HEADER MEMBRANE PROTEIN 12-JUN-13 4L6R TITLE STRUCTURE OF THE CLASS B HUMAN GLUCAGON G PROTEIN COUPLED RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562 AND GLUCAGON RECEPTOR CHIMERA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 23-128 AND 123-434; COMPND 5 SYNONYM: CYTOCHROME B-562, GL-R; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 562, 9606; SOURCE 5 GENE: CYBC, GCGR_HUMAN, GCGR; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC KEYWDS HUMAN GLUCAGON RECEPTOR, DIABETES, GPCR NETWORK, PSI-BIOLOGY, KEYWDS 2 MEMBRANE PROTEIN, NOVEL PROTEIN ENGINEERING, STRUCTURAL GENOMICS, KEYWDS 3 PROTEIN STRUCTURE INITIATIVE, GPCR, MEMBRANE EXPDTA X-RAY DIFFRACTION AUTHOR F.Y.SIU,M.HE,C.DE GRAAF,G.W.HAN,D.YANG,Z.ZHANG,C.ZHOU,Q.XU,D.WACKER, AUTHOR 2 J.S.JOSEPH,W.LIU,J.LAU,V.CHEREZOV,V.KATRITCH,M.W.WANG,R.C.STEVENS, AUTHOR 3 GPCR NETWORK (GPCR) REVDAT 5 15-NOV-17 4L6R 1 REMARK REVDAT 4 16-AUG-17 4L6R 1 SOURCE REMARK REVDAT 3 07-AUG-13 4L6R 1 JRNL REVDAT 2 31-JUL-13 4L6R 1 JRNL REVDAT 1 24-JUL-13 4L6R 0 JRNL AUTH F.Y.SIU,M.HE,C.DE GRAAF,G.W.HAN,D.YANG,Z.ZHANG,C.ZHOU,Q.XU, JRNL AUTH 2 D.WACKER,J.S.JOSEPH,W.LIU,J.LAU,V.CHEREZOV,V.KATRITCH, JRNL AUTH 3 M.W.WANG,R.C.STEVENS JRNL TITL STRUCTURE OF THE HUMAN GLUCAGON CLASS B G-PROTEIN-COUPLED JRNL TITL 2 RECEPTOR. JRNL REF NATURE V. 499 444 2013 JRNL REFN ISSN 0028-0836 JRNL PMID 23863937 JRNL DOI 10.1038/NATURE12393 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.12 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6 REMARK 3 NUMBER OF REFLECTIONS : 8981 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) : 0.286 REMARK 3 R VALUE (WORKING SET) : 0.284 REMARK 3 FREE R VALUE : 0.339 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790 REMARK 3 FREE R VALUE TEST SET COUNT : 430 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 5 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.69 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.59 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2308 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2830 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2190 REMARK 3 BIN R VALUE (WORKING SET) : 0.2812 REMARK 3 BIN FREE R VALUE : 0.3136 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.11 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 118 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 : 3049 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 7 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 110.4 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 126.8 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.12960 REMARK 3 B22 (A**2) : 21.55530 REMARK 3 B33 (A**2) : -20.42560 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) : 1.234 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 : 0.883 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.842 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3118 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4228 ; 2.500 ; HARMONIC REMARK 3 TORSION ANGLES : 1432 ; 15.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 65 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 459 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3118 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 403 ; 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 : 3725 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.04 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.79 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 1.81 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|1001 - A|1106 } REMARK 3 ORIGIN FOR THE GROUP (A): 16.4176 4.5252 -2.0054 REMARK 3 T TENSOR REMARK 3 T11: 0.1043 T22: 0.0470 REMARK 3 T33: -0.5395 T12: -0.2881 REMARK 3 T13: -0.1636 T23: 0.1298 REMARK 3 L TENSOR REMARK 3 L11: 16.6309 L22: 6.0851 REMARK 3 L33: 14.8771 L12: 2.3438 REMARK 3 L13: 3.4299 L23: 0.6799 REMARK 3 S TENSOR REMARK 3 S11: 0.1704 S12: -0.1676 S13: -0.5400 REMARK 3 S21: 0.7744 S22: -0.1591 S23: -0.9671 REMARK 3 S31: -0.0046 S32: 0.2207 S33: -0.0112 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|123 - A|429 } REMARK 3 ORIGIN FOR THE GROUP (A): 16.1524 -11.4685 -44.8801 REMARK 3 T TENSOR REMARK 3 T11: -0.3790 T22: 0.6079 REMARK 3 T33: -0.6079 T12: -0.2048 REMARK 3 T13: 0.0527 T23: -0.1883 REMARK 3 L TENSOR REMARK 3 L11: 0.9466 L22: 1.2789 REMARK 3 L33: 5.4002 L12: 0.6168 REMARK 3 L13: 1.8062 L23: 2.0350 REMARK 3 S TENSOR REMARK 3 S11: 0.3433 S12: 0.0555 S13: -0.2635 REMARK 3 S21: 0.1079 S22: 0.3087 S23: -0.2990 REMARK 3 S31: -0.3608 S32: 1.0885 S33: -0.6520 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 1. THE DIFFRACTION DATA ARE REMARK 3 ANISOTROPIC. THE RESOLUTION LIMITS OF A*, B*, AND C* AXES ARE REMARK 3 3.3, 3.4 AND 3.3A, RESPECTIVELY. DIFFRAC DATA WERE INCLUDED IN REMARK 3 REFINEMENT TO 3.3A IN THE A* AND C* DIRECTIONS, WITH AN OVERALL REMARK 3 EFFECTIVE AND REPORTED RESOLUTION OF 3.4A. 2. THE DENSITIES AT REMARK 3 THE BOTTOM OF HELIX VI AND VII NEAR LYS349 WERE MODELLED AS A REMARK 3 PEG-400 FRAGMENT (PEG) MOLECULE FROM THE CRYSTALLIZATION REMARK 3 CONDITION. REMARK 4 REMARK 4 4L6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-13. REMARK 100 THE DEPOSITION ID IS D_1000080251. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : AUG-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 14 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0330 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9067 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 200 DATA REDUNDANCY : 6.200 REMARK 200 R MERGE (I) : 0.01050 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.20 REMARK 200 R MERGE FOR SHELL (I) : 0.88200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2Z73 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 140-200 MM NAK REMARK 280 TARTRATE TETRAHYDRATE, 9-17% (V/V) PEG 400, 0.35-0.55% (V/V) REMARK 280 JEFFAMINE M-600 PH 7.0, 200 UM NNC0640, LIPIDIC CUBIC PHASE (LCP) REMARK 280 , TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.30750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.66550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.32550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.66550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.30750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.32550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ARG A 201 REMARK 465 TYR A 202 REMARK 465 SER A 203 REMARK 465 GLN A 204 REMARK 465 LYS A 205 REMARK 465 ILE A 206 REMARK 465 GLY A 207 REMARK 465 ASP A 208 REMARK 465 ASP A 209 REMARK 465 LEU A 210 REMARK 465 SER A 211 REMARK 465 VAL A 212 REMARK 465 SER A 213 REMARK 465 THR A 214 REMARK 465 TRP A 215 REMARK 465 THR A 430 REMARK 465 SER A 431 REMARK 465 ASN A 432 REMARK 465 GLY A 433 REMARK 465 ARG A 434 REMARK 465 PRO A 435 REMARK 465 LEU A 436 REMARK 465 GLU A 437 REMARK 465 VAL A 438 REMARK 465 LEU A 439 REMARK 465 PHE A 440 REMARK 465 GLN A 441 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 TYR A1101 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 225 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 235 CG1 CG2 CD1 REMARK 470 GLU A 260 CG CD OE1 OE2 REMARK 470 ARG A 261 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 263 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A 270 CG1 CG2 CD1 REMARK 470 LEU A 277 CG CD1 CD2 REMARK 470 PHE A 278 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL A 280 CG1 CG2 REMARK 470 TRP A 282 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 282 CZ3 CH2 REMARK 470 VAL A 285 CG1 CG2 REMARK 470 LYS A 286 CG CD CE NZ REMARK 470 CYS A 287 SG REMARK 470 LEU A 288 CG CD1 CD2 REMARK 470 GLU A 290 CG CD OE1 OE2 REMARK 470 ASN A 291 CG OD1 ND2 REMARK 470 VAL A 292 CG1 CG2 REMARK 470 GLN A 293 CG CD OE1 NE2 REMARK 470 TRP A 295 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 295 CZ3 CH2 REMARK 470 THR A 296 OG1 CG2 REMARK 470 SER A 297 OG REMARK 470 ASN A 298 CG OD1 ND2 REMARK 470 ASP A 299 CG OD1 OD2 REMARK 470 ILE A 306 CG1 CG2 CD1 REMARK 470 PHE A 312 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2 REMARK 470 MET A 338 CG SD CE REMARK 470 LYS A 344 CG CD CE NZ REMARK 470 VAL A 363 CG1 CG2 REMARK 470 PHE A 367 CG CD1 CD2 CE1 CE2 CZ REMARK 470 VAL A 368 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 166 -158.71 -165.19 REMARK 500 ASN A 174 44.53 -79.33 REMARK 500 ALA A 175 -39.28 -147.80 REMARK 500 ALA A 220 -33.92 -133.23 REMARK 500 ASN A 238 23.05 -75.58 REMARK 500 LEU A 252 -82.15 -98.63 REMARK 500 ARG A 261 -48.45 -151.72 REMARK 500 LEU A 268 -86.45 -77.59 REMARK 500 VAL A 279 -62.06 -139.61 REMARK 500 TRP A 282 0.52 -67.39 REMARK 500 ALA A 283 -34.72 -136.54 REMARK 500 VAL A 292 -101.01 -135.88 REMARK 500 ASN A 300 -73.42 63.48 REMARK 500 ILE A 306 -79.42 -66.54 REMARK 500 HIS A 340 -19.24 -49.87 REMARK 500 VAL A 368 -41.22 -147.62 REMARK 500 ALA A 373 -85.44 48.21 REMARK 500 PHE A 391 21.77 -73.91 REMARK 500 CYS A 401 -70.08 -95.38 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1200 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: GPCR-49 RELATED DB: TARGETTRACK REMARK 999 REMARK 999 SEQUENCE REMARK 999 GLY430-PRO432 ARE CLONING-SITE RESIDUES AND LEU433-GLN438 ARE REMARK 999 PRECISION CLEAVAGE-SITE RESIDUES. DBREF 4L6R A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 4L6R A 123 432 UNP P47871 GLR_HUMAN 123 432 SEQADV 4L6R TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 4L6R ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 4L6R LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 4L6R GLY A 433 UNP P47871 SEE REMARK 999 SEQADV 4L6R ARG A 434 UNP P47871 SEE REMARK 999 SEQADV 4L6R PRO A 435 UNP P47871 SEE REMARK 999 SEQADV 4L6R LEU A 436 UNP P47871 SEE REMARK 999 SEQADV 4L6R GLU A 437 UNP P47871 SEE REMARK 999 SEQADV 4L6R VAL A 438 UNP P47871 SEE REMARK 999 SEQADV 4L6R LEU A 439 UNP P47871 SEE REMARK 999 SEQADV 4L6R PHE A 440 UNP P47871 SEE REMARK 999 SEQADV 4L6R GLN A 441 UNP P47871 SEE REMARK 999 SEQRES 1 A 425 ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN SEQRES 2 A 425 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL SEQRES 3 A 425 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP SEQRES 4 A 425 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER SEQRES 5 A 425 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE SEQRES 6 A 425 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 7 A 425 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 8 A 425 GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS SEQRES 9 A 425 TYR LEU MET ASP GLY GLU GLU ILE GLU VAL GLN LYS GLU SEQRES 10 A 425 VAL ALA LYS MET TYR SER SER PHE GLN VAL MET TYR THR SEQRES 11 A 425 VAL GLY TYR SER LEU SER LEU GLY ALA LEU LEU LEU ALA SEQRES 12 A 425 LEU ALA ILE LEU GLY GLY LEU SER LYS LEU HIS CYS THR SEQRES 13 A 425 ARG ASN ALA ILE HIS ALA ASN LEU PHE ALA SER PHE VAL SEQRES 14 A 425 LEU LYS ALA SER SER VAL LEU VAL ILE ASP GLY LEU LEU SEQRES 15 A 425 ARG THR ARG TYR SER GLN LYS ILE GLY ASP ASP LEU SER SEQRES 16 A 425 VAL SER THR TRP LEU SER ASP GLY ALA VAL ALA GLY CYS SEQRES 17 A 425 ARG VAL ALA ALA VAL PHE MET GLN TYR GLY ILE VAL ALA SEQRES 18 A 425 ASN TYR CYS TRP LEU LEU VAL GLU GLY LEU TYR LEU HIS SEQRES 19 A 425 ASN LEU LEU GLY LEU ALA THR LEU PRO GLU ARG SER PHE SEQRES 20 A 425 PHE SER LEU TYR LEU GLY ILE GLY TRP GLY ALA PRO MET SEQRES 21 A 425 LEU PHE VAL VAL PRO TRP ALA VAL VAL LYS CYS LEU PHE SEQRES 22 A 425 GLU ASN VAL GLN CYS TRP THR SER ASN ASP ASN MET GLY SEQRES 23 A 425 PHE TRP TRP ILE LEU ARG PHE PRO VAL PHE LEU ALA ILE SEQRES 24 A 425 LEU ILE ASN PHE PHE ILE PHE VAL ARG ILE VAL GLN LEU SEQRES 25 A 425 LEU VAL ALA LYS LEU ARG ALA ARG GLN MET HIS HIS THR SEQRES 26 A 425 ASP TYR LYS PHE ARG LEU ALA LYS SER THR LEU THR LEU SEQRES 27 A 425 ILE PRO LEU LEU GLY VAL HIS GLU VAL VAL PHE ALA PHE SEQRES 28 A 425 VAL THR ASP GLU HIS ALA GLN GLY THR LEU ARG SER ALA SEQRES 29 A 425 LYS LEU PHE PHE ASP LEU PHE LEU SER SER PHE GLN GLY SEQRES 30 A 425 LEU LEU VAL ALA VAL LEU TYR CYS PHE LEU ASN LYS GLU SEQRES 31 A 425 VAL GLN SER GLU LEU ARG ARG ARG TRP HIS ARG TRP ARG SEQRES 32 A 425 LEU GLY LYS VAL LEU TRP GLU GLU ARG ASN THR SER ASN SEQRES 33 A 425 GLY ARG PRO LEU GLU VAL LEU PHE GLN HET PEG A1200 7 HETNAM PEG DI(HYDROXYETHYL)ETHER FORMUL 2 PEG C4 H10 O3 HELIX 1 1 ASP A 1002 ALA A 1020 1 19 HELIX 2 2 ASN A 1022 GLN A 1041 1 20 HELIX 3 3 PRO A 1045 GLU A 1049 5 5 HELIX 4 4 SER A 1055 GLU A 1081 1 27 HELIX 5 5 LYS A 1083 GLU A 1092 1 10 HELIX 6 6 GLN A 1093 ILE A 1102 1 10 HELIX 7 7 GLN A 1103 LEU A 1106 5 4 HELIX 8 8 GLU A 126 GLY A 164 1 39 HELIX 9 9 THR A 172 HIS A 177 1 6 HELIX 10 10 ASN A 179 LEU A 198 1 20 HELIX 11 11 SER A 217 ALA A 222 1 6 HELIX 12 12 VAL A 226 TYR A 248 1 23 HELIX 13 13 SER A 262 TYR A 267 5 6 HELIX 14 14 ILE A 270 TRP A 272 5 3 HELIX 15 15 GLY A 273 PHE A 278 1 6 HELIX 16 16 VAL A 280 GLU A 290 1 11 HELIX 17 17 ASN A 300 LEU A 307 1 8 HELIX 18 18 LEU A 307 VAL A 330 1 24 HELIX 19 19 VAL A 330 ALA A 335 1 6 HELIX 20 20 ASP A 342 LEU A 352 1 11 HELIX 21 21 PRO A 356 GLU A 362 1 7 HELIX 22 22 GLN A 374 PHE A 391 1 18 HELIX 23 23 PHE A 391 CYS A 401 1 11 HELIX 24 24 ASN A 404 ASN A 429 1 26 SSBOND 1 CYS A 224 CYS A 294 1555 1555 2.04 SITE 1 AC1 4 ARG A 346 SER A 350 LEU A 399 LEU A 403 CRYST1 56.615 66.651 163.331 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017663 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015004 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006123 0.00000 ATOM 1 N ALA A1001 13.645 14.436 -11.317 1.00109.57 N ANISOU 1 N ALA A1001 16791 15721 9120 -3009 -1596 4616 N ATOM 2 CA ALA A1001 12.442 15.173 -10.944 1.00112.26 C ANISOU 2 CA ALA A1001 17470 15475 9710 -2347 -1863 4642 C ATOM 3 C ALA A1001 11.253 14.220 -10.760 1.00112.77 C ANISOU 3 C ALA A1001 17195 16177 9476 -1818 -1683 4100 C ATOM 4 O ALA A1001 10.802 14.044 -9.624 1.00110.88 O ANISOU 4 O ALA A1001 17057 15643 9429 -1466 -1658 3512 O ATOM 5 CB ALA A1001 12.122 16.223 -11.992 1.00121.36 C ANISOU 5 CB ALA A1001 18805 16456 10850 -2320 -2162 5565 C ATOM 6 N ASP A1002 10.761 13.586 -11.872 1.00108.91 N ANISOU 6 N ASP A1002 16270 16656 8455 -1849 -1556 4283 N ATOM 7 CA ASP A1002 9.644 12.611 -11.897 1.00105.21 C ANISOU 7 CA ASP A1002 15404 16919 7652 -1531 -1404 3818 C ATOM 8 C ASP A1002 9.969 11.431 -10.986 1.00100.38 C ANISOU 8 C ASP A1002 14688 16356 7097 -1711 -1137 3087 C ATOM 9 O ASP A1002 11.114 11.002 -11.004 1.00 98.40 O ANISOU 9 O ASP A1002 14424 16074 6890 -2140 -1005 3000 O ATOM 10 CB ASP A1002 9.390 12.128 -13.349 1.00109.52 C ANISOU 10 CB ASP A1002 15518 18523 7573 -1749 -1339 4103 C ATOM 11 CG ASP A1002 8.988 13.182 -14.366 1.00132.37 C ANISOU 11 CG ASP A1002 18456 21566 10272 -1601 -1654 4978 C ATOM 12 OD1 ASP A1002 8.992 12.866 -15.581 1.00137.42 O ANISOU 12 OD1 ASP A1002 18757 23165 10289 -1899 -1609 5278 O ATOM 13 OD2 ASP A1002 8.692 14.328 -13.955 1.00143.84 O ANISOU 13 OD2 ASP A1002 20297 22167 12187 -1185 -1973 5364 O ATOM 14 N LEU A1003 9.024 10.934 -10.161 1.00 92.07 N ANISOU 14 N LEU A1003 13540 15391 6052 -1401 -1075 2621 N ATOM 15 CA LEU A1003 9.284 9.853 -9.180 1.00 85.70 C ANISOU 15 CA LEU A1003 12707 14541 5312 -1606 -889 2081 C ATOM 16 C LEU A1003 9.676 8.507 -9.850 1.00 85.52 C ANISOU 16 C LEU A1003 12386 15033 5076 -2017 -699 1854 C ATOM 17 O LEU A1003 10.581 7.818 -9.372 1.00 82.39 O ANISOU 17 O LEU A1003 12053 14382 4867 -2260 -623 1621 O ATOM 18 CB LEU A1003 8.013 9.648 -8.329 1.00 85.58 C ANISOU 18 CB LEU A1003 12568 14731 5217 -1270 -850 1760 C ATOM 19 CG LEU A1003 8.021 8.613 -7.197 1.00 86.58 C ANISOU 19 CG LEU A1003 12689 14867 5341 -1501 -701 1354 C ATOM 20 CD1 LEU A1003 9.031 8.958 -6.135 1.00 85.63 C ANISOU 20 CD1 LEU A1003 12953 14095 5487 -1574 -769 1279 C ATOM 21 CD2 LEU A1003 6.648 8.487 -6.586 1.00 91.14 C ANISOU 21 CD2 LEU A1003 13007 15923 5698 -1255 -620 1135 C ATOM 22 N GLU A1004 8.997 8.145 -10.938 1.00 83.10 N ANISOU 22 N GLU A1004 11747 15435 4392 -2053 -663 1875 N ATOM 23 CA GLU A1004 9.257 6.896 -11.634 1.00 81.91 C ANISOU 23 CA GLU A1004 11331 15754 4037 -2401 -503 1502 C ATOM 24 C GLU A1004 10.668 6.866 -12.181 1.00 85.20 C ANISOU 24 C GLU A1004 11747 16137 4489 -2638 -407 1538 C ATOM 25 O GLU A1004 11.259 5.794 -12.246 1.00 84.65 O ANISOU 25 O GLU A1004 11559 16099 4504 -2815 -272 1075 O ATOM 26 CB GLU A1004 8.252 6.657 -12.774 1.00 86.88 C ANISOU 26 CB GLU A1004 11584 17268 4159 -2434 -525 1481 C ATOM 27 CG GLU A1004 8.161 7.705 -13.878 1.00 98.55 C ANISOU 27 CG GLU A1004 12962 19218 5265 -2322 -662 2070 C ATOM 28 CD GLU A1004 7.415 8.997 -13.606 1.00112.59 C ANISOU 28 CD GLU A1004 14874 20750 7157 -1841 -918 2627 C ATOM 29 OE1 GLU A1004 6.978 9.222 -12.454 1.00106.18 O ANISOU 29 OE1 GLU A1004 14225 19412 6707 -1532 -949 2475 O ATOM 30 OE2 GLU A1004 7.239 9.776 -14.568 1.00103.67 O ANISOU 30 OE2 GLU A1004 13668 19996 5727 -1746 -1105 3211 O ATOM 31 N ASP A1005 11.199 8.034 -12.592 1.00 82.53 N ANISOU 31 N ASP A1005 11511 15741 4106 -2647 -488 2092 N ATOM 32 CA ASP A1005 12.550 8.161 -13.123 1.00 83.57 C ANISOU 32 CA ASP A1005 11544 16005 4204 -2957 -374 2221 C ATOM 33 C ASP A1005 13.555 7.881 -12.049 1.00 83.99 C ANISOU 33 C ASP A1005 11737 15427 4749 -3008 -359 1975 C ATOM 34 O ASP A1005 14.450 7.080 -12.279 1.00 83.74 O ANISOU 34 O ASP A1005 11444 15630 4746 -3145 -196 1618 O ATOM 35 CB ASP A1005 12.785 9.545 -13.722 1.00 90.33 C ANISOU 35 CB ASP A1005 12523 16876 4922 -3077 -518 3019 C ATOM 36 CG ASP A1005 12.121 9.775 -15.076 1.00108.70 C ANISOU 36 CG ASP A1005 14606 20080 6613 -3126 -548 3405 C ATOM 37 OD1 ASP A1005 11.803 8.771 -15.766 1.00110.16 O ANISOU 37 OD1 ASP A1005 14427 21068 6362 -3192 -378 2922 O ATOM 38 OD2 ASP A1005 12.022 10.950 -15.495 1.00119.21 O ANISOU 38 OD2 ASP A1005 16118 21306 7871 -3151 -769 4204 O ATOM 39 N ASN A1006 13.401 8.509 -10.860 1.00 78.51 N ANISOU 39 N ASN A1006 11418 13989 4423 -2851 -545 2103 N ATOM 40 CA ASN A1006 14.264 8.269 -9.696 1.00 74.70 C ANISOU 40 CA ASN A1006 11075 12969 4338 -2904 -604 1891 C ATOM 41 C ASN A1006 14.084 6.851 -9.195 1.00 74.37 C ANISOU 41 C ASN A1006 10931 12940 4386 -2818 -532 1391 C ATOM 42 O ASN A1006 15.033 6.230 -8.729 1.00 72.51 O ANISOU 42 O ASN A1006 10618 12525 4405 -2875 -550 1197 O ATOM 43 CB ASN A1006 13.961 9.255 -8.590 1.00 71.42 C ANISOU 43 CB ASN A1006 11083 11893 4161 -2757 -823 2035 C ATOM 44 CG ASN A1006 14.158 10.707 -8.951 1.00 90.60 C ANISOU 44 CG ASN A1006 13746 14004 6674 -2845 -988 2535 C ATOM 45 OD1 ASN A1006 15.084 11.097 -9.672 1.00 91.08 O ANISOU 45 OD1 ASN A1006 13685 14212 6710 -3220 -972 2879 O ATOM 46 ND2 ASN A1006 13.213 11.533 -8.527 1.00 77.73 N ANISOU 46 ND2 ASN A1006 12433 11963 5139 -2493 -1153 2604 N ATOM 47 N TRP A1007 12.871 6.328 -9.318 1.00 71.52 N ANISOU 47 N TRP A1007 10546 12790 3840 -2703 -487 1225 N ATOM 48 CA TRP A1007 12.578 4.972 -8.909 1.00 71.28 C ANISOU 48 CA TRP A1007 10473 12689 3922 -2738 -457 832 C ATOM 49 C TRP A1007 13.318 3.970 -9.815 1.00 77.72 C ANISOU 49 C TRP A1007 11006 13742 4781 -2826 -334 450 C ATOM 50 O TRP A1007 13.744 2.911 -9.340 1.00 78.38 O ANISOU 50 O TRP A1007 11115 13465 5200 -2810 -385 155 O ATOM 51 CB TRP A1007 11.072 4.743 -8.948 1.00 71.00 C ANISOU 51 CB TRP A1007 10397 12942 3637 -2716 -436 770 C ATOM 52 CG TRP A1007 10.654 3.466 -8.288 1.00 72.39 C ANISOU 52 CG TRP A1007 10617 12926 3963 -2888 -453 505 C ATOM 53 CD1 TRP A1007 10.467 2.255 -8.888 1.00 77.63 C ANISOU 53 CD1 TRP A1007 11147 13678 4669 -3095 -416 131 C ATOM 54 CD2 TRP A1007 10.380 3.264 -6.898 1.00 71.57 C ANISOU 54 CD2 TRP A1007 10731 12488 3974 -2936 -539 620 C ATOM 55 NE1 TRP A1007 10.086 1.316 -7.962 1.00 77.98 N ANISOU 55 NE1 TRP A1007 11356 13343 4930 -3306 -505 97 N ATOM 56 CE2 TRP A1007 10.020 1.907 -6.731 1.00 77.83 C ANISOU 56 CE2 TRP A1007 11527 13148 4898 -3230 -566 443 C ATOM 57 CE3 TRP A1007 10.387 4.102 -5.772 1.00 72.12 C ANISOU 57 CE3 TRP A1007 11002 12391 4009 -2796 -605 833 C ATOM 58 CZ2 TRP A1007 9.709 1.358 -5.483 1.00 78.31 C ANISOU 58 CZ2 TRP A1007 11775 12959 5020 -3439 -657 627 C ATOM 59 CZ3 TRP A1007 10.078 3.552 -4.532 1.00 74.15 C ANISOU 59 CZ3 TRP A1007 11399 12533 4242 -2959 -660 896 C ATOM 60 CH2 TRP A1007 9.748 2.196 -4.398 1.00 76.62 C ANISOU 60 CH2 TRP A1007 11699 12766 4648 -3302 -685 870 C ATOM 61 N GLU A1008 13.488 4.319 -11.108 1.00 75.36 N ANISOU 61 N GLU A1008 10437 14066 4132 -2891 -190 454 N ATOM 62 CA GLU A1008 14.199 3.481 -12.048 1.00 78.21 C ANISOU 62 CA GLU A1008 10459 14835 4423 -2931 -19 -33 C ATOM 63 C GLU A1008 15.685 3.547 -11.771 1.00 83.23 C ANISOU 63 C GLU A1008 10944 15319 5361 -2880 7 -39 C ATOM 64 O GLU A1008 16.357 2.525 -11.840 1.00 85.49 O ANISOU 64 O GLU A1008 11031 15534 5919 -2727 57 -563 O ATOM 65 CB GLU A1008 13.889 3.906 -13.458 1.00 83.46 C ANISOU 65 CB GLU A1008 10841 16410 4459 -3070 132 22 C ATOM 66 CG GLU A1008 14.324 2.880 -14.475 1.00 99.93 C ANISOU 66 CG GLU A1008 12554 19074 6341 -3096 341 -709 C ATOM 67 CD GLU A1008 13.704 3.071 -15.836 1.00127.66 C ANISOU 67 CD GLU A1008 15795 23626 9085 -3284 453 -758 C ATOM 68 OE1 GLU A1008 13.487 4.233 -16.255 1.00120.21 O ANISOU 68 OE1 GLU A1008 14840 23113 7721 -3406 413 -34 O ATOM 69 OE2 GLU A1008 13.420 2.041 -16.485 1.00134.40 O ANISOU 69 OE2 GLU A1008 16467 24839 9759 -3319 538 -1525 O ATOM 70 N THR A1009 16.197 4.741 -11.413 1.00 79.25 N ANISOU 70 N THR A1009 10525 14719 4867 -2995 -65 516 N ATOM 71 CA THR A1009 17.598 4.952 -11.040 1.00 80.41 C ANISOU 71 CA THR A1009 10475 14790 5287 -3047 -88 586 C ATOM 72 C THR A1009 17.952 4.047 -9.887 1.00 82.19 C ANISOU 72 C THR A1009 10811 14386 6031 -2806 -281 319 C ATOM 73 O THR A1009 19.000 3.410 -9.912 1.00 84.96 O ANISOU 73 O THR A1009 10810 14830 6642 -2651 -263 16 O ATOM 74 CB THR A1009 17.857 6.429 -10.678 1.00 88.83 C ANISOU 74 CB THR A1009 11752 15662 6338 -3316 -225 1234 C ATOM 75 OG1 THR A1009 17.448 7.266 -11.759 1.00 89.42 O ANISOU 75 OG1 THR A1009 11791 16222 5962 -3534 -119 1635 O ATOM 76 CG2 THR A1009 19.336 6.710 -10.317 1.00 92.11 C ANISOU 76 CG2 THR A1009 11885 16114 7000 -3511 -275 1322 C ATOM 77 N LEU A1010 17.073 3.980 -8.879 1.00 75.11 N ANISOU 77 N LEU A1010 10357 12924 5256 -2756 -475 456 N ATOM 78 CA LEU A1010 17.306 3.155 -7.707 1.00 74.60 C ANISOU 78 CA LEU A1010 10457 12295 5592 -2607 -710 377 C ATOM 79 C LEU A1010 17.379 1.677 -8.089 1.00 81.81 C ANISOU 79 C LEU A1010 11225 13077 6783 -2393 -688 -117 C ATOM 80 O LEU A1010 18.297 0.988 -7.648 1.00 84.43 O ANISOU 80 O LEU A1010 11425 13117 7538 -2161 -855 -245 O ATOM 81 CB LEU A1010 16.219 3.380 -6.652 1.00 71.53 C ANISOU 81 CB LEU A1010 10516 11553 5111 -2676 -854 628 C ATOM 82 CG LEU A1010 16.199 4.761 -6.010 1.00 74.48 C ANISOU 82 CG LEU A1010 11107 11857 5333 -2780 -947 962 C ATOM 83 CD1 LEU A1010 15.056 4.880 -5.069 1.00 72.92 C ANISOU 83 CD1 LEU A1010 11240 11499 4966 -2765 -1011 1040 C ATOM 84 CD2 LEU A1010 17.488 5.043 -5.275 1.00 77.22 C ANISOU 84 CD2 LEU A1010 11390 12041 5909 -2840 -1161 1067 C ATOM 85 N ASN A1011 16.458 1.201 -8.937 1.00 79.35 N ANISOU 85 N ASN A1011 10919 12966 6266 -2451 -523 -428 N ATOM 86 CA ASN A1011 16.453 -0.201 -9.354 1.00 83.97 C ANISOU 86 CA ASN A1011 11438 13304 7161 -2292 -531 -1018 C ATOM 87 C ASN A1011 17.673 -0.570 -10.185 1.00 95.33 C ANISOU 87 C ASN A1011 12390 15086 8747 -1989 -383 -1546 C ATOM 88 O ASN A1011 18.310 -1.576 -9.874 1.00 99.52 O ANISOU 88 O ASN A1011 12873 15097 9842 -1643 -551 -1883 O ATOM 89 CB ASN A1011 15.216 -0.547 -10.145 1.00 85.11 C ANISOU 89 CB ASN A1011 11645 13706 6986 -2514 -403 -1313 C ATOM 90 CG ASN A1011 14.014 -0.968 -9.351 1.00100.41 C ANISOU 90 CG ASN A1011 13964 15197 8991 -2770 -573 -1088 C ATOM 91 OD1 ASN A1011 13.713 -0.469 -8.268 1.00 79.30 O ANISOU 91 OD1 ASN A1011 11523 12313 6293 -2856 -695 -554 O ATOM 92 ND2 ASN A1011 13.157 -1.680 -10.025 1.00102.71 N ANISOU 92 ND2 ASN A1011 14247 15594 9183 -2980 -528 -1505 N ATOM 93 N ASP A1012 18.002 0.214 -11.230 1.00 94.13 N ANISOU 93 N ASP A1012 11846 15831 8087 -2098 -83 -1600 N ATOM 94 CA ASP A1012 19.148 -0.101 -12.078 1.00101.00 C ANISOU 94 CA ASP A1012 12124 17297 8955 -1848 141 -2150 C ATOM 95 C ASP A1012 20.441 -0.074 -11.285 1.00106.56 C ANISOU 95 C ASP A1012 12573 17781 10134 -1581 -22 -1994 C ATOM 96 O ASP A1012 21.291 -0.933 -11.494 1.00113.08 O ANISOU 96 O ASP A1012 13004 18624 11338 -1121 -6 -2592 O ATOM 97 CB ASP A1012 19.251 0.862 -13.264 1.00105.40 C ANISOU 97 CB ASP A1012 12299 19000 8747 -2164 489 -2025 C ATOM 98 CG ASP A1012 18.140 0.727 -14.303 1.00123.47 C ANISOU 98 CG ASP A1012 14654 21800 10460 -2368 648 -2297 C ATOM 99 OD1 ASP A1012 17.547 -0.380 -14.411 1.00127.02 O ANISOU 99 OD1 ASP A1012 15266 21871 11125 -2220 581 -2942 O ATOM 100 OD2 ASP A1012 17.911 1.703 -15.056 1.00129.98 O ANISOU 100 OD2 ASP A1012 15345 23427 10615 -2703 808 -1865 O ATOM 101 N ASN A1013 20.589 0.870 -10.354 1.00 97.99 N ANISOU 101 N ASN A1013 11688 16487 9056 -1823 -214 -1264 N ATOM 102 CA ASN A1013 21.835 0.957 -9.601 1.00 99.59 C ANISOU 102 CA ASN A1013 11583 16620 9636 -1649 -416 -1103 C ATOM 103 C ASN A1013 21.923 -0.161 -8.562 1.00105.08 C ANISOU 103 C ASN A1013 12526 16414 10987 -1219 -816 -1187 C ATOM 104 O ASN A1013 23.035 -0.556 -8.220 1.00109.04 O ANISOU 104 O ASN A1013 12613 16919 11899 -840 -994 -1304 O ATOM 105 CB ASN A1013 22.002 2.309 -8.956 1.00 94.54 C ANISOU 105 CB ASN A1013 11092 16042 8788 -2104 -535 -399 C ATOM 106 CG ASN A1013 22.373 3.380 -9.957 1.00111.39 C ANISOU 106 CG ASN A1013 12860 19038 10426 -2529 -220 -208 C ATOM 107 OD1 ASN A1013 21.823 4.468 -9.922 1.00102.51 O ANISOU 107 OD1 ASN A1013 12090 17844 9014 -2945 -236 301 O ATOM 108 ND2 ASN A1013 23.179 3.047 -10.966 1.00105.33 N ANISOU 108 ND2 ASN A1013 11394 19116 9510 -2421 90 -631 N ATOM 109 N LEU A1014 20.785 -0.731 -8.128 1.00100.33 N ANISOU 109 N LEU A1014 12528 15106 10486 -1276 -970 -1113 N ATOM 110 CA LEU A1014 20.836 -1.915 -7.270 1.00104.26 C ANISOU 110 CA LEU A1014 13294 14708 11611 -936 -1368 -1117 C ATOM 111 C LEU A1014 21.465 -3.038 -8.039 1.00116.81 C ANISOU 111 C LEU A1014 14515 16178 13687 -363 -1326 -1900 C ATOM 112 O LEU A1014 22.282 -3.787 -7.504 1.00122.21 O ANISOU 112 O LEU A1014 15058 16377 14998 155 -1663 -1952 O ATOM 113 CB LEU A1014 19.450 -2.319 -6.755 1.00101.64 C ANISOU 113 CB LEU A1014 13628 13759 11232 -1257 -1495 -857 C ATOM 114 CG LEU A1014 18.888 -1.554 -5.567 1.00101.47 C ANISOU 114 CG LEU A1014 13999 13663 10893 -1646 -1661 -125 C ATOM 115 CD1 LEU A1014 17.433 -1.904 -5.344 1.00 99.66 C ANISOU 115 CD1 LEU A1014 14236 13150 10481 -2008 -1643 16 C ATOM 116 CD2 LEU A1014 19.699 -1.823 -4.310 1.00106.82 C ANISOU 116 CD2 LEU A1014 14727 13956 11901 -1463 -2111 316 C ATOM 117 N LYS A1015 21.120 -3.111 -9.334 1.00115.26 N ANISOU 117 N LYS A1015 14117 16508 13169 -412 -922 -2550 N ATOM 118 CA LYS A1015 21.644 -4.112 -10.253 1.00123.89 C ANISOU 118 CA LYS A1015 14822 17650 14603 137 -789 -3537 C ATOM 119 C LYS A1015 23.132 -3.911 -10.444 1.00132.38 C ANISOU 119 C LYS A1015 15086 19415 15798 609 -689 -3773 C ATOM 120 O LYS A1015 23.879 -4.881 -10.427 1.00139.56 O ANISOU 120 O LYS A1015 15709 19942 17374 1332 -861 -4338 O ATOM 121 CB LYS A1015 20.913 -4.062 -11.609 1.00127.73 C ANISOU 121 CB LYS A1015 15223 18825 14483 -138 -356 -4171 C ATOM 122 CG LYS A1015 19.381 -4.232 -11.540 1.00144.41 C ANISOU 122 CG LYS A1015 17997 20465 16405 -657 -440 -3989 C ATOM 123 CD LYS A1015 18.929 -5.536 -10.864 1.00162.39 C ANISOU 123 CD LYS A1015 20829 21395 19479 -516 -860 -4129 C ATOM 124 CE LYS A1015 17.432 -5.584 -10.697 1.00171.48 C ANISOU 124 CE LYS A1015 22517 22270 20368 -1167 -925 -3823 C ATOM 125 NZ LYS A1015 16.993 -6.818 -9.999 1.00185.35 N ANISOU 125 NZ LYS A1015 24827 22718 22878 -1207 -1349 -3804 N ATOM 126 N VAL A1016 23.565 -2.650 -10.587 1.00125.86 N ANISOU 126 N VAL A1016 13875 19566 14378 198 -449 -3315 N ATOM 127 CA VAL A1016 24.979 -2.297 -10.729 1.00131.28 C ANISOU 127 CA VAL A1016 13695 21105 15080 448 -335 -3414 C ATOM 128 C VAL A1016 25.747 -2.827 -9.529 1.00138.00 C ANISOU 128 C VAL A1016 14490 21250 16694 964 -871 -3156 C ATOM 129 O VAL A1016 26.786 -3.468 -9.695 1.00146.43 O ANISOU 129 O VAL A1016 14879 22543 18215 1672 -915 -3697 O ATOM 130 CB VAL A1016 25.179 -0.768 -10.889 1.00131.13 C ANISOU 130 CB VAL A1016 13458 22015 14352 -305 -99 -2740 C ATOM 131 CG1 VAL A1016 26.664 -0.397 -10.882 1.00137.14 C ANISOU 131 CG1 VAL A1016 13286 23663 15158 -198 -38 -2737 C ATOM 132 CG2 VAL A1016 24.503 -0.256 -12.156 1.00129.96 C ANISOU 132 CG2 VAL A1016 13300 22660 13421 -766 382 -2894 C ATOM 133 N ILE A1017 25.223 -2.566 -8.322 1.00127.69 N ANISOU 133 N ILE A1017 13854 19173 15488 646 -1289 -2342 N ATOM 134 CA ILE A1017 25.833 -2.997 -7.066 1.00129.65 C ANISOU 134 CA ILE A1017 14139 18804 16317 1018 -1876 -1908 C ATOM 135 C ILE A1017 25.906 -4.519 -7.003 1.00141.51 C ANISOU 135 C ILE A1017 15764 19348 18655 1832 -2192 -2375 C ATOM 136 O ILE A1017 26.965 -5.066 -6.690 1.00149.67 O ANISOU 136 O ILE A1017 16279 20322 20268 2544 -2509 -2507 O ATOM 137 CB ILE A1017 25.044 -2.441 -5.873 1.00124.72 C ANISOU 137 CB ILE A1017 14276 17660 15451 432 -2191 -1025 C ATOM 138 CG1 ILE A1017 25.160 -0.902 -5.831 1.00119.24 C ANISOU 138 CG1 ILE A1017 13452 17756 14098 -265 -1982 -623 C ATOM 139 CG2 ILE A1017 25.559 -3.067 -4.573 1.00129.55 C ANISOU 139 CG2 ILE A1017 14995 17640 16587 805 -2851 -539 C ATOM 140 CD1 ILE A1017 24.182 -0.226 -4.941 1.00117.05 C ANISOU 140 CD1 ILE A1017 13919 17094 13462 -826 -2131 -19 C ATOM 141 N GLU A1018 24.787 -5.193 -7.294 1.00136.41 N ANISOU 141 N GLU A1018 15789 17928 18112 1723 -2150 -2615 N ATOM 142 CA GLU A1018 24.697 -6.650 -7.286 1.00144.58 C ANISOU 142 CA GLU A1018 17112 17814 20007 2367 -2483 -3069 C ATOM 143 C GLU A1018 25.755 -7.294 -8.187 1.00158.77 C ANISOU 143 C GLU A1018 18110 19942 22275 3295 -2326 -4145 C ATOM 144 O GLU A1018 26.344 -8.307 -7.805 1.00167.93 O ANISOU 144 O GLU A1018 19213 20249 24343 4130 -2791 -4333 O ATOM 145 CB GLU A1018 23.303 -7.101 -7.744 1.00143.60 C ANISOU 145 CB GLU A1018 17709 17084 19767 1899 -2336 -3322 C ATOM 146 CG GLU A1018 22.173 -6.806 -6.764 1.00148.02 C ANISOU 146 CG GLU A1018 19053 17156 20033 1125 -2554 -2348 C ATOM 147 CD GLU A1018 20.768 -7.152 -7.228 1.00168.06 C ANISOU 147 CD GLU A1018 22157 19326 22371 563 -2386 -2562 C ATOM 148 OE1 GLU A1018 19.813 -6.799 -6.500 1.00156.50 O ANISOU 148 OE1 GLU A1018 21185 17733 20545 -90 -2469 -1820 O ATOM 149 OE2 GLU A1018 20.616 -7.725 -8.333 1.00167.25 O ANISOU 149 OE2 GLU A1018 21939 19210 22399 751 -2152 -3522 O ATOM 150 N LYS A1019 26.007 -6.705 -9.369 1.00154.64 N ANISOU 150 N LYS A1019 16941 20696 21119 3179 -1687 -4829 N ATOM 151 CA LYS A1019 26.950 -7.280 -10.323 1.00165.42 C ANISOU 151 CA LYS A1019 17450 22641 22761 4029 -1419 -5997 C ATOM 152 C LYS A1019 28.371 -6.634 -10.234 1.00172.78 C ANISOU 152 C LYS A1019 17271 24822 23557 4330 -1315 -5886 C ATOM 153 O LYS A1019 29.274 -7.062 -10.966 1.00182.47 O ANISOU 153 O LYS A1019 17598 26755 24975 5094 -1063 -6857 O ATOM 154 CB LYS A1019 26.415 -7.147 -11.760 1.00168.09 C ANISOU 154 CB LYS A1019 17638 23842 22385 3718 -755 -6912 C ATOM 155 CG LYS A1019 26.194 -5.738 -12.299 1.00173.56 C ANISOU 155 CG LYS A1019 18077 25956 21913 2785 -234 -6436 C ATOM 156 CD LYS A1019 25.645 -5.787 -13.734 1.00184.05 C ANISOU 156 CD LYS A1019 19269 28129 22533 2553 331 -7338 C ATOM 157 CE LYS A1019 25.339 -4.428 -14.325 1.00183.20 C ANISOU 157 CE LYS A1019 18990 29332 21284 1626 776 -6743 C ATOM 158 NZ LYS A1019 24.233 -3.736 -13.612 1.00175.82 N ANISOU 158 NZ LYS A1019 18927 27723 20154 877 524 -5659 N ATOM 159 N ALA A1020 28.581 -5.670 -9.315 1.00162.30 N ANISOU 159 N ALA A1020 15963 23769 21932 3755 -1532 -4791 N ATOM 160 CA ALA A1020 29.879 -4.998 -9.171 1.00165.70 C ANISOU 160 CA ALA A1020 15351 25398 22210 3843 -1486 -4612 C ATOM 161 C ALA A1020 30.983 -5.972 -8.749 1.00181.08 C ANISOU 161 C ALA A1020 16642 27064 25094 5040 -1941 -4979 C ATOM 162 O ALA A1020 30.723 -6.963 -8.062 1.00184.19 O ANISOU 162 O ALA A1020 17640 26040 26305 5632 -2528 -4852 O ATOM 163 CB ALA A1020 29.785 -3.870 -8.158 1.00157.50 C ANISOU 163 CB ALA A1020 14627 24453 20764 2970 -1746 -3438 C ATOM 164 N ASP A1021 32.219 -5.675 -9.172 1.00184.91 N ANISOU 164 N ASP A1021 15850 28948 25459 5378 -1685 -5384 N ATOM 165 CA ASP A1021 33.392 -6.483 -8.852 1.00197.40 C ANISOU 165 CA ASP A1021 16551 30566 27886 6603 -2084 -5784 C ATOM 166 C ASP A1021 34.349 -5.712 -7.948 1.00200.14 C ANISOU 166 C ASP A1021 16207 31726 28113 6323 -2447 -4926 C ATOM 167 O ASP A1021 35.269 -6.308 -7.386 1.00206.46 O ANISOU 167 O ASP A1021 16631 32122 29694 6968 -2763 -4447 O ATOM 168 CB ASP A1021 34.102 -6.911 -10.141 1.00203.38 C ANISOU 168 CB ASP A1021 16927 31600 28749 6728 -1026 -5922 C ATOM 169 CG ASP A1021 33.220 -7.725 -11.064 1.00209.73 C ANISOU 169 CG ASP A1021 18884 31212 29593 6610 -360 -6020 C ATOM 170 OD1 ASP A1021 32.707 -8.778 -10.621 1.00211.96 O ANISOU 170 OD1 ASP A1021 20009 30005 30520 7100 -672 -5952 O ATOM 171 OD2 ASP A1021 33.077 -7.336 -12.238 1.00212.49 O ANISOU 171 OD2 ASP A1021 19361 32073 29302 5994 479 -6042 O ATOM 172 N ASN A1022 34.132 -4.393 -7.795 1.00185.87 N ANISOU 172 N ASN A1022 14549 30631 25441 5029 -2224 -4178 N ATOM 173 CA ASN A1022 35.001 -3.568 -6.959 1.00185.89 C ANISOU 173 CA ASN A1022 13942 31423 25265 4570 -2571 -3427 C ATOM 174 C ASN A1022 34.206 -2.491 -6.205 1.00175.26 C ANISOU 174 C ASN A1022 13597 29654 23339 3300 -2732 -2419 C ATOM 175 O ASN A1022 33.084 -2.146 -6.583 1.00165.60 O ANISOU 175 O ASN A1022 13286 27942 21692 2676 -2391 -2337 O ATOM 176 CB ASN A1022 36.089 -2.914 -7.805 1.00194.85 C ANISOU 176 CB ASN A1022 13627 34481 25925 4330 -2010 -3854 C ATOM 177 CG ASN A1022 35.556 -2.043 -8.905 1.00211.18 C ANISOU 177 CG ASN A1022 16399 36331 27507 3055 -1119 -3426 C ATOM 178 OD1 ASN A1022 34.968 -0.985 -8.662 1.00202.77 O ANISOU 178 OD1 ASN A1022 15464 36113 25466 2143 -1172 -3210 O ATOM 179 ND2 ASN A1022 35.797 -2.448 -10.143 1.00207.04 N ANISOU 179 ND2 ASN A1022 15576 36029 27061 3332 -406 -3949 N ATOM 180 N ALA A1023 34.829 -1.937 -5.158 1.00171.31 N ANISOU 180 N ALA A1023 12839 29449 22803 2948 -3259 -1727 N ATOM 181 CA ALA A1023 34.232 -0.936 -4.279 1.00161.07 C ANISOU 181 CA ALA A1023 12400 27783 21015 1864 -3507 -889 C ATOM 182 C ALA A1023 33.888 0.362 -5.020 1.00157.64 C ANISOU 182 C ALA A1023 12084 27992 19822 692 -2886 -817 C ATOM 183 O ALA A1023 32.872 0.981 -4.695 1.00147.81 O ANISOU 183 O ALA A1023 11884 26051 18225 -4 -2882 -396 O ATOM 184 CB ALA A1023 35.176 -0.624 -3.132 1.00166.90 C ANISOU 184 CB ALA A1023 12608 28978 21830 1752 -4188 -356 C ATOM 185 N ALA A1024 34.712 0.775 -6.005 1.00159.56 N ANISOU 185 N ALA A1024 11248 29573 19804 479 -2378 -1189 N ATOM 186 CA ALA A1024 34.478 2.013 -6.761 1.00154.95 C ANISOU 186 CA ALA A1024 10733 29629 18513 -683 -1837 -979 C ATOM 187 C ALA A1024 33.152 1.957 -7.510 1.00148.47 C ANISOU 187 C ALA A1024 10884 28119 17408 -791 -1400 -1117 C ATOM 188 O ALA A1024 32.415 2.945 -7.515 1.00140.36 O ANISOU 188 O ALA A1024 10607 26773 15951 -1679 -1301 -627 O ATOM 189 CB ALA A1024 35.616 2.261 -7.737 1.00165.96 C ANISOU 189 CB ALA A1024 10702 32705 19649 -836 -1346 -1341 C ATOM 190 N GLN A1025 32.839 0.798 -8.117 1.00146.04 N ANISOU 190 N GLN A1025 10566 27541 17381 138 -1191 -1814 N ATOM 191 CA GLN A1025 31.584 0.590 -8.841 1.00138.88 C ANISOU 191 CA GLN A1025 10499 26050 16221 89 -829 -2043 C ATOM 192 C GLN A1025 30.401 0.687 -7.880 1.00131.32 C ANISOU 192 C GLN A1025 10836 23703 15359 -155 -1237 -1477 C ATOM 193 O GLN A1025 29.390 1.326 -8.198 1.00123.34 O ANISOU 193 O GLN A1025 10535 22433 13896 -764 -1008 -1217 O ATOM 194 CB GLN A1025 31.594 -0.773 -9.553 1.00146.27 C ANISOU 194 CB GLN A1025 11135 26894 17545 1163 -632 -3027 C ATOM 195 CG GLN A1025 32.683 -0.905 -10.607 1.00157.86 C ANISOU 195 CG GLN A1025 11256 29914 18811 1483 -119 -3770 C ATOM 196 CD GLN A1025 32.722 -2.273 -11.246 1.00171.89 C ANISOU 196 CD GLN A1025 12754 31510 21045 2657 33 -4920 C ATOM 197 OE1 GLN A1025 32.744 -3.313 -10.577 1.00168.55 O ANISOU 197 OE1 GLN A1025 12592 29963 21485 3588 -478 -5151 O ATOM 198 NE2 GLN A1025 32.835 -2.294 -12.561 1.00164.71 N ANISOU 198 NE2 GLN A1025 11237 31781 19566 2647 719 -5685 N ATOM 199 N VAL A1026 30.543 0.069 -6.697 1.00127.35 N ANISOU 199 N VAL A1026 10574 22411 15402 326 -1855 -1252 N ATOM 200 CA VAL A1026 29.517 0.094 -5.668 1.00119.00 C ANISOU 200 CA VAL A1026 10620 20226 14369 95 -2249 -706 C ATOM 201 C VAL A1026 29.309 1.534 -5.199 1.00117.91 C ANISOU 201 C VAL A1026 10824 20278 13699 -903 -2276 -108 C ATOM 202 O VAL A1026 28.166 1.986 -5.089 1.00109.60 O ANISOU 202 O VAL A1026 10625 18672 12345 -1324 -2186 132 O ATOM 203 CB VAL A1026 29.867 -0.836 -4.488 1.00126.41 C ANISOU 203 CB VAL A1026 11639 20482 15909 751 -2940 -473 C ATOM 204 CG1 VAL A1026 28.864 -0.673 -3.352 1.00119.31 C ANISOU 204 CG1 VAL A1026 11789 18702 14840 344 -3311 173 C ATOM 205 CG2 VAL A1026 29.935 -2.291 -4.934 1.00132.66 C ANISOU 205 CG2 VAL A1026 12286 20746 17373 1780 -2985 -1065 C ATOM 206 N LYS A1027 30.413 2.248 -4.928 1.00120.23 N ANISOU 206 N LYS A1027 10422 21348 13914 -1268 -2421 83 N ATOM 207 CA LYS A1027 30.370 3.633 -4.473 1.00117.41 C ANISOU 207 CA LYS A1027 10360 21096 13156 -2243 -2514 561 C ATOM 208 C LYS A1027 29.643 4.533 -5.443 1.00118.54 C ANISOU 208 C LYS A1027 10878 21308 12854 -2878 -2000 631 C ATOM 209 O LYS A1027 28.790 5.322 -5.031 1.00112.29 O ANISOU 209 O LYS A1027 10915 19909 11840 -3362 -2082 950 O ATOM 210 CB LYS A1027 31.776 4.183 -4.267 1.00127.36 C ANISOU 210 CB LYS A1027 10648 23316 14428 -2612 -2704 661 C ATOM 211 CG LYS A1027 32.330 3.968 -2.883 1.00145.85 C ANISOU 211 CG LYS A1027 12903 25522 16990 -2449 -3416 901 C ATOM 212 CD LYS A1027 33.690 4.651 -2.715 1.00165.72 C ANISOU 212 CD LYS A1027 14406 29105 19456 -2987 -3616 995 C ATOM 213 CE LYS A1027 33.671 6.133 -3.063 1.00173.81 C ANISOU 213 CE LYS A1027 15602 30363 20076 -4216 -3382 1226 C ATOM 214 NZ LYS A1027 32.677 6.897 -2.261 1.00174.49 N ANISOU 214 NZ LYS A1027 16904 29446 19949 -4734 -3621 1481 N ATOM 215 N ASP A1028 29.986 4.434 -6.728 1.00120.30 N ANISOU 215 N ASP A1028 10460 22333 12915 -2848 -1487 332 N ATOM 216 CA ASP A1028 29.387 5.281 -7.742 1.00118.34 C ANISOU 216 CA ASP A1028 10477 22308 12177 -3469 -1034 513 C ATOM 217 C ASP A1028 27.882 5.022 -7.837 1.00114.07 C ANISOU 217 C ASP A1028 10915 20882 11543 -3243 -958 487 C ATOM 218 O ASP A1028 27.115 5.982 -7.912 1.00109.66 O ANISOU 218 O ASP A1028 10983 19978 10704 -3782 -919 886 O ATOM 219 CB ASP A1028 30.065 5.044 -9.092 1.00127.83 C ANISOU 219 CB ASP A1028 10717 24743 13109 -3422 -490 151 C ATOM 220 CG ASP A1028 29.881 6.153 -10.116 1.00143.86 C ANISOU 220 CG ASP A1028 12757 27371 14534 -4315 -88 576 C ATOM 221 OD1 ASP A1028 30.371 5.992 -11.258 1.00151.38 O ANISOU 221 OD1 ASP A1028 12921 29498 15100 -4364 402 320 O ATOM 222 OD2 ASP A1028 29.312 7.217 -9.754 1.00146.71 O ANISOU 222 OD2 ASP A1028 13876 27070 14799 -4976 -286 1183 O ATOM 223 N ALA A1029 27.458 3.734 -7.791 1.00109.09 N ANISOU 223 N ALA A1029 10410 19839 11200 -2454 -985 29 N ATOM 224 CA ALA A1029 26.041 3.359 -7.861 1.00102.14 C ANISOU 224 CA ALA A1029 10355 18208 10247 -2288 -929 -29 C ATOM 225 C ALA A1029 25.291 3.894 -6.651 1.00 99.15 C ANISOU 225 C ALA A1029 10790 17003 9877 -2551 -1302 443 C ATOM 226 O ALA A1029 24.223 4.486 -6.813 1.00 94.23 O ANISOU 226 O ALA A1029 10753 16088 8963 -2836 -1185 641 O ATOM 227 CB ALA A1029 25.892 1.847 -7.954 1.00104.99 C ANISOU 227 CB ALA A1029 10665 18209 11017 -1496 -966 -600 C ATOM 228 N LEU A1030 25.863 3.722 -5.446 1.00 95.77 N ANISOU 228 N LEU A1030 10342 16312 9733 -2439 -1758 605 N ATOM 229 CA LEU A1030 25.254 4.219 -4.217 1.00 90.91 C ANISOU 229 CA LEU A1030 10421 15100 9021 -2695 -2106 963 C ATOM 230 C LEU A1030 25.108 5.736 -4.260 1.00 92.61 C ANISOU 230 C LEU A1030 10890 15380 8917 -3387 -2042 1226 C ATOM 231 O LEU A1030 24.113 6.271 -3.767 1.00 87.82 O ANISOU 231 O LEU A1030 10968 14274 8124 -3544 -2098 1356 O ATOM 232 CB LEU A1030 26.086 3.801 -3.011 1.00 94.56 C ANISOU 232 CB LEU A1030 10679 15516 9734 -2505 -2631 1101 C ATOM 233 CG LEU A1030 25.986 2.355 -2.579 1.00100.55 C ANISOU 233 CG LEU A1030 11490 15845 10867 -1832 -2883 1046 C ATOM 234 CD1 LEU A1030 27.036 2.031 -1.530 1.00106.67 C ANISOU 234 CD1 LEU A1030 11891 16764 11875 -1624 -3452 1276 C ATOM 235 CD2 LEU A1030 24.607 2.058 -2.044 1.00 96.68 C ANISOU 235 CD2 LEU A1030 11840 14681 10211 -1874 -2914 1221 C ATOM 236 N THR A1031 26.087 6.428 -4.868 1.00 93.80 N ANISOU 236 N THR A1031 10473 16140 9026 -3804 -1925 1299 N ATOM 237 CA THR A1031 26.027 7.881 -5.013 1.00 94.79 C ANISOU 237 CA THR A1031 10869 16195 8952 -4536 -1908 1615 C ATOM 238 C THR A1031 24.785 8.276 -5.812 1.00 95.38 C ANISOU 238 C THR A1031 11487 15966 8787 -4554 -1599 1724 C ATOM 239 O THR A1031 24.059 9.185 -5.411 1.00 93.55 O ANISOU 239 O THR A1031 11906 15149 8492 -4787 -1730 1907 O ATOM 240 CB THR A1031 27.298 8.427 -5.684 1.00115.37 C ANISOU 240 CB THR A1031 12689 19613 11535 -5082 -1794 1758 C ATOM 241 OG1 THR A1031 28.448 8.078 -4.916 1.00119.73 O ANISOU 241 OG1 THR A1031 12635 20548 12310 -5038 -2126 1651 O ATOM 242 CG2 THR A1031 27.257 9.942 -5.849 1.00119.02 C ANISOU 242 CG2 THR A1031 13511 19832 11878 -5947 -1842 2185 C ATOM 243 N LYS A1032 24.542 7.586 -6.938 1.00 91.54 N ANISOU 243 N LYS A1032 10701 15917 8162 -4263 -1216 1555 N ATOM 244 CA LYS A1032 23.392 7.837 -7.806 1.00 88.70 C ANISOU 244 CA LYS A1032 10726 15468 7508 -4252 -949 1660 C ATOM 245 C LYS A1032 22.093 7.501 -7.075 1.00 88.00 C ANISOU 245 C LYS A1032 11311 14667 7458 -3875 -1085 1548 C ATOM 246 O LYS A1032 21.096 8.204 -7.248 1.00 86.16 O ANISOU 246 O LYS A1032 11550 14136 7051 -3953 -1056 1754 O ATOM 247 CB LYS A1032 23.523 7.023 -9.103 1.00 93.38 C ANISOU 247 CB LYS A1032 10764 16841 7876 -4028 -539 1358 C ATOM 248 CG LYS A1032 24.689 7.548 -9.957 1.00112.21 C ANISOU 248 CG LYS A1032 12427 20163 10044 -4518 -312 1541 C ATOM 249 CD LYS A1032 25.413 6.537 -10.854 1.00119.79 C ANISOU 249 CD LYS A1032 12529 22109 10875 -4187 49 993 C ATOM 250 CE LYS A1032 24.658 6.014 -12.041 1.00113.22 C ANISOU 250 CE LYS A1032 11672 21736 9612 -3970 420 675 C ATOM 251 NZ LYS A1032 25.500 5.061 -12.804 1.00114.00 N ANISOU 251 NZ LYS A1032 10895 22805 9616 -3604 760 -28 N ATOM 252 N MET A1033 22.112 6.462 -6.235 1.00 83.24 N ANISOU 252 N MET A1033 10723 13825 7080 -3480 -1259 1281 N ATOM 253 CA MET A1033 20.941 6.092 -5.457 1.00 78.94 C ANISOU 253 CA MET A1033 10738 12744 6510 -3241 -1375 1238 C ATOM 254 C MET A1033 20.634 7.158 -4.424 1.00 83.08 C ANISOU 254 C MET A1033 11742 12868 6954 -3479 -1620 1431 C ATOM 255 O MET A1033 19.468 7.475 -4.213 1.00 81.38 O ANISOU 255 O MET A1033 11965 12388 6566 -3394 -1576 1439 O ATOM 256 CB MET A1033 21.125 4.740 -4.776 1.00 81.54 C ANISOU 256 CB MET A1033 10992 12886 7102 -2867 -1559 1054 C ATOM 257 CG MET A1033 21.218 3.590 -5.738 1.00 86.90 C ANISOU 257 CG MET A1033 11322 13752 7943 -2531 -1346 698 C ATOM 258 SD MET A1033 21.338 2.002 -4.891 1.00 93.50 S ANISOU 258 SD MET A1033 12227 14052 9246 -2072 -1671 577 S ATOM 259 CE MET A1033 19.683 1.773 -4.380 1.00 85.83 C ANISOU 259 CE MET A1033 11933 12629 8051 -2222 -1671 737 C ATOM 260 N ARG A1034 21.667 7.724 -3.787 1.00 82.39 N ANISOU 260 N ARG A1034 11530 12793 6981 -3768 -1883 1512 N ATOM 261 CA ARG A1034 21.459 8.764 -2.776 1.00 82.69 C ANISOU 261 CA ARG A1034 12040 12436 6944 -4019 -2148 1540 C ATOM 262 C ARG A1034 20.800 9.986 -3.406 1.00 86.50 C ANISOU 262 C ARG A1034 12883 12613 7370 -4205 -2022 1673 C ATOM 263 O ARG A1034 19.818 10.495 -2.872 1.00 85.31 O ANISOU 263 O ARG A1034 13230 12066 7119 -4049 -2073 1559 O ATOM 264 CB ARG A1034 22.785 9.161 -2.100 1.00 86.81 C ANISOU 264 CB ARG A1034 12294 13098 7592 -4403 -2489 1560 C ATOM 265 CG ARG A1034 22.574 9.955 -0.817 1.00 94.45 C ANISOU 265 CG ARG A1034 13759 13700 8429 -4606 -2825 1406 C ATOM 266 CD ARG A1034 23.871 10.305 -0.129 1.00107.73 C ANISOU 266 CD ARG A1034 15141 15605 10186 -5052 -3219 1384 C ATOM 267 NE ARG A1034 23.653 10.629 1.280 1.00123.13 N ANISOU 267 NE ARG A1034 17504 17400 11882 -5130 -3570 1123 N ATOM 268 CZ ARG A1034 23.292 11.822 1.742 1.00145.66 C ANISOU 268 CZ ARG A1034 20887 19792 14666 -5417 -3701 840 C ATOM 269 NH1 ARG A1034 23.061 12.827 0.903 1.00130.31 N ANISOU 269 NH1 ARG A1034 19192 17346 12974 -5641 -3553 900 N ATOM 270 NH2 ARG A1034 23.124 12.011 3.044 1.00143.54 N ANISOU 270 NH2 ARG A1034 20924 19552 14062 -5457 -3997 486 N ATOM 271 N ALA A1035 21.328 10.434 -4.555 1.00 84.64 N ANISOU 271 N ALA A1035 12361 12615 7182 -4510 -1862 1939 N ATOM 272 CA ALA A1035 20.792 11.584 -5.262 1.00 85.76 C ANISOU 272 CA ALA A1035 12842 12437 7307 -4714 -1811 2243 C ATOM 273 C ALA A1035 19.354 11.327 -5.683 1.00 84.22 C ANISOU 273 C ALA A1035 12903 12174 6924 -4219 -1617 2209 C ATOM 274 O ALA A1035 18.518 12.219 -5.536 1.00 84.42 O ANISOU 274 O ALA A1035 13402 11687 6989 -4096 -1722 2277 O ATOM 275 CB ALA A1035 21.652 11.897 -6.474 1.00 90.90 C ANISOU 275 CB ALA A1035 13042 13579 7918 -5196 -1645 2645 C ATOM 276 N ALA A1036 19.057 10.093 -6.171 1.00 76.55 N ANISOU 276 N ALA A1036 11598 11703 5785 -3913 -1368 2046 N ATOM 277 CA ALA A1036 17.716 9.703 -6.605 1.00 73.17 C ANISOU 277 CA ALA A1036 11298 11358 5145 -3534 -1197 1977 C ATOM 278 C ALA A1036 16.752 9.717 -5.449 1.00 75.88 C ANISOU 278 C ALA A1036 12032 11321 5478 -3236 -1320 1746 C ATOM 279 O ALA A1036 15.645 10.218 -5.597 1.00 75.12 O ANISOU 279 O ALA A1036 12160 11109 5273 -2994 -1290 1782 O ATOM 280 CB ALA A1036 17.738 8.326 -7.238 1.00 72.07 C ANISOU 280 CB ALA A1036 10746 11743 4893 -3372 -965 1735 C ATOM 281 N ALA A1037 17.169 9.173 -4.283 1.00 73.68 N ANISOU 281 N ALA A1037 11782 10947 5265 -3239 -1468 1526 N ATOM 282 CA ALA A1037 16.337 9.134 -3.075 1.00 73.14 C ANISOU 282 CA ALA A1037 12024 10716 5049 -3039 -1558 1307 C ATOM 283 C ALA A1037 16.012 10.539 -2.607 1.00 82.06 C ANISOU 283 C ALA A1037 13551 11424 6204 -3007 -1702 1214 C ATOM 284 O ALA A1037 14.875 10.806 -2.241 1.00 81.11 O ANISOU 284 O ALA A1037 13622 11278 5919 -2684 -1638 1024 O ATOM 285 CB ALA A1037 17.039 8.360 -1.971 1.00 73.90 C ANISOU 285 CB ALA A1037 12060 10873 5146 -3138 -1753 1223 C ATOM 286 N LEU A1038 16.993 11.449 -2.670 1.00 84.96 N ANISOU 286 N LEU A1038 14012 11458 6810 -3342 -1901 1319 N ATOM 287 CA LEU A1038 16.806 12.838 -2.263 1.00 90.76 C ANISOU 287 CA LEU A1038 15206 11575 7704 -3356 -2110 1182 C ATOM 288 C LEU A1038 15.764 13.534 -3.147 1.00 96.74 C ANISOU 288 C LEU A1038 16144 12073 8540 -3010 -2017 1374 C ATOM 289 O LEU A1038 14.980 14.337 -2.641 1.00 99.73 O ANISOU 289 O LEU A1038 16885 12019 8989 -2648 -2120 