HEADER HYDROLASE 12-DEC-11 3V2Y TITLE CRYSTAL STRUCTURE OF A LIPID G PROTEIN-COUPLED RECEPTOR AT 2.80A COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPHINGOSINE 1-PHOSPHATE RECEPTOR 1, LYSOZYME CHIMERA COMPND 3 (E.C.3.2.1.17); COMPND 4 CHAIN: A; COMPND 5 SYNONYM: S1P1,ENDOTHELIAL DIFFERENTIATION G-PROTEIN COUPLED RECEPTOR COMPND 6 1,SPHINGOSINE 1-PHOSPHATE RECEPTOR EDG-1,S1P RECEPTOR EDG-1,LYSIS COMPND 7 PROTEIN,LYSOZYME,MURAMIDASE; COMPND 8 EC: 3.2.1.17; COMPND 9 ENGINEERED: YES; COMPND 10 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 3V2Y 1 COMPND REMARK HETNAM LINK REVDAT 4 2 1 SITE REVDAT 3 21-JUN-17 3V2Y 1 COMPND SOURCE SEQADV REVDAT 2 14-MAR-12 3V2Y 1 JRNL REVDAT 1 15-FEB-12 3V2Y 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. 2.80 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) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.52 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 15275 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) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860 REMARK 3 FREE R VALUE TEST SET COUNT : 742 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.99 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2647 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2604 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2522 REMARK 3 BIN R VALUE (WORKING SET) : 0.2596 REMARK 3 BIN FREE R VALUE : 0.2762 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.72 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 125 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 : 3475 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 37 REMARK 3 SOLVENT ATOMS : 11 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 34.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.61 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.54870 REMARK 3 B22 (A**2) : 1.27490 REMARK 3 B33 (A**2) : -8.82360 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) : 0.440 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 : 0.906 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.859 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3585 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4893 ; 3.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1597 ; 20.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 56 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 529 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3585 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 511 ; 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 : 4387 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 0.65 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.24 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.20 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): 17.1445 18.5316 13.5414 REMARK 3 T TENSOR REMARK 3 T11: 0.2273 T22: -0.0572 REMARK 3 T33: -0.1172 T12: 0.0573 REMARK 3 T13: -0.0048 T23: 0.0225 REMARK 3 L TENSOR REMARK 3 L11: 1.7528 L22: 0.0000 REMARK 3 L33: 0.4655 L12: -0.2526 REMARK 3 L13: 0.7309 L23: -0.5602 REMARK 3 S TENSOR REMARK 3 S11: 0.0421 S12: -0.2737 S13: -0.1428 REMARK 3 S21: -0.1301 S22: -0.0121 S23: -0.0197 REMARK 3 S31: 0.0116 S32: -0.0999 S33: -0.0300 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3V2Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-11. REMARK 100 THE DEPOSITION ID IS D_1000069528. 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 : 77 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 : MICRODIFFACTION DATA ASSEMBLY REMARK 200 METHODS, SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15297 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 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 (%) : 97.2 REMARK 200 DATA REDUNDANCY : 6.000 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.42000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.900 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, LIPID 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A1211 LIES ON A SPECIAL POSITION. 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 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 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 SER A 38 OG REMARK 470 ASP A 40 CG OD1 OD2 REMARK 470 LYS A 41 CG CD CE NZ REMARK 470 GLU A 42 CG CD OE1 OE2 REMARK 470 ASN A 43 CG OD1 ND2 REMARK 470 SER A 44 OG REMARK 470 ILE A 45 CG1 CG2 CD1 REMARK 470 LYS A 72 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 ASN A 157 CG OD1 ND2 REMARK 470 ARG A 223 CG CD NE 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 LEU A 255 CG CD1 CD2 REMARK 470 LYS A 256 CG CD CE NZ 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 470 ARG A 328 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 329 C - N - CD ANGL. DEV. = -17.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 47.76 -75.60 REMARK 500 HIS A 77 33.57 -91.99 REMARK 500 MET A 180 45.94 -91.95 REMARK 500 ASN A1055 -3.86 69.11 REMARK 500 TYR A1161 -63.33 -123.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3V2W RELATED DB: PDB REMARK 900 3.35A RESOLUTION PROCESSED BY CONVENTIONAL RESOLUTION CUT OFF REMARK 900 METHODS REMARK 900 RELATED ID: GPCR-110 RELATED DB: TARGETDB 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 3V2Y A 2 231 UNP P21453 S1PR1_HUMAN 2 231 DBREF 3V2Y A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 3V2Y A 245 326 UNP P21453 S1PR1_HUMAN 244 326 SEQADV 3V2Y MET A -17 UNP P21453 EXPRESSION TAG SEQADV 3V2Y LYS A -16 UNP P21453 EXPRESSION TAG SEQADV 3V2Y THR A -15 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ILE A -14 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ILE A -13 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ALA A -12 UNP P21453 EXPRESSION TAG SEQADV 3V2Y LEU A -11 UNP P21453 EXPRESSION TAG SEQADV 3V2Y SER A -10 UNP P21453 EXPRESSION TAG SEQADV 3V2Y TYR A -9 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ILE A -8 UNP P21453 EXPRESSION TAG SEQADV 3V2Y PHE A -7 UNP P21453 EXPRESSION TAG SEQADV 3V2Y CYS A -6 UNP P21453 EXPRESSION TAG SEQADV 3V2Y LEU A -5 UNP P21453 EXPRESSION TAG SEQADV 3V2Y VAL A -4 UNP P21453 EXPRESSION TAG SEQADV 3V2Y PHE A -3 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ALA A -2 UNP P21453 EXPRESSION TAG SEQADV 3V2Y GLY A -1 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ALA A 0 UNP P21453 EXPRESSION TAG SEQADV 3V2Y PRO A 1 UNP P21453 EXPRESSION TAG SEQADV 3V2Y GLY A 1012 UNP P00720 ARG 12 CONFLICT SEQADV 3V2Y THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 3V2Y ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 3V2Y ARG A 1137 UNP P00720 ILE 137 CONFLICT SEQADV 3V2Y A UNP P21453 LYS 250 DELETION SEQADV 3V2Y ASN A 251 UNP P21453 SER 251 SEE REMARK 999 SEQADV 3V2Y VAL A 252 UNP P21453 LEU 252 SEE REMARK 999 SEQADV 3V2Y GLY A 327 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ARG A 328 UNP P21453 EXPRESSION TAG SEQADV 3V2Y PRO A 329 UNP P21453 EXPRESSION TAG SEQADV 3V2Y LEU A 330 UNP P21453 EXPRESSION TAG SEQADV 3V2Y GLU A 331 UNP P21453 EXPRESSION TAG SEQADV 3V2Y VAL A 332 UNP P21453 EXPRESSION TAG SEQADV 3V2Y LEU A 333 UNP P21453 EXPRESSION TAG SEQADV 3V2Y PHE A 334 UNP P21453 EXPRESSION TAG SEQADV 3V2Y GLN A 335 UNP P21453 EXPRESSION TAG SEQADV 3V2Y GLY A 336 UNP P21453 EXPRESSION TAG SEQADV 3V2Y PRO A 337 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 338 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 339 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 340 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 341 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 342 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 343 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 344 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 345 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 346 UNP P21453 EXPRESSION TAG SEQADV 3V2Y HIS A 347 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ASP A 348 UNP P21453 EXPRESSION TAG SEQADV 3V2Y TYR A 349 UNP P21453 EXPRESSION TAG SEQADV 3V2Y LYS A 350 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ASP A 351 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ASP A 352 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ASP A 353 UNP P21453 EXPRESSION TAG SEQADV 3V2Y ASP A 354 UNP P21453 EXPRESSION TAG SEQADV 3V2Y 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 3V2Y 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 FORMUL 4 HOH *11(H2 O) HELIX 1 1 TYR A 22 THR A 32 1 11 HELIX 2 2 LEU A 35 ASP A 40 5 6 HELIX 3 3 LYS A 41 THR A 73 1 33 HELIX 4 4 ARG A 78 SER A 105 1 28 HELIX 5 5 GLY A 106 TYR A 110 5 5 HELIX 6 6 THR A 113 LEU A 147 1 35 HELIX 7 7 ASN A 157 LEU A 177 1 21 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 GLY A 1051 1 14 HELIX 11 11 THR A 1059 LEU A 1079 1 21 HELIX 12 12 LEU A 1084 LEU A 1091 1 8 HELIX 13 13 ASP A 1092 MET A 1106 1 15 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 SER A 1136 THR A 1142 1 7 HELIX 18 18 THR A 1142 GLY A 1156 1 15 HELIX 19 19 THR A 1157 TYR A 1161 5 5 HELIX 20 20 GLU A 250 GLY A 281 1 32 HELIX 21 21 ALA A 293 ASN A 303 1 11 HELIX 22 22 THR A 306 ASN A 315 1 10 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 LEU A1032 -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 VAL A 16 -3.814 31.943 -31.268 1.00 80.16 N ANISOU 1 N VAL A 16 11262 11845 7348 192 341 1144 N ATOM 2 CA VAL A 16 -3.536 33.149 -30.490 1.00 79.15 C ANISOU 2 CA VAL A 16 11078 11604 7391 137 353 1288 C ATOM 3 C VAL A 16 -4.750 33.473 -29.608 1.00 81.20 C ANISOU 3 C VAL A 16 11441 11636 7774 47 349 1310 C ATOM 4 O VAL A 16 -5.852 33.663 -30.121 1.00 80.77 O ANISOU 4 O VAL A 16 11366 11618 7704 -20 363 1370 O ATOM 5 CB VAL A 16 -3.147 34.355 -31.401 1.00 84.01 C ANISOU 5 CB VAL A 16 11462 12434 8026 103 383 1497 C ATOM 6 CG1 VAL A 16 -2.873 35.610 -30.569 1.00 83.28 C ANISOU 6 CG1 VAL A 16 11311 12199 8132 46 378 1639 C ATOM 7 CG2 VAL A 16 -1.941 34.018 -32.283 1.00 84.95 C ANISOU 7 CG2 VAL A 16 11465 12806 8007 201 388 1483 C ATOM 8 N SER A 17 -4.542 33.492 -28.278 1.00 76.71 N ANISOU 8 N SER A 17 10983 10845 7318 51 329 1260 N ATOM 9 CA SER A 17 -5.566 33.787 -27.256 1.00 75.35 C ANISOU 9 CA SER A 17 10911 10456 7262 -15 321 1270 C ATOM 10 C SER A 17 -4.901 34.051 -25.918 1.00 78.21 C ANISOU 10 C SER A 17 11334 10637 7743 8 301 1238 C ATOM 11 O SER A 17 -3.673 33.981 -25.829 1.00 78.12 O ANISOU 11 O SER A 17 11291 10665 7725 69 295 1212 O ATOM 12 CB SER A 17 -6.553 32.624 -27.124 1.00 78.80 C ANISOU 12 CB SER A 17 11501 10817 7622 -18 300 1146 C ATOM 13 OG SER A 17 -7.433 32.552 -28.232 1.00 88.79 O ANISOU 13 OG SER A 17 12715 12219 8802 -61 315 1193 O ATOM 14 N ASP A 18 -5.705 34.309 -24.851 1.00 73.85 N ANISOU 14 N ASP A 18 10872 9895 7293 -35 291 1234 N ATOM 15 CA ASP A 18 -5.180 34.480 -23.486 1.00 72.87 C ANISOU 15 CA ASP A 18 10817 9598 7272 -9 269 1186 C ATOM 16 C ASP A 18 -4.327 33.289 -23.112 1.00 74.86 C ANISOU 16 C ASP A 18 11169 9826 7448 70 248 1038 C ATOM 17 O ASP A 18 -4.673 32.164 -23.479 1.00 74.69 O ANISOU 17 O ASP A 18 11225 9834 7319 92 238 943 O ATOM 18 CB ASP A 18 -6.330 34.637 -22.467 1.00 74.45 C ANISOU 18 CB ASP A 18 11112 9628 7548 -52 260 1177 C ATOM 19 CG ASP A 18 -6.981 36.008 -22.440 1.00 89.35 C ANISOU 19 CG ASP A 18 12905 11487 9556 -118 271 1314 C ATOM 20 OD1 ASP A 18 -6.245 37.010 -22.365 1.00 90.37 O ANISOU 20 OD1 ASP A 18 12931 11616 9787 -117 265 1389 O ATOM 21 OD2 ASP A 18 -8.231 36.070 -22.383 1.00 96.92 O1- ANISOU 21 OD2 ASP A 18 13901 12407 10519 -167 280 1343 O1- ATOM 22 N TYR A 19 -3.225 33.506 -22.377 1.00 69.88 N ANISOU 22 N TYR A 19 10536 9136 6880 112 237 1017 N ATOM 23 CA TYR A 19 -2.381 32.385 -21.958 1.00 69.07 C ANISOU 23 CA TYR A 19 10526 9004 6715 187 218 881 C ATOM 24 C TYR A 19 -3.077 31.635 -20.799 1.00 70.42 C ANISOU 24 C TYR A 19 10849 8999 6907 182 192 783 C ATOM 25 O TYR A 19 -2.496 31.344 -19.748 1.00 68.75 O ANISOU 25 O TYR A 19 10705 8680 6739 216 174 718 O ATOM 26 CB TYR A 19 -0.960 32.847 -21.618 1.00 70.39 C ANISOU 26 CB TYR A 19 10632 9179 6933 231 215 902 C ATOM 27 CG TYR A 19 -0.103 33.047 -22.855 1.00 72.82 C ANISOU 27 CG TYR A 19 10805 9695 7168 263 233 967 C ATOM 28 CD1 TYR A 19 1.254 33.329 -22.749 1.00 75.19 C ANISOU 28 CD1 TYR A 19 11040 10038 7489 310 229 995 C ATOM 29 CD2 TYR A 19 -0.642 32.905 -24.133 1.00 74.10 C ANISOU 29 CD2 TYR A 19 10901 10023 7230 250 252 1002 C ATOM 30 CE1 TYR A 19 2.051 33.486 -23.883 1.00 77.22 C ANISOU 30 CE1 TYR A 19 11162 10508 7669 345 244 1066 C ATOM 31 CE2 TYR A 19 0.144 33.056 -25.272 1.00 76.07 C ANISOU 31 CE2 TYR A 19 11015 10492 7397 288 268 1064 C ATOM 32 CZ TYR A 19 1.488 33.362 -25.143 1.00 85.38 C ANISOU 32 CZ TYR A 19 12123 11719 8598 336 264 1101 C ATOM 33 OH TYR A 19 2.269 33.503 -26.268 1.00 89.10 O ANISOU 33 OH TYR A 19 12449 12428 8979 379 279 1173 O ATOM 34 N VAL A 20 -4.371 31.367 -21.038 1.00 66.35 N ANISOU 34 N VAL A 20 10377 8470 6362 135 190 791 N ATOM 35 CA VAL A 20 -5.319 30.616 -20.234 1.00 65.17 C ANISOU 35 CA VAL A 20 10353 8194 6215 118 162 729 C ATOM 36 C VAL A 20 -5.963 29.560 -21.195 1.00 67.02 C ANISOU 36 C VAL A 20 10629 8499 6335 115 145 677 C ATOM 37 O VAL A 20 -7.043 29.030 -20.926 1.00 66.98 O ANISOU 37 O VAL A 20 10703 8425 6322 80 120 664 O ATOM 38 CB VAL A 20 -6.359 31.575 -19.553 1.00 68.77 C ANISOU 38 CB VAL A 20 10802 8565 6764 55 173 818 C ATOM 39 CG1 VAL A 20 -7.376 30.801 -18.718 1.00 68.36 C ANISOU 39 CG1 VAL A 20 10866 8404 6704 39 144 773 C ATOM 40 CG2 VAL A 20 -5.654 32.621 -18.687 1.00 68.33 C ANISOU 40 CG2 VAL A 20 10698 8442 6821 68 178 852 C ATOM 41 N ASN A 21 -5.272 29.275 -22.329 1.00 61.36 N ANISOU 41 N ASN A 21 9853 7931 5530 156 152 649 N ATOM 42 CA ASN A 21 -5.728 28.279 -23.294 1.00 60.49 C ANISOU 42 CA ASN A 21 9774 7900 5308 169 127 579 C ATOM 43 C ASN A 21 -5.019 26.951 -23.047 1.00 61.79 C ANISOU 43 C ASN A 21 10030 8020 5428 247 78 425 C ATOM 44 O ASN A 21 -3.826 26.922 -22.729 1.00 61.39 O ANISOU 44 O ASN A 21 9965 7973 5388 307 84 385 O ATOM 45 CB ASN A 21 -5.525 28.754 -24.747 1.00 60.96 C ANISOU 45 CB ASN A 21 9703 8173 5285 172 162 637 C ATOM 46 CG ASN A 21 -4.088 28.953 -25.151 1.00 78.75 C ANISOU 46 CG ASN A 21 11868 10549 7504 244 180 628 C ATOM 47 OD1 ASN A 21 -3.345 29.719 -24.538 1.00 74.19 O ANISOU 47 OD1 ASN A 21 11246 9933 7010 248 199 687 O ATOM 48 ND2 ASN A 21 -3.690 28.327 -26.244 1.00 67.81 N ANISOU 48 ND2 ASN A 21 10444 9328 5993 304 174 561 N ATOM 49 N TYR A 22 -5.767 25.853 -23.204 1.00 55.83 N ANISOU 49 N TYR A 22 9366 7218 4630 244 24 343 N ATOM 50 CA TYR A 22 -5.331 24.481 -22.947 1.00 54.42 C ANISOU 50 CA TYR A 22 9282 6966 4427 308 -41 195 C ATOM 51 C TYR A 22 -4.270 24.009 -23.956 1.00 56.51 C ANISOU 51 C TYR A 22 9500 7379 4592 401 -45 97 C ATOM 52 O TYR A 22 -3.525 23.072 -23.659 1.00 55.90 O ANISOU 52 O TYR A 22 9480 7249 4509 472 -88 -23 O ATOM 53 CB TYR A 22 -6.547 23.537 -22.987 1.00 55.21 C ANISOU 53 CB TYR A 22 9475 6984 4519 269 -110 155 C ATOM 54 CG TYR A 22 -7.731 24.042 -22.189 1.00 55.42 C ANISOU 54 CG TYR A 22 9531 6906 4621 179 -103 268 C ATOM 55 CD1 TYR A 22 -7.938 23.632 -20.876 1.00 56.79 C ANISOU 55 CD1 TYR A 22 9784 6919 4874 166 -139 265 C ATOM 56 CD2 TYR A 22 -8.646 24.933 -22.746 1.00 55.87 C ANISOU 56 CD2 TYR A 22 9529 7036 4665 109 -59 384 C ATOM 57 CE1 TYR A 22 -9.024 24.096 -20.135 1.00 56.81 C ANISOU 57 CE1 TYR A 22 9805 6847 4933 94 -133 369 C ATOM 58 CE2 TYR A 22 -9.721 25.422 -22.009 1.00 56.14 C ANISOU 58 CE2 TYR A 22 9585 6982 4763 35 -50 487 C ATOM 59 CZ TYR A 22 -9.912 24.995 -20.704 1.00 63.14 C ANISOU 59 CZ TYR A 22 10552 7720 5720 32 -87 477 C ATOM 60 OH TYR A 22 -10.982 25.461 -19.980 1.00 62.69 O ANISOU 60 OH TYR A 22 10509 7596 5713 -31 -80 578 O ATOM 61 N ASP A 23 -4.200 24.663 -25.138 1.00 52.36 N ANISOU 61 N ASP A 23 8861 7048 3987 403 0 153 N ATOM 62 CA ASP A 23 -3.262 24.333 -26.221 1.00 53.16 C ANISOU 62 CA ASP A 23 8891 7336 3971 496 3 76 C ATOM 63 C ASP A 23 -1.794 24.467 -25.762 1.00 55.57 C ANISOU 63 C ASP A 23 9165 7654 4295 569 25 57 C ATOM 64 O ASP A 23 -0.944 23.696 -26.214 1.00 55.92 O ANISOU 64 O ASP A 23 9210 7777 4260 667 1 -62 O ATOM 65 CB ASP A 23 -3.529 25.234 -27.451 1.00 55.85 C ANISOU 65 CB ASP A 23 9090 7894 4235 468 56 184 C ATOM 66 CG ASP A 23 -2.464 25.181 -28.537 1.00 67.73 C ANISOU 66 CG ASP A 23 10483 9636 5616 564 75 146 C ATOM 67 OD1 ASP A 23 -2.164 24.067 -29.024 1.00 69.24 O ANISOU 67 OD1 ASP A 23 10719 9874 5714 652 25 -15 O ATOM 68 OD2 ASP A 23 -1.964 26.259 -28.930 1.00 73.95 O1- ANISOU 68 OD2 ASP A 23 11131 10568 6399 553 133 280 O1- ATOM 69 N ILE A 24 -1.504 25.440 -24.868 1.00 50.13 N ANISOU 69 N ILE A 24 8449 6888 3710 524 65 169 N ATOM 70 CA ILE A 24 -0.157 25.655 -24.326 1.00 49.43 C ANISOU 70 CA ILE A 24 8333 6795 3653 580 84 168 C ATOM 71 C ILE A 24 0.332 24.367 -23.632 1.00 52.14 C ANISOU 71 C ILE A 24 8797 7011 4004 646 30 14 C ATOM 72 O ILE A 24 1.405 23.859 -23.975 1.00 52.05 O ANISOU 72 O ILE A 24 8765 7082 3929 739 24 -66 O ATOM 73 CB ILE A 24 -0.147 26.884 -23.363 1.00 51.59 C ANISOU 73 CB ILE A 24 8574 6972 4055 511 120 305 C ATOM 74 CG1 ILE A 24 -0.185 28.198 -24.166 1.00 52.21 C ANISOU 74 CG1 ILE A 24 8501 7204 4134 469 168 461 C ATOM 75 CG2 ILE A 24 1.069 26.853 -22.399 1.00 52.01 C ANISOU 75 CG2 ILE A 24 8649 6946 4166 558 120 278 C ATOM 76 CD1 ILE A 24 -0.350 29.433 -23.327 1.00 63.18 C ANISOU 76 CD1 ILE A 24 9855 8491 5660 398 189 588 C ATOM 77 N ILE A 25 -0.497 23.812 -22.707 1.00 47.33 N ANISOU 77 N ILE A 25 8304 6210 3469 599 -13 -21 N ATOM 78 CA ILE A 25 -0.206 22.583 -21.963 1.00 46.76 C ANISOU 78 CA ILE A 25 8343 5997 3428 643 -75 -147 C ATOM 79 C ILE A 25 0.078 21.419 -22.939 1.00 51.80 C ANISOU 79 C ILE A 25 9001 6715 3966 731 -127 -297 C ATOM 80 O ILE A 25 1.027 20.659 -22.717 1.00 51.71 O ANISOU 80 O ILE A 25 9020 6678 3949 812 -155 -400 O ATOM 81 CB ILE A 25 -1.371 22.268 -20.988 1.00 48.96 C ANISOU 81 CB ILE A 25 8717 6092 3794 565 -116 -128 C ATOM 82 CG1 ILE A 25 -1.166 23.042 -19.663 1.00 48.66 C ANISOU 82 CG1 ILE A 25 8680 5949 3859 524 -82 -40 C ATOM 83 CG2 ILE A 25 -1.516 20.753 -20.737 1.00 50.11 C ANISOU 83 CG2 ILE A 25 8967 6123 3951 601 -207 -260 C ATOM 84 CD1 ILE A 25 -2.287 22.950 -18.659 1.00 56.46 C ANISOU 84 CD1 ILE A 25 9737 6793 4924 451 -110 4 C ATOM 85 N VAL A 26 -0.698 21.332 -24.053 1.00 48.46 N ANISOU 85 N VAL A 26 8551 6400 3461 721 -140 -311 N ATOM 86 CA VAL A 26 -0.508 20.304 -25.082 1.00 49.18 C ANISOU 86 CA VAL A 26 8651 6586 3448 810 -195 -463 C ATOM 87 C VAL A 26 0.893 20.460 -25.708 1.00 54.59 C ANISOU 87 C VAL A 26 9245 7455 4042 918 -154 -500 C ATOM 88 O VAL A 26 1.660 19.504 -25.702 1.00 54.62 O ANISOU 88 O VAL A 26 9289 7443 4021 1015 -199 -639 O ATOM 89 CB VAL A 26 -1.624 20.336 -26.163 1.00 52.98 C ANISOU 89 CB VAL A 26 9108 7167 3854 772 -209 -456 C ATOM 90 CG1 VAL A 26 -1.407 19.243 -27.205 1.00 54.18 C ANISOU 90 CG1 VAL A 26 9271 7418 3896 876 -276 -635 C ATOM 91 CG2 VAL A 26 -3.005 20.203 -25.533 1.00 51.88 C ANISOU 91 CG2 VAL A 26 9055 6854 3803 665 -249 -404 C ATOM 92 N ARG A 27 1.243 21.690 -26.162 1.00 52.48 N ANISOU 92 N ARG A 27 8849 7354 3737 900 -73 -361 N ATOM 93 CA ARG A 27 2.549 22.002 -26.773 1.00 53.96 C ANISOU 93 CA ARG A 27 8925 7741 3837 993 -30 -354 C ATOM 94 C ARG A 27 3.721 21.745 -25.810 1.00 58.70 C ANISOU 94 C ARG A 27 9564 8242 4498 1044 -29 -386 C ATOM 95 O ARG A 27 4.806 21.359 -26.258 1.00 58.95 O ANISOU 95 O ARG A 27 9552 8399 4447 1154 -27 -458 O ATOM 96 CB ARG A 27 2.603 23.469 -27.242 1.00 56.00 C ANISOU 96 CB ARG A 27 9034 8161 4083 937 47 -161 C ATOM 97 CG ARG A 27 1.663 23.815 -28.401 1.00 73.04 C ANISOU 97 CG ARG A 27 11115 10478 6157 899 59 -113 C ATOM 98 CD ARG A 27 2.192 24.988 -29.230 1.00 89.03 C ANISOU 98 CD ARG A 27 12954 12749 8126 899 125 47 C ATOM 99 NE ARG A 27 2.395 26.200 -28.428 1.00 99.99 N ANISOU 99 NE ARG A 27 14295 14052 9646 817 168 221 N ATOM 100 CZ ARG A 27 1.611 27.273 -28.482 1.00116.68 C ANISOU 100 CZ ARG A 27 16343 16162 11827 712 198 378 C ATOM 101 NH1 ARG A 27 0.583 27.311 -29.323 1.00106.47 N ANISOU 101 NH1 ARG A 27 15020 14960 10475 669 200 397 N ATOM 102 NH2 ARG A 27 1.866 28.327 -27.719 1.00102.88 N ANISOU 102 NH2 ARG A 27 14556 14325 10209 650 223 515 N ATOM 103 N HIS A 28 3.513 21.996 -24.494 1.00 54.92 N ANISOU 103 N HIS A 28 9157 7553 4157 968 -28 -329 N ATOM 104 CA HIS A 28 4.561 21.828 -23.484 1.00 54.79 C ANISOU 104 CA HIS A 28 9175 7435 4207 1003 -24 -344 C ATOM 105 C HIS A 28 4.836 20.349 -23.185 1.00 59.10 C ANISOU 105 C HIS A 28 9829 7871 4754 1077 -96 -521 C ATOM 106 O HIS A 28 5.999 19.961 -23.100 1.00 58.94 O ANISOU 106 O HIS A 28 9799 7887 4710 1165 -94 -579 O ATOM 107 CB HIS A 28 4.215 22.581 -22.199 1.00 54.39 C ANISOU 107 CB HIS A 28 9158 7213 4293 902 -3 -232 C ATOM 108 CG HIS A 28 4.716 23.988 -22.209 1.00 57.62 C ANISOU 108 CG HIS A 28 9453 7713 4727 869 61 -75 C ATOM 109 ND1 HIS A 28 3.932 25.028 -22.667 1.00 59.32 N ANISOU 109 ND1 HIS A 28 9593 7993 4952 793 92 49 N ATOM 110 CD2 HIS A 28 5.947 24.466 -21.917 1.00 59.29 C ANISOU 110 CD2 HIS A 28 9604 7968 4954 905 91 -22 C ATOM 111 CE1 HIS A 28 4.690 26.107 -22.595 1.00 58.45 C ANISOU 111 CE1 HIS A 28 9381 7949 4877 783 133 172 C ATOM 112 NE2 HIS A 28 5.911 25.818 -22.148 1.00 58.85 N ANISOU 112 NE2 HIS A 28 9438 7991 4931 848 133 136 N ATOM 113 N TYR A 29 3.782 19.525 -23.061 1.00 55.47 N ANISOU 113 N TYR A 29 9465 7283 4328 1044 -165 -599 N ATOM 114 CA TYR A 29 3.953 18.089 -22.844 1.00 55.87 C ANISOU 114 CA TYR A 29 9611 7219 4398 1111 -251 -764 C ATOM 115 C TYR A 29 4.367 17.397 -24.169 1.00 62.55 C ANISOU 115 C TYR A 29 10422 8235 5110 1231 -283 -908 C ATOM 116 O TYR A 29 5.028 16.358 -24.139 1.00 62.37 O ANISOU 116 O TYR A 29 10444 8172 5083 1326 -339 -1051 O ATOM 117 CB TYR A 29 2.673 17.463 -22.254 1.00 56.12 C ANISOU 117 CB TYR A 29 9746 7055 4522 1029 -325 -781 C ATOM 118 CG TYR A 29 2.507 17.713 -20.767 1.00 55.55 C ANISOU 118 CG TYR A 29 9721 6804 4580 948 -316 -689 C ATOM 119 CD1 TYR A 29 2.854 16.743 -19.834 1.00 57.12 C ANISOU 119 CD1 TYR A 29 9995 6842 4866 969 -377 -756 C ATOM 120 CD2 TYR A 29 2.014 18.925 -20.293 1.00 55.14 C ANISOU 120 CD2 TYR A 29 9633 6751 4566 856 -250 -534 C ATOM 121 CE1 TYR A 29 2.710 16.968 -18.464 1.00 56.04 C ANISOU 121 CE1 TYR A 29 9891 6565 4838 899 -368 -669 C ATOM 122 CE2 TYR A 29 1.878 19.168 -18.926 1.00 54.80 C ANISOU 122 CE2 TYR A 29 9627 6563 4631 794 -243 -461 C ATOM 123 CZ TYR A 29 2.228 18.187 -18.014 1.00 58.70 C ANISOU 123 CZ TYR A 29 10191 6916 5197 816 -300 -527 C ATOM 124 OH TYR A 29 2.094 18.423 -16.669 1.00 54.31 O ANISOU 124 OH TYR A 29 9660 6240 4736 758 -292 -452 O ATOM 125 N ASN A 30 4.039 18.027 -25.322 1.00 61.11 N ANISOU 125 N ASN A 30 10149 8254 4816 1233 -245 -867 N ATOM 126 CA ASN A 30 4.408 17.547 -26.664 1.00 63.44 C ANISOU 126 CA ASN A 30 10386 8759 4960 1351 -265 -990 C ATOM 127 C ASN A 30 5.913 17.683 -26.891 1.00 69.37 C ANISOU 127 C ASN A 30 11055 9667 5636 1464 -219 -1002 C ATOM 128 O ASN A 30 6.548 16.768 -27.425 1.00 69.68 O ANISOU 128 O ASN A 30 11099 9779 5596 1594 -264 -1165 O ATOM 129 CB ASN A 30 3.649 18.349 -27.727 1.00 66.15 C ANISOU 129 CB ASN A 30 10635 9290 5210 1307 -225 -904 C ATOM 130 CG ASN A 30 3.726 17.821 -29.141 1.00 95.67 C ANISOU 130 CG ASN A 30 14316 13249 8786 1416 -256 -1036 C ATOM 131 OD1 ASN A 30 4.246 16.726 -29.417 1.00 88.27 O ANISOU 131 OD1 ASN A 30 13420 12316 7802 1536 -323 -1223 O ATOM 132 ND2 ASN A 30 3.164 18.595 -30.063 1.00 91.73 N ANISOU 132 ND2 ASN A 30 13717 12938 8200 1377 -211 -943 N ATOM 133 N TYR A 31 6.474 18.844 -26.504 1.00 66.54 N ANISOU 133 N TYR A 31 10616 9364 5303 1418 -133 -829 N ATOM 134 CA TYR A 31 7.892 19.152 -26.640 1.00 67.26 C ANISOU 134 CA TYR A 31 10618 9606 5333 1506 -84 -796 C ATOM 135 C TYR A 31 8.728 18.253 -25.722 1.00 71.65 C ANISOU 135 C TYR A 31 11265 10001 5958 1566 -120 -900 C ATOM 136 O TYR A 31 9.753 17.726 -26.154 1.00 71.82 O ANISOU 136 O TYR A 31 11252 10142 5893 1695 -126 -992 O ATOM 137 CB TYR A 31 8.137 20.642 -26.318 1.00 67.60 C ANISOU 137 CB TYR A 31 10561 9702 5423 1419 -2 -571 C ATOM 138 CG TYR A 31 9.563 21.102 -26.533 1.00 69.73 C ANISOU 138 CG TYR A 31 10718 10145 5631 1498 48 -501 C ATOM 139 CD1 TYR A 31 10.004 21.508 -27.789 1.00 72.79 C ANISOU 139 CD1 TYR A 31 10955 10832 5870 1569 81 -455 C ATOM 140 CD2 TYR A 31 10.449 21.213 -25.466 1.00 69.88 C ANISOU 140 CD2 TYR A 31 10768 10042 5741 1493 63 -460 C ATOM 141 CE1 TYR A 31 11.308 21.957 -27.988 1.00 74.16 C ANISOU 141 CE1 TYR A 31 11013 11179 5986 1639 123 -368 C ATOM 142 CE2 TYR A 31 11.757 21.654 -25.653 1.00 71.26 C ANISOU 142 CE2 TYR A 31 10838 10377 5863 1561 105 -380 C ATOM 143 CZ TYR A 31 12.181 22.035 -26.915 1.00 80.00 C ANISOU 143 CZ TYR A 31 11794 11781 6822 1633 134 -329 C ATOM 144 OH TYR A 31 13.467 22.484 -27.099 1.00 81.60 O ANISOU 144 OH TYR A 31 11881 12151 6971 1698 172 -231 O ATOM 145 N THR A 32 8.261 18.041 -24.470 1.00 68.18 N ANISOU 145 N THR A 32 10935 9300 5669 1477 -147 -886 N ATOM 146 CA THR A 32 8.976 17.229 -23.476 1.00 68.32 C ANISOU 146 CA THR A 32 11035 9150 5771 1515 -182 -962 C ATOM 147 C THR A 32 8.817 15.718 -23.754 1.00 73.97 C ANISOU 147 C THR A 32 11838 9788 6480 1601 -283 -1172 C ATOM 148 O THR A 32 9.595 14.919 -23.231 1.00 73.63 O ANISOU 148 O THR A 32 11841 9655 6480 1667 -316 -1260 O ATOM 149 CB THR A 32 8.511 17.573 -22.051 1.00 75.49 C ANISOU 149 CB THR A 32 12013 9833 6836 1391 -176 -862 C ATOM 150 OG1 THR A 32 7.125 17.257 -21.909 1.00 74.98 O ANISOU 150 OG1 THR A 32 12022 9639 6828 1310 -230 -880 O ATOM 151 CG2 THR A 32 8.770 19.037 -21.683 1.00 72.91 C ANISOU 151 CG2 THR A 32 11606 9562 6536 1316 -90 -672 C ATOM 152 N GLY A 33 7.824 15.353 -24.571 1.00 71.73 N ANISOU 152 N GLY A 33 11571 9536 6148 1599 -335 -1249 N ATOM 153 CA GLY A 33 7.557 13.964 -24.932 1.00 73.03 C ANISOU 153 CA GLY A 33 11813 9623 6313 1677 -447 -1453 C ATOM 154 C GLY A 33 6.717 13.236 -23.905 1.00 77.58 C ANISOU 154 C GLY A 33 12509 9914 7052 1590 -532 -1473 C ATOM 155 O GLY A 33 7.145 12.218 -23.361 1.00 77.04 O ANISOU 155 O GLY A 33 12507 9702 7064 1640 -603 -1578 O ATOM 156 N LYS A 34 5.507 13.755 -23.635 1.00 75.18 N ANISOU 156 N LYS A 34 12227 9536 6801 1460 -527 -1363 N ATOM 157 CA LYS A 34 4.584 13.180 -22.652 1.00 75.28 C ANISOU 157 CA LYS A 34 12338 9301 6963 1365 -604 -1347 C ATOM 158 C LYS A 34 3.144 13.105 -23.189 1.00 82.69 C ANISOU 158 C LYS A 34 13305 10219 7896 1295 -656 -1343 C ATOM 159 O LYS A 34 2.292 12.473 -22.560 1.00 82.18 O ANISOU 159 O LYS A 34 13318 9964 7944 1227 -741 -1342 O ATOM 160 CB LYS A 34 4.605 14.001 -21.358 1.00 75.82 C ANISOU 160 CB LYS A 34 12408 9272 7127 1261 -534 -1175 C ATOM 161 CG LYS A 34 5.807 13.735 -20.470 1.00 89.42 C ANISOU 161 CG LYS A 34 14139 10928 8908 1307 -518 -1185 C ATOM 162 CD LYS A 34 5.764 14.608 -19.227 1.00 96.78 C ANISOU 162 CD LYS A 34 15067 11780 9925 1205 -452 -1021 C ATOM 163 CE LYS A 34 6.775 14.188 -18.198 1.00104.17 C ANISOU 163 CE LYS A 34 16024 12618 10938 1234 -454 -1031 C ATOM 164 NZ LYS A 34 6.767 15.102 -17.030 1.00109.81 N ANISOU 164 NZ LYS A 34 16725 13275 11721 1143 -389 -881 N ATOM 165 N LEU A 35 2.870 13.759 -24.338 1.00 82.19 N ANISOU 165 N LEU A 35 13169 10357 7702 1307 -608 -1328 N ATOM 166 CA LEU A 35 1.534 13.808 -24.935 1.00 83.38 C ANISOU 166 CA LEU A 35 13335 10516 7832 1238 -645 -1311 C ATOM 167 C LEU A 35 1.098 12.433 -25.475 1.00 92.59 C ANISOU 167 C LEU A 35 14571 11602 9007 1298 -788 -1500 C ATOM 168 O LEU A 35 -0.004 11.979 -25.164 1.00 92.01 O ANISOU 168 O LEU A 35 14566 11372 9021 1216 -869 -1485 O ATOM 169 CB LEU A 35 1.489 14.859 -26.062 1.00 83.48 C ANISOU 169 CB LEU A 35 13236 10786 7698 1244 -554 -1244 C ATOM 170 CG LEU A 35 0.141 15.046 -26.767 1.00 88.16 C ANISOU 170 CG LEU A 35 13827 11416 8253 1169 -576 -1211 C ATOM 171 CD1 LEU A 35 -0.871 15.721 -25.855 1.00 86.83 C ANISOU 171 CD1 LEU A 35 13691 11108 8193 1019 -546 -1036 C ATOM 172 CD2 LEU A 35 0.306 15.843 -28.038 1.00 91.50 C ANISOU 172 CD2 LEU A 35 14127 12122 8518 1206 -501 -1180 C ATOM 173 N ASN A 36 1.948 11.791 -26.302 1.00 93.78 N ANISOU 173 N ASN A 36 14698 11867 9067 1443 -823 -1676 N ATOM 174 CA ASN A 36 1.630 10.495 -26.912 1.00 96.55 C ANISOU 174 CA ASN A 36 15108 12153 9422 1520 -969 -1881 C ATOM 175 C ASN A 36 1.759 9.342 -25.897 1.00104.21 C ANISOU 175 C ASN A 36 16176 12854 10567 1523 -1086 -1953 C ATOM 176 O ASN A 36 1.092 8.316 -26.053 1.00104.95 O ANISOU 176 O ASN A 36 16337 12807 10732 1527 -1228 -2067 O ATOM 177 CB ASN A 36 2.529 10.232 -28.131 1.00 98.01 C ANISOU 177 CB ASN A 36 15225 12568 9444 1688 -968 -2052 C ATOM 178 CG ASN A 36 2.285 11.171 -29.300 1.00116.05 C ANISOU 178 CG ASN A 36 17404 15135 11553 1693 -881 -1997 C ATOM 179 OD1 ASN A 36 1.145 11.527 -29.627 1.00109.28 O ANISOU 179 OD1 ASN A 36 16548 14285 10686 1597 -884 -1925 O ATOM 180 ND2 ASN A 36 3.349 11.529 -30.003 1.00106.88 N ANISOU 180 ND2 ASN A 36 16142 14221 10245 1811 -808 -2032 N ATOM 181 N ILE A 37 2.597 9.517 -24.852 1.00102.43 N ANISOU 181 N ILE A 37 15951 12553 10414 1516 -1031 -1880 N ATOM 182 CA ILE A 37 2.814 8.483 -23.829 1.00103.63 C ANISOU 182 CA ILE A 37 16178 12464 10733 1515 -1131 -1927 C ATOM 183 C ILE A 37 1.847 8.723 -22.617 1.00109.02 C ANISOU 183 C ILE A 37 16904 12959 11558 1353 -1138 -1745 C ATOM 184 O ILE A 37 1.982 8.073 -21.575 1.00108.48 O ANISOU 184 O ILE A 37 16881 12704 11635 1326 -1200 -1728 O ATOM 185 CB ILE A 37 4.323 8.436 -23.393 1.00106.84 C ANISOU 185 CB ILE A 37 16557 12904 11135 1609 -1074 -1959 C ATOM 186 CG1 ILE A 37 5.270 8.661 -24.612 1.00108.34 C ANISOU 186 CG1 ILE A 37 16670 13354 11140 1758 -1017 -2074 C ATOM 187 CG2 ILE A 37 4.653 7.108 -22.672 1.00108.37 C ANISOU 187 CG2 ILE A 37 16818 12871 11485 1648 -1203 -2065 C ATOM 188 CD1 ILE A 37 6.749 8.943 -24.263 1.00114.55 C ANISOU 188 CD1 ILE A 37 17408 14226 11891 1838 -928 -2058 C ATOM 189 N SER A 38 0.842 9.612 -22.795 1.00106.85 N ANISOU 189 N SER A 38 16611 12747 11241 1249 -1080 -1612 N ATOM 190 CA SER A 38 -0.152 9.911 -21.755 1.00106.44 C ANISOU 190 CA SER A 38 16590 12552 11300 1105 -1082 -1440 C ATOM 191 C SER A 38 -1.205 8.794 -21.642 1.00113.33 C ANISOU 191 C SER A 38 17534 13239 12288 1060 -1246 -1482 C ATOM 192 O SER A 38 -1.754 8.578 -20.557 1.00112.17 O ANISOU 192 O SER A 38 17417 12932 12269 968 -1288 -1369 O ATOM 193 CB SER A 38 -0.841 11.243 -22.038 1.00109.00 C ANISOU 193 CB SER A 38 16865 13011 11539 1020 -967 -1290 C ATOM 194 N ALA A 39 -1.478 8.081 -22.764 1.00113.08 N ANISOU 194 N ALA A 39 17521 13235 12210 1126 -1345 -1643 N ATOM 195 CA ALA A 39 -2.463 6.989 -22.816 1.00114.53 C ANISOU 195 CA ALA A 39 17768 13243 12504 1091 -1519 -1697 C ATOM 196 C ALA A 39 -1.832 5.622 -22.426 1.00121.27 C ANISOU 196 C ALA A 39 18665 13918 13493 1167 -1664 -1839 C ATOM 197 O ALA A 39 -2.419 4.566 -22.700 1.00121.89 O ANISOU 197 O ALA A 39 18791 13858 13663 1174 -1833 -1936 O ATOM 198 CB ALA A 39 -3.075 6.906 -24.211 1.00116.30 C ANISOU 198 CB ALA A 39 17990 13583 12617 1125 -1563 -1806 C ATOM 199 N ASP A 40 -0.654 5.652 -21.761 1.00118.75 N ANISOU 199 N ASP A 40 18328 13594 13198 1221 -1603 -1844 N ATOM 200 CA ASP A 40 0.040 4.447 -21.305 1.00120.01 C ANISOU 200 CA ASP A 40 18518 13589 13491 1291 -1724 -1960 C ATOM 201 C ASP A 40 -0.243 4.203 -19.822 1.00123.54 C ANISOU 201 C ASP A 40 18980 13847 14113 1182 -1759 -1795 C ATOM 202 O ASP A 40 -0.082 5.117 -19.006 1.00121.51 O ANISOU 202 O ASP A 40 18692 13641 13835 1115 -1627 -1633 O ATOM 203 CB ASP A 40 1.553 4.561 -21.558 1.00122.23 C ANISOU 203 CB ASP A 40 18763 13994 13683 1427 -1641 -2073 C ATOM 204 N LYS A 41 -0.702 2.968 -19.482 1.00121.67 N ANISOU 204 N LYS A 41 18782 13395 14051 1162 -1944 -1834 N ATOM 205 CA LYS A 41 -1.056 2.533 -18.117 1.00121.13 C ANISOU 205 CA LYS A 41 18717 13144 14165 1060 -2010 -1676 C ATOM 206 C LYS A 41 -2.111 3.482 -17.475 1.00123.92 C ANISOU 206 C LYS A 41 19052 13535 14496 915 -1926 -1442 C ATOM 207 O LYS A 41 -2.024 3.792 -16.280 1.00122.54 O ANISOU 207 O LYS A 41 18851 13328 14381 847 -1870 -1284 O ATOM 208 CB LYS A 41 0.199 2.422 -17.224 1.00123.24 C ANISOU 208 CB LYS A 41 18959 13384 14484 1104 -1955 -1668 C ATOM 209 N GLU A 42 -3.116 3.920 -18.279 1.00120.41 N ANISOU 209 N GLU A 42 18620 13166 13966 873 -1921 -1425 N ATOM 210 CA GLU A 42 -4.201 4.796 -17.815 1.00118.79 C ANISOU 210 CA GLU A 42 18400 13002 13734 745 -1850 -1217 C ATOM 211 C GLU A 42 -5.135 4.041 -16.862 1.00122.42 C ANISOU 211 C GLU A 42 18867 13277 14368 642 -1989 -1078 C ATOM 212 O GLU A 42 -5.666 4.639 -15.923 1.00120.65 O ANISOU 212 O GLU A 42 18616 13067 14159 547 -1925 -883 O ATOM 213 CB GLU A 42 -4.991 5.355 -19.006 1.00120.28 C ANISOU 213 CB GLU A 42 18595 13315 13789 734 -1819 -1246 C ATOM 214 N ASN A 43 -5.323 2.716 -17.103 1.00120.21 N ANISOU 214 N ASN A 43 18618 12829 14225 665 -2188 -1177 N ATOM 215 CA ASN A 43 -6.137 1.840 -16.251 1.00120.02 C ANISOU 215 CA ASN A 43 18592 12619 14391 573 -2350 -1046 C ATOM 216 C ASN A 43 -5.438 1.614 -14.910 1.00122.57 C ANISOU 216 C ASN A 43 18873 12873 14823 558 -2335 -948 C ATOM 217 O ASN A 43 -6.100 1.538 -13.873 1.00121.85 O ANISOU 217 O ASN A 43 18748 12723 14827 458 -2371 -750 O ATOM 218 CB ASN A 43 -6.402 0.505 -16.949 1.00121.97 C ANISOU 218 CB ASN A 43 18879 12701 14764 612 -2576 -1196 C ATOM 219 N SER A 44 -4.089 1.535 -14.932 1.00118.32 N ANISOU 219 N SER A 44 18332 12361 14263 661 -2278 -1082 N ATOM 220 CA SER A 44 -3.267 1.375 -13.733 1.00117.17 C ANISOU 220 CA SER A 44 18146 12169 14204 659 -2247 -1007 C ATOM 221 C SER A 44 -3.116 2.711 -12.990 1.00117.63 C ANISOU 221 C SER A 44 18167 12385 14144 612 -2043 -857 C ATOM 222 O SER A 44 -2.852 2.715 -11.784 1.00116.70 O ANISOU 222 O SER A 44 18005 12238 14097 570 -2019 -729 O ATOM 223 CB SER A 44 -1.894 0.819 -14.098 1.00121.76 C ANISOU 223 CB SER A 44 18739 12725 14797 789 -2259 -1207 C ATOM 224 N ILE A 45 -3.291 3.847 -13.714 1.00111.96 N ANISOU 224 N ILE A 45 17458 11832 13249 621 -1903 -873 N ATOM 225 CA ILE A 45 -3.208 5.196 -13.140 1.00109.35 C ANISOU 225 CA ILE A 45 17093 11647 12808 581 -1719 -745 C ATOM 226 C ILE A 45 -4.379 5.440 -12.173 1.00110.36 C ANISOU 226 C ILE A 45 17192 11752 12988 459 -1735 -528 C ATOM 227 O ILE A 45 -4.191 6.093 -11.144 1.00109.19 O ANISOU 227 O ILE A 45 17002 11659 12826 424 -1638 -406 O ATOM 228 CB ILE A 45 -3.172 6.268 -14.252 1.00112.01 C ANISOU 228 CB ILE A 45 17440 12156 12965 618 -1590 -813 C ATOM 229 N LYS A 46 -5.585 4.900 -12.500 1.00105.30 N ANISOU 229 N LYS A 46 16570 11035 12404 399 -1862 -481 N ATOM 230 CA LYS A 46 -6.774 5.004 -11.640 1.00103.50 C ANISOU 230 CA LYS A 46 16310 10788 12229 287 -1896 -267 C ATOM 231 C LYS A 46 -6.529 4.260 -10.324 1.00104.89 C ANISOU 231 C LYS A 46 16436 10864 12554 256 -1975 -158 C ATOM 232 O LYS A 46 -6.881 4.763 -9.257 1.00103.44 O ANISOU 232 O LYS A 46 16199 10737 12365 196 -1917 14 O ATOM 233 CB LYS A 46 -8.018 4.443 -12.360 1.00106.83 C ANISOU 233 CB LYS A 46 16761 11137 12691 236 -2035 -248 C ATOM 234 CG LYS A 46 -9.318 4.607 -11.568 1.00119.42 C ANISOU 234 CG LYS A 46 18319 12734 14323 122 -2067 -15 C ATOM 235 CD LYS A 46 -10.478 3.873 -12.220 1.00129.63 C ANISOU 235 CD LYS A 46 19640 13932 15683 69 -2231 10 C ATOM 236 CE LYS A 46 -11.740 3.976 -11.399 1.00137.31 C ANISOU 236 CE LYS A 46 20566 14911 16695 -41 -2270 257 C ATOM 237 NZ LYS A 46 -12.874 3.259 -12.038 1.00146.39 N ANISOU 237 NZ LYS A 46 21741 15964 17914 -99 -2436 293 N ATOM 238 N LEU A 47 -5.880 3.083 -10.404 1.00100.74 N ANISOU 238 N LEU A 47 15921 10199 12158 304 -2106 -264 N ATOM 239 CA LEU A 47 -5.534 2.267 -9.239 1.00 99.87 C ANISOU 239 CA LEU A 47 15755 9984 12205 279 -2193 -171 C ATOM 240 C LEU A 47 -4.492 2.971 -8.385 1.00100.05 C ANISOU 240 C LEU A 47 15741 10108 12167 308 -2036 -148 C ATOM 241 O LEU A 47 -4.542 2.882 -7.161 1.00 99.50 O ANISOU 241 O LEU A 47 15604 10037 12163 256 -2040 8 O ATOM 242 CB LEU A 47 -5.006 0.890 -9.686 1.00101.50 C ANISOU 242 CB LEU A 47 15987 10015 12566 336 -2368 -318 C ATOM 243 CG LEU A 47 -5.865 0.136 -10.707 1.00107.62 C ANISOU 243 CG LEU A 47 16809 10678 13403 329 -2538 -393 C ATOM 244 CD1 LEU A 47 -5.161 -1.114 -11.190 1.00109.35 C ANISOU 244 CD1 LEU A 47 17054 10731 13762 410 -2698 -577 C ATOM 245 CD2 LEU A 47 -7.239 -0.194 -10.138 1.00110.70 C ANISOU 245 CD2 LEU A 47 17159 11007 13893 208 -2657 -175 C ATOM 246 N THR A 48 -3.559 3.694 -9.038 1.00 93.63 N ANISOU 246 N THR A 48 14963 9390 11222 391 -1899 -297 N ATOM 247 CA THR A 48 -2.497 4.443 -8.372 1.00 91.30 C ANISOU 247 CA THR A 48 14638 9192 10858 425 -1748 -291 C ATOM 248 C THR A 48 -3.097 5.631 -7.593 1.00 90.73 C ANISOU 248 C THR A 48 14527 9251 10697 358 -1623 -126 C ATOM 249 O THR A 48 -2.850 5.762 -6.394 1.00 89.21 O ANISOU 249 O THR A 48 14277 9082 10537 329 -1589 -14 O ATOM 250 CB THR A 48 -1.452 4.908 -9.417 1.00 99.63 C ANISOU 250 CB THR A 48 15737 10323 11796 530 -1649 -482 C ATOM 251 OG1 THR A 48 -0.973 3.772 -10.139 1.00 99.81 O ANISOU 251 OG1 THR A 48 15794 10231 11897 602 -1774 -644 O ATOM 252 CG2 THR A 48 -0.276 5.659 -8.787 1.00 97.57 C ANISOU 252 CG2 THR A 48 15446 10154 11471 567 -1502 -478 C ATOM 253 N SER A 49 -3.918 6.461 -8.271 1.00 84.97 N ANISOU 253 N SER A 49 13821 8606 9857 335 -1564 -112 N ATOM 254 CA SER A 49 -4.519 7.657 -7.682 1.00 82.65 C ANISOU 254 CA SER A 49 13494 8437 9473 283 -1447 23 C ATOM 255 C SER A 49 -5.416 7.320 -6.462 1.00 84.06 C ANISOU 255 C SER A 49 13612 8594 9733 200 -1517 220 C ATOM 256 O SER A 49 -5.117 7.782 -5.361 1.00 83.47 O ANISOU 256 O SER A 49 13483 8586 9646 190 -1446 307 O ATOM 257 CB SER A 49 -5.313 8.436 -8.730 1.00 85.71 C ANISOU 257 CB SER A 49 13917 8900 9750 270 -1395 3 C ATOM 258 OG SER A 49 -6.287 7.627 -9.367 1.00 95.72 O ANISOU 258 OG SER A 49 15213 10082 11073 234 -1531 8 O ATOM 259 N VAL A 50 -6.462 6.469 -6.645 1.00 78.82 N ANISOU 259 N VAL A 50 12950 7841 9156 145 -1664 291 N ATOM 260 CA VAL A 50 -7.421 6.094 -5.579 1.00 77.54 C ANISOU 260 CA VAL A 50 12719 7671 9071 64 -1745 499 C ATOM 261 C VAL A 50 -6.676 5.583 -4.307 1.00 79.09 C ANISOU 261 C VAL A 50 12844 7848 9361 65 -1768 568 C ATOM 262 O VAL A 50 -7.070 5.931 -3.188 1.00 77.88 O ANISOU 262 O VAL A 50 12615 7783 9193 24 -1735 729 O ATOM 263 CB VAL A 50 -8.460 5.051 -6.084 1.00 82.36 C ANISOU 263 CB VAL A 50 13344 8159 9790 11 -1929 548 C ATOM 264 CG1 VAL A 50 -9.347 4.548 -4.946 1.00 82.34 C ANISOU 264 CG1 VAL A 50 13254 8151 9882 -71 -2028 781 C ATOM 265 CG2 VAL A 50 -9.316 5.636 -7.205 1.00 82.01 C ANISOU 265 CG2 VAL A 50 13358 8157 9644 -2 -1898 511 C ATOM 266 N VAL A 51 -5.588 4.809 -4.490 1.00 74.85 N ANISOU 266 N VAL A 51 12324 7207 8907 118 -1817 443 N ATOM 267 CA VAL A 51 -4.789 4.286 -3.376 1.00 74.12 C ANISOU 267 CA VAL A 51 12165 7091 8907 121 -1838 497 C ATOM 268 C VAL A 51 -4.008 5.440 -2.699 1.00 75.65 C ANISOU 268 C VAL A 51 12335 7430 8979 154 -1655 493 C ATOM 269 O VAL A 51 -4.032 5.548 -1.471 1.00 74.95 O ANISOU 269 O VAL A 51 12164 7408 8905 121 -1635 630 O ATOM 270 CB VAL A 51 -3.844 3.134 -3.838 1.00 78.76 C ANISOU 270 CB VAL A 51 12781 7520 9622 175 -1944 355 C ATOM 271 CG1 VAL A 51 -2.685 2.926 -2.865 1.00 78.27 C ANISOU 271 CG1 VAL A 51 12665 7463 9611 200 -1906 367 C ATOM 272 CG2 VAL A 51 -4.624 1.836 -4.032 1.00 79.86 C ANISOU 272 CG2 VAL A 51 12910 7501 9933 127 -2159 410 C ATOM 273 N PHE A 52 -3.361 6.321 -3.502 1.00 70.36 N ANISOU 273 N PHE A 52 11729 6817 8188 216 -1528 343 N ATOM 274 CA PHE A 52 -2.569 7.436 -2.964 1.00 68.39 C ANISOU 274 CA PHE A 52 11461 6690 7834 248 -1367 328 C ATOM 275 C PHE A 52 -3.456 8.505 -2.305 1.00 69.16 C ANISOU 275 C PHE A 52 11517 6920 7839 204 -1286 458 C ATOM 276 O PHE A 52 -2.985 9.213 -1.415 1.00 67.23 O ANISOU 276 O PHE A 52 11229 6770 7546 214 -1192 494 O ATOM 277 CB PHE A 52 -1.684 8.063 -4.047 1.00 69.93 C ANISOU 277 CB PHE A 52 11724 6910 7935 323 -1269 152 C ATOM 278 CG PHE A 52 -0.356 7.361 -4.203 1.00 72.12 C ANISOU 278 CG PHE A 52 12016 7115 8270 388 -1289 32 C ATOM 279 CD1 PHE A 52 0.704 7.645 -3.350 1.00 74.78 C ANISOU 279 CD1 PHE A 52 12317 7495 8603 412 -1211 40 C ATOM 280 CD2 PHE A 52 -0.172 6.394 -5.185 1.00 75.59 C ANISOU 280 CD2 PHE A 52 12505 7444 8771 429 -1391 -91 C ATOM 281 CE1 PHE A 52 1.918 6.965 -3.468 1.00 76.30 C ANISOU 281 CE1 PHE A 52 12519 7621 8851 471 -1231 -60 C ATOM 282 CE2 PHE A 52 1.049 5.725 -5.312 1.00 79.04 C ANISOU 282 CE2 PHE A 52 12952 7817 9263 497 -1412 -204 C ATOM 283 CZ PHE A 52 2.085 6.013 -4.451 1.00 76.55 C ANISOU 283 CZ PHE A 52 12598 7545 8942 516 -1330 -182 C ATOM 284 N ILE A 53 -4.744 8.585 -2.701 1.00 65.47 N ANISOU 284 N ILE A 53 11060 6462 7354 157 -1330 530 N ATOM 285 CA ILE A 53 -5.710 9.503 -2.082 1.00 64.47 C ANISOU 285 CA ILE A 53 10889 6459 7146 118 -1269 662 C ATOM 286 C ILE A 53 -6.000 9.021 -0.647 1.00 66.97 C ANISOU 286 C ILE A 53 11106 6813 7526 78 -1325 830 C ATOM 287 O ILE A 53 -6.070 9.840 0.269 1.00 66.18 O ANISOU 287 O ILE A 53 10950 6841 7354 81 -1240 898 O ATOM 288 CB ILE A 53 -7.009 9.628 -2.940 1.00 68.00 C ANISOU 288 CB ILE A 53 11372 6903 7561 77 -1308 700 C ATOM 289 CG1 ILE A 53 -6.703 10.290 -4.306 1.00 68.34 C ANISOU 289 CG1 ILE A 53 11497 6948 7521 118 -1232 544 C ATOM 290 CG2 ILE A 53 -8.106 10.412 -2.184 1.00 68.38 C ANISOU 290 CG2 ILE A 53 11364 7077 7541 36 -1264 858 C ATOM 291 CD1 ILE A 53 -7.744 9.998 -5.416 1.00 77.54 C ANISOU 291 CD1 ILE A 53 12710 8067 8684 84 -1304 542 C ATOM 292 N LEU A 54 -6.108 7.686 -0.452 1.00 62.96 N ANISOU 292 N LEU A 54 10568 6197 7156 45 -1473 891 N ATOM 293 CA LEU A 54 -6.319 7.089 0.872 1.00 62.69 C ANISOU 293 CA LEU A 54 10424 6199 7198 5 -1542 1064 C ATOM 294 C LEU A 54 -5.116 7.349 1.773 1.00 65.08 C ANISOU 294 C LEU A 54 10683 6559 7487 44 -1458 1032 C ATOM 295 O LEU A 54 -5.292 7.706 2.938 1.00 64.38 O ANISOU 295 O LEU A 54 10503 6599 7360 31 -1421 1152 O ATOM 296 CB LEU A 54 -6.578 5.574 0.755 1.00 64.12 C ANISOU 296 CB LEU A 54 10582 6227 7553 -38 -1732 1127 C ATOM 297 CG LEU A 54 -7.937 5.163 0.189 1.00 69.43 C ANISOU 297 CG LEU A 54 11267 6851 8263 -96 -1847 1219 C ATOM 298 CD1 LEU A 54 -7.852 3.827 -0.506 1.00 70.86 C ANISOU 298 CD1 LEU A 54 11482 6834 8609 -109 -2020 1167 C ATOM 299 CD2 LEU A 54 -9.007 5.143 1.279 1.00 71.60 C ANISOU 299 CD2 LEU A 54 11426 7241 8539 -159 -1891 1464 C ATOM 300 N ILE A 55 -3.887 7.211 1.213 1.00 60.96 N ANISOU 300 N ILE A 55 10223 5954 6984 98 -1425 865 N ATOM 301 CA ILE A 55 -2.624 7.462 1.920 1.00 60.03 C ANISOU 301 CA ILE A 55 10077 5879 6854 138 -1341 817 C ATOM 302 C ILE A 55 -2.557 8.933 2.325 1.00 62.31 C ANISOU 302 C ILE A 55 10360 6322 6995 164 -1188 805 C ATOM 303 O ILE A 55 -2.123 9.240 3.434 1.00 61.52 O ANISOU 303 O ILE A 55 10188 6315 6871 170 -1138 858 O ATOM 304 CB ILE A 55 -1.401 7.046 1.040 1.00 63.53 C ANISOU 304 CB ILE A 55 10597 6203 7338 196 -1338 637 C ATOM 305 CG1 ILE A 55 -1.451 5.539 0.699 1.00 65.33 C ANISOU 305 CG1 ILE A 55 10827 6266 7730 179 -1506 637 C ATOM 306 CG2 ILE A 55 -0.064 7.415 1.720 1.00 63.88 C ANISOU 306 CG2 ILE A 55 10617 6298 7356 238 -1241 589 C ATOM 307 CD1 ILE A 55 -0.611 5.120 -0.538 1.00 73.13 C ANISOU 307 CD1 ILE A 55 11907 7136 8742 246 -1524 438 C ATOM 308 N CYS A 56 -3.045 9.835 1.446 1.00 58.80 N ANISOU 308 N CYS A 56 9981 5906 6454 177 -1123 740 N ATOM 309 CA CYS A 56 -3.084 11.278 1.702 1.00 58.07 C ANISOU 309 CA CYS A 56 9886 5943 6235 200 -991 722 C ATOM 310 C CYS A 56 -4.013 11.596 2.888 1.00 62.74 C ANISOU 310 C CYS A 56 10385 6665 6790 170 -993 880 C ATOM 311 O CYS A 56 -3.579 12.256 3.829 1.00 61.78 O ANISOU 311 O CYS A 56 10211 6647 6617 194 -921 890 O ATOM 312 CB CYS A 56 -3.503 12.042 0.449 1.00 57.82 C ANISOU 312 CB CYS A 56 9934 5904 6131 212 -941 638 C ATOM 313 SG CYS A 56 -2.152 12.371 -0.713 1.00 61.28 S ANISOU 313 SG CYS A 56 10456 6284 6545 276 -870 444 S ATOM 314 N CYS A 57 -5.270 11.085 2.865 1.00 60.58 N ANISOU 314 N CYS A 57 10083 6390 6543 119 -1083 1006 N ATOM 315 CA CYS A 57 -6.248 11.296 3.947 1.00 60.95 C ANISOU 315 CA CYS A 57 10031 6578 6550 93 -1096 1172 C ATOM 316 C CYS A 57 -5.675 10.829 5.297 1.00 65.38 C ANISOU 316 C CYS A 57 10486 7207 7149 94 -1116 1255 C ATOM 317 O CYS A 57 -5.948 11.452 6.327 1.00 64.48 O ANISOU 317 O CYS A 57 10291 7252 6957 109 -1066 1329 O ATOM 318 CB CYS A 57 -7.563 10.591 3.632 1.00 62.12 C ANISOU 318 CB CYS A 57 10164 6694 6743 34 -1211 1305 C ATOM 319 SG CYS A 57 -8.409 11.225 2.161 1.00 65.83 S ANISOU 319 SG CYS A 57 10742 7118 7152 26 -1182 1233 S ATOM 320 N PHE A 58 -4.862 9.744 5.282 1.00 62.69 N ANISOU 320 N PHE A 58 10143 6750 6927 84 -1188 1238 N ATOM 321 CA PHE A 58 -4.192 9.232 6.475 1.00 62.70 C ANISOU 321 CA PHE A 58 10044 6804 6977 81 -1207 1312 C ATOM 322 C PHE A 58 -3.117 10.225 6.947 1.00 65.94 C ANISOU 322 C PHE A 58 10461 7294 7300 139 -1073 1201 C ATOM 323 O PHE A 58 -2.956 10.421 8.151 1.00 65.52 O ANISOU 323 O PHE A 58 10309 7376 7212 146 -1046 1277 O ATOM 324 CB PHE A 58 -3.580 7.845 6.207 1.00 65.29 C ANISOU 324 CB PHE A 58 10375 6966 7466 57 -1320 1308 C ATOM 325 CG PHE A 58 -2.895 7.237 7.408 1.00 67.48 C ANISOU 325 CG PHE A 58 10541 7291 7809 47 -1348 1399 C ATOM 326 CD1 PHE A 58 -3.636 6.689 8.450 1.00 71.54 C ANISOU 326 CD1 PHE A 58 10916 7905 8362 -2 -1430 1611 C ATOM 327 CD2 PHE A 58 -1.508 7.212 7.499 1.00 69.53 C ANISOU 327 CD2 PHE A 58 10824 7504 8089 84 -1291 1286 C ATOM 328 CE1 PHE A 58 -3.000 6.150 9.574 1.00 72.88 C ANISOU 328 CE1 PHE A 58 10968 8135 8589 -14 -1452 1705 C ATOM 329 CE2 PHE A 58 -0.874 6.660 8.618 1.00 72.72 C ANISOU 329 CE2 PHE A 58 11120 7957 8554 71 -1313 1376 C ATOM 330 CZ PHE A 58 -1.624 6.134 9.648 1.00 71.47 C ANISOU 330 CZ PHE A 58 10820 7903 8433 21 -1393 1584 C ATOM 331 N ILE A 59 -2.416 10.881 5.994 1.00 62.11 N ANISOU 331 N ILE A 59 10085 6737 6776 180 -993 1028 N ATOM 332 CA ILE A 59 -1.404 11.903 6.298 1.00 61.09 C ANISOU 332 CA ILE A 59 9972 6670 6572 233 -872 921 C ATOM 333 C ILE A 59 -2.103 13.154 6.890 1.00 64.20 C ANISOU 333 C ILE A 59 10327 7223 6845 252 -798 950 C ATOM 334 O ILE A 59 -1.589 13.741 7.846 1.00 63.39 O ANISOU 334 O ILE A 59 10168 7225 6691 282 -739 942 O ATOM 335 CB ILE A 59 -0.555 12.238 5.030 1.00 63.64 C ANISOU 335 CB ILE A 59 10411 6880 6890 268 -819 750 C ATOM 336 CG1 ILE A 59 0.332 11.033 4.629 1.00 64.56 C ANISOU 336 CG1 ILE A 59 10553 6858 7118 269 -885 705 C ATOM 337 CG2 ILE A 59 0.298 13.501 5.238 1.00 63.62 C ANISOU 337 CG2 ILE A 59 10424 6945 6803 317 -698 654 C ATOM 338 CD1 ILE A 59 0.913 11.099 3.212 1.00 71.95 C ANISOU 338 CD1 ILE A 59 11598 7689 8053 305 -862 553 C ATOM 339 N ILE A 60 -3.304 13.508 6.365 1.00 60.82 N ANISOU 339 N ILE A 60 9921 6813 6374 236 -810 987 N ATOM 340 CA ILE A 60 -4.093 14.650 6.866 1.00 60.60 C ANISOU 340 CA ILE A 60 9855 6931 6237 259 -750 1017 C ATOM 341 C ILE A 60 -4.405 14.450 8.367 1.00 65.20 C ANISOU 341 C ILE A 60 10305 7675 6793 260 -774 1149 C ATOM 342 O ILE A 60 -4.130 15.346 9.168 1.00 65.00 O ANISOU 342 O ILE A 60 10236 7771 6689 307 -705 1112 O ATOM 343 CB ILE A 60 -5.403 14.875 6.038 1.00 63.79 C ANISOU 343 CB ILE A 60 10300 7325 6613 234 -772 1058 C ATOM 344 CG1 ILE A 60 -5.146 14.903 4.505 1.00 63.96 C ANISOU 344 CG1 ILE A 60 10441 7198 6662 228 -761 941 C ATOM 345 CG2 ILE A 60 -6.165 16.125 6.509 1.00 64.58 C ANISOU 345 CG2 ILE A 60 10365 7571 6602 267 -705 1074 C ATOM 346 CD1 ILE A 60 -4.140 15.930 4.010 1.00 69.76 C ANISOU 346 CD1 ILE A 60 11237 7910 7359 276 -660 787 C ATOM 347 N LEU A 61 -4.937 13.259 8.743 1.00 61.55 N ANISOU 347 N LEU A 61 9771 7216 6400 210 -879 1301 N ATOM 348 CA LEU A 61 -5.239 12.935 10.138 1.00 61.56 C ANISOU 348 CA LEU A 61 9626 7383 6380 206 -913 1451 C ATOM 349 C LEU A 61 -3.973 12.962 10.989 1.00 63.94 C ANISOU 349 C LEU A 61 9882 7726 6685 236 -869 1399 C ATOM 350 O LEU A 61 -3.964 13.602 12.039 1.00 64.04 O ANISOU 350 O LEU A 61 9811 7913 6608 276 -821 1418 O ATOM 351 CB LEU A 61 -5.926 11.563 10.255 1.00 62.70 C ANISOU 351 CB LEU A 61 9700 7496 6626 138 -1048 1634 C ATOM 352 CG LEU A 61 -7.450 11.590 10.380 1.00 68.28 C ANISOU 352 CG LEU A 61 10349 8310 7286 114 -1098 1790 C ATOM 353 CD1 LEU A 61 -8.117 11.770 9.012 1.00 68.50 C ANISOU 353 CD1 LEU A 61 10499 8205 7322 94 -1108 1732 C ATOM 354 CD2 LEU A 61 -7.959 10.322 11.039 1.00 71.94 C ANISOU 354 CD2 LEU A 61 10684 8810 7840 54 -1230 2010 C ATOM 355 N GLU A 62 -2.886 12.315 10.507 1.00 58.47 N ANISOU 355 N GLU A 62 9248 6877 6091 222 -884 1324 N ATOM 356 CA GLU A 62 -1.592 12.277 11.201 1.00 57.28 C ANISOU 356 CA GLU A 62 9065 6745 5955 244 -842 1272 C ATOM 357 C GLU A 62 -1.161 13.668 11.669 1.00 59.18 C ANISOU 357 C GLU A 62 9311 7098 6077 308 -730 1163 C ATOM 358 O GLU A 62 -0.877 13.861 12.855 1.00 58.26 O ANISOU 358 O GLU A 62 9095 7129 5913 329 -708 1203 O ATOM 359 CB GLU A 62 -0.515 11.692 10.288 1.00 58.40 C ANISOU 359 CB GLU A 62 9303 6689 6196 238 -851 1164 C ATOM 360 CG GLU A 62 -0.455 10.182 10.273 1.00 67.84 C ANISOU 360 CG GLU A 62 10459 7782 7534 186 -968 1264 C ATOM 361 CD GLU A 62 0.723 9.661 9.478 1.00 85.78 C ANISOU 361 CD GLU A 62 12820 9878 9894 197 -970 1140 C ATOM 362 OE1 GLU A 62 0.617 9.595 8.231 1.00 85.43 O ANISOU 362 OE1 GLU A 62 12884 9703 9872 203 -984 1046 O ATOM 363 OE2 GLU A 62 1.782 9.402 10.092 1.00 73.63 O1- ANISOU 363 OE2 GLU A 62 11242 8346 8388 206 -949 1130 O1- ATOM 364 N ASN A 63 -1.149 14.641 10.741 1.00 54.98 N ANISOU 364 N ASN A 63 8889 6501 5501 337 -666 1031 N ATOM 365 CA ASN A 63 -0.740 16.014 11.022 1.00 53.83 C ANISOU 365 CA ASN A 63 8759 6429 5265 395 -573 916 C ATOM 366 C ASN A 63 -1.798 16.765 11.840 1.00 56.65 C ANISOU 366 C ASN A 63 9036 6971 5518 427 -561 973 C ATOM 367 O ASN A 63 -1.430 17.637 12.628 1.00 56.49 O ANISOU 367 O ASN A 63 8975 7060 5428 479 -508 912 O ATOM 368 CB ASN A 63 -0.432 16.750 9.736 1.00 53.12 C ANISOU 368 CB ASN A 63 8796 6211 5177 411 -522 780 C ATOM 369 CG ASN A 63 0.796 16.214 9.035 1.00 71.97 C ANISOU 369 CG ASN A 63 11254 8451 7642 402 -517 703 C ATOM 370 OD1 ASN A 63 1.899 16.141 9.602 1.00 59.30 O ANISOU 370 OD1 ASN A 63 9626 6853 6053 417 -493 670 O ATOM 371 ND2 ASN A 63 0.631 15.820 7.790 1.00 68.23 N ANISOU 371 ND2 ASN A 63 10863 7850 7213 382 -542 672 N ATOM 372 N ILE A 64 -3.104 16.405 11.692 1.00 52.20 N ANISOU 372 N ILE A 64 8443 6448 4943 399 -615 1090 N ATOM 373 CA ILE A 64 -4.169 16.988 12.522 1.00 52.06 C ANISOU 373 CA ILE A 64 8333 6626 4821 434 -610 1164 C ATOM 374 C ILE A 64 -3.932 16.552 13.976 1.00 55.97 C ANISOU 374 C ILE A 64 8683 7296 5286 447 -632 1259 C ATOM 375 O ILE A 64 -3.949 17.387 14.880 1.00 54.71 O ANISOU 375 O ILE A 64 8457 7302 5028 510 -589 1222 O ATOM 376 CB ILE A 64 -5.596 16.601 12.011 1.00 55.37 C ANISOU 376 CB ILE A 64 8749 7049 5239 395 -669 1288 C ATOM 377 CG1 ILE A 64 -5.988 17.446 10.786 1.00 55.26 C ANISOU 377 CG1 ILE A 64 8857 6929 5210 402 -625 1185 C ATOM 378 CG2 ILE A 64 -6.650 16.743 13.131 1.00 56.77 C ANISOU 378 CG2 ILE A 64 8788 7461 5319 423 -690 1424 C ATOM 379 CD1 ILE A 64 -7.259 16.963 10.030 1.00 63.09 C ANISOU 379 CD1 ILE A 64 9870 7882 6220 351 -685 1295 C ATOM 380 