7986 9687 6157 31 239 1605 C ATOM 2273 CG ARG A1096 32.262 7.974 27.354 1.00 71.21 C ANISOU 2273 CG ARG A1096 9102 10569 7385 13 215 1670 C ATOM 2274 CD ARG A1096 32.790 8.290 25.966 1.00 81.13 C ANISOU 2274 CD ARG A1096 10568 11611 8648 44 232 1540 C ATOM 2275 NE ARG A1096 32.985 7.084 25.160 1.00 92.55 N ANISOU 2275 NE ARG A1096 12054 12873 10236 36 210 1583 N ATOM 2276 CZ ARG A1096 33.606 7.061 23.983 1.00106.84 C ANISOU 2276 CZ ARG A1096 14021 14505 12070 64 228 1496 C ATOM 2277 NH1 ARG A1096 34.139 8.169 23.484 1.00 94.22 N ANISOU 2277 NH1 ARG A1096 12548 12888 10365 95 273 1379 N ATOM 2278 NH2 ARG A1096 33.738 5.921 23.319 1.00 93.35 N ANISOU 2278 NH2 ARG A1096 12333 12642 10493 64 200 1527 N ATOM 2279 N ALA A1097 31.377 11.291 30.479 1.00 65.95 N ANISOU 2279 N ALA A1097 8175 10598 6286 70 239 1530 N ATOM 2280 CA ALA A1097 31.510 12.550 31.216 1.00 65.37 C ANISOU 2280 CA ALA A1097 8067 10694 6076 102 254 1427 C ATOM 2281 C ALA A1097 31.406 12.324 32.733 1.00 68.47 C ANISOU 2281 C ALA A1097 8230 11376 6412 93 261 1535 C ATOM 2282 O ALA A1097 31.950 13.121 33.497 1.00 67.83 O ANISOU 2282 O ALA A1097 8094 11444 6232 111 290 1474 O ATOM 2283 CB ALA A1097 30.443 13.528 30.765 1.00 66.04 C ANISOU 2283 CB ALA A1097 8235 10759 6097 147 201 1288 C ATOM 2284 N ALA A1098 30.712 11.243 33.164 1.00 65.05 N ANISOU 2284 N ALA A1098 7652 11024 6040 66 231 1697 N ATOM 2285 CA ALA A1098 30.564 10.884 34.577 1.00 65.39 C ANISOU 2285 CA ALA A1098 7453 11355 6035 55 235 1831 C ATOM 2286 C ALA A1098 31.881 10.340 35.138 1.00 68.60 C ANISOU 2286 C ALA A1098 7780 11810 6475 15 302 1934 C ATOM 2287 O ALA A1098 32.211 10.613 36.296 1.00 67.98 O ANISOU 2287 O ALA A1098 7550 11976 6303 20 331 1963 O ATOM 2288 CB ALA A1098 29.453 9.863 34.752 1.00 66.74 C ANISOU 2288 CB ALA A1098 7498 11578 6283 34 176 1991 C ATOM 2289 N LEU A1099 32.638 9.587 34.311 1.00 65.14 N ANISOU 2289 N LEU A1099 7441 11143 6165 -22 328 1984 N ATOM 2290 CA LEU A1099 33.950 9.048 34.681 1.00 65.23 C ANISOU 2290 CA LEU A1099 7399 11163 6221 -60 394 2078 C ATOM 2291 C LEU A1099 34.964 10.188 34.793 1.00 68.38 C ANISOU 2291 C LEU A1099 7883 11585 6512 -38 449 1938 C ATOM 2292 O LEU A1099 35.731 10.225 35.756 1.00 68.30 O ANISOU 2292 O LEU A1099 7749 11749 6451 -53 496 1995 O ATOM 2293 CB LEU A1099 34.422 7.986 33.659 1.00 65.22 C ANISOU 2293 CB LEU A1099 7499 10896 6386 -93 399 2143 C ATOM 2294 CG LEU A1099 35.807 7.327 33.895 1.00 69.88 C ANISOU 2294 CG LEU A1099 8047 11461 7043 -134 468 2247 C ATOM 2295 CD1 LEU A1099 35.871 6.606 35.240 1.00 70.63 C ANISOU 2295 CD1 LEU A1099 7885 11799 7154 -174 479 2444 C ATOM 2296 CD2 LEU A1099 36.143 6.356 32.777 1.00 72.39 C ANISOU 2296 CD2 LEU A1099 8478 11505 7522 -151 461 2278 C ATOM 2297 N ILE A1100 34.921 11.142 33.829 1.00 63.97 N ANISOU 2297 N ILE A1100 7526 10859 5921 -1 438 1760 N ATOM 2298 CA ILE A1100 35.770 12.341 33.769 1.00 63.23 C ANISOU 2298 CA ILE A1100 7533 10752 5741 24 473 1614 C ATOM 2299 C ILE A1100 35.591 13.169 35.066 1.00 68.89 C ANISOU 2299 C ILE A1100 8102 11751 6323 50 468 1568 C ATOM 2300 O ILE A1100 36.540 13.826 35.495 1.00 68.97 O ANISOU 2300 O ILE A1100 8108 11823 6275 53 507 1515 O ATOM 2301 CB ILE A1100 35.436 13.183 32.500 1.00 65.41 C ANISOU 2301 CB ILE A1100 8024 10815 6015 60 441 1449 C ATOM 2302 CG1 ILE A1100 35.667 12.357 31.212 1.00 65.32 C ANISOU 2302 CG1 ILE A1100 8152 10542 6124 43 447 1485 C ATOM 2303 CG2 ILE A1100 36.263 14.476 32.459 1.00 65.84 C ANISOU 2303 CG2 ILE A1100 8168 10856 5993 86 465 1307 C ATOM 2304 CD1 ILE A1100 35.130 12.991 29.894 1.00 72.13 C ANISOU 2304 CD1 ILE A1100 9210 11205 6992 77 409 1346 C ATOM 2305 N ASN A1101 34.396 13.095 35.707 1.00 66.12 N ANISOU 2305 N ASN A1101 7621 11578 5924 70 418 1593 N ATOM 2306 CA ASN A1101 34.101 13.819 36.948 1.00 66.34 C ANISOU 2306 CA ASN A1101 7492 11898 5816 106 406 1546 C ATOM 2307 C ASN A1101 34.837 13.164 38.119 1.00 70.33 C ANISOU 2307 C ASN A1101 7797 12622 6303 72 454 1698 C ATOM 2308 O ASN A1101 35.354 13.883 38.974 1.00 70.56 O ANISOU 2308 O ASN A1101 7748 12834 6228 93 474 1633 O ATOM 2309 CB ASN A1101 32.589 13.873 37.207 1.00 67.33 C ANISOU 2309 CB ASN A1101 7535 12151 5896 141 339 1543 C ATOM 2310 CG ASN A1101 32.154 14.849 38.287 1.00 88.90 C ANISOU 2310 CG ASN A1101 10132 15171 8475 198 316 1449 C ATOM 2311 OD1 ASN A1101 32.602 14.816 39.442 1.00 82.17 O ANISOU 2311 OD1 ASN A1101 9101 14568 7550 198 343 1509 O ATOM 2312 ND2 ASN A1101 31.206 15.706 37.941 1.00 79.93 N ANISOU 2312 ND2 ASN A1101 9065 14020 7285 252 261 1303 N ATOM 2313 N MET A1102 34.910 11.815 38.150 1.00 66.38 N ANISOU 2313 N MET A1102 7210 12101 5910 19 470 1899 N ATOM 2314 CA MET A1102 35.632 11.098 39.206 1.00 66.49 C ANISOU 2314 CA MET A1102 7027 12311 5925 -22 518 2068 C ATOM 2315 C MET A1102 37.129 11.368 39.112 1.00 68.62 C ANISOU 2315 C MET A1102 7377 12498 6200 -44 587 2033 C ATOM 2316 O MET A1102 37.776 11.568 40.138 1.00 68.38 O ANISOU 2316 O MET A1102 7209 12681 6091 -49 624 2065 O ATOM 2317 CB MET A1102 35.373 9.587 39.148 1.00 69.41 C ANISOU 2317 CB MET A1102 7296 12638 6438 -77 510 2292 C ATOM 2318 CG MET A1102 33.948 9.186 39.467 1.00 74.01 C ANISOU 2318 CG MET A1102 7752 13349 7021 -64 442 2374 C ATOM 2319 SD MET A1102 33.706 7.384 39.553 1.00 79.00 S ANISOU 2319 SD MET A1102 8228 13950 7841 -134 423 2662 S ATOM 2320 CE MET A1102 34.779 6.959 40.955 1.00 76.17 C ANISOU 2320 CE MET A1102 7627 13872 7444 -173 493 2832 C ATOM 2321 N VAL A1103 37.668 11.393 37.873 1.00 63.94 N ANISOU 2321 N VAL A1103 7000 11603 5692 -53 602 1968 N ATOM 2322 CA VAL A1103 39.082 11.635 37.557 1.00 63.40 C ANISOU 2322 CA VAL A1103 7036 11412 5640 -72 664 1937 C ATOM 2323 C VAL A1103 39.435 13.111 37.878 1.00 69.53 C ANISOU 2323 C VAL A1103 7859 12271 6289 -29 663 1754 C ATOM 2324 O VAL A1103 40.579 13.400 38.247 1.00 69.21 O ANISOU 2324 O VAL A1103 7806 12271 6219 -45 712 1752 O ATOM 2325 CB VAL A1103 39.384 11.275 36.070 1.00 66.20 C ANISOU 2325 CB VAL A1103 7604 11435 6112 -82 669 1912 C ATOM 2326 CG1 VAL A1103 40.826 11.598 35.684 1.00 65.51 C ANISOU 2326 CG1 VAL A1103 7630 11227 6032 -94 731 1877 C ATOM 2327 CG2 VAL A1103 39.079 9.807 35.785 1.00 66.11 C ANISOU 2327 CG2 VAL A1103 7539 11337 6240 -121 661 2081 C ATOM 2328 N PHE A1104 38.437 14.023 37.795 1.00 68.02 N ANISOU 2328 N PHE A1104 7705 12112 6026 24 602 1606 N ATOM 2329 CA PHE A1104 38.600 15.459 38.071 1.00 68.71 C ANISOU 2329 CA PHE A1104 7832 12268 6009 72 581 1418 C ATOM 2330 C PHE A1104 38.764 15.710 39.608 1.00 74.89 C ANISOU 2330 C PHE A1104 8395 13385 6674 85 590 1433 C ATOM 2331 O PHE A1104 39.135 16.818 40.012 1.00 74.47 O ANISOU 2331 O PHE A1104 8347 13410 6539 121 577 1286 O ATOM 2332 CB PHE A1104 37.388 16.235 37.512 1.00 70.46 C ANISOU 2332 CB PHE A1104 8146 12424 6203 125 509 1269 C ATOM 2333 CG PHE A1104 37.586 17.708 37.231 1.00 71.87 C ANISOU 2333 CG PHE A1104 8441 12537 6331 170 479 1061 C ATOM 2334 CD1 PHE A1104 38.002 18.142 35.981 1.00 74.24 C ANISOU 2334 CD1 PHE A1104 8949 12559 6699 167 479 987 C ATOM 2335 CD2 PHE A1104 37.278 18.664 38.191 1.00 74.84 C ANISOU 2335 CD2 PHE A1104 8711 13129 6596 220 442 938 C ATOM 2336 CE1 PHE A1104 38.123 19.506 35.701 1.00 75.07 C ANISOU 2336 CE1 PHE A1104 9151 12598 6775 206 441 808 C ATOM 2337 CE2 PHE A1104 37.417 20.029 37.914 1.00 77.40 C ANISOU 2337 CE2 PHE A1104 9137 13375 6894 263 401 743 C ATOM 2338 CZ PHE A1104 37.846 20.440 36.674 1.00 74.66 C ANISOU 2338 CZ PHE A1104 8993 12744 6629 252 400 687 C ATOM 2339 N GLN A1105 38.516 14.671 40.448 1.00 73.08 N ANISOU 2339 N GLN A1105 7968 13354 6446 55 610 1616 N ATOM 2340 CA GLN A1105 38.672 14.760 41.900 1.00 74.24 C ANISOU 2340 CA GLN A1105 7889 13839 6479 66 623 1655 C ATOM 2341 C GLN A1105 39.891 13.923 42.351 1.00 78.60 C ANISOU 2341 C GLN A1105 8354 14434 7077 2 700 1826 C ATOM 2342 O GLN A1105 40.859 14.507 42.843 1.00 78.37 O ANISOU 2342 O GLN A1105 8311 14477 6989 2 731 1767 O ATOM 2343 CB GLN A1105 37.390 14.316 42.640 1.00 76.60 C ANISOU 2343 CB GLN A1105 7993 14389 6722 90 582 1737 C ATOM 2344 CG GLN A1105 37.462 14.527 44.168 1.00 95.03 C ANISOU 2344 CG GLN A1105 10082 17111 8914 116 590 1757 C ATOM 2345 CD GLN A1105 36.223 14.109 44.939 1.00113.58 C ANISOU 2345 CD GLN A1105 12223 19741 11192 147 549 1846 C ATOM 2346 OE1 GLN A1105 35.218 13.648 44.380 1.00109.20 O ANISOU 2346 OE1 GLN A1105 11698 19097 10695 148 508 1896 O ATOM 2347 NE2 GLN A1105 36.262 14.291 46.251 1.00104.44 N ANISOU 2347 NE2 GLN A1105 10843 18940 9900 176 555 1863 N ATOM 2348 N MET A1106 39.849 12.572 42.183 1.00 75.38 N ANISOU 2348 N MET A1106 7885 13976 6780 -54 724 2036 N ATOM 2349 CA MET A1106 40.950 11.692 42.601 1.00 75.43 C ANISOU 2349 CA MET A1106 7797 14019 6844 -117 795 2213 C ATOM 2350 C MET A1106 42.125 11.746 41.616 1.00 78.55 C ANISOU 2350 C MET A1106 8399 14123 7325 -145 841 2177 C ATOM 2351 O MET A1106 43.201 12.218 41.980 1.00 78.08 O ANISOU 2351 O MET A1106 8339 14108 7218 -155 886 2146 O ATOM 2352 CB MET A1106 40.508 10.222 42.773 1.00 78.28 C ANISOU 2352 CB MET A1106 8012 14417 7314 -166 797 2454 C ATOM 2353 CG MET A1106 39.611 9.967 43.968 1.00 82.99 C ANISOU 2353 CG MET A1106 8348 15358 7828 -152 768 2558 C ATOM 2354 SD MET A1106 37.909 10.508 43.758 1.00 87.57 S ANISOU 2354 SD MET A1106 8942 15986 8345 -85 676 2444 S ATOM 2355 CE MET A1106 37.319 9.289 42.593 1.00 83.96 C ANISOU 2355 CE MET A1106 8582 15227 8091 -130 645 2576 C ATOM 2356 N GLY A1107 41.920 11.227 40.407 1.00 74.89 N ANISOU 2356 N GLY A1107 8095 13377 6983 -157 829 2189 N ATOM 2357 CA GLY A1107 42.948 11.161 39.375 1.00 74.25 C ANISOU 2357 CA GLY A1107 8204 13020 6986 -178 871 2167 C ATOM 2358 C GLY A1107 43.026 9.796 38.724 1.00 78.46 C ANISOU 2358 C GLY A1107 8758 13377 7676 -220 886 2323 C ATOM 2359 O GLY A1107 42.151 8.958 38.954 1.00 78.69 O ANISOU 2359 O GLY A1107 8669 13467 7762 -233 852 2437 O ATOM 2360 N GLU A1108 44.083 9.553 37.917 1.00 74.67 N ANISOU 2360 N GLU A1108 8419 12680 7273 -239 933 2331 N ATOM 2361 CA GLU A1108 44.290 8.290 37.189 1.00 74.67 C ANISOU 2361 CA GLU A1108 8457 12486 7430 -270 945 2454 C ATOM 2362 C GLU A1108 44.377 7.090 38.139 1.00 81.25 C ANISOU 2362 C GLU A1108 9064 13471 8335 -323 966 2675 C ATOM 2363 O GLU A1108 43.636 6.125 37.958 1.00 80.74 O ANISOU 2363 O GLU A1108 8937 13362 8379 -338 924 2774 O ATOM 2364 CB GLU A1108 45.564 8.343 36.341 1.00 75.21 C ANISOU 2364 CB GLU A1108 8689 12348 7540 -275 1001 2424 C ATOM 2365 CG GLU A1108 45.635 9.503 35.373 1.00 82.96 C ANISOU 2365 CG GLU A1108 9885 13176 8461 -228 985 2231 C ATOM 2366 CD GLU A1108 46.890 9.528 34.525 1.00102.21 C ANISOU 2366 CD GLU A1108 12472 15425 10936 -230 1039 2220 C ATOM 2367 OE1 GLU A1108 47.448 8.441 34.246 1.00 95.77 O ANISOU 2367 OE1 GLU A1108 11650 14510 10229 -255 1072 2337 O ATOM 2368 OE2 GLU A1108 47.266 10.631 34.070 1.00 96.90 O ANISOU 2368 OE2 GLU A1108 11928 14695 10193 -201 1041 2091 O ATOM 2369 N THR A1109 45.283 7.157 39.147 1.00 80.01 N ANISOU 2369 N THR A1109 8780 13496 8125 -354 1027 2757 N ATOM 2370 CA THR A1109 45.497 6.099 40.144 1.00 81.33 C ANISOU 2370 CA THR A1109 8714 13836 8352 -408 1054 2979 C ATOM 2371 C THR A1109 44.323 6.078 41.136 1.00 87.56 C ANISOU 2371 C THR A1109 9299 14896 9075 -401 1004 3035 C ATOM 2372 O THR A1109 43.885 4.999 41.544 1.00 87.79 O ANISOU 2372 O THR A1109 9158 14996 9201 -436 985 3221 O ATOM 2373 CB THR A1109 46.847 6.310 40.868 1.00 89.60 C ANISOU 2373 CB THR A1109 9699 15002 9343 -439 1136 3032 C ATOM 2374 OG1 THR A1109 47.888 6.425 39.898 1.00 88.06 O ANISOU 2374 OG1 THR A1109 9703 14560 9196 -438 1178 2971 O ATOM 2375 CG2 THR A1109 47.182 5.181 41.850 1.00 89.04 C ANISOU 2375 CG2 THR A1109 9386 15100 9343 -500 1171 3276 C ATOM 2376 N GLY A1110 43.836 7.268 41.498 1.00 85.36 N ANISOU 2376 N GLY A1110 9033 14761 8637 -352 979 2875 N ATOM 2377 CA GLY A1110 42.721 7.449 42.421 1.00 86.49 C ANISOU 2377 CA GLY A1110 8995 15180 8687 -328 930 2894 C ATOM 2378 C GLY A1110 41.441 6.763 41.986 1.00 91.59 C ANISOU 2378 C GLY A1110 9622 15757 9423 -323 859 2952 C ATOM 2379 O GLY A1110 40.757 6.155 42.813 1.00 91.80 O ANISOU 2379 O GLY A1110 9431 16006 9444 -335 832 3096 O ATOM 2380 N VAL A1111 41.125 6.833 40.679 1.00 88.47 N ANISOU 2380 N VAL A1111 9446 15060 9110 -306 827 2849 N ATOM 2381 CA VAL A1111 39.945 6.187 40.092 1.00 89.14 C ANISOU 2381 CA VAL A1111 9541 15033 9294 -302 756 2890 C ATOM 2382 C VAL A1111 40.313 4.726 39.741 1.00 95.09 C ANISOU 2382 C VAL A1111 10255 15624 10249 -358 762 3078 C ATOM 2383 O VAL A1111 39.438 3.852 39.789 1.00 95.33 O ANISOU 2383 O VAL A1111 10177 15660 10384 -376 704 3208 O ATOM 2384 CB VAL A1111 39.401 6.972 38.871 1.00 92.17 C ANISOU 2384 CB VAL A1111 10171 15192 9658 -251 713 2677 C ATOM 2385 CG1 VAL A1111 38.258 6.230 38.180 1.00 92.09 C ANISOU 2385 CG1 VAL A1111 10184 15042 9764 -251 640 2723 C ATOM 2386 CG2 VAL A1111 38.947 8.359 39.296 1.00 91.90 C ANISOU 2386 CG2 VAL A1111 10149 15327 9444 -195 695 2505 C ATOM 2387 N ALA A1112 41.612 4.451 39.458 1.00 92.41 N ANISOU 2387 N ALA A1112 9985 15155 9970 -386 827 3103 N ATOM 2388 CA ALA A1112 42.083 3.086 39.193 1.00 93.02 C ANISOU 2388 CA ALA A1112 10014 15087 10241 -436 836 3276 C ATOM 2389 C ALA A1112 41.925 2.217 40.441 1.00 98.93 C ANISOU 2389 C ALA A1112 10468 16084 11036 -487 837 3520 C ATOM 2390 O ALA A1112 41.728 1.011 40.321 1.00 99.16 O ANISOU 2390 O ALA A1112 10406 16025 11246 -526 804 3685 O ATOM 2391 CB ALA A1112 43.532 3.093 38.732 1.00 93.21 C ANISOU 2391 CB ALA A1112 10167 14954 10294 -448 912 3244 C ATOM 2392 N GLY A1113 41.937 2.854 41.618 1.00 96.57 N ANISOU 2392 N GLY A1113 10016 16100 10577 -483 864 3536 N ATOM 2393 CA GLY A1113 41.749 2.196 42.909 1.00 97.83 C ANISOU 2393 CA GLY A1113 9875 16554 10742 -523 867 3763 C ATOM 2394 C GLY A1113 40.324 1.741 43.177 1.00103.44 C ANISOU 2394 C GLY A1113 10435 17373 11495 -521 782 3870 C ATOM 2395 O GLY A1113 39.947 1.529 44.336 1.00103.80 O ANISOU 2395 O GLY A1113 10221 17721 11499 -540 777 4038 O ATOM 2396 N PHE A1114 39.519 1.588 42.101 1.00100.37 N ANISOU 2396 N PHE A1114 10204 16746 11187 -496 714 3780 N ATOM 2397 CA PHE A1114 38.132 1.130 42.150 1.00101.05 C ANISOU 2397 CA PHE A1114 10178 16883 11331 -494 624 3873 C ATOM 2398 C PHE A1114 37.887 0.069 41.053 1.00104.53 C ANISOU 2398 C PHE A1114 10713 16993 12010 -520 567 3928 C ATOM 2399 O PHE A1114 36.812 0.043 40.453 1.00104.10 O ANISOU 2399 O PHE A1114 10723 16834 11997 -497 490 3880 O ATOM 2400 CB PHE A1114 37.146 2.316 42.003 1.00102.72 C ANISOU 2400 CB PHE A1114 10484 17173 11373 -425 584 3676 C ATOM 2401 CG PHE A1114 37.251 3.401 43.054 1.00104.52 C ANISOU 2401 CG PHE A1114 10619 17723 11370 -387 623 3595 C ATOM 2402 CD1 PHE A1114 36.711 3.220 44.323 1.00108.78 C ANISOU 2402 CD1 PHE A1114 10876 18624 11833 -392 612 3755 C ATOM 2403 CD2 PHE A1114 37.791 4.643 42.742 1.00105.69 C ANISOU 2403 CD2 PHE A1114 10959 17818 11378 -340 660 3352 C ATOM 2404 CE1 PHE A1114 36.780 4.234 45.282 1.00109.79 C ANISOU 2404 CE1 PHE A1114 10915 19058 11741 -347 643 3661 C ATOM 2405 CE2 PHE A1114 37.847 5.660 43.699 1.00108.61 C ANISOU 2405 CE2 PHE A1114 11244 18478 11547 -300 684 3260 C ATOM 2406 CZ PHE A1114 37.355 5.443 44.964 1.00107.77 C ANISOU 2406 CZ PHE A1114 10857 18732 11360 -301 676 3408 C ATOM 2407 N THR A1115 38.888 -0.820 40.821 1.00100.96 N ANISOU 2407 N THR A1115 10261 16385 11716 -566 603 4030 N ATOM 2408 CA THR A1115 38.855 -1.916 39.830 1.00100.92 C ANISOU 2408 CA THR A1115 10329 16064 11953 -590 552 4084 C ATOM 2409 C THR A1115 37.634 -2.827 40.013 1.00105.02 C ANISOU 2409 C THR A1115 10680 16604 12618 -614 447 4255 C ATOM 2410 O THR A1115 37.031 -3.245 39.022 1.00104.15 O ANISOU 2410 O THR A1115 10693 16244 12637 -601 373 4197 O ATOM 2411 CB THR A1115 40.128 -2.774 39.920 1.00111.42 C ANISOU 2411 CB THR A1115 11600 17313 13422 -640 609 4218 C ATOM 2412 OG1 THR A1115 40.301 -3.203 41.274 1.00112.24 O ANISOU 2412 OG1 THR A1115 11414 17716 13516 -689 633 4448 O ATOM 2413 CG2 THR A1115 41.376 -2.042 39.441 1.00110.02 C ANISOU 2413 CG2 THR A1115 11626 17029 13147 -616 701 4048 C ATOM 2414 N ASN A1116 37.275 -3.122 41.282 1.00102.49 N ANISOU 2414 N ASN A1116 10074 16592 12274 -647 439 4469 N ATOM 2415 CA ASN A1116 36.131 -3.957 41.658 1.00103.41 C ANISOU 2415 CA ASN A1116 9984 16787 12518 -675 340 4672 C ATOM 2416 C ASN A1116 34.815 -3.350 41.138 1.00107.03 C ANISOU 2416 C ASN A1116 10556 17212 12899 -623 267 4531 C ATOM 2417 O ASN A1116 33.862 -4.089 40.895 1.00107.11 O ANISOU 2417 O ASN A1116 10505 17127 13065 -640 169 4635 O ATOM 2418 CB ASN A1116 36.070 -4.139 43.192 1.00105.11 C ANISOU 2418 CB ASN A1116 