1085 O ATOM 290 CB LEU A1038 18.136 13.603 -2.312 1.00 95.99 C ANISOU 290 CB LEU A1038 15901 11912 8659 -3952 -2368 1342 C ATOM 291 CG LEU A1038 19.231 13.161 -1.322 1.00102.53 C ANISOU 291 CG LEU A1038 16531 12995 9430 -4294 -2580 1135 C ATOM 292 CD1 LEU A1038 20.539 13.893 -1.586 1.00108.56 C ANISOU 292 CD1 LEU A1038 17175 13594 10479 -4975 -2808 1352 C ATOM 293 CD2 LEU A1038 18.799 13.368 0.112 1.00106.71 C ANISOU 293 CD2 LEU A1038 17413 13390 9742 -4125 -2768 596 C ATOM 294 N ASP A1039 15.743 13.218 -4.453 1.00 92.17 N ANISOU 294 N ASP A1039 15278 11824 7918 -3070 -1840 1823 N ATOM 295 CA ASP A1039 14.776 13.801 -5.379 1.00 94.48 C ANISOU 295 CA ASP A1039 15670 12014 8213 -2749 -1807 2127 C ATOM 296 C ASP A1039 13.401 13.208 -5.178 1.00 95.62 C ANISOU 296 C ASP A1039 15693 12550 8088 -2183 -1634 1839 C ATOM 297 O ASP A1039 12.414 13.942 -5.158 1.00 99.95 O ANISOU 297 O ASP A1039 16430 12841 8704 -1705 -1715 1789 O ATOM 298 CB ASP A1039 15.206 13.600 -6.827 1.00 97.30 C ANISOU 298 CB ASP A1039 15703 12822 8446 -3065 -1675 2687 C ATOM 299 CG ASP A1039 16.473 14.326 -7.235 1.00118.73 C ANISOU 299 CG ASP A1039 18451 15293 11368 -3714 -1813 3120 C ATOM 300 OD1 ASP A1039 16.816 15.342 -6.584 1.00123.89 O ANISOU 300 OD1 ASP A1039 19534 15155 12385 -3901 -2108 3101 O ATOM 301 OD2 ASP A1039 17.085 13.923 -8.248 1.00128.07 O ANISOU 301 OD2 ASP A1039 19216 17115 12329 -4068 -1626 3459 O ATOM 302 N ALA A1040 13.328 11.877 -5.045 1.00 85.46 N ANISOU 302 N ALA A1040 14063 11875 6532 -2237 -1418 1659 N ATOM 303 CA ALA A1040 12.069 11.151 -4.845 1.00 82.24 C ANISOU 303 CA ALA A1040 13467 11941 5838 -1892 -1241 1426 C ATOM 304 C ALA A1040 11.372 11.594 -3.578 1.00 85.37 C ANISOU 304 C ALA A1040 14075 12191 6171 -1560 -1287 1007 C ATOM 305 O ALA A1040 10.140 11.663 -3.541 1.00 86.45 O ANISOU 305 O ALA A1040 14076 12639 6131 -1143 -1184 857 O ATOM 306 CB ALA A1040 12.337 9.667 -4.784 1.00 78.99 C ANISOU 306 CB ALA A1040 12769 11970 5274 -2146 -1084 1332 C ATOM 307 N GLN A1041 12.165 11.922 -2.547 1.00 80.76 N ANISOU 307 N GLN A1041 13759 11246 5680 -1745 -1444 774 N ATOM 308 CA GLN A1041 11.675 12.381 -1.258 1.00 82.85 C ANISOU 308 CA GLN A1041 14230 11460 5788 -1484 -1487 258 C ATOM 309 C GLN A1041 10.869 13.680 -1.405 1.00 90.95 C ANISOU 309 C GLN A1041 15484 12042 7030 -914 -1577 47 C ATOM 310 O GLN A1041 10.017 13.949 -0.572 1.00 94.21 O ANISOU 310 O GLN A1041 15900 12660 7235 -480 -1501 -473 O ATOM 311 CB GLN A1041 12.860 12.590 -0.306 1.00 85.18 C ANISOU 311 CB GLN A1041 14773 11455 6137 -1876 -1716 67 C ATOM 312 CG GLN A1041 12.479 13.001 1.101 1.00 93.34 C ANISOU 312 CG GLN A1041 16011 12585 6870 -1689 -1764 -561 C ATOM 313 CD GLN A1041 13.658 13.002 2.044 1.00116.50 C ANISOU 313 CD GLN A1041 19103 15437 9725 -2159 -2025 -718 C ATOM 314 OE1 GLN A1041 14.696 13.599 1.788 1.00112.21 O ANISOU 314 OE1 GLN A1041 18730 14350 9554 -2496 -2282 -614 O ATOM 315 NE2 GLN A1041 13.484 12.401 3.204 1.00115.94 N ANISOU 315 NE2 GLN A1041 18958 15983 9112 -2231 -1989 -964 N ATOM 316 N LYS A1042 11.112 14.462 -2.462 1.00 88.02 N ANISOU 316 N LYS A1042 15274 11111 7058 -888 -1745 466 N ATOM 317 CA LYS A1042 10.429 15.741 -2.655 1.00 94.38 C ANISOU 317 CA LYS A1042 16369 11280 8210 -298 -1939 375 C ATOM 318 C LYS A1042 9.190 15.599 -3.551 1.00 98.18 C ANISOU 318 C LYS A1042 16485 12247 8571 242 -1824 644 C ATOM 319 O LYS A1042 8.425 16.556 -3.691 1.00103.54 O ANISOU 319 O LYS A1042 17301 12511 9527 913 -1996 568 O ATOM 320 CB LYS A1042 11.395 16.767 -3.264 1.00100.98 C ANISOU 320 CB LYS A1042 17648 11141 9580 -649 -2277 823 C ATOM 321 CG LYS A1042 12.621 16.987 -2.391 1.00121.80 C ANISOU 321 CG LYS A1042 20582 13348 12347 -1240 -2445 529 C ATOM 322 CD LYS A1042 13.573 18.044 -2.918 1.00138.86 C ANISOU 322 CD LYS A1042 23163 14548 15050 -1734 -2794 968 C ATOM 323 CE LYS A1042 14.860 18.098 -2.107 1.00153.28 C ANISOU 323 CE LYS A1042 25124 16183 16932 -2453 -2960 696 C ATOM 324 NZ LYS A1042 14.631 18.283 -0.643 1.00165.93 N ANISOU 324 NZ LYS A1042 26957 17691 18397 -2196 -3038 -252 N ATOM 325 N ALA A1043 8.978 14.408 -4.126 1.00 90.07 N ANISOU 325 N ALA A1043 14984 12081 7156 -20 -1574 909 N ATOM 326 CA ALA A1043 7.850 14.150 -5.015 1.00 91.15 C ANISOU 326 CA ALA A1043 14695 12845 7094 352 -1489 1150 C ATOM 327 C ALA A1043 6.603 13.751 -4.236 1.00 97.70 C ANISOU 327 C ALA A1043 15138 14392 7592 798 -1270 618 C ATOM 328 O ALA A1043 6.670 13.521 -3.029 1.00 97.22 O ANISOU 328 O ALA A1043 15136 14440 7362 730 -1139 112 O ATOM 329 CB ALA A1043 8.210 13.055 -6.001 1.00 86.27 C ANISOU 329 CB ALA A1043 13753 12822 6202 -202 -1338 1550 C ATOM 330 N THR A1044 5.460 13.688 -4.940 1.00 97.35 N ANISOU 330 N THR A1044 14640 14959 7391 1218 -1243 765 N ATOM 331 CA THR A1044 4.176 13.279 -4.392 1.00 99.50 C ANISOU 331 CA THR A1044 14364 16144 7299 1587 -1015 338 C ATOM 332 C THR A1044 3.730 12.005 -5.079 1.00 99.03 C ANISOU 332 C THR A1044 13777 17018 6832 1092 -834 580 C ATOM 333 O THR A1044 3.385 12.036 -6.271 1.00 99.51 O ANISOU 333 O THR A1044 13600 17345 6865 1172 -968 985 O ATOM 334 CB THR A1044 3.125 14.379 -4.532 1.00117.61 C ANISOU 334 CB THR A1044 16476 18406 9803 2595 -1187 195 C ATOM 335 OG1 THR A1044 3.572 15.557 -3.861 1.00124.61 O ANISOU 335 OG1 THR A1044 17944 18247 11157 3044 -1390 -146 O ATOM 336 CG2 THR A1044 1.777 13.949 -3.979 1.00118.52 C ANISOU 336 CG2 THR A1044 15855 19690 9485 2972 -908 -278 C ATOM 337 N PRO A1045 3.717 10.869 -4.350 1.00 91.29 N ANISOU 337 N PRO A1045 12626 16540 5520 538 -568 354 N ATOM 338 CA PRO A1045 3.269 9.618 -4.965 1.00 88.67 C ANISOU 338 CA PRO A1045 11854 16952 4884 -1 -437 515 C ATOM 339 C PRO A1045 1.806 9.721 -5.417 1.00 98.02 C ANISOU 339 C PRO A1045 12352 19078 5812 402 -411 466 C ATOM 340 O PRO A1045 1.048 10.547 -4.901 1.00103.81 O ANISOU 340 O PRO A1045 12863 20038 6540 1111 -399 197 O ATOM 341 CB PRO A1045 3.460 8.595 -3.842 1.00 88.07 C ANISOU 341 CB PRO A1045 11814 17063 4584 -585 -223 321 C ATOM 342 CG PRO A1045 3.359 9.384 -2.603 1.00 95.08 C ANISOU 342 CG PRO A1045 12842 17876 5408 -164 -160 -51 C ATOM 343 CD PRO A1045 4.068 10.662 -2.934 1.00 91.41 C ANISOU 343 CD PRO A1045 12851 16482 5398 339 -419 -25 C ATOM 344 N PRO A1046 1.408 8.889 -6.394 1.00 93.28 N ANISOU 344 N PRO A1046 11371 19073 4999 -17 -421 659 N ATOM 345 CA PRO A1046 0.045 8.952 -6.940 1.00 98.78 C ANISOU 345 CA PRO A1046 11324 20791 5418 295 -458 652 C ATOM 346 C PRO A1046 -1.078 8.819 -5.897 1.00104.53 C ANISOU 346 C PRO A1046 11468 22396 5855 454 -208 268 C ATOM 347 O PRO A1046 -2.098 9.506 -6.007 1.00110.34 O ANISOU 347 O PRO A1046 11639 23775 6510 1183 -266 162 O ATOM 348 CB PRO A1046 0.003 7.744 -7.880 1.00 99.03 C ANISOU 348 CB PRO A1046 11129 21287 5211 -504 -464 763 C ATOM 349 CG PRO A1046 1.124 6.870 -7.434 1.00 97.52 C ANISOU 349 CG PRO A1046 11484 20388 5182 -1193 -340 702 C ATOM 350 CD PRO A1046 2.182 7.843 -7.074 1.00 90.24 C ANISOU 350 CD PRO A1046 11172 18503 4611 -775 -422 810 C ATOM 351 N LYS A1047 -0.896 7.968 -4.895 1.00 97.52 N ANISOU 351 N LYS A1047 10669 21597 4787 -192 55 96 N ATOM 352 CA LYS A1047 -1.900 7.723 -3.856 1.00102.27 C ANISOU 352 CA LYS A1047 10681 23203 4974 -244 355 -208 C ATOM 353 C LYS A1047 -2.034 8.912 -2.891 1.00109.45 C ANISOU 353 C LYS A1047 11633 24043 5910 672 447 -627 C ATOM 354 O LYS A1047 -2.996 8.964 -2.128 1.00114.61 O ANISOU 354 O LYS A1047 11649 25734 6165 875 717 -981 O ATOM 355 CB LYS A1047 -1.491 6.464 -3.087 1.00101.24 C ANISOU 355 CB LYS A1047 10778 23040 4649 -1296 543 -105 C ATOM 356 CG LYS A1047 -2.391 5.972 -1.968 1.00115.11 C ANISOU 356 CG LYS A1047 11977 25897 5862 -1691 881 -251 C ATOM 357 CD LYS A1047 -1.887 4.636 -1.475 1.00121.55 C ANISOU 357 CD LYS A1047 13144 26444 6597 -2830 928 85 C ATOM 358 CE LYS A1047 -2.793 3.955 -0.483 1.00142.94 C ANISOU 358 CE LYS A1047 15293 30310 8706 -3514 1240 148 C ATOM 359 NZ LYS A1047 -2.303 2.591 -0.148 1.00151.72 N ANISOU 359 NZ LYS A1047 16830 30960 9858 -4673 1174 633 N ATOM 360 N LEU A1048 -1.115 9.877 -2.948 1.00104.99 N ANISOU 360 N LEU A1048 11766 22328 5799 1209 226 -643 N ATOM 361 CA LEU A1048 -1.163 10.988 -2.008 1.00110.97 C ANISOU 361 CA LEU A1048 12672 22848 6646 2034 273 -1171 C ATOM 362 C LEU A1048 -1.311 12.349 -2.719 1.00121.89 C ANISOU 362 C LEU A1048 14177 23575 8561 3123 -73 -1183 C ATOM 363 O LEU A1048 -1.187 13.388 -2.063 1.00126.55 O ANISOU 363 O LEU A1048 15071 23602 9411 3863 -132 -1660 O ATOM 364 CB LEU A1048 0.107 10.992 -1.129 1.00106.48 C ANISOU 364 CB LEU A1048 12905 21387 6164 1637 275 -1272 C ATOM 365 CG LEU A1048 0.328 9.720 -0.275 1.00107.84 C ANISOU 365 CG LEU A1048 13048 22084 5841 635 536 -1170 C ATOM 366 CD1 LEU A1048 1.534 9.858 0.616 1.00104.78 C ANISOU 366 CD1 LEU A1048 13371 20932 5508 388 463 -1270 C ATOM 367 CD2 LEU A1048 -0.890 9.413 0.571 1.00117.65 C ANISOU 367 CD2 LEU A1048 13520 24750 6431 622 915 -1509 C ATOM 368 N GLU A1049 -1.654 12.347 -4.021 1.00119.95 N ANISOU 368 N GLU A1049 13672 23453 8449 3236 -325 -682 N ATOM 369 CA GLU A1049 -1.843 13.579 -4.800 1.00126.01 C ANISOU 369 CA GLU A1049 14548 23621 9709 4224 -735 -473 C ATOM 370 C GLU A1049 -2.983 14.438 -4.253 1.00140.93 C ANISOU 370 C GLU A1049 15865 26020 11662 5419 -713 -1053 C ATOM 371 O GLU A1049 -2.899 15.666 -4.292 1.00146.67 O ANISOU 371 O GLU A1049 16969 25798 12959 6378 -1029 -1157 O ATOM 372 CB GLU A1049 -2.125 13.259 -6.262 1.00126.87 C ANISOU 372 CB GLU A1049 14340 24129 9735 4027 -996 206 C ATOM 373 CG GLU A1049 -0.995 12.556 -6.994 1.00132.75 C ANISOU 373 CG GLU A1049 15612 24377 10451 3032 -1046 704 C ATOM 374 CD GLU A1049 -1.303 12.313 -8.469 1.00161.90 C ANISOU 374 CD GLU A1049 18965 28606 13944 2872 -1305 1279 C ATOM 375 OE1 GLU A1049 -1.956 13.172 -9.109 1.00160.67 O ANISOU 375 OE1 GLU A1049 18541 28593 13912 3678 -1648 1586 O ATOM 376 OE2 GLU A1049 -0.855 11.272 -8.997 1.00154.77 O ANISOU 376 OE2 GLU A1049 18085 27960 12759 1965 -1200 1412 O ATOM 377 N ASP A1050 -4.042 13.793 -3.757 1.00141.42 N ANISOU 377 N ASP A1050 15000 27567 11168 5355 -352 -1436 N ATOM 378 CA ASP A1050 -5.203 14.476 -3.190 1.00153.11 C ANISOU 378 CA ASP A1050 15713 29867 12595 6491 -238 -2099 C ATOM 379 C ASP A1050 -4.934 14.914 -1.745 1.00157.49 C ANISOU 379 C ASP A1050 16572 30181 13085 6790 70 -2971 C ATOM 380 O ASP A1050 -5.676 15.730 -1.193 1.00167.90 O ANISOU 380 O ASP A1050 17454 31855 14487 7931 141 -3710 O ATOM 381 CB ASP A1050 -6.426 13.548 -3.238 1.00159.17 C ANISOU 381 CB ASP A1050 15249 32536 12694 6133 67 -2141 C ATOM 382 CG ASP A1050 -6.257 12.296 -2.397 1.00169.72 C ANISOU 382 CG ASP A1050 16493 34613 13382 4831 559 -2240 C ATOM 383 OD1 ASP A1050 -5.288 11.538 -2.641 1.00161.37 O ANISOU 383 OD1 ASP A1050 16130 32837 12346 3780 510 -1769 O ATOM 384 OD2 ASP A1050 -7.102 12.061 -1.512 1.00180.80 O ANISOU 384 OD2 ASP A1050 17402 36698 14595 4642 1003 -2647 O ATOM 385 N LYS A1051 -3.896 14.339 -1.130 1.00143.29 N ANISOU 385 N LYS A1051 15460 27888 11093 5789 244 -2930 N ATOM 386 CA LYS A1051 -3.539 14.630 0.246 1.00144.81 C ANISOU 386 CA LYS A1051 15968 27982 11071 5864 512 -3705 C ATOM 387 C LYS A1051 -2.761 15.928 0.358 1.00149.84 C ANISOU 387 C LYS A1051 17521 26966 12445 6618 140 -4043 C ATOM 388 O LYS A1051 -2.179 16.415 -0.619 1.00146.51 O ANISOU 388 O LYS A1051 17682 25298 12687 6722 -319 -3445 O ATOM 389 CB LYS A1051 -2.706 13.484 0.848 1.00137.88 C ANISOU 389 CB LYS A1051 15456 27235 9697 4485 751 -3421 C ATOM 390 CG LYS A1051 -3.426 12.145 0.963 1.00149.47 C ANISOU 390 CG LYS A1051 16135 30213 10445 3575 1120 -3119 C ATOM 391 CD LYS A1051 -4.542 12.178 1.990 1.00172.05 C ANISOU 391 CD LYS A1051 18081 34679 12610 3913 1591 -3823 C ATOM 392 CE LYS A1051 -5.189 10.833 2.176 1.00184.51 C ANISOU 392 CE LYS A1051 19174 37223 13710 2697 1955 -3328 C ATOM 393 NZ LYS A1051 -6.279 10.894 3.190 1.00192.84 N ANISOU 393 NZ LYS A1051 20652 37237 15382 2444 2538 -3393 N ATOM 394 N SER A1052 -2.762 16.487 1.569 1.00151.82 N ANISOU 394 N SER A1052 17887 27266 12533 7079 338 -5024 N ATOM 395 CA SER A1052 -2.024 17.691 1.894 1.00155.22 C ANISOU 395 CA SER A1052 19216 26136 13623 7685 1 -5551 C ATOM 396 C SER A1052 -0.537 17.392 1.904 1.00145.64 C ANISOU 396 C SER A1052 18956 23837 12544 6578 -190 -5044 C ATOM 397 O SER A1052 -0.139 16.313 2.350 1.00137.40 O ANISOU 397 O SER A1052 17839 23503 10865 5524 87 -4786 O ATOM 398 CB SER A1052 -2.478 18.243 3.245 1.00170.29 C ANISOU 398 CB SER A1052 20896 28642 15164 8401 317 -6901 C ATOM 399 OG SER A1052 -1.689 19.342 3.672 1.00183.97 O ANISOU 399 OG SER A1052 23575 28821 17504 8830 -21 -7545 O ATOM 400 N PRO A1053 0.306 18.338 1.449 1.00140.78 N ANISOU 400 N PRO A1053 19217 21510 12765 6785 -686 -4874 N ATOM 401 CA PRO A1053 1.756 18.105 1.484 1.00131.61 C ANISOU 401 CA PRO A1053 18853 19430 11723 5732 -866 -4440 C ATOM 402 C PRO A1053 2.278 17.918 2.912 1.00135.76 C ANISOU 402 C PRO A1053 19589 20298 11695 5285 -638 -5221 C ATOM 403 O PRO A1053 3.384 17.410 3.102 1.00127.26 O ANISOU 403 O PRO A1053 18934 18930 10488 4314 -707 -4849 O ATOM 404 CB PRO A1053 2.324 19.379 0.854 1.00138.21 C ANISOU 404 CB PRO A1053 20480 18475 13561 6183 -1432 -4269 C ATOM 405 CG PRO A1053 1.200 19.920 0.020 1.00149.91 C ANISOU 405 CG PRO A1053 21531 19991 15438 7271 -1601 -4081 C ATOM 406 CD PRO A1053 -0.009 19.645 0.839 1.00151.44 C ANISOU 406 CD PRO A1053 20851 21668 15022 7937 -1147 -4966 C ATOM 407 N ASP A1054 1.466 18.302 3.912 1.00142.87 N ANISOU 407 N ASP A1054 20120 21960 12204 6014 -365 -6310 N ATOM 408 CA ASP A1054 1.822 18.196 5.320 1.00146.04 C ANISOU 408 CA ASP A1054 20644 22930 11916 5667 -136 -7151 C ATOM 409 C ASP A1054 1.054 17.060 5.995 1.00150.28 C ANISOU 409 C ASP A1054 20311 25456 11334 5252 441 -7170 C ATOM 410 O ASP A1054 1.148 16.896 7.211 1.00154.51 O ANISOU 410 O ASP A1054 20786 26837 11084 4979 697 -7827 O ATOM 411 CB ASP A1054 1.546 19.525 6.033 1.00161.76 C ANISOU 411 CB ASP A1054 22900 24354 14206 6751 -244 -8517 C ATOM 412 CG ASP A1054 2.301 20.694 5.433 1.00174.08 C ANISOU 412 CG ASP A1054 25406 23797 16940 7068 -870 -8478 C ATOM 413 OD1 ASP A1054 1.991 21.072 4.282 1.00174.40 O ANISOU 413 OD1 ASP A1054 25471 23049 17745 7567 -1154 -7809 O ATOM 414 OD2 ASP A1054 3.145 21.279 6.141 1.00184.63 O ANISOU 414 OD2 ASP A1054 27436 24308 18406 6821 -1101 -9141 O ATOM 415 N SER A1055 0.326 16.258 5.207 1.00142.99 N ANISOU 415 N SER A1055 18726 25310 10293 5094 619 -6405 N ATOM 416 CA SER A1055 -0.422 15.128 5.734 1.00143.25 C ANISOU 416 CA SER A1055 17935 27152 9341 4530 1127 -6258 C ATOM 417 C SER A1055 0.486 14.111 6.437 1.00141.78 C ANISOU 417 C SER A1055 18077 27246 8546 3256 1190 -5779 C ATOM 418 O SER A1055 1.671 14.017 6.109 1.00132.95 O ANISOU 418 O SER A1055 17685 24949 7881 2729 825 -5264 O ATOM 419 CB SER A1055 -1.183 14.422 4.619 1.00142.69 C ANISOU 419 CB SER A1055 17229 27598 9388 4395 1183 -5437 C ATOM 420 OG SER A1055 -2.244 15.212 4.126 1.00161.52 O ANISOU 420 OG SER A1055 19053 30203 12113 5587 1172 -5860 O ATOM 421 N PRO A1056 -0.066 13.317 7.387 1.00144.03 N ANISOU 421 N PRO A1056 17780 29155 7792 2733 1637 -5865 N ATOM 422 CA PRO A1056 0.745 12.282 8.053 1.00139.48 C ANISOU 422 CA PRO A1056 17503 28852 6639 1530 1629 -5242 C ATOM 423 C PRO A1056 1.296 11.257 7.063 1.00135.23 C ANISOU 423 C PRO A1056 17197 27596 6586 730 1384 -4043 C ATOM 424 O PRO A1056 2.382 10.714 7.278 1.00130.18 O ANISOU 424 O PRO A1056 17099 26389 5973 10 1135 -3527 O ATOM 425 CB PRO A1056 -0.251 11.635 9.011 1.00148.99 C ANISOU 425 CB PRO A1056 17886 32044 6678 1167 2172 -5394 C ATOM 426 CG PRO A1056 -1.255 12.717 9.284 1.00164.60 C ANISOU 426 CG PRO A1056 19300 34720 8522 2372 2464 -6603 C ATOM 427 CD PRO A1056 -1.433 13.353 7.947 1.00156.32 C ANISOU 427 CD PRO A1056 18343 32440 8612 3205 2156 -6509 C ATOM 428 N GLU A1057 0.561 11.015 5.964 1.00130.45 N ANISOU 428 N GLU A1057 16155 27042 6368 912 1426 -3668 N ATOM 429 CA GLU A1057 0.989 10.095 4.918 1.00121.34 C ANISOU 429 CA GLU A1057 15177 25253 5676 253 1210 -2718 C ATOM 430 C GLU A1057 2.228 10.638 4.223 1.00121.29 C ANISOU 430 C GLU A1057 15954 23640 6489 406 764 -2543 C ATOM 431 O GLU A1057 3.198 9.901 4.063 1.00115.30 O ANISOU 431 O GLU A1057 15598 22317 5896 -294 567 -1958 O ATOM 432 CB GLU A1057 -0.130 9.842 3.899 1.00123.25 C ANISOU 432 CB GLU A1057 14727 26040 6063 452 1330 -2502 C ATOM 433 CG GLU A1057 -1.336 9.079 4.422 1.00139.57 C ANISOU 433 CG GLU A1057 15911 29778 7339 27 1763 -2483 C ATOM 434 CD GLU A1057 -2.190 9.810 5.444 1.00173.84 C ANISOU 434 CD GLU A1057 19670 35345 11038 687 2144 -3363 C ATOM 435 OE1 GLU A1057 -2.330 11.050 5.330 1.00168.71 O ANISOU 435 OE1 GLU A1057 19061 34279 10761 1836 2059 -4098 O ATOM 436 OE2 GLU A1057 -2.757 9.136 6.334 1.00176.77 O ANISOU 436 OE2 GLU A1057 19512 37121 10531 58 2527 -3321 O ATOM 437 N MET A1058 2.211 11.938 3.834 1.00121.55 N ANISOU 437 N MET A1058 16191 22939 7055 1319 588 -3039 N ATOM 438 CA MET A1058 3.358 12.577 3.179 1.00116.97 C ANISOU 438 CA MET A1058 16329 20881 7234 1391 167 -2836 C ATOM 439 C MET A1058 4.563 12.620 4.112 1.00117.81 C ANISOU 439 C MET A1058 17010 20537 7214 914 4 -2988 C ATOM 440 O MET A1058 5.697 12.485 3.650 1.00111.09 O ANISOU 440 O MET A1058 16606 18815 6788 480 -283 -2521 O ATOM 441 CB MET A1058 3.030 13.994 2.691 1.00125.62 C ANISOU 441 CB MET A1058 17573 21224 8933 2417 -36 -3279 C ATOM 442 CG MET A1058 2.181 14.025 1.428 1.00129.82 C ANISOU 442 CG MET A1058 17666 21884 9775 2852 -75 -2858 C ATOM 443 SD MET A1058 2.916 13.161 0.014 1.00124.26 S ANISOU 443 SD MET A1058 17120 20719 9375 2062 -269 -1787 S ATOM 444 CE MET A1058 4.401 14.136 -0.257 1.00119.42 C ANISOU 444 CE MET A1058 17419 18499 9457 2002 -697 -1635 C ATOM 445 N LYS A1059 4.325 12.801 5.416 1.00119.69 N ANISOU 445 N LYS A1059 17169 21501 6808 981 187 -3657 N ATOM 446 CA LYS A1059 5.408 12.812 6.392 1.00119.54 C ANISOU 446 CA LYS A1059 17623 21276 6520 493 1 -3827 C ATOM 447 C LYS A1059 5.996 11.400 6.533 1.00116.02 C ANISOU 447 C LYS A1059 17148 21177 5757 -473 -25 -2950 C ATOM 448 O LYS A1059 7.218 11.236 6.695 1.00111.57 O ANISOU 448 O LYS A1059 17010 20015 5368 -931 -347 -2665 O ATOM 449 CB LYS A1059 4.925 13.348 7.746 1.00132.58 C ANISOU 449 CB LYS A1059 19142 23815 7417 811 219 -4829 C ATOM 450 CG LYS A1059 4.627 14.865 7.774 1.00152.32 C ANISOU 450 CG LYS A1059 21861 25647 10368 1828 124 -5895 C ATOM 451 CD LYS A1059 4.318 15.436 9.186 1.00168.95 C ANISOU 451 CD LYS A1059 23896 28602 11693 2149 321 -7114 C ATOM 452 CE LYS A1059 3.070 14.969 9.916 1.00179.24 C ANISOU 452 CE LYS A1059 24368 31762 11973 2316 897 -7497 C ATOM 453 NZ LYS A1059 1.823 15.388 9.237 1.00188.42 N ANISOU 453 NZ LYS A1059 24950 33154 13487 3284 1135 -7793 N ATOM 454 N ASP A1060 5.119 10.382 6.449 1.00111.80 N ANISOU 454 N ASP A1060 16091 21575 4814 -775 278 -2514 N ATOM 455 CA ASP A1060 5.521 8.982 6.479 1.00106.94 C ANISOU 455 CA ASP A1060 15468 21133 4033 -1641 221 -1643 C ATOM 456 C ASP A1060 6.319 8.665 5.225 1.00101.23 C ANISOU 456 C ASP A1060 15011 19295 4156 -1765 -59 -1088 C ATOM 457 O ASP A1060 7.373 8.028 5.293 1.00 97.13 O ANISOU 457 O ASP A1060 14786 18312 3809 -2242 -322 -617 O ATOM 458 CB ASP A1060 4.294 8.065 6.601 1.00112.13 C ANISOU 458 CB ASP A1060 15512 22955 4139 -1984 594 -1348 C ATOM 459 CG ASP A1060 4.643 6.583 6.560 1.00122.26 C ANISOU 459 CG ASP A1060 16864 24195 5396 -2894 476 -412 C ATOM 460 OD1 ASP A1060 5.497 6.150 7.360 1.00123.56 O ANISOU 460 OD1 ASP A1060 17365 24267 5315 -3348 251 -82 O ATOM 461 OD2 ASP A1060 4.047 5.854 5.741 1.00128.33 O ANISOU 461 OD2 ASP A1060 17350 25009 6401 -3142 568 -24 O ATOM 462 N PHE A1061 5.812 9.127 4.071 1.00 94.83 N ANISOU 462 N PHE A1061 14047 18148 3837 -1292 -11 -1157 N ATOM 463 CA PHE A1061 6.467 8.956 2.784 1.00 87.63 C ANISOU 463 CA PHE A1061 13313 16370 3612 -1362 -221 -718 C ATOM 464 C PHE A1061 7.888 9.502 2.841 1.00 92.42 C ANISOU 464 C PHE A1061 14437 16065 4615 -1422 -552 -722 C ATOM 465 O PHE A1061 8.836 8.809 2.453 1.00 88.41 O ANISOU 465 O PHE A1061 14061 15150 4382 -1837 -724 -270 O ATOM 466 CB PHE A1061 5.655 9.661 1.680 1.00 88.96 C ANISOU 466 CB PHE A1061 13245 16452 4105 -758 -161 -842 C ATOM 467 CG PHE A1061 6.338 9.719 0.336 1.00 84.18 C ANISOU 467 CG PHE A1061 12825 15072 4087 -796 -370 -435 C ATOM 468 CD1 PHE A1061 6.295 8.637 -0.530 1.00 82.50 C ANISOU 468 CD1 PHE A1061 12400 15013 3933 -1213 -329 -5 C ATOM 469 CD2 PHE A1061 7.000 10.871 -0.077 1.00 86.34 C ANISOU 469 CD2 PHE A1061 13477 14504 4826 -457 -608 -507 C ATOM 470 CE1 PHE A1061 6.924 8.697 -1.777 1.00 80.08 C ANISOU 470 CE1 PHE A1061 12201 14189 4036 -1247 -476 288 C ATOM 471 CE2 PHE A1061 7.640 10.928 -1.315 1.00 85.57 C ANISOU 471 CE2 PHE A1061 13490 13879 5144 -583 -764 -65 C ATOM 472 CZ PHE A1061 7.581 9.851 -2.169 1.00 79.72 C ANISOU 472 CZ PHE A1061 12474 13466 4351 -943 -672 300 C ATOM 473 N ARG A1062 8.035 10.735 3.350 1.00 94.24 N ANISOU 473 N ARG A1062 14925 15996 4887 -1013 -651 -1290 N ATOM 474 CA ARG A1062 9.329 11.388 3.435 1.00 94.40 C ANISOU 474 CA ARG A1062 15406 15177 5283 -1149 -990 -1352 C ATOM 475 C ARG A1062 10.240 10.700 4.477 1.00102.39 C ANISOU 475 C ARG A1062 16530 16452 5923 -1723 -1149 -1222 C ATOM 476 O ARG A1062 11.447 10.610 4.249 1.00 99.76 O ANISOU 476 O ARG A1062 16377 15592 5934 -2046 -1429 -936 O ATOM 477 CB ARG A1062 9.174 12.880 3.761 1.00 99.76 C ANISOU 477 CB ARG A1062 16385 15374 6147 -606 -1102 -2070 C ATOM 478 CG ARG A1062 8.606 13.666 2.588 1.00105.01 C ANISOU 478 CG ARG A1062 17052 15470 7377 -41 -1122 -1994 C ATOM 479 CD ARG A1062 8.756 15.172 2.713 1.00123.61 C ANISOU 479 CD ARG A1062 19872 16894 10201 432 -1384 -2543 C ATOM 480 NE ARG A1062 7.805 15.784 3.635 1.00143.97 N ANISOU 480 NE ARG A1062 22378 19846 12478 1098 -1239 -3453 N ATOM 481 CZ ARG A1062 6.576 16.156 3.289 1.00163.03 C ANISOU 481 CZ ARG A1062 24475 22507 14960 1897 -1076 -3685 C ATOM 482 NH1 ARG A1062 6.126 15.930 2.062 1.00147.94 N ANISOU 482 NH1 ARG A1062 22304 20562 13344 2053 -1065 -3012 N ATOM 483 NH2 ARG A1062 5.774 16.720 4.180 1.00156.74 N ANISOU 483 NH2 ARG A1062 23545 22134 13875 2563 -919 -4632 N ATOM 484 N HIS A1063 9.680 10.184 5.578 1.00105.30 N ANISOU 484 N HIS A1063 16730 17721 5560 -1870 -986 -1358 N ATOM 485 CA HIS A1063 10.510 9.521 6.580 1.00107.36 C ANISOU 485 CA HIS A1063 17093 18294 5403 -2408 -1204 -1107 C ATOM 486 C HIS A1063 11.109 8.220 6.016 1.00104.94 C ANISOU 486 C HIS A1063 16706 17757 5411 -2829 -1338 -260 C ATOM 487 O HIS A1063 12.240 7.862 6.367 1.00106.46 O ANISOU 487 O HIS A1063 17029 17740 5681 -3137 -1676 35 O ATOM 488 CB HIS A1063 9.719 9.234 7.862 1.00115.39 C ANISOU 488 CB HIS A1063 17925 20468 5451 -2541 -987 -1331 C ATOM 489 CG HIS A1063 10.570 8.679 8.953 1.00122.50 C ANISOU 489 CG HIS A1063 18957 21759 5829 -3080 -1282 -1030 C ATOM 490 ND1 HIS A1063 11.438 9.489 9.657 1.00128.98 N ANISOU 490 ND1 HIS A1063 20055 22449 6502 -3105 -1593 -1533 N ATOM 491 CD2 HIS A1063 10.666 7.414 9.425 1.00125.50 C ANISOU 491 CD2 HIS A1063 19235 22622 5826 -3616 -1364 -242 C ATOM 492 CE1 HIS A1063 12.058 8.694 10.510 1.00131.23 C ANISOU 492 CE1 HIS A1063 20345 23240 6277 -3620 -1863 -1019 C ATOM 493 NE2 HIS A1063 11.611 7.437 10.421 1.00129.93 N ANISOU 493 NE2 HIS A1063 19979 23420 5967 -3918 -1744 -194 N ATOM 494 N GLY A1064 10.367 7.537 5.153 1.00 94.47 N ANISOU 494 N GLY A1064 15142 16470 4281 -2808 -1107 61 N ATOM 495 CA GLY A1064 10.871 6.311 4.557 1.00 89.79 C ANISOU 495 CA GLY A1064 14504 15553 4059 -3134 -1233 700 C ATOM 496 C GLY A1064 12.149 6.578 3.799 1.00 91.70 C ANISOU 496 C GLY A1064 14873 15023 4945 -3061 -1492 765 C ATOM 497 O GLY A1064 13.099 5.786 3.861 1.00 91.49 O ANISOU 497 O GLY A1064 14861 14758 5142 -3283 -1749 1148 O ATOM 498 N PHE A1065 12.194 7.741 3.115 1.00 87.23 N ANISOU 498 N PHE A1065 14376 14090 4678 -2740 -1445 410 N ATOM 499 CA PHE A1065 13.358 8.142 2.346 1.00 84.28 C ANISOU 499 CA PHE A1065 14065 13111 4845 -2765 -1643 496 C ATOM 500 C PHE A1065 14.493 8.573 3.282 1.00 90.12 C ANISOU 500 C PHE A1065 14972 13748 5523 -2983 -1986 382 C ATOM 501 O PHE A1065 15.651 8.348 2.952 1.00 89.00 O ANISOU 501 O PHE A1065 14735 13358 5725 -3165 -2201 615 O ATOM 502 CB PHE A1065 13.013 9.243 1.348 1.00 85.62 C ANISOU 502 CB PHE A1065 14291 12919 5320 -2463 -1534 313 C ATOM 503 CG PHE A1065 12.367 8.671 0.110 1.00 84.43 C ANISOU 503 CG PHE A1065 13891 12875 5315 -2356 -1307 557 C ATOM 504 CD1 PHE A1065 13.121 7.978 -0.827 1.00 85.24 C ANISOU 504 CD1 PHE A1065 13827 12840 5720 -2539 -1327 848 C ATOM 505 CD2 PHE A1065 11.007 8.828 -0.127 1.00 87.47 C ANISOU 505 CD2 PHE A1065 14143 13595 5495 -2057 -1081 424 C ATOM 506 CE1 PHE A1065 12.523 7.421 -1.961 1.00 83.65 C ANISOU 506 CE1 PHE A1065 13395 12820 5567 -2480 -1132 960 C ATOM 507 CE2 PHE A1065 10.413 8.273 -1.268 1.00 87.60 C ANISOU 507 CE2 PHE A1065 13891 13812 5580 -2027 -922 622 C ATOM 508 CZ PHE A1065 11.172 7.566 -2.170 1.00 82.41 C ANISOU 508 CZ PHE A1065 13136 12997 5178 -2265 -952 866 C ATOM 509 N ASP A1066 14.176 9.121 4.461 1.00 90.18 N ANISOU 509 N ASP A1066 15154 14071 5038 -2979 -2040 -12 N ATOM 510 CA ASP A1066 15.212 9.448 5.436 1.00 93.97 C ANISOU 510 CA ASP A1066 15765 14601 5339 -3260 -2411 -161 C ATOM 511 C ASP A1066 15.882 8.171 5.886 1.00 97.57 C ANISOU 511 C ASP A1066 16041 15368 5665 -3539 -2639 413 C ATOM 512 O ASP A1066 17.110 8.121 6.007 1.00 98.87 O ANISOU 512 O ASP A1066 16124 15402 6041 -3739 -2995 571 O ATOM 513 CB ASP A1066 14.629 10.225 6.627 1.00102.41 C ANISOU 513 CB ASP A1066 17042 16086 5784 -3183 -2394 -817 C ATOM 514 CG ASP A1066 14.202 11.640 6.275 1.00119.74 C ANISOU 514 CG ASP A1066 19489 17738 8271 -2827 -2310 -1477 C ATOM 515 OD1 ASP A1066 14.968 12.335 5.560 1.00121.11 O ANISOU 515 OD1 ASP A1066 19806 17150 9059 -2917 -2505 -1449 O ATOM 516 OD2 ASP A1066 13.138 12.081 6.767 1.00129.75 O ANISOU 516 OD2 ASP A1066 20798 19350 9151 -2467 -2075 -2025 O ATOM 517 N ILE A1067 15.079 7.114 6.086 1.00 93.07 N ANISOU 517 N ILE A1067 15380 15179 4802 -3559 -2466 772 N ATOM 518 CA ILE A1067 15.605 5.806 6.485 1.00 93.48 C ANISOU 518 CA ILE A1067 15333 15358 4827 -3786 -2733 1427 C ATOM 519 C ILE A1067 16.479 5.240 5.373 1.00 94.83 C ANISOU 519 C ILE A1067 15319 14925 5786 -3667 -2843 1711 C ATOM 520 O ILE A1067 17.579 4.735 5.639 1.00 96.48 O ANISOU 520 O ILE A1067 15404 15058 6197 -3723 -3230 2024 O ATOM 521 CB ILE A1067 14.476 4.820 6.848 1.00 96.97 C ANISOU 521 CB ILE A1067 15764 16221 4858 -3942 -2524 1805 C ATOM 522 CG1 ILE A1067 13.646 5.338 8.047 1.00101.74 C ANISOU 522 CG1 ILE A1067 16433 17696 4527 -4080 -2369 1498 C ATOM 523 CG2 ILE A1067 15.074 3.435 7.146 1.00 99.56 C ANISOU 523 CG2 ILE A1067 16080 16400 5347 -4158 -2887 2587 C ATOM 524 CD1 ILE A1067 12.425 4.442 8.428 1.00109.42 C ANISOU 524 CD1 ILE A1067 17300 19295 4979 -4362 -2094 1898 C ATOM 525 N LEU A1068 15.982 5.322 4.134 1.00 88.24 N ANISOU 525 N LEU A1068 14411 13769 5348 -3472 -2511 1571 N ATOM 526 CA LEU A1068 16.699 4.833 2.963 1.00 86.35 C ANISOU 526 CA LEU A1068 13946 13111 5751 -3340 -2519 1698 C ATOM 527 C LEU A1068 18.034 5.535 2.809 1.00 91.01 C ANISOU 527 C LEU A1068 14380 13584 6615 -3370 -2752 1585 C ATOM 528 O LEU A1068 19.062 4.866 2.665 1.00 92.80 O ANISOU 528 O LEU A1068 14337 13738 7184 -3319 -2988 1799 O ATOM 529 CB LEU A1068 15.867 5.019 1.692 1.00 83.10 C ANISOU 529 CB LEU A1068 13478 12570 5526 -3182 -2123 1507 C ATOM 530 CG LEU A1068 14.713 4.048 1.525 1.00 88.75 C ANISOU 530 CG LEU A1068 14201 13390 6129 -3220 -1918 1646 C ATOM 531 CD1 LEU A1068 13.843 4.439 0.346 1.00 85.92 C ANISOU 531 CD1 LEU A1068 13740 13074 5830 -3075 -1577 1411 C ATOM 532 CD2 LEU A1068 15.232 2.621 1.366 1.00 95.00 C ANISOU 532 CD2 LEU A1068 14921 13867 7309 -3259 -2110 1958 C ATOM 533 N VAL A1069 18.033 6.874 2.883 1.00 86.18 N ANISOU 533 N VAL A1069 13915 12946 5883 -3460 -2719 1241 N ATOM 534 CA VAL A1069 19.256 7.661 2.768 1.00 86.78 C ANISOU 534 CA VAL A1069 13855 12915 6204 -3660 -2955 1144 C ATOM 535 C VAL A1069 20.236 7.223 3.869 1.00 93.73 C ANISOU 535 C VAL A1069 14588 14097 6926 -3827 -3416 1306 C ATOM 536 O VAL A1069 21.439 7.091 3.609 1.00 95.21 O ANISOU 536 O VAL A1069 14394 14342 7440 -3907 -3643 1436 O ATOM 537 CB VAL A1069 18.952 9.174 2.823 1.00 91.82 C ANISOU 537 CB VAL A1069 14814 13304 6770 -3780 -2914 743 C ATOM 538 CG1 VAL A1069 20.232 9.994 2.932 1.00 95.67 C ANISOU 538 CG1 VAL A1069 15204 13675 7471 -4177 -3237 656 C ATOM 539 CG2 VAL A1069 18.148 9.610 1.599 1.00 88.45 C ANISOU 539 CG2 VAL A1069 14461 12577 6569 -3572 -2554 735 C ATOM 540 N GLY A1070 19.705 6.953 5.058 1.00 92.01 N ANISOU 540 N GLY A1070 14601 14193 6166 -3874 -3549 1336 N ATOM 541 CA GLY A1070 20.514 6.483 6.172 1.00 96.72 C ANISOU 541 CA GLY A1070 15078 15186 6484 -4034 -4038 1594 C ATOM 542 C GLY A1070 21.211 5.174 5.862 1.00100.47 C ANISOU 542 C GLY A1070 15205 15577 7393 -3814 -4252 2140 C ATOM 543 O GLY A1070 22.409 5.016 6.122 1.00103.37 O ANISOU 543 O GLY A1070 15221 16124 7932 -3834 -4673 2306 O ATOM 544 N GLN A1071 20.467 4.236 5.276 1.00 94.39 N ANISOU 544 N GLN A1071 14501 14516 6846 -3578 -3987 2368 N ATOM 545 CA GLN A1071 21.002 2.923 4.922 1.00 96.07 C ANISOU 545 CA GLN A1071 14468 14451 7582 -3281 -4186 2785 C ATOM 546 C GLN A1071 22.012 3.041 3.788 1.00 99.23 C ANISOU 546 C GLN A1071 14389 14706 8608 -3047 -4120 2547 C ATOM 547 O GLN A1071 23.008 2.310 3.758 1.00102.80 O ANISOU 547 O GLN A1071 14452 15136 9473 -2762 -4447 2752 O ATOM 548 CB GLN A1071 19.869 1.978 4.524 1.00 95.46 C ANISOU 548 CB GLN A1071 14637 14027 7606 -3194 -3908 2964 C ATOM 549 CG GLN A1071 18.820 1.768 5.603 1.00116.14 C ANISOU 549 CG GLN A1071 17631 16943 9553 -3509 -3914 3270 C ATOM 550 CD GLN A1071 17.704 0.882 5.123 1.00139.34 C ANISOU 550 CD GLN A1071 20745 19573 12626 -3554 -3632 3438 C ATOM 551 OE1 GLN A1071 16.642 1.373 4.778 1.00132.19 O ANISOU 551 OE1 GLN A1071 19926 18848 11452 -3666 -3198 3122 O ATOM 552 NE2 GLN A1071 17.910 -0.430 5.074 1.00137.46 N ANISOU 552 NE2 GLN A1071 20549 18832 12847 -3466 -3908 3919 N ATOM 553 N ILE A1072 21.749 3.956 2.850 1.00 92.18 N ANISOU 553 N ILE A1072 13485 13774 7766 -3148 -3704 2144 N ATOM 554 CA ILE A1072 22.641 4.204 1.720 1.00 92.30 C ANISOU 554 CA ILE A1072 13014 13839 8216 -3061 -3560 1944 C ATOM 555 C ILE A1072 23.964 4.712 2.254 1.00101.62 C ANISOU 555 C ILE A1072 13795 15394 9420 -3258 -3957 1975 C ATOM 556 O ILE A1072 25.010 4.224 1.837 1.00105.18 O ANISOU 556 O ILE A1072 13653 16050 10262 -3029 -4082 2005 O ATOM 557 CB ILE A1072 21.999 5.192 0.707 1.00 91.15 C ANISOU 557 CB ILE A1072 13016 13616 8000 -3238 -3092 1669 C ATOM 558 CG1 ILE A1072 20.844 4.499 -0.061 1.00 87.54 C ANISOU 558 CG1 ILE A1072 12748 12934 7578 -3000 -2724 1619 C ATOM 559 CG2 ILE A1072 23.041 5.720 -0.283 1.00 93.00 C ANISOU 559 CG2 ILE A1072 12737 14096 8503 -3366 -2979 1565 C ATOM 560 CD1 ILE A1072 20.058 5.403 -1.021 1.00 88.80 C ANISOU 560 CD1 ILE A1072 13057 13079 7604 -3109 -2328 1447 C ATOM 561 N ASP A1073 23.920 5.645 3.212 1.00 99.72 N ANISOU 561 N ASP A1073 13832 15305 8753 -3663 -4175 1905 N ATOM 562 CA ASP A1073 25.127 6.215 3.807 1.00104.96 C ANISOU 562 CA ASP A1073 14135 16375 9370 -3988 -4608 1882 C ATOM 563 C ASP A1073 25.929 5.136 4.548 1.00113.33 C ANISOU 563 C ASP A1073 14804 17751 10506 -3688 -5127 2259 C ATOM 564 O ASP A1073 27.162 5.143 4.490 1.00117.03 O ANISOU 564 O ASP A1073 14620 18626 11218 -3702 -5420 2295 O ATOM 565 CB ASP A1073 24.763 7.373 4.751 1.00108.43 C ANISOU 565 CB ASP A1073 15057 16847 9297 -4471 -4758 1599 C ATOM 566 CG ASP A1073 24.314 8.627 4.012 1.00117.64 C ANISOU 566 CG ASP A1073 16524 17614 10559 -4761 -4402 1247 C ATOM 567 OD1 ASP A1073 24.616 8.741 2.801 1.00118.66 O ANISOU 567 OD1 ASP A1073 16359 17636 11091 -4764 -4122 1316 O ATOM 568 OD2 ASP A1073 23.726 9.527 4.662 1.00121.12 O ANISOU 568 OD2 ASP A1073 17475 17879 10666 -4987 -4442 899 O ATOM 569 N ASP A1074 25.232 4.188 5.192 1.00110.51 N ANISOU 569 N ASP A1074 14797 17223 9966 -3418 -5254 2598 N ATOM 570 CA ASP A1074 25.871 3.071 5.885 1.00116.90 C ANISOU 570 CA ASP A1074 15340 18175 10900 -3073 -5807 3113 C ATOM 571 C ASP A1074 26.600 2.177 4.895 1.00120.22 C ANISOU 571 C ASP A1074 15186 18382 12109 -2476 -5777 3138 C ATOM 572 O ASP A1074 27.713 1.720 5.175 1.00126.31 O ANISOU 572 O ASP A1074 15373 19457 13161 -2169 -6259 3353 O ATOM 573 CB ASP A1074 24.832 2.261 6.671 1.00120.34 C ANISOU 573 CB ASP A1074 16357 18386 10980 -3027 -5896 3570 C ATOM 574 CG ASP A1074 24.247 3.000 7.861 1.00142.44 C ANISOU 574 CG ASP A1074 19591 21657 12872 -3547 -5996 3537 C ATOM 575 OD1 ASP A1074 24.999 3.767 8.518 1.00148.90 O ANISOU 575 OD1 ASP A1074 20211 23020 13344 -3856 -6347 3362 O ATOM 576 OD2 ASP A1074 23.076 2.733 8.205 1.00149.40 O ANISOU 576 OD2 ASP A1074 20959 22455 13350 -3658 -5765 3681 O ATOM 577 N ALA A1075 25.978 1.941 3.731 1.00110.34 N ANISOU 577 N ALA A1075 14047 16689 11188 -2275 -5222 2856 N ATOM 578 CA ALA A1075 26.575 1.140 2.671 1.00111.65 C ANISOU 578 CA ALA A1075 13677 16702 12042 -1692 -5090 2668 C ATOM 579 C ALA A1075 27.756 1.879 2.052 1.00116.97 C ANISOU 579 C ALA A1075 13557 18034 12852 -1796 -5002 2343 C ATOM 580 O ALA A1075 28.751 1.249 1.691 1.00122.78 O ANISOU 580 O ALA A1075 13570 19012 14069 -1276 -5158 2262 O ATOM 581 CB ALA A1075 25.536 0.813 1.619 1.00106.85 C ANISOU 581 CB ALA A1075 13415 15602 11580 -1585 -4521 2375 C ATOM 582 N LEU A1076 27.655 3.217 1.946 1.00109.21 N ANISOU 582 N LEU A1076 12685 17340 11470 -2474 -4772 2163 N ATOM 583 CA LEU A1076 28.731 4.046 1.415 1.00111.94 C ANISOU 583 CA LEU A1076 12324 18325 11881 -2815 -4700 1960 C ATOM 584 C LEU A1076 29.967 3.969 2.288 1.00124.43 C ANISOU 584 C LEU A1076 13267 20501 13509 -2812 -5324 2146 C ATOM 585 O LEU A1076 31.086 3.902 1.768 1.00129.60 O ANISOU 585 O LEU A1076 13000 21783 14460 -2683 -5341 2024 O ATOM 586 CB LEU A1076 28.301 5.512 1.278 1.00108.15 C ANISOU 586 CB LEU A1076 12259 17805 11027 -3611 -4451 1830 C ATOM 587 CG LEU A1076 27.705 5.998 -0.042 1.00107.72 C ANISOU 587 CG LEU A1076 12355 17581 10993 -3764 -3825 1653 C ATOM 588 CD1 LEU A1076 28.675 5.802 -1.229 1.00111.32 C ANISOU 588 CD1 LEU A1076 11908 18672 11718 -3668 -3537 1520 C ATOM 589 CD2 LEU A1076 26.386 5.502 -0.292 1.00104.47 C ANISOU 589 CD2 LEU A1076 12573 16608 10512 -3434 -3536 1621 C ATOM 590 N LYS A1077 29.770 3.981 3.619 1.00122.95 N ANISOU 590 N LYS A1077 13495 20261 12959 -2967 -5839 2435 N ATOM 591 CA LYS A1077 30.875 3.884 4.563 1.00131.37 C ANISOU 591 CA LYS A1077 13982 21971 13963 -2981 -6533 2671 C ATOM 592 C LYS A1077 31.629 2.584 4.336 1.00142.23 C ANISOU 592 C LYS A1077 14652 23451 15939 -2061 -6800 2870 C ATOM 593 O LYS A1077 32.855 2.579 4.293 1.00149.16 O ANISOU 593 O LYS A1077 14568 25063 17045 -1928 -7095 2839 O ATOM 594 CB LYS A1077 30.367 3.977 6.004 1.00134.94 C ANISOU 594 CB LYS A1077 15077 22396 13798 -3257 -7012 2966 C ATOM 595 CG LYS A1077 31.506 4.024 7.014 1.00160.88 C ANISOU 595 CG LYS A1077 17759 26495 16874 -3396 -7787 3202 C ATOM 596 CD LYS A1077 31.021 4.108 8.453 1.00174.74 C ANISOU 596 CD LYS A1077 20119 28417 17859 -3712 -8265 3479 C ATOM 597 CE LYS A1077 32.165 4.245 9.450 1.00193.48 C ANISOU 597 CE LYS A1077 21861 31742 19910 -3938 -9084 3683 C ATOM 598 NZ LYS A1077 33.091 3.075 9.462 1.00206.62 N ANISOU 598 NZ LYS A1077 22755 33633 22121 -3056 -9568 4165 N ATOM 599 N LEU A1078 30.884 1.490 4.155 1.00137.45 N ANISOU 599 N LEU A1078 14501 22089 15633 -1422 -6700 3032 N ATOM 600 CA LEU A1078 31.453 0.171 3.905 1.00144.22 C ANISOU 600 CA LEU A1078 14857 22742 17197 -432 -6969 3156 C ATOM 601 C LEU A1078 32.248 0.156 2.605 1.00151.59 C ANISOU 601 C LEU A1078 14869 24112 18616 -67 -6532 2569 C ATOM 602 O LEU A1078 33.391 -0.302 2.592 1.00160.19 O ANISOU 602 O LEU A1078 15008 25733 20125 519 -6877 2539 O ATOM 603 CB LEU A1078 30.337 -0.881 3.858 1.00141.27 C ANISOU 603 CB LEU A1078 15310 21299 17067 -18 -6879 3369 C ATOM 604 CG LEU A1078 29.606 -1.125 5.173 1.00146.06 C ANISOU 604 CG LEU A1078 16712 21588 17196 -305 -7342 4072 C ATOM 605 CD1 LEU A1078 28.340 -1.906 4.949 1.00141.90 C ANISOU 605 CD1 LEU A1078 17011 20097 16809 -209 -7072 4212 C ATOM 606 CD2 LEU A1078 30.509 -1.829 6.182 1.00160.44 C ANISOU 606 CD2 LEU A1078 18148 23633 19179 156 -8241 4732 C ATOM 607 N ALA A1079 31.658 0.681 1.522 1.00142.31 N ANISOU 607 N ALA A1079 13906 22842 17324 -412 -5782 2114 N ATOM 608 CA ALA A1079 32.311 0.746 0.215 1.00145.25 C ANISOU 608 CA ALA A1079 13427 23800 17962 -203 -5266 1554 C ATOM 609 C ALA A1079 33.575 1.598 0.278 1.00157.19 C ANISOU 609 C ALA A1079 13931 26474 19319 -663 -5401 1526 C ATOM 610 O ALA A1079 34.583 1.252 -0.342 1.00164.38 O ANISOU 610 O ALA A1079 13753 28136 20569 -184 -5310 1206 O ATOM 611 CB ALA A1079 31.351 1.308 -0.816 1.00137.55 C ANISOU 611 CB ALA A1079 12970 22596 16696 -673 -4521 1246 C ATOM 612 N ASN A1080 33.538 2.690 1.058 1.00153.29 N ANISOU 612 N ASN A1080 13755 26168 18320 -1593 -5638 1806 N ATOM 613 CA ASN A1080 34.690 3.573 1.207 1.00160.48 C ANISOU 613 CA ASN A1080 13785 28123 19066 -2239 -5834 1801 C ATOM 614 C ASN A1080 35.819 2.910 1.997 1.00176.17 C ANISOU 614 C ASN A1080 14868 30749 21319 -1665 -6563 1998 C ATOM 615 O ASN A1080 36.963 3.366 1.923 1.00183.54 O ANISOU 615 O ASN A1080 14726 32764 22249 -1990 -6705 1916 O ATOM 616 CB ASN A1080 34.298 4.868 1.879 1.00159.10 C ANISOU 616 CB ASN A1080 14300 27803 18348 -3359 -5964 1946 C ATOM 617 CG ASN A1080 34.282 6.023 0.916 1.00180.28 C ANISOU 617 CG ASN A1080 16943 30687 20866 -4241 -5400 1760 C ATOM 618 OD1 ASN A1080 33.228 6.430 0.412 1.00163.90 O ANISOU 618 OD1 ASN A1080 15711 27918 18644 -4467 -4948 1710 O ATOM 619 ND2 ASN A1080 35.468 6.539 0.593 1.00180.96 N ANISOU 619 ND2 ASN A1080 15981 31790 20987 -4753 -5429 1713 N ATOM 620 N GLU A1081 35.506 1.836 2.732 1.00174.66 N ANISOU 620 N GLU A1081 15069 29931 21363 -845 -7050 2316 N ATOM 621 CA GLU A1081 36.493 1.080 3.496 1.00185.41 C ANISOU 621 CA GLU A1081 15644 31770 23033 -132 -7837 2627 C ATOM 622 C GLU A1081 37.006 -0.109 2.671 1.00196.71 C ANISOU 622 C GLU A1081 16301 33168 25270 1153 -7716 2316 C ATOM 623 O GLU A1081 37.867 -0.859 3.137 1.00206.86 O ANISOU 623 O GLU A1081 16823 34788 26987 1998 -8358 2524 O ATOM 624 CB GLU A1081 35.896 0.604 4.826 1.00186.44 C ANISOU 624 CB GLU A1081 16661 31253 22927 -14 -8523 3283 C ATOM 625 CG GLU A1081 35.499 1.737 5.758 1.00192.55 C ANISOU 625 CG GLU A1081 18075 32231 22854 -1174 -8706 3448 C ATOM 626 CD GLU A1081 34.918 1.292 7.086 1.00214.08 C ANISOU 626 CD GLU A1081 21596 34584 25161 -1132 -9334 4083 C ATOM 627 OE1 GLU A1081 34.007 0.430 7.087 1.00205.98 O ANISOU 627 OE1 GLU A1081 21331 32614 24318 -644 -9233 4364 O ATOM 628 OE2 GLU A1081 35.333 1.853 8.125 1.00210.72 O ANISOU 628 OE2 GLU A1081 21148 34727 24190 -1569 -9828 4105 O ATOM 629 N GLY A1082 36.478 -0.254 1.453 1.00188.70 N ANISOU 629 N GLY A1082 15471 31786 24439 1319 -6924 1779 N ATOM 630 CA GLY A1082 36.853 -1.319 0.529 1.00195.16 C ANISOU 630 CA GLY A1082 15634 32548 25969 2501 -6681 1243 C ATOM 631 C GLY A1082 36.105 -2.618 0.748 1.00199.85 C ANISOU 631 C GLY A1082 17072 31726 27137 3446 -6958 1386 C ATOM 632 O GLY A1082 36.434 -3.635 0.130 1.00206.75 O ANISOU 632 O GLY A1082 17484 32334 28736 4571 -6911 906 O ATOM 633 N LYS A1083 35.080 -2.591 1.610 1.00189.96 N ANISOU 633 N LYS A1083 17054 29557 25566 2967 -7233 2005 N ATOM 634 CA LYS A1083 34.291 -3.773 1.951 1.00190.78 C ANISOU 634 CA LYS A1083 18060 28285 26145 3610 -7554 2332 C ATOM 635 C LYS A1083 33.175 -3.987 0.930 1.00187.29 C ANISOU 635 C LYS A1083 18352 27049 25761 3508 -6809 1801 C ATOM 636 O LYS A1083 32.001 -3.773 1.239 1.00178.26 O ANISOU 636 O LYS A1083 18263 25272 24196 2848 -6670 2120 O ATOM 637 CB LYS A1083 33.712 -3.628 3.362 1.00190.91 C ANISOU 637 CB LYS A1083 18953 27935 25649 3030 -8158 3276 C ATOM 638 CG LYS A1083 34.773 -3.390 4.423 1.00214.83 C ANISOU 638 CG LYS A1083 21283 31855 28486 3041 -8959 3814 C ATOM 639 CD LYS A1083 34.163 -3.227 5.804 1.00223.92 C ANISOU 639 CD LYS A1083 23304 32816 28960 2408 -9512 4686 C ATOM 640 CE LYS A1083 35.205 -2.963 6.871 1.00235.46 C ANISOU 640 CE LYS A1083 24638 35214 29613 3006 -9577 3941 C ATOM 641 NZ LYS A1083 36.190 -4.068 6.996 1.00246.20 N ANISOU 641 NZ LYS A1083 25945 36447 31152 4320 -9081 3255 N ATOM 642 N VAL A1084 33.546 -4.437 -0.279 1.00188.41 N ANISOU 642 N VAL A1084 17868 27332 26389 4186 -6342 948 N ATOM 643 CA VAL A1084 32.615 -4.679 -1.389 1.00182.93 C ANISOU 643 CA VAL A1084 17696 26085 25723 4140 -5641 301 C ATOM 644 C VAL A1084 31.471 -5.612 -0.965 1.00185.91 C ANISOU 644 C VAL A1084 19274 24933 26429 4268 -5923 664 C ATOM 645 O VAL A1084 30.307 -5.241 -1.092 1.00176.04 O ANISOU 645 O VAL A1084 18864 23328 24695 3506 -5553 754 O ATOM 646 CB VAL A1084 33.331 -5.270 -2.623 1.00195.24 C ANISOU 646 CB VAL A1084 18312 28059 27811 5065 -5237 -742 C ATOM 647 CG1 VAL A1084 32.346 -5.495 -3.765 1.00189.88 C ANISOU 647 CG1 VAL A1084 18181 26930 27035 4931 -4544 -1450 C ATOM 648 CG2 VAL A1084 34.472 -4.377 -3.073 1.00198.34 C ANISOU 648 CG2 VAL A1084 17408 30126 27825 4844 -4914 -1050 C ATOM 649 N LYS A1085 31.803 -6.822 -0.500 1.00193.32 N ANISOU 649 N LYS A1085 20256 24978 28218 5222 -6587 885 N ATOM 650 CA LYS A1085 30.816 -7.823 -0.109 1.00194.34 C ANISOU 650 CA LYS A1085 21487 23575 28777 5318 -6928 1304 C ATOM 651 C LYS A1085 29.848 -7.276 0.949 1.00190.75 C ANISOU 651 C LYS A1085 21956 22980 27541 4231 -7092 2288 C ATOM 652 O LYS A1085 28.641 -7.483 0.814 1.00184.32 O ANISOU 652 O LYS A1085 22018 21440 26575 3723 -6836 2349 O ATOM 653 CB LYS A1085 31.515 -9.088 0.424 1.00211.17 C ANISOU 653 CB LYS A1085 23475 24790 31968 6494 -7796 1633 C ATOM 654 CG LYS A1085 30.585 -10.159 1.016 1.00221.11 C ANISOU 654 CG LYS A1085 25938 24937 33136 6364 -7486 2518 C ATOM 655 CD LYS A1085 29.552 -10.702 0.024 1.00225.13 C ANISOU 655 CD LYS A1085 27124 24719 33695 6122 -6570 1898 C ATOM 656 CE LYS A1085 28.602 -11.694 0.658 1.00231.84 C ANISOU 656 CE LYS A1085 29091 24876 34121 5826 -5789 2769 C ATOM 657 NZ LYS A1085 27.769 -11.084 1.735 1.00232.79 N ANISOU 657 NZ LYS A1085 29792 25180 33478 4889 -6087 3563 N ATOM 658 N GLU A1086 30.365 -6.602 1.994 1.00188.93 N ANISOU 658 N GLU A1086 21479 23519 26786 3876 -7516 2989 N ATOM 659 CA GLU A1086 29.507 -6.053 3.043 1.00182.90 C ANISOU 659 CA GLU A1086 21506 22799 25190 2898 -7655 3797 C ATOM 660 C GLU A1086 28.603 -4.967 2.505 1.00176.14 C ANISOU 660 C GLU A1086 20978 22377 23570 1979 -6851 3361 C ATOM 661 O GLU A1086 27.439 -4.909 2.897 1.00170.60 O ANISOU 661 O GLU A1086 21107 21282 22433 1361 -6729 3711 O ATOM 662 CB GLU A1086 30.305 -5.496 4.217 1.00187.99 C ANISOU 662 CB GLU A1086 21756 24319 25351 2694 -8265 4458 C ATOM 663 CG GLU A1086 30.931 -6.552 5.101 1.00211.24 C ANISOU 663 CG GLU A1086 24613 26796 28852 3442 -9237 5275 C ATOM 664 CD GLU A1086 31.450 -5.984 6.407 1.00228.35 C ANISOU 664 CD GLU A1086 26702 30383 29678 3398 -8982 5484 C ATOM 665 OE1 GLU A1086 30.641 -5.401 7.166 1.00222.32 O ANISOU 665 OE1 GLU A1086 26557 29621 28295 2363 -9272 6065 O ATOM 666 OE2 GLU A1086 32.647 -6.190 6.706 1.00227.45 O ANISOU 666 OE2 GLU A1086 25813 30881 29727 4110 -9428 5541 O ATOM 667 N ALA A1087 29.129 -4.105 1.615 1.00170.17 N ANISOU 667 N ALA A1087 19541 22471 22643 1880 -6320 2650 N ATOM 668 CA ALA A1087 28.346 -3.026 1.019 1.00159.81 C ANISOU 668 CA ALA A1087 18507 21534 20678 1079 -5612 2291 C ATOM 669 C ALA A1087 27.249 -3.601 0.138 1.00160.70 C ANISOU 669 C ALA A1087 19171 20906 20982 1122 -5146 1903 C ATOM 670 O ALA A1087 26.122 -3.112 0.173 1.00152.69 O ANISOU 670 O ALA A1087 18788 19780 19448 475 -4831 2002 O ATOM 671 CB ALA A1087 29.243 -2.101 0.220 1.00160.14 C ANISOU 671 CB ALA A1087 17677 22598 20571 957 -5224 1755 C ATOM 672 N GLN A1088 27.560 -4.671 -0.616 1.00164.20 N ANISOU 672 N GLN A1088 19360 20846 22184 1913 -5142 1416 N ATOM 673 CA GLN A1088 26.579 -5.329 -1.473 1.00162.42 C ANISOU 673 CA GLN A1088 19630 19896 22187 1952 -4771 943 C ATOM 674 C GLN A1088 25.472 -5.936 -0.633 1.00166.76 C ANISOU 674 C GLN A1088 21139 19487 22738 1591 -5096 1624 C ATOM 675 O GLN A1088 24.301 -5.820 -0.993 1.00160.50 O ANISOU 675 O GLN A1088 20871 18497 21613 1049 -4710 1506 O ATOM 676 CB GLN A1088 27.234 -6.399 -2.341 1.00172.99 C ANISOU 676 CB GLN A1088 20502 20839 24389 2935 -4786 177 C ATOM 677 CG GLN A1088 28.202 -5.846 -3.374 1.00184.04 C ANISOU 677 CG GLN A1088 20870 23386 25670 3228 -4303 -622 C ATOM 678 CD GLN A1088 28.830 -6.946 -4.190 1.00210.25 C ANISOU 678 CD GLN A1088 23683 26390 29813 4301 -4297 -1522 C ATOM 679 OE1 GLN A1088 29.476 -7.861 -3.660 1.00216.20 O ANISOU 679 OE1 GLN A1088 24283 26485 31379 5161 -4905 -1394 O ATOM 680 NE2 GLN A1088 28.703 -6.849 -5.508 1.00199.23 N ANISOU 680 NE2 GLN A1088 21963 25532 28203 4321 -3625 -2480 N ATOM 681 N ALA A1089 25.839 -6.561 0.499 1.00171.10 N ANISOU 681 N ALA A1089 21862 19549 23597 1842 -5820 2401 N ATOM 682 CA ALA A1089 24.876 -7.155 1.420 1.00172.52 C ANISOU 682 CA ALA A1089 22907 18944 23701 1401 -6180 3234 C ATOM 683 C ALA A1089 23.977 -6.085 2.003 1.00168.13 C ANISOU 683 C ALA A1089 22710 19082 22089 430 -5878 3596 C ATOM 684 O ALA A1089 22.767 -6.280 2.085 1.00164.28 O ANISOU 684 O ALA A1089 22832 18246 21343 -123 -5686 3788 O ATOM 685 CB ALA A1089 25.600 -7.901 2.527 1.00183.78 C ANISOU 685 CB ALA A1089 24350 19925 25552 1852 -7059 4109 C ATOM 686 N ALA A1090 24.569 -4.931 2.368 1.00162.64 N ANISOU 686 N ALA A1090 21594 19395 20808 224 -5826 3604 N ATOM 687 CA ALA A1090 23.839 -3.790 2.914 1.00155.56 C ANISOU 687 CA ALA A1090 20985 19163 18957 -577 -5552 3771 C ATOM 688 C ALA A1090 22.831 -3.270 1.913 1.00151.83 C ANISOU 688 C ALA A1090 20698 18753 18237 -922 -4834 3180 C ATOM 689 O ALA A1090 21.706 -2.983 2.302 1.00147.48 O ANISOU 689 O ALA A1090 20628 18261 17147 -1467 -4640 3388 O ATOM 690 CB ALA A1090 24.802 -2.677 3.309 1.00155.67 C ANISOU 690 CB ALA A1090 20484 20095 18569 -688 -5661 3707 C ATOM 691 N ALA A1091 23.209 -3.190 0.621 1.00147.42 N ANISOU 691 N ALA A1091 19710 18274 18031 -590 -4448 2457 N ATOM 692 CA ALA A1091 22.327 -2.692 -0.436 1.00140.78 C ANISOU 692 CA ALA A1091 18974 17596 16920 -882 -3814 1932 C ATOM 693 C ALA A1091 21.103 -3.590 -0.630 1.00145.54 C ANISOU 693 C ALA A1091 20121 17521 17656 -1045 -3725 1955 C ATOM 694 O ALA A1091 20.045 -3.091 -0.996 1.00139.01 O ANISOU 694 O ALA A1091 19521 16918 16380 -1476 -3324 1809 O ATOM 695 CB ALA A1091 23.086 -2.583 -1.742 1.00142.38 C ANISOU 695 CB ALA A1091 18555 18134 17410 -496 -3479 1223 C ATOM 696 N GLU A1092 21.234 -4.897 -0.353 1.00150.85 N ANISOU 696 N GLU A1092 21000 17348 18969 -726 -4145 2177 N ATOM 697 CA GLU A1092 20.139 -5.862 -0.484 1.00153.55 C ANISOU 697 CA GLU A1092 21882 16919 19540 -989 -4150 2250 C ATOM 698 C GLU A1092 