HEADER MEMBRANE PROTEIN, TRANSPORT PROTEIN 08-OCT-13 4N4W
TITLE STRUCTURE OF THE HUMAN SMOOTHENED RECEPTOR IN COMPLEX WITH SANT-1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B(562),SMOOTHENED HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 190-555;
COMPND 5 SYNONYM: SMO,PROTEIN GX;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI 5 STR. 8401, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 373384, 9606;
SOURCE 5 STRAIN: 8401;
SOURCE 6 GENE: CYBC, SFV_4255, SMO, SMOH;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS HUMAN SMOOTHENED RECEPTOR, ANTITUMOR AGENT, NOVEL PROTEIN
KEYWDS 2 ENGINEERING, GPCR NETWORK, MEMBRANE PROTEIN, PSI-BIOLOGY, STRUCTURAL
KEYWDS 3 GENOMICS, GPCR, MEMBRANE, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WANG,H.WU,G.W.HAN,V.CHEREZOV,R.C.STEVENS,GPCR NETWORK (GPCR)
REVDAT 5 29-JUL-20 4N4W 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 15-NOV-17 4N4W 1 REMARK
REVDAT 3 07-JUN-17 4N4W 1 COMPND SOURCE REMARK
REVDAT 2 30-JUL-14 4N4W 1 JRNL
REVDAT 1 22-JAN-14 4N4W 0
JRNL AUTH C.WANG,H.WU,T.EVRON,E.VARDY,G.W.HAN,X.P.HUANG,S.J.HUFEISEN,
JRNL AUTH 2 T.J.MANGANO,D.J.URBAN,V.KATRITCH,V.CHEREZOV,M.G.CARON,
JRNL AUTH 3 B.L.ROTH,R.C.STEVENS
JRNL TITL STRUCTURAL BASIS FOR SMOOTHENED RECEPTOR MODULATION AND
JRNL TITL 2 CHEMORESISTANCE TO ANTICANCER DRUGS.
JRNL REF NAT COMMUN V. 5 4355 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25008467
JRNL DOI 10.1038/NCOMMS5355
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 15986
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 776
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.05
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2598
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2243
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2454
REMARK 3 BIN R VALUE (WORKING SET) : 0.2191
REMARK 3 BIN FREE R VALUE : 0.3188
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.54
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
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 : 3551
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 129
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.51200
REMARK 3 B22 (A**2) : -6.44010
REMARK 3 B33 (A**2) : 12.95210
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.415
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) : 1.046
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 : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3794 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5157 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1697 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 75 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 547 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3794 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 498 ; 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 : 4652 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.54
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.45
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|-2 - 106 }
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2216 -50.7429 -37.6558
REMARK 3 T TENSOR
REMARK 3 T11: -0.0383 T22: -0.0304
REMARK 3 T33: -0.2776 T12: 0.0029
REMARK 3 T13: -0.0950 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 4.9400 L22: 8.2003
REMARK 3 L33: 4.0118 L12: 2.4672
REMARK 3 L13: -0.1201 L23: -2.1120
REMARK 3 S TENSOR
REMARK 3 S11: 0.1303 S12: 0.1285 S13: -0.2445
REMARK 3 S21: -0.2352 S22: -0.0555 S23: -0.0348
REMARK 3 S31: 0.3380 S32: -0.2673 S33: -0.0748
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|190 - 553 }
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7527 -23.2528 -4.8813
REMARK 3 T TENSOR
REMARK 3 T11: -0.1588 T22: 0.0844
REMARK 3 T33: -0.3040 T12: 0.0104
REMARK 3 T13: 0.0582 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 1.0947 L22: 0.7157
REMARK 3 L33: 6.1582 L12: 0.1422
REMARK 3 L13: 0.1294 L23: 0.8769
REMARK 3 S TENSOR
REMARK 3 S11: -0.0762 S12: 0.0717 S13: 0.0287
REMARK 3 S21: -0.1474 S22: 0.0442 S23: 0.0748
REMARK 3 S31: -0.3511 S32: 0.3977 S33: 0.0320
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|601 - 604 }
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4090 -20.6131 -44.7856
REMARK 3 T TENSOR
REMARK 3 T11: -0.0247 T22: 0.0413
REMARK 3 T33: -0.0171 T12: -0.0443
REMARK 3 T13: 0.0609 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: -0.1413
REMARK 3 L13: -0.1556 L23: -0.7341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: -0.0037 S13: 0.0020
REMARK 3 S21: 0.0092 S22: -0.0208 S23: 0.0043
REMARK 3 S31: 0.0002 S32: 0.0017 S33: 0.0247
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4N4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 4
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 : 16010
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 94.5
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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 4JKV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NH4F 150MM, HEPES PH 6.9 100MM, PEG
REMARK 280 400 27%, JEFFAMINE 2.5%, LIPIDIC CUBIC PHASE (LCP), TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.60500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.60500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.32000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.44000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.32000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.44000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 72.60500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.32000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.44000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 72.60500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.32000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.44000
REMARK 290 SMTRY3 8 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 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -72.60500
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 ZN ZN A 606 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS A 440
REMARK 465 ALA A 441
REMARK 465 ALA A 442
REMARK 465 ASN A 493
REMARK 465 VAL A 494
REMARK 465 THR A 495
REMARK 465 ILE A 496
REMARK 465 GLY A 497
REMARK 465 LEU A 498
REMARK 465 PRO A 499
REMARK 465 THR A 500
REMARK 465 LYS A 501
REMARK 465 GLN A 502
REMARK 465 PRO A 503
REMARK 465 ILE A 504
REMARK 465 PRO A 505
REMARK 465 GLY A 554
REMARK 465 GLN A 555
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 LYS A 47 CG CD CE NZ
REMARK 470 GLU A 194 CG CD OE1 OE2
REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 261 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 291 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 344 CG CD CE NZ
REMARK 470 LYS A 430 CG CD CE NZ
REMARK 470 GLU A 439 CG CD OE1 OE2
REMARK 470 ASN A 446 CG OD1 ND2
REMARK 470 LYS A 539 CD CE NZ
REMARK 470 ARG A 546 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 547 CG CD NE CZ NH1 NH2
REMARK 470 THR A 548 OG1 CG2
REMARK 470 CYS A 550 SG
REMARK 470 LEU A 552 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 208 -127.25 46.89
REMARK 500 GLN A 216 150.52 -47.93
REMARK 500 ASN A 219 106.13 -44.04
REMARK 500 ASP A 255 38.45 -142.44
REMARK 500 ASP A 287 111.38 -30.53
REMARK 500 ASN A 309 -31.47 66.91
REMARK 500 VAL A 404 -62.05 -127.83
REMARK 500 LEU A 437 59.25 -91.65
REMARK 500 LYS A 444 -71.38 64.29
REMARK 500 GLN A 491 69.63 -69.62
REMARK 500 CYS A 507 96.30 -164.20
REMARK 500 LYS A 510 -70.23 -65.40
REMARK 500 THR A 534 10.47 -69.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG B 1
REMARK 610 OLC A 608
REMARK 610 OLC A 609
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 606 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 ASP A 66 OD1 134.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 607 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 433 NE2
REMARK 620 2 HOH A 706 O 104.9
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JKV RELATED DB: PDB
REMARK 900 RELATED ID: GPCR-131 RELATED DB: TARGETTRACK
DBREF 4N4W A 1 106 UNP Q0SXH8 Q0SXH8_SHIF8 23 128
DBREF 4N4W A 190 555 UNP Q99835 SMO_HUMAN 190 555
SEQADV 4N4W GLY A -2 UNP Q0SXH8 EXPRESSION TAG
SEQADV 4N4W GLY A -1 UNP Q0SXH8 EXPRESSION TAG
SEQADV 4N4W THR A 0 UNP Q0SXH8 EXPRESSION TAG
SEQADV 4N4W TRP A 7 UNP Q0SXH8 MET 29 ENGINEERED MUTATION
SEQADV 4N4W ILE A 102 UNP Q0SXH8 HIS 124 ENGINEERED MUTATION
SEQADV 4N4W LEU A 106 UNP Q0SXH8 ARG 128 ENGINEERED MUTATION
SEQRES 1 A 475 GLY GLY THR ALA ASP LEU GLU ASP ASN TRP GLU THR LEU
SEQRES 2 A 475 ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA
SEQRES 3 A 475 ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA
SEQRES 4 A 475 ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU
SEQRES 5 A 475 ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG
SEQRES 6 A 475 HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA
SEQRES 7 A 475 LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN
SEQRES 8 A 475 ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR
SEQRES 9 A 475 ILE GLN LYS TYR LEU SER GLY GLN CYS GLU VAL PRO LEU
SEQRES 10 A 475 VAL ARG THR ASP ASN PRO LYS SER TRP TYR GLU ASP VAL
SEQRES 11 A 475 GLU GLY CYS GLY ILE GLN CYS GLN ASN PRO LEU PHE THR
SEQRES 12 A 475 GLU ALA GLU HIS GLN ASP MET HIS SER TYR ILE ALA ALA
SEQRES 13 A 475 PHE GLY ALA VAL THR GLY LEU CYS THR LEU PHE THR LEU
SEQRES 14 A 475 ALA THR PHE VAL ALA ASP TRP ARG ASN SER ASN ARG TYR
SEQRES 15 A 475 PRO ALA VAL ILE LEU PHE TYR VAL ASN ALA CYS PHE PHE
SEQRES 16 A 475 VAL GLY SER ILE GLY TRP LEU ALA GLN PHE MET ASP GLY
SEQRES 17 A 475 ALA ARG ARG GLU ILE VAL CYS ARG ALA ASP GLY THR MET
SEQRES 18 A 475 ARG LEU GLY GLU PRO THR SER ASN GLU THR LEU SER CYS
SEQRES 19 A 475 VAL ILE ILE PHE VAL ILE VAL TYR TYR ALA LEU MET ALA
SEQRES 20 A 475 GLY VAL VAL TRP PHE VAL VAL LEU THR TYR ALA TRP HIS
SEQRES 21 A 475 THR SER PHE LYS ALA LEU GLY THR THR TYR GLN PRO LEU
SEQRES 22 A 475 SER GLY LYS THR SER TYR PHE HIS LEU LEU THR TRP SER
SEQRES 23 A 475 LEU PRO PHE VAL LEU THR VAL ALA ILE LEU ALA VAL ALA
SEQRES 24 A 475 GLN VAL ASP GLY ASP SER VAL SER GLY ILE CYS PHE VAL
SEQRES 25 A 475 GLY TYR LYS ASN TYR ARG TYR ARG ALA GLY PHE VAL LEU
SEQRES 26 A 475 ALA PRO ILE GLY LEU VAL LEU ILE VAL GLY GLY TYR PHE
SEQRES 27 A 475 LEU ILE ARG GLY VAL MET THR LEU PHE SER ILE LYS SER
SEQRES 28 A 475 ASN HIS PRO GLY LEU LEU SER GLU LYS ALA ALA SER LYS
SEQRES 29 A 475 ILE ASN GLU THR MET LEU ARG LEU GLY ILE PHE GLY PHE
SEQRES 30 A 475 LEU ALA PHE GLY PHE VAL LEU ILE THR PHE SER CYS HIS
SEQRES 31 A 475 PHE TYR ASP PHE PHE ASN GLN ALA GLU TRP GLU ARG SER
SEQRES 32 A 475 PHE ARG ASP TYR VAL LEU CYS GLN ALA ASN VAL THR ILE
SEQRES 33 A 475 GLY LEU PRO THR LYS GLN PRO ILE PRO ASP CYS GLU ILE
SEQRES 34 A 475 LYS ASN ARG PRO SER LEU LEU VAL GLU LYS ILE ASN LEU
SEQRES 35 A 475 PHE ALA MET PHE GLY THR GLY ILE ALA MET SER THR TRP
SEQRES 36 A 475 VAL TRP THR LYS ALA THR LEU LEU ILE TRP ARG ARG THR
SEQRES 37 A 475 TRP CYS ARG LEU THR GLY GLN
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HET SNT A 605 28
HET ZN A 606 1
HET ZN A 607 1
HET OLC A 608 15
HET OLC A 609 14
HET PEG A 610 7
HET PG4 A 611 13
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM SNT (E)-N-(4-BENZYLPIPERAZIN-1-YL)-1-(3,5-DIMETHYL-1-
HETNAM 2 SNT PHENYL-1H-PYRAZOL-4-YL)METHANIMINE
HETNAM ZN ZINC ION
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN SNT SANT-1
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN C6 H12 O6
FORMUL 3 SNT C23 H27 N5
FORMUL 4 ZN 2(ZN 2+)
FORMUL 6 OLC 2(C21 H40 O4)
FORMUL 8 PEG C4 H10 O3
FORMUL 9 PG4 C8 H18 O5
FORMUL 10 HOH *8(H2 O)
HELIX 1 1 ASP A 2 LYS A 19 1 18
HELIX 2 2 ASN A 22 LYS A 42 1 21
HELIX 3 3 SER A 55 GLU A 81 1 27
HELIX 4 4 LYS A 83 GLU A 92 1 10
HELIX 5 5 GLN A 93 LEU A 106 1 14
HELIX 6 6 THR A 223 ALA A 254 1 32
HELIX 7 7 ASP A 255 ASN A 260 1 6
HELIX 8 8 ALA A 264 ALA A 283 1 20
HELIX 9 9 GLN A 284 MET A 286 5 3
HELIX 10 10 GLY A 288 CYS A 295 1 8
HELIX 11 11 LEU A 312 SER A 342 1 31
HELIX 12 12 PHE A 343 LEU A 346 5 4
HELIX 13 13 LYS A 356 ALA A 379 1 24
HELIX 14 14 ASN A 396 VAL A 404 1 9
HELIX 15 15 VAL A 404 HIS A 433 1 30
HELIX 16 16 ILE A 445 GLN A 491 1 47
HELIX 17 17 SER A 514 THR A 534 1 21
HELIX 18 18 THR A 538 ARG A 551 1 14
SHEET 1 A 2 LEU A 197 ARG A 199 0
SHEET 2 A 2 CYS A 213 ILE A 215 -1 O GLY A 214 N VAL A 198
SHEET 1 B 2 VAL A 381 GLY A 383 0
SHEET 2 B 2 CYS A 390 VAL A 392 -1 O PHE A 391 N ASP A 382
SSBOND 1 CYS A 193 CYS A 213 1555 1555 2.04
SSBOND 2 CYS A 217 CYS A 295 1555 1555 2.04
SSBOND 3 CYS A 314 CYS A 390 1555 1555 2.05
SSBOND 4 CYS A 490 CYS A 507 1555 1555 2.04
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.39
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.47
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.47
LINK ND1 HIS A 63 ZN ZN A 606 1555 1555 2.01
LINK OD1 ASP A 66 ZN ZN A 606 1555 1555 1.90
LINK NE2 HIS A 433 ZN ZN A 607 1555 1555 1.91
LINK ZN ZN A 607 O HOH A 706 1555 1555 2.50
CISPEP 1 VAL A 195 PRO A 196 0 6.13
CISPEP 2 TYR A 262 PRO A 263 0 6.97
CISPEP 3 GLU A 305 PRO A 306 0 8.10
CRYST1 84.640 110.880 145.210 90.00 90.00 90.00 C 2 2 21 8
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 0.011815 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009019 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006887 0.00000
ATOM 1 N GLY A -2 -10.019 -45.099 -51.674 1.00102.98 N
ANISOU 1 N GLY A -2 15869 14598 8663 -527 -467 299 N
ATOM 2 CA GLY A -2 -8.876 -45.903 -52.092 1.00105.05 C
ANISOU 2 CA GLY A -2 16352 14796 8765 -509 32 29 C
ATOM 3 C GLY A -2 -8.892 -47.359 -51.645 1.00109.10 C
ANISOU 3 C GLY A -2 16907 15178 9368 -457 130 -310 C
ATOM 4 O GLY A -2 -9.519 -47.701 -50.632 1.00106.21 O
ANISOU 4 O GLY A -2 16277 14760 9319 -381 -129 -327 O
ATOM 5 N GLY A -1 -8.184 -48.207 -52.407 1.00108.25 N
ANISOU 5 N GLY A -1 17145 14995 8991 -499 541 -577 N
ATOM 6 CA GLY A -1 -8.075 -49.648 -52.172 1.00108.22 C
ANISOU 6 CA GLY A -1 17257 14800 9061 -451 704 -920 C
ATOM 7 C GLY A -1 -9.136 -50.447 -52.905 1.00114.45 C
ANISOU 7 C GLY A -1 18507 15596 9382 -736 414 -1086 C
ATOM 8 O GLY A -1 -9.543 -50.056 -54.006 1.00118.25 O
ANISOU 8 O GLY A -1 19383 16226 9323 -997 278 -1011 O
ATOM 9 N THR A 0 -9.592 -51.580 -52.303 1.00108.98 N
ANISOU 9 N THR A 0 17786 14736 8886 -722 285 -1288 N
ATOM 10 CA THR A 0 -10.634 -52.473 -52.851 1.00111.19 C
ANISOU 10 CA THR A 0 18469 14979 8800 -1022 -38 -1457 C
ATOM 11 C THR A 0 -11.998 -51.762 -52.778 1.00112.73 C
ANISOU 11 C THR A 0 18502 15395 8933 -1215 -685 -1131 C
ATOM 12 O THR A 0 -12.697 -51.663 -53.791 1.00115.99 O
ANISOU 12 O THR A 0 19293 15932 8847 -1535 -988 -1076 O
ATOM 13 CB THR A 0 -10.634 -53.833 -52.111 1.00118.15 C
ANISOU 13 CB THR A 0 19299 15581 10012 -933 30 -1722 C
ATOM 14 OG1 THR A 0 -9.398 -54.499 -52.366 1.00120.95 O
ANISOU 14 OG1 THR A 0 19831 15696 10430 -753 639 -2014 O
ATOM 15 CG2 THR A 0 -11.794 -54.743 -52.512 1.00118.66 C
ANISOU 15 CG2 THR A 0 19717 15586 9782 -1271 -372 -1867 C
ATOM 16 N ALA A 1 -12.358 -51.267 -51.582 1.00103.50 N
ANISOU 16 N ALA A 1 16777 14267 8282 -1027 -886 -908 N
ATOM 17 CA ALA A 1 -13.591 -50.528 -51.323 1.00101.57 C
ANISOU 17 CA ALA A 1 16253 14194 8146 -1121 -1406 -583 C
ATOM 18 C ALA A 1 -13.272 -49.105 -50.854 1.00100.57 C
ANISOU 18 C ALA A 1 15751 14167 8296 -900 -1353 -292 C
ATOM 19 O ALA A 1 -12.216 -48.886 -50.244 1.00 98.06 O
ANISOU 19 O ALA A 1 15258 13768 8232 -661 -980 -351 O
ATOM 20 CB ALA A 1 -14.414 -51.254 -50.271 1.00100.26 C
ANISOU 20 CB ALA A 1 15786 13952 8355 -1108 -1636 -606 C
ATOM 21 N ASP A 2 -14.199 -48.147 -51.119 1.00 95.44 N
ANISOU 21 N ASP A 2 14962 13664 7637 -989 -1751 37 N
ATOM 22 CA ASP A 2 -14.104 -46.736 -50.719 1.00 92.37 C
ANISOU 22 CA ASP A 2 14238 13321 7536 -801 -1757 329 C
ATOM 23 C ASP A 2 -14.057 -46.620 -49.177 1.00 89.01 C
ANISOU 23 C ASP A 2 13352 12800 7666 -538 -1638 296 C
ATOM 24 O ASP A 2 -14.486 -47.542 -48.474 1.00 87.61 O
ANISOU 24 O ASP A 2 13070 12570 7648 -542 -1684 149 O
ATOM 25 CB ASP A 2 -15.285 -45.933 -51.297 1.00 97.57 C
ANISOU 25 CB ASP A 2 14823 14105 8144 -948 -2253 697 C
ATOM 26 CG ASP A 2 -15.500 -46.114 -52.801 1.00125.86 C
ANISOU 26 CG ASP A 2 18907 17804 11110 -1291 -2492 765 C
ATOM 27 OD1 ASP A 2 -16.624 -46.515 -53.200 1.00130.93 O
ANISOU 27 OD1 ASP A 2 19586 18520 11643 -1532 -2969 882 O
ATOM 28 OD2 ASP A 2 -14.542 -45.871 -53.579 1.00137.68 O
ANISOU 28 OD2 ASP A 2 20768 19322 12221 -1346 -2202 710 O
ATOM 29 N LEU A 3 -13.497 -45.518 -48.655 1.00 80.29 N
ANISOU 29 N LEU A 3 12023 11662 6819 -343 -1477 426 N
ATOM 30 CA LEU A 3 -13.341 -45.321 -47.212 1.00 74.99 C
ANISOU 30 CA LEU A 3 11008 10899 6587 -136 -1351 379 C
ATOM 31 C LEU A 3 -14.688 -45.409 -46.451 1.00 76.14 C
ANISOU 31 C LEU A 3 10869 11059 7003 -125 -1606 458 C
ATOM 32 O LEU A 3 -14.764 -46.066 -45.407 1.00 74.44 O
ANISOU 32 O LEU A 3 10514 10790 6978 -71 -1521 315 O
ATOM 33 CB LEU A 3 -12.638 -43.980 -46.923 1.00 73.64 C
ANISOU 33 CB LEU A 3 10703 10673 6603 8 -1201 522 C
ATOM 34 CG LEU A 3 -12.517 -43.549 -45.462 1.00 75.41 C
ANISOU 34 CG LEU A 3 10639 10792 7219 174 -1105 485 C
ATOM 35 CD1 LEU A 3 -11.701 -44.542 -44.628 1.00 72.81 C
ANISOU 35 CD1 LEU A 3 10300 10408 6956 210 -906 255 C
ATOM 36 CD2 LEU A 3 -11.946 -42.175 -45.371 1.00 79.68 C
ANISOU 36 CD2 LEU A 3 11112 11252 7909 257 -1019 633 C
ATOM 37 N GLU A 4 -15.731 -44.771 -46.991 1.00 71.98 N
ANISOU 37 N GLU A 4 10245 10599 6504 -185 -1913 712 N
ATOM 38 CA GLU A 4 -17.073 -44.716 -46.417 1.00 70.62 C
ANISOU 38 CA GLU A 4 9734 10443 6655 -165 -2137 846 C
ATOM 39 C GLU A 4 -17.708 -46.120 -46.374 1.00 75.21 C
ANISOU 39 C GLU A 4 10356 11073 7145 -350 -2284 712 C
ATOM 40 O GLU A 4 -18.337 -46.466 -45.367 1.00 74.23 O
ANISOU 40 O GLU A 4 9961 10928 7316 -301 -2252 680 O
ATOM 41 CB GLU A 4 -17.939 -43.723 -47.205 1.00 74.26 C
ANISOU 41 CB GLU A 4 10065 10947 7202 -190 -2465 1206 C
ATOM 42 CG GLU A 4 -17.113 -42.682 -47.951 1.00 80.26 C
ANISOU 42 CG GLU A 4 11023 11679 7792 -156 -2405 1348 C
ATOM 43 CD GLU A 4 -17.718 -41.301 -48.076 1.00 95.69 C
ANISOU 43 CD GLU A 4 12728 13558 10071 -29 -2580 1705 C
ATOM 44 OE1 GLU A 4 -18.254 -40.804 -47.060 1.00 83.40 O
ANISOU 44 OE1 GLU A 4 10813 11883 8992 181 -2484 1726 O
ATOM 45 OE2 GLU A 4 -17.626 -40.699 -49.173 1.00 90.67 O
ANISOU 45 OE2 GLU A 4 12276 12958 9215 -137 -2781 1963 O
ATOM 46 N ASP A 5 -17.468 -46.940 -47.427 1.00 73.25 N
ANISOU 46 N ASP A 5 10488 10869 6475 -576 -2397 608 N
ATOM 47 CA ASP A 5 -17.938 -48.325 -47.555 1.00 74.28 C
ANISOU 47 CA ASP A 5 10759 10995 6468 -797 -2542 446 C
ATOM 48 C ASP A 5 -17.361 -49.228 -46.477 1.00 76.93 C
ANISOU 48 C ASP A 5 11070 11207 6952 -694 -2236 182 C
ATOM 49 O ASP A 5 -18.109 -50.008 -45.872 1.00 77.73 O
ANISOU 49 O ASP A 5 11019 11287 7226 -782 -2343 157 O
ATOM 50 CB ASP A 5 -17.556 -48.918 -48.917 1.00 78.97 C
ANISOU 50 CB ASP A 5 11874 11608 6522 -1051 -2633 322 C
ATOM 51 CG ASP A 5 -18.131 -48.246 -50.139 1.00 87.03 C
ANISOU 51 CG ASP A 5 13037 12764 7265 -1251 -3012 595 C
ATOM 52 OD1 ASP A 5 -19.157 -47.546 -50.002 1.00 88.24 O
ANISOU 52 OD1 ASP A 5 12817 12991 7718 -1234 -3332 922 O
ATOM 53 OD2 ASP A 5 -17.594 -48.483 -51.249 1.00 91.14 O
ANISOU 53 OD2 ASP A 5 14053 13309 7267 -1441 -2992 490 O
ATOM 54 N ASN A 6 -16.024 -49.163 -46.265 1.00 71.09 N
ANISOU 54 N ASN A 6 10470 10380 6160 -532 -1879 20 N
ATOM 55 CA ASN A 6 -15.344 -49.980 -45.258 1.00 68.30 C
ANISOU 55 CA ASN A 6 10087 9894 5969 -430 -1627 -175 C
ATOM 56 C ASN A 6 -15.733 -49.517 -43.862 1.00 69.84 C
ANISOU 56 C ASN A 6 9915 10098 6523 -296 -1587 -75 C
ATOM 57 O ASN A 6 -15.789 -50.339 -42.949 1.00 68.57 O
ANISOU 57 O ASN A 6 9688 9867 6498 -308 -1532 -156 O
ATOM 58 CB ASN A 6 -13.826 -49.943 -45.426 1.00 66.38 C
ANISOU 58 CB ASN A 6 10013 9561 5649 -292 -1291 -311 C
ATOM 59 CG ASN A 6 -13.312 -50.468 -46.737 1.00 83.85 C
ANISOU 59 CG ASN A 6 12627 11737 7495 -406 -1194 -466 C
ATOM 60 OD1 ASN A 6 -13.306 -51.672 -46.988 1.00 78.78 O
ANISOU 60 OD1 ASN A 6 12213 10972 6748 -507 -1160 -672 O
ATOM 61 ND2 ASN A 6 -12.794 -49.577 -47.574 1.00 77.05 N
ANISOU 61 ND2 ASN A 6 11890 10955 6430 -392 -1098 -383 N
ATOM 62 N TRP A 7 -16.009 -48.205 -43.692 1.00 66.70 N
ANISOU 62 N TRP A 7 9312 9764 6266 -178 -1597 100 N
ATOM 63 CA TRP A 7 -16.417 -47.662 -42.389 1.00 64.94 C
ANISOU 63 CA TRP A 7 8796 9529 6350 -54 -1500 158 C
ATOM 64 C TRP A 7 -17.824 -48.103 -42.097 1.00 68.33 C
ANISOU 64 C TRP A 7 9001 10018 6943 -158 -1669 250 C
ATOM 65 O TRP A 7 -18.115 -48.404 -40.945 1.00 66.92 O
ANISOU 65 O TRP A 7 8675 9818 6933 -139 -1540 212 O
ATOM 66 CB TRP A 7 -16.277 -46.127 -42.279 1.00 63.50 C
ANISOU 66 CB TRP A 7 8489 9331 6306 110 -1422 284 C
ATOM 67 CG TRP A 7 -15.033 -45.653 -41.571 1.00 62.58 C
ANISOU 67 CG TRP A 7 8439 9125 6213 224 -1181 185 C
ATOM 68 CD1 TRP A 7 -14.129 -44.746 -42.036 1.00 65.46 C
ANISOU 68 CD1 TRP A 7 8890 9449 6533 290 -1104 230 C
ATOM 69 CD2 TRP A 7 -14.558 -46.063 -40.275 1.00 61.08 C
ANISOU 69 CD2 TRP A 7 8231 8876 6099 242 -1028 62 C
ATOM 70 NE1 TRP A 7 -13.127 -44.551 -41.106 1.00 63.64 N
ANISOU 70 NE1 TRP A 7 8668 9134 6377 344 -932 138 N
ATOM 71 CE2 TRP A 7 -13.366 -45.345 -40.018 1.00 64.21 C
ANISOU 71 CE2 TRP A 7 8693 9199 6505 312 -901 39 C
ATOM 72 CE3 TRP A 7 -15.065 -46.908 -39.269 1.00 62.39 C
ANISOU 72 CE3 TRP A 7 8334 9047 6324 180 -1004 2 C
ATOM 73 CZ2 TRP A 7 -12.654 -45.480 -38.823 1.00 62.81 C
ANISOU 73 CZ2 TRP A 7 8531 8958 6376 304 -805 -40 C
ATOM 74 CZ3 TRP A 7 -14.344 -47.061 -38.096 1.00 62.99 C
ANISOU 74 CZ3 TRP A 7 8458 9063 6412 179 -881 -74 C
ATOM 75 CH2 TRP A 7 -13.157 -46.347 -37.877 1.00 62.95 C
ANISOU 75 CH2 TRP A 7 8526 8991 6401 236 -807 -92 C
ATOM 76 N GLU A 8 -18.675 -48.213 -43.145 1.00 66.58 N
ANISOU 76 N GLU A 8 8766 9876 6655 -305 -1972 384 N
ATOM 77 CA GLU A 8 -20.051 -48.708 -43.003 1.00 68.24 C
ANISOU 77 CA GLU A 8 8716 10150 7061 -450 -2189 514 C
ATOM 78 C GLU A 8 -20.022 -50.235 -42.683 1.00 72.29 C
ANISOU 78 C GLU A 8 9379 10609 7478 -636 -2194 341 C
ATOM 79 O GLU A 8 -20.812 -50.700 -41.861 1.00 72.58 O
ANISOU 79 O GLU A 8 9175 10659 7745 -699 -2177 392 O
ATOM 80 CB GLU A 8 -20.903 -48.372 -44.254 1.00 72.43 C
ANISOU 80 CB GLU A 8 9194 10777 7548 -597 -2595 750 C
ATOM 81 CG GLU A 8 -22.359 -48.830 -44.236 1.00 79.07 C
ANISOU 81 CG GLU A 8 9700 11693 8649 -780 -2891 945 C
ATOM 82 CD GLU A 8 -23.285 -48.409 -43.103 1.00 98.93 C
ANISOU 82 CD GLU A 8 11700 14217 11673 -629 -2715 1084 C
ATOM 83 OE1 GLU A 8 -24.464 -48.835 -43.134 1.00 81.91 O
ANISOU 83 OE1 GLU A 8 9222 12129 9772 -794 -2945 1268 O
ATOM 84 OE2 GLU A 8 -22.842 -47.690 -42.176 1.00 95.22 O
ANISOU 84 OE2 GLU A 8 11156 13681 11343 -371 -2335 1002 O
ATOM 85 N THR A 9 -19.067 -50.979 -43.283 1.00 68.10 N
ANISOU 85 N THR A 9 9243 9993 6637 -708 -2167 140 N
ATOM 86 CA THR A 9 -18.844 -52.411 -43.064 1.00 67.79 C
ANISOU 86 CA THR A 9 9405 9826 6525 -852 -2145 -42 C
ATOM 87 C THR A 9 -18.518 -52.664 -41.592 1.00 70.43 C
ANISOU 87 C THR A 9 9594 10093 7073 -729 -1891 -75 C
ATOM 88 O THR A 9 -19.105 -53.560 -40.984 1.00 71.37 O
ANISOU 88 O THR A 9 9635 10170 7312 -870 -1936 -61 O
ATOM 89 CB THR A 9 -17.719 -52.896 -43.989 1.00 73.36 C
ANISOU 89 CB THR A 9 10548 10416 6911 -866 -2058 -260 C
ATOM 90 OG1 THR A 9 -18.148 -52.781 -45.349 1.00 74.86 O
ANISOU 90 OG1 THR A 9 10948 10680 6816 -1060 -2322 -231 O
ATOM 91 CG2 THR A 9 -17.267 -54.313 -43.681 1.00 71.68 C
ANISOU 91 CG2 THR A 9 10546 9991 6697 -936 -1958 -465 C
ATOM 92 N LEU A 10 -17.593 -51.864 -41.028 1.00 64.89 N
ANISOU 92 N LEU A 10 8873 9382 6400 -506 -1652 -97 N
ATOM 93 CA LEU A 10 -17.156 -51.949 -39.632 1.00 63.43 C
ANISOU 93 CA LEU A 10 8607 9147 6347 -419 -1447 -111 C
ATOM 94 C LEU A 10 -18.337 -51.700 -38.682 1.00 66.69 C
ANISOU 94 C LEU A 10 8728 9654 6956 -462 -1415 18 C
ATOM 95 O LEU A 10 -18.505 -52.440 -37.717 1.00 64.85 O
ANISOU 95 O LEU A 10 8475 9386 6780 -549 -1343 24 O
ATOM 96 CB LEU A 10 -16.021 -50.927 -39.365 1.00 61.79 C
ANISOU 96 CB LEU A 10 8432 8925 6119 -220 -1265 -137 C
ATOM 97 CG LEU A 10 -14.661 -51.271 -39.946 1.00 66.02 C
ANISOU 97 CG LEU A 10 9188 9351 6544 -157 -1193 -249 C
ATOM 98 CD1 LEU A 10 -13.875 -50.030 -40.284 1.00 64.95 C
ANISOU 98 CD1 LEU A 10 9048 9251 6380 -15 -1091 -221 C
ATOM 99 CD2 LEU A 10 -13.885 -52.150 -39.000 1.00 68.80 C
ANISOU 99 CD2 LEU A 10 9584 9570 6987 -147 -1115 -286 C
ATOM 100 N ASN A 11 -19.163 -50.677 -39.001 1.00 63.98 N
ANISOU 100 N ASN A 11 8156 9418 6736 -400 -1455 141 N
ATOM 101 CA ASN A 11 -20.341 -50.266 -38.256 1.00 65.32 C
ANISOU 101 CA ASN A 11 7988 9665 7163 -392 -1362 271 C
ATOM 102 C ASN A 11 -21.370 -51.373 -38.225 1.00 73.68 C
ANISOU 102 C ASN A 11 8909 10758 8327 -626 -1507 353 C
ATOM 103 O ASN A 11 -21.860 -51.695 -37.144 1.00 74.68 O
ANISOU 103 O ASN A 11 8903 10900 8573 -681 -1320 385 O
ATOM 104 CB ASN A 11 -20.944 -49.002 -38.863 1.00 64.88 C
ANISOU 104 CB ASN A 11 7700 9666 7286 -256 -1422 416 C
ATOM 105 CG ASN A 11 -20.120 -47.755 -38.654 1.00 75.41 C
ANISOU 105 CG ASN A 11 9118 10937 8597 -33 -1230 359 C
ATOM 106 OD1 ASN A 11 -19.399 -47.614 -37.662 1.00 63.11 O
ANISOU 106 OD1 ASN A 11 7695 9320 6964 27 -992 227 O
ATOM 107 ND2 ASN A 11 -20.217 -46.809 -39.585 1.00 65.49 N
ANISOU 107 ND2 ASN A 11 7800 9683 7401 64 -1365 481 N
ATOM 108 N ASP A 12 -21.682 -51.967 -39.400 1.00 72.70 N
ANISOU 108 N ASP A 12 8854 10639 8129 -799 -1841 386 N
ATOM 109 CA ASP A 12 -22.643 -53.064 -39.545 1.00 74.90 C
ANISOU 109 CA ASP A 12 9033 10924 8503 -1081 -2060 466 C
ATOM 110 C ASP A 12 -22.203 -54.264 -38.744 1.00 78.67 C
ANISOU 110 C ASP A 12 9710 11276 8907 -1196 -1941 351 C
ATOM 111 O ASP A 12 -22.995 -54.777 -37.959 1.00 79.96 O
ANISOU 111 O ASP A 12 9662 11465 9256 -1333 -1874 461 O
ATOM 112 CB ASP A 12 -22.826 -53.456 -41.020 1.00 78.16 C
ANISOU 112 CB ASP A 12 9622 11332 8742 -1281 -2465 470 C
ATOM 113 CG ASP A 12 -23.636 -52.480 -41.837 1.00 83.47 C
ANISOU 113 CG ASP A 12 10023 12144 9549 -1269 -2715 698 C
ATOM 114 OD1 ASP A 12 -24.366 -51.667 -41.236 1.00 83.54 O
ANISOU 114 OD1 ASP A 12 9597 12234 9911 -1125 -2585 884 O
ATOM 115 OD2 ASP A 12 -23.563 -52.550 -43.084 1.00 88.83 O
ANISOU 115 OD2 ASP A 12 10934 12836 9983 -1415 -3040 702 O
ATOM 116 N ASN A 13 -20.932 -54.680 -38.896 1.00 74.14 N
ANISOU 116 N ASN A 13 9512 10557 8102 -1130 -1889 162 N
ATOM 117 CA ASN A 13 -20.394 -55.816 -38.157 1.00 74.68 C
ANISOU 117 CA ASN A 13 9768 10461 8148 -1209 -1804 91 C
ATOM 118 C ASN A 13 -20.270 -55.510 -36.656 1.00 80.24 C
ANISOU 118 C ASN A 13 10348 11213 8927 -1123 -1530 169 C
ATOM 119 O ASN A 13 -20.405 -56.436 -35.859 1.00 81.52 O
ANISOU 119 O ASN A 13 10542 11299 9134 -1274 -1497 228 O
ATOM 120 CB ASN A 13 -19.066 -56.278 -38.723 1.00 74.85 C
ANISOU 120 CB ASN A 13 10154 10293 7994 -1119 -1792 -101 C
ATOM 121 CG ASN A 13 -19.200 -57.115 -39.968 1.00 97.86 C
ANISOU 121 CG ASN A 13 13319 13078 10784 -1297 -2012 -230 C
ATOM 122 OD1 ASN A 13 -19.625 -58.272 -39.923 1.00 93.74 O
ANISOU 122 OD1 ASN A 13 12895 12403 10319 -1518 -2137 -250 O
ATOM 123 ND2 ASN A 13 -18.814 -56.560 -41.111 1.00 88.84 N
ANISOU 123 ND2 ASN A 13 12333 11979 9445 -1231 -2060 -326 N
ATOM 124 N LEU A 14 -20.081 -54.220 -36.264 1.00 76.65 N
ANISOU 124 N LEU A 14 9782 10873 8470 -917 -1341 176 N
ATOM 125 CA LEU A 14 -20.001 -53.792 -34.847 1.00 76.58 C
ANISOU 125 CA LEU A 14 9724 10913 8460 -867 -1064 214 C
ATOM 126 C LEU A 14 -21.338 -54.018 -34.140 1.00 82.61 C
ANISOU 126 C LEU A 14 10219 11777 9392 -1021 -940 354 C
ATOM 127 O LEU A 14 -21.372 -54.414 -32.971 1.00 83.32 O
ANISOU 127 O LEU A 14 10366 11868 9425 -1127 -760 403 O
ATOM 128 CB LEU A 14 -19.592 -52.311 -34.740 1.00 75.53 C
ANISOU 128 CB LEU A 14 9560 10840 8299 -638 -898 158 C
ATOM 129 CG LEU A 14 -18.876 -51.846 -33.468 1.00 80.19 C
ANISOU 129 CG LEU A 14 10298 11416 8754 -592 -673 111 C
ATOM 130 CD1 LEU A 14 -17.789 -52.831 -33.022 1.00 79.52 C
ANISOU 130 CD1 LEU A 14 10472 11216 8525 -682 -782 109 C
ATOM 131 CD2 LEU A 14 -18.267 -50.457 -33.680 1.00 82.15 C
ANISOU 131 CD2 LEU A 14 10578 11659 8977 -388 -591 27 C
ATOM 132 N LYS A 15 -22.431 -53.788 -34.883 1.00 79.92 N
ANISOU 132 N LYS A 15 9578 11523 9266 -1054 -1050 448 N
ATOM 133 CA LYS A 15 -23.802 -53.970 -34.452 1.00 82.28 C
ANISOU 133 CA LYS A 15 9512 11923 9827 -1196 -950 619 C
ATOM 134 C LYS A 15 -24.164 -55.459 -34.485 1.00 86.46 C
ANISOU 134 C LYS A 15 10092 12381 10377 -1509 -1150 697 C
ATOM 135 O LYS A 15 -24.969 -55.894 -33.657 1.00 88.48 O
ANISOU 135 O LYS A 15 10150 12692 10778 -1675 -979 837 O
ATOM 136 CB LYS A 15 -24.742 -53.141 -35.346 1.00 86.59 C
ANISOU 136 CB LYS A 15 9673 12567 10660 -1112 -1074 742 C
ATOM 137 CG LYS A 15 -26.056 -52.738 -34.681 1.00111.49 C
ANISOU 137 CG LYS A 15 12340 15833 14189 -1112 -798 921 C
ATOM 138 CD LYS A 15 -25.934 -51.528 -33.746 1.00123.04 C
ANISOU 138 CD LYS A 15 13757 17307 15687 -843 -314 836 C
ATOM 139 CE LYS A 15 -27.176 -51.362 -32.899 1.00135.80 C
ANISOU 139 CE LYS A 15 14928 19006 17665 -855 79 979 C
ATOM 140 NZ LYS A 15 -27.017 -50.293 -31.881 1.00142.68 N
ANISOU 140 NZ LYS A 15 15851 19846 18516 -618 617 834 N
ATOM 141 N VAL A 16 -23.558 -56.254 -35.410 1.00 80.86 N
ANISOU 141 N VAL A 16 9671 11525 9527 -1598 -1472 598 N
ATOM 142 CA VAL A 16 -23.877 -57.684 -35.457 1.00 82.11 C
ANISOU 142 CA VAL A 16 9922 11551 9726 -1903 -1663 649 C
ATOM 143 C VAL A 16 -23.231 -58.386 -34.259 1.00 86.03 C
ANISOU 143 C VAL A 16 10642 11931 10115 -1947 -1473 660 C
ATOM 144 O VAL A 16 -23.847 -59.315 -33.755 1.00 89.34 O
ANISOU 144 O VAL A 16 11001 12303 10643 -2207 -1484 801 O
ATOM 145 CB VAL A 16 -23.644 -58.453 -36.793 1.00 85.75 C
ANISOU 145 CB VAL A 16 10638 11846 10096 -2045 -2044 527 C
ATOM 146 CG1 VAL A 16 -24.228 -57.713 -37.991 1.00 86.82 C
ANISOU 146 CG1 VAL A 16 10604 12115 10267 -2043 -2290 556 C
ATOM 147 CG2 VAL A 16 -22.194 -58.828 -37.028 1.00 82.80 C
ANISOU 147 CG2 VAL A 16 10706 11262 9492 -1898 -2027 310 C
ATOM 148 N ILE A 17 -22.051 -57.924 -33.772 1.00 78.94 N
ANISOU 148 N ILE A 17 9975 10998 9023 -1729 -1322 558 N
ATOM 149 CA ILE A 17 -21.392 -58.504 -32.587 1.00 79.08 C
ANISOU 149 CA ILE A 17 10204 10919 8926 -1788 -1203 624 C
ATOM 150 C ILE A 17 -22.281 -58.272 -31.351 1.00 84.91 C
ANISOU 150 C ILE A 17 10754 11831 9676 -1920 -907 788 C
ATOM 151 O ILE A 17 -22.477 -59.188 -30.554 1.00 86.10 O
ANISOU 151 O ILE A 17 10985 11918 9811 -2149 -877 942 O
ATOM 152 CB ILE A 17 -19.951 -57.943 -32.361 1.00 79.58 C
ANISOU 152 CB ILE A 17 10504 10926 8806 -1550 -1160 514 C
ATOM 153 CG1 ILE A 17 -19.040 -58.257 -33.556 1.00 78.78 C
ANISOU 153 CG1 ILE A 17 10575 10640 8716 -1420 -1366 357 C
ATOM 154 CG2 ILE A 17 -19.334 -58.481 -31.049 1.00 79.96 C
ANISOU 154 CG2 ILE A 17 10751 10897 8732 -1648 -1103 648 C
ATOM 155 CD1 ILE A 17 -17.964 -57.259 -33.775 1.00 85.00 C
ANISOU 155 CD1 ILE A 17 11428 11464 9404 -1160 -1301 244 C
ATOM 156 N GLU A 18 -22.818 -57.040 -31.225 1.00 81.75 N
ANISOU 156 N GLU A 18 10118 11628 9316 -1772 -662 757 N
ATOM 157 CA GLU A 18 -23.720 -56.555 -30.178 1.00 84.09 C
ANISOU 157 CA GLU A 18 10207 12093 9649 -1832 -267 854 C
ATOM 158 C GLU A 18 -25.003 -57.422 -30.103 1.00 91.28 C
ANISOU 158 C GLU A 18 10823 13046 10814 -2117 -254 1062 C
ATOM 159 O GLU A 18 -25.501 -57.702 -29.011 1.00 92.88 O
ANISOU 159 O GLU A 18 11003 13319 10970 -2294 46 1194 O
ATOM 160 CB GLU A 18 -24.073 -55.082 -30.487 1.00 85.38 C
ANISOU 160 CB GLU A 18 10123 12378 9939 -1564 -68 756 C
ATOM 161 CG GLU A 18 -24.768 -54.319 -29.367 1.00102.91 C
ANISOU 161 CG GLU A 18 12201 14727 12176 -1532 451 769 C
ATOM 162 CD GLU A 18 -25.382 -52.985 -29.762 1.00132.76 C
ANISOU 162 CD GLU A 18 15640 18568 16235 -1264 658 713 C
ATOM 163 OE1 GLU A 18 -24.799 -52.286 -30.623 1.00123.27 O
ANISOU 163 OE1 GLU A 18 14482 17309 15044 -1050 442 611 O
ATOM 164 OE2 GLU A 18 -26.435 -52.626 -29.183 1.00133.44 O
ANISOU 164 OE2 GLU A 18 15410 18742 16550 -1261 1066 787 O
ATOM 165 N LYS A 19 -25.516 -57.849 -31.264 1.00 89.27 N
ANISOU 165 N LYS A 19 10366 12747 10805 -2194 -588 1100 N
ATOM 166 CA LYS A 19 -26.732 -58.647 -31.340 1.00 93.57 C
ANISOU 166 CA LYS A 19 10591 13319 11643 -2495 -662 1310 C
ATOM 167 C LYS A 19 -26.428 -60.138 -31.666 1.00 99.62 C
ANISOU 167 C LYS A 19 11632 13849 12369 -2774 -1029 1342 C
ATOM 168 O LYS A 19 -27.364 -60.913 -31.889 1.00102.11 O
ANISOU 168 O LYS A 19 11731 14137 12929 -3070 -1196 1501 O
ATOM 169 CB LYS A 19 -27.706 -58.025 -32.369 1.00 97.49 C
ANISOU 169 CB LYS A 19 10627 13931 12484 -2439 -822 1371 C
ATOM 170 CG LYS A 19 -28.231 -56.624 -31.994 1.00110.87 C
ANISOU 170 CG LYS A 19 11962 15806 14359 -2166 -423 1389 C
ATOM 171 CD LYS A 19 -29.453 -56.657 -31.053 1.00125.56 C
ANISOU 171 CD LYS A 19 13381 17803 16523 -2300 4 1603 C
ATOM 172 CE LYS A 19 -29.217 -55.973 -29.720 1.00134.55 C
ANISOU 172 CE LYS A 19 14661 19007 17453 -2149 620 1505 C
ATOM 173 NZ LYS A 19 -29.343 -54.492 -29.811 1.00140.34 N
ANISOU 173 NZ LYS A 19 15187 19793 18344 -1781 901 1395 N
ATOM 174 N ALA A 20 -25.132 -60.548 -31.615 1.00 94.61 N
ANISOU 174 N ALA A 20 11457 13019 11469 -2685 -1136 1208 N
ATOM 175 CA ALA A 20 -24.683 -61.924 -31.900 1.00 94.90 C
ANISOU 175 CA ALA A 20 11798 12757 11502 -2880 -1434 1208 C
ATOM 176 C ALA A 20 -25.079 -62.926 -30.822 1.00100.59 C
ANISOU 176 C ALA A 20 12554 13399 12266 -3189 -1338 1453 C
ATOM 177 O ALA A 20 -25.258 -62.565 -29.654 1.00100.56 O
ANISOU 177 O ALA A 20 12497 13562 12149 -3209 -1002 1589 O
ATOM 178 CB ALA A 20 -23.177 -61.965 -32.086 1.00 92.46 C
ANISOU 178 CB ALA A 20 11885 12257 10987 -2639 -1519 1026 C
ATOM 179 N ASP A 21 -25.166 -64.200 -31.227 1.00 98.97 N
ANISOU 179 N ASP A 21 12496 12913 12194 -3442 -1626 1499 N
ATOM 180 CA ASP A 21 -25.528 -65.297 -30.342 1.00102.45 C
ANISOU 180 CA ASP A 21 12999 13216 12711 -3774 -1597 1761 C
ATOM 181 C ASP A 21 -24.306 -66.201 -30.042 1.00104.98 C
ANISOU 181 C ASP A 21 13773 13179 12934 -3732 -1743 1761 C
ATOM 182 O ASP A 21 -23.985 -66.396 -28.863 1.00105.03 O
ANISOU 182 O ASP A 21 13911 13196 12802 -3789 -1589 1970 O
ATOM 183 CB ASP A 21 -26.704 -66.100 -30.935 1.00108.40 C
ANISOU 183 CB ASP A 21 13533 13884 13771 -4151 -1823 1873 C
ATOM 184 CG ASP A 21 -27.953 -65.272 -31.227 1.00120.97 C
ANISOU 184 CG ASP A 21 14587 15813 15562 -4205 -1723 1948 C
ATOM 185 OD1 ASP A 21 -28.375 -64.497 -30.338 1.00121.65 O
ANISOU 185 OD1 ASP A 21 14404 16187 15632 -4125 -1313 2075 O
ATOM 186 OD2 ASP A 21 -28.525 -65.425 -32.334 1.00128.70 O
ANISOU 186 OD2 ASP A 21 15422 16752 16727 -4340 -2057 1889 O