9872 17401 12663 -708 361 4909 C ATOM 2419 CG ASN A1116 36.044 -2.869 44.033 1.00125.12 C ANISOU 2419 CG ASN A1116 12374 20263 14901 -661 423 4797 C ATOM 2420 OD1 ASN A1116 36.143 -1.737 43.541 1.00119.17 O ANISOU 2420 OD1 ASN A1116 11841 19455 13985 -602 450 4537 O ATOM 2421 ND2 ASN A1116 35.955 -3.041 45.342 1.00115.88 N ANISOU 2421 ND2 ASN A1116 10917 19449 13661 -685 446 4995 N ATOM 2422 N SER A1117 34.788 -2.014 40.938 1.00102.79 N ANISOU 2422 N SER A1117 10186 16739 12132 -562 310 4293 N ATOM 2423 CA SER A1117 33.638 -1.259 40.432 1.00102.15 C ANISOU 2423 CA SER A1117 10230 16630 11952 -508 254 4133 C ATOM 2424 C SER A1117 33.780 -0.972 38.927 1.00104.23 C ANISOU 2424 C SER A1117 10810 16530 12265 -477 244 3905 C ATOM 2425 O SER A1117 32.781 -0.993 38.207 1.00103.08 O ANISOU 2425 O SER A1117 10756 16244 12166 -456 168 3842 O ATOM 2426 CB SER A1117 33.487 0.049 41.200 1.00105.48 C ANISOU 2426 CB SER A1117 10629 17347 12102 -456 299 4011 C ATOM 2427 OG SER A1117 33.316 -0.178 42.590 1.00114.65 O ANISOU 2427 OG SER A1117 11491 18872 13197 -475 307 4211 O ATOM 2428 N LEU A1118 35.018 -0.702 38.460 1.00100.39 N ANISOU 2428 N LEU A1118 10481 15900 11761 -472 322 3787 N ATOM 2429 CA LEU A1118 35.322 -0.436 37.048 1.00 99.57 C ANISOU 2429 CA LEU A1118 10666 15472 11696 -441 324 3580 C ATOM 2430 C LEU A1118 35.005 -1.661 36.187 1.00104.01 C ANISOU 2430 C LEU A1118 11254 15762 12504 -464 245 3654 C ATOM 2431 O LEU A1118 34.548 -1.504 35.053 1.00103.08 O ANISOU 2431 O LEU A1118 11329 15422 12416 -430 200 3503 O ATOM 2432 CB LEU A1118 36.803 -0.027 36.857 1.00 98.99 C ANISOU 2432 CB LEU A1118 10712 15330 11570 -438 424 3490 C ATOM 2433 CG LEU A1118 37.265 1.321 37.443 1.00103.05 C ANISOU 2433 CG LEU A1118 11265 16042 11848 -406 499 3358 C ATOM 2434 CD1 LEU A1118 38.776 1.428 37.442 1.00102.74 C ANISOU 2434 CD1 LEU A1118 11276 15963 11798 -421 591 3347 C ATOM 2435 CD2 LEU A1118 36.644 2.500 36.707 1.00104.71 C ANISOU 2435 CD2 LEU A1118 11689 16166 11930 -344 479 3118 C ATOM 2436 N ARG A1119 35.237 -2.878 36.732 1.00101.65 N ANISOU 2436 N ARG A1119 10752 15485 12386 -522 224 3887 N ATOM 2437 CA ARG A1119 34.954 -4.141 36.048 1.00102.29 C ANISOU 2437 CA ARG A1119 10819 15318 12730 -549 138 3980 C ATOM 2438 C ARG A1119 33.456 -4.288 35.815 1.00107.42 C ANISOU 2438 C ARG A1119 11442 15948 13423 -539 27 3996 C ATOM 2439 O ARG A1119 33.039 -4.763 34.755 1.00107.05 O ANISOU 2439 O ARG A1119 11525 15633 13515 -526 -46 3921 O ATOM 2440 CB ARG A1119 35.492 -5.326 36.860 1.00103.34 C ANISOU 2440 CB ARG A1119 10700 15523 13041 -616 135 4250 C ATOM 2441 N MET A1120 32.651 -3.830 36.797 1.00104.90 N ANISOU 2441 N MET A1120 10960 15924 12972 -540 16 4084 N ATOM 2442 CA MET A1120 31.187 -3.848 36.768 1.00105.47 C ANISOU 2442 CA MET A1120 10981 16041 13053 -530 -82 4119 C ATOM 2443 C MET A1120 30.658 -2.868 35.709 1.00108.61 C ANISOU 2443 C MET A1120 11648 16294 13324 -467 -91 3848 C ATOM 2444 O MET A1120 29.624 -3.141 35.097 1.00108.24 O ANISOU 2444 O MET A1120 11646 16123 13357 -459 -182 3833 O ATOM 2445 CB MET A1120 30.620 -3.505 38.157 1.00108.50 C ANISOU 2445 CB MET A1120 11113 16815 13298 -538 -76 4276 C ATOM 2446 CG MET A1120 30.965 -4.538 39.223 1.00113.38 C ANISOU 2446 CG MET A1120 11434 17595 14051 -604 -81 4576 C ATOM 2447 SD MET A1120 30.482 -4.067 40.906 1.00118.32 S ANISOU 2447 SD MET A1120 11750 18725 14480 -605 -55 4757 S ATOM 2448 CE MET A1120 30.910 -5.549 41.781 1.00116.29 C ANISOU 2448 CE MET A1120 11178 18546 14460 -692 -77 5116 C ATOM 2449 N LEU A1121 31.385 -1.747 35.476 1.00104.49 N ANISOU 2449 N LEU A1121 11304 15778 12619 -426 1 3642 N ATOM 2450 CA LEU A1121 31.051 -0.730 34.462 1.00103.40 C ANISOU 2450 CA LEU A1121 11424 15502 12362 -368 3 3386 C ATOM 2451 C LEU A1121 31.326 -1.263 33.048 1.00107.33 C ANISOU 2451 C LEU A1121 12124 15644 13013 -359 -27 3278 C ATOM 2452 O LEU A1121 30.673 -0.835 32.093 1.00106.19 O ANISOU 2452 O LEU A1121 12155 15353 12840 -321 -67 3120 O ATOM 2453 CB LEU A1121 31.848 0.573 34.699 1.00102.46 C ANISOU 2453 CB LEU A1121 11409 15503 12020 -331 104 3221 C ATOM 2454 CG LEU A1121 31.595 1.334 36.013 1.00107.17 C ANISOU 2454 CG LEU A1121 11838 16453 12427 -320 136 3265 C ATOM 2455 CD1 LEU A1121 32.662 2.375 36.258 1.00106.44 C ANISOU 2455 CD1 LEU A1121 11841 16437 12165 -292 231 3115 C ATOM 2456 CD2 LEU A1121 30.208 1.958 36.050 1.00109.42 C ANISOU 2456 CD2 LEU A1121 12116 16841 12619 -284 71 3214 C ATOM 2457 N GLN A1122 32.301 -2.189 32.922 1.00104.80 N ANISOU 2457 N GLN A1122 11774 15195 12851 -390 -8 3360 N ATOM 2458 CA GLN A1122 32.674 -2.831 31.660 1.00104.81 C ANISOU 2458 CA GLN A1122 11939 14873 13009 -378 -38 3269 C ATOM 2459 C GLN A1122 31.663 -3.914 31.289 1.00109.86 C ANISOU 2459 C GLN A1122 12510 15369 13861 -398 -166 3365 C ATOM 2460 O GLN A1122 31.387 -4.104 30.103 1.00109.22 O ANISOU 2460 O GLN A1122 12598 15043 13859 -368 -218 3230 O ATOM 2461 CB GLN A1122 34.084 -3.429 31.754 1.00106.30 C ANISOU 2461 CB GLN A1122 12103 14995 13292 -401 26 3329 C ATOM 2462 N GLN A1123 31.108 -4.621 32.307 1.00107.62 N ANISOU 2462 N GLN A1123 11973 15247 13672 -449 -220 3602 N ATOM 2463 CA GLN A1123 30.104 -5.681 32.128 1.00108.63 C ANISOU 2463 CA GLN A1123 11992 15266 14016 -477 -351 3735 C ATOM 2464 C GLN A1123 28.670 -5.091 31.986 1.00112.53 C ANISOU 2464 C GLN A1123 12516 15830 14410 -454 -416 3684 C ATOM 2465 O GLN A1123 27.715 -5.852 31.783 1.00113.06 O ANISOU 2465 O GLN A1123 12508 15810 14639 -474 -531 3782 O ATOM 2466 CB GLN A1123 30.140 -6.687 33.297 1.00111.15 C ANISOU 2466 CB GLN A1123 12006 15735 14489 -545 -383 4036 C ATOM 2467 CG GLN A1123 31.440 -7.493 33.404 1.00127.37 C ANISOU 2467 CG GLN A1123 14005 17692 16696 -577 -341 4120 C ATOM 2468 CD GLN A1123 31.417 -8.568 34.478 1.00150.73 C ANISOU 2468 CD GLN A1123 16654 20774 19842 -648 -389 4433 C ATOM 2469 OE1 GLN A1123 32.433 -9.216 34.755 1.00146.80 O ANISOU 2469 OE1 GLN A1123 16064 20266 19447 -681 -345 4539 O ATOM 2470 NE2 GLN A1123 30.264 -8.802 35.101 1.00145.23 N ANISOU 2470 NE2 GLN A1123 15780 20200 19199 -674 -481 4598 N ATOM 2471 N LYS A1124 28.538 -3.736 32.087 1.00107.71 N ANISOU 2471 N LYS A1124 12011 15374 13539 -411 -345 3533 N ATOM 2472 CA LYS A1124 27.310 -2.919 31.955 1.00106.79 C ANISOU 2472 CA LYS A1124 11948 15344 13283 -378 -383 3450 C ATOM 2473 C LYS A1124 26.301 -3.224 33.109 1.00110.96 C ANISOU 2473 C LYS A1124 12209 16132 13820 -410 -442 3682 C ATOM 2474 O LYS A1124 25.104 -2.950 32.976 1.00110.07 O ANISOU 2474 O LYS A1124 12100 16057 13666 -394 -508 3671 O ATOM 2475 CB LYS A1124 26.619 -3.125 30.577 1.00108.74 C ANISOU 2475 CB LYS A1124 12385 15306 13624 -353 -467 3310 C ATOM 2476 CG LYS A1124 27.520 -2.895 29.353 1.00115.05 C ANISOU 2476 CG LYS A1124 13437 15855 14420 -315 -420 3089 C ATOM 2477 CD LYS A1124 28.079 -1.475 29.247 1.00119.92 C ANISOU 2477 CD LYS A1124 14211 16562 14791 -269 -311 2900 C ATOM 2478 CE LYS A1124 29.088 -1.343 28.136 1.00126.56 C ANISOU 2478 CE LYS A1124 15267 17183 15638 -236 -261 2723 C ATOM 2479 NZ LYS A1124 30.276 -2.213 28.364 1.00133.98 N ANISOU 2479 NZ LYS A1124 16133 18065 16709 -265 -225 2820 N ATOM 2480 N ARG A1125 26.804 -3.729 34.251 1.00108.51 N ANISOU 2480 N ARG A1125 11666 16016 13548 -453 -414 3891 N ATOM 2481 CA ARG A1125 25.974 -4.007 35.423 1.00109.47 C ANISOU 2481 CA ARG A1125 11511 16421 13663 -481 -460 4128 C ATOM 2482 C ARG A1125 26.112 -2.819 36.385 1.00112.31 C ANISOU 2482 C ARG A1125 11819 17113 13743 -445 -369 4075 C ATOM 2483 O ARG A1125 26.735 -2.932 37.447 1.00111.93 O ANISOU 2483 O ARG A1125 11587 17293 13649 -467 -312 4209 O ATOM 2484 CB ARG A1125 26.353 -5.363 36.084 1.00111.99 C ANISOU 2484 CB ARG A1125 11581 16763 14209 -550 -495 4410 C ATOM 2485 CG ARG A1125 26.336 -6.604 35.155 1.00125.00 C ANISOU 2485 CG ARG A1125 13268 18064 16161 -584 -592 4457 C ATOM 2486 CD ARG A1125 25.018 -6.865 34.417 1.00137.22 C ANISOU 2486 CD ARG A1125 14869 19453 17814 -577 -719 4442 C ATOM 2487 NE ARG A1125 23.882 -7.128 35.307 1.00147.29 N ANISOU 2487 NE ARG A1125 15898 20961 19106 -604 -796 4676 N ATOM 2488 CZ ARG A1125 23.489 -8.340 35.689 1.00163.01 C ANISOU 2488 CZ ARG A1125 17660 22935 21343 -664 -898 4943 C ATOM 2489 NH1 ARG A1125 24.141 -9.419 35.272 1.00153.21 N ANISOU 2489 NH1 ARG A1125 16404 21447 20361 -702 -939 5003 N ATOM 2490 NH2 ARG A1125 22.441 -8.482 36.488 1.00148.85 N ANISOU 2490 NH2 ARG A1125 15643 21372 19541 -683 -965 5156 N ATOM 2491 N TRP A1126 25.552 -1.658 35.965 1.00108.12 N ANISOU 2491 N TRP A1126 11455 16597 13027 -387 -357 3866 N ATOM 2492 CA TRP A1126 25.618 -0.357 36.652 1.00107.53 C ANISOU 2492 CA TRP A1126 11384 16789 12684 -338 -281 3750 C ATOM 2493 C TRP A1126 25.185 -0.432 38.110 1.00111.69 C ANISOU 2493 C TRP A1126 11614 17700 13125 -346 -283 3956 C ATOM 2494 O TRP A1126 25.756 0.250 38.962 1.00110.86 O ANISOU 2494 O TRP A1126 11442 17837 12843 -323 -205 3919 O ATOM 2495 CB TRP A1126 24.719 0.688 35.951 1.00105.86 C ANISOU 2495 CB TRP A1126 11360 16523 12339 -280 -305 3541 C ATOM 2496 CG TRP A1126 24.791 0.722 34.451 1.00106.31 C ANISOU 2496 CG TRP A1126 11691 16221 12479 -268 -324 3355 C ATOM 2497 CD1 TRP A1126 23.796 0.385 33.582 1.00109.41 C ANISOU 2497 CD1 TRP A1126 12170 16426 12976 -267 -414 3335 C ATOM 2498 CD2 TRP A1126 25.947 1.001 33.648 1.00105.43 C ANISOU 2498 CD2 TRP A1126 11787 15903 12368 -256 -255 3184 C ATOM 2499 NE1 TRP A1126 24.234 0.516 32.285 1.00108.26 N ANISOU 2499 NE1 TRP A1126 12276 15982 12875 -250 -403 3145 N ATOM 2500 CE2 TRP A1126 25.558 0.872 32.296 1.00109.10 C ANISOU 2500 CE2 TRP A1126 12458 16073 12922 -243 -307 3056 C ATOM 2501 CE3 TRP A1126 27.275 1.361 33.938 1.00106.26 C ANISOU 2501 CE3 TRP A1126 11921 16052 12402 -255 -156 3129 C ATOM 2502 CZ2 TRP A1126 26.445 1.097 31.237 1.00107.67 C ANISOU 2502 CZ2 TRP A1126 12501 15655 12752 -224 -260 2878 C ATOM 2503 CZ3 TRP A1126 28.159 1.559 32.889 1.00107.00 C ANISOU 2503 CZ3 TRP A1126 12238 15898 12518 -240 -113 2962 C ATOM 2504 CH2 TRP A1126 27.742 1.431 31.557 1.00107.37 C ANISOU 2504 CH2 TRP A1126 12480 15668 12646 -223 -164 2839 C ATOM 2505 N ASP A1127 24.147 -1.235 38.372 1.00109.27 N ANISOU 2505 N ASP A1127 11126 17454 12939 -376 -378 4169 N ATOM 2506 CA ASP A1127 23.478 -1.428 39.653 1.00110.16 C ANISOU 2506 CA ASP A1127 10938 17932 12988 -382 -403 4396 C ATOM 2507 C ASP A1127 24.463 -1.864 40.763 1.00113.82 C ANISOU 2507 C ASP A1127 11180 18610 13456 -419 -340 4572 C ATOM 2508 O ASP A1127 24.467 -1.247 41.828 1.00113.47 O ANISOU 2508 O ASP A1127 10987 18912 13214 -388 -290 4596 O ATOM 2509 CB ASP A1127 22.377 -2.480 39.479 1.00113.20 C ANISOU 2509 CB ASP A1127 11192 18248 13569 -421 -529 4609 C ATOM 2510 CG ASP A1127 21.402 -2.168 38.348 1.00124.59 C ANISOU 2510 CG ASP A1127 12849 19460 15028 -392 -597 4449 C ATOM 2511 OD1 ASP A1127 21.042 -0.978 38.179 1.00124.54 O ANISOU 2511 OD1 ASP A1127 12985 19522 14813 -329 -561 4240 O ATOM 2512 OD2 ASP A1127 20.958 -3.119 37.669 1.00131.84 O ANISOU 2512 OD2 ASP A1127 13782 20137 16173 -432 -691 4537 O ATOM 2513 N GLU A1128 25.305 -2.890 40.510 1.00110.09 N ANISOU 2513 N GLU A1128 10688 17939 13203 -481 -341 4684 N ATOM 2514 CA GLU A1128 26.292 -3.364 41.492 1.00110.15 C ANISOU 2514 CA GLU A1128 10492 18125 13234 -522 -280 4859 C ATOM 2515 C GLU A1128 27.411 -2.334 41.670 1.00112.08 C ANISOU 2515 C GLU A1128 10864 18445 13278 -486 -157 4654 C ATOM 2516 O GLU A1128 27.882 -2.132 42.791 1.00111.75 O ANISOU 2516 O GLU A1128 10636 18712 13113 -487 -96 4746 O ATOM 2517 CB GLU A1128 26.896 -4.730 41.096 1.00112.05 C ANISOU 2517 CB GLU A1128 10695 18104 13776 -594 -317 5016 C ATOM 2518 CG GLU A1128 25.931 -5.909 41.042 1.00124.63 C ANISOU 2518 CG GLU A1128 12118 19623 15614 -643 -447 5261 C ATOM 2519 CD GLU A1128 24.911 -5.959 39.917 1.00146.68 C ANISOU 2519 CD GLU A1128 15086 22148 18499 -625 -546 5152 C ATOM 2520 OE1 GLU A1128 24.963 -5.101 39.006 1.00136.08 O ANISOU 2520 OE1 GLU A1128 14022 20648 17033 -573 -514 4868 O ATOM 2521 OE2 GLU A1128 24.088 -6.903 39.920 1.00143.92 O ANISOU 2521 OE2 GLU A1128 14589 21736 18358 -667 -661 5358 O ATOM 2522 N ALA A1129 27.825 -1.680 40.556 1.00107.03 N ANISOU 2522 N ALA A1129 10535 17527 12606 -453 -124 4381 N ATOM 2523 CA ALA A1129 28.871 -0.650 40.528 1.00105.62 C ANISOU 2523 CA ALA A1129 10514 17363 12256 -418 -18 4166 C ATOM 2524 C ALA A1129 28.479 0.551 41.381 1.00108.87 C ANISOU 2524 C ALA A1129 10860 18109 12398 -359 17 4075 C ATOM 2525 O ALA A1129 29.327 1.122 42.062 1.00108.48 O ANISOU 2525 O ALA A1129 10767 18238 12213 -347 98 4030 O ATOM 2526 CB ALA A1129 29.133 -0.207 39.097 1.00105.21 C ANISOU 2526 CB ALA A1129 10791 16955 12229 -390 -12 3912 C ATOM 2527 N ALA A1130 27.185 0.907 41.365 1.00105.00 N ANISOU 2527 N ALA A1130 10352 17708 11836 -320 -49 4050 N ATOM 2528 CA ALA A1130 26.624 2.008 42.141 1.00104.71 C ANISOU 2528 CA ALA A1130 10243 17989 11553 -255 -33 3960 C ATOM 2529 C ALA A1130 26.627 1.695 43.645 1.00109.08 C ANISOU 2529 C ALA A1130 10462 18953 12033 -265 -19 4187 C ATOM 2530 O ALA A1130 26.695 2.615 44.461 1.00108.63 O ANISOU 2530 O ALA A1130 10331 19186 11758 -212 25 4100 O ATOM 2531 CB ALA A1130 25.206 2.291 41.675 1.00105.52 C ANISOU 2531 CB ALA A1130 10403 18061 11628 -216 -114 3905 C ATOM 2532 N VAL A1131 26.564 0.396 44.004 1.00106.12 N ANISOU 2532 N VAL A1131 9877 18602 11842 -332 -61 4477 N ATOM 2533 CA VAL A1131 26.530 -0.070 45.391 1.00106.88 C ANISOU 2533 CA VAL A1131 9630 19084 11896 -352 -55 4737 C ATOM 2534 C VAL A1131 27.968 -0.101 45.968 1.00110.21 C ANISOU 2534 C VAL A1131 9995 19588 12291 -380 42 4758 C ATOM 2535 O VAL A1131 28.184 0.454 47.048 1.00110.37 O ANISOU 2535 O VAL A1131 9854 19963 12118 -347 91 4767 O ATOM 2536 CB VAL A1131 25.837 -1.458 45.504 1.00111.75 C ANISOU 2536 CB VAL A1131 10038 19680 12743 -417 -148 5054 C ATOM 2537 CG1 VAL A1131 25.912 -2.011 46.924 1.00112.89 C ANISOU 2537 CG1 VAL A1131 9813 20218 12864 -446 -138 5350 C ATOM 2538 CG2 VAL A1131 24.385 -1.377 45.048 1.00111.74 C ANISOU 2538 CG2 VAL A1131 10066 19643 12745 -387 -244 5046 C ATOM 2539 N ASN A1132 28.936 -0.743 45.259 1.00105.58 N ANISOU 2539 N ASN A1132 9538 18684 11894 -437 67 4763 N ATOM 2540 CA ASN A1132 30.336 -0.864 45.714 1.00104.76 C ANISOU 2540 CA ASN A1132 9392 18623 11790 -471 158 4797 C ATOM 2541 C ASN A1132 30.973 0.505 45.954 1.00105.26 C ANISOU 2541 C ASN A1132 9582 18807 11606 -410 243 4540 C ATOM 2542 O ASN A1132 31.667 0.685 46.957 1.00104.73 O ANISOU 2542 O ASN A1132 9359 19000 11432 -415 308 4600 O ATOM 2543 CB ASN A1132 31.200 -1.648 44.709 1.00107.23 C ANISOU 2543 CB ASN A1132 9871 18534 12338 -527 165 4797 C ATOM 2544 CG ASN A1132 30.920 -3.133 44.588 1.00137.43 C ANISOU 2544 CG ASN A1132 13542 22231 16443 -598 89 5070 C ATOM 2545 OD1 ASN A1132 31.848 -3.949 44.597 1.00132.80 O ANISOU 2545 OD1 ASN A1132 12911 21526 16021 -655 116 5190 O ATOM 2546 ND2 ASN A1132 29.652 -3.533 44.513 1.00131.40 N ANISOU 2546 ND2 ASN A1132 12680 21498 15748 -598 -11 5185 N ATOM 2547 N LEU A1133 30.730 1.465 45.037 1.00 99.36 N ANISOU 2547 N LEU A1133 9108 17870 10774 -354 237 4261 N ATOM 2548 CA LEU A1133 31.255 2.827 45.128 1.00 97.77 C ANISOU 2548 CA LEU A1133 9044 17743 10360 -294 302 4002 C ATOM 2549 C LEU A1133 30.604 3.589 46.286 1.00100.96 C ANISOU 2549 C LEU A1133 9255 18570 10535 -232 297 3989 C ATOM 2550 O LEU A1133 31.281 4.393 46.926 1.00100.08 O ANISOU 2550 O LEU A1133 9121 18646 10259 -199 357 3876 O ATOM 2551 CB LEU A1133 31.051 3.594 43.809 1.00 96.55 C ANISOU 2551 CB LEU A1133 9219 17267 10200 -254 286 3729 C ATOM 2552 CG LEU A1133 31.917 3.157 42.616 1.00 99.98 C ANISOU 2552 CG LEU A1133 9883 17299 10806 -294 309 3670 C ATOM 2553 CD1 LEU A1133 31.415 3.757 41.325 1.00 99.10 C ANISOU 2553 CD1 LEU A1133 10053 16904 10697 -255 275 3444 C ATOM 2554 CD2 LEU A1133 33.382 3.498 42.831 1.00101.56 C ANISOU 2554 CD2 LEU A1133 10128 17498 10960 -308 402 3613 C ATOM 2555 N ALA A1134 29.313 3.315 46.579 1.00 97.68 N ANISOU 2555 N ALA A1134 8690 18312 10110 -214 222 4107 N ATOM 2556 CA ALA A1134 28.602 3.944 47.696 1.00 98.08 C ANISOU 2556 CA ALA A1134 8536 18787 9945 -147 210 4111 C ATOM 2557 C ALA A1134 29.191 3.491 49.040 1.00102.41 C ANISOU 2557 C ALA A1134 8778 19700 10434 -172 256 4320 C ATOM 2558 O ALA A1134 29.197 4.265 49.999 1.00102.64 O ANISOU 2558 O ALA A1134 8682 20071 10244 -110 284 4243 O ATOM 2559 CB ALA A1134 27.118 3.619 47.635 1.00 99.45 C ANISOU 2559 CB ALA A1134 8614 19028 10144 -130 119 4222 C ATOM 2560 N LYS A1135 29.725 2.252 49.089 1.00 98.55 N ANISOU 2560 N LYS A1135 8171 19132 10142 -259 263 4574 N ATOM 2561 CA LYS A1135 30.337 1.668 50.282 1.00 98.89 C