19.020 -5.560 0.526 1.00154.73 C ANISOU 698 C GLU A1092 22510 17277 19002 -1749 -4156 2951 C ATOM 699 O GLU A1092 17.888 -5.983 0.301 1.00153.96 O ANISOU 699 O GLU A1092 22750 16912 18835 -2194 -3979 2947 O ATOM 700 CB GLU A1092 20.686 -7.298 -0.281 1.00166.04 C ANISOU 700 CB GLU A1092 23626 17384 22076 -460 -4726 2437 C ATOM 701 CG GLU A1092 19.728 -8.477 -0.479 1.00184.98 C ANISOU 701 CG GLU A1092 26616 18718 24950 -733 -4844 2477 C ATOM 702 CD GLU A1092 18.745 -8.820 0.631 1.00212.40 C ANISOU 702 CD GLU A1092 30706 21899 28099 -1517 -5109 3487 C ATOM 703 OE1 GLU A1092 19.027 -8.501 1.810 1.00207.04 O ANISOU 703 OE1 GLU A1092 30074 21587 27004 -1663 -5428 4326 O ATOM 704 OE2 GLU A1092 17.739 -9.502 0.330 1.00211.26 O ANISOU 704 OE2 GLU A1092 30973 21167 28128 -2011 -5039 3447 O ATOM 705 N GLN A1093 19.321 -4.815 1.606 1.00150.23 N ANISOU 705 N GLN A1093 21907 17297 17877 -1926 -4337 3469 N ATOM 706 CA GLN A1093 18.361 -4.514 2.672 1.00149.22 C ANISOU 706 CA GLN A1093 22147 17553 16995 -2586 -4335 4069 C ATOM 707 C GLN A1093 17.557 -3.224 2.367 1.00144.44 C ANISOU 707 C GLN A1093 21453 17761 15667 -2915 -3754 3623 C ATOM 708 O GLN A1093 16.602 -2.934 3.089 1.00143.32 O ANISOU 708 O GLN A1093 21533 18044 14877 -3405 -3630 3918 O ATOM 709 CB GLN A1093 19.101 -4.373 4.021 1.00155.27 C ANISOU 709 CB GLN A1093 22916 18632 17448 -2591 -4857 4763 C ATOM 710 CG GLN A1093 18.240 -4.305 5.301 1.00177.58 C ANISOU 710 CG GLN A1093 26106 21926 19438 -3261 -4951 5480 C ATOM 711 CD GLN A1093 17.493 -5.578 5.661 1.00209.23 C ANISOU 711 CD GLN A1093 30563 25286 23648 -3653 -5191 6211 C ATOM 712 OE1 GLN A1093 17.700 -6.665 5.094 1.00210.64 O ANISOU 712 OE1 GLN A1093 30883 24422 24727 -3380 -5436 6264 O ATOM 713 NE2 GLN A1093 16.651 -5.477 6.675 1.00205.67 N ANISOU 713 NE2 GLN A1093 30342 25452 22351 -4330 -5157 6803 N ATOM 714 N LEU A1094 17.906 -2.482 1.304 1.00135.86 N ANISOU 714 N LEU A1094 20028 16908 14683 -2640 -3409 2950 N ATOM 715 CA LEU A1094 17.180 -1.262 0.934 1.00129.42 C ANISOU 715 CA LEU A1094 19161 16702 13308 -2862 -2941 2594 C ATOM 716 C LEU A1094 15.760 -1.570 0.492 1.00133.80 C ANISOU 716 C LEU A1094 19893 17258 13687 -3178 -2620 2495 C ATOM 717 O LEU A1094 14.834 -0.847 0.845 1.00131.49 O ANISOU 717 O LEU A1094 19670 17478 12813 -3449 -2383 2510 O ATOM 718 CB LEU A1094 17.904 -0.523 -0.188 1.00125.99 C ANISOU 718 CB LEU A1094 18344 16466 13061 -2566 -2701 2056 C ATOM 719 CG LEU A1094 19.298 -0.022 0.122 1.00131.92 C ANISOU 719 CG LEU A1094 18783 17405 13934 -2357 -2954 2086 C ATOM 720 CD1 LEU A1094 19.928 0.575 -1.102 1.00130.33 C ANISOU 720 CD1 LEU A1094 18159 17468 13893 -2192 -2664 1622 C ATOM 721 CD2 LEU A1094 19.266 0.999 1.217 1.00132.58 C ANISOU 721 CD2 LEU A1094 19020 17889 13464 -2651 -3079 2298 C ATOM 722 N LYS A1095 15.595 -2.654 -0.273 1.00133.45 N ANISOU 722 N LYS A1095 19883 16661 14160 -3125 -2634 2330 N ATOM 723 CA LYS A1095 14.315 -3.122 -0.803 1.00133.53 C ANISOU 723 CA LYS A1095 20007 16641 14088 -3494 -2394 2187 C ATOM 724 C LYS A1095 13.309 -3.330 0.337 1.00140.14 C ANISOU 724 C LYS A1095 21098 17696 14453 -4064 -2451 2784 C ATOM 725 O LYS A1095 12.121 -3.066 0.163 1.00139.37 O ANISOU 725 O LYS A1095 20935 18087 13933 -4413 -2141 2683 O ATOM 726 CB LYS A1095 14.525 -4.435 -1.590 1.00141.20 C ANISOU 726 CB LYS A1095 21055 16793 15803 -3368 -2550 1903 C ATOM 727 CG LYS A1095 15.674 -4.384 -2.614 1.00153.97 C ANISOU 727 CG LYS A1095 22337 18303 17861 -2747 -2501 1279 C ATOM 728 CD LYS A1095 15.863 -5.694 -3.371 1.00170.42 C ANISOU 728 CD LYS A1095 24496 19569 20688 -2531 -2648 811 C ATOM 729 CE LYS A1095 16.993 -5.596 -4.368 1.00178.74 C ANISOU 729 CE LYS A1095 25098 20765 22049 -1884 -2522 104 C ATOM 730 NZ LYS A1095 17.146 -6.844 -5.157 1.00194.31 N ANISOU 730 NZ LYS A1095 27125 21976 24729 -1588 -2632 -567 N ATOM 731 N THR A1096 13.793 -3.779 1.505 1.00139.83 N ANISOU 731 N THR A1096 21279 17428 14420 -4160 -2850 3428 N ATOM 732 CA THR A1096 12.954 -4.026 2.669 1.00143.27 C ANISOU 732 CA THR A1096 21925 18213 14299 -4767 -2916 4093 C ATOM 733 C THR A1096 12.305 -2.722 3.129 1.00141.03 C ANISOU 733 C THR A1096 21448 19002 13137 -4865 -2538 3898 C ATOM 734 O THR A1096 11.109 -2.706 3.409 1.00141.26 O ANISOU 734 O THR A1096 21424 19595 12653 -5327 -2275 4004 O ATOM 735 CB THR A1096 13.785 -4.657 3.783 1.00163.11 C ANISOU 735 CB THR A1096 24683 20364 16930 -4779 -3476 4866 C ATOM 736 OG1 THR A1096 14.411 -5.840 3.289 1.00169.51 O ANISOU 736 OG1 THR A1096 25667 20043 18695 -4522 -3861 4962 O ATOM 737 CG2 THR A1096 12.964 -5.014 4.986 1.00169.67 C ANISOU 737 CG2 THR A1096 25728 21638 17102 -5501 -3563 5673 C ATOM 738 N THR A1097 13.087 -1.633 3.199 1.00133.49 N ANISOU 738 N THR A1097 20358 18320 12040 -4434 -2521 3574 N ATOM 739 CA THR A1097 12.573 -0.331 3.628 1.00130.67 C ANISOU 739 CA THR A1097 19882 18788 10979 -4418 -2223 3268 C ATOM 740 C THR A1097 11.608 0.242 2.606 1.00129.05 C ANISOU 740 C THR A1097 19467 18836 10730 -4315 -1779 2743 C ATOM 741 O THR A1097 10.550 0.760 2.983 1.00129.50 O ANISOU 741 O THR A1097 19407 19583 10215 -4454 -1498 2629 O ATOM 742 CB THR A1097 13.710 0.649 3.866 1.00140.31 C ANISOU 742 CB THR A1097 21068 20045 12198 -4059 -2387 3029 C ATOM 743 OG1 THR A1097 14.575 0.111 4.868 1.00144.81 O ANISOU 743 OG1 THR A1097 21763 20526 12733 -4154 -2856 3552 O ATOM 744 CG2 THR A1097 13.208 2.039 4.292 1.00139.10 C ANISOU 744 CG2 THR A1097 20875 20543 11434 -3995 -2129 2592 C ATOM 745 N ARG A1098 11.972 0.157 1.320 1.00120.82 N ANISOU 745 N ARG A1098 18323 17344 10241 -4042 -1724 2417 N ATOM 746 CA ARG A1098 11.153 0.686 0.242 1.00116.56 C ANISOU 746 CA ARG A1098 17564 17078 9646 -3925 -1380 1993 C ATOM 747 C ARG A1098 9.780 0.042 0.232 1.00121.84 C ANISOU 747 C ARG A1098 18132 18096 10066 -4351 -1204 2090 C ATOM 748 O ARG A1098 8.792 0.760 0.155 1.00120.95 O ANISOU 748 O ARG A1098 17790 18631 9533 -4307 -931 1889 O ATOM 749 CB ARG A1098 11.817 0.491 -1.118 1.00114.40 C ANISOU 749 CB ARG A1098 17180 16388 9900 -3665 -1373 1683 C ATOM 750 CG ARG A1098 13.197 1.119 -1.219 1.00125.05 C ANISOU 750 CG ARG A1098 18502 17525 11486 -3327 -1512 1599 C ATOM 751 CD ARG A1098 13.665 1.296 -2.653 1.00136.49 C ANISOU 751 CD ARG A1098 19719 18932 13211 -3097 -1366 1244 C ATOM 752 NE ARG A1098 13.622 0.056 -3.421 1.00142.59 N ANISOU 752 NE ARG A1098 20430 19405 14342 -3131 -1372 1045 N ATOM 753 CZ ARG A1098 13.947 -0.026 -4.703 1.00148.68 C ANISOU 753 CZ ARG A1098 20963 20262 15265 -2968 -1220 644 C ATOM 754 NH1 ARG A1098 14.357 1.052 -5.360 1.00130.84 N ANISOU 754 NH1 ARG A1098 18501 18397 12815 -2821 -1058 555 N ATOM 755 NH2 ARG A1098 13.869 -1.186 -5.339 1.00137.03 N ANISOU 755 NH2 ARG A1098 19465 18486 14113 -2989 -1242 320 N ATOM 756 N ASN A1099 9.718 -1.300 0.347 1.00121.57 N ANISOU 756 N ASN A1099 18251 17619 10319 -4770 -1392 2414 N ATOM 757 CA ASN A1099 8.480 -2.088 0.336 1.00125.19 C ANISOU 757 CA ASN A1099 18624 18328 10616 -5373 -1282 2577 C ATOM 758 C ASN A1099 7.558 -1.696 1.513 1.00131.18 C ANISOU 758 C ASN A1099 19238 20009 10595 -5716 -1099 2883 C ATOM 759 O ASN A1099 6.357 -1.513 1.300 1.00132.51 O ANISOU 759 O ASN A1099 19050 20909 10388 -5939 -807 2725 O ATOM 760 CB ASN A1099 8.834 -3.585 0.396 1.00132.17 C ANISOU 760 CB ASN A1099 19838 18295 12084 -5770 -1635 2946 C ATOM 761 CG ASN A1099 7.724 -4.600 0.487 1.00168.50 C ANISOU 761 CG ASN A1099 24459 22912 16651 -6588 -1638 3245 C ATOM 762 OD1 ASN A1099 6.565 -4.353 0.136 1.00166.55 O ANISOU 762 OD1 ASN A1099 23855 23420 16007 -6893 -1334 3031 O ATOM 763 ND2 ASN A1099 8.093 -5.814 0.868 1.00166.90 N ANISOU 763 ND2 ASN A1099 24664 21796 16955 -6960 -2031 3746 N ATOM 764 N ALA A1100 8.114 -1.542 2.729 1.00127.74 N ANISOU 764 N ALA A1100 19003 19676 9856 -5737 -1262 3265 N ATOM 765 CA ALA A1100 7.317 -1.248 3.918 1.00131.23 C ANISOU 765 CA ALA A1100 19290 21125 9447 -6092 -1073 3515 C ATOM 766 C ALA A1100 6.890 0.231 4.014 1.00130.22 C ANISOU 766 C ALA A1100 18856 21814 8809 -5556 -730 2885 C ATOM 767 O ALA A1100 5.788 0.510 4.507 1.00133.56 O ANISOU 767 O ALA A1100 18923 23249 8576 -5746 -410 2797 O ATOM 768 CB ALA A1100 8.105 -1.611 5.156 1.00136.49 C ANISOU 768 CB ALA A1100 20279 21693 9886 -6310 -1414 4129 C ATOM 769 N TYR A1101 7.746 1.169 3.587 1.00120.22 N ANISOU 769 N TYR A1101 17706 20123 7848 -4905 -807 2452 N ATOM 770 CA TYR A1101 7.414 2.580 3.764 1.00119.00 C ANISOU 770 CA TYR A1101 17382 20507 7324 -4387 -575 1879 C ATOM 771 C TYR A1101 6.820 3.245 2.501 1.00119.84 C ANISOU 771 C TYR A1101 17226 20594 7714 -3935 -371 1434 C ATOM 772 O TYR A1101 5.818 3.970 2.610 1.00122.46 O ANISOU 772 O TYR A1101 17229 21636 7665 -3663 -103 1085 O ATOM 773 CB TYR A1101 8.661 3.356 4.173 1.00118.14 C ANISOU 773 CB TYR A1101 17584 19969 7335 -4043 -827 1708 C ATOM 774 N ILE A1102 7.438 3.038 1.326 1.00111.14 N ANISOU 774 N ILE A1102 16226 18773 7228 -3806 -508 1434 N ATOM 775 CA ILE A1102 7.038 3.773 0.127 1.00107.74 C ANISOU 775 CA ILE A1102 15587 18359 6991 -3377 -384 1109 C ATOM 776 C ILE A1102 6.123 2.962 -0.790 1.00111.76 C ANISOU 776 C ILE A1102 15775 19147 7543 -3668 -273 1148 C ATOM 777 O ILE A1102 5.229 3.562 -1.376 1.00112.45 O ANISOU 777 O ILE A1102 15515 19736 7474 -3383 -122 931 O ATOM 778 CB ILE A1102 8.269 4.242 -0.694 1.00106.31 C ANISOU 778 CB ILE A1102 15638 17442 7313 -3082 -566 1049 C ATOM 779 CG1 ILE A1102 9.221 5.117 0.120 1.00106.05 C ANISOU 779 CG1 ILE A1102 15894 17116 7283 -2878 -723 971 C ATOM 780 CG2 ILE A1102 7.855 4.988 -1.931 1.00106.01 C ANISOU 780 CG2 ILE A1102 15408 17485 7387 -2717 -475 871 C ATOM 781 CD1 ILE A1102 10.093 4.391 1.017 1.00107.82 C ANISOU 781 CD1 ILE A1102 16324 17126 7517 -3192 -943 1234 C ATOM 782 N GLN A1103 6.350 1.654 -0.963 1.00108.19 N ANISOU 782 N GLN A1103 15436 18333 7341 -4193 -396 1389 N ATOM 783 CA GLN A1103 5.593 0.833 -1.919 1.00108.79 C ANISOU 783 CA GLN A1103 15261 18552 7520 -4551 -349 1319 C ATOM 784 C GLN A1103 4.068 0.965 -1.753 1.00112.65 C ANISOU 784 C GLN A1103 15237 20065 7500 -4757 -112 1274 C ATOM 785 O GLN A1103 3.374 1.030 -2.759 1.00111.81 O ANISOU 785 O GLN A1103 14774 20341 7369 -4715 -53 1053 O ATOM 786 CB GLN A1103 5.969 -0.639 -1.792 1.00113.42 C ANISOU 786 CB GLN A1103 16126 18493 8474 -5148 -557 1577 C ATOM 787 CG GLN A1103 5.412 -1.536 -2.893 1.00137.33 C ANISOU 787 CG GLN A1103 18999 21444 11735 -5540 -579 1351 C ATOM 788 CD GLN A1103 5.934 -1.134 -4.250 1.00158.08 C ANISOU 788 CD GLN A1103 21561 23917 14586 -5068 -577 898 C ATOM 789 OE1 GLN A1103 7.142 -1.156 -4.538 1.00148.24 O ANISOU 789 OE1 GLN A1103 20568 22037 13718 -4744 -696 797 O ATOM 790 NE2 GLN A1103 5.020 -0.778 -5.122 1.00158.12 N ANISOU 790 NE2 GLN A1103 21154 24622 14302 -5050 -447 644 N ATOM 791 N LYS A1104 3.556 1.039 -0.516 1.00110.85 N ANISOU 791 N LYS A1104 14896 20418 6805 -4964 24 1461 N ATOM 792 CA LYS A1104 2.119 1.155 -0.267 1.00114.90 C ANISOU 792 CA LYS A1104 14788 22093 6775 -5158 296 1391 C ATOM 793 C LYS A1104 1.522 2.438 -0.891 1.00114.09 C ANISOU 793 C LYS A1104 14260 22541 6548 -4329 433 944 C ATOM 794 O LYS A1104 0.306 2.495 -1.069 1.00117.88 O ANISOU 794 O LYS A1104 14095 23999 6693 -4383 610 823 O ATOM 795 CB LYS A1104 1.819 1.134 1.249 1.00123.28 C ANISOU 795 CB LYS A1104 15779 23822 7241 -5458 464 1623 C ATOM 796 CG LYS A1104 2.416 2.272 2.084 1.00140.16 C ANISOU 796 CG LYS A1104 18133 25969 9154 -4782 502 1370 C ATOM 797 CD LYS A1104 2.095 2.080 3.570 1.00159.86 C ANISOU 797 CD LYS A1104 20523 29306 10909 -5213 674 1587 C ATOM 798 CE LYS A1104 2.593 3.192 4.471 1.00173.81 C ANISOU 798 CE LYS A1104 22471 31226 12344 -4601 714 1186 C ATOM 799 NZ LYS A1104 4.074 3.331 4.465 1.00178.76 N ANISOU 799 NZ LYS A1104 23768 30698 13454 -4410 343 1284 N ATOM 800 N TYR A1105 2.374 3.431 -1.255 1.00103.45 N ANISOU 800 N TYR A1105 13248 20555 5503 -3601 309 757 N ATOM 801 CA TYR A1105 1.922 4.702 -1.820 1.00102.79 C ANISOU 801 CA TYR A1105 12897 20746 5412 -2776 342 453 C ATOM 802 C TYR A1105 2.057 4.787 -3.342 1.00102.87 C ANISOU 802 C TYR A1105 12873 20474 5741 -2609 172 482 C ATOM 803 O TYR A1105 1.814 5.855 -3.894 1.00103.78 O ANISOU 803 O TYR A1105 12855 20668 5908 -1926 111 384 O ATOM 804 CB TYR A1105 2.692 5.875 -1.226 1.00102.73 C ANISOU 804 CB TYR A1105 13303 20208 5523 -2142 279 264 C ATOM 805 CG TYR A1105 2.523 6.026 0.267 1.00109.44 C ANISOU 805 CG TYR A1105 14148 21507 5926 -2180 449 94 C ATOM 806 CD1 TYR A1105 1.263 6.201 0.831 1.00118.51 C ANISOU 806 CD1 TYR A1105 14683 23796 6549 -2042 735 -163 C ATOM 807 CD2 TYR A1105 3.627 6.127 1.103 1.00108.27 C ANISOU 807 CD2 TYR A1105 14540 20780 5819 -2282 322 125 C ATOM 808 CE1 TYR A1105 1.101 6.376 2.202 1.00124.78 C ANISOU 808 CE1 TYR A1105 15418 25195 6796 -2076 938 -392 C ATOM 809 CE2 TYR A1105 3.480 6.317 2.475 1.00113.66 C ANISOU 809 CE2 TYR A1105 15208 22016 5962 -2326 463 -75 C ATOM 810 CZ TYR A1105 2.213 6.450 3.021 1.00129.36 C ANISOU 810 CZ TYR A1105 16601 25185 7365 -2221 793 -355 C ATOM 811 OH TYR A1105 2.051 6.663 4.374 1.00136.60 O ANISOU 811 OH TYR A1105 17446 26837 7618 -2265 981 -628 O ATOM 812 N LEU A1106 2.382 3.692 -4.021 1.00 96.42 N ANISOU 812 N LEU A1106 12157 19373 5104 -3204 79 601 N ATOM 813 CA LEU A1106 2.477 3.698 -5.476 1.00 94.05 C ANISOU 813 CA LEU A1106 11766 19020 4947 -3117 -52 553 C ATOM 814 C LEU A1106 1.371 2.814 -6.044 1.00102.78 C ANISOU 814 C LEU A1106 12349 20885 5819 -3656 -29 463 C ATOM 815 O LEU A1106 0.684 3.225 -6.964 1.00105.47 O ANISOU 815 O LEU A1106 12255 21850 5969 -3407 -89 394 O ATOM 816 CB LEU A1106 3.867 3.255 -5.952 1.00 89.07 C ANISOU 816 CB LEU A1106 11642 17492 4708 -3273 -180 579 C ATOM 817 CG LEU A1106 5.027 4.158 -5.539 1.00 88.64 C ANISOU 817 CG LEU A1106 12026 16764 4888 -2836 -241 678 C ATOM 818 CD1 LEU A1106 5.690 3.644 -4.368 1.00 87.82 C ANISOU 818 CD1 LEU A1106 12257 16198 4911 -3096 -259 760 C ATOM 819 CD2 LEU A1106 6.121 4.073 -6.540 1.00 86.58 C ANISOU 819 CD2 LEU A1106 11963 16047 4888 -2834 -337 677 C ATOM 820 N MET A 123 1.102 1.692 -5.365 1.00116.00 N ANISOU 820 N MET A 123 13373 25901 4799 -4340 2147 -2525 N ATOM 821 CA MET A 123 0.047 0.762 -5.717 1.00117.33 C ANISOU 821 CA MET A 123 13299 26408 4874 -4510 2224 -2521 C ATOM 822 C MET A 123 -1.287 1.209 -5.091 1.00124.91 C ANISOU 822 C MET A 123 13961 27985 5512 -4462 2377 -2866 C ATOM 823 O MET A 123 -1.616 0.810 -3.966 1.00127.91 O ANISOU 823 O MET A 123 14254 28740 5606 -4807 2453 -2875 O ATOM 824 CB MET A 123 0.415 -0.666 -5.268 1.00120.00 C ANISOU 824 CB MET A 123 13719 26720 5154 -5010 2169 -2193 C ATOM 825 CG MET A 123 1.731 -1.166 -5.829 1.00121.74 C ANISOU 825 CG MET A 123 14202 26384 5668 -5031 1995 -1894 C ATOM 826 SD MET A 123 1.810 -1.235 -7.642 1.00124.62 S ANISOU 826 SD MET A 123 14549 26416 6386 -4719 1941 -1851 S ATOM 827 CE MET A 123 0.610 -2.514 -7.984 1.00122.61 C ANISOU 827 CE MET A 123 14085 26500 6002 -4998 2000 -1787 C ATOM 828 N ASP A 124 -2.033 2.073 -5.803 1.00120.72 N ANISOU 828 N ASP A 124 13285 27570 5014 -4023 2409 -3171 N ATOM 829 CA ASP A 124 -3.361 2.495 -5.366 1.00123.40 C ANISOU 829 CA ASP A 124 13293 28538 5057 -3906 2536 -3558 C ATOM 830 C ASP A 124 -4.385 2.017 -6.415 1.00126.72 C ANISOU 830 C ASP A 124 13446 29193 5509 -3816 2583 -3658 C ATOM 831 O ASP A 124 -3.988 1.454 -7.441 1.00123.36 O ANISOU 831 O ASP A 124 13133 28390 5346 -3825 2511 -3417 O ATOM 832 CB ASP A 124 -3.459 4.021 -5.101 1.00126.44 C ANISOU 832 CB ASP A 124 13731 28931 5381 -3418 2504 -3913 C ATOM 833 CG ASP A 124 -3.214 4.970 -6.261 1.00133.71 C ANISOU 833 CG ASP A 124 14848 29402 6553 -2893 2377 -4013 C ATOM 834 OD1 ASP A 124 -2.394 4.639 -7.132 1.00132.74 O ANISOU 834 OD1 ASP A 124 14944 28775 6717 -2925 2294 -3726 O ATOM 835 OD2 ASP A 124 -3.739 6.106 -6.217 1.00138.73 O ANISOU 835 OD2 ASP A 124 15468 30163 7082 -2454 2343 -4380 O ATOM 836 N GLY A 125 -5.676 2.188 -6.113 1.00126.63 N ANISOU 836 N GLY A 125 13064 29833 5216 -3755 2704 -4018 N ATOM 837 CA GLY A 125 -6.787 1.774 -6.965 1.00127.53 C ANISOU 837 CA GLY A 125 12860 30295 5300 -3681 2764 -4180 C ATOM 838 C GLY A 125 -6.539 1.909 -8.455 1.00128.52 C ANISOU 838 C GLY A 125 13127 29933 5774 -3322 2646 -4093 C ATOM 839 O GLY A 125 -6.732 0.948 -9.202 1.00126.78 O ANISOU 839 O GLY A 125 12835 29678 5657 -3522 2656 -3906 O ATOM 840 N GLU A 126 -6.061 3.089 -8.891 1.00123.65 N ANISOU 840 N GLU A 126 12750 28906 5327 -2819 2524 -4213 N ATOM 841 CA GLU A 126 -5.815 3.390 -10.302 1.00120.83 C ANISOU 841 CA GLU A 126 12568 28072 5269 -2455 2403 -4161 C ATOM 842 C GLU A 126 -4.480 2.799 -10.785 1.00121.54 C ANISOU 842 C GLU A 126 12990 27529 5660 -2691 2324 -3700 C ATOM 843 O GLU A 126 -4.430 2.283 -11.906 1.00119.53 O ANISOU 843 O GLU A 126 12758 27042 5616 -2662 2283 -3548 O ATOM 844 CB GLU A 126 -5.820 4.922 -10.530 1.00122.87 C ANISOU 844 CB GLU A 126 13016 28127 5541 -1859 2282 -4476 C ATOM 845 CG GLU A 126 -5.723 5.360 -11.991 1.00127.41 C ANISOU 845 CG GLU A 126 13792 28252 6367 -1457 2148 -4479 C ATOM 846 CD GLU A 126 -5.695 6.855 -12.277 1.00141.92 C ANISOU 846 CD GLU A 126 15913 29812 8197 -890 1988 -4765 C ATOM 847 OE1 GLU A 126 -5.673 7.219 -13.475 1.00131.27 O ANISOU 847 OE1 GLU A 126 14756 28100 7019 -577 1868 -4775 O ATOM 848 OE2 GLU A 126 -5.688 7.661 -11.318 1.00137.50 O ANISOU 848 OE2 GLU A 126 15416 29377 7450 -764 1968 -4976 O ATOM 849 N GLU A 127 -3.399 2.899 -9.966 1.00117.13 N ANISOU 849 N GLU A 127 12678 26707 5117 -2898 2293 -3504 N ATOM 850 CA GLU A 127 -2.052 2.479 -10.378 1.00113.49 C ANISOU 850 CA GLU A 127 12520 25673 4927 -3065 2198 -3128 C ATOM 851 C GLU A 127 -1.901 0.935 -10.389 1.00117.81 C ANISOU 851 C GLU A 127 12993 26257 5511 -3533 2216 -2805 C ATOM 852 O GLU A 127 -1.066 0.420 -11.139 1.00115.01 O ANISOU 852 O GLU A 127 12810 25482 5408 -3592 2125 -2541 O ATOM 853 CB GLU A 127 -0.981 3.098 -9.466 1.00114.00 C ANISOU 853 CB GLU A 127 12847 25494 4974 -3124 2150 -3061 C ATOM 854 CG GLU A 127 0.460 2.833 -9.891 1.00119.48 C ANISOU 854 CG GLU A 127 13830 25634 5932 -3247 2043 -2740 C ATOM 855 CD GLU A 127 0.898 3.315 -11.263 1.00141.01 C ANISOU 855 CD GLU A 127 16737 27925 8916 -2957 1959 -2716 C ATOM 856 OE1 GLU A 127 1.866 2.736 -11.806 1.00138.59 O ANISOU 856 OE1 GLU A 127 16558 27279 8820 -3108 1892 -2453 O ATOM 857 OE2 GLU A 127 0.242 4.221 -11.826 1.00134.53 O ANISOU 857 OE2 GLU A 127 15928 27117 8072 -2579 1948 -2969 O ATOM 858 N ILE A 128 -2.721 0.207 -9.622 1.00117.33 N ANISOU 858 N ILE A 128 12694 26696 5190 -3861 2320 -2841 N ATOM 859 CA ILE A 128 -2.650 -1.255 -9.597 1.00116.94 C ANISOU 859 CA ILE A 128 12634 26669 5130 -4327 2311 -2542 C ATOM 860 C ILE A 128 -3.292 -1.825 -10.918 1.00118.56 C ANISOU 860 C ILE A 128 12695 26874 5479 -4235 2309 -2528 C ATOM 861 O ILE A 128 -2.979 -2.954 -11.308 1.00115.41 O ANISOU 861 O ILE A 128 12379 26291 5181 -4510 2244 -2245 O ATOM 862 CB ILE A 128 -3.328 -1.808 -8.302 1.00123.79 C ANISOU 862 CB ILE A 128 13337 28077 5620 -4768 2422 -2586 C ATOM 863 CG1 ILE A 128 -2.915 -3.270 -8.008 1.00124.30 C ANISOU 863 CG1 ILE A 128 13556 28028 5645 -5305 2353 -2217 C ATOM 864 CG2 ILE A 128 -4.861 -1.586 -8.282 1.00128.22 C ANISOU 864 CG2 ILE A 128 13496 29298 5924 -4701 2580 -2948 C ATOM 865 CD1 ILE A 128 -3.303 -3.811 -6.608 1.00139.09 C ANISOU 865 CD1 ILE A 128 15392 30329 7128 -5813 2431 -2197 C ATOM 866 N GLU A 129 -4.130 -1.007 -11.618 1.00116.78 N ANISOU 866 N GLU A 129 12285 26819 5266 -3815 2354 -2839 N ATOM 867 CA GLU A 129 -4.822 -1.358 -12.878 1.00116.42 C ANISOU 867 CA GLU A 129 12086 26804 5345 -3657 2353 -2884 C ATOM 868 C GLU A 129 -3.898 -1.176 -14.095 1.00115.83 C ANISOU 868 C GLU A 129 12274 26106 5631 -3395 2223 -2706 C ATOM 869 O GLU A 129 -3.885 -2.032 -14.985 1.00112.78 O ANISOU 869 O GLU A 129 11882 25569 5401 -3489 2184 -2525 O ATOM 870 CB GLU A 129 -6.093 -0.508 -13.063 1.00120.79 C ANISOU 870 CB GLU A 129 12342 27816 5738 -3281 2429 -3328 C ATOM 871 CG GLU A 129 -7.119 -0.706 -11.957 1.00141.00 C ANISOU 871 CG GLU A 129 14568 31092 7914 -3542 2577 -3559 C ATOM 872 CD GLU A 129 -8.377 0.144 -12.019 1.00177.15 C ANISOU 872 CD GLU A 129 18805 36206 12297 -3148 2640 -4058 C ATOM 873 OE1 GLU A 129 -8.713 0.648 -13.116 1.00174.19 O ANISOU 873 OE1 GLU A 129 18411 35693 12080 -2694 2566 -4220 O ATOM 874 OE2 GLU A 129 -9.064 0.251 -10.976 1.00179.49 O ANISOU 874 OE2 GLU A 129 19079 36617 12503 -3160 2731 -4165 O ATOM 875 N VAL A 130 -3.122 -0.057 -14.113 1.00111.45 N ANISOU 875 N VAL A 130 11959 25203 5185 -3092 2156 -2765 N ATOM 876 CA VAL A 130 -2.121 0.312 -15.134 1.00107.87 C ANISOU 876 CA VAL A 130 11786 24172 5026 -2878 2043 -2623 C ATOM 877 C VAL A 130 -1.125 -0.849 -15.290 1.00108.85 C ANISOU 877 C VAL A 130 12033 24004 5320 -3223 1977 -2249 C ATOM 878 O VAL A 130 -0.807 -1.236 -16.415 1.00106.03 O ANISOU 878 O VAL A 130 11738 23364 5184 -3153 1914 -2116 O ATOM 879 CB VAL A 130 -1.406 1.651 -14.758 1.00111.41 C ANISOU 879 CB VAL A 130 12493 24363 5475 -2636 1992 -2738 C ATOM 880 CG1 VAL A 130 -0.304 2.007 -15.754 1.00108.27 C ANISOU 880 CG1 VAL A 130 12395 23403 5341 -2505 1888 -2585 C ATOM 881 CG2 VAL A 130 -2.408 2.800 -14.631 1.00113.94 C ANISOU 881 CG2 VAL A 130 12730 24946 5616 -2241 2012 -3133 C ATOM 882 N GLN A 131 -0.696 -1.434 -14.147 1.00106.38 N ANISOU 882 N GLN A 131 11754 23784 4881 -3585 1978 -2099 N ATOM 883 CA GLN A 131 0.198 -2.593 -14.038 1.00104.84 C ANISOU 883 CA GLN A 131 11691 23359 4784 -3918 1879 -1774 C ATOM 884 C GLN A 131 -0.211 -3.731 -14.980 1.00109.10 C ANISOU 884 C GLN A 131 12143 23883 5426 -4025 1845 -1632 C ATOM 885 O GLN A 131 0.658 -4.366 -15.571 1.00106.88 O ANISOU 885 O GLN A 131 12008 23253 5349 -4072 1723 -1415 O ATOM 886 CB GLN A 131 0.199 -3.120 -12.590 1.00107.79 C ANISOU 886 CB GLN A 131 12070 23980 4907 -4302 1896 -1698 C ATOM 887 CG GLN A 131 0.851 -2.213 -11.549 1.00114.39 C ANISOU 887 CG GLN A 131 13033 24777 5654 -4266 1900 -1773 C ATOM 888 CD GLN A 131 2.359 -2.293 -11.515 1.00127.24 C ANISOU 888 CD GLN A 131 14916 25964 7465 -4302 1759 -1570 C ATOM 889 OE1 GLN A 131 2.947 -2.679 -10.501 1.00119.08 O ANISOU 889 OE1 GLN A 131 13995 24923 6327 -4557 1700 -1446 O ATOM 890 NE2 GLN A 131 3.023 -2.002 -12.626 1.00121.05 N ANISOU 890 NE2 GLN A 131 14223 24827 6942 -4070 1695 -1535 N ATOM 891 N LYS A 132 -1.531 -3.984 -15.110 1.00108.13 N ANISOU 891 N LYS A 132 11771 24162 5150 -4061 1947 -1774 N ATOM 892 CA LYS A 132 -2.090 -5.041 -15.955 1.00108.03 C ANISOU 892 CA LYS A 132 11656 24194 5195 -4186 1928 -1667 C ATOM 893 C LYS A 132 -2.212 -4.575 -17.418 1.00111.47 C ANISOU 893 C LYS A 132 12062 24419 5874 -3786 1911 -1754 C ATOM 894 O LYS A 132 -2.049 -5.389 -18.332 1.00109.28 O ANISOU 894 O LYS A 132 11817 23938 5764 -3828 1836 -1587 O ATOM 895 CB LYS A 132 -3.465 -5.485 -15.423 1.00113.42 C ANISOU 895 CB LYS A 132 12066 25456 5575 -4439 2056 -1806 C ATOM 896 CG LYS A 132 -3.407 -6.088 -14.009 1.00133.70 C ANISOU 896 CG LYS A 132 14690 28246 7865 -4913 2071 -1695 C ATOM 897 CD LYS A 132 -4.767 -6.602 -13.480 1.00147.66 C ANISOU 897 CD LYS A 132 16182 30634 9287 -5254 2212 -1832 C ATOM 898 CE LYS A 132 -5.806 -5.542 -13.165 1.00161.66 C ANISOU 898 CE LYS A 132 17629 32930 10865 -5014 2381 -2240 C ATOM 899 NZ LYS A 132 -5.393 -4.673 -12.032 1.00172.77 N ANISOU 899 NZ LYS A 132 19103 34397 12144 -4958 2413 -2350 N ATOM 900 N GLU A 133 -2.498 -3.266 -17.632 1.00109.22 N ANISOU 900 N GLU A 133 11743 24166 5589 -3395 1962 -2020 N ATOM 901 CA GLU A 133 -2.670 -2.665 -18.968 1.00107.62 C ANISOU 901 CA GLU A 133 11558 23758 5574 -2995 1933 -2132 C ATOM 902 C GLU A 133 -1.340 -2.669 -19.717 1.00105.61 C ANISOU 902 C GLU A 133 11573 22961 5592 -2938 1822 -1917 C ATOM 903 O GLU A 133 -1.292 -3.015 -20.898 1.00103.74 O ANISOU 903 O GLU A 133 11351 22526 5539 -2833 1775 -1841 O ATOM 904 CB GLU A 133 -3.233 -1.222 -18.881 1.00111.10 C ANISOU 904 CB GLU A 133 11977 24327 5908 -2592 1970 -2475 C ATOM 905 CG GLU A 133 -4.368 -0.995 -17.880 1.00130.86 C ANISOU 905 CG GLU A 133 14208 27409 8103 -2621 2077 -2748 C ATOM 906 CD GLU A 133 -5.655 -1.798 -17.972 1.00169.78 C ANISOU 906 CD GLU A 133 18783 32849 12879 -2771 2166 -2856 C ATOM 907 OE1 GLU A 133 -6.036 -2.212 -19.092 1.00178.16 O ANISOU 907 OE1 GLU A 133 19771 33846 14074 -2669 2139 -2832 O ATOM 908 OE2 GLU A 133 -6.343 -1.909 -16.930 1.00167.39 O ANISOU 908 OE2 GLU A 133 18259 33045 12295 -2974 2268 -3005 O ATOM 909 N VAL A 134 -0.261 -2.282 -19.013 1.00 99.17 N ANISOU 909 N VAL A 134 10954 21939 4787 -3017 1783 -1835 N ATOM 910 CA VAL A 134 1.115 -2.292 -19.505 1.00 95.49 C ANISOU 910 CA VAL A 134 10713 21035 4535 -3021 1685 -1655 C ATOM 911 C VAL A 134 1.530 -3.760 -19.766 1.00 99.18 C ANISOU 911 C VAL A 134 11159 21412 5112 -3285 1599 -1395 C ATOM 912 O VAL A 134 2.148 -4.045 -20.783 1.00 96.62 O ANISOU 912 O VAL A 134 10907 20810 4994 -3210 1525 -1292 O ATOM 913 CB VAL A 134 2.054 -1.576 -18.491 1.00 97.93 C ANISOU 913 CB VAL A 134 11193 21240 4777 -3083 1670 -1661 C ATOM 914 CG1 VAL A 134 3.519 -1.782 -18.823 1.00 95.43 C ANISOU 914 CG1 VAL A 134 11051 20561 4645 -3164 1569 -1481 C ATOM 915 CG2 VAL A 134 1.731 -0.096 -18.387 1.00 98.66 C ANISOU 915 CG2 VAL A 134 11371 21341 4774 -2792 1717 -1914 C ATOM 916 N ALA A 135 1.117 -4.689 -18.872 1.00 98.14 N ANISOU 916 N ALA A 135 10942 21529 4818 -3594 1600 -1305 N ATOM 917 CA ALA A 135 1.430 -6.123 -18.937 1.00 97.53 C ANISOU 917 CA ALA A 135 10905 21364 4787 -3868 1482 -1064 C ATOM 918 C ALA A 135 0.846 -6.788 -20.177 1.00100.27 C ANISOU 918 C ALA A 135 11156 21682 5261 -3798 1464 -1025 C ATOM 919 O ALA A 135 1.526 -7.615 -20.790 1.00 98.15 O ANISOU 919 O ALA A 135 10985 21154 5156 -3841 1330 -851 O ATOM 920 CB ALA A 135 0.898 -6.830 -17.700 1.00100.51 C ANISOU 920 CB ALA A 135 11250 22041 4900 -4233 1496 -1005 C ATOM 921 N LYS A 136 -0.416 -6.454 -20.537 1.00 97.89 N ANISOU 921 N LYS A 136 10656 21664 4873 -3679 1586 -1205 N ATOM 922 CA LYS A 136 -1.085 -7.075 -21.682 1.00 97.03 C ANISOU 922 CA LYS A 136 10435 21568 4863 -3620 1577 -1187 C ATOM 923 C LYS A 136 -0.570 -6.452 -23.003 1.00 97.52 C ANISOU 923 C LYS A 136 10574 21298 5182 -3263 1544 -1223 C ATOM 924 O LYS A 136 -0.854 -6.979 -24.076 1.00 95.50 O ANISOU 924 O LYS A 136 10268 20963 5054 -3192 1511 -1178 O ATOM 925 CB LYS A 136 -2.625 -6.961 -21.573 1.00102.21 C ANISOU 925 CB LYS A 136 10823 22696 5316 -3626 1713 -1395 C ATOM 926 CG LYS A 136 -3.216 -5.561 -21.738 1.00123.29 C ANISOU 926 CG LYS A 136 13386 25515 7943 -3241 1811 -1705 C ATOM 927 CD LYS A 136 -4.744 -5.611 -21.657 1.00139.38 C ANISOU 927 CD LYS A 136 15110 28078 9770 -3244 1924 -1939 C ATOM 928 CE LYS A 136 -5.437 -4.340 -22.103 1.00155.18 C ANISOU 928 CE LYS A 136 17006 30206 11749 -2778 1970 -2275 C ATOM 929 NZ LYS A 136 -5.053 -3.156 -21.296 1.00165.00 N ANISOU 929 NZ LYS A 136 18367 31419 12906 -2601 1983 -2424 N ATOM 930 N MET A 137 0.204 -5.360 -22.909 1.00 93.43 N ANISOU 930 N MET A 137 10196 20585 4718 -3075 1549 -1297 N ATOM 931 CA MET A 137 0.803 -4.684 -24.051 1.00 91.68 C ANISOU 931 CA MET A 137 10098 20043 4691 -2802 1519 -1327 C ATOM 932 C MET A 137 2.116 -5.363 -24.447 1.00 95.15 C ANISOU 932 C MET A 137 10664 20174 5314 -2913 1401 -1122 C ATOM 933 O MET A 137 2.368 -5.531 -25.638 1.00 93.29 O ANISOU 933 O MET A 137 10452 19745 5249 -2789 1360 -1085 O ATOM 934 CB MET A 137 1.027 -3.214 -23.731 1.00 94.30 C ANISOU 934 CB MET A 137 10562 20313 4957 -2600 1567 -1504 C ATOM 935 CG MET A 137 1.866 -2.516 -24.734 1.00 96.51 C ANISOU 935 CG MET A 137 11040 20237 5394 -2421 1526 -1504 C ATOM 936 SD MET A 137 1.969 -0.756 -24.447 1.00102.27 S ANISOU 936 SD MET A 137 11993 20861 6005 -2190 1555 -1720 S ATOM 937 CE MET A 137 0.248 -0.253 -24.893 1.00100.76 C ANISOU 937 CE MET A 137 11674 20912 5700 -1851 1593 -1981 C ATOM 938 N TYR A 138 2.946 -5.752 -23.465 1.00 93.23 N ANISOU 938 N TYR A 138 10495 19903 5026 -3131 1335 -1009 N ATOM 939 CA TYR A 138 4.193 -6.459 -23.740 1.00 92.54 C ANISOU 939 CA TYR A 138 10500 19571 5088 -3213 1193 -853 C ATOM 940 C TYR A 138 3.913 -7.880 -24.233 1.00 97.34 C ANISOU 940 C TYR A 138 11056 20166 5762 -3321 1083 -705 C ATOM 941 O TYR A 138 4.644 -8.359 -25.099 1.00 96.35 O ANISOU 941 O TYR A 138 10965 19834 5810 -3253 979 -636 O ATOM 942 CB TYR A 138 5.097 -6.495 -22.516 1.00 95.08 C ANISOU 942 CB TYR A 138 10918 19883 5327 -3387 1127 -798 C ATOM 943 CG TYR A 138 5.748 -5.165 -22.207 1.00 98.79 C ANISOU 943 CG TYR A 138 11479 20283 5775 -3290 1197 -922 C ATOM 944 CD1 TYR A 138 5.133 -4.246 -21.368 1.00102.70 C ANISOU 944 CD1 TYR A 138 11978 20947 6096 -3269 1310 -1051 C ATOM 945 CD2 TYR A 138 7.007 -4.852 -22.704 1.00 99.19 C ANISOU 945 CD2 TYR A 138 11613 20118 5955 -3241 1141 -921 C ATOM 946 CE1 TYR A 138 5.739 -3.029 -21.062 1.00104.80 C ANISOU 946 CE1 TYR A 138 12370 21121 6327 -3191 1353 -1161 C ATOM 947 CE2 TYR A 138 7.627 -3.643 -22.397 1.00100.81 C ANISOU 947 CE2 TYR A 138 11930 20259 6114 -3206 1200 -1029 C ATOM 948 CZ TYR A 138 6.992 -2.735 -21.569 1.00111.34 C ANISOU 948 CZ TYR A 138 13307 21716 7280 -3179 1298 -1139 C ATOM 949 OH TYR A 138 7.601 -1.545 -21.240 1.00114.77 O ANISOU 949 OH TYR A 138 13890 22063 7655 -3154 1338 -1242 O ATOM 950 N SER A 139 2.841 -8.535 -23.731 1.00 95.79 N ANISOU 950 N SER A 139 10779 20203 5412 -3496 1107 -671 N ATOM 951 CA SER A 139 2.462 -9.868 -24.201 1.00 96.48 C ANISOU 951 CA SER A 139 10853 20274 5530 -3630 998 -531 C ATOM 952 C SER A 139 1.811 -9.781 -25.591 1.00102.63 C ANISOU 952 C SER A 139 11517 21033 6445 -3418 1056 -596 C ATOM 953 O SER A 139 1.822 -10.772 -26.326 1.00103.14 O ANISOU 953 O SER A 139 11595 20982 6610 -3449 945 -485 O ATOM 954 CB SER A 139 1.525 -10.555 -23.220 1.00102.81 C ANISOU 954 CB SER A 139 11626 21351 6086 -3948 1014 -477 C ATOM 955 OG SER A 139 0.289 -9.866 -23.155 1.00116.54 O ANISOU 955 OG SER A 139 13171 23416 7693 -3898 1206 -656 O ATOM 956 N SER A 140 1.223 -8.603 -25.949 1.00 99.35 N ANISOU 956 N SER A 140 11010 20718 6019 -3189 1210 -786 N ATOM 957 CA SER A 140 0.652 -8.388 -27.287 1.00 97.84 C ANISOU 957 CA SER A 140 10739 20484 5951 -2951 1251 -866 C ATOM 958 C SER A 140 1.789 -8.167 -28.268 1.00 99.68 C ANISOU 958 C SER A 140 11093 20383 6399 -2787 1182 -825 C ATOM 959 O SER A 140 1.774 -8.760 -29.341 1.00 98.38 O ANISOU 959 O SER A 140 10906 20101 6374 -2717 1125 -768 O ATOM 960 CB SER A 140 -0.342 -7.230 -27.310 1.00102.05 C ANISOU 960 CB SER A 140 11175 21221 6378 -2737 1393 -1099 C ATOM 961 OG SER A 140 -1.496 -7.502 -26.531 1.00111.92 O ANISOU 961 OG SER A 140 12250 22857 7417 -2889 1468 -1176 O ATOM 962 N PHE A 141 2.830 -7.398 -27.860 1.00 96.37 N ANISOU 962 N PHE A 141 10796 19829 5990 -2762 1183 -851 N ATOM 963 CA PHE A 141 4.031 -7.196 -28.674 1.00 95.09 C ANISOU 963 CA PHE A 141 10733 19406 5992 -2672 1125 -828 C ATOM 964 C PHE A 141 4.754 -8.520 -28.881 1.00 98.39 C ANISOU 964 C PHE A 141 11141 19723 6519 -2786 961 -676 C ATOM 965 O PHE A 141 5.402 -8.702 -29.905 1.00 95.43 O ANISOU 965 O PHE A 141 10774 19190 6294 -2689 907 -667 O ATOM 966 CB PHE A 141 4.989 -6.165 -28.056 1.00 97.29 C ANISOU 966 CB PHE A 141 11135 19610 6222 -2685 1158 -894 C ATOM 967 CG PHE A 141 4.498 -4.741 -27.881 1.00 99.54 C ANISOU 967 CG PHE A 141 11504 19924 6394 -2547 1279 -1057 C ATOM 968 CD1 PHE A 141 3.473 -4.235 -28.678 1.00102.45 C ANISOU 968 CD1 PHE A 141 11862 20311 6755 -2334 1340 -1167 C ATOM 969 CD2 PHE A 141 5.175 -3.854 -27.045 1.00101.73 C ANISOU 969 CD2 PHE A 141 11903 20171 6579 -2600 1306 -1115 C ATOM 970 CE1 PHE A 141 3.064 -2.904 -28.561 1.00104.15 C ANISOU 970 CE1 PHE A 141 12202 20514 6855 -2161 1405 -1338 C ATOM 971 CE2 PHE A 141 4.783 -2.514 -26.947 1.00105.11 C ANISOU 971 CE2 PHE A 141 12462 20578 6896 -2451 1384 -1273 C ATOM 972 CZ PHE A 141 3.729 -2.048 -27.705 1.00103.57 C ANISOU 972 CZ PHE A 141 12275 20392 6683 -2220 1422 -1387 C ATOM 973 N GLN A 142 4.615 -9.450 -27.905 1.00 97.91 N ANISOU 973 N GLN A 142 11082 19757 6363 -2991 869 -568 N ATOM 974 CA GLN A 142 5.169 -10.809 -27.910 1.00 98.77 C ANISOU 974 CA GLN A 142 11239 19760 6529 -3100 662 -425 C ATOM 975 C GLN A 142 4.553 -11.644 -29.033 1.00102.91 C ANISOU 975 C GLN A 142 11710 20237 7155 -3040 611 -371 C ATOM 976 O GLN A 142 5.258 -12.449 -29.626 1.00102.71 O ANISOU 976 O GLN A 142 11721 20050 7252 -2993 446 -310 O ATOM 977 CB GLN A 142 4.935 -11.496 -26.553 1.00102.39 C ANISOU 977 CB GLN A 142 11773 20325 6804 -3360 578 -323 C ATOM 978 CG GLN A 142 5.397 -12.957 -26.463 1.00128.53 C ANISOU 978 CG GLN A 142 15211 23494 10129 -3478 317 -169 C ATOM 979 CD GLN A 142 4.882 -13.652 -25.219 1.00159.67 C ANISOU 979 CD GLN A 142 19276 27544 13846 -3783 242 -55 C ATOM 980 OE1 GLN A 142 4.676 -13.045 -24.154 1.00155.82 O ANISOU 980 OE1 GLN A 142 18789 27218 13198 -3910 351 -90 O ATOM 981 NE2 GLN A 142 4.681 -14.958 -25.325 1.00157.79 N ANISOU 981 NE2 GLN A 142 19172 27208 13572 -3924 43 86 N ATOM 982 N VAL A 143 3.255 -11.489 -29.315 1.00 99.81 N ANISOU 982 N VAL A 143 11221 20001 6703 -3031 737 -411 N ATOM 983 CA VAL A 143 2.692 -12.255 -30.422 1.00 99.52 C ANISOU 983 CA VAL A 143 11130 19919 6765 -2974 688 -366 C ATOM 984 C VAL A 143 2.832 -11.420 -31.693 1.00102.81 C ANISOU 984 C VAL A 143 11497 20231 7334 -2699 779 -478 C ATOM 985 O VAL A 143 3.004 -11.982 -32.770 1.00101.41 O ANISOU 985 O VAL A 143 11309 19923 7300 -2603 702 -442 O ATOM 986 CB VAL A 143 1.237 -12.741 -30.215 1.00104.97 C ANISOU 986 CB VAL A 143 11728 20846 7312 -3130 747 -352 C ATOM 987 CG1 VAL A 143 1.143 -13.686 -29.021 1.00106.72 C ANISOU 987 CG1 VAL A 143 12050 21146 7351 -3466 637 -218 C ATOM 988 CG2 VAL A 143 0.250 -11.581 -30.084 1.00105.43 C ANISOU 988 CG2 VAL A 143 11644 21148 7267 -3023 959 -532 C ATOM 989 N MET A 144 2.845 -10.078 -31.546 1.00100.49 N ANISOU 989 N MET A 144 11211 19973 6999 -2582 924 -611 N ATOM 990 CA MET A 144 2.926 -9.115 -32.647 1.00100.19 C ANISOU 990 CA MET A 144 11197 19820 7052 -2349 1007 -722 C ATOM 991 C MET A 144 4.204 -9.339 -33.470 1.00100.24 C ANISOU 991 C MET A 144 11260 19614 7214 -2306 920 -685 C ATOM 992 O MET A 144 4.175 -9.098 -34.672 1.00 98.35 O ANISOU 992 O MET A 144 11027 19272 7070 -2159 946 -727 O ATOM 993 CB MET A 144 2.873 -7.681 -32.100 1.00103.89 C ANISOU 993 CB MET A 144 11741 20327 7405 -2273 1129 -860 C ATOM 994 CG MET A 144 2.191 -6.688 -33.029 1.00108.52 C ANISOU 994 CG MET A 144 12370 20869 7992 -2028 1213 -1000 C ATOM 995 SD MET A 144 1.819 -5.072 -32.250 1.00114.93 S ANISOU 995 SD MET A 144 13305 21742 8620 -1906 1312 -1188 S ATOM 996 CE MET A 144 3.476 -4.364 -32.127 1.00111.37 C ANISOU 996 CE MET A 144 13068 21050 8197 -2004 1298 -1159 C ATOM 997 N TYR A 145 5.292 -9.859 -32.846 1.00 96.16 N ANISOU 997 N TYR A 145 10772 19055 6711 -2430 806 -622 N ATOM 998 CA TYR A 145 6.524 -10.182 -33.574 1.00 94.83 C ANISOU 998 CA TYR A 145 10604 18755 6672 -2385 707 -625 C ATOM 999 C TYR A 145 6.539 -11.690 -33.902 1.00 96.33 C ANISOU 999 C TYR A 145 10754 18901 6948 -2396 516 -521 C ATOM 1000 O TYR A 145 7.190 -12.093 -34.867 1.00 95.30 O ANISOU 1000 O TYR A 145 10587 18683 6941 -2296 435 -543 O ATOM 1001 CB TYR A 145 7.805 -9.762 -32.808 1.00 97.03 C ANISOU 1001 CB TYR A 145 10923 19033 6910 -2470 677 -671 C ATOM 1002 CG TYR A 145 8.341 -10.747 -31.785 1.00100.45 C ANISOU 1002 CG TYR A 145 11364 19493 7311 -2584 494 -593 C ATOM 1003 CD1 TYR A 145 7.873 -10.747 -30.476 1.00103.89 C ANISOU 1003 CD1 TYR A 145 11853 20015 7604 -2724 500 -537 C ATOM 1004 CD2 TYR A 145 9.425 -11.570 -32.082 1.00101.69 C ANISOU 1004 CD2 TYR A 145 11488 19594 7556 -2542 305 -602 C ATOM 1005 CE1 TYR A 145 8.395 -11.618 -29.515 1.00106.97 C ANISOU 1005 CE1 TYR A 145 12302 20401 7939 -2838 312 -461 C ATOM 1006 CE2 TYR A 145 9.957 -12.448 -31.134 1.00104.12 C ANISOU 1006 CE2 TYR A 145 11846 19896 7817 -2611 95 -547 C ATOM 1007 CZ TYR A 145 9.441 -12.467 -29.846 1.00113.82 C ANISOU 1007 CZ TYR A 145 13169 21177 8901 -2769 96 -464 C ATOM 1008 OH TYR A 145 9.973 -13.314 -28.891 1.00114.78 O ANISOU 1008 OH TYR A 145 13390 21267 8954 -2847 -131 -404 O ATOM 1009 N THR A 146 5.823 -12.518 -33.102 1.00 91.61 N ANISOU 1009 N THR A 146 10178 18366 6263 -2530 436 -414 N ATOM 1010 CA THR A 146 5.719 -13.960 -33.348 1.00 90.60 C ANISOU 1010 CA THR A 146 10081 18164 6179 -2568 230 -302 C ATOM 1011 C THR A 146 4.916 -14.162 -34.633 1.00 90.96 C ANISOU 1011 C THR A 146 10053 18185 6321 -2451 280 -307 C ATOM 1012 O THR A 146 5.286 -15.005 -35.450 1.00 90.16 O ANISOU 1012 O THR A 146 9956 17965 6334 -2366 131 -278 O ATOM 1013 CB THR A 146 5.101 -14.686 -32.136 1.00 98.55 C ANISOU 1013 CB THR A 146 11180 19245 7019 -2806 146 -183 C ATOM 1014 OG1 THR A 146 5.923 -14.450 -31.001 1.00 98.08 O ANISOU 1014 OG1 THR A 146 11197 19193 6876 -2892 92 -187 O ATOM 1015 CG2 THR A 146 4.978 -16.199 -32.343 1.00 97.82 C ANISOU 1015 CG2 THR A 146 11196 19034 6936 -2881 -100 -54 C ATOM 1016 N VAL A 147 3.844 -13.362 -34.822 1.00 85.37 N ANISOU 1016 N VAL A 147 9280 17594 5564 -2419 476 -363 N ATOM 1017 CA VAL A 147 3.007 -13.390 -36.022 1.00 84.00 C ANISOU 1017 CA VAL A 147 9032 17417 5468 -2287 536 -392 C ATOM 1018 C VAL A 147 3.880 -12.946 -37.227 1.00 87.50 C ANISOU 1018 C VAL A 147 9476 17708 6061 -2093 547 -465 C ATOM 1019 O VAL A 147 3.983 -13.681 -38.217 1.00 86.45 O ANISOU 1019 O VAL A 147 9319 17484 6045 -2011 452 -437 O ATOM 1020 CB VAL A 147 1.723 -12.522 -35.850 1.00 87.36 C ANISOU 1020 CB VAL A 147 9383 18028 5781 -2257 722 -483 C ATOM 1021 CG1 VAL A 147 1.055 -12.218 -37.185 1.00 86.38 C ANISOU 1021 CG1 VAL A 147 9200 17876 5744 -2050 788 -557 C ATOM 1022 CG2 VAL A 147 0.737 -13.184 -34.891 1.00 88.34 C ANISOU 1022 CG2 VAL A 147 9460 18361 5745 -2483 713 -423 C ATOM 1023 N GLY A 148 4.546 -11.798 -37.081 1.00 83.85 N ANISOU 1023 N GLY A 148 9056 17230 5574 -2054 652 -558 N ATOM 1024 CA GLY A 148 5.433 -11.228 -38.088 1.00 82.57 C ANISOU 1024 CA GLY A 148 8916 16960 5498 -1946 686 -639 C ATOM 1025 C GLY A 148 6.413 -12.225 -38.648 1.00 86.30 C ANISOU 1025 C GLY A 148 9337 17367 6086 -1925 524 -618 C ATOM 1026 O GLY A 148 6.467 -12.406 -39.861 1.00 84.67 O ANISOU 1026 O GLY A 148 9096 17098 5975 -1814 516 -646 O ATOM 1027 N TYR A 149 7.149 -12.922 -37.756 1.00 84.85 N ANISOU 1027 N TYR A 149 9152 17202 5883 -2013 372 -581 N ATOM 1028 CA TYR A 149 8.121 -13.955 -38.122 1.00 85.05 C ANISOU 1028 CA TYR A 149 9134 17182 6000 -1954 163 -593 C ATOM 1029 C TYR A 149 7.469 -15.213 -38.692 1.00 84.76 C ANISOU 1029 C TYR A 149 9102 17066 6035 -1894 7 -501 C ATOM 1030 O TYR A 149 8.078 -15.821 -39.558 1.00 84.55 O ANISOU 1030 O TYR A 149 9026 16990 6110 -1770 -118 -551 O ATOM 1031 CB TYR A 149 8.998 -14.381 -36.935 1.00 88.97 C ANISOU 1031 CB TYR A 149 9663 17706 6437 -2033 1 -589 C ATOM 1032 CG TYR A 149 10.200 -13.502 -36.675 1.00 93.32 C ANISOU 1032 CG TYR A 149 10165 18338 6956 -2056 69 -724 C ATOM 1033 CD1 TYR A 149 11.273 -13.481 -37.562 1.00 95.81 C ANISOU 1033 CD1 TYR A 149 10365 18698 7339 -1967 37 -866 C ATOM 1034 CD2 TYR A 149 10.374 -12.880 -35.442 1.00 95.60 C ANISOU 1034 CD2 TYR A 149 10510 18685 7130 -2186 125 -720 C ATOM 1035 CE1 TYR A 149 12.430 -12.757 -37.287 1.00 98.61 C ANISOU 1035 CE1 TYR A 149 10656 19172 7641 -2031 89 -1006 C ATOM 1036 CE2 TYR A 149 11.527 -12.149 -35.154 1.00 97.53 C ANISOU 1036 CE2 TYR A 149 10709 19014 7335 -2231 168 -847 C ATOM 1037 CZ TYR A 149 12.552 -12.089 -36.081 1.00107.86 C ANISOU 1037 CZ TYR A 149 11896 20384 8703 -2165 152 -992 C ATOM 1038 OH TYR A 149 13.685 -11.357 -35.816 1.00114.00 O ANISOU 1038 OH TYR A 149 12611 21288 9416 -2251 207 -1135 O ATOM 1039 N SER A 150 6.290 -15.648 -38.183 1.00 78.34 N ANISOU 1039 N SER A 150 8348 16262 5154 -1999 1 -381 N ATOM 1040 CA SER A 150 5.627 -16.860 -38.688 1.00 76.86 C ANISOU 1040 CA SER A 150 8194 15999 5009 -1991 -152 -286 C ATOM 1041 C SER A 150 5.185 -16.651 -40.135 1.00 78.51 C ANISOU 1041 C SER A 150 8316 16183 5331 -1836 -54 -336 C ATOM 1042 O SER A 150 5.404 -17.536 -40.964 1.00 77.97 O ANISOU 1042 O SER A 150 8245 16020 5361 -1735 -208 -327 O ATOM 1043 CB SER A 150 4.441 -17.250 -37.813 1.00 79.77 C ANISOU 1043 CB SER A 150 8632 16437 5240 -2200 -145 -166 C ATOM 1044 OG SER A 150 4.863 -17.636 -36.515 1.00 85.64 O ANISOU 1044 OG SER A 150 9497 17177 5866 -2362 -275 -101 O ATOM 1045 N LEU A 151 4.623 -15.455 -40.449 1.00 73.72 N ANISOU 1045 N LEU A 151 7660 15647 4703 -1798 183 -401 N ATOM 1046 CA LEU A 151 4.225 -15.048 -41.810 1.00 72.38 C ANISOU 1046 CA LEU A 151 7441 15441 4618 -1642 285 -460 C ATOM 1047 C LEU A 151 5.476 -14.844 -42.698 1.00 74.99 C ANISOU 1047 C LEU A 151 7746 15708 5040 -1534 265 -556 C ATOM 1048 O LEU A 151 5.486 -15.243 -43.861 1.00 72.47 O ANISOU 1048 O LEU A 151 7388 15331 4817 -1418 225 -577 O ATOM 1049 CB LEU A 151 3.363 -13.756 -41.785 1.00 72.14 C ANISOU 1049 CB LEU A 151 7419 15483 4508 -1610 502 -525 C ATOM 1050 CG LEU A 151 1.829 -13.882 -41.588 1.00 76.66 C ANISOU 1050 CG LEU A 151 7942 16174 5010 -1632 556 -500 C ATOM 1051 CD1 LEU A 151 1.454 -14.579 -40.277 1.00 78.16 C ANISOU 1051 CD1 LEU A 151 8128 16483 5088 -1849 490 -410 C ATOM 1052 CD2 LEU A 151 1.173 -12.520 -41.655 1.00 77.51 C ANISOU 1052 CD2 LEU A 151 8066 16345 5038 -1521 731 -618 C ATOM 1053 N SER A 152 6.527 -14.244 -42.119 1.00 73.67 N ANISOU 1053 N SER A 152 7587 15579 4826 -1592 294 -624 N ATOM 1054 CA SER A 152 7.827 -14.000 -42.736 1.00 73.90 C ANISOU 1054 CA SER A 152 7562 15624 4893 -1551 287 -744 C ATOM 1055 C SER A 152 8.483 -15.360 -43.120 1.00 79.51 C ANISOU 1055 C SER A 152 8193 16318 5700 -1454 45 -760 C ATOM 1056 O SER A 152 9.009 -15.501 -44.225 1.00 79.71 O ANISOU 1056 O SER A 152 8138 16355 5793 -1354 29 -853 O ATOM 1057 CB SER A 152 8.691 -13.196 -41.771 1.00 77.40 C ANISOU 1057 CB SER A 152 8024 16145 5240 -1672 349 -808 C ATOM 1058 OG SER A 152 9.933 -12.803 -42.314 1.00 89.04 O ANISOU 1058 OG SER A 152 9428 17690 6712 -1685 375 -949 O ATOM 1059 N LEU A 153 8.370 -16.370 -42.217 1.00 75.99 N ANISOU 1059 N LEU A 153 7797 15835 5241 -1484 -157 -670 N ATOM 1060 CA LEU A 153 8.801 -17.768 -42.377 1.00 75.86 C ANISOU 1060 CA LEU A 153 7787 15751 5287 -1377 -449 -665 C ATOM 1061 C LEU A 153 8.046 -18.440 -43.512 1.00 81.26 C ANISOU 1061 C LEU A 153 8470 16343 6062 -1275 -495 -618 C ATOM 1062 O LEU A 153 8.665 -18.926 -44.458 1.00 80.79 O ANISOU 1062 O LEU A 153 8333 16276 6087 -1118 -603 -717 O ATOM 1063 CB LEU A 153 8.545 -18.531 -41.054 1.00 76.29 C ANISOU 1063 CB LEU A 153 7990 15742 5257 -1490 -635 -540 C ATOM 1064 CG LEU A 153 8.680 -20.044 -41.063 1.00 81.02 C ANISOU 1064 CG LEU A 153 8705 16200 5878 -1409 -979 -490 C ATOM 1065 CD1 LEU A 153 10.118 -20.460 -41.143 1.00 82.24 C ANISOU 1065 CD1 LEU A 153 8798 16381 6068 -1225 -1200 -659 C ATOM 1066 CD2 LEU A 153 8.074 -20.629 -39.830 1.00 82.95 C ANISOU 1066 CD2 LEU A 153 9156 16365 5995 -1602 -1107 -325 C ATOM 1067 N GLY A 154 6.712 -18.467 -43.382 1.00 78.97 N ANISOU 1067 N GLY A 154 8251 16013 5741 -1369 -414 -484 N ATOM 1068 CA GLY A 154 5.787 -19.051 -44.344 1.00 79.14 C ANISOU 1068 CA GLY A 154 8277 15965 5830 -1308 -438 -426 C ATOM 1069 C GLY A 154 5.933 -18.478 -45.736 1.00 84.14 C ANISOU 1069 C GLY A 154 8805 16611 6552 -1160 -303 -531 C ATOM 1070 O GLY A 154 5.867 -19.224 -46.717 1.00 83.67 O ANISOU 1070 O GLY A 154 8725 16484 6582 -1038 -414 -540 O ATOM 1071 N ALA A 155 6.159 -17.141 -45.830 1.00 81.72 N ANISOU 1071 N ALA A 155 8464 16380 6207 -1181 -73 -611 N ATOM 1072 CA ALA A 155 6.373 -16.449 -47.107 1.00 81.40 C ANISOU 1072 CA ALA A 155 8377 16344 6208 -1087 63 -710 C ATOM 1073 C ALA A 155 7.556 -17.071 -47.837 1.00 86.75 C ANISOU 1073 C ALA A 155 8956 17050 6954 -984 -72 -825 C ATOM 1074 O ALA A 155 7.381 -17.580 -48.946 1.00 87.12 O ANISOU 1074 O ALA A 155 8966 17054 7081 -865 -123 -845 O ATOM 1075 CB ALA A 155 6.599 -14.950 -46.884 1.00 81.97 C ANISOU 1075 CB ALA A 155 8498 16464 6183 -1170 284 -774 C ATOM 1076 N LEU A 156 8.724 -17.135 -47.155 1.00 82.80 N ANISOU 1076 N LEU A 156 8401 16640 6418 -1016 -156 -913 N ATOM 1077 CA LEU A 156 9.972 -17.699 -47.665 1.00 82.62 C ANISOU 1077 CA LEU A 156 8243 16716 6434 -904 -303 -1078 C ATOM 1078 C LEU A 156 9.843 -19.191 -47.964 1.00 86.55 C ANISOU 1078 C LEU A 156 8748 17115 7021 -732 -592 -1052 C ATOM 1079 O LEU A 156 10.403 -19.638 -48.955 1.00 86.59 O ANISOU 1079 O LEU A 156 8644 17174 7083 -584 -676 -1184 O ATOM 1080 CB LEU A 156 11.099 -17.477 -46.660 1.00 83.47 C ANISOU 1080 CB LEU A 156 8291 16956 6467 -968 -354 -1181 C ATOM 1081 CG LEU A 156 11.431 -16.026 -46.343 1.00 87.36 C ANISOU 1081 CG LEU A 156 8788 17551 6853 -1154 -95 -1229 C ATOM 1082 CD1 LEU A 156 12.325 -15.941 -45.165 1.00 88.45 C ANISOU 1082 CD1 LEU A 156 8887 17798 6921 -1223 -169 -1296 C ATOM 1083 CD2 LEU A 156 12.024 -15.308 -47.534 1.00 89.27 C ANISOU 1083 CD2 LEU A 156 8941 17914 7064 -1192 70 -1377 C ATOM 1084 N LEU A 157 9.092 -19.956 -47.139 1.00 83.12 N ANISOU 1084 N LEU A 157 8462 16539 6581 -768 -748 -890 N ATOM 1085 CA LEU A 157 8.872 -21.394 -47.384 1.00 83.57 C ANISOU 1085 CA LEU A 157 8605 16454 6695 -639 -1048 -842 C ATOM 1086 C LEU A 157 8.093 -21.597 -48.680 1.00 85.71 C ANISOU 1086 C LEU A 157 8854 16660 7050 -561 -988 -811 C ATOM 1087 O LEU A 157 8.384 -22.527 -49.427 1.00 85.46 O ANISOU 1087 O LEU A 157 8809 16574 7087 -386 -1194 -877 O ATOM 1088 CB LEU A 157 8.136 -22.075 -46.212 1.00 84.37 C ANISOU 1088 CB LEU A 157 8916 16414 6725 -778 -1202 -654 C ATOM 1089 CG LEU A 157 8.894 -22.193 -44.885 1.00 90.12 C ANISOU 1089 CG LEU A 157 9720 17158 7364 -833 -1350 -668 C ATOM 1090 CD1 LEU A 157 7.977 -22.640 -43.777 1.00 90.65 C ANISOU 1090 CD1 LEU A 157 10008 17108 7326 -1045 -1426 -463 C ATOM 1091 CD2 LEU A 157 10.092 -23.125 -45.004 1.00 94.19 C ANISOU 1091 CD2 LEU A 157 10231 17652 7906 -600 -1688 -827 C ATOM 1092 N LEU A 158 7.141 -20.696 -48.960 1.00 80.84 N ANISOU 1092 N LEU A 158 8236 16058 6422 -666 -719 -734 N ATOM 1093 CA LEU A 158 6.345 -20.709 -50.175 1.00 79.88 C ANISOU 1093 CA LEU A 158 8094 15888 6368 -595 -636 -713 C ATOM 1094 C LEU A 158 7.157 -20.166 -51.368 1.00 84.31 C ANISOU 1094 C LEU A 158 8525 16543 6967 -483 -529 -881 C ATOM 1095 O LEU A 158 7.082 -20.730 -52.464 1.00 85.26 O ANISOU 1095 O LEU A 158 8606 16626 7162 -348 -603 -922 O ATOM 1096 CB LEU A 158 5.071 -19.874 -49.967 1.00 79.19 C ANISOU 1096 CB LEU A 158 8054 15804 6231 -718 -410 -606 C ATOM 1097 CG LEU A 158 4.054 -19.877 -51.111 1.00 84.03 C ANISOU 1097 CG LEU A 158 8658 16370 6900 -641 -335 -579 C ATOM 1098 CD1 LEU A 158 3.451 -21.266 -51.307 1.00 85.18 C ANISOU 1098 CD1 LEU A 158 8855 16414 7096 -620 -557 -487 C ATOM 1099 CD2 LEU A 158 2.943 -18.887 -50.844 1.00 87.00 C ANISOU 1099 CD2 LEU A 158 9058 16794 7206 -717 -121 -536 C ATOM 1100 N ALA A 159 7.914 -19.061 -51.156 1.00 79.11 N ANISOU 1100 N ALA A 159 7809 16012 6235 -569 -351 -980 N ATOM 1101 CA ALA A 159 8.717 -18.405 -52.188 1.00 78.39 C ANISOU 1101 CA ALA A 159 7615 16044 6126 -550 -218 -1142 C ATOM 1102 C ALA A 159 9.766 -19.351 -52.755 1.00 83.66 C ANISOU 1102 C ALA A 159 8129 16816 6842 -392 -420 -1311 C ATOM 1103 O ALA A 159 10.025 -19.333 -53.959 1.00 83.49 O ANISOU 1103 O ALA A 159 8022 16861 6839 -323 -374 -1418 O ATOM 1104 CB ALA A 159 9.389 -17.169 -51.620 1.00 79.35 C ANISOU 1104 CB ALA A 159 7736 16285 6129 -723 -30 -1210 C ATOM 1105 N LEU A 160 10.349 -20.193 -51.889 1.00 81.21 N ANISOU 1105 N LEU A 160 7795 16521 6540 -319 -662 -1347 N ATOM 1106 CA LEU A 160 11.366 -21.171 -52.266 1.00 82.11 C ANISOU 1106 CA LEU A 160 7771 16738 6689 -111 -916 -1541 C ATOM 1107 C LEU A 160 10.740 -22.382 -52.908 1.00 85.49 C ANISOU 1107 C LEU A 160 8277 16988 7215 74 -1142 -1478 C ATOM 1108 O LEU A 160 11.315 -22.934 -53.839 1.00 85.26 O ANISOU 1108 O LEU A 160 8122 17047 7225 260 -1262 -1649 O ATOM 1109 CB LEU A 160 12.182 -21.602 -51.038 1.00 83.36 C ANISOU 1109 CB LEU A 160 7923 16948 6802 -73 -1131 -1609 C ATOM 1110 CG LEU A 160 13.029 -20.521 -50.399 1.00 87.96 C ANISOU 1110 CG LEU A 160 8395 17744 7282 -238 -948 -1717 C ATOM 1111 CD1 LEU A 160 13.587 -20.981 -49.095 1.00 89.55 C ANISOU 1111 CD1 LEU A 160 8634 17947 7443 -201 -1171 -1740 C ATOM 1112 CD2 LEU A 160 14.109 -20.086 -51.312 1.00 91.54 C ANISOU 1112 CD2 LEU A 160 8600 18493 7687 -224 -843 -1984 C ATOM 1113 N ALA A 161 9.567 -22.801 -52.414 1.00 81.91 N ANISOU 1113 N ALA A 161 8027 16308 6788 9 -1202 -1246 N ATOM 1114 CA ALA A 161 8.852 -23.966 -52.930 1.00 82.35 C ANISOU 1114 CA ALA A 161 8201 16172 6917 130 -1420 -1158 C ATOM 1115 C ALA A 161 8.437 -23.783 -54.380 1.00 85.22 C ANISOU 1115 C ALA A 161 8483 16551 7346 201 -1283 -1191 C ATOM 1116 O ALA A 161 8.288 -24.779 -55.092 1.00 85.23 O ANISOU 1116 O ALA A 161 8515 16455 7414 366 -1488 -1211 O ATOM 1117 CB ALA A 161 7.617 -24.240 -52.089 1.00 82.96 C ANISOU 1117 CB ALA A 161 8491 16064 6966 -43 -1443 -909 C ATOM 1118 N ILE A 162 8.230 -22.526 -54.818 1.00 81.10 N ANISOU 1118 N ILE A 162 7892 16128 6795 78 -956 -1195 N ATOM 1119 CA ILE A 162 7.788 -22.278 -56.184 1.00 80.55 C ANISOU 1119 CA ILE A 162 7783 16055 6767 132 -825 -1216 C ATOM 1120 C ILE A 162 9.077 -22.139 -57.076 1.00 84.94 C ANISOU 1120 C ILE A 162 8143 16828 7301 229 -807 -1469 C ATOM 1121 O ILE A 162 9.120 -22.754 -58.141 1.00 83.48 O ANISOU 1121 O ILE A 162 7900 16645 7173 385 -900 -1549 O ATOM 1122 CB ILE A 162 6.784 -21.057 -56.297 1.00 82.22 C ANISOU 1122 CB ILE A 162 8077 16225 6936 -24 -527 -1094 C ATOM 1123 CG1 ILE A 162 7.373 -19.654 -55.974 1.00 82.29 C ANISOU 1123 CG1 ILE A 162 8069 16362 6833 -182 -283 -1161 C ATOM 1124 CG2 ILE A 162 5.500 -21.315 -55.496 1.00 82.20 C ANISOU 1124 CG2 ILE A 162 8207 16084 6941 -103 -557 -896 C ATOM 1125 CD1 ILE A 162 7.992 -18.915 -57.142 1.00 86.30 C ANISOU 1125 CD1 ILE A 162 8518 16986 7287 -204 -120 -1304 C ATOM 1126 N LEU A 163 10.140 -21.460 -56.592 1.00 83.65 N ANISOU 1126 N LEU A 163 7868 16869 7047 135 -716 -1609 N ATOM 1127 CA LEU A 163 11.388 -21.309 -57.359 1.00 85.53 C ANISOU 1127 CA LEU A 163 7885 17386 7227 178 -685 -1878 C ATOM 1128 C LEU A 163 12.152 -22.644 -57.466 1.00 93.45 C ANISOU 1128 C LEU A 163 8754 18468 8284 457 -1024 -2063 C ATOM 1129 O LEU A 163 12.700 -22.959 -58.524 1.00 94.64 O ANISOU 1129 O LEU A 163 8740 18785 8433 588 -1062 -2262 O ATOM 1130 CB LEU A 163 12.302 -20.242 -56.743 1.00 86.16 C ANISOU 1130 CB LEU A 163 7877 17688 7173 -31 -502 -1988 C ATOM 1131 CG LEU A 163 11.783 -18.805 -56.781 1.00 89.80 C ANISOU 1131 CG LEU A 163 8486 18093 7542 -297 -180 -1865 C ATOM 1132 CD1 LEU A 163 12.692 -17.891 -56.027 1.00 91.25 C ANISOU 1132 CD1 LEU A 163 8613 18469 7590 -508 -47 -1963 C ATOM 1133 CD2 LEU A 163 11.631 -18.300 -58.200 1.00 92.28 C ANISOU 1133 CD2 LEU A 163 8813 18439 7810 -352 -9 -1909 C ATOM 1134 N GLY A 164 12.163 -23.409 -56.385 1.00 91.96 N ANISOU 1134 N GLY A 164 8660 18155 8126 550 -1282 -2005 N ATOM 1135 CA GLY A 164 12.795 -24.719 -56.353 1.00 94.21 C ANISOU 1135 CA GLY A 164 8902 18444 8449 847 -1668 -2167 C ATOM 1136 C GLY A 164 11.944 -25.743 -57.070 1.00 98.91 C ANISOU 1136 C GLY A 164 9646 18791 9145 1011 -1859 -2061 C ATOM 1137 O GLY A 164 10.762 -25.910 -56.747 1.00 96.53 O ANISOU 1137 O GLY A 164 9575 18217 8884 902 -1853 -1790 O ATOM 1138 N GLY A 165 12.541 -26.403 -58.057 1.00 98.87 N ANISOU 1138 N GLY A 165 9493 18909 9164 1261 -2020 -2290 N ATOM 1139 CA GLY A 165 11.847 -27.385 -58.877 1.00 99.54 C ANISOU 1139 CA GLY A 165 9704 18779 9338 1436 -2212 -2226 C ATOM 1140 C GLY A 165 10.890 -26.694 -59.825 1.00102.77 C ANISOU 1140 C GLY A 165 10127 19139 9782 1269 -1897 -2074 C ATOM 1141 O GLY A 165 9.690 -26.578 -59.531 1.00100.63 O ANISOU 1141 O GLY A 165 10059 18629 9547 1114 -1815 -1801 O ATOM 1142 N LEU A 166 11.443 -26.170 -60.945 1.00100.12 N ANISOU 1142 N LEU A 166 9568 19060 9413 1284 -1711 -2270 N ATOM 1143 CA LEU A 166 10.698 -25.431 -61.971 1.00 98.36 C ANISOU 1143 CA LEU A 166 9363 18813 9196 1141 -1419 -2168 C ATOM 1144 C LEU A 166 11.560 -25.307 -63.274 1.00104.89 C ANISOU 1144 C LEU A 166 9944 19941 9967 1225 -1341 -2449 C ATOM 1145 O LEU A 166 12.475 -26.115 -63.513 1.00105.09 O ANISOU 1145 O LEU A 166 9795 20147 9987 1467 -1577 -2711 O ATOM 1146 CB LEU A 166 10.330 -24.020 -61.387 1.00 96.39 C ANISOU 1146 CB LEU A 166 9185 18566 8873 825 -1081 -2012 C ATOM 1147 CG LEU A 166 8.945 -23.434 -61.727 1.00 97.99 C ANISOU 1147 CG LEU A 166 9576 18550 9106 691 -884 -1766 C ATOM 1148 CD1 LEU A 166 7.824 -24.165 -60.972 1.00 96.66 C ANISOU 1148 CD1 LEU A 166 9598 18105 9022 715 -1052 -1535 C ATOM 1149 CD2 LEU A 166 8.865 -21.995 -61.322 1.00 99.04 C ANISOU 1149 CD2 LEU A 166 9764 18733 9135 436 -582 -1700 C ATOM 1150 N SER A 167 11.226 -24.315 -64.118 1.00102.32 N ANISOU 1150 N SER A 167 9624 19668 9585 1031 -1029 -2403 N ATOM 1151 CA SER A 167 12.007 -23.896 -65.273 1.00103.86 C ANISOU 1151 CA SER A 167 9618 20174 9672 988 -873 -2641 C ATOM 1152 C SER A 167 12.862 -22.700 -64.825 1.00110.16 C ANISOU 1152 C SER A 167 10314 21241 10300 698 -621 -2743 C ATOM 1153 O SER A 167 13.764 -22.265 -65.539 1.00110.58 O ANISOU 1153 O SER A 167 10170 21637 10209 586 -480 -2981 O ATOM 1154 CB SER A 167 11.113 -23.588 -66.475 1.00106.34 C ANISOU 1154 CB SER A 167 10057 20347 10002 937 -718 -2520 C ATOM 1155 OG SER A 167 10.206 -22.528 -66.227 1.00113.04 O ANISOU 1155 OG SER A 167 11134 20993 10821 705 -485 -2274 O ATOM 1156 N LYS A 168 12.563 -22.197 -63.593 1.00108.48 N ANISOU 1156 N LYS A 168 10243 20882 10091 560 -572 -2566 N ATOM 1157 CA LYS A 168 13.289 -21.155 -62.854 1.00109.82 C ANISOU 1157 CA LYS A 168 10363 21246 10117 296 -382 -2627 C ATOM 1158 C LYS A 168 14.564 -21.749 -62.256 1.00117.98 C ANISOU 1158 C LYS A 168 11124 22585 11118 429 -575 -2904 C ATOM 1159 O LYS A 168 15.558 -21.047 -62.077 1.00118.66 O ANISOU 1159 O LYS A 168 11040 22997 11049 234 -428 -3093 O ATOM 1160 CB LYS A 168 12.401 -20.534 -61.750 1.00110.02 C ANISOU 1160 CB LYS A 168 10645 20984 10175 153 -298 -2340 C ATOM 1161 CG LYS A 168 11.202 -19.686 -62.217 1.00120.36 C ANISOU 1161 CG LYS A 168 12216 22038 11476 12 -89 -2107 C ATOM 1162 CD LYS A 168 11.462 -18.210 -62.669 1.00133.36 C ANISOU 1162 CD LYS A 168 13964 23777 12928 -301 219 -2131 C ATOM 1163 CE LYS A 168 12.220 -17.924 -63.961 1.00149.47 C ANISOU 1163 CE LYS A 168 15893 26072 14828 -417 342 -2334 C ATOM 1164 NZ LYS A 168 13.681 -18.183 -63.866 1.00161.95 N ANISOU 1164 NZ LYS A 168 17154 28071 16311 -459 309 -2632 N ATOM 1165 N LEU A 169 14.515 -23.068 -61.965 1.00116.94 N ANISOU 1165 N LEU A 169 10973 22341 11118 766 -925 -2937 N ATOM 1166 CA LEU A 169 15.597 -23.922 -61.470 1.00119.98 C ANISOU 1166 CA LEU A 169 11142 22951 11494 1017 -1218 -3215 C ATOM 1167 C LEU A 169 16.839 -23.789 -62.384 1.00128.90 C ANISOU 1167 C LEU A 169 11902 24590 12484 1031 -1149 -3616 C ATOM 1168 O LEU A 169 17.975 -23.853 -61.904 1.00131.05 O ANISOU 1168 O LEU A 169 11921 25208 12664 1088 -1237 -3902 O ATOM 1169 CB LEU A 169 15.062 -25.383 -61.425 1.00120.02 C ANISOU 1169 CB LEU A 169 11292 22657 11653 1379 -1615 -3149 C ATOM 1170 CG LEU A 169 15.999 -26.547 -61.049 1.00127.36 C ANISOU 1170 CG LEU A 169 12089 23713 12590 1752 -2034 -3432 C ATOM 1171 CD1 LEU A 169 15.229 -27.682 -60.416 1.00127.34 C ANISOU 1171 CD1 LEU A 169 12410 23267 12706 1960 -2398 -3222 C ATOM 1172 CD2 LEU A 169 16.808 -27.048 -62.251 1.00131.60 C ANISOU 1172 CD2 LEU A 169 12329 24590 13084 1996 -2131 -3803 C ATOM 1173 N HIS A 170 16.607 -23.546 -63.686 1.00126.76 N ANISOU 1173 N HIS A 170 11597 24389 12176 955 -975 -3643 N ATOM 1174 CA HIS A 170 17.649 -23.379 -64.699 1.00129.88 C ANISOU 1174 CA HIS A 170 11654 25282 12411 911 -868 -4009 C ATOM 1175 C HIS A 170 18.267 -21.957 -64.650 1.00131.24 C ANISOU 1175 C HIS A 170 11741 25762 12360 444 -494 -4074 C ATOM 1176 O HIS A 170 19.129 -21.646 -65.486 1.00133.84 O ANISOU 1176 O HIS A 170 11801 26546 12506 298 -347 -4370 O ATOM 1177 CB HIS A 170 17.065 -23.654 -66.099 1.00131.34 C ANISOU 1177 CB HIS A 170 11889 25384 12632 978 -824 -3978 C ATOM 1178 CG HIS A 170 16.476 -25.023 -66.239 1.00135.45 C ANISOU 1178 CG HIS A 170 12508 25608 13347 1402 -1186 -3923 C ATOM 1179 ND1 HIS A 170 15.155 -25.279 -65.901 1.00135.32 N ANISOU 1179 ND1 HIS A 170 12845 25075 13496 1437 -1257 -3544 N ATOM 1180 CD2 HIS A 170 17.050 -26.174 -66.661 1.00140.06 C ANISOU 1180 CD2 HIS A 170 12893 26360 13964 1788 -1502 -4215 C ATOM 1181 CE1 HIS A 170 14.968 -26.568 -66.136 1.00135.67 C ANISOU 1181 CE1 HIS A 170 12919 24970 13661 1803 -1603 -3596 C ATOM 1182 NE2 HIS A 170 16.079 -27.149 -66.595 1.00138.76 N ANISOU 1182 NE2 HIS A 170 13001 25738 13983 2046 -1775 -3993 N ATOM 1183 N CYS A 171 17.840 -21.108 -63.675 1.00122.04 N ANISOU 1183 N CYS A 171 10813 24366 11191 195 -347 -3813 N ATOM 1184 CA CYS A 171 18.361 -19.747 -63.508 1.00120.85 C ANISOU 1184 CA CYS A 171 10657 24437 10822 -259 -21 -3843 C ATOM 1185 C CYS A 171 19.405 -19.733 -62.378 1.00123.57 C ANISOU 1185 C CYS A 171 10774 25078 11100 -267 -106 -4050 C ATOM 1186 O CYS A 171 19.267 -20.486 -61.412 1.00121.94 O ANISOU 1186 O CYS A 171 10598 24689 11045 19 -376 -3994 O ATOM 1187 CB CYS A 171 17.223 -18.763 -63.236 1.00118.12 C ANISOU 1187 CB CYS A 171 10732 23653 10495 -508 184 -3450 C ATOM 1188 SG CYS A 171 17.727 -17.020 -63.183 1.00122.89 S ANISOU 1188 SG CYS A 171 11452 24435 10806 -1086 567 -3453 S ATOM 1189 N THR A 172 20.468 -18.902 -62.523 1.00121.32 N ANISOU 1189 N THR A 172 10265 25263 10568 -608 115 -4303 N ATOM 1190 CA THR A 172 21.537 -18.770 -61.517 1.00122.77 C ANISOU 1190 CA THR A 172 10198 25793 10654 -659 65 -4536 C ATOM 1191 C THR A 172 21.180 -17.630 -60.537 1.00123.01 C ANISOU 1191 C THR A 172 10524 25579 10633 -1007 266 -4259 C ATOM 1192 O THR A 172 21.567 -17.695 -59.368 1.00123.13 O ANISOU 1192 O THR A 172 10479 25630 10673 -948 152 -4292 O ATOM 1193 CB THR A 172 22.920 -18.548 -62.160 1.00136.81 C ANISOU 1193 CB THR A 172 11530 28278 12173 -849 184 -5001 C ATOM 1194 OG1 THR A 172 22.910 -17.344 -62.927 1.00138.66 O ANISOU 1194 OG1 THR A 172 11896 28613 12177 -1379 559 -4939 O ATOM 1195 CG2 THR A 172 23.358 -19.721 -63.026 1.00137.74 C ANISOU 1195 CG2 THR A 172 11312 28690 12333 -451 -48 -5332 C ATOM 1196 N ARG A 173 20.429 -16.600 -61.011 1.00115.71 N ANISOU 1196 N ARG A 173 9940 24391 9633 -1344 540 -3994 N ATOM 1197 CA ARG A 173 19.929 -15.502 -60.172 1.00112.74 C ANISOU 1197 CA ARG A 173 9905 23720 9211 -1634 710 -3717 C ATOM 1198 C ARG A 173 18.992 -16.071 -59.115 1.00112.57 C ANISOU 1198 C ARG A 173 10078 23254 9440 -1322 500 -3445 C ATOM 1199 O ARG A 173 19.123 -15.763 -57.939 1.00111.51 O ANISOU 1199 O ARG A 173 9994 23070 9306 -1382 482 -3382 O ATOM 1200 CB ARG A 173 19.220 -14.446 -61.039 1.00110.20 C ANISOU 1200 CB ARG A 173 9944 23162 8763 -1960 973 -3509 C ATOM 1201 CG ARG A 173 18.628 -13.279 -60.259 1.00112.72 C ANISOU 1201 CG ARG A 173 10660 23147 9023 -2220 1123 -3237 C ATOM 1202 CD ARG A 173 17.794 -12.351 -61.128 1.00119.71 C ANISOU 1202 CD ARG A 173 11959 23726 9800 -2444 1308 -3030 C ATOM 1203 NE ARG A 173 16.630 -13.031 -61.704 1.00128.02 N ANISOU 1203 NE ARG A 173 13138 24437 11067 -2104 1187 -2848 N ATOM 1204 CZ ARG A 173 15.722 -12.451 -62.485 1.00137.05 C ANISOU 1204 CZ ARG A 173 14632 25271 12168 -2174 1283 -2664 C ATOM 1205 NH1 ARG A 173 15.819 -11.160 -62.783 1.00120.56 N ANISOU 1205 NH1 ARG A 173 12858 23125 9824 -2571 1486 -2621 N ATOM 1206 NH2 ARG A 173 14.704 -13.152 -62.963 1.00120.27 N ANISOU 1206 NH2 ARG A 173 12573 22881 10244 -1852 1160 -2526 N ATOM 1207 N ASN A 174 18.110 -16.989 -59.543 1.00107.09 N ANISOU 1207 N ASN A 174 9467 22275 8946 -992 325 -3309 N ATOM 1208 CA ASN A 174 17.127 -17.688 -58.717 1.00104.24 C ANISOU 1208 CA ASN A 174 9293 21507 8805 -714 114 -3055 C ATOM 1209 C ASN A 174 17.816 -18.853 -57.936 1.00107.00 C ANISOU 1209 C ASN A 174 9412 21998 9246 -393 -216 -3237 C ATOM 1210 O ASN A 174 17.304 -19.975 -57.854 1.00105.33 O ANISOU 1210 O ASN A 174 9253 21566 9200 -66 -489 -3163 O ATOM 1211 CB ASN A 174 15.986 -18.191 -59.624 1.00103.29 C ANISOU 1211 CB ASN A 174 9345 21078 8824 -537 67 -2873 C ATOM 1212 CG ASN A 174 15.241 -17.087 -60.373 1.00123.83 C ANISOU 1212 CG ASN A 174 12212 23502 11336 -798 343 -2698 C ATOM 1213 OD1 ASN A 174 14.864 -17.251 -61.537 1.00119.95 O ANISOU 1213 OD1 ASN A 174 11753 22966 10855 -748 375 -2695 O ATOM 1214 ND2 ASN A 174 15.056 -15.915 -59.751 1.00112.94 N ANISOU 1214 ND2 ASN A 174 11046 22018 9848 -1075 533 -2567 N ATOM 1215 N ALA A 175 18.991 -18.544 -57.368 1.00104.70 N ANISOU 1215 N ALA A 175 8886 22074 8821 -503 -200 -3483 N ATOM 1216 CA ALA A 175 19.838 -19.411 -56.540 1.00106.03 C ANISOU 1216 CA ALA A 175 8830 22434 9021 -231 -501 -3707 C ATOM 1217 C ALA A 175 20.570 -18.559 -55.500 1.00109.55 C ANISOU 1217 C ALA A 175 9208 23085 9332 -488 -380 -3779 C ATOM 1218 O ALA A 175 20.655 -18.945 -54.329 1.00108.47 O ANISOU 1218 O ALA A 175 9114 22843 9256 -343 -581 -3739 O ATOM 1219 CB ALA A 175 20.822 -20.192 -57.403 1.00109.39 C ANISOU 1219 CB ALA A 175 8880 23283 9400 5 -661 -4110 C ATOM 1220 N ILE A 176 21.025 -17.347 -55.924 1.00106.08 N ANISOU 1220 N ILE A 176 8714 22901 8692 -905 -46 -3858 N ATOM 1221 CA ILE A 176 21.670 -16.354 -55.055 1.00105.84 C ANISOU 1221 CA ILE A 176 8657 23056 8501 -1231 119 -3909 C ATOM 1222 C ILE A 176 20.549 -15.673 -54.212 1.00103.13 C ANISOU 1222 C ILE A 176 8739 22218 8229 -1367 222 -3502 C ATOM 1223 O ILE A 176 20.853 -14.909 -53.299 1.00103.19 O ANISOU 1223 O ILE A 176 8804 22264 8141 -1592 323 -3475 O ATOM 1224 CB ILE A 176 22.559 -15.328 -55.847 1.00111.38 C ANISOU 1224 CB ILE A 176 9185 24207 8926 -1673 426 -4143 C ATOM 1225 CG1 ILE A 176 21.737 -14.331 -56.705 1.00110.60 C ANISOU 1225 CG1 ILE A 176 9435 23844 8743 -2007 718 -3894 C ATOM 1226 CG2 ILE A 176 23.645 -16.048 -56.672 1.00114.05 C ANISOU 1226 CG2 ILE A 176 9054 25100 9181 -1525 323 -4584 C ATOM 1227 CD1 ILE A 176 22.575 -13.228 -57.445 1.00120.12 C ANISOU 1227 CD1 ILE A 176 10567 25445 9626 -2531 1025 -4088 C ATOM 1228 N HIS A 177 19.259 -15.974 -54.552 1.00 94.50 N ANISOU 1228 N HIS A 177 7921 20691 7293 -1221 191 -3211 N ATOM 1229 CA HIS A 177 18.017 -15.619 -53.851 1.00 90.48 C ANISOU 1229 CA HIS A 177 7774 19724 6879 -1245 231 -2851 C ATOM 1230 C HIS A 177 17.579 -16.733 -52.946 1.00 90.39 C ANISOU 1230 C HIS A 177 7800 19499 7044 -925 -68 -2742 C ATOM 1231 O HIS A 177 17.179 -16.495 -51.814 1.00 88.24 O ANISOU 1231 O HIS A 177 7691 19043 6791 -973 -82 -2571 O ATOM 1232 CB HIS A 177 16.859 -15.307 -54.827 1.00 89.58 C ANISOU 1232 CB HIS A 177 7912 19317 6808 -1277 367 -2637 C ATOM 1233 CG HIS A 177 17.049 -14.153 -55.746 1.00 93.31 C ANISOU 1233 CG HIS A 177 8476 19888 7091 -1610 649 -2679 C ATOM 1234 ND1 HIS A 177 17.100 -12.860 -55.266 1.00 95.30 N ANISOU 1234 ND1 HIS A 177 8935 20094 7181 -1942 856 -2606 N ATOM 1235 CD2 HIS A 177 16.928 -14.109 -57.091 1.00 94.62 C ANISOU 1235 CD2 HIS A 177 8649 20091 7211 -1649 737 -2726 C ATOM 1236 CE1 HIS A 177 17.166 -12.086 -56.335 1.00 95.04 C ANISOU 1236 CE1 HIS A 177 9024 20103 6985 -2194 1051 -2637 C ATOM 1237 NE2 HIS A 177 17.053 -12.794 -57.455 1.00 95.17 N ANISOU 1237 NE2 HIS A 177 8922 20173 7064 -2032 994 -2706 N ATOM 1238 N ALA A 178 17.589 -17.970 -53.498 1.00 87.24 N ANISOU 1238 N ALA A 178 7284 19104 6761 -605 -317 -2832 N ATOM 1239 CA ALA A 178 17.189 -19.224 -52.858 1.00 87.25 C ANISOU 1239 CA ALA A 178 7362 18880 6910 -289 -656 -2743 C ATOM 1240 C ALA A 178 17.989 -19.487 -51.595 1.00 94.58 C ANISOU 1240 C ALA A 178 8210 19926 7801 -222 -846 -2858 C ATOM 1241 O ALA A 178 17.562 -20.270 -50.744 1.00 93.92 O ANISOU 1241 O ALA A 178 8292 19595 7799 -57 -1097 -2719 O ATOM 1242 CB ALA A 178 17.369 -20.378 -53.825 1.00 88.92 C ANISOU 1242 CB ALA A 178 7437 19147 7200 22 -889 -2903 C ATOM 1243 N ASN A 179 19.162 -18.841 -51.487 1.00 94.45 N ANISOU 1243 N ASN A 179 7947 20298 7642 -369 -733 -3119 N ATOM 1244 CA ASN A 179 20.042 -18.909 -50.327 1.00 96.15 C ANISOU 1244 CA ASN A 179 8049 20688 7796 -334 -880 -3267 C ATOM 1245 C ASN A 179 19.820 -17.674 -49.449 1.00 98.18 C ANISOU 1245 C ASN A 179 8464 20872 7968 -685 -616 -3090 C ATOM 1246 O ASN A 179 19.807 -17.811 -48.228 1.00 97.46 O ANISOU 1246 O ASN A 179 8474 20667 7888 -651 -747 -3005 O ATOM 1247 CB ASN A 179 21.501 -19.049 -50.737 1.00101.23 C ANISOU 1247 CB ASN A 179 8281 21858 8324 -256 -947 -3710 C ATOM 1248 CG ASN A 179 21.923 -20.401 -51.305 1.00129.74 C ANISOU 1248 CG ASN A 179 11711 25578 12005 181 -1305 -3957 C ATOM 1249 OD1 ASN A 179 23.036 -20.880 -51.041 1.00129.97 O ANISOU 1249 OD1 ASN A 179 11460 25952 11970 395 -1531 -4308 O ATOM 1250 ND2 ASN A 179 21.036 -21.092 -52.019 1.00119.38 N ANISOU 1250 ND2 ASN A 179 10570 23967 10823 356 -1400 -3793 N ATOM 1251 N LEU A 180 19.593 -16.479 -50.068 1.00 93.59 N ANISOU 1251 N LEU A 180 7946 20323 7291 -1016 -264 -3023 N ATOM 1252 CA LEU A 180 19.220 -15.255 -49.347 1.00 92.22 C ANISOU 1252 CA LEU A 180 7991 20017 7033 -1333 -21 -2836 C ATOM 1253 C LEU A 180 17.950 -15.518 -48.564 1.00 96.40 C ANISOU 1253 C LEU A 180 8819 20120 7689 -1234 -100 -2508 C ATOM 1254 O LEU A 180 17.859 -15.135 -47.404 1.00 95.89 O ANISOU 1254 O LEU A 180 8868 19974 7593 -1328 -89 -2408 O ATOM 1255 CB LEU A 180 19.046 -14.056 -50.304 1.00 91.44 C ANISOU 1255 CB LEU A 180 7994 19943 6805 -1658 310 -2805 C ATOM 1256 CG LEU A 180 18.497 -12.739 -49.710 1.00 94.19 C ANISOU 1256 CG LEU A 180 8647 20084 7058 -1956 542 -2600 C ATOM 1257 CD1 LEU A 180 19.495 -12.074 -48.793 1.00 95.60 C ANISOU 1257 CD1 LEU A 180 8731 20506 7087 -2183 604 -2741 C ATOM 1258 CD2 LEU A 180 18.157 -11.771 -50.794 1.00 96.05 C ANISOU 1258 CD2 LEU A 180 9065 20253 7176 -2200 790 -2549 C ATOM 1259 N PHE A 181 17.000 -16.254 -49.173 1.00 94.08 N ANISOU 1259 N PHE A 181 8634 19584 7528 -1043 -195 -2361 N ATOM 1260 CA PHE A 181 15.762 -16.635 -48.502 1.00 93.66 C ANISOU 1260 CA PHE A 181 8833 19178 7577 -966 -279 -2075 C ATOM 1261 C PHE A 181 16.048 -17.728 -47.461 1.00 99.29 C ANISOU 1261 C PHE A 181 9538 19850 8340 -769 -606 -2087 C ATOM 1262 O PHE A 181 15.359 -17.790 -46.442 1.00 97.70 O ANISOU 1262 O PHE A 181 9530 19442 8149 -812 -650 -1885 O ATOM 1263 CB PHE A 181 14.677 -17.104 -49.499 1.00 94.55 C ANISOU 1263 CB PHE A 181 9052 19074 7797 -847 -284 -1932 C ATOM 1264 CG PHE A 181 14.243 -16.146 -50.599 1.00 95.99 C ANISOU 1264 CG PHE A 181 9300 19238 7935 -998 -9 -1901 C ATOM 1265 CD1 PHE A 181 14.324 -14.766 -50.420 1.00 99.67 C ANISOU 1265 CD1 PHE A 181 9869 19736 8267 -1266 250 -1884 C ATOM 1266 CD2 PHE A 181 13.587 -16.617 -51.732 1.00 97.62 C ANISOU 1266 CD2 PHE A 181 9531 19334 8226 -869 -28 -1854 C ATOM 1267 CE1 PHE A 181 13.902 -13.886 -51.423 1.00100.23 C ANISOU 1267 CE1 PHE A 181 10071 19741 8270 -1399 465 -1849 C ATOM 1268 CE2 PHE A 181 13.142 -15.736 -52.722 1.00 99.81 C ANISOU 1268 CE2 PHE A 181 9910 19563 8448 -996 202 -1818 C ATOM 1269 CZ PHE A 181 13.306 -14.377 -52.563 1.00 98.24 C ANISOU 1269 CZ PHE A 181 9831 19395 8101 -1258 438 -1815 C ATOM 1270 N ALA A 182 17.091 -18.556 -47.699 1.00 98.38 N ANISOU 1270 N ALA A 182 9207 19943 8230 -555 -845 -2343 N ATOM 1271 CA ALA A 182 17.478 -19.616 -46.775 1.00 99.93 C ANISOU 1271 CA ALA A 182 9429 20089 8450 -331 -1208 -2391 C ATOM 1272 C ALA A 182 18.153 -19.039 -45.516 1.00106.46 C ANISOU 1272 C ALA A 182 10229 21045 9176 -465 -1188 -2445 C ATOM 1273 O ALA A 182 18.128 -19.692 -44.468 1.00106.92 O ANISOU 1273 O ALA A 182 10427 20961 9237 -359 -1443 -2377 O ATOM 1274 CB ALA A 182 18.403 -20.606 -47.458 1.00102.63 C ANISOU 1274 CB ALA A 182 9549 20631 8814 -18 -1488 -2691 C ATOM 1275 N SER A 183 18.735 -17.816 -45.604 1.00104.24 N ANISOU 1275 N SER A 183 9801 21016 8788 -718 -894 -2559 N ATOM 1276 CA SER A 183 19.389 -17.175 -44.453 1.00105.48 C ANISOU 1276 CA SER A 183 9926 21311 8840 -871 -851 -2618 C ATOM 1277 C SER A 183 18.354 -16.546 -43.521 1.00107.81 C ANISOU 1277 C SER A 183 10515 21318 9129 -1069 -703 -2305 C ATOM 1278 O SER A 183 18.554 -16.534 -42.300 1.00108.80 O ANISOU 1278 O SER A 183 10710 21419 9211 -1098 -798 -2269 O ATOM 1279 CB SER A 183 20.391 -16.118 -44.901 1.00111.01 C ANISOU 1279 CB SER A 183 10383 22392 9402 -1107 -600 -2860 C ATOM 1280 OG SER A 183 19.724 -15.034 -45.523 1.00121.27 O ANISOU 1280 OG SER A 183 11825 23592 10662 -1384 -262 -2706 O ATOM 1281 N PHE A 184 17.260 -16.007 -44.096 1.00101.12 N ANISOU 1281 N PHE A 184 9831 20276 8315 -1193 -478 -2100 N ATOM 1282 CA PHE A 184 16.177 -15.407 -43.322 1.00 98.67 C ANISOU 1282 CA PHE A 184 9773 19725 7991 -1347 -337 -1836 C ATOM 1283 C PHE A 184 15.247 -16.478 -42.719 1.00101.03 C ANISOU 1283 C PHE A 184 10250 19767 8370 -1207 -562 -1633 C ATOM 1284 O PHE A 184 14.661 -16.225 -41.663 1.00 99.79 O ANISOU 1284 O PHE A 184 10255 19491 8171 -1320 -530 -1470 O ATOM 1285 CB PHE A 184 15.360 -14.442 -44.178 1.00 98.65 C ANISOU 1285 CB PHE A 184 9879 19627 7975 -1492 -47 -1732 C ATOM 1286 CG PHE A 184 15.996 -13.100 -44.413 1.00100.38 C ANISOU 1286 CG PHE A 184 10073 20009 8058 -1740 208 -1848 C ATOM 1287 CD1 PHE A 184 15.663 -12.010 -43.626 1.00102.88 C ANISOU 1287 CD1 PHE A 184 10567 20243 8279 -1936 378 -1747 C ATOM 1288 CD2 PHE A 184 16.922 -12.922 -45.427 1.00103.79 C ANISOU 1288 CD2 PHE A 184 10319 20684 8434 -1797 273 -2064 C ATOM 1289 CE1 PHE A 184 16.240 -10.763 -43.855 1.00104.69 C ANISOU 1289 CE1 PHE A 184 10832 20587 8358 -2192 593 -1845 C ATOM 1290 CE2 PHE A 184 17.487 -11.670 -45.664 1.00107.52 C ANISOU 1290 CE2 PHE A 184 10812 21300 8742 -2091 510 -2159 C ATOM 1291 CZ PHE A 184 17.153 -10.602 -44.868 1.00105.22 C ANISOU 1291 CZ PHE A 184 10739 20883 8356 -2289 659 -2043 C ATOM 1292 N VAL A 185 15.110 -17.664 -43.376 1.00 97.67 N ANISOU 1292 N VAL A 185 9809 19263 8039 -986 -791 -1646 N ATOM 1293 CA VAL A 185 14.236 -18.748 -42.891 1.00 97.24 C ANISOU 1293 CA VAL A 185 9961 18953 8032 -896 -1023 -1452 C ATOM 1294 C VAL A 185 14.933 -19.442 -41.701 1.00101.24 C ANISOU 1294 C VAL A 185 10528 19454 8483 -818 -1323 -1499 C ATOM 1295 O VAL A 185 14.245 -19.852 -40.761 1.00101.27 O ANISOU 1295 O VAL A 185 10759 19270 8450 -893 -1431 -1304 O ATOM 1296 CB VAL A 185 13.826 -19.772 -44.002 1.00101.77 C ANISOU 1296 CB VAL A 185 10546 19413 8710 -701 -1183 -1443 C ATOM 1297 CG1 VAL A 185 15.010 -20.601 -44.488 1.00103.66 C ANISOU 1297 CG1 VAL A 185 10619 19792 8975 -437 -1458 -1703 C ATOM 1298 CG2 VAL A 185 12.703 -20.690 -43.530 1.00101.41 C ANISOU 1298 CG2 VAL A 185 10759 19094 8680 -711 -1357 -1203 C ATOM 1299 N LEU A 186 16.289 -19.525 -41.726 1.00 97.42 N ANISOU 1299 N LEU A 186 9842 19201 7974 -682 -1453 -1771 N ATOM 1300 CA LEU A 186 17.084 -20.123 -40.653 1.00 98.28 C ANISOU 1300 CA LEU A 186 9991 19331 8021 -565 -1761 -1865 C ATOM 1301 C LEU A 186 17.000 -19.266 -39.380 1.00100.01 C ANISOU 1301 C LEU A 186 10299 19557 8144 -808 -1605 -1756 C ATOM 1302 O LEU A 186 16.888 -19.812 -38.285 1.00 99.65 O ANISOU 1302 O LEU A 186 10455 19363 8042 -802 -1824 -1653 O ATOM 1303 CB LEU A 186 18.534 -20.274 -41.108 1.00100.31 C ANISOU 1303 CB LEU A 186 9945 19906 8263 -356 -1899 -2232 C ATOM 1304 CG LEU A 186 19.436 -21.137 -40.230 1.00107.85 C ANISOU 1304 CG LEU A 186 10926 20888 9163 -117 -2312 -2396 C ATOM 1305 CD1 LEU A 186 19.008 -22.611 -40.283 1.00109.09 C ANISOU 1305 CD1 LEU A 186 11350 20737 9364 145 -2730 -2311 C ATOM 1306 CD2 LEU A 186 20.880 -21.027 -40.680 1.00112.40 C ANISOU 1306 CD2 LEU A 186 11121 21882 9702 58 -2378 -2809 C ATOM 1307 N LYS A 187 17.019 -17.921 -39.548 1.00 95.34 N ANISOU 1307 N LYS A 187 9589 19118 7518 -1031 -1235 -1773 N ATOM 1308 CA LYS A 187 16.891 -16.918 -38.485 1.00 94.69 C ANISOU 1308 CA LYS A 187 9585 19052 7343 -1271 -1040 -1681 C ATOM 1309 C LYS A 187 15.492 -16.953 -37.838 1.00 98.51 C ANISOU 1309 C LYS A 187 10336 19278 7816 -1401 -979 -1381 C ATOM 1310 O LYS A 187 15.391 -17.128 -36.622 1.00 99.16 O ANISOU 1310 O LYS A 187 10564 19289 7824 -1470 -1086 -1287 O ATOM 1311 CB LYS A 187 17.163 -15.505 -39.049 1.00 95.63 C ANISOU 1311 CB LYS A 187 9566 19354 7417 -1469 -680 -1773 C ATOM 1312 CG LYS A 187 16.883 -14.376 -38.052 1.00 99.00 C ANISOU 1312 CG LYS A 187 10112 19758 7744 -1714 -465 -1668 C ATOM 1313 CD LYS A 187 16.797 -13.032 -38.748 1.00 99.17 C ANISOU 1313 CD LYS A 187 10120 19848 7715 -1911 -130 -1697 C ATOM 1314 CE LYS A 187 16.338 -11.934 -37.823 1.00 94.51 C ANISOU 1314 CE LYS A 187 9697 19185 7026 -2116 61 -1583 C ATOM 1315 NZ LYS A 187 16.139 -10.655 -38.555 1.00 93.80 N ANISOU 1315 NZ LYS A 187 9677 19092 6871 -2287 344 -1597 N ATOM 1316 N ALA A 188 14.427 -16.732 -38.647 1.00 94.13 N ANISOU 1316 N ALA A 188 9830 18617 7317 -1446 -796 -1252 N ATOM 1317 CA ALA A 188 13.025 -16.671 -38.208 1.00 93.38 C ANISOU 1317 CA ALA A 188 9927 18353 7200 -1574 -698 -1012 C ATOM 1318 C ALA A 188 12.620 -17.923 -37.421 1.00 99.09 C ANISOU 1318 C ALA A 188 10842 18914 7895 -1552 -993 -873 C ATOM 1319 O ALA A 188 11.924 -17.805 -36.413 1.00 98.45 O ANISOU 1319 O ALA A 188 10908 18777 7720 -1721 -952 -722 O ATOM 1320 CB ALA A 188 12.107 -16.505 -39.410 1.00 92.62 C ANISOU 1320 CB ALA A 188 9816 18195 7182 -1549 -536 -953 C ATOM 1321 N SER A 189 13.069 -19.112 -37.877 1.00 97.05 N ANISOU 1321 N SER A 189 10600 18581 7693 -1352 -1300 -933 N ATOM 1322 CA SER A 189 12.798 -20.392 -37.215 1.00 98.04 C ANISOU 1322 CA SER A 189 10975 18508 7766 -1326 -1641 -810 C ATOM 1323 C SER A 189 13.574 -20.499 -35.894 1.00101.16 C ANISOU 1323 C SER A 189 11468 18918 8051 -1349 -1829 -847 C ATOM 1324 O SER A 189 13.065 -21.080 -34.937 1.00100.87 O ANISOU 1324 O SER A 189 11695 18725 7906 -1477 -1988 -679 O ATOM 1325 CB SER A 189 13.156 -21.553 -38.135 1.00103.26 C ANISOU 1325 CB SER A 189 11649 19073 8512 -1066 -1942 -899 C ATOM 1326 OG SER A 189 14.506 -21.462 -38.560 1.00115.35 O ANISOU 1326 OG SER A 189 12953 20788 10088 -841 -2034 -1177 O ATOM 1327 N SER A 190 14.795 -19.931 -35.840 1.00 97.41 N ANISOU 1327 N SER A 190 10784 18644 7583 -1249 -1808 -1072 N ATOM 1328 CA SER A 190 15.599 -19.933 -34.623 1.00 98.58 C ANISOU 1328 CA SER A 190 10991 18838 7628 -1254 -1975 -1137 C ATOM 1329 C SER A 190 14.931 -19.074 -33.554 1.00102.57 C ANISOU 1329 C SER A 190 11598 19343 8031 -1548 -1731 -967 C ATOM 1330 O SER A 190 14.814 -19.524 -32.416 1.00104.09 O ANISOU 1330 O SER A 190 12016 19425 8110 -1633 -1912 -857 O ATOM 1331 CB SER A 190 17.017 -19.448 -34.897 1.00101.22 C ANISOU 1331 CB SER A 190 11030 19445 7983 -1105 -1973 -1443 C ATOM 1332 OG SER A 190 17.703 -20.336 -35.762 1.00108.46 O ANISOU 1332 OG SER A 190 11840 20400 8970 -803 -2244 -1640 O ATOM 1333 N VAL A 191 14.412 -17.884 -33.938 1.00 96.70 N ANISOU 1333 N VAL A 191 10723 18706 7313 -1698 -1341 -941 N ATOM 1334 CA VAL A 191 13.721 -16.961 -33.029 1.00 95.47 C ANISOU 1334 CA VAL A 191 10642 18573 7060 -1943 -1093 -813 C ATOM 1335 C VAL A 191 12.445 -17.637 -32.463 1.00 99.00 C ANISOU 1335 C VAL A 191 11328 18859 7430 -2090 -1155 -575 C ATOM 1336 O VAL A 191 12.144 -17.434 -31.297 1.00 99.10 O ANISOU 1336 O VAL A 191 11465 18876 7313 -2267 -1131 -481 O ATOM 1337 CB VAL A 191 13.379 -15.611 -33.718 1.00 97.88 C ANISOU 1337 CB VAL A 191 10801 18988 7401 -2023 -713 -854 C ATOM 1338 CG1 VAL A 191 12.638 -14.668 -32.768 1.00 97.07 C ANISOU 1338 CG1 VAL A 191 10787 18908 7188 -2229 -489 -750 C ATOM 1339 CG2 VAL A 191 14.635 -14.933 -34.262 1.00 97.97 C ANISOU 1339 CG2 VAL A 191 10605 19176 7444 -1959 -641 -1083 C ATOM 1340 N LEU A 192 11.735 -18.465 -33.259 1.00 96.03 N ANISOU 1340 N LEU A 192 11014 18359 7112 -2038 -1243 -488 N ATOM 1341 CA LEU A 192 10.514 -19.146 -32.787 1.00 96.74 C ANISOU 1341 CA LEU A 192 11322 18331 7103 -2228 -1297 -275 C ATOM 1342 C LEU A 192 10.836 -20.348 -31.884 1.00103.06 C ANISOU 1342 C LEU A 192 12409 18963 7786 -2262 -1683 -192 C ATOM 1343 O LEU A 192 9.917 -20.914 -31.299 1.00103.51 O ANISOU 1343 O LEU A 192 12689 18932 7708 -2489 -1742 -10 O ATOM 1344 CB LEU A 192 9.611 -19.631 -33.946 1.00 96.13 C ANISOU 1344 CB LEU A 192 11228 18184 7113 -2189 -1263 -211 C ATOM 1345 CG LEU A 192 8.969 -18.577 -34.871 1.00 98.84 C ANISOU 1345 CG LEU A 192 11359 18650 7544 -2171 -910 -256 C ATOM 1346 CD1 LEU A 192 8.099 -19.253 -35.897 1.00 98.54 C ANISOU 1346 CD1 LEU A 192 11334 18530 7577 -2132 -937 -186 C ATOM 1347 CD2 LEU A 192 8.113 -17.559 -34.092 1.00100.55 C ANISOU 1347 CD2 LEU A 192 11558 19000 7648 -2373 -629 -202 C ATOM 1348 N VAL A 193 12.112 -20.746 -31.781 1.00101.77 N ANISOU 1348 N VAL A 193 12254 18764 7651 -2046 -1956 -337 N ATOM 1349 CA VAL A 193 12.531 -21.835 -30.889 1.00104.85 C ANISOU 1349 CA VAL A 193 12957 18967 7913 -2032 -2370 -284 C ATOM 1350 C VAL A 193 13.005 -21.179 -29.558 1.00111.20 C ANISOU 1350 C VAL A 193 13786 19870 8594 -2159 -2322 -299 C ATOM 1351 O VAL A 193 12.774 -21.736 -28.483 1.00112.05 O ANISOU 1351 O VAL A 193 14200 19848 8528 -2329 -2515 -160 O ATOM 1352 CB VAL A 193 13.599 -22.764 -31.541 1.00110.06 C ANISOU 1352 CB VAL A 193 13631 19527 8660 -1671 -2757 -462 C ATOM 1353 CG1 VAL A 193 14.062 -23.853 -30.577 1.00112.71 C ANISOU 1353 CG1 VAL A 193 14344 19638 8843 -1620 -3232 -425 C ATOM 1354 CG2 VAL A 193 13.053 -23.400 -32.816 1.00109.27 C ANISOU 1354 CG2 VAL A 193 13523 19325 8672 -1564 -2796 -435 C ATOM 1355 N ILE A 194 13.595 -19.955 -29.644 1.00108.29 N ANISOU 1355 N ILE A 194 13118 19730 8298 -2113 -2047 -457 N ATOM 1356 CA ILE A 194 14.010 -19.155 -28.478 1.00109.09 C ANISOU 1356 CA ILE A 194 13206 19949 8294 -2240 -1947 -484 C ATOM 1357 C ILE A 194 12.735 -18.729 -27.742 1.00114.49 C ANISOU 1357 C ILE A 194 14007 20645 8849 -2564 -1707 -279 C ATOM 1358 O ILE A 194 12.559 -19.101 -26.588 1.00115.91 O ANISOU 1358 O ILE A 194 14425 20756 8858 -2737 -1843 -163 O ATOM 1359 CB ILE A 194 14.920 -17.934 -28.863 1.00110.76 C ANISOU 1359 CB ILE A 194 13086 20399 8600 -2144 -1707 -706 C ATOM 1360 CG1 ILE A 194 16.098 -18.312 -29.821 1.00111.63 C ANISOU 1360 CG1 ILE A 194 13000 20584 8832 -1840 -1893 -950 C ATOM 1361 CG2 ILE A 194 15.380 -17.129 -27.640 1.00111.18 C ANISOU 1361 CG2 ILE A 194 13139 20564 8538 -2278 -1623 -739 C ATOM 1362 CD1 ILE A 194 17.067 -19.450 -29.378 1.00120.26 C ANISOU 1362 CD1 ILE A 194 14222 21593 9880 -1607 -2370 -1062 C ATOM 1363 N ASP A 195 11.812 -18.038 -28.456 1.00110.63 N ANISOU 1363 N ASP A 195 13361 20246 8425 -2637 -1376 -246 N ATOM 1364 CA ASP A 195 10.487 -17.605 -27.988 1.00111.15 C ANISOU 1364 CA ASP A 195 13470 20384 8378 -2899 -1128 -104 C ATOM 1365 C ASP A 195 9.693 -18.774 -27.363 1.00117.60 C ANISOU 1365 C ASP A 195 14580 21073 9029 -3117 -1336 92 C ATOM 1366 O ASP A 195 9.082 -18.608 -26.299 1.00118.18 O ANISOU 1366 O ASP A 195 14763 21222 8917 -3382 -1255 192 O ATOM 1367 CB ASP A 195 9.698 -17.012 -29.179 1.00111.80 C ANISOU 1367 CB ASP A 195 13355 20542 8581 -2842 -850 -133 C ATOM 1368 CG ASP A 195 8.235 -16.670 -28.933 1.00128.40 C ANISOU 1368 CG ASP A 195 15456 22753 10577 -3052 -618 -32 C ATOM 1369 OD1 ASP A 195 7.897 -16.256 -27.790 1.00131.94 O ANISOU 1369 OD1 ASP A 195 15960 23308 10863 -3245 -527 7 O ATOM 1370 OD2 ASP A 195 7.441 -16.734 -29.902 1.00132.57 O ANISOU 1370 OD2 ASP A 195 15899 23291 11180 -3008 -514 -20 O ATOM 1371 N GLY A 196 9.712 -19.923 -28.046 1.00114.92 N ANISOU 1371 N GLY A 196 14374 20549 8740 -3021 -1600 138 N ATOM 1372 CA GLY A 196 9.019 -21.137 -27.634 1.00116.89 C ANISOU 1372 CA GLY A 196 14956 20634 8825 -3239 -1839 326 C ATOM 1373 C GLY A 196 9.541 -21.730 -26.345 1.00124.36 C ANISOU 1373 C GLY A 196 16226 21449 9576 -3362 -2138 399 C ATOM 1374 O GLY A 196 8.764 -21.939 -25.412 1.00125.70 O ANISOU 1374 O GLY A 196 16601 21639 9521 -3709 -2115 555 O ATOM 1375 N LEU A 197 10.868 -21.983 -26.275 1.00122.16 N ANISOU 1375 N LEU A 197 15989 21061 9366 -3080 -2420 269 N ATOM 1376 CA LEU A 197 11.526 -22.571 -25.099 1.00124.70 C ANISOU 1376 CA LEU A 197 16638 21232 9512 -3123 -2763 306 C ATOM 1377 C LEU A 197 11.547 -21.613 -23.895 1.00129.18 C ANISOU 1377 C LEU A 197 17146 21982 9953 -3324 -2544 314 C ATOM 1378 O LEU A 197 11.554 -22.097 -22.759 1.00130.79 O ANISOU 1378 O LEU A 197 17679 22077 9938 -3520 -2752 427 O ATOM 1379 CB LEU A 197 12.977 -23.003 -25.411 1.00125.61 C ANISOU 1379 CB LEU A 197 16745 21241 9742 -2708 -3119 104 C ATOM 1380 CG LEU A 197 13.219 -24.430 -25.966 1.00132.34 C ANISOU 1380 CG LEU A 197 17897 21793 10593 -2505 -3590 112 C ATOM 1381 CD1 LEU A 197 12.846 -25.496 -24.944 1.00135.85 C ANISOU 1381 CD1 LEU A 197 18906 21948 10762 -2752 -3952 322 C ATOM 1382 CD2 LEU A 197 12.512 -24.681 -27.286 1.00133.38 C ANISOU 1382 CD2 LEU A 197 17904 21907 10867 -2464 -3468 141 C ATOM 1383 N LEU A 198 11.533 -20.274 -24.126 1.00123.94 N ANISOU 1383 N LEU A 198 16107 21576 9408 -3288 -2144 199 N ATOM 1384 CA LEU A 198 11.553 -19.293 -23.030 1.00123.79 C ANISOU 1384 CA LEU A 198 16026 21731 9276 -3456 -1930 188 C ATOM 1385 C LEU A 198 10.181 -19.231 -22.301 1.00128.61 C ANISOU 1385 C LEU A 198 16756 22437 9673 -3854 -1736 368 C ATOM 1386 O LEU A 198 10.079 -18.561 -21.269 1.00128.02 O ANISOU 1386 O LEU A 198 16677 22503 9462 -4027 -1589 374 O ATOM 1387 CB LEU A 198 11.954 -17.878 -23.508 1.00121.37 C ANISOU 1387 CB LEU A 198 15338 21642 9135 -3306 -1590 7 C ATOM 1388 CG LEU A 198 13.422 -17.659 -23.961 1.00125.39 C ANISOU 1388 CG LEU A 198 15676 22168 9799 -2993 -1716 -210 C ATOM 1389 CD1 LEU A 198 13.636 -16.233 -24.404 1.00123.37 C ANISOU 1389 CD1 LEU A 198 15107 22117 9652 -2949 -1355 -354 C ATOM 1390 CD2 LEU A 198 14.424 -17.977 -22.850 1.00129.88 C ANISOU 1390 CD2 LEU A 198 16407 22686 10253 -2957 -2006 -258 C ATOM 1391 N ARG A 199 9.158 -19.962 -22.800 1.00126.48 N ANISOU 1391 N ARG A 199 16589 22111 9355 -4010 -1749 497 N ATOM 1392 CA ARG A 199 7.856 -20.041 -22.139 1.00127.78 C ANISOU 1392 CA ARG A 199 16854 22413 9283 -4418 -1588 643 C ATOM 1393 C ARG A 199 7.360 -21.509 -22.186 1.00133.78 C ANISOU 1393 C ARG A 199 17990 22952 9888 -4634 -1895 826 C ATOM 1394 O ARG A 199 6.496 -21.866 -22.994 1.00133.00 O ANISOU 1394 O ARG A 199 17840 22877 9817 -4710 -1817 876 O ATOM 1395 CB ARG A 199 6.827 -19.057 -22.755 1.00126.68 C ANISOU 1395 CB ARG A 199 16359 22556 9220 -4439 -1161 572 C ATOM 1396 CG ARG A 199 5.471 -18.930 -21.999 1.00139.84 C ANISOU 1396 CG ARG A 199 18029 24479 10623 -4845 -944 652 C ATOM 1397 CD ARG A 199 5.508 -18.296 -20.588 1.00152.38 C ANISOU 1397 CD ARG A 199 19651 26240 12005 -5047 -837 643 C ATOM 1398 NE ARG A 199 6.220 -19.102 -19.583 1.00160.39 N ANISOU 1398 NE ARG A 199 21044 27046 12852 -5195 -1167 762 N ATOM 1399 CZ ARG A 199 6.350 -18.772 -18.298 1.00167.70 C ANISOU 1399 CZ ARG A 199 22073 28070 13574 -5392 -1144 781 C ATOM 1400 NH1 ARG A 199 5.801 -17.655 -17.834 1.00152.11 N ANISOU 1400 NH1 ARG A 199 19843 26415 11537 -5468 -802 681 N ATOM 1401 NH2 ARG A 199 7.018 -19.562 -17.467 1.00149.52 N ANISOU 1401 NH2 ARG A 199 20149 25543 11119 -5502 -1482 890 N ATOM 1402 N THR A 200 7.961 -22.354 -21.321 1.00132.48 N ANISOU 1402 N THR A 200 18232 22554 9550 -4723 -2269 920 N ATOM 1403 CA THR A 200 7.643 -23.778 -21.130 1.00159.27 C ANISOU 1403 CA THR A 200 22112 25671 12734 -4961 -2637 1108 C ATOM 1404 C THR A 200 7.706 -24.141 -19.634 1.00192.52 C ANISOU 1404 C THR A 200 26726 29809 16614 -5301 -2824 1240 C ATOM 1405 O THR A 200 8.201 -23.365 -18.811 1.00149.93 O ANISOU 1405 O THR A 200 21225 24546 11196 -5269 -2718 1167 O ATOM 1406 CB THR A 200 8.578 -24.698 -21.947 1.00166.69 C ANISOU 1406 CB THR A 200 23233 26266 13836 -4579 -3061 1058 C ATOM 1407 OG1 THR A 200 9.936 -24.308 -21.731 1.00165.29 O ANISOU 1407 OG1 THR A 200 22963 26048 13793 -4204 -3205 886 O ATOM 1408 CG2 THR A 200 8.274 -24.683 -23.438 1.00163.29 C ANISOU 1408 CG2 THR A 200 22519 25867 13658 -4353 -2929 984 C ATOM 1409 N LEU A 216 16.851 -33.562 -16.195 1.00191.21 N ANISOU 1409 N LEU A 216 31470 25820 15364 -2723 -8872 882 N ATOM 1410 CA LEU A 216 15.448 -33.716 -16.571 1.00190.22 C ANISOU 1410 CA LEU A 216 31433 25689 15152 -3300 -8534 1183 C ATOM 1411 C LEU A 216 15.000 -32.542 -17.460 1.00190.73 C ANISOU 1411 C LEU A 216 30619 26281 15567 -3325 -7799 1099 C ATOM 1412 O LEU A 216 14.737 -32.741 -18.650 1.00188.45 O ANISOU 1412 O LEU A 216 30111 26010 15480 -3164 -7718 1047 O ATOM 1413 CB LEU A 216 14.546 -33.820 -15.314 1.00192.24 C ANISOU 1413 CB LEU A 216 32195 25853 14995 -4043 -8452 1528 C ATOM 1414 CG LEU A 216 14.779 -35.006 -14.355 1.00197.87 C ANISOU 1414 CG LEU A 216 33125 26410 15647 -3664 -8602 1475 C ATOM 1415 CD1 LEU A 216 13.988 -34.834 -13.075 1.00197.37 C ANISOU 1415 CD1 LEU A 216 33082 26512 15399 -4096 -8194 1658 C ATOM 1416 CD2 LEU A 216 14.437 -36.342 -15.007 1.00199.69 C ANISOU 1416 CD2 LEU A 216 33310 26537 16027 -3308 -8599 1440 C ATOM 1417 N SER A 217 14.933 -31.320 -16.880 1.00186.33 N ANISOU 1417 N SER A 217 29591 26134 15070 -3510 -7290 1080 N ATOM 1418 CA SER A 217 14.532 -30.084 -17.565 1.00182.15 C ANISOU 1418 CA SER A 217 28281 26092 14836 -3544 -6605 997 C ATOM 1419 C SER A 217 15.618 -29.611 -18.535 1.00184.03 C ANISOU 1419 C SER A 217 27956 26522 15443 -2907 -6584 646 C ATOM 1420 O SER A 217 15.295 -29.083 -19.602 1.00179.95 O ANISOU 1420 O SER A 217 26946 26246 15182 -2833 -6202 575 O ATOM 1421 CB SER A 217 14.234 -28.985 -16.546 1.00184.86 C ANISOU 1421 CB SER A 217 28385 26762 15091 -3899 -6160 1063 C ATOM 1422 OG SER A 217 13.845 -27.766 -17.162 1.00189.80 O ANISOU 1422 OG SER A 217 28315 27824 15976 -3918 -5536 977 O ATOM 1423 N ASP A 218 16.905 -29.833 -18.169 1.00182.98 N ANISOU 1423 N ASP A 218 27913 26295 15317 -2455 -7013 414 N ATOM 1424 CA ASP A 218 18.102 -29.461 -18.937 1.00181.67 C ANISOU 1424 CA ASP A 218 27237 26347 15442 -1851 -7062 33 C ATOM 1425 C ASP A 218 18.091 -30.146 -20.330 1.00184.95 C ANISOU 1425 C ASP A 218 27588 26651 16033 -1535 -7226 -71 C ATOM 1426 O ASP A 218 18.804 -29.705 -21.234 1.00183.18 O ANISOU 1426 O ASP A 218 26829 26698 16074 -1132 -7109 -365 O ATOM 1427 CB ASP A 218 19.376 -29.843 -18.142 1.00187.05 C ANISOU 1427 CB ASP A 218 28160 26898 16012 -1459 -7605 -183 C ATOM 1428 CG ASP A 218 20.700 -29.286 -18.656 1.00195.60 C ANISOU 1428 CG ASP A 218 28657 28319 17344 -899 -7614 -615 C ATOM 1429 OD1 ASP A 218 20.674 -28.360 -19.498 1.00191.52 O ANISOU 1429 OD1 ASP A 218 27503 28183 17083 -879 -7113 -732 O ATOM 1430 OD2 ASP A 218 21.756 -29.690 -18.125 1.00205.34 O ANISOU 1430 OD2 ASP A 218 30063 29467 18491 -519 -8100 -837 O ATOM 1431 N GLY A 219 17.231 -31.161 -20.498 1.00182.40 N ANISOU 1431 N GLY A 219 27796 25961 15548 -1768 -7457 177 N ATOM 1432 CA GLY A 219 17.021 -31.855 -21.766 1.00181.73 C ANISOU 1432 CA GLY A 219 27715 25736 15597 -1550 -7598 131 C ATOM 1433 C GLY A 219 16.269 -30.998 -22.771 1.00180.59 C ANISOU 1433 C GLY A 219 26976 25939 15700 -1719 -6956 162 C ATOM 1434 O GLY A 219 16.069 -31.406 -23.919 1.00179.15 O ANISOU 1434 O GLY A 219 26698 25706 15664 -1545 -6984 113 O ATOM 1435 N ALA A 220 15.853 -29.790 -22.331 1.00174.17 N ANISOU 1435 N ALA A 220 25778 25473 14925 -2045 -6390 235 N ATOM 1436 CA ALA A 220 15.150 -28.780 -23.120 1.00169.66 C ANISOU 1436 CA ALA A 220 24646 25252 14564 -2210 -5762 253 C ATOM 1437 C ALA A 220 15.776 -27.377 -22.914 1.00170.39 C ANISOU 1437 C ALA A 220 24169 25756 14813 -2114 -5356 61 C ATOM 1438 O ALA A 220 15.807 -26.590 -23.861 1.00167.06 O ANISOU 1438 O ALA A 220 23234 25611 14631 -1990 -4985 -74 O ATOM 1439 CB ALA A 220 13.675 -28.760 -22.748 1.00169.95 C ANISOU 1439 CB ALA A 220 24880 25270 14421 -2811 -5471 581 C ATOM 1440 N VAL A 221 16.287 -27.080 -21.683 1.00167.61 N ANISOU 1440 N VAL A 221 23943 25429 14312 -2180 -5445 49 N ATOM 1441 CA VAL A 221 16.913 -25.792 -21.309 1.00165.08 C ANISOU 1441 CA VAL A 221 23160 25468 14095 -2128 -5107 -121 C ATOM 1442 C VAL A 221 18.185 -25.563 -22.174 1.00167.62 C ANISOU 1442 C VAL A 221 23056 25981 14649 -1608 -5197 -490 C ATOM 1443 O VAL A 221 18.410 -24.446 -22.650 1.00164.08 O ANISOU 1443 O VAL A 221 22095 25873 14376 -1582 -4776 -631 O ATOM 1444 CB VAL A 221 17.241 -25.728 -19.784 1.00170.97 C ANISOU 1444 CB VAL A 221 24203 26151 14605 -2287 -5274 -59 C ATOM 1445 CG1 VAL A 221 17.959 -24.430 -19.421 1.00169.11 C ANISOU 1445 CG1 VAL A 221 23503 26277 14474 -2216 -4956 -252 C ATOM 1446 CG2 VAL A 221 15.979 -25.882 -18.939 1.00171.30 C ANISOU 1446 CG2 VAL A 221 24619 26075 14392 -2846 -5140 283 C ATOM 1447 N ALA A 222 18.981 -26.626 -22.394 1.00167.00 N ANISOU 1447 N ALA A 222 23208 25694 14551 -1208 -5751 -653 N ATOM 1448 CA ALA A 222 20.181 -26.581 -23.233 1.00167.02 C ANISOU 1448 CA ALA A 222 22816 25905 14738 -700 -5893 -1038 C ATOM 1449 C ALA A 222 19.815 -26.749 -24.721 1.00168.67 C ANISOU 1449 C ALA A 222 22786 26159 15143 -577 -5747 -1082 C ATOM 1450 O ALA A 222 20.666 -26.559 -25.594 1.00167.71 O ANISOU 1450 O ALA A 222 22252 26284 15185 -222 -5747 -1397 O ATOM 1451 CB ALA A 222 21.162 -27.664 -22.802 1.00171.99 C ANISOU 1451 CB ALA A 222 23799 26307 15243 -283 -6582 -1227 C ATOM 1452 N GLY A 223 18.552 -27.084 -24.982 1.00164.39 N ANISOU 1452 N GLY A 223 22489 25408 14565 -894 -5613 -778 N ATOM 1453 CA GLY A 223 18.017 -27.281 -26.324 1.00162.89 C ANISOU 1453 CA GLY A 223 22132 25221 14538 -835 -5468 -768 C ATOM 1454 C GLY A 223 17.904 -26.015 -27.154 1.00164.23 C ANISOU 1454 C GLY A 223 21706 25775 14919 -899 -4886 -860 C ATOM 1455 O GLY A 223 17.977 -26.081 -28.385 1.00162.80 O ANISOU 1455 O GLY A 223 21271 25681 14904 -699 -4817 -987 O ATOM 1456 N CYS A 224 17.698 -24.851 -26.496 1.00159.57 N ANISOU 1456 N CYS A 224 20919 25402 14307 -1186 -4473 -792 N ATOM 1457 CA CYS A 224 17.588 -23.567 -27.198 1.00156.40 C ANISOU 1457 CA CYS A 224 20022 25331 14071 -1268 -3939 -871 C ATOM 1458 C CYS A 224 18.965 -22.892 -27.253 1.00157.60 C ANISOU 1458 C CYS A 224 19792 25791 14297 -1017 -3919 -1206 C ATOM 1459 O CYS A 224 19.154 -21.953 -28.030 1.00155.22 O ANISOU 1459 O CYS A 224 19087 25763 14128 -1021 -3559 -1337 O ATOM 1460 CB CYS A 224 16.551 -22.660 -26.543 1.00155.78 C ANISOU 1460 CB CYS A 224 19954 25316 13919 -1700 -3513 -635 C ATOM 1461 SG CYS A 224 17.014 -22.064 -24.896 1.00161.38 S ANISOU 1461 SG CYS A 224 20762 26101 14453 -1868 -3512 -623 S ATOM 1462 N ARG A 225 19.911 -23.349 -26.400 1.00154.50 N ANISOU 1462 N ARG A 225 19544 25362 13796 -824 -4309 -1348 N ATOM 1463 CA ARG A 225 21.283 -22.838 -26.360 1.00154.07 C ANISOU 1463 CA ARG A 225 19131 25629 13779 -577 -4350 -1700 C ATOM 1464 C ARG A 225 21.972 -23.135 -27.686 1.00155.32 C ANISOU 1464 C ARG A 225 18966 25967 14082 -224 -4443 -1998 C ATOM 1465 O ARG A 225 22.647 -22.261 -28.231 1.00153.88 O ANISOU 1465 O ARG A 225 18329 26156 13983 -193 -4174 -2236 O ATOM 1466 CB ARG A 225 22.062 -23.445 -25.181 1.00157.71 C ANISOU 1466 CB ARG A 225 19864 25980 14079 -405 -4818 -1791 C ATOM 1467 N VAL A 226 21.725 -24.348 -28.243 1.00151.11 N ANISOU 1467 N VAL A 226 18683 25169 13562 4 -4805 -1972 N ATOM 1468 CA VAL A 226 22.264 -24.791 -29.536 1.00150.38 C ANISOU 1468 CA VAL A 226 18328 25213 13595 359 -4934 -2245 C ATOM 1469 C VAL A 226 21.457 -24.122 -30.675 1.00147.58 C ANISOU 1469 C VAL A 226 17725 24961 13388 139 -4441 -2125 C ATOM 1470 O VAL A 226 21.946 -24.031 -31.801 1.00146.27 O ANISOU 1470 O VAL A 226 17212 25031 13333 337 -4371 -2367 O ATOM 1471 CB VAL A 226 22.292 -26.345 -29.694 1.00157.27 C ANISOU 1471 CB VAL A 226 19605 25735 14416 704 -5537 -2268 C ATOM 1472 CG1 VAL A 226 23.168 -26.994 -28.622 1.00160.73 C ANISOU 1472 CG1 VAL A 226 20309 26066 14696 975 -6071 -2424 C ATOM 1473 CG2 VAL A 226 20.888 -26.954 -29.692 1.00156.10 C ANISOU 1473 CG2 VAL A 226 19923 25160 14227 429 -5541 -1858 C ATOM 1474 N ALA A 227 20.231 -23.656 -30.368 1.00140.22 N ANISOU 1474 N ALA A 227 16970 23870 12439 -261 -4113 -1773 N ATOM 1475 CA ALA A 227 19.369 -22.971 -31.324 1.00136.46 C ANISOU 1475 CA ALA A 227 16303 23465 12081 -471 -3660 -1646 C ATOM 1476 C ALA A 227 19.764 -21.499 -31.455 1.00137.54 C ANISOU 1476 C ALA A 227 16042 23956 12261 -634 -3204 -1769 C ATOM 1477 O ALA A 227 19.640 -20.940 -32.546 1.00136.20 O ANISOU 1477 O ALA A 227 15609 23942 12197 -661 -2913 -1832 O ATOM 1478 CB ALA A 227 17.913 -23.091 -30.906 1.00135.89 C ANISOU 1478 CB ALA A 227 16566 23118 11950 -806 -3526 -1265 C ATOM 1479 N ALA A 228 20.267 -20.877 -30.358 1.00133.00 N ANISOU 1479 N ALA A 228 15449 23496 11588 -748 -3160 -1808 N ATOM 1480 CA ALA A 228 20.718 -19.478 -30.344 1.00130.96 C ANISOU 1480 CA ALA A 228 14869 23553 11337 -926 -2766 -1927 C ATOM 1481 C ALA A 228 21.949 -19.286 -31.251 1.00135.12 C ANISOU 1481 C ALA A 228 14985 24434 11920 -710 -2777 -2306 C ATOM 1482 O ALA A 228 22.238 -18.164 -31.684 1.00133.80 O ANISOU 1482 O ALA A 228 14542 24531 11766 -884 -2418 -2409 O ATOM 1483 CB ALA A 228 21.039 -19.051 -28.923 1.00132.52 C ANISOU 1483 CB ALA A 228 15172 23775 11405 -1063 -2792 -1898 C ATOM 1484 N VAL A 229 22.651 -20.404 -31.550 1.00132.96 N ANISOU 1484 N VAL A 229 14692 24168 11657 -337 -3204 -2521 N ATOM 1485 CA VAL A 229 23.827 -20.476 -32.421 1.00133.70 C ANISOU 1485 CA VAL A 229 14385 24629 11784 -74 -3291 -2926 C ATOM 1486 C VAL A 229 23.410 -20.107 -33.836 1.00135.12 C ANISOU 1486 C VAL A 229 14366 24902 12072 -156 -2978 -2921 C ATOM 1487 O VAL A 229 23.965 -19.172 -34.410 1.00134.25 O ANISOU 1487 O VAL A 229 13913 25141 11956 -292 -2675 -3109 O ATOM 1488 CB VAL A 229 24.488 -21.886 -32.370 1.00140.46 C ANISOU 1488 CB VAL A 229 15339 25410 12618 395 -3879 -3143 C ATOM 1489 CG1 VAL A 229 25.713 -21.958 -33.276 1.00142.23 C ANISOU 1489 CG1 VAL A 229 15096 26085 12861 688 -3969 -3613 C ATOM 1490 CG2 VAL A 229 24.858 -22.277 -30.944 1.00142.49 C ANISOU 1490 CG2 VAL A 229 15860 25530 12751 479 -4224 -3131 C ATOM 1491 N PHE A 230 22.392 -20.822 -34.370 1.00130.52 N ANISOU 1491 N PHE A 230 14027 23996 11567 -109 -3047 -2692 N ATOM 1492 CA PHE A 230 