N PHE A 65 -3.624 15.251 14.174 1.00 53.70 N ANISOU 380 N PHE A 65 8346 6965 5091 390 -702 1372 N ATOM 381 CA PHE A 65 -3.321 14.662 15.483 1.00 54.27 C ANISOU 381 CA PHE A 65 8270 7192 5156 388 -731 1484 C ATOM 382 C PHE A 65 -2.093 15.337 16.132 1.00 56.19 C ANISOU 382 C PHE A 65 8509 7484 5359 439 -655 1354 C ATOM 383 O PHE A 65 -2.091 15.546 17.346 1.00 56.22 O ANISOU 383 O PHE A 65 8388 7692 5282 476 -644 1399 O ATOM 384 CB PHE A 65 -3.094 13.144 15.352 1.00 56.73 C ANISOU 384 CB PHE A 65 8549 7397 5609 310 -825 1613 C ATOM 385 CG PHE A 65 -4.342 12.299 15.507 1.00 59.33 C ANISOU 385 CG PHE A 65 8785 7791 5967 261 -927 1823 C ATOM 386 CD1 PHE A 65 -5.279 12.216 14.482 1.00 62.35 C ANISOU 386 CD1 PHE A 65 9248 8067 6375 232 -966 1842 C ATOM 387 CD2 PHE A 65 -4.550 11.541 16.654 1.00 62.62 C ANISOU 387 CD2 PHE A 65 9026 8373 6393 237 -990 2014 C ATOM 388 CE1 PHE A 65 -6.416 11.415 14.615 1.00 64.06 C ANISOU 388 CE1 PHE A 65 9376 8336 6627 181 -1069 2047 C ATOM 389 CE2 PHE A 65 -5.683 10.732 16.782 1.00 66.32 C ANISOU 389 CE2 PHE A 65 9398 8899 6900 186 -1095 2228 C ATOM 390 CZ PHE A 65 -6.610 10.676 15.762 1.00 64.27 C ANISOU 390 CZ PHE A 65 9226 8525 6668 158 -1136 2242 C ATOM 391 N VAL A 66 -1.068 15.705 15.319 1.00 50.44 N ANISOU 391 N VAL A 66 7910 6577 4678 444 -605 1194 N ATOM 392 CA VAL A 66 0.116 16.418 15.823 1.00 49.49 C ANISOU 392 CA VAL A 66 7797 6482 4525 489 -537 1067 C ATOM 393 C VAL A 66 -0.301 17.838 16.251 1.00 52.97 C ANISOU 393 C VAL A 66 8227 7056 4844 565 -482 973 C ATOM 394 O VAL A 66 0.062 18.286 17.341 1.00 52.31 O ANISOU 394 O VAL A 66 8058 7127 4689 612 -458 947 O ATOM 395 CB VAL A 66 1.274 16.442 14.783 1.00 52.36 C ANISOU 395 CB VAL A 66 8296 6627 4971 475 -503 938 C ATOM 396 CG1 VAL A 66 2.410 17.363 15.233 1.00 51.43 C ANISOU 396 CG1 VAL A 66 8192 6534 4815 523 -434 808 C ATOM 397 CG2 VAL A 66 1.798 15.035 14.525 1.00 52.51 C ANISOU 397 CG2 VAL A 66 8312 6528 5109 415 -560 1016 C ATOM 398 N LEU A 67 -1.127 18.503 15.424 1.00 49.68 N ANISOU 398 N LEU A 67 7886 6589 4403 579 -470 928 N ATOM 399 CA LEU A 67 -1.640 19.841 15.714 1.00 49.85 C ANISOU 399 CA LEU A 67 7899 6716 4323 652 -429 839 C ATOM 400 C LEU A 67 -2.608 19.840 16.915 1.00 56.58 C ANISOU 400 C LEU A 67 8605 7823 5070 693 -455 945 C ATOM 401 O LEU A 67 -2.701 20.843 17.623 1.00 56.26 O ANISOU 401 O LEU A 67 8520 7920 4936 772 -424 861 O ATOM 402 CB LEU A 67 -2.337 20.412 14.482 1.00 49.16 C ANISOU 402 CB LEU A 67 7920 6508 4250 646 -416 791 C ATOM 403 CG LEU A 67 -1.411 20.965 13.413 1.00 53.11 C ANISOU 403 CG LEU A 67 8550 6814 4815 639 -374 651 C ATOM 404 CD1 LEU A 67 -2.070 20.932 12.054 1.00 52.59 C ANISOU 404 CD1 LEU A 67 8578 6615 4787 601 -380 658 C ATOM 405 CD2 LEU A 67 -0.948 22.373 13.763 1.00 56.29 C ANISOU 405 CD2 LEU A 67 8962 7253 5175 709 -326 506 C ATOM 406 N LEU A 68 -3.306 18.708 17.151 1.00 54.88 N ANISOU 406 N LEU A 68 8307 7674 4870 643 -517 1130 N ATOM 407 CA LEU A 68 -4.262 18.578 18.248 1.00 55.93 C ANISOU 407 CA LEU A 68 8285 8066 4902 677 -548 1263 C ATOM 408 C LEU A 68 -3.547 18.401 19.594 1.00 62.46 C ANISOU 408 C LEU A 68 8980 9073 5681 708 -544 1284 C ATOM 409 O LEU A 68 -3.922 19.051 20.570 1.00 62.34 O ANISOU 409 O LEU A 68 8863 9285 5540 788 -528 1269 O ATOM 410 CB LEU A 68 -5.212 17.395 17.991 1.00 56.11 C ANISOU 410 CB LEU A 68 8258 8088 4975 604 -627 1473 C ATOM 411 CG LEU A 68 -6.703 17.669 18.222 1.00 61.15 C ANISOU 411 CG LEU A 68 8822 8899 5514 635 -650 1581 C ATOM 412 CD1 LEU A 68 -7.254 18.671 17.194 1.00 60.43 C ANISOU 412 CD1 LEU A 68 8863 8695 5403 660 -607 1460 C ATOM 413 CD2 LEU A 68 -7.503 16.385 18.159 1.00 64.62 C ANISOU 413 CD2 LEU A 68 9186 9353 6014 556 -743 1815 C ATOM 414 N THR A 69 -2.510 17.531 19.641 1.00 60.90 N ANISOU 414 N THR A 69 8782 8778 5580 650 -559 1314 N ATOM 415 CA THR A 69 -1.746 17.244 20.864 1.00 62.46 C ANISOU 415 CA THR A 69 8853 9132 5746 665 -556 1348 C ATOM 416 C THR A 69 -1.133 18.520 21.451 1.00 69.16 C ANISOU 416 C THR A 69 9709 10069 6499 756 -490 1162 C ATOM 417 O THR A 69 -1.226 18.744 22.659 1.00 69.52 O ANISOU 417 O THR A 69 9617 10361 6438 813 -489 1186 O ATOM 418 CB THR A 69 -0.651 16.201 20.592 1.00 71.62 C ANISOU 418 CB THR A 69 10043 10125 7044 587 -576 1385 C ATOM 419 OG1 THR A 69 0.112 16.605 19.456 1.00 72.40 O ANISOU 419 OG1 THR A 69 10318 9974 7217 576 -535 1224 O ATOM 420 CG2 THR A 69 -1.214 14.804 20.376 1.00 69.96 C ANISOU 420 CG2 THR A 69 9776 9873 6933 503 -663 1591 C ATOM 421 N ILE A 70 -0.537 19.365 20.590 1.00 66.98 N ANISOU 421 N ILE A 70 9587 9598 6263 770 -444 982 N ATOM 422 CA ILE A 70 0.095 20.627 20.992 1.00 67.77 C ANISOU 422 CA ILE A 70 9712 9735 6301 850 -395 795 C ATOM 423 C ILE A 70 -0.989 21.626 21.495 1.00 75.57 C ANISOU 423 C ILE A 70 10642 10912 7159 945 -392 748 C ATOM 424 O ILE A 70 -0.785 22.306 22.508 1.00 75.55 O ANISOU 424 O ILE A 70 10559 11084 7062 1026 -380 665 O ATOM 425 CB ILE A 70 0.922 21.197 19.797 1.00 69.63 C ANISOU 425 CB ILE A 70 10122 9702 6632 830 -359 647 C ATOM 426 CG1 ILE A 70 2.047 20.202 19.392 1.00 69.36 C ANISOU 426 CG1 ILE A 70 10133 9508 6712 751 -360 687 C ATOM 427 CG2 ILE A 70 1.498 22.592 20.117 1.00 70.02 C ANISOU 427 CG2 ILE A 70 10201 9767 6637 909 -323 457 C ATOM 428 CD1 ILE A 70 2.618 20.400 18.000 1.00 75.47 C ANISOU 428 CD1 ILE A 70 11067 10025 7583 717 -337 598 C ATOM 429 N TRP A 71 -2.154 21.643 20.823 1.00 74.52 N ANISOU 429 N TRP A 71 10540 10753 7019 936 -408 808 N ATOM 430 CA TRP A 71 -3.295 22.511 21.143 1.00 75.88 C ANISOU 430 CA TRP A 71 10666 11088 7077 1022 -408 778 C ATOM 431 C TRP A 71 -3.988 22.082 22.466 1.00 80.02 C ANISOU 431 C TRP A 71 10997 11933 7475 1068 -438 915 C ATOM 432 O TRP A 71 -4.675 22.898 23.089 1.00 79.94 O ANISOU 432 O TRP A 71 10916 12116 7341 1169 -433 861 O ATOM 433 CB TRP A 71 -4.301 22.474 19.969 1.00 74.96 C ANISOU 433 CB TRP A 71 10638 10841 7001 981 -417 832 C ATOM 434 CG TRP A 71 -5.546 23.290 20.152 1.00 77.00 C ANISOU 434 CG TRP A 71 10856 11246 7153 1061 -416 819 C ATOM 435 CD1 TRP A 71 -5.731 24.593 19.792 1.00 79.89 C ANISOU 435 CD1 TRP A 71 11295 11559 7500 1129 -387 655 C ATOM 436 CD2 TRP A 71 -6.824 22.811 20.595 1.00 77.86 C ANISOU 436 CD2 TRP A 71 10850 11556 7176 1072 -451 993 C ATOM 437 NE1 TRP A 71 -7.032 24.972 20.036 1.00 80.15 N ANISOU 437 NE1 TRP A 71 11265 11756 7434 1190 -397 703 N ATOM 438 CE2 TRP A 71 -7.726 23.895 20.526 1.00 82.25 C ANISOU 438 CE2 TRP A 71 11415 12186 7650 1157 -434 913 C ATOM 439 CE3 TRP A 71 -7.292 21.569 21.067 1.00 79.81 C ANISOU 439 CE3 TRP A 71 10978 11935 7412 1019 -502 1217 C ATOM 440 CZ2 TRP A 71 -9.070 23.779 20.910 1.00 82.43 C ANISOU 440 CZ2 TRP A 71 11334 12417 7568 1195 -459 1049 C ATOM 441 CZ3 TRP A 71 -8.622 21.454 21.445 1.00 82.16 C ANISOU 441 CZ3 TRP A 71 11168 12438 7610 1051 -532 1362 C ATOM 442 CH2 TRP A 71 -9.494 22.549 21.369 1.00 83.05 C ANISOU 442 CH2 TRP A 71 11295 12631 7630 1140 -506 1277 C ATOM 443 N LYS A 72 -3.801 20.812 22.889 1.00 76.56 N ANISOU 443 N LYS A 72 10463 11556 7069 999 -473 1094 N ATOM 444 CA LYS A 72 -4.450 20.276 24.086 1.00 77.25 C ANISOU 444 CA LYS A 72 10350 11953 7047 1029 -509 1261 C ATOM 445 C LYS A 72 -3.485 20.187 25.289 1.00 82.04 C ANISOU 445 C LYS A 72 10841 12728 7604 1061 -499 1236 C ATOM 446 O LYS A 72 -3.895 20.489 26.413 1.00 82.95 O ANISOU 446 O LYS A 72 10803 13141 7574 1147 -503 1256 O ATOM 447 CB LYS A 72 -5.052 18.896 23.797 1.00 79.51 C ANISOU 447 CB LYS A 72 10582 12219 7409 927 -572 1511 C ATOM 448 N THR A 73 -2.223 19.754 25.066 1.00 77.65 N ANISOU 448 N THR A 73 10349 11994 7160 994 -486 1199 N ATOM 449 CA THR A 73 -1.246 19.616 26.158 1.00 77.69 C ANISOU 449 CA THR A 73 10249 12142 7128 1013 -474 1184 C ATOM 450 C THR A 73 -0.666 20.994 26.530 1.00 80.76 C ANISOU 450 C THR A 73 10682 12563 7440 1115 -429 938 C ATOM 451 O THR A 73 -0.164 21.708 25.660 1.00 79.66 O ANISOU 451 O THR A 73 10708 12185 7373 1114 -401 774 O ATOM 452 CB THR A 73 -0.134 18.622 25.770 1.00 86.02 C ANISOU 452 CB THR A 73 11353 12994 8335 905 -479 1242 C ATOM 453 OG1 THR A 73 -0.726 17.435 25.240 1.00 87.72 O ANISOU 453 OG1 THR A 73 11553 13132 8645 813 -534 1443 O ATOM 454 CG2 THR A 73 0.774 18.270 26.942 1.00 84.51 C ANISOU 454 CG2 THR A 73 11028 12970 8111 908 -474 1277 C ATOM 455 N LYS A 74 -0.731 21.354 27.834 1.00 77.46 N ANISOU 455 N LYS A 74 10109 12446 6877 1206 -430 917 N ATOM 456 CA LYS A 74 -0.224 22.635 28.352 1.00 76.90 C ANISOU 456 CA LYS A 74 10057 12435 6727 1314 -404 682 C ATOM 457 C LYS A 74 1.311 22.681 28.303 1.00 78.60 C ANISOU 457 C LYS A 74 10349 12480 7033 1270 -379 579 C ATOM 458 O LYS A 74 1.881 23.717 27.962 1.00 77.56 O ANISOU 458 O LYS A 74 10335 12204 6931 1311 -361 376 O ATOM 459 CB LYS A 74 -0.714 22.877 29.796 1.00 80.73 C ANISOU 459 CB LYS A 74 10337 13312 7023 1425 -418 696 C ATOM 460 CG LYS A 74 -2.240 22.857 29.967 1.00 94.45 C ANISOU 460 CG LYS A 74 11977 15263 8649 1482 -443 809 C ATOM 461 CD LYS A 74 -2.906 24.161 29.532 1.00102.42 C ANISOU 461 CD LYS A 74 13082 16224 9611 1584 -434 618 C ATOM 462 CE LYS A 74 -4.392 24.136 29.798 1.00110.94 C ANISOU 462 CE LYS A 74 14048 17541 10563 1648 -456 736 C ATOM 463 NZ LYS A 74 -5.041 25.419 29.426 1.00118.51 N ANISOU 463 NZ LYS A 74 15091 18461 11477 1754 -448 548 N ATOM 464 N LYS A 75 1.976 21.546 28.625 1.00 74.31 N ANISOU 464 N LYS A 75 9738 11952 6546 1184 -383 729 N ATOM 465 CA LYS A 75 3.440 21.423 28.598 1.00 73.23 C ANISOU 465 CA LYS A 75 9662 11665 6498 1133 -359 664 C ATOM 466 C LYS A 75 3.980 21.492 27.157 1.00 75.12 C ANISOU 466 C LYS A 75 10110 11539 6894 1063 -340 596 C ATOM 467 O LYS A 75 5.187 21.667 26.955 1.00 73.55 O ANISOU 467 O LYS A 75 9991 11187 6767 1036 -316 507 O ATOM 468 CB LYS A 75 3.876 20.108 29.260 1.00 76.02 C ANISOU 468 CB LYS A 75 9879 12128 6877 1056 -372 865 C ATOM 469 N PHE A 76 3.076 21.357 26.161 1.00 71.27 N ANISOU 469 N PHE A 76 9701 10926 6452 1036 -352 644 N ATOM 470 CA PHE A 76 3.415 21.396 24.739 1.00 69.90 C ANISOU 470 CA PHE A 76 9711 10436 6412 976 -338 592 C ATOM 471 C PHE A 76 3.192 22.800 24.150 1.00 73.55 C ANISOU 471 C PHE A 76 10289 10799 6860 1044 -321 401 C ATOM 472 O PHE A 76 3.261 22.967 22.934 1.00 72.62 O ANISOU 472 O PHE A 76 10311 10447 6834 1004 -310 361 O ATOM 473 CB PHE A 76 2.593 20.347 23.963 1.00 71.39 C ANISOU 473 CB PHE A 76 9916 10541 6669 899 -368 762 C ATOM 474 CG PHE A 76 3.215 18.969 23.884 1.00 72.71 C ANISOU 474 CG PHE A 76 10056 10629 6941 802 -388 910 C ATOM 475 CD1 PHE A 76 3.131 18.217 22.721 1.00 75.44 C ANISOU 475 CD1 PHE A 76 10503 10750 7410 724 -407 972 C ATOM 476 CD2 PHE A 76 3.906 18.433 24.968 1.00 75.28 C ANISOU 476 CD2 PHE A 76 10253 11104 7247 791 -390 981 C ATOM 477 CE1 PHE A 76 3.708 16.945 22.649 1.00 76.34 C ANISOU 477 CE1 PHE A 76 10591 10782 7633 643 -435 1097 C ATOM 478 CE2 PHE A 76 4.493 17.168 24.888 1.00 77.89 C ANISOU 478 CE2 PHE A 76 10556 11350 7689 702 -413 1117 C ATOM 479 CZ PHE A 76 4.391 16.434 23.732 1.00 75.48 C ANISOU 479 CZ PHE A 76 10354 10813 7512 631 -438 1171 C ATOM 480 N HIS A 77 2.969 23.815 25.011 1.00 70.50 N ANISOU 480 N HIS A 77 9837 10590 6361 1148 -323 281 N ATOM 481 CA HIS A 77 2.814 25.202 24.561 1.00 70.03 C ANISOU 481 CA HIS A 77 9872 10436 6300 1219 -320 93 C ATOM 482 C HIS A 77 4.184 25.928 24.576 1.00 74.36 C ANISOU 482 C HIS A 77 10492 10854 6909 1227 -308 -65 C ATOM 483 O HIS A 77 4.252 27.136 24.813 1.00 73.75 O ANISOU 483 O HIS A 77 10432 10786 6805 1310 -321 -234 O ATOM 484 CB HIS A 77 1.778 25.939 25.420 1.00 71.56 C ANISOU 484 CB HIS A 77 9961 10879 6351 1336 -340 36 C ATOM 485 CG HIS A 77 0.367 25.645 25.024 1.00 75.01 C ANISOU 485 CG HIS A 77 10377 11375 6748 1336 -350 151 C ATOM 486 ND1 HIS A 77 -0.234 24.441 25.336 1.00 77.02 N ANISOU 486 ND1 HIS A 77 10526 11770 6968 1287 -365 364 N ATOM 487 CD2 HIS A 77 -0.517 26.410 24.342 1.00 76.74 C ANISOU 487 CD2 HIS A 77 10664 11526 6967 1375 -353 88 C ATOM 488 CE1 HIS A 77 -1.456 24.507 24.833 1.00 76.50 C ANISOU 488 CE1 HIS A 77 10472 11718 6877 1297 -375 424 C ATOM 489 NE2 HIS A 77 -1.673 25.675 24.228 1.00 76.62 N ANISOU 489 NE2 HIS A 77 10591 11613 6908 1350 -365 261 N ATOM 490 N ARG A 78 5.267 25.175 24.284 1.00 71.77 N ANISOU 490 N ARG A 78 10205 10394 6670 1141 -289 -5 N ATOM 491 CA ARG A 78 6.638 25.682 24.236 1.00 71.91 C ANISOU 491 CA ARG A 78 10289 10281 6754 1132 -277 -118 C ATOM 492 C ARG A 78 6.991 26.168 22.809 1.00 76.39 C ANISOU 492 C ARG A 78 11017 10564 7442 1092 -266 -179 C ATOM 493 O ARG A 78 6.391 25.689 21.840 1.00 75.55 O ANISOU 493 O ARG A 78 10970 10353 7381 1045 -259 -99 O ATOM 494 CB ARG A 78 7.621 24.590 24.694 1.00 72.14 C ANISOU 494 CB ARG A 78 10267 10334 6810 1063 -261 -9 C ATOM 495 N PRO A 79 7.989 27.090 22.653 1.00 73.61 N ANISOU 495 N PRO A 79 10733 10090 7147 1109 -269 -311 N ATOM 496 CA PRO A 79 8.319 27.601 21.306 1.00 72.88 C ANISOU 496 CA PRO A 79 10775 9750 7166 1074 -261 -355 C ATOM 497 C PRO A 79 8.633 26.504 20.274 1.00 76.62 C ANISOU 497 C PRO A 79 11318 10078 7717 980 -231 -231 C ATOM 498 O PRO A 79 8.170 26.614 19.142 1.00 75.74 O ANISOU 498 O PRO A 79 11286 9835 7654 957 -225 -220 O ATOM 499 CB PRO A 79 9.550 28.489 21.548 1.00 74.67 C ANISOU 499 CB PRO A 79 11030 9901 7441 1094 -275 -476 C ATOM 500 CG PRO A 79 10.000 28.187 22.947 1.00 79.81 C ANISOU 500 CG PRO A 79 11571 10742 8012 1121 -280 -479 C ATOM 501 CD PRO A 79 8.780 27.781 23.687 1.00 75.92 C ANISOU 501 CD PRO A 79 10971 10471 7403 1164 -287 -426 C ATOM 502 N MET A 80 9.399 25.451 20.652 1.00 74.06 N ANISOU 502 N MET A 80 10957 9778 7403 930 -214 -141 N ATOM 503 CA MET A 80 9.745 24.377 19.703 1.00 74.03 C ANISOU 503 CA MET A 80 11017 9635 7478 851 -193 -37 C ATOM 504 C MET A 80 8.494 23.704 19.131 1.00 77.70 C ANISOU 504 C MET A 80 11485 10103 7935 828 -204 56 C ATOM 505 O MET A 80 8.410 23.506 17.916 1.00 77.09 O ANISOU 505 O MET A 80 11500 9868 7922 791 -196 71 O ATOM 506 CB MET A 80 10.652 23.311 20.347 1.00 76.79 C ANISOU 506 CB MET A 80 11308 10029 7840 807 -181 50 C ATOM 507 CG MET A 80 11.153 22.266 19.333 1.00 80.33 C ANISOU 507 CG MET A 80 11828 10315 8381 737 -166 133 C ATOM 508 SD MET A 80 12.127 20.913 20.034 1.00 85.28 S ANISOU 508 SD MET A 80 12381 10982 9039 683 -158 248 S ATOM 509 CE MET A 80 10.848 19.995 20.908 1.00 82.67 C ANISOU 509 CE MET A 80 11915 10846 8652 674 -195 384 C ATOM 510 N TYR A 81 7.524 23.356 20.006 1.00 73.95 N ANISOU 510 N TYR A 81 10902 9816 7378 850 -224 122 N ATOM 511 CA TYR A 81 6.294 22.680 19.598 1.00 73.18 C ANISOU 511 CA TYR A 81 10793 9742 7271 827 -244 229 C ATOM 512 C TYR A 81 5.462 23.540 18.639 1.00 75.38 C ANISOU 512 C TYR A 81 11155 9931 7553 850 -243 162 C ATOM 513 O TYR A 81 4.794 22.988 17.765 1.00 74.63 O ANISOU 513 O TYR A 81 11106 9757 7493 809 -251 234 O ATOM 514 CB TYR A 81 5.458 22.289 20.812 1.00 75.02 C ANISOU 514 CB TYR A 81 10877 10221 7405 855 -268 318 C ATOM 515 CG TYR A 81 6.095 21.223 21.677 1.00 76.81 C ANISOU 515 CG TYR A 81 11003 10543 7637 816 -275 428 C ATOM 516 CD1 TYR A 81 6.081 19.886 21.293 1.00 78.50 C ANISOU 516 CD1 TYR A 81 11211 10688 7928 738 -295 574 C ATOM 517 CD2 TYR A 81 6.639 21.538 22.918 1.00 78.15 C ANISOU 517 CD2 TYR A 81 11074 10885 7736 859 -269 392 C ATOM 518 CE1 TYR A 81 6.643 18.895 22.097 1.00 79.51 C ANISOU 518 CE1 TYR A 81 11235 10901 8074 700 -307 686 C ATOM 519 CE2 TYR A 81 7.192 20.554 23.738 1.00 79.31 C ANISOU 519 CE2 TYR A 81 11115 11134 7887 820 -274 506 C ATOM 520 CZ TYR A 81 7.188 19.232 23.324 1.00 85.49 C ANISOU 520 CZ TYR A 81 11890 11835 8756 738 -293 659 C ATOM 521 OH TYR A 81 7.722 18.256 24.127 1.00 85.41 O ANISOU 521 OH TYR A 81 11766 11919 8764 696 -304 781 O ATOM 522 N TYR A 82 5.529 24.885 18.771 1.00 71.23 N ANISOU 522 N TYR A 82 10650 9410 7003 915 -239 24 N ATOM 523 CA TYR A 82 4.822 25.783 17.853 1.00 70.54 C ANISOU 523 CA TYR A 82 10638 9230 6934 935 -240 -41 C ATOM 524 C TYR A 82 5.379 25.638 16.428 1.00 71.89 C ANISOU 524 C TYR A 82 10928 9180 7208 875 -221 -39 C ATOM 525 O TYR A 82 4.614 25.684 15.463 1.00 71.30 O ANISOU 525 O TYR A 82 10908 9031 7153 856 -220 -16 O ATOM 526 CB TYR A 82 4.911 27.247 18.321 1.00 72.35 C ANISOU 526 CB TYR A 82 10858 9493 7139 1017 -251 -193 C ATOM 527 CG TYR A 82 4.093 27.558 19.558 1.00 75.22 C ANISOU 527 CG TYR A 82 11108 10086 7386 1097 -273 -216 C ATOM 528 CD1 TYR A 82 2.702 27.498 19.531 1.00 77.55 C ANISOU 528 CD1 TYR A 82 11367 10482 7617 1122 -283 -161 C ATOM 529 CD2 TYR A 82 4.699 28.042 20.713 1.00 76.65 C ANISOU 529 CD2 TYR A 82 11218 10387 7517 1158 -287 -306 C ATOM 530 CE1 TYR A 82 1.941 27.819 20.656 1.00 79.35 C ANISOU 530 CE1 TYR A 82 11483 10941 7727 1208 -302 -183 C ATOM 531 CE2 TYR A 82 3.950 28.372 21.842 1.00 78.48 C ANISOU 531 CE2 TYR A 82 11338 10850 7630 1246 -309 -340 C ATOM 532 CZ TYR A 82 2.569 28.260 21.809 1.00 85.99 C ANISOU 532 CZ TYR A 82 12249 11911 8512 1274 -315 -278 C ATOM 533 OH TYR A 82 1.826 28.595 22.918 1.00 87.12 O ANISOU 533 OH TYR A 82 12273 12301 8526 1371 -336 -310 O ATOM 534 N PHE A 83 6.705 25.421 16.304 1.00 66.52 N ANISOU 534 N PHE A 83 10280 8408 6584 846 -205 -56 N ATOM 535 CA PHE A 83 7.349 25.212 15.010 1.00 65.09 C ANISOU 535 CA PHE A 83 10199 8044 6488 797 -186 -50 C ATOM 536 C PHE A 83 7.066 23.800 14.492 1.00 66.54 C ANISOU 536 C PHE A 83 10396 8193 6694 739 -189 65 C ATOM 537 O PHE A 83 6.984 23.600 13.281 1.00 65.17 O ANISOU 537 O PHE A 83 10299 7895 6566 709 -182 75 O ATOM 538 CB PHE A 83 8.862 25.459 15.098 1.00 66.85 C ANISOU 538 CB PHE A 83 10443 8197 6758 792 -171 -99 C ATOM 539 CG PHE A 83 9.273 26.822 15.610 1.00 68.82 C ANISOU 539 CG PHE A 83 10681 8463 7007 844 -184 -213 C ATOM 540 CD1 PHE A 83 8.769 27.982 15.032 1.00 72.07 C ANISOU 540 CD1 PHE A 83 11128 8816 7441 874 -199 -285 C ATOM 541 CD2 PHE A 83 10.245 26.947 16.595 1.00 71.46 C ANISOU 541 CD2 PHE A 83 10969 8852 7331 860 -187 -248 C ATOM 542 CE1 PHE A 83 9.180 29.242 15.480 1.00 73.45 C ANISOU 542 CE1 PHE A 83 11289 8984 7635 922 -226 -394 C ATOM 543 CE2 PHE A 83 10.660 28.208 17.036 1.00 74.70 C ANISOU 543 CE2 PHE A 83 11370 9261 7752 908 -213 -361 C ATOM 544 CZ PHE A 83 10.128 29.346 16.472 1.00 72.80 C ANISOU 544 CZ PHE A 83 11164 8954 7542 940 -236 -435 C ATOM 545 N ILE A 84 6.901 22.821 15.416 1.00 62.63 N ANISOU 545 N ILE A 84 9818 7811 6168 725 -205 152 N ATOM 546 CA ILE A 84 6.548 21.433 15.073 1.00 62.01 C ANISOU 546 CA ILE A 84 9733 7703 6123 671 -227 270 C ATOM 547 C ILE A 84 5.120 21.419 14.503 1.00 65.23 C ANISOU 547 C ILE A 84 10156 8118 6510 666 -249 312 C ATOM 548 O ILE A 84 4.858 20.739 13.506 1.00 64.75 O ANISOU 548 O ILE A 84 10154 7947 6500 625 -263 355 O ATOM 549 CB ILE A 84 6.704 20.484 16.305 1.00 65.44 C ANISOU 549 CB ILE A 84 10054 8271 6539 656 -248 368 C ATOM 550 CG1 ILE A 84 8.172 20.440 16.778 1.00 65.81 C ANISOU 550 CG1 ILE A 84 10093 8298 6613 654 -222 332 C ATOM 551 CG2 ILE A 84 6.183 19.063 15.991 1.00 66.11 C ANISOU 551 CG2 ILE A 84 10121 8323 6675 599 -290 501 C ATOM 552 CD1 ILE A 84 8.374 19.842 18.138 1.00 74.32 C ANISOU 552 CD1 ILE A 84 11045 9538 7657 650 -235 409 C ATOM 553 N GLY A 85 4.236 22.218 15.112 1.00 61.39 N ANISOU 553 N GLY A 85 9618 7761 5948 714 -253 292 N ATOM 554 CA GLY A 85 2.864 22.397 14.651 1.00 61.06 C ANISOU 554 CA GLY A 85 9585 7741 5875 717 -270 327 C ATOM 555 C GLY A 85 2.812 23.083 13.299 1.00 63.64 C ANISOU 555 C GLY A 85 10022 7912 6244 710 -249 255 C ATOM 556 O GLY A 85 2.041 22.679 12.424 1.00 62.35 O ANISOU 556 O GLY A 85 9901 7689 6099 676 -262 308 O ATOM 557 N ASN A 86 3.686 24.099 13.100 1.00 60.17 N ANISOU 557 N ASN A 86 9627 7407 5829 738 -221 141 N ATOM 558 CA ASN A 86 3.799 24.814 11.828 1.00 59.59 C ANISOU 558 CA ASN A 86 9643 7194 5803 730 -202 81 C ATOM 559 C ASN A 86 4.336 23.876 10.746 1.00 62.41 C ANISOU 559 C ASN A 86 10068 7424 6222 676 -197 120 C ATOM 560 O ASN A 86 3.915 23.968 9.592 1.00 61.95 O ANISOU 560 O ASN A 86 10070 7283 6185 656 -193 122 O ATOM 561 CB ASN A 86 4.693 26.047 11.970 1.00 61.06 C ANISOU 561 CB ASN A 86 9841 7345 6013 769 -187 -30 C ATOM 562 CG ASN A 86 4.761 26.892 10.718 1.00 87.75 C ANISOU 562 CG ASN A 86 13292 10601 9446 762 -175 -75 C ATOM 563 OD1 ASN A 86 3.759 27.112 10.024 1.00 79.77 O ANISOU 563 OD1 ASN A 86 12304 9574 8430 754 -176 -55 O ATOM 564 ND2 ASN A 86 5.942 27.412 10.421 1.00 81.99 N ANISOU 564 ND2 ASN A 86 12591 9790 8772 762 -164 -128 N ATOM 565 N LEU A 87 5.238 22.944 11.134 1.00 58.08 N ANISOU 565 N LEU A 87 9504 6866 5698 655 -200 151 N ATOM 566 CA LEU A 87 5.764 21.914 10.238 1.00 57.49 C ANISOU 566 CA LEU A 87 9484 6681 5680 615 -203 183 C ATOM 567 C LEU A 87 4.666 20.911 9.907 1.00 61.42 C ANISOU 567 C LEU A 87 9979 7178 6180 580 -244 271 C ATOM 568 O LEU A 87 4.545 20.485 8.758 1.00 60.65 O ANISOU 568 O LEU A 87 9947 6981 6118 556 -252 272 O ATOM 569 CB LEU A 87 6.970 21.206 10.882 1.00 57.62 C ANISOU 569 CB LEU A 87 9473 6697 5725 607 -200 196 C ATOM 570 CG LEU A 87 7.584 20.050 10.087 1.00 62.23 C ANISOU 570 CG LEU A 87 10102 7171 6370 575 -210 223 C ATOM 571 CD1 LEU A 87 8.225 20.547 8.798 1.00 62.29 C ANISOU 571 CD1 LEU A 87 10194 7071 6401 585 -180 153 C ATOM 572 CD2 LEU A 87 8.586 19.292 10.923 1.00 64.19 C ANISOU 572 CD2 LEU A 87 10304 7438 6646 566 -212 254 C ATOM 573 N ALA A 88 3.835 20.564 10.916 1.00 58.53 N ANISOU 573 N ALA A 88 9530 6933 5775 579 -274 348 N ATOM 574 CA ALA A 88 2.686 19.675 10.738 1.00 58.51 C ANISOU 574 CA ALA A 88 9510 6946 5776 544 -324 452 C ATOM 575 C ALA A 88 1.655 20.316 9.809 1.00 60.86 C ANISOU 575 C ALA A 88 9861 7213 6051 545 -319 435 C ATOM 576 O ALA A 88 0.957 19.608 9.091 1.00 59.56 O ANISOU 576 O ALA A 88 9725 6993 5911 508 -356 492 O ATOM 577 CB ALA A 88 2.055 19.353 12.084 1.00 59.78 C ANISOU 577 CB ALA A 88 9553 7272 5888 550 -354 547 C ATOM 578 N LEU A 89 1.587 21.662 9.799 1.00 57.48 N ANISOU 578 N LEU A 89 9445 6812 5583 586 -278 354 N ATOM 579 CA LEU A 89 0.692 22.390 8.907 1.00 57.54 C ANISOU 579 CA LEU A 89 9499 6789 5575 588 -268 334 C ATOM 580 C LEU A 89 1.207 22.307 7.461 1.00 62.28 C ANISOU 580 C LEU A 89 10190 7244 6228 562 -253 291 C ATOM 581 O LEU A 89 0.415 22.101 6.536 1.00 61.97 O ANISOU 581 O LEU A 89 10191 7161 6193 535 -266 321 O ATOM 582 CB LEU A 89 0.552 23.855 9.353 1.00 57.40 C ANISOU 582 CB LEU A 89 9458 6834 5516 643 -238 257 C ATOM 583 CG LEU A 89 -0.597 24.641 8.720 1.00 61.79 C ANISOU 583 CG LEU A 89 10035 7392 6050 650 -233 256 C ATOM 584 CD1 LEU A 89 -1.954 24.059 9.122 1.00 62.13 C ANISOU 584 CD1 LEU A 89 10029 7536 6040 639 -266 364 C ATOM 585 CD2 LEU A 89 -0.531 26.096 9.112 1.00 64.69 C ANISOU 585 CD2 LEU A 89 10383 7793 6402 708 -212 163 C ATOM 586 N SER A 90 2.543 22.416 7.278 1.00 58.71 N ANISOU 586 N SER A 90 9765 6729 5813 571 -227 227 N ATOM 587 CA SER A 90 3.176 22.312 5.964 1.00 58.35 C ANISOU 587 CA SER A 90 9792 6571 5807 557 -211 187 C ATOM 588 C SER A 90 2.900 20.951 5.353 1.00 62.31 C ANISOU 588 C SER A 90 10323 7016 6335 522 -252 236 C ATOM 589 O SER A 90 2.498 20.872 4.195 1.00 61.65 O ANISOU 589 O SER A 90 10291 6877 6257 507 -256 228 O ATOM 590 CB SER A 90 4.679 22.543 6.072 1.00 62.19 C ANISOU 590 CB SER A 90 10286 7022 6321 577 -182 129 C ATOM 591 OG SER A 90 4.966 23.779 6.702 1.00 73.27 O ANISOU 591 OG SER A 90 11658 8468 7711 610 -159 81 O ATOM 592 N ASP A 91 3.050 19.880 6.159 1.00 59.43 N ANISOU 592 N ASP A 91 9918 6671 5991 507 -289 291 N ATOM 593 CA ASP A 91 2.804 18.507 5.723 1.00 59.52 C ANISOU 593 CA ASP A 91 9947 6618 6050 474 -348 341 C ATOM 594 C ASP A 91 1.297 18.213 5.609 1.00 61.85 C ANISOU 594 C ASP A 91 10229 6942 6330 443 -395 422 C ATOM 595 O ASP A 91 0.911 17.304 4.873 1.00 61.61 O ANISOU 595 O ASP A 91 10233 6837 6339 414 -448 448 O ATOM 596 CB ASP A 91 3.479 17.506 6.676 1.00 62.14 C ANISOU 596 CB ASP A 91 10226 6959 6424 465 -379 386 C ATOM 597 CG ASP A 91 4.985 17.368 6.475 1.00 77.00 C ANISOU 597 CG ASP A 91 12137 8780 8340 485 -348 317 C ATOM 598 OD1 ASP A 91 5.494 17.835 5.422 1.00 77.86 O ANISOU 598 OD1 ASP A 91 12310 8828 8444 505 -312 239 O ATOM 599 OD2 ASP A 91 5.637 16.704 7.314 1.00 84.51 O1- ANISOU 599 OD2 ASP A 91 13041 9745 9325 480 -363 350 O1- ATOM 600 N LEU A 92 0.450 18.985 6.324 1.00 57.40 N ANISOU 600 N LEU A 92 9616 6486 5708 454 -381 460 N ATOM 601 CA LEU A 92 -1.003 18.830 6.245 1.00 57.27 C ANISOU 601 CA LEU A 92 9582 6512 5667 429 -420 546 C ATOM 602 C LEU A 92 -1.492 19.362 4.924 1.00 60.53 C ANISOU 602 C LEU A 92 10069 6860 6070 421 -401 502 C ATOM 603 O LEU A 92 -2.207 18.665 4.208 1.00 59.86 O ANISOU 603 O LEU A 92 10013 6725 6006 385 -448 548 O ATOM 604 CB LEU A 92 -1.702 19.562 7.414 1.00 57.53 C ANISOU 604 CB LEU A 92 9534 6697 5630 457 -406 590 C ATOM 605 CG LEU A 92 -3.221 19.354 7.552 1.00 62.60 C ANISOU 605 CG LEU A 92 10136 7413 6235 435 -448 703 C ATOM 606 CD1 LEU A 92 -3.651 19.519 8.976 1.00 63.29 C ANISOU 606 CD1 LEU A 92 10114 7671 6261 465 -456 773 C ATOM 607 CD2 LEU A 92 -4.010 20.315 6.656 1.00 64.33 C ANISOU 607 CD2 LEU A 92 10408 7614 6420 441 -415 668 C ATOM 608 N LEU A 93 -1.113 20.611 4.597 1.00 57.26 N ANISOU 608 N LEU A 93 9679 6449 5630 453 -336 418 N ATOM 609 CA LEU A 93 -1.519 21.255 3.353 1.00 57.18 C ANISOU 609 CA LEU A 93 9725 6392 5610 445 -311 383 C ATOM 610 C LEU A 93 -0.830 20.587 2.155 1.00 61.50 C ANISOU 610 C LEU A 93 10336 6835 6196 431 -319 336 C ATOM 611 O LEU A 93 -1.370 20.625 1.048 1.00 61.29 O ANISOU 611 O LEU A 93 10351 6772 6163 413 -322 332 O ATOM 612 CB LEU A 93 -1.224 22.768 3.391 1.00 57.00 C ANISOU 612 CB LEU A 93 9695 6397 5567 482 -251 316 C ATOM 613 CG LEU A 93 -1.889 23.564 4.550 1.00 61.89 C ANISOU 613 CG LEU A 93 10249 7123 6141 513 -244 335 C ATOM 614 CD1 LEU A 93 -1.464 25.014 4.527 1.00 62.04 C ANISOU 614 CD1 LEU A 93 10265 7143 6165 551 -200 255 C ATOM 615 CD2 LEU A 93 -3.419 23.463 4.507 1.00 63.90 C ANISOU 615 CD2 LEU A 93 10489 7434 6358 494 -268 420 C ATOM 616 N ALA A 94 0.322 19.901 2.397 1.00 57.88 N ANISOU 616 N ALA A 94 9881 6336 5775 443 -327 304 N ATOM 617 CA ALA A 94 1.026 19.130 1.367 1.00 57.76 C ANISOU 617 CA ALA A 94 9918 6232 5794 443 -343 254 C ATOM 618 C ALA A 94 0.158 17.971 0.898 1.00 61.72 C ANISOU 618 C ALA A 94 10441 6686 6323 408 -420 301 C ATOM 619 O ALA A 94 -0.008 17.772 -0.309 1.00 61.63 O ANISOU 619 O ALA A 94 10481 6626 6310 404 -431 262 O ATOM 620 CB ALA A 94 2.350 18.609 1.909 1.00 58.58 C ANISOU 620 CB ALA A 94 10011 6312 5934 465 -340 221 C ATOM 621 N GLY A 95 -0.429 17.252 1.861 1.00 57.73 N ANISOU 621 N GLY A 95 9889 6205 5841 382 -476 390 N ATOM 622 CA GLY A 95 -1.335 16.142 1.599 1.00 57.71 C ANISOU 622 CA GLY A 95 9892 6156 5880 341 -567 459 C ATOM 623 C GLY A 95 -2.600 16.583 0.891 1.00 60.68 C ANISOU 623 C GLY A 95 10290 6549 6215 316 -570 492 C ATOM 624 O GLY A 95 -3.103 15.866 0.028 1.00 60.13 O ANISOU 624 O GLY A 95 10261 6411 6173 291 -630 496 O ATOM 625 N VAL A 96 -3.118 17.790 1.245 1.00 57.02 N ANISOU 625 N VAL A 96 9802 6175 5687 326 -509 511 N ATOM 626 CA VAL A 96 -4.305 18.380 0.605 1.00 56.69 C ANISOU 626 CA VAL A 96 9777 6160 5602 305 -499 546 C ATOM 627 C VAL A 96 -3.954 18.733 -0.839 1.00 60.94 C ANISOU 627 C VAL A 96 10381 6640 6132 311 -466 456 C ATOM 628 O VAL A 96 -4.696 18.382 -1.760 1.00 60.81 O ANISOU 628 O VAL A 96 10400 6591 6115 282 -500 472 O ATOM 629 CB VAL A 96 -4.848 19.623 1.382 1.00 59.84 C ANISOU 629 CB VAL A 96 10127 6668 5942 325 -443 576 C ATOM 630 CG1 VAL A 96 -6.044 20.243 0.666 1.00 59.27 C ANISOU 630 CG1 VAL A 96 10072 6617 5830 304 -430 613 C ATOM 631 CG2 VAL A 96 -5.216 19.261 2.812 1.00 60.01 C ANISOU 631 CG2 VAL A 96 10069 6777 5954 327 -477 667 C ATOM 632 N ALA A 97 -2.784 19.374 -1.036 1.00 57.51 N ANISOU 632 N ALA A 97 9957 6201 5693 350 -403 367 N ATOM 633 CA ALA A 97 -2.300 19.772 -2.355 1.00 57.55 C ANISOU 633 CA ALA A 97 10005 6177 5684 363 -366 290 C ATOM 634 C ALA A 97 -2.048 18.560 -3.247 1.00 62.07 C ANISOU 634 C ALA A 97 10624 6676 6284 361 -424 248 C ATOM 635 O ALA A 97 -2.332 18.625 -4.440 1.00 62.19 O ANISOU 635 O ALA A 97 10672 6683 6276 356 -423 217 O ATOM 636 CB ALA A 97 -1.029 20.595 -2.222 1.00 58.07 C ANISOU 636 CB ALA A 97 10058 6258 5748 405 -301 224 C ATOM 637 N TYR A 98 -1.542 17.447 -2.677 1.00 59.01 N ANISOU 637 N TYR A 98 10234 6239 5950 366 -481 245 N ATOM 638 CA TYR A 98 -1.277 16.262 -3.481 1.00 59.91 C ANISOU 638 CA TYR A 98 10390 6272 6102 372 -549 192 C ATOM 639 C TYR A 98 -2.573 15.485 -3.761 1.00 64.49 C ANISOU 639 C TYR A 98 10983 6813 6705 325 -638 255 C ATOM 640 O TYR A 98 -2.673 14.838 -4.807 1.00 64.72 O ANISOU 640 O TYR A 98 11056 6786 6746 328 -689 198 O ATOM 641 CB TYR A 98 -0.221 15.354 -2.840 1.00 61.97 C ANISOU 641 CB TYR A 98 10640 6481 6424 397 -583 164 C ATOM 642 CG TYR A 98 0.328 14.323 -3.807 1.00 65.07 C ANISOU 642 CG TYR A 98 11079 6793 6853 426 -639 73 C ATOM 643 CD1 TYR A 98 1.085 14.706 -4.911 1.00 67.10 C ANISOU 643 CD1 TYR A 98 11367 7068 7060 475 -589 -29 C ATOM 644 CD2 TYR A 98 0.047 12.970 -3.648 1.00 66.88 C ANISOU 644 CD2 TYR A 98 11312 6932 7165 408 -752 90 C ATOM 645 CE1 TYR A 98 1.568 13.766 -5.820 1.00 68.86 C ANISOU 645 CE1 TYR A 98 11628 7234 7303 516 -643 -126 C ATOM 646 CE2 TYR A 98 0.541 12.017 -4.539 1.00 68.68 C ANISOU 646 CE2 TYR A 98 11584 7081 7433 446 -814 -11 C ATOM 647 CZ TYR A 98 1.293 12.421 -5.631 1.00 76.55 C ANISOU 647 CZ TYR A 98 12614 8108 8365 504 -757 -126 C ATOM 648 OH TYR A 98 1.773 11.489 -6.520 1.00 78.67 O ANISOU 648 OH TYR A 98 12919 8313 8659 554 -820 -237 O ATOM 649 N THR A 99 -3.585 15.584 -2.863 1.00 60.80 N ANISOU 649 N THR A 99 10476 6384 6241 283 -660 372 N ATOM 650 CA THR A 99 -4.893 14.961 -3.124 1.00 61.11 C ANISOU 650 CA THR A 99 10522 6397 6300 232 -744 453 C ATOM 651 C THR A 99 -5.523 15.679 -4.310 1.00 64.54 C ANISOU 651 C THR A 99 10994 6855 6671 223 -705 425 C ATOM 652 O THR A 99 -6.020 15.031 -5.232 1.00 64.52 O ANISOU 652 O THR A 99 11032 6800 6684 204 -770 408 O ATOM 653 CB THR A 99 -5.798 14.996 -1.873 1.00 69.33 C ANISOU 653 CB THR A 99 11496 7501 7343 197 -769 598 C ATOM 654 OG1 THR A 99 -5.091 14.453 -0.765 1.00 69.89 O ANISOU 654 OG1 THR A 99 11519 7572 7464 209 -792 623 O ATOM 655 CG2 THR A 99 -7.106 14.223 -2.072 1.00 67.70 C ANISOU 655 CG2 THR A 99 11288 7265 7169 140 -870 704 C ATOM 656 N ALA A 100 -5.418 17.028 -4.319 1.00 60.15 N ANISOU 656 N ALA A 100 10425 6379 6052 240 -601 414 N ATOM 657 CA ALA A 100 -5.900 17.868 -5.410 1.00 59.54 C ANISOU 657 CA ALA A 100 10369 6337 5918 232 -551 394 C ATOM 658 C ALA A 100 -5.036 17.676 -6.660 1.00 63.17 C ANISOU 658 C ALA A 100 10869 6768 6366 266 -540 277 C ATOM 659 O ALA A 100 -5.546 17.798 -7.777 1.00 63.25 O ANISOU 659 O ALA A 100 10902 6789 6341 252 -541 260 O ATOM 660 CB ALA A 100 -5.901 19.330 -4.985 1.00 59.61 C ANISOU 660 CB ALA A 100 10340 6425 5883 245 -456 414 C ATOM 661 N ASN A 101 -3.732 17.335 -6.472 1.00 58.70 N ANISOU 661 N ASN A 101 10305 6175 5824 313 -532 199 N ATOM 662 CA ASN A 101 -2.821 17.072 -7.589 1.00 58.39 C ANISOU 662 CA ASN A 101 10294 6124 5767 359 -525 87 C ATOM 663 C ASN A 101 -3.250 15.801 -8.318 1.00 61.61 C ANISOU 663 C ASN A 101 10745 6461 6204 352 -628 47 C ATOM 664 O ASN A 101 -3.552 15.870 -9.500 1.00 60.86 O ANISOU 664 O ASN A 101 10671 6389 6063 356 -629 2 O ATOM 665 CB ASN A 101 -1.359 16.966 -7.113 1.00 58.67 C ANISOU 665 CB ASN A 101 10318 6149 5824 411 -496 25 C ATOM 666 CG ASN A 101 -0.339 16.793 -8.226 1.00 78.83 C ANISOU 666 CG ASN A 101 12890 8715 8345 470 -480 -85 C ATOM 667 OD1 ASN A 101 -0.567 17.155 -9.385 1.00 76.07 O ANISOU 667 OD1 ASN A 101 12548 8416 7940 478 -459 -116 O ATOM 668 ND2 ASN A 101 0.834 16.290 -7.880 1.00 67.84 N ANISOU 668 ND2 ASN A 101 11498 7294 6983 516 -483 -140 N ATOM 669 N LEU A 102 -3.365 14.658 -7.586 1.00 58.36 N ANISOU 669 N LEU A 102 10338 5965 5872 338 -722 72 N ATOM 670 CA LEU A 102 -3.795 13.364 -8.152 1.00 58.75 C ANISOU 670 CA LEU A 102 10425 5923 5976 329 -844 38 C ATOM 671 C LEU A 102 -5.101 13.499 -8.932 1.00 61.71 C ANISOU 671 C LEU A 102 10818 6312 6316 282 -874 81 C ATOM 672 O LEU A 102 -5.241 12.900 -10.000 1.00 62.51 O ANISOU 672 O LEU A 102 10958 6379 6414 296 -934 0 O ATOM 673 CB LEU A 102 -3.971 12.310 -7.045 1.00 59.26 C ANISOU 673 CB LEU A 102 10469 5901 6146 300 -944 111 C ATOM 674 CG LEU A 102 -2.708 11.835 -6.333 1.00 64.38 C ANISOU 674 CG LEU A 102 11100 6513 6849 343 -944 67 C ATOM 675 CD1 LEU A 102 -3.040 11.302 -4.952 1.00 64.86 C ANISOU 675 CD1 LEU A 102 11109 6544 6990 299 -1002 192 C ATOM 676 CD2 LEU A 102 -1.965 10.783 -7.156 1.00 66.77 C ANISOU 676 CD2 LEU A 102 11444 6728 7198 397 -1018 -68 C ATOM 677 N LEU A 103 -6.054 14.299 -8.403 1.00 56.20 N ANISOU 677 N LEU A 103 10093 5672 5590 230 -831 203 N ATOM 678 CA LEU A 103 -7.343 14.529 -9.050 1.00 55.68 C ANISOU 678 CA LEU A 103 10039 5629 5489 179 -849 263 C ATOM 679 C LEU A 103 -7.191 15.393 -10.322 1.00 59.24 C ANISOU 679 C LEU A 103 10502 6155 5850 201 -768 191 C ATOM 680 O LEU A 103 -7.917 15.174 -11.296 1.00 58.97 O ANISOU 680 O LEU A 103 10494 6121 5791 178 -807 180 O ATOM 681 CB LEU A 103 -8.330 15.190 -8.074 1.00 54.80 C ANISOU 681 CB LEU A 103 9886 5570 5366 128 -820 414 C ATOM 682 CG LEU A 103 -8.912 14.283 -6.990 1.00 59.34 C ANISOU 682 CG LEU A 103 10435 6096 6017 90 -919 526 C ATOM 683 CD1 LEU A 103 -9.494 15.096 -5.859 1.00 58.90 C ANISOU 683 CD1 LEU A 103 10322 6128 5929 70 -863 651 C ATOM 684 CD2 LEU A 103 -9.962 13.348 -7.557 1.00 61.93 C ANISOU 684 CD2 LEU A 103 10790 6356 6386 39 -1040 575 C ATOM 685 N LEU A 104 -6.241 16.356 -10.318 1.00 55.03 N ANISOU 685 N LEU A 104 9944 5690 5275 243 -662 148 N ATOM 686 CA LEU A 104 -6.021 17.236 -11.470 1.00 54.77 C ANISOU 686 CA LEU A 104 9903 5743 5164 263 -584 100 C ATOM 687 C LEU A 104 -4.772 16.811 -12.288 1.00 60.43 C ANISOU 687 C LEU A 104 10631 6470 5859 336 -584 -37 C ATOM 688 O LEU A 104 -4.307 17.570 -13.140 1.00 59.77 O ANISOU 688 O LEU A 104 10522 6477 5710 365 -512 -73 O ATOM 689 CB LEU A 104 -5.898 18.705 -11.019 1.00 53.74 C ANISOU 689 CB LEU A 104 9723 5689 5005 257 -474 162 C ATOM 690 CG LEU A 104 -7.156 19.333 -10.386 1.00 57.60 C ANISOU 690 CG LEU A 104 10193 6196 5496 198 -461 286 C ATOM 691 CD1 LEU A 104 -6.851 20.713 -9.824 1.00 57.09 C ANISOU 691 CD1 LEU A 104 10080 6190 5421 208 -367 321 C ATOM 692 CD2 LEU A 104 -8.309 19.414 -11.386 1.00 59.47 C ANISOU 692 CD2 LEU A 104 10442 6460 5693 151 -476 327 C ATOM 693 N SER A 105 -4.284 15.575 -12.073 1.00 58.82 N ANISOU 693 N SER A 105 10459 6179 5712 368 -669 -107 N ATOM 694 CA SER A 105 -3.146 15.028 -12.818 1.00 59.87 C ANISOU 694 CA SER A 105 10605 6318 5826 448 -682 -244 C ATOM 695 C SER A 105 -3.612 13.887 -13.732 1.00 65.92 C ANISOU 695 C SER A 105 11415 7030 6602 460 -794 -329 C ATOM 696 O SER A 105 -4.772 13.471 -13.654 1.00 65.97 O ANISOU 696 O SER A 105 11442 6978 6644 399 -868 -269 O ATOM 697 CB SER A 105 -2.060 14.540 -11.860 1.00 63.67 C ANISOU 697 CB SER A 105 11083 6739 6369 486 -691 -273 C ATOM 698 OG SER A 105 -0.864 14.210 -12.546 1.00 74.11 O ANISOU 698 OG SER A 105 12409 8088 7662 571 -683 -399 O ATOM 699 N GLY A 106 -2.714 13.411 -14.597 1.00 63.71 N ANISOU 699 N GLY A 106 11145 6776 6288 543 -809 -469 N ATOM 700 CA GLY A 106 -3.001 12.326 -15.527 1.00 64.73 C ANISOU 700 CA GLY A 106 11313 6858 6422 575 -921 -582 C ATOM 701 C GLY A 106 -3.712 12.800 -16.772 1.00 69.27 C ANISOU 701 C GLY A 106 11882 7537 6899 564 -900 -597 C ATOM 702 O GLY A 106 -3.182 13.636 -17.509 1.00 68.66 O ANISOU 702 O GLY A 106 11765 7603 6722 603 -804 -621 O ATOM 703 N ALA A 107 -4.931 12.277 -17.015 1.00 66.74 N ANISOU 703 N ALA A 107 11595 7153 6610 506 -993 -569 N ATOM 704 CA ALA A 107 -5.739 12.651 -18.185 1.00 67.05 C ANISOU 704 CA ALA A 107 11629 7285 6561 485 -983 -574 C ATOM 705 C ALA A 107 -6.326 14.065 -18.035 1.00 69.60 C ANISOU 705 C ALA A 107 11907 7707 6830 415 -860 -424 C ATOM 706 O ALA A 107 -6.482 14.772 -19.031 1.00 69.01 O ANISOU 706 O ALA A 107 11799 7764 6659 418 -797 -428 O ATOM 707 CB ALA A 107 -6.858 11.642 -18.392 1.00 68.57 C ANISOU 707 CB ALA A 107 11872 7366 6817 439 -1127 -579 C ATOM 708 N THR A 108 -6.622 14.478 -16.785 1.00 65.40 N ANISOU 708 N THR A 108 11368 7120 6361 356 -830 -295 N ATOM 709 CA THR A 108 -7.197 15.792 -16.468 1.00 64.29 C ANISOU 709 CA THR A 108 11186 7054 6188 295 -726 -157 C ATOM 710 C THR A 108 -6.160 16.929 -16.647 1.00 66.72 C ANISOU 710 C THR A 108 11436 7477 6436 339 -600 -167 C ATOM 711 O THR A 108 -6.547 18.104 -16.683 1.00 66.02 O ANISOU 711 O THR A 108 11304 7465 6316 299 -515 -73 O ATOM 712 CB THR A 108 -7.764 15.800 -15.025 1.00 73.23 C ANISOU 712 CB THR A 108 12322 8100 7401 237 -742 -32 C ATOM 713 OG1 THR A 108 -6.825 15.179 -14.143 1.00 72.15 O ANISOU 713 OG1 THR A 108 12193 7888 7331 279 -773 -76 O ATOM 714 CG2 THR A 108 -9.112 15.094 -14.922 1.00 73.27 C ANISOU 714 CG2 THR A 108 12359 8029 7450 168 -845 43 C ATOM 715 N THR A 109 -4.847 16.577 -16.764 1.00 61.71 N ANISOU 715 N THR A 109 10797 6855 5794 422 -595 -276 N ATOM 716 CA THR A 109 -3.751 17.552 -16.926 1.00 60.04 C ANISOU 716 CA THR A 109 10528 6751 5534 468 -490 -280 C ATOM 717 C THR A 109 -4.010 18.472 -18.131 1.00 59.95 C ANISOU 717 C THR A 109 10459 6889 5429 460 -424 -254 C ATOM 718 O THR A 109 -3.798 19.683 -18.038 1.00 57.91 O ANISOU 718 O THR A 109 10141 6704 5157 442 -334 -171 O ATOM 719 CB THR A 109 -2.401 16.821 -17.080 1.00 70.25 C ANISOU 719 CB THR A 109 11829 8043 6821 563 -512 -409 C ATOM 720 OG1 THR A 109 -2.281 15.826 -16.060 1.00 71.63 O ANISOU 720 OG1 THR A 109 12054 8073 7091 564 -589 -431 O ATOM 721 CG2 THR A 109 -1.211 17.771 -17.020 1.00 68.23 C ANISOU 721 CG2 THR A 109 11511 7882 6531 606 -412 -392 C ATOM 722 N TYR A 110 -4.504 17.896 -19.236 1.00 55.60 N ANISOU 722 N TYR A 110 9924 6381 4822 471 -475 -320 N ATOM 723 CA TYR A 110 -4.789 18.627 -20.466 1.00 55.02 C ANISOU 723 CA TYR A 110 9789 6463 4652 465 -422 -298 C ATOM 724 C TYR A 110 -6.105 19.419 -20.349 1.00 57.50 C ANISOU 724 C TYR A 110 10091 6776 4980 364 -392 -158 C ATOM 725 O TYR A 110 -6.284 20.418 -21.061 1.00 56.40 O ANISOU 725 O TYR A 110 9881 6763 4786 342 -319 -90 O ATOM 726 CB TYR A 110 -4.829 17.663 -21.658 1.00 56.87 C ANISOU 726 CB TYR A 110 10042 6749 4815 521 -495 -433 C ATOM 727 CG TYR A 110 -3.570 16.833 -21.773 1.00 59.12 C ANISOU 727 CG TYR A 110 10341 7035 5088 631 -531 -581 C ATOM 728 CD1 TYR A 110 -2.377 17.398 -22.219 1.00 61.28 C ANISOU 728 CD1 TYR A 110 10541 7452 5291 704 -454 -604 C ATOM 729 CD2 TYR A 110 -3.550 15.501 -21.371 1.00 60.36 C ANISOU 729 CD2 TYR A 110 10577 7045 5314 661 -645 -685 C ATOM 730 CE1 TYR A 110 -1.200 16.652 -22.278 1.00 62.74 C ANISOU 730 CE1 TYR A 110 10736 7642 5462 809 -483 -734 C ATOM 731 CE2 TYR A 110 -2.380 14.743 -21.431 1.00 61.92 C ANISOU 731 CE2 TYR A 110 10785 7234 5509 765 -679 -822 C ATOM 732 CZ TYR A 110 -1.207 15.322 -21.889 1.00 69.05 C ANISOU 732 CZ TYR A 110 11619 8290 6329 842 -594 -848 C ATOM 733 OH TYR A 110 -0.053 14.581 -21.959 1.00 70.77 O ANISOU 733 OH TYR A 110 11844 8508 6536 950 -625 -979 O ATOM 734 N LYS A 111 -6.986 19.029 -19.394 1.00 52.72 N ANISOU 734 N LYS A 111 9544 6034 4453 304 -444 -101 N ATOM 735 CA LYS A 111 -8.252 19.729 -19.165 1.00 50.96 C ANISOU 735 CA LYS A 111 9312 5807 4245 214 -418 36 C ATOM 736 C LYS A 111 -8.040 20.955 -18.225 1.00 50.57 C ANISOU 736 C LYS A 111 9217 5762 4237 192 -330 139 C ATOM 737 O LYS A 111 -8.998 21.663 -17.904 1.00 49.41 O ANISOU 737 O LYS A 111 9055 5612 4107 128 -300 251 O ATOM 738 CB LYS A 111 -9.324 18.760 -18.602 1.00 53.53 C ANISOU 738 CB LYS A 111 9708 6003 4627 163 -520 63 C ATOM 739 CG LYS A 111 -10.780 19.254 -18.775 1.00 65.96 C ANISOU 739 CG LYS A 111 11276 7596 6189 76 -511 189 C ATOM 740 CD LYS A 111 -11.139 19.588 -20.245 1.00 72.12 C ANISOU 740 CD LYS A 111 12023 8501 6881 65 -485 176 C ATOM 741 CE LYS A 111 -12.269 20.587 -20.340 1.00 73.95 C ANISOU 741 CE LYS A 111 12217 8781 7098 -16 -426 322 C ATOM 742 NZ LYS A 111 -12.406 21.133 -21.714 1.00 77.86 N ANISOU 742 NZ LYS A 111 12654 9421 7507 -24 -378 322 N ATOM 743 N LEU A 112 -6.780 21.243 -17.864 1.00 45.42 N ANISOU 743 N LEU A 112 8537 5123 3596 249 -289 97 N ATOM 744 CA LEU A 112 -6.443 22.415 -17.051 1.00 44.12 C ANISOU 744 CA LEU A 112 8326 4964 3475 237 -215 176 C ATOM 745 C LEU A 112 -5.948 23.561 -17.912 1.00 46.69 C ANISOU 745 C LEU A 112 8562 5418 3760 246 -137 211 C ATOM 746 O LEU A 112 -5.379 23.334 -18.978 1.00 47.14 O ANISOU 746 O LEU A 112 8590 5572 3751 289 -134 151 O ATOM 747 CB LEU A 112 -5.364 22.078 -16.001 1.00 43.94 C ANISOU 747 CB LEU A 112 8322 4870 3503 286 -224 125 C ATOM 748 CG LEU A 112 -5.768 21.156 -14.856 1.00 48.29 C ANISOU 748 CG LEU A 112 8937 5297 4114 271 -293 123 C ATOM 749 CD1 LEU A 112 -4.564 20.771 -14.041 1.00 48.23 C ANISOU 749 CD1 LEU A 112 8939 5240 4145 325 -298 64 C ATOM 750 CD2 LEU A 112 -6.819 21.804 -13.967 1.00 49.83 C ANISOU 750 CD2 LEU A 112 9125 5464 4345 210 -277 237 C ATOM 751 N THR A 113 -6.131 24.788 -17.436 1.00 41.44 N ANISOU 751 N THR A 113 7847 4760 3139 212 -81 308 N ATOM 752 CA THR A 113 -5.582 25.971 -18.084 1.00 40.85 C ANISOU 752 CA THR A 113 7674 4791 3056 215 -15 361 C ATOM 753 C THR A 113 -4.168 26.177 -17.526 1.00 43.84 C ANISOU 753 C THR A 113 8031 5159 3468 273 2 324 C ATOM 754 O THR A 113 -3.890 25.666 -16.433 1.00 43.14 O ANISOU 754 O THR A 113 8001 4969 3422 291 -25 281 O ATOM 755 CB THR A 113 -6.500 27.190 -17.848 1.00 46.58 C ANISOU 755 CB THR A 113 8353 5514 3830 150 24 482 C ATOM 756 OG1 THR A 113 -6.526 27.505 -16.453 1.00 41.20 O ANISOU 756 OG1 THR A 113 7698 4729 3225 148 21 498 O ATOM 757 CG2 THR A 113 -7.917 26.971 -18.368 1.00 45.05 C ANISOU 757 CG2 THR A 113 8183 5333 3603 91 9 529 C ATOM 758 N PRO A 114 -3.249 26.921 -18.217 1.00 39.34 N ANISOU 758 N PRO A 114 7371 4696 2881 299 44 350 N ATOM 759 CA PRO A 114 -1.899 27.128 -17.645 1.00 37.96 C ANISOU 759 CA PRO A 114 7174 4506 2741 350 56 326 C ATOM 760 C PRO A 114 -1.950 27.713 -16.218 1.00 37.55 C ANISOU 760 C PRO A 114 7144 4336 2789 328 58 359 C ATOM 761 O PRO A 114 -1.183 27.274 -15.364 1.00 35.63 O ANISOU 761 O PRO A 114 6939 4027 2571 366 43 303 O ATOM 762 CB PRO A 114 -1.240 28.097 -18.630 1.00 40.04 C ANISOU 762 CB PRO A 114 7317 4910 2985 359 99 398 C ATOM 763 CG PRO A 114 -1.961 27.897 -19.897 1.00 45.64 C ANISOU 763 CG PRO A 114 7998 5732 3612 341 102 410 C ATOM 764 CD PRO A 114 -3.384 27.596 -19.521 1.00 41.14 C ANISOU 764 CD PRO A 114 7503 5069 3059 282 79 416 C ATOM 765 N ALA A 115 -2.901 28.653 -15.947 1.00 32.21 N ANISOU 765 N ALA A 115 6441 3634 2164 272 74 443 N ATOM 766 CA ALA A 115 -3.089 29.233 -14.608 1.00 31.21 C ANISOU 766 CA ALA A 115 6329 3407 2121 260 71 463 C ATOM 767 C ALA A 115 -3.463 28.136 -13.594 1.00 36.51 C ANISOU 767 C ALA A 115 7098 3988 2786 269 31 400 C ATOM 768 O ALA A 115 -2.857 28.052 -12.520 1.00 35.00 O ANISOU 768 O ALA A 115 6927 3736 2635 296 22 366 O ATOM 769 CB ALA A 115 -4.168 30.309 -14.646 1.00 31.24 C ANISOU 769 CB ALA A 115 6290 3411 2170 205 88 554 C ATOM 770 N GLN A 116 -4.411 27.245 -13.980 1.00 34.56 N ANISOU 770 N GLN A 116 6903 3739 2489 245 3 390 N ATOM 771 CA GLN A 116 -4.850 26.117 -13.156 1.00 34.77 C ANISOU 771 CA GLN A 116 7010 3687 2514 246 -48 350 C ATOM 772 C GLN A 116 -3.715 25.095 -12.982 1.00 39.95 C ANISOU 772 C GLN A 116 7702 4315 3161 300 -76 258 C ATOM 773 O GLN A 116 -3.764 24.265 -12.074 1.00 39.09 O ANISOU 773 O GLN A 116 7644 4134 3075 307 -118 230 O ATOM 774 CB GLN A 116 -6.082 25.444 -13.783 1.00 36.40 C ANISOU 774 CB GLN A 116 7255 3899 2678 204 -81 370 C ATOM 775 CG GLN A 116 -7.373 26.247 -13.645 1.00 52.23 C ANISOU 775 CG GLN A 116 9238 5910 4695 148 -62 468 C ATOM 776 CD GLN A 116 -8.477 25.730 -14.548 1.00 73.24 C ANISOU 776 CD GLN A 116 11924 8598 7307 103 -88 497 C ATOM 777 OE1 GLN A 116 -8.237 25.025 -15.545 1.00 67.83 O ANISOU 777 OE1 GLN A 116 11253 7948 6571 115 -110 443 O ATOM 778 NE2 GLN A 116 -9.709 26.123 -14.254 1.00 65.95 N ANISOU 778 NE2 GLN A 116 10999 7667 6392 55 -85 583 N ATOM 779 N TRP A 117 -2.701 25.161 -13.855 1.00 38.17 N ANISOU 779 N TRP A 117 7443 4158 2903 340 -54 219 N ATOM 780 CA TRP A 117 -1.547 24.279 -13.804 1.00 39.10 C ANISOU 780 CA TRP A 117 7586 4264 3008 400 -75 131 C ATOM 781 C TRP A 117 -0.460 24.890 -12.905 1.00 42.77 C ANISOU 781 C TRP A 117 8021 4706 3523 427 -46 137 C ATOM 782 O TRP A 117 0.086 24.199 -12.038 1.00 41.95 O ANISOU 782 O TRP A 117 7957 4537 3445 453 -71 90 O ATOM 783 CB TRP A 117 -1.014 24.030 -15.223 1.00 38.95 C ANISOU 783 CB TRP A 117 7536 4349 2913 440 -67 86 C ATOM 784 CG TRP A 117 -0.099 22.855 -15.330 1.00 41.00 C ANISOU 784 CG TRP A 117 7835 4595 3147 507 -104 -22 C ATOM 785 CD1 TRP A 117 -0.418 21.604 -15.767 1.00 44.75 C ANISOU 785 CD1 TRP A 117 8368 5043 3592 527 -167 -106 C ATOM 786 CD2 TRP A 117 1.293 22.821 -14.997 1.00 41.11 C ANISOU 786 CD2 TRP A 117 7832 4618 3171 565 -86 -58 C ATOM 787 NE1 TRP A 117 0.694 20.795 -15.743 1.00 45.06 N ANISOU 787 NE1 TRP A 117 8425 5072 3623 600 -189 -199 N ATOM 788 CE2 TRP A 117 1.757 21.515 -15.263 1.00 46.13 C ANISOU 788 CE2 TRP A 117 8516 5233 3778 623 -136 -167 C ATOM 789 CE3 TRP A 117 2.201 23.774 -14.508 1.00 42.09 C ANISOU 789 CE3 TRP A 117 7902 4760 3329 574 -39 -8 C ATOM 790 CZ2 TRP A 117 3.088 21.138 -15.057 1.00 45.76 C ANISOU 790 CZ2 TRP A 117 8465 5192 3730 690 -131 -223 C ATOM 791 CZ3 TRP A 117 3.511 23.394 -14.291 1.00 43.87 C ANISOU 791 CZ3 TRP A 117 8125 4991 3553 635 -36 -57 C ATOM 792 CH2 TRP A 117 3.947 22.094 -14.570 1.00 45.18 C ANISOU 792 CH2 TRP A 117 8339 5145 3683 694 -77 -162 C ATOM 793 N PHE A 118 -0.155 26.197 -13.106 1.00 39.52 N ANISOU 793 N PHE A 118 7536 4347 3135 417 0 201 N ATOM 794 CA PHE A 118 0.851 26.910 -12.317 1.00 39.23 C ANISOU 794 CA PHE A 118 7465 4288 3154 438 20 214 C ATOM 795 C PHE A 118 0.436 26.980 -10.849 1.00 44.29 C ANISOU 795 C PHE A 118 8140 4834 3852 421 4 215 C ATOM 796 O PHE A 118 1.295 27.072 -9.968 1.00 43.33 O ANISOU 796 O PHE A 118 8018 4677 3769 447 4 194 O ATOM 797 CB PHE A 118 1.091 28.313 -12.876 1.00 40.78 C ANISOU 797 CB PHE A 118 7567 4547 3379 422 55 294 C ATOM 798 CG PHE A 118 1.907 28.341 -14.143 1.00 42.84 C ANISOU 798 CG PHE A 118 7767 4925 3585 453 75 304 C ATOM 799 CD1 PHE A 118 3.235 27.934 -14.143 1.00 46.05 C ANISOU 799 CD1 PHE A 118 8166 5358 3972 510 77 263 C ATOM 800 CD2 PHE A 118 1.379 28.858 -15.317 1.00 45.70 C ANISOU 800 CD2 PHE A 118 8066 5384 3914 426 93 365 C ATOM 801 CE1 PHE A 118 3.993 27.971 -15.314 1.00 47.61 C ANISOU 801 CE1 PHE A 118 8297 5687 4107 547 95 278 C ATOM 802 CE2 PHE A 118 2.139 28.897 -16.487 1.00 49.15 C ANISOU 802 CE2 PHE A 118 8431 5956 4289 460 111 382 C ATOM 803 CZ PHE A 118 3.442 28.456 -16.477 1.00 47.33 C ANISOU 803 CZ PHE A 118 8193 5758 4030 524 111 338 C ATOM 804 N LEU A 119 -0.885 26.893 -10.589 1.00 41.79 N ANISOU 804 N LEU A 119 7852 4491 3535 381 -12 243 N ATOM 805 CA LEU A 119 -1.441 26.846 -9.244 1.00 41.32 C ANISOU 805 CA LEU A 119 7820 4370 3511 371 -31 250 C ATOM 806 C LEU A 119 -1.351 25.413 -8.704 1.00 46.00 C ANISOU 806 C LEU A 119 8473 4916 4088 385 -75 201 C ATOM 807 O LEU A 119 -1.099 25.220 -7.512 1.00 44.98 O ANISOU 807 O LEU A 119 8353 4749 3989 398 -89 191 O ATOM 808 CB LEU A 119 -2.908 27.342 -9.260 1.00 40.97 C ANISOU 808 CB LEU A 119 7769 4331 3466 325 -31 313 C ATOM 809 CG LEU A 119 -3.537 27.698 -7.904 1.00 44.86 C ANISOU 809 CG LEU A 119 8262 4792 3990 323 -41 334 C ATOM 810 CD1 LEU A 119 -4.555 28.798 -8.056 1.00 44.64 C ANISOU 810 CD1 LEU A 119 8197 4785 3979 294 -21 396 C ATOM 811 CD2 LEU A 119 -4.182 26.477 -7.247 1.00 47.05 C ANISOU 811 CD2 LEU A 119 8591 5044 4242 314 -85 334 C ATOM 812 N ARG A 120 -1.543 24.406 -9.592 1.00 43.80 N ANISOU 812 N ARG A 120 8231 4644 3768 384 -104 171 N ATOM 813 CA ARG A 120 -1.520 22.991 -9.215 1.00 44.51 C ANISOU 813 CA ARG A 120 8375 4678 3860 395 -161 128 C ATOM 814 C ARG A 120 -0.143 22.592 -8.668 1.00 50.95 C ANISOU 814 C ARG A 120 9192 5469 4698 443 -160 72 C ATOM 815 O ARG A 120 -0.044 22.171 -7.515 1.00 50.56 O ANISOU 815 O ARG A 120 9153 5372 4684 443 -184 76 O ATOM 816 CB ARG A 120 -1.900 22.104 -10.416 1.00 44.36 C ANISOU 816 CB ARG A 120 8389 4667 3799 393 -199 91 C ATOM 817 CG ARG A 120 -2.174 20.649 -10.048 1.00 52.67 C ANISOU 817 CG ARG A 120 9495 5643 4874 392 -281 59 C ATOM 818 CD ARG A 120 -2.246 19.758 -11.273 1.00 55.18 C ANISOU 818 CD ARG A 120 9844 5963 5156 409 -327 -10 C ATOM 819 NE ARG A 120 -0.936 19.594 -11.906 1.00 54.87 N ANISOU 819 NE ARG A 120 9796 5962 5089 476 -306 -97 N ATOM 820 CZ ARG A 120 -0.701 18.796 -12.942 1.00 57.15 C ANISOU 820 CZ ARG A 120 10106 6268 5341 517 -345 -185 C ATOM 821 NH1 ARG A 120 -1.685 18.080 -13.473 1.00 32.78 N ANISOU 821 NH1 ARG A 120 7056 3151 2248 492 -413 -200 N ATOM 822 NH2 ARG A 120 0.519 18.701 -13.450 1.00 41.28 N ANISOU 822 NH2 ARG A 120 8078 4309 3297 587 -322 -259 N ATOM 823 N GLU A 121 0.919 22.759 -9.477 1.00 49.41 N ANISOU 823 N GLU A 121 8978 5318 4479 483 -132 29 N ATOM 824 CA GLU A 121 2.272 22.390 -9.067 1.00 49.94 C ANISOU 824 CA GLU A 121 9045 5370 4562 531 -127 -19 C ATOM 825 C GLU A 121 2.877 23.444 -8.139 1.00 54.50 C ANISOU 825 C GLU A 121 9580 5948 5178 531 -88 17 C ATOM 826 O GLU A 121 3.770 23.123 -7.356 1.00 53.88 O ANISOU 826 O GLU A 121 9506 5839 5126 557 -90 -7 O ATOM 827 CB GLU A 121 3.177 22.158 -10.285 1.00 51.99 C ANISOU 827 CB GLU A 121 9292 5692 4771 582 -114 -72 C ATOM 828 CG GLU A 121 2.776 20.940 -11.114 1.00 64.61 C ANISOU 828 CG GLU A 121 10935 7281 6333 600 -167 -139 C ATOM 829 CD GLU A 121 2.682 19.626 -10.354 1.00 88.88 C ANISOU 829 CD GLU A 121 14064 10254 9453 603 -236 -182 C ATOM 830 OE1 GLU A 121 3.572 19.353 -9.515 1.00 77.85 O ANISOU 830 OE1 GLU A 121 12666 8818 8093 627 -234 -196 O ATOM 831 OE2 GLU A 121 1.727 18.859 -10.614 1.00 87.74 O1- ANISOU 831 OE2 GLU A 121 13957 10067 9313 580 -296 -194 O1- ATOM 832 N GLY A 122 2.348 24.673 -8.198 1.00 51.76 N ANISOU 832 N GLY A 122 9194 5630 4843 503 -58 73 N ATOM 833 CA GLY A 122 2.764 25.764 -7.320 1.00 51.57 C ANISOU 833 CA GLY A 122 9130 5597 4867 502 -34 101 C ATOM 834 C GLY A 122 2.469 25.476 -5.860 1.00 56.18 C ANISOU 834 C GLY A 122 9732 6132 5480 497 -57 97 C ATOM 835 O GLY A 122 3.267 25.818 -4.986 1.00 55.58 O ANISOU 835 O GLY A 122 9639 6043 5437 516 -49 86 O ATOM 836 N SER A 123 1.333 24.781 -5.597 1.00 53.78 N ANISOU 836 N SER A 123 9461 5811 5161 471 -89 112 N ATOM 837 CA SER A 123 0.901 24.367 -4.256 1.00 53.78 C ANISOU 837 CA SER A 123 9468 5789 5178 464 -116 125 C ATOM 838 C SER A 123 1.908 23.413 -3.621 1.00 58.07 C ANISOU 838 C SER A 123 10025 6302 5737 489 -135 89 C ATOM 839 O SER A 123 2.138 23.479 -2.415 1.00 57.25 O ANISOU 839 O SER A 123 9902 6198 5654 497 -138 95 O ATOM 840 CB SER A 123 -0.466 23.693 -4.322 1.00 57.80 C ANISOU 840 CB SER A 123 10001 6294 5667 429 -155 166 C ATOM 841 OG SER A 123 -1.455 24.562 -4.845 1.00 68.70 O ANISOU 841 OG SER A 123 11368 7704 7032 404 -135 207 O ATOM 842 N MET A 124 2.505 22.524 -4.435 1.00 55.35 N ANISOU 842 N MET A 124 9710 5938 5383 506 -149 49 N ATOM 843 CA MET A 124 3.498 21.556 -3.968 1.00 55.54 C ANISOU 843 