ATOM 187 N ASN A 22 -23.608 -66.711 -31.092 1.00 99.55 N
ANISOU 187 N ASN A 22 13333 12173 12319 -3626 -2024 1536 N
ATOM 188 CA ASN A 22 -22.436 -67.582 -30.904 1.00 98.77 C
ANISOU 188 CA ASN A 22 13607 11678 12242 -3536 -2146 1538 C
ATOM 189 C ASN A 22 -21.086 -66.890 -31.282 1.00 97.37 C
ANISOU 189 C ASN A 22 13582 11480 11936 -3107 -2116 1310 C
ATOM 190 O ASN A 22 -21.072 -65.788 -31.857 1.00 93.54 O
ANISOU 190 O ASN A 22 12959 11258 11323 -2901 -2030 1118 O
ATOM 191 CB ASN A 22 -22.601 -68.916 -31.657 1.00101.58 C
ANISOU 191 CB ASN A 22 14170 11581 12844 -3759 -2418 1472 C
ATOM 192 CG ASN A 22 -22.970 -68.821 -33.121 1.00121.18 C
ANISOU 192 CG ASN A 22 16665 14020 15356 -3782 -2595 1157 C
ATOM 193 OD1 ASN A 22 -22.241 -68.262 -33.941 1.00110.69 O
ANISOU 193 OD1 ASN A 22 15459 12689 13908 -3488 -2589 872 O
ATOM 194 ND2 ASN A 22 -24.072 -69.453 -33.499 1.00117.02 N
ANISOU 194 ND2 ASN A 22 16053 13423 14986 -4174 -2783 1216 N
ATOM 195 N ALA A 23 -19.953 -67.546 -30.910 1.00 92.70 N
ANISOU 195 N ALA A 23 13240 10561 11420 -2982 -2191 1380 N
ATOM 196 CA ALA A 23 -18.591 -67.067 -31.167 1.00 89.00 C
ANISOU 196 CA ALA A 23 12874 10022 10919 -2601 -2169 1231 C
ATOM 197 C ALA A 23 -18.282 -67.062 -32.649 1.00 90.14 C
ANISOU 197 C ALA A 23 13113 10001 11135 -2423 -2207 862 C
ATOM 198 O ALA A 23 -17.592 -66.163 -33.114 1.00 86.54 O
ANISOU 198 O ALA A 23 12623 9688 10569 -2139 -2111 685 O
ATOM 199 CB ALA A 23 -17.572 -67.919 -30.427 1.00 91.43 C
ANISOU 199 CB ALA A 23 13361 9982 11396 -2544 -2278 1462 C
ATOM 200 N ALA A 24 -18.811 -68.052 -33.388 1.00 88.83 N
ANISOU 200 N ALA A 24 13097 9533 11123 -2626 -2342 746 N
ATOM 201 CA ALA A 24 -18.652 -68.205 -34.833 1.00 88.59 C
ANISOU 201 CA ALA A 24 13259 9308 11092 -2551 -2383 373 C
ATOM 202 C ALA A 24 -19.054 -66.942 -35.581 1.00 87.35 C
ANISOU 202 C ALA A 24 12942 9569 10676 -2476 -2337 198 C
ATOM 203 O ALA A 24 -18.325 -66.548 -36.490 1.00 85.57 O
ANISOU 203 O ALA A 24 12854 9302 10356 -2241 -2263 -65 O
ATOM 204 CB ALA A 24 -19.478 -69.376 -35.326 1.00 93.64 C
ANISOU 204 CB ALA A 24 14083 9623 11873 -2909 -2574 314 C
ATOM 205 N GLN A 25 -20.182 -66.292 -35.182 1.00 81.70 N
ANISOU 205 N GLN A 25 11923 9242 9876 -2662 -2353 367 N
ATOM 206 CA GLN A 25 -20.653 -65.060 -35.821 1.00 78.82 C
ANISOU 206 CA GLN A 25 11356 9255 9336 -2585 -2333 267 C
ATOM 207 C GLN A 25 -19.898 -63.836 -35.288 1.00 77.82 C
ANISOU 207 C GLN A 25 11098 9387 9081 -2252 -2111 295 C
ATOM 208 O GLN A 25 -19.631 -62.924 -36.072 1.00 75.16 O
ANISOU 208 O GLN A 25 10746 9200 8610 -2064 -2078 130 O
ATOM 209 CB GLN A 25 -22.188 -64.873 -35.763 1.00 81.85 C
ANISOU 209 CB GLN A 25 11420 9899 9781 -2895 -2440 435 C
ATOM 210 CG GLN A 25 -22.891 -65.134 -34.445 1.00 93.87 C
ANISOU 210 CG GLN A 25 12705 11530 11433 -3089 -2326 754 C
ATOM 211 CD GLN A 25 -24.336 -65.501 -34.686 1.00111.59 C
ANISOU 211 CD GLN A 25 14690 13857 13852 -3471 -2492 897 C
ATOM 212 OE1 GLN A 25 -24.677 -66.657 -34.948 1.00108.20 O
ANISOU 212 OE1 GLN A 25 14410 13144 13559 -3779 -2706 918 O
ATOM 213 NE2 GLN A 25 -25.217 -64.520 -34.645 1.00106.07 N
ANISOU 213 NE2 GLN A 25 13579 13523 13199 -3463 -2408 1006 N
ATOM 214 N VAL A 26 -19.488 -63.842 -33.994 1.00 74.31 N
ANISOU 214 N VAL A 26 10610 8967 8657 -2203 -1986 504 N
ATOM 215 CA VAL A 26 -18.652 -62.774 -33.401 1.00 70.94 C
ANISOU 215 CA VAL A 26 10124 8734 8095 -1935 -1817 526 C
ATOM 216 C VAL A 26 -17.292 -62.778 -34.162 1.00 75.55 C
ANISOU 216 C VAL A 26 10894 9107 8705 -1652 -1823 331 C
ATOM 217 O VAL A 26 -16.950 -61.777 -34.796 1.00 73.42 O
ANISOU 217 O VAL A 26 10573 9002 8319 -1454 -1744 184 O
ATOM 218 CB VAL A 26 -18.480 -62.900 -31.850 1.00 73.71 C
ANISOU 218 CB VAL A 26 10470 9135 8400 -2017 -1736 799 C
ATOM 219 CG1 VAL A 26 -17.526 -61.847 -31.305 1.00 70.30 C
ANISOU 219 CG1 VAL A 26 10038 8866 7808 -1786 -1624 796 C
ATOM 220 CG2 VAL A 26 -19.819 -62.807 -31.131 1.00 75.03 C
ANISOU 220 CG2 VAL A 26 10447 9532 8530 -2286 -1625 974 C
ATOM 221 N LYS A 27 -16.587 -63.940 -34.167 1.00 74.85 N
ANISOU 221 N LYS A 27 11005 8628 8805 -1637 -1895 337 N
ATOM 222 CA LYS A 27 -15.315 -64.183 -34.864 1.00 75.46 C
ANISOU 222 CA LYS A 27 11234 8431 9007 -1367 -1842 164 C
ATOM 223 C LYS A 27 -15.419 -63.815 -36.359 1.00 80.88 C
ANISOU 223 C LYS A 27 12025 9146 9558 -1301 -1786 -162 C
ATOM 224 O LYS A 27 -14.464 -63.282 -36.930 1.00 78.72 O
ANISOU 224 O LYS A 27 11779 8874 9259 -1044 -1646 -305 O
ATOM 225 CB LYS A 27 -14.907 -65.661 -34.712 1.00 81.12 C
ANISOU 225 CB LYS A 27 12138 8661 10023 -1405 -1919 223 C
ATOM 226 CG LYS A 27 -13.416 -65.942 -34.870 1.00 98.34 C
ANISOU 226 CG LYS A 27 14370 10534 12462 -1080 -1825 186 C
ATOM 227 CD LYS A 27 -13.085 -66.594 -36.215 1.00110.67 C
ANISOU 227 CD LYS A 27 16178 11732 14140 -974 -1698 -167 C
ATOM 228 CE LYS A 27 -11.602 -66.856 -36.357 1.00125.12 C
ANISOU 228 CE LYS A 27 17994 13240 16305 -617 -1526 -195 C
ATOM 229 NZ LYS A 27 -11.199 -67.063 -37.771 1.00139.40 N
ANISOU 229 NZ LYS A 27 20041 14813 18110 -472 -1271 -606 N
ATOM 230 N ASP A 28 -16.592 -64.079 -36.971 1.00 80.61 N
ANISOU 230 N ASP A 28 12046 9154 9429 -1565 -1914 -249 N
ATOM 231 CA ASP A 28 -16.867 -63.789 -38.378 1.00 81.80 C
ANISOU 231 CA ASP A 28 12345 9350 9384 -1600 -1944 -517 C
ATOM 232 C ASP A 28 -16.899 -62.287 -38.634 1.00 83.56 C
ANISOU 232 C ASP A 28 12372 9972 9404 -1454 -1878 -510 C
ATOM 233 O ASP A 28 -16.419 -61.829 -39.676 1.00 83.74 O
ANISOU 233 O ASP A 28 12542 10014 9263 -1333 -1805 -709 O
ATOM 234 CB ASP A 28 -18.203 -64.417 -38.818 1.00 86.23 C
ANISOU 234 CB ASP A 28 12964 9886 9913 -1985 -2191 -530 C
ATOM 235 CG ASP A 28 -18.140 -65.191 -40.115 1.00 96.78 C
ANISOU 235 CG ASP A 28 14708 10921 11145 -2114 -2268 -846 C
ATOM 236 OD1 ASP A 28 -18.683 -66.318 -40.158 1.00100.98 O
ANISOU 236 OD1 ASP A 28 15413 11163 11790 -2394 -2429 -873 O
ATOM 237 OD2 ASP A 28 -17.571 -64.662 -41.098 1.00101.67 O
ANISOU 237 OD2 ASP A 28 15504 11584 11542 -1965 -2161 -1072 O
ATOM 238 N ALA A 29 -17.475 -61.527 -37.694 1.00 77.75 N
ANISOU 238 N ALA A 29 11330 9534 8677 -1476 -1875 -284 N
ATOM 239 CA ALA A 29 -17.572 -60.084 -37.831 1.00 75.41 C
ANISOU 239 CA ALA A 29 10838 9569 8248 -1334 -1804 -260 C
ATOM 240 C ALA A 29 -16.184 -59.439 -37.715 1.00 77.83 C
ANISOU 240 C ALA A 29 11179 9862 8530 -1031 -1620 -310 C
ATOM 241 O ALA A 29 -15.769 -58.739 -38.644 1.00 77.11 O
ANISOU 241 O ALA A 29 11143 9846 8310 -900 -1563 -438 O
ATOM 242 CB ALA A 29 -18.518 -59.526 -36.789 1.00 75.52 C
ANISOU 242 CB ALA A 29 10545 9834 8316 -1424 -1778 -39 C
ATOM 243 N LEU A 30 -15.450 -59.734 -36.618 1.00 73.02 N
ANISOU 243 N LEU A 30 10545 9148 8050 -952 -1554 -184 N
ATOM 244 CA LEU A 30 -14.117 -59.208 -36.362 1.00 71.42 C
ANISOU 244 CA LEU A 30 10326 8922 7890 -708 -1437 -173 C
ATOM 245 C LEU A 30 -13.140 -59.491 -37.541 1.00 75.91 C
ANISOU 245 C LEU A 30 11056 9281 8505 -534 -1330 -380 C
ATOM 246 O LEU A 30 -12.384 -58.594 -37.916 1.00 74.28 O
ANISOU 246 O LEU A 30 10796 9176 8250 -356 -1208 -426 O
ATOM 247 CB LEU A 30 -13.545 -59.790 -35.040 1.00 72.24 C
ANISOU 247 CB LEU A 30 10407 8896 8146 -722 -1482 41 C
ATOM 248 CG LEU A 30 -13.843 -59.139 -33.649 1.00 75.71 C
ANISOU 248 CG LEU A 30 10733 9565 8468 -821 -1493 248 C
ATOM 249 CD1 LEU A 30 -13.680 -57.631 -33.636 1.00 73.05 C
ANISOU 249 CD1 LEU A 30 10293 9486 7977 -705 -1389 194 C
ATOM 250 CD2 LEU A 30 -15.170 -59.543 -33.119 1.00 79.83 C
ANISOU 250 CD2 LEU A 30 11227 10175 8929 -1073 -1517 342 C
ATOM 251 N THR A 31 -13.161 -60.710 -38.128 1.00 74.84 N
ANISOU 251 N THR A 31 11133 8840 8463 -596 -1342 -513 N
ATOM 252 CA THR A 31 -12.258 -61.057 -39.245 1.00 76.60 C
ANISOU 252 CA THR A 31 11558 8825 8719 -433 -1153 -754 C
ATOM 253 C THR A 31 -12.630 -60.312 -40.550 1.00 80.82 C
ANISOU 253 C THR A 31 12230 9554 8922 -478 -1106 -952 C
ATOM 254 O THR A 31 -11.758 -60.097 -41.400 1.00 80.98 O
ANISOU 254 O THR A 31 12374 9504 8890 -315 -879 -1117 O
ATOM 255 CB THR A 31 -12.179 -62.570 -39.486 1.00 83.25 C
ANISOU 255 CB THR A 31 12645 9231 9755 -490 -1144 -878 C
ATOM 256 OG1 THR A 31 -13.475 -63.147 -39.344 1.00 84.82 O
ANISOU 256 OG1 THR A 31 12923 9436 9870 -805 -1377 -848 O
ATOM 257 CG2 THR A 31 -11.166 -63.257 -38.576 1.00 77.83 C
ANISOU 257 CG2 THR A 31 11846 8250 9478 -309 -1097 -702 C
ATOM 258 N LYS A 32 -13.909 -59.912 -40.689 1.00 76.74 N
ANISOU 258 N LYS A 32 11674 9279 8204 -703 -1318 -903 N
ATOM 259 CA LYS A 32 -14.404 -59.131 -41.822 1.00 76.47 C
ANISOU 259 CA LYS A 32 11734 9459 7863 -783 -1374 -998 C
ATOM 260 C LYS A 32 -14.178 -57.637 -41.514 1.00 75.62 C
ANISOU 260 C LYS A 32 11361 9650 7721 -618 -1313 -842 C
ATOM 261 O LYS A 32 -14.023 -56.828 -42.432 1.00 75.06 O
ANISOU 261 O LYS A 32 11365 9713 7443 -577 -1267 -896 O
ATOM 262 CB LYS A 32 -15.890 -59.450 -42.093 1.00 80.57 C
ANISOU 262 CB LYS A 32 12271 10066 8275 -1108 -1682 -960 C
ATOM 263 CG LYS A 32 -16.382 -59.046 -43.481 1.00 86.75 C
ANISOU 263 CG LYS A 32 13267 10972 8721 -1267 -1824 -1072 C
ATOM 264 CD LYS A 32 -17.866 -59.302 -43.626 1.00 95.02 C
ANISOU 264 CD LYS A 32 14237 12126 9742 -1605 -2196 -961 C
ATOM 265 CE LYS A 32 -18.371 -58.942 -44.999 1.00107.81 C
ANISOU 265 CE LYS A 32 16088 13867 11007 -1812 -2427 -1025 C
ATOM 266 NZ LYS A 32 -19.761 -59.425 -45.209 1.00119.21 N
ANISOU 266 NZ LYS A 32 17469 15361 12464 -2194 -2850 -913 N
ATOM 267 N MET A 33 -14.153 -57.288 -40.213 1.00 69.19 N
ANISOU 267 N MET A 33 10280 8918 7090 -548 -1311 -651 N
ATOM 268 CA MET A 33 -13.885 -55.936 -39.716 1.00 66.50 C
ANISOU 268 CA MET A 33 9724 8795 6746 -407 -1242 -527 C
ATOM 269 C MET A 33 -12.410 -55.600 -39.904 1.00 69.68 C
ANISOU 269 C MET A 33 10154 9115 7204 -191 -1043 -573 C
ATOM 270 O MET A 33 -12.091 -54.493 -40.336 1.00 67.57 O
ANISOU 270 O MET A 33 9839 8990 6845 -101 -970 -560 O
ATOM 271 CB MET A 33 -14.267 -55.809 -38.235 1.00 67.44 C
ANISOU 271 CB MET A 33 9644 8991 6990 -444 -1275 -352 C
ATOM 272 CG MET A 33 -15.669 -55.338 -38.011 1.00 70.89 C
ANISOU 272 CG MET A 33 9917 9620 7396 -581 -1367 -260 C
ATOM 273 SD MET A 33 -16.123 -55.485 -36.263 1.00 74.69 S
ANISOU 273 SD MET A 33 10254 10153 7972 -669 -1313 -93 S
ATOM 274 CE MET A 33 -15.219 -54.089 -35.547 1.00 68.79 C
ANISOU 274 CE MET A 33 9455 9509 7173 -483 -1161 -72 C
ATOM 275 N ARG A 34 -11.516 -56.570 -39.590 1.00 68.08 N
ANISOU 275 N ARG A 34 10001 8663 7201 -111 -960 -599 N
ATOM 276 CA ARG A 34 -10.065 -56.455 -39.716 1.00 68.66 C
ANISOU 276 CA ARG A 34 10028 8617 7441 100 -763 -607 C
ATOM 277 C ARG A 34 -9.688 -56.245 -41.172 1.00 74.55 C
ANISOU 277 C ARG A 34 10956 9348 8023 163 -553 -802 C
ATOM 278 O ARG A 34 -8.883 -55.361 -41.475 1.00 74.52 O
ANISOU 278 O ARG A 34 10859 9431 8023 290 -396 -771 O
ATOM 279 CB ARG A 34 -9.370 -57.701 -39.161 1.00 71.56 C
ANISOU 279 CB ARG A 34 10388 8675 8128 171 -742 -567 C
ATOM 280 CG ARG A 34 -8.011 -57.394 -38.557 1.00 81.25 C
ANISOU 280 CG ARG A 34 11385 9843 9642 357 -669 -407 C
ATOM 281 CD ARG A 34 -7.078 -58.588 -38.582 1.00 88.02 C
ANISOU 281 CD ARG A 34 12224 10333 10888 510 -561 -399 C
ATOM 282 NE ARG A 34 -5.683 -58.151 -38.499 1.00 96.61 N
ANISOU 282 NE ARG A 34 13052 11376 12280 716 -426 -275 N
ATOM 283 CZ ARG A 34 -4.758 -58.700 -37.720 1.00108.56 C
ANISOU 283 CZ ARG A 34 14340 12678 14228 829 -506 -47 C
ATOM 284 NH1 ARG A 34 -5.058 -59.742 -36.955 1.00104.52 N
ANISOU 284 NH1 ARG A 34 13873 11962 13877 763 -710 80 N
ATOM 285 NH2 ARG A 34 -3.523 -58.221 -37.710 1.00 87.46 N
ANISOU 285 NH2 ARG A 34 11377 9989 11863 995 -403 91 N
ATOM 286 N ALA A 35 -10.307 -57.028 -42.077 1.00 72.19 N
ANISOU 286 N ALA A 35 10943 8943 7543 36 -558 -998 N
ATOM 287 CA ALA A 35 -10.107 -56.915 -43.520 1.00 73.54 C
ANISOU 287 CA ALA A 35 11396 9106 7439 25 -367 -1208 C
ATOM 288 C ALA A 35 -10.514 -55.507 -43.999 1.00 74.58 C
ANISOU 288 C ALA A 35 11480 9562 7295 -31 -453 -1106 C
ATOM 289 O ALA A 35 -9.774 -54.878 -44.769 1.00 76.10 O
ANISOU 289 O ALA A 35 11744 9808 7362 54 -227 -1146 O
ATOM 290 CB ALA A 35 -10.921 -57.982 -44.238 1.00 77.19 C
ANISOU 290 CB ALA A 35 12221 9404 7704 -186 -455 -1426 C
ATOM 291 N ALA A 36 -11.665 -55.001 -43.491 1.00 66.53 N
ANISOU 291 N ALA A 36 10309 8739 6231 -162 -754 -949 N
ATOM 292 CA ALA A 36 -12.194 -53.681 -43.806 1.00 64.65 C
ANISOU 292 CA ALA A 36 9975 8761 5827 -196 -873 -810 C
ATOM 293 C ALA A 36 -11.226 -52.597 -43.315 1.00 68.03 C
ANISOU 293 C ALA A 36 10188 9257 6404 -2 -709 -688 C
ATOM 294 O ALA A 36 -10.758 -51.816 -44.141 1.00 69.05 O
ANISOU 294 O ALA A 36 10390 9466 6381 34 -594 -673 O
ATOM 295 CB ALA A 36 -13.578 -53.501 -43.196 1.00 64.31 C
ANISOU 295 CB ALA A 36 9747 8853 5836 -331 -1166 -666 C
ATOM 296 N ALA A 37 -10.851 -52.605 -42.001 1.00 62.14 N
ANISOU 296 N ALA A 37 9211 8465 5932 88 -706 -594 N
ATOM 297 CA ALA A 37 -9.902 -51.654 -41.405 1.00 59.50 C
ANISOU 297 CA ALA A 37 8686 8168 5753 219 -608 -478 C
ATOM 298 C ALA A 37 -8.602 -51.567 -42.225 1.00 66.93 C
ANISOU 298 C ALA A 37 9674 9033 6724 337 -342 -529 C
ATOM 299 O ALA A 37 -8.165 -50.468 -42.570 1.00 65.79 O
ANISOU 299 O ALA A 37 9473 8985 6538 374 -262 -449 O
ATOM 300 CB ALA A 37 -9.594 -52.054 -39.978 1.00 58.69 C
ANISOU 300 CB ALA A 37 8427 7989 5884 237 -677 -392 C
ATOM 301 N LEU A 38 -8.026 -52.728 -42.592 1.00 67.76 N
ANISOU 301 N LEU A 38 9886 8943 6918 393 -173 -663 N
ATOM 302 CA LEU A 38 -6.793 -52.811 -43.387 1.00 70.40 C
ANISOU 302 CA LEU A 38 10247 9171 7329 525 173 -735 C
ATOM 303 C LEU A 38 -6.995 -52.260 -44.793 1.00 76.79 C
ANISOU 303 C LEU A 38 11322 10101 7755 448 318 -829 C
ATOM 304 O LEU A 38 -6.072 -51.634 -45.324 1.00 78.30 O
ANISOU 304 O LEU A 38 11467 10323 7960 525 583 -790 O
ATOM 305 CB LEU A 38 -6.275 -54.256 -43.463 1.00 72.74 C
ANISOU 305 CB LEU A 38 10621 9177 7841 621 355 -884 C
ATOM 306 CG LEU A 38 -5.528 -54.764 -42.247 1.00 76.04 C
ANISOU 306 CG LEU A 38 10738 9430 8725 745 289 -725 C
ATOM 307 CD1 LEU A 38 -5.616 -56.255 -42.168 1.00 78.44 C
ANISOU 307 CD1 LEU A 38 11169 9433 9201 780 322 -849 C
ATOM 308 CD2 LEU A 38 -4.087 -54.318 -42.261 1.00 78.17 C
ANISOU 308 CD2 LEU A 38 10722 9655 9323 921 528 -602 C
ATOM 309 N ASP A 39 -8.195 -52.477 -45.388 1.00 73.36 N
ANISOU 309 N ASP A 39 11156 9741 6977 268 123 -919 N
ATOM 310 CA ASP A 39 -8.494 -51.946 -46.716 1.00 75.31 C
ANISOU 310 CA ASP A 39 11697 10121 6797 138 168 -961 C
ATOM 311 C ASP A 39 -8.761 -50.447 -46.642 1.00 77.22 C
ANISOU 311 C ASP A 39 11768 10579 6992 120 6 -714 C
ATOM 312 O ASP A 39 -8.341 -49.724 -47.547 1.00 79.93 O
ANISOU 312 O ASP A 39 12241 11009 7122 93 162 -663 O
ATOM 313 CB ASP A 39 -9.675 -52.668 -47.404 1.00 79.04 C
ANISOU 313 CB ASP A 39 12513 10596 6924 -96 -63 -1101 C
ATOM 314 CG ASP A 39 -9.797 -52.337 -48.897 1.00 87.77 C
ANISOU 314 CG ASP A 39 14023 11808 7516 -271 -2 -1165 C
ATOM 315 OD1 ASP A 39 -8.803 -52.547 -49.642 1.00 86.90 O
ANISOU 315 OD1 ASP A 39 14133 11611 7275 -213 420 -1322 O
ATOM 316 OD2 ASP A 39 -10.882 -51.872 -49.316 1.00 96.96 O
ANISOU 316 OD2 ASP A 39 15279 13142 8420 -475 -370 -1039 O
ATOM 317 N ALA A 40 -9.469 -49.982 -45.582 1.00 69.07 N
ANISOU 317 N ALA A 40 10472 9612 6158 129 -275 -564 N
ATOM 318 CA ALA A 40 -9.791 -48.566 -45.367 1.00 66.54 C
ANISOU 318 CA ALA A 40 9982 9430 5872 140 -416 -349 C
ATOM 319 C ALA A 40 -8.512 -47.770 -45.127 1.00 70.19 C
ANISOU 319 C ALA A 40 10286 9863 6519 261 -189 -263 C
ATOM 320 O ALA A 40 -8.413 -46.622 -45.563 1.00 70.42 O
ANISOU 320 O ALA A 40 10304 9969 6484 247 -190 -113 O
ATOM 321 CB ALA A 40 -10.748 -48.407 -44.204 1.00 64.63 C
ANISOU 321 CB ALA A 40 9517 9214 5827 141 -660 -271 C
ATOM 322 N GLN A 41 -7.509 -48.418 -44.500 1.00 65.73 N
ANISOU 322 N GLN A 41 9594 9171 6210 365 -12 -329 N
ATOM 323 CA GLN A 41 -6.187 -47.873 -44.215 1.00 64.69 C
ANISOU 323 CA GLN A 41 9255 8994 6330 459 182 -232 C
ATOM 324 C GLN A 41 -5.444 -47.562 -45.519 1.00 71.09 C
ANISOU 324 C GLN A 41 10200 9835 6976 456 500 -232 C
ATOM 325 O GLN A 41 -4.670 -46.605 -45.547 1.00 71.96 O
ANISOU 325 O GLN A 41 10159 9973 7209 468 604 -78 O
ATOM 326 CB GLN A 41 -5.408 -48.881 -43.376 1.00 65.55 C
ANISOU 326 CB GLN A 41 9191 8946 6768 558 249 -274 C
ATOM 327 CG GLN A 41 -4.228 -48.302 -42.626 1.00 69.22 C
ANISOU 327 CG GLN A 41 9347 9372 7583 612 274 -106 C
ATOM 328 CD GLN A 41 -3.547 -49.378 -41.828 1.00 80.03 C
ANISOU 328 CD GLN A 41 10534 10578 9296 700 268 -92 C
ATOM 329 OE1 GLN A 41 -3.106 -50.406 -42.364 1.00 70.29 O
ANISOU 329 OE1 GLN A 41 9331 9205 8172 809 507 -199 O
ATOM 330 NE2 GLN A 41 -3.488 -49.181 -40.519 1.00 74.55 N
ANISOU 330 NE2 GLN A 41 9675 9878 8772 646 -10 41 N
ATOM 331 N LYS A 42 -5.692 -48.356 -46.595 1.00 69.03 N
ANISOU 331 N LYS A 42 10254 9561 6411 409 662 -407 N
ATOM 332 CA LYS A 42 -5.095 -48.193 -47.941 1.00 72.22 C
ANISOU 332 CA LYS A 42 10896 10003 6540 367 1021 -449 C
ATOM 333 C LYS A 42 -5.717 -47.013 -48.705 1.00 76.13 C
ANISOU 333 C LYS A 42 11565 10679 6683 210 857 -274 C
ATOM 334 O LYS A 42 -5.212 -46.627 -49.770 1.00 78.01 O
ANISOU 334 O LYS A 42 12003 10979 6656 137 1129 -238 O
ATOM 335 CB LYS A 42 -5.276 -49.476 -48.793 1.00 77.14 C
ANISOU 335 CB LYS A 42 11900 10529 6880 323 1224 -739 C
ATOM 336 CG LYS A 42 -4.372 -50.641 -48.405 1.00 91.69 C
ANISOU 336 CG LYS A 42 13615 12131 9092 511 1540 -912 C
ATOM 337 CD LYS A 42 -4.700 -51.905 -49.199 1.00100.02 C
ANISOU 337 CD LYS A 42 15106 13032 9864 452 1716 -1239 C
ATOM 338 CE LYS A 42 -3.634 -52.962 -49.069 1.00107.16 C
ANISOU 338 CE LYS A 42 15904 13645 11168 677 2155 -1410 C
ATOM 339 NZ LYS A 42 -3.921 -54.141 -49.925 1.00122.13 N
ANISOU 339 NZ LYS A 42 18297 15338 12768 612 2388 -1775 N
ATOM 340 N ALA A 43 -6.838 -46.476 -48.177 1.00 69.96 N
ANISOU 340 N ALA A 43 10708 9967 5906 157 428 -151 N
ATOM 341 CA ALA A 43 -7.603 -45.409 -48.802 1.00 70.36 C
ANISOU 341 CA ALA A 43 10877 10147 5710 31 193 57 C
ATOM 342 C ALA A 43 -7.065 -44.021 -48.483 1.00 73.41 C
ANISOU 342 C ALA A 43 11039 10532 6322 80 212 298 C
ATOM 343 O ALA A 43 -6.224 -43.855 -47.600 1.00 71.72 O
ANISOU 343 O ALA A 43 10554 10231 6465 187 338 302 O
ATOM 344 CB ALA A 43 -9.060 -45.507 -48.374 1.00 69.57 C
ANISOU 344 CB ALA A 43 10738 10085 5611 -18 -236 89 C
ATOM 345 N THR A 44 -7.554 -43.022 -49.229 1.00 71.28 N
ANISOU 345 N THR A 44 10897 10340 5844 -26 53 522 N
ATOM 346 CA THR A 44 -7.242 -41.618 -49.003 1.00 70.67 C
ANISOU 346 CA THR A 44 10652 10219 5978 -4 20 772 C
ATOM 347 C THR A 44 -8.573 -40.889 -48.676 1.00 74.30 C
ANISOU 347 C THR A 44 11034 10663 6535 8 -389 935 C
ATOM 348 O THR A 44 -9.489 -40.914 -49.507 1.00 75.30 O
ANISOU 348 O THR A 44 11346 10880 6383 -99 -619 1044 O
ATOM 349 CB THR A 44 -6.430 -40.992 -50.150 1.00 78.50 C
ANISOU 349 CB THR A 44 11830 11267 6729 -122 276 941 C
ATOM 350 OG1 THR A 44 -6.509 -39.566 -50.043 1.00 71.92 O
ANISOU 350 OG1 THR A 44 10887 10369 6071 -138 125 1232 O
ATOM 351 CG2 THR A 44 -6.898 -41.442 -51.532 1.00 86.16 C
ANISOU 351 CG2 THR A 44 13229 12377 7129 -302 274 940 C
ATOM 352 N PRO A 45 -8.706 -40.292 -47.451 1.00 69.17 N
ANISOU 352 N PRO A 45 10111 9885 6286 131 -477 944 N
ATOM 353 CA PRO A 45 -9.960 -39.595 -47.081 1.00 69.21 C
ANISOU 353 CA PRO A 45 10001 9832 6464 189 -774 1076 C
ATOM 354 C PRO A 45 -10.329 -38.434 -48.022 1.00 78.84 C
ANISOU 354 C PRO A 45 11309 11030 7617 132 -932 1406 C
ATOM 355 O PRO A 45 -9.439 -37.786 -48.570 1.00 79.59 O
ANISOU 355 O PRO A 45 11502 11101 7637 62 -780 1543 O
ATOM 356 CB PRO A 45 -9.690 -39.095 -45.669 1.00 68.43 C
ANISOU 356 CB PRO A 45 9685 9571 6746 303 -713 985 C
ATOM 357 CG PRO A 45 -8.591 -39.927 -45.186 1.00 71.17 C
ANISOU 357 CG PRO A 45 10007 9938 7097 291 -504 792 C
ATOM 358 CD PRO A 45 -7.731 -40.229 -46.349 1.00 68.21 C
ANISOU 358 CD PRO A 45 9787 9656 6474 206 -310 836 C
ATOM 359 N PRO A 46 -11.651 -38.187 -48.220 1.00 79.93 N
ANISOU 359 N PRO A 46 11387 11172 7811 153 -1247 1570 N
ATOM 360 CA PRO A 46 -12.100 -37.191 -49.207 1.00 84.04 C
ANISOU 360 CA PRO A 46 11991 11670 8269 86 -1474 1947 C
ATOM 361 C PRO A 46 -11.439 -35.811 -49.197 1.00 90.80 C
ANISOU 361 C PRO A 46 12825 12333 9342 123 -1376 2156 C
ATOM 362 O PRO A 46 -11.244 -35.263 -50.285 1.00 95.02 O
ANISOU 362 O PRO A 46 13555 12904 9646 -15 -1447 2445 O
ATOM 363 CB PRO A 46 -13.591 -37.060 -48.910 1.00 86.81 C
ANISOU 363 CB PRO A 46 12109 11980 8894 185 -1802 2075 C
ATOM 364 CG PRO A 46 -13.987 -38.416 -48.445 1.00 89.15 C
ANISOU 364 CG PRO A 46 12364 12410 9098 165 -1796 1786 C
ATOM 365 CD PRO A 46 -12.811 -38.921 -47.655 1.00 81.43 C
ANISOU 365 CD PRO A 46 11417 11403 8122 211 -1430 1461 C
ATOM 366 N LYS A 47 -11.122 -35.235 -48.031 1.00 85.39 N
ANISOU 366 N LYS A 47 11948 11436 9060 269 -1232 2030 N
ATOM 367 CA LYS A 47 -10.517 -33.895 -48.023 1.00 86.90 C
ANISOU 367 CA LYS A 47 12142 11397 9478 271 -1165 2224 C
ATOM 368 C LYS A 47 -8.982 -33.961 -47.823 1.00 88.52 C
ANISOU 368 C LYS A 47 12402 11611 9620 166 -860 2090 C
ATOM 369 O LYS A 47 -8.369 -32.968 -47.417 1.00 88.87 O
ANISOU 369 O LYS A 47 12402 11435 9928 156 -785 2155 O
ATOM 370 CB LYS A 47 -11.189 -33.002 -46.959 1.00 89.68 C
ANISOU 370 CB LYS A 47 12293 11446 10333 468 -1218 2198 C
ATOM 371 N LEU A 48 -8.370 -35.122 -48.147 1.00 82.55 N
ANISOU 371 N LEU A 48 11730 11086 8549 82 -689 1919 N
ATOM 372 CA LEU A 48 -6.931 -35.357 -48.000 1.00 80.49 C
ANISOU 372 CA LEU A 48 11443 10851 8288 5 -385 1814 C
ATOM 373 C LEU A 48 -6.283 -35.803 -49.320 1.00 85.81 C
ANISOU 373 C LEU A 48 12326 11721 8559 -143 -170 1909 C
ATOM 374 O LEU A 48 -5.195 -36.383 -49.305 1.00 84.31 O
ANISOU 374 O LEU A 48 12085 11594 8353 -175 137 1781 O
ATOM 375 CB LEU A 48 -6.641 -36.380 -46.880 1.00 76.84 C
ANISOU 375 CB LEU A 48 10828 10417 7951 87 -300 1482 C
ATOM 376 CG LEU A 48 -6.972 -35.981 -45.448 1.00 79.00 C
ANISOU 376 CG LEU A 48 10946 10506 8564 180 -418 1348 C
ATOM 377 CD1 LEU A 48 -6.356 -36.948 -44.473 1.00 76.82 C
ANISOU 377 CD1 LEU A 48 10557 10276 8356 192 -330 1099 C
ATOM 378 CD2 LEU A 48 -6.455 -34.600 -45.114 1.00 83.20 C
ANISOU 378 CD2 LEU A 48 11445 10800 9367 125 -420 1487 C
ATOM 379 N GLU A 49 -6.927 -35.487 -50.461 1.00 86.51 N
ANISOU 379 N GLU A 49 12650 11891 8331 -243 -321 2152 N
ATOM 380 CA GLU A 49 -6.391 -35.772 -51.806 1.00 90.24 C
ANISOU 380 CA GLU A 49 13420 12547 8322 -432 -102 2259 C
ATOM 381 C GLU A 49 -5.160 -34.860 -52.071 1.00 96.46 C
ANISOU 381 C GLU A 49 14167 13257 9226 -538 184 2470 C
ATOM 382 O GLU A 49 -4.161 -35.308 -52.641 1.00 96.54 O
ANISOU 382 O GLU A 49 14259 13388 9033 -635 584 2418 O
ATOM 383 CB GLU A 49 -7.484 -35.603 -52.892 1.00 94.77 C
ANISOU 383 CB GLU A 49 14287 13226 8495 -563 -429 2510 C
ATOM 384 CG GLU A 49 -8.071 -34.197 -53.027 1.00110.43 C
ANISOU 384 CG GLU A 49 16226 15040 10694 -570 -752 2927 C
ATOM 385 CD GLU A 49 -9.583 -34.029 -53.021 1.00140.45 C
ANISOU 385 CD GLU A 49 19967 18801 14595 -496 -1247 3088 C
ATOM 386 OE1 GLU A 49 -10.313 -35.044 -53.112 1.00141.90 O
ANISOU 386 OE1 GLU A 49 20206 19144 14565 -509 -1402 2917 O
ATOM 387 OE2 GLU A 49 -10.037 -32.862 -52.972 1.00136.27 O
ANISOU 387 OE2 GLU A 49 19325 18062 14388 -435 -1481 3412 O
ATOM 388 N ASP A 50 -5.241 -33.605 -51.558 1.00 94.46 N
ANISOU 388 N ASP A 50 13759 12772 9362 -510 1 2685 N
ATOM 389 CA ASP A 50 -4.271 -32.510 -51.610 1.00 96.83 C
ANISOU 389 CA ASP A 50 13983 12918 9891 -625 158 2927 C
ATOM 390 C ASP A 50 -3.079 -32.727 -50.662 1.00 98.17 C
ANISOU 390 C ASP A 50 13856 13025 10419 -602 414 2720 C
ATOM 391 O ASP A 50 -2.090 -32.002 -50.775 1.00100.45 O
ANISOU 391 O ASP A 50 14052 13223 10893 -741 588 2910 O
ATOM 392 CB ASP A 50 -4.973 -31.183 -51.237 1.00100.18 C
ANISOU 392 CB ASP A 50 14359 13043 10661 -576 -183 3168 C
ATOM 393 CG ASP A 50 -5.151 -30.962 -49.732 1.00116.87 C
ANISOU 393 CG ASP A 50 16223 14918 13263 -406 -299 2917 C
ATOM 394 OD1 ASP A 50 -4.411 -30.121 -49.160 1.00119.97 O
ANISOU 394 OD1 ASP A 50 16507 15080 13996 -471 -243 2964 O
ATOM 395 OD2 ASP A 50 -6.003 -31.659 -49.119 1.00120.98 O
ANISOU 395 OD2 ASP A 50 16682 15486 13800 -239 -435 2666 O
ATOM 396 N LYS A 51 -3.198 -33.658 -49.690 1.00 89.71 N
ANISOU 396 N LYS A 51 12623 11984 9478 -450 388 2375 N
ATOM 397 CA LYS A 51 -2.135 -33.940 -48.724 1.00 87.42 C
ANISOU 397 CA LYS A 51 12042 11638 9535 -437 536 2212 C
ATOM 398 C LYS A 51 -1.180 -35.020 -49.228 1.00 92.83 C
ANISOU 398 C LYS A 51 12659 12519 10094 -448 932 2107 C
ATOM 399 O LYS A 51 -1.588 -35.917 -49.977 1.00 92.70 O
ANISOU 399 O LYS A 51 12849 12671 9700 -405 1052 1987 O
ATOM 400 CB LYS A 51 -2.726 -34.353 -47.370 1.00 84.96 C
ANISOU 400 CB LYS A 51 11611 11237 9431 -289 287 1937 C
ATOM 401 CG LYS A 51 -2.719 -33.238 -46.339 1.00 93.27 C
ANISOU 401 CG LYS A 51 12577 12014 10848 -324 78 1969 C
ATOM 402 CD LYS A 51 -3.870 -32.261 -46.509 1.00105.42 C
ANISOU 402 CD LYS A 51 14279 13379 12397 -267 -145 2098 C
ATOM 403 CE LYS A 51 -4.108 -31.462 -45.253 1.00120.02 C
ANISOU 403 CE LYS A 51 16089 14929 14586 -240 -313 1980 C
ATOM 404 NZ LYS A 51 -5.491 -30.919 -45.199 1.00132.53 N
ANISOU 404 NZ LYS A 51 17773 16353 16230 -79 -490 2002 N
ATOM 405 N SER A 52 0.096 -34.926 -48.804 1.00 90.38 N
ANISOU 405 N SER A 52 12048 12158 10136 -511 1132 2154 N
ATOM 406 CA SER A 52 1.156 -35.881 -49.131 1.00 92.04 C
ANISOU 406 CA SER A 52 12074 12494 10403 -485 1553 2080 C
ATOM 407 C SER A 52 0.843 -37.260 -48.513 1.00 95.13 C
ANISOU 407 C SER A 52 12412 12933 10799 -290 1510 1755 C
ATOM 408 O SER A 52 0.174 -37.315 -47.474 1.00 91.98 O
ANISOU 408 O SER A 52 11981 12450 10516 -221 1143 1628 O
ATOM 409 CB SER A 52 2.500 -35.368 -48.623 1.00 96.57 C
ANISOU 409 CB SER A 52 12242 12969 11483 -598 1659 2251 C
ATOM 410 OG SER A 52 2.770 -34.069 -49.121 1.00108.60 O
ANISOU 410 OG SER A 52 13812 14414 13036 -803 1679 2563 O
ATOM 411 N PRO A 53 1.293 -38.391 -49.109 1.00 93.40 N
ANISOU 411 N PRO A 53 12203 12822 10463 -203 1899 1611 N
ATOM 412 CA PRO A 53 0.983 -39.704 -48.497 1.00 90.75 C
ANISOU 412 CA PRO A 53 11827 12480 10174 -24 1833 1323 C
ATOM 413 C PRO A 53 1.728 -39.945 -47.178 1.00 92.20 C
ANISOU 413 C PRO A 53 11578 12550 10905 36 1682 1324 C
ATOM 414 O PRO A 53 1.287 -40.762 -46.376 1.00 89.15 O
ANISOU 414 O PRO A 53 11169 12127 10577 144 1462 1146 O
ATOM 415 CB PRO A 53 1.426 -40.704 -49.569 1.00 96.04 C
ANISOU 415 CB PRO A 53 12633 13232 10624 39 2355 1185 C
ATOM 416 CG PRO A 53 2.478 -39.987 -50.348 1.00104.57 C
ANISOU 416 CG PRO A 53 13607 14352 11772 -82 2771 1423 C
ATOM 417 CD PRO A 53 2.089 -38.540 -50.347 1.00 99.31 C
ANISOU 417 CD PRO A 53 13026 13675 11034 -264 2452 1691 C
ATOM 418 N ASP A 54 2.876 -39.250 -46.983 1.00 90.40 N
ANISOU 418 N ASP A 54 11009 12269 11070 -69 1781 1555 N
ATOM 419 CA ASP A 54 3.744 -39.313 -45.798 1.00 89.25 C
ANISOU 419 CA ASP A 54 10425 12021 11463 -89 1585 1642 C
ATOM 420 C ASP A 54 3.394 -38.190 -44.811 1.00 87.55 C
ANISOU 420 C ASP A 54 10241 11697 11326 -260 1098 1724 C
ATOM 421 O ASP A 54 4.109 -38.012 -43.816 1.00 87.73 O
ANISOU 421 O ASP A 54 9966 11631 11738 -364 861 1824 O
ATOM 422 CB ASP A 54 5.232 -39.203 -46.203 1.00 95.96 C
ANISOU 422 CB ASP A 54 10849 12870 12740 -140 1970 1875 C
ATOM 423 CG ASP A 54 5.685 -40.178 -47.269 1.00112.32 C
ANISOU 423 CG ASP A 54 12899 15014 14763 29 2581 1785 C
ATOM 424 OD1 ASP A 54 6.214 -41.259 -46.903 1.00113.93 O
ANISOU 424 OD1 ASP A 54 12813 15159 15315 208 2703 1710 O
ATOM 425 OD2 ASP A 54 5.541 -39.852 -48.469 1.00121.20 O
ANISOU 425 OD2 ASP A 54 14306 16234 15511 -26 2950 1801 O
ATOM 426 N SER A 55 2.302 -37.430 -45.088 1.00 79.14 N
ANISOU 426 N SER A 55 9543 10618 9909 -300 943 1689 N
ATOM 427 CA SER A 55 1.871 -36.313 -44.247 1.00 76.44 C
ANISOU 427 CA SER A 55 9290 10120 9634 -433 561 1725 C
ATOM 428 C SER A 55 1.357 -36.790 -42.879 1.00 77.63 C
ANISOU 428 C SER A 55 9457 10212 9825 -388 217 1519 C
ATOM 429 O SER A 55 0.828 -37.906 -42.772 1.00 75.75 O
ANISOU 429 O SER A 55 9276 10067 9437 -228 235 1340 O
ATOM 430 CB SER A 55 0.812 -35.475 -44.951 1.00 77.87 C
ANISOU 430 CB SER A 55 9816 10272 9497 -433 521 1761 C
ATOM 431 OG SER A 55 -0.405 -36.185 -45.084 1.00 83.05 O
ANISOU 431 OG SER A 55 10701 11017 9838 -266 452 1563 O
ATOM 432 N PRO A 56 1.491 -35.948 -41.827 1.00 73.62 N
ANISOU 432 N PRO A 56 8944 9538 9488 -557 -90 1536 N
ATOM 433 CA PRO A 56 1.024 -36.351 -40.482 1.00 71.31 C
ANISOU 433 CA PRO A 56 8731 9197 9166 -562 -393 1341 C
ATOM 434 C PRO A 56 -0.453 -36.717 -40.424 1.00 72.06 C
ANISOU 434 C PRO A 56 9111 9333 8937 -384 -414 1121 C
ATOM 435 O PRO A 56 -0.813 -37.584 -39.625 1.00 69.98 O
ANISOU 435 O PRO A 56 8867 9116 8606 -330 -532 970 O
ATOM 436 CB PRO A 56 1.297 -35.119 -39.629 1.00 74.82 C
ANISOU 436 CB PRO A 56 9253 9425 9749 -808 -656 1376 C
ATOM 437 CG PRO A 56 2.372 -34.391 -40.356 1.00 82.52 C
ANISOU 437 CG PRO A 56 10011 10359 10985 -962 -532 1648 C
ATOM 438 CD PRO A 56 2.097 -34.603 -41.802 1.00 77.61 C
ANISOU 438 CD PRO A 56 9411 9876 10200 -787 -168 1727 C
ATOM 439 N GLU A 57 -1.295 -36.062 -41.274 1.00 67.99 N
ANISOU 439 N GLU A 57 8788 8795 8248 -309 -317 1143 N
ATOM 440 CA GLU A 57 -2.733 -36.331 -41.439 1.00 64.98 C
ANISOU 440 CA GLU A 57 8611 8460 7619 -144 -337 1003 C
ATOM 441 C GLU A 57 -2.931 -37.755 -41.985 1.00 66.05 C
ANISOU 441 C GLU A 57 8716 8800 7579 -13 -209 922 C
ATOM 442 O GLU A 57 -3.705 -38.524 -41.409 1.00 64.14 O
ANISOU 442 O GLU A 57 8529 8603 7239 68 -301 756 O
ATOM 443 CB GLU A 57 -3.412 -35.308 -42.384 1.00 67.27 C
ANISOU 443 CB GLU A 57 9052 8678 7831 -113 -301 1142 C
ATOM 444 CG GLU A 57 -3.326 -33.851 -41.954 1.00 80.30 C
ANISOU 444 CG GLU A 57 10772 10057 9683 -221 -406 1217 C
ATOM 445 CD GLU A 57 -2.082 -33.080 -42.365 1.00111.44 C
ANISOU 445 CD GLU A 57 14618 13915 13811 -413 -344 1442 C
ATOM 446 OE1 GLU A 57 -1.834 -32.005 -41.774 1.00102.97 O
ANISOU 446 OE1 GLU A 57 13604 12585 12937 -550 -463 1464 O
ATOM 447 OE2 GLU A 57 -1.362 -33.535 -43.284 1.00115.24 O
ANISOU 447 OE2 GLU A 57 14974 14568 14245 -440 -150 1590 O
ATOM 448 N MET A 58 -2.216 -38.112 -43.085 1.00 62.23 N
ANISOU 448 N MET A 58 8165 8422 7058 -6 33 1031 N
ATOM 449 CA MET A 58 -2.325 -39.435 -43.704 1.00 61.22 C
ANISOU 449 CA MET A 58 8066 8438 6758 105 206 922 C
ATOM 450 C MET A 58 -1.808 -40.501 -42.774 1.00 64.46 C
ANISOU 450 C MET A 58 8293 8837 7363 149 164 814 C
ATOM 451 O MET A 58 -2.410 -41.570 -42.694 1.00 62.82 O
ANISOU 451 O MET A 58 8164 8677 7028 244 149 659 O
ATOM 452 CB MET A 58 -1.594 -39.519 -45.057 1.00 66.06 C
ANISOU 452 CB MET A 58 8692 9136 7272 88 553 1032 C
ATOM 453 CG MET A 58 -2.364 -38.928 -46.224 1.00 70.37 C
ANISOU 453 CG MET A 58 9519 9747 7471 45 582 1130 C
ATOM 454 SD MET A 58 -4.109 -39.391 -46.400 1.00 72.36 S
ANISOU 454 SD MET A 58 10035 10065 7392 112 320 1001 S
ATOM 455 CE MET A 58 -3.974 -41.197 -46.726 1.00 68.74 C
ANISOU 455 CE MET A 58 9655 9709 6755 185 521 747 C
ATOM 456 N LYS A 59 -0.707 -40.207 -42.060 1.00 62.11 N
ANISOU 456 N LYS A 59 7746 8461 7391 58 107 927 N
ATOM 457 CA LYS A 59 -0.087 -41.109 -41.088 1.00 61.41 C
ANISOU 457 CA LYS A 59 7443 8343 7546 69 -11 910 C
ATOM 458 C LYS A 59 -1.030 -41.336 -39.895 1.00 63.12 C
ANISOU 458 C LYS A 59 7821 8534 7627 47 -315 765 C
ATOM 459 O LYS A 59 -1.133 -42.473 -39.421 1.00 61.79 O
ANISOU 459 O LYS A 59 7624 8383 7472 118 -367 690 O
ATOM 460 CB LYS A 59 1.272 -40.545 -40.625 1.00 66.16 C
ANISOU 460 CB LYS A 59 7732 8871 8535 -82 -88 1124 C
ATOM 461 CG LYS A 59 2.385 -40.636 -41.690 1.00 73.13 C
ANISOU 461 CG LYS A 59 8350 9786 9650 -40 287 1286 C
ATOM 462 CD LYS A 59 3.724 -40.082 -41.204 1.00 76.04 C
ANISOU 462 CD LYS A 59 8328 10084 10478 -211 181 1542 C
ATOM 463 CE LYS A 59 4.879 -40.738 -41.920 1.00 90.75 C
ANISOU 463 CE LYS A 59 9806 11973 12701 -98 573 1686 C
ATOM 464 NZ LYS A 59 6.197 -40.209 -41.472 1.00107.43 N
ANISOU 464 NZ LYS A 59 11457 14027 15336 -280 457 1989 N
ATOM 465 N ASP A 60 -1.764 -40.271 -39.448 1.00 59.12 N
ANISOU 465 N ASP A 60 7501 7967 6993 -43 -472 721 N
ATOM 466 CA ASP A 60 -2.710 -40.382 -38.326 1.00 57.67 C
ANISOU 466 CA ASP A 60 7493 7758 6663 -69 -672 567 C
ATOM 467 C ASP A 60 -4.009 -41.089 -38.711 1.00 61.09 C
ANISOU 467 C ASP A 60 8065 8279 6866 80 -595 431 C
ATOM 468 O ASP A 60 -4.618 -41.762 -37.854 1.00 59.90 O
ANISOU 468 O ASP A 60 7978 8148 6631 80 -698 324 O
ATOM 469 CB ASP A 60 -3.050 -39.022 -37.732 1.00 60.09 C
ANISOU 469 CB ASP A 60 7961 7926 6944 -190 -784 531 C
ATOM 470 CG ASP A 60 -3.920 -39.116 -36.488 1.00 70.62 C
ANISOU 470 CG ASP A 60 9490 9222 8120 -233 -911 351 C
ATOM 471 OD1 ASP A 60 -5.034 -38.540 -36.501 1.00 70.97 O
ANISOU 471 OD1 ASP A 60 9693 9210 8061 -155 -836 242 O
ATOM 472 OD2 ASP A 60 -3.505 -39.809 -35.516 1.00 74.72 O
ANISOU 472 OD2 ASP A 60 9994 9767 8630 -342 -1072 341 O
ATOM 473 N PHE A 61 -4.461 -40.890 -39.983 1.00 56.54 N
ANISOU 473 N PHE A 61 7549 7758 6174 171 -441 458 N
ATOM 474 CA PHE A 61 -5.665 -41.525 -40.507 1.00 54.36 C
ANISOU 474 CA PHE A 61 7392 7572 5690 268 -420 366 C
ATOM 475 C PHE A 61 -5.413 -43.016 -40.544 1.00 58.20 C
ANISOU 475 C PHE A 61 7838 8114 6162 314 -367 288 C
ATOM 476 O PHE A 61 -6.263 -43.807 -40.114 1.00 57.55 O
ANISOU 476 O PHE A 61 7815 8060 5993 334 -450 184 O
ATOM 477 CB PHE A 61 -6.026 -40.962 -41.897 1.00 56.77 C
ANISOU 477 CB PHE A 61 7793 7925 5850 297 -329 462 C
ATOM 478 CG PHE A 61 -6.741 -41.932 -42.810 1.00 57.78 C
ANISOU 478 CG PHE A 61 8039 8172 5742 339 -296 399 C
ATOM 479 CD1 PHE A 61 -8.077 -42.247 -42.606 1.00 58.78 C
ANISOU 479 CD1 PHE A 61 8217 8338 5781 363 -450 334 C
ATOM 480 CD2 PHE A 61 -6.070 -42.548 -43.861 1.00 62.09 C
ANISOU 480 CD2 PHE A 61 8653 8778 6159 334 -96 395 C
ATOM 481 CE1 PHE A 61 -8.731 -43.156 -43.434 1.00 60.19 C
ANISOU 481 CE1 PHE A 61 8516 8613 5741 348 -477 282 C
ATOM 482 CE2 PHE A 61 -6.722 -43.465 -44.683 1.00 65.53 C
ANISOU 482 CE2 PHE A 61 9273 9296 6330 327 -82 298 C
ATOM 483 CZ PHE A 61 -8.052 -43.751 -44.473 1.00 62.30 C
ANISOU 483 CZ PHE A 61 8917 8925 5830 317 -309 251 C
ATOM 484 N ARG A 62 -4.218 -43.385 -41.043 1.00 55.71 N
ANISOU 484 N ARG A 62 7401 7786 5979 331 -206 350 N
ATOM 485 CA ARG A 62 -3.746 -44.759 -41.148 1.00 55.86 C
ANISOU 485 CA ARG A 62 7355 7788 6081 407 -99 286 C
ATOM 486 C ARG A 62 -3.612 -45.344 -39.770 1.00 59.39 C
ANISOU 486 C ARG A 62 7699 8174 6692 376 -312 291 C
ATOM 487 O ARG A 62 -4.045 -46.478 -39.563 1.00 60.08 O
ANISOU 487 O ARG A 62 7836 8240 6750 422 -339 205 O
ATOM 488 CB ARG A 62 -2.414 -44.852 -41.923 1.00 55.62 C
ANISOU 488 CB ARG A 62 7163 7729 6242 456 186 371 C
ATOM 489 CG ARG A 62 -2.582 -44.665 -43.440 1.00 59.32 C
ANISOU 489 CG ARG A 62 7824 8272 6442 471 459 339 C
ATOM 490 CD ARG A 62 -1.394 -45.162 -44.236 1.00 61.66 C