21.849 -20.641 -35.716 1.00128.45 C ANISOU 1492 CA PHE A 230 13640 23755 11411 -156 -2800 -2653 C ATOM 1493 C PHE A 230 21.279 -19.244 -35.922 1.00129.20 C ANISOU 1493 C PHE A 230 13652 23926 11511 -541 -2278 -2501 C ATOM 1494 O PHE A 230 21.300 -18.746 -37.045 1.00128.29 O ANISOU 1494 O PHE A 230 13327 23974 11445 -599 -2031 -2586 O ATOM 1495 CB PHE A 230 20.741 -21.668 -36.017 1.00129.65 C ANISOU 1495 CB PHE A 230 14127 23507 11626 -76 -2985 -2394 C ATOM 1496 CG PHE A 230 21.071 -23.120 -35.775 1.00134.09 C ANISOU 1496 CG PHE A 230 14912 23872 12163 282 -3541 -2477 C ATOM 1497 CD1 PHE A 230 22.062 -23.757 -36.515 1.00139.56 C ANISOU 1497 CD1 PHE A 230 15379 24766 12883 668 -3823 -2835 C ATOM 1498 CD2 PHE A 230 20.284 -23.894 -34.931 1.00136.91 C ANISOU 1498 CD2 PHE A 230 15734 23827 12456 226 -3789 -2193 C ATOM 1499 CE1 PHE A 230 22.343 -25.111 -36.318 1.00143.36 C ANISOU 1499 CE1 PHE A 230 16113 25028 13329 1040 -4380 -2925 C ATOM 1500 CE2 PHE A 230 20.553 -25.253 -34.746 1.00142.63 C ANISOU 1500 CE2 PHE A 230 16747 24313 13134 545 -4337 -2255 C ATOM 1501 CZ PHE A 230 21.578 -25.854 -35.444 1.00143.00 C ANISOU 1501 CZ PHE A 230 16586 24534 13213 974 -4644 -2622 C ATOM 1502 N MET A 231 20.747 -18.626 -34.854 1.00123.85 N ANISOU 1502 N MET A 231 13168 23119 10770 -795 -2126 -2280 N ATOM 1503 CA MET A 231 20.132 -17.305 -34.927 1.00121.01 C ANISOU 1503 CA MET A 231 12793 22786 10398 -1128 -1676 -2133 C ATOM 1504 C MET A 231 21.189 -16.220 -35.169 1.00122.01 C ANISOU 1504 C MET A 231 12614 23282 10464 -1255 -1450 -2391 C ATOM 1505 O MET A 231 20.957 -15.328 -35.981 1.00119.59 O ANISOU 1505 O MET A 231 12221 23053 10163 -1439 -1127 -2382 O ATOM 1506 CB MET A 231 19.347 -17.007 -33.647 1.00123.02 C ANISOU 1506 CB MET A 231 13326 22836 10582 -1330 -1617 -1869 C ATOM 1507 CG MET A 231 18.497 -15.759 -33.744 1.00124.97 C ANISOU 1507 CG MET A 231 13609 23057 10815 -1616 -1199 -1708 C ATOM 1508 SD MET A 231 17.593 -15.423 -32.230 1.00129.13 S ANISOU 1508 SD MET A 231 14418 23406 11239 -1833 -1134 -1447 S ATOM 1509 CE MET A 231 18.959 -15.146 -31.078 1.00127.92 C ANISOU 1509 CE MET A 231 14178 23449 10978 -1837 -1270 -1641 C ATOM 1510 N GLN A 232 22.336 -16.297 -34.475 1.00118.76 N ANISOU 1510 N GLN A 232 12056 23095 9973 -1173 -1630 -2623 N ATOM 1511 CA GLN A 232 23.421 -15.324 -34.650 1.00118.57 C ANISOU 1511 CA GLN A 232 11723 23468 9860 -1327 -1433 -2897 C ATOM 1512 C GLN A 232 24.160 -15.611 -35.966 1.00121.78 C ANISOU 1512 C GLN A 232 11803 24177 10291 -1183 -1456 -3195 C ATOM 1513 O GLN A 232 24.618 -14.682 -36.637 1.00120.56 O ANISOU 1513 O GLN A 232 11436 24301 10069 -1413 -1168 -3341 O ATOM 1514 CB GLN A 232 24.378 -15.352 -33.447 1.00121.58 C ANISOU 1514 CB GLN A 232 12037 24016 10141 -1278 -1630 -3064 C ATOM 1515 CG GLN A 232 23.686 -15.053 -32.103 1.00127.49 C ANISOU 1515 CG GLN A 232 13105 24490 10847 -1436 -1604 -2780 C ATOM 1516 CD GLN A 232 23.023 -13.686 -32.018 1.00138.51 C ANISOU 1516 CD GLN A 232 14598 25827 12202 -1806 -1178 -2593 C ATOM 1517 OE1 GLN A 232 23.459 -12.695 -32.625 1.00129.93 O ANISOU 1517 OE1 GLN A 232 13335 24966 11065 -2011 -904 -2725 O ATOM 1518 NE2 GLN A 232 22.002 -13.587 -31.181 1.00130.36 N ANISOU 1518 NE2 GLN A 232 13866 24502 11162 -1908 -1135 -2300 N ATOM 1519 N TYR A 233 24.221 -16.913 -36.336 1.00118.93 N ANISOU 1519 N TYR A 233 11435 23743 10009 -816 -1808 -3277 N ATOM 1520 CA TYR A 233 24.780 -17.475 -37.572 1.00120.07 C ANISOU 1520 CA TYR A 233 11302 24128 10190 -593 -1908 -3553 C ATOM 1521 C TYR A 233 24.010 -16.891 -38.776 1.00121.16 C ANISOU 1521 C TYR A 233 11453 24199 10382 -803 -1557 -3404 C ATOM 1522 O TYR A 233 24.599 -16.193 -39.609 1.00121.43 O ANISOU 1522 O TYR A 233 11217 24570 10349 -971 -1319 -3609 O ATOM 1523 CB TYR A 233 24.673 -19.027 -37.486 1.00122.85 C ANISOU 1523 CB TYR A 233 11805 24256 10618 -153 -2397 -3569 C ATOM 1524 CG TYR A 233 25.144 -19.850 -38.672 1.00126.97 C ANISOU 1524 CG TYR A 233 12095 24959 11188 168 -2591 -3847 C ATOM 1525 CD1 TYR A 233 24.294 -20.109 -39.746 1.00127.44 C ANISOU 1525 CD1 TYR A 233 12243 24827 11351 173 -2489 -3687 C ATOM 1526 CD2 TYR A 233 26.349 -20.550 -38.623 1.00131.13 C ANISOU 1526 CD2 TYR A 233 12363 25801 11659 530 -2952 -4263 C ATOM 1527 CE1 TYR A 233 24.686 -20.933 -40.802 1.00129.77 C ANISOU 1527 CE1 TYR A 233 12350 25267 11689 489 -2693 -3937 C ATOM 1528 CE2 TYR A 233 26.746 -21.388 -39.666 1.00133.61 C ANISOU 1528 CE2 TYR A 233 12479 26277 12011 874 -3173 -4536 C ATOM 1529 CZ TYR A 233 25.912 -21.574 -40.756 1.00139.20 C ANISOU 1529 CZ TYR A 233 13271 26796 12821 843 -3036 -4365 C ATOM 1530 OH TYR A 233 26.299 -22.389 -41.795 1.00140.79 O ANISOU 1530 OH TYR A 233 13277 27161 13056 1183 -3251 -4640 O ATOM 1531 N GLY A 234 22.689 -17.111 -38.781 1.00114.11 N ANISOU 1531 N GLY A 234 10890 22883 9585 -830 -1519 -3047 N ATOM 1532 CA GLY A 234 21.764 -16.646 -39.807 1.00110.94 C ANISOU 1532 CA GLY A 234 10567 22343 9243 -987 -1231 -2866 C ATOM 1533 C GLY A 234 21.328 -15.198 -39.671 1.00112.66 C ANISOU 1533 C GLY A 234 10880 22536 9390 -1370 -828 -2713 C ATOM 1534 O GLY A 234 20.416 -14.769 -40.386 1.00110.19 O ANISOU 1534 O GLY A 234 10698 22052 9118 -1486 -611 -2534 O ATOM 1535 N ILE A 235 21.952 -14.433 -38.737 1.00109.77 N ANISOU 1535 N ILE A 235 10474 22323 8909 -1554 -746 -2785 N ATOM 1536 CA ILE A 235 21.678 -12.996 -38.543 1.00108.16 C ANISOU 1536 CA ILE A 235 10385 22103 8610 -1917 -393 -2675 C ATOM 1537 C ILE A 235 22.736 -12.197 -39.300 1.00112.33 C ANISOU 1537 C ILE A 235 10654 23017 9009 -2132 -198 -2951 C ATOM 1538 O ILE A 235 22.484 -11.079 -39.762 1.00110.84 O ANISOU 1538 O ILE A 235 10573 22806 8735 -2429 100 -2885 O ATOM 1539 CB ILE A 235 21.622 -12.594 -37.046 1.00111.06 C ANISOU 1539 CB ILE A 235 10906 22377 8913 -2023 -409 -2564 C ATOM 1540 N VAL A 236 23.928 -12.785 -39.417 1.00110.70 N ANISOU 1540 N VAL A 236 10118 23175 8767 -1984 -385 -3279 N ATOM 1541 CA VAL A 236 25.042 -12.188 -40.135 1.00112.46 C ANISOU 1541 CA VAL A 236 10029 23858 8841 -2194 -226 -3598 C ATOM 1542 C VAL A 236 24.963 -12.690 -41.566 1.00115.89 C ANISOU 1542 C VAL A 236 10326 24378 9328 -2075 -221 -3693 C ATOM 1543 O VAL A 236 25.179 -11.914 -42.494 1.00116.14 O ANISOU 1543 O VAL A 236 10291 24591 9246 -2363 43 -3774 O ATOM 1544 CB VAL A 236 26.414 -12.494 -39.454 1.00119.48 C ANISOU 1544 CB VAL A 236 10584 25176 9638 -2100 -426 -3954 C ATOM 1545 CG1 VAL A 236 27.543 -11.707 -40.110 1.00121.54 C ANISOU 1545 CG1 VAL A 236 10514 25968 9699 -2416 -209 -4289 C ATOM 1546 CG2 VAL A 236 26.371 -12.178 -37.965 1.00119.18 C ANISOU 1546 CG2 VAL A 236 10720 24990 9572 -2158 -482 -3825 C ATOM 1547 N ALA A 237 24.586 -13.986 -41.743 1.00111.38 N ANISOU 1547 N ALA A 237 9761 23640 8918 -1668 -517 -3662 N ATOM 1548 CA ALA A 237 24.449 -14.640 -43.050 1.00110.73 C ANISOU 1548 CA ALA A 237 9561 23603 8906 -1490 -564 -3747 C ATOM 1549 C ALA A 237 23.507 -13.865 -43.956 1.00112.10 C ANISOU 1549 C ALA A 237 9951 23556 9085 -1743 -248 -3510 C ATOM 1550 O ALA A 237 23.814 -13.713 -45.133 1.00112.54 O ANISOU 1550 O ALA A 237 9844 23833 9085 -1828 -120 -3664 O ATOM 1551 CB ALA A 237 23.953 -16.063 -42.886 1.00110.99 C ANISOU 1551 CB ALA A 237 9699 23363 9107 -1050 -938 -3662 C ATOM 1552 N ASN A 238 22.420 -13.289 -43.401 1.00106.41 N ANISOU 1552 N ASN A 238 9588 22438 8403 -1879 -115 -3164 N ATOM 1553 CA ASN A 238 21.470 -12.498 -44.184 1.00104.66 C ANISOU 1553 CA ASN A 238 9606 21983 8176 -2083 156 -2949 C ATOM 1554 C ASN A 238 22.080 -11.088 -44.508 1.00110.56 C ANISOU 1554 C ASN A 238 10347 22953 8708 -2518 467 -3057 C ATOM 1555 O ASN A 238 21.342 -10.154 -44.828 1.00108.91 O ANISOU 1555 O ASN A 238 10425 22510 8446 -2735 687 -2867 O ATOM 1556 CB ASN A 238 20.107 -12.378 -43.456 1.00103.04 C ANISOU 1556 CB ASN A 238 9758 21328 8066 -2049 169 -2592 C ATOM 1557 CG ASN A 238 20.101 -11.681 -42.110 1.00137.39 C ANISOU 1557 CG ASN A 238 14250 25609 12341 -2209 222 -2498 C ATOM 1558 OD1 ASN A 238 20.529 -10.529 -41.962 1.00136.96 O ANISOU 1558 OD1 ASN A 238 14234 25668 12136 -2509 431 -2553 O ATOM 1559 ND2 ASN A 238 19.413 -12.283 -41.150 1.00128.61 N ANISOU 1559 ND2 ASN A 238 13283 24260 11322 -2045 56 -2315 N ATOM 1560 N TYR A 239 23.424 -10.971 -44.488 1.00110.49 N ANISOU 1560 N TYR A 239 10020 23404 8557 -2643 466 -3382 N ATOM 1561 CA TYR A 239 24.118 -9.734 -44.832 1.00112.29 C ANISOU 1561 CA TYR A 239 10227 23893 8545 -3103 743 -3516 C ATOM 1562 C TYR A 239 25.248 -10.011 -45.845 1.00117.64 C ANISOU 1562 C TYR A 239 10498 25099 9100 -3173 761 -3890 C ATOM 1563 O TYR A 239 25.684 -9.068 -46.513 1.00117.77 O ANISOU 1563 O TYR A 239 10523 25325 8898 -3593 1013 -3988 O ATOM 1564 CB TYR A 239 24.659 -9.010 -43.592 1.00115.11 C ANISOU 1564 CB TYR A 239 10614 24340 8782 -3320 786 -3548 C ATOM 1565 CG TYR A 239 23.768 -7.859 -43.180 1.00115.91 C ANISOU 1565 CG TYR A 239 11164 24046 8830 -3567 982 -3248 C ATOM 1566 CD1 TYR A 239 22.741 -8.040 -42.256 1.00115.81 C ANISOU 1566 CD1 TYR A 239 11405 23632 8967 -3358 886 -2972 C ATOM 1567 CD2 TYR A 239 23.893 -6.607 -43.779 1.00117.77 C ANISOU 1567 CD2 TYR A 239 11597 24301 8848 -4004 1248 -3247 C ATOM 1568 CE1 TYR A 239 21.884 -6.992 -41.914 1.00115.68 C ANISOU 1568 CE1 TYR A 239 11782 23276 8894 -3537 1049 -2733 C ATOM 1569 CE2 TYR A 239 23.046 -5.554 -43.443 1.00117.42 C ANISOU 1569 CE2 TYR A 239 12004 23866 8746 -4180 1387 -2991 C ATOM 1570 CZ TYR A 239 22.044 -5.749 -42.510 1.00123.46 C ANISOU 1570 CZ TYR A 239 12971 24265 9672 -3923 1286 -2749 C ATOM 1571 OH TYR A 239 21.219 -4.703 -42.190 1.00124.81 O ANISOU 1571 OH TYR A 239 13561 24088 9773 -4061 1408 -2540 O ATOM 1572 N CYS A 240 25.682 -11.291 -46.003 1.00115.57 N ANISOU 1572 N CYS A 240 9907 25047 8956 -2772 488 -4104 N ATOM 1573 CA CYS A 240 26.644 -11.657 -47.061 1.00118.13 C ANISOU 1573 CA CYS A 240 9822 25889 9174 -2775 488 -4481 C ATOM 1574 C CYS A 240 25.854 -11.963 -48.328 1.00119.30 C ANISOU 1574 C CYS A 240 10092 25828 9410 -2685 541 -4350 C ATOM 1575 O CYS A 240 26.333 -11.736 -49.442 1.00121.07 O ANISOU 1575 O CYS A 240 10136 26377 9487 -2886 693 -4550 O ATOM 1576 CB CYS A 240 27.546 -12.823 -46.663 1.00121.14 C ANISOU 1576 CB CYS A 240 9794 26621 9614 -2362 148 -4823 C ATOM 1577 SG CYS A 240 26.786 -14.458 -46.862 1.00123.25 S ANISOU 1577 SG CYS A 240 10124 26538 10168 -1720 -242 -4718 S ATOM 1578 N TRP A 241 24.637 -12.518 -48.141 1.00110.36 N ANISOU 1578 N TRP A 241 9257 24171 8505 -2389 408 -4023 N ATOM 1579 CA TRP A 241 23.702 -12.771 -49.214 1.00107.17 C ANISOU 1579 CA TRP A 241 9024 23494 8203 -2295 452 -3846 C ATOM 1580 C TRP A 241 23.131 -11.443 -49.661 1.00108.54 C ANISOU 1580 C TRP A 241 9531 23466 8244 -2716 780 -3636 C ATOM 1581 O TRP A 241 22.746 -11.312 -50.816 1.00108.38 O ANISOU 1581 O TRP A 241 9594 23387 8200 -2788 897 -3594 O ATOM 1582 CB TRP A 241 22.610 -13.770 -48.803 1.00103.34 C ANISOU 1582 CB TRP A 241 8740 22551 7973 -1885 205 -3582 C ATOM 1583 CG TRP A 241 23.123 -15.171 -48.699 1.00105.42 C ANISOU 1583 CG TRP A 241 8739 22968 8347 -1450 -153 -3797 C ATOM 1584 CD1 TRP A 241 23.394 -15.868 -47.556 1.00108.72 C ANISOU 1584 CD1 TRP A 241 9126 23350 8832 -1196 -441 -3833 C ATOM 1585 CD2 TRP A 241 23.600 -15.975 -49.783 1.00106.91 C ANISOU 1585 CD2 TRP A 241 8647 23423 8549 -1229 -276 -4061 C ATOM 1586 NE1 TRP A 241 23.948 -17.087 -47.866 1.00109.74 N ANISOU 1586 NE1 TRP A 241 9015 23660 9023 -801 -763 -4091 N ATOM 1587 CE2 TRP A 241 24.110 -17.170 -49.227 1.00112.19 C ANISOU 1587 CE2 TRP A 241 9144 24179 9302 -806 -665 -4251 C ATOM 1588 CE3 TRP A 241 23.629 -15.809 -51.186 1.00108.45 C ANISOU 1588 CE3 TRP A 241 8740 23784 8683 -1338 -109 -4161 C ATOM 1589 CZ2 TRP A 241 24.655 -18.191 -50.023 1.00113.59 C ANISOU 1589 CZ2 TRP A 241 9041 24610 9507 -465 -900 -4554 C ATOM 1590 CZ3 TRP A 241 24.161 -16.820 -51.972 1.00111.58 C ANISOU 1590 CZ3 TRP A 241 8833 24453 9110 -1025 -314 -4453 C ATOM 1591 CH2 TRP A 241 24.666 -17.994 -51.395 1.00113.73 C ANISOU 1591 CH2 TRP A 241 8929 24813 9471 -580 -710 -4655 C ATOM 1592 N LEU A 242 23.157 -10.430 -48.773 1.00103.31 N ANISOU 1592 N LEU A 242 9068 22714 7471 -3002 916 -3530 N ATOM 1593 CA LEU A 242 22.752 -9.070 -49.113 1.00102.07 C ANISOU 1593 CA LEU A 242 9269 22371 7142 -3416 1196 -3367 C ATOM 1594 C LEU A 242 23.948 -8.353 -49.773 1.00106.52 C ANISOU 1594 C LEU A 242 9649 23414 7411 -3866 1394 -3655 C ATOM 1595 O LEU A 242 23.775 -7.332 -50.430 1.00105.65 O ANISOU 1595 O LEU A 242 9823 23209 7109 -4245 1615 -3576 O ATOM 1596 CB LEU A 242 22.235 -8.313 -47.871 1.00101.13 C ANISOU 1596 CB LEU A 242 9465 21938 7021 -3509 1234 -3140 C ATOM 1597 CG LEU A 242 21.549 -6.953 -48.121 1.00105.50 C ANISOU 1597 CG LEU A 242 10490 22171 7426 -3835 1458 -2930 C ATOM 1598 CD1 LEU A 242 20.165 -7.123 -48.771 1.00102.93 C ANISOU 1598 CD1 LEU A 242 10445 21415 7247 -3607 1442 -2677 C ATOM 1599 CD2 LEU A 242 21.396 -6.187 -46.840 1.00108.79 C ANISOU 1599 CD2 LEU A 242 11130 22413 7793 -3953 1487 -2808 C ATOM 1600 N LEU A 243 25.159 -8.909 -49.610 1.00105.54 N ANISOU 1600 N LEU A 243 9054 23816 7229 -3824 1299 -4007 N ATOM 1601 CA LEU A 243 26.374 -8.403 -50.256 1.00109.44 C ANISOU 1601 CA LEU A 243 9272 24881 7429 -4242 1473 -4345 C ATOM 1602 C LEU A 243 26.436 -8.938 -51.682 1.00114.34 C ANISOU 1602 C LEU A 243 9710 25700 8033 -4178 1494 -4489 C ATOM 1603 O LEU A 243 26.710 -8.180 -52.614 1.00115.79 O ANISOU 1603 O LEU A 243 9971 26058 7968 -4620 1729 -4557 O ATOM 1604 CB LEU A 243 27.641 -8.793 -49.458 1.00112.43 C ANISOU 1604 CB LEU A 243 9178 25796 7746 -4190 1347 -4706 C ATOM 1605 CG LEU A 243 28.985 -8.278 -49.988 1.00121.56 C ANISOU 1605 CG LEU A 243 9975 27644 8569 -4649 1529 -5110 C ATOM 1606 CD1 LEU A 243 29.115 -6.785 -49.775 1.00122.71 C ANISOU 1606 CD1 LEU A 243 10456 27733 8436 -5287 1812 -4996 C ATOM 1607 CD2 LEU A 243 30.131 -8.958 -49.287 1.00126.80 C ANISOU 1607 CD2 LEU A 243 10103 28851 9223 -4435 1332 -5507 C ATOM 1608 N VAL A 244 26.150 -10.254 -51.840 1.00109.29 N ANISOU 1608 N VAL A 244 8867 25011 7649 -3634 1235 -4526 N ATOM 1609 CA VAL A 244 26.072 -10.977 -53.110 1.00108.94 C ANISOU 1609 CA VAL A 244 8651 25092 7648 -3452 1194 -4644 C ATOM 1610 C VAL A 244 25.060 -10.241 -54.039 1.00112.04 C ANISOU 1610 C VAL A 244 9499 25074 7998 -3691 1407 -4338 C ATOM 1611 O VAL A 244 25.452 -9.859 -55.135 1.00113.56 O ANISOU 1611 O VAL A 244 9631 25535 7980 -4003 1586 -4483 O ATOM 1612 CB VAL A 244 25.694 -12.475 -52.863 1.00110.75 C ANISOU 1612 CB VAL A 244 8732 25163 8187 -2799 836 -4643 C ATOM 1613 CG1 VAL A 244 25.149 -13.159 -54.111 1.00109.59 C ANISOU 1613 CG1 VAL A 244 8581 24914 8143 -2576 788 -4618 C ATOM 1614 CG2 VAL A 244 26.874 -13.255 -52.283 1.00113.05 C ANISOU 1614 CG2 VAL A 244 8539 25950 8465 -2546 599 -5043 C ATOM 1615 N GLU A 245 23.819 -9.955 -53.560 1.00106.51 N ANISOU 1615 N GLU A 245 9251 23760 7457 -3583 1392 -3940 N ATOM 1616 CA GLU A 245 22.758 -9.265 -54.326 1.00105.30 C ANISOU 1616 CA GLU A 245 9557 23174 7277 -3733 1546 -3651 C ATOM 1617 C GLU A 245 23.183 -7.879 -54.833 1.00113.01 C ANISOU 1617 C GLU A 245 10774 24258 7906 -4344 1828 -3680 C ATOM 1618 O GLU A 245 22.738 -7.467 -55.908 1.00112.78 O ANISOU 1618 O GLU A 245 11001 24076 7774 -4511 1949 -3588 O ATOM 1619 CB GLU A 245 21.481 -9.095 -53.494 1.00103.48 C ANISOU 1619 CB GLU A 245 9721 22358 7239 -3526 1476 -3283 C ATOM 1620 CG GLU A 245 20.733 -10.399 -53.275 1.00114.42 C ANISOU 1620 CG GLU A 245 11007 23528 8941 -2989 1221 -3176 C ATOM 1621 CD GLU A 245 20.211 -11.088 -54.526 1.00145.46 C ANISOU 1621 CD GLU A 245 14910 27384 12974 -2780 1174 -3160 C ATOM 1622 OE1 GLU A 245 19.812 -10.382 -55.482 1.00144.35 O ANISOU 1622 OE1 GLU A 245 15017 27116 12713 -3001 1348 -3074 O ATOM 1623 OE2 GLU A 245 20.121 -12.337 -54.512 1.00143.37 O ANISOU 1623 OE2 GLU A 245 14425 27139 12909 -2383 943 -3212 O ATOM 1624 N GLY A 246 24.018 -7.186 -54.067 1.00112.38 N ANISOU 1624 N GLY A 246 10642 24422 7636 -4678 1918 -3803 N ATOM 1625 CA GLY A 246 24.531 -5.873 -54.437 1.00115.63 C ANISOU 1625 CA GLY A 246 11299 24958 7679 -5314 2170 -3846 C ATOM 1626 C GLY A 246 25.666 -5.936 -55.444 1.00125.78 C ANISOU 1626 C GLY A 246 12223 26867 8700 -5654 2300 -4202 C ATOM 1627 O GLY A 246 25.752 -5.090 -56.343 1.00127.54 O ANISOU 1627 O GLY A 246 12720 27105 8633 -6133 2499 -4188 O ATOM 1628 N LEU A 247 26.540 -6.956 -55.310 1.00124.98 N ANISOU 1628 N LEU A 247 11514 27295 8679 -5402 2172 -4539 N ATOM 1629 CA LEU A 247 27.698 -7.138 -56.186 1.00129.13 C ANISOU 1629 CA LEU A 247 11584 28524 8954 -5670 2275 -4952 C ATOM 1630 C LEU A 247 27.318 -7.808 -57.511 1.00134.09 C ANISOU 1630 C LEU A 247 12139 29158 9649 -5470 2254 -4980 C ATOM 1631 O LEU A 247 27.818 -7.388 -58.547 1.00136.05 O ANISOU 1631 O LEU A 247 12342 29748 9602 -5904 2449 -5148 O ATOM 1632 CB LEU A 247 28.795 -7.974 -55.496 1.00131.14 C ANISOU 1632 CB LEU A 247 11199 29369 9260 -5418 2110 -5350 C ATOM 1633 CG LEU A 247 29.452 -7.370 -54.244 1.00137.23 C ANISOU 1633 CG LEU A 247 11921 30301 9919 -5652 2136 -5423 C ATOM 1634 CD1 LEU A 247 30.393 -8.359 -53.593 1.00139.05 C ANISOU 1634 CD1 LEU A 247 11536 31051 10245 -5272 1907 -5809 C ATOM 1635 CD2 LEU A 247 30.177 -6.078 -54.557 1.00142.88 C ANISOU 1635 CD2 LEU A 247 12755 31336 10196 -6444 2444 -5535 C ATOM 1636 N TYR A 248 26.440 -8.834 -57.489 1.00129.10 N ANISOU 1636 N TYR A 248 11512 28159 9383 -4851 2022 -4817 N ATOM 1637 CA TYR A 248 26.052 -9.576 -58.699 1.00128.88 C ANISOU 1637 CA TYR A 248 11399 28121 9446 -4606 1971 -4846 C ATOM 1638 C TYR A 248 24.876 -8.857 -59.432 1.00129.93 C ANISOU 1638 C TYR A 248 12137 27673 9560 -4774 2103 -4465 C ATOM 1639 O TYR A 248 24.109 -9.475 -60.176 1.00127.15 O ANISOU 1639 O TYR A 248 11857 27071 9384 -4457 2015 -4347 O ATOM 1640 CB TYR A 248 25.700 -11.032 -58.362 1.00128.75 C ANISOU 1640 CB TYR A 248 11125 27992 9801 -3890 1642 -4866 C ATOM 1641 CG TYR A 248 26.916 -11.849 -57.960 1.00134.07 C ANISOU 1641 CG TYR A 248 11192 29287 10462 -3673 1472 -5312 C ATOM 1642 CD1 TYR A 248 27.633 -12.580 -58.903 1.00138.62 C ANISOU 1642 CD1 TYR A 248 11310 30396 10962 -3546 1420 -5698 C ATOM 1643 CD2 TYR A 248 27.378 -11.856 -56.643 1.00135.38 C ANISOU 1643 CD2 TYR A 248 11237 29531 10670 -3592 1357 -5376 C ATOM 1644 CE1 TYR A 248 28.758 -13.323 -58.543 1.00142.47 C ANISOU 1644 CE1 TYR A 248 11230 31479 11422 -3301 1235 -6153 C ATOM 1645 CE2 TYR A 248 28.500 -12.597 -56.270 1.00139.04 C ANISOU 1645 CE2 TYR A 248 11152 30568 11110 -3357 1171 -5811 C ATOM 1646 CZ TYR A 248 29.186 -13.333 -57.225 1.00149.91 C ANISOU 1646 CZ TYR A 248 12073 32473 12413 -3197 1102 -6209 C ATOM 1647 OH TYR A 248 30.286 -14.077 -56.872 1.00154.52 O ANISOU 1647 OH TYR A 248 12106 33640 12964 -2912 886 -6679 O ATOM 1648 N LEU A 249 24.796 -7.536 -59.228 1.00127.51 N ANISOU 1648 N LEU A 249 12263 27172 9012 -5277 2299 -4300 N ATOM 1649 CA LEU A 249 23.995 -6.565 -59.959 1.00127.12 C ANISOU 1649 CA LEU A 249 12814 26676 8809 -5581 2446 -4022 C ATOM 1650 C LEU A 249 24.961 -5.663 -60.689 1.00139.06 C ANISOU 1650 C LEU A 249 14361 28612 9863 -6288 2696 -4227 C ATOM 1651 O LEU A 249 24.661 -5.155 -61.763 1.00139.17 O ANISOU 1651 O LEU A 249 14712 28488 9679 -6577 2818 -4140 O ATOM 1652 CB LEU A 249 23.023 -5.767 -59.073 1.00124.14 C ANISOU 1652 CB LEU A 249 12987 25666 8515 -5550 2420 -3659 C ATOM 1653 CG LEU A 249 22.130 -4.787 -59.854 1.00127.03 C ANISOU 1653 CG LEU A 249 14010 25534 8722 -5786 2519 -3390 C ATOM 1654 CD1 LEU A 249 20.861 -5.454 -60.313 1.00123.59 C ANISOU 1654 CD1 LEU A 249 13706 24664 8589 -5268 2374 -3174 C ATOM 1655 CD2 LEU A 249 21.774 -3.612 -59.036 1.00127.67 C ANISOU 1655 CD2 LEU A 249 14603 25225 8682 -6017 2560 -3182 C ATOM 1656 N HIS A 250 26.146 -5.473 -60.069 1.00141.48 N ANISOU 1656 N HIS A 250 14316 29454 9985 -6585 2767 -4511 N ATOM 1657 CA HIS A 250 27.284 -4.685 -60.540 1.00146.96 C ANISOU 1657 CA HIS A 250 14926 30698 10213 -7310 3007 -4777 C ATOM 1658 C HIS A 250 28.209 -5.566 -61.383 1.00155.93 C ANISOU 1658 C HIS A 250 15404 32576 11266 -7280 3028 -5208 C ATOM 1659 O HIS A 250 28.270 -5.413 -62.605 1.00156.58 O ANISOU 1659 O HIS A 250 15558 32807 11126 -7573 3164 -5271 O ATOM 1660 CB HIS A 250 28.027 -4.099 -59.317 1.00148.76 C ANISOU 1660 CB HIS A 250 15074 31133 10315 -7587 3049 -4874 C ATOM 1661 CG HIS A 250 29.196 -3.231 -59.648 1.00157.02 C ANISOU 1661 CG HIS A 250 16048 32752 10862 -8385 3298 -5144 C ATOM 1662 ND1 HIS A 250 29.064 -1.861 -59.759 1.00159.46 N ANISOU 1662 ND1 HIS A 250 17042 32652 10894 -8943 3449 -4894 N ATOM 1663 CD2 HIS A 250 30.494 -3.564 -59.837 1.00159.11 C ANISOU 1663 CD2 HIS A 250 15913 33285 11256 -8220 3281 -5362 C ATOM 1664 CE1 HIS A 250 30.277 -1.406 -60.028 1.00159.25 C ANISOU 1664 CE1 HIS A 250 17026 32572 10911 -9006 3505 -4914 C ATOM 1665 NE2 HIS A 250 31.169 -2.396 -60.092 1.00159.19 N ANISOU 1665 NE2 HIS A 250 16378 32956 11152 -8588 3415 -5186 N ATOM 1666 N ASN A 251 28.891 -6.527 -60.719 1.00155.17 N ANISOU 1666 N ASN A 251 14676 32930 11353 -6881 2867 -5512 N ATOM 1667 CA ASN A 251 29.830 -7.481 -61.313 1.00158.64 C ANISOU 1667 CA ASN A 251 14413 34118 11745 -6725 2823 -5986 C ATOM 1668 C ASN A 251 29.166 -8.302 -62.427 1.00163.39 C ANISOU 1668 C ASN A 251 15031 34496 12554 -6312 2726 -5908 C ATOM 1669 O ASN A 251 29.842 -8.702 -63.378 1.00163.14 O ANISOU 1669 O ASN A 251 14843 34534 12608 -6163 2723 -6032 O ATOM 1670 CB ASN A 251 30.392 -8.424 -60.233 1.00158.00 C ANISOU 1670 CB ASN A 251 13792 34335 11907 -6198 2570 -6241 C ATOM 1671 CG ASN A 251 31.217 -7.750 -59.145 1.00168.24 C ANISOU 1671 CG ASN A 251 15588 34671 13663 -5942 2480 -5828 C ATOM 1672 OD1 ASN A 251 31.613 -6.578 -59.235 1.00163.17 O ANISOU 1672 OD1 ASN A 251 15101 34284 12611 -6657 2745 -5873 O ATOM 1673 ND2 ASN A 251 31.557 -8.511 -58.120 1.00162.16 N ANISOU 1673 ND2 ASN A 251 14134 34709 12771 -5804 2327 -6279 N ATOM 1674 N LEU A 252 27.846 -8.514 -62.328 1.00158.41 N ANISOU 1674 N LEU A 252 14814 33154 12219 -5928 2595 -5509 N ATOM 1675 CA LEU A 252 27.118 -9.282 -63.320 1.00157.75 C ANISOU 1675 CA LEU A 252 14760 32853 12323 -5550 2497 -5425 C ATOM 1676 C LEU A 252 26.415 -8.320 -64.323 1.00163.71 C ANISOU 1676 C LEU A 252 16116 33221 12867 -5990 2703 -5140 C ATOM 1677 O LEU A 252 26.978 -8.064 -65.391 1.00166.66 O ANISOU 1677 O LEU A 252 16395 34007 12922 -6409 2883 -5348 O ATOM 1678 CB LEU A 252 26.108 -10.226 -62.624 1.00153.68 C ANISOU 1678 CB LEU A 252 14320 31785 12287 -4814 2196 -5171 C ATOM 1679 CG LEU A 252 25.458 -11.341 -63.468 1.00156.84 C ANISOU 1679 CG LEU A 252 14627 32025 12939 -4299 2021 -5145 C ATOM 1680 CD1 LEU A 252 26.489 -12.390 -63.884 1.00159.74 C ANISOU 1680 CD1 LEU A 252 14328 33082 13285 -4052 1898 -5633 C ATOM 1681 CD2 LEU A 252 24.375 -12.048 -62.676 1.00155.87 C ANISOU 1681 CD2 LEU A 252 14694 31300 13231 -3715 1758 -4835 C ATOM 1682 N LEU A 253 25.220 -7.771 -63.970 1.00157.98 N ANISOU 1682 N LEU A 253 16005 31731 12290 -5903 2669 -4692 N ATOM 1683 CA LEU A 253 24.407 -6.915 -64.855 1.00157.76 C ANISOU 1683 CA LEU A 253 16605 31239 12098 -6202 2795 -4404 C ATOM 1684 C LEU A 253 25.004 -5.506 -65.057 1.00166.52 C ANISOU 1684 C LEU A 253 18077 32475 12719 -7018 3050 -4421 C ATOM 1685 O LEU A 253 24.842 -4.945 -66.141 1.00167.60 O ANISOU 1685 O LEU A 253 18566 32527 12587 -7395 3182 -4358 O ATOM 1686 CB LEU A 253 22.959 -6.748 -64.331 1.00153.63 C ANISOU 1686 CB LEU A 253 16600 29902 11870 -5820 2654 -3967 C ATOM 1687 CG LEU A 253 21.903 -7.880 -64.573 1.00154.69 C ANISOU 1687 CG LEU A 253 16659 29695 12420 -5131 2435 -3818 C ATOM 1688 CD1 LEU A 253 21.544 -8.027 -66.047 1.00155.33 C ANISOU 1688 CD1 LEU A 253 16863 29738 12418 -5168 2485 -3809 C ATOM 1689 CD2 LEU A 253 22.289 -9.208 -63.938 1.00156.09 C ANISOU 1689 CD2 LEU A 253 16243 30167 12896 -4621 2231 -4019 C ATOM 1690 N GLY A 254 25.631 -4.938 -64.032 1.00165.75 N ANISOU 1690 N GLY A 254 17942 32535 12500 -7290 3104 -4486 N ATOM 1691 CA GLY A 254 26.215 -3.604 -64.124 1.00170.06 C ANISOU 1691 CA GLY A 254 18861 33179 12574 -8084 3327 -4495 C ATOM 1692 C GLY A 254 27.228 -3.526 -65.239 1.00174.77 C ANISOU 1692 C GLY A 254 19589 33348 13469 -7746 3317 -4367 C ATOM 1693 O GLY A 254 27.087 -2.702 -66.147 1.00174.78 O ANISOU 1693 O GLY A 254 20113 33022 13274 -8041 3414 -4182 O ATOM 1694 N LEU A 255 28.214 -4.449 -65.211 1.00174.15 N ANISOU 1694 N LEU A 255 18894 33663 13612 -7409 3253 -4634 N ATOM 1695 CA LEU A 255 29.276 -4.569 -66.217 1.00175.06 C ANISOU 1695 CA LEU A 255 18925 33735 13855 -7269 3284 -4675 C ATOM 1696 C LEU A 255 28.706 -5.099 -67.529 1.00179.20 C ANISOU 1696 C LEU A 255 19601 33933 14554 -6933 3232 -4539 C ATOM 1697 O LEU A 255 28.898 -4.466 -68.567 1.00179.18 O ANISOU 1697 O LEU A 255 19949 33724 14407 -7157 3341 -4413 O ATOM 1698 CB LEU A 255 30.417 -5.488 -65.715 1.00174.94 C ANISOU 1698 CB LEU A 255 18294 34046 14129 -6857 3163 -4941 C ATOM 1699 CG LEU A 255 31.243 -4.991 -64.511 1.00178.41 C ANISOU 1699 CG LEU A 255 18832 34135 14820 -6691 3090 -4801 C ATOM 1700 CD1 LEU A 255 32.087 -6.099 -63.930 1.00178.40 C ANISOU 1700 CD1 LEU A 255 18243 34433 15108 -6235 2915 -5064 C ATOM 1701 CD2 LEU A 255 32.116 -3.789 -64.879 1.00180.65 C ANISOU 1701 CD2 LEU A 255 19575 33956 15108 -6871 3195 -4551 C ATOM 1702 N ALA A 256 27.984 -6.254 -67.470 1.00177.79 N ANISOU 1702 N ALA A 256 18980 34154 14420 -6694 3129 -4752 N ATOM 1703 CA ALA A 256 27.335 -6.957 -68.593 1.00178.40 C ANISOU 1703 CA ALA A 256 18995 34273 14518 -6516 3098 -4784 C ATOM 1704 C ALA A 256 28.304 -7.112 -69.801 1.00182.66 C ANISOU 1704 C ALA A 256 19641 34425 15335 -6196 3088 -4679 C ATOM 1705 O ALA A 256 27.868 -7.088 -70.958 1.00182.68 O ANISOU 1705 O ALA A 256 19838 34352 15219 -6286 3149 -4621 O ATOM 1706 CB ALA A 256 26.068 -6.218 -69.022 1.00179.04 C ANISOU 1706 CB ALA A 256 19651 34027 14351 -6845 3177 -4529 C ATOM 1707 N THR A 257 29.613 -7.294 -69.513 1.00181.42 N ANISOU 1707 N THR A 257 19161 34478 15293 -6103 3076 -4850 N ATOM 1708 CA THR A 257 30.664 -7.446 -70.527 1.00182.08 C ANISOU 1708 CA THR A 257 19185 34518 15479 -5989 3111 -4888 C ATOM 1709 C THR A 257 31.533 -8.708 -70.259 1.00185.35 C ANISOU 1709 C THR A 257 19168 34884 16374 -5325 2887 -5015 C ATOM 1710 O THR A 257 32.041 -9.300 -71.218 1.00185.23 O ANISOU 1710 O THR A 257 18986 34953 16442 -5150 2872 -5121 O ATOM 1711 CB THR A 257 31.562 -6.185 -70.583 1.00187.83 C ANISOU 1711 CB THR A 257 20498 34482 16388 -5978 3164 -4482 C ATOM 1712 OG1 THR A 257 32.006 -5.856 -69.263 1.00187.38 O ANISOU 1712 OG1 THR A 257 20350 34465 16380 -6022 3131 -4505 O ATOM 1713 CG2 THR A 257 30.851 -4.974 -71.193 1.00186.90 C ANISOU 1713 CG2 THR A 257 20959 34137 15919 -6448 3317 -4256 C ATOM 1714 N LEU A 258 31.685 -9.117 -68.970 1.00183.04 N ANISOU 1714 N LEU A 258 18491 34934 16121 -5231 2776 -5224 N ATOM 1715 CA LEU A 258 32.513 -10.262 -68.548 1.00182.70 C ANISOU 1715 CA LEU A 258 17946 35119 16353 -4773 2568 -5479 C ATOM 1716 C LEU A 258 31.826 -11.621 -68.845 1.00184.63 C ANISOU 1716 C LEU A 258 17972 35339 16842 -4248 2343 -5557 C ATOM 1717 O LEU A 258 30.616 -11.760 -68.629 1.00183.87 O ANISOU 1717 O LEU A 258 17876 35355 16632 -4272 2318 -5555 O ATOM 1718 CB LEU A 258 32.858 -10.183 -67.042 1.00182.63 C ANISOU 1718 CB LEU A 258 17799 35154 16438 -4701 2464 -5521 C ATOM 1719 CG LEU A 258 33.954 -9.177 -66.580 1.00186.08 C ANISOU 1719 CG LEU A 258 18569 35121 17011 -4809 2533 -5271 C ATOM 1720 CD1 LEU A 258 35.331 -9.539 -67.141 1.00186.33 C ANISOU 1720 CD1 LEU A 258 18419 35166 17212 -4629 2499 -5368 C ATOM 1721 CD2 LEU A 258 33.592 -7.722 -66.874 1.00188.14 C ANISOU 1721 CD2 LEU A 258 19438 34948 17098 -5215 2741 -4923 C ATOM 1722 N PRO A 259 32.609 -12.640 -69.307 1.00182.21 N ANISOU 1722 N PRO A 259 17224 35375 16633 -3955 2217 -5860 N ATOM 1723 CA PRO A 259 32.005 -13.941 -69.663 1.00181.84 C ANISOU 1723 CA PRO A 259 16885 35488 16718 -3512 2002 -6035 C ATOM 1724 C PRO A 259 31.571 -14.766 -68.443 1.00183.96 C ANISOU 1724 C PRO A 259 17016 35631 17249 -3053 1705 -6042 C ATOM 1725 O PRO A 259 30.526 -15.419 -68.513 1.00183.23 O ANISOU 1725 O PRO A 259 16796 35684 17141 -2841 1582 -6116 O ATOM 1726 CB PRO A 259 33.134 -14.668 -70.414 1.00183.13 C ANISOU 1726 CB PRO A 259 16926 35532 17124 -3201 1901 -6109 C ATOM 1727 CG PRO A 259 34.143 -13.609 -70.748 1.00186.34 C ANISOU 1727 CG PRO A 259 17726 35503 17573 -3477 2101 -5829 C ATOM 1728 CD PRO A 259 34.048 -12.622 -69.635 1.00183.37 C ANISOU 1728 CD PRO A 259 17354 35375 16943 -3877 2223 -5858 C ATOM 1729 N GLU A 260 32.368 -14.756 -67.346 1.00181.63 N ANISOU 1729 N GLU A 260 16467 35585 16958 -3025 1619 -6217 N ATOM 1730 CA GLU A 260 32.073 -15.508 -66.118 1.00181.18 C ANISOU 1730 CA GLU A 260 16166 35646 17029 -2652 1338 -6345 C ATOM 1731 C GLU A 260 30.748 -15.040 -65.500 1.00182.68 C ANISOU 1731 C GLU A 260 16581 35707 17122 -2796 1391 -6140 C ATOM 1732 O GLU A 260 30.545 -13.835 -65.328 1.00182.40 O ANISOU 1732 O GLU A 260 16808 35632 16863 -3295 1649 -5979 O ATOM 1733 CB GLU A 260 33.217 -15.359 -65.102 1.00182.33 C ANISOU 1733 CB GLU A 260 16293 35645 17338 -2587 1250 -6335 C ATOM 1734 N ARG A 261 29.831 -16.001 -65.217 1.00179.34 N ANISOU 1734 N ARG A 261 15788 35726 16628 -2462 1169 -6392 N ATOM 1735 CA ARG A 261 28.499 -15.745 -64.646 1.00178.53 C ANISOU 1735 CA ARG A 261 15723 35768 16342 -2575 1196 -6316 C ATOM 1736 C ARG A 261 27.993 -16.946 -63.817 1.00179.39 C ANISOU 1736 C ARG A 261 15633 35861 16666 -1954 808 -6397 C ATOM 1737 O ARG A 261 27.528 -16.757 -62.695 1.00178.39 O ANISOU 1737 O ARG A 261 15453 35886 16442 -1977 758 -6390 O ATOM 1738 CB ARG A 261 27.485 -15.426 -65.757 1.00178.59 C ANISOU 1738 CB ARG A 261 15914 35770 16170 -2819 1382 -6192 C ATOM 1739 N SER A 262 28.080 -18.171 -64.383 1.00176.69 N ANISOU 1739 N SER A 262 14940 35801 16392 -1466 545 -6700 N ATOM 1740 CA SER A 262 27.596 -19.422 -63.784 1.00176.24 C ANISOU 1740 CA SER A 262 14688 35789 16485 -824 127 -6839 C ATOM 1741 C SER A 262 28.664 -20.111 -62.898 1.00178.05 C ANISOU 1741 C SER A 262 14910 35729 17013 -435 -187 -6888 C ATOM 1742 O SER A 262 28.302 -20.833 -61.966 1.00177.58 O ANISOU 1742 O SER A 262 14770 35684 17017 -18 -514 -6962 O ATOM 1743 CB SER A 262 27.164 -20.388 -64.887 1.00178.50 C ANISOU 1743 CB SER A 262 15056 35791 16977 -436 -42 -6794 C ATOM 1744 OG SER A 262 26.661 -21.609 -64.371 1.00183.51 O ANISOU 1744 OG SER A 262 15921 35813 17992 180 -468 -6599 O ATOM 1745 N PHE A 263 29.963 -19.896 -63.196 1.00175.28 N ANISOU 1745 N PHE A 263 14364 35622 16614 -586 -96 -7104 N ATOM 1746 CA PHE A 263 31.079 -20.513 -62.473 1.00175.09 C ANISOU 1746 CA PHE A 263 14225 35520 16781 -258 -378 -7246 C ATOM 1747 C PHE A 263 31.438 -19.734 -61.179 1.00176.50 C ANISOU 1747 C PHE A 263 14527 35587 16950 -506 -302 -7110 C ATOM 1748 O PHE A 263 32.466 -20.032 -60.559 1.00176.12 O ANISOU 1748 O PHE A 263 14388 35509 17021 -333 -481 -7221 O ATOM 1749 CB PHE A 263 32.312 -20.597 -63.384 1.00176.46 C ANISOU 1749 CB PHE A 263 14444 35488 17115 -314 -304 -7233 C ATOM 1750 N PHE A 264 30.576 -18.780 -60.747 1.00173.84 N ANISOU 1750 N PHE A 264 14136 35636 16279 -917 -49 -7107 N ATOM 1751 CA PHE A 264 30.795 -18.008 -59.518 1.00173.51 C ANISOU 1751 CA PHE A 264 14128 35659 16137 -1182 37 -7055 C ATOM 1752 C PHE A 264 30.393 -18.792 -58.246 1.00174.28 C ANISOU 1752 C PHE A 264 14197 35668 16352 -707 -341 -7075 C ATOM 1753 O PHE A 264 30.394 -18.198 -57.166 1.00173.46 O ANISOU 1753 O PHE A 264 14089 35692 16125 -907 -282 -7054 O ATOM 1754 CB PHE A 264 30.029 -16.671 -59.526 1.00174.51 C ANISOU 1754 CB PHE A 264 14528 35741 16037 -1808 436 -6780 C ATOM 1755 CG PHE A 264 30.582 -15.551 -60.370 1.00175.44 C ANISOU 1755 CG PHE A 264 14892 35700 16066 -2366 814 -6622 C ATOM 1756 CD1 PHE A 264 31.715 -14.854 -59.967 1.00177.53 C ANISOU 1756 CD1 PHE A 264 15342 35675 16436 -2577 916 -6501 C ATOM 1757 CD2 PHE A 264 29.858 -15.049 -61.442 1.00176.57 C ANISOU 1757 CD2 PHE A 264 15280 35712 16096 -2668 1057 -6436 C ATOM 1758 CE1 PHE A 264 32.189 -13.769 -60.707 1.00178.25 C ANISOU 1758 CE1 PHE A 264 15701 35602 16423 -3067 1240 -6340 C ATOM 1759 CE2 PHE A 264 30.317 -13.946 -62.165 1.00178.48 C ANISOU 1759 CE2 PHE A 264 15887 35649 16280 -3150 1372 -6212 C ATOM 1760 CZ PHE A 264 31.485 -13.321 -61.801 1.00177.52 C ANISOU 1760 CZ PHE A 264 15764 35553 16130 -3381 1470 -6255 C ATOM 1761 N SER A 265 30.090 -20.117 -58.359 1.00171.06 N ANISOU 1761 N SER A 265 13507 35523 15964 -84 -742 -7379 N ATOM 1762 CA SER A 265 29.749 -20.987 -57.217 1.00169.50 C ANISOU 1762 CA SER A 265 13419 35056 15929 428 -1166 -7334 C ATOM 1763 C SER A 265 30.920 -21.055 -56.217 1.00172.20 C ANISOU 1763 C SER A 265 13694 35384 16351 528 -1341 -7460 C ATOM 1764 O SER A 265 30.737 -21.445 -55.061 1.00172.17 O ANISOU 1764 O SER A 265 13725 35330 16361 811 -1624 -7481 O ATOM 1765 CB SER A 265 29.379 -22.387 -57.696 1.00172.90 C ANISOU 1765 CB SER A 265 13896 35248 16551 1057 -1578 -7396 C ATOM 1766 OG SER A 265 29.068 -23.235 -56.603 1.00178.65 O ANISOU 1766 OG SER A 265 15018 35303 17559 1474 -1991 -7128 O ATOM 1767 N LEU A 266 32.114 -20.637 -56.684 1.00169.15 N ANISOU 1767 N LEU A 266 13068 35307 15894 289 -1167 -7680 N ATOM 1768 CA LEU A 266 33.369 -20.540 -55.943 1.00168.92 C ANISOU 1768 CA LEU A 266 12990 35240 15951 291 -1258 -7763 C ATOM 1769 C LEU A 266 33.317 -19.309 -54.997 1.00170.87 C ANISOU 1769 C LEU A 266 13415 35404 16105 -209 -973 -7531 C ATOM 1770 O LEU A 266 34.141 -19.194 -54.090 1.00171.52 O ANISOU 1770 O LEU A 266 13523 35380 16268 -191 -1075 -7536 O ATOM 1771 CB LEU A 266 34.534 -20.443 -56.971 1.00168.71 C ANISOU 1771 CB LEU A 266 12891 35199 16012 141 -1111 -7825 C ATOM 1772 CG LEU A 266 35.990 -20.613 -56.490 1.00171.96 C ANISOU 1772 CG LEU A 266 13451 35183 16704 223 -1254 -7713 C ATOM 1773 CD1 LEU A 266 36.252 -22.035 -55.992 1.00172.43 C ANISOU 1773 CD1 LEU A 266 13532 35002 16981 867 -1790 -7802 C ATOM 1774 CD2 LEU A 266 36.962 -20.325 -57.623 1.00173.30 C ANISOU 1774 CD2 LEU A 266 13658 35217 16969 -13 -1024 -7637 C ATOM 1775 N TYR A 267 32.330 -18.403 -55.212 1.00166.56 N ANISOU 1775 N TYR A 267 12685 35449 15152 -668 -623 -7615 N ATOM 1776 CA TYR A 267 32.086 -17.204 -54.399 1.00165.66 C ANISOU 1776 CA TYR A 267 12625 35519 14799 -1203 -329 -7507 C ATOM 1777 C TYR A 267 30.563 -17.039 -54.127 1.00162.38 C ANISOU 1777 C TYR A 267 12809 34307 14581 -1224 -282 -6906 C ATOM 1778 O TYR A 267 30.156 -16.081 -53.463 1.00161.10 O ANISOU 1778 O TYR A 267 12970 33846 14393 -1604 -65 -6581 O ATOM 1779 CB TYR A 267 32.664 -15.940 -55.073 1.00166.46 C ANISOU 1779 CB TYR A 267 12906 35524 14819 -1863 117 -7344 C ATOM 1780 CG TYR A 267 34.166 -15.973 -55.267 1.00168.71 C ANISOU 1780 CG TYR A 267 13258 35486 15358 -1798 73 -7332 C ATOM 1781 CD1 TYR A 267 35.030 -15.539 -54.264 1.00170.30 C ANISOU 1781 CD1 TYR A 267 13561 35491 15656 -1878 45 -7258 C ATOM 1782 CD2 TYR A 267 34.726 -16.400 -56.468 1.00169.69 C ANISOU 1782 CD2 TYR A 267 13380 35461 15632 -1675 70 -7353 C ATOM 1783 CE1 TYR A 267 36.416 -15.564 -54.438 1.00171.45 C ANISOU 1783 CE1 TYR A 267 13708 35450 15986 -1832 6 -7279 C ATOM 1784 CE2 TYR A 267 36.110 -16.426 -56.658 1.00170.79 C ANISOU 1784 CE2 TYR A 267 13523 35420 15950 -1641 41 -7369 C ATOM 1785 CZ TYR A 267 36.951 -16.007 -55.639 1.00175.48 C ANISOU 1785 CZ TYR A 267 14405 35494 16777 -1673 -8 -7112 C ATOM 1786 OH TYR A 267 38.313 -16.031 -55.826 1.00176.20 O ANISOU 1786 OH TYR A 267 14472 35457 17019 -1645 -37 -7133 O ATOM 1787 N LEU A 268 29.738 -17.991 -54.615 1.00154.12 N ANISOU 1787 N LEU A 268 11952 32843 13762 -796 -503 -6735 N ATOM 1788 CA LEU A 268 28.288 -17.999 -54.396 1.00148.31 C ANISOU 1788 CA LEU A 268 11788 31305 13258 -754 -499 -6163 C ATOM 1789 C LEU A 268 27.994 -18.502 -52.974 1.00148.40 C ANISOU 1789 C LEU A 268 12020 30923 13443 -442 -804 -5980 C ATOM 1790 O LEU A 268 27.942 -17.700 -52.035 1.00146.23 O ANISOU 1790 O LEU A 268 11909 30528 13122 -728 -661 -5802 O ATOM 1791 CB LEU A 268 27.574 -18.874 -55.464 1.00146.96 C ANISOU 1791 CB LEU A 268 11709 30887 13242 -433 -630 -6083 C ATOM 1792 CG LEU A 268 26.519 -18.216 -56.375 1.00147.90 C ANISOU 1792 CG LEU A 268 12172 30644 13379 -758 -315 -5713 C ATOM 1793 CD1 LEU A 268 27.158 -17.278 -57.388 1.00149.78 C ANISOU 1793 CD1 LEU A 268 12192 31383 13335 -1257 54 -5930 C ATOM 1794 CD2 LEU A 268 25.734 -19.267 -57.139 1.00147.09 C ANISOU 1794 CD2 LEU A 268 12192 30219 13477 -351 -529 -5605 C ATOM 1795 N GLY A 269 27.898 -19.827 -52.823 1.00144.57 N ANISOU 1795 N GLY A 269 11531 30275 13125 132 -1237 -6060 N ATOM 1796 CA GLY A 269 27.682 -20.486 -51.541 1.00143.91 C ANISOU 1796 CA GLY A 269 11671 29831 13179 461 -1589 -5923 C ATOM 1797 C GLY A 269 28.947 -20.527 -50.708 1.00152.06 C ANISOU 1797 C GLY A 269 12355 31343 14078 574 -1764 -6328 C ATOM 1798 O GLY A 269 29.072 -21.354 -49.802 1.00152.36 O ANISOU 1798 O GLY A 269 12485 31206 14198 976 -2167 -6368 O ATOM 1799 N ILE A 270 29.908 -19.638 -51.039 1.00151.84 N ANISOU 1799 N ILE A 270 11932 31940 13821 204 -1469 -6647 N ATOM 1800 CA ILE A 270 31.205 -19.472 -50.380 1.00155.60 C ANISOU 1800 CA ILE A 270 11994 33004 14122 212 -1554 -7087 C ATOM 1801 C ILE A 270 31.236 -18.125 -49.662 1.00158.14 C ANISOU 1801 C ILE A 270 12437 33328 14321 -367 -1189 -6886 C ATOM 1802 O ILE A 270 31.933 -17.983 -48.654 1.00158.43 O ANISOU 1802 O ILE A 270 12333 33579 14283 -350 -1298 -7057 O ATOM 1803 CB ILE A 270 32.348 -19.597 -51.401 1.00163.01 C ANISOU 1803 CB ILE A 270 12327 34750 14858 239 -1518 -7678 C ATOM 1804 N GLY A 271 30.454 -17.163 -50.178 1.00152.93 N ANISOU 1804 N GLY A 271 12067 32400 13639 -851 -787 -6525 N ATOM 1805 CA GLY A 271 30.236 -15.862 -49.552 1.00151.63 C ANISOU 1805 CA GLY A 271 12148 32090 13375 -1390 -453 -6254 C ATOM 1806 C GLY A 271 29.550 -16.106 -48.222 1.00153.29 C ANISOU 1806 C GLY A 271 12734 31741 13769 -1181 -657 -5911 C ATOM 1807 O GLY A 271 29.770 -15.375 -47.256 1.00153.31 O ANISOU 1807 O GLY A 271 12810 31746 13692 -1434 -554 -5843 O ATOM 1808 N TRP A 272 28.763 -17.217 -48.176 1.00147.27 N ANISOU 1808 N TRP A 272 12196 30523 13237 -711 -971 -5722 N ATOM 1809 CA TRP A 272 28.093 -17.875 -47.048 1.00144.78 C ANISOU 1809 CA TRP A 272 12225 29684 13100 -404 -1271 -5440 C ATOM 1810 C TRP A 272 29.087 -18.159 -45.898 1.00151.05 C ANISOU 1810 C TRP A 272 12818 30747 13826 -207 -1545 -5721 C ATOM 1811 O TRP A 272 28.670 -18.274 -44.742 1.00149.87 O ANISOU 1811 O TRP A 272 12966 30226 13752 -137 -1690 -5475 O ATOM 1812 CB TRP A 272 27.491 -19.200 -47.584 1.00142.82 C ANISOU 1812 CB TRP A 272 12102 29129 13034 77 -1602 -5380 C ATOM 1813 CG TRP A 272 26.814 -20.105 -46.594 1.00142.61 C ANISOU 1813 CG TRP A 272 12446 28576 13165 409 -1967 -5121 C ATOM 1814 CD1 TRP A 272 27.429 -20.897 -45.667 1.00147.92 C ANISOU 1814 CD1 TRP A 272 13083 29288 13834 772 -2382 -5312 C ATOM 1815 CD2 TRP A 272 25.448 -20.551 -46.650 1.00139.54 C ANISOU 1815 CD2 TRP A 272 12493 27582 12943 473 -2017 -4688 C ATOM 1816 NE1 TRP A 272 26.499 -21.678 -45.021 1.00146.05 N ANISOU 1816 NE1 TRP A 272 13293 28468 13732 978 -2654 -4975 N ATOM 1817 CE2 TRP A 272 25.276 -21.505 -45.622 1.00144.19 C ANISOU 1817 CE2 TRP A 272 13331 27852 13602 793 -2431 -4598 C ATOM 1818 CE3 TRP A 272 24.338 -20.201 -47.438 1.00137.55 C ANISOU 1818 CE3 TRP A 272 12459 27033 12770 268 -1750 -4370 C ATOM 1819 CZ2 TRP A 272 24.034 -22.096 -45.347 1.00141.07 C ANISOU 1819 CZ2 TRP A 272 13383 26879 13336 860 -2560 -4196 C ATOM 1820 CZ3 TRP A 272 23.111 -20.779 -47.161 1.00136.75 C ANISOU 1820 CZ3 TRP A 272 12762 26382 12813 371 -1879 -3992 C ATOM 1821 CH2 TRP A 272 22.968 -21.720 -46.132 1.00138.04 C ANISOU 1821 CH2 TRP A 272 13156 26264 13030 642 -2271 -3908 C ATOM 1822 N GLY A 273 30.380 -18.279 -46.247 1.00150.52 N ANISOU 1822 N GLY A 273 12241 31347 13605 -120 -1615 -6248 N ATOM 1823 CA GLY A 273 31.483 -18.593 -45.340 1.00153.02 C ANISOU 1823 CA GLY A 273 12272 32039 13830 114 -1898 -6624 C ATOM 1824 C GLY A 273 31.959 -17.493 -44.406 1.00156.20 C ANISOU 1824 C GLY A 273 12630 32632 14089 -305 -1667 -6620 C ATOM 1825 O GLY A 273 32.381 -17.800 -43.287 1.00157.20 O ANISOU 1825 O GLY A 273 12756 32759 14214 -86 -1939 -6712 O ATOM 1826 N ALA A 274 31.935 -16.207 -44.860 1.00151.20 N ANISOU 1826 N ALA A 274 11976 32161 13312 -910 -1183 -6529 N ATOM 1827 CA ALA A 274 32.366 -15.041 -44.055 1.00151.28 C ANISOU 1827 CA ALA A 274 11978 32341 13159 -1377 -929 -6512 C ATOM 1828 C ALA A 274 31.488 -14.878 -42.769 1.00152.87 C ANISOU 1828 C ALA A 274 12675 31908 13499 -1366 -992 -6054 C ATOM 1829 O ALA A 274 32.070 -14.742 -41.686 1.00153.67 O ANISOU 1829 O ALA A 274 12704 32144 13538 -1352 -1108 -6168 O ATOM 1830 CB ALA A 274 32.322 -13.764 -44.886 1.00151.45 C ANISOU 1830 CB ALA A 274 12013 32531 12999 -2020 -435 -6441 C ATOM 1831 N PRO A 275 30.123 -14.997 -42.820 1.00145.96 N ANISOU 1831 N PRO A 275 12276 30375 12807 -1328 -957 -5571 N ATOM 1832 CA PRO A 275 29.326 -14.886 -41.581 1.00143.72 C ANISOU 1832 CA PRO A 275 12415 29566 12627 -1320 -1021 -5182 C ATOM 1833 C PRO A 275 29.348 -16.160 -40.714 1.00148.52 C ANISOU 1833 C PRO A 275 13100 29975 13357 -794 -1510 -5209 C ATOM 1834 O PRO A 275 28.510 -16.308 -39.812 1.00146.19 O ANISOU 1834 O PRO A 275 13197 29190 13160 -748 -1601 -4856 O ATOM 1835 CB PRO A 275 27.908 -14.646 -42.107 1.00141.66 C ANISOU 1835 CB PRO A 275 12562 28772 12491 -1447 -822 -4732 C ATOM 1836 CG PRO A 275 28.057 -14.357 -43.548 1.00145.96 C ANISOU 1836 CG PRO A 275 12920 29571 12967 -1617 -597 -4872 C ATOM 1837 CD PRO A 275 29.225 -15.134 -43.979 1.00144.82 C ANISOU 1837 CD PRO A 275 12300 29966 12760 -1338 -826 -5360 C ATOM 1838 N MET A 276 30.288 -17.082 -41.004 1.00147.61 N ANISOU 1838 N MET A 276 12632 30239 13216 -398 -1836 -5638 N ATOM 1839 CA MET A 276 30.499 -18.333 -40.284 1.00148.56 C ANISOU 1839 CA MET A 276 12820 30216 13411 141 -2362 -5746 C ATOM 1840 C MET A 276 31.919 -18.318 -39.711 1.00156.02 C ANISOU 1840 C MET A 276 13349 31732 14199 266 -2541 -6235 C ATOM 1841 O MET A 276 32.101 -18.568 -38.520 1.00156.59 O ANISOU 1841 O MET A 276 13567 31666 14266 425 -2798 -6212 O ATOM 1842 CB MET A 276 30.247 -19.529 -41.226 1.00151.35 C ANISOU 1842 CB MET A 276 13172 30458 13876 575 -2647 -5831 C ATOM 1843 CG MET A 276 30.262 -20.903 -40.557 1.00156.59 C ANISOU 1843 CG MET A 276 14047 30835 14614 1138 -3233 -5875 C ATOM 1844 SD MET A 276 31.860 -21.502 -39.948 1.00166.24 S ANISOU 1844 SD MET A 276 14867 32599 15698 1594 -3695 -6495 S ATOM 1845 CE MET A 276 31.413 -23.164 -39.477 1.00164.07 C ANISOU 1845 CE MET A 276 15058 31751 15532 2225 -4373 -6395 C ATOM 1846 N LEU A 277 32.916 -17.971 -40.550 1.00154.68 N ANISOU 1846 N LEU A 277 12658 32230 13882 159 -2388 -6681 N ATOM 1847 CA LEU A 277 34.324 -17.907 -40.156 1.00158.51 C ANISOU 1847 CA LEU A 277 12658 33379 14190 250 -2525 -7216 C ATOM 1848 C LEU A 277 34.565 -16.792 -39.118 1.00161.50 C ANISOU 1848 C LEU A 277 13084 33821 14455 -192 -2280 -7110 C ATOM 1849 O LEU A 277 35.077 -17.082 -38.041 1.00162.47 O ANISOU 1849 O LEU A 277 13189 33992 14550 36 -2570 -7246 O ATOM 1850 CB LEU A 277 35.220 -17.684 -41.385 1.00161.37 C ANISOU 1850 CB LEU A 277 12446 34475 14392 131 -2342 -7697 C ATOM 1851 N PHE A 278 34.166 -15.540 -39.419 1.00155.96 N ANISOU 1851 N PHE A 278 12490 33082 13686 -804 -1776 -6857 N ATOM 1852 CA PHE A 278 34.385 -14.404 -38.521 1.00155.71 C ANISOU 1852 CA PHE A 278 12525 33108 13530 -1256 -1524 -6759 C ATOM 1853 C PHE A 278 33.189 -14.212 -37.540 1.00156.65 C ANISOU 1853 C PHE A 278 13242 32482 13797 -1312 -1510 -6192 C ATOM 1854 O PHE A 278 32.947 -13.092 -37.075 1.00154.34 O ANISOU 1854 O PHE A 278 13133 32079 13429 -1767 -1197 -5971 O ATOM 1855 CB PHE A 278 34.617 -13.126 -39.341 1.00157.62 C ANISOU 1855 CB PHE A 278 12617 33689 13581 -1900 -1018 -6803 C ATOM 1856 N VAL A 279 32.478 -15.314 -37.193 1.00153.29 N ANISOU 1856 N VAL A 279 13116 31569 13557 -855 -1865 -5980 N ATOM 1857 CA VAL A 279 31.349 -15.282 -36.250 1.00150.79 C ANISOU 1857 CA VAL A 279 13335 30600 13360 -887 -1884 -5480 C ATOM 1858 C VAL A 279 31.397 -16.515 -35.324 1.00155.86 C ANISOU 1858 C VAL A 279 14140 31003 14078 -375 -2411 -5499 C ATOM 1859 O VAL A 279 31.479 -16.340 -34.106 1.00155.65 O ANISOU 1859 O VAL A 279 14274 30855 14012 -408 -2506 -5410 O ATOM 1860 CB VAL A 279 29.944 -15.190 -36.945 1.00151.57 C ANISOU 1860 CB VAL A 279 13800 30193 13598 -1015 -1670 -5037 C ATOM 1861 CG1 VAL A 279 28.805 -15.255 -35.921 1.00148.63 C ANISOU 1861 CG1 VAL A 279 13929 29220 13324 -1026 -1718 -4574 C ATOM 1862 CG2 VAL A 279 29.809 -13.938 -37.807 1.00150.50 C ANISOU 1862 CG2 VAL A 279 13605 30208 13372 -1518 -1180 -4981 C ATOM 1863 N VAL A 280 31.288 -17.750 -35.908 1.00152.87 N ANISOU 1863 N VAL A 280 13771 30516 13796 83 -2759 -5594 N ATOM 1864 CA VAL A 280 31.177 -19.038 -35.203 1.00153.69 C ANISOU 1864 CA VAL A 280 14143 30290 13964 579 -3300 -5571 C ATOM 1865 C VAL A 280 32.192 -19.130 -34.040 1.00160.45 C ANISOU 1865 C VAL A 280 14874 31389 14701 754 -3590 -5852 C ATOM 1866 O VAL A 280 31.719 -19.260 -32.917 1.00159.56 O ANISOU 1866 O VAL A 280 15152 30873 14599 748 -3731 -5569 O ATOM 1867 CB VAL A 280 31.331 -20.267 -36.121 1.00159.24 C ANISOU 1867 CB VAL A 280 14754 31020 14732 1068 -3661 -5801 C ATOM 1868 N PRO A 281 33.540 -19.026 -34.217 1.00160.02 N ANISOU 1868 N PRO A 281 14292 31991 14518 883 -3672 -6397 N ATOM 1869 CA PRO A 281 34.427 -19.141 -33.041 1.00162.47 C ANISOU 1869 CA PRO A 281 14516 32497 14718 1072 -3975 -6650 C ATOM 1870 C PRO A 281 34.250 -17.975 -32.061 1.00163.66 C ANISOU 1870 C PRO A 281 14801 32574 14807 579 -3637 -6392 C ATOM 1871 O PRO A 281 34.267 -18.195 -30.849 1.00163.36 O ANISOU 1871 O PRO A 281 15019 32306 14744 695 -3887 -6295 O ATOM 1872 CB PRO A 281 35.834 -19.135 -33.650 1.00168.42 C ANISOU 1872 CB PRO A 281 14602 34053 15335 1243 -4043 -7308 C ATOM 1873 CG PRO A 281 35.681 -18.475 -34.969 1.00171.55 C ANISOU 1873 CG PRO A 281 14736 34718 15729 878 -3578 -7322 C ATOM 1874 CD PRO A 281 34.322 -18.862 -35.461 1.00163.42 C ANISOU 1874 CD PRO A 281 14175 33037 14880 877 -3522 -6831 C ATOM 1875 N TRP A 282 34.001 -16.754 -32.592 1.00157.59 N ANISOU 1875 N TRP A 282 13922 31948 14009 28 -3084 -6256 N ATOM 1876 CA TRP A 282 33.832 -15.514 -31.829 1.00155.53 C ANISOU 1876 CA TRP A 282 13780 31639 13674 -475 -2721 -6031 C ATOM 1877 C TRP A 282 32.542 -15.526 -30.971 1.00155.06 C ANISOU 1877 C TRP A 282 14318 30877 13720 -560 -2710 -5470 C ATOM 1878 O TRP A 282 32.280 -14.559 -30.252 1.00152.93 O ANISOU 1878 O TRP A 282 14203 30504 13397 -933 -2443 -5257 O ATOM 1879 CB TRP A 282 33.803 -14.321 -32.789 1.00153.05 C ANISOU 1879 CB TRP A 282 13274 31587 13289 -1004 -2185 -6022 C ATOM 1880 N ALA A 