CA MET A 124 9748 5928 5428 533 -169 12 C ATOM 844 C MET A 124 4.797 22.262 -3.541 1.00 58.41 C ANISOU 844 C MET A 124 10080 6306 5805 563 -126 -4 C ATOM 845 O MET A 124 5.432 21.841 -2.572 1.00 57.07 O ANISOU 845 O MET A 124 9905 6118 5661 574 -134 -10 O ATOM 846 CB MET A 124 3.794 20.510 -5.059 1.00 58.62 C ANISOU 846 CB MET A 124 10174 6296 5803 555 -197 -40 C ATOM 847 CG MET A 124 2.558 19.757 -5.561 1.00 62.98 C ANISOU 847 CG MET A 124 10759 6822 6348 525 -253 -30 C ATOM 848 SD MET A 124 1.550 18.992 -4.259 1.00 67.69 S ANISOU 848 SD MET A 124 11354 7375 6991 480 -317 38 S ATOM 849 CE MET A 124 2.702 17.775 -3.610 1.00 64.86 C ANISOU 849 CE MET A 124 11000 6957 6686 510 -356 0 C ATOM 850 N PHE A 125 5.181 23.347 -4.263 1.00 55.24 N ANISOU 850 N PHE A 125 9653 5942 5392 573 -85 -1 N ATOM 851 CA PHE A 125 6.380 24.136 -3.959 1.00 54.84 C ANISOU 851 CA PHE A 125 9568 5906 5363 596 -53 -3 C ATOM 852 C PHE A 125 6.202 24.924 -2.669 1.00 56.96 C ANISOU 852 C PHE A 125 9810 6166 5667 584 -52 16 C ATOM 853 O PHE A 125 7.106 24.923 -1.830 1.00 56.85 O ANISOU 853 O PHE A 125 9783 6143 5676 601 -48 3 O ATOM 854 CB PHE A 125 6.719 25.085 -5.114 1.00 57.12 C ANISOU 854 CB PHE A 125 9822 6241 5639 604 -23 17 C ATOM 855 CG PHE A 125 7.531 24.449 -6.215 1.00 59.82 C ANISOU 855 CG PHE A 125 10170 6619 5940 641 -15 -10 C ATOM 856 CD1 PHE A 125 8.903 24.653 -6.297 1.00 63.41 C ANISOU 856 CD1 PHE A 125 10597 7099 6398 676 6 -9 C ATOM 857 CD2 PHE A 125 6.925 23.642 -7.173 1.00 62.77 C ANISOU 857 CD2 PHE A 125 10574 7008 6267 645 -32 -39 C ATOM 858 CE1 PHE A 125 9.653 24.068 -7.322 1.00 64.92 C ANISOU 858 CE1 PHE A 125 10786 7343 6539 722 15 -36 C ATOM 859 CE2 PHE A 125 7.677 23.052 -8.192 1.00 66.09 C ANISOU 859 CE2 PHE A 125 10995 7475 6641 693 -28 -79 C ATOM 860 CZ PHE A 125 9.034 23.277 -8.266 1.00 64.32 C ANISOU 860 CZ PHE A 125 10738 7288 6412 734 -2 -76 C ATOM 861 N VAL A 126 5.027 25.582 -2.496 1.00 51.82 N ANISOU 861 N VAL A 126 9147 5524 5017 559 -57 41 N ATOM 862 CA VAL A 126 4.703 26.363 -1.289 1.00 50.78 C ANISOU 862 CA VAL A 126 8986 5398 4910 559 -62 46 C ATOM 863 C VAL A 126 4.819 25.455 -0.044 1.00 53.33 C ANISOU 863 C VAL A 126 9315 5721 5229 566 -83 37 C ATOM 864 O VAL A 126 5.503 25.818 0.916 1.00 52.18 O ANISOU 864 O VAL A 126 9143 5582 5103 584 -80 20 O ATOM 865 CB VAL A 126 3.292 27.028 -1.392 1.00 54.23 C ANISOU 865 CB VAL A 126 9412 5852 5340 538 -66 74 C ATOM 866 CG1 VAL A 126 2.895 27.702 -0.077 1.00 53.82 C ANISOU 866 CG1 VAL A 126 9328 5819 5302 552 -77 66 C ATOM 867 CG2 VAL A 126 3.239 28.026 -2.547 1.00 53.97 C ANISOU 867 CG2 VAL A 126 9359 5823 5324 528 -47 94 C ATOM 868 N ALA A 127 4.216 24.241 -0.112 1.00 49.90 N ANISOU 868 N ALA A 127 8908 5279 4773 549 -109 54 N ATOM 869 CA ALA A 127 4.251 23.243 0.961 1.00 49.56 C ANISOU 869 CA ALA A 127 8859 5239 4734 548 -138 67 C ATOM 870 C ALA A 127 5.681 22.781 1.244 1.00 54.86 C ANISOU 870 C ALA A 127 9530 5888 5428 569 -129 38 C ATOM 871 O ALA A 127 6.030 22.576 2.406 1.00 54.33 O ANISOU 871 O ALA A 127 9433 5840 5370 575 -136 45 O ATOM 872 CB ALA A 127 3.381 22.056 0.599 1.00 50.18 C ANISOU 872 CB ALA A 127 8964 5297 4805 522 -181 99 C ATOM 873 N LEU A 128 6.523 22.662 0.191 1.00 53.28 N ANISOU 873 N LEU A 128 9355 5660 5229 585 -112 9 N ATOM 874 CA LEU A 128 7.929 22.284 0.351 1.00 54.14 C ANISOU 874 CA LEU A 128 9464 5753 5355 610 -99 -15 C ATOM 875 C LEU A 128 8.710 23.405 1.040 1.00 59.68 C ANISOU 875 C LEU A 128 10128 6476 6073 623 -71 -18 C ATOM 876 O LEU A 128 9.355 23.156 2.061 1.00 59.58 O ANISOU 876 O LEU A 128 10097 6467 6075 629 -72 -19 O ATOM 877 CB LEU A 128 8.578 21.933 -1.007 1.00 54.49 C ANISOU 877 CB LEU A 128 9535 5784 5385 634 -87 -44 C ATOM 878 CG LEU A 128 10.117 21.767 -0.999 1.00 59.39 C ANISOU 878 CG LEU A 128 10149 6402 6014 669 -65 -63 C ATOM 879 CD1 LEU A 128 10.552 20.560 -0.161 1.00 59.87 C ANISOU 879 CD1 LEU A 128 10216 6429 6101 673 -90 -69 C ATOM 880 CD2 LEU A 128 10.650 21.642 -2.385 1.00 61.96 C ANISOU 880 CD2 LEU A 128 10487 6746 6308 702 -50 -88 C ATOM 881 N SER A 129 8.644 24.643 0.482 1.00 56.96 N ANISOU 881 N SER A 129 9769 6143 5732 624 -52 -17 N ATOM 882 CA SER A 129 9.334 25.822 1.028 1.00 56.93 C ANISOU 882 CA SER A 129 9727 6144 5759 634 -41 -21 C ATOM 883 C SER A 129 9.016 26.002 2.515 1.00 61.08 C ANISOU 883 C SER A 129 10228 6689 6291 635 -58 -32 C ATOM 884 O SER A 129 9.928 26.223 3.314 1.00 60.08 O ANISOU 884 O SER A 129 10079 6564 6183 648 -56 -46 O ATOM 885 CB SER A 129 8.944 27.078 0.250 1.00 59.95 C ANISOU 885 CB SER A 129 10089 6529 6159 628 -36 -7 C ATOM 886 OG SER A 129 9.608 28.232 0.742 1.00 67.14 O ANISOU 886 OG SER A 129 10961 7430 7119 637 -42 -10 O ATOM 887 N ALA A 130 7.724 25.841 2.887 1.00 58.50 N ANISOU 887 N ALA A 130 9900 6386 5941 623 -75 -23 N ATOM 888 CA ALA A 130 7.252 25.972 4.264 1.00 58.71 C ANISOU 888 CA ALA A 130 9891 6460 5955 631 -91 -29 C ATOM 889 C ALA A 130 7.908 24.936 5.178 1.00 63.09 C ANISOU 889 C ALA A 130 10434 7034 6505 632 -97 -20 C ATOM 890 O ALA A 130 8.352 25.291 6.269 1.00 63.47 O ANISOU 890 O ALA A 130 10444 7118 6554 649 -100 -38 O ATOM 891 CB ALA A 130 5.739 25.834 4.314 1.00 59.49 C ANISOU 891 CB ALA A 130 9988 6595 6022 619 -108 -2 C ATOM 892 N SER A 131 8.012 23.666 4.716 1.00 59.12 N ANISOU 892 N SER A 131 9959 6503 6002 616 -104 7 N ATOM 893 CA SER A 131 8.644 22.587 5.485 1.00 59.09 C ANISOU 893 CA SER A 131 9940 6505 6008 612 -115 26 C ATOM 894 C SER A 131 10.122 22.888 5.754 1.00 62.58 C ANISOU 894 C SER A 131 10374 6933 6471 630 -90 0 C ATOM 895 O SER A 131 10.591 22.694 6.875 1.00 61.89 O ANISOU 895 O SER A 131 10247 6882 6385 632 -92 8 O ATOM 896 CB SER A 131 8.513 21.255 4.752 1.00 63.29 C ANISOU 896 CB SER A 131 10507 6987 6553 597 -137 47 C ATOM 897 OG SER A 131 7.165 20.821 4.684 1.00 72.97 O ANISOU 897 OG SER A 131 11733 8225 7767 574 -172 86 O ATOM 898 N VAL A 132 10.843 23.390 4.728 1.00 59.33 N ANISOU 898 N VAL A 132 9991 6480 6072 642 -67 -21 N ATOM 899 CA VAL A 132 12.267 23.737 4.815 1.00 59.19 C ANISOU 899 CA VAL A 132 9965 6449 6075 658 -45 -32 C ATOM 900 C VAL A 132 12.484 24.806 5.898 1.00 62.40 C ANISOU 900 C VAL A 132 10330 6887 6491 665 -49 -50 C ATOM 901 O VAL A 132 13.309 24.608 6.792 1.00 61.78 O ANISOU 901 O VAL A 132 10227 6826 6420 668 -46 -49 O ATOM 902 CB VAL A 132 12.823 24.209 3.438 1.00 63.55 C ANISOU 902 CB VAL A 132 10541 6973 6632 670 -25 -34 C ATOM 903 CG1 VAL A 132 14.274 24.676 3.555 1.00 63.32 C ANISOU 903 CG1 VAL A 132 10494 6939 6625 685 -8 -28 C ATOM 904 CG2 VAL A 132 12.694 23.108 2.386 1.00 63.76 C ANISOU 904 CG2 VAL A 132 10607 6980 6640 676 -25 -34 C ATOM 905 N PHE A 133 11.730 25.924 5.826 1.00 58.84 N ANISOU 905 N PHE A 133 9867 6444 6043 669 -61 -70 N ATOM 906 CA PHE A 133 11.846 27.014 6.792 1.00 58.70 C ANISOU 906 CA PHE A 133 9810 6451 6043 685 -77 -105 C ATOM 907 C PHE A 133 11.376 26.577 8.190 1.00 62.34 C ANISOU 907 C PHE A 133 10234 6987 6467 692 -91 -115 C ATOM 908 O PHE A 133 11.917 27.060 9.186 1.00 62.02 O ANISOU 908 O PHE A 133 10157 6977 6431 709 -101 -146 O ATOM 909 CB PHE A 133 11.071 28.250 6.324 1.00 60.67 C ANISOU 909 CB PHE A 133 10053 6683 6313 692 -94 -127 C ATOM 910 CG PHE A 133 11.783 29.069 5.273 1.00 62.40 C ANISOU 910 CG PHE A 133 10278 6846 6584 688 -92 -113 C ATOM 911 CD1 PHE A 133 12.735 30.017 5.634 1.00 65.57 C ANISOU 911 CD1 PHE A 133 10652 7222 7041 698 -113 -128 C ATOM 912 CD2 PHE A 133 11.475 28.923 3.927 1.00 64.78 C ANISOU 912 CD2 PHE A 133 10603 7128 6881 673 -76 -78 C ATOM 913 CE1 PHE A 133 13.394 30.777 4.660 1.00 66.71 C ANISOU 913 CE1 PHE A 133 10786 7321 7240 690 -120 -92 C ATOM 914 CE2 PHE A 133 12.129 29.689 2.955 1.00 67.80 C ANISOU 914 CE2 PHE A 133 10973 7481 7308 670 -76 -48 C ATOM 915 CZ PHE A 133 13.085 30.609 3.329 1.00 65.98 C ANISOU 915 CZ PHE A 133 10709 7225 7137 677 -99 -48 C ATOM 916 N SER A 134 10.399 25.689 8.230 1.00 59.06 N ANISOU 916 N SER A 134 9820 6603 6016 679 -95 -82 N ATOM 917 CA SER A 134 9.889 25.196 9.484 1.00 59.39 C ANISOU 917 CA SER A 134 9811 6735 6019 684 -110 -67 C ATOM 918 C SER A 134 10.984 24.387 10.160 1.00 64.08 C ANISOU 918 C SER A 134 10384 7342 6621 675 -102 -45 C ATOM 919 O SER A 134 11.190 24.480 11.355 1.00 63.76 O ANISOU 919 O SER A 134 10288 7379 6559 689 -109 -54 O ATOM 920 CB SER A 134 8.663 24.334 9.257 1.00 62.81 C ANISOU 920 CB SER A 134 10246 7192 6424 665 -124 -14 C ATOM 921 OG SER A 134 7.532 25.141 9.030 1.00 70.59 O ANISOU 921 OG SER A 134 11232 8200 7389 677 -133 -31 O ATOM 922 N LEU A 135 11.692 23.586 9.380 1.00 61.12 N ANISOU 922 N LEU A 135 10049 6897 6276 657 -87 -19 N ATOM 923 CA LEU A 135 12.760 22.773 9.925 1.00 61.17 C ANISOU 923 CA LEU A 135 10037 6906 6298 648 -78 7 C ATOM 924 C LEU A 135 13.838 23.659 10.473 1.00 67.47 C ANISOU 924 C LEU A 135 10817 7713 7106 664 -65 -29 C ATOM 925 O LEU A 135 14.404 23.379 11.512 1.00 67.92 O ANISOU 925 O LEU A 135 10829 7822 7157 662 -64 -17 O ATOM 926 CB LEU A 135 13.358 21.877 8.857 1.00 60.82 C ANISOU 926 CB LEU A 135 10044 6780 6285 638 -67 27 C ATOM 927 CG LEU A 135 12.472 20.740 8.380 1.00 65.21 C ANISOU 927 CG LEU A 135 10617 7315 6847 620 -93 62 C ATOM 928 CD1 LEU A 135 13.107 20.017 7.229 1.00 65.18 C ANISOU 928 CD1 LEU A 135 10666 7230 6870 626 -86 55 C ATOM 929 CD2 LEU A 135 12.197 19.793 9.501 1.00 67.50 C ANISOU 929 CD2 LEU A 135 10847 7659 7141 600 -119 120 C ATOM 930 N LEU A 136 14.125 24.733 9.759 1.00 64.90 N ANISOU 930 N LEU A 136 10521 7338 6802 677 -61 -65 N ATOM 931 CA LEU A 136 15.144 25.670 10.175 1.00 65.22 C ANISOU 931 CA LEU A 136 10544 7370 6866 690 -62 -95 C ATOM 932 C LEU A 136 14.723 26.300 11.486 1.00 71.04 C ANISOU 932 C LEU A 136 11227 8186 7578 709 -88 -140 C ATOM 933 O LEU A 136 15.512 26.443 12.404 1.00 70.49 O ANISOU 933 O LEU A 136 11122 8151 7509 715 -92 -153 O ATOM 934 CB LEU A 136 15.291 26.740 9.106 1.00 65.07 C ANISOU 934 CB LEU A 136 10555 7285 6885 696 -67 -111 C ATOM 935 CG LEU A 136 16.337 27.822 9.299 1.00 69.50 C ANISOU 935 CG LEU A 136 11099 7816 7492 705 -84 -129 C ATOM 936 CD1 LEU A 136 17.706 27.252 9.090 1.00 69.22 C ANISOU 936 CD1 LEU A 136 11073 7759 7469 695 -58 -83 C ATOM 937 CD2 LEU A 136 16.069 28.939 8.326 1.00 71.60 C ANISOU 937 CD2 LEU A 136 11375 8028 7802 708 -103 -136 C ATOM 938 N ALA A 137 13.457 26.670 11.564 1.00 69.39 N ANISOU 938 N ALA A 137 11008 8015 7344 724 -106 -164 N ATOM 939 CA ALA A 137 12.906 27.289 12.773 1.00 70.30 C ANISOU 939 CA ALA A 137 11065 8223 7421 757 -133 -217 C ATOM 940 C ALA A 137 13.122 26.402 14.009 1.00 75.74 C ANISOU 940 C ALA A 137 11694 9020 8064 755 -128 -187 C ATOM 941 O ALA A 137 13.353 26.929 15.099 1.00 75.50 O ANISOU 941 O ALA A 137 11611 9067 8009 784 -146 -237 O ATOM 942 CB ALA A 137 11.426 27.574 12.586 1.00 71.10 C ANISOU 942 CB ALA A 137 11163 8360 7492 774 -148 -230 C ATOM 943 N ILE A 138 13.079 25.058 13.834 1.00 73.19 N ANISOU 943 N ILE A 138 11373 8700 7735 720 -110 -107 N ATOM 944 CA ILE A 138 13.321 24.118 14.937 1.00 73.85 C ANISOU 944 CA ILE A 138 11389 8881 7789 708 -108 -55 C ATOM 945 C ILE A 138 14.832 24.015 15.195 1.00 78.41 C ANISOU 945 C ILE A 138 11968 9425 8399 695 -89 -53 C ATOM 946 O ILE A 138 15.251 23.935 16.351 1.00 78.49 O ANISOU 946 O ILE A 138 11913 9530 8382 701 -92 -50 O ATOM 947 CB ILE A 138 12.692 22.713 14.676 1.00 77.11 C ANISOU 947 CB ILE A 138 11796 9300 8204 673 -111 39 C ATOM 948 CG1 ILE A 138 11.199 22.827 14.273 1.00 77.82 C ANISOU 948 CG1 ILE A 138 11892 9411 8266 680 -131 47 C ATOM 949 CG2 ILE A 138 12.859 21.804 15.909 1.00 78.20 C ANISOU 949 CG2 ILE A 138 11842 9553 8319 658 -118 108 C ATOM 950 CD1 ILE A 138 10.561 21.519 13.699 1.00 86.23 C ANISOU 950 CD1 ILE A 138 12970 10441 9354 641 -147 136 C ATOM 951 N ALA A 139 15.644 24.037 14.114 1.00 75.05 N ANISOU 951 N ALA A 139 11611 8877 8026 681 -70 -49 N ATOM 952 CA ALA A 139 17.106 23.945 14.195 1.00 75.12 C ANISOU 952 CA ALA A 139 11628 8847 8067 670 -50 -36 C ATOM 953 C ALA A 139 17.702 25.069 15.058 1.00 79.97 C ANISOU 953 C ALA A 139 12209 9500 8677 691 -67 -96 C ATOM 954 O ALA A 139 18.415 24.779 16.021 1.00 79.94 O ANISOU 954 O ALA A 139 12158 9556 8660 684 -61 -80 O ATOM 955 CB ALA A 139 17.709 23.987 12.802 1.00 75.63 C ANISOU 955 CB ALA A 139 11765 8795 8176 664 -32 -26 C ATOM 956 N ILE A 140 17.383 26.349 14.732 1.00 76.67 N ANISOU 956 N ILE A 140 11812 9046 8275 718 -94 -165 N ATOM 957 CA ILE A 140 17.885 27.523 15.466 1.00 76.75 C ANISOU 957 CA ILE A 140 11793 9071 8297 743 -129 -236 C ATOM 958 C ILE A 140 17.383 27.490 16.928 1.00 80.82 C ANISOU 958 C ILE A 140 12230 9731 8745 770 -147 -277 C ATOM 959 O ILE A 140 18.160 27.765 17.844 1.00 80.54 O ANISOU 959 O ILE A 140 12155 9743 8703 778 -160 -305 O ATOM 960 CB ILE A 140 17.483 28.850 14.751 1.00 79.99 C ANISOU 960 CB ILE A 140 12235 9403 8755 766 -167 -297 C ATOM 961 CG1 ILE A 140 17.954 28.851 13.273 1.00 80.13 C ANISOU 961 CG1 ILE A 140 12313 9305 8829 740 -148 -242 C ATOM 962 CG2 ILE A 140 18.031 30.078 15.509 1.00 81.24 C ANISOU 962 CG2 ILE A 140 12363 9559 8946 794 -221 -378 C ATOM 963 CD1 ILE A 140 17.386 30.001 12.407 1.00 89.00 C ANISOU 963 CD1 ILE A 140 13457 10357 10002 753 -181 -276 C ATOM 964 N GLU A 141 16.105 27.098 17.138 1.00 77.47 N ANISOU 964 N GLU A 141 11778 9389 8266 784 -148 -271 N ATOM 965 CA GLU A 141 15.482 27.005 18.465 1.00 77.78 C ANISOU 965 CA GLU A 141 11729 9597 8226 817 -164 -295 C ATOM 966 C GLU A 141 16.331 26.138 19.419 1.00 82.08 C ANISOU 966 C GLU A 141 12213 10228 8746 792 -143 -237 C ATOM 967 O GLU A 141 16.487 26.495 20.587 1.00 82.48 O ANISOU 967 O GLU A 141 12192 10400 8747 823 -162 -284 O ATOM 968 CB GLU A 141 14.053 26.439 18.343 1.00 79.11 C ANISOU 968 CB GLU A 141 11879 9835 8347 822 -162 -252 C ATOM 969 CG GLU A 141 13.236 26.482 19.627 1.00 89.90 C ANISOU 969 CG GLU A 141 13143 11395 9619 867 -182 -274 C ATOM 970 CD GLU A 141 13.451 25.329 20.595 1.00113.10 C ANISOU 970 CD GLU A 141 15992 14470 12510 843 -167 -181 C ATOM 971 OE1 GLU A 141 13.938 24.260 20.158 1.00102.96 O ANISOU 971 OE1 GLU A 141 14730 13120 11272 785 -142 -83 O ATOM 972 OE2 GLU A 141 13.051 25.469 21.773 1.00111.69 O1- ANISOU 972 OE2 GLU A 141 15715 14474 12249 885 -184 -202 O1- ATOM 973 N ARG A 142 16.888 25.014 18.912 1.00 78.10 N ANISOU 973 N ARG A 142 11734 9663 8278 740 -108 -138 N ATOM 974 CA ARG A 142 17.714 24.098 19.710 1.00 78.15 C ANISOU 974 CA ARG A 142 11682 9737 8276 708 -87 -67 C ATOM 975 C ARG A 142 19.050 24.746 20.117 1.00 83.75 C ANISOU 975 C ARG A 142 12394 10421 9006 709 -86 -109 C ATOM 976 O ARG A 142 19.585 24.419 21.176 1.00 83.68 O ANISOU 976 O ARG A 142 12312 10517 8966 701 -81 -85 O ATOM 977 CB ARG A 142 17.978 22.786 18.946 1.00 76.72 C ANISOU 977 CB ARG A 142 11534 9472 8144 659 -58 37 C ATOM 978 CG ARG A 142 16.723 21.946 18.661 1.00 80.68 C ANISOU 978 CG ARG A 142 12021 10001 8634 648 -69 97 C ATOM 979 CD ARG A 142 16.260 21.133 19.857 1.00 84.00 C ANISOU 979 CD ARG A 142 12324 10584 9008 637 -81 174 C ATOM 980 NE ARG A 142 15.522 21.943 20.828 1.00 88.62 N ANISOU 980 NE ARG A 142 12836 11328 9507 685 -102 118 N ATOM 981 CZ ARG A 142 14.941 21.451 21.919 1.00103.77 C ANISOU 981 CZ ARG A 142 14636 13429 11363 690 -117 179 C ATOM 982 NH1 ARG A 142 14.983 20.148 22.171 1.00 90.90 N ANISOU 982 NH1 ARG A 142 12944 11834 9760 641 -117 310 N ATOM 983 NH2 ARG A 142 14.282 22.251 22.744 1.00 91.76 N ANISOU 983 NH2 ARG A 142 13050 12062 9754 747 -136 114 N ATOM 984 N TYR A 143 19.574 25.668 19.289 1.00 81.49 N ANISOU 984 N TYR A 143 12184 10004 8776 717 -97 -161 N ATOM 985 CA TYR A 143 20.825 26.374 19.586 1.00 82.22 C ANISOU 985 CA TYR A 143 12281 10058 8901 715 -109 -193 C ATOM 986 C TYR A 143 20.606 27.451 20.673 1.00 88.46 C ANISOU 986 C TYR A 143 13017 10941 9654 763 -160 -303 C ATOM 987 O TYR A 143 21.554 27.823 21.368 1.00 88.52 O ANISOU 987 O TYR A 143 12997 10970 9666 762 -176 -328 O ATOM 988 CB TYR A 143 21.399 27.010 18.302 1.00 83.19 C ANISOU 988 CB TYR A 143 12490 10019 9102 706 -113 -194 C ATOM 989 CG TYR A 143 22.783 27.606 18.463 1.00 84.96 C ANISOU 989 CG TYR A 143 12720 10191 9371 695 -127 -195 C ATOM 990 CD1 TYR A 143 23.922 26.814 18.356 1.00 86.67 C ANISOU 990 CD1 TYR A 143 12942 10384 9603 657 -85 -106 C ATOM 991 CD2 TYR A 143 22.957 28.975 18.646 1.00 86.07 C ANISOU 991 CD2 TYR A 143 12860 10293 9548 721 -189 -279 C ATOM 992 CE1 TYR A 143 25.199 27.360 18.483 1.00 87.50 C ANISOU 992 CE1 TYR A 143 13052 10445 9749 644 -99 -93 C ATOM 993 CE2 TYR A 143 24.229 29.532 18.782 1.00 87.09 C ANISOU 993 CE2 TYR A 143 12993 10369 9729 706 -213 -269 C ATOM 994 CZ TYR A 143 25.349 28.721 18.695 1.00 93.78 C ANISOU 994 CZ TYR A 143 13846 11206 10582 666 -165 -171 C ATOM 995 OH TYR A 143 26.606 29.263 18.820 1.00 94.50 O ANISOU 995 OH TYR A 143 13937 11247 10720 648 -189 -147 O ATOM 996 N ILE A 144 19.356 27.939 20.821 1.00 86.44 N ANISOU 996 N ILE A 144 12742 10744 9358 809 -189 -373 N ATOM 997 CA ILE A 144 19.011 28.993 21.783 1.00 87.60 C ANISOU 997 CA ILE A 144 12837 10981 9465 872 -245 -498 C ATOM 998 C ILE A 144 18.697 28.386 23.178 1.00 94.30 C ANISOU 998 C ILE A 144 13575 12045 10208 893 -237 -491 C ATOM 999 O ILE A 144 18.868 29.072 24.189 1.00 95.07 O ANISOU 999 O ILE A 144 13616 12242 10265 940 -277 -586 O ATOM 1000 CB ILE A 144 17.817 29.850 21.246 1.00 90.77 C ANISOU 1000 CB ILE A 144 13267 11346 9875 919 -282 -577 C ATOM 1001 CG1 ILE A 144 18.152 30.467 19.860 1.00 90.63 C ANISOU 1001 CG1 ILE A 144 13343 11129 9965 894 -292 -570 C ATOM 1002 CG2 ILE A 144 17.406 30.947 22.252 1.00 92.52 C ANISOU 1002 CG2 ILE A 144 13432 11664 10057 999 -347 -723 C ATOM 1003 CD1 ILE A 144 16.939 30.997 19.069 1.00 96.70 C ANISOU 1003 CD1 ILE A 144 14145 11850 10749 920 -309 -604 C ATOM 1004 N THR A 145 18.259 27.105 23.229 1.00 91.85 N ANISOU 1004 N THR A 145 13228 11812 9858 859 -192 -375 N ATOM 1005 CA THR A 145 17.892 26.441 24.496 1.00 92.76 C ANISOU 1005 CA THR A 145 13221 12147 9876 872 -185 -337 C ATOM 1006 C THR A 145 19.088 26.332 25.464 1.00 98.41 C ANISOU 1006 C THR A 145 13879 12936 10577 856 -179 -331 C ATOM 1007 O THR A 145 18.913 26.533 26.669 1.00 98.80 O ANISOU 1007 O THR A 145 13827 13175 10538 899 -199 -377 O ATOM 1008 CB THR A 145 17.298 25.054 24.239 1.00 99.43 C ANISOU 1008 CB THR A 145 14038 13028 10712 825 -149 -192 C ATOM 1009 OG1 THR A 145 18.200 24.294 23.432 1.00 98.38 O ANISOU 1009 OG1 THR A 145 13972 12744 10665 758 -113 -104 O ATOM 1010 CG2 THR A 145 15.924 25.118 23.590 1.00 97.07 C ANISOU 1010 CG2 THR A 145 13766 12715 10399 848 -161 -194 C ATOM 1011 N MET A 146 20.292 26.021 24.939 1.00 95.48 N ANISOU 1011 N MET A 146 13568 12427 10284 798 -152 -272 N ATOM 1012 CA MET A 146 21.504 25.874 25.756 1.00 95.92 C ANISOU 1012 CA MET A 146 13576 12535 10334 773 -142 -251 C ATOM 1013 C MET A 146 21.994 27.241 26.305 1.00101.49 C ANISOU 1013 C MET A 146 14282 13243 11035 822 -198 -395 C ATOM 1014 O MET A 146 22.375 27.323 27.477 1.00101.82 O ANISOU 1014 O MET A 146 14238 13435 11016 838 -211 -425 O ATOM 1015 CB MET A 146 22.633 25.176 24.961 1.00 97.52 C ANISOU 1015 CB MET A 146 13845 12584 10623 703 -98 -145 C ATOM 1016 CG MET A 146 22.926 25.816 23.605 1.00100.74 C ANISOU 1016 CG MET A 146 14376 12782 11118 699 -106 -175 C ATOM 1017 SD MET A 146 24.354 25.106 22.755 1.00104.45 S ANISOU 1017 SD MET A 146 14912 13104 11670 635 -57 -62 S ATOM 1018 CE MET A 146 25.689 25.804 23.724 1.00101.61 C ANISOU 1018 CE MET A 146 14517 12781 11310 629 -78 -94 C ATOM 1019 N LEU A 147 21.969 28.303 25.467 1.00 98.46 N ANISOU 1019 N LEU A 147 13989 12700 10721 844 -239 -481 N ATOM 1020 CA LEU A 147 22.438 29.629 25.869 1.00 99.08 C ANISOU 1020 CA LEU A 147 14075 12747 10825 888 -310 -616 C ATOM 1021 C LEU A 147 21.352 30.693 25.639 1.00103.03 C ANISOU 1021 C LEU A 147 14594 13225 11327 960 -370 -748 C ATOM 1022 O LEU A 147 21.052 31.043 24.492 1.00102.04 O ANISOU 1022 O LEU A 147 14549 12944 11277 951 -376 -741 O ATOM 1023 CB LEU A 147 23.729 29.995 25.101 1.00 98.94 C ANISOU 1023 CB LEU A 147 14137 12536 10917 838 -317 -579 C ATOM 1024 CG LEU A 147 24.463 31.274 25.548 1.00104.70 C ANISOU 1024 CG LEU A 147 14870 13216 11695 866 -401 -693 C ATOM 1025 CD1 LEU A 147 25.115 31.093 26.925 1.00105.41 C ANISOU 1025 CD1 LEU A 147 14874 13463 11716 870 -406 -715 C ATOM 1026 CD2 LEU A 147 25.516 31.677 24.530 1.00107.22 C ANISOU 1026 CD2 LEU A 147 15271 13333 12135 817 -413 -632 C ATOM 1027 N LYS A 148 20.776 31.213 26.742 1.00100.26 N ANISOU 1027 N LYS A 148 14162 13040 10892 1037 -416 -869 N ATOM 1028 CA LYS A 148 19.736 32.244 26.704 1.00125.62 C ANISOU 1028 CA LYS A 148 17379 16255 14098 1120 -480 -1009 C ATOM 1029 C LYS A 148 20.318 33.601 27.102 1.00157.12 C ANISOU 1029 C LYS A 148 21376 20178 18146 1169 -577 -1167 C ATOM 1030 O LYS A 148 19.663 34.630 26.945 1.00120.66 O ANISOU 1030 O LYS A 148 16775 15511 13561 1236 -646 -1295 O ATOM 1031 CB LYS A 148 18.565 31.870 27.632 1.00128.56 C ANISOU 1031 CB LYS A 148 17647 16873 14326 1186 -469 -1038 C ATOM 1032 CG LYS A 148 17.794 30.633 27.189 1.00139.95 C ANISOU 1032 CG LYS A 148 19079 18369 15727 1141 -394 -885 C ATOM 1033 CD LYS A 148 16.661 30.317 28.149 1.00149.14 C ANISOU 1033 CD LYS A 148 20126 19791 16750 1207 -392 -898 C ATOM 1034 CE LYS A 148 15.904 29.081 27.743 1.00158.26 C ANISOU 1034 CE LYS A 148 21262 20993 17875 1158 -333 -734 C ATOM 1035 NZ LYS A 148 14.794 28.784 28.685 1.00167.68 N ANISOU 1035 NZ LYS A 148 22328 22453 18931 1221 -336 -726 N ATOM 1036 N ASN A 156 8.213 36.880 24.735 1.00 96.83 N ANISOU 1036 N ASN A 156 13699 12866 10228 1726 -686 -1593 N ATOM 1037 CA ASN A 156 8.739 36.610 23.397 1.00 95.43 C ANISOU 1037 CA ASN A 156 13625 12452 10182 1607 -650 -1472 C ATOM 1038 C ASN A 156 7.837 35.596 22.646 1.00 97.94 C ANISOU 1038 C ASN A 156 13963 12795 10454 1545 -572 -1304 C ATOM 1039 O ASN A 156 8.339 34.729 21.922 1.00 96.57 O ANISOU 1039 O ASN A 156 13842 12529 10321 1443 -518 -1165 O ATOM 1040 CB ASN A 156 10.205 36.106 23.471 1.00 95.86 C ANISOU 1040 CB ASN A 156 13702 12438 10283 1527 -632 -1413 C ATOM 1041 CG ASN A 156 10.430 34.860 24.316 1.00117.00 C ANISOU 1041 CG ASN A 156 16309 15311 12836 1502 -573 -1316 C ATOM 1042 OD1 ASN A 156 9.556 34.401 25.065 1.00112.22 O ANISOU 1042 OD1 ASN A 156 15617 14925 12095 1555 -556 -1301 O ATOM 1043 ND2 ASN A 156 11.633 34.310 24.239 1.00107.10 N ANISOU 1043 ND2 ASN A 156 15080 13987 11627 1424 -547 -1242 N ATOM 1044 N ASN A 157 6.504 35.735 22.803 1.00 94.28 N ANISOU 1044 N ASN A 157 13459 12455 9909 1613 -574 -1322 N ATOM 1045 CA ASN A 157 5.529 34.862 22.143 1.00 93.02 C ANISOU 1045 CA ASN A 157 13313 12326 9706 1562 -514 -1169 C ATOM 1046 C ASN A 157 4.999 35.509 20.857 1.00 95.26 C ANISOU 1046 C ASN A 157 13681 12417 10097 1537 -520 -1167 C ATOM 1047 O ASN A 157 4.643 34.798 19.914 1.00 93.41 O ANISOU 1047 O ASN A 157 13496 12115 9881 1458 -470 -1032 O ATOM 1048 CB ASN A 157 4.374 34.533 23.087 1.00 94.58 C ANISOU 1048 CB ASN A 157 13405 12792 9741 1644 -508 -1160 C ATOM 1049 N PHE A 158 4.945 36.859 20.822 1.00 92.13 N ANISOU 1049 N PHE A 158 13295 11934 9776 1606 -588 -1318 N ATOM 1050 CA PHE A 158 4.467 37.609 19.658 1.00 91.39 C ANISOU 1050 CA PHE A 158 13267 11662 9796 1586 -604 -1321 C ATOM 1051 C PHE A 158 5.467 37.518 18.498 1.00 94.25 C ANISOU 1051 C PHE A 158 13714 11801 10296 1475 -587 -1240 C ATOM 1052 O PHE A 158 5.051 37.486 17.338 1.00 93.36 O ANISOU 1052 O PHE A 158 13654 11576 10241 1418 -561 -1157 O ATOM 1053 CB PHE A 158 4.201 39.080 20.026 1.00 94.09 C ANISOU 1053 CB PHE A 158 13584 11970 10196 1693 -694 -1507 C ATOM 1054 CG PHE A 158 3.749 39.946 18.871 1.00 95.22 C ANISOU 1054 CG PHE A 158 13781 11926 10473 1674 -720 -1510 C ATOM 1055 CD1 PHE A 158 2.465 39.825 18.350 1.00 97.94 C ANISOU 1055 CD1 PHE A 158 14128 12310 10774 1679 -684 -1447 C ATOM 1056 CD2 PHE A 158 4.596 40.903 18.324 1.00 97.33 C ANISOU 1056 CD2 PHE A 158 14086 11981 10913 1649 -785 -1566 C ATOM 1057 CE1 PHE A 158 2.049 40.625 17.281 1.00 98.69 C ANISOU 1057 CE1 PHE A 158 14265 12239 10994 1657 -706 -1441 C ATOM 1058 CE2 PHE A 158 4.174 41.709 17.263 1.00100.08 C ANISOU 1058 CE2 PHE A 158 14468 12165 11392 1627 -813 -1554 C ATOM 1059 CZ PHE A 158 2.905 41.562 16.746 1.00 97.93 C ANISOU 1059 CZ PHE A 158 14200 11938 11071 1631 -770 -1493 C ATOM 1060 N ARG A 159 6.782 37.455 18.811 1.00 90.42 N ANISOU 1060 N ARG A 159 13235 11266 9854 1447 -602 -1259 N ATOM 1061 CA ARG A 159 7.826 37.337 17.787 1.00 89.17 C ANISOU 1061 CA ARG A 159 13145 10921 9813 1350 -587 -1176 C ATOM 1062 C ARG A 159 7.765 35.952 17.101 1.00 90.85 C ANISOU 1062 C ARG A 159 13394 11148 9976 1261 -498 -1008 C ATOM 1063 O ARG A 159 8.190 35.826 15.954 1.00 89.83 O ANISOU 1063 O ARG A 159 13326 10878 9929 1188 -475 -927 O ATOM 1064 CB ARG A 159 9.234 37.593 18.381 1.00 90.13 C ANISOU 1064 CB ARG A 159 13259 11003 9984 1346 -627 -1232 C ATOM 1065 CG ARG A 159 9.712 36.534 19.386 1.00102.31 C ANISOU 1065 CG ARG A 159 14759 12706 11410 1341 -584 -1198 C ATOM 1066 CD ARG A 159 11.159 36.742 19.805 1.00114.45 C ANISOU 1066 CD ARG A 159 16296 14185 13004 1322 -616 -1231 C ATOM 1067 NE ARG A 159 11.315 37.889 20.704 1.00126.50 N ANISOU 1067 NE ARG A 159 17780 15730 14556 1411 -709 -1404 N ATOM 1068 CZ ARG A 159 12.460 38.224 21.292 1.00141.53 C ANISOU 1068 CZ ARG A 159 19670 17603 16501 1413 -756 -1462 C ATOM 1069 NH1 ARG A 159 13.557 37.507 21.081 1.00129.82 N ANISOU 1069 NH1 ARG A 159 18213 16076 15036 1331 -712 -1355 N ATOM 1070 NH2 ARG A 159 12.515 39.275 22.099 1.00128.03 N ANISOU 1070 NH2 ARG A 159 17920 15908 14816 1500 -852 -1632 N ATOM 1071 N LEU A 160 7.202 34.929 17.800 1.00 86.40 N ANISOU 1071 N LEU A 160 12787 10761 9281 1272 -456 -955 N ATOM 1072 CA LEU A 160 7.071 33.561 17.279 1.00 85.01 C ANISOU 1072 CA LEU A 160 12634 10603 9063 1194 -388 -803 C ATOM 1073 C LEU A 160 6.038 33.487 16.147 1.00 86.75 C ANISOU 1073 C LEU A 160 12899 10760 9300 1164 -365 -734 C ATOM 1074 O LEU A 160 6.303 32.855 15.122 1.00 85.32 O ANISOU 1074 O LEU A 160 12777 10479 9162 1088 -328 -638 O ATOM 1075 CB LEU A 160 6.680 32.579 18.402 1.00 85.47 C ANISOU 1075 CB LEU A 160 12614 10872 8990 1217 -366 -758 C ATOM 1076 CG LEU A 160 7.708 32.361 19.519 1.00 90.95 C ANISOU 1076 CG LEU A 160 13254 11652 9650 1232 -375 -793 C ATOM 1077 CD1 LEU A 160 7.076 31.653 20.706 1.00 91.82 C ANISOU 1077 CD1 LEU A 160 13261 12005 9623 1273 -366 -759 C ATOM 1078 CD2 LEU A 160 8.914 31.577 19.021 1.00 92.77 C ANISOU 1078 CD2 LEU A 160 13534 11773 9942 1144 -340 -706 C ATOM 1079 N PHE A 161 4.862 34.129 16.333 1.00 82.63 N ANISOU 1079 N PHE A 161 12349 10304 8743 1227 -388 -787 N ATOM 1080 CA PHE A 161 3.800 34.120 15.325 1.00 81.51 C ANISOU 1080 CA PHE A 161 12244 10115 8612 1201 -368 -722 C ATOM 1081 C PHE A 161 4.167 35.001 14.121 1.00 81.72 C ANISOU 1081 C PHE A 161 12332 9945 8772 1166 -384 -740 C ATOM 1082 O PHE A 161 3.662 34.761 13.025 1.00 81.06 O ANISOU 1082 O PHE A 161 12292 9793 8713 1114 -354 -658 O ATOM 1083 CB PHE A 161 2.455 34.551 15.928 1.00 84.46 C ANISOU 1083 CB PHE A 161 12560 10627 8903 1283 -387 -767 C ATOM 1084 CG PHE A 161 1.852 33.519 16.860 1.00 86.89 C ANISOU 1084 CG PHE A 161 12798 11143 9071 1303 -365 -698 C ATOM 1085 CD1 PHE A 161 1.285 32.350 16.359 1.00 89.69 C ANISOU 1085 CD1 PHE A 161 13167 11523 9387 1235 -325 -547 C ATOM 1086 CD2 PHE A 161 1.830 33.728 18.235 1.00 90.49 C ANISOU 1086 CD2 PHE A 161 13167 11778 9438 1391 -392 -779 C ATOM 1087 CE1 PHE A 161 0.732 31.394 17.221 1.00 90.99 C ANISOU 1087 CE1 PHE A 161 13255 11880 9438 1248 -316 -463 C ATOM 1088 CE2 PHE A 161 1.267 32.774 19.096 1.00 93.63 C ANISOU 1088 CE2 PHE A 161 13481 12388 9705 1408 -375 -695 C ATOM 1089 CZ PHE A 161 0.724 31.615 18.582 1.00 91.04 C ANISOU 1089 CZ PHE A 161 13164 12074 9352 1333 -338 -529 C ATOM 1090 N LEU A 162 5.079 35.987 14.309 1.00 75.59 N ANISOU 1090 N LEU A 162 11553 9081 8086 1191 -434 -836 N ATOM 1091 CA LEU A 162 5.586 36.802 13.200 1.00 73.78 C ANISOU 1091 CA LEU A 162 11366 8671 7995 1151 -457 -832 C ATOM 1092 C LEU A 162 6.473 35.954 12.300 1.00 74.08 C ANISOU 1092 C LEU A 162 11454 8631 8060 1061 -408 -719 C ATOM 1093 O LEU A 162 6.381 36.052 11.080 1.00 73.36 O ANISOU 1093 O LEU A 162 11400 8445 8028 1011 -391 -651 O ATOM 1094 CB LEU A 162 6.368 38.024 13.711 1.00 74.49 C ANISOU 1094 CB LEU A 162 11431 8688 8183 1198 -538 -954 C ATOM 1095 CG LEU A 162 5.550 39.218 14.204 1.00 80.24 C ANISOU 1095 CG LEU A 162 12118 9429 8939 1288 -607 -1082 C ATOM 1096 CD1 LEU A 162 6.458 40.283 14.777 1.00 81.27 C ANISOU 1096 CD1 LEU A 162 12225 9481 9173 1332 -698 -1205 C ATOM 1097 CD2 LEU A 162 4.708 39.823 13.080 1.00 82.40 C ANISOU 1097 CD2 LEU A 162 12412 9608 9290 1268 -610 -1042 C ATOM 1098 N LEU A 163 7.312 35.088 12.913 1.00 68.30 N ANISOU 1098 N LEU A 163 10718 7953 7279 1046 -385 -697 N ATOM 1099 CA LEU A 163 8.214 34.179 12.203 1.00 66.31 C ANISOU 1099 CA LEU A 163 10508 7644 7042 973 -339 -600 C ATOM 1100 C LEU A 163 7.423 33.130 11.418 1.00 67.55 C ANISOU 1100 C LEU A 163 10699 7823 7145 929 -286 -500 C ATOM 1101 O LEU A 163 7.767 32.843 10.273 1.00 67.29 O ANISOU 1101 O LEU A 163 10709 7703 7153 877 -260 -433 O ATOM 1102 CB LEU A 163 9.180 33.488 13.189 1.00 66.19 C ANISOU 1102 CB LEU A 163 10471 7694 6983 974 -330 -604 C ATOM 1103 CG LEU A 163 10.290 34.366 13.779 1.00 70.96 C ANISOU 1103 CG LEU A 163 11056 8253 7653 998 -381 -684 C ATOM 1104 CD1 LEU A 163 10.852 33.754 15.045 1.00 71.12 C ANISOU 1104 CD1 LEU A 163 11035 8387 7601 1017 -374 -705 C ATOM 1105 CD2 LEU A 163 11.399 34.621 12.764 1.00 72.93 C ANISOU 1105 CD2 LEU A 163 11344 8361 8003 946 -382 -631 C ATOM 1106 N ILE A 164 6.350 32.574 12.026 1.00 61.40 N ANISOU 1106 N ILE A 164 9892 7165 6274 952 -275 -487 N ATOM 1107 CA ILE A 164 5.482 31.587 11.375 1.00 59.26 C ANISOU 1107 CA ILE A 164 9645 6915 5955 911 -239 -391 C ATOM 1108 C ILE A 164 4.763 32.259 10.186 1.00 59.84 C ANISOU 1108 C ILE A 164 9753 6905 6077 896 -239 -378 C ATOM 1109 O ILE A 164 4.697 31.670 9.106 1.00 59.22 O ANISOU 1109 O ILE A 164 9720 6770 6011 842 -210 -305 O ATOM 1110 CB ILE A 164 4.488 30.955 12.399 1.00 62.57 C ANISOU 1110 CB ILE A 164 10010 7495 6269 943 -239 -369 C ATOM 1111 CG1 ILE A 164 5.257 30.097 13.438 1.00 63.25 C ANISOU 1111 CG1 ILE A 164 10055 7666 6311 942 -234 -352 C ATOM 1112 CG2 ILE A 164 3.403 30.118 11.691 1.00 62.89 C ANISOU 1112 CG2 ILE A 164 10072 7548 6273 902 -218 -269 C ATOM 1113 CD1 ILE A 164 4.466 29.718 14.700 1.00 73.41 C ANISOU 1113 CD1 ILE A 164 11256 9141 7493 988 -245 -340 C ATOM 1114 N SER A 165 4.308 33.524 10.363 1.00 53.97 N ANISOU 1114 N SER A 165 8985 6151 5369 944 -275 -454 N ATOM 1115 CA SER A 165 3.670 34.285 9.284 1.00 52.31 C ANISOU 1115 CA SER A 165 8796 5861 5219 929 -279 -440 C ATOM 1116 C SER A 165 4.678 34.588 8.170 1.00 54.74 C ANISOU 1116 C SER A 165 9136 6039 5623 879 -276 -408 C ATOM 1117 O SER A 165 4.383 34.338 6.998 1.00 53.41 O ANISOU 1117 O SER A 165 8999 5828 5468 831 -248 -336 O ATOM 1118 CB SER A 165 3.059 35.576 9.817 1.00 54.21 C ANISOU 1118 CB SER A 165 8995 6112 5490 998 -328 -535 C ATOM 1119 OG SER A 165 1.944 35.299 10.646 1.00 58.21 O ANISOU 1119 OG SER A 165 9467 6756 5895 1047 -325 -548 O ATOM 1120 N ALA A 166 5.898 35.047 8.544 1.00 51.05 N ANISOU 1120 N ALA A 166 8656 5524 5216 889 -305 -453 N ATOM 1121 CA ALA A 166 6.976 35.329 7.591 1.00 50.55 C ANISOU 1121 CA ALA A 166 8610 5356 5241 846 -306 -410 C ATOM 1122 C ALA A 166 7.379 34.067 6.840 1.00 54.38 C ANISOU 1122 C ALA A 166 9137 5848 5678 794 -249 -323 C ATOM 1123 O ALA A 166 7.620 34.125 5.633 1.00 53.75 O ANISOU 1123 O ALA A 166 9074 5713 5637 756 -234 -262 O ATOM 1124 CB ALA A 166 8.178 35.913 8.312 1.00 51.49 C ANISOU 1124 CB ALA A 166 8705 5439 5420 867 -351 -468 C ATOM 1125 N CYS A 167 7.393 32.911 7.548 1.00 51.08 N ANISOU 1125 N CYS A 167 8729 5505 5176 796 -222 -315 N ATOM 1126 CA CYS A 167 7.729 31.593 6.992 1.00 50.75 C ANISOU 1126 CA CYS A 167 8724 5467 5090 756 -179 -245 C ATOM 1127 C CYS A 167 6.787 31.235 5.834 1.00 53.33 C ANISOU 1127 C CYS A 167 9081 5782 5398 725 -156 -190 C ATOM 1128 O CYS A 167 7.244 30.709 4.817 1.00 52.09 O ANISOU 1128 O CYS A 167 8955 5588 5247 694 -132 -143 O ATOM 1129 CB CYS A 167 7.689 30.528 8.085 1.00 51.41 C ANISOU 1129 CB CYS A 167 8795 5635 5102 765 -169 -244 C ATOM 1130 SG CYS A 167 7.859 28.831 7.481 1.00 55.07 S ANISOU 1130 SG CYS A 167 9300 6097 5527 720 -133 -164 S ATOM 1131 N TRP A 168 5.476 31.533 5.988 1.00 49.81 N ANISOU 1131 N TRP A 168 8624 5375 4926 738 -165 -196 N ATOM 1132 CA TRP A 168 4.475 31.266 4.955 1.00 48.99 C ANISOU 1132 CA TRP A 168 8546 5265 4802 707 -147 -142 C ATOM 1133 C TRP A 168 4.513 32.332 3.846 1.00 51.22 C ANISOU 1133 C TRP A 168 8825 5479 5156 693 -151 -132 C ATOM 1134 O TRP A 168 4.328 31.989 2.680 1.00 49.69 O ANISOU 1134 O TRP A 168 8655 5266 4957 657 -128 -78 O ATOM 1135 CB TRP A 168 3.069 31.178 5.562 1.00 47.81 C ANISOU 1135 CB TRP A 168 8379 5190 4594 726 -155 -139 C ATOM 1136 CG TRP A 168 2.812 29.888 6.280 1.00 48.72 C ANISOU 1136 CG TRP A 168 8493 5379 4637 721 -151 -105 C ATOM 1137 CD1 TRP A 168 2.848 29.677 7.627 1.00 51.96 C ANISOU 1137 CD1 TRP A 168 8861 5875 5005 757 -166 -129 C ATOM 1138 CD2 TRP A 168 2.551 28.614 5.680 1.00 48.28 C ANISOU 1138 CD2 TRP A 168 8474 5319 4553 678 -139 -36 C ATOM 1139 NE1 TRP A 168 2.598 28.353 7.906 1.00 51.21 N ANISOU 1139 NE1 TRP A 168 8766 5830 4862 732 -163 -63 N ATOM 1140 CE2 TRP A 168 2.415 27.676 6.729 1.00 52.29 C ANISOU 1140 CE2 TRP A 168 8954 5902 5013 684 -152 -9 C ATOM 1141 CE3 TRP A 168 2.405 28.172 4.355 1.00 49.32 C ANISOU 1141 CE3 TRP A 168 8652 5392 4696 637 -126 5 C ATOM 1142 CZ2 TRP A 168 2.135 26.324 6.493 1.00 51.48 C ANISOU 1142 CZ2 TRP A 168 8870 5801 4890 647 -160 60 C ATOM 1143 CZ3 TRP A 168 2.119 26.836 4.125 1.00 50.83 C ANISOU 1143 CZ3 TRP A 168 8868 5586 4857 607 -132 57 C ATOM 1144 CH2 TRP A 168 1.994 25.927 5.185 1.00 51.59 C ANISOU 1144 CH2 TRP A 168 8937 5741 4923 610 -153 86 C ATOM 1145 N VAL A 169 4.773 33.615 4.206 1.00 48.05 N ANISOU 1145 N VAL A 169 8385 5043 4827 721 -186 -180 N ATOM 1146 CA VAL A 169 4.841 34.724 3.232 1.00 47.82 C ANISOU 1146 CA VAL A 169 8335 4947 4887 705 -203 -158 C ATOM 1147 C VAL A 169 5.975 34.466 2.224 1.00 51.00 C ANISOU 1147 C VAL A 169 8746 5313 5318 669 -185 -101 C ATOM 1148 O VAL A 169 5.731 34.516 1.020 1.00 50.06 O ANISOU 1148 O VAL A 169 8627 5187 5208 637 -166 -40 O ATOM 1149 CB VAL A 169 4.997 36.108 3.927 1.00 52.08 C ANISOU 1149 CB VAL A 169 8827 5443 5517 745 -263 -227 C ATOM 1150 CG1 VAL A 169 5.474 37.176 2.946 1.00 52.03 C ANISOU 1150 CG1 VAL A 169 8787 5354 5629 719 -292 -185 C ATOM 1151 CG2 VAL A 169 3.692 36.534 4.594 1.00 52.11 C ANISOU 1151 CG2 VAL A 169 8815 5489 5495 786 -280 -278 C ATOM 1152 N ILE A 170 7.189 34.127 2.721 1.00 47.85 N ANISOU 1152 N ILE A 170 8351 4909 4923 678 -187 -116 N ATOM 1153 CA ILE A 170 8.352 33.826 1.871 1.00 47.94 C ANISOU 1153 CA ILE A 170 8366 4902 4950 656 -169 -62 C ATOM 1154 C ILE A 170 8.051 32.581 1.007 1.00 52.84 C ANISOU 1154 C ILE A 170 9029 5561 5488 634 -120 -20 C ATOM 1155 O ILE A 170 8.433 32.541 -0.171 1.00 52.35 O ANISOU 1155 O ILE A 170 8961 5501 5430 616 -103 33 O ATOM 1156 CB ILE A 170 9.647 33.645 2.730 1.00 51.03 C ANISOU 1156 CB ILE A 170 8753 5284 5353 673 -180 -89 C ATOM 1157 CG1 ILE A 170 9.988 34.953 3.505 1.00 52.03 C ANISOU 1157 CG1 ILE A 170 8834 5362 5572 695 -242 -136 C ATOM 1158 CG2 ILE A 170 10.837 33.197 1.858 1.00 51.09 C ANISOU 1158 CG2 ILE A 170 8764 5289 5360 656 -155 -26 C ATOM 1159 CD1 ILE A 170 11.016 34.783 4.680 1.00 58.52 C ANISOU 1159 CD1 ILE A 170 9653 6187 6394 717 -259 -183 C ATOM 1160 N SER A 171 7.317 31.599 1.577 1.00 49.95 N ANISOU 1160 N SER A 171 8697 5231 5049 638 -106 -43 N ATOM 1161 CA SER A 171 6.933 30.380 0.864 1.00 49.84 C ANISOU 1161 CA SER A 171 8726 5242 4970 619 -77 -14 C ATOM 1162 C SER A 171 5.957 30.688 -0.273 1.00 54.61 C ANISOU 1162 C SER A 171 9330 5850 5568 596 -69 24 C ATOM 1163 O SER A 171 6.076 30.093 -1.343 1.00 54.53 O ANISOU 1163 O SER A 171 9340 5851 5528 581 -49 53 O ATOM 1164 CB SER A 171 6.316 29.369 1.822 1.00 53.18 C ANISOU 1164 CB SER A 171 9172 5698 5338 624 -80 -31 C ATOM 1165 OG SER A 171 7.255 28.964 2.802 1.00 62.41 O ANISOU 1165 OG SER A 171 10335 6873 6507 641 -84 -56 O ATOM 1166 N LEU A 172 5.004 31.636 -0.051 1.00 51.50 N ANISOU 1166 N LEU A 172 8911 5452 5202 596 -86 20 N ATOM 1167 CA LEU A 172 4.016 32.034 -1.068 1.00 51.44 C ANISOU 1167 CA LEU A 172 8897 5450 5196 570 -77 63 C ATOM 1168 C LEU A 172 4.679 32.810 -2.209 1.00 55.88 C ANISOU 1168 C LEU A 172 9420 5997 5814 554 -74 109 C ATOM 1169 O LEU A 172 4.194 32.766 -3.342 1.00 55.75 O ANISOU 1169 O LEU A 172 9399 6003 5778 528 -56 156 O ATOM 1170 CB LEU A 172 2.884 32.878 -0.450 1.00 51.67 C ANISOU 1170 CB LEU A 172 8904 5481 5246 580 -98 46 C ATOM 1171 CG LEU A 172 1.910 32.149 0.493 1.00 56.41 C ANISOU 1171 CG LEU A 172 9529 6128 5778 594 -100 27 C ATOM 1172 CD1 LEU A 172 1.028 33.142 1.234 1.00 56.98 C ANISOU 1172 CD1 LEU A 172 9566 6212 5871 624 -123 -2 C ATOM 1173 CD2 LEU A 172 1.055 31.132 -0.257 1.00 58.08 C ANISOU 1173 CD2 LEU A 172 9779 6365 5924 559 -81 78 C ATOM 1174 N ILE A 173 5.784 33.521 -1.912 1.00 52.64 N ANISOU 1174 N ILE A 173 8973 5556 5472 568 -95 103 N ATOM 1175 CA ILE A 173 6.537 34.261 -2.920 1.00 52.99 C ANISOU 1175 CA ILE A 173 8964 5595 5576 553 -101 166 C ATOM 1176 C ILE A 173 7.445 33.281 -3.686 1.00 59.42 C ANISOU 1176 C ILE A 173 9796 6454 6327 554 -68 192 C ATOM 1177 O ILE A 173 7.309 33.160 -4.903 1.00 58.86 O ANISOU 1177 O ILE A 173 9708 6430 6227 539 -47 244 O ATOM 1178 CB ILE A 173 7.345 35.432 -2.287 1.00 56.28 C ANISOU 1178 CB ILE A 173 9328 5954 6101 565 -151 159 C ATOM 1179 CG1 ILE A 173 6.411 36.421 -1.549 1.00 56.83 C ANISOU 1179 CG1 ILE A 173 9378 5979 6236 576 -191 114 C ATOM 1180 CG2 ILE A 173 8.184 36.159 -3.355 1.00 57.48 C ANISOU 1180 CG2 ILE A 173 9410 6108 6321 545 -164 250 C ATOM 1181 CD1 ILE A 173 7.119 37.295 -0.472 1.00 63.18 C ANISOU 1181 CD1 ILE A 173 10152 6722 7131 606 -251 60 C ATOM 1182 N LEU A 174 8.327 32.535 -2.957 1.00 57.94 N ANISOU 1182 N LEU A 174 9641 6261 6112 578 -63 152 N ATOM 1183 CA LEU A 174 9.262 31.560 -3.553 1.00 58.39 C ANISOU 1183 CA LEU A 174 9717 6358 6112 591 -35 165 C ATOM 1184 C LEU A 174 8.538 30.352 -4.177 1.00 61.55 C ANISOU 1184 C LEU A 174 10169 6794 6425 589 -10 147 C ATOM 1185 O LEU A 174 9.165 29.569 -4.888 1.00 61.10 O ANISOU 1185 O LEU A 174 10123 6774 6318 607 9 149 O ATOM 1186 CB LEU A 174 10.291 31.057 -2.515 1.00 58.73 C ANISOU 1186 CB LEU A 174 9780 6379 6155 614 -39 127 C ATOM 1187 CG LEU A 174 11.467 31.996 -2.203 1.00 64.12 C ANISOU 1187 CG LEU A 174 10412 7038 6913 620 -63 156 C ATOM 1188 CD1 LEU A 174 12.354 31.408 -1.120 1.00 64.20 C ANISOU 1188 CD1 LEU A 174 10447 7032 6913 640 -63 116 C ATOM 1189 CD2 LEU A 174 12.301 32.280 -3.454 1.00 67.24 C ANISOU 1189 CD2 LEU A 174 10757 7480 7313 620 -54 236 C ATOM 1190 N GLY A 175 7.244 30.222 -3.915 1.00 57.93 N ANISOU 1190 N GLY A 175 9737 6324 5951 572 -15 129 N ATOM 1191 CA GLY A 175 6.443 29.132 -4.452 1.00 57.91 C ANISOU 1191 CA GLY A 175 9782 6343 5878 564 -5 117 C ATOM 1192 C GLY A 175 5.620 29.517 -5.662 1.00 62.15 C ANISOU 1192 C GLY A 175 10300 6916 6399 539 5 159 C ATOM 1193 O GLY A 175 5.480 28.721 -6.597 1.00 61.33 O ANISOU 1193 O GLY A 175 10218 6848 6236 541 14 156 O ATOM 1194 N GLY A 176 5.081 30.742 -5.645 1.00 59.28 N ANISOU 1194 N GLY A 176 9892 6542 6091 519 -2 195 N ATOM 1195 CA GLY A 176 4.196 31.232 -6.699 1.00 59.30 C ANISOU 1195 CA GLY A 176 9866 6578 6088 489 7 246 C ATOM 1196 C GLY A 176 4.747 32.307 -7.622 1.00 62.78 C ANISOU 1196 C GLY A 176 10224 7052 6578 479 10 316 C ATOM 1197 O GLY A 176 3.986 32.887 -8.402 1.00 62.31 O ANISOU 1197 O GLY A 176 10127 7020 6530 449 16 369 O ATOM 1198 N LEU A 177 6.077 32.556 -7.592 1.00 59.03 N ANISOU 1198 N LEU A 177 9714 6582 6135 500 5 330 N ATOM 1199 CA LEU A 177 6.656 33.568 -8.481 1.00 58.90 C ANISOU 1199 CA LEU A 177 9602 6606 6171 488 0 418 C ATOM 1200 C LEU A 177 6.708 33.070 -9.973 1.00 61.30 C ANISOU 1200 C LEU A 177 9878 7023 6390 489 30 462 C ATOM 1201 O LEU A 177 6.622 33.919 -10.865 1.00 60.70 O ANISOU 1201 O LEU A 177 9717 7001 6347 465 29 551 O ATOM 1202 CB LEU A 177 8.044 34.072 -8.008 1.00 59.31 C ANISOU 1202 CB LEU A 177 9613 6635 6287 507 -23 438 C ATOM 1203 CG LEU A 177 9.267 33.177 -8.205 1.00 64.43 C ANISOU 1203 CG LEU A 177 10276 7333 6870 545 -3 426 C ATOM 1204 CD1 LEU A 177 10.521 34.006 -8.282 1.00 64.97 C ANISOU 1204 CD1 LEU A 177 10265 7413 7009 550 -27 502 C ATOM 1205 CD2 LEU A 177 9.404 32.198 -7.091 1.00 67.11 C ANISOU 1205 CD2 LEU A 177 10704 7621 7175 569 1 332 C ATOM 1206 N PRO A 178 6.717 31.727 -10.284 1.00 57.19 N ANISOU 1206 N PRO A 178 9423 6542 5764 516 53 401 N ATOM 1207 CA PRO A 178 6.656 31.315 -11.700 1.00 57.07 C ANISOU 1207 CA PRO A 178 9378 6642 5665 524 75 427 C ATOM 1208 C PRO A 178 5.327 31.716 -12.358 1.00 60.41 C ANISOU 1208 C PRO A 178 9782 7088 6083 479 80 466 C ATOM 1209 O PRO A 178 5.295 31.973 -13.559 1.00 60.38 O ANISOU 1209 O PRO A 178 9709 7190 6043 472 95 528 O ATOM 1210 CB PRO A 178 6.812 29.790 -11.636 1.00 58.68 C ANISOU 1210 CB PRO A 178 9669 6846 5779 565 80 329 C ATOM 1211 CG PRO A 178 6.387 29.418 -10.279 1.00 62.70 C ANISOU 1211 CG PRO A 178 10255 7241 6325 555 62 270 C ATOM 1212 CD PRO A 178 6.818 30.547 -9.398 1.00 58.38 C ANISOU 1212 CD PRO A 178 9667 6640 5875 542 50 307 C ATOM 1213 N ILE A 179 4.240 31.805 -11.554 1.00 56.38 N ANISOU 1213 N ILE A 179 9325 6490 5608 449 69 439 N ATOM 1214 CA ILE A 179 2.913 32.246 -12.008 1.00 56.11 C ANISOU 1214 CA ILE A 179 9276 6465 5578 404 73 480 C ATOM 1215 C ILE A 179 3.002 33.686 -12.513 1.00 61.53 C ANISOU 1215 C ILE A 179 9851 7178 6350 374 70 585 C ATOM 1216 O ILE A 179 2.548 33.984 -13.620 1.00 62.26 O ANISOU 1216 O ILE A 179 9884 7352 6419 347 85 654 O ATOM 1217 CB ILE A 179 1.861 32.124 -10.856 1.00 58.53 C ANISOU 1217 CB ILE A 179 9654 6677 5910 388 58 436 C ATOM 1218 CG1 ILE A 179 1.840 30.694 -10.254 1.00 59.15 C ANISOU 1218 CG1 ILE A 179 9828 6724 5922 414 51 350 C ATOM 1219 CG2 ILE A 179 0.459 32.574 -11.323 1.00 58.28 C ANISOU 1219 CG2 ILE A 179 9607 6657 5880 342 65 486 C ATOM 1220 CD1 ILE A 179 1.165 30.572 -8.879 1.00 67.88 C ANISOU 1220 CD1 ILE A 179 10984 7752 7054 410 31 315 C ATOM 1221 N MET A 180 3.618 34.569 -11.709 1.00 57.95 N ANISOU 1221 N MET A 180 9363 6656 6001 378 43 601 N ATOM 1222 CA MET A 180 3.730 35.986 -12.021 1.00 58.08 C ANISOU 1222 CA MET A 180 9269 6668 6129 349 20 701 C ATOM 1223 C MET A 180 5.044 36.313 -12.785 1.00 61.88 C ANISOU 1223 C MET A 180 9656 7233 6624 361 15 783 C ATOM 1224 O MET A 180 5.698 37.316 -12.483 1.00 62.40 O ANISOU 1224 O MET A 180 9649 7255 6805 353 -24 841 O ATOM 1225 CB MET A 180 3.614 36.838 -10.731 1.00 60.53 C ANISOU 1225 CB MET A 180 9587 6851 6558 350 -23 669 C ATOM 1226 CG MET A 180 4.567 36.404 -9.610 1.00 64.50 C ANISOU 1226 CG MET A 180 10146 7298 7064 392 -38 589 C ATOM 1227 SD MET A 180 4.200 37.144 -7.993 1.00 68.99 S ANISOU 1227 SD MET A 180 10742 7738 7734 406 -85 515 S ATOM 1228 CE MET A 180 2.694 36.239 -7.547 1.00 65.18 C ANISOU 1228 CE MET A 180 10355 7257 7152 406 -55 445 C ATOM 1229 N GLY A 181 5.376 35.509 -13.805 1.00 57.38 N ANISOU 1229 N GLY A 181 9076 6788 5938 380 49 793 N ATOM 1230 CA GLY A 181 6.504 35.821 -14.679 1.00 57.26 C ANISOU 1230 CA GLY A 181 8952 6888 5915 395 49 887 C ATOM 1231 C GLY A 181 7.514 34.748 -15.030 1.00 60.20 C ANISOU 1231 C GLY A 181 9349 7352 6170 455 73 842 C ATOM 1232 O GLY A 181 7.816 34.556 -16.212 1.00 60.13 O ANISOU 1232 O GLY A 181 9269 7498 6079 473 95 896 O ATOM 1233 N TRP A 182 8.134 34.118 -14.011 1.00 55.63 N ANISOU 1233 N TRP A 182 8857 6690 5588 491 68 750 N ATOM 1234 CA TRP A 182 9.259 33.200 -14.221 1.00 54.96 C ANISOU 1234 CA TRP A 182 8789 6679 5413 553 85 712 C ATOM 1235 C TRP A 182 8.781 31.785 -14.688 1.00 56.92 C ANISOU 1235 C TRP A 182 9123 6976 5527 589 112 604 C ATOM 1236 O TRP A 182 8.991 30.786 -13.992 1.00 55.54 O ANISOU 1236 O TRP A 182 9046 6736 5320 622 112 499 O ATOM 1237 CB TRP A 182 10.122 33.094 -12.950 1.00 53.42 C ANISOU 1237 CB TRP A 182 8647 6376 5274 572 66 665 C ATOM 1238 CG TRP A 182 11.554 32.701 -13.203 1.00 54.94 C ANISOU 1238 CG TRP A 182 8805 6650 5418 626 75 685 C ATOM 1239 CD1 TRP A 182 12.146 32.470 -14.413 1.00 58.54 C ANISOU 1239 CD1 TRP A 182 9187 7273 5784 665 96 739 C ATOM 1240 CD2 TRP A 182 12.573 32.506 -12.214 1.00 54.64 C ANISOU 1240 CD2 TRP A 182 8803 6543 5413 650 64 655 C ATOM 1241 NE1 TRP A 182 13.465 32.123 -14.236 1.00 58.34 N ANISOU 1241 NE1 TRP A 182 9150 7284 5732 715 100 745 N ATOM 1242 CE2 TRP A 182 13.754 32.133 -12.895 1.00 59.19 C ANISOU 1242 CE2 TRP A 182 9328 7244 5918 703 81 695 C ATOM 1243 CE3 TRP A 182 12.603 32.602 -10.812 1.00 55.27 C ANISOU 1243 CE3 TRP A 182 8949 6480 5571 635 42 598 C ATOM 1244 CZ2 TRP A 182 14.949 31.853 -12.222 1.00 58.45 C ANISOU 1244 CZ2 TRP A 182 9251 7124 5833 737 78 686 C ATOM 1245 CZ3 TRP A 182 13.782 32.308 -10.146 1.00 56.71 C ANISOU 1245 CZ3 TRP A 182 9147 6639 5759 666 38 585 C ATOM 1246 CH2 TRP A 182 14.938 31.943 -10.847 1.00 57.92 C ANISOU 1246 CH2 TRP A 182 9253 6906 5847 713 57 631 C ATOM 1247 N ASN A 183 8.237 31.714 -15.916 1.00 53.13 N ANISOU 1247 N ASN A 183 8595 6619 4974 586 129 635 N ATOM 1248 CA ASN A 183 7.806 30.464 -16.559 1.00 52.60 C ANISOU 1248 CA ASN A 183 8592 6612 4782 623 143 537 C ATOM 1249 C ASN A 183 8.527 30.302 -17.932 1.00 57.33 C ANISOU 1249 C ASN A 183 9094 7416 5273 677 163 576 C ATOM 1250 O ASN A 183 9.448 31.072 -18.223 1.00 57.67 O ANISOU 1250 O ASN A 183 9028 7544 5341 686 166 684 O ATOM 1251 CB ASN A 183 6.282 30.432 -16.713 1.00 50.38 C ANISOU 1251 CB ASN A 183 8352 6290 4499 570 142 520 C ATOM 1252 CG ASN A 183 5.705 31.644 -17.397 1.00 71.66 C ANISOU 1252 CG ASN A 183 10940 9048 7239 514 149 647 C ATOM 1253 OD1 ASN A 183 5.979 31.918 -18.573 1.00 71.20 O ANISOU 1253 OD1 ASN A 183 10777 9150 7124 525 164 720 O ATOM 1254 ND2 ASN A 183 4.880 32.393 -16.676 1.00 58.61 N ANISOU 1254 ND2 ASN A 183 9303 7279 5688 455 137 678 N ATOM 1255 N CYS A 184 8.117 29.314 -18.765 1.00 53.58 N ANISOU 1255 N CYS A 184 8652 7026 4679 717 169 492 N ATOM 1256 CA CYS A 184 8.801 29.063 -20.042 1.00 54.25 C ANISOU 1256 CA CYS A 184 8646 7324 4643 785 186 508 C ATOM 1257 C CYS A 184 7.796 28.893 -21.220 1.00 56.65 C ANISOU 1257 C CYS A 184 8918 7748 4857 775 193 500 C ATOM 1258 O CYS A 184 8.152 28.300 -22.244 1.00 56.22 O ANISOU 1258 O CYS A 184 8822 7864 4675 847 200 457 O ATOM 1259 CB CYS A 184 9.711 27.842 -19.916 1.00 55.22 C ANISOU 1259 CB CYS A 184 8834 7459 4689 879 180 382 C ATOM 1260 SG CYS A 184 8.825 26.265 -19.744 1.00 59.18 S ANISOU 1260 SG CYS A 184 9493 7853 5140 904 150 189 S ATOM 1261 N ILE A 185 6.581 29.478 -21.096 1.00 52.10 N ANISOU 1261 N ILE A 185 8352 7097 4346 689 191 548 N ATOM 1262 CA ILE A 185 5.481 29.340 -22.072 1.00 51.76 C ANISOU 1262 CA ILE A 185 8292 7142 4232 664 197 545 C ATOM 1263 C ILE A 185 5.974 29.522 -23.558 1.00 56.62 C ANISOU 1263 C ILE A 185 8761 8023 4728 712 219 609 C ATOM 1264 O ILE A 185 5.665 28.671 -24.404 1.00 56.81 O ANISOU 1264 O ILE A 185 8803 8154 4629 759 215 516 O ATOM 1265 CB ILE A 185 4.304 30.302 -21.742 1.00 53.82 C ANISOU 1265 CB ILE A 185 8544 7307 4598 561 199 638 C ATOM 1266 CG1 ILE A 185 3.773 30.055 -20.303 1.00 53.19 C ANISOU 1266 CG1 ILE A 185 8600 6995 4613 527 177 570 C ATOM 1267 CG2 ILE A 185 3.179 30.164 -22.777 1.00 54.34 C ANISOU 1267 CG2 ILE A 185 8589 7470 4588 531 207 645 C ATOM 1268 CD1 ILE A 185 2.835 31.172 -19.741 1.00 60.08 C ANISOU 1268 CD1 ILE A 185 9457 7765 5607 439 177 664 C ATOM 1269 N SER A 186 6.731 30.600 -23.860 1.00 52.96 N ANISOU 1269 N SER A 186 8152 7670 4302 702 234 765 N ATOM 1270 CA SER A 186 7.212 30.826 -25.235 1.00 53.67 C ANISOU 1270 CA SER A 186 8082 8034 4277 746 253 849 C ATOM 1271 C SER A 186 8.716 30.501 -25.377 1.00 58.50 C ANISOU 1271 C SER A 186 8640 8767 4818 845 257 842 C ATOM 1272 O SER A 186 9.300 30.723 -26.443 1.00 59.54 O ANISOU 1272 O SER A 186 8624 9147 4851 894 272 925 O ATOM 1273 CB SER A 186 6.931 32.256 -25.685 1.00 56.64 C ANISOU 1273 CB SER A 186 8299 8487 4734 664 262 1057 C ATOM 1274 OG SER A 186 5.561 32.424 -26.011 1.00 63.44 O ANISOU 1274 OG SER A 186 9177 9322 5605 593 268 1065 O ATOM 1275 N ALA A 187 9.319 29.921 -24.326 1.00 54.15 N ANISOU 1275 N ALA A 187 8207 8056 4311 878 243 743 N ATOM 1276 CA ALA A 187 10.715 29.501 -24.356 1.00 54.37 C ANISOU 1276 CA ALA A 187 8205 8178 4275 974 247 723 C ATOM 1277 C ALA A 187 10.812 28.008 -24.038 1.00 57.85 C ANISOU 1277 C ALA A 187 8797 8541 4643 1054 233 509 C ATOM 1278 O ALA A 187 11.187 27.629 -22.923 1.00 57.22 O ANISOU 1278 O ALA A 187 8822 8280 4637 1056 220 445 O ATOM 1279 CB ALA A 187 11.539 30.323 -23.370 1.00 54.58 C ANISOU 1279 CB ALA A 187 8209 8091 4438 937 238 831 C ATOM 1280 N LEU A 188 10.432 27.157 -25.016 1.00 54.33 N ANISOU 1280 N LEU A 188 8358 8226 4058 1119 230 398 N ATOM 1281 CA LEU A 188 10.420 25.696 -24.864 1.00 53.98 C ANISOU 1281 CA LEU A 188 8449 8111 3952 1198 201 188 C ATOM 1282 C LEU A 188 11.825 25.142 -24.601 1.00 58.02 C ANISOU 1282 C LEU A 188 8963 8657 4424 1301 202 136 C ATOM 1283 O LEU A 188 11.967 24.169 -23.860 1.00 56.43 O ANISOU 1283 O LEU A 188 8891 8297 4253 1333 175 -2 O ATOM 1284 CB LEU A 188 9.816 25.022 -26.108 1.00 54.98 C ANISOU 1284 CB LEU A 188 8556 8399 3933 1255 189 87 C ATOM 1285 CG LEU A 188 8.347 25.349 -26.417 1.00 59.05 C ANISOU 1285 CG LEU A 188 9086 8877 4474 1160 184 114 C ATOM 1286 CD1 LEU A 188 7.952 24.815 -27.770 1.00 60.26 C ANISOU 1286 CD1 LEU A 188 9189 9238 4468 1224 175 34 C ATOM 1287 CD2 LEU A 188 7.411 24.805 -25.336 1.00 60.28 C ANISOU 1287 CD2 LEU A 188 9413 8750 4742 1092 148 24 C ATOM 1288 N SER A 189 12.865 25.802 -25.165 1.00 56.33 N ANISOU 1288 N SER A 189 8599 8651 4154 1345 232 264 N ATOM 1289 CA SER A 189 14.275 25.426 -24.996 1.00 57.04 C ANISOU 1289 CA SER A 189 8666 8806 4198 1443 239 248 C ATOM 1290 C SER A 189 14.710 25.483 -23.515 1.00 61.20 C ANISOU 1290 C SER A 189 9293 9088 4873 1393 231 256 C ATOM 1291 O SER A 189 15.718 24.872 -23.143 1.00 61.31 O ANISOU 1291 O SER A 189 9338 9091 4865 1469 231 198 O ATOM 1292 CB SER A 189 15.167 26.341 -25.831 1.00 61.39 C ANISOU 1292 CB SER A 189 9020 9626 4681 1475 268 432 C ATOM 1293 OG SER A 189 14.804 26.308 -27.202 1.00 71.04 O ANISOU 1293 OG SER A 189 10133 11102 5756 1525 277 433 O ATOM 1294 N SER A 190 13.939 26.206 -22.676 1.00 57.27 N ANISOU 1294 N SER A 190 8840 8400 4519 1271 225 324 N ATOM 1295 CA SER A 190 14.216 26.350 -21.249 1.00 56.12 C ANISOU 1295 CA SER A 190 8782 8030 4512 1217 216 332 C ATOM 1296 C SER A 190 13.151 25.639 -20.382 1.00 59.53 C ANISOU 1296 C SER A 190 9374 8231 5013 1168 189 200 C ATOM 1297 O SER A 190 13.070 25.905 -19.183 1.00 58.91 O ANISOU 1297 O SER A 190 9360 7969 5053 1105 181 218 O ATOM 1298 CB SER A 190 14.290 27.828 -20.873 1.00 59.05 