ANISOU 490 CD ARG A 62 8007 8534 6888 546 856 353 C
ATOM 491 NE ARG A 62 -0.196 -44.365 -43.981 1.00 69.51 N
ANISOU 491 NE ARG A 62 8687 9499 8223 504 924 566 N
ATOM 492 CZ ARG A 62 0.200 -43.346 -44.732 1.00 87.00 C
ANISOU 492 CZ ARG A 62 10909 11768 10379 418 1092 704 C
ATOM 493 NH1 ARG A 62 -0.497 -42.996 -45.805 1.00 74.58 N
ANISOU 493 NH1 ARG A 62 9661 10288 8389 372 1202 667 N
ATOM 494 NH2 ARG A 62 1.296 -42.670 -44.420 1.00 82.12 N
ANISOU 494 NH2 ARG A 62 9973 11109 10121 348 1123 913 N
ATOM 495 N HIS A 63 -3.109 -44.541 -38.805 1.00 54.85 N
ANISOU 495 N HIS A 63 7030 7563 6249 261 -491 394 N
ATOM 496 CA HIS A 63 -2.889 -44.981 -37.420 1.00 54.63 C
ANISOU 496 CA HIS A 63 6950 7489 6320 167 -743 437 C
ATOM 497 C HIS A 63 -4.178 -45.376 -36.717 1.00 55.53 C
ANISOU 497 C HIS A 63 7270 7637 6190 138 -852 307 C
ATOM 498 O HIS A 63 -4.142 -46.237 -35.847 1.00 56.04 O
ANISOU 498 O HIS A 63 7329 7676 6286 90 -999 337 O
ATOM 499 CB HIS A 63 -2.132 -43.920 -36.590 1.00 56.48 C
ANISOU 499 CB HIS A 63 7118 7674 6668 -15 -940 556 C
ATOM 500 CG HIS A 63 -1.716 -44.398 -35.236 1.00 60.09 C
ANISOU 500 CG HIS A 63 7541 8094 7198 -163 -1241 646 C
ATOM 501 ND1 HIS A 63 -0.813 -45.439 -35.080 1.00 63.04 N
ANISOU 501 ND1 HIS A 63 7663 8423 7866 -120 -1320 811 N
ATOM 502 CD2 HIS A 63 -2.120 -43.981 -34.017 1.00 61.47 C
ANISOU 502 CD2 HIS A 63 7926 8259 7171 -359 -1472 600 C
ATOM 503 CE1 HIS A 63 -0.696 -45.619 -33.772 1.00 63.17 C
ANISOU 503 CE1 HIS A 63 7742 8421 7839 -310 -1657 902 C
ATOM 504 NE2 HIS A 63 -1.464 -44.772 -33.090 1.00 62.76 N
ANISOU 504 NE2 HIS A 63 7996 8399 7449 -475 -1745 762 N
ATOM 505 N GLY A 64 -5.295 -44.766 -37.091 1.00 50.68 N
ANISOU 505 N GLY A 64 6811 7075 5369 162 -782 199 N
ATOM 506 CA GLY A 64 -6.586 -45.084 -36.488 1.00 49.61 C
ANISOU 506 CA GLY A 64 6813 6980 5055 142 -833 92 C
ATOM 507 C GLY A 64 -6.932 -46.539 -36.693 1.00 54.31 C
ANISOU 507 C GLY A 64 7408 7593 5634 192 -823 59 C
ATOM 508 O GLY A 64 -7.506 -47.186 -35.818 1.00 53.68 O
ANISOU 508 O GLY A 64 7388 7520 5488 124 -912 38 O
ATOM 509 N PHE A 65 -6.512 -47.068 -37.845 1.00 52.64 N
ANISOU 509 N PHE A 65 7154 7367 5479 293 -693 51 N
ATOM 510 CA PHE A 65 -6.755 -48.448 -38.204 1.00 53.00 C
ANISOU 510 CA PHE A 65 7240 7372 5526 339 -656 -14 C
ATOM 511 C PHE A 65 -5.736 -49.354 -37.530 1.00 60.06 C
ANISOU 511 C PHE A 65 8009 8141 6670 356 -713 79 C
ATOM 512 O PHE A 65 -6.018 -50.541 -37.382 1.00 62.48 O
ANISOU 512 O PHE A 65 8359 8365 7014 367 -744 49 O
ATOM 513 CB PHE A 65 -6.812 -48.626 -39.724 1.00 54.62 C
ANISOU 513 CB PHE A 65 7533 7590 5629 415 -467 -100 C
ATOM 514 CG PHE A 65 -8.023 -47.914 -40.296 1.00 55.10 C
ANISOU 514 CG PHE A 65 7711 7771 5454 371 -514 -133 C
ATOM 515 CD1 PHE A 65 -9.316 -48.326 -39.970 1.00 56.19 C
ANISOU 515 CD1 PHE A 65 7901 7955 5495 307 -648 -176 C
ATOM 516 CD2 PHE A 65 -7.875 -46.816 -41.138 1.00 57.55 C
ANISOU 516 CD2 PHE A 65 8046 8140 5681 384 -439 -76 C
ATOM 517 CE1 PHE A 65 -10.434 -47.667 -40.499 1.00 56.33 C
ANISOU 517 CE1 PHE A 65 7950 8071 5381 278 -720 -154 C
ATOM 518 CE2 PHE A 65 -8.995 -46.170 -41.679 1.00 59.13 C
ANISOU 518 CE2 PHE A 65 8322 8427 5717 352 -530 -47 C
ATOM 519 CZ PHE A 65 -10.264 -46.580 -41.330 1.00 56.09 C
ANISOU 519 CZ PHE A 65 7941 8084 5288 309 -679 -80 C
ATOM 520 N ASP A 66 -4.597 -48.803 -37.061 1.00 55.53 N
ANISOU 520 N ASP A 66 7266 7535 6296 337 -770 221 N
ATOM 521 CA ASP A 66 -3.610 -49.590 -36.326 1.00 56.19 C
ANISOU 521 CA ASP A 66 7174 7498 6677 338 -902 383 C
ATOM 522 C ASP A 66 -4.167 -49.862 -34.978 1.00 60.70 C
ANISOU 522 C ASP A 66 7858 8088 7119 178 -1171 441 C
ATOM 523 O ASP A 66 -4.075 -50.990 -34.520 1.00 62.34 O
ANISOU 523 O ASP A 66 8044 8193 7451 183 -1274 524 O
ATOM 524 CB ASP A 66 -2.253 -48.889 -36.227 1.00 58.89 C
ANISOU 524 CB ASP A 66 7264 7814 7298 322 -937 561 C
ATOM 525 CG ASP A 66 -1.497 -48.828 -37.536 1.00 69.30 C
ANISOU 525 CG ASP A 66 8427 9095 8807 487 -603 542 C
ATOM 526 OD1 ASP A 66 -0.678 -47.909 -37.696 1.00 71.66 O
ANISOU 526 OD1 ASP A 66 8553 9421 9255 448 -569 659 O
ATOM 527 OD2 ASP A 66 -1.717 -49.715 -38.399 1.00 71.63 O
ANISOU 527 OD2 ASP A 66 8798 9324 9094 634 -359 406 O
ATOM 528 N ILE A 67 -4.810 -48.837 -34.373 1.00 56.99 N
ANISOU 528 N ILE A 67 7538 7729 6385 36 -1247 386 N
ATOM 529 CA ILE A 67 -5.484 -48.874 -33.066 1.00 56.57 C
ANISOU 529 CA ILE A 67 7665 7722 6107 -150 -1421 396 C
ATOM 530 C ILE A 67 -6.677 -49.846 -33.137 1.00 63.37 C
ANISOU 530 C ILE A 67 8636 8601 6841 -125 -1343 307 C
ATOM 531 O ILE A 67 -6.831 -50.726 -32.289 1.00 63.53 O
ANISOU 531 O ILE A 67 8720 8587 6832 -230 -1481 403 O
ATOM 532 CB ILE A 67 -5.923 -47.440 -32.651 1.00 57.61 C
ANISOU 532 CB ILE A 67 7947 7927 6017 -259 -1395 292 C
ATOM 533 CG1 ILE A 67 -4.704 -46.506 -32.486 1.00 58.10 C
ANISOU 533 CG1 ILE A 67 7922 7943 6212 -346 -1524 394 C
ATOM 534 CG2 ILE A 67 -6.787 -47.468 -31.392 1.00 57.19 C
ANISOU 534 CG2 ILE A 67 8130 7922 5677 -438 -1450 242 C
ATOM 535 CD1 ILE A 67 -5.036 -45.073 -32.288 1.00 59.78 C
ANISOU 535 CD1 ILE A 67 8291 8157 6267 -427 -1464 269 C
ATOM 536 N LEU A 68 -7.491 -49.690 -34.181 1.00 62.18 N
ANISOU 536 N LEU A 68 8503 8499 6623 -14 -1152 157 N
ATOM 537 CA LEU A 68 -8.674 -50.499 -34.442 1.00 62.27 C
ANISOU 537 CA LEU A 68 8587 8533 6541 -16 -1099 76 C
ATOM 538 C LEU A 68 -8.318 -51.981 -34.633 1.00 66.91 C
ANISOU 538 C LEU A 68 9157 8972 7294 19 -1143 124 C
ATOM 539 O LEU A 68 -8.982 -52.809 -34.046 1.00 68.16 O
ANISOU 539 O LEU A 68 9387 9107 7404 -82 -1214 156 O
ATOM 540 CB LEU A 68 -9.383 -49.949 -35.688 1.00 61.74 C
ANISOU 540 CB LEU A 68 8520 8538 6401 77 -958 -47 C
ATOM 541 CG LEU A 68 -10.863 -50.224 -35.830 1.00 66.80 C
ANISOU 541 CG LEU A 68 9197 9256 6929 25 -945 -108 C
ATOM 542 CD1 LEU A 68 -11.707 -49.301 -34.918 1.00 66.46 C
ANISOU 542 CD1 LEU A 68 9149 9306 6798 -37 -903 -108 C
ATOM 543 CD2 LEU A 68 -11.285 -50.056 -37.275 1.00 69.45 C
ANISOU 543 CD2 LEU A 68 9540 9628 7219 93 -900 -176 C
ATOM 544 N VAL A 69 -7.271 -52.315 -35.409 1.00 63.54 N
ANISOU 544 N VAL A 69 8634 8423 7088 161 -1071 133 N
ATOM 545 CA VAL A 69 -6.894 -53.708 -35.682 1.00 64.45 C
ANISOU 545 CA VAL A 69 8737 8328 7423 239 -1051 147 C
ATOM 546 C VAL A 69 -6.382 -54.377 -34.412 1.00 70.86 C
ANISOU 546 C VAL A 69 9485 9029 8410 162 -1280 376 C
ATOM 547 O VAL A 69 -6.731 -55.526 -34.175 1.00 72.17 O
ANISOU 547 O VAL A 69 9720 9048 8653 133 -1340 412 O
ATOM 548 CB VAL A 69 -5.915 -53.836 -36.870 1.00 69.05 C
ANISOU 548 CB VAL A 69 9234 8791 8211 434 -819 72 C
ATOM 549 CG1 VAL A 69 -5.108 -55.130 -36.818 1.00 71.58 C
ANISOU 549 CG1 VAL A 69 9465 8828 8904 557 -786 142 C
ATOM 550 CG2 VAL A 69 -6.665 -53.724 -38.193 1.00 68.31 C
ANISOU 550 CG2 VAL A 69 9321 8759 7873 454 -628 -157 C
ATOM 551 N GLY A 70 -5.615 -53.651 -33.599 1.00 68.20 N
ANISOU 551 N GLY A 70 9045 8754 8114 94 -1440 545 N
ATOM 552 CA GLY A 70 -5.111 -54.139 -32.321 1.00 69.58 C
ANISOU 552 CA GLY A 70 9190 8858 8391 -39 -1737 811 C
ATOM 553 C GLY A 70 -6.266 -54.470 -31.393 1.00 73.61 C
ANISOU 553 C GLY A 70 9934 9452 8585 -252 -1836 823 C
ATOM 554 O GLY A 70 -6.297 -55.556 -30.809 1.00 74.28 O
ANISOU 554 O GLY A 70 10056 9403 8763 -321 -1989 993 O
ATOM 555 N GLN A 71 -7.263 -53.551 -31.320 1.00 69.38 N
ANISOU 555 N GLN A 71 9538 9116 7706 -343 -1712 650 N
ATOM 556 CA GLN A 71 -8.499 -53.699 -30.539 1.00 69.16 C
ANISOU 556 CA GLN A 71 9700 9198 7381 -529 -1692 626 C
ATOM 557 C GLN A 71 -9.338 -54.879 -31.071 1.00 74.59 C
ANISOU 557 C GLN A 71 10398 9792 8149 -500 -1616 581 C
ATOM 558 O GLN A 71 -9.811 -55.685 -30.260 1.00 76.71 O
ANISOU 558 O GLN A 71 10768 10026 8351 -666 -1709 716 O
ATOM 559 CB GLN A 71 -9.312 -52.397 -30.543 1.00 68.38 C
ANISOU 559 CB GLN A 71 9672 9284 7025 -557 -1506 437 C
ATOM 560 CG GLN A 71 -8.699 -51.317 -29.673 1.00 72.20 C
ANISOU 560 CG GLN A 71 10255 9830 7350 -681 -1596 467 C
ATOM 561 CD GLN A 71 -9.590 -50.119 -29.534 1.00 86.09 C
ANISOU 561 CD GLN A 71 12118 11706 8886 -702 -1371 270 C
ATOM 562 OE1 GLN A 71 -10.348 -49.980 -28.581 1.00 84.92 O
ANISOU 562 OE1 GLN A 71 12152 11631 8483 -862 -1276 233 O
ATOM 563 NE2 GLN A 71 -9.485 -49.203 -30.455 1.00 79.31 N
ANISOU 563 NE2 GLN A 71 11151 10849 8134 -538 -1257 150 N
ATOM 564 N ILE A 72 -9.473 -55.003 -32.427 1.00 69.25 N
ANISOU 564 N ILE A 72 9651 9063 7599 -325 -1465 406 N
ATOM 565 CA ILE A 72 -10.154 -56.104 -33.118 1.00 69.67 C
ANISOU 565 CA ILE A 72 9750 8991 7731 -318 -1420 326 C
ATOM 566 C ILE A 72 -9.486 -57.414 -32.690 1.00 78.72 C
ANISOU 566 C ILE A 72 10908 9870 9133 -321 -1562 501 C
ATOM 567 O ILE A 72 -10.194 -58.314 -32.267 1.00 80.98 O
ANISOU 567 O ILE A 72 11286 10080 9404 -468 -1632 576 O
ATOM 568 CB ILE A 72 -10.171 -55.909 -34.668 1.00 71.82 C
ANISOU 568 CB ILE A 72 10012 9243 8035 -160 -1260 106 C
ATOM 569 CG1 ILE A 72 -11.319 -54.970 -35.084 1.00 70.97 C
ANISOU 569 CG1 ILE A 72 9904 9364 7697 -213 -1188 -9 C
ATOM 570 CG2 ILE A 72 -10.257 -57.241 -35.448 1.00 73.66 C
ANISOU 570 CG2 ILE A 72 10345 9228 8416 -133 -1234 12 C
ATOM 571 CD1 ILE A 72 -11.106 -54.178 -36.383 1.00 76.16 C
ANISOU 571 CD1 ILE A 72 10553 10082 8302 -81 -1074 -149 C
ATOM 572 N ASP A 73 -8.133 -57.482 -32.717 1.00 77.08 N
ANISOU 572 N ASP A 73 10576 9513 9197 -169 -1613 606 N
ATOM 573 CA ASP A 73 -7.336 -58.648 -32.323 1.00 80.16 C
ANISOU 573 CA ASP A 73 10910 9607 9942 -118 -1760 822 C
ATOM 574 C ASP A 73 -7.538 -59.028 -30.858 1.00 86.73 C
ANISOU 574 C ASP A 73 11822 10459 10671 -358 -2038 1121 C
ATOM 575 O ASP A 73 -7.535 -60.218 -30.548 1.00 89.76 O
ANISOU 575 O ASP A 73 12246 10595 11262 -392 -2160 1288 O
ATOM 576 CB ASP A 73 -5.837 -58.411 -32.580 1.00 83.49 C
ANISOU 576 CB ASP A 73 11093 9910 10719 93 -1759 924 C
ATOM 577 CG ASP A 73 -5.425 -58.305 -34.038 1.00 95.58 C
ANISOU 577 CG ASP A 73 12557 11350 12409 341 -1432 667 C
ATOM 578 OD1 ASP A 73 -6.252 -58.635 -34.919 1.00 95.13 O
ANISOU 578 OD1 ASP A 73 12683 11263 12199 347 -1249 407 O
ATOM 579 OD2 ASP A 73 -4.284 -57.864 -34.299 1.00104.80 O
ANISOU 579 OD2 ASP A 73 13497 12488 13833 498 -1363 734 O
ATOM 580 N ASP A 74 -7.694 -58.035 -29.960 1.00 82.25 N
ANISOU 580 N ASP A 74 11316 10160 9776 -537 -2131 1190 N
ATOM 581 CA ASP A 74 -7.909 -58.283 -28.528 1.00 84.08 C
ANISOU 581 CA ASP A 74 11704 10452 9788 -819 -2367 1459 C
ATOM 582 C ASP A 74 -9.281 -58.906 -28.306 1.00 90.02 C
ANISOU 582 C ASP A 74 12625 11243 10335 -992 -2257 1414 C
ATOM 583 O ASP A 74 -9.456 -59.716 -27.392 1.00 93.05 O
ANISOU 583 O ASP A 74 13133 11548 10675 -1193 -2429 1673 O
ATOM 584 CB ASP A 74 -7.764 -56.991 -27.711 1.00 84.70 C
ANISOU 584 CB ASP A 74 11877 10791 9513 -984 -2432 1466 C
ATOM 585 CG ASP A 74 -6.360 -56.425 -27.708 1.00 90.64 C
ANISOU 585 CG ASP A 74 12456 11504 10481 -900 -2627 1590 C
ATOM 586 OD1 ASP A 74 -6.219 -55.195 -27.852 1.00 90.44 O
ANISOU 586 OD1 ASP A 74 12430 11639 10294 -899 -2541 1430 O
ATOM 587 OD2 ASP A 74 -5.399 -57.215 -27.558 1.00 95.07 O
ANISOU 587 OD2 ASP A 74 12855 11851 11417 -837 -2873 1869 O
ATOM 588 N ALA A 75 -10.243 -58.526 -29.156 1.00 84.23 N
ANISOU 588 N ALA A 75 11877 10626 9500 -930 -1993 1123 N
ATOM 589 CA ALA A 75 -11.589 -59.060 -29.144 1.00 84.50 C
ANISOU 589 CA ALA A 75 11989 10701 9416 -1087 -1880 1076 C
ATOM 590 C ALA A 75 -11.597 -60.401 -29.871 1.00 90.24 C
ANISOU 590 C ALA A 75 12708 11115 10463 -1024 -1930 1078 C
ATOM 591 O ALA A 75 -12.309 -61.311 -29.455 1.00 92.59 O
ANISOU 591 O ALA A 75 13094 11323 10762 -1218 -1980 1205 O
ATOM 592 CB ALA A 75 -12.541 -58.078 -29.805 1.00 82.99 C
ANISOU 592 CB ALA A 75 11732 10740 9060 -1043 -1638 811 C
ATOM 593 N LEU A 76 -10.786 -60.521 -30.948 1.00 85.45 N
ANISOU 593 N LEU A 76 12019 10322 10125 -766 -1889 930 N
ATOM 594 CA LEU A 76 -10.629 -61.714 -31.779 1.00 86.22 C
ANISOU 594 CA LEU A 76 12156 10065 10537 -664 -1874 852 C
ATOM 595 C LEU A 76 -9.946 -62.821 -30.979 1.00 92.45 C
ANISOU 595 C LEU A 76 12964 10539 11626 -688 -2084 1168 C
ATOM 596 O LEU A 76 -10.309 -63.981 -31.139 1.00 94.47 O
ANISOU 596 O LEU A 76 13325 10507 12063 -754 -2118 1191 O
ATOM 597 CB LEU A 76 -9.825 -61.382 -33.042 1.00 85.39 C
ANISOU 597 CB LEU A 76 11982 9871 10593 -378 -1700 609 C
ATOM 598 CG LEU A 76 -10.207 -62.124 -34.315 1.00 91.23 C
ANISOU 598 CG LEU A 76 12859 10376 11427 -319 -1553 331 C
ATOM 599 CD1 LEU A 76 -10.193 -61.197 -35.493 1.00 88.99 C
ANISOU 599 CD1 LEU A 76 12582 10276 10955 -206 -1357 50 C
ATOM 600 CD2 LEU A 76 -9.249 -63.273 -34.589 1.00 98.44 C
ANISOU 600 CD2 LEU A 76 13786 10833 12785 -122 -1510 355 C
ATOM 601 N LYS A 77 -8.990 -62.462 -30.094 1.00 88.55 N
ANISOU 601 N LYS A 77 12373 10084 11188 -665 -2264 1437 N
ATOM 602 CA LYS A 77 -8.305 -63.402 -29.202 1.00 91.54 C
ANISOU 602 CA LYS A 77 12740 10192 11848 -711 -2547 1831 C
ATOM 603 C LYS A 77 -9.347 -64.060 -28.266 1.00 96.32 C
ANISOU 603 C LYS A 77 13553 10826 12220 -1051 -2667 2035 C
ATOM 604 O LYS A 77 -9.415 -65.291 -28.180 1.00 97.88 O
ANISOU 604 O LYS A 77 13816 10677 12697 -1090 -2771 2197 O
ATOM 605 CB LYS A 77 -7.201 -62.670 -28.398 1.00 94.46 C
ANISOU 605 CB LYS A 77 12975 10693 12221 -705 -2780 2097 C
ATOM 606 CG LYS A 77 -6.562 -63.492 -27.264 1.00110.23 C
ANISOU 606 CG LYS A 77 14968 12480 14436 -828 -3178 2599 C
ATOM 607 CD LYS A 77 -5.600 -62.682 -26.388 1.00118.23 C
ANISOU 607 CD LYS A 77 15888 13677 15357 -922 -3489 2880 C
ATOM 608 CE LYS A 77 -6.273 -61.922 -25.262 1.00127.47 C
ANISOU 608 CE LYS A 77 17345 15227 15859 -1310 -3592 2943 C
ATOM 609 NZ LYS A 77 -6.797 -60.594 -25.701 1.00130.02 N
ANISOU 609 NZ LYS A 77 17714 15886 15803 -1295 -3279 2533 N
ATOM 610 N LEU A 78 -10.191 -63.213 -27.628 1.00 91.55 N
ANISOU 610 N LEU A 78 13051 10616 11120 -1290 -2602 2003 N
ATOM 611 CA LEU A 78 -11.264 -63.567 -26.692 1.00 92.73 C
ANISOU 611 CA LEU A 78 13381 10892 10960 -1638 -2613 2171 C
ATOM 612 C LEU A 78 -12.398 -64.355 -27.359 1.00 96.25 C
ANISOU 612 C LEU A 78 13853 11214 11503 -1713 -2460 2018 C
ATOM 613 O LEU A 78 -12.929 -65.272 -26.736 1.00 98.64 O
ANISOU 613 O LEU A 78 14273 11391 11813 -1957 -2551 2259 O
ATOM 614 CB LEU A 78 -11.819 -62.287 -26.040 1.00 91.12 C
ANISOU 614 CB LEU A 78 13250 11126 10246 -1799 -2459 2078 C
ATOM 615 CG LEU A 78 -11.463 -62.032 -24.566 1.00 98.23 C
ANISOU 615 CG LEU A 78 14349 12174 10799 -2068 -2654 2394 C
ATOM 616 CD1 LEU A 78 -9.965 -62.179 -24.295 1.00100.05 C
ANISOU 616 CD1 LEU A 78 14521 12221 11272 -1967 -3030 2660 C
ATOM 617 CD2 LEU A 78 -11.887 -60.652 -24.159 1.00 99.63 C
ANISOU 617 CD2 LEU A 78 14617 12719 10519 -2157 -2428 2187 C
ATOM 618 N ALA A 79 -12.763 -64.001 -28.613 1.00 90.26 N
ANISOU 618 N ALA A 79 13000 10488 10807 -1541 -2261 1646 N
ATOM 619 CA ALA A 79 -13.798 -64.692 -29.390 1.00 90.55 C
ANISOU 619 CA ALA A 79 13066 10404 10937 -1638 -2175 1480 C
ATOM 620 C ALA A 79 -13.307 -66.080 -29.802 1.00 97.57 C
ANISOU 620 C ALA A 79 14049 10785 12241 -1572 -2304 1536 C
ATOM 621 O ALA A 79 -14.111 -67.012 -29.876 1.00 99.24 O
ANISOU 621 O ALA A 79 14356 10810 12540 -1782 -2342 1571 O
ATOM 622 CB ALA A 79 -14.182 -63.879 -30.616 1.00 88.43 C
ANISOU 622 CB ALA A 79 12706 10306 10588 -1491 -1996 1106 C
ATOM 623 N ASN A 80 -11.977 -66.213 -30.054 1.00 94.87 N
ANISOU 623 N ASN A 80 13660 10192 12194 -1281 -2358 1554 N
ATOM 624 CA ASN A 80 -11.324 -67.477 -30.405 1.00 98.24 C
ANISOU 624 CA ASN A 80 14149 10074 13102 -1143 -2432 1610 C
ATOM 625 C ASN A 80 -11.307 -68.369 -29.184 1.00107.04 C
ANISOU 625 C ASN A 80 15335 10992 14344 -1353 -2693 2072 C
ATOM 626 O ASN A 80 -11.443 -69.590 -29.305 1.00110.54 O
ANISOU 626 O ASN A 80 15899 10997 15106 -1407 -2763 2148 O
ATOM 627 CB ASN A 80 -9.903 -67.252 -30.940 1.00 97.47 C
ANISOU 627 CB ASN A 80 13905 9795 13335 -754 -2365 1539 C
ATOM 628 CG ASN A 80 -9.817 -66.832 -32.397 1.00114.30 C
ANISOU 628 CG ASN A 80 16048 11931 15450 -536 -2070 1072 C
ATOM 629 OD1 ASN A 80 -10.681 -67.138 -33.233 1.00100.51 O
ANISOU 629 OD1 ASN A 80 14476 10137 13574 -646 -1957 779 O
ATOM 630 ND2 ASN A 80 -8.746 -66.131 -32.740 1.00108.59 N
ANISOU 630 ND2 ASN A 80 15145 11265 14848 -253 -1956 1016 N
ATOM 631 N GLU A 81 -11.207 -67.733 -27.994 1.00103.48 N
ANISOU 631 N GLU A 81 14854 10867 13598 -1510 -2839 2378 N
ATOM 632 CA GLU A 81 -11.228 -68.369 -26.674 1.00106.39 C
ANISOU 632 CA GLU A 81 15334 11160 13930 -1781 -3109 2871 C
ATOM 633 C GLU A 81 -12.674 -68.747 -26.270 1.00111.29 C
ANISOU 633 C GLU A 81 16109 11914 14262 -2171 -3029 2919 C
ATOM 634 O GLU A 81 -12.906 -69.208 -25.146 1.00113.91 O
ANISOU 634 O GLU A 81 16576 12253 14452 -2468 -3194 3323 O
ATOM 635 CB GLU A 81 -10.583 -67.434 -25.635 1.00107.11 C
ANISOU 635 CB GLU A 81 15398 11585 13712 -1847 -3277 3122 C
ATOM 636 CG GLU A 81 -9.063 -67.419 -25.713 1.00115.56 C
ANISOU 636 CG GLU A 81 16279 12432 15195 -1547 -3490 3283 C
ATOM 637 CD GLU A 81 -8.331 -66.390 -24.874 1.00123.74 C
ANISOU 637 CD GLU A 81 17274 13794 15949 -1617 -3694 3479 C
ATOM 638 OE1 GLU A 81 -8.975 -65.440 -24.373 1.00109.47 O
ANISOU 638 OE1 GLU A 81 15610 12419 13565 -1847 -3584 3370 O
ATOM 639 OE2 GLU A 81 -7.094 -66.526 -24.739 1.00113.91 O
ANISOU 639 OE2 GLU A 81 15841 12349 15092 -1439 -3958 3737 O
ATOM 640 N GLY A 82 -13.617 -68.552 -27.206 1.00105.61 N
ANISOU 640 N GLY A 82 15359 11299 13468 -2184 -2787 2537 N
ATOM 641 CA GLY A 82 -15.042 -68.844 -27.065 1.00105.78 C
ANISOU 641 CA GLY A 82 15431 11454 13307 -2529 -2682 2539 C
ATOM 642 C GLY A 82 -15.763 -67.941 -26.086 1.00107.69 C
ANISOU 642 C GLY A 82 15654 12203 13060 -2770 -2537 2655 C
ATOM 643 O GLY A 82 -16.986 -68.043 -25.925 1.00108.10 O
ANISOU 643 O GLY A 82 15677 12420 12977 -3045 -2386 2667 O
ATOM 644 N LYS A 83 -14.994 -67.043 -25.433 1.00102.00 N
ANISOU 644 N LYS A 83 14948 11716 12089 -2677 -2567 2736 N
ATOM 645 CA LYS A 83 -15.432 -66.089 -24.421 1.00100.67 C
ANISOU 645 CA LYS A 83 14842 11990 11417 -2879 -2408 2811 C
ATOM 646 C LYS A 83 -16.228 -64.953 -25.083 1.00 99.90 C
ANISOU 646 C LYS A 83 14567 12229 11161 -2775 -2077 2418 C
ATOM 647 O LYS A 83 -15.796 -63.797 -25.078 1.00 97.16 O
ANISOU 647 O LYS A 83 14187 12106 10622 -2609 -1991 2247 O
ATOM 648 CB LYS A 83 -14.219 -65.558 -23.636 1.00102.84 C
ANISOU 648 CB LYS A 83 15226 12332 11515 -2819 -2619 2996 C
ATOM 649 CG LYS A 83 -13.386 -66.628 -22.932 1.00117.47 C
ANISOU 649 CG LYS A 83 17216 13855 13563 -2918 -3013 3461 C
ATOM 650 CD LYS A 83 -12.107 -66.027 -22.380 1.00126.14 C
ANISOU 650 CD LYS A 83 18345 15015 14569 -2831 -3287 3627 C
ATOM 651 CE LYS A 83 -11.115 -67.059 -21.914 1.00139.56 C
ANISOU 651 CE LYS A 83 20073 16330 16624 -2836 -3736 4103 C
ATOM 652 NZ LYS A 83 -9.872 -66.422 -21.401 1.00148.67 N
ANISOU 652 NZ LYS A 83 21205 17567 17718 -2784 -4058 4301 N
ATOM 653 N VAL A 84 -17.408 -65.315 -25.650 1.00 95.57 N
ANISOU 653 N VAL A 84 13892 11691 10730 -2894 -1924 2310 N
ATOM 654 CA VAL A 84 -18.382 -64.451 -26.336 1.00 92.97 C
ANISOU 654 CA VAL A 84 13336 11635 10353 -2835 -1660 2016 C
ATOM 655 C VAL A 84 -18.640 -63.180 -25.519 1.00 96.53 C
ANISOU 655 C VAL A 84 13778 12476 10422 -2854 -1376 1978 C
ATOM 656 O VAL A 84 -18.390 -62.083 -26.008 1.00 93.62 O
ANISOU 656 O VAL A 84 13316 12257 10000 -2609 -1281 1726 O
ATOM 657 CB VAL A 84 -19.733 -65.173 -26.676 1.00 98.49 C
ANISOU 657 CB VAL A 84 13888 12303 11230 -3086 -1591 2050 C
ATOM 658 CG1 VAL A 84 -19.753 -65.696 -28.101 1.00 96.66 C
ANISOU 658 CG1 VAL A 84 13595 11809 11320 -2968 -1771 1822 C
ATOM 659 CG2 VAL A 84 -20.072 -66.282 -25.676 1.00102.79 C
ANISOU 659 CG2 VAL A 84 14577 12712 11768 -3446 -1644 2426 C
ATOM 660 N LYS A 85 -19.098 -63.352 -24.266 1.00 96.43 N
ANISOU 660 N LYS A 85 13905 12598 10134 -3156 -1230 2227 N
ATOM 661 CA LYS A 85 -19.439 -62.335 -23.276 1.00 96.74 C
ANISOU 661 CA LYS A 85 14035 12967 9756 -3254 -895 2204 C
ATOM 662 C LYS A 85 -18.428 -61.169 -23.310 1.00 97.33 C
ANISOU 662 C LYS A 85 14204 13124 9653 -3000 -941 1998 C
ATOM 663 O LYS A 85 -18.798 -60.051 -23.684 1.00 94.23 O
ANISOU 663 O LYS A 85 13659 12911 9235 -2822 -684 1724 O
ATOM 664 CB LYS A 85 -19.502 -63.017 -21.883 1.00103.11 C
ANISOU 664 CB LYS A 85 15148 13790 10238 -3638 -886 2573 C
ATOM 665 CG LYS A 85 -19.569 -62.104 -20.659 1.00115.46 C
ANISOU 665 CG LYS A 85 16979 15646 11244 -3804 -578 2569 C
ATOM 666 CD LYS A 85 -19.187 -62.878 -19.395 1.00124.26 C
ANISOU 666 CD LYS A 85 18497 16718 11998 -4181 -754 2980 C
ATOM 667 CE LYS A 85 -18.713 -61.994 -18.268 1.00131.86 C
ANISOU 667 CE LYS A 85 19863 17896 12342 -4336 -648 2966 C
ATOM 668 NZ LYS A 85 -19.828 -61.236 -17.643 1.00142.48 N
ANISOU 668 NZ LYS A 85 21264 19540 13333 -4489 1 2793 N
ATOM 669 N GLU A 86 -17.154 -61.456 -22.979 1.00 94.52 N
ANISOU 669 N GLU A 86 14061 12608 9243 -2981 -1296 2155 N
ATOM 670 CA GLU A 86 -16.092 -60.456 -22.882 1.00 92.66 C
ANISOU 670 CA GLU A 86 13922 12433 8851 -2811 -1405 2031 C
ATOM 671 C GLU A 86 -15.552 -60.056 -24.245 1.00 92.75 C
ANISOU 671 C GLU A 86 13684 12338 9221 -2434 -1494 1771 C
ATOM 672 O GLU A 86 -14.907 -59.013 -24.323 1.00 90.77 O
ANISOU 672 O GLU A 86 13447 12177 8866 -2284 -1489 1613 O
ATOM 673 CB GLU A 86 -14.952 -60.895 -21.933 1.00 96.46 C
ANISOU 673 CB GLU A 86 14686 12805 9160 -2978 -1790 2363 C
ATOM 674 CG GLU A 86 -14.456 -62.317 -22.130 1.00107.67 C
ANISOU 674 CG GLU A 86 16071 13886 10953 -2985 -2155 2670 C
ATOM 675 CD GLU A 86 -13.713 -62.918 -20.953 1.00123.74 C
ANISOU 675 CD GLU A 86 18385 15830 12800 -3252 -2521 3120 C
ATOM 676 OE1 GLU A 86 -14.369 -63.564 -20.103 1.00109.31 O
ANISOU 676 OE1 GLU A 86 16764 14038 10730 -3593 -2474 3385 O
ATOM 677 OE2 GLU A 86 -12.469 -62.778 -20.901 1.00114.70 O
ANISOU 677 OE2 GLU A 86 17232 14569 11781 -3133 -2877 3245 O
ATOM 678 N ALA A 87 -15.812 -60.850 -25.313 1.00 88.55 N
ANISOU 678 N ALA A 87 12960 11608 9076 -2310 -1563 1718 N
ATOM 679 CA ALA A 87 -15.391 -60.486 -26.675 1.00 85.16 C
ANISOU 679 CA ALA A 87 12345 11094 8919 -1987 -1596 1454 C
ATOM 680 C ALA A 87 -16.266 -59.333 -27.156 1.00 88.20 C
ANISOU 680 C ALA A 87 12569 11734 9210 -1895 -1303 1191 C
ATOM 681 O ALA A 87 -15.744 -58.381 -27.727 1.00 86.38 O
ANISOU 681 O ALA A 87 12275 11559 8987 -1672 -1278 1004 O
ATOM 682 CB ALA A 87 -15.479 -61.673 -27.617 1.00 86.18 C
ANISOU 682 CB ALA A 87 12407 10931 9407 -1937 -1730 1445 C
ATOM 683 N GLN A 88 -17.580 -59.379 -26.836 1.00 86.57 N
ANISOU 683 N GLN A 88 12279 11677 8937 -2077 -1071 1216 N
ATOM 684 CA GLN A 88 -18.566 -58.318 -27.093 1.00 86.23 C
ANISOU 684 CA GLN A 88 12033 11864 8867 -2007 -762 1037 C
ATOM 685 C GLN A 88 -18.248 -57.063 -26.246 1.00 93.76 C
ANISOU 685 C GLN A 88 13129 12986 9511 -1966 -550 946 C
ATOM 686 O GLN A 88 -18.640 -55.955 -26.618 1.00 93.23 O
ANISOU 686 O GLN A 88 12916 13033 9474 -1797 -339 753 O
ATOM 687 CB GLN A 88 -19.991 -58.796 -26.777 1.00 89.63 C
ANISOU 687 CB GLN A 88 12305 12392 9359 -2240 -549 1154 C
ATOM 688 CG GLN A 88 -20.479 -59.982 -27.591 1.00 87.16 C
ANISOU 688 CG GLN A 88 11853 11914 9352 -2342 -759 1228 C
ATOM 689 CD GLN A 88 -21.858 -60.409 -27.157 1.00105.85 C
ANISOU 689 CD GLN A 88 14023 14392 11804 -2610 -550 1385 C
ATOM 690 OE1 GLN A 88 -22.155 -60.553 -25.959 1.00108.10 O
ANISOU 690 OE1 GLN A 88 14418 14772 11884 -2826 -328 1558 O
ATOM 691 NE2 GLN A 88 -22.738 -60.624 -28.124 1.00 93.58 N
ANISOU 691 NE2 GLN A 88 12177 12834 10546 -2635 -624 1349 N
ATOM 692 N ALA A 89 -17.568 -57.248 -25.095 1.00 93.61 N
ANISOU 692 N ALA A 89 13416 12959 9192 -2147 -625 1097 N
ATOM 693 CA ALA A 89 -17.142 -56.150 -24.222 1.00 94.80 C
ANISOU 693 CA ALA A 89 13804 13233 8985 -2180 -485 1004 C
ATOM 694 C ALA A 89 -15.884 -55.452 -24.803 1.00 96.56 C
ANISOU 694 C ALA A 89 14034 13370 9282 -1953 -732 887 C
ATOM 695 O ALA A 89 -15.740 -54.232 -24.675 1.00 96.98 O
ANISOU 695 O ALA A 89 14153 13503 9190 -1873 -578 696 O
ATOM 696 CB ALA A 89 -16.865 -56.669 -22.821 1.00 99.03 C
ANISOU 696 CB ALA A 89 14703 13793 9129 -2519 -551 1244 C
ATOM 697 N ALA A 90 -14.980 -56.241 -25.441 1.00 89.55 N
ANISOU 697 N ALA A 90 13073 12296 8655 -1853 -1085 1001 N
ATOM 698 CA ALA A 90 -13.753 -55.756 -26.071 1.00 85.60 C
ANISOU 698 CA ALA A 90 12518 11702 8305 -1639 -1298 934 C
ATOM 699 C ALA A 90 -14.103 -55.050 -27.339 1.00 86.69 C
ANISOU 699 C ALA A 90 12422 11868 8647 -1376 -1141 686 C
ATOM 700 O ALA A 90 -13.460 -54.059 -27.663 1.00 86.68 O
ANISOU 700 O ALA A 90 12401 11885 8648 -1232 -1146 564 O
ATOM 701 CB ALA A 90 -12.807 -56.907 -26.354 1.00 86.24 C
ANISOU 701 CB ALA A 90 12562 11550 8657 -1597 -1633 1140 C
ATOM 702 N ALA A 91 -15.134 -55.561 -28.062 1.00 80.82 N
ANISOU 702 N ALA A 91 11509 11127 8074 -1346 -1033 639 N
ATOM 703 CA ALA A 91 -15.688 -55.014 -29.304 1.00 77.03 C
ANISOU 703 CA ALA A 91 10812 10688 7769 -1151 -931 456 C
ATOM 704 C ALA A 91 -16.342 -53.669 -29.041 1.00 79.56 C
ANISOU 704 C ALA A 91 11073 11176 7981 -1097 -655 325 C
ATOM 705 O ALA A 91 -16.365 -52.821 -29.922 1.00 78.00 O
ANISOU 705 O ALA A 91 10742 10998 7895 -905 -617 198 O
ATOM 706 CB ALA A 91 -16.701 -55.978 -29.891 1.00 78.16 C
ANISOU 706 CB ALA A 91 10819 10793 8083 -1230 -950 491 C
ATOM 707 N GLU A 92 -16.841 -53.468 -27.812 1.00 77.77 N
ANISOU 707 N GLU A 92 10971 11046 7532 -1268 -442 360 N
ATOM 708 CA GLU A 92 -17.461 -52.237 -27.347 1.00 78.69 C
ANISOU 708 CA GLU A 92 11082 11271 7545 -1224 -97 215 C
ATOM 709 C GLU A 92 -16.392 -51.117 -27.230 1.00 81.82 C
ANISOU 709 C GLU A 92 11658 11621 7807 -1126 -149 84 C
ATOM 710 O GLU A 92 -16.741 -49.933 -27.246 1.00 82.39 O
ANISOU 710 O GLU A 92 11704 11711 7891 -1006 94 -80 O
ATOM 711 CB GLU A 92 -18.167 -52.504 -26.002 1.00 83.60 C
ANISOU 711 CB GLU A 92 11865 11987 7911 -1475 184 280 C
ATOM 712 CG GLU A 92 -19.266 -51.518 -25.626 1.00 99.34 C
ANISOU 712 CG GLU A 92 13760 14073 9911 -1415 672 129 C
ATOM 713 CD GLU A 92 -20.502 -51.455 -26.509 1.00126.69 C
ANISOU 713 CD GLU A 92 16766 17581 13788 -1262 831 142 C
ATOM 714 OE1 GLU A 92 -20.837 -52.476 -27.154 1.00128.36 O
ANISOU 714 OE1 GLU A 92 16777 17792 14203 -1323 608 295 O
ATOM 715 OE2 GLU A 92 -21.162 -50.390 -26.521 1.00120.85 O
ANISOU 715 OE2 GLU A 92 15869 16859 13189 -1097 1173 11 O
ATOM 716 N GLN A 93 -15.096 -51.493 -27.159 1.00 76.89 N
ANISOU 716 N GLN A 93 11184 10913 7117 -1173 -475 176 N
ATOM 717 CA GLN A 93 -13.972 -50.553 -27.086 1.00 75.67 C
ANISOU 717 CA GLN A 93 11161 10707 6884 -1126 -599 103 C
ATOM 718 C GLN A 93 -13.713 -49.891 -28.439 1.00 75.79 C
ANISOU 718 C GLN A 93 10949 10673 7174 -856 -625 2 C
ATOM 719 O GLN A 93 -13.301 -48.731 -28.477 1.00 75.95 O
ANISOU 719 O GLN A 93 11025 10666 7167 -789 -575 -112 O
ATOM 720 CB GLN A 93 -12.691 -51.244 -26.577 1.00 77.68 C
ANISOU 720 CB GLN A 93 11563 10887 7063 -1273 -967 301 C
ATOM 721 CG GLN A 93 -12.376 -50.954 -25.113 1.00104.74 C
ANISOU 721 CG GLN A 93 15354 14359 10082 -1569 -1009 349 C
ATOM 722 CD GLN A 93 -11.582 -49.679 -24.938 1.00129.43 C
ANISOU 722 CD GLN A 93 18621 17457 13101 -1579 -1066 217 C
ATOM 723 OE1 GLN A 93 -10.348 -49.683 -24.930 1.00126.91 O
ANISOU 723 OE1 GLN A 93 18299 17069 12853 -1623 -1417 352 O
ATOM 724 NE2 GLN A 93 -12.268 -48.556 -24.781 1.00122.24 N
ANISOU 724 NE2 GLN A 93 17815 16569 12060 -1542 -721 -37 N
ATOM 725 N LEU A 94 -13.966 -50.619 -29.539 1.00 69.77 N
ANISOU 725 N LEU A 94 9972 9890 6648 -734 -704 45 N
ATOM 726 CA LEU A 94 -13.792 -50.164 -30.928 1.00 67.40 C
ANISOU 726 CA LEU A 94 9497 9560 6551 -518 -736 -24 C
ATOM 727 C LEU A 94 -14.696 -48.962 -31.278 1.00 68.43 C
ANISOU 727 C LEU A 94 9515 9746 6738 -396 -517 -136 C
ATOM 728 O LEU A 94 -14.345 -48.182 -32.157 1.00 66.33 O
ANISOU 728 O LEU A 94 9181 9449 6573 -246 -544 -178 O
ATOM 729 CB LEU A 94 -14.078 -51.325 -31.893 1.00 67.66 C
ANISOU 729 CB LEU A 94 9415 9556 6737 -489 -847 24 C
ATOM 730 CG LEU A 94 -13.052 -52.461 -31.889 1.00 73.69 C
ANISOU 730 CG LEU A 94 10250 10184 7565 -521 -1044 120 C
ATOM 731 CD1 LEU A 94 -13.702 -53.796 -32.152 1.00 74.77 C
ANISOU 731 CD1 LEU A 94 10369 10253 7785 -603 -1102 167 C
ATOM 732 CD2 LEU A 94 -12.006 -52.225 -32.913 1.00 76.31 C
ANISOU 732 CD2 LEU A 94 10534 10435 8026 -351 -1099 75 C
ATOM 733 N LYS A 95 -15.840 -48.808 -30.576 1.00 65.67 N
ANISOU 733 N LYS A 95 9133 9463 6356 -455 -282 -162 N
ATOM 734 CA LYS A 95 -16.796 -47.702 -30.709 1.00 65.58 C
ANISOU 734 CA LYS A 95 8974 9466 6478 -319 -26 -245 C
ATOM 735 C LYS A 95 -16.131 -46.353 -30.410 1.00 68.06 C
ANISOU 735 C LYS A 95 9451 9683 6725 -245 65 -374 C
ATOM 736 O LYS A 95 -16.473 -45.360 -31.030 1.00 66.90 O
ANISOU 736 O LYS A 95 9171 9480 6770 -66 150 -412 O
ATOM 737 CB LYS A 95 -17.990 -47.909 -29.763 1.00 70.65 C
ANISOU 737 CB LYS A 95 9563 10179 7102 -416 281 -248 C
ATOM 738 CG LYS A 95 -18.922 -49.043 -30.176 1.00 86.64 C
ANISOU 738 CG LYS A 95 11348 12288 9283 -492 212 -104 C
ATOM 739 CD LYS A 95 -20.246 -48.965 -29.433 1.00100.87 C
ANISOU 739 CD LYS A 95 12984 14165 11177 -544 585 -87 C
ATOM 740 CE LYS A 95 -21.217 -50.037 -29.869 1.00113.48 C
ANISOU 740 CE LYS A 95 14294 15842 12983 -651 491 84 C
ATOM 741 NZ LYS A 95 -22.511 -49.932 -29.143 1.00122.87 N
ANISOU 741 NZ LYS A 95 15246 17111 14328 -698 898 130 N
ATOM 742 N THR A 96 -15.154 -46.329 -29.492 1.00 65.84 N
ANISOU 742 N THR A 96 9464 9366 6187 -405 -2 -413 N
ATOM 743 CA THR A 96 -14.416 -45.118 -29.128 1.00 66.78 C
ANISOU 743 CA THR A 96 9788 9372 6213 -408 28 -537 C
ATOM 744 C THR A 96 -13.555 -44.647 -30.326 1.00 69.93 C
ANISOU 744 C THR A 96 10058 9707 6805 -261 -186 -484 C
ATOM 745 O THR A 96 -13.661 -43.492 -30.749 1.00 70.59 O
ANISOU 745 O THR A 96 10103 9693 7026 -125 -81 -555 O
ATOM 746 CB THR A 96 -13.579 -45.350 -27.848 1.00 73.90 C
ANISOU 746 CB THR A 96 11040 10270 6768 -685 -88 -544 C
ATOM 747 OG1 THR A 96 -14.375 -46.015 -26.854 1.00 70.99 O
ANISOU 747 OG1 THR A 96 10800 9991 6183 -850 102 -542 O
ATOM 748 CG2 THR A 96 -13.036 -44.046 -27.270 1.00 75.79 C
ANISOU 748 CG2 THR A 96 11556 10378 6861 -760 -28 -712 C
ATOM 749 N THR A 97 -12.745 -45.560 -30.887 1.00 64.50 N
ANISOU 749 N THR A 97 9301 9057 6151 -283 -450 -352 N
ATOM 750 CA THR A 97 -11.855 -45.314 -32.020 1.00 62.08 C
ANISOU 750 CA THR A 97 8880 8709 6000 -168 -600 -291 C
ATOM 751 C THR A 97 -12.699 -44.950 -33.244 1.00 65.46 C
ANISOU 751 C THR A 97 9117 9158 6596 18 -516 -286 C
ATOM 752 O THR A 97 -12.438 -43.922 -33.870 1.00 65.67 O
ANISOU 752 O THR A 97 9115 9119 6717 116 -499 -286 O
ATOM 753 CB THR A 97 -10.943 -46.532 -32.219 1.00 65.21 C
ANISOU 753 CB THR A 97 9239 9116 6421 -218 -812 -168 C
ATOM 754 OG1 THR A 97 -10.263 -46.765 -30.986 1.00 67.54 O
ANISOU 754 OG1 THR A 97 9696 9388 6576 -411 -943 -118 O
ATOM 755 CG2 THR A 97 -9.908 -46.328 -33.305 1.00 62.50 C
ANISOU 755 CG2 THR A 97 8783 8729 6236 -109 -890 -113 C
ATOM 756 N ARG A 98 -13.747 -45.743 -33.520 1.00 61.27 N
ANISOU 756 N ARG A 98 8465 8713 6104 34 -487 -255 N
ATOM 757 CA ARG A 98 -14.692 -45.543 -34.616 1.00 61.25 C
ANISOU 757 CA ARG A 98 8270 8750 6253 156 -484 -204 C
ATOM 758 C ARG A 98 -15.275 -44.129 -34.561 1.00 66.76 C
ANISOU 758 C ARG A 98 8898 9372 7095 284 -320 -230 C
ATOM 759 O ARG A 98 -15.195 -43.401 -35.547 1.00 66.62 O
ANISOU 759 O ARG A 98 8809 9316 7188 395 -388 -158 O
ATOM 760 CB ARG A 98 -15.813 -46.615 -34.540 1.00 61.21 C
ANISOU 760 CB ARG A 98 8140 8837 6280 83 -491 -159 C
ATOM 761 CG ARG A 98 -16.881 -46.629 -35.650 1.00 59.84 C
ANISOU 761 CG ARG A 98 7744 8724 6267 142 -581 -62 C
ATOM 762 CD ARG A 98 -18.133 -45.800 -35.363 1.00 61.24 C
ANISOU 762 CD ARG A 98 7687 8904 6676 239 -407 -17 C
ATOM 763 NE ARG A 98 -18.743 -46.028 -34.047 1.00 66.60 N
ANISOU 763 NE ARG A 98 8341 9601 7364 172 -148 -75 N
ATOM 764 CZ ARG A 98 -19.747 -46.868 -33.803 1.00 79.03 C
ANISOU 764 CZ ARG A 98 9735 11264 9028 69 -114 1 C
ATOM 765 NH1 ARG A 98 -20.249 -47.616 -34.778 1.00 66.35 N
ANISOU 765 NH1 ARG A 98 7970 9727 7512 1 -376 127 N
ATOM 766 NH2 ARG A 98 -20.248 -46.973 -32.581 1.00 65.86 N
ANISOU 766 NH2 ARG A 98 8071 9615 7339 0 185 -48 N
ATOM 767 N ASN A 99 -15.843 -43.736 -33.413 1.00 64.79 N
ANISOU 767 N ASN A 99 8693 9080 6845 266 -83 -328 N
ATOM 768 CA ASN A 99 -16.448 -42.415 -33.284 1.00 66.32 C
ANISOU 768 CA ASN A 99 8824 9140 7234 418 136 -380 C
ATOM 769 C ASN A 99 -15.426 -41.289 -33.504 1.00 70.00 C
ANISOU 769 C ASN A 99 9451 9446 7698 458 89 -423 C
ATOM 770 O ASN A 99 -15.761 -40.319 -34.172 1.00 70.57 O
ANISOU 770 O ASN A 99 9409 9401 8004 620 123 -363 O
ATOM 771 CB ASN A 99 -17.154 -42.256 -31.938 1.00 66.78 C
ANISOU 771 CB ASN A 99 8961 9160 7253 378 483 -528 C
ATOM 772 CG ASN A 99 -18.355 -43.167 -31.744 1.00 87.64 C
ANISOU 772 CG ASN A 99 11367 11942 9989 353 597 -452 C
ATOM 773 OD1 ASN A 99 -18.916 -43.741 -32.690 1.00 76.02 O
ANISOU 773 OD1 ASN A 99 9621 10570 8695 394 409 -283 O
ATOM 774 ND2 ASN A 99 -18.761 -43.357 -30.495 1.00 83.02 N
ANISOU 774 ND2 ASN A 99 10911 11373 9261 244 900 -569 N
ATOM 775 N ALA A 100 -14.178 -41.442 -33.022 1.00 65.46 N
ANISOU 775 N ALA A 100 9109 8858 6903 302 -27 -479 N
ATOM 776 CA ALA A 100 -13.172 -40.386 -33.161 1.00 64.88 C
ANISOU 776 CA ALA A 100 9173 8629 6848 290 -86 -504 C
ATOM 777 C ALA A 100 -12.633 -40.259 -34.584 1.00 64.94 C
ANISOU 777 C ALA A 100 9043 8661 6969 372 -269 -332 C
ATOM 778 O ALA A 100 -12.586 -39.152 -35.106 1.00 66.60 O
ANISOU 778 O ALA A 100 9243 8729 7334 461 -245 -288 O
ATOM 779 CB ALA A 100 -12.028 -40.605 -32.183 1.00 65.68 C
ANISOU 779 CB ALA A 100 9523 8718 6714 61 -195 -576 C
ATOM 780 N TYR A 101 -12.257 -41.363 -35.223 1.00 57.89 N
ANISOU 780 N TYR A 101 8072 7924 5998 338 -423 -237 N
ATOM 781 CA TYR A 101 -11.684 -41.314 -36.564 1.00 55.89 C
ANISOU 781 CA TYR A 101 7749 7703 5781 387 -534 -102 C
ATOM 782 C TYR A 101 -12.720 -41.044 -37.648 1.00 59.82 C
ANISOU 782 C TYR A 101 8116 8237 6378 511 -557 14 C
ATOM 783 O TYR A 101 -12.386 -40.296 -38.563 1.00 61.95 O
ANISOU 783 O TYR A 101 8386 8459 6694 553 -601 133 O
ATOM 784 CB TYR A 101 -10.852 -42.556 -36.848 1.00 56.01 C
ANISOU 784 CB TYR A 101 7766 7825 5690 314 -631 -78 C
ATOM 785 CG TYR A 101 -9.531 -42.474 -36.110 1.00 59.21 C
ANISOU 785 CG TYR A 101 8238 8167 6091 202 -679 -88 C
ATOM 786 CD1 TYR A 101 -8.428 -41.843 -36.684 1.00 62.07 C
ANISOU 786 CD1 TYR A 101 8573 8473 6538 189 -697 -2 C
ATOM 787 CD2 TYR A 101 -9.416 -42.917 -34.792 1.00 60.07 C
ANISOU 787 CD2 TYR A 101 8436 8270 6117 77 -724 -153 C
ATOM 788 CE1 TYR A 101 -7.229 -41.704 -35.986 1.00 63.74 C
ANISOU 788 CE1 TYR A 101 8792 8623 6804 59 -787 29 C
ATOM 789 CE2 TYR A 101 -8.218 -42.794 -34.090 1.00 61.60 C
ANISOU 789 CE2 TYR A 101 8684 8407 6314 -66 -849 -117 C
ATOM 790 CZ TYR A 101 -7.132 -42.176 -34.688 1.00 68.70 C
ANISOU 790 CZ TYR A 101 9504 9248 7351 -73 -893 -24 C