283 31.770 -16.626 -31.016 1.00150.16 N ANISOU 1880 N ALA A 283 14027 29801 13227 -223 -3010 -5256 N ATOM 1881 CA ALA A 283 30.554 -16.771 -30.226 1.00147.01 C ANISOU 1881 CA ALA A 283 14169 28789 12900 -302 -3027 -4760 C ATOM 1882 C ALA A 283 30.458 -18.170 -29.593 1.00152.26 C ANISOU 1882 C ALA A 283 15134 29126 13591 162 -3590 -4733 C ATOM 1883 O ALA A 283 29.944 -18.259 -28.486 1.00151.31 O ANISOU 1883 O ALA A 283 15392 28653 13446 99 -3692 -4456 O ATOM 1884 CB ALA A 283 29.327 -16.504 -31.082 1.00144.18 C ANISOU 1884 CB ALA A 283 14011 28117 12653 -526 -2706 -4405 C ATOM 1885 N VAL A 284 30.939 -19.255 -30.273 1.00150.82 N ANISOU 1885 N VAL A 284 14817 29049 13439 618 -3969 -5021 N ATOM 1886 CA VAL A 284 30.848 -20.623 -29.714 1.00152.28 C ANISOU 1886 CA VAL A 284 15363 28872 13624 1073 -4556 -4998 C ATOM 1887 C VAL A 284 31.948 -20.808 -28.662 1.00158.56 C ANISOU 1887 C VAL A 284 16064 29893 14289 1321 -4916 -5316 C ATOM 1888 O VAL A 284 31.706 -21.456 -27.641 1.00159.30 O ANISOU 1888 O VAL A 284 16592 29599 14335 1478 -5281 -5149 O ATOM 1889 CB VAL A 284 30.884 -21.800 -30.748 1.00157.91 C ANISOU 1889 CB VAL A 284 16059 29532 14408 1518 -4899 -5173 C ATOM 1890 CG1 VAL A 284 29.718 -21.726 -31.732 1.00154.14 C ANISOU 1890 CG1 VAL A 284 15726 28779 14061 1295 -4586 -4834 C ATOM 1891 CG2 VAL A 284 32.223 -21.909 -31.481 1.00161.23 C ANISOU 1891 CG2 VAL A 284 15893 30590 14777 1831 -5030 -5778 C ATOM 1892 N VAL A 285 33.148 -20.256 -28.913 1.00156.45 N ANISOU 1892 N VAL A 285 15239 30260 13944 1343 -4825 -5781 N ATOM 1893 CA VAL A 285 34.259 -20.369 -27.975 1.00159.57 C ANISOU 1893 CA VAL A 285 15474 30947 14207 1584 -5153 -6137 C ATOM 1894 C VAL A 285 34.087 -19.337 -26.850 1.00160.27 C ANISOU 1894 C VAL A 285 15695 30968 14232 1143 -4860 -5891 C ATOM 1895 O VAL A 285 34.358 -19.654 -25.695 1.00160.96 O ANISOU 1895 O VAL A 285 16004 30915 14239 1306 -5187 -5898 O ATOM 1896 CB VAL A 285 35.619 -20.211 -28.680 1.00167.00 C ANISOU 1896 CB VAL A 285 15729 32657 15068 1771 -5174 -6771 C ATOM 1897 N LYS A 286 33.596 -18.122 -27.183 1.00153.13 N ANISOU 1897 N LYS A 286 14699 30129 13356 597 -4268 -5663 N ATOM 1898 CA LYS A 286 33.355 -17.054 -26.210 1.00150.85 C ANISOU 1898 CA LYS A 286 14545 29764 13006 160 -3956 -5422 C ATOM 1899 C LYS A 286 32.139 -17.377 -25.316 1.00151.54 C ANISOU 1899 C LYS A 286 15251 29191 13135 87 -4035 -4904 C ATOM 1900 O LYS A 286 32.018 -16.791 -24.240 1.00149.74 O ANISOU 1900 O LYS A 286 15194 28864 12836 -146 -3935 -4738 O ATOM 1901 CB LYS A 286 33.142 -15.712 -26.923 1.00151.03 C ANISOU 1901 CB LYS A 286 14347 30006 13031 -368 -3345 -5340 C ATOM 1902 N CYS A 287 31.251 -18.310 -25.754 1.00147.46 N ANISOU 1902 N CYS A 287 15063 28250 12715 268 -4213 -4663 N ATOM 1903 CA CYS A 287 30.067 -18.725 -24.987 1.00145.63 C ANISOU 1903 CA CYS A 287 15410 27429 12494 173 -4299 -4191 C ATOM 1904 C CYS A 287 30.488 -19.670 -23.858 1.00153.34 C ANISOU 1904 C CYS A 287 16689 28212 13363 504 -4862 -4257 C ATOM 1905 O CYS A 287 30.191 -19.381 -22.706 1.00152.08 O ANISOU 1905 O CYS A 287 16808 27857 13119 305 -4845 -4036 O ATOM 1906 CB CYS A 287 29.014 -19.374 -25.884 1.00143.72 C ANISOU 1906 CB CYS A 287 15396 26842 12368 212 -4288 -3935 C ATOM 1907 N LEU A 288 31.213 -20.775 -24.179 1.00154.03 N ANISOU 1907 N LEU A 288 16726 28363 13435 1020 -5376 -4582 N ATOM 1908 CA LEU A 288 31.687 -21.773 -23.202 1.00157.57 C ANISOU 1908 CA LEU A 288 17501 28607 13764 1409 -5995 -4690 C ATOM 1909 C LEU A 288 32.606 -21.134 -22.124 1.00163.54 C ANISOU 1909 C LEU A 288 18078 29664 14397 1369 -6021 -4904 C ATOM 1910 O LEU A 288 32.829 -21.728 -21.068 1.00165.07 O ANISOU 1910 O LEU A 288 18619 29630 14470 1574 -6458 -4898 O ATOM 1911 CB LEU A 288 32.438 -22.897 -23.927 1.00161.10 C ANISOU 1911 CB LEU A 288 17822 29170 14217 2006 -6510 -5097 C ATOM 1912 N PHE A 289 33.101 -19.912 -22.404 1.00159.96 N ANISOU 1912 N PHE A 289 17116 29703 13959 1075 -5552 -5078 N ATOM 1913 CA PHE A 289 33.956 -19.084 -21.554 1.00161.45 C ANISOU 1913 CA PHE A 289 17052 30252 14038 942 -5460 -5287 C ATOM 1914 C PHE A 289 33.106 -18.339 -20.513 1.00163.46 C ANISOU 1914 C PHE A 289 17667 30183 14256 483 -5163 -4835 C ATOM 1915 O PHE A 289 33.393 -18.430 -19.324 1.00164.50 O ANISOU 1915 O PHE A 289 18006 30223 14273 534 -5402 -4828 O ATOM 1916 CB PHE A 289 34.739 -18.098 -22.448 1.00163.31 C ANISOU 1916 CB PHE A 289 16628 31134 14288 753 -5055 -5639 C ATOM 1917 CG PHE A 289 35.650 -17.102 -21.775 1.00166.27 C ANISOU 1917 CG PHE A 289 16671 31961 14545 535 -4880 -5883 C ATOM 1918 CD1 PHE A 289 36.977 -17.417 -21.513 1.00174.27 C ANISOU 1918 CD1 PHE A 289 17323 33443 15449 893 -5238 -6412 C ATOM 1919 CD2 PHE A 289 35.216 -15.808 -21.509 1.00165.65 C ANISOU 1919 CD2 PHE A 289 16601 31883 14454 -27 -4348 -5625 C ATOM 1920 CE1 PHE A 289 37.836 -16.478 -20.930 1.00176.91 C ANISOU 1920 CE1 PHE A 289 17322 34234 15663 662 -5062 -6656 C ATOM 1921 CE2 PHE A 289 36.074 -14.868 -20.929 1.00170.30 C ANISOU 1921 CE2 PHE A 289 16892 32891 14921 -255 -4184 -5856 C ATOM 1922 CZ PHE A 289 37.379 -15.210 -20.643 1.00172.94 C ANISOU 1922 CZ PHE A 289 16868 33693 15148 73 -4532 -6365 C ATOM 1923 N GLU A 290 32.051 -17.625 -20.960 1.00157.62 N ANISOU 1923 N GLU A 290 17009 29276 13605 58 -4664 -4474 N ATOM 1924 CA GLU A 290 31.162 -16.864 -20.081 1.00155.71 C ANISOU 1924 CA GLU A 290 17074 28761 13326 -370 -4351 -4068 C ATOM 1925 C GLU A 290 29.678 -17.083 -20.483 1.00158.57 C ANISOU 1925 C GLU A 290 17795 28678 13776 -558 -4164 -3620 C ATOM 1926 O GLU A 290 28.994 -16.146 -20.915 1.00154.82 O ANISOU 1926 O GLU A 290 17248 28215 13361 -913 -3681 -3430 O ATOM 1927 CB GLU A 290 31.528 -15.372 -20.122 1.00155.89 C ANISOU 1927 CB GLU A 290 16740 29162 13328 -761 -3853 -4162 C ATOM 1928 N ASN A 291 29.190 -18.336 -20.323 1.00157.98 N ANISOU 1928 N ASN A 291 18126 28210 13689 -316 -4572 -3464 N ATOM 1929 CA ASN A 291 27.808 -18.730 -20.628 1.00156.08 C ANISOU 1929 CA ASN A 291 18247 27555 13501 -478 -4467 -3061 C ATOM 1930 C ASN A 291 26.891 -18.440 -19.448 1.00160.97 C ANISOU 1930 C ASN A 291 19266 27883 14013 -820 -4342 -2684 C ATOM 1931 O ASN A 291 27.285 -18.631 -18.291 1.00162.69 O ANISOU 1931 O ASN A 291 19689 28035 14093 -778 -4602 -2698 O ATOM 1932 CB ASN A 291 27.728 -20.217 -20.998 1.00157.73 C ANISOU 1932 CB ASN A 291 18736 27479 13714 -101 -4976 -3076 C ATOM 1933 N VAL A 292 25.663 -17.987 -19.743 1.00156.00 N ANISOU 1933 N VAL A 292 18741 27099 13435 -1147 -3954 -2365 N ATOM 1934 CA VAL A 292 24.673 -17.669 -18.723 1.00155.50 C ANISOU 1934 CA VAL A 292 19010 26813 13261 -1492 -3788 -2023 C ATOM 1935 C VAL A 292 23.314 -18.237 -19.150 1.00159.53 C ANISOU 1935 C VAL A 292 19806 27015 13793 -1631 -3724 -1702 C ATOM 1936 O VAL A 292 23.085 -19.441 -19.011 1.00160.55 O ANISOU 1936 O VAL A 292 20289 26858 13855 -1497 -4117 -1603 O ATOM 1937 CB VAL A 292 24.608 -16.143 -18.464 1.00157.52 C ANISOU 1937 CB VAL A 292 19021 27307 13520 -1808 -3291 -2016 C ATOM 1938 N GLN A 293 22.430 -17.373 -19.683 1.00155.03 N ANISOU 1938 N GLN A 293 19096 26504 13302 -1895 -3250 -1556 N ATOM 1939 CA GLN A 293 21.085 -17.732 -20.121 1.00154.37 C ANISOU 1939 CA GLN A 293 19212 26201 13239 -2058 -3121 -1276 C ATOM 1940 C GLN A 293 21.099 -18.267 -21.558 1.00160.22 C ANISOU 1940 C GLN A 293 19801 26932 14142 -1835 -3175 -1368 C ATOM 1941 O GLN A 293 22.166 -18.361 -22.173 1.00160.93 O ANISOU 1941 O GLN A 293 19627 27203 14316 -1556 -3313 -1658 O ATOM 1942 CB GLN A 293 20.157 -16.509 -20.015 1.00153.22 C ANISOU 1942 CB GLN A 293 18972 26150 13095 -2395 -2610 -1122 C ATOM 1943 N CYS A 294 19.906 -18.634 -22.080 1.00157.19 N ANISOU 1943 N CYS A 294 19573 26364 13787 -1963 -3068 -1136 N ATOM 1944 CA CYS A 294 19.709 -19.142 -23.437 1.00157.07 C ANISOU 1944 CA CYS A 294 19450 26309 13919 -1791 -3092 -1178 C ATOM 1945 C CYS A 294 20.102 -18.050 -24.447 1.00161.01 C ANISOU 1945 C CYS A 294 19503 27103 14569 -1766 -2724 -1369 C ATOM 1946 O CYS A 294 21.105 -18.203 -25.148 1.00161.11 O ANISOU 1946 O CYS A 294 19269 27283 14663 -1508 -2853 -1640 O ATOM 1947 CB CYS A 294 18.265 -19.602 -23.626 1.00156.34 C ANISOU 1947 CB CYS A 294 19614 25990 13800 -2003 -3005 -878 C ATOM 1948 SG CYS A 294 17.905 -20.273 -25.270 1.00159.40 S ANISOU 1948 SG CYS A 294 19905 26299 14360 -1810 -3040 -902 S ATOM 1949 N TRP A 295 19.352 -16.927 -24.464 1.00157.32 N ANISOU 1949 N TRP A 295 18949 26713 14111 -2040 -2283 -1249 N ATOM 1950 CA TRP A 295 19.651 -15.772 -25.307 1.00156.37 C ANISOU 1950 CA TRP A 295 18495 26831 14089 -2080 -1929 -1398 C ATOM 1951 C TRP A 295 20.747 -14.953 -24.623 1.00163.62 C ANISOU 1951 C TRP A 295 19248 27980 14940 -2117 -1884 -1596 C ATOM 1952 O TRP A 295 20.455 -14.137 -23.740 1.00162.90 O ANISOU 1952 O TRP A 295 19234 27904 14758 -2337 -1692 -1502 O ATOM 1953 CB TRP A 295 18.381 -14.943 -25.576 1.00152.69 C ANISOU 1953 CB TRP A 295 18062 26316 13637 -2320 -1534 -1201 C ATOM 1954 N THR A 296 22.019 -15.243 -24.977 1.00163.42 N ANISOU 1954 N THR A 296 18997 28151 14943 -1890 -2090 -1887 N ATOM 1955 CA THR A 296 23.216 -14.636 -24.391 1.00165.65 C ANISOU 1955 CA THR A 296 19085 28702 15154 -1895 -2105 -2129 C ATOM 1956 C THR A 296 23.146 -13.101 -24.458 1.00170.06 C ANISOU 1956 C THR A 296 19502 29423 15689 -2195 -1659 -2134 C ATOM 1957 O THR A 296 22.852 -12.530 -25.512 1.00168.00 O ANISOU 1957 O THR A 296 19117 29218 15499 -2282 -1389 -2140 O ATOM 1958 CB THR A 296 24.468 -15.147 -25.097 1.00176.07 C ANISOU 1958 CB THR A 296 20106 30277 16516 -1605 -2343 -2481 C ATOM 1959 N SER A 297 23.382 -12.452 -23.300 1.00168.83 N ANISOU 1959 N SER A 297 19412 29315 15420 -2354 -1604 -2121 N ATOM 1960 CA SER A 297 23.335 -10.998 -23.120 1.00168.29 C ANISOU 1960 CA SER A 297 19288 29360 15295 -2641 -1232 -2119 C ATOM 1961 C SER A 297 24.658 -10.326 -23.545 1.00174.86 C ANISOU 1961 C SER A 297 19794 30548 16097 -2685 -1157 -2441 C ATOM 1962 O SER A 297 25.632 -11.012 -23.869 1.00176.03 O ANISOU 1962 O SER A 297 19724 30895 16265 -2472 -1401 -2688 O ATOM 1963 CB SER A 297 23.031 -10.661 -21.662 1.00172.06 C ANISOU 1963 CB SER A 297 19985 29739 15651 -2786 -1230 -1977 C ATOM 1964 N ASN A 298 24.676 -8.974 -23.528 1.00172.02 N ANISOU 1964 N ASN A 298 19413 30278 15669 -2973 -826 -2451 N ATOM 1965 CA ASN A 298 25.803 -8.124 -23.914 1.00173.74 C ANISOU 1965 CA ASN A 298 19366 30832 15813 -3134 -686 -2726 C ATOM 1966 C ASN A 298 27.073 -8.453 -23.108 1.00181.59 C ANISOU 1966 C ASN A 298 20170 32097 16729 -3037 -940 -2984 C ATOM 1967 O ASN A 298 27.117 -8.240 -21.893 1.00181.60 O ANISOU 1967 O ASN A 298 20308 32044 16650 -3095 -999 -2924 O ATOM 1968 CB ASN A 298 25.437 -6.651 -23.718 1.00173.88 C ANISOU 1968 CB ASN A 298 19530 30799 15736 -3474 -340 -2633 C ATOM 1969 N ASP A 299 28.099 -8.982 -23.802 1.00181.21 N ANISOU 1969 N ASP A 299 19793 32362 16695 -2874 -1099 -3292 N ATOM 1970 CA ASP A 299 29.401 -9.330 -23.222 1.00184.51 C ANISOU 1970 CA ASP A 299 19959 33113 17034 -2733 -1362 -3614 C ATOM 1971 C ASP A 299 30.474 -8.300 -23.637 1.00191.23 C ANISOU 1971 C ASP A 299 20478 34418 17763 -3018 -1134 -3921 C ATOM 1972 O ASP A 299 31.609 -8.367 -23.150 1.00193.69 O ANISOU 1972 O ASP A 299 20533 35079 17980 -2965 -1297 -4225 O ATOM 1973 CB ASP A 299 29.818 -10.746 -23.655 1.00187.87 C ANISOU 1973 CB ASP A 299 20239 33606 17539 -2300 -1756 -3793 C ATOM 1974 N ASN A 300 30.088 -7.337 -24.529 1.00186.84 N ANISOU 1974 N ASN A 300 19951 33851 17188 -3338 -764 -3840 N ATOM 1975 CA ASN A 300 30.892 -6.243 -25.112 1.00188.00 C ANISOU 1975 CA ASN A 300 19877 34365 17189 -3715 -489 -4068 C ATOM 1976 C ASN A 300 32.028 -6.833 -25.962 1.00193.64 C ANISOU 1976 C ASN A 300 20124 35575 17876 -3581 -622 -4476 C ATOM 1977 O ASN A 300 31.953 -6.784 -27.190 1.00192.44 O ANISOU 1977 O ASN A 300 19861 35516 17740 -3657 -475 -4527 O ATOM 1978 CB ASN A 300 31.449 -5.282 -24.030 1.00190.90 C ANISOU 1978 CB ASN A 300 20278 34860 17395 -3999 -399 -4131 C ATOM 1979 CG ASN A 300 32.247 -4.098 -24.553 1.00209.84 C ANISOU 1979 CG ASN A 300 23209 36170 20350 -3867 -241 -3852 C ATOM 1980 OD1 ASN A 300 32.170 -3.712 -25.729 1.00206.18 O ANISOU 1980 OD1 ASN A 300 22583 36024 19733 -4147 -15 -3958 O ATOM 1981 ND2 ASN A 300 32.978 -3.448 -23.661 1.00204.34 N ANISOU 1981 ND2 ASN A 300 22301 35996 19342 -4200 -196 -4093 N ATOM 1982 N MET A 301 33.061 -7.397 -25.302 1.00192.75 N ANISOU 1982 N MET A 301 19735 35788 17712 -3366 -910 -4779 N ATOM 1983 CA MET A 301 34.222 -8.027 -25.932 1.00194.22 C ANISOU 1983 CA MET A 301 19572 36246 17978 -3107 -1111 -5132 C ATOM 1984 C MET A 301 33.784 -9.288 -26.712 1.00196.42 C ANISOU 1984 C MET A 301 19844 36364 18424 -2678 -1349 -5106 C ATOM 1985 O MET A 301 34.326 -9.568 -27.782 1.00196.12 O ANISOU 1985 O MET A 301 19662 36324 18532 -2552 -1363 -5238 O ATOM 1986 CB MET A 301 35.273 -8.374 -24.851 1.00196.90 C ANISOU 1986 CB MET A 301 20015 36290 18507 -2790 -1449 -5190 C ATOM 1987 CG MET A 301 36.613 -8.886 -25.396 1.00199.87 C ANISOU 1987 CG MET A 301 20401 36286 19255 -2442 -1686 -5281 C ATOM 1988 SD MET A 301 37.570 -7.700 -26.394 1.00201.80 S ANISOU 1988 SD MET A 301 20740 36200 19735 -2730 -1348 -5189 S ATOM 1989 CE MET A 301 37.906 -6.418 -25.173 1.00199.59 C ANISOU 1989 CE MET A 301 20497 36096 19240 -3125 -1165 -5213 C ATOM 1990 N GLY A 302 32.790 -10.001 -26.182 1.00190.76 N ANISOU 1990 N GLY A 302 19366 35387 17726 -2466 -1528 -4874 N ATOM 1991 CA GLY A 302 32.270 -11.222 -26.780 1.00189.29 C ANISOU 1991 CA GLY A 302 19257 34973 17691 -2067 -1782 -4804 C ATOM 1992 C GLY A 302 31.509 -11.038 -28.079 1.00189.79 C ANISOU 1992 C GLY A 302 19370 34903 17839 -2198 -1516 -4642 C ATOM 1993 O GLY A 302 31.909 -11.589 -29.110 1.00190.42 O ANISOU 1993 O GLY A 302 19179 35225 17949 -2019 -1597 -4878 O ATOM 1994 N PHE A 303 30.395 -10.275 -28.040 1.00182.34 N ANISOU 1994 N PHE A 303 18773 33580 16928 -2488 -1212 -4256 N ATOM 1995 CA PHE A 303 29.516 -10.099 -29.198 1.00179.13 C ANISOU 1995 CA PHE A 303 18478 32977 16605 -2590 -978 -4063 C ATOM 1996 C PHE A 303 30.020 -9.057 -30.220 1.00180.92 C ANISOU 1996 C PHE A 303 18488 33538 16715 -2967 -631 -4238 C ATOM 1997 O PHE A 303 29.583 -9.138 -31.372 1.00179.82 O ANISOU 1997 O PHE A 303 18347 33343 16634 -2978 -510 -4187 O ATOM 1998 CB PHE A 303 28.096 -9.695 -28.789 1.00178.08 C ANISOU 1998 CB PHE A 303 18793 32331 16537 -2721 -811 -3617 C ATOM 1999 CG PHE A 303 27.193 -10.848 -28.410 1.00178.72 C ANISOU 1999 CG PHE A 303 19129 32026 16751 -2399 -1082 -3376 C ATOM 2000 CD1 PHE A 303 26.632 -11.663 -29.390 1.00180.76 C ANISOU 2000 CD1 PHE A 303 19407 32139 17134 -2192 -1164 -3308 C ATOM 2001 CD2 PHE A 303 26.802 -11.043 -27.091 1.00180.97 C ANISOU 2001 CD2 PHE A 303 19672 32071 17016 -2360 -1225 -3190 C ATOM 2002 CE1 PHE A 303 25.764 -12.701 -29.050 1.00180.78 C ANISOU 2002 CE1 PHE A 303 19679 31778 17231 -1955 -1406 -3074 C ATOM 2003 CE2 PHE A 303 25.925 -12.079 -26.753 1.00182.97 C ANISOU 2003 CE2 PHE A 303 20198 31969 17352 -2139 -1459 -2954 C ATOM 2004 CZ PHE A 303 25.408 -12.896 -27.737 1.00180.14 C ANISOU 2004 CZ PHE A 303 19859 31477 17110 -1949 -1547 -2895 C ATOM 2005 N TRP A 304 30.906 -8.100 -29.851 1.00176.94 N ANISOU 2005 N TRP A 304 17826 33373 16032 -3297 -473 -4438 N ATOM 2006 CA TRP A 304 31.361 -7.136 -30.866 1.00176.63 C ANISOU 2006 CA TRP A 304 17631 33639 15844 -3711 -149 -4592 C ATOM 2007 C TRP A 304 32.217 -7.863 -31.912 1.00178.81 C ANISOU 2007 C TRP A 304 17454 34382 16104 -3543 -262 -4969 C ATOM 2008 O TRP A 304 32.154 -7.545 -33.100 1.00177.87 O ANISOU 2008 O TRP A 304 17271 34372 15940 -3743 -51 -5007 O ATOM 2009 CB TRP A 304 32.126 -5.963 -30.257 1.00177.54 C ANISOU 2009 CB TRP A 304 17697 34018 15742 -4146 39 -4726 C ATOM 2010 CG TRP A 304 32.043 -4.731 -31.105 1.00178.83 C ANISOU 2010 CG TRP A 304 17986 34216 15746 -4662 415 -4681 C ATOM 2011 CD1 TRP A 304 32.699 -4.491 -32.277 1.00183.72 C ANISOU 2011 CD1 TRP A 304 18340 35237 16227 -4913 570 -4934 C ATOM 2012 CD2 TRP A 304 31.268 -3.555 -30.830 1.00176.99 C ANISOU 2012 CD2 TRP A 304 18209 33594 15445 -4998 662 -4374 C ATOM 2013 NE1 TRP A 304 32.345 -3.257 -32.774 1.00182.89 N ANISOU 2013 NE1 TRP A 304 18546 34974 15971 -5401 893 -4773 N ATOM 2014 CE2 TRP A 304 31.484 -2.651 -31.894 1.00182.18 C ANISOU 2014 CE2 TRP A 304 18905 34394 15922 -5443 942 -4440 C ATOM 2015 CE3 TRP A 304 30.411 -3.173 -29.780 1.00176.16 C ANISOU 2015 CE3 TRP A 304 18495 33041 15397 -4963 662 -4065 C ATOM 2016 CZ2 TRP A 304 30.877 -1.388 -31.941 1.00180.60 C ANISOU 2016 CZ2 TRP A 304 19160 33863 15597 -5826 1189 -4204 C ATOM 2017 CZ3 TRP A 304 29.811 -1.922 -29.827 1.00176.65 C ANISOU 2017 CZ3 TRP A 304 18957 32815 15346 -5318 918 -3855 C ATOM 2018 CH2 TRP A 304 30.045 -1.044 -30.896 1.00178.48 C ANISOU 2018 CH2 TRP A 304 19258 33155 15400 -5731 1163 -3923 C ATOM 2019 N TRP A 305 32.974 -8.874 -31.459 1.00175.16 N ANISOU 2019 N TRP A 305 16701 34179 15674 -3146 -620 -5251 N ATOM 2020 CA TRP A 305 33.769 -9.763 -32.298 1.00176.53 C ANISOU 2020 CA TRP A 305 16436 34790 15846 -2857 -818 -5645 C ATOM 2021 C TRP A 305 32.886 -10.812 -32.964 1.00177.05 C ANISOU 2021 C TRP A 305 16665 34488 16118 -2467 -993 -5457 C ATOM 2022 O TRP A 305 33.192 -11.253 -34.073 1.00177.89 O ANISOU 2022 O TRP A 305 16502 34862 16228 -2353 -1011 -5681 O ATOM 2023 CB TRP A 305 34.863 -10.453 -31.465 1.00178.37 C ANISOU 2023 CB TRP A 305 16345 35397 16029 -2520 -1189 -6026 C ATOM 2024 CG TRP A 305 36.048 -9.596 -31.128 1.00180.82 C ANISOU 2024 CG TRP A 305 16508 35925 16270 -2803 -1065 -6217 C ATOM 2025 CD1 TRP A 305 36.069 -8.522 -30.288 1.00182.54 C ANISOU 2025 CD1 TRP A 305 16991 35912 16454 -3162 -865 -6009 C ATOM 2026 CD2 TRP A 305 37.418 -9.891 -31.432 1.00181.10 C ANISOU 2026 CD2 TRP A 305 16424 35860 16523 -2575 -1238 -6402 C ATOM 2027 NE1 TRP A 305 37.356 -8.054 -30.150 1.00182.45 N ANISOU 2027 NE1 TRP A 305 16943 35827 16553 -3226 -864 -6120 N ATOM 2028 CE2 TRP A 305 38.208 -8.889 -30.825 1.00183.77 C ANISOU 2028 CE2 TRP A 305 17002 35841 16980 -2832 -1104 -6244 C ATOM 2029 CE3 TRP A 305 38.056 -10.887 -32.192 1.00182.32 C ANISOU 2029 CE3 TRP A 305 16495 35850 16927 -2142 -1505 -6515 C ATOM 2030 CZ2 TRP A 305 39.602 -8.849 -30.958 1.00183.72 C ANISOU 2030 CZ2 TRP A 305 16898 35771 17136 -2753 -1197 -6383 C ATOM 2031 CZ3 TRP A 305 39.436 -10.847 -32.323 1.00183.64 C ANISOU 2031 CZ3 TRP A 305 16662 35794 17321 -2061 -1597 -6570 C ATOM 2032 CH2 TRP A 305 40.195 -9.838 -31.711 1.00184.08 C ANISOU 2032 CH2 TRP A 305 16803 35763 17376 -2369 -1441 -6516 C ATOM 2033 N ILE A 306 31.798 -11.224 -32.284 1.00169.71 N ANISOU 2033 N ILE A 306 16169 32969 15344 -2278 -1121 -5059 N ATOM 2034 CA ILE A 306 30.894 -12.258 -32.778 1.00167.08 C ANISOU 2034 CA ILE A 306 16036 32251 15195 -1930 -1308 -4854 C ATOM 2035 C ILE A 306 30.155 -11.770 -34.036 1.00166.07 C ANISOU 2035 C ILE A 306 15996 31999 15106 -2166 -980 -4679 C ATOM 2036 O ILE A 306 30.568 -12.138 -35.135 1.00166.45 O ANISOU 2036 O ILE A 306 15766 32330 15150 -2072 -991 -4917 O ATOM 2037 CB ILE A 306 29.887 -12.716 -31.696 1.00168.31 C ANISOU 2037 CB ILE A 306 16645 31844 15463 -1768 -1488 -4467 C ATOM 2038 N LEU A 307 29.091 -10.944 -33.892 1.00158.20 N ANISOU 2038 N LEU A 307 15374 30601 14132 -2454 -702 -4292 N ATOM 2039 CA LEU A 307 28.294 -10.556 -35.048 1.00155.52 C ANISOU 2039 CA LEU A 307 15169 30088 13835 -2620 -441 -4112 C ATOM 2040 C LEU A 307 28.616 -9.128 -35.545 1.00157.54 C ANISOU 2040 C LEU A 307 15403 30549 13907 -3136 -50 -4167 C ATOM 2041 O LEU A 307 28.612 -8.937 -36.759 1.00158.11 O ANISOU 2041 O LEU A 307 15393 30738 13944 -3265 113 -4232 O ATOM 2042 CB LEU A 307 26.760 -10.656 -34.782 1.00152.48 C ANISOU 2042 CB LEU A 307 15230 29112 13593 -2555 -411 -3661 C ATOM 2043 CG LEU A 307 26.033 -9.685 -33.821 1.00155.89 C ANISOU 2043 CG LEU A 307 16004 29245 13981 -2809 -224 -3373 C ATOM 2044 CD1 LEU A 307 24.524 -9.751 -34.020 1.00153.11 C ANISOU 2044 CD1 LEU A 307 15997 28427 13749 -2759 -146 -3009 C ATOM 2045 CD2 LEU A 307 26.394 -9.927 -32.373 1.00159.48 C ANISOU 2045 CD2 LEU A 307 16488 29699 14408 -2715 -429 -3388 C ATOM 2046 N ARG A 308 28.874 -8.141 -34.655 1.00151.50 N ANISOU 2046 N ARG A 308 14744 29810 13008 -3442 90 -4137 N ATOM 2047 CA ARG A 308 29.100 -6.745 -35.077 1.00150.81 C ANISOU 2047 CA ARG A 308 14736 29842 12721 -3965 441 -4155 C ATOM 2048 C ARG A 308 30.269 -6.593 -36.081 1.00155.78 C ANISOU 2048 C ARG A 308 14961 31052 13177 -4188 541 -4545 C ATOM 2049 O ARG A 308 30.281 -5.605 -36.818 1.00155.64 O ANISOU 2049 O ARG A 308 15058 31082 12995 -4619 828 -4528 O ATOM 2050 CB ARG A 308 29.371 -5.813 -33.883 1.00151.33 C ANISOU 2050 CB ARG A 308 14946 29896 12656 -4235 524 -4117 C ATOM 2051 CG ARG A 308 28.126 -5.281 -33.151 1.00155.16 C ANISOU 2051 CG ARG A 308 15915 29830 13211 -4255 602 -3717 C ATOM 2052 CD ARG A 308 27.339 -6.301 -32.342 1.00154.47 C ANISOU 2052 CD ARG A 308 15946 29420 13325 -3830 346 -3513 C ATOM 2053 NE ARG A 308 26.166 -5.694 -31.708 1.00151.21 N ANISOU 2053 NE ARG A 308 15950 28563 12940 -3896 458 -3175 N ATOM 2054 CZ ARG A 308 26.167 -5.139 -30.499 1.00158.34 C ANISOU 2054 CZ ARG A 308 17004 29386 13771 -4005 470 -3104 C ATOM 2055 NH1 ARG A 308 27.282 -5.108 -29.775 1.00144.94 N ANISOU 2055 NH1 ARG A 308 15088 28006 11976 -4071 376 -3332 N ATOM 2056 NH2 ARG A 308 25.057 -4.609 -30.005 1.00137.12 N ANISOU 2056 NH2 ARG A 308 14672 26327 11102 -4040 570 -2826 N ATOM 2057 N PHE A 309 31.213 -7.562 -36.135 1.00153.36 N ANISOU 2057 N PHE A 309 14203 31181 12887 -3898 297 -4901 N ATOM 2058 CA PHE A 309 32.367 -7.515 -37.043 1.00155.70 C ANISOU 2058 CA PHE A 309 14040 32117 13003 -4079 374 -5330 C ATOM 2059 C PHE A 309 31.915 -7.705 -38.530 1.00156.16 C ANISOU 2059 C PHE A 309 14105 32136 13094 -4093 497 -5292 C ATOM 2060 O PHE A 309 32.038 -6.740 -39.290 1.00155.91 O ANISOU 2060 O PHE A 309 14138 32232 12870 -4579 804 -5304 O ATOM 2061 CB PHE A 309 33.430 -8.575 -36.653 1.00160.43 C ANISOU 2061 CB PHE A 309 14151 33187 13618 -3673 30 -5750 C ATOM 2062 CG PHE A 309 34.666 -8.666 -37.530 1.00165.86 C ANISOU 2062 CG PHE A 309 14280 34625 14115 -3789 68 -6265 C ATOM 2063 CD1 PHE A 309 34.708 -9.538 -38.615 1.00169.28 C ANISOU 2063 CD1 PHE A 309 14474 35227 14619 -3497 -43 -6441 C ATOM 2064 CD2 PHE A 309 35.812 -7.938 -37.226 1.00170.17 C ANISOU 2064 CD2 PHE A 309 14659 35469 14527 -4096 175 -6481 C ATOM 2065 CE1 PHE A 309 35.855 -9.640 -39.408 1.00171.11 C ANISOU 2065 CE1 PHE A 309 14503 35569 14943 -3447 -51 -6661 C ATOM 2066 CE2 PHE A 309 36.963 -8.048 -38.015 1.00172.11 C ANISOU 2066 CE2 PHE A 309 14898 35455 15040 -3939 134 -6527 C ATOM 2067 CZ PHE A 309 36.977 -8.898 -39.100 1.00170.72 C ANISOU 2067 CZ PHE A 309 14479 35470 14916 -3678 41 -6702 C ATOM 2068 N PRO A 310 31.395 -8.879 -38.987 1.00150.31 N ANISOU 2068 N PRO A 310 13333 31209 12569 -3609 269 -5241 N ATOM 2069 CA PRO A 310 31.104 -9.018 -40.421 1.00149.56 C ANISOU 2069 CA PRO A 310 13200 31148 12479 -3648 393 -5251 C ATOM 2070 C PRO A 310 29.820 -8.293 -40.882 1.00149.33 C ANISOU 2070 C PRO A 310 13680 30562 12498 -3871 637 -4813 C ATOM 2071 O PRO A 310 29.700 -8.078 -42.089 1.00149.87 O ANISOU 2071 O PRO A 310 13745 30699 12500 -4046 807 -4834 O ATOM 2072 CB PRO A 310 30.941 -10.530 -40.607 1.00150.97 C ANISOU 2072 CB PRO A 310 13220 31266 12876 -3032 31 -5329 C ATOM 2073 CG PRO A 310 31.514 -11.144 -39.376 1.00156.68 C ANISOU 2073 CG PRO A 310 13799 32092 13639 -2715 -289 -5484 C ATOM 2074 CD PRO A 310 31.211 -10.172 -38.300 1.00151.00 C ANISOU 2074 CD PRO A 310 13389 31116 12866 -3023 -133 -5229 C ATOM 2075 N VAL A 311 28.883 -7.900 -39.977 1.00141.51 N ANISOU 2075 N VAL A 311 13112 29052 11601 -3866 652 -4445 N ATOM 2076 CA VAL A 311 27.673 -7.177 -40.429 1.00137.92 C ANISOU 2076 CA VAL A 311 13122 28107 11174 -4043 864 -4078 C ATOM 2077 C VAL A 311 28.058 -5.728 -40.805 1.00141.63 C ANISOU 2077 C VAL A 311 13741 28708 11364 -4639 1184 -4115 C ATOM 2078 O VAL A 311 27.433 -5.150 -41.693 1.00140.28 O ANISOU 2078 O VAL A 311 13851 28310 11140 -4836 1366 -3953 O ATOM 2079 CB VAL A 311 26.467 -7.177 -39.441 1.00138.98 C ANISOU 2079 CB VAL A 311 13653 27681 11474 -3853 793 -3698 C ATOM 2080 CG1 VAL A 311 25.901 -8.576 -39.244 1.00137.22 C ANISOU 2080 CG1 VAL A 311 13381 27260 11496 -3338 497 -3608 C ATOM 2081 CG2 VAL A 311 26.805 -6.517 -38.105 1.00139.62 C ANISOU 2081 CG2 VAL A 311 13822 27768 11460 -4022 807 -3684 C ATOM 2082 N PHE A 312 29.081 -5.159 -40.133 1.00139.47 N ANISOU 2082 N PHE A 312 13305 28789 10900 -4928 1235 -4329 N ATOM 2083 CA PHE A 312 29.575 -3.810 -40.395 1.00140.76 C ANISOU 2083 CA PHE A 312 13617 29108 10759 -5542 1515 -4390 C ATOM 2084 C PHE A 312 30.428 -3.799 -41.660 1.00145.46 C ANISOU 2084 C PHE A 312 13896 30215 11155 -5823 1645 -4700 C ATOM 2085 O PHE A 312 30.367 -2.845 -42.440 1.00145.47 O ANISOU 2085 O PHE A 312 14158 30177 10937 -6293 1885 -4644 O ATOM 2086 CB PHE A 312 30.376 -3.285 -39.198 1.00144.55 C ANISOU 2086 CB PHE A 312 14010 29810 11102 -5751 1510 -4523 C ATOM 2087 N LEU A 313 31.214 -4.876 -41.861 1.00142.65 N ANISOU 2087 N LEU A 313 12997 30340 10862 -5526 1468 -5037 N ATOM 2088 CA LEU A 313 32.089 -5.089 -43.019 1.00145.07 C ANISOU 2088 CA LEU A 313 12891 31232 10995 -5704 1551 -5401 C ATOM 2089 C LEU A 313 31.268 -5.200 -44.316 1.00147.60 C ANISOU 2089 C LEU A 313 13428 31281 11373 -5681 1646 -5220 C ATOM 2090 O LEU A 313 31.723 -4.755 -45.370 1.00149.30 O ANISOU 2090 O LEU A 313 13559 31817 11350 -6086 1849 -5383 O ATOM 2091 CB LEU A 313 32.917 -6.379 -42.789 1.00146.52 C ANISOU 2091 CB LEU A 313 12480 31898 11291 -5219 1256 -5786 C ATOM 2092 CG LEU A 313 33.896 -6.839 -43.884 1.00154.02 C ANISOU 2092 CG LEU A 313 12888 33548 12085 -5269 1276 -6247 C ATOM 2093 CD1 LEU A 313 34.965 -5.790 -44.166 1.00157.90 C ANISOU 2093 CD1 LEU A 313 13180 34636 12179 -5968 1562 -6542 C ATOM 2094 CD2 LEU A 313 34.553 -8.141 -43.495 1.00157.32 C ANISOU 2094 CD2 LEU A 313 12802 34327 12645 -4674 914 -6599 C ATOM 2095 N ALA A 314 30.060 -5.785 -44.221 1.00140.58 N ANISOU 2095 N ALA A 314 12818 29814 10781 -5231 1501 -4887 N ATOM 2096 CA ALA A 314 29.157 -5.991 -45.341 1.00138.66 C ANISOU 2096 CA ALA A 314 12790 29260 10634 -5128 1553 -4692 C ATOM 2097 C ALA A 314 28.381 -4.704 -45.693 1.00142.41 C ANISOU 2097 C ALA A 314 13843 29301 10967 -5552 1804 -4380 C ATOM 2098 O ALA A 314 28.334 -4.359 -46.873 1.00144.26 O ANISOU 2098 O ALA A 314 14171 29585 11056 -5814 1963 -4396 O ATOM 2099 CB ALA A 314 28.181 -7.114 -45.024 1.00136.13 C ANISOU 2099 CB ALA A 314 12540 28519 10664 -4507 1290 -4474 C ATOM 2100 N ILE A 315 27.784 -3.995 -44.690 1.00136.23 N ANISOU 2100 N ILE A 315 13458 28095 10208 -5610 1822 -4112 N ATOM 2101 CA ILE A 315 26.965 -2.781 -44.917 1.00134.77 C ANISOU 2101 CA ILE A 315 13872 27440 9894 -5928 2002 -3821 C ATOM 2102 C ILE A 315 27.856 -1.609 -45.437 1.00140.98 C ANISOU 2102 C ILE A 315 14762 28525 10279 -6624 2244 -3986 C ATOM 2103 O ILE A 315 27.357 -0.764 -46.190 1.00140.74 O ANISOU 2103 O ILE A 315 15184 28204 10085 -6923 2388 -3823 O ATOM 2104 CB ILE A 315 26.155 -2.335 -43.638 1.00135.79 C ANISOU 2104 CB ILE A 315 14367 27092 10134 -5787 1941 -3541 C ATOM 2105 CG1 ILE A 315 25.241 -1.107 -43.908 1.00135.84 C ANISOU 2105 CG1 ILE A 315 15011 26593 10008 -6035 2082 -3268 C ATOM 2106 CG2 ILE A 315 27.048 -2.062 -42.424 1.00138.08 C ANISOU 2106 CG2 ILE A 315 14483 27651 10329 -5940 1915 -3694 C ATOM 2107 CD1 ILE A 315 24.221 -1.254 -45.027 1.00144.90 C ANISOU 2107 CD1 ILE A 315 16403 27409 11245 -5867 2096 -3091 C ATOM 2108 N LEU A 316 29.148 -1.578 -45.062 1.00139.66 N ANISOU 2108 N LEU A 316 14191 28936 9936 -6883 2274 -4313 N ATOM 2109 CA LEU A 316 30.069 -0.520 -45.483 1.00142.93 C ANISOU 2109 CA LEU A 316 14666 29702 9939 -7596 2503 -4497 C ATOM 2110 C LEU A 316 30.314 -0.569 -47.015 1.00147.75 C ANISOU 2110 C LEU A 316 15192 30576 10370 -7860 2642 -4633 C ATOM 2111 O LEU A 316 29.977 0.386 -47.718 1.00148.05 O ANISOU 2111 O LEU A 316 15723 30353 10175 -8292 2806 -4476 O ATOM 2112 CB LEU A 316 31.412 -0.648 -44.719 1.00145.80 C ANISOU 2112 CB LEU A 316 14515 30709 10174 -7757 2484 -4864 C ATOM 2113 CG LEU A 316 32.512 0.393 -45.015 1.00154.45 C ANISOU 2113 CG LEU A 316 15589 32281 10813 -8545 2721 -5108 C ATOM 2114 CD1 LEU A 316 32.100 1.797 -44.556 1.00154.68 C ANISOU 2114 CD1 LEU A 316 16304 31828 10638 -8999 2845 -4828 C ATOM 2115 CD2 LEU A 316 33.810 0.006 -44.340 1.00157.76 C ANISOU 2115 CD2 LEU A 316 15446 33244 11252 -8468 2637 -5455 C ATOM 2116 N ILE A 317 30.856 -1.699 -47.514 1.00144.30 N ANISOU 2116 N ILE A 317 14162 30625 10040 -7571 2552 -4923 N ATOM 2117 CA ILE A 317 31.240 -1.912 -48.913 1.00146.01 C ANISOU 2117 CA ILE A 317 14170 31216 10090 -7780 2669 -5126 C ATOM 2118 C ILE A 317 29.973 -2.038 -49.827 1.00146.39 C ANISOU 2118 C ILE A 317 14639 30683 10298 -7550 2660 -4797 C ATOM 2119 O ILE A 317 30.089 -1.820 -51.034 1.00147.15 O ANISOU 2119 O ILE A 317 14792 30925 10191 -7862 2806 -4863 O ATOM 2120 CB ILE A 317 32.166 -3.159 -49.044 1.00150.89 C ANISOU 2120 CB ILE A 317 14007 32522 10801 -7435 2526 -5562 C ATOM 2121 CG1 ILE A 317 31.507 -4.455 -48.497 1.00147.88 C ANISOU 2121 CG1 ILE A 317 13469 31848 10871 -6605 2210 -5456 C ATOM 2122 CG2 ILE A 317 33.506 -2.889 -48.342 1.00155.45 C ANISOU 2122 CG2 ILE A 317 14165 33750 11150 -7749 2565 -5938 C ATOM 2123 CD1 ILE A 317 32.404 -5.775 -48.544 1.00155.78 C ANISOU 2123 CD1 ILE A 317 13741 33471 11976 -6162 1989 -5901 C ATOM 2124 N ASN A 318 28.783 -2.318 -49.253 1.00139.13 N ANISOU 2124 N ASN A 318 14026 29131 9707 -7055 2503 -4454 N ATOM 2125 CA ASN A 318 27.526 -2.378 -50.011 1.00136.39 C ANISOU 2125 CA ASN A 318 14084 28229 9508 -6828 2486 -4146 C ATOM 2126 C ASN A 318 27.005 -0.970 -50.366 1.00140.83 C ANISOU 2126 C ASN A 318 15342 28360 9808 -7309 2656 -3902 C ATOM 2127 O ASN A 318 26.135 -0.856 -51.233 1.00139.15 O ANISOU 2127 O ASN A 318 15475 27771 9624 -7237 2671 -3705 O ATOM 2128 CB ASN A 318 26.438 -3.140 -49.251 1.00133.73 C ANISOU 2128 CB ASN A 318 13817 27419 9575 -6175 2264 -3892 C ATOM 2129 CG ASN A 318 26.359 -4.621 -49.553 1.00150.76 C ANISOU 2129 CG ASN A 318 15532 29732 12017 -5625 2069 -4001 C ATOM 2130 OD1 ASN A 318 26.463 -5.055 -50.708 1.00136.03 O ANISOU 2130 OD1 ASN A 318 13506 28054 10127 -5610 2098 -4118 O ATOM 2131 ND2 ASN A 318 25.913 -5.390 -48.569 1.00144.72 N ANISOU 2131 ND2 ASN A 318 14680 28767 11541 -5143 1854 -3897 N ATOM 2132 N PHE A 319 27.509 0.087 -49.688 1.00138.92 N ANISOU 2132 N PHE A 319 15329 28146 9307 -7775 2758 -3916 N ATOM 2133 CA PHE A 319 27.111 1.477 -49.953 1.00139.33 C ANISOU 2133 CA PHE A 319 16095 27777 9067 -8254 2885 -3707 C ATOM 2134 C PHE A 319 27.855 2.050 -51.158 1.00144.15 C ANISOU 2134 C PHE A 319 16787 28721 9264 -8914 3084 -3874 C ATOM 2135 O PHE A 319 27.254 2.732 -51.994 1.00143.70 O ANISOU 2135 O PHE A 319 17291 28271 9036 -9135 3142 -3687 O ATOM 2136 CB PHE A 319 27.358 2.381 -48.720 1.00142.14 C ANISOU 2136 CB PHE A 319 16700 28012 9295 -8501 2897 -3656 C ATOM 2137 CG PHE A 319 27.381 3.871 -49.023 1.00146.49 C ANISOU 2137 CG PHE A 319 17938 28288 9432 -9147 3031 -3545 C ATOM 2138 CD1 PHE A 319 26.202 4.571 -49.258 1.00148.25 C ANISOU 2138 CD1 PHE A 319 18869 27810 9650 -9048 2976 -3233 C ATOM 2139 CD2 PHE A 319 28.580 4.576 -49.044 1.00152.87 C ANISOU 2139 CD2 PHE A 319 18704 29542 9837 -9854 3193 -3767 C ATOM 2140 CE1 PHE A 319 26.226 5.945 -49.536 1.00151.94 C ANISOU 2140 CE1 PHE A 319 20038 27978 9714 -9625 3055 -3135 C ATOM 2141 CE2 PHE A 319 28.602 5.948 -49.323 1.00158.49 C ANISOU 2141 CE2 PHE A 319 20117 29966 10137 -10486 3295 -3654 C ATOM 2142 CZ PHE A 319 27.425 6.623 -49.564 1.00155.13 C ANISOU 2142 CZ PHE A 319 20437 28793 9711 -10356 3212 -3333 C ATOM 2143 N PHE A 320 29.170 1.833 -51.206 1.00142.14 N ANISOU 2143 N PHE A 320 15996 29197 8816 -9253 3185 -4237 N ATOM 2144 CA PHE A 320 30.011 2.388 -52.249 1.00145.59 C ANISOU 2144 CA PHE A 320 16447 30062 8807 -9964 3398 -4442 C ATOM 2145 C PHE A 320 29.717 1.700 -53.572 1.00146.78 C ANISOU 2145 C PHE A 320 16456 30293 9020 -9792 3410 -4478 C ATOM 2146 O PHE A 320 29.925 2.312 -54.614 1.00149.06 O ANISOU 2146 O PHE A 320 17023 30658 8953 -10343 3571 -4503 O ATOM 2147 CB PHE A 320 31.492 2.268 -51.874 1.00151.06 C ANISOU 2147 CB PHE A 320 16533 31548 9315 -10292 3485 -4849 C ATOM 2148 CG PHE A 320 31.790 2.939 -50.552 1.00152.46 C ANISOU 2148 CG PHE A 320 16895 31483 9548 -10305 3433 -4747 C ATOM 2149 CD1 PHE A 320 31.924 4.321 -50.468 1.00154.99 C ANISOU 2149 CD1 PHE A 320 17943 31105 9840 -10483 3453 -4428 C ATOM 2150 CD2 PHE A 320 31.918 2.192 -49.387 1.00154.01 C ANISOU 2150 CD2 PHE A 320 16616 31923 9978 -9898 3291 -4880 C ATOM 2151 CE1 PHE A 320 32.168 4.943 -49.238 1.00155.92 C ANISOU 2151 CE1 PHE A 320 18223 31030 9988 -10506 3403 -4352 C ATOM 2152 CE2 PHE A 320 32.159 2.816 -48.157 1.00156.06 C ANISOU 2152 CE2 PHE A 320 17080 31894 10323 -9861 3231 -4758 C ATOM 2153 CZ PHE A 320 32.287 4.186 -48.091 1.00155.15 C ANISOU 2153 CZ PHE A 320 17593 31368 9990 -10310 3326 -4559 C ATOM 2154 N ILE A 321 29.152 0.478 -53.543 1.00138.62 N ANISOU 2154 N ILE A 321 15068 29179 8422 -9047 3231 -4451 N ATOM 2155 CA ILE A 321 28.779 -0.204 -54.781 1.00137.21 C ANISOU 2155 CA ILE A 321 14781 29023 8329 -8835 3224 -4465 C ATOM 2156 C ILE A 321 27.402 0.363 -55.210 1.00136.64 C ANISOU 2156 C ILE A 321 15460 28137 8318 -8724 3187 -4047 C ATOM 2157 O ILE A 321 27.229 0.682 -56.383 1.00136.66 O ANISOU 2157 O ILE A 321 15741 28070 8115 -9005 3285 -4008 O ATOM 2158 CB ILE A 321 28.814 -1.775 -54.675 1.00138.33 C ANISOU 2158 CB ILE A 321 14244 29444 8871 -8118 3032 -4640 C ATOM 2159 CG1 ILE A 321 27.814 -2.399 -53.671 1.00134.45 C ANISOU 2159 CG1 ILE A 321 13824 28429 8833 -7411 2794 -4378 C ATOM 2160 CG2 ILE A 321 30.222 -2.266 -54.386 1.00142.49 C ANISOU 2160 CG2 ILE A 321 14051 30808 9282 -8234 3050 -5103 C ATOM 2161 CD1 ILE A 321 26.367 -2.588 -54.139 1.00139.68 C ANISOU 2161 CD1 ILE A 321 14908 28422 9741 -7014 2703 -4023 C ATOM 2162 N PHE A 322 26.492 0.598 -54.228 1.00129.64 N ANISOU 2162 N PHE A 322 14920 26672 7667 -8371 3053 -3762 N ATOM 2163 CA PHE A 322 25.130 1.125 -54.389 1.00126.61 C ANISOU 2163 CA PHE A 322 15209 25526 7372 -8166 2978 -3396 C ATOM 2164 C PHE A 322 25.132 2.494 -55.082 1.00132.61 C ANISOU 2164 C PHE A 322 16670 26031 7687 -8813 3110 -3294 C ATOM 2165 O PHE A 322 24.299 2.727 -55.961 1.00131.13 O ANISOU 2165 O PHE A 322 16924 25429 7471 -8748 3082 -3112 O ATOM 2166 CB PHE A 322 24.441 1.237 -53.006 1.00125.50 C ANISOU 2166 CB PHE A 322 15225 24976 7483 -7776 2835 -3198 C ATOM 2167 CG PHE A 322 23.151 2.026 -52.960 1.00125.48 C ANISOU 2167 CG PHE A 322 15936 24240 7500 -7630 2760 -2873 C ATOM 2168 CD1 PHE A 322 23.155 3.380 -52.641 1.00130.86 C ANISOU 2168 CD1 PHE A 322 17228 24619 7872 -8057 2806 -2772 C ATOM 2169 CD2 PHE A 322 21.937 1.423 -53.251 1.00124.43 C ANISOU 2169 CD2 PHE A 322 15871 23733 7676 -7063 2628 -2690 C ATOM 2170 CE1 PHE A 322 21.965 4.115 -52.619 1.00130.75 C ANISOU 2170 CE1 PHE A 322 17880 23937 7861 -7872 2702 -2510 C ATOM 2171 CE2 PHE A 322 20.743 2.153 -53.202 1.00126.18 C ANISOU 2171 CE2 PHE A 322 16714 23326 7904 -6893 2544 -2435 C ATOM 2172 CZ PHE A 322 20.766 3.496 -52.900 1.00126.47 C ANISOU 2172 CZ PHE A 322 17352 23068 7633 -7279 2573 -2356 C ATOM 2173 N VAL A 323 26.035 3.402 -54.668 1.00132.29 N ANISOU 2173 N VAL A 323 16767 26209 7288 -9434 3233 -3405 N ATOM 2174 CA VAL A 323 26.106 4.747 -55.246 1.00135.38 C ANISOU 2174 CA VAL A 323 17892 26339 7208 -10114 3337 -3306 C ATOM 2175 C VAL A 323 26.667 4.660 -56.695 1.00143.05 C ANISOU 2175 C VAL A 323 18782 27692 7879 -10573 3493 -3469 C ATOM 2176 O VAL A 323 26.340 5.528 -57.507 1.00145.34 O ANISOU 2176 O VAL A 323 19752 27620 7851 -10968 3528 -3320 O ATOM 2177 CB VAL A 323 26.910 5.759 -54.390 1.00141.80 C ANISOU 2177 CB VAL A 323 18914 27268 7696 -10694 3420 -3374 C ATOM 2178 CG1 VAL A 323 26.157 6.104 -53.112 1.00139.04 C ANISOU 2178 CG1 VAL A 323 18858 26396 7576 -10292 3261 -3159 C ATOM 2179 CG2 VAL A 323 28.321 5.261 -54.081 1.00143.89 C ANISOU 2179 CG2 VAL A 323 18411 28392 7870 -10985 3553 -3748 C ATOM 2180 N ARG A 324 27.456 3.611 -57.037 1.00138.97 N ANISOU 2180 N ARG A 324 17469 27878 7455 -10493 3564 -3775 N ATOM 2181 CA ARG A 324 27.920 3.490 -58.416 1.00140.92 C ANISOU 2181 CA ARG A 324 17617 28500 7425 -10890 3710 -3939 C ATOM 2182 C ARG A 324 26.816 2.820 -59.233 1.00142.37 C ANISOU 2182 C ARG A 324 17901 28286 7907 -10317 3589 -3755 C ATOM 2183 O ARG A 324 26.680 3.110 -60.421 1.00143.68 O ANISOU 2183 O ARG A 324 18386 28380 7826 -10625 3666 -3718 O ATOM 2184 CB ARG A 324 29.256 2.744 -58.544 1.00142.14 C ANISOU 2184 CB ARG A 324 16901 29614 7491 -11083 3838 -4387 C ATOM 2185 CG ARG A 324 29.887 3.001 -59.913 1.00150.81 C ANISOU 2185 CG ARG A 324 18157 30469 8674 -10982 3871 -4287 C ATOM 2186 CD ARG A 324 31.175 2.260 -60.189 1.00155.39 C ANISOU 2186 CD ARG A 324 18111 31174 9757 -10311 3797 -4400 C ATOM 2187 NE ARG A 324 31.708 2.631 -61.504 1.00157.68 N ANISOU 2187 NE ARG A 324 18639 31149 10122 -10219 3827 -4252 N ATOM 2188 CZ ARG A 324 31.397 2.021 -62.648 1.00165.77 C ANISOU 2188 CZ ARG A 324 19713 31678 11593 -9493 3704 -4043 C ATOM 2189 NH1 ARG A 324 30.563 0.988 -62.654 1.00156.33 N ANISOU 2189 NH1 ARG A 324 18016 31458 9925 -10032 3829 -4481 N ATOM 2190 NH2 ARG A 324 31.923 2.437 -63.792 1.00157.45 N ANISOU 2190 NH2 ARG A 324 18702 31103 10018 -10233 3920 -4230 N ATOM 2191 N ILE A 325 25.999 1.958 -58.578 1.00134.79 N ANISOU 2191 N ILE A 325 16706 27051 7459 -9511 3396 -3630 N ATOM 2192 CA ILE A 325 24.845 1.286 -59.187 1.00131.22 C ANISOU 2192 CA ILE A 325 16340 26188 7329 -8915 3259 -3440 C ATOM 2193 C ILE A 325 23.897 2.338 -59.759 1.00134.45 C ANISOU 2193 C ILE A 325 17636 25906 7544 -9088 3233 -3139 C ATOM 2194 O ILE A 325 23.525 2.247 -60.927 1.00133.80 O ANISOU 2194 O ILE A 325 17741 25712 7385 -9112 3247 -3092 O ATOM 2195 CB ILE A 325 24.112 0.355 -58.164 1.00130.17 C ANISOU 2195 CB ILE A 325 15896 25839 7724 -8114 3055 -3334 C ATOM 2196 CG1 ILE A 325 24.974 -0.863 -57.746 1.00130.63 C ANISOU 2196 CG1 ILE A 325 15100 26539 7994 -7844 3021 -3638 C ATOM 2197 CG2 ILE A 325 22.742 -0.103 -58.685 1.00127.97 C ANISOU 2197 CG2 ILE A 325 15851 25032 7740 -7555 2911 -3088 C ATOM 2198 CD1 ILE A 325 25.388 -1.835 -58.869 1.00140.58 C ANISOU 2198 CD1 ILE A 325 15871 28264 9280 -7748 3048 -3875 C ATOM 2199 N VAL A 326 23.530 3.343 -58.944 1.00131.11 N ANISOU 2199 N VAL A 326 17769 25024 7024 -9199 3178 -2953 N ATOM 2200 CA VAL A 326 22.628 4.410 -59.377 1.00131.48 C ANISOU 2200 CA VAL A 326 18712 24377 6868 -9319 3103 -2688 C ATOM 2201 C VAL A 326 23.382 5.320 -60.389 1.00140.61 C ANISOU 2201 C VAL A 326 20302 25674 7451 -10175 3266 -2762 C ATOM 2202 O VAL A 326 22.776 5.720 -61.387 1.00140.69 O ANISOU 2202 O VAL A 326 20862 25296 7296 -10254 3223 -2619 O ATOM 2203 CB VAL A 326 22.003 5.236 -58.204 1.00134.05 C ANISOU 2203 CB VAL A 326 19526 24166 7239 -9158 2970 -2494 C ATOM 2204 CG1 VAL A 326 20.986 4.411 -57.421 1.00128.99 C ANISOU 2204 CG1 VAL A 326 18595 23292 7122 -8322 2799 -2378 C ATOM 2205 CG2 VAL A 326 23.059 5.825 -57.274 1.00136.33 C ANISOU 2205 CG2 VAL A 326 19742 24759 7296 -9656 3074 -2624 C ATOM 2206 N GLN A 327 24.708 5.569 -60.170 1.00141.47 N ANISOU 2206 N GLN A 327 20126 26374 7252 -10812 3450 -3002 N ATOM 2207 CA GLN A 327 25.555 6.392 -61.054 1.00146.96 C ANISOU 2207 CA GLN A 327 21165 27314 7359 -11721 3632 -3107 C ATOM 2208 C GLN A 327 25.567 5.811 -62.482 1.00151.52 C ANISOU 2208 C GLN A 327 21571 28131 7868 -11775 3710 -3192 C ATOM 2209 O GLN A 327 25.507 6.575 -63.445 1.00151.69 O ANISOU 2209 O GLN A 327 22195 27759 7682 -11980 3694 -3027 O ATOM 2210 CB GLN A 327 26.998 6.499 -60.502 1.00149.96 C ANISOU 2210 CB GLN A 327 21043 28256 7679 -12016 3764 -3333 C ATOM 2211 CG GLN A 327 27.952 7.442 -61.279 1.00161.97 C ANISOU 2211 CG GLN A 327 22785 28889 9866 -11028 3561 -2926 C ATOM 2212 CD GLN A 327 27.666 8.936 -61.164 1.00173.54 C ANISOU 2212 CD GLN A 327 24971 29143 11824 -10140 3245 -2403 C ATOM 2213 OE1 GLN A 327 28.008 9.724 -62.056 1.00169.68 O ANISOU 2213 OE1 GLN A 327 24870 28572 11030 -10543 3289 -2351 O ATOM 2214 NE2 GLN A 327 27.066 9.371 -60.060 1.00167.66 N ANISOU 2214 NE2 GLN A 327 24616 28425 10663 -10726 3266 -2459 N ATOM 2215 N LEU A 328 25.621 4.471 -62.616 1.00146.07 N ANISOU 2215 N LEU A 328 20070 27862 7569 -11235 3704 -3357 N ATOM 2216 CA LEU A 328 25.604 3.855 -63.933 1.00146.80 C ANISOU 2216 CA LEU A 328 19967 28186 7627 -11226 3764 -3449 C ATOM 2217 C LEU A 328 24.156 3.698 -64.406 1.00148.48 C ANISOU 2217 C LEU A 328 20626 27672 8119 -10626 3569 -3145 C ATOM 2218 O LEU A 328 23.924 3.710 -65.609 1.00149.20 O ANISOU 2218 O LEU A 328 20957 27690 8044 -10773 3599 -3113 O ATOM 2219 CB LEU A 328 26.355 2.501 -63.964 1.00146.10 C ANISOU 2219 CB LEU A 328 18839 28885 7788 -10931 3825 -3794 C ATOM 2220 CG LEU A 328 25.867 1.308 -63.125 1.00145.97 C ANISOU 2220 CG LEU A 328 18251 28834 8379 -10025 3639 -3790 C ATOM 2221 CD1 LEU A 328 24.700 0.577 -63.804 1.00142.28 C ANISOU 2221 CD1 LEU A 328 17859 27945 8258 -9383 3488 -3602 C ATOM 2222 CD2 LEU A 328 26.970 0.288 -62.994 1.00150.32 C ANISOU 2222 CD2 LEU A 328 17868 30236 9013 -9947 3702 -4195 C ATOM 2223 N LEU A 329 23.187 3.580 -63.468 1.00141.95 N ANISOU 2223 N LEU A 329 19914 26332 7689 -9977 3373 -2935 N ATOM 2224 CA LEU A 329 21.763 3.411 -63.788 1.00138.81 C ANISOU 2224 CA LEU A 329 19884 25283 7575 -9364 3177 -2673 C ATOM 2225 C LEU A 329 21.207 4.647 -64.519 1.00147.04 C ANISOU 2225 C LEU A 329 21917 25723 8227 -9730 3124 -2461 C ATOM 2226 O LEU A 329 20.473 4.490 -65.499 1.00146.32 O ANISOU 2226 O LEU A 329 22082 25347 8166 -9522 3049 -2356 O ATOM 2227 CB LEU A 329 20.945 3.148 -62.505 1.00134.72 C ANISOU 2227 CB LEU A 329 19279 24418 7492 -8696 2999 -2528 C ATOM 2228 CG LEU A 329 19.451 2.805 -62.658 1.00135.69 C ANISOU 2228 CG LEU A 329 19624 23970 7963 -7987 2795 -2302 C ATOM 2229 CD1 LEU A 329 19.255 1.433 -63.305 1.00133.49 C ANISOU 2229 CD1 LEU A 329 18737 23970 8013 -7541 2780 -2387 C ATOM 2230 CD2 LEU A 329 18.760 2.803 -61.306 1.00135.71 C ANISOU 2230 CD2 LEU A 329 19617 23670 8275 -7498 2651 -2179 C ATOM 2231 N VAL A 330 21.577 5.864 -64.058 1.00147.42 N ANISOU 2231 N VAL A 330 22541 25576 7895 -10277 3147 -2408 N ATOM 2232 CA VAL A 330 21.119 7.131 -64.649 1.00150.23 C ANISOU 2232 CA VAL A 330 23934 25317 7830 -10660 3057 -2213 C ATOM 2233 C VAL A 330 21.822 7.379 -66.014 1.00158.37 C ANISOU 2233 C VAL A 330 25162 26631 8380 -11389 3224 -2311 C ATOM 2234 O VAL A 330 21.309 8.160 -66.817 1.00159.74 O ANISOU 2234 O VAL A 330 26090 26218 8386 -11387 3085 -2106 O ATOM 2235 CB VAL A 330 21.316 8.347 -63.706 1.00156.02 C ANISOU 2235 CB VAL A 330 25259 25734 8286 -11027 3006 -2132 C ATOM 2236 CG1 VAL A 330 20.407 8.246 -62.486 1.00152.16 C ANISOU 2236 CG1 VAL A 330 24733 24852 8227 -10290 2812 -2005 C ATOM 2237 CG2 VAL A 330 22.777 8.523 -63.293 1.00158.06 C ANISOU 2237 CG2 VAL A 330 25111 26597 8349 -11604 3215 -2330 C ATOM 2238 N ALA A 331 22.978 6.721 -66.273 1.00155.52 N ANISOU 2238 N ALA A 331 24053 27084 7953 -11734 3458 -2589 N ATOM 2239 CA ALA A 331 23.689 6.840 -67.555 1.00155.45 C ANISOU 2239 CA ALA A 331 23973 27149 7944 -11726 3510 -2575 C ATOM 2240 C ALA A 331 22.911 6.124 -68.653 1.00158.16 C ANISOU 2240 C ALA A 331 24299 27411 8383 -11439 3467 -2546 C ATOM 2241 O ALA A 331 22.929 6.547 -69.812 1.00158.56 O ANISOU 2241 O ALA A 331 24708 27184 8354 -11419 3425 -2416 O ATOM 2242 CB ALA A 331 25.096 6.274 -67.437 1.00155.29 C ANISOU 2242 CB ALA A 331 23063 27801 8141 -11648 3666 -2808 C ATOM 2243 N LYS A 332 22.186 5.060 -68.256 1.00152.53 N ANISOU 2243 N LYS A 332 23156 26883 7917 -11093 3443 -2637 N ATOM 2244 CA LYS A 332 21.323 4.248 -69.103 1.00149.53 C ANISOU 2244 CA LYS A 332 22652 26330 7832 -10522 3341 -2568 C ATOM 2245 C LYS A 332 19.952 4.925 -69.326 1.00154.96 C ANISOU 2245 C LYS A 332 24211 26119 8547 -10181 3095 -2251 C ATOM 2246 O LYS A 332 19.108 4.343 -70.006 1.00153.51 O ANISOU 2246 O LYS A 332 24002 25720 8604 -9686 2986 -2172 O ATOM 2247 CB LYS A 332 21.125 2.850 -68.483 1.00145.78 C ANISOU 2247 CB LYS A 332 21277 26150 7963 -9743 3288 -2671 C ATOM 2248 CG LYS A 332 22.228 1.813 -68.738 1.00139.47 C ANISOU 2248 CG LYS A 332 19560 26222 7211 -9848 3464 -3013 C ATOM 2249 CD LYS A 332 23.624 2.152 -68.257 1.00145.94 C ANISOU 2249 CD LYS A 332 20063 27677 7708 -10500 3665 -3275 C ATOM 2250 CE LYS A 332 24.591 1.015 -68.469 1.00151.01 C ANISOU 2250 CE LYS A 332 19745 29178 8453 -10440 3785 -3648 C ATOM 2251 NZ LYS A 332 24.754 0.673 -69.906 1.00162.20 N ANISOU 2251 NZ LYS A 332 21122 30534 9971 -10207 3789 -3624 N ATOM 2252 N LEU A 333 19.730 6.143 -68.769 1.00153.49 N ANISOU 2252 N LEU A 333 24793 25421 8105 -10427 2992 -2091 N ATOM 2253 CA LEU A 333 18.476 6.889 -68.956 1.00153.18 C ANISOU 2253 CA LEU A 333 25628 24536 8038 -10105 2726 -1831 C ATOM 2254 C LEU A 333 18.483 7.530 -70.359 1.00161.48 C ANISOU 2254 C LEU A 333 27398 25360 8599 -10629 2724 -1767 C ATOM 2255 O LEU A 333 17.639 7.179 -71.191 1.00158.79 O ANISOU 2255 O LEU A 333 27195 24744 8395 -10223 2601 -1681 O ATOM 2256 CB LEU A 333 18.287 7.949 -67.835 1.00154.15 C ANISOU 2256 CB LEU A 333 26312 24209 8047 -10160 2594 -1715 C ATOM 2257 CG LEU A 333 16.936 8.715 -67.710 1.00158.37 C ANISOU 2257 CG LEU A 333 27685 23877 8612 -9679 2270 -1490 C ATOM 2258 CD1 LEU A 333 16.856 9.466 -66.384 1.00158.53 C ANISOU 2258 CD1 LEU A 333 27980 23623 8631 -9621 2166 -1439 C ATOM 2259 CD2 LEU A 333 16.699 9.691 -68.864 1.00165.13 C ANISOU 2259 CD2 LEU A 333 29547 24237 8958 -10101 2150 -1372 C ATOM 2260 N ARG A 334 19.441 8.457 -70.620 1.00161.66 N ANISOU 2260 N ARG A 334 27665 25399 8360 -11054 2776 -1738 N ATOM 2261 CA ARG A 334 19.576 9.130 -71.917 1.00162.33 C ANISOU 2261 CA ARG A 334 28116 25170 8391 -10939 2673 -1583 C ATOM 2262 C ARG A 334 19.980 8.105 -72.996 1.00165.46 C ANISOU 2262 C ARG A 334 27794 26034 9040 -10690 2808 -1687 C ATOM 2263 O ARG A 334 19.410 8.118 -74.094 1.00165.74 O ANISOU 2263 O ARG A 334 28179 25811 8984 -10605 2719 -1600 O ATOM 2264 CB ARG A 334 20.593 10.291 -71.836 1.00161.76 C ANISOU 2264 CB ARG A 334 28150 25006 8307 -11008 2648 -1487 C ATOM 2265 CG ARG A 334 20.904 11.001 -73.172 1.00167.26 C ANISOU 2265 CG ARG A 334 28871 25412 9270 -10450 2500 -1287 C ATOM 2266 CD ARG A 334 19.706 11.658 -73.853 1.00171.80 C ANISOU 2266 CD ARG A 334 30030 25280 9965 -9860 2169 -1059 C ATOM 2267 NE ARG A 334 20.073 12.236 -75.151 1.00173.52 N ANISOU 2267 NE ARG A 334 30290 25398 10240 -9666 2106 -942 N ATOM 2268 CZ ARG A 334 20.003 11.588 -76.313 1.00181.36 C ANISOU 2268 CZ ARG