C ANISOU 1298 CB SER A 190 9063 8372 5000 1124 222 520 C ATOM 1299 OG SER A 190 15.447 28.454 -21.404 1.00 67.92 O ANISOU 1299 OG SER A 190 10043 9676 6088 1164 235 659 O ATOM 1300 N CYS A 191 12.356 24.724 -20.976 1.00 56.52 N ANISOU 1300 N CYS A 191 9052 7867 4557 1199 170 72 N ATOM 1301 CA CYS A 191 11.318 24.003 -20.228 1.00 55.99 C ANISOU 1301 CA CYS A 191 9125 7595 4555 1152 135 -37 C ATOM 1302 C CYS A 191 11.855 22.668 -19.696 1.00 59.97 C ANISOU 1302 C CYS A 191 9730 8002 5052 1224 103 -186 C ATOM 1303 O CYS A 191 12.394 21.868 -20.470 1.00 60.41 O ANISOU 1303 O CYS A 191 9774 8175 5005 1328 93 -282 O ATOM 1304 CB CYS A 191 10.071 23.792 -21.081 1.00 56.83 C ANISOU 1304 CB CYS A 191 9241 7747 4607 1130 119 -80 C ATOM 1305 SG CYS A 191 9.190 25.317 -21.512 1.00 60.59 S ANISOU 1305 SG CYS A 191 9614 8289 5121 1024 150 96 S ATOM 1306 N SER A 192 11.699 22.426 -18.369 1.00 55.50 N ANISOU 1306 N SER A 192 9258 7230 4600 1173 85 -205 N ATOM 1307 CA SER A 192 12.097 21.161 -17.742 1.00 55.19 C ANISOU 1307 CA SER A 192 9314 7076 4580 1224 49 -332 C ATOM 1308 C SER A 192 11.100 20.077 -18.131 1.00 58.56 C ANISOU 1308 C SER A 192 9819 7446 4985 1237 -8 -463 C ATOM 1309 O SER A 192 9.922 20.378 -18.307 1.00 57.63 O ANISOU 1309 O SER A 192 9714 7301 4882 1168 -19 -437 O ATOM 1310 CB SER A 192 12.187 21.307 -16.223 1.00 57.76 C ANISOU 1310 CB SER A 192 9696 7219 5029 1159 47 -294 C ATOM 1311 OG SER A 192 10.920 21.537 -15.631 1.00 65.45 O ANISOU 1311 OG SER A 192 10721 8070 6076 1066 28 -273 O ATOM 1312 N THR A 193 11.569 18.841 -18.341 1.00 55.34 N ANISOU 1312 N THR A 193 9456 7027 4542 1329 -51 -601 N ATOM 1313 CA THR A 193 10.697 17.776 -18.823 1.00 55.40 C ANISOU 1313 CA THR A 193 9531 6985 4533 1351 -121 -734 C ATOM 1314 C THR A 193 9.819 17.183 -17.679 1.00 57.42 C ANISOU 1314 C THR A 193 9889 7010 4916 1270 -177 -752 C ATOM 1315 O THR A 193 8.668 16.839 -17.939 1.00 56.62 O ANISOU 1315 O THR A 193 9830 6857 4826 1230 -225 -787 O ATOM 1316 CB THR A 193 11.508 16.687 -19.561 1.00 66.75 C ANISOU 1316 CB THR A 193 10971 8502 5890 1489 -158 -886 C ATOM 1317 OG1 THR A 193 10.618 15.723 -20.127 1.00 70.05 O ANISOU 1317 OG1 THR A 193 11448 8874 6294 1512 -237 -1019 O ATOM 1318 CG2 THR A 193 12.522 16.006 -18.680 1.00 64.65 C ANISOU 1318 CG2 THR A 193 10744 8133 5685 1534 -171 -929 C ATOM 1319 N VAL A 194 10.341 17.101 -16.427 1.00 52.88 N ANISOU 1319 N VAL A 194 9346 6313 4435 1243 -171 -717 N ATOM 1320 CA VAL A 194 9.569 16.532 -15.306 1.00 52.09 C ANISOU 1320 CA VAL A 194 9324 6018 4450 1171 -225 -719 C ATOM 1321 C VAL A 194 8.417 17.523 -14.887 1.00 55.58 C ANISOU 1321 C VAL A 194 9760 6428 4930 1057 -200 -602 C ATOM 1322 O VAL A 194 7.370 17.081 -14.396 1.00 54.41 O ANISOU 1322 O VAL A 194 9666 6164 4843 997 -252 -603 O ATOM 1323 CB VAL A 194 10.480 16.119 -14.105 1.00 55.29 C ANISOU 1323 CB VAL A 194 9752 6321 4936 1179 -226 -714 C ATOM 1324 CG1 VAL A 194 11.094 17.328 -13.405 1.00 54.18 C ANISOU 1324 CG1 VAL A 194 9560 6214 4811 1138 -148 -590 C ATOM 1325 CG2 VAL A 194 9.735 15.223 -13.117 1.00 54.78 C ANISOU 1325 CG2 VAL A 194 9757 6076 4982 1124 -300 -732 C ATOM 1326 N LEU A 195 8.612 18.840 -15.139 1.00 52.37 N ANISOU 1326 N LEU A 195 9282 6129 4488 1032 -128 -500 N ATOM 1327 CA LEU A 195 7.608 19.892 -14.924 1.00 51.46 C ANISOU 1327 CA LEU A 195 9147 6004 4401 940 -102 -395 C ATOM 1328 C LEU A 195 7.567 20.787 -16.187 1.00 56.44 C ANISOU 1328 C LEU A 195 9694 6805 4945 950 -58 -346 C ATOM 1329 O LEU A 195 8.334 21.745 -16.299 1.00 55.86 O ANISOU 1329 O LEU A 195 9543 6819 4860 957 -6 -265 O ATOM 1330 CB LEU A 195 7.906 20.703 -13.645 1.00 50.40 C ANISOU 1330 CB LEU A 195 9002 5800 4349 887 -68 -304 C ATOM 1331 CG LEU A 195 7.396 20.090 -12.326 1.00 54.47 C ANISOU 1331 CG LEU A 195 9586 6160 4951 842 -109 -314 C ATOM 1332 CD1 LEU A 195 8.386 19.091 -11.754 1.00 54.57 C ANISOU 1332 CD1 LEU A 195 9629 6114 4992 895 -134 -379 C ATOM 1333 CD2 LEU A 195 7.157 21.160 -11.298 1.00 56.71 C ANISOU 1333 CD2 LEU A 195 9847 6404 5294 777 -76 -218 C ATOM 1334 N PRO A 196 6.748 20.394 -17.200 1.00 54.39 N ANISOU 1334 N PRO A 196 9442 6601 4623 958 -85 -396 N ATOM 1335 CA PRO A 196 6.822 21.050 -18.521 1.00 55.39 C ANISOU 1335 CA PRO A 196 9478 6917 4651 983 -48 -361 C ATOM 1336 C PRO A 196 6.663 22.582 -18.542 1.00 60.40 C ANISOU 1336 C PRO A 196 10025 7615 5308 915 11 -207 C ATOM 1337 O PRO A 196 7.323 23.227 -19.355 1.00 60.34 O ANISOU 1337 O PRO A 196 9918 7770 5239 950 50 -150 O ATOM 1338 CB PRO A 196 5.683 20.394 -19.293 1.00 57.40 C ANISOU 1338 CB PRO A 196 9772 7177 4861 975 -96 -432 C ATOM 1339 CG PRO A 196 5.604 19.040 -18.723 1.00 61.57 C ANISOU 1339 CG PRO A 196 10400 7557 5435 1002 -171 -551 C ATOM 1340 CD PRO A 196 5.866 19.208 -17.251 1.00 56.06 C ANISOU 1340 CD PRO A 196 9738 6716 4847 955 -162 -495 C ATOM 1341 N LEU A 197 5.787 23.161 -17.711 1.00 57.29 N ANISOU 1341 N LEU A 197 9659 7105 5002 825 13 -136 N ATOM 1342 CA LEU A 197 5.560 24.610 -17.775 1.00 57.30 C ANISOU 1342 CA LEU A 197 9577 7155 5038 764 58 0 C ATOM 1343 C LEU A 197 6.547 25.407 -16.873 1.00 61.25 C ANISOU 1343 C LEU A 197 10041 7616 5614 759 83 70 C ATOM 1344 O LEU A 197 6.550 26.640 -16.912 1.00 60.39 O ANISOU 1344 O LEU A 197 9853 7542 5549 717 109 183 O ATOM 1345 CB LEU A 197 4.108 24.953 -17.415 1.00 56.77 C ANISOU 1345 CB LEU A 197 9546 6999 5023 677 47 43 C ATOM 1346 CG LEU A 197 3.081 24.809 -18.545 1.00 61.92 C ANISOU 1346 CG LEU A 197 10186 7734 5606 657 40 39 C ATOM 1347 CD1 LEU A 197 2.709 23.348 -18.776 1.00 62.96 C ANISOU 1347 CD1 LEU A 197 10407 7823 5690 694 -17 -92 C ATOM 1348 CD2 LEU A 197 1.827 25.595 -18.233 1.00 63.83 C ANISOU 1348 CD2 LEU A 197 10428 7919 5907 566 49 128 C ATOM 1349 N TYR A 198 7.420 24.710 -16.135 1.00 58.14 N ANISOU 1349 N TYR A 198 9697 7156 5237 804 70 6 N ATOM 1350 CA TYR A 198 8.406 25.372 -15.281 1.00 57.78 C ANISOU 1350 CA TYR A 198 9621 7075 5258 803 88 64 C ATOM 1351 C TYR A 198 9.701 25.663 -16.046 1.00 61.01 C ANISOU 1351 C TYR A 198 9938 7632 5610 866 114 104 C ATOM 1352 O TYR A 198 10.177 24.822 -16.816 1.00 60.00 O ANISOU 1352 O TYR A 198 9810 7598 5389 941 111 32 O ATOM 1353 CB TYR A 198 8.706 24.521 -14.035 1.00 59.07 C ANISOU 1353 CB TYR A 198 9874 7099 5471 814 64 -10 C ATOM 1354 CG TYR A 198 7.749 24.757 -12.884 1.00 60.82 C ANISOU 1354 CG TYR A 198 10147 7185 5776 743 48 7 C ATOM 1355 CD1 TYR A 198 8.163 25.417 -11.733 1.00 62.64 C ANISOU 1355 CD1 TYR A 198 10370 7345 6085 719 56 49 C ATOM 1356 CD2 TYR A 198 6.432 24.314 -12.944 1.00 61.70 C ANISOU 1356 CD2 TYR A 198 10311 7250 5883 706 22 -20 C ATOM 1357 CE1 TYR A 198 7.292 25.620 -10.661 1.00 63.32 C ANISOU 1357 CE1 TYR A 198 10495 7329 6234 667 40 57 C ATOM 1358 CE2 TYR A 198 5.551 24.518 -11.882 1.00 62.24 C ANISOU 1358 CE2 TYR A 198 10416 7215 6016 649 7 3 C ATOM 1359 CZ TYR A 198 5.987 25.168 -10.740 1.00 70.08 C ANISOU 1359 CZ TYR A 198 11397 8151 7077 634 18 38 C ATOM 1360 OH TYR A 198 5.126 25.361 -9.687 1.00 70.66 O ANISOU 1360 OH TYR A 198 11500 8146 7203 590 3 54 O ATOM 1361 N HIS A 199 10.271 26.858 -15.821 1.00 58.02 N ANISOU 1361 N HIS A 199 9479 7277 5290 838 133 221 N ATOM 1362 CA HIS A 199 11.535 27.273 -16.428 1.00 58.73 C ANISOU 1362 CA HIS A 199 9467 7507 5341 889 153 293 C ATOM 1363 C HIS A 199 12.686 26.537 -15.747 1.00 61.27 C ANISOU 1363 C HIS A 199 9835 7786 5659 947 151 233 C ATOM 1364 O HIS A 199 12.741 26.501 -14.512 1.00 60.35 O ANISOU 1364 O HIS A 199 9782 7521 5626 916 139 213 O ATOM 1365 CB HIS A 199 11.707 28.797 -16.307 1.00 59.80 C ANISOU 1365 CB HIS A 199 9501 7653 5566 829 157 446 C ATOM 1366 CG HIS A 199 12.678 29.386 -17.282 1.00 64.40 C ANISOU 1366 CG HIS A 199 9946 8420 6103 865 171 559 C ATOM 1367 ND1 HIS A 199 14.041 29.342 -17.057 1.00 66.63 N ANISOU 1367 ND1 HIS A 199 10195 8742 6379 915 175 591 N ATOM 1368 CD2 HIS A 199 12.445 30.075 -18.425 1.00 67.09 C ANISOU 1368 CD2 HIS A 199 10167 8916 6408 853 181 664 C ATOM 1369 CE1 HIS A 199 14.593 29.988 -18.073 1.00 66.99 C ANISOU 1369 CE1 HIS A 199 10100 8971 6383 934 184 716 C ATOM 1370 NE2 HIS A 199 13.672 30.448 -18.920 1.00 67.58 N ANISOU 1370 NE2 HIS A 199 10115 9125 6440 897 187 765 N ATOM 1371 N LYS A 200 13.577 25.905 -16.544 1.00 56.95 N ANISOU 1371 N LYS A 200 9253 7375 5009 1036 162 200 N ATOM 1372 CA LYS A 200 14.707 25.109 -16.039 1.00 55.87 C ANISOU 1372 CA LYS A 200 9155 7214 4857 1103 162 140 C ATOM 1373 C LYS A 200 15.520 25.856 -14.958 1.00 57.54 C ANISOU 1373 C LYS A 200 9349 7345 5168 1066 167 227 C ATOM 1374 O LYS A 200 15.888 25.250 -13.952 1.00 56.17 O ANISOU 1374 O LYS A 200 9252 7054 5036 1072 159 167 O ATOM 1375 CB LYS A 200 15.635 24.694 -17.187 1.00 58.62 C ANISOU 1375 CB LYS A 200 9431 7764 5079 1208 178 129 C ATOM 1376 CG LYS A 200 15.143 23.491 -17.968 1.00 67.40 C ANISOU 1376 CG LYS A 200 10594 8923 6092 1277 160 -20 C ATOM 1377 CD LYS A 200 16.172 23.064 -19.005 1.00 78.83 C ANISOU 1377 CD LYS A 200 11967 10578 7407 1397 174 -44 C ATOM 1378 CE LYS A 200 15.746 21.840 -19.773 1.00 88.52 C ANISOU 1378 CE LYS A 200 13246 11850 8539 1479 145 -213 C ATOM 1379 NZ LYS A 200 16.727 21.497 -20.834 1.00 98.92 N ANISOU 1379 NZ LYS A 200 14477 13395 9713 1609 159 -241 N ATOM 1380 N HIS A 201 15.774 27.171 -15.163 1.00 53.67 N ANISOU 1380 N HIS A 201 8755 6914 4722 1024 173 372 N ATOM 1381 CA HIS A 201 16.544 28.004 -14.232 1.00 52.83 C ANISOU 1381 CA HIS A 201 8620 6736 4717 988 166 463 C ATOM 1382 C HIS A 201 15.857 28.119 -12.866 1.00 53.79 C ANISOU 1382 C HIS A 201 8833 6658 4946 920 146 414 C ATOM 1383 O HIS A 201 16.540 28.084 -11.839 1.00 52.72 O ANISOU 1383 O HIS A 201 8729 6436 4866 917 139 409 O ATOM 1384 CB HIS A 201 16.778 29.398 -14.820 1.00 54.34 C ANISOU 1384 CB HIS A 201 8675 7023 4951 951 159 630 C ATOM 1385 CG HIS A 201 17.793 29.413 -15.918 1.00 59.22 C ANISOU 1385 CG HIS A 201 9180 7850 5472 1020 176 712 C ATOM 1386 ND1 HIS A 201 17.427 29.254 -17.242 1.00 61.94 N ANISOU 1386 ND1 HIS A 201 9457 8369 5707 1057 192 721 N ATOM 1387 CD2 HIS A 201 19.139 29.531 -15.848 1.00 61.80 C ANISOU 1387 CD2 HIS A 201 9446 8245 5788 1061 179 788 C ATOM 1388 CE1 HIS A 201 18.552 29.304 -17.935 1.00 62.40 C ANISOU 1388 CE1 HIS A 201 9411 8608 5689 1123 205 804 C ATOM 1389 NE2 HIS A 201 19.611 29.458 -17.139 1.00 62.64 N ANISOU 1389 NE2 HIS A 201 9444 8579 5776 1128 197 850 N ATOM 1390 N TYR A 202 14.511 28.236 -12.850 1.00 48.75 N ANISOU 1390 N TYR A 202 8233 5959 4331 870 136 381 N ATOM 1391 CA TYR A 202 13.744 28.347 -11.607 1.00 46.93 C ANISOU 1391 CA TYR A 202 8078 5566 4187 814 117 338 C ATOM 1392 C TYR A 202 13.887 27.079 -10.752 1.00 50.00 C ANISOU 1392 C TYR A 202 8570 5868 4560 842 114 226 C ATOM 1393 O TYR A 202 14.038 27.181 -9.534 1.00 49.56 O ANISOU 1393 O TYR A 202 8549 5708 4572 817 103 214 O ATOM 1394 CB TYR A 202 12.264 28.631 -11.898 1.00 47.10 C ANISOU 1394 CB TYR A 202 8113 5563 4218 764 111 332 C ATOM 1395 CG TYR A 202 11.392 28.623 -10.661 1.00 46.68 C ANISOU 1395 CG TYR A 202 8136 5366 4234 718 92 282 C ATOM 1396 CD1 TYR A 202 11.489 29.631 -9.712 1.00 48.23 C ANISOU 1396 CD1 TYR A 202 8311 5484 4530 682 75 325 C ATOM 1397 CD2 TYR A 202 10.465 27.611 -10.445 1.00 46.83 C ANISOU 1397 CD2 TYR A 202 8242 5334 4219 716 85 196 C ATOM 1398 CE1 TYR A 202 10.698 29.625 -8.567 1.00 48.57 C ANISOU 1398 CE1 TYR A 202 8413 5419 4622 651 58 276 C ATOM 1399 CE2 TYR A 202 9.658 27.600 -9.310 1.00 47.25 C ANISOU 1399 CE2 TYR A 202 8349 5278 4325 677 67 166 C ATOM 1400 CZ TYR A 202 9.764 28.621 -8.381 1.00 54.41 C ANISOU 1400 CZ TYR A 202 9231 6128 5317 649 58 204 C ATOM 1401 OH TYR A 202 8.970 28.622 -7.260 1.00 53.75 O ANISOU 1401 OH TYR A 202 9191 5960 5272 622 41 171 O ATOM 1402 N ILE A 203 13.847 25.893 -11.388 1.00 46.30 N ANISOU 1402 N ILE A 203 8141 5444 4005 895 118 144 N ATOM 1403 CA ILE A 203 14.007 24.624 -10.679 1.00 45.77 C ANISOU 1403 CA ILE A 203 8161 5295 3935 923 104 44 C ATOM 1404 C ILE A 203 15.420 24.575 -10.055 1.00 50.87 C ANISOU 1404 C ILE A 203 8792 5937 4600 955 116 66 C ATOM 1405 O ILE A 203 15.537 24.310 -8.857 1.00 49.94 O ANISOU 1405 O ILE A 203 8719 5714 4540 932 107 43 O ATOM 1406 CB ILE A 203 13.701 23.414 -11.614 1.00 48.80 C ANISOU 1406 CB ILE A 203 8582 5727 4234 979 92 -52 C ATOM 1407 CG1 ILE A 203 12.211 23.019 -11.480 1.00 48.95 C ANISOU 1407 CG1 ILE A 203 8663 5664 4270 931 62 -100 C ATOM 1408 CG2 ILE A 203 14.619 22.215 -11.326 1.00 48.98 C ANISOU 1408 CG2 ILE A 203 8647 5725 4238 1046 83 -131 C ATOM 1409 CD1 ILE A 203 11.703 22.027 -12.489 1.00 59.10 C ANISOU 1409 CD1 ILE A 203 9980 6993 5485 974 37 -188 C ATOM 1410 N LEU A 204 16.465 24.960 -10.840 1.00 48.66 N ANISOU 1410 N LEU A 204 8434 5780 4273 1001 138 128 N ATOM 1411 CA LEU A 204 17.859 25.043 -10.371 1.00 48.62 C ANISOU 1411 CA LEU A 204 8402 5789 4283 1031 150 172 C ATOM 1412 C LEU A 204 17.971 26.003 -9.177 1.00 52.03 C ANISOU 1412 C LEU A 204 8827 6122 4821 963 139 235 C ATOM 1413 O LEU A 204 18.685 25.705 -8.219 1.00 50.89 O ANISOU 1413 O LEU A 204 8710 5914 4710 966 139 224 O ATOM 1414 CB LEU A 204 18.778 25.511 -11.524 1.00 49.41 C ANISOU 1414 CB LEU A 204 8398 6061 4312 1083 170 258 C ATOM 1415 CG LEU A 204 20.254 25.782 -11.178 1.00 53.98 C ANISOU 1415 CG LEU A 204 8929 6677 4903 1110 181 336 C ATOM 1416 CD1 LEU A 204 21.017 24.484 -10.961 1.00 54.01 C ANISOU 1416 CD1 LEU A 204 8989 6677 4857 1183 193 247 C ATOM 1417 CD2 LEU A 204 20.922 26.591 -12.272 1.00 57.21 C ANISOU 1417 CD2 LEU A 204 9212 7261 5264 1139 192 463 C ATOM 1418 N PHE A 205 17.229 27.138 -9.232 1.00 48.79 N ANISOU 1418 N PHE A 205 8377 5696 4465 904 125 296 N ATOM 1419 CA PHE A 205 17.189 28.153 -8.181 1.00 48.33 C ANISOU 1419 CA PHE A 205 8307 5544 4512 846 103 342 C ATOM 1420 C PHE A 205 16.575 27.588 -6.911 1.00 53.22 C ANISOU 1420 C PHE A 205 9014 6041 5167 821 92 254 C ATOM 1421 O PHE A 205 17.122 27.795 -5.833 1.00 52.50 O ANISOU 1421 O PHE A 205 8931 5887 5130 807 82 258 O ATOM 1422 CB PHE A 205 16.401 29.385 -8.661 1.00 50.16 C ANISOU 1422 CB PHE A 205 8477 5788 4794 797 85 413 C ATOM 1423 CG PHE A 205 16.190 30.475 -7.630 1.00 51.45 C ANISOU 1423 CG PHE A 205 8628 5846 5073 744 50 441 C ATOM 1424 CD1 PHE A 205 17.235 31.315 -7.255 1.00 54.32 C ANISOU 1424 CD1 PHE A 205 8933 6199 5509 736 25 520 C ATOM 1425 CD2 PHE A 205 14.927 30.718 -7.098 1.00 53.15 C ANISOU 1425 CD2 PHE A 205 8884 5983 5328 705 35 392 C ATOM 1426 CE1 PHE A 205 17.030 32.340 -6.327 1.00 54.82 C ANISOU 1426 CE1 PHE A 205 8983 6162 5685 693 -19 531 C ATOM 1427 CE2 PHE A 205 14.723 31.752 -6.178 1.00 55.24 C ANISOU 1427 CE2 PHE A 205 9133 6161 5697 668 -2 404 C ATOM 1428 CZ PHE A 205 15.774 32.555 -5.800 1.00 53.39 C ANISOU 1428 CZ PHE A 205 8843 5906 5536 664 -32 466 C ATOM 1429 N CYS A 206 15.453 26.854 -7.034 1.00 51.44 N ANISOU 1429 N CYS A 206 8846 5789 4908 815 91 182 N ATOM 1430 CA CYS A 206 14.785 26.240 -5.880 1.00 51.62 C ANISOU 1430 CA CYS A 206 8939 5715 4959 791 76 114 C ATOM 1431 C CYS A 206 15.657 25.137 -5.292 1.00 56.17 C ANISOU 1431 C CYS A 206 9553 6268 5521 826 82 70 C ATOM 1432 O CYS A 206 15.892 25.120 -4.084 1.00 55.45 O ANISOU 1432 O CYS A 206 9478 6117 5476 807 74 63 O ATOM 1433 CB CYS A 206 13.407 25.710 -6.267 1.00 52.05 C ANISOU 1433 CB CYS A 206 9036 5756 4983 776 66 67 C ATOM 1434 SG CYS A 206 12.220 26.997 -6.733 1.00 55.92 S ANISOU 1434 SG CYS A 206 9486 6259 5502 726 60 119 S ATOM 1435 N THR A 207 16.181 24.248 -6.154 1.00 53.87 N ANISOU 1435 N THR A 207 9270 6032 5166 881 93 40 N ATOM 1436 CA THR A 207 17.032 23.135 -5.744 1.00 54.19 C ANISOU 1436 CA THR A 207 9343 6052 5196 922 96 -3 C ATOM 1437 C THR A 207 18.271 23.640 -4.988 1.00 59.05 C ANISOU 1437 C THR A 207 9925 6664 5847 921 111 53 C ATOM 1438 O THR A 207 18.603 23.078 -3.948 1.00 58.77 O ANISOU 1438 O THR A 207 9918 6568 5843 914 107 30 O ATOM 1439 CB THR A 207 17.439 22.295 -6.964 1.00 63.41 C ANISOU 1439 CB THR A 207 10511 7296 6285 994 103 -47 C ATOM 1440 OG1 THR A 207 16.301 22.103 -7.802 1.00 63.26 O ANISOU 1440 OG1 THR A 207 10509 7296 6231 990 87 -87 O ATOM 1441 CG2 THR A 207 18.028 20.942 -6.575 1.00 62.78 C ANISOU 1441 CG2 THR A 207 10475 7173 6204 1038 93 -115 C ATOM 1442 N THR A 208 18.934 24.717 -5.489 1.00 56.12 N ANISOU 1442 N THR A 208 9487 6360 5476 924 123 135 N ATOM 1443 CA THR A 208 20.153 25.224 -4.853 1.00 55.99 C ANISOU 1443 CA THR A 208 9435 6342 5496 922 129 198 C ATOM 1444 C THR A 208 19.821 25.958 -3.538 1.00 59.66 C ANISOU 1444 C THR A 208 9907 6718 6044 862 106 206 C ATOM 1445 O THR A 208 20.528 25.756 -2.555 1.00 59.72 O ANISOU 1445 O THR A 208 9924 6687 6080 857 107 205 O ATOM 1446 CB THR A 208 20.997 26.099 -5.817 1.00 64.41 C ANISOU 1446 CB THR A 208 10417 7513 6542 944 137 299 C ATOM 1447 OG1 THR A 208 22.314 26.232 -5.282 1.00 63.33 O ANISOU 1447 OG1 THR A 208 10255 7382 6427 956 143 355 O ATOM 1448 CG2 THR A 208 20.386 27.488 -6.082 1.00 62.97 C ANISOU 1448 CG2 THR A 208 10179 7332 6414 894 113 368 C ATOM 1449 N VAL A 209 18.721 26.750 -3.500 1.00 55.47 N ANISOU 1449 N VAL A 209 9370 6158 5548 820 85 205 N ATOM 1450 CA VAL A 209 18.313 27.478 -2.285 1.00 54.42 C ANISOU 1450 CA VAL A 209 9239 5951 5487 776 59 196 C ATOM 1451 C VAL A 209 17.962 26.478 -1.163 1.00 58.27 C ANISOU 1451 C VAL A 209 9784 6389 5969 770 60 126 C ATOM 1452 O VAL A 209 18.380 26.676 -0.017 1.00 57.44 O ANISOU 1452 O VAL A 209 9673 6249 5901 756 50 122 O ATOM 1453 CB VAL A 209 17.136 28.463 -2.568 1.00 57.47 C ANISOU 1453 CB VAL A 209 9606 6322 5907 742 36 204 C ATOM 1454 CG1 VAL A 209 16.331 28.767 -1.302 1.00 56.45 C ANISOU 1454 CG1 VAL A 209 9500 6126 5823 713 12 154 C ATOM 1455 CG2 VAL A 209 17.647 29.751 -3.206 1.00 57.63 C ANISOU 1455 CG2 VAL A 209 9550 6371 5978 732 17 293 C ATOM 1456 N PHE A 210 17.242 25.385 -1.507 1.00 55.18 N ANISOU 1456 N PHE A 210 9437 5996 5532 782 66 76 N ATOM 1457 CA PHE A 210 16.803 24.406 -0.518 1.00 54.95 C ANISOU 1457 CA PHE A 210 9448 5925 5507 771 57 29 C ATOM 1458 C PHE A 210 17.951 23.471 -0.078 1.00 58.75 C ANISOU 1458 C PHE A 210 9937 6400 5984 796 70 25 C ATOM 1459 O PHE A 210 18.000 23.117 1.099 1.00 57.64 O ANISOU 1459 O PHE A 210 9800 6230 5869 778 63 16 O ATOM 1460 CB PHE A 210 15.607 23.600 -1.028 1.00 56.83 C ANISOU 1460 CB PHE A 210 9724 6153 5716 768 44 -11 C ATOM 1461 CG PHE A 210 14.364 24.430 -1.276 1.00 58.05 C ANISOU 1461 CG PHE A 210 9873 6309 5875 738 32 -5 C ATOM 1462 CD1 PHE A 210 13.952 25.392 -0.356 1.00 60.66 C ANISOU 1462 CD1 PHE A 210 10180 6622 6244 710 20 5 C ATOM 1463 CD2 PHE A 210 13.553 24.186 -2.378 1.00 60.24 C ANISOU 1463 CD2 PHE A 210 10167 6605 6117 741 29 -17 C ATOM 1464 CE1 PHE A 210 12.798 26.150 -0.580 1.00 61.42 C ANISOU 1464 CE1 PHE A 210 10269 6719 6348 687 8 9 C ATOM 1465 CE2 PHE A 210 12.397 24.942 -2.599 1.00 62.95 C ANISOU 1465 CE2 PHE A 210 10502 6950 6465 711 21 -4 C ATOM 1466 CZ PHE A 210 12.022 25.914 -1.694 1.00 60.62 C ANISOU 1466 CZ PHE A 210 10183 6636 6213 685 11 10 C ATOM 1467 N THR A 211 18.905 23.125 -0.987 1.00 55.80 N ANISOU 1467 N THR A 211 9557 6065 5577 841 91 38 N ATOM 1468 CA THR A 211 20.080 22.330 -0.573 1.00 55.70 C ANISOU 1468 CA THR A 211 9548 6050 5565 868 105 41 C ATOM 1469 C THR A 211 21.008 23.193 0.283 1.00 60.87 C ANISOU 1469 C THR A 211 10166 6705 6256 848 113 95 C ATOM 1470 O THR A 211 21.607 22.682 1.223 1.00 61.28 O ANISOU 1470 O THR A 211 10222 6735 6328 842 118 97 O ATOM 1471 CB THR A 211 20.837 21.721 -1.760 1.00 58.67 C ANISOU 1471 CB THR A 211 9924 6480 5888 933 124 34 C ATOM 1472 OG1 THR A 211 21.049 22.716 -2.753 1.00 61.15 O ANISOU 1472 OG1 THR A 211 10196 6866 6173 946 135 83 O ATOM 1473 CG2 THR A 211 20.133 20.528 -2.351 1.00 54.16 C ANISOU 1473 CG2 THR A 211 9396 5890 5291 961 105 -41 C ATOM 1474 N LEU A 212 21.097 24.512 -0.017 1.00 57.32 N ANISOU 1474 N LEU A 212 9678 6277 5824 833 106 143 N ATOM 1475 CA LEU A 212 21.901 25.437 0.782 1.00 57.33 C ANISOU 1475 CA LEU A 212 9643 6267 5874 810 97 192 C ATOM 1476 C LEU A 212 21.295 25.608 2.173 1.00 62.15 C ANISOU 1476 C LEU A 212 10263 6828 6523 772 75 152 C ATOM 1477 O LEU A 212 22.036 25.664 3.155 1.00 61.94 O ANISOU 1477 O LEU A 212 10223 6790 6520 761 73 164 O ATOM 1478 CB LEU A 212 22.040 26.805 0.088 1.00 57.60 C ANISOU 1478 CB LEU A 212 9626 6324 5935 801 78 256 C ATOM 1479 CG LEU A 212 23.174 26.930 -0.938 1.00 62.76 C ANISOU 1479 CG LEU A 212 10236 7049 6560 837 95 336 C ATOM 1480 CD1 LEU A 212 22.908 28.061 -1.902 1.00 63.55 C ANISOU 1480 CD1 LEU A 212 10279 7186 6679 827 74 401 C ATOM 1481 CD2 LEU A 212 24.525 27.127 -0.255 1.00 64.84 C ANISOU 1481 CD2 LEU A 212 10475 7310 6852 835 94 394 C ATOM 1482 N LEU A 213 19.944 25.664 2.264 1.00 59.49 N ANISOU 1482 N LEU A 213 9944 6475 6185 755 59 106 N ATOM 1483 CA LEU A 213 19.252 25.788 3.549 1.00 59.48 C ANISOU 1483 CA LEU A 213 9944 6453 6205 728 38 68 C ATOM 1484 C LEU A 213 19.341 24.477 4.335 1.00 64.27 C ANISOU 1484 C LEU A 213 10568 7059 6793 728 50 50 C ATOM 1485 O LEU A 213 19.605 24.514 5.532 1.00 64.31 O ANISOU 1485 O LEU A 213 10552 7069 6813 714 43 46 O ATOM 1486 CB LEU A 213 17.781 26.208 3.363 1.00 59.52 C ANISOU 1486 CB LEU A 213 9956 6451 6207 715 19 37 C ATOM 1487 CG LEU A 213 17.510 27.725 3.304 1.00 64.52 C ANISOU 1487 CG LEU A 213 10557 7072 6886 704 -10 43 C ATOM 1488 CD1 LEU A 213 16.127 28.014 2.739 1.00 64.63 C ANISOU 1488 CD1 LEU A 213 10580 7085 6891 696 -19 25 C ATOM 1489 CD2 LEU A 213 17.657 28.371 4.679 1.00 66.66 C ANISOU 1489 CD2 LEU A 213 10802 7331 7193 697 -39 14 C ATOM 1490 N LEU A 214 19.188 23.315 3.649 1.00 60.81 N ANISOU 1490 N LEU A 214 10160 6617 6327 745 62 41 N ATOM 1491 CA LEU A 214 19.315 22.002 4.297 1.00 60.75 C ANISOU 1491 CA LEU A 214 10163 6599 6323 744 62 34 C ATOM 1492 C LEU A 214 20.760 21.750 4.747 1.00 64.64 C ANISOU 1492 C LEU A 214 10638 7096 6826 754 84 65 C ATOM 1493 O LEU A 214 20.977 21.074 5.754 1.00 64.07 O ANISOU 1493 O LEU A 214 10551 7021 6770 739 82 73 O ATOM 1494 CB LEU A 214 18.843 20.874 3.366 1.00 61.19 C ANISOU 1494 CB LEU A 214 10255 6634 6361 764 55 9 C ATOM 1495 CG LEU A 214 17.325 20.693 3.255 1.00 66.20 C ANISOU 1495 CG LEU A 214 10906 7256 6991 743 25 -14 C ATOM 1496 CD1 LEU A 214 16.956 19.970 1.983 1.00 66.69 C ANISOU 1496 CD1 LEU A 214 11006 7302 7033 770 14 -44 C ATOM 1497 CD2 LEU A 214 16.759 19.969 4.474 1.00 69.06 C ANISOU 1497 CD2 LEU A 214 11250 7612 7377 713 -1 -2 C ATOM 1498 N LEU A 215 21.747 22.319 4.017 1.00 61.26 N ANISOU 1498 N LEU A 215 10203 6683 6390 778 103 94 N ATOM 1499 CA LEU A 215 23.159 22.213 4.381 1.00 61.09 C ANISOU 1499 CA LEU A 215 10163 6673 6377 789 125 136 C ATOM 1500 C LEU A 215 23.434 23.037 5.638 1.00 65.36 C ANISOU 1500 C LEU A 215 10670 7214 6948 753 113 152 C ATOM 1501 O LEU A 215 24.233 22.628 6.479 1.00 64.83 O ANISOU 1501 O LEU A 215 10588 7153 6893 744 124 175 O ATOM 1502 CB LEU A 215 24.056 22.678 3.217 1.00 61.27 C ANISOU 1502 CB LEU A 215 10176 6728 6377 825 143 177 C ATOM 1503 CG LEU A 215 25.569 22.448 3.377 1.00 66.10 C ANISOU 1503 CG LEU A 215 10768 7360 6987 845 168 232 C ATOM 1504 CD1 LEU A 215 25.862 21.322 4.366 1.00 68.52 C ANISOU 1504 CD1 LEU A 215 11083 7642 7309 836 178 218 C ATOM 1505 CD2 LEU A 215 26.218 22.164 2.036 1.00 66.68 C ANISOU 1505 CD2 LEU A 215 10839 7483 7013 904 190 254 C ATOM 1506 N SER A 216 22.727 24.171 5.790 1.00 62.54 N ANISOU 1506 N SER A 216 10302 6855 6607 735 86 135 N ATOM 1507 CA SER A 216 22.859 25.036 6.960 1.00 62.86 C ANISOU 1507 CA SER A 216 10311 6897 6678 710 62 129 C ATOM 1508 C SER A 216 22.383 24.322 8.224 1.00 68.44 C ANISOU 1508 C SER A 216 11006 7625 7374 693 60 100 C ATOM 1509 O SER A 216 22.979 24.506 9.286 1.00 68.85 O ANISOU 1509 O SER A 216 11028 7696 7437 680 55 106 O ATOM 1510 CB SER A 216 22.074 26.329 6.764 1.00 65.92 C ANISOU 1510 CB SER A 216 10688 7270 7090 704 25 104 C ATOM 1511 OG SER A 216 22.549 27.049 5.639 1.00 74.67 O ANISOU 1511 OG SER A 216 11788 8368 8216 713 21 149 O ATOM 1512 N ILE A 217 21.337 23.474 8.102 1.00 65.18 N ANISOU 1512 N ILE A 217 10610 7214 6940 692 59 78 N ATOM 1513 CA ILE A 217 20.779 22.720 9.233 1.00 65.19 C ANISOU 1513 CA ILE A 217 10587 7249 6933 674 51 71 C ATOM 1514 C ILE A 217 21.789 21.669 9.724 1.00 69.15 C ANISOU 1514 C ILE A 217 11073 7756 7445 668 73 113 C ATOM 1515 O ILE A 217 22.054 21.591 10.923 1.00 68.89 O ANISOU 1515 O ILE A 217 10996 7766 7414 650 71 126 O ATOM 1516 CB ILE A 217 19.418 22.041 8.864 1.00 68.48 C ANISOU 1516 CB ILE A 217 11021 7662 7336 671 36 56 C ATOM 1517 CG1 ILE A 217 18.549 22.899 7.905 1.00 69.12 C ANISOU 1517 CG1 ILE A 217 11131 7725 7408 680 25 26 C ATOM 1518 CG2 ILE A 217 18.647 21.632 10.105 1.00 69.29 C ANISOU 1518 CG2 ILE A 217 11078 7822 7427 651 16 62 C ATOM 1519 CD1 ILE A 217 18.004 24.201 8.472 1.00 76.92 C ANISOU 1519 CD1 ILE A 217 12094 8738 8396 678 3 -6 C ATOM 1520 N VAL A 218 22.347 20.867 8.791 1.00 66.00 N ANISOU 1520 N VAL A 218 10706 7319 7053 687 92 131 N ATOM 1521 CA VAL A 218 23.280 19.777 9.099 1.00 66.39 C ANISOU 1521 CA VAL A 218 10744 7362 7120 688 110 168 C ATOM 1522 C VAL A 218 24.527 20.319 9.839 1.00 72.15 C ANISOU 1522 C VAL A 218 11443 8117 7854 678 131 203 C ATOM 1523 O VAL A 218 24.906 19.761 10.875 1.00 72.03 O ANISOU 1523 O VAL A 218 11389 8128 7852 656 136 233 O ATOM 1524 CB VAL A 218 23.674 18.985 7.820 1.00 70.12 C ANISOU 1524 CB VAL A 218 11258 7792 7592 728 122 163 C ATOM 1525 CG1 VAL A 218 24.660 17.863 8.145 1.00 69.88 C ANISOU 1525 CG1 VAL A 218 11215 7748 7589 735 138 196 C ATOM 1526 CG2 VAL A 218 22.438 18.424 7.124 1.00 70.01 C ANISOU 1526 CG2 VAL A 218 11275 7749 7577 735 94 123 C ATOM 1527 N ILE A 219 25.131 21.418 9.334 1.00 69.80 N ANISOU 1527 N ILE A 219 11154 7814 7551 691 136 208 N ATOM 1528 CA ILE A 219 26.323 22.019 9.958 1.00 70.27 C ANISOU 1528 CA ILE A 219 11187 7891 7622 680 145 248 C ATOM 1529 C ILE A 219 25.952 22.594 11.352 1.00 75.60 C ANISOU 1529 C ILE A 219 11820 8605 8301 649 120 224 C ATOM 1530 O ILE A 219 26.747 22.482 12.294 1.00 75.31 O ANISOU 1530 O ILE A 219 11749 8597 8269 630 129 253 O ATOM 1531 CB ILE A 219 26.970 23.103 9.033 1.00 73.38 C ANISOU 1531 CB ILE A 219 11591 8270 8021 697 141 273 C ATOM 1532 CG1 ILE A 219 27.253 22.533 7.617 1.00 73.67 C ANISOU 1532 CG1 ILE A 219 11657 8298 8035 739 166 292 C ATOM 1533 CG2 ILE A 219 28.262 23.673 9.665 1.00 74.19 C ANISOU 1533 CG2 ILE A 219 11663 8384 8143 682 142 326 C ATOM 1534 CD1 ILE A 219 27.522 23.597 6.526 1.00 79.93 C ANISOU 1534 CD1 ILE A 219 12447 9097 8825 758 156 323 C ATOM 1535 N LEU A 220 24.728 23.150 11.486 1.00 72.95 N ANISOU 1535 N LEU A 220 11483 8278 7955 648 90 169 N ATOM 1536 CA LEU A 220 24.245 23.708 12.749 1.00 73.32 C ANISOU 1536 CA LEU A 220 11487 8380 7993 634 62 130 C ATOM 1537 C LEU A 220 24.033 22.604 13.804 1.00 78.44 C ANISOU 1537 C LEU A 220 12089 9091 8622 615 73 152 C ATOM 1538 O LEU A 220 24.390 22.807 14.965 1.00 78.74 O ANISOU 1538 O LEU A 220 12077 9191 8650 603 68 152 O ATOM 1539 CB LEU A 220 22.938 24.498 12.531 1.00 73.39 C ANISOU 1539 CB LEU A 220 11503 8388 7992 647 29 68 C ATOM 1540 CG LEU A 220 22.367 25.248 13.749 1.00 78.19 C ANISOU 1540 CG LEU A 220 12064 9060 8584 651 -7 10 C ATOM 1541 CD1 LEU A 220 23.318 26.333 14.233 1.00 78.65 C ANISOU 1541 CD1 LEU A 220 12105 9107 8671 652 -33 -9 C ATOM 1542 CD2 LEU A 220 21.018 25.853 13.428 1.00 80.53 C ANISOU 1542 CD2 LEU A 220 12372 9356 8870 669 -34 -46 C ATOM 1543 N TYR A 221 23.469 21.437 13.400 1.00 74.99 N ANISOU 1543 N TYR A 221 11664 8641 8186 613 83 175 N ATOM 1544 CA TYR A 221 23.212 20.336 14.335 1.00 74.99 C ANISOU 1544 CA TYR A 221 11610 8698 8185 590 83 216 C ATOM 1545 C TYR A 221 24.508 19.673 14.799 1.00 79.50 C ANISOU 1545 C TYR A 221 12155 9273 8779 573 111 276 C ATOM 1546 O TYR A 221 24.580 19.227 15.945 1.00 79.11 O ANISOU 1546 O TYR A 221 12037 9298 8725 548 110 312 O ATOM 1547 CB TYR A 221 22.262 19.297 13.733 1.00 76.13 C ANISOU 1547 CB TYR A 221 11772 8810 8343 588 69 229 C ATOM 1548 CG TYR A 221 20.814 19.606 14.034 1.00 77.91 C ANISOU 1548 CG TYR A 221 11977 9087 8540 588 38 202 C ATOM 1549 CD1 TYR A 221 20.264 19.324 15.281 1.00 80.23 C ANISOU 1549 CD1 TYR A 221 12189 9484 8810 570 20 232 C ATOM 1550 CD2 TYR A 221 20.014 20.257 13.104 1.00 78.57 C ANISOU 1550 CD2 TYR A 221 12113 9130 8611 607 26 153 C ATOM 1551 CE1 TYR A 221 18.941 19.646 15.579 1.00 81.35 C ANISOU 1551 CE1 TYR A 221 12305 9691 8914 576 -8 212 C ATOM 1552 CE2 TYR A 221 18.689 20.581 13.389 1.00 79.64 C ANISOU 1552 CE2 TYR A 221 12228 9316 8715 609 -1 132 C ATOM 1553 CZ TYR A 221 18.159 20.283 14.631 1.00 87.70 C ANISOU 1553 CZ TYR A 221 13170 10443 9710 596 -18 160 C ATOM 1554 OH TYR A 221 16.861 20.622 14.918 1.00 89.00 O ANISOU 1554 OH TYR A 221 13309 10673 9835 606 -44 144 O ATOM 1555 N CYS A 222 25.548 19.651 13.935 1.00 76.70 N ANISOU 1555 N CYS A 222 11846 8851 8443 588 137 292 N ATOM 1556 CA CYS A 222 26.868 19.128 14.305 1.00 76.70 C ANISOU 1556 CA CYS A 222 11825 8854 8463 577 167 352 C ATOM 1557 C CYS A 222 27.510 20.053 15.340 1.00 80.45 C ANISOU 1557 C CYS A 222 12260 9387 8922 558 166 355 C ATOM 1558 O CYS A 222 28.201 19.583 16.243 1.00 80.21 O ANISOU 1558 O CYS A 222 12179 9402 8897 533 183 404 O ATOM 1559 CB CYS A 222 27.757 18.964 13.077 1.00 77.06 C ANISOU 1559 CB CYS A 222 11926 8831 8522 608 192 367 C ATOM 1560 SG CYS A 222 27.263 17.613 11.981 1.00 81.18 S ANISOU 1560 SG CYS A 222 12487 9289 9067 638 189 357 S ATOM 1561 N ARG A 223 27.242 21.369 15.225 1.00 76.74 N ANISOU 1561 N ARG A 223 11807 8915 8437 571 141 299 N ATOM 1562 CA ARG A 223 27.726 22.363 16.173 1.00 76.64 C ANISOU 1562 CA ARG A 223 11757 8947 8415 559 122 281 C ATOM 1563 C ARG A 223 26.945 22.269 17.484 1.00 80.46 C ANISOU 1563 C ARG A 223 12173 9534 8864 548 103 251 C ATOM 1564 O ARG A 223 27.554 22.298 18.551 1.00 80.41 O ANISOU 1564 O ARG A 223 12112 9596 8845 529 106 269 O ATOM 1565 CB ARG A 223 27.620 23.777 15.581 1.00 76.88 C ANISOU 1565 CB ARG A 223 11823 8929 8459 579 86 229 C ATOM 1566 N ILE A 224 25.596 22.109 17.401 1.00 76.71 N ANISOU 1566 N ILE A 224 11695 9084 8369 560 85 215 N ATOM 1567 CA ILE A 224 24.711 22.011 18.575 1.00 76.89 C ANISOU 1567 CA ILE A 224 11641 9226 8346 558 65 194 C ATOM 1568 C ILE A 224 25.070 20.771 19.428 1.00 81.47 C ANISOU 1568 C ILE A 224 12149 9881 8925 524 89 281 C ATOM 1569 O ILE A 224 25.262 20.906 20.634 1.00 81.53 O ANISOU 1569 O ILE A 224 12080 10001 8898 515 84 284 O ATOM 1570 CB ILE A 224 23.209 21.999 18.147 1.00 79.94 C ANISOU 1570 CB ILE A 224 12041 9618 8713 577 43 158 C ATOM 1571 CG1 ILE A 224 22.754 23.413 17.709 1.00 80.33 C ANISOU 1571 CG1 ILE A 224 12134 9631 8759 610 11 66 C ATOM 1572 CG2 ILE A 224 22.303 21.456 19.277 1.00 81.00 C ANISOU 1572 CG2 ILE A 224 12084 9892 8801 571 29 179 C ATOM 1573 CD1 ILE A 224 21.411 23.461 16.975 1.00 86.87 C ANISOU 1573 CD1 ILE A 224 12993 10435 9578 627 -4 38 C ATOM 1574 N TYR A 225 25.192 19.586 18.795 1.00 78.13 N ANISOU 1574 N TYR A 225 11745 9395 8544 508 109 348 N ATOM 1575 CA TYR A 225 25.500 18.334 19.498 1.00 78.34 C ANISOU 1575 CA TYR A 225 11700 9473 8593 473 123 440 C ATOM 1576 C TYR A 225 26.901 18.376 20.162 1.00 82.18 C ANISOU 1576 C TYR A 225 12154 9987 9085 451 152 482 C ATOM 1577 O TYR A 225 27.090 17.767 21.217 1.00 81.69 O ANISOU 1577 O TYR A 225 11999 10021 9017 420 158 546 O ATOM 1578 CB TYR A 225 25.407 17.137 18.533 1.00 79.64 C ANISOU 1578 CB TYR A 225 11904 9537 8820 468 126 487 C ATOM 1579 CG TYR A 225 25.283 15.799 19.231 1.00 81.86 C ANISOU 1579 CG TYR A 225 12098 9863 9141 431 116 583 C ATOM 1580 CD1 TYR A 225 26.404 15.012 19.480 1.00 83.92 C ANISOU 1580 CD1 TYR A 225 12331 10105 9450 408 142 655 C ATOM 1581 CD2 TYR A 225 24.040 15.306 19.620 1.00 82.88 C ANISOU 1581 CD2 TYR A 225 12168 10057 9267 418 77 613 C ATOM 1582 CE1 TYR A 225 26.295 13.778 20.122 1.00 85.17 C ANISOU 1582 CE1 TYR A 225 12398 10300 9661 369 126 754 C ATOM 1583 CE2 TYR A 225 23.918 14.073 20.262 1.00 84.18 C ANISOU 1583 CE2 TYR A 225 12238 10264 9483 379 57 721 C ATOM 1584 CZ TYR A 225 25.049 13.312 20.511 1.00 91.37 C ANISOU 1584 CZ TYR A 225 13119 11148 10451 353 80 790 C ATOM 1585 OH TYR A 225 24.936 12.097 21.146 1.00 91.74 O ANISOU 1585 OH TYR A 225 13062 11231 10563 311 53 905 O ATOM 1586 N SER A 226 27.868 19.097 19.547 1.00 78.61 N ANISOU 1586 N SER A 226 11769 9456 8644 465 169 456 N ATOM 1587 CA SER A 226 29.236 19.200 20.069 1.00 78.34 C ANISOU 1587 CA SER A 226 11713 9438 8617 444 195 502 C ATOM 1588 C SER A 226 29.332 20.217 21.218 1.00 82.36 C ANISOU 1588 C SER A 226 12168 10047 9076 440 173 456 C ATOM 1589 O SER A 226 30.027 19.958 22.203 1.00 82.22 O ANISOU 1589 O SER A 226 12082 10109 9048 411 188 505 O ATOM 1590 CB SER A 226 30.208 19.581 18.957 1.00 81.40 C ANISOU 1590 CB SER A 226 12184 9714 9032 462 213 506 C ATOM 1591 OG SER A 226 29.889 20.849 18.408 1.00 89.72 O ANISOU 1591 OG SER A 226 13288 10729 10074 489 183 431 O ATOM 1592 N LEU A 227 28.659 21.382 21.081 1.00 78.76 N ANISOU 1592 N LEU A 227 11740 9588 8595 472 133 359 N ATOM 1593 CA LEU A 227 28.679 22.433 22.104 1.00 78.82 C ANISOU 1593 CA LEU A 227 11703 9683 8562 482 98 289 C ATOM 1594 C LEU A 227 27.925 21.994 23.358 1.00 82.46 C ANISOU 1594 C LEU A 227 12058 10310 8963 479 90 289 C ATOM 1595 O LEU A 227 28.379 22.277 24.467 1.00 82.49 O ANISOU 1595 O LEU A 227 11992 10421 8929 472 83 280 O ATOM 1596 CB LEU A 227 28.085 23.746 21.561 1.00 79.10 C ANISOU 1596 CB LEU A 227 11794 9660 8601 523 49 182 C ATOM 1597 CG LEU A 227 28.982 24.548 20.602 1.00 84.02 C ANISOU 1597 CG LEU A 227 12492 10151 9280 525 38 183 C ATOM 1598 CD1 LEU A 227 28.167 25.536 19.790 1.00 84.23 C ANISOU 1598 CD1 LEU A 227 12571 10107 9327 559 -5 104 C ATOM 1599 CD2 LEU A 227 30.099 25.269 21.355 1.00 87.35 C ANISOU 1599 CD2 LEU A 227 12888 10590 9711 511 14 179 C ATOM 1600 N VAL A 228 26.784 21.285 23.185 1.00 78.23 N ANISOU 1600 N VAL A 228 11502 9805 8415 484 90 308 N ATOM 1601 CA VAL A 228 25.991 20.766 24.305 1.00 78.07 C ANISOU 1601 CA VAL A 228 11368 9957 8338 481 81 335 C ATOM 1602 C VAL A 228 26.816 19.698 25.045 1.00 81.65 C ANISOU 1602 C VAL A 228 11738 10479 8806 430 114 453 C ATOM 1603 O VAL A 228 26.802 19.670 26.275 1.00 82.05 O ANISOU 1603 O VAL A 228 11679 10696 8799 424 109 470 O ATOM 1604 CB VAL A 228 24.605 20.227 23.835 1.00 81.86 C ANISOU 1604 CB VAL A 228 11848 10440 8815 492 66 348 C ATOM 1605 CG1 VAL A 228 23.936 19.368 24.910 1.00 82.07 C ANISOU 1605 CG1 VAL A 228 11740 10643 8799 475 59 429 C ATOM 1606 CG2 VAL A 228 23.688 21.374 23.421 1.00 81.73 C ANISOU 1606 CG2 VAL A 228 11884 10402 8767 544 31 230 C ATOM 1607 N ARG A 229 27.605 18.888 24.295 1.00 77.21 N ANISOU 1607 N ARG A 229 11225 9792 8318 399 148 531 N ATOM 1608 CA ARG A 229 28.491 17.863 24.867 1.00 76.90 C ANISOU 1608 CA ARG A 229 11117 9791 8311 351 180 648 C ATOM 1609 C ARG A 229 29.537 18.498 25.800 1.00 80.04 C ANISOU 1609 C ARG A 229 11473 10269 8672 338 192 640 C ATOM 1610 O ARG A 229 29.850 17.933 26.851 1.00 80.22 O ANISOU 1610 O ARG A 229 11384 10419 8676 303 206 717 O ATOM 1611 CB ARG A 229 29.189 17.069 23.751 1.00 77.27 C ANISOU 1611 CB ARG A 229 11242 9673 8443 338 209 705 C ATOM 1612 N THR A 230 30.042 19.694 25.426 1.00 75.06 N ANISOU 1612 N THR A 230 10922 9566 8033 364 180 551 N ATOM 1613 CA THR A 230 31.020 20.448 26.211 1.00 74.22 C ANISOU 1613 CA THR A 230 10788 9513 7899 355 176 529 C ATOM 1614 C THR A 230 30.301 21.238 27.339 1.00 76.74 C ANISOU 1614 C THR A 230 11028 9996 8133 386 132 434 C ATOM 1615 O THR A 230 30.881 21.454 28.403 1.00 76.69 O ANISOU 1615 O THR A 230 10946 10107 8084 373 129 435 O ATOM 1616 CB THR A 230 31.832 21.370 25.282 1.00 81.20 C ANISOU 1616 CB THR A 230 11784 10242 8825 368 167 487 C ATOM 1617 OG1 THR A 230 32.337 20.595 24.192 1.00 78.85 O ANISOU 1617 OG1 THR A 230 11552 9818 8590 355 207 566 O ATOM 1618 CG2 THR A 230 32.989 22.061 25.996 1.00 80.74 C ANISOU 1618 CG2 THR A 230 11705 10216 8758 350 157 484 C ATOM 1619 N ARG A 231 29.045 21.655 27.103 1.00 72.08 N ANISOU 1619 N ARG A 231 10452 9422 7513 431 98 351 N ATOM 1620 CA ARG A 231 28.263 22.389 28.102 1.00 71.94 C ANISOU 1620 CA ARG A 231 10359 9568 7407 476 54 251 C ATOM 1621 C ARG A 231 27.774 21.456 29.209 1.00 74.65 C ANISOU 1621 C ARG A 231 10556 10121 7687 460 69 332 C ATOM 1622 O ARG A 231 27.647 21.885 30.352 1.00 74.95 O ANISOU 1622 O ARG A 231 10497 10340 7640 486 47 281 O ATOM 1623 CB ARG A 231 27.070 23.101 27.450 1.00 72.53 C ANISOU 1623 CB ARG A 231 10492 9592 7473 532 15 146 C ATOM 1624 N ASN A1002 27.505 20.180 28.871 1.00 69.75 N ANISOU 1624 N ASN A1002 9911 9482 7108 420 101 460 N ATOM 1625 CA ASN A1002 27.030 19.189 29.837 1.00 69.54 C ANISOU 1625 CA ASN A1002 9734 9646 7042 395 109 569 C ATOM 1626 C ASN A1002 28.129 18.809 30.831 1.00 71.50 C ANISOU 1626 C ASN A1002 9887 10002 7278 349 137 649 C ATOM 1627 O ASN A1002 27.842 18.657 32.016 1.00 71.50 O ANISOU 1627 O ASN A1002 9742 10226 7199 351 129 680 O ATOM 1628 CB ASN A1002 26.502 17.942 29.128 1.00 71.35 C ANISOU 1628 CB ASN A1002 9968 9794 7346 360 120 687 C ATOM 1629 CG ASN A1002 25.146 18.124 28.477 1.00 98.01 C ANISOU 1629 CG ASN A1002 13388 13138 10712 400 87 634 C ATOM 1630 OD1 ASN A1002 24.479 19.157 28.627 1.00 93.38 O ANISOU 1630 OD1 ASN A1002 12815 12610 10054 457 59 515 O ATOM 1631 ND2 ASN A1002 24.702 17.112 27.749 1.00 90.70 N ANISOU 1631 ND2 ASN A1002 12484 12119 9861 372 87 722 N ATOM 1632 N ILE A1003 29.388 18.680 30.358 1.00 66.27 N ANISOU 1632 N ILE A1003 9298 9195 6689 311 169 687 N ATOM 1633 CA ILE A1003 30.518 18.360 31.235 1.00 65.89 C ANISOU 1633 CA ILE A1003 9168 9232 6634 264 199 767 C ATOM 1634 C ILE A1003 30.857 19.597 32.104 1.00 69.75 C ANISOU 1634 C ILE A1003 9632 9834 7035 298 171 646 C ATOM 1635 O ILE A1003 31.250 19.435 33.260 1.00 69.82 O ANISOU 1635 O ILE A1003 9519 10023 6987 277 179 688 O ATOM 1636 CB ILE A1003 31.766 17.818 30.436 1.00 68.52 C ANISOU 1636 CB ILE A1003 9587 9379 7070 217 243 850 C ATOM 1637 CG1 ILE A1003 32.972 17.502 31.359 1.00 69.38 C ANISOU 1637 CG1 ILE A1003 9610 9577 7172 164 277 941 C ATOM 1638 CG2 ILE A1003 32.180 18.743 29.307 1.00 68.90 C ANISOU 1638 CG2 ILE A1003 9796 9231 7154 248 234 754 C ATOM 1639 CD1 ILE A1003 32.792 16.311 32.279 1.00 79.29 C ANISOU 1639 CD1 ILE A1003 10704 10997 8427 115 296 1086 C ATOM 1640 N PHE A1004 30.623 20.822 31.572 1.00 66.23 N ANISOU 1640 N PHE A1004 9293 9292 6582 354 129 494 N ATOM 1641 CA PHE A1004 30.868 22.063 32.313 1.00 66.62 C ANISOU 1641 CA PHE A1004 9327 9422 6565 395 82 359 C ATOM 1642 C PHE A1004 29.857 22.231 33.449 1.00 72.09 C ANISOU 1642 C PHE A1004 9886 10366 7138 446 52 297 C ATOM 1643 O PHE A1004 30.260 22.465 34.589 1.00 71.95 O ANISOU 1643 O PHE A1004 9768 10524 7047 450 41 275 O ATOM 1644 CB PHE A1004 30.827 23.290 31.380 1.00 68.09 C ANISOU 1644 CB PHE A1004 9655 9423 6796 440 35 223 C ATOM 1645 CG PHE A1004 31.061 24.610 32.089 1.00 70.18 C ANISOU 1645 CG PHE A1004 9909 9743 7014 487 -32 72 C ATOM 1646 CD1 PHE A1004 32.347 25.097 32.280 1.00 72.90 C ANISOU 1646 CD1 PHE A1004 10280 10027 7393 458 -45 72 C ATOM 1647 CD2 PHE A1004 29.992 25.358 32.573 1.00 73.14 C ANISOU 1647 CD2 PHE A1004 10244 10231 7314 565 -89 -72 C ATOM 1648 CE1 PHE A1004 32.561 26.310 32.941 1.00 74.62 C ANISOU 1648 CE1 PHE A1004 10487 10284 7580 502 -122 -74 C ATOM 1649 CE2 PHE A1004 30.210 26.560 33.253 1.00 76.64 C ANISOU 1649 CE2 PHE A1004 10674 10723 7721 616 -162 -226 C ATOM 1650 CZ PHE A1004 31.492 27.030 33.429 1.00 74.65 C ANISOU 1650 CZ PHE A1004 10452 10398 7514 583 -182 -229 C ATOM 1651 N GLU A1005 28.545 22.133 33.135 1.00 69.98 N ANISOU 1651 N GLU A1005 9614 10128 6846 487 36 270 N ATOM 1652 CA GLU A1005 27.474 22.306 34.122 1.00 71.37 C ANISOU 1652 CA GLU A1005 9662 10555 6901 546 6 216 C ATOM 1653 C GLU A1005 27.507 21.197 35.190 1.00 76.46 C ANISOU 1653 C GLU A1005 10128 11433 7489 503 39 369 C ATOM 1654 O GLU A1005 27.128 21.447 36.337 1.00 77.35 O ANISOU 1654 O GLU A1005 10105 11801 7482 547 18 328 O ATOM 1655 CB GLU A1005 26.091 22.353 33.446 1.00 72.88 C ANISOU 1655 CB GLU A1005 9892 10712 7088 592 -14 180 C ATOM 1656 CG GLU A1005 25.895 23.523 32.481 1.00 85.56 C ANISOU 1656 CG GLU A1005 11651 12119 8740 641 -54 27 C ATOM 1657 CD GLU A1005 25.980 24.923 33.066 1.00112.60 C ANISOU 1657 CD GLU A1005 15078 15597 12109 715 -117 -161 C ATOM 1658 OE1 GLU A1005 25.588 25.109 34.241 1.00109.91 O ANISOU 1658 OE1 GLU A1005 14609 15499 11652 765 -140 -216 O ATOM 1659 OE2 GLU A1005 26.366 25.850 32.318 1.00110.23 O1- ANISOU 1659 OE2 GLU A1005 14901 15099 11883 728 -151 -257 O1- ATOM 1660 N MET A1006 27.981 19.983 34.820 1.00 72.52 N ANISOU 1660 N MET A1006 9622 10853 7078 421 88 545 N ATOM 1661 CA MET A1006 28.112 18.855 35.752 1.00 72.77 C ANISOU 1661 CA MET A1006 9482 11082 7088 366 117 716 C ATOM 1662 C MET A1006 29.103 19.194 36.868 1.00 76.85 C ANISOU 1662 C MET A1006 9910 11751 7537 354 126 702 C ATOM 1663 O MET A1006 28.826 18.939 38.042 1.00 76.95 O ANISOU 1663 O MET A1006 9747 12040 7451 361 122 750 O ATOM 1664 CB MET A1006 28.575 17.592 35.004 1.00 74.53 C ANISOU 1664 CB MET A1006 9737 11135 7444 283 158 887 C ATOM 1665 CG MET A1006 28.570 16.353 35.859 1.00 78.86 C ANISOU 1665 CG MET A1006 10102 11864 7995 222 177 1080 C ATOM 1666 SD MET A1006 29.518 15.000 35.137 1.00 82.55 S ANISOU 1666 SD MET A1006 10609 12123 8634 127 220 1259 S ATOM 1667 CE MET A1006 28.973 13.665 36.156 1.00 79.89 C ANISOU 1667 CE MET A1006 10032 12023 8298 72 212 1477 C ATOM 1668 N LEU A1007 30.254 19.781 36.492 1.00 72.98 N ANISOU 1668 N LEU A1007 9536 11091 7100 337 133 642 N ATOM 1669 CA LEU A1007 31.309 20.150 37.426 1.00 73.07 C ANISOU 1669 CA LEU A1007 9488 11211 7065 319 138 626 C ATOM 1670 C LEU A1007 31.097 21.578 37.982 1.00 78.18 C ANISOU 1670 C LEU A1007 10144 11950 7613 407 73 412 C ATOM 1671 O LEU A1007 31.800 21.983 38.909 1.00 78.33 O ANISOU 1671 O LEU A1007 10094 12097 7569 407 61 372 O ATOM 1672 CB LEU A1007 32.682 20.015 36.751 1.00 72.10 C ANISOU 1672 CB LEU A1007 9478 10862 7053 254 173 686 C ATOM 1673 CG LEU A1007 33.171 18.569 36.575 1.00 75.99 C ANISOU 1673 CG LEU A1007 9924 11318 7632 168 236 898 C ATOM 1674 CD1 LEU A1007 34.129 18.454 35.436 1.00 75.15 C ANISOU 1674 CD1 LEU A1007 9971 10939 7645 132 265 934 C ATOM 1675 CD2 LEU A1007 33.790 18.030 37.861 1.00 79.19 C ANISOU 1675 CD2 LEU A1007 10157 11948 7984 117 264 1011 C ATOM 1676 N ARG A1008 30.066 22.294 37.482 1.00 75.27 N ANISOU 1676 N ARG A1008 9843 11530 7225 483 27 276 N ATOM 1677 CA ARG A1008 29.684 23.618 37.996 1.00 76.11 C ANISOU 1677 CA ARG A1008 9950 11725 7245 579 -45 63 C ATOM 1678 C ARG A1008 28.914 23.461 39.323 1.00 82.16 C ANISOU 1678 C ARG A1008 10520 12845 7852 633 -58 49 C ATOM 1679 O ARG A1008 28.699 24.445 40.039 1.00 83.34 O ANISOU 1679 O ARG A1008 10629 13131 7904 719 -117 -125 O ATOM 1680 CB ARG A1008 28.824 24.372 36.961 1.00 75.84 C ANISOU 1680 CB ARG A1008 10050 11512 7254 640 -87 -63 C ATOM 1681 CG ARG A1008 28.775 25.883 37.168 1.00 86.10 C ANISOU 1681 CG ARG A1008 11401 12790 8523 727 -172 -291 C ATOM 1682 CD ARG A1008 27.468 26.485 36.677 1.00 95.50 C ANISOU 1682 CD ARG A1008 12636 13953 9695 811 -215 -412 C ATOM 1683 NE ARG A1008 26.434 26.479 37.718 1.00105.84 N ANISOU 1683 NE ARG A1008 13796 15565 10854 891 -234 -468 N ATOM 1684 CZ ARG A1008 25.466 25.568 37.812 1.00119.36 C ANISOU 1684 CZ ARG A1008 15417 17423 12511 889 -195 -351 C ATOM 1685 NH1 ARG A1008 25.381 24.586 36.922 1.00105.95 N ANISOU 1685 NH1 ARG A1008 13770 15581 10904 811 -140 -184 N ATOM 1686 NH2 ARG A1008 24.570 25.641 38.787 1.00105.00 N ANISOU 1686 NH2 ARG A1008 13451 15897 10545 969 -217 -399 N ATOM 1687 N ILE A1009 28.491 22.217 39.636 1.00 78.38 N ANISOU 1687 N ILE A1009 9912 12517 7351 587 -9 235 N ATOM 1688 CA ILE A1009 27.729 21.893 40.845 1.00 79.04 C ANISOU 1688 CA ILE A1009 9787 12958 7287 629 -15 270 C ATOM 1689 C ILE A1009 28.608 21.093 41.825 1.00 82.47 C ANISOU 1689 C ILE A1009 10067 13577 7692 555 27 425 C ATOM 1690 O ILE A1009 28.610 21.378 43.027 1.00 82.80 O ANISOU 1690 O ILE A1009 9958 13907 7597 600 9 377 O ATOM 1691 CB ILE A1009 26.433 21.106 40.468 1.00 82.03 C ANISOU 1691 CB ILE A1009 10115 13387 7666 634 -6 382 C ATOM 1692 CG1 ILE A1009 25.623 21.848 39.366 1.00 81.88 C ANISOU 1692 CG1 ILE A1009 10263 13157 7692 694 -40 243 C ATOM 1693 CG2 ILE A1009 25.571 20.826 41.714 1.00 84.08 C ANISOU 1693 CG2 ILE A1009 10144 14039 7761 686 -19 428 C ATOM 1694 CD1 ILE A1009 24.608 20.971 38.595 1.00 87.38 C ANISOU 1694 CD1 ILE A1009 10969 13787 8445 668 -25 375 C ATOM 1695 N ASP A1010 29.347 20.089 41.303 1.00 77.82 N ANISOU 1695 N ASP A1010 9510 12826 7230 447 83 609 N ATOM 1696 CA ASP A1010 30.189 19.192 42.096 1.00 77.57 C ANISOU 1696 CA ASP A1010 9337 12937 7199 363 129 787 C ATOM 1697 C ASP A1010 31.398 19.913 42.710 1.00 80.84 C ANISOU 1697 C ASP A1010 9762 13377 7577 357 124 697 C ATOM 1698 O ASP A1010 31.757 19.624 43.853 1.00 80.77 O ANISOU 1698 O ASP A1010 9582 13626 7480 337 138 765 O ATOM 1699 CB ASP A1010 30.664 18.010 41.238 1.00 78.45 C ANISOU 1699 CB ASP A1010 9506 12828 7475 259 180 983 C ATOM 1700 CG ASP A1010 29.568 17.009 40.900 1.00 88.82 C ANISOU 1700 CG ASP A1010 10753 14166 8828 243 180 1123 C ATOM 1701 OD1 ASP A1010 28.384 17.294 41.205 1.00 90.16 O ANISOU 1701 OD1 ASP A1010 10852 14505 8899 314 144 1067 O ATOM 1702 OD2 ASP A1010 29.895 15.936 40.352 1.00 93.26 O1- ANISOU 1702 OD2 ASP A1010 11330 14583 9522 162 212 1290 O1- ATOM 1703 N GLU A1011 32.035 20.829 41.957 1.00 76.67 N ANISOU 1703 N GLU A1011 9425 12587 7119 371 101 557 N ATOM 1704 CA GLU A1011 33.211 21.548 42.457 1.00 76.62 C ANISOU 1704 CA GLU A1011 9441 12575 7095 361 86 477 C ATOM 1705 C GLU A1011 32.982 23.077 42.430 1.00 80.08 C ANISOU 1705 C GLU A1011 9975 12965 7486 463 0 214 C ATOM 1706 O GLU A1011 33.885 23.848 42.769 1.00 79.81 O ANISOU 1706 O GLU A1011 9976 12899 7448 465 -35 117 O ATOM 1707 CB GLU A1011 34.471 21.159 41.661 1.00 77.01 C ANISOU 1707 CB GLU A1011 9614 12356 7290 265 132 591 C ATOM 1708 CG GLU A1011 34.846 19.692 41.844 1.00 87.90 C ANISOU 1708 CG GLU A1011 10885 13793 8719 167 208 839 C ATOM 1709 CD GLU A1011 36.248 19.280 41.435 1.00109.46 C ANISOU 1709 CD GLU A1011 13689 16340 11561 77 258 958 C ATOM 1710 OE1 GLU A1011 37.039 20.161 41.031 1.00106.68 O ANISOU 1710 OE1 GLU A1011 13471 15818 11244 84 234 858 O ATOM 1711 OE2 GLU A1011 36.568 18.075 41.559 1.00102.14 O1- ANISOU 1711 OE2 GLU A1011 12675 15447 10688 -1 316 1158 O1- ATOM 1712 N GLY A1012 31.754 23.479 42.103 1.00 76.42 N ANISOU 1712 N GLY A1012 9536 12512 6988 547 -38 105 N ATOM 1713 CA GLY A1012 31.336 24.877 42.087 1.00 76.72 C ANISOU 1713 CA GLY A1012 9649 12516 6986 654 -126 -146 C ATOM 1714 C GLY A1012 32.053 25.745 41.075 1.00 79.58 C ANISOU 1714 C GLY A1012 10213 12542 7482 641 -165 -237 C ATOM 1715 O GLY A1012 32.434 25.275 39.999 1.00 78.37 O ANISOU 1715 O GLY A1012 10174 12147 7455 571 -121 -121 O ATOM 1716 N LEU A1013 32.215 27.036 41.409 1.00 76.11 N ANISOU 1716 N LEU A1013 9811 12091 7018 715 -256 -449 N ATOM 1717 CA LEU A1013 32.882 28.029 40.567 1.00 75.29 C ANISOU 1717 CA LEU A1013 9879 11687 7043 711 -317 -547 C ATOM 1718 C LEU A1013 33.397 29.176 41.432 1.00 80.60 C ANISOU 1718 C LEU A1013 10527 12426 7671 768 -416 -737 C ATOM 1719 O LEU A1013 32.808 29.469 42.474 1.00 81.79 O ANISOU 1719 O LEU A1013 10555 12837 7684 854 -456 -863 O ATOM 1720 CB LEU A1013 31.912 28.554 39.481 1.00 74.81 C ANISOU 1720 CB LEU A1013 9937 11441 7047 765 -351 -635 C ATOM 1721 CG LEU A1013 32.495 29.511 38.422 1.00 78.68 C ANISOU 1721 CG LEU A1013 10600 11607 7687 754 -412 -702 C ATOM 1722 CD1 LEU A1013 33.542 28.819 37.561 1.00 77.57 C ANISOU 1722 CD1 LEU A1013 10543 11268 7662 641 -342 -507 C ATOM 1723 CD2 LEU A1013 31.408 30.067 37.549 1.00 80.61 C ANISOU 1723 CD2 LEU A1013 10929 11725 7975 818 -451 -801 C ATOM 1724 N ARG A1014 34.512 29.808 41.021 1.00 76.69 N ANISOU 1724 N ARG A1014 10142 11707 7290 724 -461 -754 N ATOM 1725 CA ARG A1014 35.087 30.921 41.769 1.00 77.56 C ANISOU 1725 CA ARG A1014 10241 11845 7385 771 -571 -932 C ATOM 1726 C ARG A1014 35.807 31.900 40.857 1.00 81.44 C ANISOU 1726 C ARG A1014 10892 12009 8043 749 -654 -983 C ATOM 1727 O ARG A1014 36.467 31.493 39.901 1.00 79.54 O ANISOU 1727 O ARG A1014 10746 11562 7915 660 -600 -819 O ATOM 1728 CB ARG A1014 36.049 30.416 42.844 1.00 77.87 C ANISOU 1728 CB ARG A1014 10164 12074 7347 714 -535 -847 C ATOM 1729 N LEU A1015 35.690 33.198 41.168 1.00 79.86 N ANISOU 1729 N LEU A1015 10714 11770 7859 834 -792 -1210 N ATOM 1730 CA LEU A1015 36.384 34.263 40.447 1.00 79.86 C ANISOU 1730 CA LEU A1015 10844 11474 8025 819 -898 -1269 C ATOM 1731 C LEU A1015 37.652 34.640 41.206 1.00 84.47 C ANISOU 1731 C LEU A1015 11400 12073 8620 778 -958 -1282 C ATOM 1732 O LEU A1015 38.679 34.915 40.587 1.00 83.38 O ANISOU 1732 O LEU A1015 11353 11712 8617 702 -986 -1188 O ATOM 1733 CB LEU A1015 35.470 35.493 40.263 1.00 80.91 C ANISOU 1733 CB LEU A1015 11020 11525 8197 935 -1029 -1508 C ATOM 1734 CG LEU A1015 34.098 35.241 39.608 1.00 85.11 C ANISOU 1734 CG LEU A1015 11570 12061 8705 989 -982 -1521 C ATOM 1735 CD1 LEU A1015 33.180 36.441 39.789 1.00 86.64 C ANISOU 1735 CD1 LEU A1015 11770 12248 8903 1121 -1114 -1782 C ATOM 1736 CD2 LEU A1015 34.239 34.883 38.129 1.00 85.44 C ANISOU 1736 CD2 LEU A1015 11735 11846 8882 907 -920 -1346 C ATOM 1737 N LYS A1016 37.588 34.595 42.562 1.00 82.36 N ANISOU 1737 N LYS A1016 10999 12088 8204 828 -974 -1384 N ATOM 1738 CA LYS A1016 38.720 34.879 43.446 1.00 83.18 C ANISOU 1738 CA LYS A1016 11057 12256 8292 794 -1028 -1405 C ATOM 1739 C LYS A1016 39.328 33.577 43.990 1.00 87.24 C ANISOU 1739 C LYS A1016 11472 12963 8712 700 -885 -1187 C ATOM 1740 O LYS A1016 38.640 32.556 44.054 1.00 86.28 O ANISOU 1740 O LYS A1016 11277 13007 8499 695 -769 -1081 O ATOM 1741 CB LYS A1016 38.287 35.790 44.604 1.00 87.51 C ANISOU 1741 CB LYS A1016 11518 12994 8739 921 -1155 -1684 C ATOM 1742 N ILE A1017 40.619 33.619 44.380 1.00 84.64 N ANISOU 1742 N ILE A1017 11138 12608 8414 622 -900 -1113 N ATOM 1743 CA ILE A1017 41.345 32.458 44.918 1.00 84.35 C ANISOU 1743 CA ILE A1017 11007 12737 8304 525 -774 -901 C ATOM 1744 C ILE A1017 40.789 32.087 46.307 1.00 90.67 C ANISOU 1744 C ILE A1017 11622 13925 8905 586 -750 -980 C ATOM 1745 O ILE A1017 40.598 32.966 47.150 1.00 92.04 O ANISOU 1745 O ILE A1017 11742 14225 9006 678 -864 -1204 O ATOM 1746 CB ILE A1017 42.884 32.743 44.975 1.00 87.34 C ANISOU 1746 CB ILE A1017 11432 12980 8772 431 -810 -814 C ATOM 1747 CG1 ILE A1017 43.443 33.078 43.568 1.00 86.70 C ANISOU 1747 CG1 ILE A1017 11521 12539 8883 372 -830 -711 C ATOM 1748 CG2 ILE A1017 43.651 31.569 45.614 1.00 87.49 C ANISOU 1748 CG2 ILE A1017 11345 13185 8713 332 -682 -600 C ATOM 1749 CD1 ILE A1017 44.870 33.664 43.555 1.00 93.51 C ANISOU 1749 CD1 ILE A1017 12441 13241 9850 299 -906 -656 C ATOM 1750 N TYR A1018 40.527 30.784 46.532 1.00 87.24 N ANISOU 1750 N TYR A1018 11081 13680 8384 537 -610 -792 N ATOM 1751 CA TYR A1018 40.017 30.276 47.809 1.00 88.35 C ANISOU 1751 CA TYR A1018 11022 14211 