ATOM 791 OH TYR A 101 -5.953 -42.044 -34.007 1.00 69.99 O
ANISOU 791 OH TYR A 101 9665 9356 7570 -239 -1061 50 O
ATOM 792 N ILE A 102 -13.975 -41.561 -37.542 1.00 54.77 N
ANISOU 792 N ILE A 102 7350 7673 5789 548 -546 17 N
ATOM 793 CA ILE A 102 -15.045 -41.216 -38.506 1.00 55.31 C
ANISOU 793 CA ILE A 102 7245 7766 6005 645 -634 180 C
ATOM 794 C ILE A 102 -15.248 -39.666 -38.475 1.00 60.39 C
ANISOU 794 C ILE A 102 7845 8208 6890 786 -543 242 C
ATOM 795 O ILE A 102 -15.351 -39.028 -39.515 1.00 62.11 O
ANISOU 795 O ILE A 102 8014 8394 7193 844 -672 435 O
ATOM 796 CB ILE A 102 -16.395 -41.992 -38.266 1.00 58.49 C
ANISOU 796 CB ILE A 102 7451 8271 6502 640 -644 200 C
ATOM 797 CG1 ILE A 102 -16.276 -43.474 -38.672 1.00 57.07 C
ANISOU 797 CG1 ILE A 102 7327 8247 6112 491 -799 183 C
ATOM 798 CG2 ILE A 102 -17.581 -41.324 -38.994 1.00 60.29 C
ANISOU 798 CG2 ILE A 102 7422 8478 7008 758 -739 409 C
ATOM 799 CD1 ILE A 102 -17.579 -44.295 -38.678 1.00 57.17 C
ANISOU 799 CD1 ILE A 102 7139 8361 6222 429 -875 245 C
ATOM 800 N GLN A 103 -15.256 -39.090 -37.281 1.00 55.82 N
ANISOU 800 N GLN A 103 7331 7477 6400 819 -321 78 N
ATOM 801 CA GLN A 103 -15.435 -37.673 -37.027 1.00 57.38 C
ANISOU 801 CA GLN A 103 7542 7413 6847 950 -173 66 C
ATOM 802 C GLN A 103 -14.323 -36.816 -37.666 1.00 61.26 C
ANISOU 802 C GLN A 103 8178 7782 7315 913 -281 154 C
ATOM 803 O GLN A 103 -14.602 -35.791 -38.305 1.00 62.58 O
ANISOU 803 O GLN A 103 8279 7784 7715 1032 -313 319 O
ATOM 804 CB GLN A 103 -15.442 -37.466 -35.509 1.00 58.92 C
ANISOU 804 CB GLN A 103 7904 7482 7001 911 106 -206 C
ATOM 805 CG GLN A 103 -16.252 -36.284 -35.050 1.00 65.91 C
ANISOU 805 CG GLN A 103 8745 8087 8211 1097 383 -278 C
ATOM 806 CD GLN A 103 -16.483 -36.301 -33.568 1.00 74.88 C
ANISOU 806 CD GLN A 103 10071 9146 9235 1038 719 -573 C
ATOM 807 OE1 GLN A 103 -15.692 -36.842 -32.788 1.00 66.32 O
ANISOU 807 OE1 GLN A 103 9256 8149 7792 813 690 -727 O
ATOM 808 NE2 GLN A 103 -17.580 -35.702 -33.147 1.00 71.76 N
ANISOU 808 NE2 GLN A 103 9541 8575 9150 1234 1054 -642 N
ATOM 809 N LYS A 104 -13.072 -37.254 -37.479 1.00 55.26 N
ANISOU 809 N LYS A 104 7587 7096 6312 742 -341 76 N
ATOM 810 CA LYS A 104 -11.859 -36.569 -37.911 1.00 54.37 C
ANISOU 810 CA LYS A 104 7588 6889 6180 658 -411 150 C
ATOM 811 C LYS A 104 -11.681 -36.540 -39.447 1.00 58.93 C
ANISOU 811 C LYS A 104 8094 7564 6733 679 -551 407 C
ATOM 812 O LYS A 104 -11.409 -35.467 -40.001 1.00 59.50 O
ANISOU 812 O LYS A 104 8198 7477 6933 697 -571 556 O
ATOM 813 CB LYS A 104 -10.649 -37.264 -37.249 1.00 53.23 C
ANISOU 813 CB LYS A 104 7555 6834 5837 471 -451 37 C
ATOM 814 CG LYS A 104 -9.402 -36.400 -37.027 1.00 63.20 C
ANISOU 814 CG LYS A 104 8933 7936 7143 333 -487 47 C
ATOM 815 CD LYS A 104 -8.751 -36.616 -35.624 1.00 82.31 C
ANISOU 815 CD LYS A 104 11510 10316 9447 143 -517 -133 C
ATOM 816 CE LYS A 104 -8.417 -38.060 -35.221 1.00 91.70 C
ANISOU 816 CE LYS A 104 12650 11726 10466 63 -605 -151 C
ATOM 817 NZ LYS A 104 -7.889 -38.169 -33.825 1.00 91.13 N
ANISOU 817 NZ LYS A 104 12761 11606 10259 -151 -688 -277 N
ATOM 818 N TYR A 105 -11.832 -37.715 -40.118 1.00 55.21 N
ANISOU 818 N TYR A 105 7568 7336 6073 650 -640 453 N
ATOM 819 CA TYR A 105 -11.529 -37.936 -41.537 1.00 55.68 C
ANISOU 819 CA TYR A 105 7654 7524 5976 607 -743 639 C
ATOM 820 C TYR A 105 -12.766 -38.019 -42.464 1.00 62.95 C
ANISOU 820 C TYR A 105 8493 8530 6894 663 -908 817 C
ATOM 821 O TYR A 105 -12.657 -37.650 -43.645 1.00 66.73 O
ANISOU 821 O TYR A 105 9042 9046 7267 620 -1017 1032 O
ATOM 822 CB TYR A 105 -10.599 -39.166 -41.672 1.00 55.16 C
ANISOU 822 CB TYR A 105 7652 7622 5686 503 -703 536 C
ATOM 823 CG TYR A 105 -9.286 -38.901 -40.952 1.00 55.89 C
ANISOU 823 CG TYR A 105 7766 7623 5846 432 -609 464 C
ATOM 824 CD1 TYR A 105 -8.381 -37.963 -41.440 1.00 59.80 C
ANISOU 824 CD1 TYR A 105 8288 8031 6403 378 -568 600 C
ATOM 825 CD2 TYR A 105 -9.028 -39.455 -39.701 1.00 54.56 C
ANISOU 825 CD2 TYR A 105 7588 7440 5702 389 -598 298 C
ATOM 826 CE1 TYR A 105 -7.232 -37.617 -40.726 1.00 59.65 C
ANISOU 826 CE1 TYR A 105 8250 7913 6501 277 -534 567 C
ATOM 827 CE2 TYR A 105 -7.872 -39.130 -38.987 1.00 55.20 C
ANISOU 827 CE2 TYR A 105 7680 7433 5860 283 -595 273 C
ATOM 828 CZ TYR A 105 -6.976 -38.210 -39.509 1.00 62.50 C
ANISOU 828 CZ TYR A 105 8595 8270 6880 225 -572 406 C
ATOM 829 OH TYR A 105 -5.835 -37.835 -38.846 1.00 64.88 O
ANISOU 829 OH TYR A 105 8875 8479 7298 83 -613 416 O
ATOM 830 N LEU A 106 -13.936 -38.429 -41.942 1.00 57.60 N
ANISOU 830 N LEU A 106 7664 7882 6340 733 -942 766 N
ATOM 831 CA LEU A 106 -15.184 -38.413 -42.719 1.00 57.92 C
ANISOU 831 CA LEU A 106 7553 7983 6469 773 -1152 983 C
ATOM 832 C LEU A 106 -16.091 -37.330 -42.132 1.00 58.61 C
ANISOU 832 C LEU A 106 7427 7853 6988 965 -1085 1063 C
ATOM 833 O LEU A 106 -17.273 -37.571 -41.879 1.00 59.85 O
ANISOU 833 O LEU A 106 7342 8033 7365 1044 -1118 1107 O
ATOM 834 CB LEU A 106 -15.883 -39.790 -42.764 1.00 57.60 C
ANISOU 834 CB LEU A 106 7449 8144 6294 683 -1263 915 C
ATOM 835 CG LEU A 106 -15.264 -40.858 -43.653 1.00 61.87 C
ANISOU 835 CG LEU A 106 8212 8859 6438 506 -1362 872 C
ATOM 836 CD1 LEU A 106 -15.928 -42.156 -43.404 1.00 63.04 C
ANISOU 836 CD1 LEU A 106 8307 9125 6519 417 -1440 761 C
ATOM 837 CD2 LEU A 106 -15.426 -40.526 -45.124 1.00 65.08 C
ANISOU 837 CD2 LEU A 106 8733 9335 6660 414 -1599 1127 C
ATOM 838 N SER A 190 -15.501 -36.138 -41.914 1.00 64.52 N
ANISOU 838 N SER A 190 8491 12428 3594 -245 429 -1098 N
ATOM 839 CA SER A 190 -16.081 -34.914 -41.359 1.00 62.05 C
ANISOU 839 CA SER A 190 8109 12075 3392 -340 358 -904 C
ATOM 840 C SER A 190 -17.323 -34.403 -42.089 1.00 69.08 C
ANISOU 840 C SER A 190 9010 13000 4236 -463 240 -844 C
ATOM 841 O SER A 190 -18.205 -33.855 -41.438 1.00 68.95 O
ANISOU 841 O SER A 190 8972 12885 4340 -491 163 -747 O
ATOM 842 CB SER A 190 -15.040 -33.799 -41.366 1.00 64.21 C
ANISOU 842 CB SER A 190 8292 12512 3594 -365 405 -773 C
ATOM 843 OG SER A 190 -14.268 -33.762 -42.557 1.00 72.36 O
ANISOU 843 OG SER A 190 9298 13793 4403 -397 457 -822 O
ATOM 844 N GLY A 191 -17.359 -34.550 -43.416 1.00 68.85 N
ANISOU 844 N GLY A 191 9004 13138 4018 -516 224 -904 N
ATOM 845 CA GLY A 191 -18.427 -34.077 -44.288 1.00 69.21 C
ANISOU 845 CA GLY A 191 9053 13275 3968 -610 107 -857 C
ATOM 846 C GLY A 191 -18.448 -32.569 -44.376 1.00 72.91 C
ANISOU 846 C GLY A 191 9506 13804 4392 -639 47 -644 C
ATOM 847 O GLY A 191 -17.399 -31.931 -44.494 1.00 73.20 O
ANISOU 847 O GLY A 191 9547 13917 4348 -659 113 -562 O
ATOM 848 N GLN A 192 -19.648 -31.998 -44.287 1.00 69.41 N
ANISOU 848 N GLN A 192 9056 13336 3982 -641 -79 -561 N
ATOM 849 CA GLN A 192 -19.928 -30.565 -44.294 1.00 69.69 C
ANISOU 849 CA GLN A 192 9135 13375 3969 -623 -167 -359 C
ATOM 850 C GLN A 192 -19.316 -29.855 -43.051 1.00 76.75 C
ANISOU 850 C GLN A 192 10045 14109 5008 -592 -115 -237 C
ATOM 851 O GLN A 192 -19.245 -28.626 -43.026 1.00 77.12 O
ANISOU 851 O GLN A 192 10187 14125 4990 -596 -158 -67 O
ATOM 852 CB GLN A 192 -21.457 -30.358 -44.336 1.00 70.90 C
ANISOU 852 CB GLN A 192 9250 13561 4127 -571 -318 -345 C
ATOM 853 CG GLN A 192 -22.201 -30.698 -43.025 1.00 74.29 C
ANISOU 853 CG GLN A 192 9589 13865 4773 -523 -336 -384 C
ATOM 854 CD GLN A 192 -22.566 -32.153 -42.813 1.00 87.02 C
ANISOU 854 CD GLN A 192 11139 15466 6460 -599 -292 -586 C
ATOM 855 OE1 GLN A 192 -21.917 -33.089 -43.289 1.00 78.36 O
ANISOU 855 OE1 GLN A 192 10088 14370 5315 -658 -205 -714 O
ATOM 856 NE2 GLN A 192 -23.619 -32.373 -42.047 1.00 84.16 N
ANISOU 856 NE2 GLN A 192 10688 15086 6202 -602 -347 -622 N
ATOM 857 N CYS A 193 -18.918 -30.634 -42.011 1.00 74.24 N
ANISOU 857 N CYS A 193 9662 13677 4870 -560 -29 -325 N
ATOM 858 CA CYS A 193 -18.331 -30.140 -40.768 1.00 72.89 C
ANISOU 858 CA CYS A 193 9482 13370 4842 -531 26 -239 C
ATOM 859 C CYS A 193 -16.872 -29.809 -40.932 1.00 73.83 C
ANISOU 859 C CYS A 193 9610 13580 4862 -594 136 -205 C
ATOM 860 O CYS A 193 -16.087 -30.624 -41.416 1.00 74.19 O
ANISOU 860 O CYS A 193 9610 13750 4831 -595 225 -331 O
ATOM 861 CB CYS A 193 -18.535 -31.142 -39.645 1.00 73.33 C
ANISOU 861 CB CYS A 193 9475 13288 5098 -470 67 -348 C
ATOM 862 SG CYS A 193 -20.251 -31.653 -39.428 1.00 78.28 S
ANISOU 862 SG CYS A 193 10063 13869 5811 -462 -45 -414 S
ATOM 863 N GLU A 194 -16.522 -28.596 -40.524 1.00 68.21 N
ANISOU 863 N GLU A 194 8964 12821 4133 -649 131 -43 N
ATOM 864 CA GLU A 194 -15.178 -28.048 -40.542 1.00 67.91 C
ANISOU 864 CA GLU A 194 8931 12890 3981 -767 233 10 C
ATOM 865 C GLU A 194 -14.877 -27.542 -39.131 1.00 70.16 C
ANISOU 865 C GLU A 194 9205 13033 4422 -758 261 83 C
ATOM 866 O GLU A 194 -15.771 -26.995 -38.461 1.00 68.50 O
ANISOU 866 O GLU A 194 9063 12632 4334 -696 173 169 O
ATOM 867 CB GLU A 194 -15.055 -26.951 -41.614 1.00 71.01 C
ANISOU 867 CB GLU A 194 9478 13368 4134 -914 196 146 C
ATOM 868 N VAL A 195 -13.638 -27.774 -38.663 1.00 67.22 N
ANISOU 868 N VAL A 195 8725 12779 4035 -800 382 33 N
ATOM 869 CA VAL A 195 -13.158 -27.449 -37.309 1.00 66.45 C
ANISOU 869 CA VAL A 195 8583 12597 4068 -799 426 74 C
ATOM 870 C VAL A 195 -13.513 -25.977 -36.976 1.00 71.30 C
ANISOU 870 C VAL A 195 9379 13051 4661 -914 360 263 C
ATOM 871 O VAL A 195 -13.428 -25.141 -37.872 1.00 72.65 O
ANISOU 871 O VAL A 195 9698 13270 4636 -1060 338 360 O
ATOM 872 CB VAL A 195 -11.636 -27.762 -37.163 1.00 71.56 C
ANISOU 872 CB VAL A 195 9073 13504 4612 -851 563 -9 C
ATOM 873 CG1 VAL A 195 -11.130 -27.478 -35.744 1.00 71.29 C
ANISOU 873 CG1 VAL A 195 8974 13414 4700 -847 606 22 C
ATOM 874 CG2 VAL A 195 -11.339 -29.210 -37.529 1.00 71.34 C
ANISOU 874 CG2 VAL A 195 8919 13606 4581 -677 615 -202 C
ATOM 875 N PRO A 196 -14.009 -25.625 -35.763 1.00 67.01 N
ANISOU 875 N PRO A 196 8866 12294 4299 -840 318 321 N
ATOM 876 CA PRO A 196 -14.192 -26.440 -34.541 1.00 65.25 C
ANISOU 876 CA PRO A 196 8509 11977 4306 -687 337 237 C
ATOM 877 C PRO A 196 -15.496 -27.243 -34.477 1.00 69.16 C
ANISOU 877 C PRO A 196 8980 12353 4944 -525 255 169 C
ATOM 878 O PRO A 196 -15.793 -27.831 -33.446 1.00 67.89 O
ANISOU 878 O PRO A 196 8748 12085 4960 -427 263 118 O
ATOM 879 CB PRO A 196 -14.165 -25.388 -33.442 1.00 66.28 C
ANISOU 879 CB PRO A 196 8725 11949 4508 -734 322 356 C
ATOM 880 CG PRO A 196 -14.819 -24.196 -34.091 1.00 71.87 C
ANISOU 880 CG PRO A 196 9666 12550 5090 -797 225 497 C
ATOM 881 CD PRO A 196 -14.352 -24.208 -35.512 1.00 68.85 C
ANISOU 881 CD PRO A 196 9320 12355 4483 -922 250 491 C
ATOM 882 N LEU A 197 -16.288 -27.242 -35.543 1.00 66.77 N
ANISOU 882 N LEU A 197 8735 12084 4550 -518 178 168 N
ATOM 883 CA LEU A 197 -17.506 -28.036 -35.561 1.00 66.03 C
ANISOU 883 CA LEU A 197 8594 11939 4557 -411 106 85 C
ATOM 884 C LEU A 197 -17.117 -29.442 -35.985 1.00 69.89 C
ANISOU 884 C LEU A 197 9001 12517 5035 -396 178 -83 C
ATOM 885 O LEU A 197 -16.252 -29.604 -36.845 1.00 71.26 O
ANISOU 885 O LEU A 197 9172 12843 5061 -447 239 -123 O
ATOM 886 CB LEU A 197 -18.599 -27.439 -36.474 1.00 67.23 C
ANISOU 886 CB LEU A 197 8827 12117 4599 -391 -23 145 C
ATOM 887 CG LEU A 197 -19.232 -26.092 -36.068 1.00 71.50 C
ANISOU 887 CG LEU A 197 9493 12539 5136 -331 -122 300 C
ATOM 888 CD1 LEU A 197 -20.227 -25.620 -37.114 1.00 72.83 C
ANISOU 888 CD1 LEU A 197 9742 12776 5152 -264 -254 345 C
ATOM 889 CD2 LEU A 197 -19.888 -26.154 -34.699 1.00 72.64 C
ANISOU 889 CD2 LEU A 197 9562 12557 5479 -227 -144 289 C
ATOM 890 N VAL A 198 -17.716 -30.455 -35.353 1.00 64.26 N
ANISOU 890 N VAL A 198 8244 11708 4462 -329 178 -185 N
ATOM 891 CA VAL A 198 -17.409 -31.864 -35.612 1.00 63.13 C
ANISOU 891 CA VAL A 198 8095 11584 4307 -297 243 -351 C
ATOM 892 C VAL A 198 -18.659 -32.615 -36.014 1.00 68.28 C
ANISOU 892 C VAL A 198 8769 12207 4965 -327 175 -445 C
ATOM 893 O VAL A 198 -19.746 -32.269 -35.553 1.00 69.08 O
ANISOU 893 O VAL A 198 8841 12262 5144 -342 96 -400 O
ATOM 894 CB VAL A 198 -16.699 -32.555 -34.411 1.00 63.85 C
ANISOU 894 CB VAL A 198 8170 11571 4520 -207 330 -405 C
ATOM 895 CG1 VAL A 198 -15.258 -32.063 -34.273 1.00 62.70 C
ANISOU 895 CG1 VAL A 198 7966 11552 4305 -187 412 -364 C
ATOM 896 CG2 VAL A 198 -17.484 -32.397 -33.104 1.00 61.69 C
ANISOU 896 CG2 VAL A 198 7886 11124 4428 -192 294 -352 C
ATOM 897 N AARG A 199 -18.498 -33.658 -36.839 0.50 66.04 N
ANISOU 897 N AARG A 199 8536 11972 4586 -338 209 -588 N
ATOM 898 N BARG A 199 -18.512 -33.646 -36.865 0.50 65.37 N
ANISOU 898 N BARG A 199 8450 11889 4498 -339 207 -587 N
ATOM 899 CA AARG A 199 -19.569 -34.520 -37.339 0.50 66.79 C
ANISOU 899 CA AARG A 199 8671 12058 4647 -412 160 -708 C
ATOM 900 CA BARG A 199 -19.629 -34.466 -37.346 0.50 65.73 C
ANISOU 900 CA BARG A 199 8533 11928 4513 -416 154 -702 C
ATOM 901 C AARG A 199 -20.255 -35.281 -36.169 0.50 70.86 C
ANISOU 901 C AARG A 199 9221 12394 5311 -438 167 -764 C
ATOM 902 C BARG A 199 -20.265 -35.257 -36.182 0.50 70.37 C
ANISOU 902 C BARG A 199 9156 12335 5247 -438 165 -762 C
ATOM 903 O AARG A 199 -19.576 -35.990 -35.425 0.50 71.18 O
ANISOU 903 O AARG A 199 9340 12288 5417 -367 247 -814 O
ATOM 904 O BARG A 199 -19.562 -35.957 -35.454 0.50 70.67 O
ANISOU 904 O BARG A 199 9272 12229 5350 -366 246 -811 O
ATOM 905 CB AARG A 199 -18.975 -35.481 -38.396 0.50 67.05 C
ANISOU 905 CB AARG A 199 8792 12153 4531 -407 215 -856 C
ATOM 906 CB BARG A 199 -19.158 -35.399 -38.478 0.50 64.14 C
ANISOU 906 CB BARG A 199 8416 11798 4158 -424 199 -849 C
ATOM 907 CG AARG A 199 -19.909 -36.563 -38.916 0.50 76.69 C
ANISOU 907 CG AARG A 199 10102 13344 5693 -512 184 -1011 C
ATOM 908 CG BARG A 199 -20.281 -36.106 -39.226 0.50 67.23 C
ANISOU 908 CG BARG A 199 8850 12225 4467 -548 136 -968 C
ATOM 909 CD AARG A 199 -20.718 -36.126 -40.114 0.50 81.02 C
ANISOU 909 CD AARG A 199 10591 14090 6103 -614 90 -1006 C
ATOM 910 CD BARG A 199 -19.738 -37.327 -39.933 0.50 61.68 C
ANISOU 910 CD BARG A 199 8291 11498 3645 -537 203 -1145 C
ATOM 911 NE AARG A 199 -21.996 -36.833 -40.149 0.50 83.21 N
ANISOU 911 NE AARG A 199 10886 14362 6367 -762 32 -1113 N
ATOM 912 NE BARG A 199 -20.762 -38.325 -40.238 0.50 52.97 N
ANISOU 912 NE BARG A 199 7292 10342 2493 -687 170 -1291 N
ATOM 913 CZ AARG A 199 -23.159 -36.280 -39.829 0.50 90.29 C
ANISOU 913 CZ AARG A 199 11656 15347 7302 -829 -62 -1054 C
ATOM 914 CZ BARG A 199 -20.531 -39.422 -40.947 0.50 59.26 C
ANISOU 914 CZ BARG A 199 8260 11094 3163 -706 212 -1463 C
ATOM 915 NH1AARG A 199 -23.221 -35.000 -39.490 0.50 69.69 N
ANISOU 915 NH1AARG A 199 8935 12797 4747 -730 -117 -884 N
ATOM 916 NH1BARG A 199 -19.328 -39.652 -41.451 0.50 45.79 N
ANISOU 916 NH1BARG A 199 6614 9417 1366 -549 285 -1513 N
ATOM 917 NH2AARG A 199 -24.274 -36.994 -39.877 0.50 77.83 N
ANISOU 917 NH2AARG A 199 10070 13819 5682 -998 -104 -1173 N
ATOM 918 NH2BARG A 199 -21.512 -40.278 -41.192 0.50 44.91 N
ANISOU 918 NH2BARG A 199 6555 9225 1285 -893 181 -1595 N
ATOM 919 N THR A 200 -21.588 -35.091 -35.987 1.00 67.12 N
ANISOU 919 N THR A 200 8681 11956 4867 -532 80 -754 N
ATOM 920 CA THR A 200 -22.388 -35.759 -34.923 1.00 66.56 C
ANISOU 920 CA THR A 200 8623 11762 4904 -612 85 -809 C
ATOM 921 C THR A 200 -23.862 -35.979 -35.368 1.00 73.26 C
ANISOU 921 C THR A 200 9395 12766 5675 -777 -3 -883 C
ATOM 922 O THR A 200 -24.506 -35.059 -35.890 1.00 73.93 O
ANISOU 922 O THR A 200 9344 13050 5697 -753 -100 -816 O
ATOM 923 CB THR A 200 -22.329 -35.016 -33.577 1.00 66.39 C
ANISOU 923 CB THR A 200 8528 11654 5042 -532 91 -685 C
ATOM 924 OG1 THR A 200 -23.322 -35.574 -32.712 1.00 64.89 O
ANISOU 924 OG1 THR A 200 8326 11407 4921 -644 83 -739 O
ATOM 925 CG2 THR A 200 -22.556 -33.517 -33.715 1.00 64.06 C
ANISOU 925 CG2 THR A 200 8113 11485 4743 -456 9 -535 C
ATOM 926 N ASP A 201 -24.387 -37.198 -35.145 1.00 70.44 N
ANISOU 926 N ASP A 201 9139 12325 5298 -945 30 -1025 N
ATOM 927 CA ASP A 201 -25.759 -37.530 -35.525 1.00 71.69 C
ANISOU 927 CA ASP A 201 9215 12669 5357 -1156 -39 -1123 C
ATOM 928 C ASP A 201 -26.787 -37.111 -34.450 1.00 77.30 C
ANISOU 928 C ASP A 201 9755 13467 6148 -1214 -81 -1081 C
ATOM 929 O ASP A 201 -27.974 -37.048 -34.777 1.00 77.99 O
ANISOU 929 O ASP A 201 9685 13813 6134 -1351 -158 -1143 O
ATOM 930 CB ASP A 201 -25.886 -39.027 -35.852 1.00 75.08 C
ANISOU 930 CB ASP A 201 9867 12973 5688 -1365 19 -1307 C
ATOM 931 CG ASP A 201 -25.625 -39.402 -37.317 1.00 85.54 C
ANISOU 931 CG ASP A 201 11277 14379 6846 -1388 8 -1403 C
ATOM 932 OD1 ASP A 201 -25.587 -40.618 -37.621 1.00 87.93 O
ANISOU 932 OD1 ASP A 201 11813 14540 7057 -1533 61 -1558 O
ATOM 933 OD2 ASP A 201 -25.487 -38.475 -38.164 1.00 85.48 O
ANISOU 933 OD2 ASP A 201 11128 14568 6783 -1268 -54 -1325 O
ATOM 934 N ASN A 202 -26.333 -36.807 -33.190 1.00 73.57 N
ANISOU 934 N ASN A 202 9294 12820 5840 -1105 -32 -984 N
ATOM 935 CA ASN A 202 -27.165 -36.365 -32.058 1.00 73.62 C
ANISOU 935 CA ASN A 202 9145 12898 5931 -1129 -59 -939 C
ATOM 936 C ASN A 202 -27.691 -34.958 -32.331 1.00 80.09 C
ANISOU 936 C ASN A 202 9741 13963 6727 -960 -173 -834 C
ATOM 937 O ASN A 202 -26.883 -34.026 -32.321 1.00 79.27 O
ANISOU 937 O ASN A 202 9662 13775 6682 -754 -179 -702 O
ATOM 938 CB ASN A 202 -26.346 -36.390 -30.752 1.00 73.10 C
ANISOU 938 CB ASN A 202 9180 12562 6031 -1031 26 -861 C
ATOM 939 CG ASN A 202 -27.072 -36.041 -29.464 1.00 81.82 C
ANISOU 939 CG ASN A 202 10152 13706 7229 -1054 18 -818 C
ATOM 940 OD1 ASN A 202 -28.271 -35.771 -29.419 1.00 73.74 O
ANISOU 940 OD1 ASN A 202 8936 12937 6145 -1143 -49 -855 O
ATOM 941 ND2 ASN A 202 -26.345 -36.065 -28.364 1.00 73.59 N
ANISOU 941 ND2 ASN A 202 9199 12441 6321 -966 88 -749 N
ATOM 942 N PRO A 203 -29.022 -34.762 -32.562 1.00 79.77 N
ANISOU 942 N PRO A 203 9496 14236 6578 -1037 -266 -893 N
ATOM 943 CA PRO A 203 -29.517 -33.413 -32.902 1.00 80.68 C
ANISOU 943 CA PRO A 203 9438 14580 6636 -812 -390 -796 C
ATOM 944 C PRO A 203 -29.457 -32.411 -31.750 1.00 86.60 C
ANISOU 944 C PRO A 203 10133 15256 7515 -610 -403 -670 C
ATOM 945 O PRO A 203 -29.496 -31.203 -31.987 1.00 87.44 O
ANISOU 945 O PRO A 203 10208 15428 7587 -375 -491 -559 O
ATOM 946 CB PRO A 203 -30.964 -33.656 -33.360 1.00 84.47 C
ANISOU 946 CB PRO A 203 9695 15454 6944 -944 -481 -924 C
ATOM 947 CG PRO A 203 -31.070 -35.129 -33.602 1.00 89.45 C
ANISOU 947 CG PRO A 203 10425 16042 7519 -1282 -400 -1087 C
ATOM 948 CD PRO A 203 -30.114 -35.755 -32.636 1.00 83.30 C
ANISOU 948 CD PRO A 203 9869 14870 6910 -1331 -267 -1059 C
ATOM 949 N LYS A 204 -29.334 -32.897 -30.514 1.00 83.48 N
ANISOU 949 N LYS A 204 9762 14703 7253 -697 -315 -683 N
ATOM 950 CA LYS A 204 -29.248 -32.028 -29.352 1.00 82.31 C
ANISOU 950 CA LYS A 204 9571 14476 7229 -524 -316 -576 C
ATOM 951 C LYS A 204 -27.828 -31.434 -29.260 1.00 86.22 C
ANISOU 951 C LYS A 204 10252 14680 7826 -372 -268 -440 C
ATOM 952 O LYS A 204 -27.621 -30.416 -28.589 1.00 86.26 O
ANISOU 952 O LYS A 204 10259 14615 7900 -197 -290 -329 O
ATOM 953 CB LYS A 204 -29.631 -32.808 -28.094 1.00 84.56 C
ANISOU 953 CB LYS A 204 9817 14715 7597 -697 -237 -643 C
ATOM 954 CG LYS A 204 -30.293 -31.937 -27.030 1.00107.33 C
ANISOU 954 CG LYS A 204 12534 17717 10531 -553 -278 -594 C
ATOM 955 CD LYS A 204 -30.520 -32.684 -25.711 1.00116.40 C
ANISOU 955 CD LYS A 204 13669 18797 11763 -738 -185 -645 C
ATOM 956 CE LYS A 204 -31.849 -33.401 -25.646 1.00128.50 C
ANISOU 956 CE LYS A 204 15008 20656 13162 -991 -197 -795 C
ATOM 957 NZ LYS A 204 -31.946 -34.267 -24.443 1.00135.27 N
ANISOU 957 NZ LYS A 204 15922 21398 14078 -1227 -89 -839 N
ATOM 958 N SER A 205 -26.861 -32.050 -29.976 1.00 81.84 N
ANISOU 958 N SER A 205 9854 13985 7258 -443 -204 -460 N
ATOM 959 CA SER A 205 -25.462 -31.616 -30.020 1.00 79.60 C
ANISOU 959 CA SER A 205 9714 13500 7029 -340 -148 -359 C
ATOM 960 C SER A 205 -25.191 -30.614 -31.145 1.00 83.25 C
ANISOU 960 C SER A 205 10212 14043 7374 -229 -220 -272 C
ATOM 961 O SER A 205 -24.146 -29.950 -31.112 1.00 80.70 O
ANISOU 961 O SER A 205 9991 13598 7074 -157 -186 -169 O
ATOM 962 CB SER A 205 -24.546 -32.816 -30.201 1.00 81.78 C
ANISOU 962 CB SER A 205 10128 13627 7318 -442 -42 -440 C
ATOM 963 OG SER A 205 -24.736 -33.780 -29.182 1.00 87.43 O
ANISOU 963 OG SER A 205 10879 14221 8119 -542 26 -509 O
ATOM 964 N TRP A 206 -26.127 -30.504 -32.132 1.00 82.03 N
ANISOU 964 N TRP A 206 9980 14111 7076 -230 -320 -314 N
ATOM 965 CA TRP A 206 -25.996 -29.616 -33.297 1.00 83.50 C
ANISOU 965 CA TRP A 206 10225 14384 7116 -128 -402 -234 C
ATOM 966 C TRP A 206 -25.981 -28.140 -32.910 1.00 86.73 C
ANISOU 966 C TRP A 206 10696 14735 7522 68 -471 -78 C
ATOM 967 O TRP A 206 -26.811 -27.687 -32.124 1.00 86.71 O
ANISOU 967 O TRP A 206 10604 14786 7555 181 -531 -66 O
ATOM 968 CB TRP A 206 -27.092 -29.854 -34.361 1.00 84.70 C
ANISOU 968 CB TRP A 206 10267 14814 7100 -155 -505 -321 C
ATOM 969 CG TRP A 206 -27.179 -31.241 -34.946 1.00 86.47 C
ANISOU 969 CG TRP A 206 10474 15100 7280 -371 -451 -482 C
ATOM 970 CD1 TRP A 206 -26.270 -32.254 -34.830 1.00 88.59 C
ANISOU 970 CD1 TRP A 206 10860 15180 7620 -499 -326 -547 C
ATOM 971 CD2 TRP A 206 -28.240 -31.747 -35.762 1.00 88.26 C
ANISOU 971 CD2 TRP A 206 10579 15599 7356 -473 -525 -604 C
ATOM 972 NE1 TRP A 206 -26.727 -33.377 -35.480 1.00 89.34 N
ANISOU 972 NE1 TRP A 206 10952 15370 7622 -680 -316 -704 N
ATOM 973 CE2 TRP A 206 -27.924 -33.087 -36.081 1.00 92.44 C
ANISOU 973 CE2 TRP A 206 11190 16055 7878 -693 -434 -742 C
ATOM 974 CE3 TRP A 206 -29.441 -31.202 -36.244 1.00 91.29 C
ANISOU 974 CE3 TRP A 206 10796 16301 7591 -389 -666 -619 C
ATOM 975 CZ2 TRP A 206 -28.759 -33.885 -36.873 1.00 93.70 C
ANISOU 975 CZ2 TRP A 206 11280 16432 7888 -876 -472 -895 C
ATOM 976 CZ3 TRP A 206 -30.259 -31.989 -37.042 1.00 94.64 C
ANISOU 976 CZ3 TRP A 206 11107 16989 7864 -560 -706 -771 C
ATOM 977 CH2 TRP A 206 -29.927 -33.319 -37.331 1.00 95.40 C
ANISOU 977 CH2 TRP A 206 11296 16989 7961 -825 -606 -908 C
ATOM 978 N TYR A 207 -25.043 -27.403 -33.514 1.00 83.34 N
ANISOU 978 N TYR A 207 10438 14205 7023 98 -462 32 N
ATOM 979 CA TYR A 207 -24.770 -25.984 -33.322 1.00 83.78 C
ANISOU 979 CA TYR A 207 10652 14144 7037 237 -512 190 C
ATOM 980 C TYR A 207 -25.555 -25.133 -34.321 1.00 91.48 C
ANISOU 980 C TYR A 207 11697 15250 7812 392 -661 250 C
ATOM 981 O TYR A 207 -25.463 -25.362 -35.534 1.00 91.31 O
ANISOU 981 O TYR A 207 11705 15337 7650 334 -683 233 O
ATOM 982 CB TYR A 207 -23.255 -25.752 -33.487 1.00 84.14 C
ANISOU 982 CB TYR A 207 10858 14034 7077 121 -408 265 C
ATOM 983 CG TYR A 207 -22.778 -24.343 -33.208 1.00 85.79 C
ANISOU 983 CG TYR A 207 11280 14083 7233 183 -433 425 C
ATOM 984 CD1 TYR A 207 -22.498 -23.927 -31.907 1.00 86.99 C
ANISOU 984 CD1 TYR A 207 11458 14077 7517 209 -392 468 C
ATOM 985 CD2 TYR A 207 -22.532 -23.448 -34.248 1.00 87.13 C
ANISOU 985 CD2 TYR A 207 11660 14243 7203 188 -490 533 C
ATOM 986 CE1 TYR A 207 -22.040 -22.634 -31.643 1.00 88.76 C
ANISOU 986 CE1 TYR A 207 11918 14131 7674 235 -412 606 C
ATOM 987 CE2 TYR A 207 -22.076 -22.154 -33.997 1.00 88.34 C
ANISOU 987 CE2 TYR A 207 12075 14211 7278 207 -509 681 C
ATOM 988 CZ TYR A 207 -21.824 -21.753 -32.693 1.00 96.70 C
ANISOU 988 CZ TYR A 207 13164 15108 8471 223 -469 713 C
ATOM 989 OH TYR A 207 -21.365 -20.484 -32.426 1.00 99.66 O
ANISOU 989 OH TYR A 207 13832 15282 8755 212 -484 849 O
ATOM 990 N GLU A 208 -26.305 -24.128 -33.791 1.00 90.41 N
ANISOU 990 N GLU A 208 11602 15101 7648 614 -766 319 N
ATOM 991 CA GLU A 208 -27.140 -23.147 -34.515 1.00 93.22 C
ANISOU 991 CA GLU A 208 12058 15562 7800 857 -931 388 C
ATOM 992 C GLU A 208 -28.035 -23.823 -35.586 1.00 98.25 C
ANISOU 992 C GLU A 208 12508 16521 8302 858 -1011 277 C
ATOM 993 O GLU A 208 -28.757 -24.772 -35.270 1.00 97.69 O
ANISOU 993 O GLU A 208 12167 16652 8298 784 -997 130 O
ATOM 994 CB GLU A 208 -26.287 -22.014 -35.151 1.00 95.81 C
ANISOU 994 CB GLU A 208 12746 15677 7981 880 -951 560 C
ATOM 995 CG GLU A 208 -25.412 -21.210 -34.192 1.00108.89 C
ANISOU 995 CG GLU A 208 14623 17030 9719 852 -883 672 C
ATOM 996 CD GLU A 208 -26.090 -20.271 -33.212 1.00135.61 C
ANISOU 996 CD GLU A 208 18098 20311 13116 1115 -971 721 C
ATOM 997 OE1 GLU A 208 -26.612 -19.223 -33.657 1.00145.58 O
ANISOU 997 OE1 GLU A 208 19585 21541 14187 1362 -1110 809 O
ATOM 998 OE2 GLU A 208 -26.034 -20.547 -31.992 1.00123.16 O
ANISOU 998 OE2 GLU A 208 16399 18669 11726 1086 -899 676 O
ATOM 999 N ASP A 209 -27.975 -23.338 -36.838 1.00 96.15 N
ANISOU 999 N ASP A 209 12399 16304 7830 915 -1090 347 N
ATOM 1000 CA ASP A 209 -28.758 -23.854 -37.962 1.00 97.30 C
ANISOU 1000 CA ASP A 209 12397 16761 7813 922 -1177 255 C
ATOM 1001 C ASP A 209 -28.007 -24.975 -38.672 1.00 97.87 C
ANISOU 1001 C ASP A 209 12423 16848 7913 622 -1059 169 C
ATOM 1002 O ASP A 209 -28.592 -25.655 -39.524 1.00 99.02 O
ANISOU 1002 O ASP A 209 12424 17248 7950 561 -1103 58 O
ATOM 1003 CB ASP A 209 -29.089 -22.722 -38.956 1.00102.22 C
ANISOU 1003 CB ASP A 209 13240 17425 8174 1166 -1334 381 C
ATOM 1004 CG ASP A 209 -29.290 -21.353 -38.327 1.00119.24 C
ANISOU 1004 CG ASP A 209 15632 19396 10277 1467 -1427 522 C
ATOM 1005 OD1 ASP A 209 -28.728 -20.368 -38.862 1.00121.12 O
ANISOU 1005 OD1 ASP A 209 16235 19418 10367 1531 -1464 684 O
ATOM 1006 OD2 ASP A 209 -29.983 -21.271 -37.273 1.00126.85 O
ANISOU 1006 OD2 ASP A 209 16440 20422 11337 1625 -1457 468 O
ATOM 1007 N VAL A 210 -26.710 -25.173 -38.315 1.00 90.04 N
ANISOU 1007 N VAL A 210 11553 15608 7051 447 -910 209 N
ATOM 1008 CA VAL A 210 -25.842 -26.203 -38.899 1.00 87.31 C
ANISOU 1008 CA VAL A 210 11187 15262 6725 207 -788 124 C
ATOM 1009 C VAL A 210 -26.391 -27.574 -38.523 1.00 89.79 C
ANISOU 1009 C VAL A 210 11270 15694 7152 81 -740 -65 C
ATOM 1010 O VAL A 210 -26.519 -27.924 -37.350 1.00 89.10 O
ANISOU 1010 O VAL A 210 11094 15524 7235 63 -688 -105 O
ATOM 1011 CB VAL A 210 -24.338 -26.054 -38.559 1.00 88.19 C
ANISOU 1011 CB VAL A 210 11450 15142 6917 84 -647 198 C
ATOM 1012 CG1 VAL A 210 -23.506 -27.049 -39.345 1.00 87.31 C
ANISOU 1012 CG1 VAL A 210 11317 15090 6767 -99 -542 101 C
ATOM 1013 CG2 VAL A 210 -23.851 -24.639 -38.837 1.00 88.67 C
ANISOU 1013 CG2 VAL A 210 11774 15073 6845 154 -691 387 C
ATOM 1014 N GLU A 211 -26.805 -28.287 -39.548 1.00 86.74 N
ANISOU 1014 N GLU A 211 10807 15509 6640 -10 -769 -176 N
ATOM 1015 CA GLU A 211 -27.400 -29.606 -39.490 1.00 86.34 C
ANISOU 1015 CA GLU A 211 10591 15590 6626 -178 -736 -366 C
ATOM 1016 C GLU A 211 -26.293 -30.666 -39.533 1.00 87.52 C
ANISOU 1016 C GLU A 211 10830 15567 6855 -359 -581 -449 C
ATOM 1017 O GLU A 211 -25.539 -30.759 -40.519 1.00 88.03 O
ANISOU 1017 O GLU A 211 10996 15636 6813 -402 -549 -448 O
ATOM 1018 CB GLU A 211 -28.421 -29.778 -40.650 1.00 90.23 C
ANISOU 1018 CB GLU A 211 10970 16408 6903 -186 -857 -452 C
ATOM 1019 CG GLU A 211 -28.032 -29.077 -41.956 1.00104.41 C
ANISOU 1019 CG GLU A 211 12906 18259 8505 -106 -920 -357 C
ATOM 1020 CD GLU A 211 -29.096 -28.947 -43.036 1.00126.21 C
ANISOU 1020 CD GLU A 211 15562 21360 11032 -38 -1072 -403 C
ATOM 1021 OE1 GLU A 211 -30.036 -28.137 -42.860 1.00128.96 O
ANISOU 1021 OE1 GLU A 211 15833 21867 11300 183 -1210 -345 O
ATOM 1022 OE2 GLU A 211 -28.941 -29.596 -44.096 1.00108.91 O
ANISOU 1022 OE2 GLU A 211 13379 19285 8718 -180 -1058 -494 O
ATOM 1023 N GLY A 212 -26.176 -31.415 -38.440 1.00 80.07 N
ANISOU 1023 N GLY A 212 9860 14478 6083 -439 -490 -516 N
ATOM 1024 CA GLY A 212 -25.218 -32.503 -38.343 1.00 78.21 C
ANISOU 1024 CA GLY A 212 9728 14074 5916 -559 -353 -607 C
ATOM 1025 C GLY A 212 -23.846 -32.176 -37.804 1.00 79.41 C
ANISOU 1025 C GLY A 212 9985 14020 6168 -487 -253 -513 C
ATOM 1026 O GLY A 212 -23.021 -33.080 -37.714 1.00 79.15 O
ANISOU 1026 O GLY A 212 10030 13876 6170 -535 -147 -596 O
ATOM 1027 N CYS A 213 -23.566 -30.910 -37.452 1.00 74.49 N
ANISOU 1027 N CYS A 213 9380 13354 5571 -368 -286 -349 N
ATOM 1028 CA CYS A 213 -22.276 -30.537 -36.853 1.00 72.35 C
ANISOU 1028 CA CYS A 213 9187 12924 5379 -336 -190 -262 C
ATOM 1029 C CYS A 213 -22.476 -30.041 -35.438 1.00 74.01 C
ANISOU 1029 C CYS A 213 9365 13004 5752 -268 -191 -188 C
ATOM 1030 O CYS A 213 -23.380 -29.251 -35.193 1.00 72.44 O
ANISOU 1030 O CYS A 213 9131 12844 5547 -184 -291 -120 O
ATOM 1031 CB CYS A 213 -21.531 -29.493 -37.675 1.00 73.00 C
ANISOU 1031 CB CYS A 213 9368 13050 5317 -320 -203 -137 C
ATOM 1032 SG CYS A 213 -21.313 -29.913 -39.412 1.00 78.70 S
ANISOU 1032 SG CYS A 213 10127 13955 5819 -397 -208 -209 S
ATOM 1033 N GLY A 214 -21.569 -30.427 -34.556 1.00 71.24 N
ANISOU 1033 N GLY A 214 9032 12514 5520 -277 -84 -199 N
ATOM 1034 CA GLY A 214 -21.547 -29.985 -33.169 1.00 71.28 C
ANISOU 1034 CA GLY A 214 9017 12389 5678 -222 -68 -130 C
ATOM 1035 C GLY A 214 -20.230 -29.330 -32.806 1.00 77.32 C
ANISOU 1035 C GLY A 214 9845 13080 6455 -212 6 -37 C
ATOM 1036 O GLY A 214 -19.215 -29.583 -33.456 1.00 78.03 O
ANISOU 1036 O GLY A 214 9963 13228 6456 -255 74 -63 O
ATOM 1037 N ILE A 215 -20.225 -28.487 -31.771 1.00 73.98 N
ANISOU 1037 N ILE A 215 9434 12555 6121 -164 -5 61 N
ATOM 1038 CA ILE A 215 -18.996 -27.833 -31.323 1.00 74.01 C
ANISOU 1038 CA ILE A 215 9490 12506 6123 -194 66 143 C
ATOM 1039 C ILE A 215 -18.115 -28.880 -30.626 1.00 76.68 C
ANISOU 1039 C ILE A 215 9759 12823 6551 -194 178 52 C
ATOM 1040 O ILE A 215 -18.568 -29.487 -29.656 1.00 75.54 O
ANISOU 1040 O ILE A 215 9572 12587 6544 -148 187 6 O
ATOM 1041 CB ILE A 215 -19.261 -26.575 -30.426 1.00 77.31 C
ANISOU 1041 CB ILE A 215 9978 12806 6592 -149 17 269 C
ATOM 1042 CG1 ILE A 215 -17.960 -26.034 -29.793 1.00 77.84 C
ANISOU 1042 CG1 ILE A 215 10088 12829 6661 -227 104 331 C
ATOM 1043 CG2 ILE A 215 -20.348 -26.801 -29.356 1.00 76.86 C
ANISOU 1043 CG2 ILE A 215 9840 12680 6684 -53 -28 240 C
ATOM 1044 CD1 ILE A 215 -16.942 -25.489 -30.823 1.00 90.62 C
ANISOU 1044 CD1 ILE A 215 11796 14549 8087 -362 142 382 C
ATOM 1045 N GLN A 216 -16.867 -29.089 -31.128 1.00 72.83 N
ANISOU 1045 N GLN A 216 9265 12442 5964 -234 260 22 N
ATOM 1046 CA GLN A 216 -15.888 -30.053 -30.591 1.00 71.87 C
ANISOU 1046 CA GLN A 216 9083 12345 5878 -178 360 -72 C
ATOM 1047 C GLN A 216 -15.750 -29.940 -29.082 1.00 76.33 C
ANISOU 1047 C GLN A 216 9617 12795 6592 -129 385 -37 C
ATOM 1048 O GLN A 216 -15.945 -28.854 -28.530 1.00 76.29 O
ANISOU 1048 O GLN A 216 9631 12731 6624 -171 350 73 O
ATOM 1049 CB GLN A 216 -14.502 -29.898 -31.248 1.00 73.42 C
ANISOU 1049 CB GLN A 216 9239 12744 5912 -222 438 -87 C
ATOM 1050 CG GLN A 216 -13.870 -28.516 -31.100 1.00 72.04 C
ANISOU 1050 CG GLN A 216 9075 12632 5665 -352 451 41 C
ATOM 1051 CD GLN A 216 -12.464 -28.426 -31.635 1.00 79.67 C
ANISOU 1051 CD GLN A 216 9964 13857 6448 -435 542 10 C
ATOM 1052 OE1 GLN A 216 -11.553 -27.975 -30.928 1.00 69.57 O
ANISOU 1052 OE1 GLN A 216 8617 12672 5144 -496 601 37 O
ATOM 1053 NE2 GLN A 216 -12.253 -28.809 -32.896 1.00 69.29 N
ANISOU 1053 NE2 GLN A 216 8645 12701 4984 -457 557 -53 N
ATOM 1054 N CYS A 217 -15.417 -31.056 -28.416 1.00 73.64 N
ANISOU 1054 N CYS A 217 9255 12406 6318 -30 441 -130 N
ATOM 1055 CA CYS A 217 -15.257 -31.088 -26.963 1.00 72.82 C
ANISOU 1055 CA CYS A 217 9126 12199 6345 28 466 -104 C
ATOM 1056 C CYS A 217 -14.157 -30.135 -26.491 1.00 76.26 C
ANISOU 1056 C CYS A 217 9493 12745 6738 -9 508 -31 C
ATOM 1057 O CYS A 217 -14.414 -29.305 -25.624 1.00 76.72 O
ANISOU 1057 O CYS A 217 9555 12719 6878 -48 485 57 O
ATOM 1058 CB CYS A 217 -15.006 -32.501 -26.452 1.00 73.85 C
ANISOU 1058 CB CYS A 217 9295 12251 6513 156 515 -216 C
ATOM 1059 SG CYS A 217 -14.674 -32.562 -24.674 1.00 77.41 S
ANISOU 1059 SG CYS A 217 9722 12599 7093 242 548 -179 S
ATOM 1060 N GLN A 218 -12.937 -30.277 -27.035 1.00 72.29 N
ANISOU 1060 N GLN A 218 8923 12453 6092 -5 574 -78 N
ATOM 1061 CA GLN A 218 -11.765 -29.474 -26.685 1.00 71.46 C
ANISOU 1061 CA GLN A 218 8725 12526 5900 -83 627 -33 C
ATOM 1062 C GLN A 218 -11.966 -28.001 -27.042 1.00 74.60 C
ANISOU 1062 C GLN A 218 9195 12913 6236 -291 590 95 C
ATOM 1063 O GLN A 218 -12.113 -27.681 -28.213 1.00 75.94 O
ANISOU 1063 O GLN A 218 9423 13144 6287 -382 569 115 O
ATOM 1064 CB GLN A 218 -10.526 -30.038 -27.386 1.00 73.85 C
ANISOU 1064 CB GLN A 218 8914 13121 6025 -32 704 -137 C
ATOM 1065 CG GLN A 218 -9.309 -30.108 -26.483 1.00 82.69 C
ANISOU 1065 CG GLN A 218 9883 14439 7097 30 771 -171 C
ATOM 1066 CD GLN A 218 -8.120 -29.384 -27.062 1.00104.11 C
ANISOU 1066 CD GLN A 218 12458 17510 9588 -135 835 -175 C
ATOM 1067 OE1 GLN A 218 -8.231 -28.526 -27.963 1.00 97.40 O
ANISOU 1067 OE1 GLN A 218 11668 16705 8635 -357 826 -107 O
ATOM 1068 NE2 GLN A 218 -6.947 -29.705 -26.530 1.00 97.69 N
ANISOU 1068 NE2 GLN A 218 11460 16980 8676 -38 900 -256 N
ATOM 1069 N ASN A 219 -11.982 -27.122 -26.029 1.00 70.47 N
ANISOU 1069 N ASN A 219 8700 12295 5781 -358 578 182 N
ATOM 1070 CA ASN A 219 -12.193 -25.673 -26.126 1.00 71.14 C
ANISOU 1070 CA ASN A 219 8925 12299 5805 -536 538 309 C
ATOM 1071 C ASN A 219 -11.386 -25.086 -27.285 1.00 78.82 C
ANISOU 1071 C ASN A 219 9929 13472 6547 -732 575 332 C
ATOM 1072 O ASN A 219 -10.160 -25.008 -27.193 1.00 80.78 O
ANISOU 1072 O ASN A 219 10058 13964 6670 -843 660 296 O
ATOM 1073 CB ASN A 219 -11.833 -24.995 -24.799 1.00 70.53 C
ANISOU 1073 CB ASN A 219 8848 12164 5787 -591 556 360 C
ATOM 1074 CG ASN A 219 -12.301 -23.570 -24.654 1.00 85.30 C
ANISOU 1074 CG ASN A 219 10931 13852 7625 -721 498 486 C
ATOM 1075 OD1 ASN A 219 -12.404 -22.804 -25.636 1.00 82.24 O
ANISOU 1075 OD1 ASN A 219 10707 13446 7093 -847 467 554 O
ATOM 1076 ND2 ASN A 219 -12.525 -23.167 -23.403 1.00 65.99 N
ANISOU 1076 ND2 ASN A 219 8514 11264 5293 -690 484 518 N
ATOM 1077 N PRO A 220 -12.053 -24.714 -28.407 1.00 75.99 N
ANISOU 1077 N PRO A 220 9714 13049 6108 -777 514 384 N
ATOM 1078 CA PRO A 220 -11.306 -24.249 -29.586 1.00 76.93 C
ANISOU 1078 CA PRO A 220 9875 13367 5989 -976 554 405 C
ATOM 1079 C PRO A 220 -10.672 -22.863 -29.458 1.00 82.26 C
ANISOU 1079 C PRO A 220 10704 14047 6503 -1254 578 516 C
ATOM 1080 O PRO A 220 -10.086 -22.388 -30.445 1.00 86.68 O
ANISOU 1080 O PRO A 220 11331 14766 6838 -1467 615 546 O
ATOM 1081 CB PRO A 220 -12.367 -24.246 -30.684 1.00 78.75 C
ANISOU 1081 CB PRO A 220 10240 13489 6194 -915 464 437 C
ATOM 1082 CG PRO A 220 -13.628 -24.016 -29.980 1.00 82.28 C
ANISOU 1082 CG PRO A 220 10782 13665 6815 -767 365 489 C
ATOM 1083 CD PRO A 220 -13.504 -24.774 -28.692 1.00 76.69 C
ANISOU 1083 CD PRO A 220 9912 12928 6296 -645 406 415 C
ATOM 1084 N LEU A 221 -10.794 -22.209 -28.286 1.00 74.54 N
ANISOU 1084 N LEU A 221 9808 12894 5621 -1274 560 576 N
ATOM 1085 CA LEU A 221 -10.215 -20.886 -28.043 1.00 73.91 C
ANISOU 1085 CA LEU A 221 9924 12776 5384 -1560 583 676 C
ATOM 1086 C LEU A 221 -8.856 -20.994 -27.369 1.00 76.33 C
ANISOU 1086 C LEU A 221 10016 13372 5614 -1728 698 606 C
ATOM 1087 O LEU A 221 -8.175 -19.982 -27.203 1.00 78.05 O