A 334 30727 26494 11688 -8955 2083 -900 C ATOM 2269 NH1 ARG A 334 19.563 10.336 -76.358 1.00172.11 N ANISOU 2269 NH1 ARG A 334 29761 25675 9959 -9843 2313 -1128 N ATOM 2270 NH2 ARG A 334 20.361 12.191 -77.437 1.00172.41 N ANISOU 2270 NH2 ARG A 334 30202 25354 9952 -9741 2153 -888 N ATOM 2271 N ALA A 335 20.915 7.185 -72.655 1.00162.70 N ANISOU 2271 N ALA A 335 26630 26484 8706 -11004 3079 -1962 N ATOM 2272 CA ALA A 335 21.370 6.111 -73.550 1.00162.28 C ANISOU 2272 CA ALA A 335 25917 27018 8723 -11019 3252 -2158 C ATOM 2273 C ALA A 335 20.249 5.088 -73.803 1.00164.16 C ANISOU 2273 C ALA A 335 26050 27278 9045 -10811 3214 -2212 C ATOM 2274 O ALA A 335 20.331 4.319 -74.754 1.00163.39 O ANISOU 2274 O ALA A 335 25614 27532 8934 -10840 3310 -2340 O ATOM 2275 CB ALA A 335 22.587 5.415 -72.957 1.00162.13 C ANISOU 2275 CB ALA A 335 24959 27717 8928 -10998 3442 -2406 C ATOM 2276 N ARG A 336 19.209 5.095 -72.940 1.00159.85 N ANISOU 2276 N ARG A 336 25798 26368 8570 -10618 3076 -2125 N ATOM 2277 CA ARG A 336 18.023 4.244 -72.989 1.00155.19 C ANISOU 2277 CA ARG A 336 24974 25478 8514 -9704 2887 -2022 C ATOM 2278 C ARG A 336 18.417 2.761 -73.176 1.00157.18 C ANISOU 2278 C ARG A 336 24187 26395 9140 -9369 3012 -2240 C ATOM 2279 O ARG A 336 17.863 2.057 -74.024 1.00155.22 O ANISOU 2279 O ARG A 336 23791 26110 9077 -9003 2956 -2227 O ATOM 2280 CB ARG A 336 17.084 4.703 -74.096 1.00155.85 C ANISOU 2280 CB ARG A 336 25823 24967 8424 -9621 2716 -1837 C ATOM 2281 N GLN A 337 19.380 2.307 -72.361 1.00153.83 N ANISOU 2281 N GLN A 337 23070 26566 8814 -9484 3159 -2449 N ATOM 2282 CA GLN A 337 19.862 0.927 -72.305 1.00151.43 C ANISOU 2282 CA GLN A 337 21777 26901 8858 -9141 3239 -2689 C ATOM 2283 C GLN A 337 18.941 0.133 -71.356 1.00149.90 C ANISOU 2283 C GLN A 337 21252 26438 9266 -8264 3042 -2579 C ATOM 2284 O GLN A 337 18.162 -0.710 -71.818 1.00146.84 O ANISOU 2284 O GLN A 337 20670 25915 9205 -7704 2927 -2526 O ATOM 2285 CB GLN A 337 21.341 0.912 -71.851 1.00155.50 C ANISOU 2285 CB GLN A 337 21765 28170 9146 -9691 3460 -2987 C ATOM 2286 CG GLN A 337 22.000 -0.467 -71.719 1.00161.68 C ANISOU 2286 CG GLN A 337 21523 29668 10240 -9352 3518 -3292 C ATOM 2287 CD GLN A 337 22.545 -1.010 -73.008 1.00176.08 C ANISOU 2287 CD GLN A 337 23090 31486 12328 -8919 3507 -3299 C ATOM 2288 OE1 GLN A 337 23.063 -0.269 -73.854 1.00172.70 O ANISOU 2288 OE1 GLN A 337 23016 31006 11597 -9324 3602 -3260 O ATOM 2289 NE2 GLN A 337 22.632 -2.328 -73.088 1.00170.41 N ANISOU 2289 NE2 GLN A 337 21554 31669 11523 -9042 3600 -3712 N ATOM 2290 N MET A 338 18.985 0.465 -70.035 1.00144.89 N ANISOU 2290 N MET A 338 20608 25697 8747 -8179 2999 -2531 N ATOM 2291 CA MET A 338 18.150 -0.145 -68.994 1.00139.92 C ANISOU 2291 CA MET A 338 19724 24814 8625 -7444 2824 -2420 C ATOM 2292 C MET A 338 16.774 0.535 -69.006 1.00142.06 C ANISOU 2292 C MET A 338 20718 24310 8947 -7124 2627 -2135 C ATOM 2293 O MET A 338 16.491 1.412 -68.182 1.00141.59 O ANISOU 2293 O MET A 338 21097 23891 8811 -7167 2555 -2012 O ATOM 2294 CB MET A 338 18.825 -0.058 -67.610 1.00141.85 C ANISOU 2294 CB MET A 338 19656 25306 8934 -7522 2867 -2508 C ATOM 2295 N HIS A 339 15.939 0.137 -69.995 1.00136.77 N ANISOU 2295 N HIS A 339 20172 23405 8389 -6802 2533 -2053 N ATOM 2296 CA HIS A 339 14.588 0.645 -70.265 1.00134.65 C ANISOU 2296 CA HIS A 339 20536 22458 8167 -6441 2328 -1829 C ATOM 2297 C HIS A 339 13.638 0.349 -69.064 1.00134.85 C ANISOU 2297 C HIS A 339 20408 22216 8612 -5793 2163 -1723 C ATOM 2298 O HIS A 339 13.895 -0.565 -68.274 1.00131.13 O ANISOU 2298 O HIS A 339 19279 22082 8464 -5535 2193 -1807 O ATOM 2299 CB HIS A 339 14.055 0.009 -71.573 1.00133.83 C ANISOU 2299 CB HIS A 339 20396 22315 8138 -6216 2286 -1819 C ATOM 2300 CG HIS A 339 12.747 0.559 -72.061 1.00136.04 C ANISOU 2300 CG HIS A 339 21341 21943 8404 -5893 2074 -1626 C ATOM 2301 ND1 HIS A 339 11.567 -0.152 -71.922 1.00133.84 N ANISOU 2301 ND1 HIS A 339 20862 21447 8543 -5180 1906 -1548 N ATOM 2302 CD2 HIS A 339 12.475 1.744 -72.657 1.00140.29 C ANISOU 2302 CD2 HIS A 339 22737 22025 8542 -6194 1992 -1517 C ATOM 2303 CE1 HIS A 339 10.624 0.610 -72.454 1.00133.92 C ANISOU 2303 CE1 HIS A 339 21566 20913 8405 -5045 1732 -1417 C ATOM 2304 NE2 HIS A 339 11.120 1.764 -72.900 1.00138.18 N ANISOU 2304 NE2 HIS A 339 22781 21263 8456 -5620 1761 -1389 N ATOM 2305 N HIS A 340 12.552 1.153 -68.940 1.00132.32 N ANISOU 2305 N HIS A 340 20724 21297 8255 -5547 1977 -1555 N ATOM 2306 CA HIS A 340 11.525 1.113 -67.883 1.00129.97 C ANISOU 2306 CA HIS A 340 20411 20703 8269 -4976 1810 -1461 C ATOM 2307 C HIS A 340 10.968 -0.295 -67.659 1.00128.75 C ANISOU 2307 C HIS A 340 19559 20758 8603 -4396 1770 -1482 C ATOM 2308 O HIS A 340 10.375 -0.565 -66.606 1.00125.95 O ANISOU 2308 O HIS A 340 18997 20335 8525 -3999 1685 -1442 O ATOM 2309 CB HIS A 340 10.356 2.050 -68.245 1.00132.39 C ANISOU 2309 CB HIS A 340 21491 20376 8435 -4744 1592 -1329 C ATOM 2310 CG HIS A 340 10.773 3.459 -68.541 1.00140.59 C ANISOU 2310 CG HIS A 340 23347 21106 8966 -5287 1573 -1288 C ATOM 2311 ND1 HIS A 340 10.924 3.911 -69.847 1.00145.49 N ANISOU 2311 ND1 HIS A 340 24472 21572 9236 -5641 1570 -1265 N ATOM 2312 CD2 HIS A 340 11.096 4.464 -67.691 1.00144.69 C ANISOU 2312 CD2 HIS A 340 24265 21450 9260 -5555 1552 -1267 C ATOM 2313 CE1 HIS A 340 11.308 5.175 -69.748 1.00148.75 C ANISOU 2313 CE1 HIS A 340 25603 21700 9213 -6120 1536 -1222 C ATOM 2314 NE2 HIS A 340 11.431 5.552 -68.470 1.00148.73 N ANISOU 2314 NE2 HIS A 340 25563 21675 9273 -6083 1523 -1224 N ATOM 2315 N THR A 341 11.152 -1.182 -68.654 1.00123.77 N ANISOU 2315 N THR A 341 18591 20380 8056 -4367 1825 -1547 N ATOM 2316 CA THR A 341 10.661 -2.556 -68.633 1.00119.90 C ANISOU 2316 CA THR A 341 17498 20071 7989 -3862 1772 -1569 C ATOM 2317 C THR A 341 11.818 -3.576 -68.817 1.00121.39 C ANISOU 2317 C THR A 341 17029 20843 8251 -4039 1915 -1745 C ATOM 2318 O THR A 341 11.572 -4.697 -69.264 1.00119.64 O ANISOU 2318 O THR A 341 16397 20777 8285 -3721 1872 -1785 O ATOM 2319 CB THR A 341 9.594 -2.747 -69.735 1.00130.19 C ANISOU 2319 CB THR A 341 19033 21080 9352 -3543 1647 -1492 C ATOM 2320 OG1 THR A 341 10.176 -2.468 -71.014 1.00134.27 O ANISOU 2320 OG1 THR A 341 19785 21670 9560 -3947 1737 -1541 O ATOM 2321 CG2 THR A 341 8.351 -1.876 -69.514 1.00129.69 C ANISOU 2321 CG2 THR A 341 19545 20476 9255 -3247 1463 -1361 C ATOM 2322 N ASP A 342 13.058 -3.210 -68.451 1.00117.75 N ANISOU 2322 N ASP A 342 16459 20714 7565 -4521 2066 -1869 N ATOM 2323 CA ASP A 342 14.183 -4.144 -68.573 1.00116.93 C ANISOU 2323 CA ASP A 342 15709 21207 7513 -4655 2180 -2086 C ATOM 2324 C ASP A 342 14.200 -5.066 -67.361 1.00116.90 C ANISOU 2324 C ASP A 342 15164 21377 7875 -4269 2105 -2122 C ATOM 2325 O ASP A 342 13.894 -4.608 -66.263 1.00115.47 O ANISOU 2325 O ASP A 342 15128 20992 7753 -4191 2058 -2024 O ATOM 2326 CB ASP A 342 15.517 -3.380 -68.720 1.00122.07 C ANISOU 2326 CB ASP A 342 16436 22203 7744 -5350 2375 -2240 C ATOM 2327 CG ASP A 342 16.754 -4.225 -68.988 1.00128.92 C ANISOU 2327 CG ASP A 342 16642 23752 8589 -5530 2499 -2524 C ATOM 2328 OD1 ASP A 342 16.607 -5.444 -69.226 1.00125.65 O ANISOU 2328 OD1 ASP A 342 15743 23524 8476 -5108 2420 -2604 O ATOM 2329 OD2 ASP A 342 17.863 -3.658 -69.011 1.00139.05 O ANISOU 2329 OD2 ASP A 342 17907 25392 9532 -6100 2665 -2682 O ATOM 2330 N TYR A 343 14.562 -6.363 -67.553 1.00112.03 N ANISOU 2330 N TYR A 343 13952 21128 7487 -4026 2075 -2268 N ATOM 2331 CA TYR A 343 14.618 -7.337 -66.451 1.00109.69 C ANISOU 2331 CA TYR A 343 13173 20987 7519 -3660 1970 -2308 C ATOM 2332 C TYR A 343 15.736 -6.934 -65.493 1.00114.61 C ANISOU 2332 C TYR A 343 13627 21924 7997 -3986 2064 -2443 C ATOM 2333 O TYR A 343 15.636 -7.163 -64.284 1.00113.37 O ANISOU 2333 O TYR A 343 13320 21730 8025 -3784 1985 -2401 O ATOM 2334 CB TYR A 343 14.808 -8.784 -66.963 1.00110.19 C ANISOU 2334 CB TYR A 343 12708 21344 7814 -3338 1882 -2451 C ATOM 2335 CG TYR A 343 16.243 -9.242 -67.113 1.00114.53 C ANISOU 2335 CG TYR A 343 12777 22495 8242 -3558 1961 -2759 C ATOM 2336 CD1 TYR A 343 16.993 -8.893 -68.229 1.00119.59 C ANISOU 2336 CD1 TYR A 343 13424 23441 8576 -3961 2117 -2928 C ATOM 2337 CD2 TYR A 343 16.827 -10.083 -66.173 1.00114.87 C ANISOU 2337 CD2 TYR A 343 12349 22825 8471 -3343 1862 -2901 C ATOM 2338 CE1 TYR A 343 18.308 -9.334 -68.387 1.00123.55 C ANISOU 2338 CE1 TYR A 343 13429 24567 8949 -4151 2190 -3258 C ATOM 2339 CE2 TYR A 343 18.144 -10.523 -66.312 1.00118.35 C ANISOU 2339 CE2 TYR A 343 12319 23852 8794 -3493 1907 -3229 C ATOM 2340 CZ TYR A 343 18.881 -10.148 -67.424 1.00129.15 C ANISOU 2340 CZ TYR A 343 13653 25566 9853 -3893 2078 -3420 C ATOM 2341 OH TYR A 343 20.173 -10.595 -67.581 1.00131.85 O ANISOU 2341 OH TYR A 343 13481 26553 10062 -4030 2124 -3787 O ATOM 2342 N LYS A 344 16.791 -6.312 -66.050 1.00112.84 N ANISOU 2342 N LYS A 344 13437 22018 7417 -4520 2237 -2608 N ATOM 2343 CA LYS A 344 17.908 -5.763 -65.306 1.00114.36 C ANISOU 2343 CA LYS A 344 13515 22540 7397 -4930 2355 -2756 C ATOM 2344 C LYS A 344 17.430 -4.565 -64.485 1.00117.57 C ANISOU 2344 C LYS A 344 14462 22518 7692 -5088 2361 -2550 C ATOM 2345 O LYS A 344 17.796 -4.440 -63.319 1.00117.11 O ANISOU 2345 O LYS A 344 14270 22545 7681 -5104 2354 -2575 O ATOM 2346 CB LYS A 344 19.045 -5.370 -66.262 1.00120.57 C ANISOU 2346 CB LYS A 344 14237 23784 7790 -5509 2548 -2987 C ATOM 2347 N PHE A 345 16.556 -3.722 -65.073 1.00113.65 N ANISOU 2347 N PHE A 345 14586 21538 7058 -5151 2346 -2352 N ATOM 2348 CA PHE A 345 16.023 -2.544 -64.397 1.00113.67 C ANISOU 2348 CA PHE A 345 15165 21091 6933 -5256 2316 -2172 C ATOM 2349 C PHE A 345 14.994 -2.931 -63.327 1.00114.40 C ANISOU 2349 C PHE A 345 15190 20887 7390 -4696 2153 -2023 C ATOM 2350 O PHE A 345 14.868 -2.193 -62.349 1.00114.99 O ANISOU 2350 O PHE A 345 15511 20768 7411 -4753 2135 -1947 O ATOM 2351 CB PHE A 345 15.394 -1.577 -65.400 1.00117.05 C ANISOU 2351 CB PHE A 345 16296 21088 7091 -5443 2304 -2034 C ATOM 2352 CG PHE A 345 14.811 -0.318 -64.796 1.00119.16 C ANISOU 2352 CG PHE A 345 17226 20853 7195 -5516 2230 -1869 C ATOM 2353 CD1 PHE A 345 15.636 0.726 -64.390 1.00124.71 C ANISOU 2353 CD1 PHE A 345 18237 21600 7546 -6072 2330 -1907 C ATOM 2354 CD2 PHE A 345 13.434 -0.138 -64.719 1.00119.14 C ANISOU 2354 CD2 PHE A 345 17569 20342 7357 -5044 2052 -1695 C ATOM 2355 CE1 PHE A 345 15.095 1.908 -63.876 1.00126.36 C ANISOU 2355 CE1 PHE A 345 19110 21315 7585 -6126 2234 -1764 C ATOM 2356 CE2 PHE A 345 12.893 1.047 -64.209 1.00122.81 C ANISOU 2356 CE2 PHE A 345 18663 20348 7650 -5074 1957 -1578 C ATOM 2357 CZ PHE A 345 13.727 2.060 -63.789 1.00123.63 C ANISOU 2357 CZ PHE A 345 19094 20465 7415 -5606 2040 -1608 C ATOM 2358 N ARG A 346 14.260 -4.064 -63.494 1.00107.46 N ANISOU 2358 N ARG A 346 13992 19981 6857 -4183 2036 -1985 N ATOM 2359 CA ARG A 346 13.293 -4.510 -62.473 1.00104.22 C ANISOU 2359 CA ARG A 346 13483 19347 6768 -3699 1892 -1858 C ATOM 2360 C ARG A 346 14.008 -4.914 -61.180 1.00106.42 C ANISOU 2360 C ARG A 346 13361 19910 7162 -3698 1896 -1941 C ATOM 2361 O ARG A 346 13.609 -4.494 -60.083 1.00104.16 O ANISOU 2361 O ARG A 346 13213 19437 6928 -3606 1852 -1847 O ATOM 2362 CB ARG A 346 12.426 -5.684 -62.954 1.00102.84 C ANISOU 2362 CB ARG A 346 13051 19117 6906 -3219 1769 -1810 C ATOM 2363 CG ARG A 346 11.523 -5.420 -64.136 1.00117.41 C ANISOU 2363 CG ARG A 346 15258 20656 8697 -3113 1729 -1717 C ATOM 2364 CD ARG A 346 10.499 -6.536 -64.260 1.00128.70 C ANISOU 2364 CD ARG A 346 16437 21998 10464 -2605 1588 -1648 C ATOM 2365 NE ARG A 346 11.098 -7.869 -64.378 1.00135.63 N ANISOU 2365 NE ARG A 346 16761 23237 11535 -2485 1565 -1768 N ATOM 2366 CZ ARG A 346 11.340 -8.483 -65.530 1.00144.38 C ANISOU 2366 CZ ARG A 346 17712 24500 12646 -2475 1573 -1855 C ATOM 2367 NH1 ARG A 346 11.029 -7.898 -66.680 1.00131.85 N ANISOU 2367 NH1 ARG A 346 16477 22741 10878 -2599 1616 -1821 N ATOM 2368 NH2 ARG A 346 11.881 -9.693 -65.543 1.00125.92 N ANISOU 2368 NH2 ARG A 346 14886 22477 10481 -2323 1517 -1983 N ATOM 2369 N LEU A 347 15.069 -5.747 -61.327 1.00103.00 N ANISOU 2369 N LEU A 347 12428 19947 6761 -3780 1935 -2139 N ATOM 2370 CA LEU A 347 15.911 -6.239 -60.238 1.00102.09 C ANISOU 2370 CA LEU A 347 11891 20162 6735 -3774 1918 -2267 C ATOM 2371 C LEU A 347 16.576 -5.066 -59.526 1.00106.52 C ANISOU 2371 C LEU A 347 12683 20759 7030 -4204 2035 -2293 C ATOM 2372 O LEU A 347 16.687 -5.075 -58.301 1.00104.39 O ANISOU 2372 O LEU A 347 12306 20504 6853 -4126 1991 -2277 O ATOM 2373 CB LEU A 347 16.965 -7.216 -60.802 1.00103.02 C ANISOU 2373 CB LEU A 347 11482 20793 6868 -3796 1926 -2524 C ATOM 2374 CG LEU A 347 17.927 -7.877 -59.807 1.00107.82 C ANISOU 2374 CG LEU A 347 11609 21793 7565 -3734 1867 -2712 C ATOM 2375 CD1 LEU A 347 17.184 -8.717 -58.772 1.00105.14 C ANISOU 2375 CD1 LEU A 347 11150 21239 7557 -3260 1670 -2576 C ATOM 2376 CD2 LEU A 347 18.925 -8.741 -60.532 1.00111.72 C ANISOU 2376 CD2 LEU A 347 11620 22796 8032 -3734 1860 -3005 C ATOM 2377 N ALA A 348 16.961 -4.034 -60.315 1.00105.33 N ANISOU 2377 N ALA A 348 12897 20593 6533 -4673 2175 -2320 N ATOM 2378 CA ALA A 348 17.589 -2.798 -59.867 1.00107.26 C ANISOU 2378 CA ALA A 348 13463 20837 6454 -5170 2291 -2339 C ATOM 2379 C ALA A 348 16.672 -2.024 -58.930 1.00109.43 C ANISOU 2379 C ALA A 348 14178 20629 6772 -5016 2210 -2130 C ATOM 2380 O ALA A 348 17.097 -1.735 -57.825 1.00109.43 O ANISOU 2380 O ALA A 348 14111 20711 6756 -5113 2222 -2157 O ATOM 2381 CB ALA A 348 17.962 -1.935 -61.059 1.00110.98 C ANISOU 2381 CB ALA A 348 14324 21307 6538 -5680 2424 -2373 C ATOM 2382 N LYS A 349 15.399 -1.768 -59.310 1.00104.55 N ANISOU 2382 N LYS A 349 13959 19539 6227 -4729 2111 -1946 N ATOM 2383 CA LYS A 349 14.474 -1.025 -58.433 1.00103.67 C ANISOU 2383 CA LYS A 349 14247 18998 6144 -4538 2017 -1786 C ATOM 2384 C LYS A 349 13.951 -1.924 -57.248 1.00103.90 C ANISOU 2384 C LYS A 349 13869 19069 6539 -4070 1912 -1744 C ATOM 2385 O LYS A 349 13.137 -1.459 -56.439 1.00101.92 O ANISOU 2385 O LYS A 349 13857 18528 6342 -3864 1834 -1635 O ATOM 2386 CB LYS A 349 13.277 -0.439 -59.226 1.00105.92 C ANISOU 2386 CB LYS A 349 15080 18797 6366 -4355 1922 -1645 C ATOM 2387 CG LYS A 349 12.305 -1.437 -59.864 1.00106.01 C ANISOU 2387 CG LYS A 349 14876 18738 6663 -3877 1824 -1592 C ATOM 2388 CD LYS A 349 11.149 -0.673 -60.506 1.00111.42 C ANISOU 2388 CD LYS A 349 16146 18942 7247 -3702 1714 -1477 C ATOM 2389 CE LYS A 349 10.089 -1.552 -61.119 1.00117.36 C ANISOU 2389 CE LYS A 349 16723 19606 8263 -3233 1611 -1426 C ATOM 2390 NZ LYS A 349 8.986 -0.743 -61.709 1.00123.35 N ANISOU 2390 NZ LYS A 349 18055 19912 8902 -3045 1485 -1345 N ATOM 2391 N SER A 350 14.452 -3.180 -57.145 1.00 99.27 N ANISOU 2391 N SER A 350 12696 18850 6171 -3922 1901 -1845 N ATOM 2392 CA SER A 350 14.087 -4.130 -56.096 1.00 96.87 C ANISOU 2392 CA SER A 350 12024 18606 6175 -3540 1791 -1810 C ATOM 2393 C SER A 350 15.291 -4.459 -55.189 1.00103.35 C ANISOU 2393 C SER A 350 12462 19812 6993 -3705 1821 -1957 C ATOM 2394 O SER A 350 15.087 -4.750 -54.012 1.00101.74 O ANISOU 2394 O SER A 350 12126 19590 6940 -3518 1745 -1910 O ATOM 2395 CB SER A 350 13.531 -5.412 -56.704 1.00 97.69 C ANISOU 2395 CB SER A 350 11825 18749 6544 -3165 1690 -1794 C ATOM 2396 OG SER A 350 13.127 -6.347 -55.716 1.00 99.89 O ANISOU 2396 OG SER A 350 11809 19054 7089 -2832 1567 -1745 O ATOM 2397 N THR A 351 16.535 -4.414 -55.714 1.00103.09 N ANISOU 2397 N THR A 351 12243 20150 6775 -4057 1926 -2150 N ATOM 2398 CA THR A 351 17.706 -4.716 -54.875 1.00103.91 C ANISOU 2398 CA THR A 351 11959 20661 6863 -4196 1940 -2329 C ATOM 2399 C THR A 351 18.212 -3.407 -54.189 1.00108.17 C ANISOU 2399 C THR A 351 12804 21166 7129 -4620 2053 -2333 C ATOM 2400 O THR A 351 18.628 -3.481 -53.034 1.00107.11 O ANISOU 2400 O THR A 351 12492 21160 7046 -4605 2021 -2375 O ATOM 2401 CB THR A 351 18.831 -5.420 -55.668 1.00114.59 C ANISOU 2401 CB THR A 351 12868 22517 8156 -4323 1979 -2591 C ATOM 2402 OG1 THR A 351 19.870 -5.818 -54.769 1.00116.52 O ANISOU 2402 OG1 THR A 351 12705 23154 8413 -4360 1947 -2784 O ATOM 2403 CG2 THR A 351 19.391 -4.590 -56.795 1.00116.04 C ANISOU 2403 CG2 THR A 351 13257 22830 8002 -4809 2157 -2686 C ATOM 2404 N LEU A 352 18.120 -2.218 -54.868 1.00105.75 N ANISOU 2404 N LEU A 352 13001 20648 6529 -4985 2163 -2277 N ATOM 2405 CA LEU A 352 18.524 -0.925 -54.281 1.00107.16 C ANISOU 2405 CA LEU A 352 13562 20732 6424 -5404 2248 -2264 C ATOM 2406 C LEU A 352 17.422 -0.414 -53.320 1.00109.09 C ANISOU 2406 C LEU A 352 14163 20509 6777 -5121 2145 -2061 C ATOM 2407 O LEU A 352 17.515 0.704 -52.803 1.00109.76 O ANISOU 2407 O LEU A 352 14650 20409 6644 -5386 2178 -2020 O ATOM 2408 CB LEU A 352 18.863 0.161 -55.353 1.00110.03 C ANISOU 2408 CB LEU A 352 14398 21017 6390 -5935 2376 -2280 C ATOM 2409 CG LEU A 352 17.844 0.598 -56.447 1.00114.20 C ANISOU 2409 CG LEU A 352 15445 21099 6846 -5853 2334 -2121 C ATOM 2410 CD1 LEU A 352 16.543 1.171 -55.878 1.00112.67 C ANISOU 2410 CD1 LEU A 352 15717 20346 6748 -5507 2196 -1913 C ATOM 2411 CD2 LEU A 352 18.465 1.620 -57.381 1.00119.08 C ANISOU 2411 CD2 LEU A 352 16505 21719 7022 -6475 2460 -2168 C ATOM 2412 N THR A 353 16.382 -1.236 -53.111 1.00103.15 N ANISOU 2412 N THR A 353 13263 19588 6341 -4597 2017 -1949 N ATOM 2413 CA THR A 353 15.245 -0.964 -52.233 1.00101.47 C ANISOU 2413 CA THR A 353 13281 19015 6259 -4270 1915 -1789 C ATOM 2414 C THR A 353 15.408 -1.852 -50.975 1.00104.37 C ANISOU 2414 C THR A 353 13196 19593 6866 -4037 1848 -1810 C ATOM 2415 O THR A 353 14.663 -1.708 -50.011 1.00102.38 O ANISOU 2415 O THR A 353 13042 19147 6711 -3815 1780 -1709 O ATOM 2416 CB THR A 353 13.924 -1.223 -53.025 1.00105.60 C ANISOU 2416 CB THR A 353 13977 19227 6917 -3900 1827 -1666 C ATOM 2417 OG1 THR A 353 13.972 -0.551 -54.287 1.00108.53 O ANISOU 2417 OG1 THR A 353 14724 19456 7056 -4140 1879 -1670 O ATOM 2418 CG2 THR A 353 12.676 -0.792 -52.274 1.00101.36 C ANISOU 2418 CG2 THR A 353 13711 18343 6459 -3579 1727 -1540 C ATOM 2419 N LEU A 354 16.415 -2.741 -50.984 1.00101.86 N ANISOU 2419 N LEU A 354 12399 19685 6618 -4096 1858 -1960 N ATOM 2420 CA LEU A 354 16.667 -3.701 -49.911 1.00100.39 C ANISOU 2420 CA LEU A 354 11797 19701 6643 -3870 1759 -1997 C ATOM 2421 C LEU A 354 18.066 -3.553 -49.323 1.00106.16 C ANISOU 2421 C LEU A 354 12289 20809 7237 -4177 1814 -2185 C ATOM 2422 O LEU A 354 18.368 -4.155 -48.299 1.00104.22 O ANISOU 2422 O LEU A 354 11765 20713 7119 -4029 1723 -2224 O ATOM 2423 CB LEU A 354 16.508 -5.113 -50.495 1.00 99.13 C ANISOU 2423 CB LEU A 354 11268 19677 6721 -3549 1650 -2028 C ATOM 2424 CG LEU A 354 16.314 -6.247 -49.516 1.00101.81 C ANISOU 2424 CG LEU A 354 11299 20076 7307 -3214 1485 -2000 C ATOM 2425 CD1 LEU A 354 14.913 -6.223 -48.974 1.00 99.55 C ANISOU 2425 CD1 LEU A 354 11234 19439 7152 -2953 1423 -1786 C ATOM 2426 CD2 LEU A 354 16.517 -7.566 -50.196 1.00104.66 C ANISOU 2426 CD2 LEU A 354 11313 20620 7833 -2982 1369 -2087 C ATOM 2427 N ILE A 355 18.940 -2.811 -49.998 1.00106.88 N ANISOU 2427 N ILE A 355 12474 21080 7054 -4615 1955 -2316 N ATOM 2428 CA ILE A 355 20.302 -2.628 -49.527 1.00109.57 C ANISOU 2428 CA ILE A 355 12562 21839 7230 -4950 2022 -2529 C ATOM 2429 C ILE A 355 20.317 -1.446 -48.522 1.00115.23 C ANISOU 2429 C ILE A 355 13636 22367 7779 -5198 2076 -2452 C ATOM 2430 O ILE A 355 21.025 -1.567 -47.520 1.00114.99 O ANISOU 2430 O ILE A 355 13362 22575 7753 -5250 2054 -2556 O ATOM 2431 CB ILE A 355 21.315 -2.440 -50.702 1.00115.65 C ANISOU 2431 CB ILE A 355 13211 22979 7752 -5359 2161 -2742 C ATOM 2432 CG1 ILE A 355 22.762 -2.775 -50.319 1.00118.89 C ANISOU 2432 CG1 ILE A 355 13128 23979 8067 -5566 2188 -3043 C ATOM 2433 CG2 ILE A 355 21.183 -1.140 -51.469 1.00117.79 C ANISOU 2433 CG2 ILE A 355 14027 23022 7704 -5803 2307 -2666 C ATOM 2434 CD1 ILE A 355 22.984 -4.211 -50.027 1.00127.29 C ANISOU 2434 CD1 ILE A 355 13656 25300 9407 -5114 2012 -3169 C ATOM 2435 N PRO A 356 19.507 -0.353 -48.684 1.00113.23 N ANISOU 2435 N PRO A 356 13960 21675 7389 -5300 2115 -2279 N ATOM 2436 CA PRO A 356 19.538 0.720 -47.679 1.00114.44 C ANISOU 2436 CA PRO A 356 14449 21648 7384 -5499 2138 -2224 C ATOM 2437 C PRO A 356 18.479 0.504 -46.578 1.00116.40 C ANISOU 2437 C PRO A 356 14749 21611 7867 -5058 2013 -2064 C ATOM 2438 O PRO A 356 18.831 0.547 -45.402 1.00116.14 O ANISOU 2438 O PRO A 356 14594 21679 7856 -5069 1990 -2091 O ATOM 2439 CB PRO A 356 19.250 1.986 -48.503 1.00118.06 C ANISOU 2439 CB PRO A 356 15535 21780 7544 -5825 2209 -2149 C ATOM 2440 CG PRO A 356 18.684 1.496 -49.826 1.00121.54 C ANISOU 2440 CG PRO A 356 15991 22130 8058 -5656 2196 -2107 C ATOM 2441 CD PRO A 356 18.587 0.002 -49.783 1.00114.57 C ANISOU 2441 CD PRO A 356 14522 21494 7514 -5238 2120 -2149 C ATOM 2442 N LEU A 357 17.196 0.258 -46.959 1.00111.32 N ANISOU 2442 N LEU A 357 14266 20647 7383 -4685 1935 -1913 N ATOM 2443 CA LEU A 357 16.072 0.010 -46.047 1.00109.33 C ANISOU 2443 CA LEU A 357 14042 20167 7332 -4277 1827 -1778 C ATOM 2444 C LEU A 357 16.458 -1.022 -44.984 1.00112.70 C ANISOU 2444 C LEU A 357 13996 20865 7960 -4109 1759 -1817 C ATOM 2445 O LEU A 357 16.453 -0.690 -43.800 1.00112.37 O ANISOU 2445 O LEU A 357 13999 20794 7904 -4110 1739 -1795 O ATOM 2446 CB LEU A 357 14.841 -0.478 -46.847 1.00107.78 C ANISOU 2446 CB LEU A 357 13906 19746 7298 -3914 1759 -1670 C ATOM 2447 CG LEU A 357 13.514 -0.676 -46.086 1.00110.87 C ANISOU 2447 CG LEU A 357 14344 19921 7860 -3511 1660 -1548 C ATOM 2448 CD1 LEU A 357 12.940 0.664 -45.628 1.00112.59 C ANISOU 2448 CD1 LEU A 357 15057 19829 7892 -3541 1656 -1509 C ATOM 2449 CD2 LEU A 357 12.469 -1.362 -46.972 1.00111.05 C ANISOU 2449 CD2 LEU A 357 14319 19827 8050 -3187 1598 -1477 C ATOM 2450 N LEU A 358 16.872 -2.236 -45.418 1.00108.83 N ANISOU 2450 N LEU A 358 13079 20639 7632 -3983 1710 -1892 N ATOM 2451 CA LEU A 358 17.276 -3.339 -44.541 1.00108.12 C ANISOU 2451 CA LEU A 358 12570 20787 7722 -3798 1597 -1942 C ATOM 2452 C LEU A 358 18.630 -3.027 -43.884 1.00114.78 C ANISOU 2452 C LEU A 358 13248 21943 8419 -4098 1638 -2113 C ATOM 2453 O LEU A 358 18.818 -3.339 -42.708 1.00114.23 O ANISOU 2453 O LEU A 358 13033 21948 8419 -4005 1557 -2116 O ATOM 2454 CB LEU A 358 17.338 -4.657 -45.356 1.00107.23 C ANISOU 2454 CB LEU A 358 12119 20834 7792 -3568 1503 -1993 C ATOM 2455 CG LEU A 358 17.483 -6.019 -44.622 1.00110.67 C ANISOU 2455 CG LEU A 358 12192 21420 8438 -3278 1318 -2016 C ATOM 2456 CD1 LEU A 358 16.903 -7.152 -45.444 1.00109.08 C ANISOU 2456 CD1 LEU A 358 11850 21170 8426 -2981 1207 -1972 C ATOM 2457 CD2 LEU A 358 18.916 -6.317 -44.200 1.00114.35 C ANISOU 2457 CD2 LEU A 358 12332 22275 8841 -3409 1276 -2240 C ATOM 2458 N GLY A 359 19.530 -2.394 -44.633 1.00114.22 N ANISOU 2458 N GLY A 359 13211 22059 8128 -4473 1765 -2257 N ATOM 2459 CA GLY A 359 20.868 -2.041 -44.170 1.00116.87 C ANISOU 2459 CA GLY A 359 13369 22752 8286 -4815 1825 -2456 C ATOM 2460 C GLY A 359 20.954 -1.002 -43.066 1.00122.78 C ANISOU 2460 C GLY A 359 14389 23374 8889 -5024 1870 -2408 C ATOM 2461 O GLY A 359 21.581 -1.255 -42.035 1.00122.31 O ANISOU 2461 O GLY A 359 14091 23526 8856 -5019 1815 -2496 O ATOM 2462 N VAL A 360 20.337 0.176 -43.277 1.00121.28 N ANISOU 2462 N VAL A 360 14717 22831 8534 -5195 1952 -2279 N ATOM 2463 CA VAL A 360 20.358 1.312 -42.348 1.00123.17 C ANISOU 2463 CA VAL A 360 15303 22898 8600 -5408 1989 -2235 C ATOM 2464 C VAL A 360 19.578 0.991 -41.049 1.00130.50 C ANISOU 2464 C VAL A 360 16202 23657 9725 -5039 1876 -2111 C ATOM 2465 O VAL A 360 20.103 1.266 -39.968 1.00130.28 O ANISOU 2465 O VAL A 360 16124 23737 9640 -5154 1870 -2160 O ATOM 2466 CB VAL A 360 19.784 2.596 -43.009 1.00127.35 C ANISOU 2466 CB VAL A 360 16454 23036 8897 -5619 2055 -2133 C ATOM 2467 CG1 VAL A 360 19.663 3.744 -42.009 1.00127.98 C ANISOU 2467 CG1 VAL A 360 16938 22880 8809 -5767 2054 -2081 C ATOM 2468 CG2 VAL A 360 20.626 3.020 -44.205 1.00129.55 C ANISOU 2468 CG2 VAL A 360 16818 23487 8919 -6080 2178 -2251 C ATOM 2469 N HIS A 361 18.334 0.437 -41.145 1.00129.91 N ANISOU 2469 N HIS A 361 16160 23341 9859 -4628 1792 -1961 N ATOM 2470 CA HIS A 361 17.502 0.208 -39.949 1.00130.55 C ANISOU 2470 CA HIS A 361 16244 23278 10083 -4328 1702 -1847 C ATOM 2471 C HIS A 361 18.095 -0.919 -39.061 1.00136.08 C ANISOU 2471 C HIS A 361 16490 24271 10943 -4202 1605 -1905 C ATOM 2472 O HIS A 361 17.787 -0.951 -37.867 1.00136.18 O ANISOU 2472 O HIS A 361 16507 24236 11001 -4089 1549 -1846 O ATOM 2473 CB HIS A 361 16.021 -0.117 -40.292 1.00130.33 C ANISOU 2473 CB HIS A 361 16336 22976 10208 -3956 1644 -1699 C ATOM 2474 CG HIS A 361 15.670 -1.575 -40.449 1.00132.65 C ANISOU 2474 CG HIS A 361 16259 23388 10755 -3654 1546 -1660 C ATOM 2475 ND1 HIS A 361 15.309 -2.350 -39.354 1.00133.70 N ANISOU 2475 ND1 HIS A 361 16196 23570 11033 -3443 1446 -1600 N ATOM 2476 CD2 HIS A 361 15.502 -2.312 -41.572 1.00133.90 C ANISOU 2476 CD2 HIS A 361 16278 23575 11021 -3535 1524 -1660 C ATOM 2477 CE1 HIS A 361 15.007 -3.542 -39.842 1.00131.98 C ANISOU 2477 CE1 HIS A 361 15740 23410 10997 -3226 1358 -1566 C ATOM 2478 NE2 HIS A 361 15.105 -3.567 -41.171 1.00132.27 N ANISOU 2478 NE2 HIS A 361 15790 23438 11028 -3258 1401 -1604 N ATOM 2479 N GLU A 362 18.932 -1.820 -39.618 1.00133.28 N ANISOU 2479 N GLU A 362 15769 24215 10657 -4211 1568 -2033 N ATOM 2480 CA GLU A 362 19.525 -2.869 -38.791 1.00133.03 C ANISOU 2480 CA GLU A 362 15357 24434 10753 -4062 1431 -2108 C ATOM 2481 C GLU A 362 20.989 -2.476 -38.471 1.00138.56 C ANISOU 2481 C GLU A 362 15883 25479 11283 -4383 1476 -2325 C ATOM 2482 O GLU A 362 21.752 -3.266 -37.907 1.00137.50 O ANISOU 2482 O GLU A 362 15411 25617 11213 -4291 1352 -2455 O ATOM 2483 CB GLU A 362 19.412 -4.236 -39.475 1.00133.55 C ANISOU 2483 CB GLU A 362 15131 24596 11017 -3778 1303 -2126 C ATOM 2484 CG GLU A 362 19.116 -5.392 -38.522 1.00144.00 C ANISOU 2484 CG GLU A 362 16278 25913 12522 -3470 1102 -2060 C ATOM 2485 CD GLU A 362 17.760 -5.437 -37.821 1.00161.37 C ANISOU 2485 CD GLU A 362 18695 27810 14807 -3286 1072 -1833 C ATOM 2486 OE1 GLU A 362 17.279 -6.564 -37.566 1.00156.47 O ANISOU 2486 OE1 GLU A 362 17962 27150 14340 -3038 913 -1753 O ATOM 2487 OE2 GLU A 362 17.156 -4.368 -37.569 1.00151.23 O ANISOU 2487 OE2 GLU A 362 17701 26337 13423 -3391 1195 -1749 O ATOM 2488 N VAL A 363 21.336 -1.210 -38.798 1.00137.98 N ANISOU 2488 N VAL A 363 16078 25378 10972 -4765 1639 -2367 N ATOM 2489 CA VAL A 363 22.596 -0.537 -38.480 1.00141.14 C ANISOU 2489 CA VAL A 363 16406 26071 11150 -5164 1720 -2557 C ATOM 2490 C VAL A 363 22.332 0.447 -37.336 1.00147.01 C ANISOU 2490 C VAL A 363 17473 26596 11787 -5281 1749 -2460 C ATOM 2491 O VAL A 363 23.227 0.719 -36.536 1.00148.57 O ANISOU 2491 O VAL A 363 17552 27019 11877 -5483 1754 -2585 O ATOM 2492 CB VAL A 363 23.236 0.158 -39.699 1.00147.29 C ANISOU 2492 CB VAL A 363 17276 26994 11692 -5580 1880 -2682 C ATOM 2493 N VAL A 364 21.082 0.962 -37.252 1.00142.91 N ANISOU 2493 N VAL A 364 17350 25653 11297 -5128 1757 -2254 N ATOM 2494 CA VAL A 364 20.585 1.820 -36.165 1.00143.15 C ANISOU 2494 CA VAL A 364 17702 25437 11251 -5139 1758 -2155 C ATOM 2495 C VAL A 364 20.465 0.939 -34.904 1.00147.79 C ANISOU 2495 C VAL A 364 18010 26121 12022 -4856 1630 -2124 C ATOM 2496 O VAL A 364 20.651 1.409 -33.781 1.00147.39 O ANISOU 2496 O VAL A 364 18039 26065 11899 -4933 1621 -2127 O ATOM 2497 CB VAL A 364 19.240 2.505 -36.575 1.00145.80 C ANISOU 2497 CB VAL A 364 18495 25336 11567 -4989 1774 -1991 C ATOM 2498 CG1 VAL A 364 18.516 3.136 -35.388 1.00145.16 C ANISOU 2498 CG1 VAL A 364 18674 25025 11458 -4864 1737 -1903 C ATOM 2499 CG2 VAL A 364 19.458 3.531 -37.683 1.00147.44 C ANISOU 2499 CG2 VAL A 364 19078 25407 11535 -5320 1874 -2022 C ATOM 2500 N PHE A 365 20.232 -0.367 -35.142 1.00145.42 N ANISOU 2500 N PHE A 365 17396 25916 11941 -4555 1521 -2102 N ATOM 2501 CA PHE A 365 20.083 -1.470 -34.200 1.00145.39 C ANISOU 2501 CA PHE A 365 17138 25989 12115 -4272 1363 -2062 C ATOM 2502 C PHE A 365 21.219 -1.529 -33.167 1.00151.90 C ANISOU 2502 C PHE A 365 17760 27083 12872 -4404 1303 -2204 C ATOM 2503 O PHE A 365 20.935 -1.568 -31.970 1.00151.01 O ANISOU 2503 O PHE A 365 17697 26901 12780 -4314 1237 -2129 O ATOM 2504 CB PHE A 365 20.054 -2.791 -34.997 1.00146.87 C ANISOU 2504 CB PHE A 365 17036 26283 12484 -4031 1251 -2081 C ATOM 2505 CG PHE A 365 20.022 -4.073 -34.199 1.00148.49 C ANISOU 2505 CG PHE A 365 17006 26561 12851 -3755 1045 -2054 C ATOM 2506 CD1 PHE A 365 18.813 -4.653 -33.830 1.00150.57 C ANISOU 2506 CD1 PHE A 365 17368 26599 13243 -3508 968 -1861 C ATOM 2507 CD2 PHE A 365 21.201 -4.740 -33.878 1.00152.52 C ANISOU 2507 CD2 PHE A 365 17206 27377 13367 -3745 911 -2238 C ATOM 2508 CE1 PHE A 365 18.783 -5.853 -33.108 1.00151.48 C ANISOU 2508 CE1 PHE A 365 17329 26753 13471 -3299 760 -1822 C ATOM 2509 CE2 PHE A 365 21.172 -5.936 -33.152 1.00155.39 C ANISOU 2509 CE2 PHE A 365 17422 27762 13857 -3479 678 -2211 C ATOM 2510 CZ PHE A 365 19.962 -6.487 -32.775 1.00151.99 C ANISOU 2510 CZ PHE A 365 17145 27067 13538 -3277 603 -1989 C ATOM 2511 N ALA A 366 22.485 -1.585 -33.625 1.00151.75 N ANISOU 2511 N ALA A 366 17492 27400 12768 -4606 1319 -2422 N ATOM 2512 CA ALA A 366 23.655 -1.742 -32.754 1.00154.21 C ANISOU 2512 CA ALA A 366 17546 28032 13015 -4705 1241 -2605 C ATOM 2513 C ALA A 366 24.048 -0.412 -32.025 1.00161.10 C ANISOU 2513 C ALA A 366 18653 28889 13669 -5058 1368 -2634 C ATOM 2514 O ALA A 366 24.174 -0.420 -30.792 1.00160.52 O ANISOU 2514 O ALA A 366 18568 28826 13596 -5011 1290 -2620 O ATOM 2515 CB ALA A 366 24.838 -2.250 -33.564 1.00156.75 C ANISOU 2515 CB ALA A 366 17484 28773 13301 -4789 1216 -2873 C ATOM 2516 N PHE A 367 24.271 0.704 -32.775 1.00159.87 N ANISOU 2516 N PHE A 367 18729 28703 13310 -5426 1548 -2674 N ATOM 2517 CA PHE A 367 24.675 1.983 -32.173 1.00161.43 C ANISOU 2517 CA PHE A 367 19195 28867 13274 -5794 1654 -2706 C ATOM 2518 C PHE A 367 24.255 3.201 -33.050 1.00165.77 C ANISOU 2518 C PHE A 367 20218 29139 13629 -6086 1811 -2628 C ATOM 2519 O PHE A 367 24.876 3.501 -34.077 1.00167.10 O ANISOU 2519 O PHE A 367 20375 29473 13644 -6400 1912 -2746 O ATOM 2520 CB PHE A 367 26.198 2.017 -31.936 1.00165.86 C ANISOU 2520 CB PHE A 367 19425 29907 13687 -6097 1665 -2980 C ATOM 2521 N VAL A 368 23.194 3.893 -32.601 1.00160.48 N ANISOU 2521 N VAL A 368 19975 28053 12947 -5973 1812 -2443 N ATOM 2522 CA VAL A 368 22.613 5.135 -33.140 1.00160.45 C ANISOU 2522 CA VAL A 368 20527 27685 12752 -6161 1896 -2353 C ATOM 2523 C VAL A 368 22.059 5.897 -31.953 1.00162.71 C ANISOU 2523 C VAL A 368 21132 27709 12980 -6090 1859 -2266 C ATOM 2524 O VAL A 368 22.219 7.113 -31.825 1.00163.72 O ANISOU 2524 O VAL A 368 21681 27660 12864 -6388 1905 -2278 O ATOM 2525 CB VAL A 368 21.563 4.878 -34.239 1.00162.68 C ANISOU 2525 CB VAL A 368 20958 27712 13142 -5912 1890 -2230 C ATOM 2526 N THR A 369 21.432 5.125 -31.060 1.00156.76 N ANISOU 2526 N THR A 369 20173 26946 12441 -5702 1763 -2187 N ATOM 2527 CA THR A 369 20.951 5.480 -29.735 1.00156.13 C ANISOU 2527 CA THR A 369 20233 26732 12357 -5567 1713 -2125 C ATOM 2528 C THR A 369 21.698 4.471 -28.834 1.00159.70 C ANISOU 2528 C THR A 369 20215 27527 12936 -5501 1638 -2195 C ATOM 2529 O THR A 369 21.116 3.501 -28.335 1.00157.44 O ANISOU 2529 O THR A 369 19720 27255 12845 -5169 1543 -2113 O ATOM 2530 CB THR A 369 19.406 5.486 -29.704 1.00159.18 C ANISOU 2530 CB THR A 369 20836 26800 12847 -5184 1670 -1977 C ATOM 2531 OG1 THR A 369 18.922 6.330 -30.755 1.00156.74 O ANISOU 2531 OG1 THR A 369 20935 26209 12411 -5249 1712 -1953 O ATOM 2532 CG2 THR A 369 18.846 5.950 -28.358 1.00157.13 C ANISOU 2532 CG2 THR A 369 20734 26421 12548 -5052 1628 -1939 C ATOM 2533 N ASP A 370 23.044 4.655 -28.761 1.00157.97 N ANISOU 2533 N ASP A 370 19828 27607 12588 -5840 1671 -2364 N ATOM 2534 CA ASP A 370 24.035 3.786 -28.107 1.00157.51 C ANISOU 2534 CA ASP A 370 19315 27928 12602 -5823 1584 -2498 C ATOM 2535 C ASP A 370 24.132 4.017 -26.558 1.00160.74 C ANISOU 2535 C ASP A 370 19759 28337 12979 -5799 1520 -2486 C ATOM 2536 O ASP A 370 24.759 3.192 -25.879 1.00161.03 O ANISOU 2536 O ASP A 370 19453 28634 13098 -5697 1406 -2571 O ATOM 2537 CB ASP A 370 25.432 4.010 -28.745 1.00161.20 C ANISOU 2537 CB ASP A 370 19578 28764 12905 -6220 1657 -2729 C ATOM 2538 CG ASP A 370 25.908 5.455 -28.785 1.00166.71 C ANISOU 2538 CG ASP A 370 20635 29403 13303 -6705 1791 -2786 C ATOM 2539 OD1 ASP A 370 26.496 5.914 -27.784 1.00168.29 O ANISOU 2539 OD1 ASP A 370 20842 29710 13389 -6880 1781 -2861 O ATOM 2540 OD2 ASP A 370 25.745 6.106 -29.845 1.00168.00 O ANISOU 2540 OD2 ASP A 370 21083 29419 13329 -6932 1895 -2763 O ATOM 2541 N GLU A 371 23.498 5.084 -25.999 1.00155.80 N ANISOU 2541 N GLU A 371 19549 27416 12231 -5860 1572 -2392 N ATOM 2542 CA GLU A 371 23.532 5.349 -24.546 1.00154.91 C ANISOU 2542 CA GLU A 371 19487 27296 12076 -5837 1519 -2381 C ATOM 2543 C GLU A 371 22.610 4.361 -23.803 1.00154.98 C ANISOU 2543 C GLU A 371 19360 27240 12287 -5426 1407 -2245 C ATOM 2544 O GLU A 371 21.492 4.112 -24.254 1.00152.46 O ANISOU 2544 O GLU A 371 19141 26718 12069 -5186 1411 -2117 O ATOM 2545 CB GLU A 371 23.129 6.811 -24.237 1.00157.23 C ANISOU 2545 CB GLU A 371 20287 27294 12161 -6014 1593 -2344 C ATOM 2546 CG GLU A 371 23.293 7.199 -22.769 1.00166.17 C ANISOU 2546 CG GLU A 371 21479 28441 13218 -6039 1551 -2358 C ATOM 2547 CD GLU A 371 22.886 8.597 -22.333 1.00183.07 C ANISOU 2547 CD GLU A 371 24124 30285 15151 -6168 1590 -2337 C ATOM 2548 OE1 GLU A 371 22.320 9.352 -23.156 1.00178.80 O ANISOU 2548 OE1 GLU A 371 23960 29462 14513 -6203 1632 -2298 O ATOM 2549 OE2 GLU A 371 23.109 8.924 -21.146 1.00173.62 O ANISOU 2549 OE2 GLU A 371 22963 29123 13882 -6209 1557 -2365 O ATOM 2550 N HIS A 372 23.090 3.802 -22.669 1.00151.53 N ANISOU 2550 N HIS A 372 18705 26986 11885 -5368 1300 -2280 N ATOM 2551 CA HIS A 372 22.335 2.859 -21.816 1.00149.70 C ANISOU 2551 CA HIS A 372 18372 26712 11793 -5053 1181 -2154 C ATOM 2552 C HIS A 372 21.053 3.530 -21.255 1.00151.37 C ANISOU 2552 C HIS A 372 18907 26651 11956 -4939 1240 -2021 C ATOM 2553 O HIS A 372 20.010 2.878 -21.159 1.00149.93 O ANISOU 2553 O HIS A 372 18704 26381 11883 -4688 1202 -1897 O ATOM 2554 CB HIS A 372 23.216 2.343 -20.656 1.00151.29 C ANISOU 2554 CB HIS A 372 18356 27143 11985 -5069 1046 -2235 C ATOM 2555 CG HIS A 372 23.598 3.414 -19.687 1.00155.98 C ANISOU 2555 CG HIS A 372 19133 27731 12400 -5286 1099 -2291 C ATOM 2556 ND1 HIS A 372 22.874 3.627 -18.527 1.00157.41 N ANISOU 2556 ND1 HIS A 372 19484 27778 12545 -5185 1080 -2188 N ATOM 2557 CD2 HIS A 372 24.534 4.382 -19.800 1.00159.64 C ANISOU 2557 CD2 HIS A 372 19665 28294 12697 -5615 1183 -2437 C ATOM 2558 CE1 HIS A 372 23.432 4.674 -17.942 1.00158.47 C ANISOU 2558 CE1 HIS A 372 19776 27926 12509 -5424 1136 -2275 C ATOM 2559 NE2 HIS A 372 24.431 5.167 -18.674 1.00160.22 N ANISOU 2559 NE2 HIS A 372 19955 28278 12643 -5700 1198 -2421 N ATOM 2560 N ALA A 373 21.159 4.843 -20.897 1.00146.94 N ANISOU 2560 N ALA A 373 18644 25976 11210 -5134 1324 -2070 N ATOM 2561 CA ALA A 373 20.120 5.726 -20.355 1.00145.65 C ANISOU 2561 CA ALA A 373 18817 25573 10950 -5041 1368 -2009 C ATOM 2562 C ALA A 373 19.357 5.058 -19.193 1.00146.34 C ANISOU 2562 C ALA A 373 18797 25704 11103 -4809 1299 -1920 C ATOM 2563 O ALA A 373 19.710 5.273 -18.033 1.00147.02 O ANISOU 2563 O ALA A 373 18893 25864 11104 -4884 1266 -1950 O ATOM 2564 CB ALA A 373 19.145 6.140 -21.451 1.00145.79 C ANISOU 2564 CB ALA A 373 19066 25353 10977 -4917 1429 -1960 C ATOM 2565 N GLN A 374 18.315 4.260 -19.511 1.00139.47 N ANISOU 2565 N GLN A 374 17834 24797 10362 -4559 1280 -1816 N ATOM 2566 CA GLN A 374 17.451 3.577 -18.544 1.00137.74 C ANISOU 2566 CA GLN A 374 17527 24631 10176 -4379 1228 -1725 C ATOM 2567 C GLN A 374 16.705 2.426 -19.231 1.00138.01 C ANISOU 2567 C GLN A 374 17387 24679 10370 -4191 1191 -1622 C ATOM 2568 O GLN A 374 16.674 2.365 -20.457 1.00137.35 O ANISOU 2568 O GLN A 374 17293 24527 10367 -4158 1222 -1625 O ATOM 2569 CB GLN A 374 16.463 4.580 -17.897 1.00139.74 C ANISOU 2569 CB GLN A 374 18037 24769 10287 -4295 1295 -1745 C ATOM 2570 CG GLN A 374 15.633 5.418 -18.888 1.00152.55 C ANISOU 2570 CG GLN A 374 19902 26185 11875 -4174 1367 -1778 C ATOM 2571 CD GLN A 374 14.871 6.566 -18.245 1.00173.67 C ANISOU 2571 CD GLN A 374 22863 28745 14380 -4076 1396 -1855 C ATOM 2572 OE1 GLN A 374 14.491 7.529 -18.917 1.00169.67 O ANISOU 2572 OE1 GLN A 374 22648 28029 13791 -4010 1417 -1920 O ATOM 2573 NE2 GLN A 374 14.718 6.557 -16.922 1.00166.11 N ANISOU 2573 NE2 GLN A 374 21862 27909 13342 -4070 1381 -1865 N ATOM 2574 N GLY A 375 16.135 1.527 -18.433 1.00132.49 N ANISOU 2574 N GLY A 375 16572 24070 9699 -4098 1121 -1531 N ATOM 2575 CA GLY A 375 15.390 0.369 -18.914 1.00130.80 C ANISOU 2575 CA GLY A 375 16216 23875 9609 -3955 1070 -1423 C ATOM 2576 C GLY A 375 14.126 0.689 -19.695 1.00133.89 C ANISOU 2576 C GLY A 375 16686 24170 10017 -3800 1171 -1407 C ATOM 2577 O GLY A 375 13.847 0.028 -20.699 1.00133.27 O ANISOU 2577 O GLY A 375 16513 24061 10063 -3711 1153 -1358 O ATOM 2578 N THR A 376 13.347 1.705 -19.243 1.00130.10 N ANISOU 2578 N THR A 376 16379 23650 9403 -3743 1261 -1467 N ATOM 2579 CA THR A 376 12.082 2.145 -19.862 1.00129.39 C ANISOU 2579 CA THR A 376 16376 23491 9296 -3551 1336 -1499 C ATOM 2580 C THR A 376 12.332 2.580 -21.336 1.00132.16 C ANISOU 2580 C THR A 376 16833 23661 9719 -3515 1364 -1532 C ATOM 2581 O THR A 376 11.570 2.182 -22.223 1.00130.72 O ANISOU 2581 O THR A 376 16595 23449 9623 -3367 1374 -1501 O ATOM 2582 CB THR A 376 11.454 3.292 -19.023 1.00137.79 C ANISOU 2582 CB THR A 376 17628 24549 10176 -3481 1392 -1610 C ATOM 2583 OG1 THR A 376 11.126 2.780 -17.732 1.00137.12 O ANISOU 2583 OG1 THR A 376 17420 24664 10017 -3526 1377 -1576 O ATOM 2584 CG2 THR A 376 10.182 3.869 -19.645 1.00137.60 C ANISOU 2584 CG2 THR A 376 17706 24465 10110 -3233 1439 -1696 C ATOM 2585 N LEU A 377 13.402 3.366 -21.585 1.00128.96 N ANISOU 2585 N LEU A 377 16582 23154 9264 -3678 1375 -1595 N ATOM 2586 CA LEU A 377 13.761 3.852 -22.921 1.00128.29 C ANISOU 2586 CA LEU A 377 16636 22909 9200 -3718 1405 -1629 C ATOM 2587 C LEU A 377 14.565 2.801 -23.703 1.00129.70 C ANISOU 2587 C LEU A 377 16565 23181 9535 -3802 1368 -1579 C ATOM 2588 O LEU A 377 14.559 2.850 -24.935 1.00129.15 O ANISOU 2588 O LEU A 377 16538 23018 9516 -3786 1394 -1584 O ATOM 2589 CB LEU A 377 14.560 5.171 -22.848 1.00130.06 C ANISOU 2589 CB LEU A 377 17160 22999 9256 -3918 1435 -1726 C ATOM 2590 CG LEU A 377 13.769 6.500 -22.718 1.00136.45 C ANISOU 2590 CG LEU A 377 18356 23596 9894 -3800 1448 -1808 C ATOM 2591 CD1 LEU A 377 12.850 6.535 -21.488 1.00136.99 C ANISOU 2591 CD1 LEU A 377 18383 23761 9904 -3613 1436 -1833 C ATOM 2592 CD2 LEU A 377 14.711 7.691 -22.690 1.00141.01 C ANISOU 2592 CD2 LEU A 377 19260 24023 10294 -4061 1457 -1886 C ATOM 2593 N ARG A 378 15.234 1.848 -23.007 1.00124.56 N ANISOU 2593 N ARG A 378 15669 22710 8950 -3872 1290 -1544 N ATOM 2594 CA ARG A 378 16.009 0.784 -23.663 1.00123.33 C ANISOU 2594 CA ARG A 378 15267 22660 8933 -3900 1214 -1529 C ATOM 2595 C ARG A 378 15.071 -0.234 -24.339 1.00124.38 C ANISOU 2595 C ARG A 378 15277 22771 9209 -3699 1177 -1429 C ATOM 2596 O ARG A 378 15.304 -0.613 -25.491 1.00122.98 O ANISOU 2596 O ARG A 378 15019 22577 9130 -3673 1171 -1437 O ATOM 2597 CB ARG A 378 16.938 0.065 -22.663 1.00124.41 C ANISOU 2597 CB ARG A 378 15217 22973 9078 -3981 1094 -1541 C ATOM 2598 CG ARG A 378 17.844 -0.986 -23.317 1.00136.24 C ANISOU 2598 CG ARG A 378 16466 24598 10702 -3972 978 -1577 C ATOM 2599 CD ARG A 378 18.575 -1.859 -22.318 1.00146.76 C ANISOU 2599 CD ARG A 378 17638 26079 12045 -3970 804 -1589 C ATOM 2600 NE ARG A 378 19.484 -1.102 -21.460 1.00156.13 N ANISOU 2600 NE ARG A 378 18857 27362 13104 -4148 818 -1696 N ATOM 2601 CZ ARG A 378 20.247 -1.652 -20.521 1.00170.61 C ANISOU 2601 CZ ARG A 378 20575 29332 14917 -4160 663 -1739 C ATOM 2602 NH1 ARG A 378 20.218 -2.964 -20.316 1.00157.73 N ANISOU 2602 NH1 ARG A 378 18826 27730 13376 -4002 465 -1679 N ATOM 2603 NH2 ARG A 378 21.051 -0.896 -19.785 1.00157.67 N ANISOU 2603 NH2 ARG A 378 18964 27787 13156 -4330 687 -1845 N ATOM 2604 N SER A 379 14.024 -0.680 -23.610 1.00119.80 N ANISOU 2604 N SER A 379 14680 22214 8624 -3582 1156 -1344 N ATOM 2605 CA SER A 379 13.036 -1.652 -24.085 1.00118.29 C ANISOU 2605 CA SER A 379 14382 22026 8538 -3430 1122 -1248 C ATOM 2606 C SER A 379 12.305 -1.142 -25.337 1.00121.00 C ANISOU 2606 C SER A 379 14818 22242 8915 -3305 1212 -1272 C ATOM 2607 O SER A 379 12.094 -1.925 -26.260 1.00120.10 O ANISOU 2607 O SER A 379 14593 22113 8926 -3223 1176 -1223 O ATOM 2608 CB SER A 379 12.027 -1.965 -22.987 1.00122.14 C ANISOU 2608 CB SER A 379 14861 22600 8946 -3396 1115 -1183 C ATOM 2609 OG SER A 379 11.374 -0.789 -22.538 1.00131.99 O ANISOU 2609 OG SER A 379 16266 23828 10057 -3358 1226 -1262 O ATOM 2610 N ALA A 380 11.976 0.179 -25.390 1.00117.12 N ANISOU 2610 N ALA A 380 14556 21641 8303 -3284 1307 -1357 N ATOM 2611 CA ALA A 380 11.303 0.834 -26.528 1.00116.10 C ANISOU 2611 CA ALA A 380 14589 21354 8171 -3151 1366 -1399 C ATOM 2612 C ALA A 380 12.115 0.673 -27.828 1.00117.48 C ANISOU 2612 C ALA A 380 14749 21456 8432 -3231 1364 -1401 C ATOM 2613 O ALA A 380 11.529 0.536 -28.906 1.00115.83 O ANISOU 2613 O ALA A 380 14559 21162 8290 -3103 1377 -1386 O ATOM 2614 CB ALA A 380 11.088 2.310 -26.230 1.00118.18 C ANISOU 2614 CB ALA A 380 15163 21481 8258 -3136 1416 -1504 C ATOM 2615 N LYS A 381 13.462 0.678 -27.712 1.00113.18 N ANISOU 2615 N LYS A 381 14152 20978 7875 -3445 1349 -1437 N ATOM 2616 CA LYS A 381 14.365 0.469 -28.833 1.00112.21 C ANISOU 2616 CA LYS A 381 13958 20868 7808 -3557 1352 -1473 C ATOM 2617 C LYS A 381 14.273 -0.990 -29.243 1.00115.23 C ANISOU 2617 C LYS A 381 14053 21356 8372 -3431 1262 -1405 C ATOM 2618 O LYS A 381 13.903 -1.267 -30.380 1.00114.59 O ANISOU 2618 O LYS A 381 13956 21210 8372 -3338 1275 -1385 O ATOM 2619 CB LYS A 381 15.810 0.889 -28.475 1.00115.08 C ANISOU 2619 CB LYS A 381 14303 21343 8078 -3828 1360 -1570 C ATOM 2620 CG LYS A 381 16.809 0.744 -29.631 1.00119.51 C ANISOU 2620 CG LYS A 381 14761 21989 8656 -3983 1380 -1650 C ATOM 2621 CD LYS A 381 18.238 1.119 -29.238 1.00123.93 C ANISOU 2621 CD LYS A 381 15250 22734 9104 -4271 1392 -1780 C ATOM 2622 CE LYS A 381 19.215 0.934 -30.380 1.00122.87 C ANISOU 2622 CE LYS A 381 14963 22759 8962 -4440 1421 -1894 C ATOM 2623 NZ LYS A 381 20.608 1.274 -29.984 1.00128.20 N ANISOU 2623 NZ LYS A 381 15520 23682 9508 -4734 1436 -2055 N ATOM 2624 N LEU A 382 14.525 -1.916 -28.286 1.00111.93 N ANISOU 2624 N LEU A 382 13447 21075 8005 -3417 1155 -1364 N ATOM 2625 CA LEU A 382 14.480 -3.374 -28.458 1.00111.60 C ANISOU 2625 CA LEU A 382 13185 21108 8109 -3302 1020 -1295 C ATOM 2626 C LEU A 382 13.182 -3.838 -29.132 1.00114.49 C ANISOU 2626 C LEU A 382 13559 21382 8558 -3127 1033 -1200 C ATOM 2627 O LEU A 382 13.251 -4.567 -30.122 1.00114.49 O ANISOU 2627 O LEU A 382 13451 21376 8676 -3050 982 -1187 O ATOM 2628 CB LEU A 382 14.617 -4.070 -27.088 1.00112.62 C ANISOU 2628 CB LEU A 382 13241 21331 8218 -3317 894 -1243 C ATOM 2629 CG LEU A 382 14.396 -5.601 -27.030 1.00117.90 C ANISOU 2629 CG LEU A 382 13777 22027 8994 -3207 713 -1147 C ATOM 2630 CD1 LEU A 382 15.429 -6.362 -27.863 1.00118.35 C ANISOU 2630 CD1 LEU A 382 13664 22145 9157 -3157 584 -1227 C ATOM 2631 CD2 LEU A 382 14.426 -6.095 -25.593 1.00122.39 C ANISOU 2631 CD2 LEU A 382 14364 22650 9488 -3259 594 -1085 C ATOM 2632 N PHE A 383 12.013 -3.440 -28.587 1.00109.87 N ANISOU 2632 N PHE A 383 13084 20758 7905 -3061 1097 -1155 N ATOM 2633 CA PHE A 383 10.708 -3.821 -29.126 1.00108.46 C ANISOU 2633 CA PHE A 383 12890 20541 7778 -2903 1116 -1093 C ATOM 2634 C PHE A 383 10.486 -3.221 -30.512 1.00110.66 C ANISOU 2634 C PHE A 383 13265 20689 8089 -2816 1192 -1143 C ATOM 2635 O PHE A 383 9.873 -3.890 -31.346 1.00109.86 O ANISOU 2635 O PHE A 383 13085 20568 8091 -2698 1168 -1096 O ATOM 2636 CB PHE A 383 9.564 -3.404 -28.187 1.00110.97 C ANISOU 2636 CB PHE A 383 13272 20912 7979 -2856 1175 -1089 C ATOM 2637 CG PHE A 383 9.371 -4.347 -27.019 1.00113.06 C ANISOU 2637 CG PHE A 383 13428 21315 8214 -2937 1092 -1000 C ATOM 2638 CD1 PHE A 383 10.107 -4.196 -25.850 1.00117.22 C ANISOU 2638 CD1 PHE A 383 13982 21900 8656 -3073 1055 -1007 C ATOM 2639 CD2 PHE A 383 8.456 -5.390 -27.092 1.00114.78 C ANISOU 2639 CD2 PHE A 383 13542 21601 8469 -2904 1042 -909 C ATOM 2640 CE1 PHE A 383 9.944 -5.082 -24.783 1.00118.58 C ANISOU 2640 CE1 PHE A 383 14099 22178 8778 -3165 961 -917 C ATOM 2641 CE2 PHE A 383 8.286 -6.269 -26.021 1.00118.23 C ANISOU 2641 CE2 PHE A 383 13936 22148 8841 -3030 954 -816 C ATOM 2642 CZ PHE A 383 9.043 -6.119 -24.881 1.00117.26 C ANISOU 2642 CZ PHE A 383 13861 22062 8631 -3156 908 -817 C ATOM 2643 N PHE A 384 11.018 -2.002 -30.785 1.00106.61 N ANISOU 2643 N PHE A 384 12948 20080 7479 -2896 1271 -1234 N ATOM 2644 CA PHE A 384 10.867 -1.371 -32.103 1.00105.55 C ANISOU 2644 CA PHE A 384 12971 19792 7339 -2848 1327 -1277 C ATOM 2645 C PHE A 384 11.734 -2.099 -33.146 1.00104.47 C ANISOU 2645 C PHE A 384 12682 19695 7316 -2915 1294 -1275 C ATOM 2646 O PHE A 384 11.297 -2.255 -34.284 1.00102.53 O ANISOU 2646 O PHE A 384 12454 19368 7133 -2813 1305 -1263 O ATOM 2647 CB PHE A 384 11.215 0.123 -32.063 1.00109.09 C ANISOU 2647 CB PHE A 384 13736 20101 7612 -2958 1396 -1366 C ATOM 2648 CG PHE A 384 10.752 0.880 -33.286 1.00111.43 C ANISOU 2648 CG PHE A 384 14290 20190 7856 -2880 1429 -1403 C ATOM 2649 CD1 PHE A 384 11.610 1.098 -34.358 1.00115.11 C ANISOU 2649 CD1 PHE A 384 14839 20595 8301 -3050 1458 -1429 C ATOM 2650 CD2 PHE A 384 9.449 1.359 -33.375 1.00114.08 C ANISOU 2650 CD2 PHE A 384 14785 20413 8148 -2632 1420 -1428 C ATOM 2651 CE1 PHE A 384 11.180 1.806 -35.488 1.00116.50 C ANISOU 2651 CE1 PHE A 384 15304 20555 8405 -2997 1474 -1452 C ATOM 2652 CE2 PHE A 384 9.017 2.055 -34.511 1.00117.39 C ANISOU 2652 CE2 PHE A 384 15479 20616 8507 -2532 1416 -1468 C ATOM 2653 CZ PHE A 384 9.886 2.274 -35.559 1.00115.71 C ANISOU 2653 CZ PHE A 384 15394 20302 8269 -2724 1441 -1467 C ATOM 2654 N ASP A 385 12.940 -2.566 -32.749 1.00 99.49 N ANISOU 2654 N ASP A 385 11888 19209 6705 -3063 1242 -1306 N ATOM 2655 CA ASP A 385 13.825 -3.323 -33.632 1.00 98.55 C ANISOU 2655 CA ASP A 385 11575 19187 6680 -3101 1190 -1348 C ATOM 2656 C ASP A 385 13.272 -4.716 -33.862 1.00100.18 C ANISOU 2656 C ASP A 385 11591 19423 7051 -2911 1071 -1260 C ATOM 2657 O ASP A 385 13.320 -5.172 -34.994 1.00 99.62 O ANISOU 2657 O ASP A 385 11444 19342 7067 -2847 1055 -1272 O ATOM 2658 CB ASP A 385 15.270 -3.407 -33.106 1.00101.33 C ANISOU 2658 CB ASP A 385 11785 19727 6989 -3280 1146 -1452 C ATOM 2659 CG ASP A 385 16.200 -2.314 -33.637 1.00111.60 C ANISOU 2659 CG ASP A 385 13201 21058 8143 -3533 1262 -1578 C ATOM 2660 OD1 ASP