8334 581 -573 -815 C ATOM 1752 C TYR A1018 40.761 28.998 48.214 1.00 91.38 C ANISOU 1752 C TYR A1018 11302 14733 8686 461 -444 -550 C ATOM 1753 O TYR A1018 41.197 28.242 47.347 1.00 89.54 O ANISOU 1753 O TYR A1018 11144 14312 8564 363 -356 -343 O ATOM 1754 CB TYR A1018 38.493 30.013 47.725 1.00 90.10 C ANISOU 1754 CB TYR A1018 11189 14574 8472 673 -549 -872 C ATOM 1755 CG TYR A1018 38.110 28.820 46.869 1.00 90.99 C ANISOU 1755 CG TYR A1018 11322 14608 8641 599 -424 -639 C ATOM 1756 CD1 TYR A1018 37.831 27.583 47.445 1.00 93.00 C ANISOU 1756 CD1 TYR A1018 11415 15122 8800 557 -318 -458 C ATOM 1757 CD2 TYR A1018 38.002 28.934 45.487 1.00 90.77 C ANISOU 1757 CD2 TYR A1018 11469 14254 8766 575 -420 -602 C ATOM 1758 CE1 TYR A1018 37.485 26.480 46.662 1.00 92.75 C ANISOU 1758 CE1 TYR A1018 11401 15004 8835 491 -219 -251 C ATOM 1759 CE2 TYR A1018 37.663 27.837 44.693 1.00 90.54 C ANISOU 1759 CE2 TYR A1018 11461 14150 8790 513 -313 -403 C ATOM 1760 CZ TYR A1018 37.396 26.614 45.285 1.00 98.10 C ANISOU 1760 CZ TYR A1018 12262 15350 9661 472 -217 -233 C ATOM 1761 OH TYR A1018 37.048 25.536 44.504 1.00 97.96 O ANISOU 1761 OH TYR A1018 12265 15246 9710 414 -128 -46 O ATOM 1762 N LYS A1019 40.881 28.743 49.524 1.00 88.90 N ANISOU 1762 N LYS A1019 10806 14754 8219 472 -432 -558 N ATOM 1763 CA LYS A1019 41.516 27.521 50.017 1.00 88.21 C ANISOU 1763 CA LYS A1019 10592 14830 8095 360 -312 -305 C ATOM 1764 C LYS A1019 40.510 26.369 49.998 1.00 92.06 C ANISOU 1764 C LYS A1019 10964 15490 8524 358 -213 -155 C ATOM 1765 O LYS A1019 39.341 26.574 50.336 1.00 92.51 O ANISOU 1765 O LYS A1019 10944 15734 8473 464 -245 -282 O ATOM 1766 CB LYS A1019 42.076 27.732 51.432 1.00 91.88 C ANISOU 1766 CB LYS A1019 10898 15593 8419 369 -344 -365 C ATOM 1767 N ASP A1020 40.949 25.164 49.581 1.00 87.51 N ANISOU 1767 N ASP A1020 10376 14848 8027 240 -99 114 N ATOM 1768 CA ASP A1020 40.059 24.001 49.530 1.00 87.01 C ANISOU 1768 CA ASP A1020 10200 14925 7935 224 -14 279 C ATOM 1769 C ASP A1020 39.935 23.342 50.929 1.00 92.45 C ANISOU 1769 C ASP A1020 10627 16037 8463 216 25 370 C ATOM 1770 O ASP A1020 40.621 23.752 51.872 1.00 92.57 O ANISOU 1770 O ASP A1020 10562 16220 8392 216 -4 310 O ATOM 1771 CB ASP A1020 40.537 22.975 48.465 1.00 87.09 C ANISOU 1771 CB ASP A1020 10303 14676 8109 110 79 518 C ATOM 1772 CG ASP A1020 41.863 22.271 48.745 1.00 94.55 C ANISOU 1772 CG ASP A1020 11204 15615 9105 -14 150 723 C ATOM 1773 OD1 ASP A1020 42.533 22.632 49.735 1.00 95.64 O ANISOU 1773 OD1 ASP A1020 11252 15927 9158 -24 127 684 O ATOM 1774 OD2 ASP A1020 42.229 21.368 47.966 1.00 98.49 O1- ANISOU 1774 OD2 ASP A1020 11759 15933 9728 -98 225 915 O1- ATOM 1775 N THR A1021 39.060 22.320 51.049 1.00 89.70 N ANISOU 1775 N THR A1021 10142 15863 8077 207 86 524 N ATOM 1776 CA THR A1021 38.810 21.596 52.305 1.00 90.80 C ANISOU 1776 CA THR A1021 10012 16418 8070 197 124 645 C ATOM 1777 C THR A1021 40.058 20.790 52.767 1.00 94.27 C ANISOU 1777 C THR A1021 10363 16906 8551 62 199 870 C ATOM 1778 O THR A1021 40.169 20.467 53.954 1.00 94.73 O ANISOU 1778 O THR A1021 10201 17314 8478 51 216 938 O ATOM 1779 CB THR A1021 37.586 20.666 52.156 1.00 99.77 C ANISOU 1779 CB THR A1021 11036 17681 9191 208 163 784 C ATOM 1780 OG1 THR A1021 37.703 19.916 50.941 1.00 97.22 O ANISOU 1780 OG1 THR A1021 10851 17031 9057 124 215 943 O ATOM 1781 CG2 THR A1021 36.265 21.432 52.167 1.00 99.31 C ANISOU 1781 CG2 THR A1021 10980 17727 9025 355 91 570 C ATOM 1782 N GLU A1022 40.990 20.486 51.838 1.00 89.48 N ANISOU 1782 N GLU A1022 9919 15959 8119 -36 241 983 N ATOM 1783 CA GLU A1022 42.213 19.745 52.162 1.00 88.95 C ANISOU 1783 CA GLU A1022 9789 15901 8108 -164 313 1196 C ATOM 1784 C GLU A1022 43.253 20.665 52.844 1.00 92.98 C ANISOU 1784 C GLU A1022 10314 16460 8553 -164 267 1071 C ATOM 1785 O GLU A1022 43.771 20.323 53.911 1.00 93.26 O ANISOU 1785 O GLU A1022 10170 16764 8499 -211 297 1165 O ATOM 1786 CB GLU A1022 42.808 19.101 50.898 1.00 88.80 C ANISOU 1786 CB GLU A1022 9938 15509 8291 -254 372 1354 C ATOM 1787 N GLY A1023 43.536 21.815 52.222 1.00 88.61 N ANISOU 1787 N GLY A1023 9966 15649 8052 -113 191 868 N ATOM 1788 CA GLY A1023 44.498 22.786 52.737 1.00 88.59 C ANISOU 1788 CA GLY A1023 10003 15642 8013 -109 125 734 C ATOM 1789 C GLY A1023 45.434 23.345 51.679 1.00 89.90 C ANISOU 1789 C GLY A1023 10407 15409 8342 -153 99 716 C ATOM 1790 O GLY A1023 46.645 23.443 51.905 1.00 88.96 O ANISOU 1790 O GLY A1023 10307 15237 8257 -229 106 785 O ATOM 1791 N TYR A1024 44.874 23.725 50.513 1.00 84.77 N ANISOU 1791 N TYR A1024 9933 14484 7792 -104 67 630 N ATOM 1792 CA TYR A1024 45.635 24.295 49.397 1.00 83.07 C ANISOU 1792 CA TYR A1024 9939 13893 7732 -135 36 616 C ATOM 1793 C TYR A1024 44.772 25.294 48.615 1.00 84.92 C ANISOU 1793 C TYR A1024 10319 13944 8005 -29 -59 396 C ATOM 1794 O TYR A1024 43.547 25.149 48.575 1.00 84.64 O ANISOU 1794 O TYR A1024 10238 14007 7912 45 -59 329 O ATOM 1795 CB TYR A1024 46.151 23.185 48.470 1.00 82.80 C ANISOU 1795 CB TYR A1024 9967 13663 7832 -237 146 871 C ATOM 1796 N TYR A1025 45.407 26.316 48.009 1.00 79.73 N ANISOU 1796 N TYR A1025 9827 13023 7446 -23 -143 295 N ATOM 1797 CA TYR A1025 44.687 27.355 47.266 1.00 79.02 C ANISOU 1797 CA TYR A1025 9873 12744 7409 72 -244 90 C ATOM 1798 C TYR A1025 44.137 26.819 45.932 1.00 80.06 C ANISOU 1798 C TYR A1025 10116 12658 7646 62 -183 187 C ATOM 1799 O TYR A1025 44.797 26.024 45.257 1.00 78.48 O ANISOU 1799 O TYR A1025 9965 12316 7536 -28 -96 394 O ATOM 1800 CB TYR A1025 45.582 28.571 47.029 1.00 80.40 C ANISOU 1800 CB TYR A1025 10174 12702 7673 70 -361 -21 C ATOM 1801 CG TYR A1025 45.883 29.346 48.294 1.00 83.24 C ANISOU 1801 CG TYR A1025 10439 13259 7929 112 -458 -189 C ATOM 1802 CD1 TYR A1025 47.061 29.134 49.001 1.00 85.20 C ANISOU 1802 CD1 TYR A1025 10624 13594 8155 28 -437 -81 C ATOM 1803 CD2 TYR A1025 44.983 30.284 48.793 1.00 85.20 C ANISOU 1803 CD2 TYR A1025 10658 13614 8099 241 -573 -461 C ATOM 1804 CE1 TYR A1025 47.342 29.842 50.167 1.00 87.14 C ANISOU 1804 CE1 TYR A1025 10780 14026 8302 68 -532 -243 C ATOM 1805 CE2 TYR A1025 45.252 30.996 49.960 1.00 87.49 C ANISOU 1805 CE2 TYR A1025 10860 14093 8291 290 -671 -634 C ATOM 1806 CZ TYR A1025 46.438 30.779 50.639 1.00 95.37 C ANISOU 1806 CZ TYR A1025 11797 15172 9267 202 -651 -526 C ATOM 1807 OH TYR A1025 46.712 31.477 51.792 1.00 99.32 O ANISOU 1807 OH TYR A1025 12208 15864 9667 252 -752 -703 O ATOM 1808 N THR A1026 42.902 27.237 45.584 1.00 75.62 N ANISOU 1808 N THR A1026 9585 12082 7064 159 -229 34 N ATOM 1809 CA THR A1026 42.169 26.766 44.403 1.00 73.86 C ANISOU 1809 CA THR A1026 9453 11690 6920 164 -180 99 C ATOM 1810 C THR A1026 41.380 27.936 43.751 1.00 76.62 C ANISOU 1810 C THR A1026 9921 11878 7312 263 -287 -118 C ATOM 1811 O THR A1026 41.107 28.937 44.417 1.00 77.32 O ANISOU 1811 O THR A1026 9982 12056 7340 344 -392 -327 O ATOM 1812 CB THR A1026 41.211 25.614 44.822 1.00 82.20 C ANISOU 1812 CB THR A1026 10363 12984 7883 169 -92 197 C ATOM 1813 OG1 THR A1026 41.810 24.827 45.857 1.00 82.17 O ANISOU 1813 OG1 THR A1026 10201 13216 7805 103 -29 337 O ATOM 1814 CG2 THR A1026 40.824 24.728 43.669 1.00 79.60 C ANISOU 1814 CG2 THR A1026 10109 12484 7651 133 -15 344 C ATOM 1815 N ILE A1027 41.009 27.796 42.454 1.00 71.13 N ANISOU 1815 N ILE A1027 9352 10951 6723 258 -263 -68 N ATOM 1816 CA ILE A1027 40.220 28.807 41.729 1.00 70.65 C ANISOU 1816 CA ILE A1027 9400 10729 6714 342 -354 -246 C ATOM 1817 C ILE A1027 39.291 28.117 40.688 1.00 72.83 C ANISOU 1817 C ILE A1027 9729 10913 7030 348 -284 -168 C ATOM 1818 O ILE A1027 39.557 26.985 40.269 1.00 71.79 O ANISOU 1818 O ILE A1027 9593 10755 6930 275 -180 29 O ATOM 1819 CB ILE A1027 41.135 29.886 41.060 1.00 73.57 C ANISOU 1819 CB ILE A1027 9910 10825 7219 325 -447 -294 C ATOM 1820 CG1 ILE A1027 40.328 31.171 40.720 1.00 74.54 C ANISOU 1820 CG1 ILE A1027 10105 10836 7380 426 -575 -523 C ATOM 1821 CG2 ILE A1027 41.876 29.321 39.826 1.00 72.67 C ANISOU 1821 CG2 ILE A1027 9905 10476 7229 238 -373 -89 C ATOM 1822 CD1 ILE A1027 41.139 32.420 40.588 1.00 81.45 C ANISOU 1822 CD1 ILE A1027 11061 11525 8361 427 -708 -620 C ATOM 1823 N GLY A1028 38.218 28.819 40.302 1.00 68.45 N ANISOU 1823 N GLY A1028 9223 10310 6477 436 -349 -329 N ATOM 1824 CA GLY A1028 37.243 28.349 39.322 1.00 66.77 C ANISOU 1824 CA GLY A1028 9065 10007 6297 452 -302 -286 C ATOM 1825 C GLY A1028 36.644 27.003 39.657 1.00 68.77 C ANISOU 1825 C GLY A1028 9205 10452 6473 427 -200 -146 C ATOM 1826 O GLY A1028 36.136 26.801 40.766 1.00 68.63 O ANISOU 1826 O GLY A1028 9042 10708 6327 465 -199 -186 O ATOM 1827 N ILE A1029 36.736 26.055 38.708 1.00 63.57 N ANISOU 1827 N ILE A1029 8603 9657 5894 364 -118 25 N ATOM 1828 CA ILE A1029 36.222 24.709 38.911 1.00 62.70 C ANISOU 1828 CA ILE A1029 8391 9690 5743 331 -30 177 C ATOM 1829 C ILE A1029 37.381 23.781 39.347 1.00 66.44 C ANISOU 1829 C ILE A1029 8797 10215 6232 234 42 364 C ATOM 1830 O ILE A1029 38.057 23.174 38.506 1.00 65.45 O ANISOU 1830 O ILE A1029 8749 9910 6208 169 97 502 O ATOM 1831 CB ILE A1029 35.467 24.178 37.657 1.00 64.55 C ANISOU 1831 CB ILE A1029 8716 9758 6053 331 4 235 C ATOM 1832 CG1 ILE A1029 34.339 25.160 37.238 1.00 64.93 C ANISOU 1832 CG1 ILE A1029 8828 9755 6086 424 -68 51 C ATOM 1833 CG2 ILE A1029 34.912 22.770 37.918 1.00 65.50 C ANISOU 1833 CG2 ILE A1029 8721 10023 6145 294 77 396 C ATOM 1834 CD1 ILE A1029 33.481 24.727 36.052 1.00 69.56 C ANISOU 1834 CD1 ILE A1029 9498 10198 6734 431 -41 92 C ATOM 1835 N GLY A1030 37.627 23.751 40.662 1.00 63.35 N ANISOU 1835 N GLY A1030 8260 10072 5737 231 38 358 N ATOM 1836 CA GLY A1030 38.628 22.904 41.308 1.00 62.87 C ANISOU 1836 CA GLY A1030 8102 10114 5671 143 104 531 C ATOM 1837 C GLY A1030 40.035 22.931 40.737 1.00 65.47 C ANISOU 1837 C GLY A1030 8538 10231 6107 69 127 622 C ATOM 1838 O GLY A1030 40.790 21.967 40.916 1.00 63.59 O ANISOU 1838 O GLY A1030 8244 10021 5898 -12 201 804 O ATOM 1839 N HIS A1031 40.419 24.041 40.072 1.00 62.47 N ANISOU 1839 N HIS A1031 8303 9644 5788 97 60 505 N ATOM 1840 CA HIS A1031 41.760 24.160 39.512 1.00 61.79 C ANISOU 1840 CA HIS A1031 8314 9365 5799 33 74 597 C ATOM 1841 C HIS A1031 42.754 24.435 40.622 1.00 66.30 C ANISOU 1841 C HIS A1031 8804 10070 6318 -6 57 607 C ATOM 1842 O HIS A1031 42.819 25.557 41.130 1.00 66.00 O ANISOU 1842 O HIS A1031 8771 10062 6244 39 -38 443 O ATOM 1843 CB HIS A1031 41.826 25.253 38.433 1.00 62.48 C ANISOU 1843 CB HIS A1031 8566 9198 5975 70 0 490 C ATOM 1844 CG HIS A1031 43.162 25.342 37.758 1.00 65.50 C ANISOU 1844 CG HIS A1031 9042 9388 6455 8 13 606 C ATOM 1845 ND1 HIS A1031 43.431 24.638 36.598 1.00 66.40 N ANISOU 1845 ND1 HIS A1031 9238 9338 6654 -25 82 744 N ATOM 1846 CD2 HIS A1031 44.270 26.030 38.118 1.00 67.70 C ANISOU 1846 CD2 HIS A1031 9336 9631 6755 -25 -36 606 C ATOM 1847 CE1 HIS A1031 44.686 24.922 36.287 1.00 65.67 C ANISOU 1847 CE1 HIS A1031 9203 9125 6623 -72 77 829 C ATOM 1848 NE2 HIS A1031 45.231 25.757 37.171 1.00 66.77 N ANISOU 1848 NE2 HIS A1031 9307 9331 6732 -78 6 757 N ATOM 1849 N LEU A1032 43.504 23.392 41.034 1.00 63.76 N ANISOU 1849 N LEU A1032 8398 9833 5994 -88 144 796 N ATOM 1850 CA LEU A1032 44.520 23.501 42.081 1.00 64.28 C ANISOU 1850 CA LEU A1032 8378 10035 6012 -138 142 837 C ATOM 1851 C LEU A1032 45.704 24.320 41.571 1.00 68.52 C ANISOU 1851 C LEU A1032 9040 10360 6632 -168 96 836 C ATOM 1852 O LEU A1032 46.424 23.880 40.669 1.00 67.37 O ANISOU 1852 O LEU A1032 8982 10034 6583 -219 149 980 O ATOM 1853 CB LEU A1032 44.980 22.104 42.546 1.00 63.98 C ANISOU 1853 CB LEU A1032 8216 10127 5965 -223 252 1059 C ATOM 1854 CG LEU A1032 45.867 22.069 43.797 1.00 69.39 C ANISOU 1854 CG LEU A1032 8774 11012 6579 -278 262 1114 C ATOM 1855 CD1 LEU A1032 45.079 22.467 45.039 1.00 70.81 C ANISOU 1855 CD1 LEU A1032 8807 11485 6611 -218 211 972 C ATOM 1856 CD2 LEU A1032 46.480 20.696 43.989 1.00 70.87 C ANISOU 1856 CD2 LEU A1032 8867 11261 6799 -372 372 1360 C ATOM 1857 N LEU A1033 45.858 25.540 42.103 1.00 66.29 N ANISOU 1857 N LEU A1033 8770 10099 6318 -128 -12 668 N ATOM 1858 CA LEU A1033 46.906 26.470 41.694 1.00 66.57 C ANISOU 1858 CA LEU A1033 8916 9939 6439 -152 -84 654 C ATOM 1859 C LEU A1033 48.270 26.020 42.216 1.00 72.88 C ANISOU 1859 C LEU A1033 9665 10785 7239 -247 -33 824 C ATOM 1860 O LEU A1033 49.240 25.979 41.453 1.00 72.02 O ANISOU 1860 O LEU A1033 9647 10491 7225 -301 -12 956 O ATOM 1861 CB LEU A1033 46.577 27.884 42.193 1.00 67.56 C ANISOU 1861 CB LEU A1033 9054 10078 6537 -76 -231 412 C ATOM 1862 CG LEU A1033 45.317 28.513 41.599 1.00 72.26 C ANISOU 1862 CG LEU A1033 9714 10595 7148 20 -296 236 C ATOM 1863 CD1 LEU A1033 44.809 29.636 42.468 1.00 73.74 C ANISOU 1863 CD1 LEU A1033 9859 10890 7269 107 -425 -12 C ATOM 1864 CD2 LEU A1033 45.557 28.991 40.175 1.00 74.07 C ANISOU 1864 CD2 LEU A1033 10103 10521 7520 14 -327 270 C ATOM 1865 N THR A1034 48.339 25.664 43.515 1.00 71.70 N ANISOU 1865 N THR A1034 9364 10897 6980 -267 -10 829 N ATOM 1866 CA THR A1034 49.561 25.183 44.166 1.00 72.26 C ANISOU 1866 CA THR A1034 9364 11052 7039 -360 44 991 C ATOM 1867 C THR A1034 49.212 24.434 45.453 1.00 78.79 C ANISOU 1867 C THR A1034 9997 12203 7737 -373 100 1021 C ATOM 1868 O THR A1034 48.136 24.648 46.025 1.00 79.62 O ANISOU 1868 O THR A1034 10023 12483 7747 -297 62 871 O ATOM 1869 CB THR A1034 50.549 26.356 44.451 1.00 79.49 C ANISOU 1869 CB THR A1034 10335 11888 7982 -374 -65 918 C ATOM 1870 OG1 THR A1034 51.736 25.829 45.045 1.00 78.12 O ANISOU 1870 OG1 THR A1034 10093 11795 7795 -470 -5 1091 O ATOM 1871 CG2 THR A1034 49.947 27.443 45.358 1.00 78.62 C ANISOU 1871 CG2 THR A1034 10175 11910 7786 -291 -194 660 C ATOM 1872 N LYS A1035 50.126 23.560 45.911 1.00 75.74 N ANISOU 1872 N LYS A1035 9525 11905 7346 -467 189 1223 N ATOM 1873 CA LYS A1035 49.973 22.855 47.183 1.00 76.32 C ANISOU 1873 CA LYS A1035 9397 12298 7303 -495 241 1283 C ATOM 1874 C LYS A1035 50.510 23.737 48.314 1.00 81.47 C ANISOU 1874 C LYS A1035 9982 13109 7863 -490 160 1166 C ATOM 1875 O LYS A1035 50.122 23.566 49.471 1.00 82.03 O ANISOU 1875 O LYS A1035 9884 13480 7805 -474 162 1125 O ATOM 1876 CB LYS A1035 50.697 21.499 47.146 1.00 78.10 C ANISOU 1876 CB LYS A1035 9554 12541 7578 -599 370 1559 C ATOM 1877 N SER A1036 51.379 24.717 47.955 1.00 78.24 N ANISOU 1877 N SER A1036 9704 12500 7523 -501 79 1109 N ATOM 1878 CA SER A1036 51.992 25.685 48.871 1.00 79.27 C ANISOU 1878 CA SER A1036 9802 12721 7596 -497 -21 985 C ATOM 1879 C SER A1036 50.915 26.536 49.584 1.00 84.41 C ANISOU 1879 C SER A1036 10395 13543 8135 -378 -130 706 C ATOM 1880 O SER A1036 49.936 26.943 48.952 1.00 84.00 O ANISOU 1880 O SER A1036 10419 13388 8108 -294 -176 569 O ATOM 1881 CB SER A1036 52.959 26.590 48.108 1.00 82.35 C ANISOU 1881 CB SER A1036 10361 12816 8111 -523 -103 981 C ATOM 1882 OG SER A1036 53.647 27.485 48.965 1.00 91.41 O ANISOU 1882 OG SER A1036 11481 14029 9221 -530 -208 879 O ATOM 1883 N PRO A1037 51.075 26.815 50.906 1.00 81.87 N ANISOU 1883 N PRO A1037 9931 13492 7683 -366 -172 617 N ATOM 1884 CA PRO A1037 50.050 27.602 51.613 1.00 82.85 C ANISOU 1884 CA PRO A1037 9989 13801 7688 -239 -275 342 C ATOM 1885 C PRO A1037 50.279 29.123 51.496 1.00 86.91 C ANISOU 1885 C PRO A1037 10627 14137 8257 -175 -450 102 C ATOM 1886 O PRO A1037 49.845 29.883 52.369 1.00 87.83 O ANISOU 1886 O PRO A1037 10672 14431 8268 -82 -555 -131 O ATOM 1887 CB PRO A1037 50.182 27.120 53.059 1.00 85.64 C ANISOU 1887 CB PRO A1037 10124 14542 7875 -257 -235 374 C ATOM 1888 CG PRO A1037 51.616 26.693 53.194 1.00 89.57 C ANISOU 1888 CG PRO A1037 10617 14988 8426 -391 -176 590 C ATOM 1889 CD PRO A1037 52.164 26.396 51.816 1.00 83.62 C ANISOU 1889 CD PRO A1037 10040 13879 7853 -461 -124 761 C ATOM 1890 N SER A1038 50.900 29.569 50.384 1.00 82.12 N ANISOU 1890 N SER A1038 10201 13182 7819 -215 -489 156 N ATOM 1891 CA SER A1038 51.160 30.985 50.126 1.00 82.34 C ANISOU 1891 CA SER A1038 10351 12999 7937 -167 -663 -37 C ATOM 1892 C SER A1038 50.139 31.553 49.141 1.00 85.42 C ANISOU 1892 C SER A1038 10859 13192 8405 -76 -724 -177 C ATOM 1893 O SER A1038 49.971 31.013 48.044 1.00 83.62 O ANISOU 1893 O SER A1038 10717 12792 8265 -108 -641 -34 O ATOM 1894 CB SER A1038 52.575 31.176 49.593 1.00 84.95 C ANISOU 1894 CB SER A1038 10786 13088 8404 -276 -679 132 C ATOM 1895 OG SER A1038 52.774 32.474 49.057 1.00 92.75 O ANISOU 1895 OG SER A1038 11907 13817 9518 -239 -846 -12 O ATOM 1896 N LEU A1039 49.444 32.636 49.542 1.00 82.97 N ANISOU 1896 N LEU A1039 10548 12915 8062 41 -871 -464 N ATOM 1897 CA LEU A1039 48.430 33.296 48.713 1.00 82.57 C ANISOU 1897 CA LEU A1039 10598 12692 8083 136 -945 -622 C ATOM 1898 C LEU A1039 49.059 33.882 47.439 1.00 85.25 C ANISOU 1898 C LEU A1039 11114 12649 8628 86 -1007 -545 C ATOM 1899 O LEU A1039 48.459 33.788 46.366 1.00 84.27 O ANISOU 1899 O LEU A1039 11080 12359 8581 104 -976 -511 O ATOM 1900 CB LEU A1039 47.711 34.404 49.519 1.00 84.43 C ANISOU 1900 CB LEU A1039 10788 13046 8246 274 -1105 -953 C ATOM 1901 CG LEU A1039 46.603 35.194 48.787 1.00 89.48 C ANISOU 1901 CG LEU A1039 11519 13524 8954 385 -1198 -1145 C ATOM 1902 CD1 LEU A1039 45.374 34.330 48.534 1.00 88.82 C ANISOU 1902 CD1 LEU A1039 11386 13582 8780 430 -1070 -1105 C ATOM 1903 CD2 LEU A1039 46.210 36.423 49.570 1.00 94.36 C ANISOU 1903 CD2 LEU A1039 12106 14211 9534 513 -1382 -1471 C ATOM 1904 N ASN A1040 50.278 34.461 47.556 1.00 81.25 N ANISOU 1904 N ASN A1040 10650 12016 8206 21 -1094 -503 N ATOM 1905 CA ASN A1040 50.988 35.062 46.423 1.00 79.94 C ANISOU 1905 CA ASN A1040 10632 11509 8234 -32 -1165 -409 C ATOM 1906 C ASN A1040 51.532 33.992 45.470 1.00 81.89 C ANISOU 1906 C ASN A1040 10928 11655 8533 -134 -1001 -104 C ATOM 1907 O ASN A1040 51.641 34.254 44.271 1.00 80.53 O ANISOU 1907 O ASN A1040 10872 11230 8495 -149 -1019 -25 O ATOM 1908 CB ASN A1040 52.113 35.965 46.906 1.00 78.98 C ANISOU 1908 CB ASN A1040 10525 11301 8182 -72 -1313 -445 C ATOM 1909 CG ASN A1040 51.628 37.237 47.561 1.00 93.54 C ANISOU 1909 CG ASN A1040 12356 13154 10030 38 -1515 -763 C ATOM 1910 OD1 ASN A1040 50.424 37.512 47.649 1.00 84.75 O ANISOU 1910 OD1 ASN A1040 11225 12112 8864 152 -1548 -969 O ATOM 1911 ND2 ASN A1040 52.555 38.051 48.016 1.00 85.62 N ANISOU 1911 ND2 ASN A1040 11363 12073 9095 8 -1662 -812 N ATOM 1912 N ALA A1041 51.844 32.779 45.992 1.00 78.08 N ANISOU 1912 N ALA A1041 10348 11376 7942 -198 -843 65 N ATOM 1913 CA ALA A1041 52.298 31.658 45.155 1.00 76.45 C ANISOU 1913 CA ALA A1041 10176 11094 7777 -284 -683 341 C ATOM 1914 C ALA A1041 51.168 31.197 44.242 1.00 78.90 C ANISOU 1914 C ALA A1041 10532 11348 8100 -230 -613 334 C ATOM 1915 O ALA A1041 51.413 30.830 43.090 1.00 77.03 O ANISOU 1915 O ALA A1041 10386 10925 7957 -267 -552 490 O ATOM 1916 CB ALA A1041 52.779 30.507 46.023 1.00 76.97 C ANISOU 1916 CB ALA A1041 10112 11401 7731 -356 -546 501 C ATOM 1917 N ALA A1042 49.918 31.254 44.751 1.00 75.97 N ANISOU 1917 N ALA A1042 10094 11142 7630 -137 -628 147 N ATOM 1918 CA ALA A1042 48.720 30.945 43.977 1.00 75.24 C ANISOU 1918 CA ALA A1042 10038 11006 7543 -76 -581 109 C ATOM 1919 C ALA A1042 48.509 32.008 42.906 1.00 79.40 C ANISOU 1919 C ALA A1042 10707 11253 8207 -33 -697 13 C ATOM 1920 O ALA A1042 48.183 31.674 41.768 1.00 78.05 O ANISOU 1920 O ALA A1042 10619 10932 8106 -36 -640 101 O ATOM 1921 CB ALA A1042 47.511 30.866 44.895 1.00 76.79 C ANISOU 1921 CB ALA A1042 10117 11464 7593 15 -586 -68 C ATOM 1922 N LYS A1043 48.769 33.291 43.258 1.00 77.27 N ANISOU 1922 N LYS A1043 10465 10909 7987 4 -865 -157 N ATOM 1923 CA LYS A1043 48.676 34.423 42.329 1.00 77.46 C ANISOU 1923 CA LYS A1043 10610 10661 8162 38 -1000 -244 C ATOM 1924 C LYS A1043 49.734 34.300 41.227 1.00 80.58 C ANISOU 1924 C LYS A1043 11101 10825 8691 -55 -971 -9 C ATOM 1925 O LYS A1043 49.467 34.658 40.083 1.00 79.44 O ANISOU 1925 O LYS A1043 11050 10478 8656 -39 -1000 13 O ATOM 1926 CB LYS A1043 48.837 35.760 43.078 1.00 81.47 C ANISOU 1926 CB LYS A1043 11107 11147 8700 91 -1197 -468 C ATOM 1927 CG LYS A1043 47.683 36.085 44.021 1.00 95.50 C ANISOU 1927 CG LYS A1043 12800 13133 10353 210 -1250 -737 C ATOM 1928 CD LYS A1043 47.928 37.378 44.786 1.00107.68 C ANISOU 1928 CD LYS A1043 14330 14653 11929 267 -1452 -968 C ATOM 1929 CE LYS A1043 46.851 37.642 45.810 1.00119.28 C ANISOU 1929 CE LYS A1043 15701 16366 13252 394 -1500 -1237 C ATOM 1930 NZ LYS A1043 47.098 38.903 46.558 1.00129.73 N ANISOU 1930 NZ LYS A1043 17014 17666 14613 460 -1707 -1481 N ATOM 1931 N SER A1044 50.926 33.765 41.573 1.00 77.36 N ANISOU 1931 N SER A1044 10661 10462 8269 -148 -908 175 N ATOM 1932 CA SER A1044 52.025 33.553 40.631 1.00 76.53 C ANISOU 1932 CA SER A1044 10631 10177 8271 -235 -869 417 C ATOM 1933 C SER A1044 51.642 32.525 39.571 1.00 79.62 C ANISOU 1933 C SER A1044 11062 10526 8663 -244 -717 567 C ATOM 1934 O SER A1044 51.734 32.820 38.383 1.00 78.91 O ANISOU 1934 O SER A1044 11064 10238 8681 -245 -739 639 O ATOM 1935 CB SER A1044 53.281 33.098 41.371 1.00 80.54 C ANISOU 1935 CB SER A1044 11081 10782 8740 -327 -822 572 C ATOM 1936 OG SER A1044 54.363 32.886 40.479 1.00 89.28 O ANISOU 1936 OG SER A1044 12253 11728 9940 -405 -782 812 O ATOM 1937 N GLU A1045 51.178 31.326 40.006 1.00 75.89 N ANISOU 1937 N GLU A1045 10512 10247 8074 -247 -573 612 N ATOM 1938 CA GLU A1045 50.774 30.233 39.112 1.00 74.52 C ANISOU 1938 CA GLU A1045 10365 10050 7898 -253 -431 745 C ATOM 1939 C GLU A1045 49.523 30.601 38.297 1.00 78.90 C ANISOU 1939 C GLU A1045 10983 10511 8485 -170 -467 611 C ATOM 1940 O GLU A1045 49.392 30.165 37.151 1.00 77.35 O ANISOU 1940 O GLU A1045 10855 10193 8342 -173 -403 715 O ATOM 1941 CB GLU A1045 50.520 28.948 39.912 1.00 75.50 C ANISOU 1941 CB GLU A1045 10375 10408 7903 -275 -295 811 C ATOM 1942 N LEU A1046 48.610 31.403 38.887 1.00 77.27 N ANISOU 1942 N LEU A1046 10750 10367 8242 -93 -569 379 N ATOM 1943 CA LEU A1046 47.381 31.842 38.219 1.00 77.57 C ANISOU 1943 CA LEU A1046 10839 10326 8306 -11 -612 238 C ATOM 1944 C LEU A1046 47.703 32.780 37.051 1.00 81.66 C ANISOU 1944 C LEU A1046 11473 10579 8976 -11 -708 257 C ATOM 1945 O LEU A1046 47.163 32.598 35.960 1.00 80.80 O ANISOU 1945 O LEU A1046 11427 10361 8912 9 -670 294 O ATOM 1946 CB LEU A1046 46.442 32.542 39.227 1.00 79.05 C ANISOU 1946 CB LEU A1046 10962 10656 8417 76 -709 -17 C ATOM 1947 CG LEU A1046 45.110 33.089 38.682 1.00 84.29 C ANISOU 1947 CG LEU A1046 11669 11256 9100 170 -764 -185 C ATOM 1948 CD1 LEU A1046 44.179 31.960 38.245 1.00 83.60 C ANISOU 1948 CD1 LEU A1046 11566 11248 8948 182 -626 -115 C ATOM 1949 CD2 LEU A1046 44.424 33.950 39.716 1.00 88.13 C ANISOU 1949 CD2 LEU A1046 12094 11870 9522 260 -881 -442 C ATOM 1950 N ASP A1047 48.602 33.765 37.277 1.00 79.07 N ANISOU 1950 N ASP A1047 11162 10152 8728 -37 -836 241 N ATOM 1951 CA ASP A1047 49.000 34.738 36.255 1.00 79.11 C ANISOU 1951 CA ASP A1047 11257 9912 8889 -45 -947 276 C ATOM 1952 C ASP A1047 49.761 34.063 35.111 1.00 81.63 C ANISOU 1952 C ASP A1047 11631 10126 9260 -109 -845 532 C ATOM 1953 O ASP A1047 49.685 34.530 33.977 1.00 81.07 O ANISOU 1953 O ASP A1047 11627 9885 9290 -99 -887 577 O ATOM 1954 CB ASP A1047 49.848 35.863 36.870 1.00 82.25 C ANISOU 1954 CB ASP A1047 11647 10240 9363 -66 -1114 218 C ATOM 1955 CG ASP A1047 49.090 36.749 37.852 1.00 94.92 C ANISOU 1955 CG ASP A1047 13210 11915 10940 16 -1249 -64 C ATOM 1956 OD1 ASP A1047 47.839 36.773 37.791 1.00 95.43 O ANISOU 1956 OD1 ASP A1047 13271 12028 10960 97 -1241 -218 O ATOM 1957 OD2 ASP A1047 49.749 37.412 38.681 1.00103.34 O1- ANISOU 1957 OD2 ASP A1047 14245 12991 12027 2 -1365 -132 O1- ATOM 1958 N LYS A1048 50.468 32.953 35.402 1.00 77.38 N ANISOU 1958 N LYS A1048 11054 9699 8650 -170 -710 698 N ATOM 1959 CA LYS A1048 51.180 32.177 34.379 1.00 76.11 C ANISOU 1959 CA LYS A1048 10935 9465 8520 -219 -600 933 C ATOM 1960 C LYS A1048 50.184 31.401 33.513 1.00 79.17 C ANISOU 1960 C LYS A1048 11352 9850 8878 -174 -496 934 C ATOM 1961 O LYS A1048 50.371 31.295 32.300 1.00 77.80 O ANISOU 1961 O LYS A1048 11240 9554 8765 -176 -467 1049 O ATOM 1962 CB LYS A1048 52.185 31.207 35.028 1.00 77.81 C ANISOU 1962 CB LYS A1048 11093 9802 8668 -291 -491 1096 C ATOM 1963 CG LYS A1048 53.354 31.888 35.718 1.00 86.54 C ANISOU 1963 CG LYS A1048 12176 10895 9809 -349 -584 1141 C ATOM 1964 CD LYS A1048 54.145 30.895 36.549 1.00 94.06 C ANISOU 1964 CD LYS A1048 13057 12004 10677 -415 -471 1273 C ATOM 1965 CE LYS A1048 55.125 31.580 37.463 1.00105.02 C ANISOU 1965 CE LYS A1048 14409 13414 12079 -467 -568 1279 C ATOM 1966 NZ LYS A1048 55.819 30.611 38.352 1.00113.61 N ANISOU 1966 NZ LYS A1048 15415 14674 13078 -532 -455 1400 N ATOM 1967 N ALA A1049 49.118 30.868 34.145 1.00 76.20 N ANISOU 1967 N ALA A1049 10925 9620 8407 -133 -445 808 N ATOM 1968 CA ALA A1049 48.080 30.089 33.474 1.00 75.64 C ANISOU 1968 CA ALA A1049 10873 9563 8304 -92 -353 798 C ATOM 1969 C ALA A1049 47.223 30.964 32.550 1.00 80.92 C ANISOU 1969 C ALA A1049 11613 10090 9044 -31 -437 686 C ATOM 1970 O ALA A1049 46.862 30.525 31.455 1.00 80.11 O ANISOU 1970 O ALA A1049 11561 9912 8964 -16 -377 750 O ATOM 1971 CB ALA A1049 47.199 29.404 34.505 1.00 76.43 C ANISOU 1971 CB ALA A1049 10884 9867 8289 -68 -296 701 C ATOM 1972 N ILE A1050 46.903 32.199 32.983 1.00 78.95 N ANISOU 1972 N ILE A1050 11363 9802 8831 6 -581 517 N ATOM 1973 CA ILE A1050 46.085 33.120 32.189 1.00 79.28 C ANISOU 1973 CA ILE A1050 11464 9708 8952 63 -674 404 C ATOM 1974 C ILE A1050 46.984 33.918 31.220 1.00 83.82 C ANISOU 1974 C ILE A1050 12099 10086 9664 29 -757 521 C ATOM 1975 O ILE A1050 46.728 33.927 30.015 1.00 83.40 O ANISOU 1975 O ILE A1050 12098 9925 9665 42 -739 586 O ATOM 1976 CB ILE A1050 45.236 34.064 33.103 1.00 83.49 C ANISOU 1976 CB ILE A1050 11961 10294 9467 130 -797 156 C ATOM 1977 CG1 ILE A1050 44.385 33.265 34.143 1.00 83.80 C ANISOU 1977 CG1 ILE A1050 11920 10565 9356 166 -716 57 C ATOM 1978 CG2 ILE A1050 44.368 35.023 32.274 1.00 84.72 C ANISOU 1978 CG2 ILE A1050 12173 10301 9714 190 -895 42 C ATOM 1979 CD1 ILE A1050 43.372 32.179 33.555 1.00 88.69 C ANISOU 1979 CD1 ILE A1050 12543 11241 9912 188 -585 99 C ATOM 1980 N GLY A1051 48.019 34.566 31.758 1.00 80.78 N ANISOU 1980 N GLY A1051 11697 9666 9331 -13 -849 553 N ATOM 1981 CA GLY A1051 48.953 35.369 30.971 1.00 80.58 C ANISOU 1981 CA GLY A1051 11711 9467 9440 -52 -944 681 C ATOM 1982 C GLY A1051 48.795 36.862 31.185 1.00 84.64 C ANISOU 1982 C GLY A1051 12230 9859 10072 -26 -1146 535 C ATOM 1983 O GLY A1051 49.104 37.652 30.289 1.00 84.55 O ANISOU 1983 O GLY A1051 12251 9681 10192 -38 -1242 611 O ATOM 1984 N ARG A1052 48.303 37.260 32.385 1.00 81.01 N ANISOU 1984 N ARG A1052 11729 9486 9566 14 -1217 323 N ATOM 1985 CA ARG A1052 48.082 38.667 32.764 1.00 81.55 C ANISOU 1985 CA ARG A1052 11795 9449 9742 53 -1421 142 C ATOM 1986 C ARG A1052 47.977 38.811 34.298 1.00 85.71 C ANISOU 1986 C ARG A1052 12259 10126 10179 83 -1470 -48 C ATOM 1987 O ARG A1052 47.733 37.820 34.992 1.00 84.59 O ANISOU 1987 O ARG A1052 12072 10184 9883 87 -1337 -61 O ATOM 1988 CB ARG A1052 46.803 39.230 32.088 1.00 80.39 C ANISOU 1988 CB ARG A1052 11680 9216 9648 129 -1474 1 C ATOM 1989 CG ARG A1052 45.510 38.566 32.560 1.00 85.75 C ANISOU 1989 CG ARG A1052 12336 10065 10181 200 -1373 -158 C ATOM 1990 CD ARG A1052 44.285 39.389 32.227 1.00 89.84 C ANISOU 1990 CD ARG A1052 12875 10505 10757 283 -1467 -344 C ATOM 1991 NE ARG A1052 43.087 38.868 32.890 1.00 91.50 N ANISOU 1991 NE ARG A1052 13048 10897 10819 357 -1393 -509 N ATOM 1992 CZ ARG A1052 42.682 39.243 34.101 1.00101.99 C ANISOU 1992 CZ ARG A1052 14321 12350 12080 419 -1463 -719 C ATOM 1993 NH1 ARG A1052 43.380 40.133 34.796 1.00 87.96 N ANISOU 1993 NH1 ARG A1052 12524 10525 10371 416 -1612 -803 N ATOM 1994 NH2 ARG A1052 41.586 38.718 34.632 1.00 87.68 N ANISOU 1994 NH2 ARG A1052 12467 10720 10128 486 -1388 -842 N ATOM 1995 N ASN A1053 48.124 40.051 34.815 1.00 83.25 N ANISOU 1995 N ASN A1053 11940 9725 9968 107 -1667 -199 N ATOM 1996 CA ASN A1053 47.984 40.327 36.250 1.00 83.82 C ANISOU 1996 CA ASN A1053 11950 9940 9958 151 -1736 -408 C ATOM 1997 C ASN A1053 46.507 40.291 36.637 1.00 87.59 C ANISOU 1997 C ASN A1053 12403 10542 10337 260 -1717 -642 C ATOM 1998 O ASN A1053 45.698 41.024 36.063 1.00 87.74 O ANISOU 1998 O ASN A1053 12456 10436 10444 320 -1805 -756 O ATOM 1999 CB ASN A1053 48.613 41.679 36.616 1.00 84.96 C ANISOU 1999 CB ASN A1053 12096 9931 10254 149 -1968 -503 C ATOM 2000 CG ASN A1053 50.103 41.759 36.369 1.00104.47 C ANISOU 2000 CG ASN A1053 14579 12295 12818 41 -2001 -270 C ATOM 2001 OD1 ASN A1053 50.661 41.083 35.490 1.00 94.98 O ANISOU 2001 OD1 ASN A1053 13407 11058 11625 -28 -1881 -19 O ATOM 2002 ND2 ASN A1053 50.770 42.641 37.096 1.00 97.88 N ANISOU 2002 ND2 ASN A1053 13724 11401 12065 29 -2176 -352 N ATOM 2003 N THR A1054 46.149 39.401 37.570 1.00 83.42 N ANISOU 2003 N THR A1054 11806 10265 9624 281 -1597 -694 N ATOM 2004 CA THR A1054 44.759 39.206 37.986 1.00 83.32 C ANISOU 2004 CA THR A1054 11754 10411 9492 382 -1559 -885 C ATOM 2005 C THR A1054 44.520 39.708 39.405 1.00 87.81 C ANISOU 2005 C THR A1054 12242 11151 9972 457 -1657 -1127 C ATOM 2006 O THR A1054 43.394 40.087 39.733 1.00 87.39 O ANISOU 2006 O THR A1054 12162 11174 9866 564 -1704 -1342 O ATOM 2007 CB THR A1054 44.385 37.719 37.891 1.00 92.34 C ANISOU 2007 CB THR A1054 12867 11730 10490 356 -1342 -745 C ATOM 2008 OG1 THR A1054 45.274 36.959 38.716 1.00 91.83 O ANISOU 2008 OG1 THR A1054 12737 11823 10331 290 -1261 -633 O ATOM 2009 CG2 THR A1054 44.418 37.195 36.461 1.00 90.45 C ANISOU 2009 CG2 THR A1054 12706 11338 10324 305 -1245 -543 C ATOM 2010 N ASN A1055 45.571 39.635 40.271 1.00 85.11 N ANISOU 2010 N ASN A1055 11852 10890 9595 404 -1677 -1088 N ATOM 2011 CA ASN A1055 45.541 40.006 41.702 1.00 86.38 C ANISOU 2011 CA ASN A1055 11923 11244 9652 466 -1762 -1298 C ATOM 2012 C ASN A1055 44.675 39.002 42.519 1.00 89.51 C ANISOU 2012 C ASN A1055 12217 11967 9826 518 -1615 -1350 C ATOM 2013 O ASN A1055 44.630 39.080 43.751 1.00 90.18 O ANISOU 2013 O ASN A1055 12205 12272 9786 568 -1650 -1496 O ATOM 2014 CB ASN A1055 45.043 41.459 41.904 1.00 89.67 C ANISOU 2014 CB ASN A1055 12359 11543 10170 570 -1985 -1579 C ATOM 2015 CG ASN A1055 45.247 42.007 43.305 1.00120.29 C ANISOU 2015 CG ASN A1055 16155 15580 13971 632 -2106 -1800 C ATOM 2016 OD1 ASN A1055 46.205 41.659 44.012 1.00114.76 O ANISOU 2016 OD1 ASN A1055 15406 14986 13213 566 -2081 -1718 O ATOM 2017 ND2 ASN A1055 44.365 42.905 43.722 1.00115.51 N ANISOU 2017 ND2 ASN A1055 15530 14992 13367 764 -2247 -2090 N ATOM 2018 N GLY A1056 44.051 38.049 41.822 1.00 84.36 N ANISOU 2018 N GLY A1056 11578 11345 9127 501 -1457 -1214 N ATOM 2019 CA GLY A1056 43.216 37.024 42.438 1.00 83.68 C ANISOU 2019 CA GLY A1056 11394 11547 8853 538 -1317 -1219 C ATOM 2020 C GLY A1056 41.897 36.786 41.727 1.00 86.48 C ANISOU 2020 C GLY A1056 11776 11890 9191 600 -1261 -1254 C ATOM 2021 O GLY A1056 41.355 35.682 41.796 1.00 85.38 O ANISOU 2021 O GLY A1056 11581 11921 8939 591 -1115 -1155 O ATOM 2022 N VAL A1057 41.368 37.820 41.032 1.00 82.94 N ANISOU 2022 N VAL A1057 11410 11239 8866 662 -1383 -1389 N ATOM 2023 CA VAL A1057 40.075 37.739 40.338 1.00 82.08 C ANISOU 2023 CA VAL A1057 11331 11105 8749 726 -1346 -1439 C ATOM 2024 C VAL A1057 40.284 37.403 38.847 1.00 84.31 C ANISOU 2024 C VAL A1057 11723 11151 9161 647 -1277 -1232 C ATOM 2025 O VAL A1057 41.092 38.051 38.177 1.00 84.15 O ANISOU 2025 O VAL A1057 11779 10897 9297 597 -1359 -1170 O ATOM 2026 CB VAL A1057 39.249 39.051 40.504 1.00 87.31 C ANISOU 2026 CB VAL A1057 12005 11709 9458 852 -1517 -1721 C ATOM 2027 CG1 VAL A1057 37.858 38.911 39.883 1.00 86.62 C ANISOU 2027 CG1 VAL A1057 11938 11630 9345 921 -1469 -1771 C ATOM 2028 CG2 VAL A1057 39.142 39.454 41.973 1.00 88.77 C ANISOU 2028 CG2 VAL A1057 12083 12130 9517 940 -1600 -1941 C ATOM 2029 N ILE A1058 39.524 36.410 38.328 1.00 79.15 N ANISOU 2029 N ILE A1058 11068 10564 8441 641 -1135 -1129 N ATOM 2030 CA ILE A1058 39.566 36.011 36.908 1.00 77.28 C ANISOU 2030 CA ILE A1058 10927 10133 8304 582 -1062 -951 C ATOM 2031 C ILE A1058 38.154 36.091 36.287 1.00 80.50 C ANISOU 2031 C ILE A1058 11362 10522 8704 655 -1051 -1038 C ATOM 2032 O ILE A1058 37.159 35.953 37.002 1.00 80.52 O ANISOU 2032 O ILE A1058 11292 10718 8585 733 -1040 -1169 O ATOM 2033 CB ILE A1058 40.181 34.594 36.715 1.00 79.03 C ANISOU 2033 CB ILE A1058 11132 10422 8473 487 -894 -705 C ATOM 2034 CG1 ILE A1058 39.368 33.506 37.478 1.00 79.09 C ANISOU 2034 CG1 ILE A1058 11036 10700 8313 512 -780 -702 C ATOM 2035 CG2 ILE A1058 41.668 34.581 37.096 1.00 80.12 C ANISOU 2035 CG2 ILE A1058 11261 10534 8645 405 -906 -591 C ATOM 2036 CD1 ILE A1058 39.655 32.082 37.062 1.00 83.49 C ANISOU 2036 CD1 ILE A1058 11586 11293 8845 432 -621 -472 C ATOM 2037 N THR A1059 38.079 36.283 34.952 1.00 76.14 N ANISOU 2037 N THR A1059 10906 9750 8275 630 -1050 -954 N ATOM 2038 CA THR A1059 36.808 36.366 34.211 1.00 75.57 C ANISOU 2038 CA THR A1059 10869 9635 8210 687 -1038 -1013 C ATOM 2039 C THR A1059 36.133 34.973 34.145 1.00 78.24 C ANISOU 2039 C THR A1059 11172 10132 8425 674 -875 -905 C ATOM 2040 O THR A1059 36.814 33.952 34.278 1.00 76.83 O ANISOU 2040 O THR A1059 10967 10022 8201 602 -771 -742 O ATOM 2041 CB THR A1059 37.058 36.933 32.786 1.00 82.92 C ANISOU 2041 CB THR A1059 11902 10294 9308 652 -1082 -930 C ATOM 2042 OG1 THR A1059 38.043 37.967 32.840 1.00 83.74 O ANISOU 2042 OG1 THR A1059 12028 10250 9540 629 -1217 -951 O ATOM 2043 CG2 THR A1059 35.786 37.461 32.127 1.00 81.17 C ANISOU 2043 CG2 THR A1059 11716 10003 9124 723 -1120 -1041 C ATOM 2044 N LYS A1060 34.794 34.944 33.931 1.00 74.84 N ANISOU 2044 N LYS A1060 10737 9752 7948 742 -862 -993 N ATOM 2045 CA LYS A1060 34.018 33.704 33.794 1.00 73.73 C ANISOU 2045 CA LYS A1060 10563 9743 7707 734 -729 -895 C ATOM 2046 C LYS A1060 34.569 32.860 32.637 1.00 76.39 C ANISOU 2046 C LYS A1060 10971 9940 8113 646 -631 -681 C ATOM 2047 O LYS A1060 34.719 31.646 32.785 1.00 75.41 O ANISOU 2047 O LYS A1060 10808 9920 7925 598 -520 -544 O ATOM 2048 CB LYS A1060 32.522 34.025 33.575 1.00 76.19 C ANISOU 2048 CB LYS A1060 10876 10088 7985 821 -752 -1024 C ATOM 2049 CG LYS A1060 31.599 32.803 33.616 1.00 85.89 C ANISOU 2049 CG LYS A1060 12052 11480 9103 822 -635 -939 C ATOM 2050 CD LYS A1060 31.174 32.352 32.214 1.00 91.63 C ANISOU 2050 CD LYS A1060 12869 12046 9902 787 -574 -825 C ATOM 2051 CE LYS A1060 30.254 31.156 32.261 1.00 97.08 C ANISOU 2051 CE LYS A1060 13506 12884 10497 785 -474 -741 C ATOM 2052 NZ LYS A1060 29.840 30.728 30.901 1.00102.97 N ANISOU 2052 NZ LYS A1060 14340 13471 11311 755 -424 -645 N ATOM 2053 N ASP A1061 34.894 33.516 31.493 1.00 72.57 N ANISOU 2053 N ASP A1061 10585 9225 7763 627 -678 -650 N ATOM 2054 CA ASP A1061 35.479 32.859 30.319 1.00 71.37 C ANISOU 2054 CA ASP A1061 10501 8939 7677 556 -599 -460 C ATOM 2055 C ASP A1061 36.887 32.347 30.631 1.00 73.77 C ANISOU 2055 C ASP A1061 10789 9254 7986 480 -556 -318 C ATOM 2056 O ASP A1061 37.222 31.224 30.253 1.00 72.38 O ANISOU 2056 O ASP A1061 10617 9096 7788 430 -446 -163 O ATOM 2057 CB ASP A1061 35.518 33.821 29.117 1.00 73.60 C ANISOU 2057 CB ASP A1061 10871 8998 8096 560 -674 -465 C ATOM 2058 CG ASP A1061 34.153 34.181 28.553 1.00 86.44 C ANISOU 2058 CG ASP A1061 12523 10592 9728 622 -696 -566 C ATOM 2059 OD1 ASP A1061 33.143 34.016 29.281 1.00 87.93 O ANISOU 2059 OD1 ASP A1061 12659 10931 9820 679 -688 -679 O ATOM 2060 OD2 ASP A1061 34.096 34.659 27.401 1.00 92.25 O1- ANISOU 2060 OD2 ASP A1061 13324 11162 10564 615 -725 -528 O1- ATOM 2061 N GLU A1062 37.695 33.154 31.367 1.00 70.12 N ANISOU 2061 N GLU A1062 10304 8786 7552 475 -647 -377 N ATOM 2062 CA GLU A1062 39.059 32.777 31.774 1.00 69.10 C ANISOU 2062 CA GLU A1062 10154 8675 7425 403 -618 -249 C ATOM 2063 C GLU A1062 39.036 31.546 32.688 1.00 71.46 C ANISOU 2063 C GLU A1062 10366 9189 7597 381 -507 -189 C ATOM 2064 O GLU A1062 39.973 30.750 32.658 1.00 70.17 O ANISOU 2064 O GLU A1062 10194 9036 7432 313 -429 -26 O ATOM 2065 CB GLU A1062 39.773 33.946 32.472 1.00 71.31 C ANISOU 2065 CB GLU A1062 10420 8916 7757 409 -753 -347 C ATOM 2066 CG GLU A1062 40.110 35.093 31.532 1.00 80.61 C ANISOU 2066 CG GLU A1062 11675 9863 9090 406 -868 -351 C ATOM 2067 CD GLU A1062 40.942 36.213 32.129 1.00 97.86 C ANISOU 2067 CD GLU A1062 13849 11979 11354 400 -1015 -422 C ATOM 2068 OE1 GLU A1062 40.903 36.399 33.367 1.00 90.16 O ANISOU 2068 OE1 GLU A1062 12809 11143 10306 431 -1059 -554 O ATOM 2069 OE2 GLU A1062 41.617 36.923 31.349 1.00 89.54 O1- ANISOU 2069 OE2 GLU A1062 12846 10737 10437 366 -1095 -346 O1- ATOM 2070 N ALA A1063 37.948 31.378 33.478 1.00 67.87 N ANISOU 2070 N ALA A1063 9839 8912 7038 440 -502 -310 N ATOM 2071 CA ALA A1063 37.763 30.214 34.346 1.00 67.25 C ANISOU 2071 CA ALA A1063 9658 9055 6841 422 -406 -245 C ATOM 2072 C ALA A1063 37.435 28.986 33.519 1.00 69.52 C ANISOU 2072 C ALA A1063 9967 9315 7132 387 -290 -92 C ATOM 2073 O ALA A1063 37.941 27.900 33.803 1.00 68.58 O ANISOU 2073 O ALA A1063 9797 9278 6982 330 -201 52 O ATOM 2074 CB ALA A1063 36.655 30.479 35.354 1.00 68.83 C ANISOU 2074 CB ALA A1063 9766 9458 6928 504 -445 -413 C ATOM 2075 N GLU A1064 36.597 29.169 32.471 1.00 65.38 N ANISOU 2075 N GLU A1064 9518 8669 6655 421 -297 -124 N ATOM 2076 CA GLU A1064 36.170 28.108 31.560 1.00 64.10 C ANISOU 2076 CA GLU A1064 9389 8461 6506 399 -205 -4 C ATOM 2077 C GLU A1064 37.345 27.626 30.697 1.00 66.67 C ANISOU 2077 C GLU A1064 9779 8642 6910 332 -151 161 C ATOM 2078 O GLU A1064 37.496 26.420 30.487 1.00 65.48 O ANISOU 2078 O GLU A1064 9611 8518 6750 294 -60 292 O ATOM 2079 CB GLU A1064 35.016 28.606 30.672 1.00 65.40 C ANISOU 2079 CB GLU A1064 9619 8530 6700 455 -240 -96 C ATOM 2080 CG GLU A1064 34.349 27.506 29.862 1.00 76.98 C ANISOU 2080 CG GLU A1064 11107 9977 8165 443 -156 0 C ATOM 2081 CD GLU A1064 33.210 27.956 28.968 1.00102.98 C ANISOU 2081 CD GLU A1064 14463 13182 11483 493 -185 -80 C ATOM 2082 OE1 GLU A1064 32.605 29.017 29.253 1.00101.84 O ANISOU 2082 OE1 GLU A1064 14317 13048 11331 551 -267 -230 O ATOM 2083 OE2 GLU A1064 32.887 27.218 28.010 1.00 98.33 O ANISOU 2083 OE2 GLU A1064 13920 12520 10920 478 -129 3 O ATOM 2084 N LYS A1065 38.180 28.568 30.209 1.00 63.13 N ANISOU 2084 N LYS A1065 9398 8045 6544 322 -214 158 N ATOM 2085 CA LYS A1065 39.355 28.244 29.395 1.00 62.34 C ANISOU 2085 CA LYS A1065 9353 7822 6512 267 -172 316 C ATOM 2086 C LYS A1065 40.388 27.506 30.238 1.00 66.33 C ANISOU 2086 C LYS A1065 9793 8429 6981 209 -115 428 C ATOM 2087 O LYS A1065 41.089 26.631 29.730 1.00 65.60 O ANISOU 2087 O LYS A1065 9717 8298 6910 167 -35 579 O ATOM 2088 CB LYS A1065 39.959 29.518 28.769 1.00 65.12 C ANISOU 2088 CB LYS A1065 9771 8009 6960 270 -269 294 C ATOM 2089 CG LYS A1065 39.461 29.808 27.337 1.00 78.71 C ANISOU 2089 CG LYS A1065 11575 9583 8749 295 -279 303 C ATOM 2090 CD LYS A1065 37.978 30.216 27.277 1.00 86.35 C ANISOU 2090 CD LYS A1065 12547 10567 9697 358 -317 150 C ATOM 2091 CE LYS A1065 37.455 30.298 25.868 1.00 93.46 C ANISOU 2091 CE LYS A1065 13519 11341 10650 377 -308 176 C ATOM 2092 NZ LYS A1065 36.003 30.611 25.844 1.00101.30 N ANISOU 2092 NZ LYS A1065 14512 12358 11618 434 -338 38 N ATOM 2093 N LEU A1066 40.431 27.808 31.539 1.00 63.58 N ANISOU 2093 N LEU A1066 9364 8222 6572 211 -153 350 N ATOM 2094 CA LEU A1066 41.303 27.119 32.481 1.00 63.52 C ANISOU 2094 CA LEU A1066 9276 8339 6518 156 -99 449 C ATOM 2095 C LEU A1066 40.692 25.765 32.851 1.00 66.93 C ANISOU 2095 C LEU A1066 9630 8917 6883 145 -3 517 C ATOM 2096 O LEU A1066 41.423 24.817 33.140 1.00 65.99 O ANISOU 2096 O LEU A1066 9464 8852 6758 88 72 659 O ATOM 2097 CB LEU A1066 41.516 27.991 33.739 1.00 64.50 C ANISOU 2097 CB LEU A1066 9336 8576 6596 169 -184 328 C ATOM 2098 CG LEU A1066 42.652 27.586 34.682 1.00 69.33 C ANISOU 2098 CG LEU A1066 9873 9294 7173 105 -151 427 C ATOM 2099 CD1 LEU A1066 43.998 27.601 33.968 1.00 71.46 C ANISOU 2099 CD1 LEU A1066 10214 9408 7531 45 -135 579 C ATOM 2100 CD2 LEU A1066 42.702 28.501 35.883 1.00 70.54 C ANISOU 2100 CD2 LEU A1066 9964 9565 7274 132 -246 279 C ATOM 2101 N PHE A1067 39.344 25.674 32.809 1.00 63.89 N ANISOU 2101 N PHE A1067 9229 8589 6459 198 -10 425 N ATOM 2102 CA PHE A1067 38.591 24.456 33.128 1.00 63.61 C ANISOU 2102 CA PHE A1067 9111 8688 6369 191 62 488 C ATOM 2103 C PHE A1067 38.803 23.380 32.062 1.00 64.70 C ANISOU 2103 C PHE A1067 9303 8704 6574 157 141 634 C ATOM 2104 O PHE A1067 38.936 22.201 32.407 1.00 63.93 O ANISOU 2104 O PHE A1067 9134 8691 6467 116 209 754 O ATOM 2105 CB PHE A1067 37.089 24.772 33.280 1.00 66.03 C ANISOU 2105 CB PHE A1067 9393 9076 6619 261 22 352 C ATOM 2106 CG PHE A1067 36.168 23.575 33.254 1.00 67.41 C ANISOU 2106 CG PHE A1067 9507 9341 6765 258 83 428 C ATOM 2107 CD1 PHE A1067 36.049 22.744 34.361 1.00 70.94 C ANISOU 2107 CD1 PHE A1067 9811 10003 7142 232 120 500 C ATOM 2108 CD2 PHE A1067 35.386 23.304 32.137 1.00 69.00 C ANISOU 2108 CD2 PHE A1067 9785 9418 7012 279 95 430 C ATOM 2109 CE1 PHE A1067 35.175 21.657 34.348 1.00 71.71 C ANISOU 2109 CE1 PHE A1067 9841 10180 7225 225 162 582 C ATOM 2110 CE2 PHE A1067 34.516 22.213 32.123 1.00 71.72 C ANISOU 2110 CE2 PHE A1067 10073 9838 7341 273 137 502 C ATOM 2111 CZ PHE A1067 34.407 21.402 33.233 1.00 70.23 C ANISOU 2111 CZ PHE A1067 9739 9855 7092 246 166 580 C ATOM 2112 N ASN A1068 38.824 23.782 30.767 1.00 59.21 N ANISOU 2112 N ASN A1068 8729 7818 5949 177 126 621 N ATOM 2113 CA ASN A1068 39.038 22.854 29.648 1.00 57.66 C ANISOU 2113 CA ASN A1068 8592 7503 5813 159 192 737 C ATOM 2114 C ASN A1068 40.402 22.186 29.771 1.00 60.12 C ANISOU 2114 C ASN A1068 8886 7805 6152 101 250 888 C ATOM 2115 O ASN A1068 40.523 20.989 29.516 1.00 58.58 O ANISOU 2115 O ASN A1068 8672 7606 5979 77 318 996 O ATOM 2116 CB ASN A1068 38.915 23.579 28.300 1.00 57.01 C ANISOU 2116 CB ASN A1068 8631 7242 5789 195 158 692 C ATOM 2117 CG ASN A1068 37.583 24.259 28.076 1.00 75.74 C ANISOU 2117 CG ASN A1068 11026 9608 8144 252 102 550 C ATOM 2118 OD1 ASN A1068 37.520 25.402 27.608 1.00 68.30 O ANISOU 2118 OD1 ASN A1068 10144 8572 7235 281 35 467 O ATOM 2119 ND2 ASN A1068 36.485 23.580 28.415 1.00 65.95 N ANISOU 2119 ND2 ASN A1068 9732 8468 6858 268 123 528 N ATOM 2120 N GLN A1069 41.417 22.956 30.227 1.00 57.28 N ANISOU 2120 N GLN A1069 8527 7444 5794 77 218 892 N ATOM 2121 CA GLN A1069 42.778 22.470 30.471 1.00 57.04 C ANISOU 2121 CA GLN A1069 8474 7418 5782 19 268 1035 C ATOM 2122 C GLN A1069 42.777 21.361 31.528 1.00 61.43 C ANISOU 2122 C GLN A1069 8908 8137 6296 -23 327 1114 C ATOM 2123 O GLN A1069 43.516 20.393 31.393 1.00 61.03 O ANISOU 2123 O GLN A1069 8839 8072 6277 -64 396 1255 O ATOM 2124 CB GLN A1069 43.690 23.625 30.922 1.00 58.72 C ANISOU 2124 CB GLN A1069 8696 7616 5998 2 203 1008 C ATOM 2125 CG GLN A1069 43.894 24.712 29.869 1.00 72.34 C ANISOU 2125 CG GLN A1069 10528 9172 7785 31 137 967 C ATOM 2126 CD GLN A1069 44.523 25.959 30.453 1.00 92.99 C ANISOU 2126 CD GLN A1069 13142 11778 10414 19 43 911 C ATOM 2127 OE1 GLN A1069 44.029 27.075 30.266 1.00 88.93 O ANISOU 2127 OE1 GLN A1069 12665 11200 9925 59 -51 786 O ATOM 2128 NE2 GLN A1069 45.614 25.798 31.193 1.00 85.81 N ANISOU 2128 NE2 GLN A1069 12185 10927 9492 -35 60 1001 N ATOM 2129 N ASP A1070 41.942 21.505 32.577 1.00 58.95 N ANISOU 2129 N ASP A1070 8502 7987 5911 -10 298 1028 N ATOM 2130 CA ASP A1070 41.826 20.501 33.632 1.00 59.31 C ANISOU 2130 CA ASP A1070 8409 8214 5911 -49 347 1110 C ATOM 2131 C ASP A1070 41.048 19.284 33.135 1.00 62.51 C ANISOU 2131 C ASP A1070 8796 8606 6350 -47 394 1179 C ATOM 2132 O ASP A1070 41.355 18.164 33.539 1.00 62.23 O ANISOU 2132 O ASP A1070 8674 8638 6332 -96 449 1313 O ATOM 2133 CB ASP A1070 41.165 21.093 34.894 1.00 62.21 C ANISOU 2133 CB ASP A1070 8673 8784 6179 -25 295 995 C ATOM 2134 CG ASP A1070 42.151 21.655 35.918 1.00 72.51 C ANISOU 2134 CG ASP A1070 9921 10187 7441 -58 274 993 C ATOM 2135 OD1 ASP A1070 43.256 22.087 35.509 1.00 72.60 O ANISOU 2135 OD1 ASP A1070 10010 10071 7506 -85 268 1033 O ATOM 2136 OD2 ASP A1070 41.808 21.679 37.122 1.00 78.59 O1- ANISOU 2136 OD2 ASP A1070 10566 11172 8123 -54 259 952 O1- ATOM 2137 N VAL A1071 40.060 19.497 32.233 1.00 58.53 N ANISOU 2137 N VAL A1071 8371 8005 5864 6 367 1093 N ATOM 2138 CA VAL A1071 39.276 18.399 31.644 1.00 57.81 C ANISOU 2138 CA VAL A1071 8274 7877 5813 12 398 1147 C ATOM 2139 C VAL A1071 40.163 17.616 30.677 1.00 60.33 C ANISOU 2139 C VAL A1071 8662 8042 6220 -10 451 1262 C ATOM 2140 O VAL A1071 40.305 16.405 30.832 1.00 59.51 O ANISOU 2140 O VAL A1071 8492 7962 6157 -46 494 1379 O ATOM 2141 CB VAL A1071 37.970 18.899 30.951 1.00 61.49 C ANISOU 2141 CB VAL A1071 8807 8288 6269 75 352 1020 C ATOM 2142 CG1 VAL A1071 37.305 17.783 30.143 1.00 60.68 C ANISOU 2142 CG1 VAL A1071 8722 8110 6225 79 378 1080 C ATOM 2143 CG2 VAL A1071 36.998 19.465 31.973 1.00 62.01 C ANISOU 2143 CG2 VAL A1071 8784 8532 6243 104 305 918 C ATOM 2144 N ASP A1072 40.802 18.321 29.712 1.00 56.38 N ANISOU 2144 N ASP A1072 8282 7389 5748 12 442 1232 N ATOM 2145 CA ASP A1072 41.681 17.704 28.714 1.00 55.53 C ANISOU 2145 CA ASP A1072 8244 7146 5709 8 490 1329 C ATOM 2146 C ASP A1072 42.735 16.831 29.381 1.00 57.49 C ANISOU 2146 C ASP A1072 8413 7453 5977 -51 546 1474 C ATOM 2147 O ASP A1072 42.919 15.690 28.970 1.00 56.95 O ANISOU 2147 O ASP A1072 8335 7336 5967 -59 590 1564 O ATOM 2148 CB ASP A1072 42.352 18.769 27.837 1.00 57.43 C ANISOU 2148 CB ASP A1072 8595 7264 5960 35 466 1294 C ATOM 2149 CG ASP A1072 43.064 18.185 26.635 1.00 68.51 C ANISOU 2149 CG ASP A1072 10072 8540 7418 51 510 1377 C ATOM 2150 OD1 ASP A1072 42.426 18.077 25.562 1.00 68.75 O ANISOU 2150 OD1 ASP A1072 10171 8481 7469 100 503 1328 O ATOM 2151 OD2 ASP A1072 44.249 17.798 26.775 1.00 74.56 O1- ANISOU 2151 OD2 ASP A1072 10822 9307 8202 19 553 1491 O1- ATOM 2152 N ALA A1073 43.378 17.346 30.452 1.00 53.03 N ANISOU 2152 N ALA A1073 7784 6998 5368 -92 540 1492 N ATOM 2153 CA ALA A1073 44.393 16.612 31.210 1.00 52.67 C ANISOU 2153 CA ALA A1073 7652 7026 5334 -155 593 1633 C ATOM 2154 C ALA A1073 43.799 15.349 31.853 1.00 56.16 C ANISOU 2154 C ALA A1073 7970 7573 5794 -186 622 1709 C ATOM 2155 O ALA A1073 44.425 14.287 31.805 1.00 54.83 O ANISOU 2155 O ALA A1073 7764 7382 5687 -220 673 1841 O ATOM 2156 CB ALA A1073 44.998 17.509 32.277 1.00 53.70 C ANISOU 2156 CB ALA A1073 7733 7268 5403 -188 569 1615 C ATOM 2157 N ALA A1074 42.568 15.460 32.413 1.00 53.37 N ANISOU 2157 N ALA A1074 7550 7333 5393 -170 583 1632 N ATOM 2158 CA ALA A1074 41.865 14.333 33.039 1.00 53.54 C ANISOU 2158 CA ALA A1074 7441 7470 5433 -199 595 1712 C ATOM 2159 C ALA A1074 41.425 13.318 31.989 1.00 56.69 C ANISOU 2159 C ALA A1074 7889 7725 5927 -180 604 1751 C ATOM 2160 O ALA A1074 41.414 12.118 32.267 1.00 56.59 O ANISOU 2160 O ALA A1074 7782 7740 5980 -219 625 1872 O ATOM 2161 CB ALA A1074 40.660 14.832 33.824 1.00 54.71 C ANISOU 2161 CB ALA A1074 7510 7783 5493 -177 546 1617 C ATOM 2162 N VAL A1075 41.086 13.801 30.769 1.00 52.15 N ANISOU 2162 N VAL A1075 7456 6993 5367 -120 583 1649 N ATOM 2163 CA VAL A1075 40.698 12.955 29.635 1.00 51.37 C ANISOU 2163 CA VAL A1075 7422 6746 5352 -90 586 1661 C ATOM 2164 C VAL A1075 41.937 12.177 29.147 1.00 54.86 C ANISOU 2164 C VAL A1075 7890 7086 5870 -105 637 1770 C ATOM 2165 O VAL A1075 41.855 10.961 28.949 1.00 54.23 O ANISOU 2165 O VAL A1075 7769 6959 5875 -116 647 1849 O ATOM 2166 CB VAL A1075 40.039 13.794 28.500 1.00 54.50 C ANISOU 2166 CB VAL A1075 7955 7024 5727 -21 551 1521 C ATOM 2167 CG1 VAL A1075 39.921 12.992 27.204 1.00 53.92 C ANISOU 2167 CG1 VAL A1075 7963 6790 5734 17 558 1528 C ATOM 2168 CG2 VAL A1075 38.672 14.310 28.934 1.00 54.54 C ANISOU 2168 CG2 VAL A1075 7925 7126 5673 -1 501 1424 C ATOM 2169 N ARG A1076 43.102 12.869 29.040 1.00 51.51 N ANISOU 2169 N ARG A1076 7521 6634 5417 -108 664 1782 N ATOM 2170 CA ARG A1076 44.377 12.244 28.650 1.00 51.62 C ANISOU 2170 CA ARG A1076 7555 6571 5487 -119 717 1892 C ATOM 2171 C ARG A1076 44.791 11.181 29.675 1.00 56.99 C ANISOU 2171 C ARG A1076 8095 7346 6213 -188 750 2034 C ATOM 2172 O ARG A1076 45.369 10.158 29.304 1.00 56.47 O ANISOU 2172 O ARG A1076 8020 7205 6230 -191 782 2125 O ATOM 2173 CB ARG A1076 45.492 13.300 28.502 1.00 51.24 C ANISOU 2173 CB ARG A1076 7575 6504 5390 -117 731 1892 C ATOM 2174 CG ARG A1076 45.238 14.305 27.389 1.00 60.65 C ANISOU 2174 CG ARG A1076 8897 7593 6554 -53 697 1780 C ATOM 2175 CD ARG A1076 46.362 14.357 26.383 1.00 65.11 C ANISOU 2175 CD ARG A1076 9545 8053 7139 -22 730 1836 C ATOM 2176 NE ARG A1076 46.059 15.305 25.315 1.00 70.26 N ANISOU 2176 NE ARG A1076 10304 8623 7768 38 693 1742 N ATOM 2177 CZ ARG A1076 46.777 15.435 24.206 1.00 86.91 C ANISOU 2177 CZ ARG A1076 12490 10647 9884 83 710 1774 C ATOM 2178 NH1 ARG A1076 47.845 14.671 24.005 1.00 74.70 N ANISOU 2178 NH1 ARG A1076 10933 9085 8365 83 765 1887 N ATOM 2179 NH2 ARG A1076 46.424 16.317 23.281 1.00 73.45 N ANISOU 2179 NH2 ARG A1076 10865 8883 8158 132 672 1696 N ATOM 2180 N GLY A1077 44.459 11.429 30.946 1.00 54.55 N ANISOU 2180 N GLY A1077 7670 7206 5849 -238 737 2048 N ATOM 2181 CA GLY A1077 44.731 10.511 32.042 1.00 55.21 C ANISOU 2181 CA GLY A1077 7596 7414 5966 -310 763 2189 C ATOM 2182 C GLY A1077 43.940 9.220 31.945 1.00 60.67 C ANISOU 2182 C GLY A1077 8213 8083 6755 -318 745 2250 C ATOM 2183 O GLY A1077 44.337 8.199 32.515 1.00 60.80 O ANISOU 2183 O GLY A1077 8113 8143 6845 -373 767 2393 O ATOM 2184 N ILE A1078 42.812 9.257 31.221 1.00 57.69 N ANISOU 2184 N ILE A1078 7899 7634 6388 -265 699 2149 N ATOM 2185 CA ILE A1078 41.972 8.086 31.011 1.00 58.36 C ANISOU 2185 CA ILE A1078 7926 7676 6575 -268 665 2197 C ATOM 2186 C ILE A1078 42.533 7.269 29.838 1.00 64.37 C ANISOU 2186 C ILE A1078 8776 8234 7446 -231 678 2215 C ATOM 2187 O ILE A1078 42.745 6.059 29.975 1.00 64.61 O ANISOU 2187 O ILE A1078 8725 8231 7592 -261 676 2329 O ATOM 2188 CB ILE A1078 40.490 8.513 30.778 1.00 61.29 C ANISOU 2188 CB ILE A1078 8321 8066 6901 -228 606 2082 C ATOM 2189 CG1 ILE A1078 39.919 9.232 32.023 1.00 61.68 C ANISOU 2189 CG1 ILE A1078 8261 8339 6838 -255 590 2066 C ATOM 2190 CG2 ILE A1078 39.617 7.309 30.384 1.00 62.32 C ANISOU 2190 CG2 ILE A1078 8409 8121 7148 -227 559 2129 C ATOM 2191 CD1 ILE A1078 38.699 10.102 31.751 1.00 69.64 C ANISOU 2191 CD1 ILE A1078 9327 9368 7766 -201 543 1920 C ATOM 2192 N LEU A1079 42.838 7.949 28.709 1.00 61.75 N ANISOU 2192 N LEU A1079 8605 7778 7079 -162 689 2107 N ATOM 2193 CA LEU A1079 43.348 7.328 27.476 1.00 62.09 C ANISOU 2193 CA LEU A1079 8745 7645 7200 -106 700 2096 C ATOM 2194 C LEU A1079 44.825 6.841 27.607 1.00 67.81 C ANISOU 2194 C LEU A1079 9448 8351 7967 -127 760 2213 C ATOM 2195 O LEU A1079 45.441 6.487 26.596 1.00 67.31 O ANISOU 2195 O LEU A1079 9470 8161 7945 -69 778 2200 O ATOM 2196 CB LEU A1079 43.235 8.323 26.296 1.00 61.67 C ANISOU 2196 CB LEU A1079 8853 7504 7077 -27 695 1957 C ATOM 2197 CG LEU A1079 41.825 8.840 25.956 1.00 66.08 C ANISOU 2197 CG LEU A1079 9453 8058 7596 4 640 1834 C ATOM 2198 CD1 LEU A1079 41.899 10.082 25.093 1.00 65.44 C ANISOU 2198 CD1 LEU A1079 9503 7929 7431 