ANISOU 1087 O LEU A 221 10364 13631 5661 -2033 739 665 O
ATOM 1088 CB LEU A 221 -11.142 -20.049 -27.162 1.00 72.81 C
ANISOU 1088 CB LEU A 221 10020 12280 5366 -1481 494 770 C
ATOM 1089 CG LEU A 221 -12.534 -19.785 -27.672 1.00 76.61 C
ANISOU 1089 CG LEU A 221 10706 12504 5899 -1286 367 837 C
ATOM 1090 CD1 LEU A 221 -13.481 -19.605 -26.505 1.00 75.69 C
ANISOU 1090 CD1 LEU A 221 10637 12144 5978 -1077 296 854 C
ATOM 1091 CD2 LEU A 221 -12.567 -18.573 -28.592 1.00 78.67 C
ANISOU 1091 CD2 LEU A 221 11327 12644 5921 -1469 323 964 C
ATOM 1092 N PHE A 222 -8.468 -22.206 -26.947 1.00 69.84 N
ANISOU 1092 N PHE A 222 8886 12752 4898 -1530 745 477 N
ATOM 1093 CA PHE A 222 -7.215 -22.386 -26.236 1.00 69.59 C
ANISOU 1093 CA PHE A 222 8617 13036 4787 -1623 841 397 C
ATOM 1094 C PHE A 222 -6.354 -23.519 -26.822 1.00 76.11 C
ANISOU 1094 C PHE A 222 9148 14256 5514 -1509 915 253 C
ATOM 1095 O PHE A 222 -6.852 -24.599 -27.147 1.00 74.40 O
ANISOU 1095 O PHE A 222 8869 13987 5414 -1227 887 183 O
ATOM 1096 CB PHE A 222 -7.499 -22.595 -24.746 1.00 68.58 C
ANISOU 1096 CB PHE A 222 8433 12753 4871 -1454 818 387 C
ATOM 1097 CG PHE A 222 -8.086 -21.353 -24.102 1.00 68.66 C
ANISOU 1097 CG PHE A 222 8719 12444 4924 -1594 763 510 C
ATOM 1098 CD1 PHE A 222 -7.265 -20.301 -23.698 1.00 71.57 C
ANISOU 1098 CD1 PHE A 222 9166 12902 5124 -1920 813 550 C
ATOM 1099 CD2 PHE A 222 -9.463 -21.223 -23.922 1.00 68.12 C
ANISOU 1099 CD2 PHE A 222 8843 12004 5037 -1405 662 577 C
ATOM 1100 CE1 PHE A 222 -7.813 -19.144 -23.122 1.00 71.76 C
ANISOU 1100 CE1 PHE A 222 9502 12596 5168 -2036 759 657 C
ATOM 1101 CE2 PHE A 222 -10.008 -20.065 -23.345 1.00 69.62 C
ANISOU 1101 CE2 PHE A 222 9305 11905 5243 -1487 606 679 C
ATOM 1102 CZ PHE A 222 -9.177 -19.044 -22.933 1.00 68.47 C
ANISOU 1102 CZ PHE A 222 9277 11800 4937 -1791 654 719 C
ATOM 1103 N THR A 223 -5.049 -23.240 -26.965 1.00 76.68 N
ANISOU 1103 N THR A 223 9049 14742 5344 -1743 1010 200 N
ATOM 1104 CA THR A 223 -4.063 -24.155 -27.547 1.00 78.82 C
ANISOU 1104 CA THR A 223 9020 15472 5456 -1648 1089 51 C
ATOM 1105 C THR A 223 -3.779 -25.319 -26.602 1.00 85.60 C
ANISOU 1105 C THR A 223 9645 16432 6448 -1280 1096 -71 C
ATOM 1106 O THR A 223 -4.072 -25.241 -25.410 1.00 84.32 O
ANISOU 1106 O THR A 223 9518 16061 6459 -1192 1061 -34 O
ATOM 1107 CB THR A 223 -2.761 -23.415 -27.956 1.00 84.64 C
ANISOU 1107 CB THR A 223 9623 16677 5857 -2040 1192 26 C
ATOM 1108 OG1 THR A 223 -2.015 -23.027 -26.797 1.00 83.86 O
ANISOU 1108 OG1 THR A 223 9382 16766 5715 -2168 1234 3 O
ATOM 1109 CG2 THR A 223 -3.021 -22.205 -28.871 1.00 81.37 C
ANISOU 1109 CG2 THR A 223 9517 16117 5283 -2437 1184 164 C
ATOM 1110 N GLU A 224 -3.206 -26.396 -27.159 1.00 86.06 N
ANISOU 1110 N GLU A 224 9490 16801 6407 -1050 1139 -215 N
ATOM 1111 CA GLU A 224 -2.828 -27.638 -26.488 1.00 86.87 C
ANISOU 1111 CA GLU A 224 9408 17025 6575 -649 1145 -347 C
ATOM 1112 C GLU A 224 -1.741 -27.392 -25.451 1.00 91.58 C
ANISOU 1112 C GLU A 224 9756 17982 7057 -693 1197 -398 C
ATOM 1113 O GLU A 224 -1.639 -28.149 -24.488 1.00 92.12 O
ANISOU 1113 O GLU A 224 9741 18037 7226 -381 1179 -458 O
ATOM 1114 CB GLU A 224 -2.342 -28.658 -27.539 1.00 90.76 C
ANISOU 1114 CB GLU A 224 9770 17797 6917 -421 1182 -495 C
ATOM 1115 CG GLU A 224 -2.408 -30.106 -27.083 1.00108.30 C
ANISOU 1115 CG GLU A 224 11969 19934 9245 61 1156 -613 C
ATOM 1116 CD GLU A 224 -3.814 -30.660 -26.985 1.00137.20 C
ANISOU 1116 CD GLU A 224 15922 23031 13177 213 1073 -553 C
ATOM 1117 OE1 GLU A 224 -4.327 -31.145 -28.020 1.00136.50 O
ANISOU 1117 OE1 GLU A 224 15952 22828 13084 271 1056 -587 O
ATOM 1118 OE2 GLU A 224 -4.411 -30.583 -25.884 1.00130.27 O
ANISOU 1118 OE2 GLU A 224 15145 21851 12501 251 1028 -477 O
ATOM 1119 N ALA A 225 -0.936 -26.333 -25.650 1.00 88.71 N
ANISOU 1119 N ALA A 225 9293 17946 6466 -1098 1260 -375 N
ATOM 1120 CA ALA A 225 0.140 -25.914 -24.755 1.00 89.66 C
ANISOU 1120 CA ALA A 225 9166 18470 6431 -1244 1316 -424 C
ATOM 1121 C ALA A 225 -0.424 -25.224 -23.513 1.00 90.79 C
ANISOU 1121 C ALA A 225 9483 18239 6772 -1349 1265 -305 C
ATOM 1122 O ALA A 225 0.144 -25.359 -22.432 1.00 90.32 O
ANISOU 1122 O ALA A 225 9242 18368 6706 -1254 1275 -358 O
ATOM 1123 CB ALA A 225 1.086 -24.977 -25.488 1.00 93.18 C
ANISOU 1123 CB ALA A 225 9490 19371 6544 -1718 1406 -437 C
ATOM 1124 N GLU A 226 -1.531 -24.476 -23.691 1.00 85.10 N
ANISOU 1124 N GLU A 226 9113 17012 6208 -1525 1208 -153 N
ATOM 1125 CA GLU A 226 -2.259 -23.724 -22.667 1.00 83.13 C
ANISOU 1125 CA GLU A 226 9089 16349 6146 -1620 1152 -33 C
ATOM 1126 C GLU A 226 -3.197 -24.626 -21.858 1.00 85.97 C
ANISOU 1126 C GLU A 226 9512 16343 6811 -1208 1077 -28 C
ATOM 1127 O GLU A 226 -3.394 -24.383 -20.659 1.00 84.99 O
ANISOU 1127 O GLU A 226 9425 16057 6813 -1187 1051 11 O
ATOM 1128 CB GLU A 226 -3.064 -22.611 -23.323 1.00 83.94 C
ANISOU 1128 CB GLU A 226 9551 16091 6252 -1914 1114 114 C
ATOM 1129 CG GLU A 226 -2.210 -21.506 -23.896 1.00 91.74 C
ANISOU 1129 CG GLU A 226 10573 17354 6930 -2403 1186 140 C
ATOM 1130 CD GLU A 226 -2.994 -20.613 -24.828 1.00102.16 C
ANISOU 1130 CD GLU A 226 12280 18322 8215 -2623 1143 278 C
ATOM 1131 OE1 GLU A 226 -3.737 -21.149 -25.683 1.00 90.27 O
ANISOU 1131 OE1 GLU A 226 10852 16647 6800 -2410 1095 293 O
ATOM 1132 OE2 GLU A 226 -2.890 -19.374 -24.684 1.00 89.39 O
ANISOU 1132 OE2 GLU A 226 10915 16583 6467 -3001 1151 373 O
ATOM 1133 N HIS A 227 -3.809 -25.637 -22.530 1.00 81.37 N
ANISOU 1133 N HIS A 227 8964 15621 6330 -915 1045 -66 N
ATOM 1134 CA HIS A 227 -4.637 -26.662 -21.895 1.00 79.18 C
ANISOU 1134 CA HIS A 227 8751 15038 6297 -550 988 -81 C
ATOM 1135 C HIS A 227 -3.738 -27.394 -20.913 1.00 84.95 C
ANISOU 1135 C HIS A 227 9252 16036 6989 -318 1018 -181 C
ATOM 1136 O HIS A 227 -3.985 -27.366 -19.702 1.00 83.44 O
ANISOU 1136 O HIS A 227 9089 15678 6935 -243 991 -145 O
ATOM 1137 CB HIS A 227 -5.203 -27.645 -22.939 1.00 79.59 C
ANISOU 1137 CB HIS A 227 8872 14982 6387 -338 966 -132 C
ATOM 1138 CG HIS A 227 -6.559 -27.314 -23.465 1.00 81.47 C
ANISOU 1138 CG HIS A 227 9365 14821 6771 -409 897 -33 C
ATOM 1139 ND1 HIS A 227 -6.729 -26.418 -24.508 1.00 84.05 N
ANISOU 1139 ND1 HIS A 227 9800 15149 6985 -667 891 36 N
ATOM 1140 CD2 HIS A 227 -7.760 -27.836 -23.136 1.00 81.70 C
ANISOU 1140 CD2 HIS A 227 9542 14484 7015 -244 831 -4 C
ATOM 1141 CE1 HIS A 227 -8.028 -26.393 -24.754 1.00 82.22 C
ANISOU 1141 CE1 HIS A 227 9768 14563 6908 -617 814 103 C
ATOM 1142 NE2 HIS A 227 -8.690 -27.232 -23.957 1.00 81.25 N
ANISOU 1142 NE2 HIS A 227 9658 14231 6981 -379 779 76 N
ATOM 1143 N GLN A 228 -2.608 -27.936 -21.441 1.00 84.04 N
ANISOU 1143 N GLN A 228 8893 16387 6651 -218 1077 -310 N
ATOM 1144 CA GLN A 228 -1.592 -28.650 -20.668 1.00 85.09 C
ANISOU 1144 CA GLN A 228 8774 16879 6677 47 1104 -427 C
ATOM 1145 C GLN A 228 -0.977 -27.783 -19.554 1.00 87.16 C
ANISOU 1145 C GLN A 228 8896 17341 6879 -164 1124 -400 C
ATOM 1146 O GLN A 228 -0.562 -28.337 -18.534 1.00 87.20 O
ANISOU 1146 O GLN A 228 8774 17469 6890 90 1113 -454 O
ATOM 1147 CB GLN A 228 -0.494 -29.223 -21.582 1.00 89.27 C
ANISOU 1147 CB GLN A 228 9051 17933 6933 175 1163 -579 C
ATOM 1148 CG GLN A 228 -0.784 -30.668 -22.010 1.00115.24 C
ANISOU 1148 CG GLN A 228 12429 21083 10272 629 1135 -671 C
ATOM 1149 CD GLN A 228 -1.096 -31.595 -20.840 1.00144.86 C
ANISOU 1149 CD GLN A 228 16284 24576 14182 1007 1083 -680 C
ATOM 1150 OE1 GLN A 228 -2.254 -31.989 -20.615 1.00141.17 O
ANISOU 1150 OE1 GLN A 228 16099 23588 13950 1079 1029 -605 O
ATOM 1151 NE2 GLN A 228 -0.082 -31.928 -20.043 1.00137.80 N
ANISOU 1151 NE2 GLN A 228 15160 24055 13141 1234 1097 -770 N
ATOM 1152 N ASP A 229 -0.948 -26.441 -19.741 1.00 82.01 N
ANISOU 1152 N ASP A 229 8302 16702 6156 -626 1148 -315 N
ATOM 1153 CA ASP A 229 -0.449 -25.491 -18.751 1.00 81.75 C
ANISOU 1153 CA ASP A 229 8194 16811 6054 -904 1169 -285 C
ATOM 1154 C ASP A 229 -1.464 -25.380 -17.584 1.00 83.34 C
ANISOU 1154 C ASP A 229 8616 16512 6538 -807 1100 -184 C
ATOM 1155 O ASP A 229 -1.069 -25.433 -16.410 1.00 82.35 O
ANISOU 1155 O ASP A 229 8370 16500 6421 -732 1097 -209 O
ATOM 1156 CB ASP A 229 -0.161 -24.118 -19.376 1.00 84.21 C
ANISOU 1156 CB ASP A 229 8587 17227 6182 -1443 1216 -224 C
ATOM 1157 CG ASP A 229 0.499 -23.170 -18.396 1.00 93.39 C
ANISOU 1157 CG ASP A 229 9675 18586 7223 -1772 1248 -216 C
ATOM 1158 OD1 ASP A 229 1.749 -23.193 -18.293 1.00 95.79 O
ANISOU 1158 OD1 ASP A 229 9645 19488 7261 -1882 1314 -333 O
ATOM 1159 OD2 ASP A 229 -0.233 -22.477 -17.663 1.00 96.45 O
ANISOU 1159 OD2 ASP A 229 10320 18553 7773 -1892 1203 -108 O
ATOM 1160 N MET A 230 -2.764 -25.260 -17.910 1.00 77.98 N
ANISOU 1160 N MET A 230 8238 15319 6072 -793 1044 -81 N
ATOM 1161 CA MET A 230 -3.803 -25.191 -16.881 1.00 75.72 C
ANISOU 1161 CA MET A 230 8142 14590 6038 -691 982 3 C
ATOM 1162 C MET A 230 -3.879 -26.467 -16.081 1.00 77.91 C
ANISOU 1162 C MET A 230 8336 14834 6434 -284 959 -56 C
ATOM 1163 O MET A 230 -4.039 -26.414 -14.862 1.00 77.35 O
ANISOU 1163 O MET A 230 8273 14655 6462 -224 939 -31 O
ATOM 1164 CB MET A 230 -5.182 -24.908 -17.483 1.00 76.29 C
ANISOU 1164 CB MET A 230 8508 14199 6280 -721 924 103 C
ATOM 1165 CG MET A 230 -5.600 -23.492 -17.328 1.00 79.44 C
ANISOU 1165 CG MET A 230 9121 14385 6679 -1034 903 209 C
ATOM 1166 SD MET A 230 -5.607 -22.916 -15.627 1.00 82.20 S
ANISOU 1166 SD MET A 230 9487 14631 7114 -1080 892 238 S
ATOM 1167 CE MET A 230 -6.470 -21.379 -15.877 1.00 78.87 C
ANISOU 1167 CE MET A 230 9436 13829 6702 -1361 846 365 C
ATOM 1168 N HIS A 231 -3.758 -27.615 -16.771 1.00 72.64 N
ANISOU 1168 N HIS A 231 7616 14245 5737 -6 963 -136 N
ATOM 1169 CA HIS A 231 -3.845 -28.925 -16.151 1.00 70.80 C
ANISOU 1169 CA HIS A 231 7381 13933 5585 395 939 -192 C
ATOM 1170 C HIS A 231 -2.743 -29.069 -15.095 1.00 75.46 C
ANISOU 1170 C HIS A 231 7742 14880 6050 516 960 -256 C
ATOM 1171 O HIS A 231 -3.053 -29.402 -13.943 1.00 72.35 O
ANISOU 1171 O HIS A 231 7410 14303 5775 670 928 -226 O
ATOM 1172 CB HIS A 231 -3.820 -30.023 -17.220 1.00 71.50 C
ANISOU 1172 CB HIS A 231 7492 14057 5616 643 944 -278 C
ATOM 1173 CG HIS A 231 -4.971 -29.931 -18.190 1.00 72.99 C
ANISOU 1173 CG HIS A 231 7901 13903 5928 528 916 -219 C
ATOM 1174 ND1 HIS A 231 -4.956 -30.613 -19.395 1.00 75.24 N
ANISOU 1174 ND1 HIS A 231 8209 14246 6133 634 926 -291 N
ATOM 1175 CD2 HIS A 231 -6.115 -29.207 -18.118 1.00 72.03 C
ANISOU 1175 CD2 HIS A 231 7965 13426 5978 330 875 -106 C
ATOM 1176 CE1 HIS A 231 -6.097 -30.310 -19.992 1.00 72.76 C
ANISOU 1176 CE1 HIS A 231 8088 13610 5948 488 890 -216 C
ATOM 1177 NE2 HIS A 231 -6.818 -29.460 -19.270 1.00 71.43 N
ANISOU 1177 NE2 HIS A 231 8015 13201 5926 315 857 -106 N
ATOM 1178 N SER A 232 -1.496 -28.675 -15.448 1.00 75.12 N
ANISOU 1178 N SER A 232 7427 15366 5751 396 1013 -338 N
ATOM 1179 CA SER A 232 -0.345 -28.682 -14.534 1.00 76.28 C
ANISOU 1179 CA SER A 232 7294 15964 5723 473 1033 -416 C
ATOM 1180 C SER A 232 -0.594 -27.812 -13.281 1.00 79.00 C
ANISOU 1180 C SER A 232 7686 16160 6169 254 1017 -330 C
ATOM 1181 O SER A 232 -0.383 -28.286 -12.160 1.00 78.11 O
ANISOU 1181 O SER A 232 7514 16083 6080 488 991 -349 O
ATOM 1182 CB SER A 232 0.911 -28.218 -15.256 1.00 79.67 C
ANISOU 1182 CB SER A 232 7416 17012 5843 271 1101 -517 C
ATOM 1183 OG SER A 232 1.358 -29.302 -16.046 1.00 88.81 O
ANISOU 1183 OG SER A 232 8469 18398 6877 621 1110 -633 O
ATOM 1184 N TYR A 233 -1.075 -26.563 -13.491 1.00 74.34 N
ANISOU 1184 N TYR A 233 7239 15378 5628 -172 1027 -237 N
ATOM 1185 CA TYR A 233 -1.377 -25.566 -12.466 1.00 72.70 C
ANISOU 1185 CA TYR A 233 7131 14992 5502 -424 1014 -158 C
ATOM 1186 C TYR A 233 -2.418 -26.115 -11.496 1.00 72.65 C
ANISOU 1186 C TYR A 233 7306 14540 5756 -159 955 -94 C
ATOM 1187 O TYR A 233 -2.177 -26.117 -10.288 1.00 73.18 O
ANISOU 1187 O TYR A 233 7303 14668 5836 -94 944 -99 O
ATOM 1188 CB TYR A 233 -1.862 -24.275 -13.140 1.00 74.06 C
ANISOU 1188 CB TYR A 233 7523 14940 5678 -849 1024 -67 C
ATOM 1189 CG TYR A 233 -1.995 -23.088 -12.214 1.00 76.40 C
ANISOU 1189 CG TYR A 233 7940 15101 5987 -1156 1019 -4 C
ATOM 1190 CD1 TYR A 233 -0.903 -22.271 -11.936 1.00 80.27 C
ANISOU 1190 CD1 TYR A 233 8273 15994 6231 -1501 1073 -54 C
ATOM 1191 CD2 TYR A 233 -3.227 -22.747 -11.655 1.00 75.24 C
ANISOU 1191 CD2 TYR A 233 8072 14441 6076 -1119 964 95 C
ATOM 1192 CE1 TYR A 233 -1.024 -21.155 -11.110 1.00 81.22 C
ANISOU 1192 CE1 TYR A 233 8550 15963 6346 -1806 1070 -4 C
ATOM 1193 CE2 TYR A 233 -3.359 -21.637 -10.820 1.00 76.52 C
ANISOU 1193 CE2 TYR A 233 8375 14464 6236 -1378 958 142 C
ATOM 1194 CZ TYR A 233 -2.256 -20.834 -10.564 1.00 88.16 C
ANISOU 1194 CZ TYR A 233 9733 16297 7469 -1728 1011 95 C
ATOM 1195 OH TYR A 233 -2.365 -19.728 -9.758 1.00 92.29 O
ANISOU 1195 OH TYR A 233 10432 16664 7969 -2006 1007 133 O
ATOM 1196 N ILE A 234 -3.526 -26.654 -12.029 1.00 65.53 N
ANISOU 1196 N ILE A 234 6620 13239 5039 -7 920 -45 N
ATOM 1197 CA ILE A 234 -4.594 -27.272 -11.250 1.00 62.66 C
ANISOU 1197 CA ILE A 234 6435 12470 4902 214 872 8 C
ATOM 1198 C ILE A 234 -4.067 -28.519 -10.531 1.00 66.48 C
ANISOU 1198 C ILE A 234 6818 13095 5348 590 865 -60 C
ATOM 1199 O ILE A 234 -4.361 -28.654 -9.361 1.00 66.71 O
ANISOU 1199 O ILE A 234 6895 12984 5469 679 843 -26 O
ATOM 1200 CB ILE A 234 -5.838 -27.578 -12.116 1.00 64.27 C
ANISOU 1200 CB ILE A 234 6863 12295 5264 248 842 56 C
ATOM 1201 CG1 ILE A 234 -6.521 -26.253 -12.586 1.00 62.72 C
ANISOU 1201 CG1 ILE A 234 6815 11902 5114 -75 828 141 C
ATOM 1202 CG2 ILE A 234 -6.816 -28.520 -11.363 1.00 64.45 C
ANISOU 1202 CG2 ILE A 234 7036 11981 5471 492 805 80 C
ATOM 1203 CD1 ILE A 234 -7.744 -26.380 -13.548 1.00 59.45 C
ANISOU 1203 CD1 ILE A 234 6594 11173 4822 -62 790 186 C
ATOM 1204 N ALA A 235 -3.282 -29.400 -11.188 1.00 64.41 N
ANISOU 1204 N ALA A 235 6430 13110 4932 824 882 -157 N
ATOM 1205 CA ALA A 235 -2.712 -30.603 -10.543 1.00 64.95 C
ANISOU 1205 CA ALA A 235 6440 13316 4921 1239 865 -227 C
ATOM 1206 C ALA A 235 -1.835 -30.231 -9.362 1.00 69.67 C
ANISOU 1206 C ALA A 235 6827 14241 5406 1244 867 -250 C
ATOM 1207 O ALA A 235 -2.040 -30.764 -8.274 1.00 68.97 O
ANISOU 1207 O ALA A 235 6820 14004 5381 1460 834 -225 O
ATOM 1208 CB ALA A 235 -1.906 -31.425 -11.537 1.00 67.51 C
ANISOU 1208 CB ALA A 235 6647 13950 5053 1485 883 -345 C
ATOM 1209 N ALA A 236 -0.878 -29.301 -9.560 1.00 67.84 N
ANISOU 1209 N ALA A 236 6332 14454 4989 976 907 -297 N
ATOM 1210 CA ALA A 236 0.025 -28.863 -8.496 1.00 69.04 C
ANISOU 1210 CA ALA A 236 6249 14986 4999 923 912 -335 C
ATOM 1211 C ALA A 236 -0.771 -28.280 -7.313 1.00 72.71 C
ANISOU 1211 C ALA A 236 6883 15089 5656 769 886 -231 C
ATOM 1212 O ALA A 236 -0.646 -28.780 -6.197 1.00 71.87 O
ANISOU 1212 O ALA A 236 6755 14997 5555 1001 855 -232 O
ATOM 1213 CB ALA A 236 1.027 -27.844 -9.032 1.00 71.33 C
ANISOU 1213 CB ALA A 236 6268 15783 5052 550 969 -401 C
ATOM 1214 N PHE A 237 -1.649 -27.292 -7.588 1.00 68.99 N
ANISOU 1214 N PHE A 237 6603 14275 5335 420 894 -141 N
ATOM 1215 CA PHE A 237 -2.460 -26.615 -6.584 1.00 67.80 C
ANISOU 1215 CA PHE A 237 6621 13788 5353 267 872 -53 C
ATOM 1216 C PHE A 237 -3.511 -27.525 -5.950 1.00 69.37 C
ANISOU 1216 C PHE A 237 7025 13570 5763 559 830 5 C
ATOM 1217 O PHE A 237 -3.704 -27.443 -4.743 1.00 69.22 O
ANISOU 1217 O PHE A 237 7034 13464 5804 592 812 36 O
ATOM 1218 CB PHE A 237 -3.116 -25.359 -7.172 1.00 69.43 C
ANISOU 1218 CB PHE A 237 7005 13744 5630 -123 883 16 C
ATOM 1219 CG PHE A 237 -2.393 -24.074 -6.821 1.00 73.02 C
ANISOU 1219 CG PHE A 237 7377 14442 5926 -511 914 1 C
ATOM 1220 CD1 PHE A 237 -2.366 -23.605 -5.508 1.00 76.33 C
ANISOU 1220 CD1 PHE A 237 7795 14843 6364 -580 903 12 C
ATOM 1221 CD2 PHE A 237 -1.776 -23.313 -7.805 1.00 76.36 C
ANISOU 1221 CD2 PHE A 237 7751 15097 6166 -838 958 -25 C
ATOM 1222 CE1 PHE A 237 -1.709 -22.413 -5.187 1.00 78.87 C
ANISOU 1222 CE1 PHE A 237 8074 15371 6521 -973 934 -12 C
ATOM 1223 CE2 PHE A 237 -1.128 -22.116 -7.484 1.00 80.85 C
ANISOU 1223 CE2 PHE A 237 8291 15866 6562 -1252 992 -41 C
ATOM 1224 CZ PHE A 237 -1.102 -21.673 -6.180 1.00 79.28 C
ANISOU 1224 CZ PHE A 237 8102 15638 6384 -1320 979 -38 C
ATOM 1225 N GLY A 238 -4.165 -28.368 -6.747 1.00 65.04 N
ANISOU 1225 N GLY A 238 6623 12783 5305 738 818 15 N
ATOM 1226 CA GLY A 238 -5.170 -29.322 -6.286 1.00 63.86 C
ANISOU 1226 CA GLY A 238 6691 12250 5323 969 787 61 C
ATOM 1227 C GLY A 238 -4.577 -30.333 -5.320 1.00 71.53 C
ANISOU 1227 C GLY A 238 7623 13346 6210 1305 770 28 C
ATOM 1228 O GLY A 238 -5.167 -30.620 -4.272 1.00 71.63 O
ANISOU 1228 O GLY A 238 7765 13125 6324 1379 750 82 O
ATOM 1229 N ALA A 239 -3.374 -30.844 -5.647 1.00 69.65 N
ANISOU 1229 N ALA A 239 7198 13504 5761 1520 775 -65 N
ATOM 1230 CA ALA A 239 -2.656 -31.826 -4.848 1.00 70.58 C
ANISOU 1230 CA ALA A 239 7275 13797 5746 1908 748 -110 C
ATOM 1231 C ALA A 239 -2.172 -31.222 -3.533 1.00 74.05 C
ANISOU 1231 C ALA A 239 7551 14455 6128 1839 739 -100 C
ATOM 1232 O ALA A 239 -2.217 -31.911 -2.515 1.00 73.80 O
ANISOU 1232 O ALA A 239 7612 14341 6088 2097 705 -77 O
ATOM 1233 CB ALA A 239 -1.484 -32.384 -5.640 1.00 73.87 C
ANISOU 1233 CB ALA A 239 7500 14641 5924 2167 753 -230 C
ATOM 1234 N VAL A 240 -1.731 -29.939 -3.545 1.00 70.63 N
ANISOU 1234 N VAL A 240 6909 14283 5642 1473 768 -114 N
ATOM 1235 CA VAL A 240 -1.264 -29.251 -2.334 1.00 71.11 C
ANISOU 1235 CA VAL A 240 6819 14564 5638 1347 763 -116 C
ATOM 1236 C VAL A 240 -2.455 -29.082 -1.388 1.00 72.34 C
ANISOU 1236 C VAL A 240 7224 14243 6020 1275 746 -9 C
ATOM 1237 O VAL A 240 -2.419 -29.641 -0.294 1.00 70.17 O
ANISOU 1237 O VAL A 240 6986 13944 5734 1501 717 9 O
ATOM 1238 CB VAL A 240 -0.520 -27.909 -2.591 1.00 76.04 C
ANISOU 1238 CB VAL A 240 7206 15565 6121 927 804 -165 C
ATOM 1239 CG1 VAL A 240 -0.241 -27.172 -1.269 1.00 75.97 C
ANISOU 1239 CG1 VAL A 240 7108 15686 6072 754 798 -159 C
ATOM 1240 CG2 VAL A 240 0.784 -28.141 -3.360 1.00 78.35 C
ANISOU 1240 CG2 VAL A 240 7185 16447 6136 1010 826 -289 C
ATOM 1241 N THR A 241 -3.526 -28.379 -1.849 1.00 68.83 N
ANISOU 1241 N THR A 241 6957 13430 5763 994 762 57 N
ATOM 1242 CA THR A 241 -4.782 -28.157 -1.114 1.00 67.10 C
ANISOU 1242 CA THR A 241 6961 12781 5754 915 750 145 C
ATOM 1243 C THR A 241 -5.291 -29.501 -0.591 1.00 73.55 C
ANISOU 1243 C THR A 241 7946 13364 6634 1243 726 178 C
ATOM 1244 O THR A 241 -5.516 -29.623 0.612 1.00 74.59 O
ANISOU 1244 O THR A 241 8131 13410 6798 1301 713 215 O
ATOM 1245 CB THR A 241 -5.829 -27.457 -1.999 1.00 65.72 C
ANISOU 1245 CB THR A 241 6944 12294 5732 671 760 191 C
ATOM 1246 OG1 THR A 241 -5.182 -26.441 -2.757 1.00 63.91 O
ANISOU 1246 OG1 THR A 241 6601 12289 5391 403 783 157 O
ATOM 1247 CG2 THR A 241 -6.990 -26.850 -1.188 1.00 56.58 C
ANISOU 1247 CG2 THR A 241 5947 10808 4743 542 749 258 C
ATOM 1248 N GLY A 242 -5.373 -30.500 -1.480 1.00 69.88 N
ANISOU 1248 N GLY A 242 7579 12816 6158 1447 722 160 N
ATOM 1249 CA GLY A 242 -5.772 -31.864 -1.164 1.00 69.64 C
ANISOU 1249 CA GLY A 242 7770 12546 6145 1748 701 183 C
ATOM 1250 C GLY A 242 -5.043 -32.445 0.030 1.00 75.26 C
ANISOU 1250 C GLY A 242 8450 13423 6721 2020 674 177 C
ATOM 1251 O GLY A 242 -5.688 -32.803 1.016 1.00 75.31 O
ANISOU 1251 O GLY A 242 8633 13183 6798 2060 664 242 O
ATOM 1252 N LEU A 243 -3.699 -32.472 -0.008 1.00 73.27 N
ANISOU 1252 N LEU A 243 7956 13626 6257 2196 661 96 N
ATOM 1253 CA LEU A 243 -2.894 -33.046 1.083 1.00 75.05 C
ANISOU 1253 CA LEU A 243 8125 14080 6313 2511 622 79 C
ATOM 1254 C LEU A 243 -2.874 -32.205 2.359 1.00 79.39 C
ANISOU 1254 C LEU A 243 8560 14724 6882 2326 619 114 C
ATOM 1255 O LEU A 243 -2.807 -32.780 3.446 1.00 79.98 O
ANISOU 1255 O LEU A 243 8731 14755 6902 2547 587 149 O
ATOM 1256 CB LEU A 243 -1.454 -33.293 0.642 1.00 77.52 C
ANISOU 1256 CB LEU A 243 8161 14931 6362 2767 605 -38 C
ATOM 1257 CG LEU A 243 -1.235 -34.250 -0.519 1.00 82.87 C
ANISOU 1257 CG LEU A 243 8939 15589 6959 3054 599 -97 C
ATOM 1258 CD1 LEU A 243 0.201 -34.237 -0.925 1.00 85.65 C
ANISOU 1258 CD1 LEU A 243 8939 16568 7037 3252 591 -228 C
ATOM 1259 CD2 LEU A 243 -1.683 -35.664 -0.182 1.00 85.38 C
ANISOU 1259 CD2 LEU A 243 9648 15523 7268 3445 559 -53 C
ATOM 1260 N CYS A 244 -2.910 -30.865 2.232 1.00 75.64 N
ANISOU 1260 N CYS A 244 7911 14365 6464 1930 652 103 N
ATOM 1261 CA CYS A 244 -2.896 -29.923 3.356 1.00 75.56 C
ANISOU 1261 CA CYS A 244 7807 14436 6467 1710 654 122 C
ATOM 1262 C CYS A 244 -4.170 -30.023 4.175 1.00 78.36 C
ANISOU 1262 C CYS A 244 8425 14329 7018 1657 655 219 C
ATOM 1263 O CYS A 244 -4.108 -30.049 5.413 1.00 79.53 O
ANISOU 1263 O CYS A 244 8578 14506 7134 1718 637 244 O
ATOM 1264 CB CYS A 244 -2.677 -28.495 2.869 1.00 76.01 C
ANISOU 1264 CB CYS A 244 7695 14666 6518 1291 690 83 C
ATOM 1265 SG CYS A 244 -1.006 -28.172 2.250 1.00 83.11 S
ANISOU 1265 SG CYS A 244 8214 16242 7122 1259 701 -47 S
ATOM 1266 N THR A 245 -5.318 -30.058 3.483 1.00 71.95 N
ANISOU 1266 N THR A 245 7815 13130 6392 1537 675 266 N
ATOM 1267 CA THR A 245 -6.642 -30.138 4.092 1.00 69.35 C
ANISOU 1267 CA THR A 245 7711 12400 6239 1458 684 344 C
ATOM 1268 C THR A 245 -6.894 -31.588 4.565 1.00 72.14 C
ANISOU 1268 C THR A 245 8289 12563 6560 1758 666 388 C
ATOM 1269 O THR A 245 -7.628 -31.778 5.529 1.00 70.36 O
ANISOU 1269 O THR A 245 8210 12126 6399 1733 671 447 O
ATOM 1270 CB THR A 245 -7.731 -29.585 3.127 1.00 70.94 C
ANISOU 1270 CB THR A 245 8009 12332 6614 1221 707 363 C
ATOM 1271 OG1 THR A 245 -7.771 -30.381 1.943 1.00 68.36 O
ANISOU 1271 OG1 THR A 245 7760 11933 6282 1340 707 347 O
ATOM 1272 CG2 THR A 245 -7.497 -28.108 2.742 1.00 64.48 C
ANISOU 1272 CG2 THR A 245 7050 11646 5803 927 719 332 C
ATOM 1273 N LEU A 246 -6.256 -32.594 3.925 1.00 70.17 N
ANISOU 1273 N LEU A 246 8085 12389 6187 2043 646 356 N
ATOM 1274 CA LEU A 246 -6.391 -33.991 4.346 1.00 71.46 C
ANISOU 1274 CA LEU A 246 8529 12343 6280 2347 623 396 C
ATOM 1275 C LEU A 246 -5.712 -34.188 5.685 1.00 76.49 C
ANISOU 1275 C LEU A 246 9127 13163 6773 2548 589 413 C
ATOM 1276 O LEU A 246 -6.287 -34.834 6.566 1.00 77.36 O
ANISOU 1276 O LEU A 246 9490 13016 6887 2621 584 486 O
ATOM 1277 CB LEU A 246 -5.814 -34.978 3.308 1.00 73.35 C
ANISOU 1277 CB LEU A 246 8857 12614 6397 2640 604 343 C
ATOM 1278 CG LEU A 246 -5.822 -36.467 3.701 1.00 79.88 C
ANISOU 1278 CG LEU A 246 10045 13202 7104 2998 572 377 C
ATOM 1279 CD1 LEU A 246 -7.247 -36.989 3.903 1.00 79.19 C
ANISOU 1279 CD1 LEU A 246 10317 12617 7157 2811 603 461 C
ATOM 1280 CD2 LEU A 246 -5.085 -37.302 2.684 1.00 83.24 C
ANISOU 1280 CD2 LEU A 246 10532 13718 7379 3326 548 302 C
ATOM 1281 N PHE A 247 -4.490 -33.628 5.836 1.00 72.63 N
ANISOU 1281 N PHE A 247 8318 13141 6138 2615 567 343 N
ATOM 1282 CA PHE A 247 -3.704 -33.695 7.068 1.00 73.38 C
ANISOU 1282 CA PHE A 247 8308 13507 6066 2805 526 341 C
ATOM 1283 C PHE A 247 -4.450 -33.027 8.232 1.00 77.53 C
ANISOU 1283 C PHE A 247 8867 13882 6709 2548 546 406 C
ATOM 1284 O PHE A 247 -4.440 -33.559 9.348 1.00 78.82 O
ANISOU 1284 O PHE A 247 9155 14003 6790 2724 518 457 O
ATOM 1285 CB PHE A 247 -2.322 -33.031 6.872 1.00 75.93 C
ANISOU 1285 CB PHE A 247 8224 14423 6205 2833 509 232 C
ATOM 1286 CG PHE A 247 -1.497 -32.905 8.140 1.00 78.05 C
ANISOU 1286 CG PHE A 247 8317 15049 6290 2974 465 214 C
ATOM 1287 CD1 PHE A 247 -1.433 -31.701 8.833 1.00 78.76 C
ANISOU 1287 CD1 PHE A 247 8198 15318 6408 2635 485 198 C
ATOM 1288 CD2 PHE A 247 -0.792 -33.995 8.644 1.00 82.18 C
ANISOU 1288 CD2 PHE A 247 8907 15724 6594 3460 399 209 C
ATOM 1289 CE1 PHE A 247 -0.688 -31.592 10.006 1.00 81.11 C
ANISOU 1289 CE1 PHE A 247 8329 15960 6527 2749 444 175 C
ATOM 1290 CE2 PHE A 247 -0.042 -33.882 9.816 1.00 86.18 C
ANISOU 1290 CE2 PHE A 247 9241 16589 6915 3606 351 190 C
ATOM 1291 CZ PHE A 247 0.005 -32.680 10.489 1.00 83.09 C
ANISOU 1291 CZ PHE A 247 8614 16393 6563 3235 376 172 C
ATOM 1292 N THR A 248 -5.077 -31.853 7.970 1.00 71.48 N
ANISOU 1292 N THR A 248 8002 13044 6114 2153 590 400 N
ATOM 1293 CA THR A 248 -5.782 -31.071 8.978 1.00 69.05 C
ANISOU 1293 CA THR A 248 7707 12618 5911 1908 611 440 C
ATOM 1294 C THR A 248 -6.999 -31.868 9.462 1.00 72.49 C
ANISOU 1294 C THR A 248 8461 12631 6452 1938 627 531 C
ATOM 1295 O THR A 248 -7.238 -31.897 10.671 1.00 71.95 O
ANISOU 1295 O THR A 248 8452 12523 6361 1938 626 574 O
ATOM 1296 CB THR A 248 -6.058 -29.679 8.445 1.00 72.06 C
ANISOU 1296 CB THR A 248 7944 13027 6408 1541 645 399 C
ATOM 1297 OG1 THR A 248 -4.792 -29.030 8.314 1.00 71.23 O
ANISOU 1297 OG1 THR A 248 7560 13360 6143 1494 633 317 O
ATOM 1298 CG2 THR A 248 -6.911 -28.849 9.371 1.00 71.42 C
ANISOU 1298 CG2 THR A 248 7911 12786 6440 1310 667 428 C
ATOM 1299 N LEU A 249 -7.696 -32.590 8.557 1.00 69.58 N
ANISOU 1299 N LEU A 249 8300 11974 6162 1964 643 555 N
ATOM 1300 CA LEU A 249 -8.821 -33.461 8.956 1.00 69.38 C
ANISOU 1300 CA LEU A 249 8593 11573 6196 1958 664 632 C
ATOM 1301 C LEU A 249 -8.296 -34.587 9.869 1.00 77.64 C
ANISOU 1301 C LEU A 249 9839 12603 7059 2272 628 683 C
ATOM 1302 O LEU A 249 -8.847 -34.828 10.953 1.00 77.60 O
ANISOU 1302 O LEU A 249 9986 12457 7043 2229 640 748 O
ATOM 1303 CB LEU A 249 -9.558 -34.066 7.733 1.00 68.32 C
ANISOU 1303 CB LEU A 249 8641 11171 6146 1912 685 633 C
ATOM 1304 CG LEU A 249 -10.157 -33.112 6.695 1.00 69.84 C
ANISOU 1304 CG LEU A 249 8690 11344 6502 1643 712 592 C
ATOM 1305 CD1 LEU A 249 -10.912 -33.876 5.626 1.00 68.83 C
ANISOU 1305 CD1 LEU A 249 8766 10957 6430 1613 728 595 C
ATOM 1306 CD2 LEU A 249 -11.030 -32.061 7.340 1.00 70.30 C
ANISOU 1306 CD2 LEU A 249 8658 11368 6686 1376 739 603 C
ATOM 1307 N ALA A 250 -7.181 -35.224 9.438 1.00 76.73 N
ANISOU 1307 N ALA A 250 9715 12660 6777 2605 580 646 N
ATOM 1308 CA ALA A 250 -6.506 -36.308 10.147 1.00 78.71 C
ANISOU 1308 CA ALA A 250 10167 12927 6811 2996 526 682 C
ATOM 1309 C ALA A 250 -6.083 -35.863 11.546 1.00 81.86 C
ANISOU 1309 C ALA A 250 10427 13555 7122 3025 502 704 C
ATOM 1310 O ALA A 250 -6.370 -36.578 12.492 1.00 83.03 O
ANISOU 1310 O ALA A 250 10847 13511 7189 3133 491 786 O
ATOM 1311 CB ALA A 250 -5.302 -36.797 9.345 1.00 81.22 C
ANISOU 1311 CB ALA A 250 10398 13503 6957 3361 475 605 C
ATOM 1312 N THR A 251 -5.488 -34.657 11.685 1.00 76.59 N
ANISOU 1312 N THR A 251 9363 13272 6467 2879 501 633 N
ATOM 1313 CA THR A 251 -5.034 -34.092 12.964 1.00 76.23 C
ANISOU 1313 CA THR A 251 9143 13489 6332 2863 479 634 C
ATOM 1314 C THR A 251 -6.198 -33.874 13.906 1.00 79.53 C
ANISOU 1314 C THR A 251 9728 13615 6877 2615 523 712 C
ATOM 1315 O THR A 251 -6.057 -34.122 15.107 1.00 80.97 O
ANISOU 1315 O THR A 251 9981 13840 6944 2726 499 759 O
ATOM 1316 CB THR A 251 -4.267 -32.793 12.729 1.00 79.88 C
ANISOU 1316 CB THR A 251 9187 14376 6789 2664 483 530 C
ATOM 1317 OG1 THR A 251 -3.239 -33.053 11.776 1.00 83.42 O
ANISOU 1317 OG1 THR A 251 9470 15121 7107 2871 453 451 O
ATOM 1318 CG2 THR A 251 -3.640 -32.245 13.993 1.00 76.27 C
ANISOU 1318 CG2 THR A 251 8533 14246 6199 2659 454 510 C
ATOM 1319 N PHE A 252 -7.345 -33.418 13.365 1.00 74.27 N
ANISOU 1319 N PHE A 252 9115 12679 6427 2296 585 719 N
ATOM 1320 CA PHE A 252 -8.559 -33.159 14.134 1.00 72.98 C
ANISOU 1320 CA PHE A 252 9073 12276 6380 2047 635 773 C
ATOM 1321 C PHE A 252 -9.154 -34.453 14.672 1.00 79.41 C
ANISOU 1321 C PHE A 252 10267 12783 7121 2165 642 872 C
ATOM 1322 O PHE A 252 -9.344 -34.546 15.886 1.00 79.61 O
ANISOU 1322 O PHE A 252 10373 12796 7078 2155 646 925 O
ATOM 1323 CB PHE A 252 -9.594 -32.408 13.295 1.00 72.61 C
ANISOU 1323 CB PHE A 252 8973 12067 6548 1734 689 742 C
ATOM 1324 CG PHE A 252 -9.641 -30.913 13.512 1.00 72.86 C
ANISOU 1324 CG PHE A 252 8749 12267 6667 1494 704 680 C
ATOM 1325 CD1 PHE A 252 -8.903 -30.053 12.705 1.00 75.60 C
ANISOU 1325 CD1 PHE A 252 8875 12827 7023 1428 689 604 C
ATOM 1326 CD2 PHE A 252 -10.473 -30.360 14.484 1.00 74.42 C
ANISOU 1326 CD2 PHE A 252 8958 12393 6924 1319 737 692 C
ATOM 1327 CE1 PHE A 252 -8.960 -28.667 12.896 1.00 75.82 C
ANISOU 1327 CE1 PHE A 252 8742 12959 7107 1188 703 548 C
ATOM 1328 CE2 PHE A 252 -10.548 -28.973 14.661 1.00 76.20 C
ANISOU 1328 CE2 PHE A 252 9004 12732 7215 1117 748 627 C
ATOM 1329 CZ PHE A 252 -9.789 -28.134 13.865 1.00 73.93 C
ANISOU 1329 CZ PHE A 252 8545 12617 6929 1049 729 558 C
ATOM 1330 N VAL A 253 -9.402 -35.460 13.794 1.00 77.62 N
ANISOU 1330 N VAL A 253 10299 12309 6885 2267 644 896 N
ATOM 1331 CA VAL A 253 -9.987 -36.753 14.193 1.00 79.80 C
ANISOU 1331 CA VAL A 253 11013 12243 7064 2340 655 990 C
ATOM 1332 C VAL A 253 -9.015 -37.550 15.066 1.00 87.39 C
ANISOU 1332 C VAL A 253 12144 13281 7779 2720 587 1042 C
ATOM 1333 O VAL A 253 -9.467 -38.322 15.919 1.00 89.83 O
ANISOU 1333 O VAL A 253 12788 13361 7983 2733 597 1136 O
ATOM 1334 CB VAL A 253 -10.532 -37.617 13.025 1.00 84.74 C
ANISOU 1334 CB VAL A 253 11910 12564 7722 2322 675 992 C
ATOM 1335 CG1 VAL A 253 -11.678 -36.910 12.298 1.00 82.31 C
ANISOU 1335 CG1 VAL A 253 11468 12172 7636 1937 740 953 C
ATOM 1336 CG2 VAL A 253 -9.434 -38.009 12.048 1.00 85.94 C
ANISOU 1336 CG2 VAL A 253 12026 12840 7788 2652 617 936 C
ATOM 1337 N ALA A 254 -7.696 -37.313 14.917 1.00 84.58 N
ANISOU 1337 N ALA A 254 11542 13281 7313 3015 519 980 N
ATOM 1338 CA ALA A 254 -6.678 -37.968 15.746 1.00 87.26 C
ANISOU 1338 CA ALA A 254 11973 13788 7394 3431 439 1010 C
ATOM 1339 C ALA A 254 -6.766 -37.503 17.209 1.00 91.36 C
ANISOU 1339 C ALA A 254 12422 14427 7865 3337 439 1058 C
ATOM 1340 O ALA A 254 -6.210 -38.152 18.090 1.00 93.54 O
ANISOU 1340 O ALA A 254 12866 14756 7920 3647 378 1114 O
ATOM 1341 CB ALA A 254 -5.288 -37.694 15.193 1.00 88.92 C
ANISOU 1341 CB ALA A 254 11840 14452 7494 3716 374 905 C
ATOM 1342 N ASP A 255 -7.488 -36.399 17.456 1.00 86.01 N
ANISOU 1342 N ASP A 255 11516 13785 7378 2933 504 1033 N
ATOM 1343 CA ASP A 255 -7.680 -35.792 18.763 1.00 86.14 C
ANISOU 1343 CA ASP A 255 11430 13921 7376 2790 517 1056 C
ATOM 1344 C ASP A 255 -9.132 -35.256 18.865 1.00 91.33 C
ANISOU 1344 C ASP A 255 12119 14340 8243 2358 611 1070 C
ATOM 1345 O ASP A 255 -9.369 -34.202 19.463 1.00 90.87 O
ANISOU 1345 O ASP A 255 11824 14437 8264 2140 639 1028 O
ATOM 1346 CB ASP A 255 -6.620 -34.679 18.934 1.00 87.29 C
ANISOU 1346 CB ASP A 255 11124 14553 7489 2808 477 952 C
ATOM 1347 CG ASP A 255 -6.535 -34.011 20.291 1.00 96.19 C
ANISOU 1347 CG ASP A 255 12108 15882 8557 2706 474 953 C
ATOM 1348 OD1 ASP A 255 -6.539 -32.769 20.334 1.00 95.51 O
ANISOU 1348 OD1 ASP A 255 11723 15994 8575 2445 500 868 O
ATOM 1349 OD2 ASP A 255 -6.458 -34.733 21.310 1.00103.35 O
ANISOU 1349 OD2 ASP A 255 13229 16742 9297 2891 444 1037 O
ATOM 1350 N TRP A 256 -10.108 -36.009 18.302 1.00 88.60 N
ANISOU 1350 N TRP A 256 12073 13629 7961 2244 659 1120 N
ATOM 1351 CA TRP A 256 -11.525 -35.619 18.244 1.00 87.35 C
ANISOU 1351 CA TRP A 256 11927 13288 7975 1856 746 1118 C
ATOM 1352 C TRP A 256 -12.193 -35.352 19.601 1.00 89.16 C
ANISOU 1352 C TRP A 256 12177 13528 8171 1675 790 1159 C
ATOM 1353 O TRP A 256 -12.995 -34.424 19.680 1.00 88.10 O
ANISOU 1353 O TRP A 256 11844 13447 8182 1403 844 1105 O
ATOM 1354 CB TRP A 256 -12.360 -36.651 17.481 1.00 87.40 C
ANISOU 1354 CB TRP A 256 12269 12941 7996 1766 785 1162 C
ATOM 1355 CG TRP A 256 -13.720 -36.147 17.079 1.00 87.00 C
ANISOU 1355 CG TRP A 256 12134 12798 8124 1386 865 1125 C
ATOM 1356 CD1 TRP A 256 -14.925 -36.539 17.587 1.00 90.39 C
ANISOU 1356 CD1 TRP A 256 12748 13061 8535 1118 937 1168 C
ATOM 1357 CD2 TRP A 256 -14.005 -35.138 16.101 1.00 84.93 C
ANISOU 1357 CD2 TRP A 256 11571 12641 8056 1242 878 1030 C
ATOM 1358 NE1 TRP A 256 -15.945 -35.853 16.973 1.00 88.40 N
ANISOU 1358 NE1 TRP A 256 12297 12839 8452 843 989 1097 N
ATOM 1359 CE2 TRP A 256 -15.409 -34.999 16.039 1.00 88.48 C
ANISOU 1359 CE2 TRP A 256 12032 12989 8596 930 949 1018 C
ATOM 1360 CE3 TRP A 256 -13.210 -34.365 15.236 1.00 84.96 C
ANISOU 1360 CE3 TRP A 256 11312 12825 8145 1343 835 955 C
ATOM 1361 CZ2 TRP A 256 -16.035 -34.114 15.149 1.00 86.02 C
ANISOU 1361 CZ2 TRP A 256 11487 12741 8458 767 968 934 C
ATOM 1362 CZ3 TRP A 256 -13.830 -33.475 14.374 1.00 84.62 C
ANISOU 1362 CZ3 TRP A 256 11070 12806 8274 1147 860 885 C
ATOM 1363 CH2 TRP A 256 -15.225 -33.352 14.338 1.00 84.71 C
ANISOU 1363 CH2 TRP A 256 11107 12705 8375 886 919 876 C
ATOM 1364 N ARG A 257 -11.910 -36.137 20.646 1.00 85.31 N
ANISOU 1364 N ARG A 257 11935 12994 7483 1833 766 1250 N
ATOM 1365 CA ARG A 257 -12.534 -35.866 21.939 1.00 84.68 C
ANISOU 1365 CA ARG A 257 11866 12947 7359 1651 812 1286 C
ATOM 1366 C ARG A 257 -12.183 -34.457 22.396 1.00 86.84 C
ANISOU 1366 C ARG A 257 11726 13552 7718 1586 802 1191 C
ATOM 1367 O ARG A 257 -13.059 -33.745 22.886 1.00 85.58 O
ANISOU 1367 O ARG A 257 11450 13424 7643 1328 865 1157 O
ATOM 1368 CB ARG A 257 -12.115 -36.892 22.994 1.00 86.82 C
ANISOU 1368 CB ARG A 257 12478 13135 7374 1868 774 1404 C
ATOM 1369 N ASN A 258 -10.923 -34.032 22.148 1.00 83.15 N
ANISOU 1369 N ASN A 258 11036 13340 7216 1807 728 1135 N
ATOM 1370 CA ASN A 258 -10.391 -32.723 22.530 1.00 81.80 C
ANISOU 1370 CA ASN A 258 10504 13490 7085 1737 711 1038 C
ATOM 1371 C ASN A 258 -10.709 -31.612 21.546 1.00 82.50 C
ANISOU 1371 C ASN A 258 10354 13609 7383 1522 742 933 C
ATOM 1372 O ASN A 258 -11.103 -30.536 21.975 1.00 80.26 O
ANISOU 1372 O ASN A 258 9906 13410 7178 1320 773 868 O
ATOM 1373 CB ASN A 258 -8.870 -32.784 22.691 1.00 84.15 C
ANISOU 1373 CB ASN A 258 10661 14102 7211 2036 619 1014 C
ATOM 1374 CG ASN A 258 -8.341 -33.498 23.906 1.00110.12 C
ANISOU 1374 CG ASN A 258 14104 17473 10262 2278 569 1095 C
ATOM 1375 OD1 ASN A 258 -9.032 -33.719 24.911 1.00 98.88 O
ANISOU 1375 OD1 ASN A 258 12850 15926 8793 2175 606 1163 O
ATOM 1376 ND2 ASN A 258 -7.056 -33.804 23.860 1.00108.24 N
ANISOU 1376 ND2 ASN A 258 13783 17495 9846 2610 480 1081 N
ATOM 1377 N SER A 259 -10.467 -31.845 20.243 1.00 79.66 N
ANISOU 1377 N SER A 259 9989 13185 7091 1585 726 913 N
ATOM 1378 CA SER A 259 -10.602 -30.850 19.176 1.00 77.63 C
ANISOU 1378 CA SER A 259 9532 12961 7003 1417 742 822 C
ATOM 1379 C SER A 259 -12.021 -30.577 18.714 1.00 78.46 C
ANISOU 1379 C SER A 259 9697 12832 7283 1178 808 813 C
ATOM 1380 O SER A 259 -12.218 -29.535 18.100 1.00 78.93 O
ANISOU 1380 O SER A 259 9596 12930 7465 1035 818 737 O
ATOM 1381 CB SER A 259 -9.760 -31.239 17.971 1.00 82.44 C
ANISOU 1381 CB SER A 259 10107 13623 7593 1585 700 803 C
ATOM 1382 OG SER A 259 -8.407 -30.883 18.206 1.00 96.63 O
ANISOU 1382 OG SER A 259 11694 15770 9250 1730 642 753 O
ATOM 1383 N ASN A 260 -13.005 -31.448 18.991 1.00 72.49 N
ANISOU 1383 N ASN A 260 9169 11855 6518 1124 852 884 N
ATOM 1384 CA ASN A 260 -14.388 -31.185 18.565 1.00 70.24 C
ANISOU 1384 CA ASN A 260 8894 11423 6372 891 915 858 C
ATOM 1385 C ASN A 260 -15.056 -30.148 19.495 1.00 70.55 C