ANISOU 2561 CA LYS A1135 7919 19492 10165 -297 306 4806 C ATOM 2562 C LYS A1135 31.833 2.041 50.403 1.00101.22 C ANISOU 2562 C LYS A1135 8306 19735 10418 -314 403 4694 C ATOM 2563 O LYS A1135 32.393 1.894 51.491 1.00101.80 O ANISOU 2563 O LYS A1135 8151 20116 10414 -329 452 4828 O ATOM 2564 CB LYS A1135 30.187 0.140 50.266 1.00102.10 C ANISOU 2564 CB LYS A1135 8145 19825 10824 -386 261 5145 C ATOM 2565 N SER A1136 32.478 2.519 49.305 1.00 95.29 N ANISOU 2565 N SER A1136 7879 18612 9714 -313 431 4459 N ATOM 2566 CA SER A1136 33.902 2.891 49.322 1.00 93.66 C ANISOU 2566 CA SER A1136 7778 18331 9477 -330 520 4353 C ATOM 2567 C SER A1136 34.111 4.277 49.986 1.00 96.44 C ANISOU 2567 C SER A1136 8143 18937 9564 -251 557 4122 C ATOM 2568 O SER A1136 33.145 5.012 50.209 1.00 96.09 O ANISOU 2568 O SER A1136 8073 19067 9371 -177 513 4008 O ATOM 2569 CB SER A1136 34.485 2.888 47.912 1.00 95.38 C ANISOU 2569 CB SER A1136 8321 18076 9845 -354 531 4204 C ATOM 2570 OG SER A1136 33.848 3.831 47.071 1.00103.61 O ANISOU 2570 OG SER A1136 9602 18951 10815 -291 495 3946 O ATOM 2571 N ARG A1137 35.381 4.606 50.311 1.00 92.48 N ANISOU 2571 N ARG A1137 7673 18453 9011 -266 635 4058 N ATOM 2572 CA ARG A1137 35.815 5.832 51.000 1.00 92.31 C ANISOU 2572 CA ARG A1137 7650 18660 8763 -201 673 3852 C ATOM 2573 C ARG A1137 35.445 7.123 50.234 1.00 94.77 C ANISOU 2573 C ARG A1137 8224 18805 8979 -124 642 3526 C ATOM 2574 O ARG A1137 35.218 8.154 50.876 1.00 94.92 O ANISOU 2574 O ARG A1137 8186 19078 8801 -47 630 3366 O ATOM 2575 CB ARG A1137 37.336 5.809 51.207 1.00 92.63 C ANISOU 2575 CB ARG A1137 7728 18644 8822 -248 758 3851 C ATOM 2576 N TRP A1138 35.415 7.069 48.881 1.00 89.24 N ANISOU 2576 N TRP A1138 7802 17685 8421 -143 626 3427 N ATOM 2577 CA TRP A1138 35.090 8.199 47.999 1.00 87.54 C ANISOU 2577 CA TRP A1138 7849 17263 8150 -82 595 3140 C ATOM 2578 C TRP A1138 33.659 8.738 48.251 1.00 92.61 C ANISOU 2578 C TRP A1138 8421 18091 8674 -7 523 3067 C ATOM 2579 O TRP A1138 33.485 9.957 48.314 1.00 92.28 O ANISOU 2579 O TRP A1138 8466 18109 8489 67 507 2827 O ATOM 2580 CB TRP A1138 35.239 7.784 46.525 1.00 84.66 C ANISOU 2580 CB TRP A1138 7745 16447 7974 -123 587 3112 C ATOM 2581 CG TRP A1138 34.569 8.697 45.538 1.00 84.51 C ANISOU 2581 CG TRP A1138 7965 16216 7929 -68 539 2876 C ATOM 2582 CD1 TRP A1138 34.890 9.995 45.269 1.00 86.75 C ANISOU 2582 CD1 TRP A1138 8419 16436 8106 -14 545 2616 C ATOM 2583 CD2 TRP A1138 33.573 8.324 44.579 1.00 83.88 C ANISOU 2583 CD2 TRP A1138 7995 15917 7959 -70 478 2888 C ATOM 2584 NE1 TRP A1138 34.086 10.483 44.267 1.00 85.44 N ANISOU 2584 NE1 TRP A1138 8446 16054 7966 20 493 2471 N ATOM 2585 CE2 TRP A1138 33.279 9.472 43.811 1.00 86.92 C ANISOU 2585 CE2 TRP A1138 8606 16141 8281 -13 454 2630 C ATOM 2586 CE3 TRP A1138 32.874 7.135 44.312 1.00 85.37 C ANISOU 2586 CE3 TRP A1138 8104 16034 8298 -115 435 3094 C ATOM 2587 CZ2 TRP A1138 32.315 9.468 42.798 1.00 85.83 C ANISOU 2587 CZ2 TRP A1138 8615 15786 8212 0 395 2574 C ATOM 2588 CZ3 TRP A1138 31.917 7.134 43.311 1.00 86.43 C ANISOU 2588 CZ3 TRP A1138 8388 15948 8502 -100 373 3030 C ATOM 2589 CH2 TRP A1138 31.644 8.289 42.567 1.00 86.32 C ANISOU 2589 CH2 TRP A1138 8597 15789 8411 -43 356 2773 C ATOM 2590 N TYR A1139 32.654 7.846 48.403 1.00 89.72 N ANISOU 2590 N TYR A1139 7898 17816 8374 -25 475 3274 N ATOM 2591 CA TYR A1139 31.266 8.254 48.641 1.00 90.00 C ANISOU 2591 CA TYR A1139 7856 18034 8306 43 406 3235 C ATOM 2592 C TYR A1139 31.069 8.779 50.068 1.00 95.29 C ANISOU 2592 C TYR A1139 8266 19183 8758 107 411 3235 C ATOM 2593 O TYR A1139 29.992 9.289 50.386 1.00 94.94 O ANISOU 2593 O TYR A1139 8147 19334 8591 180 359 3172 O ATOM 2594 CB TYR A1139 30.314 7.087 48.390 1.00 91.54 C ANISOU 2594 CB TYR A1139 7952 18178 8651 -2 351 3478 C ATOM 2595 N ASN A1140 32.110 8.665 50.917 1.00 93.28 N ANISOU 2595 N ASN A1140 7869 19125 8450 85 473 3303 N ATOM 2596 CA ASN A1140 32.080 9.107 52.309 1.00 94.90 C ANISOU 2596 CA ASN A1140 7814 19801 8443 146 483 3304 C ATOM 2597 C ASN A1140 32.799 10.466 52.478 1.00 98.28 C ANISOU 2597 C ASN A1140 8362 20260 8720 209 509 3001 C ATOM 2598 O ASN A1140 32.332 11.288 53.273 1.00 98.64 O ANISOU 2598 O ASN A1140 8286 20621 8571 301 483 2871 O ATOM 2599 CB ASN A1140 32.710 8.050 53.223 1.00 99.52 C ANISOU 2599 CB ASN A1140 8123 20627 9062 80 529 3600 C ATOM 2600 CG ASN A1140 32.002 6.700 53.223 1.00132.07 C ANISOU 2600 CG ASN A1140 12081 24759 13339 18 493 3920 C ATOM 2601 OD1 ASN A1140 31.231 6.351 52.313 1.00126.64 O ANISOU 2601 OD1 ASN A1140 11539 23782 12798 -4 444 3940 O ATOM 2602 ND2 ASN A1140 32.299 5.884 54.224 1.00127.57 N ANISOU 2602 ND2 ASN A1140 11203 24511 12755 -17 515 4185 N ATOM 2603 N GLN A1141 33.915 10.706 51.732 1.00 93.65 N ANISOU 2603 N GLN A1141 8007 19348 8226 166 553 2889 N ATOM 2604 CA GLN A1141 34.662 11.976 51.763 1.00 93.31 C ANISOU 2604 CA GLN A1141 8100 19280 8073 217 570 2607 C ATOM 2605 C GLN A1141 33.715 13.128 51.349 1.00 97.12 C ANISOU 2605 C GLN A1141 8721 19709 8470 310 500 2343 C ATOM 2606 O GLN A1141 33.301 13.908 52.211 1.00 97.78 O ANISOU 2606 O GLN A1141 8668 20111 8373 399 470 2219 O ATOM 2607 CB GLN A1141 35.911 11.903 50.851 1.00 93.70 C ANISOU 2607 CB GLN A1141 8386 18952 8265 146 623 2568 C ATOM 2608 CG GLN A1141 36.788 13.173 50.863 1.00112.30 C ANISOU 2608 CG GLN A1141 10880 21257 10530 189 636 2298 C ATOM 2609 CD GLN A1141 37.933 13.179 49.855 1.00129.70 C ANISOU 2609 CD GLN A1141 13330 23076 12873 126 682 2258 C ATOM 2610 OE1 GLN A1141 37.998 12.376 48.911 1.00124.10 O ANISOU 2610 OE1 GLN A1141 12744 22077 12331 62 696 2378 O ATOM 2611 NE2 GLN A1141 38.817 14.157 49.983 1.00120.46 N ANISOU 2611 NE2 GLN A1141 12246 21885 11637 150 697 2070 N ATOM 2612 N THR A1142 33.338 13.188 50.042 1.00 92.25 N ANISOU 2612 N THR A1142 8363 18704 7984 293 474 2267 N ATOM 2613 CA THR A1142 32.366 14.144 49.483 1.00 91.58 C ANISOU 2613 CA THR A1142 8420 18523 7852 368 407 2051 C ATOM 2614 C THR A1142 31.099 13.325 49.172 1.00 95.02 C ANISOU 2614 C THR A1142 8797 18950 8356 354 364 2226 C ATOM 2615 O THR A1142 31.059 12.623 48.160 1.00 93.59 O ANISOU 2615 O THR A1142 8743 18468 8350 283 369 2341 O ATOM 2616 CB THR A1142 32.941 14.914 48.274 1.00 97.56 C ANISOU 2616 CB THR A1142 9497 18875 8695 361 408 1837 C ATOM 2617 OG1 THR A1142 33.301 13.983 47.254 1.00 96.58 O ANISOU 2617 OG1 THR A1142 9517 18420 8760 272 437 1978 O ATOM 2618 CG2 THR A1142 34.141 15.784 48.637 1.00 95.46 C ANISOU 2618 CG2 THR A1142 9275 18634 8362 378 439 1668 C ATOM 2619 N PRO A1143 30.107 13.300 50.093 1.00 92.59 N ANISOU 2619 N PRO A1143 8269 18994 7918 416 323 2277 N ATOM 2620 CA PRO A1143 28.957 12.401 49.910 1.00 92.69 C ANISOU 2620 CA PRO A1143 8192 19023 8004 394 282 2485 C ATOM 2621 C PRO A1143 27.929 12.838 48.867 1.00 95.70 C ANISOU 2621 C PRO A1143 8790 19137 8433 423 224 2344 C ATOM 2622 O PRO A1143 27.585 12.025 48.010 1.00 94.64 O ANISOU 2622 O PRO A1143 8773 18718 8469 359 213 2456 O ATOM 2623 CB PRO A1143 28.265 12.422 51.279 1.00 96.03 C ANISOU 2623 CB PRO A1143 8294 19946 8246 460 261 2578 C ATOM 2624 CG PRO A1143 28.731 13.657 52.008 1.00100.96 C ANISOU 2624 CG PRO A1143 8839 20816 8707 513 296 2416 C ATOM 2625 CD PRO A1143 30.036 13.990 51.393 1.00 95.25 C ANISOU 2625 CD PRO A1143 8412 19742 8036 511 310 2159 C ATOM 2626 N ASN A1144 27.430 14.091 48.941 1.00 92.20 N ANISOU 2626 N ASN A1144 8394 18791 7848 521 185 2100 N ATOM 2627 CA ASN A1144 26.466 14.640 47.979 1.00 91.31 C ANISOU 2627 CA ASN A1144 8474 18456 7763 558 129 1953 C ATOM 2628 C ASN A1144 27.067 14.759 46.578 1.00 93.66 C ANISOU 2628 C ASN A1144 9082 18283 8223 501 145 1854 C ATOM 2629 O ASN A1144 26.339 14.617 45.591 1.00 92.98 O ANISOU 2629 O ASN A1144 9144 17952 8233 485 110 1855 O ATOM 2630 CB ASN A1144 25.965 16.011 48.431 1.00 91.93 C ANISOU 2630 CB ASN A1144 8540 18725 7663 675 89 1691 C ATOM 2631 CG ASN A1144 25.171 16.009 49.718 1.00111.65 C ANISOU 2631 CG ASN A1144 10740 21700 9982 751 62 1760 C ATOM 2632 OD1 ASN A1144 24.885 14.964 50.322 1.00105.69 O ANISOU 2632 OD1 ASN A1144 9765 21163 9230 716 72 2027 O ATOM 2633 ND2 ASN A1144 24.766 17.192 50.148 1.00103.29 N ANISOU 2633 ND2 ASN A1144 9661 20820 8767 861 24 1522 N ATOM 2634 N ARG A1145 28.390 15.001 46.493 1.00 89.24 N ANISOU 2634 N ARG A1145 8611 17606 7689 471 199 1778 N ATOM 2635 CA ARG A1145 29.110 15.123 45.226 1.00 87.51 C ANISOU 2635 CA ARG A1145 8669 16970 7612 419 221 1695 C ATOM 2636 C ARG A1145 29.094 13.760 44.523 1.00 90.10 C ANISOU 2636 C ARG A1145 9029 17088 8117 330 235 1925 C ATOM 2637 O ARG A1145 28.599 13.668 43.398 1.00 88.98 O ANISOU 2637 O ARG A1145 9069 16662 8078 314 206 1894 O ATOM 2638 CB ARG A1145 30.545 15.646 45.478 1.00 87.23 C ANISOU 2638 CB ARG A1145 8680 16911 7553 409 274 1592 C ATOM 2639 CG ARG A1145 31.351 16.028 44.233 1.00 93.57 C ANISOU 2639 CG ARG A1145 9765 17314 8474 373 295 1474 C ATOM 2640 CD ARG A1145 32.142 14.889 43.607 1.00100.07 C ANISOU 2640 CD ARG A1145 10653 17913 9456 278 347 1659 C ATOM 2641 NE ARG A1145 32.760 15.288 42.339 1.00104.04 N ANISOU 2641 NE ARG A1145 11426 18047 10059 256 359 1541 N ATOM 2642 CZ ARG A1145 33.923 15.923 42.229 1.00114.71 C ANISOU 2642 CZ ARG A1145 12876 19303 11406 251 395 1433 C ATOM 2643 NH1 ARG A1145 34.592 16.293 43.314 1.00 98.13 N ANISOU 2643 NH1 ARG A1145 10638 17443 9205 268 420 1404 N ATOM 2644 NH2 ARG A1145 34.401 16.238 41.033 1.00102.23 N ANISOU 2644 NH2 ARG A1145 11530 17397 9917 232 403 1346 N ATOM 2645 N ALA A1146 29.545 12.697 45.227 1.00 86.49 N ANISOU 2645 N ALA A1146 8377 16792 7695 276 271 2158 N ATOM 2646 CA ALA A1146 29.567 11.321 44.724 1.00 85.75 C ANISOU 2646 CA ALA A1146 8274 16529 7780 192 277 2393 C ATOM 2647 C ALA A1146 28.159 10.819 44.424 1.00 89.02 C ANISOU 2647 C ALA A1146 8646 16939 8240 198 208 2493 C ATOM 2648 O ALA A1146 27.965 10.143 43.415 1.00 87.85 O ANISOU 2648 O ALA A1146 8624 16502 8252 148 188 2562 O ATOM 2649 CB ALA A1146 30.236 10.405 45.735 1.00 87.17 C ANISOU 2649 CB ALA A1146 8214 16936 7971 142 321 2621 C ATOM 2650 N LYS A1147 27.173 11.192 45.285 1.00 85.93 N ANISOU 2650 N LYS A1147 8079 16869 7701 264 167 2491 N ATOM 2651 CA LYS A1147 25.752 10.817 45.190 1.00 85.72 C ANISOU 2651 CA LYS A1147 7979 16903 7687 281 98 2591 C ATOM 2652 C LYS A1147 25.197 11.150 43.795 1.00 86.16 C ANISOU 2652 C LYS A1147 8308 16596 7831 283 59 2450 C ATOM 2653 O LYS A1147 24.548 10.305 43.178 1.00 85.44 O ANISOU 2653 O LYS A1147 8240 16351 7874 240 19 2586 O ATOM 2654 CB LYS A1147 24.932 11.544 46.287 1.00 89.51 C ANISOU 2654 CB LYS A1147 8267 17786 7957 374 68 2533 C ATOM 2655 CG LYS A1147 23.479 11.079 46.458 1.00107.00 C ANISOU 2655 CG LYS A1147 10341 20153 10161 395 0 2682 C ATOM 2656 CD LYS A1147 23.370 9.646 47.018 1.00119.10 C ANISOU 2656 CD LYS A1147 11622 21846 11785 328 -5 3024 C ATOM 2657 CE LYS A1147 21.942 9.181 47.213 1.00132.62 C ANISOU 2657 CE LYS A1147 13175 23730 13486 349 -77 3188 C ATOM 2658 NZ LYS A1147 21.183 9.128 45.933 1.00141.89 N ANISOU 2658 NZ LYS A1147 14564 24562 14785 330 -131 3141 N ATOM 2659 N ARG A1148 25.501 12.355 43.292 1.00 80.22 N ANISOU 2659 N ARG A1148 7757 15708 7015 329 70 2182 N ATOM 2660 CA ARG A1148 25.075 12.809 41.975 1.00 78.52 C ANISOU 2660 CA ARG A1148 7803 15163 6868 335 40 2031 C ATOM 2661 C ARG A1148 25.803 12.049 40.864 1.00 82.30 C ANISOU 2661 C ARG A1148 8455 15279 7534 256 64 2090 C ATOM 2662 O ARG A1148 25.174 11.703 39.863 1.00 81.59 O ANISOU 2662 O ARG A1148 8490 14962 7550 235 25 2109 O ATOM 2663 CB ARG A1148 25.311 14.312 41.820 1.00 76.01 C ANISOU 2663 CB ARG A1148 7629 14812 6441 403 45 1745 C ATOM 2664 CG ARG A1148 24.397 15.167 42.672 1.00 79.44 C ANISOU 2664 CG ARG A1148 7938 15543 6702 495 2 1638 C ATOM 2665 CD ARG A1148 24.629 16.645 42.441 1.00 79.64 C ANISOU 2665 CD ARG A1148 8108 15505 6647 560 -4 1351 C ATOM 2666 NE ARG A1148 25.941 17.083 42.911 1.00 83.11 N ANISOU 2666 NE ARG A1148 8522 16012 7043 560 46 1276 N ATOM 2667 CZ ARG A1148 26.180 17.515 44.145 1.00 98.67 C ANISOU 2667 CZ ARG A1148 10301 18321 8868 616 50 1234 C ATOM 2668 NH1 ARG A1148 25.203 17.553 45.045 1.00 85.26 N ANISOU 2668 NH1 ARG A1148 8413 16937 7047 680 10 1264 N ATOM 2669 NH2 ARG A1148 27.397 17.905 44.492 1.00 88.44 N ANISOU 2669 NH2 ARG A1148 8996 17062 7543 611 92 1164 N ATOM 2670 N VAL A1149 27.118 11.787 41.042 1.00 78.96 N ANISOU 2670 N VAL A1149 8037 14813 7150 215 128 2120 N ATOM 2671 CA VAL A1149 27.960 11.073 40.067 1.00 78.07 C ANISOU 2671 CA VAL A1149 8076 14381 7205 147 159 2171 C ATOM 2672 C VAL A1149 27.460 9.612 39.927 1.00 83.44 C ANISOU 2672 C VAL A1149 8654 15011 8038 87 125 2417 C ATOM 2673 O VAL A1149 27.295 9.125 38.807 1.00 82.21 O ANISOU 2673 O VAL A1149 8654 14564 8019 58 101 2420 O ATOM 2674 CB VAL A1149 29.462 11.129 40.470 1.00 81.32 C ANISOU 2674 CB VAL A1149 8477 14814 7609 120 234 2169 C ATOM 2675 CG1 VAL A1149 30.331 10.341 39.498 1.00 80.37 C ANISOU 2675 CG1 VAL A1149 8497 14382 7658 56 267 2232 C ATOM 2676 CG2 VAL A1149 29.951 12.569 40.561 1.00 80.73 C ANISOU 2676 CG2 VAL A1149 8506 14761 7405 176 255 1927 C ATOM 2677 N ILE A1150 27.184 8.948 41.063 1.00 82.08 N ANISOU 2677 N ILE A1150 8215 15130 7842 74 118 2618 N ATOM 2678 CA ILE A1150 26.698 7.568 41.133 1.00 82.89 C ANISOU 2678 CA ILE A1150 8173 15229 8093 17 78 2876 C ATOM 2679 C ILE A1150 25.277 7.475 40.497 1.00 88.53 C ANISOU 2679 C ILE A1150 8938 15852 8845 35 -5 2876 C ATOM 2680 O ILE A1150 25.013 6.506 39.777 1.00 88.22 O ANISOU 2680 O ILE A1150 8942 15595 8984 -15 -46 2989 O ATOM 2681 CB ILE A1150 26.715 7.093 42.611 1.00 86.86 C ANISOU 2681 CB ILE A1150 8356 16116 8530 9 90 3082 C ATOM 2682 CG1 ILE A1150 28.185 7.012 43.119 1.00 86.79 C ANISOU 2682 CG1 ILE A1150 8308 16150 8520 -24 172 3107 C ATOM 2683 CG2 ILE A1150 26.014 5.741 42.773 1.00 88.57 C ANISOU 2683 CG2 ILE A1150 8391 16367 8894 -43 31 3364 C ATOM 2684 CD1 ILE A1150 28.375 6.721 44.607 1.00 94.55 C ANISOU 2684 CD1 ILE A1150 8986 17530 9408 -26 198 3278 C ATOM 2685 N THR A1151 24.401 8.496 40.715 1.00 86.15 N ANISOU 2685 N THR A1151 8644 15702 8385 107 -32 2738 N ATOM 2686 CA THR A1151 23.036 8.548 40.145 1.00 86.33 C ANISOU 2686 CA THR A1151 8721 15656 8424 129 -108 2723 C ATOM 2687 C THR A1151 23.119 8.623 38.599 1.00 90.04 C ANISOU 2687 C THR A1151 9482 15716 9013 111 -119 2586 C ATOM 2688 O THR A1151 22.260 8.068 37.911 1.00 89.38 O ANISOU 2688 O THR A1151 9444 15479 9036 90 -180 2652 O ATOM 2689 CB THR A1151 22.243 9.746 40.730 1.00 94.00 C ANISOU 2689 CB THR A1151 9647 16878 9190 217 -124 2579 C ATOM 2690 OG1 THR A1151 22.238 9.659 42.155 1.00 95.21 O ANISOU 2690 OG1 THR A1151 9524 17426 9225 241 -111 2700 O ATOM 2691 CG2 THR A1151 20.798 9.810 40.230 1.00 91.99 C ANISOU 2691 CG2 THR A1151 9430 16581 8941 242 -200 2577 C ATOM 2692 N THR A1152 24.172 9.283 38.069 1.00 86.67 N ANISOU 2692 N THR A1152 9242 15122 8567 117 -61 2405 N ATOM 2693 CA THR A1152 24.413 9.429 36.631 1.00 85.80 C ANISOU 2693 CA THR A1152 9400 14649 8550 105 -62 2269 C ATOM 2694 C THR A1152 24.925 8.068 36.077 1.00 89.00 C ANISOU 2694 C THR A1152 9819 14841 9157 34 -64 2425 C ATOM 2695 O THR A1152 24.534 7.697 34.971 1.00 88.10 O ANISOU 2695 O THR A1152 9850 14469 9154 19 -104 2400 O ATOM 2696 CB THR A1152 25.384 10.601 36.377 1.00 96.10 C ANISOU 2696 CB THR A1152 10865 15884 9764 138 -3 2049 C ATOM 2697 OG1 THR A1152 24.763 11.802 36.844 1.00 96.41 O ANISOU 2697 OG1 THR A1152 10890 16100 9643 207 -20 1903 O ATOM 2698 CG2 THR A1152 25.733 10.780 34.907 1.00 94.90 C ANISOU 2698 CG2 THR A1152 10978 15379 9700 127 3 1921 C ATOM 2699 N PHE A1153 25.745 7.310 36.855 1.00 85.60 N ANISOU 2699 N PHE A1153 9228 14522 8775 -8 -26 2586 N ATOM 2700 CA PHE A1153 26.190 5.973 36.426 1.00 85.31 C ANISOU 2700 CA PHE A1153 9179 14295 8941 -73 -36 2743 C ATOM 2701 C PHE A1153 25.038 4.970 36.493 1.00 88.66 C ANISOU 2701 C PHE A1153 9468 14736 9483 -101 -123 2933 C ATOM 2702 O PHE A1153 24.999 4.036 35.691 1.00 88.29 O ANISOU 2702 O PHE A1153 9486 14443 9618 -140 -165 2995 O ATOM 2703 CB PHE A1153 27.379 5.446 37.245 1.00 87.54 C ANISOU 2703 CB PHE A1153 9320 14690 9252 -113 28 2871 C ATOM 2704 CG PHE A1153 28.719 6.012 36.848 1.00 88.60 C ANISOU 2704 CG PHE A1153 9617 14694 9352 -108 107 2722 C ATOM 2705 CD1 PHE A1153 29.380 5.547 35.717 1.00 91.46 C ANISOU 2705 CD1 PHE A1153 10162 14739 9849 -131 119 2675 C ATOM 2706 CD2 PHE A1153 29.369 6.934 37.656 1.00 90.99 C ANISOU 2706 CD2 PHE A1153 9872 15204 9497 -81 169 2644 C ATOM 2707 CE1 PHE A1153 30.632 6.055 35.357 1.00 91.82 C ANISOU 2707 CE1 PHE A1153 10349 14677 9862 -126 192 2554 C ATOM 2708 CE2 PHE A1153 30.627 7.434 37.302 