61 641 1720 C ATOM 2199 CD2 LEU A1079 40.987 7.766 25.271 1.00 69.09 C ANISOU 2199 CD2 LEU A1079 9840 8336 8075 34 595 1815 C ATOM 2200 N ARG A1080 45.375 6.804 28.838 1.00 66.30 N ANISOU 2200 N ARG A1080 9138 8291 7761 -205 790 2327 N ATOM 2201 CA ARG A1080 46.744 6.326 29.070 1.00 67.50 C ANISOU 2201 CA ARG A1080 9255 8437 7953 -235 848 2452 C ATOM 2202 C ARG A1080 46.762 5.145 30.079 1.00 74.95 C ANISOU 2202 C ARG A1080 10028 9452 8999 -313 847 2603 C ATOM 2203 O ARG A1080 47.829 4.578 30.345 1.00 74.72 O ANISOU 2203 O ARG A1080 9950 9418 9023 -344 893 2723 O ATOM 2204 CB ARG A1080 47.661 7.473 29.554 1.00 68.17 C ANISOU 2204 CB ARG A1080 9363 8612 7926 -261 891 2464 C ATOM 2205 CG ARG A1080 47.277 8.056 30.913 1.00 80.22 C ANISOU 2205 CG ARG A1080 10780 10324 9376 -331 879 2480 C ATOM 2206 CD ARG A1080 48.215 9.165 31.344 1.00 90.47 C ANISOU 2206 CD ARG A1080 12105 11692 10577 -354 908 2483 C ATOM 2207 NE ARG A1080 49.434 8.639 31.960 1.00 99.12 N ANISOU 2207 NE ARG A1080 13123 12834 11704 -415 965 2639 N ATOM 2208 CZ ARG A1080 50.392 9.401 32.478 1.00114.01 C ANISOU 2208 CZ ARG A1080 15009 14788 13521 -451 993 2678 C ATOM 2209 NH1 ARG A1080 50.284 10.724 32.455 1.00 99.80 N ANISOU 2209 NH1 ARG A1080 13282 13010 11626 -431 961 2570 N ATOM 2210 NH2 ARG A1080 51.466 8.845 33.025 1.00102.52 N ANISOU 2210 NH2 ARG A1080 13479 13375 12099 -508 1046 2829 N ATOM 2211 N ASN A1081 45.578 4.773 30.621 1.00 73.78 N ANISOU 2211 N ASN A1081 9781 9372 8880 -343 793 2609 N ATOM 2212 CA ASN A1081 45.447 3.681 31.587 1.00 74.95 C ANISOU 2212 CA ASN A1081 9748 9602 9130 -421 778 2765 C ATOM 2213 C ASN A1081 44.787 2.451 30.931 1.00 81.84 C ANISOU 2213 C ASN A1081 10605 10328 10161 -395 716 2778 C ATOM 2214 O ASN A1081 43.831 2.600 30.159 1.00 81.66 O ANISOU 2214 O ASN A1081 10668 10224 10135 -338 665 2658 O ATOM 2215 CB ASN A1081 44.643 4.144 32.802 1.00 75.12 C ANISOU 2215 CB ASN A1081 9639 9839 9065 -478 757 2788 C ATOM 2216 CG ASN A1081 44.716 3.204 33.980 1.00 97.12 C ANISOU 2216 CG ASN A1081 12212 12760 11927 -570 754 2976 C ATOM 2217 OD1 ASN A1081 44.096 2.134 33.997 1.00 88.29 O ANISOU 2217 OD1 ASN A1081 11000 11606 10940 -590 701 3056 O ATOM 2218 ND2 ASN A1081 45.441 3.608 35.015 1.00 89.79 N ANISOU 2218 ND2 ASN A1081 11196 12001 10921 -630 804 3054 N ATOM 2219 N ALA A1082 45.293 1.232 31.260 1.00 79.94 N ANISOU 2219 N ALA A1082 10252 10054 10068 -440 713 2926 N ATOM 2220 CA ALA A1082 44.811 -0.037 30.687 1.00 80.82 C ANISOU 2220 CA ALA A1082 10338 10011 10360 -420 642 2950 C ATOM 2221 C ALA A1082 43.464 -0.498 31.298 1.00 85.86 C ANISOU 2221 C ALA A1082 10840 10728 11056 -470 558 3006 C ATOM 2222 O ALA A1082 42.902 -1.501 30.847 1.00 86.00 O ANISOU 2222 O ALA A1082 10831 10616 11229 -458 479 3024 O ATOM 2223 CB ALA A1082 45.858 -1.125 30.881 1.00 82.08 C ANISOU 2223 CB ALA A1082 10415 10106 10665 -452 662 3093 C ATOM 2224 N LYS A1083 42.959 0.220 32.319 1.00 82.60 N ANISOU 2224 N LYS A1083 10335 10530 10520 -522 568 3035 N ATOM 2225 CA LYS A1083 41.692 -0.124 32.969 1.00 82.89 C ANISOU 2225 CA LYS A1083 10228 10680 10586 -567 493 3101 C ATOM 2226 C LYS A1083 40.656 1.000 32.806 1.00 85.79 C ANISOU 2226 C LYS A1083 10678 11124 10796 -522 478 2950 C ATOM 2227 O LYS A1083 39.464 0.755 32.980 1.00 85.98 O ANISOU 2227 O LYS A1083 10629 11198 10843 -532 408 2967 O ATOM 2228 CB LYS A1083 41.914 -0.429 34.460 1.00 85.88 C ANISOU 2228 CB LYS A1083 10379 11286 10964 -670 510 3295 C ATOM 2229 N LEU A1084 41.110 2.228 32.474 1.00 80.79 N ANISOU 2229 N LEU A1084 10190 10497 10011 -473 539 2810 N ATOM 2230 CA LEU A1084 40.217 3.379 32.313 1.00 79.86 C ANISOU 2230 CA LEU A1084 10154 10442 9747 -427 525 2660 C ATOM 2231 C LEU A1084 39.792 3.564 30.855 1.00 83.19 C ANISOU 2231 C LEU A1084 10763 10658 10187 -340 498 2503 C ATOM 2232 O LEU A1084 38.611 3.803 30.594 1.00 82.63 O ANISOU 2232 O LEU A1084 10716 10592 10089 -313 445 2428 O ATOM 2233 CB LEU A1084 40.884 4.671 32.832 1.00 79.27 C ANISOU 2233 CB LEU A1084 10117 10495 9506 -427 590 2598 C ATOM 2234 CG LEU A1084 41.179 4.741 34.339 1.00 84.07 C ANISOU 2234 CG LEU A1084 10542 11347 10053 -504 616 2722 C ATOM 2235 CD1 LEU A1084 41.970 5.991 34.679 1.00 83.54 C ANISOU 2235 CD1 LEU A1084 10539 11362 9841 -495 671 2643 C ATOM 2236 CD2 LEU A1084 39.897 4.696 35.160 1.00 87.09 C ANISOU 2236 CD2 LEU A1084 10778 11920 10392 -526 562 2755 C ATOM 2237 N LYS A1085 40.755 3.465 29.902 1.00 79.56 N ANISOU 2237 N LYS A1085 10433 10029 9767 -294 534 2457 N ATOM 2238 CA LYS A1085 40.489 3.642 28.467 1.00 79.15 C ANISOU 2238 CA LYS A1085 10556 9795 9724 -205 514 2310 C ATOM 2239 C LYS A1085 39.464 2.594 27.934 1.00 83.94 C ANISOU 2239 C LYS A1085 11141 10287 10464 -191 427 2311 C ATOM 2240 O LYS A1085 38.540 2.995 27.226 1.00 83.01 O ANISOU 2240 O LYS A1085 11114 10118 10309 -141 389 2192 O ATOM 2241 CB LYS A1085 41.793 3.586 27.645 1.00 81.42 C ANISOU 2241 CB LYS A1085 10952 9954 10030 -158 569 2288 C ATOM 2242 CG LYS A1085 41.620 4.032 26.190 1.00 94.18 C ANISOU 2242 CG LYS A1085 12747 11426 11613 -60 561 2130 C ATOM 2243 CD LYS A1085 42.940 4.057 25.434 1.00102.26 C ANISOU 2243 CD LYS A1085 13862 12359 12632 -8 618 2120 C ATOM 2244 CE LYS A1085 42.759 4.542 24.014 1.00110.76 C ANISOU 2244 CE LYS A1085 15099 13325 13662 91 610 1972 C ATOM 2245 NZ LYS A1085 44.054 4.636 23.291 1.00118.83 N ANISOU 2245 NZ LYS A1085 16198 14288 14662 147 667 1972 N ATOM 2246 N PRO A1086 39.561 1.270 28.282 1.00 82.11 N ANISOU 2246 N PRO A1086 10786 10015 10396 -236 386 2447 N ATOM 2247 CA PRO A1086 38.556 0.311 27.772 1.00 82.63 C ANISOU 2247 CA PRO A1086 10832 9962 10602 -224 286 2447 C ATOM 2248 C PRO A1086 37.140 0.638 28.259 1.00 86.22 C ANISOU 2248 C PRO A1086 11219 10537 11003 -252 231 2450 C ATOM 2249 O PRO A1086 36.188 0.529 27.482 1.00 85.73 O ANISOU 2249 O PRO A1086 11227 10377 10970 -210 167 2364 O ATOM 2250 CB PRO A1086 39.033 -1.040 28.329 1.00 85.18 C ANISOU 2250 CB PRO A1086 11004 10252 11108 -284 253 2620 C ATOM 2251 CG PRO A1086 40.462 -0.832 28.680 1.00 89.28 C ANISOU 2251 CG PRO A1086 11523 10812 11588 -299 347 2671 C ATOM 2252 CD PRO A1086 40.574 0.584 29.115 1.00 84.05 C ANISOU 2252 CD PRO A1086 10905 10312 10720 -302 420 2609 C ATOM 2253 N VAL A1087 37.009 1.072 29.538 1.00 82.46 N ANISOU 2253 N VAL A1087 10607 10285 10439 -318 257 2544 N ATOM 2254 CA VAL A1087 35.726 1.446 30.143 1.00 82.33 C ANISOU 2254 CA VAL A1087 10505 10426 10349 -340 212 2556 C ATOM 2255 C VAL A1087 35.142 2.672 29.402 1.00 86.15 C ANISOU 2255 C VAL A1087 11157 10889 10688 -266 227 2362 C ATOM 2256 O VAL A1087 33.996 2.618 28.960 1.00 85.59 O ANISOU 2256 O VAL A1087 11111 10781 10628 -242 164 2315 O ATOM 2257 CB VAL A1087 35.867 1.700 31.674 1.00 86.09 C ANISOU 2257 CB VAL A1087 10798 11169 10744 -413 245 2687 C ATOM 2258 CG1 VAL A1087 34.603 2.324 32.257 1.00 85.94 C ANISOU 2258 CG1 VAL A1087 10709 11338 10606 -413 212 2670 C ATOM 2259 CG2 VAL A1087 36.211 0.410 32.409 1.00 86.67 C ANISOU 2259 CG2 VAL A1087 10680 11273 10976 -494 214 2901 C ATOM 2260 N TYR A1088 35.965 3.736 29.201 1.00 82.89 N ANISOU 2260 N TYR A1088 10858 10484 10152 -230 306 2258 N ATOM 2261 CA TYR A1088 35.571 4.973 28.498 1.00 82.42 C ANISOU 2261 CA TYR A1088 10954 10400 9964 -163 322 2082 C ATOM 2262 C TYR A1088 35.072 4.670 27.073 1.00 87.13 C ANISOU 2262 C TYR A1088 11688 10791 10627 -98 279 1978 C ATOM 2263 O TYR A1088 34.152 5.335 26.590 1.00 86.38 O ANISOU 2263 O TYR A1088 11669 10689 10463 -59 255 1870 O ATOM 2264 CB TYR A1088 36.760 5.954 28.447 1.00 83.13 C ANISOU 2264 CB TYR A1088 11132 10499 9955 -143 401 2019 C ATOM 2265 CG TYR A1088 36.431 7.321 27.873 1.00 84.70 C ANISOU 2265 CG TYR A1088 11467 10689 10028 -83 413 1856 C ATOM 2266 CD1 TYR A1088 36.056 8.375 28.703 1.00 86.56 C ANISOU 2266 CD1 TYR A1088 11662 11091 10135 -92 418 1813 C ATOM 2267 CD2 TYR A1088 36.601 7.590 26.517 1.00 85.12 C ANISOU 2267 CD2 TYR A1088 11683 10571 10089 -16 418 1746 C ATOM 2268 CE1 TYR A1088 35.799 9.647 28.188 1.00 86.47 C ANISOU 2268 CE1 TYR A1088 11772 11060 10026 -38 421 1666 C ATOM 2269 CE2 TYR A1088 36.339 8.855 25.990 1.00 85.45 C ANISOU 2269 CE2 TYR A1088 11838 10604 10026 32 425 1612 C ATOM 2270 CZ TYR A1088 35.941 9.882 26.830 1.00 91.86 C ANISOU 2270 CZ TYR A1088 12609 11565 10728 19 424 1573 C ATOM 2271 OH TYR A1088 35.687 11.130 26.315 1.00 91.64 O ANISOU 2271 OH TYR A1088 12688 11516 10616 66 421 1443 O ATOM 2272 N ASP A1089 35.681 3.666 26.408 1.00 84.57 N ANISOU 2272 N ASP A1089 11394 10305 10436 -85 267 2009 N ATOM 2273 CA ASP A1089 35.304 3.256 25.056 1.00 84.67 C ANISOU 2273 CA ASP A1089 11528 10125 10518 -18 222 1908 C ATOM 2274 C ASP A1089 33.963 2.508 25.054 1.00 88.29 C ANISOU 2274 C ASP A1089 11920 10559 11069 -38 123 1944 C ATOM 2275 O ASP A1089 33.252 2.529 24.048 1.00 88.18 O ANISOU 2275 O ASP A1089 12008 10432 11065 15 79 1837 O ATOM 2276 CB ASP A1089 36.403 2.376 24.433 1.00 87.17 C ANISOU 2276 CB ASP A1089 11881 10290 10948 10 234 1926 C ATOM 2277 CG ASP A1089 37.729 3.094 24.214 1.00 99.95 C ANISOU 2277 CG ASP A1089 13582 11916 12478 41 327 1890 C ATOM 2278 OD1 ASP A1089 37.706 4.309 23.895 1.00100.01 O ANISOU 2278 OD1 ASP A1089 13685 11965 12349 75 366 1791 O ATOM 2279 OD2 ASP A1089 38.786 2.431 24.316 1.00107.53 O1- ANISOU 2279 OD2 ASP A1089 14510 12834 13512 34 355 1965 O1- ATOM 2280 N SER A1090 33.615 1.862 26.182 1.00 84.35 N ANISOU 2280 N SER A1090 11241 10173 10633 -116 85 2101 N ATOM 2281 CA SER A1090 32.369 1.104 26.310 1.00 84.33 C ANISOU 2281 CA SER A1090 11149 10165 10729 -146 -18 2172 C ATOM 2282 C SER A1090 31.213 1.978 26.866 1.00 86.07 C ANISOU 2282 C SER A1090 11328 10562 10812 -157 -26 2157 C ATOM 2283 O SER A1090 30.067 1.520 26.913 1.00 85.87 O ANISOU 2283 O SER A1090 11239 10548 10842 -176 -109 2208 O ATOM 2284 CB SER A1090 32.580 -0.116 27.206 1.00 89.21 C ANISOU 2284 CB SER A1090 11576 10817 11502 -225 -66 2372 C ATOM 2285 OG SER A1090 32.961 0.251 28.522 1.00 97.83 O ANISOU 2285 OG SER A1090 12530 12130 12511 -286 -10 2485 O ATOM 2286 N LEU A1091 31.513 3.228 27.271 1.00 80.84 N ANISOU 2286 N LEU A1091 10702 10036 9978 -142 54 2086 N ATOM 2287 CA LEU A1091 30.504 4.137 27.829 1.00 80.10 C ANISOU 2287 CA LEU A1091 10571 10118 9745 -140 50 2055 C ATOM 2288 C LEU A1091 29.924 5.076 26.765 1.00 82.24 C ANISOU 2288 C LEU A1091 11017 10300 9929 -67 55 1873 C ATOM 2289 O LEU A1091 30.495 5.222 25.680 1.00 81.06 O ANISOU 2289 O LEU A1091 11018 9983 9799 -17 79 1768 O ATOM 2290 CB LEU A1091 31.105 4.987 28.976 1.00 79.96 C ANISOU 2290 CB LEU A1091 10479 10310 9593 -162 121 2075 C ATOM 2291 CG LEU A1091 31.565 4.255 30.242 1.00 85.28 C ANISOU 2291 CG LEU A1091 10951 11137 10314 -240 124 2262 C ATOM 2292 CD1 LEU A1091 32.394 5.174 31.122 1.00 85.19 C ANISOU 2292 CD1 LEU A1091 10909 11292 10167 -249 201 2245 C ATOM 2293 CD2 LEU A1091 30.386 3.691 31.023 1.00 88.26 C ANISOU 2293 CD2 LEU A1091 11150 11670 10716 -283 51 2397 C ATOM 2294 N ASP A1092 28.798 5.737 27.103 1.00 78.28 N ANISOU 2294 N ASP A1092 10487 9927 9328 -57 33 1843 N ATOM 2295 CA ASP A1092 28.162 6.762 26.270 1.00 77.18 C ANISOU 2295 CA ASP A1092 10493 9738 9096 6 39 1681 C ATOM 2296 C ASP A1092 28.584 8.158 26.771 1.00 79.52 C ANISOU 2296 C ASP A1092 10819 10160 9236 30 104 1590 C ATOM 2297 O ASP A1092 29.139 8.263 27.864 1.00 79.28 O ANISOU 2297 O ASP A1092 10679 10280 9163 -5 135 1659 O ATOM 2298 CB ASP A1092 26.625 6.604 26.285 1.00 79.25 C ANISOU 2298 CB ASP A1092 10706 10052 9354 5 -33 1703 C ATOM 2299 CG ASP A1092 26.006 6.685 27.670 1.00 87.79 C ANISOU 2299 CG ASP A1092 11604 11386 10364 -33 -49 1813 C ATOM 2300 OD1 ASP A1092 25.246 7.645 27.924 1.00 87.38 O ANISOU 2300 OD1 ASP A1092 11558 11459 10184 1 -43 1740 O ATOM 2301 OD2 ASP A1092 26.290 5.790 28.502 1.00 93.41 O1- ANISOU 2301 OD2 ASP A1092 12162 12181 11151 -92 -68 1974 O1- ATOM 2302 N ALA A1093 28.301 9.222 25.986 1.00 74.58 N ANISOU 2302 N ALA A1093 10332 9473 8531 87 119 1438 N ATOM 2303 CA ALA A1093 28.677 10.615 26.307 1.00 73.53 C ANISOU 2303 CA ALA A1093 10244 9424 8271 117 165 1335 C ATOM 2304 C ALA A1093 28.311 11.025 27.762 1.00 75.92 C ANISOU 2304 C ALA A1093 10398 9972 8476 96 162 1377 C ATOM 2305 O ALA A1093 29.095 11.721 28.414 1.00 74.96 O ANISOU 2305 O ALA A1093 10258 9938 8285 95 200 1350 O ATOM 2306 CB ALA A1093 28.013 11.571 25.328 1.00 73.92 C ANISOU 2306 CB ALA A1093 10430 9390 8267 175 155 1190 C ATOM 2307 N VAL A1094 27.126 10.598 28.253 1.00 71.80 N ANISOU 2307 N VAL A1094 9767 9568 7946 84 113 1443 N ATOM 2308 CA VAL A1094 26.649 10.935 29.600 1.00 71.39 C ANISOU 2308 CA VAL A1094 9560 9776 7789 77 106 1486 C ATOM 2309 C VAL A1094 27.492 10.198 30.661 1.00 74.30 C ANISOU 2309 C VAL A1094 9776 10267 8188 15 126 1634 C ATOM 2310 O VAL A1094 27.963 10.829 31.610 1.00 74.43 O ANISOU 2310 O VAL A1094 9725 10449 8107 16 156 1616 O ATOM 2311 CB VAL A1094 25.133 10.630 29.775 1.00 75.66 C ANISOU 2311 CB VAL A1094 10017 10419 8311 84 46 1536 C ATOM 2312 CG1 VAL A1094 24.623 11.146 31.117 1.00 75.98 C ANISOU 2312 CG1 VAL A1094 9901 10752 8216 96 41 1557 C ATOM 2313 CG2 VAL A1094 24.314 11.224 28.629 1.00 75.07 C ANISOU 2313 CG2 VAL A1094 10095 10205 8224 137 27 1404 C ATOM 2314 N ARG A1095 27.686 8.874 30.493 1.00 69.57 N ANISOU 2314 N ARG A1095 9121 9582 7729 -38 104 1776 N ATOM 2315 CA ARG A1095 28.449 8.069 31.450 1.00 69.15 C ANISOU 2315 CA ARG A1095 8914 9633 7726 -104 118 1935 C ATOM 2316 C ARG A1095 29.970 8.273 31.283 1.00 70.71 C ANISOU 2316 C ARG A1095 9192 9732 7943 -112 184 1902 C ATOM 2317 O ARG A1095 30.717 8.016 32.230 1.00 70.62 O ANISOU 2317 O ARG A1095 9061 9846 7925 -159 212 2001 O ATOM 2318 CB ARG A1095 28.090 6.586 31.332 1.00 70.53 C ANISOU 2318 CB ARG A1095 8993 9742 8062 -158 58 2103 C ATOM 2319 CG ARG A1095 26.705 6.251 31.882 1.00 83.79 C ANISOU 2319 CG ARG A1095 10528 11586 9724 -170 -10 2201 C ATOM 2320 CD ARG A1095 26.496 4.756 31.984 1.00 96.31 C ANISOU 2320 CD ARG A1095 11983 13126 11484 -238 -79 2400 C ATOM 2321 NE ARG A1095 25.129 4.414 32.382 1.00106.62 N ANISOU 2321 NE ARG A1095 13155 14572 12783 -251 -156 2506 N ATOM 2322 CZ ARG A1095 24.170 4.062 31.530 1.00120.90 C ANISOU 2322 CZ ARG A1095 15028 16242 14664 -237 -225 2493 C ATOM 2323 NH1 ARG A1095 24.416 4.013 30.226 1.00107.66 N ANISOU 2323 NH1 ARG A1095 13548 14291 13066 -205 -226 2367 N ATOM 2324 NH2 ARG A1095 22.958 3.760 31.975 1.00107.32 N ANISOU 2324 NH2 ARG A1095 13173 14669 12935 -253 -295 2610 N ATOM 2325 N ARG A1096 30.428 8.747 30.091 1.00 64.99 N ANISOU 2325 N ARG A1096 8661 8797 7235 -68 207 1771 N ATOM 2326 CA ARG A1096 31.848 9.065 29.860 1.00 63.35 C ANISOU 2326 CA ARG A1096 8537 8502 7032 -67 268 1737 C ATOM 2327 C ARG A1096 32.258 10.234 30.733 1.00 64.95 C ANISOU 2327 C ARG A1096 8715 8867 7098 -59 302 1675 C ATOM 2328 O ARG A1096 33.280 10.163 31.418 1.00 64.31 O ANISOU 2328 O ARG A1096 8571 8852 7010 -97 341 1740 O ATOM 2329 CB ARG A1096 32.117 9.388 28.382 1.00 62.69 C ANISOU 2329 CB ARG A1096 8651 8188 6982 -14 278 1616 C ATOM 2330 CG ARG A1096 32.411 8.170 27.527 1.00 72.62 C ANISOU 2330 CG ARG A1096 9943 9262 8385 -21 263 1676 C ATOM 2331 CD ARG A1096 32.640 8.565 26.085 1.00 80.99 C ANISOU 2331 CD ARG A1096 11187 10131 9453 42 274 1549 C ATOM 2332 NE ARG A1096 32.873 7.402 25.231 1.00 88.70 N ANISOU 2332 NE ARG A1096 12199 10939 10564 51 252 1585 N ATOM 2333 CZ ARG A1096 33.095 7.476 23.923 1.00 99.08 C ANISOU 2333 CZ ARG A1096 13656 12091 11898 110 257 1489 C ATOM 2334 NH1 ARG A1096 33.118 8.654 23.312 1.00 77.95 N ANISOU 2334 NH1 ARG A1096 11095 9398 9125 157 283 1370 N ATOM 2335 NH2 ARG A1096 33.298 6.373 23.215 1.00 88.84 N ANISOU 2335 NH2 ARG A1096 12381 10653 10722 125 229 1512 N ATOM 2336 N ALA A1097 31.411 11.295 30.757 1.00 60.04 N ANISOU 2336 N ALA A1097 8130 8313 6368 -9 281 1549 N ATOM 2337 CA ALA A1097 31.605 12.491 31.580 1.00 59.28 C ANISOU 2337 CA ALA A1097 8011 8373 6142 13 294 1461 C ATOM 2338 C ALA A1097 31.528 12.148 33.073 1.00 61.87 C ANISOU 2338 C ALA A1097 8135 8963 6412 -27 293 1570 C ATOM 2339 O ALA A1097 32.194 12.793 33.884 1.00 61.14 O ANISOU 2339 O ALA A1097 7999 8993 6238 -30 316 1541 O ATOM 2340 CB ALA A1097 30.561 13.538 31.230 1.00 59.98 C ANISOU 2340 CB ALA A1097 8173 8469 6149 80 260 1310 C ATOM 2341 N ALA A1098 30.726 11.115 33.430 1.00 57.91 N ANISOU 2341 N ALA A1098 7498 8550 5954 -59 262 1703 N ATOM 2342 CA ALA A1098 30.599 10.636 34.806 1.00 58.09 C ANISOU 2342 CA ALA A1098 7304 8837 5933 -102 257 1839 C ATOM 2343 C ALA A1098 31.935 10.101 35.305 1.00 61.12 C ANISOU 2343 C ALA A1098 7625 9230 6369 -166 303 1952 C ATOM 2344 O ALA A1098 32.329 10.389 36.435 1.00 61.00 O ANISOU 2344 O ALA A1098 7487 9427 6265 -184 323 1983 O ATOM 2345 CB ALA A1098 29.530 9.560 34.890 1.00 59.36 C ANISOU 2345 CB ALA A1098 7341 9051 6161 -129 205 1981 C ATOM 2346 N LEU A1099 32.661 9.374 34.438 1.00 57.20 N ANISOU 2346 N LEU A1099 7218 8504 6012 -195 321 2002 N ATOM 2347 CA LEU A1099 33.996 8.858 34.738 1.00 57.31 C ANISOU 2347 CA LEU A1099 7196 8491 6089 -251 368 2104 C ATOM 2348 C LEU A1099 35.015 10.019 34.784 1.00 62.01 C ANISOU 2348 C LEU A1099 7894 9072 6594 -227 415 1985 C ATOM 2349 O LEU A1099 35.905 10.018 35.636 1.00 61.67 O ANISOU 2349 O LEU A1099 7764 9145 6522 -270 451 2054 O ATOM 2350 CB LEU A1099 34.405 7.805 33.681 1.00 56.97 C ANISOU 2350 CB LEU A1099 7233 8197 6217 -269 366 2168 C ATOM 2351 CG LEU A1099 35.732 7.063 33.912 1.00 61.37 C ANISOU 2351 CG LEU A1099 7746 8709 6864 -326 411 2294 C ATOM 2352 CD1 LEU A1099 35.652 6.147 35.127 1.00 62.25 C ANISOU 2352 CD1 LEU A1099 7623 9015 7013 -403 398 2491 C ATOM 2353 CD2 LEU A1099 36.118 6.256 32.687 1.00 63.18 C ANISOU 2353 CD2 LEU A1099 8091 8673 7243 -314 406 2300 C ATOM 2354 N ILE A1100 34.851 11.025 33.885 1.00 58.64 N ANISOU 2354 N ILE A1100 7643 8510 6126 -162 409 1813 N ATOM 2355 CA ILE A1100 35.710 12.215 33.834 1.00 58.28 C ANISOU 2355 CA ILE A1100 7701 8434 6008 -136 435 1696 C ATOM 2356 C ILE A1100 35.594 12.989 35.163 1.00 64.66 C ANISOU 2356 C ILE A1100 8391 9496 6681 -133 425 1657 C ATOM 2357 O ILE A1100 36.614 13.402 35.721 1.00 64.44 O ANISOU 2357 O ILE A1100 8347 9522 6616 -157 453 1662 O ATOM 2358 CB ILE A1100 35.352 13.108 32.605 1.00 60.48 C ANISOU 2358 CB ILE A1100 8169 8531 6280 -68 415 1533 C ATOM 2359 CG1 ILE A1100 35.660 12.367 31.280 1.00 60.17 C ANISOU 2359 CG1 ILE A1100 8245 8253 6362 -64 428 1566 C ATOM 2360 CG2 ILE A1100 36.090 14.457 32.665 1.00 61.09 C ANISOU 2360 CG2 ILE A1100 8331 8596 6284 -41 420 1415 C ATOM 2361 CD1 ILE A1100 35.087 13.014 30.021 1.00 66.18 C ANISOU 2361 CD1 ILE A1100 9167 8855 7124 0 405 1430 C ATOM 2362 N ASN A1101 34.355 13.119 35.695 1.00 63.00 N ANISOU 2362 N ASN A1101 8087 9454 6395 -104 385 1627 N ATOM 2363 CA ASN A1101 34.072 13.795 36.967 1.00 63.95 C ANISOU 2363 CA ASN A1101 8079 9844 6374 -84 369 1580 C ATOM 2364 C ASN A1101 34.838 13.132 38.117 1.00 69.49 C ANISOU 2364 C ASN A1101 8605 10730 7066 -155 402 1736 C ATOM 2365 O ASN A1101 35.379 13.831 38.975 1.00 69.31 O ANISOU 2365 O ASN A1101 8532 10855 6946 -151 409 1685 O ATOM 2366 CB ASN A1101 32.565 13.779 37.254 1.00 65.20 C ANISOU 2366 CB ASN A1101 8151 10156 6467 -41 323 1558 C ATOM 2367 CG ASN A1101 32.123 14.742 38.335 1.00 94.53 C ANISOU 2367 CG ASN A1101 11770 14130 10018 14 297 1450 C ATOM 2368 OD1 ASN A1101 32.518 14.642 39.506 1.00 91.62 O ANISOU 2368 OD1 ASN A1101 11246 13990 9576 -12 309 1512 O ATOM 2369 ND2 ASN A1101 31.226 15.645 37.982 1.00 87.34 N ANISOU 2369 ND2 ASN A1101 10939 13204 9044 93 257 1288 N ATOM 2370 N MET A1102 34.898 11.783 38.119 1.00 67.27 N ANISOU 2370 N MET A1102 8231 10435 6893 -220 417 1925 N ATOM 2371 CA MET A1102 35.621 11.014 39.132 1.00 68.18 C ANISOU 2371 CA MET A1102 8171 10711 7024 -297 448 2101 C ATOM 2372 C MET A1102 37.121 11.323 39.072 1.00 72.10 C ANISOU 2372 C MET A1102 8748 11106 7541 -328 499 2094 C ATOM 2373 O MET A1102 37.724 11.600 40.108 1.00 72.04 O ANISOU 2373 O MET A1102 8635 11284 7453 -355 519 2122 O ATOM 2374 CB MET A1102 35.378 9.505 38.952 1.00 70.93 C ANISOU 2374 CB MET A1102 8422 11010 7519 -359 441 2302 C ATOM 2375 CG MET A1102 33.954 9.080 39.251 1.00 75.63 C ANISOU 2375 CG MET A1102 8889 11752 8095 -345 386 2358 C ATOM 2376 SD MET A1102 33.738 7.279 39.310 1.00 80.70 S ANISOU 2376 SD MET A1102 9367 12373 8921 -433 359 2626 S ATOM 2377 CE MET A1102 34.602 6.898 40.836 1.00 78.16 C ANISOU 2377 CE MET A1102 8807 12334 8557 -511 398 2803 C ATOM 2378 N VAL A1103 37.705 11.332 37.845 1.00 68.03 N ANISOU 2378 N VAL A1103 8420 10307 7123 -318 517 2052 N ATOM 2379 CA VAL A1103 39.128 11.628 37.609 1.00 67.40 C ANISOU 2379 CA VAL A1103 8433 10108 7069 -342 563 2053 C ATOM 2380 C VAL A1103 39.438 13.092 38.007 1.00 72.26 C ANISOU 2380 C VAL A1103 9105 10794 7558 -302 549 1894 C ATOM 2381 O VAL A1103 40.482 13.359 38.610 1.00 72.09 O ANISOU 2381 O VAL A1103 9052 10834 7505 -339 577 1927 O ATOM 2382 CB VAL A1103 39.529 11.347 36.126 1.00 70.36 C ANISOU 2382 CB VAL A1103 8989 10182 7562 -324 577 2036 C ATOM 2383 CG1 VAL A1103 41.015 11.619 35.890 1.00 69.75 C ANISOU 2383 CG1 VAL A1103 8996 10000 7507 -346 625 2057 C ATOM 2384 CG2 VAL A1103 39.177 9.920 35.719 1.00 70.15 C ANISOU 2384 CG2 VAL A1103 8910 10074 7669 -354 574 2170 C ATOM 2385 N PHE A1104 38.504 14.020 37.701 1.00 69.30 N ANISOU 2385 N PHE A1104 8805 10411 7114 -228 501 1725 N ATOM 2386 CA PHE A1104 38.630 15.455 37.982 1.00 69.65 C ANISOU 2386 CA PHE A1104 8910 10498 7056 -178 467 1552 C ATOM 2387 C PHE A1104 38.866 15.741 39.488 1.00 77.08 C ANISOU 2387 C PHE A1104 9686 11720 7881 -196 463 1560 C ATOM 2388 O PHE A1104 39.529 16.726 39.819 1.00 77.29 O ANISOU 2388 O PHE A1104 9754 11761 7851 -182 446 1462 O ATOM 2389 CB PHE A1104 37.368 16.189 37.508 1.00 71.16 C ANISOU 2389 CB PHE A1104 9172 10664 7202 -96 412 1390 C ATOM 2390 CG PHE A1104 37.552 17.649 37.167 1.00 72.23 C ANISOU 2390 CG PHE A1104 9441 10705 7296 -39 368 1203 C ATOM 2391 CD1 PHE A1104 37.775 18.051 35.857 1.00 74.56 C ANISOU 2391 CD1 PHE A1104 9915 10743 7670 -17 363 1147 C ATOM 2392 CD2 PHE A1104 37.421 18.629 38.143 1.00 74.72 C ANISOU 2392 CD2 PHE A1104 9696 11197 7498 0 324 1080 C ATOM 2393 CE1 PHE A1104 37.899 19.407 35.534 1.00 75.40 C ANISOU 2393 CE1 PHE A1104 10132 10762 7754 33 312 988 C ATOM 2394 CE2 PHE A1104 37.551 19.984 37.820 1.00 77.49 C ANISOU 2394 CE2 PHE A1104 10165 11446 7831 55 268 904 C ATOM 2395 CZ PHE A1104 37.787 20.364 36.518 1.00 74.91 C ANISOU 2395 CZ PHE A1104 10011 10856 7596 67 261 867 C ATOM 2396 N GLN A1105 38.329 14.881 40.390 1.00 75.66 N ANISOU 2396 N GLN A1105 9313 11768 7668 -226 473 1682 N ATOM 2397 CA GLN A1105 38.459 15.081 41.839 1.00 77.12 C ANISOU 2397 CA GLN A1105 9317 12254 7729 -238 470 1697 C ATOM 2398 C GLN A1105 39.714 14.378 42.406 1.00 82.57 C ANISOU 2398 C GLN A1105 9918 12993 8462 -331 527 1872 C ATOM 2399 O GLN A1105 40.557 15.043 43.011 1.00 82.16 O ANISOU 2399 O GLN A1105 9859 13013 8346 -341 530 1825 O ATOM 2400 CB GLN A1105 37.196 14.592 42.576 1.00 79.31 C ANISOU 2400 CB GLN A1105 9411 12791 7933 -217 447 1747 C ATOM 2401 CG GLN A1105 37.129 15.048 44.041 1.00 94.41 C ANISOU 2401 CG GLN A1105 11141 15049 9681 -198 431 1714 C ATOM 2402 CD GLN A1105 35.890 14.562 44.767 1.00110.85 C ANISOU 2402 CD GLN A1105 13026 17411 11680 -173 408 1780 C ATOM 2403 OE1 GLN A1105 35.158 13.679 44.299 1.00105.84 O ANISOU 2403 OE1 GLN A1105 12362 16725 11127 -192 406 1897 O ATOM 2404 NE2 GLN A1105 35.640 15.120 45.942 1.00101.26 N ANISOU 2404 NE2 GLN A1105 11664 16510 10300 -127 385 1710 N ATOM 2405 N MET A1106 39.819 13.038 42.244 1.00 80.63 N ANISOU 2405 N MET A1106 9597 12711 8328 -399 566 2073 N ATOM 2406 CA MET A1106 40.945 12.271 42.793 1.00 81.44 C ANISOU 2406 CA MET A1106 9598 12863 8482 -491 621 2256 C ATOM 2407 C MET A1106 42.151 12.229 41.803 1.00 86.00 C ANISOU 2407 C MET A1106 10353 13151 9173 -518 661 2276 C ATOM 2408 O MET A1106 43.200 12.804 42.104 1.00 85.72 O ANISOU 2408 O MET A1106 10351 13117 9102 -539 681 2256 O ATOM 2409 CB MET A1106 40.511 10.842 43.213 1.00 84.36 C ANISOU 2409 CB MET A1106 9777 13351 8926 -553 635 2475 C ATOM 2410 CG MET A1106 39.637 10.123 42.187 1.00 87.98 C ANISOU 2410 CG MET A1106 10300 13626 9504 -535 609 2503 C ATOM 2411 SD MET A1106 38.626 8.793 42.896 1.00 93.33 S ANISOU 2411 SD MET A1106 10720 14513 10227 -584 582 2718 S ATOM 2412 CE MET A1106 37.455 9.740 43.812 1.00 90.81 C ANISOU 2412 CE MET A1106 10292 14509 9701 -509 536 2590 C ATOM 2413 N GLY A1107 41.980 11.576 40.650 1.00 82.91 N ANISOU 2413 N GLY A1107 10067 12525 8910 -513 668 2312 N ATOM 2414 CA GLY A1107 43.033 11.462 39.643 1.00 82.41 C ANISOU 2414 CA GLY A1107 10162 12203 8948 -525 705 2334 C ATOM 2415 C GLY A1107 43.011 10.159 38.864 1.00 86.75 C ANISOU 2415 C GLY A1107 10720 12589 9651 -549 724 2463 C ATOM 2416 O GLY A1107 41.990 9.463 38.839 1.00 86.52 O ANISOU 2416 O GLY A1107 10616 12594 9665 -545 693 2504 O ATOM 2417 N GLU A1108 44.149 9.819 38.215 1.00 83.28 N ANISOU 2417 N GLU A1108 10371 11971 9300 -571 769 2527 N ATOM 2418 CA GLU A1108 44.292 8.598 37.404 1.00 83.00 C ANISOU 2418 CA GLU A1108 10358 11760 9419 -583 785 2634 C ATOM 2419 C GLU A1108 44.323 7.344 38.283 1.00 87.09 C ANISOU 2419 C GLU A1108 10668 12407 10014 -662 797 2835 C ATOM 2420 O GLU A1108 43.518 6.434 38.078 1.00 86.40 O ANISOU 2420 O GLU A1108 10519 12289 10020 -666 762 2896 O ATOM 2421 CB GLU A1108 45.570 8.656 36.548 1.00 83.87 C ANISOU 2421 CB GLU A1108 10610 11674 9584 -576 831 2645 C ATOM 2422 CG GLU A1108 45.622 9.811 35.567 1.00 94.74 C ANISOU 2422 CG GLU A1108 12183 12910 10905 -502 816 2475 C ATOM 2423 CD GLU A1108 46.946 9.959 34.838 1.00117.72 C ANISOU 2423 CD GLU A1108 15211 15668 13849 -496 861 2505 C ATOM 2424 OE1 GLU A1108 47.667 8.945 34.689 1.00113.37 O ANISOU 2424 OE1 GLU A1108 14627 15056 13393 -526 903 2639 O ATOM 2425 OE2 GLU A1108 47.249 11.088 34.390 1.00113.94 O1- ANISOU 2425 OE2 GLU A1108 14854 15131 13306 -457 849 2399 O1- ATOM 2426 N THR A1109 45.270 7.292 39.250 1.00 84.03 N ANISOU 2426 N THR A1109 10171 12162 9597 -729 842 2947 N ATOM 2427 CA THR A1109 45.451 6.148 40.152 1.00 84.49 C ANISOU 2427 CA THR A1109 10016 12356 9728 -814 858 3158 C ATOM 2428 C THR A1109 44.279 6.063 41.157 1.00 89.28 C ANISOU 2428 C THR A1109 10436 13221 10267 -829 813 3189 C ATOM 2429 O THR A1109 43.986 4.979 41.670 1.00 89.66 O ANISOU 2429 O THR A1109 10304 13359 10404 -887 800 3364 O ATOM 2430 CB THR A1109 46.810 6.248 40.876 1.00 92.22 C ANISOU 2430 CB THR A1109 10938 13421 10678 -879 922 3260 C ATOM 2431 OG1 THR A1109 47.797 6.738 39.965 1.00 90.72 O ANISOU 2431 OG1 THR A1109 10942 13026 10501 -846 956 3190 O ATOM 2432 CG2 THR A1109 47.267 4.908 41.462 1.00 90.95 C ANISOU 2432 CG2 THR A1109 10594 13319 10643 -968 949 3496 C ATOM 2433 N GLY A1110 43.620 7.199 41.403 1.00 85.64 N ANISOU 2433 N GLY A1110 10011 12874 9652 -773 784 3024 N ATOM 2434 CA GLY A1110 42.466 7.279 42.294 1.00 85.96 C ANISOU 2434 CA GLY A1110 9887 13173 9600 -766 740 3027 C ATOM 2435 C GLY A1110 41.283 6.471 41.797 1.00 89.02 C ANISOU 2435 C GLY A1110 10242 13499 10084 -751 687 3071 C ATOM 2436 O GLY A1110 40.722 5.666 42.545 1.00 88.80 O ANISOU 2436 O GLY A1110 10006 13649 10086 -798 662 3228 O ATOM 2437 N VAL A1111 40.920 6.653 40.511 1.00 84.94 N ANISOU 2437 N VAL A1111 9924 12727 9623 -688 664 2943 N ATOM 2438 CA VAL A1111 39.809 5.929 39.885 1.00 85.24 C ANISOU 2438 CA VAL A1111 9958 12669 9759 -669 607 2967 C ATOM 2439 C VAL A1111 40.265 4.502 39.524 1.00 90.01 C ANISOU 2439 C VAL A1111 10513 13121 10566 -728 607 3145 C ATOM 2440 O VAL A1111 39.461 3.566 39.594 1.00 90.15 O ANISOU 2440 O VAL A1111 10412 13155 10684 -753 552 3260 O ATOM 2441 CB VAL A1111 39.248 6.687 38.650 1.00 88.63 C ANISOU 2441 CB VAL A1111 10615 12895 10167 -579 582 2759 C ATOM 2442 CG1 VAL A1111 38.013 5.986 38.086 1.00 88.68 C ANISOU 2442 CG1 VAL A1111 10608 12826 10261 -560 517 2781 C ATOM 2443 CG2 VAL A1111 38.917 8.132 39.008 1.00 88.43 C ANISOU 2443 CG2 VAL A1111 10640 13001 9958 -521 578 2581 C ATOM 2444 N ALA A1112 41.571 4.327 39.205 1.00 86.85 N ANISOU 2444 N ALA A1112 10189 12582 10229 -750 663 3177 N ATOM 2445 CA ALA A1112 42.146 3.008 38.912 1.00 87.26 C ANISOU 2445 CA ALA A1112 10192 12490 10474 -800 666 3338 C ATOM 2446 C ALA A1112 42.171 2.125 40.177 1.00 92.77 C ANISOU 2446 C ALA A1112 10619 13407 11222 -896 660 3569 C ATOM 2447 O ALA A1112 42.296 0.901 40.077 1.00 92.41 O ANISOU 2447 O ALA A1112 10484 13272 11357 -944 635 3727 O ATOM 2448 CB ALA A1112 43.552 3.160 38.347 1.00 87.39 C ANISOU 2448 CB ALA A1112 10348 12340 10518 -794 733 3313 C ATOM 2449 N GLY A1113 42.005 2.763 41.345 1.00 90.61 N ANISOU 2449 N GLY A1113 10212 13425 10791 -919 675 3584 N ATOM 2450 CA GLY A1113 41.951 2.094 42.641 1.00 91.67 C ANISOU 2450 CA GLY A1113 10070 13825 10935 -1005 671 3799 C ATOM 2451 C GLY A1113 40.574 1.560 42.998 1.00 97.19 C ANISOU 2451 C GLY A1113 10605 14663 11660 -1013 591 3886 C ATOM 2452 O GLY A1113 40.301 1.281 44.170 1.00 97.58 O ANISOU 2452 O GLY A1113 10413 15001 11664 -1069 581 4041 O ATOM 2453 N PHE A1114 39.687 1.424 41.985 1.00 94.32 N ANISOU 2453 N PHE A1114 10366 14106 11366 -957 532 3794 N ATOM 2454 CA PHE A1114 38.341 0.864 42.141 1.00 95.30 C ANISOU 2454 CA PHE A1114 10355 14318 11536 -962 446 3880 C ATOM 2455 C PHE A1114 38.073 -0.139 41.009 1.00 99.17 C ANISOU 2455 C PHE A1114 10932 14500 12250 -958 383 3909 C ATOM 2456 O PHE A1114 37.074 -0.020 40.292 1.00 98.78 O ANISOU 2456 O PHE A1114 10976 14348 12207 -903 326 3810 O ATOM 2457 CB PHE A1114 37.268 1.980 42.167 1.00 97.33 C ANISOU 2457 CB PHE A1114 10672 14707 11602 -880 425 3702 C ATOM 2458 CG PHE A1114 37.430 3.003 43.270 1.00 99.57 C ANISOU 2458 CG PHE A1114 10871 15297 11663 -868 471 3646 C ATOM 2459 CD1 PHE A1114 37.226 2.655 44.602 1.00103.97 C ANISOU 2459 CD1 PHE A1114 11151 16191 12163 -925 464 3826 C ATOM 2460 CD2 PHE A1114 37.711 4.332 42.972 1.00101.45 C ANISOU 2460 CD2 PHE A1114 11299 15498 11750 -794 510 3410 C ATOM 2461 CE1 PHE A1114 37.367 3.603 45.620 1.00105.32 C ANISOU 2461 CE1 PHE A1114 11241 16656 12119 -903 501 3758 C ATOM 2462 CE2 PHE A1114 37.838 5.283 43.991 1.00104.78 C ANISOU 2462 CE2 PHE A1114 11643 16195 11973 -775 538 3342 C ATOM 2463 CZ PHE A1114 37.666 4.912 45.308 1.00103.86 C ANISOU 2463 CZ PHE A1114 11256 16414 11792 -826 534 3508 C ATOM 2464 N THR A1115 38.990 -1.125 40.846 1.00 95.99 N ANISOU 2464 N THR A1115 10497 13945 12029 -1014 392 4041 N ATOM 2465 CA THR A1115 38.938 -2.159 39.797 1.00 96.08 C ANISOU 2465 CA THR A1115 10585 13651 12269 -1008 331 4066 C ATOM 2466 C THR A1115 37.620 -2.939 39.860 1.00101.14 C ANISOU 2466 C THR A1115 11088 14320 13022 -1030 215 4182 C ATOM 2467 O THR A1115 37.051 -3.270 38.815 1.00100.33 O ANISOU 2467 O THR A1115 11111 13985 13026 -984 149 4099 O ATOM 2468 CB THR A1115 40.142 -3.114 39.933 1.00105.05 C ANISOU 2468 CB THR A1115 11651 14689 13575 -1073 357 4222 C ATOM 2469 OG1 THR A1115 41.324 -2.355 40.198 1.00104.97 O ANISOU 2469 OG1 THR A1115 11715 14734 13437 -1071 466 4162 O ATOM 2470 CG2 THR A1115 40.348 -3.982 38.691 1.00103.62 C ANISOU 2470 CG2 THR A1115 11604 14160 13608 -1039 308 4185 C ATOM 2471 N ASN A1116 37.134 -3.219 41.088 1.00 99.13 N ANISOU 2471 N ASN A1116 10568 14361 12738 -1099 187 4377 N ATOM 2472 CA ASN A1116 35.879 -3.931 41.325 1.00100.26 C ANISOU 2472 CA ASN A1116 10538 14582 12973 -1130 74 4526 C ATOM 2473 C ASN A1116 34.688 -3.183 40.693 1.00104.84 C ANISOU 2473 C ASN A1116 11260 15138 13438 -1045 38 4343 C ATOM 2474 O ASN A1116 33.812 -3.821 40.108 1.00104.90 O ANISOU 2474 O ASN A1116 11269 15007 13582 -1040 -62 4377 O ATOM 2475 CB ASN A1116 35.649 -4.142 42.836 1.00102.00 C ANISOU 2475 CB ASN A1116 10443 15182 13131 -1210 69 4760 C ATOM 2476 CG ASN A1116 35.791 -2.896 43.696 1.00124.05 C ANISOU 2476 CG ASN A1116 13213 18281 15638 -1180 159 4663 C ATOM 2477 OD1 ASN A1116 36.352 -1.871 43.285 1.00117.88 O ANISOU 2477 OD1 ASN A1116 12646 17425 14718 -1115 238 4439 O ATOM 2478 ND2 ASN A1116 35.344 -2.988 44.939 1.00116.49 N ANISOU 2478 ND2 ASN A1116 11984 17682 14595 -1228 144 4840 N ATOM 2479 N SER A1117 34.691 -1.834 40.761 1.00101.30 N ANISOU 2479 N SER A1117 10937 14804 12750 -976 114 4144 N ATOM 2480 CA SER A1117 33.630 -1.008 40.179 1.00100.93 C ANISOU 2480 CA SER A1117 11030 14739 12580 -891 89 3959 C ATOM 2481 C SER A1117 33.756 -0.939 38.650 1.00104.55 C ANISOU 2481 C SER A1117 11766 14834 13125 -827 82 3769 C ATOM 2482 O SER A1117 32.777 -1.195 37.946 1.00104.22 O ANISOU 2482 O SER A1117 11780 14670 13149 -797 5 3734 O ATOM 2483 CB SER A1117 33.659 0.399 40.771 1.00103.87 C ANISOU 2483 CB SER A1117 11437 15343 12686 -839 164 3807 C ATOM 2484 OG SER A1117 33.425 0.378 42.169 1.00113.05 O ANISOU 2484 OG SER A1117 12337 16869 13747 -884 165 3965 O ATOM 2485 N LEU A1118 34.972 -0.614 38.142 1.00100.78 N ANISOU 2485 N LEU A1118 11454 14194 12645 -805 160 3657 N ATOM 2486 CA LEU A1118 35.263 -0.474 36.704 1.00100.07 C ANISOU 2486 CA LEU A1118 11622 13785 12613 -736 167 3475 C ATOM 2487 C LEU A1118 34.920 -1.749 35.918 1.00105.05 C ANISOU 2487 C LEU A1118 12253 14177 13483 -749 72 3550 C ATOM 2488 O LEU A1118 34.394 -1.655 34.806 1.00104.10 O ANISOU 2488 O LEU A1118 12301 13860 13392 -685 34 3408 O ATOM 2489 CB LEU A1118 36.747 -0.117 36.486 1.00 99.44 C ANISOU 2489 CB LEU A1118 11662 13613 12509 -726 262 3407 C ATOM 2490 CG LEU A1118 37.194 1.271 36.961 1.00103.57 C ANISOU 2490 CG LEU A1118 12246 14298 12808 -697 348 3283 C ATOM 2491 CD1 LEU A1118 38.687 1.302 37.218 1.00103.43 C ANISOU 2491 CD1 LEU A1118 12241 14265 12794 -728 429 3322 C ATOM 2492 CD2 LEU A1118 36.800 2.353 35.960 1.00105.34 C ANISOU 2492 CD2 LEU A1118 12700 14401 12924 -603 357 3044 C ATOM 2493 N ARG A1119 35.224 -2.938 36.495 1.00103.15 N ANISOU 2493 N ARG A1119 11822 13952 13419 -831 29 3772 N ATOM 2494 CA ARG A1119 34.935 -4.230 35.862 1.00103.99 C ANISOU 2494 CA ARG A1119 11902 13831 13778 -850 -79 3859 C ATOM 2495 C ARG A1119 33.425 -4.410 35.674 1.00109.42 C ANISOU 2495 C ARG A1119 12547 14535 14492 -842 -187 3876 C ATOM 2496 O ARG A1119 32.984 -4.858 34.611 1.00109.25 O ANISOU 2496 O ARG A1119 12646 14270 14595 -802 -262 3796 O ATOM 2497 CB ARG A1119 35.514 -5.382 36.696 1.00104.85 C ANISOU 2497 CB ARG A1119 11782 13989 14066 -949 -109 4114 C ATOM 2498 N MET A1120 32.633 -4.001 36.688 1.00106.67 N ANISOU 2498 N MET A1120 12033 14484 14012 -873 -193 3971 N ATOM 2499 CA MET A1120 31.169 -4.077 36.658 1.00107.04 C ANISOU 2499 CA MET A1120 12018 14599 14055 -867 -288 4008 C ATOM 2500 C MET A1120 30.584 -3.020 35.697 1.00109.73 C ANISOU 2500 C MET A1120 12600 14845 14246 -768 -263 3748 C ATOM 2501 O MET A1120 29.489 -3.219 35.167 1.00109.48 O ANISOU 2501 O MET A1120 12596 14740 14262 -748 -349 3733 O ATOM 2502 CB MET A1120 30.591 -3.904 38.074 1.00110.07 C ANISOU 2502 CB MET A1120 12141 15361 14318 -920 -292 4188 C ATOM 2503 CG MET A1120 30.901 -5.079 38.999 1.00114.71 C ANISOU 2503 CG MET A1120 12454 16052 15078 -1028 -345 4484 C ATOM 2504 SD MET A1120 30.649 -4.699 40.754 1.00119.45 S ANISOU 2504 SD MET A1120 12750 17145 15489 -1082 -307 4676 S ATOM 2505 CE MET A1120 31.015 -6.279 41.475 1.00117.47 C ANISOU 2505 CE MET A1120 12204 16919 15509 -1211 -391 5027 C ATOM 2506 N LEU A1121 31.330 -1.913 35.457 1.00104.94 N ANISOU 2506 N LEU A1121 12166 14235 13472 -709 -149 3554 N ATOM 2507 CA LEU A1121 30.924 -0.852 34.526 1.00103.71 C ANISOU 2507 CA LEU A1121 12240 13983 13181 -617 -119 3310 C ATOM 2508 C LEU A1121 31.151 -1.286 33.079 1.00106.80 C ANISOU 2508 C LEU A1121 12832 14035 13713 -570 -149 3188 C ATOM 2509 O LEU A1121 30.323 -0.994 32.212 1.00105.74 O ANISOU 2509 O LEU A1121 12827 13791 13558 -515 -188 3063 O ATOM 2510 CB LEU A1121 31.695 0.454 34.810 1.00102.92 C ANISOU 2510 CB LEU A1121 12237 13996 12874 -577 -1 3164 C ATOM 2511 CG LEU A1121 31.285 1.230 36.065 1.00107.86 C ANISOU 2511 CG LEU A1121 12714 14961 13309 -587 29 3201 C ATOM 2512 CD1 LEU A1121 32.361 2.214 36.473 1.00107.36 C ANISOU 2512 CD1 LEU A1121 12711 14984 13099 -569 132 3100 C ATOM 2513 CD2 LEU A1121 29.957 1.945 35.864 1.00110.26 C ANISOU 2513 CD2 LEU A1121 13060 15342 13492 -529 -7 3098 C ATOM 2514 N GLN A1122 32.279 -1.988 32.817 1.00103.48 N ANISOU 2514 N GLN A1122 12432 13456 13430 -588 -132 3225 N ATOM 2515 CA GLN A1122 32.627 -2.494 31.484 1.00103.08 C ANISOU 2515 CA GLN A1122 12555 13097 13515 -536 -161 3113 C ATOM 2516 C GLN A1122 31.725 -3.673 31.097 1.00107.43 C ANISOU 2516 C GLN A1122 13038 13508 14273 -559 -302 3204 C ATOM 2517 O GLN A1122 31.538 -3.938 29.907 1.00106.99 O ANISOU 2517 O GLN A1122 13135 13219 14299 -500 -349 3077 O ATOM 2518 CB GLN A1122 34.104 -2.915 31.436 1.00104.36 C ANISOU 2518 CB GLN A1122 12736 13160 13757 -546 -102 3139 C ATOM 2519 N GLN A1123 31.148 -4.363 32.107 1.00104.46 N ANISOU 2519 N GLN A1123 12424 13284 13980 -643 -375 3428 N ATOM 2520 CA GLN A1123 30.233 -5.493 31.910 1.00105.13 C ANISOU 2520 CA GLN A1123 12409 13262 14274 -680 -525 3553 C ATOM 2521 C GLN A1123 28.773 -4.988 31.716 1.00108.17 C ANISOU 2521 C GLN A1123 12816 13722 14561 -655 -578 3507 C ATOM 2522 O GLN A1123 27.850 -5.800 31.570 1.00108.86 O ANISOU 2522 O GLN A1123 12821 13742 14800 -686 -709 3613 O ATOM 2523 CB GLN A1123 30.324 -6.463 33.108 1.00107.70 C ANISOU 2523 CB GLN A1123 12450 13728 14741 -788 -583 3841 C ATOM 2524 CG GLN A1123 29.946 -7.906 32.767 1.00124.25 C ANISOU 2524 CG GLN A1123 14455 15620 17136 -831 -744 3978 C ATOM 2525 CD GLN A1123 29.894 -8.791 33.990 1.00143.04 C ANISOU 2525 CD GLN A1123 16532 18165 19653 -944 -810 4284 C ATOM 2526 OE1 GLN A1123 30.860 -8.902 34.757 1.00137.93 O ANISOU 2526 OE1 GLN A1123 15777 17627 19005 -990 -740 4388 O ATOM 2527 NE2 GLN A1123 28.783 -9.488 34.164 1.00136.68 N ANISOU 2527 NE2 GLN A1123 15578 17374 18982 -993 -954 4447 N ATOM 2528 N LYS A1124 28.584 -3.633 31.694 1.00102.53 N ANISOU 2528 N LYS A1124 12217 13140 13600 -599 -481 3348 N ATOM 2529 CA LYS A1124 27.294 -2.934 31.504 1.00101.49 C ANISOU 2529 CA LYS A1124 12128 13094 13339 -563 -507 3276 C ATOM 2530 C LYS A1124 26.319 -3.194 32.690 1.00105.93 C ANISOU 2530 C LYS A1124 12436 13928 13883 -629 -569 3497 C ATOM 2531 O LYS A1124 25.105 -3.027 32.540 1.00105.44 O ANISOU 2531 O LYS A1124 12366 13917 13782 -615 -631 3500 O ATOM 2532 CB LYS A1124 26.622 -3.317 30.155 1.00103.34 C ANISOU 2532 CB LYS A1124 12519 13059 13687 -516 -595 3162 C ATOM 2533 CG LYS A1124 27.519 -3.165 28.918 1.00110.39 C ANISOU 2533 CG LYS A1124 13646 13695 14602 -443 -546 2953 C ATOM 2534 CD LYS A1124 27.908 -1.710 28.625 1.00116.81 C ANISOU 2534 CD LYS A1124 14629 14571 15184 -373 -416 2752 C ATOM 2535 CE LYS A1124 28.749 -1.585 27.376 1.00123.37 C ANISOU 2535 CE LYS A1124 15674 15167 16036 -300 -374 2567 C ATOM 2536 NZ LYS A1124 30.041 -2.316 27.496 1.00131.02 N ANISOU 2536 NZ LYS A1124 16609 16048 17125 -320 -350 2629 N ATOM 2537 N ARG A1125 26.862 -3.546 33.870 1.00103.28 N ANISOU 2537 N ARG A1125 11893 13787 13562 -698 -549 3684 N ATOM 2538 CA ARG A1125 26.059 -3.777 35.074 1.00104.25 C ANISOU 2538 CA ARG A1125 11751 14208 13652 -760 -599 3909 C ATOM 2539 C ARG A1125 26.202 -2.567 36.008 1.00107.35 C ANISOU 2539 C ARG A1125 12100 14913 13774 -732 -485 3853 C ATOM 2540 O ARG A1125 27.073 -2.551 36.888 1.00106.89 O ANISOU 2540 O ARG A1125 11927 15009 13677 -770 -422 3935 O ATOM 2541 CB ARG A1125 26.474 -5.096 35.779 1.00106.91 C ANISOU 2541 CB ARG A1125 11852 14563 14206 -861 -672 4182 C ATOM 2542 CG ARG A1125 26.446 -6.354 34.880 1.00120.23 C ANISOU 2542 CG ARG A1125 13576 15919 16188 -886 -799 4231 C ATOM 2543 CD ARG A1125 25.063 -6.676 34.313 1.00132.70 C ANISOU 2543 CD ARG A1125 15163 17414 17842 -878 -928 4254 C ATOM 2544 NE ARG A1125 24.105 -7.061 35.353 1.00143.90 N ANISOU 2544 NE ARG A1125 16305 19098 19270 -948 -1012 4519 N ATOM 2545 CZ ARG A1125 23.883 -8.316 35.732 1.00160.86 C ANISOU 2545 CZ ARG A1125 18241 21220 21661 -1037 -1147 4780 C ATOM 2546 NH1 ARG A1125 24.553 -9.316 35.170 1.00149.05 N ANISOU 2546 NH1 ARG A1125 16779 19430 20422 -1064 -1216 4798 N ATOM 2547 NH2 ARG A1125 22.992 -8.581 36.678 1.00149.71 N ANISOU 2547 NH2 ARG A1125 16570 20076 20237 -1097 -1219 5029 N ATOM 2548 N TRP A1126 25.378 -1.525 35.763 1.00103.16 N ANISOU 2548 N TRP A1126 11675 14463 13058 -660 -461 3698 N ATOM 2549 CA TRP A1126 25.442 -0.234 36.461 1.00102.41 C ANISOU 2549 CA TRP A1126 11582 14627 12703 -611 -362 3588 C ATOM 2550 C TRP A1126 25.045 -0.341 37.939 1.00107.20 C ANISOU 2550 C TRP A1126 11898 15615 13218 -655 -374 3795 C ATOM 2551 O TRP A1126 25.655 0.323 38.782 1.00106.29 O ANISOU 2551 O TRP A1126 11724 15713 12948 -646 -291 3765 O ATOM 2552 CB TRP A1126 24.541 0.805 35.765 1.00100.42 C ANISOU 2552 CB TRP A1126 11504 14344 12306 -523 -352 3381 C ATOM 2553 CG TRP A1126 24.567 0.753 34.262 1.00100.59 C ANISOU 2553 CG TRP A1126 11775 14015 12430 -483 -369 3216 C ATOM 2554 CD1 TRP A1126 23.524 0.453 33.436 1.00103.64 C ANISOU 2554 CD1 TRP A1126 12227 14261 12889 -466 -453 3200 C ATOM 2555 CD2 TRP A1126 25.704 0.963 33.413 1.00 99.57 C ANISOU 2555 CD2 TRP A1126 11849 13644 12340 -454 -305 3056 C ATOM 2556 NE1 TRP A1126 23.934 0.487 32.123 1.00102.34 N ANISOU 2556 NE1 TRP A1126 12295 13790 12800 -426 -443 3028 N ATOM 2557 CE2 TRP A1126 25.270 0.793 32.079 1.00103.17 C ANISOU 2557 CE2 TRP A1126 12484 13831 12883 -415 -352 2941 C ATOM 2558 CE3 TRP A1126 27.052 1.287 33.649 1.00100.34 C ANISOU 2558 CE3 TRP A1126 11988 13735 12400 -456 -213 3004 C ATOM 2559 CZ2 TRP A1126 26.133 0.939 30.985 1.00101.72 C ANISOU 2559 CZ2 TRP A1126 12513 13392 12745 -373 -308 2776 C ATOM 2560 CZ3 TRP A1126 27.909 1.414 32.567 1.00101.07 C ANISOU 2560 CZ3 TRP A1126 12291 13565 12545 -418 -172 2852 C ATOM 2561 CH2 TRP A1126 27.447 1.251 31.253 1.00101.43 C ANISOU 2561 CH2 TRP A1126 12507 13364 12670 -374 -218 2738 C ATOM 2562 N ASP A1127 24.010 -1.145 38.245 1.00105.19 N ANISOU 2562 N ASP A1127 11458 15457 13053 -700 -482 4004 N ATOM 2563 CA ASP A1127 23.484 -1.312 39.608 1.00106.35 C ANISOU 2563 CA ASP A1127 11305 15989 13112 -739 -507 4226 C ATOM 2564 C ASP A1127 24.517 -1.962 40.542 1.00110.46 C ANISOU 2564 C ASP A1127 11633 16630 13706 -821 -483 4412 C ATOM 2565 O ASP A1127 24.542 -1.656 41.736 1.00110.45 O ANISOU 2565 O ASP A1127 11432 16980 13554 -830 -445 4508 O ATOM 2566 CB ASP A1127 22.200 -2.153 39.584 1.00109.41 C ANISOU 2566 CB ASP A1127 11543 16412 13618 -777 -643 4432 C ATOM 2567 CG ASP A1127 21.174 -1.681 38.568 1.00120.84 C ANISOU 2567 CG ASP A1127 13180 17706 15028 -709 -678 4271 C ATOM 2568 OD1 ASP A1127 20.684 -0.535 38.705 1.00121.34 O ANISOU 2568 OD1 ASP A1127 13308 17934 14863 -627 -619 4116 O ATOM 2569 OD2 ASP A1127 20.833 -2.470 37.659 1.00127.27 O1- ANISOU 2569 OD2 ASP A1127 14069 18242 16045 -736 -771 4305 O1- ATOM 2570 N GLU A1128 25.366 -2.852 39.994 1.00106.80 N ANISOU 2570 N GLU A1128 11225 15882 13471 -876 -504 4457 N ATOM 2571 CA GLU A1128 26.406 -3.550 40.752 1.00107.10 C ANISOU 2571 CA GLU A1128 11096 15987 13610 -958 -483 4634 C ATOM 2572 C GLU A1128 27.541 -2.592 41.143 1.00110.07 C ANISOU 2572 C GLU A1128 11558 16457 13807 -925 -343 4477 C ATOM 2573 O GLU A1128 28.013 -2.633 42.281 1.00109.98 O ANISOU 2573 O GLU A1128 11345 16714 13728 -971 -303 4615 O ATOM 2574 CB GLU A1128 26.961 -4.735 39.939 1.00108.60 C ANISOU 2574 CB GLU A1128 11346 15818 14100 -1012 -552 4700 C ATOM 2575 CG GLU A1128 26.083 -5.983 39.968 1.00120.93 C ANISOU 2575 CG GLU A1128 12720 17339 15890 -1083 -710 4953 C ATOM 2576 CD GLU A1128 24.780 -5.946 39.180 1.00141.13 C ANISOU 2576 CD GLU A1128 15369 19786 18466 -1041 -803 4893 C ATOM 2577 OE1 GLU A1128 24.538 -4.956 38.453 1.00136.00 O ANISOU 2577 OE1 GLU A1128 14956 19056 17662 -950 -743 4634 O ATOM 2578 OE2 GLU A1128 24.013 -6.930 39.274 1.00134.57 O1- ANISOU 2578 OE2 GLU A1128 14371 18943 17817 -1103 -942 5115 O1- ATOM 2579 N ALA A1129 27.964 -1.719 40.202 1.00105.57 N ANISOU 2579 N ALA A1129 11280 15672 13161 -847 -272 4196 N ATOM 2580 CA ALA A1129 29.032 -0.739 40.433 1.00104.49 C ANISOU 2580 CA ALA A1129 11252 15585 12864 -811 -150 4031 C ATOM 2581 C ALA A1129 28.562 0.389 41.353 1.00108.23 C ANISOU 2581 C ALA A1129 11647 16407 13068 -759 -104 3960 C ATOM 2582 O ALA A1129 29.386 1.027 42.012 1.00107.58 O ANISOU 2582 O ALA A1129 11548 16474 12855 -753 -21 3904 O ATOM 2583 CB ALA A1129 29.506 -0.163 39.109 1.00103.96 C ANISOU 2583 CB ALA A1129 11503 15191 12807 -742 -106 3772 C ATOM 2584 N ALA A1130 27.234 0.631 41.394 1.00105.05 N ANISOU 2584 N ALA A1130 11195 16135 12585 -718 -161 3960 N ATOM 2585 CA ALA A1130 26.617 1.670 42.220 1.00105.10 C ANISOU 2585 CA ALA A1130 11121 16477 12336 -654 -132 3886 C ATOM 2586 C ALA A1130 26.744 1.355 43.720 1.00110.04 C ANISOU 2586 C ALA A1130 11433 17492 12884 -706 -126 4103 C ATOM 2587 O ALA A1130 26.867 2.275 44.528 1.00109.61 O ANISOU 2587 O ALA A1130 11326 17708 12613 -656 -69 4011 O ATOM 2588 CB ALA A1130 25.152 1.825 41.847 1.00106.07 C ANISOU 2588 CB ALA A1130 11254 16630 12417 -603 -203 3866 C ATOM 2589 N VAL A1131 26.717 0.058 44.085 1.00107.51 N ANISOU 2589 N VAL A1131 10900 17203 12746 -805 -192 4389 N ATOM 2590 CA VAL A1131 26.811 -0.390 45.479 1.00108.55 C ANISOU 2590 CA VAL A1131 10707 17709 12830 -867 -196 4636 C ATOM 2591 C VAL A1131 28.279 -0.334 45.958 1.00111.81 C ANISOU 2591 C VAL A1131 11111 18133 13239 -911 -107 4631 C ATOM 2592 O VAL A1131 28.538 0.117 47.078 1.00111.78 O ANISOU 2592 O VAL A1131 10944 18470 13059 -906 -58 4663 O ATOM 2593 CB VAL A1131 26.208 -1.812 45.653 1.00113.68 C ANISOU 2593 CB VAL A1131 11122 18374 13698 -963 -313 4963 C ATOM 2594 CG1 VAL A1131 26.305 -2.285 47.104 1.00114.80 C ANISOU 2594 CG1 VAL A1131 10905 18922 13791 -1032 -319 5240 C ATOM 2595 CG2 VAL A1131 24.760 -1.851 45.173 1.00113.86 C ANISOU 2595 CG2 VAL A1131 11155 18384 13723 -923 -404 4974 C ATOM 2596 N ASN A1132 29.231 -0.785 45.106 1.00107.51 N ANISOU 2596 N ASN A1132 10741 17226 12882 -949 -88 4588 N ATOM 2597 CA ASN A1132 30.670 -0.796 45.422 1.00106.93 C ANISOU 2597 CA ASN A1132 10681 17120 12828 -993 -5 4589 C ATOM 2598 C ASN A1132 31.184 0.608 45.762 1.00108.87 C ANISOU 2598 C ASN A1132 11042 17501 12822 -918 93 4352 C ATOM 2599 O ASN A1132 31.946 0.769 46.717 1.00108.76 O ANISOU 2599 O ASN A1132 10898 17707 12719 -951 150 4411 O ATOM 2600 CB ASN A1132 31.479 -1.371 44.246 1.00108.93 C ANISOU 2600 CB ASN A1132 11146 16938 13305 -1017 -3 4536 C ATOM 2601 CG ASN A1132 31.201 -2.826 43.933 1.00139.61 C ANISOU 2601 CG ASN A1132 14918 20658 17470 -1096 -106 4765 C ATOM 2602 OD1 ASN A1132 30.127 -3.368 44.231 1.00137.49 O ANISOU 2602 OD1 ASN A1132 14472 20519 17250 -1121 -200 4932 O ATOM 2603 ND2 ASN A1132 32.150 -3.475 43.274 1.00131.14 N ANISOU 2603 ND2 ASN A1132 13951 19284 16591 -1131 -98 4770 N ATOM 2604 N LEU A1133 30.761 1.618 44.980 1.00103.46 N ANISOU 2604 N LEU A1133 10597 16684 12030 -819 106 4087 N ATOM 2605 CA LEU A1133 31.178 3.005 45.173 1.00102.14 C ANISOU 2605 CA LEU A1133 10561 16602 11646 -740 180 3843 C ATOM 2606 C LEU A1133 30.456 3.655 46.358 1.00105.56 C ANISOU 2606 C LEU A1133 10799 17464 11846 -693 175 3844 C ATOM 2607 O LEU A1133 30.990 4.592 46.947 1.00104.87 O ANISOU 2607 O LEU A1133 10725 17534 11585 -652 231 3708 O ATOM 2608 CB LEU A1133 30.930 3.825 43.895 1.00101.10 C ANISOU 2608 CB LEU A1133 10738 16174 11500 -654 184 3575 C ATOM 2609 CG LEU A1133 31.795 3.468 42.682 1.00104.81 C ANISOU 2609 CG LEU A1133 11434 16239 12151 -675 204 3515 C ATOM 2610 CD1 LEU A1133 31.213 4.048 41.414 1.00104.17 C ANISOU 2610 CD1 LEU A1133 11604 15902 12072 -596 185 3305 C ATOM 2611 CD2 LEU A1133 33.236 3.937 42.870 1.00106.79 C ANISOU 2611 CD2 LEU A1133 11762 16449 12363 -690 289 3444 C ATOM 2612 N ALA A1134 29.246 3.161 46.707 1.00102.32 N ANISOU 2612 N ALA A1134 10202 17246 11430 -694 103 3997 N ATOM 2613 CA ALA A1134 28.452 3.705 47.818 1.00102.96 C ANISOU 2613 CA ALA A1134 10076 17760 11283 -638 92 4012 C ATOM 2614 C ALA A1134 29.078 3.375 49.182 1.00107.65 C ANISOU 2614 C ALA A1134 10392 18702 11808 -699 123 4197 C ATOM 2615 O ALA A1134 28.863 4.111 50.148 1.00108.20 O ANISOU 2615 O ALA A1134 10333 19128 11649 -637 143 4136 O ATOM 2616 CB ALA A1134 27.032 3.166 47.759 1.00104.41 C ANISOU 2616 CB ALA A1134 10130 18045 11497 -630 4 4156 C ATOM 2617 N LYS A1135 29.839 2.268 49.263 1.00103.71 N ANISOU 2617 N LYS A1135 9794 18106 11505 -815 123 4421 N ATOM 2618 CA LYS A1135 30.474 1.831 50.506 1.00104.08 C ANISOU 2618 CA LYS A1135 9566 18464 11514 -889 151 4627 C ATOM 2619 C LYS A1135 31.916 2.354 50.624 1.00106.47 C ANISOU 2619 C LYS A1135 9991 18682 11779 -903 243 4498 C ATOM 2620 O LYS A1135 32.453 2.408 51.731 1.00106.87 O ANISOU 2620 O LYS A1135 9848 19036 11722 -935 282 4587 O ATOM 2621 CB LYS A1135 30.465 0.298 50.599 1.00107.24 C ANISOU 2621 CB LYS A1135 9761 18822 12162 -1014 92 4968 C ATOM 2622 N SER A1136 32.535 2.747 49.485 1.00100.91 N ANISOU 2622 N SER A1136 9604 17579 11160 -880 276 4294 N ATOM 2623 CA SER A1136 33.925 3.230 49.423 1.00 99.42 C ANISOU 2623 CA SER A1136 9559 17259 10956 -894 357 4175 C ATOM 2624 C SER A1136 34.124 4.571 50.172 1.00102.49 C ANISOU 2624 C SER A1136 9960 17902 11079 -814 400 3968 C ATOM 2625 O SER A1136 33.147 5.234 50.536 1.00102.41 O ANISOU 2625 O SER A1136 9897 18118 10896 -727 369 3867 O ATOM 2626 CB SER A1136 34.365 3.386 47.972 1.00101.27 C ANISOU 2626 CB SER A1136 10119 17030 11328 -873 370 4006 C ATOM 2627 OG SER A1136 33.566 4.340 47.293 1.00108.94 O ANISOU 2627 OG SER A1136 11283 17911 12199 -766 348 3765 O ATOM 2628 N ARG A1137 35.405 4.966 50.380 1.00 98.28 N ANISOU 2628 N ARG A1137 9498 17323 10519 -840 467 3902 N ATOM 2629 CA ARG A1137 35.792 6.205 51.072 1.00 98.12 C ANISOU 2629 CA ARG A1137 9501 17507 10274 -774 501 3704 C ATOM 2630 C ARG A1137 35.272 7.449 50.339 1.00101.10 C ANISOU 2630 C ARG A1137 10128 17736 10551 -651 481 3393 C ATOM 2631 O ARG A1137 34.902 8.432 50.987 1.00101.11 O ANISOU 2631 O ARG A1137 10089 17982 10344 -565 470 3232 O ATOM 2632 CB ARG A1137 37.320 6.285 51.213 1.00 97.49 C ANISOU 2632 CB ARG A1137 9484 17328 10232 -838 569 3709 C ATOM 2633 N TRP A1138 35.237 7.392 48.984 1.00 96.16 N ANISOU 2633 N TRP A1138 9750 16713 10073 -641 472 3308 N ATOM 2634 CA TRP A1138 34.763 8.471 48.108 1.00 94.86 C ANISOU 2634 CA TRP A1138 9834 16358 9852 -536 452 3035 C ATOM 2635 C TRP A1138 33.303 8.870 48.440 1.00 99.01 C ANISOU 2635 C TRP A1138 10266 17118 10236 -447 396 2970 C ATOM 2636 O TRP A1138 32.978 10.059 48.423 1.00 98.37 O ANISOU 2636 O TRP A1138 10291 17076 10011 -347 382 2732 O ATOM 2637 CB TRP A1138 34.891 8.038 46.631 1.00 92.26 C ANISOU 2637 CB TRP A1138 9733 15599 9724 -556 449 3020 C ATOM 2638 CG TRP A1138 34.238 8.959 45.636 1.00 92.40 C ANISOU 2638 CG TRP A1138 9983 15418 9708 -458 421 2781 C ATOM 2639 CD1 TRP A1138 34.505 10.283 45.443 1.00 94.87 C ANISOU 2639 CD1 TRP A1138 10464 15674 9910 -382 428 2534 C ATOM 2640 CD2 TRP A1138 33.308 8.584 44.612 1.00 91.74 C ANISOU 2640 CD2 TRP A1138 9998 15133 9727 -436 379 2776 C ATOM 2641 NE1 TRP A1138 33.754 10.770 44.398 1.00 93.64 N ANISOU 2641 NE1 