ANISOU 1385 C ASN A 260 8789 11570 6447 732 952 803 C
ATOM 1386 O ASN A 260 -16.003 -30.459 20.227 1.00 69.72 O
ANISOU 1386 O ASN A 260 8770 11415 6304 614 1006 830 O
ATOM 1387 CB ASN A 260 -15.214 -32.476 18.479 1.00 71.86 C
ANISOU 1387 CB ASN A 260 9383 11392 6527 834 957 936 C
ATOM 1388 CG ASN A 260 -16.602 -32.298 17.905 1.00 85.31 C
ANISOU 1388 CG ASN A 260 11061 13006 8346 591 1017 896 C
ATOM 1389 OD1 ASN A 260 -16.874 -31.405 17.084 1.00 77.87 O
ANISOU 1389 OD1 ASN A 260 9928 12119 7541 532 1012 817 O
ATOM 1390 ND2 ASN A 260 -17.499 -33.185 18.293 1.00 74.98 N
ANISOU 1390 ND2 ASN A 260 9960 11569 6960 444 1074 949 N
ATOM 1391 N ARG A 261 -14.526 -28.913 19.466 1.00 65.04 N
ANISOU 1391 N ARG A 261 7886 11028 5799 722 924 721 N
ATOM 1392 CA ARG A 261 -14.984 -27.790 20.284 1.00 64.50 C
ANISOU 1392 CA ARG A 261 7698 11057 5750 608 947 649 C
ATOM 1393 C ARG A 261 -15.091 -26.557 19.416 1.00 69.40 C
ANISOU 1393 C ARG A 261 8195 11682 6490 534 934 555 C
ATOM 1394 O ARG A 261 -14.291 -26.398 18.483 1.00 69.81 O
ANISOU 1394 O ARG A 261 8206 11752 6567 575 895 543 O
ATOM 1395 CB ARG A 261 -14.034 -27.538 21.487 1.00 61.76 C
ANISOU 1395 CB ARG A 261 7298 10899 5269 675 919 648 C
ATOM 1396 N TYR A 262 -16.080 -25.688 19.704 1.00 65.58 N
ANISOU 1396 N TYR A 262 7667 11188 6061 438 966 485 N
ATOM 1397 CA TYR A 262 -16.247 -24.446 18.955 1.00 64.92 C
ANISOU 1397 CA TYR A 262 7526 11074 6065 393 946 396 C
ATOM 1398 C TYR A 262 -15.496 -23.291 19.658 1.00 71.37 C
ANISOU 1398 C TYR A 262 8301 11997 6819 358 923 326 C
ATOM 1399 O TYR A 262 -15.350 -23.308 20.879 1.00 72.64 O
ANISOU 1399 O TYR A 262 8447 12262 6889 357 936 323 O
ATOM 1400 CB TYR A 262 -17.719 -24.121 18.728 1.00 65.16 C
ANISOU 1400 CB TYR A 262 7550 11041 6167 357 980 346 C
ATOM 1401 CG TYR A 262 -18.380 -25.055 17.738 1.00 66.12 C
ANISOU 1401 CG TYR A 262 7701 11072 6350 347 995 393 C
ATOM 1402 CD1 TYR A 262 -18.479 -24.721 16.388 1.00 66.78 C
ANISOU 1402 CD1 TYR A 262 7779 11073 6521 359 964 372 C
ATOM 1403 CD2 TYR A 262 -18.934 -26.262 18.154 1.00 67.77 C
ANISOU 1403 CD2 TYR A 262 7967 11274 6509 302 1042 456 C
ATOM 1404 CE1 TYR A 262 -19.116 -25.568 15.476 1.00 66.93 C
ANISOU 1404 CE1 TYR A 262 7822 11022 6585 336 976 404 C
ATOM 1405 CE2 TYR A 262 -19.565 -27.119 17.254 1.00 69.09 C
ANISOU 1405 CE2 TYR A 262 8185 11356 6712 253 1059 488 C
ATOM 1406 CZ TYR A 262 -19.658 -26.770 15.915 1.00 75.24 C
ANISOU 1406 CZ TYR A 262 8931 12071 7586 274 1025 458 C
ATOM 1407 OH TYR A 262 -20.291 -27.640 15.054 1.00 73.27 O
ANISOU 1407 OH TYR A 262 8731 11750 7358 211 1042 482 O
ATOM 1408 N PRO A 263 -14.916 -22.336 18.909 1.00 67.85 N
ANISOU 1408 N PRO A 263 7851 11534 6395 307 888 272 N
ATOM 1409 CA PRO A 263 -15.016 -22.158 17.453 1.00 66.75 C
ANISOU 1409 CA PRO A 263 7739 11279 6345 297 868 271 C
ATOM 1410 C PRO A 263 -13.961 -22.909 16.626 1.00 70.90 C
ANISOU 1410 C PRO A 263 8225 11862 6851 326 843 329 C
ATOM 1411 O PRO A 263 -14.028 -22.829 15.402 1.00 71.64 O
ANISOU 1411 O PRO A 263 8338 11872 7010 313 829 330 O
ATOM 1412 CB PRO A 263 -14.898 -20.633 17.279 1.00 68.69 C
ANISOU 1412 CB PRO A 263 8047 11474 6579 206 846 180 C
ATOM 1413 CG PRO A 263 -14.398 -20.069 18.606 1.00 74.25 C
ANISOU 1413 CG PRO A 263 8742 12295 7172 147 851 129 C
ATOM 1414 CD PRO A 263 -14.171 -21.231 19.537 1.00 69.98 C
ANISOU 1414 CD PRO A 263 8115 11896 6578 219 869 197 C
ATOM 1415 N ALA A 264 -13.033 -23.664 17.254 1.00 66.15 N
ANISOU 1415 N ALA A 264 7572 11415 6148 391 834 372 N
ATOM 1416 CA ALA A 264 -11.954 -24.365 16.541 1.00 64.65 C
ANISOU 1416 CA ALA A 264 7329 11331 5904 470 804 409 C
ATOM 1417 C ALA A 264 -12.459 -25.340 15.510 1.00 64.15 C
ANISOU 1417 C ALA A 264 7336 11115 5924 555 811 466 C
ATOM 1418 O ALA A 264 -12.062 -25.212 14.348 1.00 63.16 O
ANISOU 1418 O ALA A 264 7184 10988 5825 542 794 453 O
ATOM 1419 CB ALA A 264 -11.039 -25.087 17.514 1.00 66.83 C
ANISOU 1419 CB ALA A 264 7552 11805 6034 590 786 443 C
ATOM 1420 N VAL A 265 -13.377 -26.260 15.895 1.00 59.26 N
ANISOU 1420 N VAL A 265 6818 10367 5332 607 841 522 N
ATOM 1421 CA VAL A 265 -13.913 -27.291 14.992 1.00 58.91 C
ANISOU 1421 CA VAL A 265 6876 10166 5342 656 852 573 C
ATOM 1422 C VAL A 265 -14.572 -26.702 13.680 1.00 61.40 C
ANISOU 1422 C VAL A 265 7172 10373 5783 568 852 531 C
ATOM 1423 O VAL A 265 -14.765 -27.459 12.732 1.00 60.33 O
ANISOU 1423 O VAL A 265 7099 10140 5682 601 852 559 O
ATOM 1424 CB VAL A 265 -14.840 -28.302 15.710 1.00 62.44 C
ANISOU 1424 CB VAL A 265 7460 10502 5765 655 893 633 C
ATOM 1425 CG1 VAL A 265 -16.277 -27.816 15.754 1.00 61.64 C
ANISOU 1425 CG1 VAL A 265 7339 10333 5748 512 936 592 C
ATOM 1426 CG2 VAL A 265 -14.745 -29.688 15.074 1.00 62.54 C
ANISOU 1426 CG2 VAL A 265 7637 10383 5744 746 892 700 C
ATOM 1427 N ILE A 266 -14.840 -25.376 13.605 1.00 57.95 N
ANISOU 1427 N ILE A 266 6677 9947 5394 474 846 464 N
ATOM 1428 CA ILE A 266 -15.356 -24.735 12.376 1.00 57.59 C
ANISOU 1428 CA ILE A 266 6639 9804 5438 423 833 430 C
ATOM 1429 C ILE A 266 -14.339 -24.930 11.252 1.00 61.65 C
ANISOU 1429 C ILE A 266 7134 10355 5936 442 805 443 C
ATOM 1430 O ILE A 266 -14.734 -25.195 10.114 1.00 61.36 O
ANISOU 1430 O ILE A 266 7127 10227 5961 447 800 452 O
ATOM 1431 CB ILE A 266 -15.668 -23.215 12.560 1.00 60.11 C
ANISOU 1431 CB ILE A 266 6963 10106 5771 351 820 357 C
ATOM 1432 CG1 ILE A 266 -16.832 -22.994 13.525 1.00 59.55 C
ANISOU 1432 CG1 ILE A 266 6894 10019 5711 363 848 324 C
ATOM 1433 CG2 ILE A 266 -15.846 -22.457 11.187 1.00 58.82 C
ANISOU 1433 CG2 ILE A 266 6845 9841 5661 318 790 331 C
ATOM 1434 CD1 ILE A 266 -16.796 -21.729 14.142 1.00 62.01 C
ANISOU 1434 CD1 ILE A 266 7236 10340 5987 333 837 256 C
ATOM 1435 N LEU A 267 -13.031 -24.811 11.592 1.00 58.11 N
ANISOU 1435 N LEU A 267 6617 10076 5386 452 789 436 N
ATOM 1436 CA LEU A 267 -11.920 -24.941 10.652 1.00 58.40 C
ANISOU 1436 CA LEU A 267 6591 10231 5366 467 768 432 C
ATOM 1437 C LEU A 267 -11.835 -26.370 10.081 1.00 63.71 C
ANISOU 1437 C LEU A 267 7304 10867 6036 628 767 481 C
ATOM 1438 O LEU A 267 -11.522 -26.535 8.891 1.00 64.00 O
ANISOU 1438 O LEU A 267 7328 10906 6081 641 757 475 O
ATOM 1439 CB LEU A 267 -10.600 -24.502 11.296 1.00 59.03 C
ANISOU 1439 CB LEU A 267 6552 10574 5305 433 753 396 C
ATOM 1440 CG LEU A 267 -10.305 -22.973 11.330 1.00 63.43 C
ANISOU 1440 CG LEU A 267 7096 11181 5824 211 750 330 C
ATOM 1441 CD1 LEU A 267 -10.164 -22.362 9.934 1.00 62.30 C
ANISOU 1441 CD1 LEU A 267 6984 10989 5698 89 744 312 C
ATOM 1442 CD2 LEU A 267 -11.271 -22.204 12.226 1.00 65.02 C
ANISOU 1442 CD2 LEU A 267 7396 11230 6080 147 762 308 C
ATOM 1443 N PHE A 268 -12.217 -27.379 10.893 1.00 59.48 N
ANISOU 1443 N PHE A 268 6852 10266 5480 736 781 530 N
ATOM 1444 CA PHE A 268 -12.305 -28.766 10.455 1.00 58.88 C
ANISOU 1444 CA PHE A 268 6901 10085 5386 877 782 579 C
ATOM 1445 C PHE A 268 -13.313 -28.871 9.295 1.00 61.91 C
ANISOU 1445 C PHE A 268 7353 10283 5885 792 797 575 C
ATOM 1446 O PHE A 268 -12.957 -29.363 8.223 1.00 61.29 O
ANISOU 1446 O PHE A 268 7302 10185 5800 858 784 572 O
ATOM 1447 CB PHE A 268 -12.710 -29.676 11.631 1.00 60.65 C
ANISOU 1447 CB PHE A 268 7263 10228 5554 948 800 638 C
ATOM 1448 CG PHE A 268 -13.197 -31.051 11.239 1.00 62.01 C
ANISOU 1448 CG PHE A 268 7655 10198 5710 1021 814 690 C
ATOM 1449 CD1 PHE A 268 -12.298 -32.047 10.877 1.00 65.38 C
ANISOU 1449 CD1 PHE A 268 8184 10629 6027 1240 784 713 C
ATOM 1450 CD2 PHE A 268 -14.553 -31.350 11.234 1.00 63.69 C
ANISOU 1450 CD2 PHE A 268 7980 10229 5990 868 856 707 C
ATOM 1451 CE1 PHE A 268 -12.748 -33.316 10.520 1.00 67.10 C
ANISOU 1451 CE1 PHE A 268 8668 10617 6210 1300 796 757 C
ATOM 1452 CE2 PHE A 268 -15.003 -32.623 10.879 1.00 67.08 C
ANISOU 1452 CE2 PHE A 268 8645 10462 6378 881 874 749 C
ATOM 1453 CZ PHE A 268 -14.097 -33.599 10.534 1.00 66.12 C
ANISOU 1453 CZ PHE A 268 8679 10292 6153 1094 844 777 C
ATOM 1454 N TYR A 269 -14.550 -28.365 9.500 1.00 58.31 N
ANISOU 1454 N TYR A 269 6906 9728 5520 657 820 562 N
ATOM 1455 CA TYR A 269 -15.602 -28.384 8.474 1.00 57.71 C
ANISOU 1455 CA TYR A 269 6862 9528 5535 576 827 547 C
ATOM 1456 C TYR A 269 -15.250 -27.521 7.264 1.00 62.57 C
ANISOU 1456 C TYR A 269 7406 10174 6192 546 797 510 C
ATOM 1457 O TYR A 269 -15.622 -27.896 6.156 1.00 62.16 O
ANISOU 1457 O TYR A 269 7391 10048 6179 538 792 508 O
ATOM 1458 CB TYR A 269 -16.948 -27.985 9.056 1.00 57.52 C
ANISOU 1458 CB TYR A 269 6825 9468 5562 473 853 526 C
ATOM 1459 CG TYR A 269 -17.459 -29.037 10.006 1.00 59.06 C
ANISOU 1459 CG TYR A 269 7121 9618 5702 452 895 568 C
ATOM 1460 CD1 TYR A 269 -17.937 -30.258 9.533 1.00 61.09 C
ANISOU 1460 CD1 TYR A 269 7518 9756 5936 416 917 598 C
ATOM 1461 CD2 TYR A 269 -17.387 -28.851 11.386 1.00 60.21 C
ANISOU 1461 CD2 TYR A 269 7253 9831 5794 454 913 579 C
ATOM 1462 CE1 TYR A 269 -18.360 -31.254 10.411 1.00 64.69 C
ANISOU 1462 CE1 TYR A 269 8123 10146 6309 361 959 644 C
ATOM 1463 CE2 TYR A 269 -17.818 -29.836 12.275 1.00 61.42 C
ANISOU 1463 CE2 TYR A 269 7528 9938 5872 417 954 627 C
ATOM 1464 CZ TYR A 269 -18.304 -31.035 11.784 1.00 71.79 C
ANISOU 1464 CZ TYR A 269 9005 11116 7154 362 978 663 C
ATOM 1465 OH TYR A 269 -18.725 -32.002 12.665 1.00 76.65 O
ANISOU 1465 OH TYR A 269 9791 11663 7668 288 1022 716 O
ATOM 1466 N VAL A 270 -14.488 -26.412 7.462 1.00 59.37 N
ANISOU 1466 N VAL A 270 6920 9881 5759 509 779 482 N
ATOM 1467 CA VAL A 270 -14.005 -25.574 6.359 1.00 58.85 C
ANISOU 1467 CA VAL A 270 6820 9846 5693 446 755 455 C
ATOM 1468 C VAL A 270 -13.045 -26.431 5.524 1.00 65.37 C
ANISOU 1468 C VAL A 270 7623 10755 6462 529 750 466 C
ATOM 1469 O VAL A 270 -13.192 -26.484 4.310 1.00 66.20 O
ANISOU 1469 O VAL A 270 7746 10811 6596 511 741 460 O
ATOM 1470 CB VAL A 270 -13.333 -24.247 6.823 1.00 61.89 C
ANISOU 1470 CB VAL A 270 7166 10327 6021 339 744 419 C
ATOM 1471 CG1 VAL A 270 -12.734 -23.495 5.633 1.00 61.80 C
ANISOU 1471 CG1 VAL A 270 7159 10346 5976 235 726 400 C
ATOM 1472 CG2 VAL A 270 -14.303 -23.353 7.577 1.00 60.69 C
ANISOU 1472 CG2 VAL A 270 7069 10077 5913 293 745 395 C
ATOM 1473 N ASN A 271 -12.095 -27.132 6.192 1.00 62.80 N
ANISOU 1473 N ASN A 271 7258 10566 6039 645 751 476 N
ATOM 1474 CA ASN A 271 -11.089 -28.009 5.571 1.00 63.13 C
ANISOU 1474 CA ASN A 271 7271 10729 5988 792 741 473 C
ATOM 1475 C ASN A 271 -11.723 -29.224 4.874 1.00 66.60 C
ANISOU 1475 C ASN A 271 7857 10979 6468 892 747 498 C
ATOM 1476 O ASN A 271 -11.215 -29.636 3.826 1.00 67.10 O
ANISOU 1476 O ASN A 271 7914 11085 6495 961 739 478 O
ATOM 1477 CB ASN A 271 -10.061 -28.467 6.609 1.00 63.17 C
ANISOU 1477 CB ASN A 271 7213 10931 5858 942 731 475 C
ATOM 1478 CG ASN A 271 -8.875 -27.539 6.708 1.00 71.68 C
ANISOU 1478 CG ASN A 271 8096 12314 6825 861 720 422 C
ATOM 1479 OD1 ASN A 271 -7.808 -27.823 6.171 1.00 69.25 O
ANISOU 1479 OD1 ASN A 271 7672 12246 6396 956 708 386 O
ATOM 1480 ND2 ASN A 271 -9.044 -26.386 7.343 1.00 51.53 N
ANISOU 1480 ND2 ASN A 271 5508 9777 4294 669 727 404 N
ATOM 1481 N ALA A 272 -12.838 -29.773 5.433 1.00 61.51 N
ANISOU 1481 N ALA A 272 7349 10140 5883 872 766 534 N
ATOM 1482 CA ALA A 272 -13.583 -30.908 4.860 1.00 61.41 C
ANISOU 1482 CA ALA A 272 7510 9931 5893 897 779 553 C
ATOM 1483 C ALA A 272 -14.099 -30.558 3.468 1.00 65.19 C
ANISOU 1483 C ALA A 272 7961 10359 6449 796 773 521 C
ATOM 1484 O ALA A 272 -13.994 -31.355 2.527 1.00 66.05 O
ANISOU 1484 O ALA A 272 8157 10404 6534 858 770 512 O
ATOM 1485 CB ALA A 272 -14.753 -31.279 5.765 1.00 62.04 C
ANISOU 1485 CB ALA A 272 7701 9867 6004 803 810 585 C
ATOM 1486 N CYS A 273 -14.619 -29.324 3.350 1.00 59.16 N
ANISOU 1486 N CYS A 273 7091 9626 5762 659 766 502 N
ATOM 1487 CA CYS A 273 -15.171 -28.732 2.149 1.00 57.04 C
ANISOU 1487 CA CYS A 273 6795 9322 5555 571 750 478 C
ATOM 1488 C CYS A 273 -14.113 -28.573 1.072 1.00 59.90 C
ANISOU 1488 C CYS A 273 7107 9786 5866 605 734 460 C
ATOM 1489 O CYS A 273 -14.339 -29.072 -0.021 1.00 59.09 O
ANISOU 1489 O CYS A 273 7050 9628 5774 610 729 449 O
ATOM 1490 CB CYS A 273 -15.837 -27.405 2.485 1.00 55.74 C
ANISOU 1490 CB CYS A 273 6572 9160 5447 472 738 464 C
ATOM 1491 SG CYS A 273 -17.322 -27.579 3.494 1.00 58.87 S
ANISOU 1491 SG CYS A 273 6988 9491 5891 427 760 461 S
ATOM 1492 N PHE A 274 -12.958 -27.936 1.382 1.00 57.29 N
ANISOU 1492 N PHE A 274 6677 9629 5461 612 730 450 N
ATOM 1493 CA PHE A 274 -11.834 -27.748 0.438 1.00 58.31 C
ANISOU 1493 CA PHE A 274 6724 9928 5504 616 724 423 C
ATOM 1494 C PHE A 274 -11.220 -29.081 0.017 1.00 63.35 C
ANISOU 1494 C PHE A 274 7388 10615 6069 806 728 409 C
ATOM 1495 O PHE A 274 -10.867 -29.254 -1.154 1.00 63.09 O
ANISOU 1495 O PHE A 274 7333 10641 5997 821 726 382 O
ATOM 1496 CB PHE A 274 -10.764 -26.818 1.020 1.00 61.00 C
ANISOU 1496 CB PHE A 274 6938 10489 5749 539 725 403 C
ATOM 1497 CG PHE A 274 -11.242 -25.392 0.942 1.00 62.70 C
ANISOU 1497 CG PHE A 274 7188 10629 6008 337 717 404 C
ATOM 1498 CD1 PHE A 274 -12.021 -24.849 1.955 1.00 64.37 C
ANISOU 1498 CD1 PHE A 274 7456 10718 6285 299 713 416 C
ATOM 1499 CD2 PHE A 274 -11.023 -24.631 -0.206 1.00 65.94 C
ANISOU 1499 CD2 PHE A 274 7612 11060 6383 202 709 394 C
ATOM 1500 CE1 PHE A 274 -12.529 -23.557 1.853 1.00 65.01 C
ANISOU 1500 CE1 PHE A 274 7618 10695 6390 164 697 411 C
ATOM 1501 CE2 PHE A 274 -11.534 -23.337 -0.309 1.00 68.23 C
ANISOU 1501 CE2 PHE A 274 8007 11224 6693 46 693 402 C
ATOM 1502 CZ PHE A 274 -12.283 -22.813 0.725 1.00 65.57 C
ANISOU 1502 CZ PHE A 274 7738 10758 6416 45 684 407 C
ATOM 1503 N PHE A 275 -11.163 -30.050 0.944 1.00 60.38 N
ANISOU 1503 N PHE A 275 7090 10193 5660 962 732 428 N
ATOM 1504 CA PHE A 275 -10.696 -31.379 0.594 1.00 60.55 C
ANISOU 1504 CA PHE A 275 7212 10199 5594 1182 729 416 C
ATOM 1505 C PHE A 275 -11.617 -31.977 -0.468 1.00 64.08 C
ANISOU 1505 C PHE A 275 7811 10427 6109 1138 735 412 C
ATOM 1506 O PHE A 275 -11.116 -32.364 -1.527 1.00 64.79 O
ANISOU 1506 O PHE A 275 7902 10575 6142 1223 730 373 O
ATOM 1507 CB PHE A 275 -10.612 -32.291 1.819 1.00 62.53 C
ANISOU 1507 CB PHE A 275 7591 10385 5783 1353 727 450 C
ATOM 1508 CG PHE A 275 -10.145 -33.685 1.476 1.00 64.75 C
ANISOU 1508 CG PHE A 275 8051 10603 5949 1618 716 438 C
ATOM 1509 CD1 PHE A 275 -8.825 -33.921 1.097 1.00 67.30 C
ANISOU 1509 CD1 PHE A 275 8262 11185 6122 1849 695 385 C
ATOM 1510 CD2 PHE A 275 -11.020 -34.764 1.541 1.00 67.02 C
ANISOU 1510 CD2 PHE A 275 8633 10580 6250 1635 727 471 C
ATOM 1511 CE1 PHE A 275 -8.396 -35.204 0.770 1.00 69.45 C
ANISOU 1511 CE1 PHE A 275 8729 11388 6269 2145 678 364 C
ATOM 1512 CE2 PHE A 275 -10.581 -36.054 1.240 1.00 71.25 C
ANISOU 1512 CE2 PHE A 275 9405 11010 6658 1891 713 458 C
ATOM 1513 CZ PHE A 275 -9.275 -36.260 0.838 1.00 70.00 C
ANISOU 1513 CZ PHE A 275 9146 11092 6358 2170 685 403 C
ATOM 1514 N VAL A 276 -12.958 -32.002 -0.206 1.00 58.71 N
ANISOU 1514 N VAL A 276 7236 9537 5535 992 746 441 N
ATOM 1515 CA VAL A 276 -13.967 -32.547 -1.127 1.00 57.87 C
ANISOU 1515 CA VAL A 276 7256 9252 5479 906 751 429 C
ATOM 1516 C VAL A 276 -13.913 -31.779 -2.476 1.00 61.35 C
ANISOU 1516 C VAL A 276 7580 9780 5952 825 734 397 C
ATOM 1517 O VAL A 276 -13.987 -32.412 -3.522 1.00 62.50 O
ANISOU 1517 O VAL A 276 7803 9870 6073 852 732 367 O
ATOM 1518 CB VAL A 276 -15.392 -32.582 -0.504 1.00 60.68 C
ANISOU 1518 CB VAL A 276 7681 9463 5913 740 768 452 C
ATOM 1519 CG1 VAL A 276 -16.451 -32.998 -1.525 1.00 60.50 C
ANISOU 1519 CG1 VAL A 276 7731 9330 5925 610 770 423 C
ATOM 1520 CG2 VAL A 276 -15.441 -33.517 0.695 1.00 61.17 C
ANISOU 1520 CG2 VAL A 276 7916 9414 5914 798 792 488 C
ATOM 1521 N GLY A 277 -13.717 -30.458 -2.431 1.00 56.15 N
ANISOU 1521 N GLY A 277 6767 9244 5325 730 723 402 N
ATOM 1522 CA GLY A 277 -13.582 -29.618 -3.616 1.00 55.51 C
ANISOU 1522 CA GLY A 277 6608 9238 5245 641 706 385 C
ATOM 1523 C GLY A 277 -12.366 -30.005 -4.443 1.00 61.44 C
ANISOU 1523 C GLY A 277 7312 10147 5886 740 712 350 C
ATOM 1524 O GLY A 277 -12.463 -30.128 -5.659 1.00 60.92 O
ANISOU 1524 O GLY A 277 7264 10074 5808 719 706 327 O
ATOM 1525 N SER A 278 -11.219 -30.243 -3.781 1.00 60.35 N
ANISOU 1525 N SER A 278 7099 10182 5650 866 722 337 N
ATOM 1526 CA SER A 278 -9.978 -30.685 -4.426 1.00 61.54 C
ANISOU 1526 CA SER A 278 7166 10556 5659 1008 728 285 C
ATOM 1527 C SER A 278 -10.179 -31.999 -5.198 1.00 64.33 C
ANISOU 1527 C SER A 278 7675 10780 5987 1173 728 254 C
ATOM 1528 O SER A 278 -9.686 -32.106 -6.320 1.00 63.44 O
ANISOU 1528 O SER A 278 7516 10785 5804 1205 731 207 O
ATOM 1529 CB SER A 278 -8.867 -30.873 -3.393 1.00 66.32 C
ANISOU 1529 CB SER A 278 7668 11383 6148 1165 729 269 C
ATOM 1530 OG SER A 278 -8.516 -29.653 -2.768 1.00 75.25 O
ANISOU 1530 OG SER A 278 8650 12674 7269 991 733 280 O
ATOM 1531 N ILE A 279 -10.893 -32.994 -4.597 1.00 60.60 N
ANISOU 1531 N ILE A 279 7409 10063 5555 1257 727 277 N
ATOM 1532 CA ILE A 279 -11.142 -34.316 -5.198 1.00 61.44 C
ANISOU 1532 CA ILE A 279 7739 9988 5618 1389 728 246 C
ATOM 1533 C ILE A 279 -11.921 -34.114 -6.466 1.00 66.62 C
ANISOU 1533 C ILE A 279 8410 10562 6341 1218 727 227 C
ATOM 1534 O ILE A 279 -11.633 -34.774 -7.471 1.00 68.48 O
ANISOU 1534 O ILE A 279 8717 10797 6504 1314 728 173 O
ATOM 1535 CB ILE A 279 -11.846 -35.305 -4.226 1.00 64.90 C
ANISOU 1535 CB ILE A 279 8435 10157 6066 1433 734 284 C
ATOM 1536 CG1 ILE A 279 -11.067 -35.475 -2.910 1.00 66.29 C
ANISOU 1536 CG1 ILE A 279 8603 10422 6163 1618 727 312 C
ATOM 1537 CG2 ILE A 279 -12.170 -36.671 -4.876 1.00 65.21 C
ANISOU 1537 CG2 ILE A 279 8777 9963 6038 1526 738 249 C
ATOM 1538 CD1 ILE A 279 -12.025 -35.753 -1.748 1.00 74.33 C
ANISOU 1538 CD1 ILE A 279 9786 11219 7239 1512 740 376 C
ATOM 1539 N GLY A 280 -12.860 -33.165 -6.425 1.00 62.13 N
ANISOU 1539 N GLY A 280 7767 9949 5891 990 721 264 N
ATOM 1540 CA GLY A 280 -13.655 -32.777 -7.583 1.00 61.17 C
ANISOU 1540 CA GLY A 280 7631 9787 5824 834 708 252 C
ATOM 1541 C GLY A 280 -12.807 -32.181 -8.691 1.00 64.61 C
ANISOU 1541 C GLY A 280 7938 10420 6192 836 703 224 C
ATOM 1542 O GLY A 280 -13.045 -32.486 -9.856 1.00 66.60 O
ANISOU 1542 O GLY A 280 8235 10649 6422 816 698 189 O
ATOM 1543 N TRP A 281 -11.796 -31.343 -8.334 1.00 59.69 N
ANISOU 1543 N TRP A 281 7155 10010 5515 838 710 233 N
ATOM 1544 CA TRP A 281 -10.867 -30.656 -9.240 1.00 59.95 C
ANISOU 1544 CA TRP A 281 7049 10279 5449 787 717 208 C
ATOM 1545 C TRP A 281 -9.769 -31.574 -9.770 1.00 65.87 C
ANISOU 1545 C TRP A 281 7764 11211 6054 993 736 134 C
ATOM 1546 O TRP A 281 -9.234 -31.319 -10.855 1.00 67.97 O
ANISOU 1546 O TRP A 281 7946 11647 6231 951 746 97 O
ATOM 1547 CB TRP A 281 -10.218 -29.452 -8.543 1.00 58.67 C
ANISOU 1547 CB TRP A 281 6747 10291 5255 665 723 235 C
ATOM 1548 CG TRP A 281 -11.063 -28.213 -8.588 1.00 59.01 C
ANISOU 1548 CG TRP A 281 6830 10207 5385 452 701 291 C
ATOM 1549 CD1 TRP A 281 -11.854 -27.717 -7.590 1.00 61.05 C
ANISOU 1549 CD1 TRP A 281 7136 10315 5743 402 685 333 C
ATOM 1550 CD2 TRP A 281 -11.229 -27.333 -9.707 1.00 58.96 C
ANISOU 1550 CD2 TRP A 281 6844 10207 5349 291 687 307 C
ATOM 1551 NE1 TRP A 281 -12.495 -26.576 -8.016 1.00 60.00 N
ANISOU 1551 NE1 TRP A 281 7060 10095 5643 251 657 368 N
ATOM 1552 CE2 TRP A 281 -12.138 -26.321 -9.314 1.00 62.29 C
ANISOU 1552 CE2 TRP A 281 7350 10464 5854 179 655 360 C
ATOM 1553 CE3 TRP A 281 -10.702 -27.300 -11.009 1.00 60.75 C
ANISOU 1553 CE3 TRP A 281 7042 10568 5473 243 697 281 C
ATOM 1554 CZ2 TRP A 281 -12.539 -25.297 -10.184 1.00 61.79 C
ANISOU 1554 CZ2 TRP A 281 7373 10339 5767 43 625 393 C
ATOM 1555 CZ3 TRP A 281 -11.067 -26.262 -11.852 1.00 62.12 C
ANISOU 1555 CZ3 TRP A 281 7288 10691 5626 67 674 321 C
ATOM 1556 CH2 TRP A 281 -11.972 -25.274 -11.439 1.00 62.15 C
ANISOU 1556 CH2 TRP A 281 7405 10503 5707 -21 635 380 C
ATOM 1557 N LEU A 282 -9.421 -32.625 -9.011 1.00 60.64 N
ANISOU 1557 N LEU A 282 7175 10519 5347 1229 738 111 N
ATOM 1558 CA LEU A 282 -8.380 -33.576 -9.397 1.00 61.06 C
ANISOU 1558 CA LEU A 282 7219 10744 5237 1504 747 30 C
ATOM 1559 C LEU A 282 -8.944 -34.799 -10.126 1.00 65.46 C
ANISOU 1559 C LEU A 282 8025 11057 5790 1632 742 -10 C
ATOM 1560 O LEU A 282 -8.156 -35.597 -10.642 1.00 67.72 O
ANISOU 1560 O LEU A 282 8339 11462 5931 1880 745 -90 O
ATOM 1561 CB LEU A 282 -7.565 -34.044 -8.178 1.00 61.75 C
ANISOU 1561 CB LEU A 282 7277 10954 5232 1748 741 21 C
ATOM 1562 CG LEU A 282 -6.636 -33.032 -7.521 1.00 64.62 C
ANISOU 1562 CG LEU A 282 7365 11661 5525 1673 749 23 C
ATOM 1563 CD1 LEU A 282 -6.593 -33.259 -6.023 1.00 64.61 C
ANISOU 1563 CD1 LEU A 282 7406 11608 5535 1792 733 63 C
ATOM 1564 CD2 LEU A 282 -5.253 -33.053 -8.142 1.00 62.94 C
ANISOU 1564 CD2 LEU A 282 6921 11893 5100 1809 763 -72 C
ATOM 1565 N ALA A 283 -10.280 -34.951 -10.205 1.00 59.81 N
ANISOU 1565 N ALA A 283 7487 10030 5209 1464 733 31 N
ATOM 1566 CA ALA A 283 -10.874 -36.091 -10.899 1.00 61.08 C
ANISOU 1566 CA ALA A 283 7903 9954 5350 1523 732 -15 C
ATOM 1567 C ALA A 283 -10.389 -36.206 -12.352 1.00 71.21 C
ANISOU 1567 C ALA A 283 9134 11383 6539 1569 737 -92 C
ATOM 1568 O ALA A 283 -10.147 -37.317 -12.821 1.00 73.96 O
ANISOU 1568 O ALA A 283 9671 11649 6783 1769 739 -165 O
ATOM 1569 CB ALA A 283 -12.382 -35.998 -10.871 1.00 60.23 C
ANISOU 1569 CB ALA A 283 7911 9593 5381 1267 724 30 C
ATOM 1570 N GLN A 284 -10.204 -35.064 -13.041 1.00 68.58 N
ANISOU 1570 N GLN A 284 8574 11262 6222 1392 739 -78 N
ATOM 1571 CA GLN A 284 -9.780 -34.968 -14.446 1.00 69.34 C
ANISOU 1571 CA GLN A 284 8593 11529 6225 1380 748 -139 C
ATOM 1572 C GLN A 284 -8.432 -35.651 -14.752 1.00 75.25 C
ANISOU 1572 C GLN A 284 9284 12530 6779 1679 768 -239 C
ATOM 1573 O GLN A 284 -8.170 -35.973 -15.912 1.00 76.60 O
ANISOU 1573 O GLN A 284 9464 12787 6854 1734 778 -313 O
ATOM 1574 CB GLN A 284 -9.693 -33.488 -14.870 1.00 69.66 C
ANISOU 1574 CB GLN A 284 8420 11761 6288 1127 749 -87 C
ATOM 1575 CG GLN A 284 -8.730 -32.655 -14.010 1.00 76.24 C
ANISOU 1575 CG GLN A 284 9050 12845 7071 1108 765 -60 C
ATOM 1576 CD GLN A 284 -8.636 -31.231 -14.472 1.00 91.75 C
ANISOU 1576 CD GLN A 284 10880 14956 9024 831 770 -11 C
ATOM 1577 OE1 GLN A 284 -8.194 -30.939 -15.596 1.00 86.63 O
ANISOU 1577 OE1 GLN A 284 10156 14495 8265 754 787 -44 O
ATOM 1578 NE2 GLN A 284 -9.037 -30.310 -13.598 1.00 79.17 N
ANISOU 1578 NE2 GLN A 284 9281 13273 7527 675 756 67 N
ATOM 1579 N PHE A 285 -7.584 -35.837 -13.739 1.00 71.75 N
ANISOU 1579 N PHE A 285 8767 12233 6262 1883 771 -247 N
ATOM 1580 CA PHE A 285 -6.254 -36.411 -13.913 1.00 73.70 C
ANISOU 1580 CA PHE A 285 8913 12794 6297 2210 783 -351 C
ATOM 1581 C PHE A 285 -6.268 -37.950 -13.931 1.00 81.11 C
ANISOU 1581 C PHE A 285 10168 13501 7148 2565 766 -421 C
ATOM 1582 O PHE A 285 -5.246 -38.555 -14.251 1.00 84.25 O
ANISOU 1582 O PHE A 285 10523 14139 7348 2898 768 -527 O
ATOM 1583 CB PHE A 285 -5.299 -35.866 -12.834 1.00 75.44 C
ANISOU 1583 CB PHE A 285 8888 13332 6444 2279 785 -338 C
ATOM 1584 CG PHE A 285 -5.231 -34.354 -12.858 1.00 75.11 C
ANISOU 1584 CG PHE A 285 8593 13490 6455 1907 805 -278 C
ATOM 1585 CD1 PHE A 285 -5.870 -33.599 -11.886 1.00 76.33 C
ANISOU 1585 CD1 PHE A 285 8764 13471 6765 1693 793 -175 C
ATOM 1586 CD2 PHE A 285 -4.598 -33.685 -13.901 1.00 76.74 C
ANISOU 1586 CD2 PHE A 285 8586 14028 6544 1756 837 -323 C
ATOM 1587 CE1 PHE A 285 -5.853 -32.200 -11.938 1.00 76.13 C
ANISOU 1587 CE1 PHE A 285 8580 13574 6774 1357 807 -122 C
ATOM 1588 CE2 PHE A 285 -4.574 -32.290 -13.946 1.00 78.24 C
ANISOU 1588 CE2 PHE A 285 8623 14345 6762 1388 854 -261 C
ATOM 1589 CZ PHE A 285 -5.223 -31.557 -12.979 1.00 74.93 C
ANISOU 1589 CZ PHE A 285 8260 13712 6496 1198 836 -160 C
ATOM 1590 N MET A 286 -7.415 -38.576 -13.655 1.00 77.61 N
ANISOU 1590 N MET A 286 10053 12609 6826 2489 751 -374 N
ATOM 1591 CA MET A 286 -7.557 -40.031 -13.698 1.00 80.31 C
ANISOU 1591 CA MET A 286 10784 12654 7075 2761 737 -434 C
ATOM 1592 C MET A 286 -7.702 -40.455 -15.129 1.00 88.11 C
ANISOU 1592 C MET A 286 11867 13611 8000 2756 747 -525 C
ATOM 1593 O MET A 286 -8.486 -39.843 -15.853 1.00 86.43 O
ANISOU 1593 O MET A 286 11580 13355 7904 2427 755 -495 O
ATOM 1594 CB MET A 286 -8.771 -40.486 -12.886 1.00 81.94 C
ANISOU 1594 CB MET A 286 11307 12416 7412 2594 728 -351 C
ATOM 1595 CG MET A 286 -8.584 -40.414 -11.385 1.00 85.04 C
ANISOU 1595 CG MET A 286 11704 12784 7823 2683 716 -275 C
ATOM 1596 SD MET A 286 -10.179 -40.760 -10.623 1.00 88.32 S
ANISOU 1596 SD MET A 286 12434 12731 8391 2373 721 -180 S
ATOM 1597 CE MET A 286 -10.201 -42.603 -10.712 1.00 88.17 C
ANISOU 1597 CE MET A 286 13002 12310 8188 2650 712 -246 C
ATOM 1598 N ASP A 287 -6.940 -41.480 -15.551 1.00 90.01 N
ANISOU 1598 N ASP A 287 12271 13887 8040 3143 742 -642 N
ATOM 1599 CA ASP A 287 -6.868 -41.990 -16.933 1.00 92.27 C
ANISOU 1599 CA ASP A 287 12653 14185 8220 3213 753 -756 C
ATOM 1600 C ASP A 287 -8.185 -41.814 -17.710 1.00 94.18 C
ANISOU 1600 C ASP A 287 13008 14163 8612 2806 759 -723 C
ATOM 1601 O ASP A 287 -9.221 -42.375 -17.330 1.00 94.76 O
ANISOU 1601 O ASP A 287 13403 13834 8767 2660 749 -684 O
ATOM 1602 CB ASP A 287 -6.409 -43.457 -16.954 1.00 98.14 C
ANISOU 1602 CB ASP A 287 13790 14738 8759 3670 734 -866 C
ATOM 1603 CG ASP A 287 -4.999 -43.643 -16.412 1.00119.17 C
ANISOU 1603 CG ASP A 287 16290 17765 11222 4145 719 -931 C
ATOM 1604 OD1 ASP A 287 -4.100 -42.862 -16.808 1.00121.90 O
ANISOU 1604 OD1 ASP A 287 16196 18629 11492 4175 739 -980 O
ATOM 1605 OD2 ASP A 287 -4.794 -44.565 -15.590 1.00129.14 O
ANISOU 1605 OD2 ASP A 287 17868 18815 12385 4481 686 -934 O
ATOM 1606 N GLY A 288 -8.138 -40.925 -18.704 1.00 87.03 N
ANISOU 1606 N GLY A 288 11809 13524 7733 2597 775 -729 N
ATOM 1607 CA GLY A 288 -9.264 -40.594 -19.571 1.00 84.85 C
ANISOU 1607 CA GLY A 288 11565 13102 7572 2238 772 -703 C
ATOM 1608 C GLY A 288 -10.524 -39.991 -18.961 1.00 85.62 C
ANISOU 1608 C GLY A 288 11669 12985 7875 1888 755 -581 C
ATOM 1609 O GLY A 288 -11.505 -39.809 -19.697 1.00 85.34 O
ANISOU 1609 O GLY A 288 11672 12843 7909 1626 744 -573 O
ATOM 1610 N ALA A 289 -10.526 -39.646 -17.634 1.00 78.08 N
ANISOU 1610 N ALA A 289 10660 12000 7007 1885 750 -492 N
ATOM 1611 CA ALA A 289 -11.705 -39.064 -16.971 1.00 74.90 C
ANISOU 1611 CA ALA A 289 10248 11427 6784 1582 737 -387 C
ATOM 1612 C ALA A 289 -12.063 -37.667 -17.495 1.00 74.65 C
ANISOU 1612 C ALA A 289 9928 11586 6850 1316 726 -324 C
ATOM 1613 O ALA A 289 -13.247 -37.390 -17.679 1.00 73.21 O
ANISOU 1613 O ALA A 289 9775 11272 6769 1075 705 -287 O
ATOM 1614 CB ALA A 289 -11.513 -39.005 -15.466 1.00 75.31 C
ANISOU 1614 CB ALA A 289 10305 11426 6882 1665 737 -316 C
ATOM 1615 N ARG A 290 -11.065 -36.789 -17.740 1.00 69.45 N
ANISOU 1615 N ARG A 290 9006 11245 6137 1355 737 -316 N
ATOM 1616 CA ARG A 290 -11.312 -35.425 -18.235 1.00 67.07 C
ANISOU 1616 CA ARG A 290 8495 11095 5894 1107 726 -249 C
ATOM 1617 C ARG A 290 -12.274 -35.431 -19.429 1.00 70.73 C
ANISOU 1617 C ARG A 290 9033 11465 6377 938 701 -265 C
ATOM 1618 O ARG A 290 -13.149 -34.577 -19.480 1.00 67.83 O
ANISOU 1618 O ARG A 290 8616 11048 6107 735 669 -193 O
ATOM 1619 CB ARG A 290 -10.000 -34.706 -18.596 1.00 64.96 C
ANISOU 1619 CB ARG A 290 7990 11192 5500 1147 754 -265 C
ATOM 1620 CG ARG A 290 -10.159 -33.191 -18.769 1.00 62.73 C
ANISOU 1620 CG ARG A 290 7550 11024 5262 879 744 -174 C
ATOM 1621 CD ARG A 290 -8.868 -32.516 -19.181 1.00 64.03 C
ANISOU 1621 CD ARG A 290 7504 11560 5265 849 783 -197 C
ATOM 1622 NE ARG A 290 -7.901 -32.421 -18.089 1.00 73.79 N
ANISOU 1622 NE ARG A 290 8601 12987 6449 951 808 -204 N
ATOM 1623 CZ ARG A 290 -6.848 -33.217 -17.946 1.00 89.55 C
ANISOU 1623 CZ ARG A 290 10511 15215 8300 1212 835 -300 C
ATOM 1624 NH1 ARG A 290 -6.615 -34.183 -18.823 1.00 79.13 N
ANISOU 1624 NH1 ARG A 290 9253 13938 6874 1409 845 -401 N
ATOM 1625 NH2 ARG A 290 -6.020 -33.052 -16.925 1.00 79.12 N
ANISOU 1625 NH2 ARG A 290 9041 14099 6921 1297 849 -305 N
ATOM 1626 N ARG A 291 -12.138 -36.406 -20.363 1.00 70.62 N
ANISOU 1626 N ARG A 291 9145 11432 6257 1042 711 -366 N
ATOM 1627 CA ARG A 291 -13.047 -36.499 -21.505 1.00 70.91 C
ANISOU 1627 CA ARG A 291 9255 11396 6293 883 686 -395 C
ATOM 1628 C ARG A 291 -14.411 -36.969 -21.040 1.00 73.90 C
ANISOU 1628 C ARG A 291 9802 11502 6774 743 660 -381 C
ATOM 1629 O ARG A 291 -15.414 -36.393 -21.441 1.00 73.93 O
ANISOU 1629 O ARG A 291 9747 11503 6838 542 622 -344 O
ATOM 1630 CB ARG A 291 -12.510 -37.410 -22.617 1.00 73.19 C
ANISOU 1630 CB ARG A 291 9646 11738 6426 1027 707 -518 C
ATOM 1631 N GLU A 292 -14.451 -37.968 -20.157 1.00 69.68 N
ANISOU 1631 N GLU A 292 9471 10762 6240 845 678 -408 N
ATOM 1632 CA GLU A 292 -15.700 -38.519 -19.638 1.00 69.67 C
ANISOU 1632 CA GLU A 292 9648 10519 6304 674 667 -404 C
ATOM 1633 C GLU A 292 -16.541 -37.445 -18.918 1.00 73.40 C
ANISOU 1633 C GLU A 292 9933 11040 6917 490 640 -302 C
ATOM 1634 O GLU A 292 -17.769 -37.496 -18.975 1.00 72.86 O
ANISOU 1634 O GLU A 292 9889 10908 6887 284 618 -306 O
ATOM 1635 CB GLU A 292 -15.387 -39.702 -18.701 1.00 72.26 C
ANISOU 1635 CB GLU A 292 10260 10615 6581 832 696 -433 C
ATOM 1636 CG GLU A 292 -16.569 -40.323 -17.969 1.00 81.76 C
ANISOU 1636 CG GLU A 292 11675 11568 7822 625 699 -422 C
ATOM 1637 CD GLU A 292 -17.752 -40.791 -18.799 1.00104.39 C
ANISOU 1637 CD GLU A 292 14664 14347 10654 354 688 -490 C
ATOM 1638 OE1 GLU A 292 -18.882 -40.757 -18.265 1.00 79.96 O
ANISOU 1638 OE1 GLU A 292 11567 11201 7612 101 685 -464 O
ATOM 1639 OE2 GLU A 292 -17.555 -41.220 -19.961 1.00108.58 O
ANISOU 1639 OE2 GLU A 292 15283 14884 11087 388 685 -577 O
ATOM 1640 N ILE A 293 -15.878 -36.459 -18.287 1.00 70.33 N
ANISOU 1640 N ILE A 293 9352 10788 6581 563 642 -223 N
ATOM 1641 CA ILE A 293 -16.530 -35.379 -17.536 1.00 68.69 C
ANISOU 1641 CA ILE A 293 8990 10617 6491 437 617 -133 C
ATOM 1642 C ILE A 293 -17.032 -34.247 -18.449 1.00 72.39 C
ANISOU 1642 C ILE A 293 9305 11227 6974 315 570 -99 C
ATOM 1643 O ILE A 293 -18.156 -33.797 -18.272 1.00 73.60 O
ANISOU 1643 O ILE A 293 9409 11366 7189 192 533 -71 O
ATOM 1644 CB ILE A 293 -15.569 -34.791 -16.440 1.00 70.60 C
ANISOU 1644 CB ILE A 293 9128 10933 6764 557 638 -70 C
ATOM 1645 CG1 ILE A 293 -15.083 -35.870 -15.442 1.00 70.41 C
ANISOU 1645 CG1 ILE A 293 9265 10776 6711 713 672 -92 C
ATOM 1646 CG2 ILE A 293 -16.215 -33.593 -15.702 1.00 70.88 C
ANISOU 1646 CG2 ILE A 293 9028 10997 6907 437 610 15 C
ATOM 1647 CD1 ILE A 293 -13.788 -35.531 -14.720 1.00 71.70 C
ANISOU 1647 CD1 ILE A 293 9319 11086 6837 895 692 -69 C
ATOM 1648 N VAL A 294 -16.203 -33.787 -19.392 1.00 66.99 N
ANISOU 1648 N VAL A 294 8550 10690 6213 359 571 -103 N
ATOM 1649 CA VAL A 294 -16.375 -32.585 -20.197 1.00 65.78 C
ANISOU 1649 CA VAL A 294 8287 10663 6043 266 530 -50 C
ATOM 1650 C VAL A 294 -16.931 -32.818 -21.643 1.00 70.81 C
ANISOU 1650 C VAL A 294 8958 11342 6603 197 496 -101 C
ATOM 1651 O VAL A 294 -17.446 -31.870 -22.261 1.00 69.20 O
ANISOU 1651 O VAL A 294 8699 11208 6386 120 443 -51 O
ATOM 1652 CB VAL A 294 -14.970 -31.931 -20.170 1.00 69.50 C
ANISOU 1652 CB VAL A 294 8666 11292 6448 322 565 -18 C
ATOM 1653 CG1 VAL A 294 -14.703 -31.006 -21.337 1.00 70.59 C
ANISOU 1653 CG1 VAL A 294 8754 11574 6494 230 546 14 C
ATOM 1654 CG2 VAL A 294 -14.730 -31.229 -18.847 1.00 68.01 C
ANISOU 1654 CG2 VAL A 294 8418 11087 6336 324 573 53 C
ATOM 1655 N CYS A 295 -16.848 -34.051 -22.162 1.00 69.34 N
ANISOU 1655 N CYS A 295 8887 11103 6355 236 522 -200 N
ATOM 1656 CA CYS A 295 -17.343 -34.369 -23.500 1.00 70.24 C
ANISOU 1656 CA CYS A 295 9041 11260 6385 164 494 -262 C
ATOM 1657 C CYS A 295 -18.587 -35.193 -23.436 1.00 71.92 C
ANISOU 1657 C CYS A 295 9355 11353 6618 49 474 -325 C
ATOM 1658 O CYS A 295 -18.708 -36.098 -22.601 1.00 72.13 O
ANISOU 1658 O CYS A 295 9514 11220 6671 56 508 -363 O
ATOM 1659 CB CYS A 295 -16.295 -35.102 -24.334 1.00 73.26 C
ANISOU 1659 CB CYS A 295 9487 11704 6642 276 539 -348 C
ATOM 1660 SG CYS A 295 -14.597 -34.522 -24.117 1.00 77.99 S
ANISOU 1660 SG CYS A 295 9959 12494 7180 423 593 -315 S
ATOM 1661 N ARG A 296 -19.467 -34.953 -24.412 1.00 66.60 N
ANISOU 1661 N ARG A 296 8637 10769 5899 -69 418 -345 N
ATOM 1662 CA ARG A 296 -20.656 -35.746 -24.699 1.00 65.88 C
ANISOU 1662 CA ARG A 296 8614 10642 5774 -226 395 -430 C
ATOM 1663 C ARG A 296 -20.169 -37.064 -25.327 1.00 72.16 C
ANISOU 1663 C ARG A 296 9622 11329 6468 -211 442 -548 C
ATOM 1664 O ARG A 296 -19.007 -37.144 -25.750 1.00 71.42 O
ANISOU 1664 O ARG A 296 9563 11252 6322 -53 477 -560 O
ATOM 1665 CB ARG A 296 -21.592 -34.991 -25.676 1.00 59.98 C
ANISOU 1665 CB ARG A 296 7730 10084 4976 -315 312 -421 C
ATOM 1666 CG ARG A 296 -22.479 -33.949 -25.044 1.00 48.14 C
ANISOU 1666 CG ARG A 296 6069 8676 3544 -331 252 -344 C
ATOM 1667 CD ARG A 296 -23.673 -33.647 -25.923 1.00 48.62 C
ANISOU 1667 CD ARG A 296 6024 8930 3520 -418 166 -380 C
ATOM 1668 NE ARG A 296 -24.717 -32.900 -25.216 1.00 60.29 N
ANISOU 1668 NE ARG A 296 7347 10521 5038 -410 107 -341 N
ATOM 1669 CZ ARG A 296 -25.202 -31.717 -25.592 1.00 79.97 C
ANISOU 1669 CZ ARG A 296 9729 13164 7494 -304 16 -277 C
ATOM 1670 NH1 ARG A 296 -24.747 -31.121 -26.687 1.00 75.45 N
ANISOU 1670 NH1 ARG A 296 9194 12631 6841 -231 -25 -232 N
ATOM 1671 NH2 ARG A 296 -26.141 -31.118 -24.872 1.00 68.39 N
ANISOU 1671 NH2 ARG A 296 8128 11807 6050 -258 -36 -259 N
ATOM 1672 N ALA A 297 -21.049 -38.070 -25.438 1.00 71.00 N
ANISOU 1672 N ALA A 297 9619 11090 6267 -380 443 -645 N
ATOM 1673 CA ALA A 297 -20.716 -39.362 -26.038 1.00 72.90 C
ANISOU 1673 CA ALA A 297 10124 11183 6390 -382 483 -769 C
ATOM 1674 C ALA A 297 -20.218 -39.208 -27.495 1.00 78.00 C
ANISOU 1674 C ALA A 297 10732 11971 6932 -316 466 -817 C
ATOM 1675 O ALA A 297 -19.369 -39.982 -27.953 1.00 78.88 O
ANISOU 1675 O ALA A 297 11024 11998 6951 -183 508 -899 O
ATOM 1676 CB ALA A 297 -21.938 -40.268 -25.998 1.00 75.27 C
ANISOU 1676 CB ALA A 297 10576 11394 6631 -659 479 -861 C
ATOM 1677 N ASP A 298 -20.716 -38.168 -28.188 1.00 74.09 N
ANISOU 1677 N ASP A 298 10012 11700 6440 -381 402 -763 N
ATOM 1678 CA ASP A 298 -20.441 -37.849 -29.596 1.00 74.21 C
ANISOU 1678 CA ASP A 298 9970 11880 6345 -359 375 -790 C
ATOM 1679 C ASP A 298 -19.190 -36.944 -29.811 1.00 75.84 C
ANISOU 1679 C ASP A 298 10061 12205 6551 -178 395 -703 C
ATOM 1680 O ASP A 298 -18.918 -36.525 -30.932 1.00 75.21 O
ANISOU 1680 O ASP A 298 9920 12282 6373 -174 375 -703 O
ATOM 1681 CB ASP A 298 -21.696 -37.209 -30.228 1.00 76.18 C
ANISOU 1681 CB ASP A 298 10064 12315 6564 -523 287 -776 C
ATOM 1682 CG ASP A 298 -22.429 -36.246 -29.309 1.00 87.38 C
ANISOU 1682 CG ASP A 298 11310 13798 8094 -544 239 -668 C
ATOM 1683 OD1 ASP A 298 -22.425 -35.047 -29.596 1.00 85.46 O
ANISOU 1683 OD1 ASP A 298 10924 13689 7857 -468 185 -567 O
ATOM 1684 OD2 ASP A 298 -22.997 -36.707 -28.286 1.00 97.95 O