1.00 93.36 C ANISOU 2708 CE2 PHE A1153 10315 15383 9775 -81 238 2523 C ATOM 2709 CZ PHE A1153 31.251 6.988 36.157 1.00 90.88 C ANISOU 2709 CZ PHE A1153 10184 14756 9589 -104 251 2486 C ATOM 2710 N ARG A1154 24.094 5.174 37.432 1.00 84.74 N ANISOU 2710 N ARG A1154 8783 14530 8884 -77 -157 3021 N ATOM 2711 CA ARG A1154 22.927 4.310 37.587 1.00 84.76 C ANISOU 2711 CA ARG A1154 8638 14584 8984 -100 -245 3214 C ATOM 2712 C ARG A1154 21.922 4.555 36.444 1.00 86.62 C ANISOU 2712 C ARG A1154 9061 14600 9250 -79 -310 3094 C ATOM 2713 O ARG A1154 21.609 3.620 35.704 1.00 86.52 O ANISOU 2713 O ARG A1154 9089 14364 9420 -119 -371 3176 O ATOM 2714 CB ARG A1154 22.260 4.534 38.956 1.00 85.82 C ANISOU 2714 CB ARG A1154 8507 15123 8976 -72 -256 3341 C ATOM 2715 N THR A1155 21.456 5.813 36.278 1.00 81.16 N ANISOU 2715 N THR A1155 8485 13962 8388 -16 -297 2893 N ATOM 2716 CA THR A1155 20.464 6.186 35.263 1.00 79.84 C ANISOU 2716 CA THR A1155 8489 13620 8226 9 -353 2773 C ATOM 2717 C THR A1155 21.081 6.235 33.858 1.00 81.73 C ANISOU 2717 C THR A1155 8999 13498 8557 -2 -336 2612 C ATOM 2718 O THR A1155 20.596 5.554 32.951 1.00 81.38 O ANISOU 2718 O THR A1155 9038 13230 8651 -27 -396 2640 O ATOM 2719 CB THR A1155 19.823 7.552 35.591 1.00 85.59 C ANISOU 2719 CB THR A1155 9241 14534 8745 82 -344 2613 C ATOM 2720 OG1 THR A1155 20.842 8.550 35.670 1.00 83.52 O ANISOU 2720 OG1 THR A1155 9079 14283 8370 114 -267 2428 O ATOM 2721 CG2 THR A1155 19.013 7.533 36.878 1.00 85.07 C ANISOU 2721 CG2 THR A1155 8912 14835 8575 108 -372 2760 C ATOM 2722 N GLY A1156 22.125 7.043 33.696 1.00 76.72 N ANISOU 2722 N GLY A1156 8490 12819 7840 19 -260 2446 N ATOM 2723 CA GLY A1156 22.765 7.272 32.409 1.00 75.32 C ANISOU 2723 CA GLY A1156 8564 12337 7717 20 -236 2283 C ATOM 2724 C GLY A1156 22.242 8.537 31.769 1.00 77.69 C ANISOU 2724 C GLY A1156 9035 12585 7898 73 -239 2072 C ATOM 2725 O GLY A1156 22.363 8.722 30.555 1.00 76.49 O ANISOU 2725 O GLY A1156 9087 12183 7792 77 -243 1949 O ATOM 2726 N THR A1157 21.645 9.419 32.595 1.00 73.99 N ANISOU 2726 N THR A1157 8474 12363 7276 117 -241 2032 N ATOM 2727 CA THR A1157 21.074 10.686 32.152 1.00 73.02 C ANISOU 2727 CA THR A1157 8485 12222 7038 172 -249 1839 C ATOM 2728 C THR A1157 21.439 11.807 33.149 1.00 75.78 C ANISOU 2728 C THR A1157 8761 12811 7220 221 -206 1738 C ATOM 2729 O THR A1157 21.841 11.533 34.286 1.00 75.78 O ANISOU 2729 O THR A1157 8576 13038 7179 216 -181 1841 O ATOM 2730 CB THR A1157 19.551 10.564 31.976 1.00 82.38 C ANISOU 2730 CB THR A1157 9638 13439 8225 184 -327 1886 C ATOM 2731 OG1 THR A1157 19.067 11.757 31.365 1.00 83.15 O ANISOU 2731 OG1 THR A1157 9888 13472 8231 233 -334 1693 O ATOM 2732 CG2 THR A1157 18.808 10.284 33.287 1.00 81.26 C ANISOU 2732 CG2 THR A1157 9240 13617 8019 195 -357 2046 C ATOM 2733 N TRP A1158 21.270 13.070 32.715 1.00 71.03 N ANISOU 2733 N TRP A1158 8300 12160 6530 270 -203 1536 N ATOM 2734 CA TRP A1158 21.603 14.247 33.512 1.00 70.47 C ANISOU 2734 CA TRP A1158 8184 12277 6314 324 -174 1404 C ATOM 2735 C TRP A1158 20.480 14.602 34.507 1.00 74.27 C ANISOU 2735 C TRP A1158 8493 13051 6675 376 -216 1426 C ATOM 2736 O TRP A1158 20.532 15.675 35.112 1.00 73.99 O ANISOU 2736 O TRP A1158 8424 13175 6515 434 -208 1290 O ATOM 2737 CB TRP A1158 21.884 15.454 32.602 1.00 68.38 C ANISOU 2737 CB TRP A1158 8133 11823 6023 355 -164 1184 C ATOM 2738 CG TRP A1158 22.969 15.241 31.585 1.00 68.46 C ANISOU 2738 CG TRP A1158 8316 11565 6132 316 -123 1152 C ATOM 2739 CD1 TRP A1158 22.809 15.045 30.244 1.00 70.77 C ANISOU 2739 CD1 TRP A1158 8787 11591 6513 297 -138 1118 C ATOM 2740 CD2 TRP A1158 24.376 15.120 31.843 1.00 68.02 C ANISOU 2740 CD2 TRP A1158 8256 11493 6093 292 -61 1162 C ATOM 2741 NE1 TRP A1158 24.034 14.880 29.640 1.00 69.64 N ANISOU 2741 NE1 TRP A1158 8753 11275 6432 270 -89 1097 N ATOM 2742 CE2 TRP A1158 25.012 14.903 30.600 1.00 71.16 C ANISOU 2742 CE2 TRP A1158 8839 11612 6587 264 -41 1129 C ATOM 2743 CE3 TRP A1158 25.165 15.196 33.003 1.00 69.50 C ANISOU 2743 CE3 TRP A1158 8301 11886 6219 295 -20 1195 C ATOM 2744 CZ2 TRP A1158 26.399 14.751 30.487 1.00 70.03 C ANISOU 2744 CZ2 TRP A1158 8741 11386 6480 239 19 1133 C ATOM 2745 CZ3 TRP A1158 26.538 15.055 32.886 1.00 70.48 C ANISOU 2745 CZ3 TRP A1158 8475 11920 6384 265 39 1199 C ATOM 2746 CH2 TRP A1158 27.142 14.843 31.641 1.00 70.38 C ANISOU 2746 CH2 TRP A1158 8649 11626 6468 238 58 1169 C ATOM 2747 N ASP A1159 19.493 13.696 34.715 1.00 70.94 N ANISOU 2747 N ASP A1159 7952 12708 6293 357 -264 1598 N ATOM 2748 CA ASP A1159 18.400 13.910 35.673 1.00 71.31 C ANISOU 2748 CA ASP A1159 7817 13051 6226 406 -306 1648 C ATOM 2749 C ASP A1159 18.915 13.667 37.103 1.00 74.43 C ANISOU 2749 C ASP A1159 7972 13768 6541 416 -276 1755 C ATOM 2750 O ASP A1159 18.405 12.816 37.834 1.00 74.73 O ANISOU 2750 O ASP A1159 7806 14007 6581 403 -302 1955 O ATOM 2751 CB ASP A1159 17.183 13.014 35.353 1.00 73.72 C ANISOU 2751 CB ASP A1159 8076 13322 6610 379 -372 1810 C ATOM 2752 CG ASP A1159 16.448 13.350 34.066 1.00 84.31 C ANISOU 2752 CG ASP A1159 9629 14401 8003 381 -410 1702 C ATOM 2753 OD1 ASP A1159 16.605 14.493 33.569 1.00 84.55 O ANISOU 2753 OD1 ASP A1159 9816 14335 7974 420 -392 1493 O ATOM 2754 OD2 ASP A1159 15.632 12.513 33.613 1.00 90.27 O ANISOU 2754 OD2 ASP A1159 10378 15065 8854 346 -463 1831 O ATOM 2755 N ALA A1160 19.944 14.432 37.476 1.00 69.91 N ANISOU 2755 N ALA A1160 7422 13243 5899 439 -223 1623 N ATOM 2756 CA ALA A1160 20.617 14.420 38.768 1.00 70.08 C ANISOU 2756 CA ALA A1160 7243 13556 5830 454 -186 1677 C ATOM 2757 C ALA A1160 21.288 15.769 39.018 1.00 73.60 C ANISOU 2757 C ALA A1160 7754 14045 6164 511 -156 1441 C ATOM 2758 O ALA A1160 21.579 16.107 40.167 1.00 74.03 O ANISOU 2758 O ALA A1160 7641 14388 6099 552 -140 1426 O ATOM 2759 CB ALA A1160 21.638 13.289 38.820 1.00 70.66 C ANISOU 2759 CB ALA A1160 7268 13556 6022 374 -143 1851 C ATOM 2760 N TYR A1161 21.502 16.554 37.929 1.00 68.82 N ANISOU 2760 N TYR A1161 7390 13159 5601 517 -156 1257 N ATOM 2761 CA TYR A1161 22.140 17.874 37.942 1.00 68.09 C ANISOU 2761 CA TYR A1161 7393 13040 5439 565 -141 1026 C ATOM 2762 C TYR A1161 21.156 18.959 37.457 1.00 74.91 C ANISOU 2762 C TYR A1161 8359 13850 6253 629 -194 846 C ATOM 2763 O TYR A1161 20.999 19.978 38.136 1.00 75.09 O ANISOU 2763 O TYR A1161 8316 14054 6159 704 -213 697 O ATOM 2764 CB TYR A1161 23.415 17.869 37.071 1.00 66.98 C ANISOU 2764 CB TYR A1161 7436 12608 5404 511 -93 981 C ATOM 2765 CG TYR A1161 24.490 16.944 37.602 1.00 66.81 C ANISOU 2765 CG TYR A1161 7315 12647 5424 456 -37 1133 C ATOM 2766 CD1 TYR A1161 25.435 17.396 38.517 1.00 68.65 C ANISOU 2766 CD1 TYR A1161 7459 13044 5579 474 0 1078 C ATOM 2767 CD2 TYR A1161 24.541 15.607 37.217 1.00 66.73 C ANISOU 2767 CD2 TYR A1161 7288 12532 5534 386 -26 1334 C ATOM 2768 CE1 TYR A1161 26.400 16.541 39.041 1.00 68.34 C ANISOU 2768 CE1 TYR A1161 7318 13074 5574 422 54 1227 C ATOM 2769 CE2 TYR A1161 25.498 14.741 37.740 1.00 67.25 C ANISOU 2769 CE2 TYR A1161 7250 12658 5644 336 23 1481 C ATOM 2770 CZ TYR A1161 26.432 15.215 38.646 1.00 72.55 C ANISOU 2770 CZ TYR A1161 7836 13500 6230 352 67 1430 C ATOM 2771 OH TYR A1161 27.379 14.373 39.175 1.00 71.47 O ANISOU 2771 OH TYR A1161 7592 13429 6136 301 118 1581 O ATOM 2772 N ALA A 245 20.489 18.734 36.302 1.00 73.09 N ANISOU 2772 N ALA A 245 8282 13378 6112 602 -220 859 N ATOM 2773 CA ALA A 245 19.507 19.667 35.742 1.00 73.88 C ANISOU 2773 CA ALA A 245 8483 13408 6180 654 -270 712 C ATOM 2774 C ALA A 245 18.259 18.905 35.262 1.00 81.39 C ANISOU 2774 C ALA A 245 9430 14320 7175 633 -312 845 C ATOM 2775 O ALA A 245 18.385 17.921 34.526 1.00 80.78 O ANISOU 2775 O ALA A 245 9418 14058 7215 565 -303 975 O ATOM 2776 CB ALA A 245 20.122 20.466 34.605 1.00 73.60 C ANISOU 2776 CB ALA A 245 8680 13072 6215 644 -260 551 C ATOM 2777 N SER A 246 17.056 19.358 35.717 1.00 80.87 N ANISOU 2777 N SER A 246 9278 14435 7014 696 -361 810 N ATOM 2778 CA SER A 246 15.726 18.772 35.465 1.00 81.72 C ANISOU 2778 CA SER A 246 9350 14562 7137 690 -409 933 C ATOM 2779 C SER A 246 15.455 18.532 33.960 1.00 86.60 C ANISOU 2779 C SER A 246 10187 14834 7883 639 -424 927 C ATOM 2780 O SER A 246 15.238 17.385 33.567 1.00 85.74 O ANISOU 2780 O SER A 246 10074 14633 7872 579 -434 1096 O ATOM 2781 CB SER A 246 14.637 19.679 36.030 1.00 85.88 C ANISOU 2781 CB SER A 246 9791 15308 7530 780 -454 834 C ATOM 2782 N ARG A 247 15.458 19.598 33.132 1.00 84.66 N ANISOU 2782 N ARG A 247 10120 14406 7641 664 -429 735 N ATOM 2783 CA ARG A 247 15.229 19.470 31.690 1.00 84.72 C ANISOU 2783 CA ARG A 247 10331 14103 7755 622 -441 717 C ATOM 2784 C ARG A 247 16.576 19.282 30.955 1.00 89.74 C ANISOU 2784 C ARG A 247 11106 14503 8487 569 -391 694 C ATOM 2785 O ARG A 247 17.123 20.234 30.383 1.00 88.82 O ANISOU 2785 O ARG A 247 11136 14229 8383 581 -377 540 O ATOM 2786 CB ARG A 247 14.454 20.680 31.106 1.00 85.45 C ANISOU 2786 CB ARG A 247 10538 14121 7809 673 -475 543 C ATOM 2787 CG ARG A 247 12.964 20.808 31.478 1.00 97.23 C ANISOU 2787 CG ARG A 247 11936 15783 9225 720 -530 570 C ATOM 2788 CD ARG A 247 12.652 21.333 32.874 1.00107.59 C ANISOU 2788 CD ARG A 247 13051 17431 10396 798 -542 532 C ATOM 2789 NE ARG A 247 11.208 21.510 33.053 1.00114.13 N ANISOU 2789 NE ARG A 247 13811 18397 11157 845 -595 554 N ATOM 2790 CZ ARG A 247 10.640 22.047 34.129 1.00127.67 C ANISOU 2790 CZ ARG A 247 15363 20407 12738 927 -618 508 C ATOM 2791 NH1 ARG A 247 11.389 22.488 35.133 1.00115.31 N ANISOU 2791 NH1 ARG A 247 13687 19032 11093 973 -595 427 N ATOM 2792 NH2 ARG A 247 9.321 22.169 34.199 1.00113.92 N ANISOU 2792 NH2 ARG A 247 13568 18778 10940 968 -665 537 N ATOM 2793 N SER A 248 17.115 18.049 31.002 1.00 87.55 N ANISOU 2793 N SER A 248 10773 14209 8282 512 -366 854 N ATOM 2794 CA SER A 248 18.384 17.692 30.356 1.00 87.30 C ANISOU 2794 CA SER A 248 10856 13973 8342 463 -318 854 C ATOM 2795 C SER A 248 18.339 16.249 29.823 1.00 92.50 C ANISOU 2795 C SER A 248 11513 14511 9123 398 -325 1029 C ATOM 2796 O SER A 248 19.347 15.736 29.325 1.00 91.99 O ANISOU 2796 O SER A 248 11494 14322 9135 357 -285 1069 O ATOM 2797 CB SER A 248 19.551 17.868 31.320 1.00 90.75 C ANISOU 2797 CB SER A 248 11201 14548 8730 471 -268 834 C ATOM 2798 OG SER A 248 19.714 19.232 31.667 1.00 98.74 O ANISOU 2798 OG SER A 248 12239 15625 9654 530 -268 651 O ATOM 2799 N SER A 249 17.160 15.610 29.914 1.00 89.98 N ANISOU 2799 N SER A 249 11143 14219 8826 391 -380 1129 N ATOM 2800 CA SER A 249 16.901 14.267 29.390 1.00 89.97 C ANISOU 2800 CA SER A 249 11138 14091 8955 335 -409 1287 C ATOM 2801 C SER A 249 15.859 14.349 28.301 1.00 93.13 C ANISOU 2801 C SER A 249 11668 14325 9392 335 -461 1247 C ATOM 2802 O SER A 249 16.038 13.778 27.227 1.00 92.26 O ANISOU 2802 O SER A 249 11688 13979 9388 300 -469 1249 O ATOM 2803 CB SER A 249 16.453 13.323 30.501 1.00 94.39 C ANISOU 2803 CB SER A 249 11467 14878 9521 319 -435 1490 C ATOM 2804 OG SER A 249 16.251 12.002 30.022 1.00102.96 O ANISOU 2804 OG SER A 249 12538 15829 10752 262 -473 1647 O ATOM 2805 N GLU A 250 14.770 15.090 28.581 1.00 89.61 N ANISOU 2805 N GLU A 250 11186 14008 8852 380 -496 1200 N ATOM 2806 CA GLU A 250 13.665 15.323 27.661 1.00 89.04 C ANISOU 2806 CA GLU A 250 11225 13814 8794 387 -546 1156 C ATOM 2807 C GLU A 250 14.162 16.177 26.486 1.00 91.26 C ANISOU 2807 C GLU A 250 11723 13868 9083 395 -518 976 C ATOM 2808 O GLU A 250 13.831 15.874 25.344 1.00 90.48 O ANISOU 2808 O GLU A 250 11756 13566 9057 371 -543 965 O ATOM 2809 CB GLU A 250 12.468 15.979 28.388 1.00 90.98 C ANISOU 2809 CB GLU A 250 11360 14284 8922 440 -583 1148 C ATOM 2810 CG GLU A 250 12.737 17.321 29.058 1.00101.15 C ANISOU 2810 CG GLU A 250 12619 15732 10080 505 -552 994 C ATOM 2811 CD GLU A 250 11.559 17.905 29.812 1.00116.09 C ANISOU 2811 CD GLU A 250 14388 17864 11856 566 -591 986 C ATOM 2812 OE1 GLU A 250 11.090 18.995 29.415 1.00107.11 O ANISOU 2812 OE1 GLU A 250 13344 16686 10668 609 -605 837 O ATOM 2813 OE2 GLU A 250 11.061 17.242 30.752 1.00106.89 O ANISOU 2813 OE2 GLU A 250 13029 16928 10656 570 -611 1137 O ATOM 2814 N ASN A 251 15.028 17.179 26.767 1.00 87.00 N ANISOU 2814 N ASN A 251 11212 13365 8478 426 -470 846 N ATOM 2815 CA ASN A 251 15.650 18.048 25.761 1.00 85.82 C ANISOU 2815 CA ASN A 251 11247 13021 8340 433 -443 690 C ATOM 2816 C ASN A 251 16.685 17.266 24.954 1.00 87.65 C ANISOU 2816 C ASN A 251 11577 13055 8673 387 -409 725 C ATOM 2817 O ASN A 251 16.872 17.530 23.764 1.00 86.32 O ANISOU 2817 O ASN A 251 11570 12685 8542 380 -403 646 O ATOM 2818 CB ASN A 251 16.302 19.266 26.429 1.00 87.86 C ANISOU 2818 CB ASN A 251 11482 13390 8513 479 -412 558 C ATOM 2819 CG ASN A 251 15.367 20.147 27.232 1.00116.16 C ANISOU 2819 CG ASN A 251 14977 17166 11995 538 -447 490 C ATOM 2820 OD1 ASN A 251 14.133 20.073 27.134 1.00113.02 O ANISOU 2820 OD1 ASN A 251 14568 16795 11581 550 -493 518 O ATOM 2821 ND2 ASN A 251 15.946 21.041 28.014 1.00108.63 N ANISOU 2821 ND2 ASN A 251 13963 16342 10970 581 -429 389 N ATOM 2822 N VAL A 252 17.358 16.301 25.617 1.00 83.61 N ANISOU 2822 N VAL A 252 10957 12611 8201 357 -387 845 N ATOM 2823 CA VAL A 252 18.354 15.417 25.017 1.00 82.72 C ANISOU 2823 CA VAL A 252 10908 12333 8187 316 -357 894 C ATOM 2824 C VAL A 252 17.660 14.418 24.084 1.00 85.89 C ANISOU 2824 C VAL A 252 11367 12576 8692 284 -406 966 C ATOM 2825 O VAL A 252 18.208 14.081 23.032 1.00 85.05 O ANISOU 2825 O VAL A 252 11387 12271 8657 268 -394 935 O ATOM 2826 CB VAL A 252 19.175 14.691 26.103 1.00 86.80 C ANISOU 2826 CB VAL A 252 11273 12989 8719 294 -323 1009 C ATOM 2827 N ALA A 253 16.446 13.960 24.468 1.00 82.34 N ANISOU 2827 N ALA A 253 10820 12219 8246 281 -466 1060 N ATOM 2828 CA ALA A 253 15.637 13.024 23.683 1.00 81.98 C ANISOU 2828 CA ALA A 253 10812 12036 8302 252 -528 1133 C ATOM 2829 C ALA A 253 15.055 13.712 22.460 1.00 84.45 C ANISOU 2829 C ALA A 253 11299 12193 8597 269 -547 1006 C ATOM 2830 O ALA A 253 14.914 13.072 21.418 1.00 84.00 O ANISOU 2830 O ALA A 253 11339 11950 8628 248 -576 1007 O ATOM 2831 CB ALA A 253 14.521 12.440 24.537 1.00 83.43 C ANISOU 2831 CB ALA A 253 10825 12387 8490 243 -587 1283 C ATOM 2832 N LEU A 254 14.718 15.017 22.585 1.00 80.28 N ANISOU 2832 N LEU A 254 10803 11740 7959 309 -535 893 N ATOM 2833 CA LEU A 254 14.187 15.827 21.481 1.00 79.58 C ANISOU 2833 CA LEU A 254 10869 11519 7847 327 -548 772 C ATOM 2834 C LEU A 254 15.277 16.048 20.433 1.00 81.31 C ANISOU 2834 C LEU A 254 11242 11553 8099 324 -504 677 C ATOM 2835 O LEU A 254 15.038 15.764 19.262 1.00 80.61 O ANISOU 2835 O LEU A 254 11270 11298 8062 313 -525 653 O ATOM 2836 CB LEU A 254 13.624 17.178 21.976 1.00 79.82 C ANISOU 2836 CB LEU A 254 10880 11682 7765 373 -547 678 C ATOM 2837 CG LEU A 254 12.373 17.132 22.868 1.00 85.37 C ANISOU 2837 CG LEU A 254 11445 12575 8416 390 -595 752 C ATOM 2838 CD1 LEU A 254 12.207 18.411 23.659 1.00 85.83 C ANISOU 2838 CD1 LEU A 254 11449 12803 8361 445 -582 653 C ATOM 2839 CD2 LEU A 254 11.128 16.768 22.089 1.00 87.71 C ANISOU 2839 CD2 LEU A 254 11796 12781 8747 377 -656 788 C ATOM 2840 N LEU A 255 16.498 16.475 20.863 1.00 76.14 N ANISOU 2840 N LEU A 255 10579 10936 7416 333 -444 634 N ATOM 2841 CA LEU A 255 17.649 16.692 19.974 1.00 74.46 C ANISOU 2841 CA LEU A 255 10494 10570 7227 332 -397 559 C ATOM 2842 C LEU A 255 17.835 15.486 19.054 1.00 76.24 C ANISOU 2842 C LEU A 255 10781 10635 7551 304 -410 611 C ATOM 2843 O LEU A 255 17.859 15.662 17.842 1.00 75.42 O ANISOU 2843 O LEU A 255 10812 10382 7461 311 -412 541 O ATOM 2844 CB LEU A 255 18.934 16.965 20.773 1.00 74.30 C ANISOU 2844 CB LEU A 255 10418 10632 7180 336 -338 552 C ATOM 2845 N LYS A 256 17.844 14.262 19.622 1.00 72.09 N ANISOU 2845 N LYS A 256 10149 10146 7097 276 -430 736 N ATOM 2846 CA LYS A 256 17.967 13.016 18.862 1.00 71.70 C ANISOU 2846 CA LYS A 256 10139 9945 7160 252 -457 787 C ATOM 2847 C LYS A 256 16.838 12.903 17.820 1.00 74.37 C ANISOU 2847 C LYS A 256 10564 10169 7523 254 -519 754 C ATOM 2848 O LYS A 256 17.137 12.806 16.633 1.00 74.02 O ANISOU 2848 O LYS A 256 10647 9969 7507 262 -518 683 O ATOM 2849 CB LYS A 256 17.960 11.784 19.796 1.00 74.77 C ANISOU 2849 CB LYS A 256 10370 10407 7633 219 -481 943 C ATOM 2850 CG LYS A 256 19.168 11.659 20.745 1.00 89.71 C ANISOU 2850 CG LYS A 256 12170 12394 9520 210 -419 992 C ATOM 2851 CD LYS A 256 20.500 11.355 20.024 1.00 99.18 C ANISOU 2851 CD LYS A 256 13470 13448 10765 211 -370 943 C ATOM 2852 CE LYS A 256 21.670 11.172 20.970 1.00109.02 C ANISOU 2852 CE LYS A 256 14623 14784 12015 198 -311 1005 C ATOM 2853 NZ LYS A 256 21.977 12.404 21.748 1.00116.24 N ANISOU 2853 NZ LYS A 256 15497 15860 12809 