TRP A1138 10493 15312 9775 -313 396 2381 N ATOM 2642 CE2 TRP A1138 33.010 9.747 43.869 1.00 94.98 C ANISOU 2642 CE2 TRP A1138 10626 15393 10068 -344 369 2522 C ATOM 2643 CE3 TRP A1138 32.669 7.380 44.268 1.00 93.07 C ANISOU 2643 CE3 TRP A1138 10084 15236 10043 -485 341 2963 C ATOM 2644 CZ2 TRP A1138 32.105 9.742 42.801 1.00 93.80 C ANISOU 2644 CZ2 TRP A1138 10614 15044 9981 -301 331 2453 C ATOM 2645 CZ3 TRP A1138 31.771 7.377 43.212 1.00 94.04 C ANISOU 2645 CZ3 TRP A1138 10348 15155 10228 -441 298 2887 C ATOM 2646 CH2 TRP A1138 31.494 8.547 42.494 1.00 94.02 C ANISOU 2646 CH2 TRP A1138 10561 15019 10144 -350 298 2635 C ATOM 2647 N TYR A1139 32.445 7.884 48.772 1.00 96.31 N ANISOU 2647 N TYR A1139 9716 16939 9938 -484 359 3189 N ATOM 2648 CA TYR A1139 31.053 8.151 49.139 1.00 97.16 C ANISOU 2648 CA TYR A1139 9707 17297 9911 -404 306 3165 C ATOM 2649 C TYR A1139 30.941 8.582 50.602 1.00103.06 C ANISOU 2649 C TYR A1139 10210 18512 10434 -365 310 3175 C ATOM 2650 O TYR A1139 29.959 9.226 50.973 1.00103.18 O ANISOU 2650 O TYR A1139 10166 18757 10280 -264 276 3068 O ATOM 2651 CB TYR A1139 30.180 6.922 48.890 1.00 98.64 C ANISOU 2651 CB TYR A1139 9765 17472 10243 -461 255 3409 C ATOM 2652 N ASN A1140 31.936 8.211 51.439 1.00100.68 N ANISOU 2652 N ASN A1140 9760 18366 10128 -441 352 3307 N ATOM 2653 CA ASN A1140 31.946 8.570 52.859 1.00102.03 C ANISOU 2653 CA ASN A1140 9687 18997 10085 -409 360 3324 C ATOM 2654 C ASN A1140 32.499 9.989 53.071 1.00105.98 C ANISOU 2654 C ASN A1140 10335 19516 10419 -318 379 3017 C ATOM 2655 O ASN A1140 32.109 10.656 54.031 1.00106.91 O ANISOU 2655 O ASN A1140 10310 19993 10318 -232 362 2920 O ATOM 2656 CB ASN A1140 32.755 7.555 53.677 1.00103.74 C ANISOU 2656 CB ASN A1140 9667 19381 10368 -534 394 3605 C ATOM 2657 CG ASN A1140 32.121 6.179 53.775 1.00126.61 C ANISOU 2657 CG ASN A1140 12345 22357 13406 -619 357 3932 C ATOM 2658 OD1 ASN A1140 32.804 5.152 53.707 1.00121.28 O ANISOU 2658 OD1 ASN A1140 11603 21561 12917 -740 374 4154 O ATOM 2659 ND2 ASN A1140 30.805 6.126 53.966 1.00118.20 N ANISOU 2659 ND2 ASN A1140 11151 21502 12258 -559 300 3976 N ATOM 2660 N GLN A1141 33.399 10.451 52.173 1.00100.98 N ANISOU 2660 N GLN A1141 9979 18500 9890 -332 406 2865 N ATOM 2661 CA GLN A1141 33.982 11.793 52.256 1.00100.50 C ANISOU 2661 CA GLN A1141 10076 18402 9708 -256 410 2582 C ATOM 2662 C GLN A1141 32.976 12.845 51.753 1.00103.66 C ANISOU 2662 C GLN A1141 10625 18745 10015 -120 358 2321 C ATOM 2663 O GLN A1141 32.532 13.687 52.539 1.00104.34 O ANISOU 2663 O GLN A1141 10626 19118 9902 -18 327 2165 O ATOM 2664 CB GLN A1141 35.303 11.868 51.469 1.00100.65 C ANISOU 2664 CB GLN A1141 10321 18044 9879 -325 453 2545 C ATOM 2665 CG GLN A1141 36.466 11.157 52.165 1.00121.13 C ANISOU 2665 CG GLN A1141 12772 20735 12518 -440 507 2746 C ATOM 2666 CD GLN A1141 37.709 11.068 51.302 1.00144.73 C ANISOU 2666 CD GLN A1141 15975 23343 15672 -510 550 2746 C ATOM 2667 OE1 GLN A1141 38.036 11.977 50.524 1.00141.00 O ANISOU 2667 OE1 GLN A1141 15749 22610 15213 -460 542 2534 O ATOM 2668 NE2 GLN A1141 38.464 9.989 51.468 1.00137.19 N ANISOU 2668 NE2 GLN A1141 14916 22366 14843 -628 596 2990 N ATOM 2669 N THR A1142 32.587 12.772 50.456 1.00 98.32 N ANISOU 2669 N THR A1142 10162 17713 9482 -117 345 2277 N ATOM 2670 CA THR A1142 31.600 13.687 49.866 1.00 97.64 C ANISOU 2670 CA THR A1142 10221 17544 9332 1 297 2053 C ATOM 2671 C THR A1142 30.353 12.879 49.447 1.00100.92 C ANISOU 2671 C THR A1142 10569 17968 9807 -2 270 2199 C ATOM 2672 O THR A1142 30.297 12.355 48.331 1.00 99.18 O ANISOU 2672 O THR A1142 10498 17423 9764 -50 273 2256 O ATOM 2673 CB THR A1142 32.211 14.473 48.687 1.00103.25 C ANISOU 2673 CB THR A1142 11247 17837 10145 16 300 1853 C ATOM 2674 OG1 THR A1142 32.767 13.554 47.748 1.00100.77 O ANISOU 2674 OG1 THR A1142 11037 17209 10040 -86 335 2008 O ATOM 2675 CG2 THR A1142 33.269 15.469 49.132 1.00101.73 C ANISOU 2675 CG2 THR A1142 11121 17654 9877 38 305 1682 C ATOM 2676 N PRO A1143 29.358 12.724 50.355 1.00 98.69 N ANISOU 2676 N PRO A1143 10049 18071 9378 48 240 2274 N ATOM 2677 CA PRO A1143 28.195 11.874 50.027 1.00 98.55 C ANISOU 2677 CA PRO A1143 9941 18079 9424 34 208 2449 C ATOM 2678 C PRO A1143 27.255 12.498 48.991 1.00101.07 C ANISOU 2678 C PRO A1143 10466 18179 9756 119 172 2270 C ATOM 2679 O PRO A1143 26.761 11.783 48.121 1.00 99.79 O ANISOU 2679 O PRO A1143 10368 17802 9744 73 156 2383 O ATOM 2680 CB PRO A1143 27.487 11.701 51.375 1.00101.96 C ANISOU 2680 CB PRO A1143 10053 19021 9667 75 187 2566 C ATOM 2681 CG PRO A1143 27.911 12.864 52.182 1.00107.13 C ANISOU 2681 CG PRO A1143 10697 19887 10121 168 194 2336 C ATOM 2682 CD PRO A1143 29.292 13.227 51.743 1.00101.61 C ANISOU 2682 CD PRO A1143 10202 18883 9521 115 233 2226 C ATOM 2683 N ASN A1144 26.998 13.818 49.090 1.00 97.54 N ANISOU 2683 N ASN A1144 10117 17786 9158 242 153 1993 N ATOM 2684 CA ASN A1144 26.086 14.521 48.188 1.00 96.75 C ANISOU 2684 CA ASN A1144 10200 17505 9056 330 118 1812 C ATOM 2685 C ASN A1144 26.677 14.640 46.780 1.00 98.36 C ANISOU 2685 C ASN A1144 10696 17226 9449 284 135 1729 C ATOM 2686 O ASN A1144 25.926 14.625 45.803 1.00 97.68 O ANISOU 2686 O ASN A1144 10741 16935 9438 303 113 1698 O ATOM 2687 CB ASN A1144 25.742 15.910 48.740 1.00 99.20 C ANISOU 2687 CB ASN A1144 10522 18006 9162 475 88 1536 C ATOM 2688 CG ASN A1144 24.950 15.891 50.037 1.00125.45 C ANISOU 2688 CG ASN A1144 13562 21827 12274 551 65 1590 C ATOM 2689 OD1 ASN A1144 24.384 14.867 50.446 1.00120.26 O ANISOU 2689 OD1 ASN A1144 12694 21383 11616 503 63 1844 O ATOM 2690 ND2 ASN A1144 24.851 17.042 50.687 1.00118.55 N ANISOU 2690 ND2 ASN A1144 12674 21153 11218 678 38 1349 N ATOM 2691 N ARG A1145 27.999 14.736 46.665 1.00 93.16 N ANISOU 2691 N ARG A1145 10135 16398 8865 225 172 1702 N ATOM 2692 CA ARG A1145 28.594 14.818 45.336 1.00 90.93 C ANISOU 2692 CA ARG A1145 10114 15683 8754 185 189 1638 C ATOM 2693 C ARG A1145 28.664 13.436 44.650 1.00 92.52 C ANISOU 2693 C ARG A1145 10313 15695 9146 77 207 1874 C ATOM 2694 O ARG A1145 28.249 13.290 43.513 1.00 91.34 O ANISOU 2694 O ARG A1145 10320 15278 9107 77 194 1851 O ATOM 2695 CB ARG A1145 29.985 15.437 45.375 1.00 90.46 C ANISOU 2695 CB ARG A1145 10166 15495 8709 163 218 1530 C ATOM 2696 CG ARG A1145 30.750 15.218 44.083 1.00 97.00 C ANISOU 2696 CG ARG A1145 11218 15913 9724 101 245 1538 C ATOM 2697 CD ARG A1145 32.132 15.829 44.106 1.00102.63 C ANISOU 2697 CD ARG A1145 12036 16504 10454 78 270 1451 C ATOM 2698 NE ARG A1145 32.798 15.674 42.820 1.00105.43 N ANISOU 2698 NE ARG A1145 12601 16484 10973 33 294 1455 N ATOM 2699 CZ ARG A1145 33.749 16.479 42.375 1.00116.44 C ANISOU 2699 CZ ARG A1145 14159 17686 12398 38 299 1332 C ATOM 2700 NH1 ARG A1145 34.150 17.500 43.107 1.00101.68 N ANISOU 2700 NH1 ARG A1145 12274 15941 10418 82 275 1188 N ATOM 2701 NH2 ARG A1145 34.291 16.270 41.190 1.00103.21 N ANISOU 2701 NH2 ARG A1145 12657 15696 10863 2 321 1353 N ATOM 2702 N ALA A1146 29.179 12.425 45.351 1.00 87.97 N ANISOU 2702 N ALA A1146 9553 15261 8611 -13 231 2098 N ATOM 2703 CA ALA A1146 29.289 11.073 44.793 1.00 86.69 C ANISOU 2703 CA ALA A1146 9369 14926 8643 -115 237 2325 C ATOM 2704 C ALA A1146 27.930 10.509 44.390 1.00 89.80 C ANISOU 2704 C ALA A1146 9716 15329 9077 -101 185 2415 C ATOM 2705 O ALA A1146 27.850 9.766 43.412 1.00 88.54 O ANISOU 2705 O ALA A1146 9653 14897 9090 -150 173 2493 O ATOM 2706 CB ALA A1146 29.950 10.147 45.797 1.00 88.03 C ANISOU 2706 CB ALA A1146 9310 15303 8835 -206 261 2556 C ATOM 2707 N LYS A1147 26.860 10.865 45.139 1.00 86.92 N ANISOU 2707 N LYS A1147 9198 15279 8549 -29 150 2401 N ATOM 2708 CA LYS A1147 25.496 10.397 44.871 1.00 86.82 C ANISOU 2708 CA LYS A1147 9119 15317 8552 -10 97 2496 C ATOM 2709 C LYS A1147 25.081 10.735 43.440 1.00 88.63 C ANISOU 2709 C LYS A1147 9612 15189 8875 22 81 2350 C ATOM 2710 O LYS A1147 24.611 9.856 42.722 1.00 87.94 O ANISOU 2710 O LYS A1147 9547 14933 8935 -27 50 2478 O ATOM 2711 CB LYS A1147 24.502 11.015 45.879 1.00 90.78 C ANISOU 2711 CB LYS A1147 9443 16220 8828 87 69 2451 C ATOM 2712 CG LYS A1147 23.136 10.322 45.932 1.00108.09 C ANISOU 2712 CG LYS A1147 11484 18563 11024 90 12 2628 C ATOM 2713 CD LYS A1147 23.174 9.014 46.743 1.00120.12 C ANISOU 2713 CD LYS A1147 12724 20306 12610 -10 -5 2956 C ATOM 2714 CE LYS A1147 21.809 8.374 46.879 1.00133.33 C ANISOU 2714 CE LYS A1147 14224 22157 14278 -7 -73 3147 C ATOM 2715 NZ LYS A1147 21.292 7.874 45.575 1.00142.30 N ANISOU 2715 NZ LYS A1147 15533 22932 15602 -42 -113 3171 N ATOM 2716 N ARG A1148 25.313 11.996 43.013 1.00 84.04 N ANISOU 2716 N ARG A1148 9228 14484 8220 101 98 2084 N ATOM 2717 CA ARG A1148 24.972 12.476 41.670 1.00 82.66 C ANISOU 2717 CA ARG A1148 9303 13986 8119 138 87 1930 C ATOM 2718 C ARG A1148 25.782 11.745 40.592 1.00 85.80 C ANISOU 2718 C ARG A1148 9852 14025 8722 55 109 1994 C ATOM 2719 O ARG A1148 25.224 11.368 39.561 1.00 84.70 O ANISOU 2719 O ARG A1148 9823 13670 8691 48 84 2007 O ATOM 2720 CB ARG A1148 25.201 13.993 41.563 1.00 81.56 C ANISOU 2720 CB ARG A1148 9317 13807 7867 233 96 1650 C ATOM 2721 CG ARG A1148 24.223 14.824 42.388 1.00 90.37 C ANISOU 2721 CG ARG A1148 10321 15231 8783 341 64 1540 C ATOM 2722 CD ARG A1148 24.450 16.314 42.204 1.00 96.64 C ANISOU 2722 CD ARG A1148 11276 15948 9496 434 57 1256 C ATOM 2723 NE ARG A1148 25.715 16.758 42.794 1.00102.14 N ANISOU 2723 NE ARG A1148 11972 16674 10162 420 83 1188 N ATOM 2724 CZ ARG A1148 25.822 17.295 44.005 1.00115.25 C ANISOU 2724 CZ ARG A1148 13487 18640 11661 475 73 1119 C ATOM 2725 NH1 ARG A1148 24.744 17.469 44.760 1.00100.81 N ANISOU 2725 NH1 ARG A1148 11499 17127 9679 557 41 1105 N ATOM 2726 NH2 ARG A1148 27.007 17.672 44.466 1.00102.35 N ANISOU 2726 NH2 ARG A1148 11866 17008 10013 454 92 1060 N ATOM 2727 N VAL A1149 27.096 11.533 40.843 1.00 82.35 N ANISOU 2727 N VAL A1149 9416 13538 8337 -4 153 2034 N ATOM 2728 CA VAL A1149 28.007 10.847 39.912 1.00 81.17 C ANISOU 2728 CA VAL A1149 9397 13073 8372 -75 178 2093 C ATOM 2729 C VAL A1149 27.569 9.376 39.746 1.00 85.07 C ANISOU 2729 C VAL A1149 9778 13531 9015 -150 144 2327 C ATOM 2730 O VAL A1149 27.488 8.887 38.621 1.00 83.93 O ANISOU 2730 O VAL A1149 9769 13108 9013 -167 129 2331 O ATOM 2731 CB VAL A1149 29.494 10.950 40.374 1.00 84.74 C ANISOU 2731 CB VAL A1149 9848 13522 8829 -119 233 2100 C ATOM 2732 CG1 VAL A1149 30.435 10.329 39.345 1.00 83.60 C ANISOU 2732 CG1 VAL A1149 9850 13051 8863 -177 261 2143 C ATOM 2733 CG2 VAL A1149 29.889 12.400 40.652 1.00 84.44 C ANISOU 2733 CG2 VAL A1149 9899 13537 8648 -48 249 1879 C ATOM 2734 N ILE A1150 27.257 8.693 40.867 1.00 82.65 N ANISOU 2734 N ILE A1150 9216 13512 8676 -191 125 2520 N ATOM 2735 CA ILE A1150 26.801 7.299 40.864 1.00 82.85 C ANISOU 2735 CA ILE A1150 9097 13534 8849 -267 77 2766 C ATOM 2736 C ILE A1150 25.436 7.195 40.133 1.00 86.37 C ANISOU 2736 C ILE A1150 9594 13901 9321 -229 13 2751 C ATOM 2737 O ILE A1150 25.259 6.301 39.299 1.00 85.65 O ANISOU 2737 O ILE A1150 9557 13579 9407 -274 -27 2839 O ATOM 2738 CB ILE A1150 26.742 6.748 42.322 1.00 87.12 C ANISOU 2738 CB ILE A1150 9331 14445 9327 -314 68 2979 C ATOM 2739 CG1 ILE A1150 28.175 6.524 42.876 1.00 87.43 C ANISOU 2739 CG1 ILE A1150 9320 14502 9397 -378 127 3040 C ATOM 2740 CG2 ILE A1150 25.915 5.456 42.404 1.00 88.67 C ANISOU 2740 CG2 ILE A1150 9348 14688 9655 -379 -7 3238 C ATOM 2741 CD1 ILE A1150 28.282 6.497 44.414 1.00 96.06 C ANISOU 2741 CD1 ILE A1150 10139 16005 10353 -397 140 3167 C ATOM 2742 N THR A1151 24.512 8.156 40.396 1.00 82.86 N ANISOU 2742 N THR A1151 9146 13633 8702 -141 2 2625 N ATOM 2743 CA THR A1151 23.192 8.205 39.746 1.00 82.44 C ANISOU 2743 CA THR A1151 9145 13527 8651 -98 -53 2599 C ATOM 2744 C THR A1151 23.364 8.342 38.217 1.00 84.72 C ANISOU 2744 C THR A1151 9709 13418 9062 -89 -49 2457 C ATOM 2745 O THR A1151 22.607 7.732 37.462 1.00 84.24 O ANISOU 2745 O THR A1151 9686 13211 9108 -104 -102 2518 O ATOM 2746 CB THR A1151 22.341 9.355 40.333 1.00 88.90 C ANISOU 2746 CB THR A1151 9923 14607 9247 5 -54 2460 C ATOM 2747 OG1 THR A1151 22.276 9.209 41.752 1.00 88.06 O ANISOU 2747 OG1 THR A1151 9555 14887 9019 2 -55 2589 O ATOM 2748 CG2 THR A1151 20.923 9.394 39.762 1.00 86.85 C ANISOU 2748 CG2 THR A1151 9695 14327 8978 49 -110 2454 C ATOM 2749 N THR A1152 24.395 9.098 37.772 1.00 79.89 N ANISOU 2749 N THR A1152 9277 12638 8438 -66 9 2280 N ATOM 2750 CA THR A1152 24.695 9.278 36.348 1.00 78.45 C ANISOU 2750 CA THR A1152 9344 12104 8360 -53 20 2148 C ATOM 2751 C THR A1152 25.111 7.925 35.728 1.00 81.15 C ANISOU 2751 C THR A1152 9693 12230 8911 -132 -2 2300 C ATOM 2752 O THR A1152 24.692 7.613 34.613 1.00 80.28 O ANISOU 2752 O THR A1152 9712 11889 8902 -126 -34 2268 O ATOM 2753 CB THR A1152 25.783 10.358 36.151 1.00 85.91 C ANISOU 2753 CB THR A1152 10444 12954 9244 -17 82 1959 C ATOM 2754 OG1 THR A1152 25.478 11.493 36.962 1.00 86.42 O ANISOU 2754 OG1 THR A1152 10460 13248 9125 51 89 1837 O ATOM 2755 CG2 THR A1152 25.925 10.789 34.692 1.00 82.64 C ANISOU 2755 CG2 THR A1152 10279 12223 8899 15 90 1806 C ATOM 2756 N PHE A1153 25.904 7.114 36.470 1.00 77.33 N ANISOU 2756 N PHE A1153 9062 11828 8492 -204 10 2466 N ATOM 2757 CA PHE A1153 26.327 5.790 36.002 1.00 76.86 C ANISOU 2757 CA PHE A1153 8985 11576 8640 -278 -18 2618 C ATOM 2758 C PHE A1153 25.147 4.820 35.957 1.00 82.51 C ANISOU 2758 C PHE A1153 9580 12318 9453 -310 -111 2782 C ATOM 2759 O PHE A1153 25.070 3.992 35.049 1.00 82.16 O ANISOU 2759 O PHE A1153 9609 12028 9580 -335 -158 2820 O ATOM 2760 CB PHE A1153 27.440 5.212 36.894 1.00 78.41 C ANISOU 2760 CB PHE A1153 9038 11874 8881 -348 16 2763 C ATOM 2761 CG PHE A1153 28.811 5.813 36.704 1.00 78.46 C ANISOU 2761 CG PHE A1153 9179 11771 8860 -338 97 2640 C ATOM 2762 CD1 PHE A1153 29.545 5.562 35.550 1.00 80.53 C ANISOU 2762 CD1 PHE A1153 9626 11724 9246 -336 114 2573 C ATOM 2763 CD2 PHE A1153 29.419 6.530 37.725 1.00 79.88 C ANISOU 2763 CD2 PHE A1153 9282 12171 8898 -334 151 2613 C ATOM 2764 CE1 PHE A1153 30.833 6.081 35.394 1.00 80.53 C ANISOU 2764 CE1 PHE A1153 9738 11638 9224 -330 186 2485 C ATOM 2765 CE2 PHE A1153 30.702 7.053 37.566 1.00 81.87 C ANISOU 2765 CE2 PHE A1153 9651 12320 9135 -332 217 2519 C ATOM 2766 CZ PHE A1153 31.408 6.811 36.410 1.00 79.36 C ANISOU 2766 CZ PHE A1153 9516 11698 8940 -332 236 2465 C ATOM 2767 N ARG A1154 24.228 4.924 36.937 1.00 80.34 N ANISOU 2767 N ARG A1154 9114 12345 9068 -305 -141 2879 N ATOM 2768 CA ARG A1154 23.064 4.046 37.030 1.00 81.03 C ANISOU 2768 CA ARG A1154 9056 12497 9234 -338 -236 3063 C ATOM 2769 C ARG A1154 21.999 4.407 35.979 1.00 84.53 C ANISOU 2769 C ARG A1154 9659 12786 9672 -282 -276 2940 C ATOM 2770 O ARG A1154 21.685 3.580 35.121 1.00 84.16 O ANISOU 2770 O ARG A1154 9670 12512 9795 -313 -341 2994 O ATOM 2771 CB ARG A1154 22.459 4.100 38.443 1.00 82.24 C ANISOU 2771 CB ARG A1154 8941 13056 9250 -343 -251 3213 C ATOM 2772 N THR A1155 21.458 5.643 36.043 1.00 80.86 N ANISOU 2772 N THR A1155 9264 12441 9017 -198 -241 2770 N ATOM 2773 CA THR A1155 20.379 6.103 35.155 1.00 80.41 C ANISOU 2773 CA THR A1155 9343 12277 8932 -142 -274 2656 C ATOM 2774 C THR A1155 20.860 6.309 33.706 1.00 83.64 C ANISOU 2774 C THR A1155 10020 12325 9433 -122 -252 2481 C ATOM 2775 O THR A1155 20.126 5.990 32.768 1.00 83.15 O ANISOU 2775 O THR A1155 10049 12091 9455 -118 -305 2469 O ATOM 2776 CB THR A1155 19.754 7.407 35.689 1.00 87.45 C ANISOU 2776 CB THR A1155 10227 13405 9596 -53 -241 2518 C ATOM 2777 OG1 THR A1155 20.747 8.437 35.714 1.00 85.04 O ANISOU 2777 OG1 THR A1155 10044 13065 9201 -10 -162 2323 O ATOM 2778 CG2 THR A1155 19.125 7.239 37.073 1.00 87.32 C ANISOU 2778 CG2 THR A1155 9938 13776 9465 -56 -267 2685 C ATOM 2779 N GLY A1156 22.061 6.864 33.543 1.00 79.54 N ANISOU 2779 N GLY A1156 9618 11710 8892 -108 -177 2350 N ATOM 2780 CA GLY A1156 22.611 7.170 32.227 1.00 78.33 C ANISOU 2780 CA GLY A1156 9706 11252 8803 -81 -149 2184 C ATOM 2781 C GLY A1156 21.986 8.413 31.634 1.00 81.46 C ANISOU 2781 C GLY A1156 10254 11620 9078 0 -131 1985 C ATOM 2782 O GLY A1156 21.785 8.494 30.418 1.00 80.13 O ANISOU 2782 O GLY A1156 10254 11224 8969 22 -141 1888 O ATOM 2783 N THR A1157 21.642 9.386 32.505 1.00 78.35 N ANISOU 2783 N THR A1157 9790 11467 8513 47 -109 1924 N ATOM 2784 CA THR A1157 21.019 10.650 32.108 1.00 77.71 C ANISOU 2784 CA THR A1157 9828 11387 8310 128 -96 1736 C ATOM 2785 C THR A1157 21.413 11.774 33.094 1.00 80.26 C ANISOU 2785 C THR A1157 10104 11921 8472 178 -54 1630 C ATOM 2786 O THR A1157 21.877 11.493 34.206 1.00 80.14 O ANISOU 2786 O THR A1157 9928 12105 8416 150 -41 1727 O ATOM 2787 CB THR A1157 19.484 10.492 31.999 1.00 89.86 C ANISOU 2787 CB THR A1157 11314 13006 9822 148 -157 1788 C ATOM 2788 OG1 THR A1157 18.919 11.711 31.512 1.00 91.90 O ANISOU 2788 OG1 THR A1157 11700 13239 9978 226 -144 1602 O ATOM 2789 CG2 THR A1157 18.830 10.095 33.323 1.00 89.83 C ANISOU 2789 CG2 THR A1157 11063 13327 9741 135 -189 1955 C ATOM 2790 N TRP A1158 21.210 13.043 32.680 1.00 75.35 N ANISOU 2790 N TRP A1158 9615 11253 7761 252 -38 1431 N ATOM 2791 CA TRP A1158 21.548 14.224 33.483 1.00 74.63 C ANISOU 2791 CA TRP A1158 9503 11325 7528 310 -13 1296 C ATOM 2792 C TRP A1158 20.396 14.616 34.440 1.00 77.87 C ANISOU 2792 C TRP A1158 9763 12037 7789 370 -44 1297 C ATOM 2793 O TRP A1158 20.279 15.790 34.804 1.00 77.40 O ANISOU 2793 O TRP A1158 9725 12076 7608 447 -41 1134 O ATOM 2794 CB TRP A1158 21.896 15.415 32.564 1.00 72.42 C ANISOU 2794 CB TRP A1158 9432 10841 7245 362 5 1086 C ATOM 2795 CG TRP A1158 23.030 15.153 31.622 1.00 72.34 C ANISOU 2795 CG TRP A1158 9565 10563 7359 317 37 1078 C ATOM 2796 CD1 TRP A1158 22.944 14.871 30.292 1.00 74.58 C ANISOU 2796 CD1 TRP A1158 9994 10597 7746 306 34 1062 C ATOM 2797 CD2 TRP A1158 24.425 15.144 31.946 1.00 71.89 C ANISOU 2797 CD2 TRP A1158 9511 10477 7327 283 76 1088 C ATOM 2798 NE1 TRP A1158 24.202 14.703 29.761 1.00 73.41 N ANISOU 2798 NE1 TRP A1158 9938 10274 7681 275 70 1059 N ATOM 2799 CE2 TRP A1158 25.130 14.856 30.757 1.00 75.01 C ANISOU 2799 CE2 TRP A1158 10056 10603 7840 257 97 1080 C ATOM 2800 CE3 TRP A1158 25.152 15.351 33.129 1.00 73.52 C ANISOU 2800 CE3 TRP A1158 9604 10867 7462 274 96 1105 C ATOM 2801 CZ2 TRP A1158 26.524 14.756 30.720 1.00 73.99 C ANISOU 2801 CZ2 TRP A1158 9966 10384 7761 222 137 1098 C ATOM 2802 CZ3 TRP A1158 26.533 15.262 33.087 1.00 74.56 C ANISOU 2802 CZ3 TRP A1158 9779 10900 7649 232 135 1121 C ATOM 2803 CH2 TRP A1158 27.205 14.974 31.894 1.00 74.43 C ANISOU 2803 CH2 TRP A1158 9913 10615 7752 208 156 1121 C ATOM 2804 N ASP A1159 19.568 13.635 34.865 1.00 74.29 N ANISOU 2804 N ASP A1159 9148 11733 7345 337 -80 1484 N ATOM 2805 CA ASP A1159 18.440 13.886 35.773 1.00 74.93 C ANISOU 2805 CA ASP A1159 9066 12126 7280 394 -112 1516 C ATOM 2806 C ASP A1159 18.921 14.254 37.186 1.00 78.59 C ANISOU 2806 C ASP A1159 9363 12894 7605 423 -92 1509 C ATOM 2807 O ASP A1159 18.194 14.921 37.924 1.00 78.75 O ANISOU 2807 O ASP A1159 9285 13170 7466 505 -108 1446 O ATOM 2808 CB ASP A1159 17.505 12.667 35.836 1.00 77.48 C ANISOU 2808 CB ASP A1159 9248 12525 7665 341 -162 1747 C ATOM 2809 CG ASP A1159 16.572 12.519 34.639 1.00 88.44 C ANISOU 2809 CG ASP A1159 10767 13704 9131 344 -198 1735 C ATOM 2810 OD1 ASP A1159 16.645 13.368 33.715 1.00 87.86 O ANISOU 2810 OD1 ASP A1159 10894 13425 9062 386 -177 1546 O ATOM 2811 OD2 ASP A1159 15.766 11.561 34.629 1.00 95.72 O1- ANISOU 2811 OD2 ASP A1159 11584 14671 10114 300 -251 1920 O1- ATOM 2812 N ALA A1160 20.152 13.843 37.546 1.00 74.60 N ANISOU 2812 N ALA A1160 8827 12363 7156 360 -59 1567 N ATOM 2813 CA ALA A1160 20.743 14.134 38.852 1.00 75.00 C ANISOU 2813 CA ALA A1160 8723 12688 7085 377 -39 1566 C ATOM 2814 C ALA A1160 21.341 15.555 38.903 1.00 78.31 C ANISOU 2814 C ALA A1160 9269 13072 7415 453 -17 1310 C ATOM 2815 O ALA A1160 21.735 16.014 39.978 1.00 78.59 O ANISOU 2815 O ALA A1160 9191 13342 7328 487 -9 1262 O ATOM 2816 CB ALA A1160 21.815 13.106 39.177 1.00 75.69 C ANISOU 2816 CB ALA A1160 8728 12752 7280 273 -13 1740 C ATOM 2817 N TYR A1161 21.390 16.253 37.747 1.00 74.12 N ANISOU 2817 N TYR A1161 8964 12252 6946 480 -16 1149 N ATOM 2818 CA TYR A1161 21.936 17.611 37.658 1.00 74.05 C ANISOU 2818 CA TYR A1161 9085 12167 6883 546 -11 914 C ATOM 2819 C TYR A1161 20.900 18.583 37.080 1.00 81.67 C ANISOU 2819 C TYR A1161 10155 13078 7799 637 -44 748 C ATOM 2820 O TYR A1161 20.483 19.511 37.774 1.00 82.02 O ANISOU 2820 O TYR A1161 10145 13312 7706 730 -69 609 O ATOM 2821 CB TYR A1161 23.221 17.629 36.807 1.00 73.05 C ANISOU 2821 CB TYR A1161 9131 11734 6892 486 23 883 C ATOM 2822 CG TYR A1161 24.347 16.808 37.395 1.00 72.95 C ANISOU 2822 CG TYR A1161 9025 11767 6925 403 58 1028 C ATOM 2823 CD1 TYR A1161 25.180 17.333 38.377 1.00 75.04 C ANISOU 2823 CD1 TYR A1161 9220 12187 7106 415 70 970 C ATOM 2824 CD2 TYR A1161 24.594 15.512 36.955 1.00 72.67 C ANISOU 2824 CD2 TYR A1161 8973 11614 7024 313 75 1218 C ATOM 2825 CE1 TYR A1161 26.219 16.583 38.921 1.00 75.17 C ANISOU 2825 CE1 TYR A1161 9147 12250 7163 335 106 1110 C ATOM 2826 CE2 TYR A1161 25.631 14.752 37.491 1.00 73.27 C ANISOU 2826 CE2 TYR A1161 8960 11728 7150 236 108 1354 C ATOM 2827 CZ TYR A1161 26.442 15.292 38.475 1.00 79.66 C ANISOU 2827 CZ TYR A1161 9698 12701 7869 245 127 1306 C ATOM 2828 OH TYR A1161 27.467 14.553 39.011 1.00 79.17 O ANISOU 2828 OH TYR A1161 9545 12682 7855 167 162 1447 O ATOM 2829 N ALA A 245 20.482 18.364 35.810 1.00 80.48 N ANISOU 2829 N ALA A 245 10149 12672 7759 614 -47 758 N ATOM 2830 CA ALA A 245 19.495 19.207 35.125 1.00 81.62 C ANISOU 2830 CA ALA A 245 10400 12738 7876 688 -75 620 C ATOM 2831 C ALA A 245 18.082 18.628 35.265 1.00 89.50 C ANISOU 2831 C ALA A 245 11287 13896 8824 704 -102 734 C ATOM 2832 O ALA A 245 17.891 17.422 35.091 1.00 89.30 O ANISOU 2832 O ALA A 245 11202 13853 8877 629 -102 927 O ATOM 2833 CB ALA A 245 19.860 19.349 33.658 1.00 81.30 C ANISOU 2833 CB ALA A 245 10573 12343 7973 654 -63 567 C ATOM 2834 N SER A 246 17.092 19.489 35.576 1.00 89.00 N ANISOU 2834 N SER A 246 11194 13986 8638 804 -131 617 N ATOM 2835 CA SER A 246 15.703 19.061 35.776 1.00 90.53 C ANISOU 2835 CA SER A 246 11273 14360 8764 832 -159 722 C ATOM 2836 C SER A 246 14.975 18.862 34.439 1.00 96.19 C ANISOU 2836 C SER A 246 12134 14828 9584 807 -169 741 C ATOM 2837 O SER A 246 14.450 17.773 34.183 1.00 95.30 O ANISOU 2837 O SER A 246 11967 14708 9535 744 -182 928 O ATOM 2838 CB SER A 246 14.949 20.073 36.638 1.00 95.12 C ANISOU 2838 CB SER A 246 11763 15213 9165 958 -184 584 C ATOM 2839 N ARG A 247 14.936 19.916 33.592 1.00 94.71 N ANISOU 2839 N ARG A 247 12124 14442 9420 854 -170 553 N ATOM 2840 CA ARG A 247 14.241 19.878 32.298 1.00 94.80 C ANISOU 2840 CA ARG A 247 12277 14227 9517 839 -178 550 C ATOM 2841 C ARG A 247 15.230 19.982 31.120 1.00 99.41 C ANISOU 2841 C ARG A 247 13054 14474 10245 784 -153 490 C ATOM 2842 O ARG A 247 14.852 19.693 29.979 1.00 98.44 O ANISOU 2842 O ARG A 247 13042 14150 10211 752 -155 517 O ATOM 2843 CB ARG A 247 13.188 21.002 32.210 1.00 95.40 C ANISOU 2843 CB ARG A 247 12384 14365 9499 943 -203 400 C ATOM 2844 CG ARG A 247 12.012 20.815 33.166 1.00106.66 C ANISOU 2844 CG ARG A 247 13626 16118 10783 1002 -229 478 C ATOM 2845 CD ARG A 247 10.898 21.806 32.895 1.00115.75 C ANISOU 2845 CD ARG A 247 14822 17299 11858 1099 -253 346 C ATOM 2846 NE ARG A 247 9.738 21.566 33.756 1.00122.37 N ANISOU 2846 NE ARG A 247 15481 18460 12556 1158 -276 438 N ATOM 2847 CZ ARG A 247 8.555 22.150 33.590 1.00134.61 C ANISOU 2847 CZ ARG A 247 17033 20080 14031 1238 -298 381 C ATOM 2848 NH1 ARG A 247 8.359 22.998 32.587 1.00119.81 N ANISOU 2848 NH1 ARG A 247 15334 17971 12217 1263 -299 233 N ATOM 2849 NH2 ARG A 247 7.553 21.876 34.416 1.00121.47 N ANISOU 2849 NH2 ARG A 247 15191 18732 12232 1293 -319 483 N ATOM 2850 N SER A 248 16.496 20.374 31.394 1.00 96.96 N ANISOU 2850 N SER A 248 12775 14114 9952 775 -131 415 N ATOM 2851 CA SER A 248 17.529 20.486 30.355 1.00 96.30 C ANISOU 2851 CA SER A 248 12856 13739 9992 728 -107 371 C ATOM 2852 C SER A 248 18.096 19.095 29.986 1.00 99.45 C ANISOU 2852 C SER A 248 13249 14035 10502 631 -84 546 C ATOM 2853 O SER A 248 18.825 18.966 28.998 1.00 98.17 O ANISOU 2853 O SER A 248 13218 13636 10446 592 -64 535 O ATOM 2854 CB SER A 248 18.647 21.421 30.806 1.00100.60 C ANISOU 2854 CB SER A 248 13431 14276 10517 753 -101 240 C ATOM 2855 OG SER A 248 18.161 22.740 31.003 1.00110.67 O ANISOU 2855 OG SER A 248 14730 15603 11718 845 -135 61 O ATOM 2856 N SER A 249 17.724 18.058 30.768 1.00 96.19 N ANISOU 2856 N SER A 249 12676 13805 10068 597 -93 711 N ATOM 2857 CA SER A 249 18.113 16.667 30.531 1.00 95.55 C ANISOU 2857 CA SER A 249 12562 13644 10100 508 -88 889 C ATOM 2858 C SER A 249 17.117 15.978 29.590 1.00 98.23 C ANISOU 2858 C SER A 249 12947 13863 10513 485 -119 967 C ATOM 2859 O SER A 249 17.504 15.103 28.814 1.00 97.08 O ANISOU 2859 O SER A 249 12864 13528 10495 425 -119 1041 O ATOM 2860 CB SER A 249 18.194 15.910 31.852 1.00100.20 C ANISOU 2860 CB SER A 249 12940 14489 10641 479 -93 1041 C ATOM 2861 OG SER A 249 16.965 15.975 32.560 1.00109.80 O ANISOU 2861 OG SER A 249 14019 15954 11746 524 -127 1085 O ATOM 2862 N GLU A 250 15.826 16.374 29.670 1.00 94.86 N ANISOU 2862 N GLU A 250 12487 13551 10006 535 -149 946 N ATOM 2863 CA GLU A 250 14.742 15.840 28.830 1.00 94.46 C ANISOU 2863 CA GLU A 250 12474 13407 10009 519 -184 1015 C ATOM 2864 C GLU A 250 14.901 16.294 27.375 1.00 96.58 C ANISOU 2864 C GLU A 250 12951 13391 10355 523 -170 893 C ATOM 2865 O GLU A 250 14.432 15.612 26.463 1.00 95.59 O ANISOU 2865 O GLU A 250 12885 13119 10317 488 -194 954 O ATOM 2866 CB GLU A 250 13.370 16.292 29.371 1.00 96.61 C ANISOU 2866 CB GLU A 250 12652 13899 10156 581 -214 1017 C ATOM 2867 CG GLU A 250 13.048 15.776 30.766 1.00109.59 C ANISOU 2867 CG GLU A 250 14069 15857 11714 581 -234 1160 C ATOM 2868 CD GLU A 250 11.828 16.392 31.431 1.00132.60 C ANISOU 2868 CD GLU A 250 16879 19030 14475 663 -257 1141 C ATOM 2869 OE1 GLU A 250 11.331 17.430 30.934 1.00122.10 O ANISOU 2869 OE1 GLU A 250 15658 17640 13093 731 -252 981 O ATOM 2870 OE2 GLU A 250 11.398 15.862 32.481 1.00131.18 O1- ANISOU 2870 OE2 GLU A 250 16499 19123 14221 663 -280 1287 O1- ATOM 2871 N ASN A 251 15.569 17.454 27.166 1.00 92.32 N ANISOU 2871 N ASN A 251 12514 12779 9784 567 -138 724 N ATOM 2872 CA ASN A 251 15.813 18.053 25.848 1.00 90.93 C ANISOU 2872 CA ASN A 251 12520 12359 9669 576 -123 607 C ATOM 2873 C ASN A 251 16.766 17.196 25.001 1.00 93.23 C ANISOU 2873 C ASN A 251 12893 12442 10088 515 -106 662 C ATOM 2874 O ASN A 251 16.808 17.363 23.784 1.00 92.12 O ANISOU 2874 O ASN A 251 12888 12109 10006 515 -100 605 O ATOM 2875 CB ASN A 251 16.389 19.472 26.000 1.00 91.26 C ANISOU 2875 CB ASN A 251 12623 12395 9658 633 -106 437 C ATOM 2876 CG ASN A 251 15.548 20.409 26.846 1.00116.51 C ANISOU 2876 CG ASN A 251 15745 15792 12732 709 -128 353 C ATOM 2877 OD1 ASN A 251 14.336 20.225 27.024 1.00112.30 O ANISOU 2877 OD1 ASN A 251 15148 15377 12145 732 -152 399 O ATOM 2878 ND2 ASN A 251 16.173 21.455 27.360 1.00108.88 N ANISOU 2878 ND2 ASN A 251 14786 14865 11719 755 -126 223 N ATOM 2879 N VAL A 252 17.536 16.287 25.647 1.00 89.40 N ANISOU 2879 N VAL A 252 12320 12007 9642 466 -98 773 N ATOM 2880 CA VAL A 252 18.472 15.385 24.961 1.00 88.59 C ANISOU 2880 CA VAL A 252 12277 11723 9659 414 -84 830 C ATOM 2881 C VAL A 252 17.680 14.446 24.025 1.00 91.27 C ANISOU 2881 C VAL A 252 12655 11938 10085 387 -124 900 C ATOM 2882 O VAL A 252 18.029 14.318 22.852 1.00 90.07 O ANISOU 2882 O VAL A 252 12631 11586 10005 384 -116 852 O ATOM 2883 CB VAL A 252 19.357 14.593 25.973 1.00 92.93 C ANISOU 2883 CB VAL A 252 12703 12373 10233 367 -72 945 C ATOM 2884 CG1 VAL A 252 20.236 13.564 25.261 1.00 92.42 C ANISOU 2884 CG1 VAL A 252 12693 12122 10301 318 -64 1010 C ATOM 2885 CG2 VAL A 252 20.212 15.540 26.814 1.00 92.76 C ANISOU 2885 CG2 VAL A 252 12656 12459 10129 393 -35 866 C ATOM 2886 N ALA A 253 16.584 13.846 24.534 1.00 87.96 N ANISOU 2886 N ALA A 253 12122 11645 9653 372 -171 1011 N ATOM 2887 CA ALA A 253 15.713 12.975 23.739 1.00 87.71 C ANISOU 2887 CA ALA A 253 12114 11507 9704 345 -224 1084 C ATOM 2888 C ALA A 253 14.866 13.794 22.757 1.00 90.60 C ANISOU 2888 C ALA A 253 12603 11789 10032 388 -226 971 C ATOM 2889 O ALA A 253 14.573 13.321 21.660 1.00 89.81 O ANISOU 2889 O ALA A 253 12592 11521 10009 374 -250 968 O ATOM 2890 CB ALA A 253 14.812 12.160 24.654 1.00 89.25 C ANISOU 2890 CB ALA A 253 12136 11880 9895 313 -280 1254 C ATOM 2891 N LEU A 254 14.494 15.034 23.150 1.00 86.89 N ANISOU 2891 N LEU A 254 12133 11435 9444 443 -202 872 N ATOM 2892 CA LEU A 254 13.688 15.948 22.329 1.00 86.23 C ANISOU 2892 CA LEU A 254 12153 11290 9319 486 -202 763 C ATOM 2893 C LEU A 254 14.501 16.542 21.174 1.00 87.72 C ANISOU 2893 C LEU A 254 12502 11275 9553 499 -165 639 C ATOM 2894 O LEU A 254 13.913 17.038 20.216 1.00 86.89 O ANISOU 2894 O LEU A 254 12492 11075 9447 520 -168 571 O ATOM 2895 CB LEU A 254 13.108 17.083 23.195 1.00 86.91 C ANISOU 2895 CB LEU A 254 12178 11568 9275 547 -195 693 C ATOM 2896 CG LEU A 254 11.649 16.920 23.661 1.00 92.59 C ANISOU 2896 CG LEU A 254 12798 12454 9928 563 -236 773 C ATOM 2897 CD1 LEU A 254 11.518 15.828 24.732 1.00 93.53 C ANISOU 2897 CD1 LEU A 254 12743 12748 10047 524 -267 949 C ATOM 2898 CD2 LEU A 254 11.116 18.224 24.211 1.00 95.62 C ANISOU 2898 CD2 LEU A 254 13160 12985 10187 642 -226 658 C ATOM 2899 N LEU A 255 15.847 16.531 21.280 1.00 82.87 N ANISOU 2899 N LEU A 255 11910 10607 8972 488 -130 617 N ATOM 2900 CA LEU A 255 16.718 17.041 20.218 1.00 81.54 C ANISOU 2900 CA LEU A 255 11876 10263 8843 499 -98 521 C ATOM 2901 C LEU A 255 17.149 15.909 19.303 1.00 84.03 C ANISOU 2901 C LEU A 255 12246 10421 9261 465 -104 575 C ATOM 2902 O LEU A 255 17.144 16.075 18.086 1.00 83.34 O ANISOU 2902 O LEU A 255 12268 10194 9204 479 -99 515 O ATOM 2903 CB LEU A 255 17.947 17.753 20.799 1.00 81.45 C ANISOU 2903 CB LEU A 255 11860 10281 8806 512 -60 466 C ATOM 2904 N LYS A 256 17.487 14.738 19.886 1.00 80.14 N ANISOU 2904 N LYS A 256 11668 9957 8824 423 -121 688 N ATOM 2905 CA LYS A 256 17.917 13.557 19.134 1.00 79.57 C ANISOU 2905 CA LYS A 256 11634 9739 8862 396 -139 738 C ATOM 2906 C LYS A 256 16.851 13.129 18.125 1.00 82.20 C ANISOU 2906 C LYS A 256 12023 9974 9233 396 -187 735 C ATOM 2907 O LYS A 256 17.195 12.776 16.999 1.00 81.59 O ANISOU 2907 O LYS A 256 12042 9743 9215 405 -189 692 O ATOM 2908 CB LYS A 256 18.245 12.393 20.083 1.00 82.49 C ANISOU 2908 CB LYS A 256 11878 10174 9293 348 -164 874 C ATOM 2909 N THR A 257 15.556 13.214 18.512 1.00 77.99 N ANISOU 2909 N THR A 257 11432 9542 8659 392 -225 778 N ATOM 2910 CA THR A 257 14.434 12.836 17.648 1.00 77.58 C ANISOU 2910 CA THR A 257 11424 9413 8639 388 -276 789 C ATOM 2911 C THR A 257 14.320 13.791 16.429 1.00 80.05 C ANISOU 2911 C THR A 257 11876 9624 8915 429 -244 655 C ATOM 2912 O THR A 257 14.079 13.323 15.313 1.00 79.68 O ANISOU 2912 O THR A 257 11907 9445 8922 428 -270 633 O ATOM 2913 CB THR A 257 13.111 12.781 18.452 1.00 86.16 C ANISOU 2913 CB THR A 257 12402 10656 9677 375 -320 880 C ATOM 2914 OG1 THR A 257 12.070 12.301 17.607 1.00 86.29 O ANISOU 2914 OG1 THR A 257 12460 10588 9738 363 -376 906 O ATOM 2915 CG2 THR A 257 12.711 14.132 19.044 1.00 84.78 C ANISOU 2915 CG2 THR A 257 12209 10630 9374 419 -280 811 C ATOM 2916 N VAL A 258 14.543 15.112 16.643 1.00 75.19 N ANISOU 2916 N VAL A 258 11284 9070 8214 464 -194 568 N ATOM 2917 CA VAL A 258 14.442 16.133 15.590 1.00 74.04 C ANISOU 2917 CA VAL A 258 11250 8845 8039 499 -166 457 C ATOM 2918 C VAL A 258 15.559 15.935 14.531 1.00 76.75 C ANISOU 2918 C VAL A 258 11686 9040 8435 507 -140 407 C ATOM 2919 O VAL A 258 15.310 16.136 13.339 1.00 75.79 O ANISOU 2919 O VAL A 258 11650 8825 8321 524 -140 353 O ATOM 2920 CB VAL A 258 14.459 17.566 16.181 1.00 77.64 C ANISOU 2920 CB VAL A 258 11693 9397 8410 534 -134 383 C ATOM 2921 CG1 VAL A 258 14.432 18.614 15.077 1.00 77.15 C ANISOU 2921 CG1 VAL A 258 11735 9243 8336 564 -113 283 C ATOM 2922 CG2 VAL A 258 13.286 17.774 17.133 1.00 77.75 C ANISOU 2922 CG2 VAL A 258 11615 9568 8357 542 -161 420 C ATOM 2923 N ILE A 259 16.762 15.493 14.964 1.00 73.13 N ANISOU 2923 N ILE A 259 11202 8574 8011 497 -119 433 N ATOM 2924 CA ILE A 259 17.883 15.206 14.052 1.00 72.41 C ANISOU 2924 CA ILE A 259 11184 8363 7965 511 -94 399 C ATOM 2925 C ILE A 259 17.475 14.067 13.088 1.00 74.60 C ANISOU 2925 C ILE A 259 11502 8531 8312 508 -138 412 C ATOM 2926 O ILE A 259 17.793 14.126 11.895 1.00 73.84 O ANISOU 2926 O ILE A 259 11490 8341 8224 538 -127 349 O ATOM 2927 CB ILE A 259 19.186 14.856 14.842 1.00 75.74 C ANISOU 2927 CB ILE A 259 11557 8810 8411 498 -66 441 C ATOM 2928 CG1 ILE A 259 19.501 15.929 15.908 1.00 76.33 C ANISOU 2928 CG1 ILE A 259 11581 9002 8417 500 -35 426 C ATOM 2929 CG2 ILE A 259 20.381 14.658 13.886 1.00 76.31 C ANISOU 2929 CG2 ILE A 259 11704 8773 8518 522 -35 405 C ATOM 2930 CD1 ILE A 259 20.484 15.475 17.027 1.00 86.44 C ANISOU 2930 CD1 ILE A 259 12780 10350 9714 474 -18 492 C ATOM 2931 N ILE A 260 16.718 13.066 13.600 1.00 70.14 N ANISOU 2931 N ILE A 260 10869 7985 7796 473 -197 496 N ATOM 2932 CA ILE A 260 16.253 11.941 12.782 1.00 69.77 C ANISOU 2932 CA ILE A 260 10851 7827 7830 466 -259 511 C ATOM 2933 C ILE A 260 15.152 12.431 11.809 1.00 72.05 C ANISOU 2933 C ILE A 260 11211 8084 8081 482 -276 455 C ATOM 2934 O ILE A 260 15.085 11.935 10.685 1.00 72.28 O ANISOU 2934 O ILE A 260 11309 8005 8150 500 -302 408 O ATOM 2935 CB ILE A 260 15.772 10.728 13.643 1.00 73.39 C ANISOU 2935 CB ILE A 260 11204 8310 8370 417 -331 636 C ATOM 2936 CG1 ILE A 260 16.652 10.539 14.901 1.00 73.71 C ANISOU 2936 CG1 ILE A 260 11147 8439 8420 393 -305 710 C ATOM 2937 CG2 ILE A 260 15.748 9.441 12.795 1.00 74.67 C ANISOU 2937 CG2 ILE A 260 11399 8322 8648 415 -402 640 C ATOM 2938 CD1 ILE A 260 16.042 9.663 15.993 1.00 79.92 C ANISOU 2938 CD1 ILE A 260 11797 9309 9260 340 -368 855 C ATOM 2939 N VAL A 261 14.337 13.451 12.217 1.00 66.21 N ANISOU 2939 N VAL A 261 10452 7443 7261 481 -258 450 N ATOM 2940 CA VAL A 261 13.300 14.034 11.340 1.00 64.77 C ANISOU 2940 CA VAL A 261 10331 7239 7038 495 -266 402 C ATOM 2941 C VAL A 261 13.972 14.606 10.086 1.00 66.86 C ANISOU 2941 C VAL A 261 10697 7421 7286 534 -223 301 C ATOM 2942 O VAL A 261 13.554 14.293 8.968 1.00 66.31 O ANISOU 2942 O VAL A 261 10689 7273 7234 545 -248 265 O ATOM 2943 CB VAL A 261 12.434 15.117 12.054 1.00 67.98 C ANISOU 2943 CB VAL A 261 10696 7771 7361 497 -250 407 C ATOM 2944 CG1 VAL A 261 11.347 15.654 11.125 1.00 67.37 C ANISOU 2944 CG1 VAL A 261 10680 7666 7252 507 -260 367 C ATOM 2945 CG2 VAL A 261 11.821 14.580 13.337 1.00 68.17 C ANISOU 2945 CG2 VAL A 261 10604 7911 7385 466 -289 516 C ATOM 2946 N LEU A 262 15.042 15.412 10.283 1.00 62.18 N ANISOU 2946 N LEU A 262 10112 6853 6661 555 -164 262 N ATOM 2947 CA LEU A 262 15.814 16.024 9.198 1.00 61.44 C ANISOU 2947 CA LEU A 262 10092 6703 6548 592 -123 189 C ATOM 2948 C LEU A 262 16.498 14.946 8.336 1.00 66.53 C ANISOU 2948 C LEU A 262 10777 7256 7246 612 -137 173 C ATOM 2949 O LEU A 262 16.500 15.051 7.102 1.00 66.52 O ANISOU 2949 O LEU A 262 10838 7204 7230 644 -132 116 O ATOM 2950 CB LEU A 262 16.865 16.989 9.782 1.00 60.79 C ANISOU 2950 CB LEU A 262 9992 6669 6435 603 -71 176 C ATOM 2951 CG LEU A 262 17.779 17.678 8.772 1.00 64.89 C ANISOU 2951 CG LEU A 262 10568 7147 6939 637 -32 125 C ATOM 2952 CD1 LEU A 262 17.123 18.909 8.194 1.00 64.77 C ANISOU 2952 CD1 LEU A 262 10581 7144 6883 648 -24 85 C ATOM 2953 CD2 LEU A 262 19.107 18.029 9.395 1.00 67.09 C ANISOU 2953 CD2 LEU A 262 10823 7449 7219 641 4 139 C ATOM 2954 N SER A 263 17.056 13.903 8.991 1.00 63.17 N ANISOU 2954 N SER A 263 10308 6813 6881 597 -157 221 N ATOM 2955 CA SER A 263 17.745 12.799 8.319 1.00 63.43 C ANISOU 2955 CA SER A 263 10369 6756 6975 622 -179 203 C ATOM 2956 C SER A 263 16.792 12.028 7.390 1.00 66.63 C ANISOU 2956 C SER A 263 10814 7084 7418 629 -245 174 C ATOM 2957 O SER A 263 17.223 11.544 6.344 1.00 66.73 O ANISOU 2957 O SER A 263 10879 7028 7447 673 -256 110 O ATOM 2958 CB SER A 263 18.360 11.854 9.344 1.00 68.10 C ANISOU 2958 CB SER A 263 10892 7346 7637 595 -197 275 C ATOM 2959 OG SER A 263 19.253 12.545 10.204 1.00 76.59 O ANISOU 2959 OG SER A 263 11930 8496 8675 588 -137 300 O ATOM 2960 N VAL A 264 15.497 11.935 7.763 1.00 61.96 N ANISOU 2960 N VAL A 264 10195 6514 6835 589 -293 220 N ATOM 2961 CA VAL A 264 14.476 11.285 6.935 1.00 61.57 C ANISOU 2961 CA VAL A 264 10179 6394 6820 587 -364 201 C ATOM 2962 C VAL A 264 14.099 12.234 5.779 1.00 64.71 C ANISOU 2962 C VAL A 264 10650 6798 7138 619 -328 122 C ATOM 2963 O VAL A 264 13.983 11.794 4.633 1.00 64.88 O ANISOU 2963 O VAL A 264 10727 6753 7171 650 -357 57 O ATOM 2964 CB VAL A 264 13.232 10.860 7.778 1.00 65.21 C ANISOU 2964 CB VAL A 264 10573 6886 7317 529 -430 300 C ATOM 2965 CG1 VAL A 264 12.103 10.348 6.888 1.00 65.22 C ANISOU 2965 CG1 VAL A 264 10615 6818 7349 523 -504 285 C ATOM 2966 CG2 VAL A 264 13.609 9.808 8.813 1.00 65.48 C ANISOU 2966 CG2 VAL A 264 10523 6914 7444 496 -475 392 C ATOM 2967 N PHE A 265 13.970 13.543 6.079 1.00 60.04 N ANISOU 2967 N PHE A 265 10053 6291 6471 614 -268 123 N ATOM 2968 CA PHE A 265 13.616 14.562 5.094 1.00 59.44 C ANISOU 2968 CA PHE A 265 10029 6230 6327 636 -234 66 C ATOM 2969 C PHE A 265 14.650 14.622 3.957 1.00 63.20 C ANISOU 2969 C PHE A 265 10555 6674 6783 690 -200 -5 C ATOM 2970 O PHE A 265 14.265 14.637 2.784 1.00 62.76 O ANISOU 2970 O PHE A 265 10546 6597 6705 715 -210 -56 O ATOM 2971 CB PHE A 265 13.483 15.937 5.768 1.00 60.76 C ANISOU 2971 CB PHE A 265 10168 6482 6436 624 -184 81 C ATOM 2972 CG PHE A 265 12.959 17.024 4.859 1.00 62.06 C ANISOU 2972 CG PHE A 265 10372 6661 6547 637 -158 40 C ATOM 2973 CD1 PHE A 265 11.597 17.286 4.774 1.00 65.24 C ANISOU 2973 CD1 PHE A 265 10775 7081 6930 614 -183 56 C ATOM 2974 CD2 PHE A 265 13.830 17.805 4.106 1.00 63.86 C ANISOU 2974 CD2 PHE A 265 10626 6892 6745 670 -110 -1 C ATOM 2975 CE1 PHE A 265 11.114 18.293 3.938 1.00 65.98 C ANISOU 2975 CE1 PHE A 265 10899 7188 6982 623 -159 25 C ATOM 2976 CE2 PHE A 265 13.346 18.804 3.263 1.00 66.74 C ANISOU 2976 CE2 PHE A 265 11013 7273 7071 678 -92 -25 C ATOM 2977 CZ PHE A 265 11.991 19.044 3.185 1.00 64.94 C ANISOU 2977 CZ PHE A 265 10788 7056 6829 653 -115 -14 C ATOM 2978 N ILE A 266 15.957 14.632 4.301 1.00 59.50 N ANISOU 2978 N ILE A 266 10071 6215 6321 711 -162 -3 N ATOM 2979 CA ILE A 266 17.030 14.690 3.298 1.00 59.35 C ANISOU 2979 CA ILE A 266 10087 6187 6276 769 -127 -56 C ATOM 2980 C ILE A 266 17.126 13.349 2.528 1.00 64.01 C ANISOU 2980 C ILE A 266 10707 6704 6910 807 -179 -106 C ATOM 2981 O ILE A 266 17.664 13.321 1.429 1.00 64.03 O ANISOU 2981 O ILE A 266 10743 6709 6877 866 -164 -167 O ATOM 2982 CB ILE A 266 18.408 15.090 3.919 1.00 62.06 C ANISOU 2982 CB ILE A 266 10402 6564 6613 779 -74 -28 C ATOM 2983 CG1 ILE A 266 18.946 14.002 4.888 1.00 62.60 C ANISOU 2983 CG1 ILE A 266 10435 6600 6751 763 -96 11 C ATOM 2984 CG2 ILE A 266 18.335 16.474 4.589 1.00 61.93 C ANISOU 2984 CG2 ILE A 266 10359 6611 6560 749 -35 4 C ATOM 2985 CD1 ILE A 266 20.482 13.954 5.015 1.00 69.73 C ANISOU 2985 CD1 ILE A 266 11328 7514 7653 794 -51 20 C ATOM 2986 N ALA A 267 16.601 12.255 3.102 1.00 60.80 N ANISOU 2986 N ALA A 267 10282 6237 6583 777 -247 -79 N ATOM 2987 CA ALA A 267 16.624 10.948 2.445 1.00 61.41 C ANISOU 2987 CA ALA A 267 10384 6227 6724 812 -316 -132 C ATOM 2988 C ALA A 267 15.466 10.806 1.438 1.00 65.55 C ANISOU 2988 C ALA A 267 10952 6721 7235 818 -369 -183 C ATOM 2989 O ALA A 267 15.564 10.019 0.491 1.00 65.62 O ANISOU 2989 O ALA A 267 10997 6673 7264 869 -416 -263 O ATOM 2990 CB ALA A 267 16.549 9.841 3.485 1.00 62.43 C ANISOU 2990 CB ALA A 267 10464 6296 6962 771 -380 -67 C ATOM 2991 N CYS A 268 14.379 11.575 1.641 1.00 61.40 N ANISOU 2991 N CYS A 268 10421 6237 6672 769 -362 -142 N ATOM 2992 CA CYS A 268 13.180 11.492 0.813 1.00 61.15 C ANISOU 2992 CA CYS A 268 10425 6182 6628 762 -410 -171 C ATOM 2993 C CYS A 268 13.214 12.495 -0.349 1.00 63.69 C ANISOU 2993 C CYS A 268 10784 6565 6851 800 -351 -231 C ATOM 2994 O CYS A 268 12.742 12.170 -1.442 1.00 62.97 O ANISOU 2994 O CYS A 268 10731 6452 6743 828 -388 -295 O ATOM 2995 CB CYS A 268 11.931 11.688 1.667 1.00 61.16 C ANISOU 2995 CB CYS A 268 10392 6200 6646 689 -439 -83 C ATOM 2996 SG CYS A 268 11.593 10.323 2.812 1.00 65.53 S ANISOU 2996 SG CYS A 268 10886 6687 7326 639 -536 5 S ATOM 2997 N TRP A 269 13.728 13.721 -0.107 1.00 59.61 N ANISOU 2997 N TRP A 269 10249 6127 6273 798 -269 -204 N ATOM 2998 CA TRP A 269 13.721 14.783 -1.115 1.00 59.08 C ANISOU 2998 CA TRP A 269 10198 6125 6123 824 -218 -233 C ATOM 2999 C TRP A 269 14.976 14.769 -2.012 1.00 63.03 C ANISOU 2999 C TRP A 269 10707 6659 6581 898 -181 -288 C ATOM 3000 O TRP A 269 14.849 15.035 -3.208 1.00 63.16 O ANISOU 3000 O TRP A 269 10740 6718 6539 936 -172 -333 O ATOM 3001 CB TRP A 269 13.556 16.154 -0.458 1.00 57.03 C ANISOU 3001 CB TRP A 269 9908 5925 5833 784 -164 -174 C ATOM 3002 CG TRP A 269 12.155 16.406 0.013 1.00 57.81 C ANISOU 3002 CG TRP A 269 10001 6022 5941 729 -192 -134 C ATOM 3003 CD1 TRP A 269 11.632 16.094 1.233 1.00 60.61 C ANISOU 3003 CD1 TRP A 269 10325 6367 6337 685 -221 -78 C ATOM 3004 CD2 TRP A 269 11.067 16.917 -0.772 1.00 57.65 C ANISOU 3004 CD2 TRP A 269 10000 6020 5884 715 -197 -141 C ATOM 3005 NE1 TRP A 269 10.294 16.417 1.273 1.00 59.91 N ANISOU 3005 NE1 TRP A 269 10236 6294 6235 648 -242 -49 N ATOM 3006 CE2 TRP A 269 9.922 16.929 0.056 1.00 61.35 C ANISOU 3006 CE2 TRP A 269 10451 6485 6372 664 -228 -87 C ATOM 3007 CE3 TRP A 269 10.954 17.391 -2.091 1.00 59.08 C ANISOU 3007 CE3 TRP A 269 10203 6231 6012 742 -178 -179 C ATOM 3008 CZ2 TRP A 269 8.679 17.388 -0.393 1.00 60.53 C ANISOU 3008 CZ2 TRP A 269 10359 6398 6241 638 -238 -73 C ATOM 3009 CZ3 TRP A 269 9.720 17.839 -2.536 1.00 60.45 C ANISOU 3009 CZ3 TRP A 269 10386 6419 6163 711 -188 -165 C ATOM 3010 CH2 TRP A 269 8.601 17.837 -1.692 1.00 60.87 C ANISOU 3010 CH2 TRP A 269 10429 6459 6241 660 -218 -113 C ATOM 3011 N ALA A 270 16.169 14.407 -1.457 1.00 58.97 N ANISOU 3011 N ALA A 270 10175 6136 6093 922 -163 -279 N ATOM 3012 CA ALA A 270 17.438 14.353 -2.219 1.00 58.67 C ANISOU 3012 CA ALA A 270 10138 6142 6012 998 -127 -319 C ATOM 3013 C ALA A 270 17.307 13.594 -3.582 1.00 61.34 C ANISOU 3013 C ALA A 270 10508 6479 6318 1070 -165 -417 C ATOM 3014 O ALA A 270 17.830 14.100 -4.573 1.00 60.70 O ANISOU 3014 O ALA A 270 10419 6485 6157 1126 -126 -442 O ATOM 3015 CB ALA A 270 18.537 13.719 -1.387 1.00 59.54 C ANISOU 3015 CB ALA A 270 10230 6221 6173 1010 -121 -300 C ATOM 3016 N PRO A 271 16.605 12.417 -3.686 1.00 57.60 N ANISOU 3016 N PRO A 271 10064 5916 5905 1071 -248 -472 N ATOM 3017 CA PRO A 271 16.491 11.761 -5.005 1.00 58.05 C ANISOU 3017 CA PRO A 271 10151 5977 5927 1147 -290 -581 C ATOM 3018 C PRO A 271 15.803 12.668 -6.040 1.00 61.68 C ANISOU 3018 C PRO A 271 10615 6526 6295 1149 -263 -591 C ATOM 3019 O PRO A 271 16.265 12.747 -7.183 1.00 62.33 O ANISOU 3019 O PRO A 271 10694 6693 6297 1226 -245 -653 O ATOM 3020 CB PRO A 271 15.661 10.502 -4.712 1.00 60.12 C ANISOU 3020 CB PRO A 271 10439 6111 6294 1123 -397 -614 C ATOM 3021 CG PRO A 271 15.813 10.268 -3.258 1.00 64.27 C ANISOU 3021 CG PRO A 271 10936 6575 6908 1058 -402 -525 C ATOM 3022 CD PRO A 271 15.923 11.624 -2.639 1.00 58.99 C ANISOU 3022 CD PRO A 271 10238 5990 6185 1008 -314 -435 C ATOM 3023 N LEU A 272 14.735 13.396 -5.625 1.00 56.37 N ANISOU 3023 N LEU A 272 9940 5848 5630 1066 -257 -523 N ATOM 3024 CA LEU A 272 14.036 14.333 -6.509 1.00 55.48 C ANISOU 3024 CA LEU A 272 9823 5815 5441 1056 -229 -516 C ATOM 3025 C LEU A 272 14.945 15.504 -6.854 1.00 57.69 C ANISOU 3025 C LEU A 272 10061 6210 5649 1081 -145 -472 C ATOM 3026 O LEU A 272 15.020 15.897 -8.013 1.00 57.13 O ANISOU 3026 O LEU A 272 9974 6234 5498 1125 -124 -498 O ATOM 3027 CB LEU A 272 12.736 14.841 -5.852 1.00 54.86 C ANISOU 3027 CB LEU A 272 9748 5700 5395 964 -241 -446 C ATOM 3028 CG LEU A 272 11.870 15.768 -6.707 1.00 59.08 C ANISOU 3028 CG LEU A 272 10278 6304 5865 943 -218 -432 C ATOM 3029 CD1 LEU A 272 11.092 14.985 -7.735 1.00 59.81 C ANISOU 3029 CD1 LEU A 272 10406 6379 5940 967 -279 -508 C ATOM 3030 CD2 LEU A 272 10.930 16.587 -5.842 1.00 60.22 C ANISOU 3030 CD2 LEU A 272 10410 6433 6036 861 -205 -346 C ATOM 3031 N PHE A 273 15.653 16.045 -5.837 1.00 53.34 N ANISOU 3031 N PHE A 273 9483 5655 5127 1052 -104 -402 N ATOM 3032 CA PHE A 273 16.586 17.165 -5.980 1.00 52.82 C ANISOU 3032 CA PHE A 273 9371 5682 5015 1066 -37 -343 C ATOM 3033 C PHE A 273 17.692 16.833 -6.986 1.00 57.27 C ANISOU 3033 C PHE A 273 9918 6331 5513 1162 -18 -386 C ATOM 3034 O PHE A 273 18.015 17.667 -7.836 1.00 57.42 O ANISOU 3034 O PHE A 273 9893 6462 5462 1188 20 -353 O ATOM 3035 CB PHE A 273 17.193 17.524 -4.616 1.00 53.85 C ANISOU 3035 CB PHE A 273 9484 5775 5203 1024 -13 -276 C ATOM 3036 CG PHE A 273 16.361 18.453 -3.765 1.00 54.51 C ANISOU 3036 CG PHE A 273 9557 5836 5320 945 -8 -216 C ATOM 3037 CD1 PHE A 273 15.029 18.161 -3.478 1.00 57.21 C ANISOU 3037 CD1 PHE A 273 9924 6124 5689 898 -48 -226 C ATOM 3038 CD2 PHE A 273 16.930 19.570 -3.171 1.00 56.15 C ANISOU 3038 CD2 PHE A 273 9726 6071 5537 920 29 -151 C ATOM 3039 CE1 PHE A 273 14.271 19.004 -2.663 1.00 57.32 C ANISOU 3039 CE1 PHE A 273 9924 6129 5726 837 -44 -176 C ATOM 3040 CE2 PHE A 273 16.176 20.401 -2.340 1.00 58.23 C ANISOU 3040 CE2 PHE A 273 9979 6314 5833 859 27 -112 C ATOM 3041 CZ PHE A 273 14.850 20.117 -2.096 1.00 56.04 C ANISOU 3041 CZ PHE A 273 9725 5997 5571 821 -6 -127 C ATOM 3042 N ILE A 274 18.244 15.601 -6.911 1.00 53.46 N ANISOU 3042 N ILE A 274 9459 5800 5051 1216 -49 -456 N ATOM 3043 CA ILE A 274 19.256 15.124 -7.849 1.00 54.19 C ANISOU 3043 CA ILE A 274 9537 5975 5076 1322 -39 -514 C ATOM 3044 C ILE A 274 18.630 15.043 -9.241 1.00 59.07 C ANISOU 3044 C ILE A 274 10156 6671 5615 1373 -59 -586 C ATOM 3045 O ILE A 274 19.189 15.594 -10.193 1.00 59.43 O ANISOU 3045 O ILE A 274 10153 6860 5566 1431 -19 -573 O ATOM 3046 CB ILE A 274 19.850 13.755 -7.383 1.00 57.86 C ANISOU 3046 CB ILE A 274 10032 6351 5602 1368 -80 -583 C ATOM 3047 CG1 ILE A 274 20.793 13.952 -6.167 1.00 57.80 C ANISOU 3047 CG1 ILE A 274 10004 6311 5647 1334 -42 -499 C ATOM 3048 CG2 ILE A 274 20.577 13.028 -8.541 1.00 59.62 C ANISOU 3048 CG2 ILE A 274 10250 6651 5753 1495 -92 -685 C ATOM 3049 CD1 ILE A 274 21.150 12.668 -5.403 1.00 66.79 C ANISOU 3049 CD1 ILE A 274 11165 7336 6875 1345 -87 -539 C ATOM 3050 N LEU A 275 17.427 14.422 -9.340 1.00 55.59 N ANISOU 3050 N LEU A 275 9763 6147 5213 1344 -122 -649 N ATOM 3051 CA LEU A 275 16.678 14.272 -10.597 1.00 56.02 C ANISOU 3051 CA LEU A 275 9825 6261 5198 1382 -152 -724 C ATOM 3052 C LEU A 275 16.380 15.642 -11.234 1.00 61.12 C ANISOU 3052 C LEU A 275 10420 7036 5769 1352 -94 -642 C ATOM 3053 O LEU A 275 16.549 15.802 -12.443 1.00 61.64 O ANISOU 3053 O LEU A 275 10450 7236 5735 1419 -80 -676 O ATOM 3054 CB LEU A 275 15.367 13.506 -10.339 1.00 55.63 C ANISOU 3054 CB LEU A 275 9833 6079 5224 1329 -233 -772 C ATOM 3055 CG LEU A 275 14.429 13.352 -11.524 1.00 59.89 C ANISOU 3055 CG LEU A 275 10387 6664 5706 1351 -272 -845 C ATOM 3056 CD1 LEU A 275 14.741 12.100 -12.304 1.00 61.01 C ANISOU 3056 CD1 LEU A 275 10554 6797 5832 1457 -341 -995 C ATOM 3057 CD2 LEU A 275 13.008 13.334 -11.065 1.00 61.08 C ANISOU 3057 CD2 LEU A 275 10573 6712 5923 1254 -318 -811 C ATOM 3058 N LEU A 276 15.957 16.626 -10.415 1.00 57.73 N ANISOU 3058 N LEU A 276 9979 6570 5387 1256 -63 -535 N ATOM 3059 CA LEU A 276 15.677 17.978 -10.885 1.00 58.00 C ANISOU 3059 CA LEU A 276 9959 6703 5376 1219 -17 -447 C ATOM 3060 C LEU A 276 16.946 18.629 -11.404 1.00 64.50 C ANISOU 3060 C LEU A 276 10709 7665 6134 1276 37 -391 C ATOM 3061 O LEU A 276 16.920 19.254 -12.466 1.00 64.90 O ANISOU 3061 O LEU A 276 10702 7851 6107 1301 59 -361 O ATOM 3062 CB LEU A 276 15.063 18.833 -9.763 1.00 57.17 C ANISOU 3062 CB LEU A 276 9857 6515 5349 1115 -5 -357 C ATOM 3063 CG LEU A 276 13.615 18.515 -9.375 1.00 61.81 C ANISOU 3063 CG LEU A 276 10496 7004 5985 1050 -50 -377 C ATOM 3064 CD1 LEU A 276 13.289 19.076 -8.022 1.00 61.27 C ANISOU 3064 CD1 LEU A 276 10430 6856 5993 972 -42 -306 C ATOM 3065 CD2 LEU A 276 12.633 19.031 -10.414 1.00 64.13 C ANISOU 3065 CD2 LEU A 276 10775 7365 6226 1033 -49 -371 C ATOM 3066 N LEU A 277 18.077 18.436 -10.682 1.00 62.36 N ANISOU 3066 N LEU A 277 10433 7369 5891 1298 54 -370 N ATOM 3067 CA LEU A 277 19.376 18.983 -11.077 1.00 63.38 C ANISOU 3067 CA LEU A 277 10492 7627 5964 1353 100 -304 C ATOM 3068 C LEU A 277 19.813 18.377 -12.410 1.00 69.37 C ANISOU 3068 C LEU A 277 11222 8527 6610 1468 98 -379 C ATOM 3069 O LEU A 277 20.377 19.081 -13.253 1.00 69.12 O ANISOU 3069 O LEU A 277 11107 8659 6496 1508 132 -312 O ATOM 3070 CB LEU A 277 20.426 18.719 -9.985 1.00 63.47 C ANISOU 3070 CB LEU A 277 10515 7570 6031 1353 112 -277 C ATOM 3071 CG LEU A 277 21.560 19.752 -9.874 1.00 68.52 C ANISOU 3071 CG LEU A 277 11080 8297 6658 1352 158 -153 C ATOM 3072 CD1 LEU A 277 22.023 19.908 -8.428 1.00 67.74 C ANISOU 3072 CD1 LEU A 277 11002 8085 6650 1293 163 -104 C ATOM 3073 CD2 LEU A 277 22.739 19.396 -10.794 1.00 72.60 C ANISOU 3073 CD2 LEU A 277 11546 8963 7077 1464 180 -159 C ATOM 3074 N LEU A 278 19.483 17.091 -12.627 1.00 67.94 N ANISOU 3074 N LEU A 278 11103 8287 6425 1521 49 -518 N ATOM 3075 CA LEU A 278 19.772 16.399 -13.881 1.00 69.95 C ANISOU 3075 CA LEU A 278 11338 8667 6572 1641 34 -622 C ATOM 3076 C LEU A 278 18.929 16.967 -15.021 1.00 76.80 C ANISOU 3076 C LEU A 278 12164 9657 7359 1638 36 -617 C ATOM 3077 O LEU A 278 19.416 17.055 -16.147 1.00 77.43 O ANISOU 3077 O LEU A 278 12176 9923 7320 1729 54 -632 O ATOM 3078 CB LEU A 278 19.522 14.885 -13.743 1.00 70.53 C ANISOU 3078 CB LEU A 278 11491 8617 6690 1690 -37 -779 C ATOM 3079 CG LEU A 278 20.543 14.103 -12.916 1.00 75.26 C ANISOU 3079 CG LEU A 278 12115 9131 7348 1728 -44 -803 C ATOM 3080 CD1 LEU A 278 19.953 12.803 -12.416 1.00 75.70 C ANISOU 3080 CD1 LEU A 278 12250 9006 7505 1722 -127 -917 C ATOM 3081 CD2 LEU A 278 21.827 13.852 -13.708 1.00 78.54 C ANISOU 3081 CD2 LEU A 278 12477 9707 7658 1863 -16 -839 C ATOM 3082 N ASP A 279 17.670 17.387 -14.721 1.00 74.44 N ANISOU 3082 N ASP A 279 11899 9267 7120 1535 20 -588 N ATOM 3083 CA ASP A 279 16.759 17.960 -15.721 1.00 75.14 C ANISOU 3083 CA ASP A 279 11950 9456 7144 1516 23 -573 C ATOM 3084 C ASP A 279 17.263 19.322 -16.201 1.00 80.38 C ANISOU 3084 C ASP A 279 12503 10283 7754 1503 84 -425 C ATOM 3085 O ASP A 279 17.066 19.672 -17.367 1.00 80.74 O ANISOU 3085 O ASP A 279 12480 10494 7703 1538 95 -413 O ATOM 3086 CB ASP A 279 15.331 18.090 -15.158 1.00 76.22 C ANISOU 3086 CB ASP A 279 12147 9446 7365 1406 -7 -563 C ATOM 3087 CG ASP A 279 14.238 18.159 -16.220 1.00 87.98 C ANISOU 3087 CG ASP A 279 13629 11007 8793 1400 -27 -598 C ATOM 3088 OD1 ASP A 279 14.576 18.148 -17.428 1.00 90.06 O ANISOU 3088 OD1 ASP A 279 13832 11446 8942 1482 -16 -631 O ATOM 