ANISOU 1684 OD2 ASP A 298 12679 15040 9497 -633 258 -688 O
ATOM 1685 N GLY A 299 -18.422 -36.693 -28.764 1.00 71.95 N
ANISOU 1685 N GLY A 299 9545 11652 6143 -52 438 -637 N
ATOM 1686 CA GLY A 299 -17.215 -35.879 -28.879 1.00 71.43 C
ANISOU 1686 CA GLY A 299 9363 11728 6051 71 466 -569 C
ATOM 1687 C GLY A 299 -17.436 -34.378 -28.891 1.00 73.60 C
ANISOU 1687 C GLY A 299 9478 12123 6364 4 415 -431 C
ATOM 1688 O GLY A 299 -16.500 -33.604 -29.127 1.00 72.81 O
ANISOU 1688 O GLY A 299 9301 12152 6210 39 438 -371 O
ATOM 1689 N THR A 300 -18.681 -33.958 -28.655 1.00 68.80 N
ANISOU 1689 N THR A 300 8833 11484 5823 -95 346 -386 N
ATOM 1690 CA THR A 300 -19.038 -32.549 -28.572 1.00 66.91 C
ANISOU 1690 CA THR A 300 8496 11316 5610 -118 284 -259 C
ATOM 1691 C THR A 300 -18.950 -32.167 -27.095 1.00 69.93 C
ANISOU 1691 C THR A 300 8847 11597 6128 -75 303 -190 C
ATOM 1692 O THR A 300 -18.887 -33.047 -26.235 1.00 69.67 O
ANISOU 1692 O THR A 300 8859 11449 6164 -50 350 -243 O
ATOM 1693 CB THR A 300 -20.404 -32.298 -29.194 1.00 65.81 C
ANISOU 1693 CB THR A 300 8321 11250 5434 -193 189 -264 C
ATOM 1694 OG1 THR A 300 -21.355 -33.107 -28.512 1.00 68.54 O
ANISOU 1694 OG1 THR A 300 8665 11529 5846 -258 185 -338 O
ATOM 1695 CG2 THR A 300 -20.428 -32.582 -30.693 1.00 57.98 C
ANISOU 1695 CG2 THR A 300 7358 10378 4292 -238 166 -325 C
ATOM 1696 N MET A 301 -18.914 -30.884 -26.783 1.00 64.97 N
ANISOU 1696 N MET A 301 8173 10991 5522 -65 269 -75 N
ATOM 1697 CA MET A 301 -18.772 -30.570 -25.391 1.00 63.42 C
ANISOU 1697 CA MET A 301 7953 10703 5443 -26 292 -23 C
ATOM 1698 C MET A 301 -20.103 -30.605 -24.626 1.00 64.54 C
ANISOU 1698 C MET A 301 8056 10789 5676 -39 242 -27 C
ATOM 1699 O MET A 301 -21.185 -30.463 -25.188 1.00 63.29 O
ANISOU 1699 O MET A 301 7864 10704 5479 -69 171 -46 O
ATOM 1700 CB MET A 301 -18.009 -29.260 -25.181 1.00 65.94 C
ANISOU 1700 CB MET A 301 8270 11047 5738 -26 295 88 C
ATOM 1701 CG MET A 301 -18.727 -27.993 -25.540 1.00 70.30 C
ANISOU 1701 CG MET A 301 8861 11602 6249 -38 206 181 C
ATOM 1702 SD MET A 301 -17.443 -26.743 -25.802 1.00 76.09 S
ANISOU 1702 SD MET A 301 9677 12367 6868 -116 236 287 S
ATOM 1703 CE MET A 301 -16.481 -26.787 -24.094 1.00 72.05 C
ANISOU 1703 CE MET A 301 9102 11803 6470 -109 323 294 C
ATOM 1704 N ARG A 302 -19.974 -30.848 -23.326 1.00 60.96 N
ANISOU 1704 N ARG A 302 7595 10240 5329 -14 285 -20 N
ATOM 1705 CA ARG A 302 -21.045 -30.927 -22.360 1.00 60.84 C
ANISOU 1705 CA ARG A 302 7531 10188 5395 -35 261 -27 C
ATOM 1706 C ARG A 302 -21.696 -29.583 -22.225 1.00 68.68 C
ANISOU 1706 C ARG A 302 8463 11239 6392 16 183 51 C
ATOM 1707 O ARG A 302 -21.008 -28.572 -22.027 1.00 68.79 O
ANISOU 1707 O ARG A 302 8512 11219 6406 68 181 137 O
ATOM 1708 CB ARG A 302 -20.485 -31.400 -21.029 1.00 58.14 C
ANISOU 1708 CB ARG A 302 7218 9728 5145 -8 331 -23 C
ATOM 1709 CG ARG A 302 -21.198 -32.611 -20.516 1.00 67.97 C
ANISOU 1709 CG ARG A 302 8509 10903 6412 -91 358 -103 C
ATOM 1710 CD ARG A 302 -20.725 -33.937 -21.065 1.00 65.64 C
ANISOU 1710 CD ARG A 302 8363 10526 6053 -112 408 -191 C
ATOM 1711 NE ARG A 302 -21.570 -34.995 -20.521 1.00 65.26 N
ANISOU 1711 NE ARG A 302 8408 10385 6005 -242 430 -260 N
ATOM 1712 CZ ARG A 302 -21.153 -35.945 -19.700 1.00 75.34 C
ANISOU 1712 CZ ARG A 302 9849 11487 7291 -226 491 -281 C
ATOM 1713 NH1 ARG A 302 -19.875 -36.031 -19.369 1.00 66.61 N
ANISOU 1713 NH1 ARG A 302 8803 10311 6193 -47 531 -252 N
ATOM 1714 NH2 ARG A 302 -22.007 -36.837 -19.228 1.00 63.65 N
ANISOU 1714 NH2 ARG A 302 8481 9915 5786 -393 512 -336 N
ATOM 1715 N LEU A 303 -23.026 -29.557 -22.410 1.00 67.60 N
ANISOU 1715 N LEU A 303 8247 11209 6231 0 115 12 N
ATOM 1716 CA LEU A 303 -23.859 -28.350 -22.381 1.00 67.80 C
ANISOU 1716 CA LEU A 303 8217 11319 6225 106 20 65 C
ATOM 1717 C LEU A 303 -25.219 -28.688 -21.882 1.00 72.36 C
ANISOU 1717 C LEU A 303 8651 12034 6808 85 -14 -9 C
ATOM 1718 O LEU A 303 -25.737 -29.761 -22.210 1.00 72.89 O
ANISOU 1718 O LEU A 303 8671 12181 6844 -54 6 -106 O
ATOM 1719 CB LEU A 303 -23.988 -27.711 -23.787 1.00 68.88 C
ANISOU 1719 CB LEU A 303 8397 11546 6230 155 -60 95 C
ATOM 1720 CG LEU A 303 -22.749 -27.061 -24.387 1.00 73.75 C
ANISOU 1720 CG LEU A 303 9157 12071 6795 159 -39 182 C
ATOM 1721 CD1 LEU A 303 -22.951 -26.780 -25.842 1.00 75.26 C
ANISOU 1721 CD1 LEU A 303 9394 12361 6841 169 -108 193 C
ATOM 1722 CD2 LEU A 303 -22.309 -25.816 -23.594 1.00 76.15 C
ANISOU 1722 CD2 LEU A 303 9555 12254 7124 234 -47 288 C
ATOM 1723 N GLY A 304 -25.798 -27.759 -21.122 1.00 69.57 N
ANISOU 1723 N GLY A 304 8239 11722 6472 213 -64 29 N
ATOM 1724 CA GLY A 304 -27.137 -27.883 -20.548 1.00 70.41 C
ANISOU 1724 CA GLY A 304 8167 12025 6560 221 -101 -45 C
ATOM 1725 C GLY A 304 -27.402 -29.197 -19.846 1.00 73.34 C
ANISOU 1725 C GLY A 304 8477 12409 6980 11 -14 -132 C
ATOM 1726 O GLY A 304 -28.470 -29.783 -19.982 1.00 74.52 O
ANISOU 1726 O GLY A 304 8487 12773 7056 -106 -32 -230 O
ATOM 1727 N GLU A 305 -26.400 -29.691 -19.155 1.00 69.17 N
ANISOU 1727 N GLU A 305 8071 11660 6552 -50 79 -98 N
ATOM 1728 CA GLU A 305 -26.458 -30.906 -18.377 1.00 69.62 C
ANISOU 1728 CA GLU A 305 8154 11651 6647 -228 165 -157 C
ATOM 1729 C GLU A 305 -27.279 -30.551 -17.087 1.00 73.95 C
ANISOU 1729 C GLU A 305 8567 12302 7228 -214 167 -164 C
ATOM 1730 O GLU A 305 -27.185 -29.402 -16.652 1.00 72.61 O
ANISOU 1730 O GLU A 305 8363 12131 7094 -30 126 -99 O
ATOM 1731 CB GLU A 305 -25.001 -31.349 -18.116 1.00 69.97 C
ANISOU 1731 CB GLU A 305 8381 11441 6764 -212 245 -107 C
ATOM 1732 CG GLU A 305 -24.795 -32.800 -17.728 1.00 84.46 C
ANISOU 1732 CG GLU A 305 10349 13143 8599 -365 328 -165 C
ATOM 1733 CD GLU A 305 -24.912 -33.861 -18.800 1.00101.61 C
ANISOU 1733 CD GLU A 305 12624 15306 10678 -499 338 -253 C
ATOM 1734 OE1 GLU A 305 -25.516 -34.920 -18.508 1.00106.98 O
ANISOU 1734 OE1 GLU A 305 13378 15960 11310 -696 377 -329 O
ATOM 1735 OE2 GLU A 305 -24.356 -33.663 -19.906 1.00 80.21 O
ANISOU 1735 OE2 GLU A 305 9944 12602 7928 -427 313 -248 O
ATOM 1736 N PRO A 306 -28.190 -31.404 -16.536 1.00 72.24 N
ANISOU 1736 N PRO A 306 8271 12206 6972 -409 205 -249 N
ATOM 1737 CA PRO A 306 -28.470 -32.809 -16.888 1.00 73.18 C
ANISOU 1737 CA PRO A 306 8470 12316 7021 -681 258 -339 C
ATOM 1738 C PRO A 306 -29.310 -32.935 -18.159 1.00 78.79 C
ANISOU 1738 C PRO A 306 9070 13267 7601 -763 191 -425 C
ATOM 1739 O PRO A 306 -30.291 -32.209 -18.360 1.00 77.88 O
ANISOU 1739 O PRO A 306 8727 13452 7413 -685 111 -459 O
ATOM 1740 CB PRO A 306 -29.193 -33.359 -15.636 1.00 75.17 C
ANISOU 1740 CB PRO A 306 8664 12641 7258 -865 318 -384 C
ATOM 1741 CG PRO A 306 -29.083 -32.283 -14.570 1.00 77.84 C
ANISOU 1741 CG PRO A 306 8905 12987 7686 -657 306 -310 C
ATOM 1742 CD PRO A 306 -28.964 -31.008 -15.342 1.00 73.24 C
ANISOU 1742 CD PRO A 306 8245 12474 7110 -391 209 -262 C
ATOM 1743 N THR A 307 -28.878 -33.852 -19.033 1.00 78.33 N
ANISOU 1743 N THR A 307 9180 13082 7499 -894 219 -466 N
ATOM 1744 CA THR A 307 -29.515 -34.125 -20.319 1.00 81.06 C
ANISOU 1744 CA THR A 307 9459 13628 7713 -1000 164 -554 C
ATOM 1745 C THR A 307 -29.537 -35.638 -20.609 1.00 87.60 C
ANISOU 1745 C THR A 307 10489 14334 8461 -1306 237 -652 C
ATOM 1746 O THR A 307 -28.646 -36.370 -20.165 1.00 87.73 O
ANISOU 1746 O THR A 307 10763 14036 8536 -1331 317 -625 O
ATOM 1747 CB THR A 307 -28.867 -33.311 -21.451 1.00 91.54 C
ANISOU 1747 CB THR A 307 10803 14935 9044 -773 94 -491 C
ATOM 1748 OG1 THR A 307 -29.552 -33.634 -22.661 1.00102.41 O
ANISOU 1748 OG1 THR A 307 12110 16521 10278 -887 40 -583 O
ATOM 1749 CG2 THR A 307 -27.348 -33.536 -21.589 1.00 82.03 C
ANISOU 1749 CG2 THR A 307 9834 13408 7925 -679 153 -418 C
ATOM 1750 N SER A 308 -30.562 -36.086 -21.360 1.00 85.52 N
ANISOU 1750 N SER A 308 10121 14329 8045 -1528 204 -771 N
ATOM 1751 CA SER A 308 -30.820 -37.486 -21.701 1.00 87.50 C
ANISOU 1751 CA SER A 308 10569 14503 8175 -1875 264 -887 C
ATOM 1752 C SER A 308 -29.628 -38.183 -22.367 1.00 91.54 C
ANISOU 1752 C SER A 308 11415 14658 8710 -1820 305 -877 C
ATOM 1753 O SER A 308 -28.810 -37.523 -23.007 1.00 90.27 O
ANISOU 1753 O SER A 308 11245 14441 8613 -1553 266 -807 O
ATOM 1754 CB SER A 308 -32.041 -37.592 -22.612 1.00 94.07 C
ANISOU 1754 CB SER A 308 11184 15733 8824 -2083 200 -1016 C
ATOM 1755 OG SER A 308 -33.260 -37.349 -21.926 1.00104.33 O
ANISOU 1755 OG SER A 308 12190 17405 10044 -2217 183 -1073 O
ATOM 1756 N ASN A 309 -29.540 -39.529 -22.188 1.00 90.00 N
ANISOU 1756 N ASN A 309 11531 14226 8438 -2079 386 -951 N
ATOM 1757 CA ASN A 309 -28.562 -40.503 -22.732 1.00 90.36 C
ANISOU 1757 CA ASN A 309 11956 13924 8454 -2060 435 -981 C
ATOM 1758 C ASN A 309 -27.118 -40.334 -22.205 1.00 92.23 C
ANISOU 1758 C ASN A 309 12356 13856 8830 -1725 471 -868 C
ATOM 1759 O ASN A 309 -26.385 -41.329 -22.113 1.00 94.07 O
ANISOU 1759 O ASN A 309 12943 13773 9027 -1711 530 -894 O
ATOM 1760 CB ASN A 309 -28.520 -40.498 -24.268 1.00 92.22 C
ANISOU 1760 CB ASN A 309 12166 14273 8601 -2040 381 -1050 C
ATOM 1761 CG ASN A 309 -29.848 -40.346 -24.976 1.00118.56 C
ANISOU 1761 CG ASN A 309 15247 18003 11798 -2282 316 -1150 C
ATOM 1762 OD1 ASN A 309 -30.938 -40.384 -24.370 1.00108.47 O
ANISOU 1762 OD1 ASN A 309 13804 16954 10456 -2523 317 -1198 O
ATOM 1763 ND2 ASN A 309 -29.771 -40.145 -26.291 1.00111.99 N
ANISOU 1763 ND2 ASN A 309 14357 17295 10899 -2214 256 -1190 N
ATOM 1764 N GLU A 310 -26.704 -39.094 -21.890 1.00 83.78 N
ANISOU 1764 N GLU A 310 11046 12893 7895 -1453 432 -754 N
ATOM 1765 CA GLU A 310 -25.362 -38.766 -21.404 1.00 80.22 C
ANISOU 1765 CA GLU A 310 10679 12242 7561 -1156 460 -652 C
ATOM 1766 C GLU A 310 -25.115 -39.394 -20.040 1.00 82.92 C
ANISOU 1766 C GLU A 310 11212 12355 7940 -1185 530 -621 C
ATOM 1767 O GLU A 310 -26.075 -39.751 -19.357 1.00 83.66 O
ANISOU 1767 O GLU A 310 11305 12489 7994 -1430 551 -653 O
ATOM 1768 CB GLU A 310 -25.176 -37.238 -21.334 1.00 79.04 C
ANISOU 1768 CB GLU A 310 10239 12275 7516 -937 401 -544 C
ATOM 1769 CG GLU A 310 -25.570 -36.498 -22.602 1.00 81.81 C
ANISOU 1769 CG GLU A 310 10410 12863 7812 -906 320 -558 C
ATOM 1770 CD GLU A 310 -24.767 -36.831 -23.843 1.00 92.84 C
ANISOU 1770 CD GLU A 310 11930 14202 9143 -834 320 -590 C
ATOM 1771 OE1 GLU A 310 -23.553 -37.107 -23.702 1.00 63.99 O
ANISOU 1771 OE1 GLU A 310 8427 10365 5521 -684 372 -563 O
ATOM 1772 OE2 GLU A 310 -25.344 -36.799 -24.956 1.00 90.50 O
ANISOU 1772 OE2 GLU A 310 11561 14075 8749 -913 266 -648 O
ATOM 1773 N THR A 311 -23.839 -39.552 -19.649 1.00 77.87 N
ANISOU 1773 N THR A 311 10730 11504 7353 -942 566 -565 N
ATOM 1774 CA THR A 311 -23.503 -40.117 -18.337 1.00 77.27 C
ANISOU 1774 CA THR A 311 10850 11208 7301 -920 623 -525 C
ATOM 1775 C THR A 311 -23.691 -39.064 -17.224 1.00 80.58 C
ANISOU 1775 C THR A 311 11014 11758 7846 -860 612 -425 C
ATOM 1776 O THR A 311 -23.863 -37.870 -17.497 1.00 78.36 O
ANISOU 1776 O THR A 311 10442 11699 7632 -783 559 -383 O
ATOM 1777 CB THR A 311 -22.088 -40.726 -18.298 1.00 77.64 C
ANISOU 1777 CB THR A 311 11154 11018 7326 -647 657 -516 C
ATOM 1778 OG1 THR A 311 -21.115 -39.773 -18.730 1.00 76.12 O
ANISOU 1778 OG1 THR A 311 10750 10971 7203 -384 629 -462 O
ATOM 1779 CG2 THR A 311 -21.975 -41.997 -19.095 1.00 74.82 C
ANISOU 1779 CG2 THR A 311 11145 10462 6821 -703 679 -626 C
ATOM 1780 N LEU A 312 -23.675 -39.525 -15.965 1.00 79.04 N
ANISOU 1780 N LEU A 312 10960 11408 7662 -894 661 -390 N
ATOM 1781 CA LEU A 312 -23.831 -38.651 -14.807 1.00 77.72 C
ANISOU 1781 CA LEU A 312 10587 11343 7600 -843 659 -306 C
ATOM 1782 C LEU A 312 -22.534 -37.932 -14.479 1.00 79.89 C
ANISOU 1782 C LEU A 312 10798 11587 7969 -528 652 -220 C
ATOM 1783 O LEU A 312 -22.583 -36.912 -13.796 1.00 79.67 O
ANISOU 1783 O LEU A 312 10564 11676 8032 -460 636 -153 O
ATOM 1784 CB LEU A 312 -24.321 -39.438 -13.593 1.00 78.88 C
ANISOU 1784 CB LEU A 312 10913 11357 7702 -1031 717 -303 C
ATOM 1785 CG LEU A 312 -25.812 -39.658 -13.553 1.00 85.39 C
ANISOU 1785 CG LEU A 312 11649 12352 8444 -1388 724 -374 C
ATOM 1786 CD1 LEU A 312 -26.138 -41.134 -13.453 1.00 88.41 C
ANISOU 1786 CD1 LEU A 312 12419 12501 8672 -1669 786 -438 C
ATOM 1787 CD2 LEU A 312 -26.443 -38.874 -12.429 1.00 87.68 C
ANISOU 1787 CD2 LEU A 312 11685 12836 8796 -1426 727 -329 C
ATOM 1788 N SER A 313 -21.387 -38.442 -14.980 1.00 75.16 N
ANISOU 1788 N SER A 313 10370 10858 7329 -342 664 -232 N
ATOM 1789 CA SER A 313 -20.024 -37.937 -14.764 1.00 73.21 C
ANISOU 1789 CA SER A 313 10065 10627 7126 -59 665 -174 C
ATOM 1790 C SER A 313 -19.938 -36.407 -14.687 1.00 74.12 C
ANISOU 1790 C SER A 313 9870 10953 7340 -5 628 -104 C
ATOM 1791 O SER A 313 -19.422 -35.890 -13.686 1.00 72.46 O
ANISOU 1791 O SER A 313 9589 10755 7189 96 638 -39 O
ATOM 1792 CB SER A 313 -19.083 -38.457 -15.841 1.00 76.32 C
ANISOU 1792 CB SER A 313 10578 10987 7433 102 668 -231 C
ATOM 1793 OG SER A 313 -19.079 -39.874 -15.824 1.00 84.20 O
ANISOU 1793 OG SER A 313 11926 11744 8322 93 700 -298 O
ATOM 1794 N CYS A 314 -20.502 -35.694 -15.679 1.00 70.08 N
ANISOU 1794 N CYS A 314 9202 10594 6830 -80 581 -118 N
ATOM 1795 CA CYS A 314 -20.487 -34.233 -15.688 1.00 69.49 C
ANISOU 1795 CA CYS A 314 8907 10676 6820 -29 537 -50 C
ATOM 1796 C CYS A 314 -21.126 -33.666 -14.413 1.00 69.96 C
ANISOU 1796 C CYS A 314 8869 10757 6956 -66 535 -3 C
ATOM 1797 O CYS A 314 -20.447 -32.946 -13.669 1.00 68.04 O
ANISOU 1797 O CYS A 314 8566 10519 6765 39 540 61 O
ATOM 1798 CB CYS A 314 -21.160 -33.680 -16.942 1.00 71.21 C
ANISOU 1798 CB CYS A 314 9023 11032 6999 -92 478 -73 C
ATOM 1799 SG CYS A 314 -21.130 -31.863 -17.077 1.00 74.83 S
ANISOU 1799 SG CYS A 314 9305 11629 7498 -11 414 16 S
ATOM 1800 N VAL A 315 -22.402 -34.037 -14.139 1.00 65.69 N
ANISOU 1800 N VAL A 315 8310 10247 6402 -229 531 -46 N
ATOM 1801 CA VAL A 315 -23.155 -33.555 -12.978 1.00 64.40 C
ANISOU 1801 CA VAL A 315 8033 10148 6288 -273 531 -21 C
ATOM 1802 C VAL A 315 -22.510 -33.988 -11.641 1.00 65.86 C
ANISOU 1802 C VAL A 315 8328 10187 6510 -229 590 22 C
ATOM 1803 O VAL A 315 -22.571 -33.195 -10.699 1.00 65.23 O
ANISOU 1803 O VAL A 315 8140 10155 6488 -176 587 69 O
ATOM 1804 CB VAL A 315 -24.676 -33.868 -13.005 1.00 69.62 C
ANISOU 1804 CB VAL A 315 8609 10951 6893 -477 520 -92 C
ATOM 1805 CG1 VAL A 315 -25.280 -33.565 -14.374 1.00 70.02 C
ANISOU 1805 CG1 VAL A 315 8554 11169 6883 -505 454 -142 C
ATOM 1806 CG2 VAL A 315 -24.999 -35.292 -12.556 1.00 70.64 C
ANISOU 1806 CG2 VAL A 315 8933 10953 6954 -685 587 -143 C
ATOM 1807 N ILE A 316 -21.879 -35.201 -11.559 1.00 60.17 N
ANISOU 1807 N ILE A 316 7838 9285 5739 -227 638 5 N
ATOM 1808 CA ILE A 316 -21.225 -35.656 -10.325 1.00 58.71 C
ANISOU 1808 CA ILE A 316 7783 8962 5562 -150 684 49 C
ATOM 1809 C ILE A 316 -20.077 -34.711 -10.024 1.00 61.97 C
ANISOU 1809 C ILE A 316 8079 9434 6033 58 671 110 C
ATOM 1810 O ILE A 316 -19.983 -34.233 -8.896 1.00 62.05 O
ANISOU 1810 O ILE A 316 8023 9461 6090 90 681 158 O
ATOM 1811 CB ILE A 316 -20.787 -37.157 -10.313 1.00 62.24 C
ANISOU 1811 CB ILE A 316 8555 9182 5912 -143 726 17 C
ATOM 1812 CG1 ILE A 316 -22.027 -38.071 -10.158 1.00 64.08 C
ANISOU 1812 CG1 ILE A 316 8942 9337 6070 -432 756 -34 C
ATOM 1813 CG2 ILE A 316 -19.779 -37.449 -9.173 1.00 59.72 C
ANISOU 1813 CG2 ILE A 316 8357 8747 5587 45 754 74 C
ATOM 1814 CD1 ILE A 316 -21.851 -39.521 -10.589 1.00 71.22 C
ANISOU 1814 CD1 ILE A 316 10220 9995 6844 -488 787 -90 C
ATOM 1815 N ILE A 317 -19.270 -34.363 -11.039 1.00 57.75 N
ANISOU 1815 N ILE A 317 7503 8959 5481 167 649 104 N
ATOM 1816 CA ILE A 317 -18.137 -33.459 -10.833 1.00 55.61 C
ANISOU 1816 CA ILE A 317 7117 8781 5230 310 643 151 C
ATOM 1817 C ILE A 317 -18.658 -32.090 -10.470 1.00 56.79 C
ANISOU 1817 C ILE A 317 7099 9028 5451 257 610 196 C
ATOM 1818 O ILE A 317 -18.154 -31.505 -9.516 1.00 55.47 O
ANISOU 1818 O ILE A 317 6879 8883 5314 310 620 240 O
ATOM 1819 CB ILE A 317 -17.159 -33.460 -12.025 1.00 58.65 C
ANISOU 1819 CB ILE A 317 7495 9242 5548 402 638 124 C
ATOM 1820 CG1 ILE A 317 -16.412 -34.816 -12.138 1.00 59.43 C
ANISOU 1820 CG1 ILE A 317 7780 9244 5556 538 671 73 C
ATOM 1821 CG2 ILE A 317 -16.189 -32.283 -11.999 1.00 59.09 C
ANISOU 1821 CG2 ILE A 317 7399 9451 5601 459 631 168 C
ATOM 1822 CD1 ILE A 317 -15.908 -35.483 -10.846 1.00 60.86 C
ANISOU 1822 CD1 ILE A 317 8080 9328 5718 665 701 93 C
ATOM 1823 N PHE A 318 -19.731 -31.635 -11.129 1.00 53.50 N
ANISOU 1823 N PHE A 318 6617 8666 5045 163 569 179 N
ATOM 1824 CA PHE A 318 -20.335 -30.359 -10.781 1.00 52.82 C
ANISOU 1824 CA PHE A 318 6409 8657 5003 160 528 212 C
ATOM 1825 C PHE A 318 -20.772 -30.352 -9.278 1.00 58.51 C
ANISOU 1825 C PHE A 318 7103 9356 5771 145 553 226 C
ATOM 1826 O PHE A 318 -20.275 -29.532 -8.501 1.00 57.25 O
ANISOU 1826 O PHE A 318 6908 9203 5644 207 553 268 O
ATOM 1827 CB PHE A 318 -21.506 -30.032 -11.711 1.00 54.58 C
ANISOU 1827 CB PHE A 318 6567 8971 5200 106 470 178 C
ATOM 1828 CG PHE A 318 -22.394 -28.958 -11.129 1.00 56.43 C
ANISOU 1828 CG PHE A 318 6696 9286 5458 144 426 192 C
ATOM 1829 CD1 PHE A 318 -21.938 -27.649 -10.996 1.00 59.24 C
ANISOU 1829 CD1 PHE A 318 7057 9627 5822 240 392 248 C
ATOM 1830 CD2 PHE A 318 -23.672 -29.264 -10.667 1.00 58.70 C
ANISOU 1830 CD2 PHE A 318 6894 9672 5738 78 421 141 C
ATOM 1831 CE1 PHE A 318 -22.750 -26.667 -10.426 1.00 59.94 C
ANISOU 1831 CE1 PHE A 318 7091 9767 5917 316 347 251 C
ATOM 1832 CE2 PHE A 318 -24.487 -28.277 -10.107 1.00 60.90 C
ANISOU 1832 CE2 PHE A 318 7063 10058 6019 158 379 138 C
ATOM 1833 CZ PHE A 318 -24.009 -26.996 -9.965 1.00 58.58 C
ANISOU 1833 CZ PHE A 318 6805 9714 5740 298 340 194 C
ATOM 1834 N VAL A 319 -21.656 -31.290 -8.880 1.00 57.41 N
ANISOU 1834 N VAL A 319 6996 9198 5618 38 581 186 N
ATOM 1835 CA VAL A 319 -22.172 -31.420 -7.509 1.00 57.67 C
ANISOU 1835 CA VAL A 319 7009 9230 5672 -10 613 193 C
ATOM 1836 C VAL A 319 -20.991 -31.449 -6.490 1.00 61.81 C
ANISOU 1836 C VAL A 319 7601 9663 6220 92 649 248 C
ATOM 1837 O VAL A 319 -20.946 -30.566 -5.630 1.00 60.86 O
ANISOU 1837 O VAL A 319 7398 9588 6139 139 643 277 O
ATOM 1838 CB VAL A 319 -23.128 -32.635 -7.339 1.00 62.33 C
ANISOU 1838 CB VAL A 319 7670 9806 6205 -198 651 141 C
ATOM 1839 CG1 VAL A 319 -23.494 -32.840 -5.864 1.00 62.24 C
ANISOU 1839 CG1 VAL A 319 7662 9792 6196 -263 697 157 C
ATOM 1840 CG2 VAL A 319 -24.396 -32.469 -8.190 1.00 62.57 C
ANISOU 1840 CG2 VAL A 319 7570 10011 6194 -311 612 73 C
ATOM 1841 N ILE A 320 -20.020 -32.401 -6.631 1.00 57.32 N
ANISOU 1841 N ILE A 320 7180 8987 5611 150 678 254 N
ATOM 1842 CA ILE A 320 -18.842 -32.476 -5.756 1.00 55.60 C
ANISOU 1842 CA ILE A 320 7005 8734 5385 281 702 295 C
ATOM 1843 C ILE A 320 -18.217 -31.088 -5.626 1.00 57.99 C
ANISOU 1843 C ILE A 320 7158 9152 5726 344 676 326 C
ATOM 1844 O ILE A 320 -18.156 -30.563 -4.531 1.00 58.42 O
ANISOU 1844 O ILE A 320 7164 9228 5806 356 684 354 O
ATOM 1845 CB ILE A 320 -17.773 -33.516 -6.226 1.00 59.27 C
ANISOU 1845 CB ILE A 320 7622 9124 5772 408 718 281 C
ATOM 1846 CG1 ILE A 320 -18.328 -34.951 -6.306 1.00 60.70 C
ANISOU 1846 CG1 ILE A 320 8042 9132 5890 342 745 250 C
ATOM 1847 CG2 ILE A 320 -16.527 -33.482 -5.318 1.00 60.09 C
ANISOU 1847 CG2 ILE A 320 7720 9268 5844 578 731 315 C
ATOM 1848 CD1 ILE A 320 -17.398 -35.945 -7.128 1.00 65.68 C
ANISOU 1848 CD1 ILE A 320 8853 9677 6424 499 749 212 C
ATOM 1849 N VAL A 321 -17.802 -30.484 -6.740 1.00 53.73 N
ANISOU 1849 N VAL A 321 6566 8678 5172 359 647 320 N
ATOM 1850 CA VAL A 321 -17.119 -29.185 -6.772 1.00 52.30 C
ANISOU 1850 CA VAL A 321 6298 8585 4989 373 627 349 C
ATOM 1851 C VAL A 321 -17.993 -28.048 -6.192 1.00 55.30 C
ANISOU 1851 C VAL A 321 6629 8963 5420 330 597 366 C
ATOM 1852 O VAL A 321 -17.561 -27.415 -5.221 1.00 54.97 O
ANISOU 1852 O VAL A 321 6563 8937 5384 341 606 388 O
ATOM 1853 CB VAL A 321 -16.611 -28.846 -8.212 1.00 55.42 C
ANISOU 1853 CB VAL A 321 6684 9041 5331 361 606 340 C
ATOM 1854 CG1 VAL A 321 -16.256 -27.370 -8.358 1.00 55.22 C
ANISOU 1854 CG1 VAL A 321 6625 9073 5285 308 580 373 C
ATOM 1855 CG2 VAL A 321 -15.424 -29.723 -8.605 1.00 54.85 C
ANISOU 1855 CG2 VAL A 321 6630 9029 5183 446 638 314 C
ATOM 1856 N TYR A 322 -19.193 -27.782 -6.782 1.00 50.20 N
ANISOU 1856 N TYR A 322 5967 8316 4791 298 559 346 N
ATOM 1857 CA TYR A 322 -20.046 -26.655 -6.393 1.00 48.72 C
ANISOU 1857 CA TYR A 322 5742 8148 4623 318 518 348 C
ATOM 1858 C TYR A 322 -20.561 -26.769 -4.961 1.00 55.10 C
ANISOU 1858 C TYR A 322 6507 8964 5466 321 546 339 C
ATOM 1859 O TYR A 322 -20.536 -25.775 -4.249 1.00 55.70 O
ANISOU 1859 O TYR A 322 6580 9036 5548 363 532 351 O
ATOM 1860 CB TYR A 322 -21.207 -26.472 -7.369 1.00 48.99 C
ANISOU 1860 CB TYR A 322 5743 8234 4638 324 464 316 C
ATOM 1861 CG TYR A 322 -22.121 -25.303 -7.062 1.00 51.06 C
ANISOU 1861 CG TYR A 322 5975 8537 4890 411 408 306 C
ATOM 1862 CD1 TYR A 322 -21.879 -24.043 -7.597 1.00 53.69 C
ANISOU 1862 CD1 TYR A 322 6402 8818 5179 482 351 339 C
ATOM 1863 CD2 TYR A 322 -23.253 -25.466 -6.268 1.00 52.26 C
ANISOU 1863 CD2 TYR A 322 6023 8784 5050 428 411 259 C
ATOM 1864 CE1 TYR A 322 -22.741 -22.971 -7.348 1.00 55.43 C
ANISOU 1864 CE1 TYR A 322 6642 9052 5366 614 289 325 C
ATOM 1865 CE2 TYR A 322 -24.089 -24.390 -5.968 1.00 53.86 C
ANISOU 1865 CE2 TYR A 322 6191 9051 5222 560 355 235 C
ATOM 1866 CZ TYR A 322 -23.844 -23.149 -6.531 1.00 61.69 C
ANISOU 1866 CZ TYR A 322 7306 9963 6171 675 289 267 C
ATOM 1867 OH TYR A 322 -24.700 -22.101 -6.271 1.00 63.12 O
ANISOU 1867 OH TYR A 322 7498 10187 6299 854 224 238 O
ATOM 1868 N TYR A 323 -21.055 -27.931 -4.535 1.00 52.70 N
ANISOU 1868 N TYR A 323 6194 8662 5167 263 586 316 N
ATOM 1869 CA TYR A 323 -21.562 -28.050 -3.173 1.00 52.29 C
ANISOU 1869 CA TYR A 323 6106 8633 5128 243 619 311 C
ATOM 1870 C TYR A 323 -20.417 -27.832 -2.182 1.00 57.60 C
ANISOU 1870 C TYR A 323 6818 9259 5811 291 646 354 C
ATOM 1871 O TYR A 323 -20.545 -26.982 -1.296 1.00 57.26 O
ANISOU 1871 O TYR A 323 6735 9242 5779 323 641 356 O
ATOM 1872 CB TYR A 323 -22.239 -29.411 -2.961 1.00 53.67 C
ANISOU 1872 CB TYR A 323 6314 8803 5276 122 665 284 C
ATOM 1873 CG TYR A 323 -22.935 -29.560 -1.627 1.00 55.88 C
ANISOU 1873 CG TYR A 323 6551 9137 5544 60 704 274 C
ATOM 1874 CD1 TYR A 323 -22.210 -29.826 -0.464 1.00 57.01 C
ANISOU 1874 CD1 TYR A 323 6764 9207 5688 83 745 318 C
ATOM 1875 CD2 TYR A 323 -24.320 -29.477 -1.529 1.00 57.54 C
ANISOU 1875 CD2 TYR A 323 6636 9505 5720 -24 702 214 C
ATOM 1876 CE1 TYR A 323 -22.844 -29.969 0.766 1.00 55.97 C
ANISOU 1876 CE1 TYR A 323 6601 9131 5533 14 785 312 C
ATOM 1877 CE2 TYR A 323 -24.962 -29.606 -0.299 1.00 59.04 C
ANISOU 1877 CE2 TYR A 323 6770 9783 5880 -98 747 197 C
ATOM 1878 CZ TYR A 323 -24.217 -29.859 0.841 1.00 64.73 C
ANISOU 1878 CZ TYR A 323 7586 10399 6610 -86 790 250 C
ATOM 1879 OH TYR A 323 -24.831 -30.043 2.041 1.00 69.16 O
ANISOU 1879 OH TYR A 323 8106 11045 7128 -175 839 238 O
ATOM 1880 N ALA A 324 -19.281 -28.549 -2.372 1.00 55.33 N
ANISOU 1880 N ALA A 324 6601 8923 5499 314 670 378 N
ATOM 1881 CA ALA A 324 -18.128 -28.463 -1.474 1.00 55.53 C
ANISOU 1881 CA ALA A 324 6635 8958 5504 372 691 409 C
ATOM 1882 C ALA A 324 -17.606 -27.026 -1.305 1.00 60.47 C
ANISOU 1882 C ALA A 324 7209 9637 6130 376 666 417 C
ATOM 1883 O ALA A 324 -17.376 -26.623 -0.175 1.00 61.24 O
ANISOU 1883 O ALA A 324 7286 9756 6225 382 678 425 O
ATOM 1884 CB ALA A 324 -17.012 -29.377 -1.931 1.00 56.17 C
ANISOU 1884 CB ALA A 324 6777 9035 5531 441 706 416 C
ATOM 1885 N LEU A 325 -17.487 -26.247 -2.387 1.00 56.61 N
ANISOU 1885 N LEU A 325 6725 9155 5628 355 631 414 N
ATOM 1886 CA LEU A 325 -16.976 -24.869 -2.314 1.00 56.21 C
ANISOU 1886 CA LEU A 325 6695 9117 5547 320 608 424 C
ATOM 1887 C LEU A 325 -18.033 -23.884 -1.781 1.00 60.02 C
ANISOU 1887 C LEU A 325 7205 9545 6055 343 576 411 C
ATOM 1888 O LEU A 325 -17.669 -22.935 -1.065 1.00 60.06 O
ANISOU 1888 O LEU A 325 7253 9534 6033 324 573 412 O
ATOM 1889 CB LEU A 325 -16.400 -24.391 -3.669 1.00 55.96 C
ANISOU 1889 CB LEU A 325 6703 9099 5459 269 584 433 C
ATOM 1890 CG LEU A 325 -15.134 -25.146 -4.132 1.00 60.25 C
ANISOU 1890 CG LEU A 325 7197 9754 5942 260 617 431 C
ATOM 1891 CD1 LEU A 325 -14.816 -24.864 -5.569 1.00 61.27 C
ANISOU 1891 CD1 LEU A 325 7354 9912 6014 204 601 433 C
ATOM 1892 CD2 LEU A 325 -13.928 -24.814 -3.281 1.00 61.66 C
ANISOU 1892 CD2 LEU A 325 7322 10053 6054 222 644 431 C
ATOM 1893 N MET A 326 -19.325 -24.126 -2.082 1.00 56.12 N
ANISOU 1893 N MET A 326 6683 9046 5594 390 554 386 N
ATOM 1894 CA MET A 326 -20.394 -23.265 -1.576 1.00 56.60 C
ANISOU 1894 CA MET A 326 6743 9106 5657 464 521 355 C
ATOM 1895 C MET A 326 -20.631 -23.536 -0.079 1.00 60.49 C
ANISOU 1895 C MET A 326 7173 9639 6170 467 564 339 C
ATOM 1896 O MET A 326 -20.895 -22.598 0.657 1.00 60.29 O
ANISOU 1896 O MET A 326 7176 9603 6129 523 549 318 O
ATOM 1897 CB MET A 326 -21.693 -23.402 -2.384 1.00 59.30 C
ANISOU 1897 CB MET A 326 7030 9507 5994 524 479 319 C
ATOM 1898 CG MET A 326 -21.632 -22.767 -3.764 1.00 62.51 C
ANISOU 1898 CG MET A 326 7526 9868 6360 559 417 335 C
ATOM 1899 SD MET A 326 -21.312 -20.993 -3.779 1.00 66.86 S
ANISOU 1899 SD MET A 326 8279 10285 6840 633 359 357 S
ATOM 1900 CE MET A 326 -19.692 -20.983 -4.433 1.00 63.55 C
ANISOU 1900 CE MET A 326 7954 9803 6389 464 391 415 C
ATOM 1901 N ALA A 327 -20.467 -24.790 0.379 1.00 56.81 N
ANISOU 1901 N ALA A 327 6658 9204 5722 411 617 350 N
ATOM 1902 CA ALA A 327 -20.602 -25.127 1.793 1.00 56.83 C
ANISOU 1902 CA ALA A 327 6626 9241 5727 398 661 347 C
ATOM 1903 C ALA A 327 -19.469 -24.504 2.597 1.00 62.74 C
ANISOU 1903 C ALA A 327 7412 9969 6456 404 669 369 C
ATOM 1904 O ALA A 327 -19.704 -23.991 3.699 1.00 63.14 O
ANISOU 1904 O ALA A 327 7450 10043 6498 422 679 351 O
ATOM 1905 CB ALA A 327 -20.613 -26.636 1.975 1.00 57.47 C
ANISOU 1905 CB ALA A 327 6714 9318 5803 334 710 366 C
ATOM 1906 N GLY A 328 -18.259 -24.553 2.017 1.00 59.55 N
ANISOU 1906 N GLY A 328 7043 9554 6028 379 666 399 N
ATOM 1907 CA GLY A 328 -17.020 -24.037 2.587 1.00 58.85 C
ANISOU 1907 CA GLY A 328 6964 9506 5891 349 674 410 C
ATOM 1908 C GLY A 328 -17.037 -22.541 2.766 1.00 62.19 C
ANISOU 1908 C GLY A 328 7458 9886 6286 316 645 388 C
ATOM 1909 O GLY A 328 -16.488 -22.038 3.747 1.00 61.42 O
ANISOU 1909 O GLY A 328 7368 9820 6150 281 658 378 O
ATOM 1910 N VAL A 329 -17.702 -21.819 1.833 1.00 58.26 N
ANISOU 1910 N VAL A 329 7038 9306 5791 336 601 379 N
ATOM 1911 CA VAL A 329 -17.803 -20.357 1.934 1.00 57.44 C
ANISOU 1911 CA VAL A 329 7080 9107 5636 330 564 359 C
ATOM 1912 C VAL A 329 -18.878 -19.999 2.980 1.00 59.96 C
ANISOU 1912 C VAL A 329 7393 9416 5975 444 559 314 C
ATOM 1913 O VAL A 329 -18.772 -18.945 3.600 1.00 62.05 O
ANISOU 1913 O VAL A 329 7778 9612 6188 444 545 287 O
ATOM 1914 CB VAL A 329 -17.956 -19.571 0.584 1.00 59.85 C
ANISOU 1914 CB VAL A 329 7534 9308 5899 328 511 372 C
ATOM 1915 CG1 VAL A 329 -16.692 -19.688 -0.248 1.00 58.63 C
ANISOU 1915 CG1 VAL A 329 7393 9194 5689 175 528 407 C
ATOM 1916 CG2 VAL A 329 -19.172 -20.005 -0.227 1.00 59.20 C
ANISOU 1916 CG2 VAL A 329 7398 9232 5862 458 476 363 C
ATOM 1917 N VAL A 330 -19.854 -20.888 3.233 1.00 53.75 N
ANISOU 1917 N VAL A 330 6469 8712 5242 517 576 297 N
ATOM 1918 CA VAL A 330 -20.864 -20.632 4.277 1.00 53.74 C
ANISOU 1918 CA VAL A 330 6418 8762 5237 612 581 243 C
ATOM 1919 C VAL A 330 -20.178 -20.824 5.651 1.00 56.96 C
ANISOU 1919 C VAL A 330 6798 9208 5636 545 632 249 C
ATOM 1920 O VAL A 330 -20.247 -19.933 6.487 1.00 55.89 O
ANISOU 1920 O VAL A 330 6725 9050 5462 584 625 209 O
ATOM 1921 CB VAL A 330 -22.177 -21.453 4.136 1.00 56.29 C
ANISOU 1921 CB VAL A 330 6589 9214 5584 666 590 211 C
ATOM 1922 CG1 VAL A 330 -23.179 -21.063 5.221 1.00 56.33 C
ANISOU 1922 CG1 VAL A 330 6522 9326 5556 764 599 140 C
ATOM 1923 CG2 VAL A 330 -22.797 -21.237 2.760 1.00 56.02 C
ANISOU 1923 CG2 VAL A 330 6568 9174 5541 738 532 200 C
ATOM 1924 N TRP A 331 -19.429 -21.927 5.825 1.00 53.76 N
ANISOU 1924 N TRP A 331 6325 8851 5248 461 674 297 N
ATOM 1925 CA TRP A 331 -18.634 -22.173 7.022 1.00 53.74 C
ANISOU 1925 CA TRP A 331 6299 8903 5218 416 711 310 C
ATOM 1926 C TRP A 331 -17.682 -21.003 7.269 1.00 57.17 C
ANISOU 1926 C TRP A 331 6824 9305 5591 358 692 294 C
ATOM 1927 O TRP A 331 -17.331 -20.744 8.411 1.00 58.39 O
ANISOU 1927 O TRP A 331 6972 9506 5706 333 711 277 O
ATOM 1928 CB TRP A 331 -17.841 -23.484 6.901 1.00 52.50 C
ANISOU 1928 CB TRP A 331 6096 8791 5059 385 740 366 C
ATOM 1929 CG TRP A 331 -18.611 -24.716 7.274 1.00 53.74 C
ANISOU 1929 CG TRP A 331 6218 8967 5235 395 777 383 C
ATOM 1930 CD1 TRP A 331 -18.975 -25.738 6.446 1.00 56.57 C
ANISOU 1930 CD1 TRP A 331 6588 9292 5614 382 785 403 C
ATOM 1931 CD2 TRP A 331 -19.100 -25.059 8.578 1.00 54.24 C
ANISOU 1931 CD2 TRP A 331 6256 9080 5273 387 816 380 C
ATOM 1932 NE1 TRP A 331 -19.689 -26.682 7.147 1.00 56.51 N
ANISOU 1932 NE1 TRP A 331 6584 9299 5588 343 828 413 N
ATOM 1933 CE2 TRP A 331 -19.794 -26.284 8.455 1.00 58.61 C
ANISOU 1933 CE2 TRP A 331 6821 9624 5825 345 849 402 C
ATOM 1934 CE3 TRP A 331 -19.062 -24.423 9.838 1.00 56.08 C
ANISOU 1934 CE3 TRP A 331 6470 9367 5470 394 829 356 C
ATOM 1935 CZ2 TRP A 331 -20.394 -26.917 9.556 1.00 59.12 C
ANISOU 1935 CZ2 TRP A 331 6885 9733 5845 291 898 410 C
ATOM 1936 CZ3 TRP A 331 -19.653 -25.050 10.928 1.00 58.10 C
ANISOU 1936 CZ3 TRP A 331 6703 9680 5693 370 875 362 C
ATOM 1937 CH2 TRP A 331 -20.311 -26.280 10.785 1.00 59.22 C
ANISOU 1937 CH2 TRP A 331 6862 9813 5826 311 911 393 C
ATOM 1938 N PHE A 332 -17.279 -20.280 6.210 1.00 52.76 N
ANISOU 1938 N PHE A 332 6366 8672 5009 310 657 298 N
ATOM 1939 CA PHE A 332 -16.428 -19.102 6.370 1.00 52.46 C
ANISOU 1939 CA PHE A 332 6460 8590 4884 197 643 278 C
ATOM 1940 C PHE A 332 -17.222 -18.011 7.089 1.00 57.45 C
ANISOU 1940 C PHE A 332 7226 9113 5489 268 622 221 C
ATOM 1941 O PHE A 332 -16.691 -17.380 8.012 1.00 56.64 O
ANISOU 1941 O PHE A 332 7189 9013 5319 189 632 188 O
ATOM 1942 CB PHE A 332 -15.882 -18.597 5.028 1.00 53.90 C
ANISOU 1942 CB PHE A 332 6751 8708 5022 100 617 300 C
ATOM 1943 CG PHE A 332 -15.650 -17.106 5.022 1.00 56.52 C
ANISOU 1943 CG PHE A 332 7325 8898 5252 -1 588 271 C
ATOM 1944 CD1 PHE A 332 -14.533 -16.555 5.652 1.00 59.49 C
ANISOU 1944 CD1 PHE A 332 7748 9333 5521 -196 610 250 C
ATOM 1945 CD2 PHE A 332 -16.553 -16.247 4.403 1.00 59.60 C
ANISOU 1945 CD2 PHE A 332 7920 9095 5629 101 537 261 C
ATOM 1946 CE1 PHE A 332 -14.323 -15.173 5.660 1.00 61.73 C
ANISOU 1946 CE1 PHE A 332 8313 9453 5687 -331 588 219 C
ATOM 1947 CE2 PHE A 332 -16.342 -14.863 4.413 1.00 64.01 C
ANISOU 1947 CE2 PHE A 332 8781 9470 6069 18 507 237 C
ATOM 1948 CZ PHE A 332 -15.229 -14.336 5.046 1.00 62.44 C
ANISOU 1948 CZ PHE A 332 8659 9300 5766 -218 537 217 C
ATOM 1949 N VAL A 333 -18.504 -17.795 6.657 1.00 54.42 N
ANISOU 1949 N VAL A 333 6880 8657 5141 432 588 197 N
ATOM 1950 CA VAL A 333 -19.407 -16.813 7.277 1.00 54.63 C
ANISOU 1950 CA VAL A 333 7026 8604 5125 574 560 128 C
ATOM 1951 C VAL A 333 -19.598 -17.212 8.742 1.00 60.21 C
ANISOU 1951 C VAL A 333 7599 9437 5842 592 608 93 C
ATOM 1952 O VAL A 333 -19.562 -16.348 9.609 1.00 62.00 O
ANISOU 1952 O VAL A 333 7942 9612 6004 609 604 38 O
ATOM 1953 CB VAL A 333 -20.754 -16.647 6.539 1.00 57.52 C
ANISOU 1953 CB VAL A 333 7398 8953 5506 785 511 99 C
ATOM 1954 CG1 VAL A 333 -21.557 -15.504 7.137 1.00 58.50 C
ANISOU 1954 CG1 VAL A 333 7676 9001 5551 979 471 15 C
ATOM 1955 CG2 VAL A 333 -20.543 -16.414 5.052 1.00 57.17 C
ANISOU 1955 CG2 VAL A 333 7474 8799 5449 764 464 145 C
ATOM 1956 N VAL A 334 -19.714 -18.523 9.013 1.00 56.20 N
ANISOU 1956 N VAL A 334 6878 9078 5397 569 653 129 N
ATOM 1957 CA VAL A 334 -19.856 -19.078 10.350 1.00 56.60 C
ANISOU 1957 CA VAL A 334 6809 9253 5445 563 704 116 C
ATOM 1958 C VAL A 334 -18.620 -18.714 11.182 1.00 62.67 C
ANISOU 1958 C VAL A 334 7632 10025 6154 443 718 121 C
ATOM 1959 O VAL A 334 -18.769 -18.243 12.301 1.00 63.66 O
ANISOU 1959 O VAL A 334 7778 10178 6233 462 732 70 O
ATOM 1960 CB VAL A 334 -20.128 -20.597 10.303 1.00 59.95 C
ANISOU 1960 CB VAL A 334 7070 9786 5920 533 746 170 C
ATOM 1961 CG1 VAL A 334 -19.993 -21.237 11.689 1.00 60.10 C
ANISOU 1961 CG1 VAL A 334 7015 9911 5912 493 799 181 C
ATOM 1962 CG2 VAL A 334 -21.512 -20.864 9.715 1.00 59.83 C
ANISOU 1962 CG2 VAL A 334 6977 9822 5932 619 738 138 C
ATOM 1963 N LEU A 335 -17.426 -18.856 10.609 1.00 60.80 N
ANISOU 1963 N LEU A 335 7411 9788 5900 320 713 168 N
ATOM 1964 CA LEU A 335 -16.157 -18.507 11.248 1.00 61.74 C
ANISOU 1964 CA LEU A 335 7550 9974 5936 181 722 162 C
ATOM 1965 C LEU A 335 -16.187 -17.039 11.685 1.00 67.26 C
ANISOU 1965 C LEU A 335 8447 10556 6555 135 701 88 C
ATOM 1966 O LEU A 335 -16.015 -16.764 12.866 1.00 67.57 O
ANISOU 1966 O LEU A 335 8485 10650 6540 109 718 47 O
ATOM 1967 CB LEU A 335 -15.004 -18.764 10.261 1.00 61.86 C
ANISOU 1967 CB LEU A 335 7540 10041 5922 64 715 205 C
ATOM 1968 CG LEU A 335 -13.605 -18.944 10.813 1.00 67.24 C
ANISOU 1968 CG LEU A 335 8127 10915 6506 -60 730 207 C
ATOM 1969 CD1 LEU A 335 -12.766 -19.674 9.823 1.00 66.85 C
ANISOU 1969 CD1 LEU A 335 7980 10977 6444 -86 730 250 C
ATOM 1970 CD2 LEU A 335 -12.943 -17.609 11.103 1.00 71.67 C
ANISOU 1970 CD2 LEU A 335 8823 11461 6946 -252 721 147 C
ATOM 1971 N THR A 336 -16.469 -16.113 10.751 1.00 64.80 N
ANISOU 1971 N THR A 336 8334 10064 6223 139 660 72 N
ATOM 1972 CA THR A 336 -16.550 -14.669 11.019 1.00 65.69 C
ANISOU 1972 CA THR A 336 8725 9997 6236 111 632 3 C
ATOM 1973 C THR A 336 -17.571 -14.386 12.117 1.00 68.69 C
ANISOU 1973 C THR A 336 9115 10368 6617 295 635 -69 C
ATOM 1974 O THR A 336 -17.284 -13.580 13.004 1.00 69.68 O
ANISOU 1974 O THR A 336 9386 10439 6648 234 637 -133 O
ATOM 1975 CB THR A 336 -16.874 -13.884 9.746 1.00 73.26 C
ANISOU 1975 CB THR A 336 9926 10742 7167 143 580 12 C
ATOM 1976 OG1 THR A 336 -18.199 -14.186 9.317 1.00 70.73 O
ANISOU 1976 OG1 THR A 336 9549 10399 6926 405 553 8 O
ATOM 1977 CG2 THR A 336 -15.907 -14.169 8.630 1.00 71.28 C
ANISOU 1977 CG2 THR A 336 9654 10525 6904 -46 583 78 C
ATOM 1978 N TYR A 337 -18.739 -15.072 12.071 1.00 63.60 N
ANISOU 1978 N TYR A 337 8304 9803 6059 497 640 -67 N
ATOM 1979 CA TYR A 337 -19.802 -14.961 13.065 1.00 63.46 C
ANISOU 1979 CA TYR A 337 8231 9852 6030 676 653 -141 C
ATOM 1980 C TYR A 337 -19.276 -15.411 14.444 1.00 66.94 C
ANISOU 1980 C TYR A 337 8544 10442 6449 571 707 -147 C
ATOM 1981 O TYR A 337 -19.439 -14.678 15.426 1.00 67.64 O
ANISOU 1981 O TYR A 337 8724 10513 6461 613 711 -227 O
ATOM 1982 CB TYR A 337 -21.044 -15.774 12.647 1.00 64.08 C
ANISOU 1982 CB TYR A 337 8110 10055 6181 845 657 -137 C
ATOM 1983 CG TYR A 337 -22.031 -15.970 13.784 1.00 67.48 C