217 -263 957 N ATOM 2854 N THR A 257 15.562 13.005 18.259 1.00 69.69 N ANISOU 2854 N THR A 257 9903 9668 6908 251 -572 802 N ATOM 2855 CA THR A 257 14.357 12.904 17.421 1.00 68.81 C ANISOU 2855 CA THR A 257 9857 9472 6816 249 -637 787 C ATOM 2856 C THR A 257 14.327 14.023 16.349 1.00 70.82 C ANISOU 2856 C THR A 257 10267 9640 7000 277 -613 642 C ATOM 2857 O THR A 257 14.192 13.709 15.167 1.00 70.69 O ANISOU 2857 O THR A 257 10360 9475 7024 277 -636 596 O ATOM 2858 CB THR A 257 13.102 12.967 18.316 1.00 75.03 C ANISOU 2858 CB THR A 257 10521 10414 7573 245 -685 874 C ATOM 2859 OG1 THR A 257 13.101 11.817 19.164 1.00 74.98 O ANISOU 2859 OG1 THR A 257 10365 10476 7648 215 -715 1026 O ATOM 2860 CG2 THR A 257 11.795 13.007 17.518 1.00 72.78 C ANISOU 2860 CG2 THR A 257 10301 10058 7295 243 -750 860 C ATOM 2861 N VAL A 258 14.457 15.304 16.764 1.00 65.52 N ANISOU 2861 N VAL A 258 9599 9066 6230 302 -573 574 N ATOM 2862 CA VAL A 258 14.427 16.503 15.906 1.00 64.15 C ANISOU 2862 CA VAL A 258 9548 8831 5994 327 -553 451 C ATOM 2863 C VAL A 258 15.436 16.344 14.720 1.00 66.26 C ANISOU 2863 C VAL A 258 9941 8943 6294 331 -520 390 C ATOM 2864 O VAL A 258 15.076 16.673 13.585 1.00 65.44 O ANISOU 2864 O VAL A 258 9944 8740 6179 340 -533 326 O ATOM 2865 CB VAL A 258 14.718 17.784 16.746 1.00 67.69 C ANISOU 2865 CB VAL A 258 9953 9408 6359 353 -515 395 C ATOM 2866 CG1 VAL A 258 15.144 18.957 15.886 1.00 67.13 C ANISOU 2866 CG1 VAL A 258 10000 9256 6251 375 -487 279 C ATOM 2867 CG2 VAL A 258 13.519 18.158 17.615 1.00 67.64 C ANISOU 2867 CG2 VAL A 258 9845 9552 6303 365 -554 425 C ATOM 2868 N ILE A 259 16.644 15.793 14.971 1.00 62.17 N ANISOU 2868 N ILE A 259 9400 8412 5809 325 -478 414 N ATOM 2869 CA ILE A 259 17.651 15.566 13.922 1.00 61.52 C ANISOU 2869 CA ILE A 259 9421 8201 5750 335 -444 364 C ATOM 2870 C ILE A 259 17.155 14.445 12.957 1.00 65.00 C ANISOU 2870 C ILE A 259 9915 8515 6266 328 -497 374 C ATOM 2871 O ILE A 259 17.285 14.611 11.741 1.00 64.12 O ANISOU 2871 O ILE A 259 9916 8305 6143 348 -494 300 O ATOM 2872 CB ILE A 259 19.059 15.229 14.510 1.00 64.47 C ANISOU 2872 CB ILE A 259 9749 8602 6144 331 -388 397 C ATOM 2873 CG1 ILE A 259 19.578 16.393 15.384 1.00 64.26 C ANISOU 2873 CG1 ILE A 259 9681 8691 6045 341 -341 369 C ATOM 2874 CG2 ILE A 259 20.072 14.918 13.385 1.00 65.53 C ANISOU 2874 CG2 ILE A 259 9986 8609 6303 347 -356 351 C ATOM 2875 CD1 ILE A 259 20.920 16.158 16.103 1.00 69.92 C ANISOU 2875 CD1 ILE A 259 10339 9457 6772 335 -285 406 C ATOM 2876 N ILE A 260 16.561 13.341 13.492 1.00 61.81 N ANISOU 2876 N ILE A 260 9424 8121 5939 303 -551 466 N ATOM 2877 CA ILE A 260 16.057 12.213 12.679 1.00 61.99 C ANISOU 2877 CA ILE A 260 9483 8019 6052 295 -616 476 C ATOM 2878 C ILE A 260 14.968 12.733 11.706 1.00 66.98 C ANISOU 2878 C ILE A 260 10204 8601 6642 306 -655 410 C ATOM 2879 O ILE A 260 14.937 12.293 10.552 1.00 67.22 O ANISOU 2879 O ILE A 260 10325 8513 6701 320 -680 351 O ATOM 2880 CB ILE A 260 15.524 11.028 13.542 1.00 65.26 C ANISOU 2880 CB ILE A 260 9768 8457 6571 261 -677 604 C ATOM 2881 CG1 ILE A 260 16.501 10.683 14.680 1.00 65.85 C ANISOU 2881 CG1 ILE A 260 9729 8622 6670 247 -633 686 C ATOM 2882 CG2 ILE A 260 15.261 9.795 12.662 1.00 65.86 C ANISOU 2882 CG2 ILE A 260 9883 8377 6764 257 -745 601 C ATOM 2883 CD1 ILE A 260 15.996 9.705 15.715 1.00 74.16 C ANISOU 2883 CD1 ILE A 260 10624 9740 7814 211 -688 837 C ATOM 2884 N VAL A 261 14.117 13.707 12.160 1.00 63.10 N ANISOU 2884 N VAL A 261 9687 8209 6079 304 -659 414 N ATOM 2885 CA VAL A 261 13.064 14.344 11.340 1.00 62.31 C ANISOU 2885 CA VAL A 261 9664 8079 5933 312 -691 360 C ATOM 2886 C VAL A 261 13.726 14.934 10.082 1.00 65.05 C ANISOU 2886 C VAL A 261 10141 8341 6235 340 -651 251 C ATOM 2887 O VAL A 261 13.227 14.715 8.974 1.00 64.55 O ANISOU 2887 O VAL A 261 10158 8192 6177 347 -686 206 O ATOM 2888 CB VAL A 261 12.245 15.417 12.121 1.00 65.68 C ANISOU 2888 CB VAL A 261 10036 8637 6284 313 -690 373 C ATOM 2889 CG1 VAL A 261 11.188 16.069 11.232 1.00 65.28 C ANISOU 2889 CG1 VAL A 261 10063 8547 6193 319 -723 323 C ATOM 2890 CG2 VAL A 261 11.593 14.821 13.364 1.00 65.77 C ANISOU 2890 CG2 VAL A 261 9904 8759 6328 292 -728 490 C ATOM 2891 N LEU A 262 14.886 15.617 10.259 1.00 60.93 N ANISOU 2891 N LEU A 262 9631 7846 5672 356 -581 217 N ATOM 2892 CA LEU A 262 15.671 16.163 9.152 1.00 60.43 C ANISOU 2892 CA LEU A 262 9672 7719 5569 383 -539 136 C ATOM 2893 C LEU A 262 16.330 15.018 8.352 1.00 64.57 C ANISOU 2893 C LEU A 262 10242 8142 6149 396 -546 119 C ATOM 2894 O LEU A 262 16.317 15.055 7.115 1.00 65.08 O ANISOU 2894 O LEU A 262 10396 8138 6191 419 -553 54 O ATOM 2895 CB LEU A 262 16.745 17.159 9.653 1.00 59.92 C ANISOU 2895 CB LEU A 262 9595 7716 5457 394 -469 119 C ATOM 2896 CG LEU A 262 17.630 17.808 8.560 1.00 64.41 C ANISOU 2896 CG LEU A 262 10257 8233 5985 422 -425 55 C ATOM 2897 CD1 LEU A 262 16.856 18.833 7.747 1.00 64.27 C ANISOU 2897 CD1 LEU A 262 10299 8204 5918 430 -441 8 C ATOM 2898 CD2 LEU A 262 18.834 18.472 9.158 1.00 66.79 C ANISOU 2898 CD2 LEU A 262 10531 8581 6265 427 -365 58 C ATOM 2899 N SER A 263 16.884 13.999 9.060 1.00 59.65 N ANISOU 2899 N SER A 263 9551 7514 5597 384 -547 176 N ATOM 2900 CA SER A 263 17.572 12.854 8.450 1.00 59.17 C ANISOU 2900 CA SER A 263 9519 7358 5604 399 -557 158 C ATOM 2901 C SER A 263 16.660 12.097 7.490 1.00 60.75 C ANISOU 2901 C SER A 263 9766 7464 5852 405 -634 124 C ATOM 2902 O SER A 263 17.139 11.635 6.460 1.00 60.99 O ANISOU 2902 O SER A 263 9867 7416 5891 438 -638 54 O ATOM 2903 CB SER A 263 18.092 11.898 9.516 1.00 64.20 C ANISOU 2903 CB SER A 263 10055 8011 6328 377 -557 243 C ATOM 2904 OG SER A 263 19.033 12.524 10.374 1.00 74.84 O ANISOU 2904 OG SER A 263 11360 9442 7632 374 -485 269 O ATOM 2905 N VAL A 264 15.355 11.995 7.802 1.00 55.25 N ANISOU 2905 N VAL A 264 9030 6781 5181 376 -697 169 N ATOM 2906 CA VAL A 264 14.384 11.329 6.929 1.00 54.74 C ANISOU 2906 CA VAL A 264 9007 6628 5163 377 -778 139 C ATOM 2907 C VAL A 264 13.990 12.313 5.800 1.00 57.86 C ANISOU 2907 C VAL A 264 9507 7019 5458 402 -764 51 C ATOM 2908 O VAL A 264 13.919 11.901 4.641 1.00 57.76 O ANISOU 2908 O VAL A 264 9566 6929 5451 428 -794 -23 O ATOM 2909 CB VAL A 264 13.154 10.805 7.719 1.00 58.28 C ANISOU 2909 CB VAL A 264 9367 7097 5681 336 -854 237 C ATOM 2910 CG1 VAL A 264 12.090 10.222 6.791 1.00 58.40 C ANISOU 2910 CG1 VAL A 264 9428 7016 5747 335 -944 206 C ATOM 2911 CG2 VAL A 264 13.583 9.764 8.743 1.00 58.43 C ANISOU 2911 CG2 VAL A 264 9271 7123 5807 311 -871 337 C ATOM 2912 N PHE A 265 13.788 13.608 6.130 1.00 53.44 N ANISOU 2912 N PHE A 265 8948 6547 4810 396 -720 56 N ATOM 2913 CA PHE A 265 13.440 14.635 5.144 1.00 52.89 C ANISOU 2913 CA PHE A 265 8961 6481 4653 414 -703 -10 C ATOM 2914 C PHE A 265 14.492 14.687 4.018 1.00 57.21 C ANISOU 2914 C PHE A 265 9586 6988 5161 456 -661 -87 C ATOM 2915 O PHE A 265 14.130 14.556 2.843 1.00 57.39 O ANISOU 2915 O PHE A 265 9677 6968 5160 478 -688 -148 O ATOM 2916 CB PHE A 265 13.301 16.021 5.813 1.00 54.01 C ANISOU 2916 CB PHE A 265 9077 6718 4726 404 -660 9 C ATOM 2917 CG PHE A 265 12.930 17.166 4.885 1.00 55.39 C ANISOU 2917 CG PHE A 265 9323 6898 4825 418 -645 -44 C ATOM 2918 CD1 PHE A 265 11.601 17.505 4.667 1.00 58.44 C ANISOU 2918 CD1 PHE A 265 9719 7291 5195 403 -691 -39 C ATOM 2919 CD2 PHE A 265 13.914 17.934 4.268 1.00 57.20 C ANISOU 2919 CD2 PHE A 265 9598 7132 5003 444 -587 -86 C ATOM 2920 CE1 PHE A 265 11.260 18.572 3.826 1.00 59.00 C ANISOU 2920 CE1 PHE A 265 9845 7367 5203 413 -677 -79 C ATOM 2921 CE2 PHE A 265 13.569 18.993 3.421 1.00 59.65 C ANISOU 2921 CE2 PHE A 265 9959 7450 5254 453 -578 -119 C ATOM 2922 CZ PHE A 265 12.246 19.308 3.211 1.00 57.69 C ANISOU 2922 CZ PHE A 265 9720 7206 4995 437 -622 -116 C ATOM 2923 N ILE A 266 15.790 14.830 4.379 1.00 53.17 N ANISOU 2923 N ILE A 266 9059 6500 4642 470 -599 -81 N ATOM 2924 CA ILE A 266 16.877 14.946 3.403 1.00 53.09 C ANISOU 2924 CA ILE A 266 9111 6473 4588 514 -553 -140 C ATOM 2925 C ILE A 266 17.019 13.622 2.615 1.00 59.07 C ANISOU 2925 C ILE A 266 9898 7147 5398 543 -597 -191 C ATOM 2926 O ILE A 266 17.572 13.647 1.524 1.00 58.91 O ANISOU 2926 O ILE A 266 9937 7116 5329 588 -579 -258 O ATOM 2927 CB ILE A 266 18.236 15.369 4.061 1.00 55.53 C ANISOU 2927 CB ILE A 266 9389 6827 4881 519 -478 -112 C ATOM 2928 CG1 ILE A 266 18.835 14.319 5.044 1.00 56.20 C ANISOU 2928 CG1 ILE A 266 9407 6897 5048 505 -477 -63 C ATOM 2929 CG2 ILE A 266 18.139 16.753 4.709 1.00 55.13 C ANISOU 2929 CG2 ILE A 266 9313 6852 4783 498 -442 -82 C ATOM 2930 CD1 ILE A 266 19.625 13.104 4.429 1.00 63.58 C ANISOU 2930 CD1 ILE A 266 10366 7759 6030 541 -483 -102 C ATOM 2931 N ALA A 267 16.500 12.493 3.145 1.00 57.19 N ANISOU 2931 N ALA A 267 9612 6855 5262 520 -661 -160 N ATOM 2932 CA ALA A 267 16.593 11.186 2.486 1.00 58.28 C ANISOU 2932 CA ALA A 267 9768 6900 5475 548 -717 -214 C ATOM 2933 C ALA A 267 15.458 10.965 1.461 1.00 64.27 C ANISOU 2933 C ALA A 267 10580 7611 6228 558 -791 -276 C ATOM 2934 O ALA A 267 15.599 10.109 0.583 1.00 64.99 O ANISOU 2934 O ALA A 267 10708 7636 6350 599 -833 -357 O ATOM 2935 CB ALA A 267 16.559 10.078 3.524 1.00 59.17 C ANISOU 2935 CB ALA A 267 9795 6968 5719 516 -762 -142 C ATOM 2936 N CYS A 268 14.348 11.722 1.568 1.00 61.00 N ANISOU 2936 N CYS A 268 10167 7233 5776 525 -809 -244 N ATOM 2937 CA CYS A 268 13.201 11.560 0.671 1.00 61.46 C ANISOU 2937 CA CYS A 268 10270 7252 5828 527 -878 -290 C ATOM 2938 C CYS A 268 13.262 12.567 -0.495 1.00 66.50 C ANISOU 2938 C CYS A 268 10985 7940 6342 561 -836 -359 C ATOM 2939 O CYS A 268 12.853 12.225 -1.612 1.00 66.78 O ANISOU 2939 O CYS A 268 11072 7943 6359 591 -880 -436 O ATOM 2940 CB CYS A 268 11.897 11.709 1.445 1.00 61.30 C ANISOU 2940 CB CYS A 268 10203 7247 5842 473 -926 -208 C ATOM 2941 SG CYS A 268 11.639 10.444 2.716 1.00 65.36 S ANISOU 2941 SG CYS A 268 10610 7715 6510 431 -992 -108 S ATOM 2942 N TRP A 269 13.748 13.796 -0.238 1.00 63.02 N ANISOU 2942 N TRP A 269 10545 7579 5821 557 -758 -328 N ATOM 2943 CA TRP A 269 13.822 14.850 -1.251 1.00 62.85 C ANISOU 2943 CA TRP A 269 10577 7610 5691 583 -718 -367 C ATOM 2944 C TRP A 269 15.104 14.771 -2.099 1.00 65.46 C ANISOU 2944 C TRP A 269 10941 7960 5971 642 -671 -425 C ATOM 2945 O TRP A 269 15.026 15.066 -3.289 1.00 65.28 O ANISOU 2945 O TRP A 269 10964 7965 5875 677 -670 -480 O ATOM 2946 CB TRP A 269 13.741 16.227 -0.601 1.00 61.28 C ANISOU 2946 CB TRP A 269 10356 7480 5446 553 -666 -307 C ATOM 2947 CG TRP A 269 12.354 16.584 -0.167 1.00 62.28 C ANISOU 2947 CG TRP A 269 10465 7612 5585 511 -709 -268 C ATOM 2948 CD1 TRP A 269 11.796 16.386 1.062 1.00 64.98 C ANISOU 2948 CD1 TRP A 269 10746 7959 5982 471 -733 -204 C ATOM 2949 CD2 TRP A 269 11.317 17.120 -0.999 1.00 62.24 C ANISOU 2949 CD2 TRP A 269 10501 7615 5533 506 -737 -287 C ATOM 2950 NE1 TRP A 269 10.484 16.804 1.059 1.00 64.35 N ANISOU 2950 NE1 TRP A 269 10667 7892 5890 445 -772 -184 N ATOM 2951 CE2 TRP A 269 10.163 17.257 -0.195 1.00 65.90 C ANISOU 2951 CE2 TRP A 269 10929 8084 6028 464 -775 -234 C ATOM 2952 CE3 TRP A 269 11.252 17.505 -2.350 1.00 63.81 C ANISOU 2952 CE3 TRP A 269 10755 7828 5661 536 -732 -339 C ATOM 2953 CZ2 TRP A 269 8.961 17.770 -0.693 1.00 65.14 C ANISOU 2953 CZ2 TRP A 269 10856 7996 5899 448 -807 -232 C ATOM 2954 CZ3 TRP A 269 10.066 18.030 -2.837 1.00 65.31 C ANISOU 2954 CZ3 TRP A 269 10965 8030 5820 517 -762 -335 C ATOM 2955 CH2 TRP A 269 8.937 18.155 -2.016 1.00 65.64 C ANISOU 2955 CH2 TRP A 269 10977 8065 5899 472 -799 -283 C ATOM 2956 N ALA A 270 16.263 14.366 -1.509 1.00 60.84 N ANISOU 2956 N ALA A 270 10328 7368 5419 654 -632 -409 N ATOM 2957 CA ALA A 270 17.544 14.245 -2.229 1.00 60.34 C ANISOU 2957 CA ALA A 270 10289 7329 5308 713 -585 -456 C ATOM 2958 C ALA A 270 17.392 13.458 -3.554 1.00 63.44 C ANISOU 2958 C ALA A 270 10728 7699 5678 770 -632 -559 C ATOM 2959 O ALA A 270 17.879 13.975 -4.552 1.00 63.57 O ANISOU 2959 O ALA A 270 10774 7782 5597 817 -596 -595 O ATOM 2960 CB ALA A 270 18.594 13.577 -1.362 1.00 61.10 C ANISOU 2960 CB ALA A 270 10345 7399 5471 714 -558 -429 C ATOM 2961 N PRO A 271 16.685 12.287 -3.650 1.00 59.28 N ANISOU 2961 N PRO A 271 10202 7087 5236 771 -716 -608 N ATOM 2962 CA PRO A 271 16.556 11.621 -4.965 1.00 59.55 C ANISOU 2962 CA PRO A 271 10278 7105 5241 833 -766 -724 C ATOM 2963 C PRO A 271 15.835 12.498 -6.017 1.00 61.12 C ANISOU 2963 C PRO A 271 10517 7376 5330 843 -765 -750 C ATOM 2964 O PRO A 271 16.227 12.481 -7.193 1.00 61.10 O ANISOU 2964 O PRO A 271 10544 7429 5242 910 -757 -829 O ATOM 2965 CB PRO A 271 15.726 10.370 -4.644 1.00 61.93 C ANISOU 2965 CB PRO A 271 10562 7291 5676 811 -868 -748 C ATOM 2966 CG PRO A 271 15.964 10.118 -3.202 1.00 66.02 C ANISOU 2966 CG PRO A 271 11019 7770 6293 758 -856 -650 C ATOM 2967 CD PRO A 271 16.035 11.480 -2.594 1.00 60.71 C ANISOU 2967 CD PRO A 271 10335 7185 5545 719 -776 -560 C ATOM 2968 N LEU A 272 14.808 13.282 -5.594 1.00 54.87 N ANISOU 2968 N LEU A 272 9720 6595 4534 782 -770 -680 N ATOM 2969 CA LEU A 272 14.073 14.182 -6.487 1.00 53.39 C ANISOU 2969 CA LEU A 272 9562 6472 4251 783 -767 -688 C ATOM 2970 C LEU A 272 14.982 15.340 -6.909 1.00 56.71 C ANISOU 2970 C LEU A 272 9983 6998 4567 808 -679 -656 C ATOM 2971 O LEU A 272 15.227 15.493 -8.098 1.00 56.99 O ANISOU 2971 O LEU A 272 10039 7103 4513 863 -669 -709 O ATOM 2972 CB LEU A 272 12.786 14.701 -5.818 1.00 52.21 C ANISOU 2972 CB LEU A 272 9401 6302 4135 711 -795 -616 C ATOM 2973 CG LEU A 272 11.876 15.579 -6.671 1.00 55.61 C ANISOU 2973 CG LEU A 272 9858 6786 4484 704 -802 -618 C ATOM 2974 CD1 LEU A 272 11.300 14.802 -7.821 1.00 56.38 C ANISOU 2974 CD1 LEU A 272 9991 6863 4568 739 -872 -714 C ATOM 2975 CD2 LEU A 272 10.743 16.130 -5.853 1.00 56.29 C ANISOU 2975 CD2 LEU A 272 9926 6856 4606 636 -820 -541 C ATOM 2976 N PHE A 273 15.531 16.104 -5.927 1.00 52.49 N ANISOU 2976 N PHE A 273 9417 6481 4047 773 -621 -569 N ATOM 2977 CA PHE A 273 16.479 17.219 -6.111 1.00 52.22 C ANISOU 2977 CA PHE A 273 9370 6531 3942 788 -543 -519 C ATOM 2978 C PHE A 273 17.644 16.880 -7.055 1.00 56.63 C ANISOU 2978 C PHE A 273 9938 7147 4430 864 -511 -569 C ATOM 2979 O PHE A 273 18.138 17.772 -7.741 1.00 56.09 O ANISOU 2979 O PHE A 273 9864 7170 4278 889 -465 -539 O ATOM 2980 CB PHE A 273 17.071 17.634 -4.761 1.00 53.61 C ANISOU 2980 CB PHE A 273 9507 6690 4173 748 -500 -444 C ATOM 2981 CG PHE A 273 16.278 18.631 -3.959 1.00 54.98 C ANISOU 2981 CG PHE A 273 9657 6861 4372 686 -501 -377 C ATOM 2982 CD1 PHE A 273 15.112 18.254 -3.306 1.00 58.30 C ANISOU 2982 CD1 PHE A 273 10070 7230 4851 644 -556 -372 C ATOM 2983 CD2 PHE A 273 16.760 19.917 -3.751 1.00 57.24 C ANISOU 2983 CD2 PHE A 273 9919 7196 4633 673 -450 -317 C ATOM 2984 CE1 PHE A 273 14.396 19.173 -2.533 1.00 58.83 C ANISOU 2984 CE1 PHE A 273 10109 7307 4935 596 -556 -317 C ATOM 2985 CE2 PHE A 273 16.059 20.827 -2.958 1.00 59.65 C ANISOU 2985 CE2 PHE A 273 10198 7498 4970 623 -456 -270 C ATOM 2986 CZ PHE A 273 14.880 20.450 -2.355 1.00 57.60 C ANISOU 2986 CZ PHE A 273 9933 7198 4754 588 -506 -274 C ATOM 2987 N ILE A 274 18.107 15.616 -7.056 1.00 53.94 N ANISOU 2987 N ILE A 274 9605 6759 4129 903 -535 -639 N ATOM 2988 CA ILE A 274 19.185 15.161 -7.932 1.00 54.84 C ANISOU 2988 CA ILE A 274 9726 6931 4178 986 -510 -700 C ATOM 2989 C ILE A 274 18.621 15.030 -9.349 1.00 60.93 C ANISOU 2989 C ILE A 274 10524 7763 4865 1038 -548 -784 C ATOM 2990 O ILE A 274 19.235 15.553 -10.285 1.00 61.31 O ANISOU 2990 O ILE A 274 10565 7927 4803 1091 -507 -784 O ATOM 2991 CB ILE A 274 19.829 13.843 -7.417 1.00 58.33 C ANISOU 2991 CB ILE A 274 10163 7296 4704 1012 -529 -752 C ATOM 2992 CG1 ILE A 274 20.612 14.121 -6.100 1.00 58.22 C ANISOU 2992 CG1 ILE A 274 10115 7256 4751 966 -475 -657 C ATOM 2993 CG2 ILE A 274 20.765 13.231 -8.481 1.00 59.71 C ANISOU 2993 CG2 ILE A 274 10347 7533 4805 1111 -516 -840 C ATOM 2994 CD1 ILE A 274 21.162 12.877 -5.349 1.00 68.03 C ANISOU 2994 CD1 ILE A 274 11340 8416 6094 976 -491 -682 C ATOM 2995 N LEU A 275 17.427 14.395 -9.503 1.00 58.05 N ANISOU 2995 N LEU A 275 10181 7328 4548 1021 -628 -846 N ATOM 2996 CA LEU A 275 16.782 14.237 -10.817 1.00 58.58 C ANISOU 2996 CA LEU A 275 10271 7449 4537 1067 -672 -932 C ATOM 2997 C LEU A 275 16.432 15.606 -11.409 1.00 62.86 C ANISOU 2997 C LEU A 275 10806 8101 4978 1049 -631 -860 C ATOM 2998 O LEU A 275 16.585 15.808 -12.614 1.00 63.12 O ANISOU 2998 O LEU A 275 10836 8247 4899 1108 -622 -900 O ATOM 2999 CB LEU A 275 15.525 13.362 -10.725 1.00 58.54 C ANISOU 2999 CB LEU A 275 10288 7336 4619 1039 -770 -994 C ATOM 3000 CG LEU A 275 14.894 12.977 -12.062 1.00 63.63 C