3089 OD2 ASP A 279 13.048 18.183 -15.843 1.00 92.49 O1- ANISOU 3089 OD2 ASP A 279 14249 11467 9425 1317 -55 -593 O1- ATOM 3090 N VAL A 280 17.935 20.078 -15.312 1.00 77.16 N ANISOU 3090 N VAL A 280 12071 9835 7414 1453 116 -310 N ATOM 3091 CA VAL A 280 18.503 21.383 -15.660 1.00 77.47 C ANISOU 3091 CA VAL A 280 11999 10007 7428 1435 159 -156 C ATOM 3092 C VAL A 280 19.676 21.184 -16.657 1.00 83.36 C ANISOU 3092 C VAL A 280 12659 10963 8050 1555 181 -149 C ATOM 3093 O VAL A 280 19.799 21.942 -17.623 1.00 83.63 O ANISOU 3093 O VAL A 280 12585 11180 8009 1572 203 -59 O ATOM 3094 CB VAL A 280 18.945 22.173 -14.391 1.00 80.52 C ANISOU 3094 CB VAL A 280 12387 10280 7928 1355 173 -48 C ATOM 3095 CG1 VAL A 280 19.535 23.534 -14.760 1.00 80.47 C ANISOU 3095 CG1 VAL A 280 12260 10397 7917 1333 200 118 C ATOM 3096 CG2 VAL A 280 17.780 22.341 -13.416 1.00 79.30 C ANISOU 3096 CG2 VAL A 280 12308 9944 7880 1253 150 -63 C ATOM 3097 N GLY A 281 20.472 20.131 -16.440 1.00 80.58 N ANISOU 3097 N GLY A 281 12350 10590 7675 1639 173 -245 N ATOM 3098 CA GLY A 281 21.611 19.810 -17.293 1.00 81.58 C ANISOU 3098 CA GLY A 281 12404 10913 7680 1767 193 -255 C ATOM 3099 C GLY A 281 21.385 18.629 -18.216 1.00 86.47 C ANISOU 3099 C GLY A 281 13052 11604 8200 1883 161 -432 C ATOM 3100 O GLY A 281 22.210 17.713 -18.260 1.00 86.62 O ANISOU 3100 O GLY A 281 13087 11644 8178 1987 152 -524 O ATOM 3101 N CYS A 282 20.266 18.646 -18.977 1.00 83.50 N ANISOU 3101 N CYS A 282 12677 11265 7785 1868 139 -485 N ATOM 3102 CA CYS A 282 19.925 17.579 -19.930 1.00 84.79 C ANISOU 3102 CA CYS A 282 12865 11499 7853 1975 96 -663 C ATOM 3103 C CYS A 282 19.042 18.128 -21.049 1.00 87.81 C ANISOU 3103 C CYS A 282 13181 12032 8149 1962 99 -643 C ATOM 3104 O CYS A 282 18.078 18.842 -20.772 1.00 86.34 O ANISOU 3104 O CYS A 282 13009 11763 8035 1842 103 -564 O ATOM 3105 CB CYS A 282 19.247 16.407 -19.217 1.00 85.42 C ANISOU 3105 CB CYS A 282 13082 11338 8035 1955 30 -817 C ATOM 3106 SG CYS A 282 18.654 15.097 -20.327 1.00 91.13 S ANISOU 3106 SG CYS A 282 13847 12104 8673 2073 -47 -1049 S ATOM 3107 N LYS A 283 19.347 17.755 -22.316 1.00 85.28 N ANISOU 3107 N LYS A 283 12790 11939 7672 2092 96 -721 N ATOM 3108 CA LYS A 283 18.546 18.153 -23.484 1.00 85.59 C ANISOU 3108 CA LYS A 283 12758 12150 7611 2095 96 -716 C ATOM 3109 C LYS A 283 17.168 17.482 -23.439 1.00 88.67 C ANISOU 3109 C LYS A 283 13262 12372 8058 2045 34 -853 C ATOM 3110 O LYS A 283 17.006 16.455 -22.778 1.00 88.27 O ANISOU 3110 O LYS A 283 13329 12119 8089 2055 -20 -986 O ATOM 3111 CB LYS A 283 19.269 17.809 -24.799 1.00 89.98 C ANISOU 3111 CB LYS A 283 13208 13005 7974 2262 103 -783 C ATOM 3112 CG LYS A 283 20.407 18.763 -25.144 1.00105.12 C ANISOU 3112 CG LYS A 283 14971 15159 9813 2296 168 -595 C ATOM 3113 CD LYS A 283 21.016 18.437 -26.501 1.00115.58 C ANISOU 3113 CD LYS A 283 16175 16811 10929 2466 174 -656 C ATOM 3114 CE LYS A 283 22.126 19.391 -26.869 1.00125.02 C ANISOU 3114 CE LYS A 283 17200 18258 12043 2498 233 -446 C ATOM 3115 NZ LYS A 283 22.703 19.073 -28.201 1.00134.54 N ANISOU 3115 NZ LYS A 283 18276 19813 13031 2671 240 -499 N ATOM 3116 N VAL A 284 16.174 18.073 -24.118 1.00 84.60 N ANISOU 3116 N VAL A 284 12704 11936 7506 1987 39 -806 N ATOM 3117 CA VAL A 284 14.802 17.568 -24.098 1.00 83.93 C ANISOU 3117 CA VAL A 284 12717 11699 7474 1925 -18 -906 C ATOM 3118 C VAL A 284 14.711 16.198 -24.840 1.00 89.61 C ANISOU 3118 C VAL A 284 13485 12451 8111 2057 -91 -1139 C ATOM 3119 O VAL A 284 15.419 15.980 -25.830 1.00 90.51 O ANISOU 3119 O VAL A 284 13515 12798 8077 2192 -83 -1202 O ATOM 3120 CB VAL A 284 13.809 18.615 -24.671 1.00 87.19 C ANISOU 3120 CB VAL A 284 13061 12202 7864 1829 12 -783 C ATOM 3121 CG1 VAL A 284 13.959 18.778 -26.186 1.00 88.36 C ANISOU 3121 CG1 VAL A 284 13081 12660 7831 1925 28 -796 C ATOM 3122 CG2 VAL A 284 12.378 18.274 -24.295 1.00 86.32 C ANISOU 3122 CG2 VAL A 284 13062 11890 7847 1731 -39 -839 C ATOM 3123 N LYS A 285 13.877 15.264 -24.295 1.00 86.04 N ANISOU 3123 N LYS A 285 13165 11760 7765 2019 -170 -1264 N ATOM 3124 CA LYS A 285 13.644 13.904 -24.826 1.00 87.04 C ANISOU 3124 CA LYS A 285 13358 11852 7862 2125 -266 -1493 C ATOM 3125 C LYS A 285 14.973 13.119 -24.985 1.00 92.13 C ANISOU 3125 C LYS A 285 13987 12572 8446 2286 -279 -1613 C ATOM 3126 O LYS A 285 15.128 12.346 -25.937 1.00 93.18 O ANISOU 3126 O LYS A 285 14105 12827 8473 2424 -330 -1787 O ATOM 3127 CB LYS A 285 12.878 13.956 -26.165 1.00 90.24 C ANISOU 3127 CB LYS A 285 13712 12441 8136 2162 -286 -1558 C ATOM 3128 N THR A 286 15.909 13.294 -24.028 1.00 88.10 N ANISOU 3128 N THR A 286 13481 11984 8007 2271 -236 -1526 N ATOM 3129 CA THR A 286 17.216 12.636 -24.065 1.00 89.02 C ANISOU 3129 CA THR A 286 13581 12166 8077 2414 -238 -1613 C ATOM 3130 C THR A 286 17.379 11.704 -22.856 1.00 93.34 C ANISOU 3130 C THR A 286 14243 12430 8791 2389 -296 -1680 C ATOM 3131 O THR A 286 17.659 10.517 -23.035 1.00 94.14 O ANISOU 3131 O THR A 286 14391 12476 8900 2501 -373 -1864 O ATOM 3132 CB THR A 286 18.340 13.690 -24.118 1.00 95.88 C ANISOU 3132 CB THR A 286 14330 13236 8866 2430 -135 -1435 C ATOM 3133 OG1 THR A 286 18.048 14.638 -25.145 1.00 95.45 O ANISOU 3133 OG1 THR A 286 14159 13427 8681 2425 -87 -1339 O ATOM 3134 CG2 THR A 286 19.716 13.073 -24.353 1.00 95.82 C ANISOU 3134 CG2 THR A 286 14284 13349 8775 2594 -129 -1516 C ATOM 3135 N CYS A 287 17.222 12.248 -21.629 1.00 88.91 N ANISOU 3135 N CYS A 287 13719 11696 8365 2246 -261 -1530 N ATOM 3136 CA CYS A 287 17.381 11.482 -20.393 1.00 88.50 C ANISOU 3136 CA CYS A 287 13759 11392 8473 2207 -306 -1559 C ATOM 3137 C CYS A 287 16.118 10.660 -20.113 1.00 91.81 C ANISOU 3137 C CYS A 287 14278 11597 9009 2144 -410 -1655 C ATOM 3138 O CYS A 287 15.033 11.224 -19.955 1.00 90.28 O ANISOU 3138 O CYS A 287 14101 11350 8852 2025 -406 -1573 O ATOM 3139 CB CYS A 287 17.718 12.404 -19.225 1.00 87.56 C ANISOU 3139 CB CYS A 287 13630 11200 8438 2088 -231 -1365 C ATOM 3140 SG CYS A 287 19.246 13.359 -19.446 1.00 91.65 S ANISOU 3140 SG CYS A 287 14031 11947 8845 2151 -124 -1230 S ATOM 3141 N ASP A 288 16.265 9.321 -20.070 1.00 89.15 N ANISOU 3141 N ASP A 288 14002 11138 8734 2226 -509 -1826 N ATOM 3142 CA ASP A 288 15.150 8.392 -19.867 1.00 89.13 C ANISOU 3142 CA ASP A 288 14086 10927 8852 2179 -630 -1925 C ATOM 3143 C ASP A 288 14.670 8.389 -18.413 1.00 90.40 C ANISOU 3143 C ASP A 288 14303 10856 9190 2031 -643 -1804 C ATOM 3144 O ASP A 288 13.478 8.189 -18.167 1.00 89.42 O ANISOU 3144 O ASP A 288 14228 10598 9149 1937 -708 -1792 O ATOM 3145 CB ASP A 288 15.553 6.965 -20.292 1.00 92.99 C ANISOU 3145 CB ASP A 288 14610 11356 9365 2323 -744 -2146 C ATOM 3146 CG ASP A 288 15.921 6.816 -21.767 1.00108.26 C ANISOU 3146 CG ASP A 288 16491 13525 11119 2487 -750 -2298 C ATOM 3147 OD1 ASP A 288 15.680 7.772 -22.544 1.00109.19 O ANISOU 3147 OD1 ASP A 288 16542 13850 11094 2478 -676 -2230 O ATOM 3148 OD2 ASP A 288 16.425 5.736 -22.146 1.00117.16 O1- ANISOU 3148 OD2 ASP A 288 17636 14631 12249 2626 -834 -2487 O1- ATOM 3149 N ILE A 289 15.596 8.615 -17.450 1.00 85.61 N ANISOU 3149 N ILE A 289 13681 10212 8633 2010 -583 -1708 N ATOM 3150 CA ILE A 289 15.300 8.630 -16.003 1.00 83.72 C ANISOU 3150 CA ILE A 289 13481 9781 8549 1881 -587 -1590 C ATOM 3151 C ILE A 289 14.251 9.720 -15.682 1.00 85.55 C ANISOU 3151 C ILE A 289 13706 10014 8783 1741 -539 -1442 C ATOM 3152 O ILE A 289 13.381 9.504 -14.834 1.00 84.12 O ANISOU 3152 O ILE A 289 13569 9674 8721 1636 -586 -1389 O ATOM 3153 CB ILE A 289 16.612 8.832 -15.163 1.00 86.11 C ANISOU 3153 CB ILE A 289 13754 10091 8872 1895 -516 -1511 C ATOM 3154 CG1 ILE A 289 17.663 7.732 -15.469 1.00 88.07 C ANISOU 3154 CG1 ILE A 289 14005 10336 9120 2040 -563 -1657 C ATOM 3155 CG2 ILE A 289 16.319 8.890 -13.662 1.00 84.99 C ANISOU 3155 CG2 ILE A 289 13640 9776 8877 1765 -517 -1388 C ATOM 3156 CD1 ILE A 289 18.817 8.183 -16.362 1.00 96.48 C ANISOU 3156 CD1 ILE A 289 15001 11635 10021 2166 -484 -1678 C ATOM 3157 N LEU A 290 14.309 10.859 -16.407 1.00 81.81 N ANISOU 3157 N LEU A 290 13174 9730 8180 1743 -451 -1376 N ATOM 3158 CA LEU A 290 13.424 12.012 -16.209 1.00 80.53 C ANISOU 3158 CA LEU A 290 12994 9590 8013 1623 -397 -1236 C ATOM 3159 C LEU A 290 11.957 11.714 -16.583 1.00 85.18 C ANISOU 3159 C LEU A 290 13627 10111 8627 1568 -470 -1276 C ATOM 3160 O LEU A 290 11.057 12.376 -16.060 1.00 83.72 O ANISOU 3160 O LEU A 290 13451 9875 8486 1453 -450 -1164 O ATOM 3161 CB LEU A 290 13.926 13.214 -17.022 1.00 80.48 C ANISOU 3161 CB LEU A 290 12900 9808 7871 1652 -300 -1160 C ATOM 3162 CG LEU A 290 15.287 13.800 -16.611 1.00 85.07 C ANISOU 3162 CG LEU A 290 13426 10468 8430 1682 -221 -1074 C ATOM 3163 CD1 LEU A 290 15.741 14.857 -17.589 1.00 85.58 C ANISOU 3163 CD1 LEU A 290 13390 10765 8361 1720 -146 -1000 C ATOM 3164 CD2 LEU A 290 15.242 14.384 -15.209 1.00 86.02 C ANISOU 3164 CD2 LEU A 290 13563 10459 8662 1566 -188 -942 C ATOM 3165 N PHE A 291 11.713 10.740 -17.486 1.00 83.53 N ANISOU 3165 N PHE A 291 13444 9905 8388 1652 -556 -1435 N ATOM 3166 CA PHE A 291 10.350 10.383 -17.883 1.00 83.91 C ANISOU 3166 CA PHE A 291 13536 9885 8462 1602 -636 -1477 C ATOM 3167 C PHE A 291 9.674 9.577 -16.782 1.00 87.86 C ANISOU 3167 C PHE A 291 14103 10149 9130 1520 -728 -1459 C ATOM 3168 O PHE A 291 8.783 10.098 -16.109 1.00 87.01 O ANISOU 3168 O PHE A 291 14006 9975 9077 1400 -713 -1334 O ATOM 3169 CB PHE A 291 10.339 9.613 -19.208 1.00 87.51 C ANISOU 3169 CB PHE A 291 13993 10424 8831 1723 -708 -1660 C ATOM 3170 CG PHE A 291 10.724 10.450 -20.398 1.00 89.71 C ANISOU 3170 CG PHE A 291 14191 10963 8930 1792 -624 -1660 C ATOM 3171 CD1 PHE A 291 9.781 11.228 -21.056 1.00 92.62 C ANISOU 3171 CD1 PHE A 291 14531 11433 9228 1731 -593 -1598 C ATOM 3172 CD2 PHE A 291 12.030 10.452 -20.873 1.00 92.97 C ANISOU 3172 CD2 PHE A 291 14548 11534 9245 1919 -577 -1714 C ATOM 3173 CE1 PHE A 291 10.138 12.002 -22.159 1.00 94.22 C ANISOU 3173 CE1 PHE A 291 14642 11888 9268 1791 -519 -1582 C ATOM 3174 CE2 PHE A 291 12.386 11.229 -21.978 1.00 96.42 C ANISOU 3174 CE2 PHE A 291 14892 12232 9513 1983 -503 -1695 C ATOM 3175 CZ PHE A 291 11.437 11.997 -22.615 1.00 94.24 C ANISOU 3175 CZ PHE A 291 14581 12054 9173 1917 -476 -1627 C ATOM 3176 N ARG A 292 10.132 8.330 -16.550 1.00 84.94 N ANISOU 3176 N ARG A 292 13769 9656 8847 1585 -822 -1573 N ATOM 3177 CA ARG A 292 9.596 7.497 -15.477 1.00 84.59 C ANISOU 3177 CA ARG A 292 13772 9392 8975 1509 -918 -1543 C ATOM 3178 C ARG A 292 10.213 7.959 -14.144 1.00 86.51 C ANISOU 3178 C ARG A 292 13994 9595 9280 1447 -842 -1403 C ATOM 3179 O ARG A 292 11.001 7.238 -13.521 1.00 86.52 O ANISOU 3179 O ARG A 292 14001 9510 9365 1482 -874 -1431 O ATOM 3180 CB ARG A 292 9.863 5.996 -15.755 1.00 87.97 C ANISOU 3180 CB ARG A 292 14237 9698 9489 1602 -1059 -1714 C ATOM 3181 CG ARG A 292 8.959 5.040 -14.956 1.00102.40 C ANISOU 3181 CG ARG A 292 16108 11299 11501 1518 -1195 -1687 C ATOM 3182 CD ARG A 292 7.541 4.967 -15.514 1.00115.45 C ANISOU 3182 CD ARG A 292 17790 12920 13157 1459 -1272 -1692 C ATOM 3183 NE ARG A 292 6.595 4.434 -14.531 1.00124.08 N ANISOU 3183 NE ARG A 292 18903 13827 14414 1343 -1369 -1588 N ATOM 3184 CZ ARG A 292 5.287 4.312 -14.744 1.00137.73 C ANISOU 3184 CZ ARG A 292 20656 15499 16176 1269 -1446 -1553 C ATOM 3185 NH1 ARG A 292 4.762 4.671 -15.911 1.00123.12 N ANISOU 3185 NH1 ARG A 292 18816 13756 14208 1296 -1437 -1624 N ATOM 3186 NH2 ARG A 292 4.497 3.827 -13.797 1.00125.23 N ANISOU 3186 NH2 ARG A 292 19079 13761 14740 1167 -1534 -1439 N ATOM 3187 N ALA A 293 9.897 9.208 -13.757 1.00 80.88 N ANISOU 3187 N ALA A 293 13252 8956 8521 1361 -741 -1258 N ATOM 3188 CA ALA A 293 10.406 9.854 -12.551 1.00 79.00 C ANISOU 3188 CA ALA A 293 12989 8704 8323 1300 -662 -1126 C ATOM 3189 C ALA A 293 9.275 10.109 -11.555 1.00 80.63 C ANISOU 3189 C ALA A 293 13207 8815 8613 1172 -680 -1000 C ATOM 3190 O ALA A 293 9.395 10.970 -10.675 1.00 78.97 O ANISOU 3190 O ALA A 293 12970 8627 8408 1111 -604 -882 O ATOM 3191 CB ALA A 293 11.087 11.159 -12.919 1.00 79.13 C ANISOU 3191 CB ALA A 293 12953 8894 8218 1319 -535 -1066 C ATOM 3192 N GLU A 294 8.182 9.335 -11.684 1.00 76.80 N ANISOU 3192 N GLU A 294 12759 8227 8194 1137 -788 -1028 N ATOM 3193 CA GLU A 294 7.005 9.447 -10.823 1.00 75.43 C ANISOU 3193 CA GLU A 294 12592 7973 8097 1023 -820 -907 C ATOM 3194 C GLU A 294 7.281 8.865 -9.429 1.00 76.35 C ANISOU 3194 C GLU A 294 12696 7975 8338 981 -856 -836 C ATOM 3195 O GLU A 294 6.531 9.143 -8.495 1.00 74.84 O ANISOU 3195 O GLU A 294 12490 7751 8194 891 -857 -713 O ATOM 3196 CB GLU A 294 5.793 8.738 -11.469 1.00 77.77 C ANISOU 3196 CB GLU A 294 12926 8198 8426 1001 -935 -953 C ATOM 3197 CG GLU A 294 5.340 9.342 -12.799 1.00 90.69 C ANISOU 3197 CG GLU A 294 14567 9955 9937 1027 -900 -1007 C ATOM 3198 CD GLU A 294 4.666 10.706 -12.745 1.00115.87 C ANISOU 3198 CD GLU A 294 17730 13244 13052 952 -801 -884 C ATOM 3199 OE1 GLU A 294 4.183 11.101 -11.657 1.00113.72 O ANISOU 3199 OE1 GLU A 294 17447 12929 12834 868 -780 -757 O ATOM 3200 OE2 GLU A 294 4.563 11.351 -13.813 1.00112.97 O1- ANISOU 3200 OE2 GLU A 294 17348 13001 12574 979 -750 -916 O1- ATOM 3201 N TYR A 295 8.364 8.069 -9.289 1.00 72.21 N ANISOU 3201 N TYR A 295 12172 7402 7864 1050 -885 -910 N ATOM 3202 CA TYR A 295 8.732 7.443 -8.015 1.00 71.41 C ANISOU 3202 CA TYR A 295 12049 7198 7885 1015 -921 -843 C ATOM 3203 C TYR A 295 9.353 8.459 -7.062 1.00 72.83 C ANISOU 3203 C TYR A 295 12189 7457 8027 981 -800 -736 C ATOM 3204 O TYR A 295 9.070 8.427 -5.861 1.00 71.93 O ANISOU 3204 O TYR A 295 12047 7299 7985 908 -809 -625 O ATOM 3205 CB TYR A 295 9.702 6.269 -8.239 1.00 73.46 C ANISOU 3205 CB TYR A 295 12319 7379 8213 1104 -992 -961 C ATOM 3206 CG TYR A 295 9.255 5.307 -9.316 1.00 76.29 C ANISOU 3206 CG TYR A 295 12718 7668 8600 1163 -1115 -1102 C ATOM 3207 CD1 TYR A 295 8.052 4.616 -9.206 1.00 78.62 C ANISOU 3207 CD1 TYR A 295 13029 7843 8999 1098 -1242 -1075 C ATOM 3208 CD2 TYR A 295 10.059 5.044 -10.420 1.00 78.13 C ANISOU 3208 CD2 TYR A 295 12967 7958 8760 1287 -1113 -1263 C ATOM 3209 CE1 TYR A 295 7.632 3.732 -10.198 1.00 80.82 C ANISOU 3209 CE1 TYR A 295 13347 8050 9313 1152 -1367 -1211 C ATOM 3210 CE2 TYR A 295 9.661 4.143 -11.408 1.00 80.40 C ANISOU 3210 CE2 TYR A 295 13291 8185 9073 1351 -1234 -1411 C ATOM 3211 CZ TYR A 295 8.446 3.487 -11.291 1.00 87.91 C ANISOU 3211 CZ TYR A 295 14264 9004 10135 1281 -1364 -1388 C ATOM 3212 OH TYR A 295 8.042 2.610 -12.268 1.00 90.33 O ANISOU 3212 OH TYR A 295 14607 9244 10471 1343 -1494 -1540 O ATOM 3213 N PHE A 296 10.202 9.360 -7.596 1.00 67.87 N ANISOU 3213 N PHE A 296 11551 6951 7284 1034 -693 -766 N ATOM 3214 CA PHE A 296 10.870 10.405 -6.818 1.00 66.30 C ANISOU 3214 CA PHE A 296 11315 6828 7047 1009 -584 -675 C ATOM 3215 C PHE A 296 9.844 11.375 -6.233 1.00 68.11 C ANISOU 3215 C PHE A 296 11529 7088 7262 917 -548 -562 C ATOM 3216 O PHE A 296 9.965 11.779 -5.075 1.00 66.45 O ANISOU 3216 O PHE A 296 11288 6878 7082 867 -513 -472 O ATOM 3217 CB PHE A 296 11.881 11.165 -7.694 1.00 68.26 C ANISOU 3217 CB PHE A 296 11550 7204 7180 1085 -494 -723 C ATOM 3218 CG PHE A 296 12.880 10.289 -8.414 1.00 71.07 C ANISOU 3218 CG PHE A 296 11916 7561 7525 1193 -523 -844 C ATOM 3219 CD1 PHE A 296 14.092 9.959 -7.823 1.00 74.27 C ANISOU 3219 CD1 PHE A 296 12304 7950 7964 1231 -501 -842 C ATOM 3220 CD2 PHE A 296 12.623 9.823 -9.699 1.00 74.45 C ANISOU 3220 CD2 PHE A 296 12369 8017 7903 1263 -572 -963 C ATOM 3221 CE1 PHE A 296 15.024 9.164 -8.496 1.00 76.29 C ANISOU 3221 CE1 PHE A 296 12567 8214 8205 1340 -526 -956 C ATOM 3222 CE2 PHE A 296 13.551 9.021 -10.369 1.00 78.40 C ANISOU 3222 CE2 PHE A 296 12873 8529 8384 1378 -602 -1087 C ATOM 3223 CZ PHE A 296 14.747 8.699 -9.764 1.00 76.50 C ANISOU 3223 CZ PHE A 296 12616 8271 8180 1417 -578 -1082 C ATOM 3224 N LEU A 297 8.811 11.717 -7.033 1.00 64.47 N ANISOU 3224 N LEU A 297 11086 6656 6753 897 -560 -571 N ATOM 3225 CA LEU A 297 7.727 12.624 -6.646 1.00 63.39 C ANISOU 3225 CA LEU A 297 10938 6551 6597 818 -531 -474 C ATOM 3226 C LEU A 297 6.866 12.022 -5.529 1.00 66.00 C ANISOU 3226 C LEU A 297 11260 6794 7022 747 -602 -391 C ATOM 3227 O LEU A 297 6.354 12.761 -4.688 1.00 64.74 O ANISOU 3227 O LEU A 297 11073 6669 6857 689 -564 -295 O ATOM 3228 CB LEU A 297 6.841 12.943 -7.869 1.00 63.80 C ANISOU 3228 CB LEU A 297 11011 6648 6581 819 -538 -508 C ATOM 3229 CG LEU A 297 7.541 13.577 -9.075 1.00 68.54 C ANISOU 3229 CG LEU A 297 11602 7362 7078 887 -473 -574 C ATOM 3230 CD1 LEU A 297 6.820 13.235 -10.363 1.00 69.56 C ANISOU 3230 CD1 LEU A 297 11757 7513 7160 909 -520 -647 C ATOM 3231 CD2 LEU A 297 7.671 15.079 -8.911 1.00 68.73 C ANISOU 3231 CD2 LEU A 297 11586 7483 7047 858 -371 -491 C ATOM 3232 N VAL A 298 6.700 10.681 -5.534 1.00 62.41 N ANISOU 3232 N VAL A 298 10822 6233 6656 753 -711 -426 N ATOM 3233 CA VAL A 298 5.907 9.955 -4.540 1.00 62.25 C ANISOU 3233 CA VAL A 298 10782 6132 6739 686 -796 -335 C ATOM 3234 C VAL A 298 6.688 9.833 -3.206 1.00 65.11 C ANISOU 3234 C VAL A 298 11095 6488 7156 671 -773 -267 C ATOM 3235 O VAL A 298 6.102 10.046 -2.143 1.00 63.91 O ANISOU 3235 O VAL A 298 10900 6354 7028 609 -774 -153 O ATOM 3236 CB VAL A 298 5.472 8.571 -5.088 1.00 67.52 C ANISOU 3236 CB VAL A 298 11478 6679 7498 697 -936 -393 C ATOM 3237 CG1 VAL A 298 5.336 7.532 -3.972 1.00 67.84 C ANISOU 3237 CG1 VAL A 298 11480 6619 7679 651 -1034 -309 C ATOM 3238 CG2 VAL A 298 4.180 8.689 -5.886 1.00 67.49 C ANISOU 3238 CG2 VAL A 298 11504 6676 7462 665 -980 -392 C ATOM 3239 N LEU A 299 8.004 9.512 -3.268 1.00 61.83 N ANISOU 3239 N LEU A 299 10681 6060 6751 733 -750 -336 N ATOM 3240 CA LEU A 299 8.852 9.389 -2.074 1.00 61.54 C ANISOU 3240 CA LEU A 299 10598 6022 6763 722 -723 -277 C ATOM 3241 C LEU A 299 8.880 10.718 -1.282 1.00 64.90 C ANISOU 3241 C LEU A 299 10989 6554 7115 687 -618 -197 C ATOM 3242 O LEU A 299 8.858 10.706 -0.047 1.00 63.58 O ANISOU 3242 O LEU A 299 10771 6400 6987 644 -617 -106 O ATOM 3243 CB LEU A 299 10.282 8.973 -2.473 1.00 61.92 C ANISOU 3243 CB LEU A 299 10659 6053 6814 802 -702 -371 C ATOM 3244 CG LEU A 299 11.207 8.550 -1.323 1.00 66.34 C ANISOU 3244 CG LEU A 299 11172 6588 7444 794 -694 -318 C ATOM 3245 CD1 LEU A 299 10.886 7.142 -0.852 1.00 67.26 C ANISOU 3245 CD1 LEU A 299 11267 6583 7705 768 -820 -289 C ATOM 3246 CD2 LEU A 299 12.661 8.633 -1.738 1.00 68.59 C ANISOU 3246 CD2 LEU A 299 11470 6903 7690 873 -632 -396 C ATOM 3247 N ALA A 300 8.883 11.856 -2.005 1.00 61.59 N ANISOU 3247 N ALA A 300 10592 6215 6595 707 -539 -231 N ATOM 3248 CA ALA A 300 8.873 13.188 -1.410 1.00 60.70 C ANISOU 3248 CA ALA A 300 10450 6192 6422 681 -452 -173 C ATOM 3249 C ALA A 300 7.509 13.505 -0.790 1.00 64.61 C ANISOU 3249 C ALA A 300 10923 6706 6919 616 -475 -86 C ATOM 3250 O ALA A 300 7.435 14.271 0.174 1.00 63.89 O ANISOU 3250 O ALA A 300 10792 6674 6809 590 -431 -25 O ATOM 3251 CB ALA A 300 9.223 14.223 -2.460 1.00 61.29 C ANISOU 3251 CB ALA A 300 10545 6334 6407 720 -380 -225 C ATOM 3252 N VAL A 301 6.430 12.912 -1.340 1.00 61.79 N ANISOU 3252 N VAL A 301 10590 6304 6584 594 -548 -83 N ATOM 3253 CA VAL A 301 5.070 13.104 -0.828 1.00 61.77 C ANISOU 3253 CA VAL A 301 10565 6323 6583 534 -578 9 C ATOM 3254 C VAL A 301 4.894 12.307 0.474 1.00 66.69 C ANISOU 3254 C VAL A 301 11131 6925 7285 495 -638 104 C ATOM 3255 O VAL A 301 4.383 12.855 1.454 1.00 66.38 O ANISOU 3255 O VAL A 301 11040 6958 7222 462 -616 189 O ATOM 3256 CB VAL A 301 3.996 12.727 -1.893 1.00 65.99 C ANISOU 3256 CB VAL A 301 11142 6817 7116 520 -641 -10 C ATOM 3257 CG1 VAL A 301 2.643 12.418 -1.249 1.00 65.61 C ANISOU 3257 CG1 VAL A 301 11064 6765 7102 455 -707 103 C ATOM 3258 CG2 VAL A 301 3.858 13.830 -2.932 1.00 65.50 C ANISOU 3258 CG2 VAL A 301 11111 6817 6960 540 -568 -61 C ATOM 3259 N LEU A 302 5.363 11.028 0.492 1.00 63.74 N ANISOU 3259 N LEU A 302 10756 6460 7003 504 -717 88 N ATOM 3260 CA LEU A 302 5.258 10.121 1.648 1.00 64.01 C ANISOU 3260 CA LEU A 302 10723 6467 7132 464 -788 189 C ATOM 3261 C LEU A 302 5.857 10.731 2.928 1.00 68.33 C ANISOU 3261 C LEU A 302 11206 7107 7650 457 -715 248 C ATOM 3262 O LEU A 302 5.300 10.539 4.011 1.00 67.37 O ANISOU 3262 O LEU A 302 11010 7034 7553 413 -747 363 O ATOM 3263 CB LEU A 302 5.956 8.782 1.348 1.00 64.81 C ANISOU 3263 CB LEU A 302 10837 6447 7342 488 -872 139 C ATOM 3264 CG LEU A 302 5.319 7.908 0.267 1.00 70.31 C ANISOU 3264 CG LEU A 302 11583 7036 8095 493 -979 84 C ATOM 3265 CD1 LEU A 302 6.324 6.933 -0.300 1.00 71.27 C ANISOU 3265 CD1 LEU A 302 11735 7054 8291 552 -1029 -25 C ATOM 3266 CD2 LEU A 302 4.084 7.177 0.793 1.00 72.87 C ANISOU 3266 CD2 LEU A 302 11861 7320 8507 423 -1095 211 C ATOM 3267 N ASN A 303 6.974 11.492 2.791 1.00 65.83 N ANISOU 3267 N ASN A 303 10910 6825 7276 501 -621 173 N ATOM 3268 CA ASN A 303 7.685 12.141 3.904 1.00 65.68 C ANISOU 3268 CA ASN A 303 10840 6889 7228 501 -551 208 C ATOM 3269 C ASN A 303 6.742 13.006 4.768 1.00 70.39 C ANISOU 3269 C ASN A 303 11385 7593 7766 469 -527 287 C ATOM 3270 O ASN A 303 7.028 13.235 5.947 1.00 69.74 O ANISOU 3270 O ASN A 303 11236 7586 7675 459 -503 341 O ATOM 3271 CB ASN A 303 8.833 12.998 3.368 1.00 66.46 C ANISOU 3271 CB ASN A 303 10978 7006 7266 552 -461 117 C ATOM 3272 CG ASN A 303 9.714 13.578 4.446 1.00 90.61 C ANISOU 3272 CG ASN A 303 13990 10133 10307 555 -400 142 C ATOM 3273 OD1 ASN A 303 9.522 14.715 4.898 1.00 85.35 O ANISOU 3273 OD1 ASN A 303 13304 9547 9579 551 -347 153 O ATOM 3274 ND2 ASN A 303 10.672 12.794 4.911 1.00 81.87 N ANISOU 3274 ND2 ASN A 303 12857 8992 9256 562 -412 151 N ATOM 3275 N SER A 304 5.604 13.453 4.187 1.00 67.79 N ANISOU 3275 N SER A 304 11083 7278 7396 456 -536 292 N ATOM 3276 CA SER A 304 4.606 14.272 4.886 1.00 67.45 C ANISOU 3276 CA SER A 304 10995 7339 7294 435 -516 359 C ATOM 3277 C SER A 304 3.905 13.483 6.012 1.00 70.96 C ANISOU 3277 C SER A 304 11353 7830 7779 393 -586 489 C ATOM 3278 O SER A 304 3.328 14.089 6.917 1.00 70.67 O ANISOU 3278 O SER A 304 11255 7909 7689 387 -566 551 O ATOM 3279 CB SER A 304 3.570 14.805 3.902 1.00 71.60 C ANISOU 3279 CB SER A 304 11571 7858 7775 429 -515 340 C ATOM 3280 OG SER A 304 4.186 15.522 2.844 1.00 81.77 O ANISOU 3280 OG SER A 304 12923 9119 9026 464 -455 238 O ATOM 3281 N GLY A 305 3.982 12.152 5.951 1.00 67.18 N ANISOU 3281 N GLY A 305 10861 7265 7397 370 -672 529 N ATOM 3282 CA GLY A 305 3.396 11.273 6.957 1.00 67.05 C ANISOU 3282 CA GLY A 305 10750 7286 7441 325 -753 671 C ATOM 3283 C GLY A 305 4.413 10.412 7.687 1.00 70.05 C ANISOU 3283 C GLY A 305 11074 7641 7903 320 -779 703 C ATOM 3284 O GLY A 305 4.064 9.346 8.200 1.00 70.45 O ANISOU 3284 O GLY A 305 11053 7671 8045 279 -873 816 O ATOM 3285 N THR A 306 5.686 10.860 7.733 1.00 64.80 N ANISOU 3285 N THR A 306 10435 6974 7212 358 -700 614 N ATOM 3286 CA THR A 306 6.762 10.128 8.421 1.00 64.11 C ANISOU 3286 CA THR A 306 10296 6867 7196 356 -711 639 C ATOM 3287 C THR A 306 7.142 10.853 9.711 1.00 66.58 C ANISOU 3287 C THR A 306 10528 7327 7441 358 -643 683 C ATOM 3288 O THR A 306 7.605 10.217 10.661 1.00 66.14 O ANISOU 3288 O THR A 306 10387 7307 7438 337 -667 763 O ATOM 3289 CB THR A 306 7.983 9.947 7.505 1.00 69.60 C ANISOU 3289 CB THR A 306 11075 7451 7920 400 -681 513 C ATOM 3290 OG1 THR A 306 8.468 11.229 7.104 1.00 68.20 O ANISOU 3290 OG1 THR A 306 10955 7320 7639 441 -578 416 O ATOM 3291 CG2 THR A 306 7.678 9.088 6.282 1.00 67.60 C ANISOU 3291 CG2 THR A 306 10891 7057 7737 408 -761 458 C ATOM 3292 N ASN A 307 6.940 12.189 9.743 1.00 62.00 N ANISOU 3292 N ASN A 307 9972 6835 6750 385 -565 629 N ATOM 3293 CA ASN A 307 7.206 13.022 10.916 1.00 61.15 C ANISOU 3293 CA ASN A 307 9794 6872 6568 397 -506 647 C ATOM 3294 C ASN A 307 6.233 12.663 12.067 1.00 64.78 C ANISOU 3294 C ASN A 307 10131 7465 7017 366 -557 790 C ATOM 3295 O ASN A 307 6.705 12.347 13.157 1.00 64.48 O ANISOU 3295 O ASN A 307 9998 7513 6988 355 -559 858 O ATOM 3296 CB ASN A 307 7.120 14.515 10.565 1.00 62.02 C ANISOU 3296 CB ASN A 307 9961 7023 6580 437 -430 549 C ATOM 3297 CG ASN A 307 8.038 14.943 9.434 1.00 94.46 C ANISOU 3297 CG ASN A 307 14172 11025 10693 467 -381 430 C ATOM 3298 OD1 ASN A 307 8.991 14.239 9.057 1.00 90.29 O ANISOU 3298 OD1 ASN A 307 13673 10410 10225 471 -387 405 O ATOM 3299 ND2 ASN A 307 7.781 16.120 8.880 1.00 87.79 N ANISOU 3299 ND2 ASN A 307 13377 10192 9786 492 -335 360 N ATOM 3300 N PRO A 308 4.885 12.582 11.840 1.00 61.38 N ANISOU 3300 N PRO A 308 9690 7060 6572 347 -606 854 N ATOM 3301 CA PRO A 308 3.985 12.177 12.942 1.00 61.40 C ANISOU 3301 CA PRO A 308 9560 7206 6562 318 -660 1010 C ATOM 3302 C PRO A 308 4.302 10.770 13.475 1.00 64.07 C ANISOU 3302 C PRO A 308 9810 7515 7017 271 -742 1135 C ATOM 3303 O PRO A 308 4.125 10.511 14.668 1.00 63.41 O ANISOU 3303 O PRO A 308 9593 7581 6921 254 -763 1259 O ATOM 3304 CB PRO A 308 2.596 12.226 12.297 1.00 63.37 C ANISOU 3304 CB PRO A 308 9839 7445 6796 304 -704 1051 C ATOM 3305 CG PRO A 308 2.745 13.165 11.145 1.00 67.37 C ANISOU 3305 CG PRO A 308 10477 7861 7258 338 -640 898 C ATOM 3306 CD PRO A 308 4.114 12.897 10.617 1.00 62.81 C ANISOU 3306 CD PRO A 308 9968 7158 6740 351 -613 798 C ATOM 3307 N ILE A 309 4.802 9.877 12.597 1.00 60.23 N ANISOU 3307 N ILE A 309 9393 6845 6647 254 -789 1099 N ATOM 3308 CA ILE A 309 5.180 8.510 12.969 1.00 60.85 C ANISOU 3308 CA ILE A 309 9397 6861 6862 211 -876 1203 C ATOM 3309 C ILE A 309 6.518 8.519 13.766 1.00 64.85 C ANISOU 3309 C ILE A 309 9857 7410 7372 223 -819 1186 C ATOM 3310 O ILE A 309 6.645 7.777 14.740 1.00 64.52 O ANISOU 3310 O ILE A 309 9689 7436 7390 187 -866 1320 O ATOM 3311 CB ILE A 309 5.250 7.599 11.697 1.00 63.96 C ANISOU 3311 CB ILE A 309 9887 7036 7378 202 -953 1145 C ATOM 3312 CG1 ILE A 309 3.838 7.060 11.339 1.00 64.63 C ANISOU 3312 CG1 ILE A 309 9956 7092 7509 161 -1060 1245 C ATOM 3313 CG2 ILE A 309 6.256 6.443 11.867 1.00 64.69 C ANISOU 3313 CG2 ILE A 309 9946 7022 7610 186 -1007 1168 C ATOM 3314 CD1 ILE A 309 3.699 6.429 9.922 1.00 69.75 C ANISOU 3314 CD1 ILE A 309 10719 7536 8247 163 -1131 1155 C ATOM 3315 N ILE A 310 7.482 9.388 13.377 1.00 61.23 N ANISOU 3315 N ILE A 310 9491 6925 6850 271 -720 1035 N ATOM 3316 CA ILE A 310 8.800 9.448 14.023 1.00 60.86 C ANISOU 3316 CA ILE A 310 9414 6907 6804 283 -663 1011 C ATOM 3317 C ILE A 310 8.698 10.053 15.454 1.00 64.91 C ANISOU 3317 C ILE A 310 9804 7635 7224 283 -623 1085 C ATOM 3318 O ILE A 310 9.537 9.734 16.297 1.00 64.74 O ANISOU 3318 O ILE A 310 9705 7668 7225 271 -609 1131 O ATOM 3319 CB ILE A 310 9.831 10.223 13.140 1.00 63.22 C ANISOU 3319 CB ILE A 310 9842 7116 7062 334 -577 842 C ATOM 3320 CG1 ILE A 310 11.274 9.759 13.405 1.00 63.32 C ANISOU 3320 CG1 ILE A 310 9844 7082 7132 338 -551 826 C ATOM 3321 CG2 ILE A 310 9.691 11.736 13.275 1.00 63.78 C ANISOU 3321 CG2 ILE A 310 9943 7292 6999 371 -492 763 C ATOM 3322 CD1 ILE A 310 12.265 10.216 12.347 1.00 66.49 C ANISOU 3322 CD1 ILE A 310 10370 7377 7518 386 -490 681 C ATOM 3323 N TYR A 311 7.661 10.892 15.732 1.00 61.43 N ANISOU 3323 N TYR A 311 9340 7323 6676 299 -608 1095 N ATOM 3324 CA TYR A 311 7.500 11.499 17.065 1.00 61.47 C ANISOU 3324 CA TYR A 311 9227 7550 6580 314 -574 1147 C ATOM 3325 C TYR A 311 7.127 10.442 18.124 1.00 67.34 C ANISOU 3325 C TYR A 311 9800 8411 7373 266 -648 1342 C ATOM 3326 O TYR A 311 7.730 10.417 19.196 1.00 67.32 O ANISOU 3326 O TYR A 311 9694 8538 7345 264 -625 1391 O ATOM 3327 CB TYR A 311 6.440 12.625 17.059 1.00 61.92 C ANISOU 3327 CB TYR A 311 9297 7716 6514 353 -547 1105 C ATOM 3328 CG TYR A 311 6.687 13.739 16.060 1.00 61.88 C ANISOU 3328 CG TYR A 311 9439 7609 6464 397 -482 933 C ATOM 3329 CD1 TYR A 311 7.967 14.252 15.860 1.00 63.31 C ANISOU 3329 CD1 TYR A 311 9686 7722 6646 421 -418 817 C ATOM 3330 CD2 TYR A 311 5.627 14.371 15.419 1.00 62.11 C ANISOU 3330 CD2 TYR A 311 9523 7634 6444 414 -482 898 C ATOM 3331 CE1 TYR A 311 8.197 15.296 14.961 1.00 63.68 C ANISOU 3331 CE1 TYR A 311 9851 7687 6659 457 -366 679 C ATOM 3332 CE2 TYR A 311 5.842 15.413 14.516 1.00 62.44 C ANISOU 3332 CE2 TYR A 311 9684 7590 6451 450 -427 755 C ATOM 3333 CZ TYR A 311 7.129 15.879 14.295 1.00 69.22 C ANISOU 3333 CZ TYR A 311 10602 8378 7320 471 -371 649 C ATOM 3334 OH TYR A 311 7.342 16.920 13.421 1.00 67.72 O ANISOU 3334 OH TYR A 311 10514 8114 7103 503 -323 527 O ATOM 3335 N THR A 312 6.148 9.565 17.815 1.00 65.04 N ANISOU 3335 N THR A 312 9477 8077 7159 224 -743 1461 N ATOM 3336 CA THR A 312 5.674 8.542 18.757 1.00 66.29 C ANISOU 3336 CA THR A 312 9462 8347 7378 171 -830 1672 C ATOM 3337 C THR A 312 6.662 7.360 18.892 1.00 71.84 C ANISOU 3337 C THR A 312 10124 8939 8235 125 -877 1736 C ATOM 3338 O THR A 312 6.552 6.589 19.854 1.00 72.57 O ANISOU 3338 O THR A 312 10051 9142 8378 82 -936 1913 O ATOM 3339 CB THR A 312 4.285 8.022 18.347 1.00 74.33 C ANISOU 3339 CB THR A 312 10458 9346 8438 138 -926 1788 C ATOM 3340 OG1 THR A 312 4.315 7.620 16.977 1.00 73.73 O ANISOU 3340 OG1 THR A 312 10529 9024 8462 127 -963 1699 O ATOM 3341 CG2 THR A 312 3.183 9.050 18.574 1.00 72.45 C ANISOU 3341 CG2 THR A 312 10205 9278 8046 178 -891 1783 C ATOM 3342 N LEU A 313 7.620 7.217 17.950 1.00 68.27 N ANISOU 3342 N LEU A 313 9808 8279 7854 138 -852 1599 N ATOM 3343 CA LEU A 313 8.574 6.105 17.994 1.00 68.68 C ANISOU 3343 CA LEU A 313 9829 8211 8055 103 -897 1644 C ATOM 3344 C LEU A 313 9.907 6.496 18.660 1.00 73.90 C ANISOU 3344 C LEU A 313 10470 8935 8672 123 -805 1591 C ATOM 3345 O LEU A 313 10.483 5.677 19.383 1.00 74.02 O ANISOU 3345 O LEU A 313 10375 8974 8774 85 -837 1703 O ATOM 3346 CB LEU A 313 8.849 5.554 16.584 1.00 68.37 C ANISOU 3346 CB LEU A 313 9936 7913 8128 111 -938 1534 C ATOM 3347 CG LEU A 313 7.685 4.840 15.879 1.00 73.35 C ANISOU 3347 CG LEU A 313 10582 8439 8848 81 -1057 1596 C ATOM 3348 CD1 LEU A 313 8.066 4.464 14.472 1.00 73.43 C ANISOU 3348 CD1 LEU A 313 10745 8214 8941 106 -1083 1450 C ATOM 3349 CD2 LEU A 313 7.236 3.600 16.647 1.00 76.44 C ANISOU 3349 CD2 LEU A 313 10808 8856 9380 11 -1185 1815 C ATOM 3350 N THR A 314 10.413 7.721 18.401 1.00 70.66 N ANISOU 3350 N THR A 314 10164 8545 8138 179 -697 1429 N ATOM 3351 CA THR A 314 11.719 8.136 18.931 1.00 70.64 C ANISOU 3351 CA THR A 314 10157 8584 8098 198 -614 1371 C ATOM 3352 C THR A 314 11.585 9.200 20.055 1.00 75.28 C ANISOU 3352 C THR A 314 10663 9408 8532 223 -550 1371 C ATOM 3353 O THR A 314 12.588 9.818 20.436 1.00 74.73 O ANISOU 3353 O THR A 314 10607 9379 8407 247 -475 1296 O ATOM 3354 CB THR A 314 12.622 8.647 17.797 1.00 79.34 C ANISOU 3354 CB THR A 314 11431 9520 9196 241 -551 1191 C ATOM 3355 OG1 THR A 314 11.999 9.762 17.165 1.00 78.84 O ANISOU 3355 OG1 THR A 314 11464 9464 9029 283 -511 1080 O ATOM 3356 CG2 THR A 314 12.939 7.563 16.766 1.00 78.90 C ANISOU 3356 CG2 THR A 314 11446 9249 9284 230 -612 1175 C ATOM 3357 N ASN A 315 10.367 9.374 20.616 1.00 72.36 N ANISOU 3357 N ASN A 315 10200 9199 8094 221 -584 1460 N ATOM 3358 CA ASN A 315 10.154 10.299 21.733 1.00 72.19 C ANISOU 3358 CA ASN A 315 10084 9421 7925 256 -536 1460 C ATOM 3359 C ASN A 315 8.986 9.821 22.606 1.00 76.97 C ANISOU 3359 C ASN A 315 10518 10225 8504 232 -603 1643 C ATOM 3360 O ASN A 315 7.823 9.918 22.203 1.00 75.95 O ANISOU 3360 O ASN A 315 10403 10102 8351 238 -642 1669 O ATOM 3361 CB ASN A 315 9.921 11.724 21.234 1.00 71.58 C ANISOU 3361 CB ASN A 315 10127 9341 7729 321 -471 1286 C ATOM 3362 CG ASN A 315 10.147 12.784 22.284 1.00 91.97 C ANISOU 3362 CG ASN A 315 12644 12127 10174 371 -413 1228 C ATOM 3363 OD1 ASN A 315 9.512 12.802 23.347 1.00 87.79 O ANISOU 3363 OD1 ASN A 315 11968 11823 9566 380 -431 1322 O ATOM 3364 ND2 ASN A 315 11.023 13.723 21.985 1.00 80.96 N ANISOU 3364 ND2 ASN A 315 11354 10663 8745 408 -347 1071 N ATOM 3365 N LYS A 316 9.310 9.280 23.799 1.00 75.07 N ANISOU 3365 N LYS A 316 10105 10151 8266 203 -619 1782 N ATOM 3366 CA LYS A 316 8.323 8.745 24.743 1.00 76.02 C ANISOU 3366 CA LYS A 316 10030 10491 8364 178 -686 1986 C ATOM 3367 C LYS A 316 7.526 9.865 25.416 1.00 79.79 C ANISOU 3367 C LYS A 316 10451 11217 8650 247 -646 1946 C ATOM 3368 O LYS A 316 6.352 9.665 25.732 1.00 79.76 O ANISOU 3368 O LYS A 316 10341 11357 8606 244 -702 2077 O ATOM 3369 CB LYS A 316 9.000 7.862 25.807 1.00 79.35 C ANISOU 3369 CB LYS A 316 10276 11028 8847 126 -710 2148 C ATOM 3370 CG LYS A 316 9.499 6.525 25.258 1.00 96.22 C ANISOU 3370 CG LYS A 316 12424 12940 11196 53 -782 2239 C ATOM 3371 CD LYS A 316 9.934 5.577 26.372 1.00107.35 C ANISOU 3371 CD LYS A 316 13626 14483 12677 -6 -824 2442 C ATOM 3372 CE LYS A 316 10.343 4.226 25.835 1.00115.59 C ANISOU 3372 CE LYS A 316 14674 15296 13948 -77 -911 2535 C ATOM 3373 NZ LYS A 316 10.728 3.291 26.926 1.00123.40 N ANISOU 3373 NZ LYS A 316 15448 16416 15022 -140 -958 2750 N ATOM 3374 N GLU A 317 8.161 11.048 25.631 1.00 75.74 N ANISOU 3374 N GLU A 317 10003 10753 8020 311 -557 1766 N ATOM 3375 CA GLU A 317 7.502 12.218 26.239 1.00 75.43 C ANISOU 3375 CA GLU A 317 9924 10935 7802 392 -521 1690 C ATOM 3376 C GLU A 317 6.378 12.738 25.328 1.00 77.00 C ANISOU 3376 C GLU A 317 10229 11054 7971 422 -534 1628 C ATOM 3377 O GLU A 317 5.315 13.129 25.823 1.00 77.17 O ANISOU 3377 O GLU A 317 10163 11276 7881 465 -550 1674 O ATOM 3378 CB GLU A 317 8.520 13.333 26.532 1.00 76.53 C ANISOU 3378 CB GLU A 317 10128 11092 7858 449 -438 1498 C ATOM 3379 CG GLU A 317 9.463 12.997 27.677 1.00 91.50 C ANISOU 3379 CG GLU A 317 11888 13139 9738 432 -421 1563 C ATOM 3380 CD GLU A 317 10.527 14.036 27.988 1.00121.18 C ANISOU 3380 CD GLU A 317 15709 16908 13427 482 -350 1382 C ATOM 3381 OE1 GLU A 317 10.249 15.247 27.831 1.00121.75 O ANISOU 3381 OE1 GLU A 317 15859 16997 13404 556 -321 1218 O ATOM 3382 OE2 GLU A 317 11.618 13.637 28.455 1.00117.88 O1- ANISOU 3382 OE2 GLU A 317 15247 16491 13050 447 -329 1413 O1- ATOM 3383 N MET A 318 6.594 12.679 23.995 1.00 70.64 N ANISOU 3383 N MET A 318 9603 9969 7267 400 -532 1537 N ATOM 3384 CA MET A 318 5.592 13.066 23.005 1.00 69.07 C ANISOU 3384 CA MET A 318 9512 9671 7059 416 -546 1487 C ATOM 3385 C MET A 318 4.523 11.973 22.869 1.00 73.78 C ANISOU 3385 C MET A 318 10030 10276 7727 360 -639 1684 C ATOM 3386 O MET A 318 3.331 12.284 22.806 1.00 72.72 O ANISOU 3386 O MET A 318 9873 10232 7524 382 -662 1723 O ATOM 3387 CB MET A 318 6.249 13.355 21.641 1.00 69.93 C ANISOU 3387 CB MET A 318 9826 9499 7246 412 -512 1328 C ATOM 3388 CG MET A 318 7.055 14.633 21.624 1.00 72.35 C ANISOU 3388 CG MET A 318 10219 9792 7478 472 -430 1137 C ATOM 3389 SD MET A 318 7.227 15.338 19.970 1.00 74.98 S ANISOU 3389 SD MET A 318 10770 9864 7854 487 -396 966 S ATOM 3390 CE MET A 318 8.727 14.612 19.463 1.00 71.11 C ANISOU 3390 CE MET A 318 10349 9184 7485 446 -381 943 C ATOM 3391 N ARG A 319 4.955 10.686 22.855 1.00 72.00 N ANISOU 3391 N ARG A 319 9754 9957 7645 286 -699 1814 N ATOM 3392 CA ARG A 319 4.068 9.522 22.729 1.00 72.93 C ANISOU 3392 CA ARG A 319 9790 10055 7867 222 -808 2014 C ATOM 3393 C ARG A 319 3.107 9.417 23.921 1.00 78.31 C ANISOU 3393 C ARG A 319 10260 11040 8453 227 -848 2202 C ATOM 3394 O ARG A 319 1.965 8.984 23.749 1.00 77.69 O ANISOU 3394 O ARG A 319 10131 10992 8395 202 -923 2339 O ATOM 3395 CB ARG A 319 4.890 8.231 22.601 1.00 73.90 C ANISOU 3395 CB ARG A 319 9888 10019 8171 149 -867 2102 C ATOM 3396 N ARG A 320 3.572 9.822 25.126 1.00 76.46 N ANISOU 3396 N ARG A 320 9900 11041 8110 264 -798 2210 N ATOM 3397 CA ARG A 320 2.768 9.817 26.353 1.00 77.88 C ANISOU 3397 CA ARG A 320 9864 11554 8173 286 -825 2375 C ATOM 3398 C ARG A 320 1.612 10.820 26.232 1.00 83.00 C ANISOU 3398 C ARG A 320 10541 12325 8670 360 -803 2311 C ATOM 3399 O ARG A 320 0.487 10.518 26.641 1.00 83.14 O ANISOU 3399 O ARG A 320 10424 12523 8642 357 -862 2486 O ATOM 3400 CB ARG A 320 3.654 10.153 27.569 1.00 78.79 C ANISOU 3400 CB ARG A 320 9861 11883 8194 320 -767 2353 C ATOM 3401 CG ARG A 320 3.102 9.662 28.905 1.00 90.05 C ANISOU 3401 CG ARG A 320 11020 13649 9548 315 -814 2583 C ATOM 3402 CD ARG A 320 4.049 10.001 30.043 1.00 99.66 C ANISOU 3402 CD ARG A 320 12127 15067 10670 348 -754 2544 C ATOM 3403 NE ARG A 320 3.607 9.438 31.320 1.00111.73 N ANISOU 3403 NE ARG A 320 13384 16934 12136 339 -801 2780 N ATOM 3404 CZ ARG A 320 4.037 8.279 31.814 1.00125.39 C ANISOU 3404 CZ ARG A 320 14963 18693 13986 253 -857 2988 C ATOM 3405 NH1 ARG A 320 4.921 7.549 31.142 1.00111.15 N ANISOU 3405 NH1 ARG A 320 13263 16593 12375 175 -873 2978 N ATOM 3406 NH2 ARG A 320 3.589 7.842 32.985 1.00111.13 N ANISOU 3406 NH2 ARG A 320 12895 17221 12110 248 -899 3212 N ATOM 3407 N ALA A 321 1.887 11.998 25.631 1.00 79.89 N ANISOU 3407 N ALA A 321 10320 11825 8209 424 -722 2069 N ATOM 3408 CA ALA A 321 0.889 13.050 25.420 1.00 80.09 C ANISOU 3408 CA ALA A 321 10393 11935 8104 499 -696 1980 C ATOM 3409 C ALA A 321 -0.106 12.665 24.322 1.00 85.04 C ANISOU 3409 C ALA A 321 11107 12397 8808 457 -751 2042 C ATOM 3410 O ALA A 321 -1.272 13.033 24.408 1.00 84.47 O ANISOU 3410 O ALA A 321 10991 12461 8643 493 -767 2094 O ATOM 3411 CB ALA A 321 1.577 14.359 25.062 1.00 79.96 C ANISOU 3411 CB ALA A 321 10530 11826 8025 569 -606 1713 C ATOM 3412 N PHE A 322 0.358 11.918 23.295 1.00 82.67 N ANISOU 3412 N PHE A 322 10926 11809 8674 383 -783 2035 N ATOM 3413 CA PHE A 322 -0.465 11.488 22.157 1.00 82.81 C ANISOU 3413 CA PHE A 322 11041 11644 8781 338 -841 2078 C ATOM 3414 C PHE A 322 -1.615 10.564 22.610 1.00 88.53 C ANISOU 3414 C PHE A 322 11600 12508 9529 292 -946 2341 C ATOM 3415 O PHE A 322 -2.764 10.791 22.231 1.00 87.56 O ANISOU 3415 O PHE A 322 11492 12415 9361 301 -972 2386 O ATOM 3416 CB PHE A 322 0.410 10.784 21.107 1.00 84.25 C ANISOU 3416 CB PHE A 322 11360 11516 9134 279 -861 2013 C ATOM 3417 CG PHE A 322 -0.297 10.461 19.814 1.00 86.01 C ANISOU 3417 CG PHE A 322 11707 11532 9442 243 -913 2009 C ATOM 3418 CD1 PHE A 322 -0.421 11.418 18.813 1.00 88.70 C ANISOU 3418 CD1 PHE A 322 12216 11753 9734 283 -851 1828 C ATOM 3419 CD2 PHE A 322 -0.794 9.184 19.574 1.00 89.13 C ANISOU 3419 CD2 PHE A 322 12048 11843 9975 166 -1031 2185 C ATOM 3420 CE1 PHE A 322 -1.060 11.114 17.609 1.00 89.60 C ANISOU 3420 CE1 PHE A 322 12439 11685 9919 249 -898 1822 C ATOM 3421 CE2 PHE A 322 -1.434 8.881 18.371 1.00 91.99 C ANISOU 3421 CE2 PHE A 322 12525 12011 10414 135 -1085 2171 C ATOM 3422 CZ PHE A 322 -1.558 9.845 17.394 1.00 89.46 C ANISOU 3422 CZ PHE A 322 12371 11590 10031 177 -1015 1987 C ATOM 3423 N ILE A 323 -1.303 9.544 23.441 1.00 87.80 N ANISOU 3423 N ILE A 323 11343 12509 9508 240 -1008 2524 N ATOM 3424 CA ILE A 323 -2.299 8.599 23.973 1.00 89.73 C ANISOU 3424 CA ILE A 323 11403 12900 9791 187 -1120 2805 C ATOM 3425 C ILE A 323 -3.176 9.314 25.039 1.00 96.61 C ANISOU 3425 C ILE A 323 12115 14135 10458 262 -1092 2883 C ATOM 3426 O ILE A 323 -4.313 8.901 25.284 1.00 96.51 O ANISOU 3426 O ILE A 323 11978 14263 10428 242 -1169 3089 O ATOM 3427 CB ILE A 323 -1.601 7.320 24.551 1.00 93.53 C ANISOU 3427 CB ILE A 323 11746 13369 10423 108 -1196 2979 C ATOM 3428 CG1 ILE A 323 -0.580 6.731 23.538 1.00 93.43 C ANISOU 3428 CG1 ILE A 323 11898 13006 10596 57 -1209 2861 C ATOM 3429 CG2 ILE A 323 -2.638 6.255 24.977 1.00 95.33 C ANISOU 3429 CG2 ILE A 323 11781 13714 10725 41 -1333 3291 C ATOM 3430 CD1 ILE A 323 0.435 5.723 24.143 1.00102.02 C ANISOU 3430 CD1 ILE A 323 12874 14070 11818 -1 -1251 2968 C ATOM 3431 N ARG A 324 -2.609 10.341 25.638 1.00 95.12 N ANISOU 3431 N ARG A 324 11930 14088 10124 347 -990 2719 N ATOM 3432 CA ARG A 324 -3.298 11.089 26.649 1.00 96.37 C ANISOU 3432 CA ARG A 324 11946 14589 10081 435 -959 2750 C ATOM 3433 C ARG A 324 -4.346 11.877 25.966 1.00101.49 C ANISOU 3433 C ARG A 324 12698 15215 10650 484 -941 2673 C ATOM 3434 O ARG A 324 -5.004 12.698 26.568 1.00101.28 O ANISOU 3434 O ARG A 324 12597 15434 10450 574 -907 2650 O ATOM 3435 CB ARG A 324 -2.327 12.030 27.352 1.00 96.19 C ANISOU 3435 CB ARG A 324 11927 14682 9940 516 -860 2556 C ATOM 3436 N ILE A 325 -4.546 11.621 24.689 1.00 98.83 N ANISOU 3436 N ILE A 325 12528 14585 10437 428 -969 2635 N ATOM 3437 CA ILE A 325 -5.561 12.382 24.006 1.00 99.09 C ANISOU 3437 CA ILE A 325 12658 14594 10396 470 -950 2568 C ATOM 3438 C ILE A 325 -6.773 11.707 23.440 1.00105.80 C ANISOU 3438 C ILE A 325 13490 15400 11308 410 -1041 2755 C ATOM 3439 O ILE A 325 -7.264 12.144 22.426 1.00104.38 O ANISOU 3439 O ILE A 325 13460 15061 11137 412 -1026 2662 O ATOM 3440 CB ILE A 325 -4.957 13.118 22.874 1.00100.89 C ANISOU 3440 CB ILE A 325 13120 14547 10667 483 -880 2314 C ATOM 3441 CG1 ILE A 325 -3.636 13.738 23.320 1.00100.78 C ANISOU 3441 CG1 ILE A 325 13140 14534 10619 530 -799 2128 C ATOM 3442 CG2 ILE A 325 -5.938 14.144 22.395 1.00101.25 C ANISOU 3442 CG2 ILE A 325 13242 14622 10605 545 -843 2227 C ATOM 3443 CD1 ILE A 325 -3.777 15.091 23.889 1.00106.79 C ANISOU 3443 CD1 ILE A 325 13889 15479 11207 644 -724 1977 C ATOM 3444 N MET A 326 -7.267 10.662 24.073 1.00105.96 N ANISOU 3444 N MET A 326 13325 15562 11373 354 -1139 3025 N ATOM 3445 CA MET A 326 -8.443 9.974 23.565 1.00107.43 C ANISOU 3445 CA MET A 326 13484 15706 11628 291 -1242 3224 C ATOM 3446 C MET A 326 -9.834 10.467 23.968 1.00113.19 C ANISOU 3446 C MET A 326 14108 16701 12197 347 -1249 3347 C ATOM 3447 O MET A 326 -10.517 9.805 24.730 1.00113.82 O ANISOU 3447 O MET A 326 13984 17002 12260 324 -1331 3610 O ATOM 3448 CB MET A 326 -8.323 8.490 23.858 1.00110.90 C ANISOU 3448 CB MET A 326 13787 16113 12238 186 -1369 3473 C ATOM 3449 CG MET A 326 -7.194 7.870 23.095 1.00114.42 C ANISOU 3449 CG MET A 326 14371 16228 12874 120 -1385 3360 C ATOM 3450 SD MET A 326 -7.460 8.073 21.345 1.00118.25 S ANISOU 3450 SD MET A 326 15124 16357 13447 95 -1385 3186 S ATOM 3451 CE MET A 326 -8.891 7.040 21.111 1.00116.07 C ANISOU 3451 CE MET A 326 14747 16085 13269 11 -1547 3483 C ATOM 3452 N GLY A 327 -10.249 11.617 23.455 1.00110.06 N ANISOU 3452 N GLY A 327 13843 16287 11689 421 -1168 3166 N ATOM 3453 CA GLY A 327 -11.555 12.192 23.741 1.00110.91 C ANISOU 3453 CA GLY A 327 13871 16630 11641 486 -1165 3253 C ATOM 3454 C GLY A 327 -12.127 12.463 22.361 1.00115.34 C ANISOU 3454 C GLY A 327 14628 16933 12261 454 -1163 3169 C ATOM 3455 O GLY A 327 -11.483 13.146 21.576 1.00113.93 O ANISOU 3455 O GLY A 327 14639 16541 12108 473 -1088 2922 O ATOM 3456 N ARG A 328 -13.305 11.951 22.023 1.00113.19 N ANISOU 3456 N ARG A 328 14314 16678 12015 404 -1247 3371 N ATOM 3457 CA ARG A 328 -13.812 12.229 20.682 1.00112.52 C ANISOU 3457 CA ARG A 328 14420 16349 11985 373 -1241 3281 C ATOM 3458 C ARG A 328 -14.175 13.674 20.378 1.00116.29 C ANISOU 3458 C ARG A 328 15002 16868 12315 472 -1130 3080 C ATOM 3459 O ARG A 328 -13.732 14.234 19.393 1.00114.89 O ANISOU 3459 O ARG A 328 15016 16454 12184 471 -1071 2869 O ATOM 3460 CB ARG A 328 -15.024 11.345 20.389 1.00113.48 C ANISOU 3460 CB ARG A 328 14471 16477 12171 293 -1364 3553 C ATOM 3461 N PRO A 329 -14.970 14.288 21.226 1.00113.71 N ANISOU 3461 N PRO A 329 14543 16847 11813 562 -1104 3147 N ATOM 3462 CA PRO A 329 -15.352 15.667 21.005 1.00112.95 C ANISOU 3462 CA PRO A 329 14533 16798 11583 664 -1008 2960 C ATOM 3463 C PRO A 329 -14.192 16.613 21.169 1.00115.51 C ANISOU 3463 C PRO A 329 14944 17071 11875 739 -909 2677 C ATOM 3464 O PRO A 329 -14.075 17.569 20.441 1.00114.45 O ANISOU 3464 O PRO A 329 14962 16791 11732 775 -841 2472 O ATOM 3465 CB PRO A 329 -16.423 15.874 22.050 1.00115.94 C ANISOU 3465 CB PRO A 329 14713 17551 11788 745 -1023 3131 C ATOM 3466 CG PRO A 329 -17.131 14.514 22.069 1.00121.25 C ANISOU 3466 CG PRO A 329 15266 18252 12549 637 -1151 3456 C ATOM 3467 CD PRO A 329 -16.159 13.481 21.522 1.00116.36 C ANISOU 3467 CD PRO A 329 14725 17344 12142 517 -1208 3457 C ATOM 3468 N LEU A 330 -13.355 16.353 22.157 1.00111.74 N ANISOU 3468 N LEU A 330 14356 16723 11378 762 -907 2677 N ATOM 3469 CA LEU A 330 -12.216 17.211 22.415 1.00128.01 C ANISOU 3469 CA LEU A 330 16484 18749 13407 831 -823 2422 C ATOM 3470 C LEU A 330 -11.620 17.776 21.140 1.00139.76 C ANISOU 3470 C LEU A 330 18203 19903 14996 804 -771 2200 C ATOM 3471 O LEU A 330 -11.792 18.955 20.853 1.00 95.50 O ANISOU 3471 O LEU A 330 12681 14282 9322 880 -707 2026 O ATOM 3472 CB LEU A 330 -11.167 16.489 23.255 1.00128.31 C ANISOU 3472 CB LEU A 330 16418 18849 13487 804 -842 2468 C ATOM 3473 CG LEU A 330 -11.443 16.572 24.754 1.00134.09 C ANISOU 3473 CG LEU A 330 16920 19972 14054 891 -847 2571 C ATOM 3474 CD1 LEU A 330 -11.580 18.014 25.191 1.00136.52 C ANISOU 3474 CD1 LEU A 330 17238 20440 14194 1037 -768 2361 C ATOM 3475 CD2 LEU A 330 -12.710 15.812 25.064 1.00135.19 C ANISOU 3475 CD2 LEU A 330 16899 20309 14158 861 -930 2869 C TER 3476 LEU A 330 HETATM 3477 O4 ML5 A1201 1.859 15.406 -15.112 1.00 61.98 O ANISOU 3477 O4 ML5 A1201 10789 6872 5887 775 -508 -602 O HETATM 3478 P1 ML5 A1201 2.958 15.961 -14.230 1.00 63.34 P ANISOU 3478 P1 ML5 A1201 10931 7052 6083 791 -439 -559 P HETATM 3479 O2 ML5 A1201 4.257 16.223 -14.961 1.00 61.32 O1- ANISOU 3479 O2 ML5 A1201 10632 6915 5752 879 -385 -619 O1- HETATM 3480 O3 ML5 A1201 2.513 17.100 -13.343 1.00 63.92 O1- ANISOU 3480 O3 ML5 A1201 10977 7124 6185 714 -376 -427 O1- HETATM 3481 C16 ML5 A1201 3.339 14.620 -13.065 1.00 61.02 C ANISOU 3481 C16 ML5 A1201 10686 6595 5905 802 -525 -600 C HETATM 3482 C15 ML5 A1201 4.228 15.142 -11.935 1.00 59.17 C ANISOU 3482 C15 ML5 A1201 10425 6352 5707 797 -463 -539 C HETATM 3483 C14 ML5 A1201 3.498 16.070 -10.953 1.00 57.23 C ANISOU 3483 C14 ML5 A1201 10160 6094 5491 713 -422 -411 C HETATM 3484 N2 ML5 A1201 2.027 15.824 -10.929 1.00 55.96 N ANISOU 3484 N2 ML5 A1201 10024 5884 5354 646 -478 -365 N HETATM 3485 C13 ML5 A1201 4.104 15.918 -9.586 1.00 57.20 C ANISOU 3485 C13 ML5 A1201 10150 6027 5557 704 -417 -374 C HETATM 3486 O1 ML5 A1201 3.974 14.863 -8.984 1.00 57.79 O ANISOU 3486 O1 ML5 A1201 10248 6006 5703 696 -492 -385 O HETATM 3487 N1 ML5 A1201 4.792 16.977 -9.133 1.00 56.97 N ANISOU 3487 N1 ML5 A1201 10081 6055 5511 705 -335 -327 N HETATM 3488 C5 ML5 A1201 5.183 17.183 -7.838 1.00 58.11 C ANISOU 3488 C5 ML5 A1201 10209 6166 5706 685 -317 -276 C HETATM 3489 C4 ML5 A1201 4.971 16.239 -6.821 1.00 58.07 C ANISOU 3489 C4 ML5 A1201 10218 6072 5774 662 -378 -259 C HETATM 3490 C3 ML5 A1201 5.409 16.496 -5.517 1.00 57.44 C ANISOU 3490 C3 ML5 A1201 10110 5981 5733 645 -354 -207 C HETATM 3491 C2 ML5 A1201 6.067 17.694 -5.218 1.00 56.94 C ANISOU 3491 C2 ML5 A1201 10013 5981 5642 652 -275 -181 C HETATM 3492 C6 ML5 A1201 5.856 18.372 -7.530 1.00 57.95 C ANISOU 3492 C6 ML5 A1201 10146 6205 5665 688 -239 -236 C HETATM 3493 C1 ML5 A1201 6.314 18.621 -6.233 1.00 57.27 C ANISOU 3493 C1 ML5 A1201 10041 6094 5624 673 -222 -195 C HETATM 3494 C7 ML5 A1201 6.996 19.936 -5.924 1.00 58.74 C ANISOU 3494 C7 ML5 A1201 10184 6335 5800 675 -153 -157 C HETATM 3495 C8 ML5 A1201 8.438 19.706 -5.492 1.00 59.50 C ANISOU 3495 C8 ML5 A1201 10268 6427 5911 717 -134 -179 C HETATM 3496 C9 ML5 A1201 9.242 20.998 -5.618 1.00 58.43 C ANISOU 3496 C9 ML5 A1201 10086 6354 5759 728 -74 -146 C HETATM 3497 C10 ML5 A1201 10.511 20.780 -6.434 1.00 57.39 C ANISOU 3497 C10 ML5 A1201 9943 6272 5592 790 -53 -179 C HETATM 3498 C11 ML5 A1201 11.750 21.017 -5.582 1.00 56.60 C ANISOU 3498 C11 ML5 A1201 9820 6166 5521 805 -28 -159 C HETATM 3499 C12 ML5 A1201 12.527 22.221 -6.067 1.00 56.83 C ANISOU 3499 C12 ML5 A1201 9794 6269 5532 818 16 -110 C HETATM 3500 C1 NAG A1202 3.028 18.355 -31.468 1.00 93.65 C ANISOU 3500 C1 NAG A1202 13879 13425 8278 1456 -226 -1029 C HETATM 3501 C2 NAG A1202 4.312 17.900 -32.270 1.00 96.98 C ANISOU 3501 C2 NAG A1202 14217 14082 8547 1635 -227 -1153 C HETATM 3502 C3 NAG A1202 3.859 17.432 -33.692 1.00 99.98 C ANISOU 3502 C3 NAG A1202 14540 14686 8759 1715 -269 -1284 C HETATM 3503 C4 NAG A1202 2.619 16.480 -33.670 1.00100.69 C ANISOU 3503 C4 NAG A1202 14771 14580 8907 1673 -376 -1426 C HETATM 3504 C5 NAG A1202 1.486 17.107 -32.792 1.00 98.15 C ANISOU 3504 C5 NAG A1202 14517 14034 8743 1484 -355 -1255 C HETATM 3505 C6 NAG A1202 0.231 16.216 -32.618 1.00 99.38 C ANISOU 3505 C6 NAG A1202 14811 13974 8976 1425 -463 -1357 C HETATM 3506 C7 NAG A1202 6.708 18.794 -32.145 1.00 99.75 C ANISOU 3506 C7 NAG A1202 14390 14688 8823 1759 -111 -1016 C HETATM 3507 C8 NAG A1202 7.525 20.049 -32.331 1.00100.34 C ANISOU 3507 C8 NAG A1202 14299 14966 8859 1746 -16 -802 C HETATM 3508 N2 NAG A1202 5.350 18.965 -32.379 1.00 97.87 N ANISOU 3508 N2 NAG A1202 14182 14391 8612 1653 -129 -987 N HETATM 3509 O3 NAG A1202 4.968 16.803 -34.352 1.00103.62 O ANISOU 3509 O3 NAG A1202 14946 15342 9083 1896 -288 -1438 O HETATM 3510 O4 NAG A1202 2.158 16.320 -35.023 1.00104.48 O ANISOU 3510 O4 NAG A1202 15175 15296 9226 1729 -399 -1509 O HETATM 3511 O5 NAG A1202 1.997 17.358 -31.486 1.00 95.20 O ANISOU 3511 O5 NAG A1202 14198 13462 8510 1437 -326 -1169 O HETATM 3512 O6 NAG A1202 -0.673 16.751 -31.630 1.00 99.66 O ANISOU 3512 O6 NAG A1202 14911 13796 9161 1264 -443 -1196 O HETATM 3513 O7 NAG A1202 7.218 17.723 -31.814 1.00102.25 O ANISOU 3513 O7 NAG A1202 14800 14898 9153 1853 -171 -1191 O HETATM 3514 O HOH A1203 0.872 33.521 -16.199 1.00 12.35 O ANISOU 3514 O HOH A1203 3120 1053 519 292 132 301 O HETATM 3515 O HOH A1204 -7.268 25.745 -25.572 1.00 17.61 O ANISOU 3515 O HOH A1204 4042 2234 414 189 25 230 O HETATM 3516 O HOH A1205 41.164 3.539 46.391 1.00 67.44 O ANISOU 3516 O HOH A1205 6468 11784 7374 -1052 689 3890 O HETATM 3517 O HOH A1206 1.060 29.714 26.271 1.00 20.72 O ANISOU 3517 O HOH A1206 3198 4235 441 1667 -327 -422 O HETATM 3518 O HOH A1207 1.162 32.240 23.211 1.00 33.87 O ANISOU 3518 O HOH A1207 5567 5529 1771 1630 -418 -779 O HETATM 3519 O HOH A1208 12.700 12.040 -4.386 1.00 14.56 O ANISOU 3519 O HOH A1208 4437 605 491 882 -449 -138 O HETATM 3520 O HOH A1209 -13.774 21.336 23.352 1.00 36.48 O ANISOU 3520 O HOH A1209 4885 7627 1348 1243 -639 1957 O HETATM 3521 O HOH A1210 5.980 13.788 -14.826 1.00 19.53 O ANISOU 3521 O HOH A1210 5221 1460 740 1035 -516 -614 O HETATM 3522 O HOH A1211 53.979 34.851 49.565 0.50102.59 O ANISOU 3522 O HOH A1211 13248 14823 10908 -218 -1200 -278 O HETATM 3523 O HOH A1212 41.278 15.531 24.643 1.00 14.78 O ANISOU 3523 O HOH A1212 2972 1577 1067 195 464 871 O HETATM 3524 O HOH A1213 30.370 2.816 23.770 1.00 15.40 O ANISOU 3524 O HOH A1213 2458 1496 1898 5 -42 1297 O CONECT 132 3500 CONECT 1260 1305 CONECT 1305 1260 CONECT 3106 3140 CONECT 3140 3106 CONECT 3477 3478 CONECT 3478 3477 3479 3480 3481 CONECT 3479 3478 CONECT 3480 3478 CONECT 3481 3478 3482 CONECT 3482 3481 3483 CONECT 3483 3482 3484 3485 CONECT 3484 3483 CONECT 3485 3483 3486 3487 CONECT 3486 3485 CONECT 3487 3485 3488 CONECT 3488 3487 3489 3492 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3493 CONECT 3492 3488 3493 CONECT 3493 3491 3492 3494 CONECT 3494 3493 3495 CONECT 3495 3494 3496 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 CONECT 3499 3498 CONECT 3500 132 3501 3511 CONECT 3501 3500 3502 3508 CONECT 3502 3501 3503 3509 CONECT 3503 3502 3504 3510 CONECT 3504 3503 3505 3511 CONECT 3505 3504 3512 CONECT 3506 3507 3508 3513 CONECT 3507 3506 CONECT 3508 3501 3506 CONECT 3509 3502 CONECT 3510 3503 CONECT 3511 3500 3504 CONECT 3512 3505 CONECT 3513 3506 MASTER 408 0 2 23 3 0 0 6 3523 1 42 40 END