A 385 16.098 -1.970 -34.845 1.00110.39 O ANISOU 2660 OD1 ASP A 385 13145 20827 7970 -3569 1336 -1599 O ATOM 2661 OD2 ASP A 385 17.139 -1.947 -32.921 1.00120.74 O ANISOU 2661 OD2 ASP A 385 14323 22348 9205 -3715 1265 -1666 O ATOM 2662 N LEU A 386 12.706 -5.367 -32.830 1.00 95.83 N ANISOU 2662 N LEU A 386 10989 18898 6523 -2842 987 -1171 N ATOM 2663 CA LEU A 386 12.088 -6.695 -32.958 1.00 95.06 C ANISOU 2663 CA LEU A 386 10768 18804 6545 -2706 860 -1071 C ATOM 2664 C LEU A 386 10.894 -6.697 -33.949 1.00 98.34 C ANISOU 2664 C LEU A 386 11231 19117 7017 -2570 925 -1020 C ATOM 2665 O LEU A 386 10.685 -7.707 -34.633 1.00 97.05 O ANISOU 2665 O LEU A 386 10962 18944 6968 -2474 834 -973 O ATOM 2666 CB LEU A 386 11.601 -7.209 -31.589 1.00 95.42 C ANISOU 2666 CB LEU A 386 10817 18894 6545 -2727 781 -979 C ATOM 2667 CG LEU A 386 12.659 -7.732 -30.617 1.00101.01 C ANISOU 2667 CG LEU A 386 11459 19692 7230 -2807 634 -1000 C ATOM 2668 CD1 LEU A 386 12.110 -7.820 -29.216 1.00101.87 C ANISOU 2668 CD1 LEU A 386 11641 19829 7237 -2877 609 -915 C ATOM 2669 CD2 LEU A 386 13.232 -9.073 -31.076 1.00103.47 C ANISOU 2669 CD2 LEU A 386 11641 20019 7655 -2713 422 -998 C ATOM 2670 N PHE A 387 10.121 -5.574 -34.018 1.00 94.76 N ANISOU 2670 N PHE A 387 10947 18585 6473 -2544 1061 -1044 N ATOM 2671 CA PHE A 387 8.947 -5.431 -34.892 1.00 93.68 C ANISOU 2671 CA PHE A 387 10868 18362 6365 -2387 1113 -1027 C ATOM 2672 C PHE A 387 9.352 -5.437 -36.376 1.00 94.89 C ANISOU 2672 C PHE A 387 11030 18432 6591 -2354 1126 -1062 C ATOM 2673 O PHE A 387 8.725 -6.123 -37.180 1.00 93.47 O ANISOU 2673 O PHE A 387 10775 18228 6512 -2228 1090 -1018 O ATOM 2674 CB PHE A 387 8.169 -4.136 -34.571 1.00 96.65 C ANISOU 2674 CB PHE A 387 11449 18673 6602 -2331 1217 -1089 C ATOM 2675 CG PHE A 387 6.890 -3.989 -35.372 1.00 98.90 C ANISOU 2675 CG PHE A 387 11780 18897 6901 -2128 1244 -1104 C ATOM 2676 CD1 PHE A 387 5.700 -4.556 -34.926 1.00102.71 C ANISOU 2676 CD1 PHE A 387 12134 19503 7389 -2027 1229 -1074 C ATOM 2677 CD2 PHE A 387 6.881 -3.309 -36.587 1.00101.01 C ANISOU 2677 CD2 PHE A 387 12220 19000 7160 -2053 1277 -1156 C ATOM 2678 CE1 PHE A 387 4.525 -4.443 -35.678 1.00103.52 C ANISOU 2678 CE1 PHE A 387 12244 19591 7499 -1829 1246 -1117 C ATOM 2679 CE2 PHE A 387 5.705 -3.202 -37.339 1.00103.48 C ANISOU 2679 CE2 PHE A 387 12576 19258 7485 -1837 1279 -1184 C ATOM 2680 CZ PHE A 387 4.535 -3.765 -36.877 1.00101.69 C ANISOU 2680 CZ PHE A 387 12184 19179 7274 -1713 1263 -1174 C ATOM 2681 N LEU A 388 10.355 -4.631 -36.734 1.00 90.89 N ANISOU 2681 N LEU A 388 10626 17894 6013 -2490 1184 -1146 N ATOM 2682 CA LEU A 388 10.849 -4.512 -38.100 1.00 90.10 C ANISOU 2682 CA LEU A 388 10553 17745 5937 -2519 1215 -1195 C ATOM 2683 C LEU A 388 11.650 -5.751 -38.471 1.00 95.95 C ANISOU 2683 C LEU A 388 11026 18625 6806 -2520 1112 -1205 C ATOM 2684 O LEU A 388 11.480 -6.283 -39.560 1.00 94.57 O ANISOU 2684 O LEU A 388 10784 18426 6720 -2428 1088 -1199 O ATOM 2685 CB LEU A 388 11.704 -3.242 -38.238 1.00 90.74 C ANISOU 2685 CB LEU A 388 10846 17780 5852 -2734 1311 -1289 C ATOM 2686 CG LEU A 388 11.091 -1.918 -37.739 1.00 95.14 C ANISOU 2686 CG LEU A 388 11725 18174 6249 -2736 1376 -1303 C ATOM 2687 CD1 LEU A 388 12.090 -0.799 -37.839 1.00 96.49 C ANISOU 2687 CD1 LEU A 388 12122 18298 6240 -3005 1447 -1386 C ATOM 2688 CD2 LEU A 388 9.799 -1.555 -38.476 1.00 96.44 C ANISOU 2688 CD2 LEU A 388 12076 18158 6410 -2513 1381 -1283 C ATOM 2689 N SER A 389 12.473 -6.247 -37.526 1.00 95.74 N ANISOU 2689 N SER A 389 10851 18739 6784 -2594 1028 -1228 N ATOM 2690 CA SER A 389 13.312 -7.444 -37.655 1.00 96.80 C ANISOU 2690 CA SER A 389 10743 19014 7020 -2554 877 -1271 C ATOM 2691 C SER A 389 12.451 -8.718 -37.817 1.00101.22 C ANISOU 2691 C SER A 389 11224 19517 7719 -2361 739 -1157 C ATOM 2692 O SER A 389 12.958 -9.711 -38.337 1.00101.18 O ANISOU 2692 O SER A 389 11065 19572 7808 -2274 602 -1196 O ATOM 2693 CB SER A 389 14.230 -7.583 -36.437 1.00102.34 C ANISOU 2693 CB SER A 389 11360 19854 7672 -2647 793 -1324 C ATOM 2694 OG SER A 389 15.095 -8.706 -36.482 1.00113.78 O ANISOU 2694 OG SER A 389 12592 21440 9199 -2568 606 -1399 O ATOM 2695 N SER A 390 11.161 -8.690 -37.393 1.00 97.92 N ANISOU 2695 N SER A 390 10909 19000 7295 -2301 769 -1036 N ATOM 2696 CA SER A 390 10.280 -9.847 -37.552 1.00 97.51 C ANISOU 2696 CA SER A 390 10801 18908 7342 -2176 653 -927 C ATOM 2697 C SER A 390 9.798 -9.950 -38.998 1.00103.19 C ANISOU 2697 C SER A 390 11510 19552 8144 -2060 693 -931 C ATOM 2698 O SER A 390 10.109 -10.941 -39.663 1.00103.48 O ANISOU 2698 O SER A 390 11437 19596 8285 -1978 567 -936 O ATOM 2699 CB SER A 390 9.095 -9.787 -36.595 1.00100.29 C ANISOU 2699 CB SER A 390 11227 19250 7628 -2192 684 -826 C ATOM 2700 OG SER A 390 8.304 -8.634 -36.813 1.00108.77 O ANISOU 2700 OG SER A 390 12415 20282 8630 -2164 853 -858 O ATOM 2701 N PHE A 391 9.113 -8.899 -39.510 1.00100.29 N ANISOU 2701 N PHE A 391 11277 19107 7722 -2040 850 -948 N ATOM 2702 CA PHE A 391 8.572 -8.842 -40.881 1.00 99.97 C ANISOU 2702 CA PHE A 391 11268 18978 7738 -1926 893 -955 C ATOM 2703 C PHE A 391 9.683 -8.628 -41.950 1.00103.61 C ANISOU 2703 C PHE A 391 11708 19453 8206 -1983 920 -1056 C ATOM 2704 O PHE A 391 9.379 -8.198 -43.074 1.00103.09 O ANISOU 2704 O PHE A 391 11735 19300 8136 -1938 991 -1079 O ATOM 2705 CB PHE A 391 7.536 -7.701 -40.994 1.00102.22 C ANISOU 2705 CB PHE A 391 11744 19166 7930 -1866 1019 -967 C ATOM 2706 CG PHE A 391 6.237 -7.905 -40.249 1.00104.23 C ANISOU 2706 CG PHE A 391 11976 19462 8166 -1781 1012 -910 C ATOM 2707 CD1 PHE A 391 6.091 -7.463 -38.940 1.00108.71 C ANISOU 2707 CD1 PHE A 391 12578 20099 8628 -1854 1041 -914 C ATOM 2708 CD2 PHE A 391 5.146 -8.500 -40.872 1.00106.16 C ANISOU 2708 CD2 PHE A 391 12154 19704 8479 -1643 984 -872 C ATOM 2709 CE1 PHE A 391 4.883 -7.636 -38.256 1.00110.09 C ANISOU 2709 CE1 PHE A 391 12704 20371 8756 -1801 1049 -890 C ATOM 2710 CE2 PHE A 391 3.938 -8.672 -40.191 1.00109.80 C ANISOU 2710 CE2 PHE A 391 12561 20267 8892 -1600 991 -850 C ATOM 2711 CZ PHE A 391 3.812 -8.235 -38.888 1.00108.98 C ANISOU 2711 CZ PHE A 391 12477 20259 8671 -1684 1028 -865 C ATOM 2712 N GLN A 392 10.947 -8.966 -41.612 1.00 99.63 N ANISOU 2712 N GLN A 392 11072 19083 7701 -2081 855 -1131 N ATOM 2713 CA GLN A 392 12.125 -8.766 -42.461 1.00 99.46 C ANISOU 2713 CA GLN A 392 10976 19166 7650 -2178 888 -1268 C ATOM 2714 C GLN A 392 12.056 -9.680 -43.716 1.00100.56 C ANISOU 2714 C GLN A 392 10988 19310 7908 -2037 813 -1284 C ATOM 2715 O GLN A 392 12.041 -9.177 -44.843 1.00 98.98 O ANISOU 2715 O GLN A 392 10862 19073 7674 -2070 914 -1327 O ATOM 2716 CB GLN A 392 13.401 -9.053 -41.633 1.00101.98 C ANISOU 2716 CB GLN A 392 11131 19679 7938 -2276 805 -1372 C ATOM 2717 CG GLN A 392 14.666 -8.259 -42.022 1.00112.85 C ANISOU 2717 CG GLN A 392 12467 21224 9185 -2494 911 -1545 C ATOM 2718 CD GLN A 392 14.711 -6.809 -41.553 1.00122.45 C ANISOU 2718 CD GLN A 392 13920 22376 10228 -2717 1076 -1546 C ATOM 2719 OE1 GLN A 392 13.743 -6.032 -41.651 1.00117.27 O ANISOU 2719 OE1 GLN A 392 13523 21510 9524 -2704 1167 -1451 O ATOM 2720 NE2 GLN A 392 15.892 -6.383 -41.125 1.00107.84 N ANISOU 2720 NE2 GLN A 392 11992 20717 8263 -2926 1108 -1682 N ATOM 2721 N GLY A 393 11.944 -10.994 -43.488 1.00 96.40 N ANISOU 2721 N GLY A 393 10315 18805 7505 -1885 626 -1242 N ATOM 2722 CA GLY A 393 11.869 -12.020 -44.530 1.00 95.28 C ANISOU 2722 CA GLY A 393 10057 18660 7484 -1725 512 -1257 C ATOM 2723 C GLY A 393 10.591 -12.045 -45.358 1.00 96.89 C ANISOU 2723 C GLY A 393 10367 18701 7748 -1620 564 -1148 C ATOM 2724 O GLY A 393 10.542 -12.725 -46.387 1.00 96.84 O ANISOU 2724 O GLY A 393 10283 18685 7828 -1504 498 -1169 O ATOM 2725 N LEU A 394 9.529 -11.340 -44.905 1.00 91.18 N ANISOU 2725 N LEU A 394 9807 17865 6973 -1640 669 -1048 N ATOM 2726 CA LEU A 394 8.292 -11.207 -45.678 1.00 89.30 C ANISOU 2726 CA LEU A 394 9662 17501 6768 -1527 724 -981 C ATOM 2727 C LEU A 394 8.533 -10.338 -46.908 1.00 91.78 C ANISOU 2727 C LEU A 394 10084 17763 7026 -1553 848 -1059 C ATOM 2728 O LEU A 394 8.281 -10.762 -48.037 1.00 91.36 O ANISOU 2728 O LEU A 394 10000 17669 7043 -1452 824 -1063 O ATOM 2729 CB LEU A 394 7.151 -10.606 -44.824 1.00 89.18 C ANISOU 2729 CB LEU A 394 9768 17432 6684 -1520 793 -909 C ATOM 2730 CG LEU A 394 5.893 -10.159 -45.618 1.00 93.03 C ANISOU 2730 CG LEU A 394 10362 17818 7168 -1384 862 -893 C ATOM 2731 CD1 LEU A 394 5.133 -11.349 -46.191 1.00 92.22 C ANISOU 2731 CD1 LEU A 394 10136 17713 7189 -1261 759 -827 C ATOM 2732 CD2 LEU A 394 4.981 -9.298 -44.776 1.00 95.35 C ANISOU 2732 CD2 LEU A 394 10769 18106 7353 -1364 937 -894 C ATOM 2733 N LEU A 395 9.036 -9.117 -46.660 1.00 87.10 N ANISOU 2733 N LEU A 395 9644 17163 6288 -1711 971 -1119 N ATOM 2734 CA LEU A 395 9.295 -8.062 -47.629 1.00 86.26 C ANISOU 2734 CA LEU A 395 9735 16979 6060 -1811 1091 -1184 C ATOM 2735 C LEU A 395 10.351 -8.514 -48.677 1.00 90.22 C ANISOU 2735 C LEU A 395 10089 17613 6576 -1891 1086 -1285 C ATOM 2736 O LEU A 395 10.195 -8.146 -49.843 1.00 89.99 O ANISOU 2736 O LEU A 395 10187 17505 6502 -1902 1146 -1306 O ATOM 2737 CB LEU A 395 9.760 -6.811 -46.853 1.00 86.56 C ANISOU 2737 CB LEU A 395 9971 16997 5922 -2008 1189 -1223 C ATOM 2738 CG LEU A 395 10.001 -5.480 -47.568 1.00 90.44 C ANISOU 2738 CG LEU A 395 10784 17359 6220 -2175 1303 -1277 C ATOM 2739 CD1 LEU A 395 11.418 -5.302 -47.972 1.00 91.13 C ANISOU 2739 CD1 LEU A 395 10807 17614 6204 -2454 1365 -1388 C ATOM 2740 CD2 LEU A 395 8.917 -5.126 -48.576 1.00 91.01 C ANISOU 2740 CD2 LEU A 395 11082 17215 6282 -2008 1304 -1237 C ATOM 2741 N VAL A 396 11.367 -9.348 -48.296 1.00 86.00 N ANISOU 2741 N VAL A 396 9289 17290 6098 -1922 999 -1363 N ATOM 2742 CA VAL A 396 12.356 -9.843 -49.282 1.00 85.76 C ANISOU 2742 CA VAL A 396 9068 17443 6074 -1961 979 -1504 C ATOM 2743 C VAL A 396 11.652 -10.856 -50.223 1.00 86.55 C ANISOU 2743 C VAL A 396 9088 17468 6329 -1725 878 -1454 C ATOM 2744 O VAL A 396 11.819 -10.774 -51.449 1.00 86.13 O ANISOU 2744 O VAL A 396 9040 17438 6248 -1747 931 -1518 O ATOM 2745 CB VAL A 396 13.656 -10.453 -48.678 1.00 90.66 C ANISOU 2745 CB VAL A 396 9410 18338 6698 -2008 883 -1653 C ATOM 2746 CG1 VAL A 396 14.373 -9.454 -47.789 1.00 91.74 C ANISOU 2746 CG1 VAL A 396 9615 18568 6676 -2258 986 -1711 C ATOM 2747 CG2 VAL A 396 13.389 -11.746 -47.917 1.00 89.95 C ANISOU 2747 CG2 VAL A 396 9173 18234 6770 -1776 662 -1592 C ATOM 2748 N ALA A 397 10.827 -11.770 -49.638 1.00 79.90 N ANISOU 2748 N ALA A 397 8196 16533 5629 -1530 736 -1335 N ATOM 2749 CA ALA A 397 10.061 -12.776 -50.370 1.00 77.66 C ANISOU 2749 CA ALA A 397 7858 16163 5487 -1323 624 -1271 C ATOM 2750 C ALA A 397 9.120 -12.104 -51.358 1.00 79.19 C ANISOU 2750 C ALA A 397 8237 16198 5654 -1292 743 -1216 C ATOM 2751 O ALA A 397 8.950 -12.596 -52.469 1.00 77.94 O ANISOU 2751 O ALA A 397 8033 16020 5560 -1190 709 -1234 O ATOM 2752 CB ALA A 397 9.283 -13.652 -49.400 1.00 77.60 C ANISOU 2752 CB ALA A 397 7830 16080 5575 -1211 477 -1140 C ATOM 2753 N VAL A 398 8.577 -10.931 -50.980 1.00 75.15 N ANISOU 2753 N VAL A 398 7949 15573 5031 -1370 868 -1170 N ATOM 2754 CA VAL A 398 7.667 -10.148 -51.816 1.00 74.66 C ANISOU 2754 CA VAL A 398 8117 15338 4914 -1314 952 -1137 C ATOM 2755 C VAL A 398 8.475 -9.420 -52.944 1.00 78.77 C ANISOU 2755 C VAL A 398 8762 15865 5303 -1475 1055 -1234 C ATOM 2756 O VAL A 398 8.185 -9.646 -54.116 1.00 76.31 O ANISOU 2756 O VAL A 398 8474 15499 5020 -1394 1049 -1241 O ATOM 2757 CB VAL A 398 6.840 -9.146 -50.959 1.00 78.47 C ANISOU 2757 CB VAL A 398 8812 15700 5301 -1306 1012 -1088 C ATOM 2758 CG1 VAL A 398 6.016 -8.204 -51.831 1.00 78.68 C ANISOU 2758 CG1 VAL A 398 9123 15536 5237 -1222 1067 -1092 C ATOM 2759 CG2 VAL A 398 5.938 -9.881 -49.979 1.00 77.62 C ANISOU 2759 CG2 VAL A 398 8572 15626 5294 -1179 928 -1004 C ATOM 2760 N LEU A 399 9.479 -8.580 -52.585 1.00 78.03 N ANISOU 2760 N LEU A 399 8749 15852 5049 -1728 1149 -1312 N ATOM 2761 CA LEU A 399 10.270 -7.784 -53.537 1.00 79.74 C ANISOU 2761 CA LEU A 399 9118 16096 5082 -1969 1262 -1405 C ATOM 2762 C LEU A 399 10.956 -8.641 -54.641 1.00 86.56 C ANISOU 2762 C LEU A 399 9739 17151 5998 -1973 1241 -1506 C ATOM 2763 O LEU A 399 10.848 -8.294 -55.827 1.00 86.54 O ANISOU 2763 O LEU A 399 9893 17078 5909 -2030 1298 -1524 O ATOM 2764 CB LEU A 399 11.371 -6.958 -52.826 1.00 80.83 C ANISOU 2764 CB LEU A 399 9309 16362 5041 -2281 1354 -1488 C ATOM 2765 CG LEU A 399 10.984 -5.732 -51.977 1.00 84.80 C ANISOU 2765 CG LEU A 399 10145 16672 5402 -2372 1407 -1429 C ATOM 2766 CD1 LEU A 399 12.214 -5.104 -51.403 1.00 85.84 C ANISOU 2766 CD1 LEU A 399 10280 16972 5363 -2706 1491 -1527 C ATOM 2767 CD2 LEU A 399 10.279 -4.662 -52.804 1.00 87.82 C ANISOU 2767 CD2 LEU A 399 10972 16766 5628 -2391 1448 -1387 C ATOM 2768 N TYR A 400 11.692 -9.708 -54.260 1.00 84.49 N ANISOU 2768 N TYR A 400 9120 17130 5852 -1912 1146 -1589 N ATOM 2769 CA TYR A 400 12.418 -10.496 -55.255 1.00 85.22 C ANISOU 2769 CA TYR A 400 8965 17438 5976 -1892 1110 -1729 C ATOM 2770 C TYR A 400 11.588 -11.617 -55.882 1.00 89.19 C ANISOU 2770 C TYR A 400 9370 17839 6678 -1584 973 -1661 C ATOM 2771 O TYR A 400 11.784 -11.883 -57.064 1.00 89.51 O ANISOU 2771 O TYR A 400 9354 17949 6708 -1571 985 -1738 O ATOM 2772 CB TYR A 400 13.691 -11.146 -54.686 1.00 87.16 C ANISOU 2772 CB TYR A 400 8867 18016 6232 -1930 1035 -1905 C ATOM 2773 CG TYR A 400 14.856 -10.211 -54.431 1.00 90.77 C ANISOU 2773 CG TYR A 400 9318 18706 6466 -2281 1179 -2054 C ATOM 2774 CD1 TYR A 400 15.295 -9.331 -55.421 1.00 94.33 C ANISOU 2774 CD1 TYR A 400 9911 19232 6699 -2582 1350 -2136 C ATOM 2775 CD2 TYR A 400 15.678 -10.385 -53.320 1.00 92.16 C ANISOU 2775 CD2 TYR A 400 9296 19085 6635 -2323 1122 -2151 C ATOM 2776 CE1 TYR A 400 16.424 -8.533 -55.234 1.00 97.67 C ANISOU 2776 CE1 TYR A 400 10312 19910 6887 -2959 1483 -2290 C ATOM 2777 CE2 TYR A 400 16.821 -9.609 -53.133 1.00 94.98 C ANISOU 2777 CE2 TYR A 400 9598 19710 6779 -2660 1249 -2318 C ATOM 2778 CZ TYR A 400 17.191 -8.683 -54.093 1.00103.84 C ANISOU 2778 CZ TYR A 400 10876 20906 7674 -2994 1436 -2388 C ATOM 2779 OH TYR A 400 18.320 -7.923 -53.913 1.00105.75 O ANISOU 2779 OH TYR A 400 11068 21436 7676 -3380 1568 -2558 O ATOM 2780 N CYS A 401 10.730 -12.310 -55.121 1.00 85.55 N ANISOU 2780 N CYS A 401 8882 17243 6382 -1365 841 -1530 N ATOM 2781 CA CYS A 401 10.026 -13.474 -55.653 1.00 85.04 C ANISOU 2781 CA CYS A 401 8718 17102 6493 -1108 693 -1474 C ATOM 2782 C CYS A 401 8.615 -13.106 -56.181 1.00 89.74 C ANISOU 2782 C CYS A 401 9537 17447 7114 -1007 739 -1332 C ATOM 2783 O CYS A 401 8.382 -13.193 -57.389 1.00 89.25 O ANISOU 2783 O CYS A 401 9509 17341 7059 -948 755 -1352 O ATOM 2784 CB CYS A 401 9.932 -14.561 -54.588 1.00 85.03 C ANISOU 2784 CB CYS A 401 8571 17112 6626 -964 501 -1423 C ATOM 2785 SG CYS A 401 8.921 -15.981 -55.060 1.00 87.96 S ANISOU 2785 SG CYS A 401 8891 17342 7185 -696 300 -1321 S ATOM 2786 N PHE A 402 7.676 -12.773 -55.289 1.00 86.95 N ANISOU 2786 N PHE A 402 9308 16957 6772 -967 744 -1211 N ATOM 2787 CA PHE A 402 6.282 -12.551 -55.663 1.00 86.82 C ANISOU 2787 CA PHE A 402 9446 16756 6784 -825 754 -1113 C ATOM 2788 C PHE A 402 6.062 -11.241 -56.495 1.00 92.19 C ANISOU 2788 C PHE A 402 10417 17302 7309 -889 886 -1139 C ATOM 2789 O PHE A 402 4.967 -11.077 -57.038 1.00 91.46 O ANISOU 2789 O PHE A 402 10451 17066 7234 -733 873 -1093 O ATOM 2790 CB PHE A 402 5.392 -12.494 -54.401 1.00 88.63 C ANISOU 2790 CB PHE A 402 9700 16943 7033 -780 730 -1019 C ATOM 2791 CG PHE A 402 5.512 -13.694 -53.481 1.00 90.19 C ANISOU 2791 CG PHE A 402 9697 17231 7341 -759 588 -971 C ATOM 2792 CD1 PHE A 402 4.937 -14.913 -53.819 1.00 93.06 C ANISOU 2792 CD1 PHE A 402 9951 17574 7833 -628 448 -914 C ATOM 2793 CD2 PHE A 402 6.113 -13.578 -52.236 1.00 92.52 C ANISOU 2793 CD2 PHE A 402 9956 17606 7590 -877 581 -972 C ATOM 2794 CE1 PHE A 402 5.052 -16.019 -52.970 1.00 93.85 C ANISOU 2794 CE1 PHE A 402 9941 17716 8001 -630 286 -861 C ATOM 2795 CE2 PHE A 402 6.227 -14.683 -51.388 1.00 95.18 C ANISOU 2795 CE2 PHE A 402 10165 17996 8004 -861 423 -923 C ATOM 2796 CZ PHE A 402 5.690 -15.894 -51.757 1.00 92.92 C ANISOU 2796 CZ PHE A 402 9807 17668 7830 -743 270 -864 C ATOM 2797 N LEU A 403 7.074 -10.347 -56.627 1.00 90.53 N ANISOU 2797 N LEU A 403 10329 17137 6932 -1121 995 -1219 N ATOM 2798 CA LEU A 403 6.894 -9.086 -57.370 1.00 91.33 C ANISOU 2798 CA LEU A 403 10787 17069 6846 -1219 1092 -1231 C ATOM 2799 C LEU A 403 7.582 -9.108 -58.742 1.00 96.10 C ANISOU 2799 C LEU A 403 11414 17729 7370 -1344 1141 -1309 C ATOM 2800 O LEU A 403 7.364 -8.188 -59.538 1.00 96.84 O ANISOU 2800 O LEU A 403 11839 17655 7300 -1424 1197 -1308 O ATOM 2801 CB LEU A 403 7.433 -7.897 -56.562 1.00 92.67 C ANISOU 2801 CB LEU A 403 11173 17210 6826 -1448 1183 -1254 C ATOM 2802 CG LEU A 403 6.413 -6.809 -56.182 1.00 97.59 C ANISOU 2802 CG LEU A 403 12148 17584 7347 -1352 1181 -1203 C ATOM 2803 CD1 LEU A 403 5.180 -7.395 -55.490 1.00 96.33 C ANISOU 2803 CD1 LEU A 403 11839 17408 7354 -1059 1092 -1140 C ATOM 2804 CD2 LEU A 403 7.056 -5.743 -55.306 1.00100.76 C ANISOU 2804 CD2 LEU A 403 12751 17966 7568 -1587 1252 -1231 C ATOM 2805 N ASN A 404 8.363 -10.160 -59.042 1.00 92.99 N ANISOU 2805 N ASN A 404 10689 17566 7076 -1347 1103 -1387 N ATOM 2806 CA ASN A 404 9.038 -10.277 -60.338 1.00 93.98 C ANISOU 2806 CA ASN A 404 10779 17806 7121 -1461 1151 -1490 C ATOM 2807 C ASN A 404 8.021 -10.736 -61.387 1.00 96.48 C ANISOU 2807 C ASN A 404 11155 17960 7541 -1223 1083 -1427 C ATOM 2808 O ASN A 404 7.280 -11.690 -61.154 1.00 94.75 O ANISOU 2808 O ASN A 404 10769 17706 7527 -963 961 -1362 O ATOM 2809 CB ASN A 404 10.235 -11.224 -60.247 1.00 96.42 C ANISOU 2809 CB ASN A 404 10695 18451 7489 -1505 1112 -1638 C ATOM 2810 CG ASN A 404 11.165 -11.208 -61.437 1.00125.75 C ANISOU 2810 CG ASN A 404 14329 22384 11066 -1688 1192 -1799 C ATOM 2811 OD1 ASN A 404 10.990 -10.452 -62.401 1.00119.63 O ANISOU 2811 OD1 ASN A 404 13826 21500 10129 -1837 1291 -1786 O ATOM 2812 ND2 ASN A 404 12.233 -11.988 -61.348 1.00123.07 N ANISOU 2812 ND2 ASN A 404 13625 22379 10758 -1698 1146 -1975 N ATOM 2813 N LYS A 405 7.970 -10.029 -62.524 1.00 93.69 N ANISOU 2813 N LYS A 405 11069 17504 7026 -1335 1157 -1444 N ATOM 2814 CA LYS A 405 6.976 -10.246 -63.573 1.00 92.61 C ANISOU 2814 CA LYS A 405 11053 17184 6949 -1123 1099 -1387 C ATOM 2815 C LYS A 405 7.191 -11.590 -64.329 1.00 92.53 C ANISOU 2815 C LYS A 405 10707 17345 7105 -978 1022 -1447 C ATOM 2816 O LYS A 405 6.195 -12.189 -64.742 1.00 90.67 O ANISOU 2816 O LYS A 405 10449 16983 7018 -718 924 -1378 O ATOM 2817 CB LYS A 405 6.969 -9.080 -64.584 1.00 97.77 C ANISOU 2817 CB LYS A 405 12135 17664 7347 -1310 1182 -1394 C ATOM 2818 CG LYS A 405 6.552 -7.735 -63.930 1.00119.15 C ANISOU 2818 CG LYS A 405 15262 20125 9884 -1387 1205 -1333 C ATOM 2819 CD LYS A 405 6.168 -6.585 -64.904 1.00131.55 C ANISOU 2819 CD LYS A 405 17373 21406 11206 -1475 1212 -1311 C ATOM 2820 CE LYS A 405 7.268 -6.057 -65.803 1.00142.64 C ANISOU 2820 CE LYS A 405 18964 22894 12338 -1892 1330 -1381 C ATOM 2821 NZ LYS A 405 6.791 -4.929 -66.646 1.00150.20 N ANISOU 2821 NZ LYS A 405 20525 23508 13035 -1972 1299 -1338 N ATOM 2822 N GLU A 406 8.433 -12.080 -64.484 1.00 88.14 N ANISOU 2822 N GLU A 406 9884 17084 6521 -1122 1049 -1590 N ATOM 2823 CA GLU A 406 8.617 -13.359 -65.181 1.00 87.11 C ANISOU 2823 CA GLU A 406 9451 17104 6542 -940 945 -1668 C ATOM 2824 C GLU A 406 8.387 -14.527 -64.195 1.00 88.80 C ANISOU 2824 C GLU A 406 9400 17348 6992 -697 772 -1630 C ATOM 2825 O GLU A 406 8.140 -15.652 -64.623 1.00 86.68 O ANISOU 2825 O GLU A 406 8959 17094 6881 -477 632 -1642 O ATOM 2826 CB GLU A 406 9.995 -13.476 -65.876 1.00 90.43 C ANISOU 2826 CB GLU A 406 9673 17864 6821 -1150 1020 -1881 C ATOM 2827 CG GLU A 406 11.234 -13.272 -65.015 1.00105.99 C ANISOU 2827 CG GLU A 406 11455 20125 8691 -1367 1076 -2021 C ATOM 2828 CD GLU A 406 12.563 -13.397 -65.750 1.00138.54 C ANISOU 2828 CD GLU A 406 15333 24656 12651 -1575 1155 -2276 C ATOM 2829 OE1 GLU A 406 12.652 -14.195 -66.712 1.00141.00 O ANISOU 2829 OE1 GLU A 406 15466 25088 13020 -1428 1091 -2378 O ATOM 2830 OE2 GLU A 406 13.538 -12.745 -65.312 1.00138.41 O ANISOU 2830 OE2 GLU A 406 15272 24873 12447 -1881 1273 -2395 O ATOM 2831 N VAL A 407 8.396 -14.244 -62.895 1.00 87.28 N ANISOU 2831 N VAL A 407 9219 17136 6809 -745 772 -1574 N ATOM 2832 CA VAL A 407 8.131 -15.254 -61.863 1.00 87.44 C ANISOU 2832 CA VAL A 407 9058 17153 7011 -564 606 -1517 C ATOM 2833 C VAL A 407 6.574 -15.456 -61.778 1.00 91.99 C ANISOU 2833 C VAL A 407 9769 17478 7706 -375 542 -1341 C ATOM 2834 O VAL A 407 6.101 -16.598 -61.813 1.00 91.77 O ANISOU 2834 O VAL A 407 9615 17420 7835 -191 384 -1299 O ATOM 2835 CB VAL A 407 8.782 -14.859 -60.495 1.00 91.42 C ANISOU 2835 CB VAL A 407 9522 17756 7459 -709 634 -1534 C ATOM 2836 CG1 VAL A 407 8.436 -15.861 -59.396 1.00 90.10 C ANISOU 2836 CG1 VAL A 407 9229 17554 7451 -548 454 -1455 C ATOM 2837 CG2 VAL A 407 10.298 -14.737 -60.636 1.00 92.74 C ANISOU 2837 CG2 VAL A 407 9510 18225 7503 -889 689 -1740 C ATOM 2838 N GLN A 408 5.805 -14.340 -61.736 1.00 88.00 N ANISOU 2838 N GLN A 408 9526 16805 7104 -423 653 -1263 N ATOM 2839 CA GLN A 408 4.332 -14.311 -61.715 1.00 86.48 C ANISOU 2839 CA GLN A 408 9451 16430 6979 -250 613 -1148 C ATOM 2840 C GLN A 408 3.710 -15.074 -62.911 1.00 87.55 C ANISOU 2840 C GLN A 408 9541 16507 7216 -70 530 -1139 C ATOM 2841 O GLN A 408 2.715 -15.775 -62.742 1.00 85.18 O ANISOU 2841 O GLN A 408 9174 16154 7038 85 430 -1065 O ATOM 2842 CB GLN A 408 3.840 -12.844 -61.751 1.00 88.76 C ANISOU 2842 CB GLN A 408 10061 16564 7102 -307 729 -1131 C ATOM 2843 CG GLN A 408 4.309 -11.955 -60.585 1.00111.05 C ANISOU 2843 CG GLN A 408 12979 19407 9807 -477 809 -1134 C ATOM 2844 CD GLN A 408 3.917 -10.488 -60.737 1.00135.77 C ANISOU 2844 CD GLN A 408 16486 22353 12747 -525 890 -1136 C ATOM 2845 OE1 GLN A 408 3.066 -10.111 -61.554 1.00133.82 O ANISOU 2845 OE1 GLN A 408 16441 21942 12463 -382 866 -1126 O ATOM 2846 NE2 GLN A 408 4.511 -9.625 -59.925 1.00127.67 N ANISOU 2846 NE2 GLN A 408 15588 21334 11586 -713 965 -1154 N ATOM 2847 N SER A 409 4.307 -14.914 -64.114 1.00 84.69 N ANISOU 2847 N SER A 409 9221 16173 6783 -120 580 -1223 N ATOM 2848 CA SER A 409 3.843 -15.483 -65.382 1.00 84.13 C ANISOU 2848 CA SER A 409 9136 16049 6778 29 520 -1231 C ATOM 2849 C SER A 409 4.032 -17.004 -65.451 1.00 86.06 C ANISOU 2849 C SER A 409 9106 16393 7201 165 357 -1252 C ATOM 2850 O SER A 409 3.073 -17.707 -65.757 1.00 84.93 O ANISOU 2850 O SER A 409 8937 16156 7177 336 251 -1184 O ATOM 2851 CB SER A 409 4.576 -14.843 -66.560 1.00 89.82 C ANISOU 2851 CB SER A 409 9986 16805 7337 -114 629 -1327 C ATOM 2852 OG SER A 409 5.958 -15.164 -66.576 1.00101.71 O ANISOU 2852 OG SER A 409 11290 18558 8798 -264 656 -1460 O ATOM 2853 N GLU A 410 5.267 -17.511 -65.223 1.00 82.40 N ANISOU 2853 N GLU A 410 8449 16121 6738 99 319 -1363 N ATOM 2854 CA GLU A 410 5.554 -18.951 -65.304 1.00 81.79 C ANISOU 2854 CA GLU A 410 8152 16120 6806 259 120 -1411 C ATOM 2855 C GLU A 410 4.683 -19.713 -64.291 1.00 81.27 C ANISOU 2855 C GLU A 410 8077 15933 6870 356 -31 -1271 C ATOM 2856 O GLU A 410 4.251 -20.843 -64.542 1.00 79.09 O ANISOU 2856 O GLU A 410 7742 15595 6713 505 -209 -1238 O ATOM 2857 CB GLU A 410 7.053 -19.224 -65.071 1.00 84.94 C ANISOU 2857 CB GLU A 410 8349 16770 7156 195 90 -1592 C ATOM 2858 CG GLU A 410 7.460 -20.691 -65.214 1.00 99.92 C ANISOU 2858 CG GLU A 410 10046 18740 9179 407 -158 -1686 C ATOM 2859 CD GLU A 410 7.177 -21.370 -66.546 1.00129.69 C ANISOU 2859 CD GLU A 410 13783 22482 13011 572 -237 -1734 C ATOM 2860 OE1 GLU A 410 7.290 -20.708 -67.606 1.00119.40 O ANISOU 2860 OE1 GLU A 410 12523 21237 11609 490 -78 -1795 O ATOM 2861 OE2 GLU A 410 6.898 -22.591 -66.526 1.00131.48 O ANISOU 2861 OE2 GLU A 410 13959 22628 13371 772 -472 -1717 O ATOM 2862 N LEU A 411 4.383 -19.049 -63.182 1.00 77.49 N ANISOU 2862 N LEU A 411 7680 15420 6344 246 45 -1188 N ATOM 2863 CA LEU A 411 3.516 -19.558 -62.139 1.00 76.36 C ANISOU 2863 CA LEU A 411 7546 15197 6271 268 -54 -1056 C ATOM 2864 C LEU A 411 2.081 -19.744 -62.704 1.00 78.90 C ANISOU 2864 C LEU A 411 7935 15395 6648 373 -71 -964 C ATOM 2865 O LEU A 411 1.550 -20.850 -62.624 1.00 78.19 O ANISOU 2865 O LEU A 411 7794 15263 6652 439 -234 -903 O ATOM 2866 CB LEU A 411 3.553 -18.576 -60.951 1.00 75.96 C ANISOU 2866 CB LEU A 411 7567 15168 6124 119 71 -1018 C ATOM 2867 CG LEU A 411 2.917 -19.011 -59.651 1.00 79.83 C ANISOU 2867 CG LEU A 411 8049 15637 6645 81 -10 -907 C ATOM 2868 CD1 LEU A 411 3.701 -20.147 -59.012 1.00 80.34 C ANISOU 2868 CD1 LEU A 411 8013 15745 6767 84 -208 -919 C ATOM 2869 CD2 LEU A 411 2.881 -17.863 -58.691 1.00 82.92 C ANISOU 2869 CD2 LEU A 411 8524 16054 6928 -46 140 -890 C ATOM 2870 N ARG A 412 1.506 -18.703 -63.365 1.00 74.91 N ANISOU 2870 N ARG A 412 7560 14831 6070 390 76 -971 N ATOM 2871 CA ARG A 412 0.161 -18.814 -63.945 1.00 74.76 C ANISOU 2871 CA ARG A 412 7588 14727 6092 516 54 -919 C ATOM 2872 C ARG A 412 0.190 -19.752 -65.169 1.00 80.57 C ANISOU 2872 C ARG A 412 8261 15432 6920 638 -57 -948 C ATOM 2873 O ARG A 412 -0.833 -20.368 -65.454 1.00 80.11 O ANISOU 2873 O ARG A 412 8178 15327 6933 729 -142 -895 O ATOM 2874 CB ARG A 412 -0.459 -17.441 -64.324 1.00 74.88 C ANISOU 2874 CB ARG A 412 7794 14669 5990 550 195 -942 C ATOM 2875 CG ARG A 412 0.259 -16.649 -65.415 1.00 89.59 C ANISOU 2875 CG ARG A 412 9810 16479 7751 524 289 -1019 C ATOM 2876 CD ARG A 412 -0.341 -15.281 -65.719 1.00109.54 C ANISOU 2876 CD ARG A 412 12609 18879 10133 559 383 -1036 C ATOM 2877 NE ARG A 412 -0.224 -14.334 -64.605 1.00131.86 N ANISOU 2877 NE ARG A 412 15542 21704 12853 458 460 -1032 N ATOM 2878 CZ ARG A 412 -1.202 -14.052 -63.748 1.00158.11 C ANISOU 2878 CZ ARG A 412 18869 25032 16174 542 447 -1011 C ATOM 2879 NH1 ARG A 412 -1.001 -13.184 -62.764 1.00149.36 N ANISOU 2879 NH1 ARG A 412 17864 23925 14962 452 514 -1020 N ATOM 2880 NH2 ARG A 412 -2.392 -14.631 -63.872 1.00151.67 N ANISOU 2880 NH2 ARG A 412 17941 24243 15444 707 367 -998 N ATOM 2881 N ARG A 413 1.354 -19.903 -65.854 1.00 78.65 N ANISOU 2881 N ARG A 413 7974 15244 6666 631 -60 -1046 N ATOM 2882 CA ARG A 413 1.453 -20.810 -67.002 1.00 79.11 C ANISOU 2882 CA ARG A 413 7962 15292 6805 761 -172 -1095 C ATOM 2883 C ARG A 413 1.221 -22.245 -66.597 1.00 84.58 C ANISOU 2883 C ARG A 413 8553 15959 7625 836 -396 -1045 C ATOM 2884 O ARG A 413 0.319 -22.882 -67.127 1.00 83.94 O ANISOU 2884 O ARG A 413 8483 15794 7616 931 -488 -992 O ATOM 2885 CB ARG A 413 2.804 -20.723 -67.715 1.00 81.23 C ANISOU 2885 CB ARG A 413 8163 15689 7014 730 -134 -1246 C ATOM 2886 CG ARG A 413 3.036 -19.482 -68.556 1.00 97.88 C ANISOU 2886 CG ARG A 413 10417 17804 8969 631 62 -1302 C ATOM 2887 CD ARG A 413 4.339 -19.573 -69.355 1.00117.71 C ANISOU 2887 CD ARG A 413 12819 20503 11403 568 97 -1473 C ATOM 2888 NE ARG A 413 4.326 -20.623 -70.390 1.00132.46 N ANISOU 2888 NE ARG A 413 14571 22394 13364 742 -36 -1540 N ATOM 2889 CZ ARG A 413 4.852 -21.843 -70.257 1.00145.94 C ANISOU 2889 CZ ARG A 413 16078 24194 15178 876 -226 -1622 C ATOM 2890 NH1 ARG A 413 5.465 -22.192 -69.131 1.00122.14 N ANISOU 2890 NH1 ARG A 413 12956 21262 12189 857 -313 -1650 N ATOM 2891 NH2 ARG A 413 4.794 -22.709 -71.259 1.00138.81 N ANISOU 2891 NH2 ARG A 413 15103 23295 14345 1044 -349 -1690 N ATOM 2892 N ARG A 414 1.998 -22.740 -65.626 1.00 83.77 N ANISOU 2892 N ARG A 414 8381 15914 7532 785 -497 -1059 N ATOM 2893 CA ARG A 414 1.927 -24.125 -65.171 1.00 84.77 C ANISOU 2893 CA ARG A 414 8480 15981 7747 843 -752 -1015 C ATOM 2894 C ARG A 414 0.631 -24.372 -64.365 1.00 87.78 C ANISOU 2894 C ARG A 414 8938 16275 8140 749 -786 -850 C ATOM 2895 O ARG A 414 0.271 -25.531 -64.172 1.00 88.17 O ANISOU 2895 O ARG A 414 9022 16240 8240 760 -998 -785 O ATOM 2896 CB ARG A 414 3.167 -24.470 -64.330 1.00 87.65 C ANISOU 2896 CB ARG A 414 8781 16429 8093 827 -865 -1097 C ATOM 2897 CG ARG A 414 3.415 -25.971 -64.187 1.00105.78 C ANISOU 2897 CG ARG A 414 11088 18642 10460 953 -1189 -1110 C ATOM 2898 CD ARG A 414 4.778 -26.279 -63.592 1.00126.82 C ANISOU 2898 CD ARG A 414 13675 21414 13098 1011 -1326 -1254 C ATOM 2899 NE ARG A 414 5.873 -25.772 -64.428 1.00141.43 N ANISOU 2899 NE ARG A 414 15354 23475 14906 1083 -1216 -1471 N ATOM 2900 CZ ARG A 414 7.163 -25.974 -64.174 1.00160.81 C ANISOU 2900 CZ ARG A 414 17672 26106 17322 1162 -1316 -1668 C ATOM 2901 NH1 ARG A 414 7.535 -26.708 -63.132 1.00152.76 N ANISOU 2901 NH1 ARG A 414 16697 25034 16312 1220 -1560 -1669 N ATOM 2902 NH2 ARG A 414 8.090 -25.473 -64.980 1.00147.11 N ANISOU 2902 NH2 ARG A 414 15759 24616 15521 1179 -1187 -1880 N ATOM 2903 N TRP A 415 -0.095 -23.303 -63.953 1.00 83.00 N ANISOU 2903 N TRP A 415 8368 15702 7468 656 -590 -797 N ATOM 2904 CA TRP A 415 -1.344 -23.467 -63.209 1.00 82.92 C ANISOU 2904 CA TRP A 415 8381 15685 7439 558 -598 -683 C ATOM 2905 C TRP A 415 -2.436 -23.953 -64.146 1.00 84.81 C ANISOU 2905 C TRP A 415 8616 15879 7728 640 -649 -659 C ATOM 2906 O TRP A 415 -3.162 -24.882 -63.794 1.00 84.31 O ANISOU 2906 O TRP A 415 8558 15798 7679 558 -783 -576 O ATOM 2907 CB TRP A 415 -1.766 -22.164 -62.502 1.00 82.26 C ANISOU 2907 CB TRP A 415 8317 15678 7258 478 -392 -678 C ATOM 2908 CG TRP A 415 -2.987 -22.318 -61.634 1.00 84.48 C ANISOU 2908 CG TRP A 415 8577 16027 7495 365 -391 -599 C ATOM 2909 CD1 TRP A 415 -3.054 -22.944 -60.424 1.00 88.29 C ANISOU 2909 CD1 TRP A 415 9058 16546 7943 189 -480 -516 C ATOM 2910 CD2 TRP A 415 -4.285 -21.738 -61.859 1.00 84.86 C ANISOU 2910 CD2 TRP A 415 8596 16150 7498 410 -290 -622 C ATOM 2911 NE1 TRP A 415 -4.332 -22.853 -59.911 1.00 88.58 N ANISOU 2911 NE1 TRP A 415 9047 16700 7908 86 -426 -483 N ATOM 2912 CE2 TRP A 415 -5.103 -22.103 -60.762 1.00 89.86 C ANISOU 2912 CE2 TRP A 415 9171 16905 8067 237 -310 -562 C ATOM 2913 CE3 TRP A 415 -4.846 -20.961 -62.891 1.00 86.10 C ANISOU 2913 CE3 TRP A 415 8777 16291 7645 584 -199 -701 C ATOM 2914 CZ2 TRP A 415 -6.448 -21.714 -60.665 1.00 89.83 C ANISOU 2914 CZ2 TRP A 415 9082 17058 7991 242 -232 -607 C ATOM 2915 CZ3 TRP A 415 -6.180 -20.579 -62.794 1.00 88.13 C ANISOU 2915 CZ3 TRP A 415 8977 16666 7843 626 -148 -742 C ATOM 2916 CH2 TRP A 415 -6.965 -20.954 -61.693 1.00 89.75 C ANISOU 2916 CH2 TRP A 415 9075 17039 7986 461 -159 -708 C ATOM 2917 N HIS A 416 -2.511 -23.358 -65.359 1.00 80.34 N ANISOU 2917 N HIS A 416 8058 15295 7173 781 -552 -733 N ATOM 2918 CA HIS A 416 -3.495 -23.693 -66.393 1.00 79.13 C ANISOU 2918 CA HIS A 416 7898 15102 7064 889 -590 -732 C ATOM 2919 C HIS A 416 -3.147 -24.999 -67.069 1.00 78.17 C ANISOU 2919 C HIS A 416 7765 14899 7036 958 -795 -732 C ATOM 2920 O HIS A 416 -4.056 -25.708 -67.495 1.00 77.33 O ANISOU 2920 O HIS A 416 7655 14758 6970 977 -893 -691 O ATOM 2921 CB HIS A 416 -3.586 -22.581 -67.432 1.00 80.27 C ANISOU 2921 CB HIS A 416 8102 15229 7167 1018 -438 -813 C ATOM 2922 CG HIS A 416 -4.052 -21.284 -66.856 1.00 84.83 C ANISOU 2922 CG HIS A 416 8740 15852 7640 992 -276 -828 C ATOM 2923 ND1 HIS A 416 -3.154 -20.331 -66.402 1.00 87.26 N ANISOU 2923 ND1 HIS A 416 9125 16166 7866 923 -158 -860 N ATOM 2924 CD2 HIS A 416 -5.311 -20.839 -66.635 1.00 87.74 C ANISOU 2924 CD2 HIS A 416 9098 16278 7961 1034 -234 -835 C ATOM 2925 CE1 HIS A 416 -3.890 -19.334 -65.936 1.00 87.36 C ANISOU 2925 CE1 HIS A 416 9203 16200 7788 937 -59 -874 C ATOM 2926 NE2 HIS A 416 -5.195 -19.590 -66.062 1.00 87.97 N ANISOU 2926 NE2 HIS A 416 9219 16323 7883 1023 -103 -874 N ATOM 2927 N ARG A 417 -1.838 -25.328 -67.148 1.00 72.50 N ANISOU 2927 N ARG A 417 7037 14167 6341 1001 -872 -796 N ATOM 2928 CA ARG A 417 -1.331 -26.569 -67.750 1.00 72.04 C ANISOU 2928 CA ARG A 417 6975 14037 6362 1114 -1101 -836 C ATOM 2929 C ARG A 417 -1.674 -27.756 -66.840 1.00 75.17 C ANISOU 2929 C ARG A 417 7442 14345 6773 1015 -1334 -730 C ATOM 2930 O ARG A 417 -2.082 -28.811 -67.334 1.00 74.43 O ANISOU 2930 O ARG A 417 7405 14146 6728 1063 -1529 -701 O ATOM 2931 CB ARG A 417 0.186 -26.484 -68.015 1.00 72.00 C ANISOU 2931 CB ARG A 417 6905 14104 6348 1202 -1114 -984 C ATOM 2932 CG ARG A 417 0.582 -25.308 -68.919 1.00 82.40 C ANISOU 2932 CG ARG A 417 8189 15515 7606 1228 -881 -1085 C ATOM 2933 CD ARG A 417 2.064 -25.272 -69.248 1.00 91.37 C ANISOU 2933 CD ARG A 417 9223 16790 8704 1274 -882 -1260 C ATOM 2934 NE ARG A 417 2.410 -26.187 -70.337 1.00 88.98 N ANISOU 2934 NE ARG A 417 8858 16494 8458 1454 -1040 -1373 N ATOM 2935 CZ ARG A 417 2.656 -25.804 -71.586 1.00 88.76 C ANISOU 2935 CZ ARG A 417 8795 16539 8389 1506 -932 -1478 C ATOM 2936 NH1 ARG A 417 2.933 -26.704 -72.520 1.00 77.97 N ANISOU 2936 NH1 ARG A 417 7362 15187 7074 1680 -1089 -1588 N ATOM 2937 NH2 ARG A 417 2.625 -24.517 -71.911 1.00 60.96 N ANISOU 2937 NH2 ARG A 417 5333 13067 4760 1378 -679 -1477 N ATOM 2938 N TRP A 418 -1.557 -27.549 -65.508 1.00 71.96 N ANISOU 2938 N TRP A 418 7063 13973 6305 853 -1314 -665 N ATOM 2939 CA TRP A 418 -1.928 -28.517 -64.477 1.00 73.05 C ANISOU 2939 CA TRP A 418 7315 14031 6410 691 -1513 -546 C ATOM 2940 C TRP A 418 -3.417 -28.742 -64.512 1.00 73.56 C ANISOU 2940 C TRP A 418 7398 14105 6446 548 -1487 -442 C ATOM 2941 O TRP A 418 -3.870 -29.887 -64.501 1.00 74.06 O ANISOU 2941 O TRP A 418 7577 14060 6505 465 -1704 -366 O ATOM 2942 CB TRP A 418 -1.484 -28.027 -63.091 1.00 73.32 C ANISOU 2942 CB TRP A 418 7362 14130 6367 542 -1450 -511 C ATOM 2943 CG TRP A 418 -1.774 -28.989 -61.975 1.00 77.01 C ANISOU 2943 CG TRP A 418 7985 14507 6768 345 -1660 -385 C ATOM 2944 CD1 TRP A 418 -2.860 -28.990 -61.148 1.00 80.48 C ANISOU 2944 CD1 TRP A 418 8463 15002 7115 85 -1604 -262 C ATOM 2945 CD2 TRP A 418 -0.963 -30.108 -61.579 1.00 78.81 C ANISOU 2945 CD2 TRP A 418 8376 14577 6993 385 -1980 -383 C ATOM 2946 NE1 TRP A 418 -2.768 -30.028 -60.247 1.00 81.98 N ANISOU 2946 NE1 TRP A 418 8853 15068 7230 -86 -1854 -160 N ATOM 2947 CE2 TRP A 418 -1.620 -30.738 -60.499 1.00 84.40 C ANISOU 2947 CE2 TRP A 418 9261 15214 7592 112 -2107 -228 C ATOM 2948 CE3 TRP A 418 0.277 -30.623 -62.014 1.00 81.05 C ANISOU 2948 CE3 TRP A 418 8673 14789 7333 633 -2184 -519 C ATOM 2949 CZ2 TRP A 418 -1.095 -31.874 -59.867 1.00 85.76 C ANISOU 2949 CZ2 TRP A 418 9684 15189 7710 79 -2453 -182 C ATOM 2950 CZ3 TRP A 418 0.800 -31.739 -61.379 1.00 84.44 C ANISOU 2950 CZ3 TRP A 418 9314 15046 7722 650 -2535 -501 C ATOM 2951 CH2 TRP A 418 0.118 -32.356 -60.323 1.00 86.48 C ANISOU 2951 CH2 TRP A 418 9807 15181 7872 376 -2677 -323 C ATOM 2952 N ARG A 419 -4.182 -27.632 -64.565 1.00 66.79 N ANISOU 2952 N ARG A 419 6435 13388 5553 520 -1233 -455 N ATOM 2953 CA ARG A 419 -5.632 -27.637 -64.669 1.00 65.78 C ANISOU 2953 CA ARG A 419 6259 13349 5384 419 -1172 -413 C ATOM 2954 C ARG A 419 -6.063 -28.386 -65.927 1.00 67.11 C ANISOU 2954 C ARG A 419 6440 13431 5628 536 -1293 -429 C ATOM 2955 O ARG A 419 -6.972 -29.216 -65.850 1.00 67.90 O ANISOU 2955 O ARG A 419 6571 13533 5694 384 -1405 -361 O ATOM 2956 CB ARG A 419 -6.183 -26.209 -64.671 1.00 66.24 C ANISOU 2956 CB ARG A 419 6208 13565 5395 473 -909 -482 C ATOM 2957 CG ARG A 419 -6.099 -25.476 -63.335 1.00 75.73 C ANISOU 2957 CG ARG A 419 7391 14881 6501 327 -786 -465 C ATOM 2958 CD ARG A 419 -6.805 -24.128 -63.410 1.00 90.71 C ANISOU 2958 CD ARG A 419 9209 16920 8338 417 -570 -554 C ATOM 2959 NE ARG A 419 -8.206 -24.265 -63.831 1.00106.39 N ANISOU 2959 NE ARG A 419 11096 19033 10293 426 -560 -589 N ATOM 2960 CZ ARG A 419 -9.223 -24.485 -63.004 1.00129.96 C ANISOU 2960 CZ ARG A 419 13982 22220 13177 231 -544 -578 C ATOM 2961 NH1 ARG A 419 -9.019 -24.567 -61.695 1.00125.22 N ANISOU 2961 NH1 ARG A 419 13392 21693 12494 9 -532 -516 N ATOM 2962 NH2 ARG A 419 -10.454 -24.616 -63.479 1.00119.07 N ANISOU 2962 NH2 ARG A 419 12481 20996 11763 247 -537 -643 N ATOM 2963 N LEU A 420 -5.365 -28.135 -67.072 1.00 60.46 N ANISOU 2963 N LEU A 420 5583 12521 4870 779 -1276 -523 N ATOM 2964 CA LEU A 420 -5.583 -28.837 -68.338 1.00 58.81 C ANISOU 2964 CA LEU A 420 5390 12219 4737 921 -1397 -554 C ATOM 2965 C LEU A 420 -5.203 -30.288 -68.172 1.00 64.98 C ANISOU 2965 C LEU A 420 6302 12844 5545 878 -1696 -501 C ATOM 2966 O LEU A 420 -5.970 -31.153 -68.595 1.00 65.72 O ANISOU 2966 O LEU A 420 6453 12871 5648 829 -1838 -453 O ATOM 2967 CB LEU A 420 -4.793 -28.182 -69.481 1.00 56.99 C ANISOU 2967 CB LEU A 420 5121 11977 4558 1156 -1300 -675 C ATOM 2968 CG LEU A 420 -4.771 -28.870 -70.856 1.00 59.68 C ANISOU 2968 CG LEU A 420 5473 12227 4975 1332 -1424 -730 C ATOM 2969 CD1 LEU A 420 -6.156 -29.087 -71.418 1.00 58.69 C ANISOU 2969 CD1 LEU A 420 5333 12109 4858 1319 -1428 -692 C ATOM 2970 CD2 LEU A 420 -3.943 -28.079 -71.814 1.00 60.25 C ANISOU 2970 CD2 LEU A 420 5508 12331 5052 1499 -1292 -853 C ATOM 2971 N GLY A 421 -4.064 -30.539 -67.505 1.00 61.96 N ANISOU 2971 N GLY A 421 5984 12403 5157 891 -1807 -515 N ATOM 2972 CA GLY A 421 -3.596 -31.881 -67.177 1.00 63.61 C ANISOU 2972 CA GLY A 421 6370 12434 5365 877 -2138 -479 C ATOM 2973 C GLY A 421 -4.683 -32.697 -66.500 1.00 70.71 C ANISOU 2973 C GLY A 421 7419 13267 6180 592 -2271 -324 C ATOM 2974 O GLY A 421 -5.070 -33.756 -67.012 1.00 70.98 O ANISOU 2974 O GLY A 421 7592 13156 6223 582 -2494 -287 O ATOM 2975 N LYS A 422 -5.259 -32.150 -65.388 1.00 69.18 N ANISOU 2975 N LYS A 422 7192 13207 5887 335 -2115 -240 N ATOM 2976 CA LYS A 422 -6.357 -32.777 -64.639 1.00 71.14 C ANISOU 2976 CA LYS A 422 7549 13473 6009 -12 -2187 -104 C ATOM 2977 C LYS A 422 -7.536 -33.103 -65.545 1.00 77.98 C ANISOU 2977 C LYS A 422 8360 14387 6880 -59 -2173 -99 C ATOM 2978 O LYS A 422 -8.046 -34.216 -65.456 1.00 79.73 O ANISOU 2978 O LYS A 422 8767 14496 7030 -266 -2391 -7 O ATOM 2979 CB LYS A 422 -6.854 -31.900 -63.474 1.00 73.10 C ANISOU 2979 CB LYS A 422 7687 13942 6145 -245 -1955 -65 C ATOM 2980 CG LYS A 422 -5.950 -31.844 -62.252 1.00 80.26 C ANISOU 2980 CG LYS A 422 8704 14797 6993 -327 -2013 -23 C ATOM 2981 CD LYS A 422 -6.627 -31.058 -61.117 1.00 94.81 C ANISOU 2981 CD LYS A 422 10439 16876 8707 -586 -1789 16 C ATOM 2982 CE LYS A 422 -5.836 -31.101 -59.824 1.00123.84 C ANISOU 2982 CE LYS A 422 14249 20498 12306 -712 -1863 76 C ATOM 2983 NZ LYS A 422 -6.507 -30.373 -58.706 1.00140.05 N ANISOU 2983 NZ LYS A 422 16198 22794 14222 -971 -1649 107 N ATOM 2984 N VAL A 423 -7.951 -32.149 -66.429 1.00 74.47 N ANISOU 2984 N VAL A 423 7690 14097 6508 129 -1937 -201 N ATOM 2985 CA VAL A 423 -9.093 -32.291 -67.352 1.00 75.13 C ANISOU 2985 CA VAL A 423 7682 14262 6601 129 -1900 -227 C ATOM 2986 C VAL A 423 -8.883 -33.509 -68.271 1.00 82.84 C ANISOU 2986 C VAL A 423 8825 15006 7645 220 -2175 -210 C ATOM 2987 O VAL A 423 -9.775 -34.354 -68.375 1.00 83.17 O ANISOU 2987 O VAL A 423 8946 15033 7622 12 -2301 -146 O ATOM 2988 CB VAL A 423 -9.327 -31.000 -68.189 1.00 77.08 C ANISOU 2988 CB VAL A 423 7717 14658 6914 388 -1642 -355 C ATOM 2989 CG1 VAL A 423 -10.344 -31.227 -69.305 1.00 76.99 C ANISOU 2989 CG1 VAL A 423 7628 14696 6929 457 -1649 -402 C ATOM 2990 CG2 VAL A 423 -9.765 -29.841 -67.301 1.00 76.65 C ANISOU 2990 CG2 VAL A 423 7519 14834 6769 302 -1402 -386 C ATOM 2991 N LEU A 424 -7.704 -33.599 -68.910 1.00 82.28 N ANISOU 2991 N LEU A 424 8804 14773 7685 514 -2271 -282 N ATOM 2992 CA LEU A 424 -7.344 -34.681 -69.835 1.00 84.06 C ANISOU 2992 CA LEU A 424 9176 14782 7980 673 -2541 -306 C ATOM 2993 C LEU A 424 -7.203 -36.013 -69.077 1.00 94.95 C ANISOU 2993 C LEU A 424 10860 15942 9273 474 -2881 -195 C ATOM 2994 O LEU A 424 -7.576 -37.059 -69.616 1.00 95.94 O ANISOU 2994 O LEU A 424 11157 15904 9391 441 -3117 -161 O ATOM 2995 CB LEU A 424 -6.040 -34.334 -70.584 1.00 82.39 C ANISOU 2995 CB LEU A 424 8900 14526 7877 1031 -2535 -449 C ATOM 2996 CG LEU A 424 -6.075 -33.071 -71.457 1.00 83.72 C ANISOU 2996 CG LEU A 424 8847 14860 8102 1212 -2234 -554 C ATOM 2997 CD1 LEU A 424 -4.704 -32.617 -71.807 1.00 82.75 C ANISOU 2997 CD1 LEU A 424 8663 14752 8025 1443 -2194 -685 C ATOM 2998 CD2 LEU A 424 -6.920 -33.265 -72.691 1.00 85.30 C ANISOU 2998 CD2 LEU A 424 9008 15055 8348 1302 -2231 -580 C ATOM 2999 N TRP A 425 -6.708 -35.964 -67.816 1.00 95.69 N ANISOU 2999 N TRP A 425 11053 16019 9287 326 -2918 -135 N ATOM 3000 CA TRP A 425 -6.591 -37.137 -66.953 1.00100.11 C ANISOU 3000 CA TRP A 425 11956 16354 9727 105 -3250 -18 C ATOM 3001 C TRP A 425 -7.975 -37.756 -66.680 1.00108.49 C ANISOU 3001 C TRP A 425 13139 17440 10644 -315 -3291 122 C ATOM 3002 O TRP A 425 -8.088 -38.985 -66.651 1.00110.84 O ANISOU 3002 O TRP A 425 13770 17487 10858 -457 -3622 205 O ATOM 3003 CB TRP A 425 -5.895 -36.778 -65.634 1.00100.04 C ANISOU 3003 CB TRP A 425 12000 16364 9648 13 -3233 16 C ATOM 3004 CG TRP A 425 -6.085 -37.800 -64.551 1.00104.79 C ANISOU 3004 CG TRP A 425 12969 16773 10072 -323 -3518 171 C ATOM 3005 CD1 TRP A 425 -6.955 -37.721 -63.503 1.00108.79 C ANISOU 3005 CD1 TRP A 425 13525 17405 10407 -765 -3416 307 C ATOM 3006 CD2 TRP A 425 -5.552 -39.132 -64.529 1.00107.41 C ANISOU 3006 CD2 TRP A 425 13707 16751 10353 -274 -3974 202 C ATOM 3007 NE1 TRP A 425 -6.924 -38.886 -62.772 1.00111.38 N ANISOU 3007 NE1 TRP A 425 14284 17468 10568 -1028 -3769 439 N ATOM 3008 CE2 TRP A 425 -6.069 -39.770 -63.377 1.00113.87 C ANISOU 3008 CE2 TRP A 425 14848 17462 10955 -720 -4132 380 C ATOM 3009 CE3 TRP A 425 -4.656 -39.841 -65.349 1.00109.56 C ANISOU 3009 CE3 TRP A 425 14116 16790 10724 114 -4280 80 C ATOM 3010 CZ2 TRP A 425 -5.705 -41.072 -63.015 1.00116.37 C ANISOU 3010 CZ2 TRP A 425 15668 17399 11147 -788 -4604 457 C ATOM 3011 CZ3 TRP A 425 -4.303 -41.134 -64.991 1.00114.27 C ANISOU 3011 CZ3 TRP A 425 15180 17027 11209 89 -4754 132 C ATOM 3012 CH2 TRP A 425 -4.822 -41.736 -63.838 1.00117.20 C ANISOU 3012 CH2 TRP A 425 15917 17252 11362 -358 -4923 327 C ATOM 3013 N GLU A 426 -9.021 -36.907 -66.481 1.00105.55 N ANISOU 3013 N GLU A 426 12503 17380 10222 -515 -2968 130 N ATOM 3014 CA GLU A 426 -10.403 -37.360 -66.232 1.00107.53 C ANISOU 3014 CA GLU A 426 12780 17764 10312 -937 -2953 220 C ATOM 3015 C GLU A 426 -10.998 -37.984 -67.509 1.00112.04 C ANISOU 3015 C GLU A 426 13362 18266 10941 -858 -3059 188 C ATOM 3016 O GLU A 426 -11.835 -38.887 -67.429 1.00112.86 O ANISOU 3016 O GLU A 426 13638 18338 10905 -1204 -3209 277 O ATOM 3017 CB GLU A 426 -11.310 -36.203 -65.733 1.00108.36 C ANISOU 3017 CB GLU A 426 12544 18279 10350 -1096 -2582 174 C ATOM 3018 CG GLU A 426 -10.770 -35.343 -64.591 1.00119.53 C ANISOU 3018 CG GLU A 426 13884 19804 11726 -1122 -2420 177 C ATOM 3019 CD GLU A 426 -10.400 -35.973 -63.258 1.00146.24 C ANISOU 3019 CD GLU A 426 17555 23062 14949 -1444 -2596 314 C ATOM 3020 OE1 GLU A 426 -10.908 -37.073 -62.939 1.00152.66 O ANISOU 3020 OE1 GLU A 426 18636 23766 15600 -1807 -2816 434 O ATOM 3021 OE2 GLU A 426 -9.659 -35.313 -62.492 1.00135.04 O ANISOU 3021 OE2 GLU A 426 16099 21666 13543 -1364 -2505 304 O ATOM 3022 N GLU A 427 -10.556 -37.485 -68.683 1.00108.10 N ANISOU 3022 N GLU A 427 12688 17752 10633 -426 -2978 59 N ATOM 3023 CA GLU A 427 -10.970 -37.953 -70.004 1.00108.70 C ANISOU 3023 CA GLU A 427 12752 17759 10790 -273 -3063 7 C ATOM 3024 C GLU A 427 -10.363 -39.336 -70.288 1.00116.72 C ANISOU 3024 C GLU A 427 14143 18398 11806 -226 -3476 56 C ATOM 3025 O GLU A 427 -11.039 -40.184 -70.883 1.00117.54 O ANISOU 3025 O GLU A 427 14380 18409 11873 -346 -3641 91 O ATOM 3026 CB GLU A 427 -10.550 -36.932 -71.083 1.00107.42 C ANISOU 3026 CB GLU A 427 12322 17688 10805 164 -2851 -146 C ATOM 3027 CG GLU A 427 -11.020 -37.257 -72.496 1.00116.25 C ANISOU 3027 CG GLU A 427 13394 18768 12008 340 -2901 -212 C ATOM 3028 CD GLU A 427 -10.694 -36.237 -73.575 1.00133.84 C ANISOU 3028 CD GLU A 427 15395 21086 14372 723 -2692 -352 C ATOM 3029 OE1 GLU A 427 -9.746 -35.440 -73.389 1.00110.57 O ANISOU 3029 OE1 GLU A 427 12379 18159 11475 908 -2568 -409 O ATOM 3030 OE2 GLU A 427 -11.350 -36.280 -74.641 1.00137.62 O ANISOU 3030 OE2 GLU A 427 15793 21602 14895 826 -2671 -406 O ATOM 3031 N ARG A 428 -9.088 -39.556 -69.856 1.00115.26 N ANISOU 3031 N ARG A 428 14134 18007 11654 -37 -3658 42 N ATOM 3032 CA ARG A 428 -8.341 -40.817 -70.012 1.00117.74 C ANISOU 3032 CA ARG A 428 14826 17951 11957 85 -4094 50 C ATOM 3033 C ARG A 428 -9.133 -42.019 -69.442 1.00125.64 C ANISOU 3033 C ARG A 428 16223 18756 12756 -365 -4379 221 C ATOM 3034 O ARG A 428 -9.221 -43.071 -70.085 1.00127.17 O ANISOU 3034 O ARG A 428 16690 18693 12935 -330 -4689 232 O ATOM 3035 CB ARG A 428 -6.964 -40.724 -69.311 1.00119.09 C ANISOU 3035 CB ARG A 428 15090 18008 12149 301 -4219 -5 C ATOM 3036 CG ARG A 428 -6.206 -42.055 -69.304 1.00135.74 C ANISOU 3036 CG ARG A 428 17629 19731 14215 444 -4723 -18 C ATOM 3037 CD ARG A 428 -4.941 -42.070 -68.467 1.00147.43 C ANISOU 3037 CD ARG A 428 19229 21109 15680 629 -4894 -80 C ATOM 3038 NE ARG A 428 -4.390 -43.428 -68.407 1.00158.32 N ANISOU 3038 NE ARG A 428 21079 22093 16982 753 -5431 -94 N ATOM 3039 CZ ARG A 428 -3.263 -43.763 -67.787 1.00174.50 C ANISOU 3039 CZ ARG A 428 23323 23981 18999 976 -5717 -178 C ATOM 3040 NH1 ARG A 428 -2.529 -42.837 -67.182 1.00164.03 N ANISOU 3040 NH1 ARG A 428 21737 22871 17717 1081 -5497 -254 N ATOM 3041 NH2 ARG A 428 -2.848 -45.023 -67.789 1.00162.08 N ANISOU 3041 NH2 ARG A 428 22217 22026 17341 1116 -6243 -204 N ATOM 3042 N ASN A 429 -9.687 -41.854 -68.234 1.00123.21 N ANISOU 3042 N ASN A 429 15963 18574 12276 -802 -4277 350 N ATOM 3043 CA ASN A 429 -10.434 -42.894 -67.540 1.00155.32 C ANISOU 3043 CA ASN A 429 20418 22498 16100 -1322 -4513 522 C ATOM 3044 C ASN A 429 -11.941 -42.651 -67.674 1.00183.05 C ANISOU 3044 C ASN A 429 23696 26346 19507 -1723 -4251 558 C ATOM 3045 O ASN A 429 -12.448 -42.483 -68.784 1.00141.94 O ANISOU 3045 O ASN A 429 18261 21255 14414 -1558 -4139 469 O ATOM 3046 CB ASN A 429 -10.015 -42.926 -66.061 1.00157.05 C ANISOU 3046 CB ASN A 429 20863 22653 16158 -1577 -4589 630 C ATOM 3047 CG ASN A 429 -8.532 -43.159 -65.821 1.00173.80 C ANISOU 3047 CG ASN A 429 23201 24476 18359 -1182 -4864 571 C ATOM 3048 OD1 ASN A 429 -7.799 -43.695 -66.665 1.00168.28 O ANISOU 3048 OD1 ASN A 429 22627 23532 17781 -777 -5127 466 O ATOM 3049 ND2 ASN A 429 -8.071 -42.804 -64.634 1.00162.78 N ANISOU 3049 ND2 ASN A 429 21858 23111 16880 -1297 -4828 620 N TER 3050 ASN A 429 HETATM 3051 C1 PEG A1200 9.491 -3.620 -57.167 1.00 74.79 C HETATM 3052 O1 PEG A1200 8.868 -2.350 -57.061 1.00 74.85 O HETATM 3053 C2 PEG A1200 9.077 -4.348 -58.417 1.00 73.96 C HETATM 3054 O2 PEG A1200 9.735 -5.610 -58.495 1.00 73.87 O HETATM 3055 C3 PEG A1200 10.501 -5.768 -59.685 1.00 72.77 C HETATM 3056 C4 PEG A1200 11.009 -7.180 -59.816 1.00 70.17 C HETATM 3057 O4 PEG A1200 11.860 -7.550 -58.747 1.00 67.41 O CONECT 1461 1948 CONECT 1948 1461 CONECT 3051 3052 3053 CONECT 3052 3051 CONECT 3053 3051 3054 CONECT 3054 3053 3055 CONECT 3055 3054 3056 CONECT 3056 3055 3057 CONECT 3057 3056 MASTER 376 0 1 24 0 0 1 6 3056 1 9 33 END