ANISOU 3000 CG LEU A 275 10956 8026 5194 1093 -829 -1107 C ATOM 3001 CD1 LEU A 275 15.810 12.067 -12.859 1.00 64.94 C ANISOU 3001 CD1 LEU A 275 11123 8228 5321 1195 -841 -1233 C ATOM 3002 CD2 LEU A 275 13.620 12.276 -11.853 1.00 65.59 C ANISOU 3002 CD2 LEU A 275 11221 8161 5538 1051 -925 -1143 C ATOM 3003 N LEU A 276 15.986 16.544 -10.552 1.00 59.39 N ANISOU 3003 N LEU A 276 10353 7633 4579 970 -608 -752 N ATOM 3004 CA LEU A 276 15.679 17.919 -10.934 1.00 59.47 C ANISOU 3004 CA LEU A 276 10346 7726 4522 943 -570 -668 C ATOM 3005 C LEU A 276 16.926 18.608 -11.438 1.00 66.16 C ANISOU 3005 C LEU A 276 11162 8687 5287 989 -499 -622 C ATOM 3006 O LEU A 276 16.887 19.263 -12.477 1.00 66.55 O ANISOU 3006 O LEU A 276 11195 8850 5242 1017 -483 -602 O ATOM 3007 CB LEU A 276 15.080 18.702 -9.747 1.00 58.28 C ANISOU 3007 CB LEU A 276 10182 7511 4451 857 -563 -575 C ATOM 3008 CG LEU A 276 13.696 18.291 -9.242 1.00 62.40 C ANISOU 3008 CG LEU A 276 10723 7942 5045 804 -630 -590 C ATOM 3009 CD1 LEU A 276 13.401 18.933 -7.903 1.00 61.74 C ANISOU 3009 CD1 LEU A 276 10615 7809 5035 736 -615 -505 C ATOM 3010 CD2 LEU A 276 12.598 18.606 -10.265 1.00 64.08 C ANISOU 3010 CD2 LEU A 276 10953 8195 5198 802 -666 -610 C ATOM 3011 N LEU A 277 18.049 18.400 -10.732 1.00 64.45 N ANISOU 3011 N LEU A 277 10932 8448 5107 999 -459 -600 N ATOM 3012 CA LEU A 277 19.346 18.984 -11.058 1.00 65.64 C ANISOU 3012 CA LEU A 277 11050 8697 5192 1041 -393 -544 C ATOM 3013 C LEU A 277 19.897 18.353 -12.353 1.00 72.07 C ANISOU 3013 C LEU A 277 11866 9618 5901 1139 -394 -627 C ATOM 3014 O LEU A 277 20.625 19.026 -13.082 1.00 72.03 O ANISOU 3014 O LEU A 277 11823 9741 5802 1180 -348 -573 O ATOM 3015 CB LEU A 277 20.313 18.784 -9.872 1.00 65.48 C ANISOU 3015 CB LEU A 277 11019 8613 5247 1021 -357 -505 C ATOM 3016 CG LEU A 277 21.576 19.652 -9.809 1.00 70.53 C ANISOU 3016 CG LEU A 277 11618 9327 5852 1032 -287 -408 C ATOM 3017 CD1 LEU A 277 21.224 21.134 -9.672 1.00 70.43 C ANISOU 3017 CD1 LEU A 277 11575 9337 5849 974 -273 -301 C ATOM 3018 CD2 LEU A 277 22.434 19.256 -8.615 1.00 72.55 C ANISOU 3018 CD2 LEU A 277 11868 9511 6185 1013 -260 -386 C ATOM 3019 N LEU A 278 19.506 17.083 -12.660 1.00 70.56 N ANISOU 3019 N LEU A 278 11708 9378 5723 1178 -452 -757 N ATOM 3020 CA LEU A 278 19.879 16.396 -13.910 1.00 72.24 C ANISOU 3020 CA LEU A 278 11921 9690 5836 1280 -468 -866 C ATOM 3021 C LEU A 278 19.141 17.003 -15.088 1.00 77.67 C ANISOU 3021 C LEU A 278 12597 10498 6417 1297 -481 -867 C ATOM 3022 O LEU A 278 19.763 17.324 -16.099 1.00 77.73 O ANISOU 3022 O LEU A 278 12568 10665 6301 1367 -447 -860 O ATOM 3023 CB LEU A 278 19.600 14.878 -13.853 1.00 72.85 C ANISOU 3023 CB LEU A 278 12034 9664 5982 1315 -541 -1012 C ATOM 3024 CG LEU A 278 20.510 14.028 -12.975 1.00 77.47 C ANISOU 3024 CG LEU A 278 12621 10158 6657 1327 -532 -1035 C ATOM 3025 CD1 LEU A 278 19.934 12.643 -12.786 1.00 78.10 C ANISOU 3025 CD1 LEU A 278 12728 10105 6842 1336 -621 -1158 C ATOM 3026 CD2 LEU A 278 21.932 13.957 -13.538 1.00 80.68 C ANISOU 3026 CD2 LEU A 278 13002 10682 6970 1418 -476 -1050 C ATOM 3027 N ASP A 279 17.819 17.194 -14.935 1.00 75.14 N ANISOU 3027 N ASP A 279 12298 10110 6141 1232 -527 -863 N ATOM 3028 CA ASP A 279 16.929 17.768 -15.937 1.00 76.16 C ANISOU 3028 CA ASP A 279 12417 10334 6186 1232 -544 -856 C ATOM 3029 C ASP A 279 17.383 19.176 -16.355 1.00 80.62 C ANISOU 3029 C ASP A 279 12926 11034 6673 1224 -477 -718 C ATOM 3030 O ASP A 279 17.280 19.513 -17.537 1.00 81.50 O ANISOU 3030 O ASP A 279 13004 11295 6667 1270 -472 -717 O ATOM 3031 CB ASP A 279 15.497 17.824 -15.388 1.00 77.96 C ANISOU 3031 CB ASP A 279 12678 10443 6501 1147 -597 -847 C ATOM 3032 CG ASP A 279 14.429 18.195 -16.404 1.00 94.11 C ANISOU 3032 CG ASP A 279 14720 12567 8471 1144 -627 -858 C ATOM 3033 OD1 ASP A 279 14.718 18.142 -17.625 1.00 96.20 O ANISOU 3033 OD1 ASP A 279 14962 12977 8613 1221 -624 -908 O ATOM 3034 OD2 ASP A 279 13.284 18.441 -15.988 1.00101.71 O ANISOU 3034 OD2 ASP A 279 15702 13451 9493 1071 -659 -823 O ATOM 3035 N VAL A 280 17.894 19.987 -15.392 1.00 75.98 N ANISOU 3035 N VAL A 280 12319 10397 6152 1167 -429 -599 N ATOM 3036 CA VAL A 280 18.389 21.348 -15.646 1.00 75.66 C ANISOU 3036 CA VAL A 280 12218 10459 6071 1152 -374 -456 C ATOM 3037 C VAL A 280 19.496 21.283 -16.725 1.00 81.34 C ANISOU 3037 C VAL A 280 12890 11355 6661 1248 -337 -454 C ATOM 3038 O VAL A 280 19.487 22.080 -17.666 1.00 81.35 O ANISOU 3038 O VAL A 280 12835 11503 6573 1267 -319 -380 O ATOM 3039 CB VAL A 280 18.885 22.039 -14.344 1.00 78.46 C ANISOU 3039 CB VAL A 280 12561 10717 6532 1085 -339 -354 C ATOM 3040 CG1 VAL A 280 19.552 23.379 -14.640 1.00 78.35 C ANISOU 3040 CG1 VAL A 280 12477 10803 6489 1077 -291 -209 C ATOM 3041 CG2 VAL A 280 17.745 22.226 -13.345 1.00 77.31 C ANISOU 3041 CG2 VAL A 280 12448 10429 6496 997 -375 -349 C ATOM 3042 N GLY A 281 20.373 20.286 -16.611 1.00 79.35 N ANISOU 3042 N GLY A 281 12656 11096 6398 1311 -330 -538 N ATOM 3043 CA GLY A 281 21.456 20.055 -17.560 1.00 80.76 C ANISOU 3043 CA GLY A 281 12791 11442 6451 1414 -298 -553 C ATOM 3044 C GLY A 281 21.161 19.049 -18.661 1.00 86.66 C ANISOU 3044 C GLY A 281 13552 12276 7099 1508 -341 -711 C ATOM 3045 O GLY A 281 22.073 18.690 -19.408 1.00 87.06 O ANISOU 3045 O GLY A 281 13573 12456 7051 1606 -320 -757 O ATOM 3046 N CYS A 282 19.893 18.578 -18.775 1.00 84.29 N ANISOU 3046 N CYS A 282 13293 11909 6824 1482 -405 -800 N ATOM 3047 CA CYS A 282 19.467 17.613 -19.803 1.00 86.00 C ANISOU 3047 CA CYS A 282 13524 12195 6959 1566 -460 -964 C ATOM 3048 C CYS A 282 18.782 18.323 -20.963 1.00 89.24 C ANISOU 3048 C CYS A 282 13888 12770 7247 1579 -464 -931 C ATOM 3049 O CYS A 282 18.139 19.354 -20.762 1.00 88.55 O ANISOU 3049 O CYS A 282 13784 12673 7189 1497 -449 -803 O ATOM 3050 CB CYS A 282 18.543 16.551 -19.215 1.00 87.02 C ANISOU 3050 CB CYS A 282 13725 12132 7206 1532 -539 -1092 C ATOM 3051 SG CYS A 282 19.387 15.268 -18.254 1.00 91.52 S ANISOU 3051 SG CYS A 282 14334 12547 7893 1558 -555 -1185 S ATOM 3052 N LYS A 283 18.880 17.729 -22.176 1.00 85.71 N ANISOU 3052 N LYS A 283 13419 12478 6669 1686 -490 -1053 N ATOM 3053 CA LYS A 283 18.210 18.224 -23.383 1.00 85.65 C ANISOU 3053 CA LYS A 283 13363 12648 6531 1713 -501 -1043 C ATOM 3054 C LYS A 283 16.923 17.401 -23.574 1.00 89.16 C ANISOU 3054 C LYS A 283 13869 12997 7013 1701 -589 -1195 C ATOM 3055 O LYS A 283 16.857 16.270 -23.089 1.00 88.78 O ANISOU 3055 O LYS A 283 13882 12797 7055 1715 -643 -1332 O ATOM 3056 CB LYS A 283 19.148 18.163 -24.609 1.00 88.98 C ANISOU 3056 CB LYS A 283 13706 13334 6770 1843 -470 -1070 C ATOM 3057 CG LYS A 283 18.634 18.936 -25.822 1.00 98.36 C ANISOU 3057 CG LYS A 283 14814 14746 7813 1864 -461 -1004 C ATOM 3058 CD LYS A 283 19.631 18.962 -26.968 1.00108.01 C ANISOU 3058 CD LYS A 283 15941 16251 8847 1994 -424 -1005 C ATOM 3059 CE LYS A 283 19.107 19.768 -28.135 1.00120.07 C ANISOU 3059 CE LYS A 283 17375 18013 10232 2009 -414 -918 C ATOM 3060 NZ LYS A 283 20.060 19.791 -29.279 1.00130.48 N ANISOU 3060 NZ LYS A 283 18586 19635 11355 2141 -379 -910 N ATOM 3061 N VAL A 284 15.881 17.993 -24.198 1.00 85.51 N ANISOU 3061 N VAL A 284 13386 12605 6499 1666 -606 -1156 N ATOM 3062 CA VAL A 284 14.569 17.360 -24.382 1.00 85.50 C ANISOU 3062 CA VAL A 284 13438 12514 6535 1642 -690 -1275 C ATOM 3063 C VAL A 284 14.709 15.984 -25.062 1.00 91.83 C ANISOU 3063 C VAL A 284 14259 13346 7285 1755 -759 -1501 C ATOM 3064 O VAL A 284 15.465 15.844 -26.025 1.00 92.92 O ANISOU 3064 O VAL A 284 14341 13689 7275 1867 -740 -1559 O ATOM 3065 CB VAL A 284 13.623 18.261 -25.197 1.00 89.29 C ANISOU 3065 CB VAL A 284 13874 13122 6929 1607 -687 -1193 C ATOM 3066 N LYS A 285 14.009 14.967 -24.504 1.00 88.60 N ANISOU 3066 N LYS A 285 13925 12730 7008 1727 -842 -1624 N ATOM 3067 CA LYS A 285 13.941 13.565 -24.956 1.00 89.72 C ANISOU 3067 CA LYS A 285 14096 12836 7158 1816 -932 -1850 C ATOM 3068 C LYS A 285 15.357 12.890 -24.996 1.00 95.33 C ANISOU 3068 C LYS A 285 14789 13592 7840 1924 -910 -1937 C ATOM 3069 O LYS A 285 15.519 11.861 -25.657 1.00 96.42 O ANISOU 3069 O LYS A 285 14929 13762 7944 2029 -976 -2132 O ATOM 3070 CB LYS A 285 13.273 13.462 -26.345 1.00 93.06 C ANISOU 3070 CB LYS A 285 14488 13434 7435 1884 -979 -1957 C ATOM 3071 N THR A 286 16.344 13.427 -24.238 1.00 91.55 N ANISOU 3071 N THR A 286 14295 13101 7389 1897 -826 -1800 N ATOM 3072 CA THR A 286 17.698 12.858 -24.171 1.00 92.19 C ANISOU 3072 CA THR A 286 14360 13217 7451 1988 -798 -1859 C ATOM 3073 C THR A 286 17.782 11.941 -22.951 1.00 95.68 C ANISOU 3073 C THR A 286 14864 13400 8091 1943 -840 -1909 C ATOM 3074 O THR A 286 17.986 10.736 -23.098 1.00 96.06 O ANISOU 3074 O THR A 286 14932 13384 8184 2017 -909 -2086 O ATOM 3075 CB THR A 286 18.765 13.974 -24.133 1.00100.98 C ANISOU 3075 CB THR A 286 15412 14479 8476 1988 -685 -1675 C ATOM 3076 OG1 THR A 286 18.557 14.872 -25.223 1.00101.39 O ANISOU 3076 OG1 THR A 286 15395 14765 8363 2016 -653 -1605 O ATOM 3077 CG2 THR A 286 20.197 13.434 -24.147 1.00100.52 C ANISOU 3077 CG2 THR A 286 15331 14481 8380 2088 -650 -1725 C ATOM 3078 N CYS A 287 17.626 12.522 -21.751 1.00 91.27 N ANISOU 3078 N CYS A 287 14329 12699 7652 1823 -801 -1753 N ATOM 3079 CA CYS A 287 17.648 11.798 -20.481 1.00 90.64 C ANISOU 3079 CA CYS A 287 14294 12384 7760 1764 -832 -1762 C ATOM 3080 C CYS A 287 16.302 11.087 -20.310 1.00 93.88 C ANISOU 3080 C CYS A 287 14750 12636 8285 1714 -939 -1848 C ATOM 3081 O CYS A 287 15.256 11.737 -20.405 1.00 93.32 O ANISOU 3081 O CYS A 287 14686 12568 8202 1643 -947 -1779 O ATOM 3082 CB CYS A 287 17.957 12.753 -19.329 1.00 89.63 C ANISOU 3082 CB CYS A 287 14164 12195 7698 1662 -753 -1566 C ATOM 3083 SG CYS A 287 19.504 13.686 -19.536 1.00 93.54 S ANISOU 3083 SG CYS A 287 14599 12875 8068 1711 -634 -1442 S ATOM 3084 N ASP A 288 16.321 9.746 -20.154 1.00 89.88 N ANISOU 3084 N ASP A 288 14267 11997 7887 1756 -1025 -2000 N ATOM 3085 CA ASP A 288 15.101 8.937 -20.135 1.00 89.48 C ANISOU 3085 CA ASP A 288 14249 11801 7947 1723 -1142 -2096 C ATOM 3086 C ASP A 288 14.569 8.705 -18.707 1.00 90.70 C ANISOU 3086 C ASP A 288 14430 11732 8301 1605 -1170 -2001 C ATOM 3087 O ASP A 288 13.391 8.380 -18.555 1.00 90.14 O ANISOU 3087 O ASP A 288 14381 11551 8316 1548 -1251 -2016 O ATOM 3088 CB ASP A 288 15.368 7.581 -20.804 1.00 93.05 C ANISOU 3088 CB ASP A 288 14703 12230 8423 1837 -1237 -2321 C ATOM 3089 CG ASP A 288 14.116 6.785 -21.108 1.00104.62 C ANISOU 3089 CG ASP A 288 16194 13586 9973 1824 -1368 -2441 C ATOM 3090 OD1 ASP A 288 13.683 6.005 -20.233 1.00105.13 O ANISOU 3090 OD1 ASP A 288 16278 13435 10231 1765 -1445 -2448 O ATOM 3091 OD2 ASP A 288 13.571 6.937 -22.227 1.00111.33 O ANISOU 3091 OD2 ASP A 288 17036 14567 10696 1871 -1395 -2521 O ATOM 3092 N ILE A 289 15.404 8.898 -17.675 1.00 85.67 N ANISOU 3092 N ILE A 289 13783 11039 7727 1569 -1103 -1896 N ATOM 3093 CA ILE A 289 15.006 8.695 -16.270 1.00 84.13 C ANISOU 3093 CA ILE A 289 13598 10659 7708 1463 -1122 -1797 C ATOM 3094 C ILE A 289 13.935 9.756 -15.882 1.00 85.86 C ANISOU 3094 C ILE A 289 13827 10879 7918 1357 -1100 -1656 C ATOM 3095 O ILE A 289 13.079 9.481 -15.037 1.00 84.96 O ANISOU 3095 O ILE A 289 13722 10625 7935 1276 -1153 -1607 O ATOM 3096 CB ILE A 289 16.242 8.736 -15.303 1.00 86.65 C ANISOU 3096 CB ILE A 289 13898 10948 8076 1454 -1046 -1713 C ATOM 3097 CG1 ILE A 289 17.357 7.700 -15.691 1.00 88.58 C ANISOU 3097 CG1 ILE A 289 14131 11202 8324 1565 -1060 -1848 C ATOM 3098 CG2 ILE A 289 15.824 8.516 -13.843 1.00 86.00 C ANISOU 3098 CG2 ILE A 289 13813 10694 8169 1350 -1068 -1612 C ATOM 3099 CD1 ILE A 289 18.232 7.958 -17.011 1.00 97.48 C ANISOU 3099 CD1 ILE A 289 15241 12541 9254 1687 -1007 -1927 C ATOM 3100 N LEU A 290 13.961 10.931 -16.559 1.00 81.24 N ANISOU 3100 N LEU A 290 13231 10457 7179 1363 -1029 -1594 N ATOM 3101 CA LEU A 290 13.049 12.066 -16.358 1.00 79.37 C ANISOU 3101 CA LEU A 290 12996 10246 6914 1277 -1000 -1466 C ATOM 3102 C LEU A 290 11.601 11.721 -16.721 1.00 83.04 C ANISOU 3102 C LEU A 290 13486 10653 7412 1245 -1093 -1519 C ATOM 3103 O LEU A 290 10.678 12.271 -16.120 1.00 81.78 O ANISOU 3103 O LEU A 290 13335 10436 7303 1155 -1098 -1418 O ATOM 3104 CB LEU A 290 13.497 13.274 -17.214 1.00 79.12 C ANISOU 3104 CB LEU A 290 12937 10413 6713 1309 -914 -1404 C ATOM 3105 CG LEU A 290 14.933 13.798 -17.044 1.00 83.09 C ANISOU 3105 CG LEU A 290 13407 11004 7159 1344 -819 -1337 C ATOM 3106 CD1 LEU A 290 15.232 14.877 -18.047 1.00 83.40 C ANISOU 3106 CD1 LEU A 290 13407 11243 7037 1380 -756 -1278 C ATOM 3107 CD2 LEU A 290 15.188 14.313 -15.650 1.00 83.67 C ANISOU 3107 CD2 LEU A 290 13478 10979 7335 1259 -771 -1203 C ATOM 3108 N PHE A 291 11.402 10.824 -17.706 1.00 80.72 N ANISOU 3108 N PHE A 291 13201 10379 7089 1323 -1170 -1681 N ATOM 3109 CA PHE A 291 10.076 10.437 -18.187 1.00 81.31 C ANISOU 3109 CA PHE A 291 13298 10408 7187 1304 -1267 -1749 C ATOM 3110 C PHE A 291 9.386 9.477 -17.209 1.00 85.60 C ANISOU 3110 C PHE A 291 13858 10738 7927 1241 -1361 -1752 C ATOM 3111 O PHE A 291 8.226 9.112 -17.428 1.00 85.53 O ANISOU 3111 O PHE A 291 13866 10666 7967 1209 -1449 -1784 O ATOM 3112 CB PHE A 291 10.159 9.807 -19.580 1.00 84.90 C ANISOU 3112 CB PHE A 291 13750 10963 7546 1416 -1322 -1932 C ATOM 3113 CG PHE A 291 10.596 10.817 -20.611 1.00 87.10 C ANISOU 3113 CG PHE A 291 13999 11474 7621 1469 -1237 -1908 C ATOM 3114 CD1 PHE A 291 9.672 11.661 -21.214 1.00 90.36 C ANISOU 3114 CD1 PHE A 291 14407 11984 7941 1433 -1227 -1850 C ATOM 3115 CD2 PHE A 291 11.937 10.957 -20.948 1.00 90.04 C ANISOU 3115 CD2 PHE A 291 14340 11973 7899 1552 -1166 -1925 C ATOM 3116 CE1 PHE A 291 10.080 12.623 -22.137 1.00 91.69 C ANISOU 3116 CE1 PHE A 291 14533 12372 7932 1476 -1149 -1805 C ATOM 3117 CE2 PHE A 291 12.345 11.919 -21.875 1.00 93.22 C ANISOU 3117 CE2 PHE A 291 14701 12601 8119 1598 -1089 -1878 C ATOM 3118 CZ PHE A 291 11.414 12.746 -22.460 1.00 91.25 C ANISOU 3118 CZ PHE A 291 14441 12445 7785 1559 -1082 -1815 C ATOM 3119 N ARG A 292 10.065 9.111 -16.115 1.00 82.24 N ANISOU 3119 N ARG A 292 13421 10210 7616 1219 -1344 -1703 N ATOM 3120 CA ARG A 292 9.447 8.337 -15.053 1.00 82.06 C ANISOU 3120 CA ARG A 292 13396 10002 7780 1149 -1421 -1665 C ATOM 3121 C ARG A 292 10.089 8.797 -13.723 1.00 84.09 C ANISOU 3121 C ARG A 292 13630 10226 8093 1091 -1339 -1518 C ATOM 3122 O ARG A 292 10.923 8.115 -13.110 1.00 83.60 O ANISOU 3122 O ARG A 292 13549 10092 8122 1108 -1341 -1531 O ATOM 3123 CB ARG A 292 9.524 6.817 -15.283 1.00 84.60 C ANISOU 3123 CB ARG A 292 13716 10201 8227 1205 -1541 -1818 C ATOM 3124 CG ARG A 292 8.644 6.039 -14.294 1.00 97.15 C ANISOU 3124 CG ARG A 292 15292 11602 10017 1124 -1638 -1760 C ATOM 3125 CD ARG A 292 7.167 6.449 -14.326 1.00105.66 C ANISOU 3125 CD ARG A 292 16385 12666 11096 1049 -1683 -1691 C ATOM 3126 NE ARG A 292 6.411 5.881 -13.205 1.00111.90 N ANISOU 3126 NE ARG A 292 17149 13301 12067 964 -1757 -1593 N ATOM 3127 CZ ARG A 292 5.119 6.104 -12.982 1.00123.20 C ANISOU 3127 CZ ARG A 292 18583 14697 13532 890 -1804 -1511 C ATOM 3128 NH1 ARG A 292 4.420 6.881 -13.801 1.00110.04 N ANISOU 3128 NH1 ARG A 292 16948 13128 11732 887 -1785 -1519 N ATOM 3129 NH2 ARG A 292 4.517 5.556 -11.935 1.00107.00 N ANISOU 3129 NH2 ARG A 292 16494 12517 11642 819 -1870 -1411 N ATOM 3130 N ALA A 293 9.696 10.012 -13.336 1.00 78.86 N ANISOU 3130 N ALA A 293 12967 9627 7368 1026 -1267 -1384 N ATOM 3131 CA ALA A 293 10.130 10.719 -12.147 1.00 77.25 C ANISOU 3131 CA ALA A 293 12740 9417 7193 967 -1186 -1243 C ATOM 3132 C ALA A 293 9.136 10.542 -11.012 1.00 80.45 C ANISOU 3132 C ALA A 293 13130 9708 7727 876 -1236 -1147 C ATOM 3133 O ALA A 293 9.417 10.946 -9.882 1.00 78.99 O ANISOU 3133 O ALA A 293 12920 9509 7586 827 -1185 -1037 O ATOM 3134 CB ALA A 293 10.287 12.192 -12.475 1.00 77.30 C ANISOU 3134 CB ALA A 293 12747 9563 7061 957 -1088 -1163 C ATOM 3135 N GLU A 294 7.969 9.935 -11.312 1.00 77.68 N ANISOU 3135 N GLU A 294 12792 9287 7435 857 -1338 -1187 N ATOM 3136 CA GLU A 294 6.883 9.716 -10.352 1.00 77.07 C ANISOU 3136 CA GLU A 294 12695 9113 7475 774 -1398 -1091 C ATOM 3137 C GLU A 294 7.371 8.908 -9.142 1.00 79.95 C ANISOU 3137 C GLU A 294 13015 9375 7988 750 -1420 -1041 C ATOM 3138 O GLU A 294 6.913 9.181 -8.034 1.00 78.78 O ANISOU 3138 O GLU A 294 12833 9204 7898 681 -1412 -915 O ATOM 3139 CB GLU A 294 5.685 9.011 -11.009 1.00 79.41 C ANISOU 3139 CB GLU A 294 13010 9344 7818 769 -1516 -1157 C ATOM 3140 CG GLU A 294 5.001 9.811 -12.120 1.00 90.38 C ANISOU 3140 CG GLU A 294 14436 10835 9069 777 -1501 -1184 C ATOM 3141 CD GLU A 294 4.292 11.112 -11.767 1.00106.62 C ANISOU 3141 CD GLU A 294 16492 12958 11061 709 -1439 -1051 C ATOM 3142 OE1 GLU A 294 4.069 11.379 -10.564 1.00 96.44 O ANISOU 3142 OE1 GLU A 294 15173 11629 9840 648 -1421 -933 O ATOM 3143 OE2 GLU A 294 3.891 11.830 -12.712 1.00 99.10 O ANISOU 3143 OE2 GLU A 294 15563 12099 9991 719 -1416 -1068 O ATOM 3144 N TYR A 295 8.335 7.968 -9.333 1.00 76.50 N ANISOU 3144 N TYR A 295 12571 8889 7607 810 -1443 -1134 N ATOM 3145 CA TYR A 295 8.925 7.201 -8.224 1.00 75.91 C ANISOU 3145 CA TYR A 295 12445 8723 7674 790 -1457 -1082 C ATOM 3146 C TYR A 295 9.583 8.138 -7.201 1.00 78.09 C ANISOU 3146 C TYR A 295 12695 9070 7906 753 -1342 -957 C ATOM 3147 O TYR A 295 9.442 7.930 -5.993 1.00 77.60 O ANISOU 3147 O TYR A 295 12580 8960 7945 697 -1351 -850 O ATOM 3148 CB TYR A 295 9.957 6.171 -8.724 1.00 77.95 C ANISOU 3148 CB TYR A 295 12703 8932 7983 870 -1487 -1212 C ATOM 3149 CG TYR A 295 9.374 5.023 -9.515 1.00 80.82 C ANISOU 3149 CG TYR A 295 13077 9195 8435 908 -1621 -1344 C ATOM 3150 CD1 TYR A 295 8.858 3.900 -8.874 1.00 83.25 C ANISOU 3150 CD1 TYR A 295 13339 9350 8941 870 -1737 -1317 C ATOM 3151 CD2 TYR A 295 9.433 5.009 -10.903 1.00 82.48 C ANISOU 3151 CD2 TYR A 295 13333 9467 8540 990 -1637 -1499 C ATOM 3152 CE1 TYR A 295 8.341 2.825 -9.598 1.00 85.57 C ANISOU 3152 CE1 TYR A 295 13639 9539 9336 906 -1872 -1444 C ATOM 3153 CE2 TYR A 295 8.933 3.934 -11.639 1.00 84.76 C ANISOU 3153 CE2 TYR A 295 13629 9664 8913 1033 -1767 -1639 C ATOM 3154 CZ TYR A 295 8.382 2.846 -10.984 1.00 92.53 C ANISOU 3154 CZ TYR A 295 14572 10479 10105 989 -1888 -1614 C ATOM 3155 OH TYR A 295 7.886 1.788 -11.713 1.00 93.82 O ANISOU 3155 OH TYR A 295 14740 10541 10368 1031 -2027 -1757 O ATOM 3156 N PHE A 296 10.273 9.181 -7.693 1.00 73.29 N ANISOU 3156 N PHE A 296 12116 8582 7149 785 -1240 -967 N ATOM 3157 CA PHE A 296 10.957 10.180 -6.876 1.00 71.89 C ANISOU 3157 CA PHE A 296 11918 8477 6921 758 -1134 -865 C ATOM 3158 C PHE A 296 9.949 11.114 -6.209 1.00 74.46 C ANISOU 3158 C PHE A 296 12230 8832 7230 685 -1119 -752 C ATOM 3159 O PHE A 296 10.044 11.360 -5.003 1.00 73.50 O ANISOU 3159 O PHE A 296 12063 8707 7154 638 -1089 -653 O ATOM 3160 CB PHE A 296 11.939 10.990 -7.739 1.00 73.68 C ANISOU 3160 CB PHE A 296 12174 8818 7004 817 -1044 -910 C ATOM 3161 CG PHE A 296 12.972 10.171 -8.474 1.00 76.28 C ANISOU 3161 CG PHE A 296 12515 9145 7325 901 -1051 -1026 C ATOM 3162 CD1 PHE A 296 14.235 9.974 -7.937 1.00 79.31 C ANISOU 3162 CD1 PHE A 296 12875 9527 7731 924 -996 -1010 C ATOM 3163 CD2 PHE A 296 12.684 9.605 -9.712 1.00 79.82 C ANISOU 3163 CD2 PHE A 296 12994 9599 7736 963 -1112 -1156 C ATOM 3164 CE1 PHE A 296 15.195 9.229 -8.624 1.00 81.28 C ANISOU 3164 CE1 PHE A 296 13132 9780 7969 1008 -1001 -1119 C ATOM 3165 CE2 PHE A 296 13.643 8.855 -10.396 1.00 83.66 C ANISOU 3165 CE2 PHE A 296 13486 10094 8207 1052 -1120 -1275 C ATOM 3166 CZ PHE A 296 14.892 8.671 -9.847 1.00 81.56 C ANISOU 3166 CZ PHE A 296 13197 9825 7966 1074 -1064 -1255 C ATOM 3167 N LEU A 297 8.976 11.619 -7.003 1.00 70.40 N ANISOU 3167 N LEU A 297 11750 8351 6646 678 -1141 -772 N ATOM 3168 CA LEU A 297 7.923 12.554 -6.594 1.00 69.20 C ANISOU 3168 CA LEU A 297 11593 8234 6468 618 -1132 -680 C ATOM 3169 C LEU A 297 7.091 12.022 -5.420 1.00 72.15 C ANISOU 3169 C LEU A 297 11919 8534 6961 557 -1194 -594 C ATOM 3170 O LEU A 297 6.846 12.781 -4.486 1.00 71.57 O ANISOU 3170 O LEU A 297 11813 8500 6881 513 -1155 -497 O ATOM 3171 CB LEU A 297 6.985 12.848 -7.781 1.00 69.72 C ANISOU 3171 CB LEU A 297 11702 8331 6458 627 -1166 -731 C ATOM 3172 CG LEU A 297 7.569 13.677 -8.935 1.00 74.69 C ANISOU 3172 CG LEU A 297 12363 9068 6948 677 -1099 -782 C ATOM 3173 CD1 LEU A 297 6.812 13.451 -10.222 1.00 75.70 C ANISOU 3173 CD1 LEU A 297 12527 9216 7020 705 -1154 -866 C ATOM 3174 CD2 LEU A 297 7.658 15.156 -8.580 1.00 75.92 C ANISOU 3174 CD2 LEU A 297 12505 9305 7035 646 -1013 -687 C ATOM 3175 N VAL A 298 6.673 10.736 -5.452 1.00 68.06 N ANISOU 3175 N VAL A 298 11389 7915 6556 557 -1293 -628 N ATOM 3176 CA VAL A 298 5.831 10.150 -4.397 1.00 66.96 C ANISOU 3176 CA VAL A 298 11191 7710 6539 499 -1364 -531 C ATOM 3177 C VAL A 298 6.682 9.893 -3.125 1.00 67.51 C ANISOU 3177 C VAL A 298 11194 7776 6679 483 -1326 -455 C ATOM 3178 O VAL A 298 6.131 9.963 -2.027 1.00 66.03 O ANISOU 3178 O VAL A 298 10947 7599 6544 432 -1340 -341 O ATOM 3179 CB VAL A 298 5.107 8.857 -4.856 1.00 72.24 C ANISOU 3179 CB VAL A 298 11860 8264 7323 502 -1494 -583 C ATOM 3180 CG1 VAL A 298 4.220 8.298 -3.744 1.00 72.13 C ANISOU 3180 CG1 VAL A 298 11772 8190 7445 439 -1569 -460 C ATOM 3181 CG2 VAL A 298 4.267 9.120 -6.103 1.00 72.41 C ANISOU 3181 CG2 VAL A 298 11943 8299 7270 515 -1532 -657 C ATOM 3182 N LEU A 299 8.004 9.655 -3.258 1.00 63.36 N ANISOU 3182 N LEU A 299 10676 7252 6147 528 -1276 -511 N ATOM 3183 CA LEU A 299 8.867 9.478 -2.078 1.00 62.81 C ANISOU 3183 CA LEU A 299 10543 7188 6134 513 -1232 -438 C ATOM 3184 C LEU A 299 8.871 10.770 -1.238 1.00 65.49 C ANISOU 3184 C LEU A 299 10860 7633 6392 480 -1146 -347 C ATOM 3185 O LEU A 299 8.794 10.705 -0.009 1.00 64.10 O ANISOU 3185 O LEU A 299 10611 7474 6271 441 -1143 -247 O ATOM 3186 CB LEU A 299 10.306 9.080 -2.474 1.00 63.18 C ANISOU 3186 CB LEU A 299 10607 7223 6175 571 -1189 -518 C ATOM 3187 CG LEU A 299 11.295 8.801 -1.313 1.00 67.39 C ANISOU 3187 CG LEU A 299 11075 7758 6772 558 -1144 -446 C ATOM 3188 CD1 LEU A 299 10.892 7.565 -0.506 1.00 67.68 C ANISOU 3188 CD1 LEU A 299 11035 7703 6979 522 -1235 -381 C ATOM 3189 CD2 LEU A 299 12.699 8.613 -1.829 1.00 70.58 C ANISOU 3189 CD2 LEU A 299 11506 8165 7144 619 -1090 -527 C ATOM 3190 N ALA A 300 8.906 11.939 -1.924 1.00 61.95 N ANISOU 3190 N ALA A 300 10466 7258 5815 498 -1083 -383 N ATOM 3191 CA ALA A 300 8.870 13.274 -1.320 1.00 60.81 C ANISOU 3191 CA ALA A 300 10306 7205 5594 474 -1009 -319 C ATOM 3192 C ALA A 300 7.495 13.571 -0.724 1.00 65.34 C ANISOU 3192 C ALA A 300 10848 7794 6185 424 -1052 -241 C ATOM 3193 O ALA A 300 7.395 14.347 0.228 1.00 65.33 O ANISOU 3193 O ALA A 300 10802 7857 6162 399 -1012 -172 O ATOM 3194 CB ALA A 300 9.222 14.327 -2.358 1.00 61.18 C ANISOU 3194 CB ALA A 300 10413 7310 5521 506 -949 -375 C ATOM 3195 N VAL A 301 6.439 12.953 -1.276 1.00 62.18 N ANISOU 3195 N VAL A 301 10466 7339 5821 413 -1136 -255 N ATOM 3196 CA VAL A 301 5.070 13.131 -0.797 1.00 62.00 C ANISOU 3196 CA VAL A 301 10412 7328 5815 367 -1186 -177 C ATOM 3197 C VAL A 301 4.865 12.270 0.469 1.00 67.01 C ANISOU 3197 C VAL A 301 10956 7942 6563 334 -1234 -80 C ATOM 3198 O VAL A 301 4.333 12.779 1.457 1.00 66.32 O ANISOU 3198 O VAL A 301 10810 7923 6466 304 -1223 11 O ATOM 3199 CB VAL A 301 4.027 12.804 -1.904 1.00 66.13 C ANISOU 3199 CB VAL A 301 10989 7803 6336 366 -1260 -223 C ATOM 3200 CG1 VAL A 301 2.609 12.731 -1.344 1.00 65.86 C ANISOU 3200 CG1 VAL A 301 10914 7769 6342 317 -1326 -130 C ATOM 3201 CG2 VAL A 301 4.103 13.823 -3.034 1.00 65.59 C ANISOU 3201 CG2 VAL A 301 10992 7785 6145 392 -1206 -292 C ATOM 3202 N LEU A 302 5.325 10.996 0.456 1.00 64.90 N ANISOU 3202 N LEU A 302 10668 7589 6403 343 -1287 -97 N ATOM 3203 CA LEU A 302 5.185 10.067 1.592 1.00 65.33 C ANISOU 3203 CA LEU A 302 10622 7618 6581 310 -1340 7 C ATOM 3204 C LEU A 302 6.037 10.523 2.814 1.00 70.21 C ANISOU 3204 C LEU A 302 11172 8324 7179 304 -1259 74 C ATOM 3205 O LEU A 302 5.774 10.090 3.941 1.00 69.36 O ANISOU 3205 O LEU A 302 10965 8246 7141 272 -1287 186 O ATOM 3206 CB LEU A 302 5.579 8.642 1.176 1.00 66.09 C ANISOU 3206 CB LEU A 302 10714 7591 6808 326 -1417 -38 C ATOM 3207 CG LEU A 302 4.700 7.989 0.099 1.00 71.23 C ANISOU 3207 CG LEU A 302 11411 8143 7508 330 -1521 -102 C ATOM 3208 CD1 LEU A 302 5.310 6.705 -0.392 1.00 72.56 C ANISOU 3208 CD1 LEU A 302 11581 8190 7798 361 -1588 -179 C ATOM 3209 CD2 LEU A 302 3.267 7.771 0.584 1.00 72.86 C ANISOU 3209 CD2 LEU A 302 11562 8344 7777 277 -1605 12 C ATOM 3210 N ASN A 303 7.010 11.432 2.582 1.00 67.76 N ANISOU 3210 N ASN A 303 10910 8066 6771 335 -1162 11 N ATOM 3211 CA ASN A 303 7.863 12.073 3.592 1.00 67.29 C ANISOU 3211 CA ASN A 303 10801 8094 6672 334 -1079 53 C ATOM 3212 C ASN A 303 7.036 12.868 4.594 1.00 71.44 C ANISOU 3212 C ASN A 303 11265 8723 7156 305 -1069 138 C ATOM 3213 O ASN A 303 7.427 13.006 5.754 1.00 71.05 O ANISOU 3213 O ASN A 303 11136 8751 7110 295 -1035 203 O ATOM 3214 CB ASN A 303 8.857 13.004 2.893 1.00 67.36 C ANISOU 3214 CB ASN A 303 10884 8128 6581 372 -992 -35 C ATOM 3215 CG ASN A 303 9.667 13.883 3.806 1.00 87.29 C ANISOU 3215 CG ASN A 303 13371 10742 9055 372 -908 -5 C ATOM 3216 OD1 ASN A 303 10.236 13.444 4.816 1.00 82.93 O ANISOU 3216 OD1 ASN A 303 12744 10215 8551 361 -895 52 O ATOM 3217 ND2 ASN A 303 9.754 15.146 3.442 1.00 76.02 N ANISOU 3217 ND2 ASN A 303 11989 9362 7533 386 -854 -43 N ATOM 3218 N SER A 304 5.901 13.411 4.126 1.00 68.38 N ANISOU 3218 N SER A 304 10912 8345 6724 295 -1100 135 N ATOM 3219 CA SER A 304 4.976 14.223 4.905 1.00 68.20 C ANISOU 3219 CA SER A 304 10840 8419 6653 275 -1097 201 C ATOM 3220 C SER A 304 4.272 13.388 6.006 1.00 72.75 C ANISOU 3220 C SER A 304 11304 9028 7309 243 -1162 325 C ATOM 3221 O SER A 304 3.824 13.954 7.005 1.00 72.58 O ANISOU 3221 O SER A 304 11213 9116 7248 234 -1152 392 O ATOM 3222 CB SER A 304 3.942 14.856 3.980 1.00 71.99 C ANISOU 3222 CB SER A 304 11392 8885 7076 273 -1117 164 C ATOM 3223 OG SER A 304 4.577 15.656 2.994 1.00 80.76 O ANISOU 3223 OG SER A 304 12590 9981 8114 302 -1059 67 O ATOM 3224 N GLY A 305 4.219 12.067 5.828 1.00 69.46 N ANISOU 3224 N GLY A 305 10863 8523 7006 229 -1231 356 N ATOM 3225 CA GLY A 305 3.603 11.158 6.794 1.00 69.58 C ANISOU 3225 CA GLY A 305 10760 8560 7117 196 -1302 490 C ATOM 3226 C GLY A 305 4.569 10.393 7.686 1.00 72.93 C ANISOU 3226 C GLY A 305 11092 8996 7621 191 -1291 550 C ATOM 3227 O GLY A 305 4.129 9.642 8.561 1.00 72.83 O ANISOU 3227 O GLY A 305 10962 9017 7691 162 -1347 678 O ATOM 3228 N THR A 306 5.893 10.567 7.470 1.00 68.63 N ANISOU 3228 N THR A 306 10594 8428 7054 218 -1220 467 N ATOM 3229 CA THR A 306 6.945 9.896 8.249 1.00 68.11 C ANISOU 3229 CA THR A 306 10452 8371 7058 216 -1197 513 C ATOM 3230 C THR A 306 7.198 10.631 9.568 1.00 70.57 C ANISOU 3230 C THR A 306 10669 8844 7301 211 -1133 585 C ATOM 3231 O THR A 306 7.531 9.992 10.567 1.00 70.16 O ANISOU 3231 O THR A 306 10502 8842 7315 194 -1142 685 O ATOM 3232 CB THR A 306 8.260 9.794 7.443 1.00 75.43 C ANISOU 3232 CB THR A 306 11468 9216 7977 251 -1144 395 C ATOM 3233 OG1 THR A 306 8.749 11.104 7.138 1.00 74.07 O ANISOU 3233 OG1 THR A 306 11368 9105 7669 277 -1054 314 O ATOM 3234 CG2 THR A 306 8.115 8.972 6.167 1.00 74.33 C ANISOU 3234 CG2 THR A 306 11410 8928 7903 266 -1210 311 C ATOM 3235 N ASN A 307 7.063 11.975 9.558 1.00 66.18 N ANISOU 3235 N ASN A 307 10157 8371 6616 230 -1072 529 N ATOM 3236 CA ASN A 307 7.292 12.846 10.712 1.00 65.27 C ANISOU 3236 CA ASN A 307 9966 8411 6422 237 -1013 562 C ATOM 3237 C ASN A 307 6.300 12.521 11.868 1.00 68.42 C ANISOU 3237 C ASN A 307 10224 8929 6842 214 -1065 702 C ATOM 3238 O ASN A 307 6.793 12.254 12.956 1.00 67.77 O ANISOU 3238 O ASN A 307 10030 8945 6774 209 -1045 777 O ATOM 3239 CB ASN A 307 7.190 14.323 10.314 1.00 66.42 C ANISOU 3239 CB ASN A 307 10193 8595 6448 262 -959 466 C ATOM 3240 CG ASN A 307 8.197 14.743 9.259 1.00 97.09 C ANISOU 3240 CG ASN A 307 14197 12389 10304 286 -905 349 C ATOM 3241 OD1 ASN A 307 9.291 14.173 9.128 1.00 93.43 O ANISOU 3241 OD1 ASN A 307 13746 11870 9882 292 -880 330 O ATOM 3242 ND2 ASN A 307 7.865 15.780 8.505 1.00 89.68 N ANISOU 3242 ND2 ASN A 307 13341 11441 9292 301 -885 275 N ATOM 3243 N PRO A 308 4.944 12.447 11.694 1.00 65.05 N ANISOU 3243 N PRO A 308 9789 8507 6420 199 -1132 750 N ATOM 3244 CA PRO A 308 4.081 12.122 12.852 1.00 64.86 C ANISOU 3244 CA PRO A 308 9616 8616 6412 182 -1180 898 C ATOM 3245 C PRO A 308 4.422 10.768 13.498 1.00 68.58 C ANISOU 3245 C PRO A 308 9969 9075 7012 153 -1227 1025 C ATOM 3246 O PRO A 308 4.353 10.651 14.724 1.00 68.63 O ANISOU 3246 O PRO A 308 9830 9234 7013 147 -1227 1141 O ATOM 3247 CB PRO A 308 2.678 12.084 12.246 1.00 66.82 C ANISOU 3247 CB PRO A 308 9899 8824 6663 168 -1251 921 C ATOM 3248 CG PRO A 308 2.760 12.964 11.060 1.00 71.07 C ANISOU 3248 CG PRO A 308 10595 9274 7133 189 -1213 772 C ATOM 3249 CD PRO A 308 4.125 12.722 10.493 1.00 66.70 C ANISOU 3249 CD PRO A 308 10113 8619 6612 200 -1167 682 C ATOM 3250 N ILE A 309 4.806 9.761 12.680 1.00 64.42 N ANISOU 3250 N ILE A 309 9499 8376 6603 138 -1269 1001 N ATOM 3251 CA ILE A 309 5.179 8.415 13.138 1.00 64.36 C ANISOU 3251 CA ILE A 309 9387 8321 6745 109 -1323 1111 C ATOM 3252 C ILE A 309 6.527 8.477 13.886 1.00 67.91 C ANISOU 3252 C ILE A 309 9784 8839 7180 120 -1242 1111 C ATOM 3253 O ILE A 309 6.671 7.819 14.915 1.00 68.41 O ANISOU 3253 O ILE A 309 9699 8983 7310 98 -1262 1249 O ATOM 3254 CB ILE A 309 5.239 7.407 11.941 1.00 67.51 C ANISOU 3254 CB ILE A 309 9873 8503 7274 100 -1394 1054 C ATOM 3255 CG1 ILE A 309 3.863 7.292 11.236 1.00 67.98 C ANISOU 3255 CG1 ILE A 309 9974 8500 7354 86 -1482 1063 C ATOM 3256 CG2 ILE A 309 5.734 6.025 12.392 1.00 68.53 C ANISOU 3256 CG2 ILE A 309 9896 8566 7577 74 -1451 1156 C ATOM 3257 CD1 ILE A 309 3.829 6.411 9.974 1.00 74.35 C ANISOU 3257 CD1 ILE A 309 10875 9100 8276 85 -1559 982 C ATOM 3258 N ILE A 310 7.484 9.301 13.403 1.00 63.15 N ANISOU 3258 N ILE A 310 9292 8215 6487 152 -1153 969 N ATOM 3259 CA ILE A 310 8.831 9.398 13.972 1.00 62.46 C ANISOU 3259 CA ILE A 310 9173 8176 6384 162 -1075 957 C ATOM 3260 C ILE A 310 8.777 9.982 15.406 1.00 64.64 C ANISOU 3260 C ILE A 310 9316 8669 6577 165 -1034 1039 C ATOM 3261 O ILE A 310 9.687 9.708 16.192 1.00 63.88 O ANISOU 3261 O ILE A 310 9138 8639 6496 161 -992 1085 O ATOM 3262 CB ILE A 310 9.749 10.253 13.056 1.00 65.30 C ANISOU 3262 CB ILE A 310 9684 8463 6663 197 -997 791 C ATOM 3263 CG1 ILE A 310 11.209 9.781 13.086 1.00 65.85 C ANISOU 3263 CG1 ILE A 310 9754 8485 6782 202 -948 772 C ATOM 3264 CG2 ILE A 310 9.605 11.759 13.292 1.00 65.78 C ANISOU 3264 CG2 ILE A 310 9783 8636 6574 222 -932 720 C ATOM 3265 CD1 ILE A 310 12.049 10.448 12.050 1.00 71.52 C ANISOU 3265 CD1 ILE A 310 10618 9120 7437 236 -886 625 C ATOM 3266 N TYR A 311 7.706 10.746 15.751 1.00 60.61 N ANISOU 3266 N TYR A 311 8777 8273 5979 173 -1048 1057 N ATOM 3267 CA TYR A 311 7.582 11.337 17.080 1.00 60.40 C ANISOU 3267 CA TYR A 311 8621 8466 5864 186 -1015 1120 C ATOM 3268 C TYR A 311 7.218 10.268 18.115 1.00 66.59 C ANISOU 3268 C TYR A 311 9217 9353 6730 156 -1071 1312 C ATOM 3269 O TYR A 311 7.993 10.057 19.052 1.00 66.39 O ANISOU 3269 O TYR A 311 9083 9436 6704 154 -1034 1373 O ATOM 3270 CB TYR A 311 6.553 12.483 17.124 1.00 60.72 C ANISOU 3270 CB TYR A 311 8685 8603 5785 213 -1014 1072 C ATOM 3271 CG TYR A 311 6.830 13.622 16.164 1.00 61.58 C ANISOU 3271 CG TYR A 311 8958 8622 5817 240 -964 900 C ATOM 3272 CD1 TYR A 311 8.055 14.288 16.177 1.00 63.08 C ANISOU 3272 CD1 TYR A 311 9203 8795 5967 260 -887 800 C ATOM 3273 CD2 TYR A 311 5.812 14.163 15.386 1.00 62.18 C ANISOU 3273 CD2 TYR A 311 9114 8662 5850 248 -992 851 C ATOM 3274 CE1 TYR A 311 8.307 15.360 15.319 1.00 63.16 C ANISOU 3274 CE1 TYR A 311 9349 8733 5915 284 -845 660 C ATOM 3275 CE2 TYR A 311 6.043 15.246 14.538 1.00 62.58 C ANISOU 3275 CE2 TYR A 311 9298 8644 5834 272 -948 708 C ATOM 3276 CZ TYR A 311 7.293 15.845 14.509 1.00 69.92 C ANISOU 3276 CZ TYR A 311 10280 9548 6737 290 -876 617 C ATOM 3277 OH TYR A 311 7.523 16.910 13.667 1.00 71.22 O ANISOU 3277 OH TYR A 311 10565 9648 6848 311 -838 493 O ATOM 3278 N THR A 312 6.078 9.556 17.909 1.00 64.52 N ANISOU 3278 N THR A 312 8915 9052 6547 130 -1165 1414 N ATOM 3279 CA THR A 312 5.546 8.517 18.811 1.00 65.54 C ANISOU 3279 CA THR A 312 8857 9278 6769 98 -1235 1621 C ATOM 3280 C THR A 312 6.523 7.324 19.010 1.00 72.13 C ANISOU 3280 C THR A 312 9621 10033 7750 66 -1247 1701 C ATOM 3281 O THR A 312 6.350 6.562 19.971 1.00 72.95 O ANISOU 3281 O THR A 312 9545 10247 7927 40 -1289 1882 O ATOM 3282 CB THR A 312 4.206 7.964 18.290 1.00 70.58 C ANISOU 3282 CB THR A 312 9491 9843 7483 72 -1340 1702 C ATOM 3283 OG1 THR A 312 4.388 7.432 16.979 1.00 70.22 O ANISOU 3283 OG1 THR A 312 9586 9550 7544 57 -1379 1615 O ATOM 3284 CG2 THR A 312 3.097 9.006 18.283 1.00 68.05 C ANISOU 3284 CG2 THR A 312 9203 9626 7028 99 -1338 1664 C ATOM 3285 N LEU A 313 7.541 7.167 18.134 1.00 69.06 N ANISOU 3285 N LEU A 313 9364 9468 7407 70 -1211 1575 N ATOM 3286 CA LEU A 313 8.477 6.053 18.257 1.00 69.56 C ANISOU 3286 CA LEU A 313 9372 9444 7615 45 -1223 1637 C ATOM 3287 C LEU A 313 9.752 6.454 19.039 1.00 74.91 C ANISOU 3287 C LEU A 313 10007 10233 8223 60 -1121 1617 C ATOM 3288 O LEU A 313 10.022 5.871 20.093 1.00 75.11 O ANISOU 3288 O LEU A 313 9864 10378 8296 38 -1124 1764 O ATOM 3289 CB LEU A 313 8.878 5.497 16.874 1.00 69.34 C ANISOU 3289 CB LEU A 313 9499 9158 7689 45 -1253 1518 C ATOM 3290 CG LEU A 313 7.768 4.963 15.957 1.00 74.11 C ANISOU 3290 CG LEU A 313 10157 9620 8382 31 -1360 1519 C ATOM 3291 CD1 LEU A 313 8.357 4.439 14.675 1.00 74.28 C ANISOU 3291 CD1 LEU A 313 10321 9412 8490 43 -1380 1383 C ATOM 3292 CD2 LEU A 313 6.954 3.864 16.624 1.00 77.44 C ANISOU 3292 CD2 LEU A 313 10405 10065 8953 -14 -1469 1726 C ATOM 3293 N THR A 314 10.533 7.423 18.523 1.00 71.64 N ANISOU 3293 N THR A 314 9737 9781 7702 94 -1036 1445 N ATOM 3294 CA THR A 314 11.818 7.813 19.115 1.00 71.57 C ANISOU 3294 CA THR A 314 9709 9848 7635 107 -943 1410 C ATOM 3295 C THR A 314 11.647 8.684 20.382 1.00 77.12 C ANISOU 3295 C THR A 314 10297 10804 8200 125 -895 1449 C ATOM 3296 O THR A 314 12.392 8.475 21.345 1.00 77.35 O ANISOU 3296 O THR A 314 10217 10949 8222 120 -851 1512 O ATOM 3297 CB THR A 314 12.674 8.565 18.100 1.00 76.74 C ANISOU 3297 CB THR A 314 10552 10377 8230 138 -877 1223 C ATOM 3298 OG1 THR A 314 11.955 9.711 17.647 1.00 75.21 O ANISOU 3298 OG1 THR A 314 10455 10203 7918 165 -867 1119 O ATOM 3299 CG2 THR A 314 13.066 7.694 16.914 1.00 75.31 C ANISOU 3299 CG2 THR A 314 10473 9969 8172 132 -913 1173 C ATOM 3300 N ASN A 315 10.710 9.663 20.381 1.00 73.60 N ANISOU 3300 N ASN A 315 9872 10448 7643 150 -904 1405 N ATOM 3301 CA ASN A 315 10.510 10.532 21.548 1.00 73.23 C ANISOU 3301 CA ASN A 315 9716 10645 7462 178 -866 1420 C ATOM 3302 C ASN A 315 9.198 10.144 22.261 1.00 78.39 C ANISOU 3302 C ASN A 315 10217 11450 8119 169 -938 1575 C ATOM 3303 O ASN A 315 8.121 10.619 21.895 1.00 77.85 O ANISOU 3303 O ASN A 315 10193 11384 8001 183 -975 1545 O ATOM 3304 CB ASN A 315 10.515 12.006 21.131 1.00 70.88 C ANISOU 3304 CB ASN A 315 9551 10348 7031 221 -815 1240 C ATOM 3305 CG ASN A 315 10.484 12.966 22.285 1.00 81.36 C ANISOU 3305 CG ASN A 315 10778 11909 8225 259 -774 1220 C ATOM 3306 OD1 ASN A 315 9.424 13.346 22.773 1.00 73.12 O ANISOU 3306 OD1 ASN A 315 9660 11011 7113 280 -806 1253 O ATOM 3307 ND2 ASN A 315 11.652 13.395 22.733 1.00 70.24 N ANISOU 3307 ND2 ASN A 315 9370 10542 6774 273 -705 1155 N ATOM 3308 N LYS A 316 9.304 9.278 23.289 1.00 76.29 N ANISOU 3308 N LYS A 316 9761 11315 7911 144 -960 1752 N ATOM 3309 CA LYS A 316 8.154 8.754 24.036 1.00 77.18 C ANISOU 3309 CA LYS A 316 9698 11584 8042 131 -1033 1936 C ATOM 3310 C LYS A 316 7.529 9.837 24.953 1.00 80.46 C ANISOU 3310 C LYS A 316 10024 12270 8279 182 -1007 1921 C ATOM 3311 O LYS A 316 6.418 9.632 25.459 1.00 80.59 O ANISOU 3311 O LYS A 316 9907 12435 8279 184 -1064 2055 O ATOM 3312 CB LYS A 316 8.545 7.513 24.868 1.00 81.01 C ANISOU 3312 CB LYS A 316 9994 12135 8651 89 -1062 2141 C ATOM 3313 CG LYS A 316 8.853 6.259 24.012 1.00 97.49 C ANISOU 3313 CG LYS A 316 12137 13959 10945 39 -1119 2186 C ATOM 3314 CD LYS A 316 7.611 5.733 23.230 1.00105.79 C ANISOU 3314 CD LYS A 316 13227 14875 12091 17 -1225 2235 C ATOM 3315 CE LYS A 316 7.887 4.573 22.293 1.00112.62 C ANISOU 3315 CE LYS A 316 14163 15469 13159 -23 -1290 2244 C ATOM 3316 NZ LYS A 316 8.371 3.358 22.998 1.00120.91 N ANISOU 3316 NZ LYS A 316 15038 16531 14370 -65 -1328 2428 N ATOM 3317 N GLU A 317 8.207 10.997 25.109 1.00 75.77 N ANISOU 3317 N GLU A 317 9505 11730 7556 227 -927 1752 N ATOM 3318 CA GLU A 317 7.696 12.159 25.849 1.00 75.11 C ANISOU 3318 CA GLU A 317 9363 11871 7304 286 -904 1689 C ATOM 3319 C GLU A 317 6.430 12.672 25.139 1.00 76.59 C ANISOU 3319 C GLU A 317 9640 12001 7459 302 -951 1639 C ATOM 3320 O GLU A 317 5.423 12.963 25.786 1.00 76.24 O ANISOU 3320 O GLU A 317 9483 12150 7335 331 -984 1704 O ATOM 3321 CB GLU A 317 8.795 13.240 25.942 1.00 76.03 C ANISOU 3321 CB GLU A 317 9563 11998 7328 323 -818 1505 C ATOM 3322 CG GLU A 317 8.416 14.502 26.703 1.00 87.85 C ANISOU 3322 CG GLU A 317 11005 13713 8661 391 -796 1408 C ATOM 3323 CD GLU A 317 9.442 15.624 26.672 1.00106.92 C ANISOU 3323 CD GLU A 317 13515 16103 11006 426 -727 1216 C ATOM 3324 OE1 GLU A 317 10.372 15.572 25.833 1.00 97.82 O ANISOU 3324 OE1 GLU A 317 12505 14739 9922 399 -693 1142 O ATOM 3325 OE2 GLU A 317 9.277 16.592 27.449 1.00100.39 O ANISOU 3325 OE2 GLU A 317 12620 15469 10057 484 -712 1136 O ATOM 3326 N MET A 318 6.487 12.706 23.792 1.00 71.33 N ANISOU 3326 N MET A 318 9172 11074 6859 282 -958 1535 N ATOM 3327 CA MET A 318 5.393 13.077 22.895 1.00 70.33 C ANISOU 3327 CA MET A 318 9157 10842 6723 286 -1002 1483 C ATOM 3328 C MET A 318 4.358 11.961 22.804 1.00 75.31 C ANISOU 3328 C MET A 318 9710 11449 7456 245 -1093 1662 C ATOM 3329 O MET A 318 3.158 12.240 22.835 1.00 75.00 O ANISOU 3329 O MET A 318 9643 11484 7368 259 -1138 1701 O ATOM 3330 CB MET A 318 5.936 13.399 21.490 1.00 71.52 C ANISOU 3330 CB MET A 318 9529 10730 6914 276 -975 1324 C ATOM 3331 CG MET A 318 6.742 14.667 21.411 1.00 74.06 C ANISOU 3331 CG MET A 318 9943 11056 7139 317 -898 1145 C ATOM 3332 SD MET A 318 7.548 14.819 19.803 1.00 77.02 S ANISOU 3332 SD MET A 318 10546 11142 7576 300 -868 1000 S ATOM 3333 CE MET A 318 8.208 16.429 19.926 1.00 72.98 C ANISOU 3333 CE MET A 318 10103 10681 6947 350 -796 824 C ATOM 3334 N ARG A 319 4.828 10.692 22.682 1.00 72.61 N ANISOU 3334 N ARG A 319 9330 10995 7263 195 -1125 1772 N ATOM 3335 CA ARG A 319 3.995 9.493 22.530 1.00 73.28 C ANISOU 3335 CA ARG A 319 9340 11020 7485 149 -1224 1946 C ATOM 3336 C ARG A 319 3.000 9.323 23.676 1.00 79.34 C ANISOU 3336 C ARG A 319 9895 12043 8208 156 -1270 2133 C ATOM 3337 O ARG A 319 1.878 8.874 23.427 1.00 79.42 O ANISOU 3337 O ARG A 319 9873 12029 8275 135 -1353 2241 O ATOM 3338 CB ARG A 319 4.865 8.236 22.449 1.00 72.94 C ANISOU 3338 CB ARG A 319 9260 10845 7608 101 -1243 2029 C ATOM 3339 N ARG A 320 3.397 9.681 24.923 1.00 76.86 N ANISOU 3339 N ARG A 320 9431 11983 7791 188 -1219 2173 N ATOM 3340 CA ARG A 320 2.536 9.525 26.097 1.00 77.63 C ANISOU 3340 CA ARG A 320 9304 12361 7830 204 -1258 2357 C ATOM 3341 C ARG A 320 1.424 10.611 26.087 1.00 80.82 C ANISOU 3341 C ARG A 320 9739 12887 8083 258 -1262 2281 C ATOM 3342 O ARG A 320 0.365 10.393 26.678 1.00 80.97 O ANISOU 3342 O ARG A 320 9607 13089 8070 268 -1317 2437 O ATOM 3343 CB ARG A 320 3.361 9.573 27.398 1.00 79.31 C ANISOU 3343 CB ARG A 320 9343 12815 7975 225 -1202 2416 C ATOM 3344 CG ARG A 320 2.612 9.005 28.610 1.00 96.09 C ANISOU 3344 CG ARG A 320 11202 15224 10085 226 -1255 2661 C ATOM 3345 CD ARG A 320 3.493 8.838 29.838 1.00112.66 C ANISOU 3345 CD ARG A 320 13115 17548 12141 236 -1206 2744 C ATOM 3346 NE ARG A 320 2.755 8.237 30.956 1.00126.09 N ANISOU 3346 NE ARG A 320 14547 19529 13832 235 -1261 2999 N ATOM 3347 CZ ARG A 320 3.288 7.943 32.140 1.00143.04 C ANISOU 3347 CZ ARG A 320 16482 21922 15944 242 -1235 3129 C ATOM 3348 NH1 ARG A 320 4.574 8.176 32.374 1.00132.26 N ANISOU 3348 NH1 ARG A 320 15147 20551 14556 246 -1155 3025 N ATOM 3349 NH2 ARG A 320 2.542 7.403 33.095 1.00129.65 N ANISOU 3349 NH2 ARG A 320 14536 20488 14237 243 -1290 3373 N ATOM 3350 N ALA A 321 1.639 11.734 25.362 1.00 76.25 N ANISOU 3350 N ALA A 321 9351 12196 7423 291 -1209 2054 N ATOM 3351 CA ALA A 321 0.650 12.809 25.236 1.00 75.86 C ANISOU 3351 CA ALA A 321 9351 12228 7246 342 -1211 1963 C ATOM 3352 C ALA A 321 -0.363 12.501 24.133 1.00 80.55 C ANISOU 3352 C ALA A 321 10058 12632 7916 309 -1279 1984 C ATOM 3353 O ALA A 321 -1.505 12.959 24.209 1.00 80.47 O ANISOU 3353 O ALA A 321 10023 12723 7831 336 -1311 2007 O ATOM 3354 CB ALA A 321 1.339 14.130 24.951 1.00 75.74 C ANISOU 3354 CB ALA A 321 9475 12176 7129 390 -1131 1723 C ATOM 3355 N PHE A 322 0.054 11.738 23.104 1.00 77.46 N ANISOU 3355 N PHE A 322 9791 11970 7670 253 -1301 1970 N ATOM 3356 CA PHE A 322 -0.815 11.339 22.000 1.00 77.58 C ANISOU 3356 CA PHE A 322 9916 11790 7772 217 -1371 1984 C ATOM 3357 C PHE A 322 -1.791 10.265 22.457 1.00 82.75 C ANISOU 3357 C PHE A 322 10407 12519 8516 181 -1470 2225 C ATOM 3358 O PHE A 322 -2.994 10.400 22.223 1.00 81.95 O ANISOU 3358 O PHE A 322 10309 12432 8394 182 -1525 2275 O ATOM 3359 CB PHE A 322 0.009 10.842 20.799 1.00 79.28 C ANISOU 3359 CB PHE A 322 10301 11712 8109 178 -1366 1883 C ATOM 3360 CG PHE A 322 -0.788 10.064 19.774 1.00 81.61 C ANISOU 3360 CG PHE A 322 10671 11808 8529 134 -1455 1930 C ATOM 3361 CD1 PHE A 322 -1.658 10.713 18.906 1.00 84.71 C ANISOU 3361 CD1 PHE A 322 11194 12123 8870 144 -1470 1841 C ATOM 3362 CD2 PHE A 322 -0.637 8.685 19.653 1.00 84.86 C ANISOU 3362 CD2 PHE A 322 11026 12101 9118 82 -1527 2057 C ATOM 3363 CE1 PHE A 322 -2.406 9.988 17.972 1.00 86.10 C ANISOU 3363 CE1 PHE A 322 11435 12120 9158 103 -1556 1882 C ATOM 3364 CE2 PHE A 322 -1.377 7.963 18.711 1.00 88.05 C ANISOU 3364 CE2 PHE A 322 11495 12316 9643 43 -1619 2090 C ATOM 3365 CZ PHE A 322 -2.254 8.618 17.876 1.00 85.79 C ANISOU 3365 CZ PHE A 322 11337 11966 9294 54 -1632 2001 C ATOM 3366 N ILE A 323 -1.271 9.200 23.115 1.00 81.07 N ANISOU 3366 N ILE A 323 10043 12353 8406 149 -1495 2383 N ATOM 3367 CA ILE A 323 -2.067 8.076 23.624 1.00 82.38 C ANISOU 3367 CA ILE A 323 10027 12592 8683 109 -1595 2639 C ATOM 3368 C ILE A 323 -3.050 8.611 24.711 1.00 88.08 C ANISOU 3368 C ILE A 323 10577 13633 9256 155 -1602 2753 C ATOM 3369 O ILE A 323 -4.101 8.002 24.937 1.00 88.76 O ANISOU 3369 O ILE A 323 10545 13784 9394 133 -1690 2945 O ATOM 3370 CB ILE A 323 -1.143 6.922 24.160 1.00 85.92 C ANISOU 3370 CB ILE A 323 10343 13026 9275 66 -1610 2776 C ATOM 3371 CG1 ILE A 323 -1.855 5.547 24.261 1.00 87.46 C ANISOU 3371 CG1 ILE A 323 10393 13179 9660 6 -1736 3028 C ATOM 3372 CG2 ILE A 323 -0.372 7.282 25.427 1.00 86.36 C ANISOU 3372 CG2 ILE A 323 10250 13342 9220 102 -1533 2803 C ATOM 3373 CD1 ILE A 323 -2.256 4.888 22.899 1.00 96.10 C ANISOU 3373 CD1 ILE A 323 11640 13954 10920 -41 -1822 2988 C ATOM 3374 N ARG A 324 -2.737 9.796 25.306 1.00 84.51 N ANISOU 3374 N ARG A 324 10121 13370 8619 223 -1513 2623 N ATOM 3375 CA ARG A 324 -3.563 10.470 26.314 1.00 84.74 C ANISOU 3375 CA ARG A 324 9999 13714 8483 285 -1508 2684 C ATOM 3376 C ARG A 324 -4.850 11.055 25.687 1.00 88.37 C ANISOU 3376 C ARG A 324 10550 14144 8883 304 -1545 2643 C ATOM 3377 O ARG A 324 -5.713 11.545 26.422 1.00 88.77 O ANISOU 3377 O ARG A 324 10488 14443 8795 361 -1548 2686 O ATOM 3378 CB ARG A 324 -2.764 11.584 27.009 1.00 84.19 C ANISOU 3378 CB ARG A 324 9921 13818 8249 355 -1409 2518 C ATOM 3379 N ILE A 325 -4.987 10.981 24.345 1.00 83.51 N ANISOU 3379 N ILE A 325 10126 13234 8368 260 -1576 2566 N ATOM 3380 CA ILE A 325 -6.162 11.479 23.631 1.00 96.19 C ANISOU 3380 CA ILE A 325 11830 14785 9934 269 -1612 2530 C ATOM 3381 C ILE A 325 -7.034 10.285 23.207 1.00116.89 C ANISOU 3381 C ILE A 325 14403 17300 12710 204 -1727 2733 C ATOM 3382 O ILE A 325 -6.514 9.249 22.791 1.00 76.00 O ANISOU 3382 O ILE A 325 9240 11935 7700 144 -1769 2789 O ATOM 3383 CB ILE A 325 -5.748 12.354 22.413 1.00 98.03 C ANISOU 3383 CB ILE A 325 12318 14783 10147 275 -1558 2276 C ATOM 3384 CG1 ILE A 325 -4.623 13.390 22.747 1.00 97.48 C ANISOU 3384 CG1 ILE A 325 12303 14764 9971 326 -1452 2078 C ATOM 3385 CG2 ILE A 325 -6.963 12.993 21.727 1.00 98.79 C ANISOU 3385 CG2 ILE A 325 12506 14845 10183 289 -1586 2234 C ATOM 3386 CD1 ILE A 325 -4.928 14.488 23.824 1.00103.01 C ANISOU 3386 CD1 ILE A 325 12895 15756 10487 409 -1406 2031 C TER 3387 ILE A 325 HETATM 3388 O4 ML5 A1201 3.019 17.282 -14.222 1.00 85.23 O ANISOU 3388 O4 ML5 A1201 13789 10786 7806 645 -1119 -778 O HETATM 3389 P1 ML5 A1201 3.207 15.798 -14.426 1.00 87.62 P ANISOU 3389 P1 ML5 A1201 14113 11020 8159 689 -1197 -900 P HETATM 3390 O2 ML5 A1201 1.909 15.040 -14.614 1.00 85.12 O ANISOU 3390 O2 ML5 A1201 13819 10628 7895 661 -1300 -935 O HETATM 3391 O3 ML5 A1201 4.263 15.465 -15.454 1.00 89.41 O ANISOU 3391 O3 ML5 A1201 14339 11335 8299 778 -1176 -1006 O HETATM 3392 C16 ML5 A1201 3.896 15.175 -12.864 1.00 87.69 C ANISOU 3392 C16 ML5 A1201 14105 10908 8305 670 -1198 -867 C HETATM 3393 C15 ML5 A1201 4.171 16.309 -11.872 1.00 86.10 C ANISOU 3393 C15 ML5 A1201 13876 10728 8109 625 -1116 -744 C HETATM 3394 C14 ML5 A1201 3.182 16.358 -10.701 1.00 85.14 C ANISOU 3394 C14 ML5 A1201 13741 10531 8077 552 -1149 -654 C HETATM 3395 N2 ML5 A1201 2.035 15.419 -10.871 1.00 85.47 N ANISOU 3395 N2 ML5 A1201 13799 10499 8176 531 -1252 -684 N HETATM 3396 C13 ML5 A1201 3.886 16.134 -9.393 1.00 84.60 C ANISOU 3396 C13 ML5 A1201 13640 10410 8092 538 -1128 -610 C HETATM 3397 O1 ML5 A1201 4.276 15.017 -9.107 1.00 85.31 O ANISOU 3397 O1 ML5 A1201 13726 10431 8255 557 -1172 -657 O HETATM 3398 N1 ML5 A1201 3.996 17.198 -8.589 1.00 83.35 N ANISOU 3398 N1 ML5 A1201 13455 10286 7929 505 -1066 -520 N HETATM 3399 C5 ML5 A1201 4.858 17.299 -7.543 1.00 82.85 C ANISOU 3399 C5 ML5 A1201 13360 10214 7907 503 -1022 -484 C HETATM 3400 C4 ML5 A1201 4.961 16.286 -6.581 1.00 82.92 C ANISOU 3400 C4 ML5 A1201 13342 10147 8015 490 -1063 -473 C HETATM 3401 C3 ML5 A1201 5.834 16.428 -5.501 1.00 82.46 C ANISOU 3401 C3 ML5 A1201 13245 10092 7993 486 -1015 -431 C HETATM 3402 C2 ML5 A1201 6.569 17.606 -5.342 1.00 81.87 C ANISOU 3402 C2 ML5 A1201 13161 10086 7861 492 -931 -402 C HETATM 3403 C6 ML5 A1201 5.587 18.481 -7.371 1.00 82.34 C ANISOU 3403 C6 ML5 A1201 13278 10215 7793 507 -939 -444 C HETATM 3404 C1 ML5 A1201 6.458 18.630 -6.286 1.00 81.78 C ANISOU 3404 C1 ML5 A1201 13172 10138 7762 503 -895 -408 C HETATM 3405 C7 ML5 A1201 7.240 19.917 -6.118 1.00 76.42 C ANISOU 3405 C7 ML5 A1201 12473 9522 7042 507 -815 -367 C HETATM 3406 C8 ML5 A1201 8.718 19.634 -5.864 1.00 74.72 C ANISOU 3406 C8 ML5 A1201 12246 9310 6833 542 -770 -387 C HETATM 3407 C9 ML5 A1201 9.456 20.907 -5.460 1.00 71.88 C ANISOU 3407 C9 ML5 A1201 11855 8998 6459 536 -702 -332 C HETATM 3408 C10 ML5 A1201 10.948 20.785 -5.743 1.00 70.58 C ANISOU 3408 C10 ML5 A1201 11690 8865 6263 581 -650 -352 C HETATM 3409 C11 ML5 A1201 11.639 22.139 -5.641 1.00 69.42 C ANISOU 3409 C11 ML5 A1201 11512 8767 6097 575 -592 -294 C HETATM 3410 C12 ML5 A1201 13.109 22.044 -5.986 1.00 69.26 C ANISOU 3410 C12 ML5 A1201 11486 8783 6047 618 -541 -299 C HETATM 3411 C1 NAG A1202 3.480 18.423 -31.453 1.00 94.52 C ANISOU 3411 C1 NAG A1202 14515 14250 7147 1447 -1094 -1471 C HETATM 3412 C2 NAG A1202 4.873 18.177 -32.114 1.00 97.47 C ANISOU 3412 C2 NAG A1202 14822 14824 7388 1580 -1058 -1546 C HETATM 3413 C3 NAG A1202 4.665 17.933 -33.659 1.00100.70 C ANISOU 3413 C3 NAG A1202 15156 15510 7595 1679 -1086 -1653 C HETATM 3414 C4 NAG A1202 3.217 17.564 -34.161 1.00101.67 C ANISOU 3414 C4 NAG A1202 15312 15607 7712 1645 -1171 -1739 C HETATM 3415 C5 NAG A1202 2.093 17.443 -33.063 1.00 99.47 C ANISOU 3415 C5 NAG A1202 15139 15019 7634 1515 -1223 -1705 C HETATM 3416 C6 NAG A1202 1.131 16.245 -33.266 1.00101.40 C ANISOU 3416 C6 NAG A1202 15454 15149 7926 1531 -1352 -1910 C HETATM 3417 C7 NAG A1202 7.220 19.266 -31.611 1.00 99.57 C ANISOU 3417 C7 NAG A1202 14990 15234 7609 1634 -901 -1348 C HETATM 3418 C8 NAG A1202 7.791 20.608 -31.228 1.00 99.52 C ANISOU 3418 C8 NAG A1202 14920 15270 7623 1577 -804 -1111 C HETATM 3419 N2 NAG A1202 5.828 19.281 -31.756 1.00 97.79 N ANISOU 3419 N2 NAG A1202 14801 14932 7422 1559 -952 -1350 N HETATM 3420 O3 NAG A1202 5.565 16.897 -34.093 1.00104.04 O ANISOU 3420 O3 NAG A1202 15568 16025 7939 1818 -1117 -1850 O HETATM 3421 O4 NAG A1202 2.817 18.535 -35.152 1.00104.43 O ANISOU 3421 O4 NAG A1202 15565 16195 7921 1629 -1121 -1605 O HETATM 3422 O5 NAG A1202 2.596 17.356 -31.724 1.00 96.50 O ANISOU 3422 O5 NAG A1202 14825 14418 7423 1464 -1202 -1651 O HETATM 3423 O6 NAG A1202 0.255 16.033 -32.140 1.00102.19 O ANISOU 3423 O6 NAG A1202 15645 14962 8219 1418 -1400 -1867 O HETATM 3424 O7 NAG A1202 7.951 18.283 -31.771 1.00102.55 O ANISOU 3424 O7 NAG A1202 15381 15639 7945 1739 -933 -1520 O CONECT 125 3411 CONECT 1200 1245 CONECT 1245 1200 CONECT 3051 3083 CONECT 3083 3051 CONECT 3388 3389 CONECT 3389 3388 3390 3391 3392 CONECT 3390 3389 CONECT 3391 3389 CONECT 3392 3389 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 3396 CONECT 3395 3394 CONECT 3396 3394 3397 3398 CONECT 3397 3396 CONECT 3398 3396 3399 CONECT 3399 3398 3400 3403 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3404 CONECT 3403 3399 3404 CONECT 3404 3402 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 CONECT 3411 125 3412 3422 CONECT 3412 3411 3413 3419 CONECT 3413 3412 3414 3420 CONECT 3414 3413 3415 3421 CONECT 3415 3414 3416 3422 CONECT 3416 3415 3423 CONECT 3417 3418 3419 3424 CONECT 3418 3417 CONECT 3419 3412 3417 CONECT 3420 3413 CONECT 3421 3414 CONECT 3422 3411 3415 CONECT 3423 3416 CONECT 3424 3417 MASTER 390 0 2 23 3 0 0 6 3423 1 42 40 END