ANISOU 1983 CG TYR A 337 8397 10655 6587 970 693 -209 C
ATOM 1984 CD1 TYR A 337 -21.969 -17.097 14.604 1.00 68.69 C
ANISOU 1984 CD1 TYR A 337 8342 10990 6769 868 759 -170 C
ATOM 1985 CD2 TYR A 337 -22.974 -14.992 14.090 1.00 69.49 C
ANISOU 1985 CD2 TYR A 337 8748 10891 6764 1196 662 -319 C
ATOM 1986 CE1 TYR A 337 -22.827 -17.247 15.692 1.00 68.80 C
ANISOU 1986 CE1 TYR A 337 8229 11175 6736 945 801 -236 C
ATOM 1987 CE2 TYR A 337 -23.851 -15.145 15.156 1.00 70.99 C
ANISOU 1987 CE2 TYR A 337 8782 11282 6909 1307 701 -398 C
ATOM 1988 CZ TYR A 337 -23.773 -16.274 15.957 1.00 79.84 C
ANISOU 1988 CZ TYR A 337 9680 12594 8061 1158 775 -354 C
ATOM 1989 OH TYR A 337 -24.630 -16.422 17.024 1.00 87.87 O
ANISOU 1989 OH TYR A 337 10546 13826 9014 1235 822 -431 O
ATOM 1990 N ALA A 338 -18.659 -16.622 14.500 1.00 62.18 N
ANISOU 1990 N ALA A 338 7748 9980 5896 460 743 -64 N
ATOM 1991 CA ALA A 338 -18.059 -17.234 15.691 1.00 61.29 C
ANISOU 1991 CA ALA A 338 7512 10023 5751 377 786 -46 C
ATOM 1992 C ALA A 338 -16.964 -16.351 16.292 1.00 66.12 C
ANISOU 1992 C ALA A 338 8245 10619 6258 229 777 -88 C
ATOM 1993 O ALA A 338 -16.942 -16.191 17.497 1.00 67.62 O
ANISOU 1993 O ALA A 338 8415 10891 6389 222 799 -132 O
ATOM 1994 CB ALA A 338 -17.495 -18.602 15.363 1.00 60.60 C
ANISOU 1994 CB ALA A 338 7271 10042 5712 323 806 53 C
ATOM 1995 N TRP A 339 -16.101 -15.751 15.474 1.00 63.06 N
ANISOU 1995 N TRP A 339 7987 10144 5830 90 748 -83 N
ATOM 1996 CA TRP A 339 -15.066 -14.832 15.941 1.00 64.87 C
ANISOU 1996 CA TRP A 339 8349 10369 5928 -111 741 -135 C
ATOM 1997 C TRP A 339 -15.685 -13.619 16.620 1.00 74.51 C
ANISOU 1997 C TRP A 339 9807 11426 7077 -60 729 -238 C
ATOM 1998 O TRP A 339 -15.204 -13.184 17.672 1.00 75.00 O
ANISOU 1998 O TRP A 339 9909 11549 7040 -165 743 -298 O
ATOM 1999 CB TRP A 339 -14.164 -14.360 14.784 1.00 63.37 C
ANISOU 1999 CB TRP A 339 8276 10115 5687 -302 719 -113 C
ATOM 2000 CG TRP A 339 -13.087 -13.415 15.241 1.00 65.53 C
ANISOU 2000 CG TRP A 339 8690 10414 5796 -574 720 -176 C
ATOM 2001 CD1 TRP A 339 -12.094 -13.681 16.140 1.00 68.71 C
ANISOU 2001 CD1 TRP A 339 8932 11069 6105 -723 741 -195 C
ATOM 2002 CD2 TRP A 339 -12.929 -12.036 14.864 1.00 66.71 C
ANISOU 2002 CD2 TRP A 339 9191 10330 5827 -740 697 -234 C
ATOM 2003 NE1 TRP A 339 -11.325 -12.558 16.345 1.00 70.00 N
ANISOU 2003 NE1 TRP A 339 9295 11202 6101 -1003 737 -270 N
ATOM 2004 CE2 TRP A 339 -11.808 -11.535 15.565 1.00 71.90 C
ANISOU 2004 CE2 TRP A 339 9877 11122 6320 -1034 713 -292 C
ATOM 2005 CE3 TRP A 339 -13.614 -11.178 13.989 1.00 68.05 C
ANISOU 2005 CE3 TRP A 339 9677 10186 5992 -671 660 -242 C
ATOM 2006 CZ2 TRP A 339 -11.341 -10.226 15.393 1.00 72.59 C
ANISOU 2006 CZ2 TRP A 339 10319 11026 6237 -1306 703 -357 C
ATOM 2007 CZ3 TRP A 339 -13.153 -9.879 13.829 1.00 71.01 C
ANISOU 2007 CZ3 TRP A 339 10432 10350 6198 -902 644 -297 C
ATOM 2008 CH2 TRP A 339 -12.048 -9.408 14.545 1.00 72.80 C
ANISOU 2008 CH2 TRP A 339 10702 10695 6262 -1233 669 -356 C
ATOM 2009 N HIS A 340 -16.739 -13.059 15.999 1.00 74.76 N
ANISOU 2009 N HIS A 340 10006 11259 7140 119 698 -267 N
ATOM 2010 CA HIS A 340 -17.427 -11.893 16.529 1.00 77.69 C
ANISOU 2010 CA HIS A 340 10638 11455 7427 243 676 -374 C
ATOM 2011 C HIS A 340 -18.069 -12.220 17.871 1.00 80.82 C
ANISOU 2011 C HIS A 340 10871 12011 7825 377 712 -429 C
ATOM 2012 O HIS A 340 -17.912 -11.437 18.809 1.00 82.48 O
ANISOU 2012 O HIS A 340 11233 12177 7927 339 716 -518 O
ATOM 2013 CB HIS A 340 -18.475 -11.353 15.537 1.00 80.11 C
ANISOU 2013 CB HIS A 340 11124 11562 7754 479 624 -390 C
ATOM 2014 CG HIS A 340 -19.583 -10.584 16.197 1.00 86.24 C
ANISOU 2014 CG HIS A 340 12046 12256 8464 753 604 -505 C
ATOM 2015 ND1 HIS A 340 -20.884 -11.060 16.203 1.00 88.35 N
ANISOU 2015 ND1 HIS A 340 12118 12660 8793 1044 603 -531 N
ATOM 2016 CD2 HIS A 340 -19.534 -9.437 16.919 1.00 90.64 C
ANISOU 2016 CD2 HIS A 340 12910 12646 8884 771 588 -610 C
ATOM 2017 CE1 HIS A 340 -21.588 -10.170 16.883 1.00 89.84 C
ANISOU 2017 CE1 HIS A 340 12479 12777 8877 1261 583 -652 C
ATOM 2018 NE2 HIS A 340 -20.816 -9.183 17.346 1.00 91.59 N
ANISOU 2018 NE2 HIS A 340 13024 12794 8981 1117 573 -703 N
ATOM 2019 N THR A 341 -18.783 -13.359 17.959 1.00 74.79 N
ANISOU 2019 N THR A 341 9821 11432 7165 507 742 -381 N
ATOM 2020 CA THR A 341 -19.491 -13.743 19.176 1.00 74.71 C
ANISOU 2020 CA THR A 341 9647 11596 7142 618 786 -427 C
ATOM 2021 C THR A 341 -18.576 -14.297 20.257 1.00 77.16 C
ANISOU 2021 C THR A 341 9829 12075 7414 443 826 -396 C
ATOM 2022 O THR A 341 -18.905 -14.142 21.432 1.00 78.04 O
ANISOU 2022 O THR A 341 9915 12278 7460 488 854 -463 O
ATOM 2023 CB THR A 341 -20.604 -14.740 18.894 1.00 83.89 C
ANISOU 2023 CB THR A 341 10575 12905 8392 767 810 -392 C
ATOM 2024 OG1 THR A 341 -20.022 -15.921 18.364 1.00 86.12 O
ANISOU 2024 OG1 THR A 341 10703 13260 8759 636 827 -270 O
ATOM 2025 CG2 THR A 341 -21.676 -14.179 17.966 1.00 82.43 C
ANISOU 2025 CG2 THR A 341 10477 12626 8218 989 764 -445 C
ATOM 2026 N SER A 342 -17.441 -14.916 19.902 1.00 71.29 N
ANISOU 2026 N SER A 342 9004 11395 6689 266 826 -306 N
ATOM 2027 CA SER A 342 -16.556 -15.478 20.932 1.00 71.08 C
ANISOU 2027 CA SER A 342 8844 11562 6600 144 852 -278 C
ATOM 2028 C SER A 342 -15.819 -14.383 21.762 1.00 75.69 C
ANISOU 2028 C SER A 342 9582 12134 7043 -1 842 -374 C
ATOM 2029 O SER A 342 -15.153 -14.696 22.764 1.00 74.55 O
ANISOU 2029 O SER A 342 9331 12174 6821 -89 859 -373 O
ATOM 2030 CB SER A 342 -15.583 -16.481 20.332 1.00 73.80 C
ANISOU 2030 CB SER A 342 9047 12017 6977 53 848 -169 C
ATOM 2031 OG SER A 342 -16.299 -17.568 19.768 1.00 82.40 O
ANISOU 2031 OG SER A 342 10020 13114 8175 174 864 -89 O
ATOM 2032 N PHE A 343 -16.022 -13.099 21.385 1.00 73.07 N
ANISOU 2032 N PHE A 343 9526 11576 6662 -13 813 -462 N
ATOM 2033 CA PHE A 343 -15.530 -11.930 22.114 1.00 74.04 C
ANISOU 2033 CA PHE A 343 9875 11623 6635 -153 804 -572 C
ATOM 2034 C PHE A 343 -16.299 -11.798 23.426 1.00 80.05 C
ANISOU 2034 C PHE A 343 10615 12450 7352 -5 832 -657 C
ATOM 2035 O PHE A 343 -15.786 -11.214 24.389 1.00 82.22 O
ANISOU 2035 O PHE A 343 10982 12760 7498 -133 838 -738 O
ATOM 2036 CB PHE A 343 -15.690 -10.648 21.279 1.00 76.46 C
ANISOU 2036 CB PHE A 343 10554 11612 6886 -177 763 -635 C
ATOM 2037 CG PHE A 343 -14.489 -10.273 20.453 1.00 77.69 C
ANISOU 2037 CG PHE A 343 10830 11716 6973 -479 745 -604 C
ATOM 2038 CD1 PHE A 343 -13.313 -9.843 21.061 1.00 80.66 C
ANISOU 2038 CD1 PHE A 343 11256 12197 7194 -790 754 -654 C
ATOM 2039 CD2 PHE A 343 -14.542 -10.311 19.065 1.00 79.41 C
ANISOU 2039 CD2 PHE A 343 11111 11804 7257 -471 720 -534 C
ATOM 2040 CE1 PHE A 343 -12.194 -9.507 20.294 1.00 82.34 C
ANISOU 2040 CE1 PHE A 343 11551 12423 7313 -1108 745 -637 C
ATOM 2041 CE2 PHE A 343 -13.421 -9.974 18.296 1.00 82.24 C
ANISOU 2041 CE2 PHE A 343 11569 12150 7530 -776 712 -509 C
ATOM 2042 CZ PHE A 343 -12.257 -9.568 18.915 1.00 81.14 C
ANISOU 2042 CZ PHE A 343 11457 12144 7228 -1101 727 -563 C
ATOM 2043 N LYS A 344 -17.539 -12.364 23.456 1.00 75.07 N
ANISOU 2043 N LYS A 344 9850 11863 6812 247 852 -644 N
ATOM 2044 CA LYS A 344 -18.465 -12.379 24.596 1.00 74.23 C
ANISOU 2044 CA LYS A 344 9673 11869 6664 411 888 -722 C
ATOM 2045 C LYS A 344 -17.985 -13.364 25.690 1.00 77.21 C
ANISOU 2045 C LYS A 344 9809 12514 7015 309 933 -664 C
ATOM 2046 O LYS A 344 -18.533 -13.331 26.795 1.00 78.45 O
ANISOU 2046 O LYS A 344 9915 12787 7104 386 968 -730 O
ATOM 2047 CB LYS A 344 -19.904 -12.694 24.140 1.00 74.90 C
ANISOU 2047 CB LYS A 344 9659 11973 6825 675 897 -731 C
ATOM 2048 N ALA A 345 -16.948 -14.202 25.416 1.00 72.12 N
ANISOU 2048 N ALA A 345 9029 11973 6400 154 928 -547 N
ATOM 2049 CA ALA A 345 -16.379 -15.068 26.453 1.00 72.10 C
ANISOU 2049 CA ALA A 345 8846 12209 6340 84 954 -489 C
ATOM 2050 C ALA A 345 -15.627 -14.193 27.451 1.00 81.66 C
ANISOU 2050 C ALA A 345 10154 13475 7397 -56 945 -588 C
ATOM 2051 O ALA A 345 -15.747 -14.431 28.647 1.00 82.06 O
ANISOU 2051 O ALA A 345 10124 13686 7371 -37 974 -609 O
ATOM 2052 CB ALA A 345 -15.459 -16.124 25.867 1.00 71.23 C
ANISOU 2052 CB ALA A 345 8595 12198 6273 13 939 -355 C
ATOM 2053 N LEU A 346 -14.943 -13.114 26.963 1.00 81.49 N
ANISOU 2053 N LEU A 346 10336 13310 7316 -210 908 -660 N
ATOM 2054 CA LEU A 346 -14.193 -12.119 27.762 1.00 83.61 C
ANISOU 2054 CA LEU A 346 10755 13598 7416 -403 897 -775 C
ATOM 2055 C LEU A 346 -13.045 -12.806 28.518 1.00 89.57 C
ANISOU 2055 C LEU A 346 11289 14670 8073 -553 895 -727 C
ATOM 2056 O LEU A 346 -12.830 -12.546 29.714 1.00 89.84 O
ANISOU 2056 O LEU A 346 11319 14838 7977 -618 904 -801 O
ATOM 2057 CB LEU A 346 -15.143 -11.373 28.745 1.00 84.63 C
ANISOU 2057 CB LEU A 346 11031 13646 7479 -271 920 -906 C
ATOM 2058 CG LEU A 346 -15.360 -9.876 28.546 1.00 90.22 C
ANISOU 2058 CG LEU A 346 12121 14057 8100 -296 895 -1050 C
ATOM 2059 CD1 LEU A 346 -16.442 -9.599 27.509 1.00 89.26 C
ANISOU 2059 CD1 LEU A 346 12137 13691 8087 -56 878 -1049 C
ATOM 2060 CD2 LEU A 346 -15.718 -9.221 29.867 1.00 93.69 C
ANISOU 2060 CD2 LEU A 346 12674 14516 8406 -245 916 -1192 C
ATOM 2061 N GLY A 347 -12.358 -13.723 27.824 1.00 87.35 N
ANISOU 2061 N GLY A 347 10822 14522 7844 -575 880 -608 N
ATOM 2062 CA GLY A 347 -11.278 -14.523 28.405 1.00 88.64 C
ANISOU 2062 CA GLY A 347 10757 15015 7906 -640 865 -551 C
ATOM 2063 C GLY A 347 -11.816 -15.582 29.359 1.00 93.92 C
ANISOU 2063 C GLY A 347 11279 15815 8589 -446 891 -475 C
ATOM 2064 O GLY A 347 -11.271 -16.691 29.457 1.00 95.17 O
ANISOU 2064 O GLY A 347 11265 16167 8728 -373 877 -367 O
ATOM 2065 N THR A 348 -12.914 -15.221 30.060 1.00 87.87 N
ANISOU 2065 N THR A 348 10607 14941 7840 -354 929 -536 N
ATOM 2066 CA THR A 348 -13.750 -15.977 30.980 1.00 85.78 C
ANISOU 2066 CA THR A 348 10258 14758 7578 -203 971 -492 C
ATOM 2067 C THR A 348 -14.161 -17.322 30.308 1.00 85.71 C
ANISOU 2067 C THR A 348 10143 14733 7691 -68 985 -337 C
ATOM 2068 O THR A 348 -14.125 -17.447 29.085 1.00 85.17 O
ANISOU 2068 O THR A 348 10091 14536 7735 -55 967 -293 O
ATOM 2069 CB THR A 348 -14.912 -15.024 31.361 1.00 89.78 C
ANISOU 2069 CB THR A 348 10910 15112 8090 -136 1007 -622 C
ATOM 2070 OG1 THR A 348 -14.511 -14.170 32.443 1.00 88.14 O
ANISOU 2070 OG1 THR A 348 10782 14984 7724 -242 1004 -746 O
ATOM 2071 CG2 THR A 348 -16.261 -15.713 31.606 1.00 86.50 C
ANISOU 2071 CG2 THR A 348 10418 14706 7741 39 1063 -584 C
ATOM 2072 N THR A 349 -14.506 -18.327 31.122 1.00 80.67 N
ANISOU 2072 N THR A 349 9423 14219 7010 13 1016 -253 N
ATOM 2073 CA THR A 349 -14.886 -19.682 30.693 1.00 78.40 C
ANISOU 2073 CA THR A 349 9088 13908 6791 110 1034 -106 C
ATOM 2074 C THR A 349 -16.288 -19.793 30.054 1.00 78.26 C
ANISOU 2074 C THR A 349 9098 13733 6905 168 1084 -110 C
ATOM 2075 O THR A 349 -16.703 -20.910 29.728 1.00 77.65 O
ANISOU 2075 O THR A 349 9004 13629 6869 207 1107 2 O
ATOM 2076 CB THR A 349 -14.795 -20.640 31.875 1.00 82.53 C
ANISOU 2076 CB THR A 349 9576 14599 7184 148 1053 -19 C
ATOM 2077 OG1 THR A 349 -15.157 -19.943 33.077 1.00 75.84 O
ANISOU 2077 OG1 THR A 349 8732 13851 6233 106 1084 -122 O
ATOM 2078 CG2 THR A 349 -13.416 -21.278 31.983 1.00 81.00 C
ANISOU 2078 CG2 THR A 349 9331 14559 6886 183 990 66 C
ATOM 2079 N TYR A 350 -17.003 -18.665 29.852 1.00 71.52 N
ANISOU 2079 N TYR A 350 8299 12781 6094 179 1094 -241 N
ATOM 2080 CA TYR A 350 -18.308 -18.689 29.202 1.00 69.45 C
ANISOU 2080 CA TYR A 350 8030 12425 5931 260 1129 -264 C
ATOM 2081 C TYR A 350 -18.142 -19.147 27.739 1.00 73.88 C
ANISOU 2081 C TYR A 350 8599 12849 6625 270 1098 -183 C
ATOM 2082 O TYR A 350 -17.126 -18.844 27.081 1.00 73.98 O
ANISOU 2082 O TYR A 350 8656 12792 6660 222 1045 -172 O
ATOM 2083 CB TYR A 350 -19.017 -17.317 29.294 1.00 70.04 C
ANISOU 2083 CB TYR A 350 8186 12433 5992 331 1131 -432 C
ATOM 2084 CG TYR A 350 -20.413 -17.276 28.690 1.00 70.35 C
ANISOU 2084 CG TYR A 350 8186 12443 6100 459 1159 -478 C
ATOM 2085 CD1 TYR A 350 -20.744 -16.350 27.701 1.00 71.28 C
ANISOU 2085 CD1 TYR A 350 8412 12389 6281 559 1117 -559 C
ATOM 2086 CD2 TYR A 350 -21.390 -18.188 29.077 1.00 71.46 C
ANISOU 2086 CD2 TYR A 350 8186 12748 6220 469 1225 -441 C
ATOM 2087 CE1 TYR A 350 -22.019 -16.322 27.129 1.00 68.06 C
ANISOU 2087 CE1 TYR A 350 7943 12003 5915 708 1132 -608 C
ATOM 2088 CE2 TYR A 350 -22.670 -18.156 28.525 1.00 72.58 C
ANISOU 2088 CE2 TYR A 350 8247 12934 6395 571 1250 -500 C
ATOM 2089 CZ TYR A 350 -22.977 -17.231 27.541 1.00 73.91 C
ANISOU 2089 CZ TYR A 350 8495 12959 6630 710 1199 -584 C
ATOM 2090 OH TYR A 350 -24.253 -17.217 27.027 1.00 71.19 O
ANISOU 2090 OH TYR A 350 8045 12710 6295 840 1216 -650 O
ATOM 2091 N GLN A 351 -19.117 -19.944 27.273 1.00 68.67 N
ANISOU 2091 N GLN A 351 7885 12179 6028 307 1135 -128 N
ATOM 2092 CA GLN A 351 -19.175 -20.471 25.926 1.00 66.42 C
ANISOU 2092 CA GLN A 351 7602 11775 5860 318 1115 -58 C
ATOM 2093 C GLN A 351 -20.329 -19.765 25.180 1.00 69.72 C
ANISOU 2093 C GLN A 351 8014 12127 6348 401 1118 -155 C
ATOM 2094 O GLN A 351 -21.495 -20.194 25.237 1.00 68.51 O
ANISOU 2094 O GLN A 351 7775 12067 6190 425 1167 -171 O
ATOM 2095 CB GLN A 351 -19.318 -21.991 25.961 1.00 67.72 C
ANISOU 2095 CB GLN A 351 7741 11977 6014 279 1150 76 C
ATOM 2096 CG GLN A 351 -18.015 -22.705 26.317 1.00 88.10 C
ANISOU 2096 CG GLN A 351 10362 14586 8528 268 1119 181 C
ATOM 2097 CD GLN A 351 -18.050 -24.169 25.941 1.00124.36 C
ANISOU 2097 CD GLN A 351 15009 19121 13120 267 1133 317 C
ATOM 2098 OE1 GLN A 351 -17.979 -25.058 26.803 1.00121.78 O
ANISOU 2098 OE1 GLN A 351 14742 18848 12683 253 1158 401 O
ATOM 2099 NE2 GLN A 351 -18.142 -24.458 24.640 1.00122.93 N
ANISOU 2099 NE2 GLN A 351 14844 18815 13048 281 1115 343 N
ATOM 2100 N PRO A 352 -20.004 -18.625 24.521 1.00 67.35 N
ANISOU 2100 N PRO A 352 7815 11688 6086 444 1065 -228 N
ATOM 2101 CA PRO A 352 -21.043 -17.841 23.822 1.00 68.29 C
ANISOU 2101 CA PRO A 352 7966 11735 6244 576 1050 -324 C
ATOM 2102 C PRO A 352 -21.824 -18.601 22.751 1.00 71.85 C
ANISOU 2102 C PRO A 352 8326 12190 6783 609 1058 -271 C
ATOM 2103 O PRO A 352 -23.020 -18.330 22.567 1.00 73.52 O
ANISOU 2103 O PRO A 352 8473 12477 6985 728 1069 -352 O
ATOM 2104 CB PRO A 352 -20.249 -16.704 23.163 1.00 70.06 C
ANISOU 2104 CB PRO A 352 8380 11759 6481 570 985 -367 C
ATOM 2105 CG PRO A 352 -18.991 -16.616 23.911 1.00 74.16 C
ANISOU 2105 CG PRO A 352 8937 12312 6931 424 979 -346 C
ATOM 2106 CD PRO A 352 -18.681 -17.989 24.383 1.00 68.88 C
ANISOU 2106 CD PRO A 352 8113 11798 6260 363 1014 -230 C
ATOM 2107 N LEU A 353 -21.150 -19.543 22.055 1.00 64.82 N
ANISOU 2107 N LEU A 353 7426 11243 5960 514 1049 -148 N
ATOM 2108 CA LEU A 353 -21.704 -20.348 20.964 1.00 62.48 C
ANISOU 2108 CA LEU A 353 7071 10928 5742 511 1052 -91 C
ATOM 2109 C LEU A 353 -22.578 -21.525 21.442 1.00 69.07 C
ANISOU 2109 C LEU A 353 7791 11918 6535 438 1123 -50 C
ATOM 2110 O LEU A 353 -23.220 -22.157 20.617 1.00 67.97 O
ANISOU 2110 O LEU A 353 7600 11788 6436 409 1133 -25 O
ATOM 2111 CB LEU A 353 -20.544 -20.882 20.087 1.00 59.78 C
ANISOU 2111 CB LEU A 353 6789 10460 5463 444 1016 14 C
ATOM 2112 CG LEU A 353 -19.719 -19.821 19.360 1.00 60.77 C
ANISOU 2112 CG LEU A 353 7027 10448 5617 458 954 -19 C
ATOM 2113 CD1 LEU A 353 -18.372 -20.351 18.944 1.00 58.13 C
ANISOU 2113 CD1 LEU A 353 6708 10089 5289 374 931 69 C
ATOM 2114 CD2 LEU A 353 -20.489 -19.222 18.211 1.00 62.79 C
ANISOU 2114 CD2 LEU A 353 7322 10604 5932 549 920 -66 C
ATOM 2115 N SER A 354 -22.611 -21.817 22.749 1.00 70.60 N
ANISOU 2115 N SER A 354 7958 12236 6632 383 1172 -46 N
ATOM 2116 CA SER A 354 -23.348 -22.961 23.290 1.00 73.23 C
ANISOU 2116 CA SER A 354 8226 12707 6891 262 1247 4 C
ATOM 2117 C SER A 354 -24.832 -22.960 22.884 1.00 82.07 C
ANISOU 2117 C SER A 354 9200 13988 7993 261 1285 -81 C
ATOM 2118 O SER A 354 -25.605 -22.070 23.267 1.00 83.09 O
ANISOU 2118 O SER A 354 9229 14269 8073 371 1293 -212 O
ATOM 2119 CB SER A 354 -23.192 -23.055 24.804 1.00 77.63 C
ANISOU 2119 CB SER A 354 8785 13386 7325 214 1292 5 C
ATOM 2120 OG SER A 354 -22.044 -23.827 25.121 1.00 85.62 O
ANISOU 2120 OG SER A 354 9913 14307 8312 161 1277 133 O
ATOM 2121 N GLY A 355 -25.183 -23.954 22.069 1.00 80.46 N
ANISOU 2121 N GLY A 355 8992 13763 7817 147 1302 -15 N
ATOM 2122 CA GLY A 355 -26.538 -24.132 21.565 1.00 82.45 C
ANISOU 2122 CA GLY A 355 9085 14207 8034 103 1337 -90 C
ATOM 2123 C GLY A 355 -26.744 -23.617 20.157 1.00 86.62 C
ANISOU 2123 C GLY A 355 9582 14665 8665 231 1269 -134 C
ATOM 2124 O GLY A 355 -27.728 -23.984 19.504 1.00 86.87 O
ANISOU 2124 O GLY A 355 9488 14848 8672 175 1288 -176 O
ATOM 2125 N LYS A 356 -25.816 -22.760 19.687 1.00 82.83 N
ANISOU 2125 N LYS A 356 9219 13972 8282 383 1192 -127 N
ATOM 2126 CA LYS A 356 -25.848 -22.158 18.345 1.00 82.35 C
ANISOU 2126 CA LYS A 356 9180 13798 8310 512 1118 -156 C
ATOM 2127 C LYS A 356 -25.325 -23.114 17.272 1.00 84.57 C
ANISOU 2127 C LYS A 356 9534 13926 8673 399 1104 -44 C
ATOM 2128 O LYS A 356 -25.665 -22.931 16.105 1.00 84.20 O
ANISOU 2128 O LYS A 356 9468 13844 8679 460 1060 -65 O
ATOM 2129 CB LYS A 356 -25.060 -20.835 18.308 1.00 84.17 C
ANISOU 2129 CB LYS A 356 9548 13856 8576 673 1050 -195 C
ATOM 2130 CG LYS A 356 -25.792 -19.691 19.007 1.00 96.96 C
ANISOU 2130 CG LYS A 356 11134 15596 10112 854 1044 -338 C
ATOM 2131 CD LYS A 356 -24.864 -18.554 19.350 1.00104.82 C
ANISOU 2131 CD LYS A 356 12324 16398 11105 935 997 -366 C
ATOM 2132 CE LYS A 356 -25.610 -17.446 20.045 1.00120.97 C
ANISOU 2132 CE LYS A 356 14380 18533 13050 1140 988 -517 C
ATOM 2133 NZ LYS A 356 -24.767 -16.236 20.220 1.00131.52 N
ANISOU 2133 NZ LYS A 356 15970 19636 14367 1206 935 -558 N
ATOM 2134 N THR A 357 -24.558 -24.151 17.672 1.00 80.78 N
ANISOU 2134 N THR A 357 9147 13363 8184 256 1137 69 N
ATOM 2135 CA THR A 357 -23.936 -25.162 16.801 1.00 80.39 C
ANISOU 2135 CA THR A 357 9202 13156 8187 175 1125 174 C
ATOM 2136 C THR A 357 -24.939 -25.882 15.852 1.00 86.94 C
ANISOU 2136 C THR A 357 9972 14045 9017 74 1145 162 C
ATOM 2137 O THR A 357 -24.545 -26.253 14.741 1.00 86.13 O
ANISOU 2137 O THR A 357 9939 13805 8980 70 1110 207 O
ATOM 2138 CB THR A 357 -23.122 -26.201 17.610 1.00 85.50 C
ANISOU 2138 CB THR A 357 9980 13732 8776 83 1159 284 C
ATOM 2139 OG1 THR A 357 -23.500 -27.538 17.250 1.00 80.71 O
ANISOU 2139 OG1 THR A 357 9452 13086 8128 -70 1201 348 O
ATOM 2140 CG2 THR A 357 -23.198 -25.997 19.122 1.00 87.82 C
ANISOU 2140 CG2 THR A 357 10250 14144 8974 65 1201 268 C
ATOM 2141 N SER A 358 -26.204 -26.078 16.279 1.00 85.67 N
ANISOU 2141 N SER A 358 9671 14115 8765 -23 1201 93 N
ATOM 2142 CA SER A 358 -27.240 -26.748 15.477 1.00 86.60 C
ANISOU 2142 CA SER A 358 9700 14359 8846 -163 1227 61 C
ATOM 2143 C SER A 358 -27.516 -26.018 14.137 1.00 88.70 C
ANISOU 2143 C SER A 358 9884 14625 9193 -8 1151 -1 C
ATOM 2144 O SER A 358 -27.541 -26.670 13.089 1.00 86.74 O
ANISOU 2144 O SER A 358 9681 14299 8979 -92 1137 34 O
ATOM 2145 CB SER A 358 -28.535 -26.859 16.274 1.00 93.05 C
ANISOU 2145 CB SER A 358 10329 15507 9520 -288 1301 -29 C
ATOM 2146 OG SER A 358 -29.035 -25.572 16.602 1.00106.18 O
ANISOU 2146 OG SER A 358 11819 17354 11169 -65 1271 -153 O
ATOM 2147 N TYR A 359 -27.712 -24.673 14.194 1.00 85.36 N
ANISOU 2147 N TYR A 359 9375 14274 8786 224 1100 -92 N
ATOM 2148 CA TYR A 359 -27.981 -23.789 13.051 1.00 85.34 C
ANISOU 2148 CA TYR A 359 9336 14258 8832 419 1017 -152 C
ATOM 2149 C TYR A 359 -26.821 -23.751 12.072 1.00 83.62 C
ANISOU 2149 C TYR A 359 9301 13743 8729 447 961 -60 C
ATOM 2150 O TYR A 359 -27.041 -23.609 10.865 1.00 82.37 O
ANISOU 2150 O TYR A 359 9133 13558 8605 503 909 -71 O
ATOM 2151 CB TYR A 359 -28.268 -22.360 13.527 1.00 88.99 C
ANISOU 2151 CB TYR A 359 9764 14788 9259 679 974 -256 C
ATOM 2152 CG TYR A 359 -29.541 -22.229 14.328 1.00 95.35 C
ANISOU 2152 CG TYR A 359 10347 15950 9930 716 1019 -379 C
ATOM 2153 CD1 TYR A 359 -30.780 -22.148 13.696 1.00 99.33 C
ANISOU 2153 CD1 TYR A 359 10641 16745 10354 798 1001 -484 C
ATOM 2154 CD2 TYR A 359 -29.507 -22.136 15.720 1.00 97.34 C
ANISOU 2154 CD2 TYR A 359 10580 16287 10117 684 1079 -401 C
ATOM 2155 CE1 TYR A 359 -31.958 -22.015 14.429 1.00103.14 C
ANISOU 2155 CE1 TYR A 359 10877 17627 10685 841 1044 -616 C
ATOM 2156 CE2 TYR A 359 -30.678 -21.994 16.464 1.00100.65 C
ANISOU 2156 CE2 TYR A 359 10775 17074 10393 720 1126 -526 C
ATOM 2157 CZ TYR A 359 -31.901 -21.936 15.812 1.00112.76 C
ANISOU 2157 CZ TYR A 359 12080 18924 11839 799 1110 -637 C
ATOM 2158 OH TYR A 359 -33.066 -21.801 16.522 1.00119.80 O
ANISOU 2158 OH TYR A 359 12710 20246 12564 840 1159 -777 O
ATOM 2159 N PHE A 360 -25.582 -23.853 12.605 1.00 75.94 N
ANISOU 2159 N PHE A 360 8475 12582 7796 411 969 23 N
ATOM 2160 CA PHE A 360 -24.350 -23.871 11.835 1.00 72.67 C
ANISOU 2160 CA PHE A 360 8208 11942 7462 420 926 103 C
ATOM 2161 C PHE A 360 -24.346 -25.004 10.817 1.00 73.62 C
ANISOU 2161 C PHE A 360 8353 12009 7611 308 933 160 C
ATOM 2162 O PHE A 360 -23.846 -24.814 9.723 1.00 73.62 O
ANISOU 2162 O PHE A 360 8411 11894 7668 355 884 182 O
ATOM 2163 CB PHE A 360 -23.141 -24.008 12.762 1.00 73.62 C
ANISOU 2163 CB PHE A 360 8427 11969 7576 386 945 168 C
ATOM 2164 CG PHE A 360 -22.756 -22.810 13.598 1.00 75.34 C
ANISOU 2164 CG PHE A 360 8673 12181 7770 478 926 119 C
ATOM 2165 CD1 PHE A 360 -21.788 -22.919 14.593 1.00 77.88 C
ANISOU 2165 CD1 PHE A 360 9047 12484 8059 437 944 160 C
ATOM 2166 CD2 PHE A 360 -23.327 -21.562 13.368 1.00 77.87 C
ANISOU 2166 CD2 PHE A 360 8994 12509 8083 617 882 28 C
ATOM 2167 CE1 PHE A 360 -21.413 -21.806 15.355 1.00 78.68 C
ANISOU 2167 CE1 PHE A 360 9188 12581 8125 492 927 105 C
ATOM 2168 CE2 PHE A 360 -22.958 -20.453 14.139 1.00 80.71 C
ANISOU 2168 CE2 PHE A 360 9436 12829 8403 690 865 -24 C
ATOM 2169 CZ PHE A 360 -22.003 -20.583 15.125 1.00 78.06 C
ANISOU 2169 CZ PHE A 360 9139 12480 8040 606 891 13 C
ATOM 2170 N HIS A 361 -24.891 -26.169 11.163 1.00 68.49 N
ANISOU 2170 N HIS A 361 7683 11434 6906 145 996 180 N
ATOM 2171 CA HIS A 361 -24.925 -27.310 10.259 1.00 67.83 C
ANISOU 2171 CA HIS A 361 7669 11277 6828 18 1007 226 C
ATOM 2172 C HIS A 361 -26.144 -27.236 9.354 1.00 72.06 C
ANISOU 2172 C HIS A 361 8062 11973 7344 -17 993 146 C
ATOM 2173 O HIS A 361 -26.077 -27.668 8.213 1.00 71.96 O
ANISOU 2173 O HIS A 361 8093 11887 7361 -52 968 162 O
ATOM 2174 CB HIS A 361 -24.886 -28.619 11.054 1.00 69.42 C
ANISOU 2174 CB HIS A 361 7990 11438 6948 -162 1078 291 C
ATOM 2175 CG HIS A 361 -23.546 -28.862 11.673 1.00 72.05 C
ANISOU 2175 CG HIS A 361 8480 11608 7288 -88 1073 378 C
ATOM 2176 ND1 HIS A 361 -22.572 -29.596 11.023 1.00 73.22 N
ANISOU 2176 ND1 HIS A 361 8790 11575 7455 -52 1051 449 N
ATOM 2177 CD2 HIS A 361 -23.033 -28.390 12.829 1.00 73.50 C
ANISOU 2177 CD2 HIS A 361 8659 11819 7449 -21 1080 391 C
ATOM 2178 CE1 HIS A 361 -21.520 -29.580 11.817 1.00 72.11 C
ANISOU 2178 CE1 HIS A 361 8721 11384 7292 43 1043 502 C
ATOM 2179 NE2 HIS A 361 -21.747 -28.857 12.910 1.00 72.71 N
ANISOU 2179 NE2 HIS A 361 8703 11578 7346 52 1059 472 N
ATOM 2180 N LEU A 362 -27.236 -26.644 9.840 1.00 69.43 N
ANISOU 2180 N LEU A 362 7546 11886 6946 14 1004 50 N
ATOM 2181 CA LEU A 362 -28.476 -26.444 9.100 1.00 70.42 C
ANISOU 2181 CA LEU A 362 7484 12253 7021 23 983 -48 C
ATOM 2182 C LEU A 362 -28.244 -25.480 7.939 1.00 74.02 C
ANISOU 2182 C LEU A 362 7954 12621 7549 246 887 -65 C
ATOM 2183 O LEU A 362 -28.594 -25.816 6.824 1.00 75.20 O
ANISOU 2183 O LEU A 362 8068 12806 7697 208 859 -78 O
ATOM 2184 CB LEU A 362 -29.534 -25.897 10.058 1.00 72.47 C
ANISOU 2184 CB LEU A 362 7537 12825 7174 69 1013 -156 C
ATOM 2185 CG LEU A 362 -31.003 -25.995 9.651 1.00 79.96 C
ANISOU 2185 CG LEU A 362 8226 14152 8003 24 1018 -277 C
ATOM 2186 CD1 LEU A 362 -31.456 -27.450 9.508 1.00 81.39 C
ANISOU 2186 CD1 LEU A 362 8399 14425 8102 -347 1096 -259 C
ATOM 2187 CD2 LEU A 362 -31.886 -25.295 10.687 1.00 83.16 C
ANISOU 2187 CD2 LEU A 362 8420 14882 8295 141 1041 -394 C
ATOM 2188 N LEU A 363 -27.558 -24.349 8.175 1.00 68.83 N
ANISOU 2188 N LEU A 363 7387 11822 6943 447 839 -55 N
ATOM 2189 CA LEU A 363 -27.263 -23.332 7.162 1.00 67.76 C
ANISOU 2189 CA LEU A 363 7330 11565 6852 643 750 -60 C
ATOM 2190 C LEU A 363 -26.207 -23.753 6.125 1.00 69.77 C
ANISOU 2190 C LEU A 363 7733 11590 7186 571 729 33 C
ATOM 2191 O LEU A 363 -26.429 -23.549 4.925 1.00 69.07 O
ANISOU 2191 O LEU A 363 7647 11490 7105 631 673 24 O
ATOM 2192 CB LEU A 363 -26.790 -22.035 7.846 1.00 67.61 C
ANISOU 2192 CB LEU A 363 7416 11442 6832 823 717 -79 C
ATOM 2193 CG LEU A 363 -27.822 -20.956 8.263 1.00 72.98 C
ANISOU 2193 CG LEU A 363 8014 12292 7422 1062 678 -198 C
ATOM 2194 CD1 LEU A 363 -29.274 -21.407 8.112 1.00 74.09 C
ANISOU 2194 CD1 LEU A 363 7893 12785 7472 1068 693 -292 C
ATOM 2195 CD2 LEU A 363 -27.540 -20.463 9.671 1.00 73.40 C
ANISOU 2195 CD2 LEU A 363 8114 12328 7448 1103 711 -224 C
ATOM 2196 N THR A 364 -25.050 -24.282 6.586 1.00 64.75 N
ANISOU 2196 N THR A 364 7215 10796 6593 470 767 114 N
ATOM 2197 CA THR A 364 -23.907 -24.663 5.740 1.00 63.24 C
ANISOU 2197 CA THR A 364 7149 10425 6456 428 751 191 C
ATOM 2198 C THR A 364 -24.184 -25.854 4.812 1.00 69.04 C
ANISOU 2198 C THR A 364 7877 11163 7192 310 766 208 C
ATOM 2199 O THR A 364 -23.530 -25.966 3.767 1.00 68.82 O
ANISOU 2199 O THR A 364 7923 11028 7197 320 736 243 O
ATOM 2200 CB THR A 364 -22.679 -24.986 6.578 1.00 62.88 C
ANISOU 2200 CB THR A 364 7193 10279 6419 385 785 256 C
ATOM 2201 OG1 THR A 364 -22.980 -26.069 7.448 1.00 56.94 O
ANISOU 2201 OG1 THR A 364 6427 9578 5629 277 850 274 O
ATOM 2202 CG2 THR A 364 -22.155 -23.788 7.354 1.00 61.67 C
ANISOU 2202 CG2 THR A 364 7076 10100 6257 468 766 239 C
ATOM 2203 N TRP A 365 -25.110 -26.753 5.195 1.00 65.52 N
ANISOU 2203 N TRP A 365 7359 10842 6693 175 818 181 N
ATOM 2204 CA TRP A 365 -25.404 -27.908 4.359 1.00 64.62 C
ANISOU 2204 CA TRP A 365 7279 10716 6559 26 836 188 C
ATOM 2205 C TRP A 365 -26.709 -27.739 3.577 1.00 67.69 C
ANISOU 2205 C TRP A 365 7505 11314 6902 3 809 102 C
ATOM 2206 O TRP A 365 -26.815 -28.292 2.487 1.00 67.80 O
ANISOU 2206 O TRP A 365 7546 11303 6912 -67 793 99 O
ATOM 2207 CB TRP A 365 -25.420 -29.210 5.171 1.00 64.04 C
ANISOU 2207 CB TRP A 365 7306 10603 6425 -165 915 225 C
ATOM 2208 CG TRP A 365 -24.251 -29.381 6.102 1.00 64.42 C
ANISOU 2208 CG TRP A 365 7494 10496 6487 -109 936 303 C
ATOM 2209 CD1 TRP A 365 -24.302 -29.514 7.457 1.00 67.74 C
ANISOU 2209 CD1 TRP A 365 7927 10953 6858 -152 984 320 C
ATOM 2210 CD2 TRP A 365 -22.861 -29.463 5.745 1.00 63.44 C
ANISOU 2210 CD2 TRP A 365 7496 10199 6408 5 908 366 C
ATOM 2211 NE1 TRP A 365 -23.033 -29.612 7.977 1.00 66.67 N
ANISOU 2211 NE1 TRP A 365 7916 10678 6737 -55 978 391 N
ATOM 2212 CE2 TRP A 365 -22.128 -29.617 6.949 1.00 66.83 C
ANISOU 2212 CE2 TRP A 365 7999 10585 6809 42 934 416 C
ATOM 2213 CE3 TRP A 365 -22.158 -29.433 4.523 1.00 63.86 C
ANISOU 2213 CE3 TRP A 365 7595 10165 6505 79 864 379 C
ATOM 2214 CZ2 TRP A 365 -20.737 -29.745 6.972 1.00 64.82 C
ANISOU 2214 CZ2 TRP A 365 7836 10233 6558 161 913 471 C
ATOM 2215 CZ3 TRP A 365 -20.769 -29.523 4.554 1.00 64.51 C
ANISOU 2215 CZ3 TRP A 365 7764 10154 6593 185 851 430 C
ATOM 2216 CH2 TRP A 365 -20.075 -29.680 5.766 1.00 64.89 C
ANISOU 2216 CH2 TRP A 365 7861 10191 6604 231 874 472 C
ATOM 2217 N SER A 366 -27.686 -26.972 4.092 1.00 64.06 N
ANISOU 2217 N SER A 366 6868 11083 6390 82 798 22 N
ATOM 2218 CA SER A 366 -28.960 -26.786 3.384 1.00 64.26 C
ANISOU 2218 CA SER A 366 6699 11377 6340 96 764 -75 C
ATOM 2219 C SER A 366 -28.868 -25.767 2.287 1.00 67.20 C
ANISOU 2219 C SER A 366 7078 11709 6745 327 665 -86 C
ATOM 2220 O SER A 366 -29.458 -25.977 1.235 1.00 67.72 O
ANISOU 2220 O SER A 366 7070 11887 6773 303 629 -123 O
ATOM 2221 CB SER A 366 -30.072 -26.366 4.337 1.00 68.33 C
ANISOU 2221 CB SER A 366 6999 12209 6755 132 786 -174 C
ATOM 2222 OG SER A 366 -30.326 -27.353 5.322 1.00 78.26 O
ANISOU 2222 OG SER A 366 8244 13541 7949 -125 884 -168 O
ATOM 2223 N LEU A 367 -28.189 -24.637 2.544 1.00 63.21 N
ANISOU 2223 N LEU A 367 6676 11052 6287 537 621 -58 N
ATOM 2224 CA LEU A 367 -28.079 -23.530 1.598 1.00 62.88 C
ANISOU 2224 CA LEU A 367 6706 10935 6250 757 525 -60 C
ATOM 2225 C LEU A 367 -27.404 -23.959 0.272 1.00 66.31 C
ANISOU 2225 C LEU A 367 7252 11210 6732 682 501 4 C
ATOM 2226 O LEU A 367 -28.071 -23.770 -0.752 1.00 68.25 O
ANISOU 2226 O LEU A 367 7434 11566 6930 759 439 -34 O
ATOM 2227 CB LEU A 367 -27.386 -22.312 2.233 1.00 62.42 C
ANISOU 2227 CB LEU A 367 6803 10702 6213 927 498 -37 C
ATOM 2228 CG LEU A 367 -28.272 -21.174 2.822 1.00 67.94 C
ANISOU 2228 CG LEU A 367 7446 11543 6826 1179 453 -130 C
ATOM 2229 CD1 LEU A 367 -29.716 -21.596 3.090 1.00 68.47 C
ANISOU 2229 CD1 LEU A 367 7230 11990 6796 1193 469 -239 C
ATOM 2230 CD2 LEU A 367 -27.649 -20.602 4.064 1.00 70.54 C
ANISOU 2230 CD2 LEU A 367 7887 11743 7173 1204 485 -118 C
ATOM 2231 N PRO A 368 -26.190 -24.600 0.227 1.00 59.59 N
ANISOU 2231 N PRO A 368 6542 10147 5954 548 544 89 N
ATOM 2232 CA PRO A 368 -25.636 -25.040 -1.077 1.00 57.72 C
ANISOU 2232 CA PRO A 368 6386 9804 5740 492 522 130 C
ATOM 2233 C PRO A 368 -26.454 -26.150 -1.751 1.00 62.37 C
ANISOU 2233 C PRO A 368 6879 10528 6290 345 540 88 C
ATOM 2234 O PRO A 368 -26.464 -26.236 -2.985 1.00 62.22 O
ANISOU 2234 O PRO A 368 6880 10499 6261 347 499 88 O
ATOM 2235 CB PRO A 368 -24.247 -25.571 -0.736 1.00 58.13 C
ANISOU 2235 CB PRO A 368 6571 9668 5847 408 572 206 C
ATOM 2236 CG PRO A 368 -24.003 -25.238 0.654 1.00 63.08 C
ANISOU 2236 CG PRO A 368 7200 10285 6482 431 606 213 C
ATOM 2237 CD PRO A 368 -25.279 -24.948 1.337 1.00 60.17 C
ANISOU 2237 CD PRO A 368 6692 10102 6068 468 608 140 C
ATOM 2238 N PHE A 369 -27.144 -26.993 -0.951 1.00 58.54 N
ANISOU 2238 N PHE A 369 6302 10174 5765 194 603 48 N
ATOM 2239 CA PHE A 369 -27.992 -28.065 -1.466 1.00 59.10 C
ANISOU 2239 CA PHE A 369 6299 10390 5768 -7 630 -4 C
ATOM 2240 C PHE A 369 -29.107 -27.486 -2.334 1.00 63.68 C
ANISOU 2240 C PHE A 369 6695 11226 6274 87 556 -88 C
ATOM 2241 O PHE A 369 -29.272 -27.906 -3.482 1.00 63.86 O
ANISOU 2241 O PHE A 369 6721 11271 6271 21 528 -104 O
ATOM 2242 CB PHE A 369 -28.578 -28.889 -0.305 1.00 61.70 C
ANISOU 2242 CB PHE A 369 6576 10835 6033 -211 715 -34 C
ATOM 2243 CG PHE A 369 -29.599 -29.930 -0.712 1.00 64.58 C
ANISOU 2243 CG PHE A 369 6862 11389 6288 -478 750 -105 C
ATOM 2244 CD1 PHE A 369 -30.958 -29.632 -0.713 1.00 68.61 C
ANISOU 2244 CD1 PHE A 369 7102 12281 6685 -508 734 -216 C
ATOM 2245 CD2 PHE A 369 -29.200 -31.210 -1.086 1.00 66.49 C
ANISOU 2245 CD2 PHE A 369 7306 11443 6512 -699 798 -71 C
ATOM 2246 CE1 PHE A 369 -31.899 -30.593 -1.087 1.00 71.36 C
ANISOU 2246 CE1 PHE A 369 7362 12847 6904 -805 772 -294 C
ATOM 2247 CE2 PHE A 369 -30.142 -32.173 -1.457 1.00 70.85 C
ANISOU 2247 CE2 PHE A 369 7824 12155 6940 -993 835 -144 C
ATOM 2248 CZ PHE A 369 -31.486 -31.857 -1.454 1.00 70.81 C
ANISOU 2248 CZ PHE A 369 7527 12556 6822 -1069 824 -255 C
ATOM 2249 N VAL A 370 -29.860 -26.512 -1.773 1.00 59.57 N
ANISOU 2249 N VAL A 370 6020 10909 5706 266 520 -147 N
ATOM 2250 CA VAL A 370 -30.965 -25.805 -2.422 1.00 60.13 C
ANISOU 2250 CA VAL A 370 5902 11268 5676 441 437 -238 C
ATOM 2251 C VAL A 370 -30.464 -25.213 -3.747 1.00 62.84 C
ANISOU 2251 C VAL A 370 6375 11452 6049 602 348 -190 C
ATOM 2252 O VAL A 370 -31.130 -25.398 -4.759 1.00 63.53 O
ANISOU 2252 O VAL A 370 6356 11721 6061 598 298 -241 O
ATOM 2253 CB VAL A 370 -31.558 -24.742 -1.461 1.00 64.43 C
ANISOU 2253 CB VAL A 370 6332 11982 6168 682 410 -298 C
ATOM 2254 CG1 VAL A 370 -32.422 -23.715 -2.184 1.00 65.66 C
ANISOU 2254 CG1 VAL A 370 6370 12360 6216 994 295 -375 C
ATOM 2255 CG2 VAL A 370 -32.346 -25.410 -0.350 1.00 65.29 C
ANISOU 2255 CG2 VAL A 370 6246 12362 6201 494 497 -371 C
ATOM 2256 N LEU A 371 -29.262 -24.583 -3.750 1.00 57.60 N
ANISOU 2256 N LEU A 371 5940 10467 5478 703 334 -94 N
ATOM 2257 CA LEU A 371 -28.640 -24.001 -4.940 1.00 56.71 C
ANISOU 2257 CA LEU A 371 5985 10184 5380 813 263 -37 C
ATOM 2258 C LEU A 371 -28.302 -25.072 -5.964 1.00 61.96 C
ANISOU 2258 C LEU A 371 6675 10804 6063 615 286 -17 C
ATOM 2259 O LEU A 371 -28.695 -24.923 -7.115 1.00 63.23 O
ANISOU 2259 O LEU A 371 6807 11053 6165 672 220 -38 O
ATOM 2260 CB LEU A 371 -27.378 -23.223 -4.592 1.00 55.30 C
ANISOU 2260 CB LEU A 371 6033 9707 5270 878 267 52 C
ATOM 2261 CG LEU A 371 -27.549 -21.917 -3.866 1.00 60.96 C
ANISOU 2261 CG LEU A 371 6820 10390 5953 1101 223 39 C
ATOM 2262 CD1 LEU A 371 -26.298 -21.593 -3.098 1.00 60.54 C
ANISOU 2262 CD1 LEU A 371 6942 10091 5968 1036 271 109 C
ATOM 2263 CD2 LEU A 371 -27.919 -20.781 -4.819 1.00 63.54 C
ANISOU 2263 CD2 LEU A 371 7257 10697 6187 1348 110 35 C
ATOM 2264 N THR A 372 -27.601 -26.155 -5.552 1.00 57.68 N
ANISOU 2264 N THR A 372 6202 10130 5585 403 375 19 N
ATOM 2265 CA THR A 372 -27.229 -27.267 -6.432 1.00 57.24 C
ANISOU 2265 CA THR A 372 6212 10002 5534 228 404 29 C
ATOM 2266 C THR A 372 -28.501 -27.862 -7.076 1.00 64.64 C
ANISOU 2266 C THR A 372 6987 11200 6373 113 386 -65 C
ATOM 2267 O THR A 372 -28.576 -27.955 -8.313 1.00 67.44 O
ANISOU 2267 O THR A 372 7353 11580 6693 110 340 -77 O
ATOM 2268 CB THR A 372 -26.416 -28.347 -5.675 1.00 63.77 C
ANISOU 2268 CB THR A 372 7161 10658 6411 67 497 68 C
ATOM 2269 OG1 THR A 372 -25.377 -27.746 -4.895 1.00 65.86 O
ANISOU 2269 OG1 THR A 372 7516 10767 6742 172 512 136 O
ATOM 2270 CG2 THR A 372 -25.815 -29.388 -6.607 1.00 59.79 C
ANISOU 2270 CG2 THR A 372 6789 10023 5905 -46 520 82 C
ATOM 2271 N VAL A 373 -29.513 -28.212 -6.250 1.00 59.31 N
ANISOU 2271 N VAL A 373 6149 10752 5635 7 422 -138 N
ATOM 2272 CA VAL A 373 -30.777 -28.794 -6.724 1.00 59.82 C
ANISOU 2272 CA VAL A 373 6022 11135 5574 -152 415 -245 C
ATOM 2273 C VAL A 373 -31.411 -27.877 -7.821 1.00 63.58 C
ANISOU 2273 C VAL A 373 6363 11816 5977 72 298 -289 C
ATOM 2274 O VAL A 373 -31.821 -28.388 -8.866 1.00 65.05 O
ANISOU 2274 O VAL A 373 6502 12120 6093 -38 272 -335 O
ATOM 2275 CB VAL A 373 -31.723 -29.089 -5.528 1.00 63.98 C
ANISOU 2275 CB VAL A 373 6368 11922 6020 -290 474 -320 C
ATOM 2276 CG1 VAL A 373 -33.142 -29.408 -5.981 1.00 66.11 C
ANISOU 2276 CG1 VAL A 373 6369 12630 6122 -431 455 -452 C
ATOM 2277 CG2 VAL A 373 -31.173 -30.235 -4.693 1.00 62.94 C
ANISOU 2277 CG2 VAL A 373 6416 11577 5921 -558 586 -274 C
ATOM 2278 N ALA A 374 -31.384 -26.539 -7.614 1.00 57.55 N
ANISOU 2278 N ALA A 374 5590 11054 5223 391 226 -267 N
ATOM 2279 CA ALA A 374 -31.894 -25.534 -8.540 1.00 57.39 C
ANISOU 2279 CA ALA A 374 5512 11176 5119 669 104 -291 C
ATOM 2280 C ALA A 374 -31.072 -25.471 -9.876 1.00 61.00 C
ANISOU 2280 C ALA A 374 6165 11402 5610 689 59 -214 C
ATOM 2281 O ALA A 374 -31.637 -25.170 -10.936 1.00 60.33 O
ANISOU 2281 O ALA A 374 6015 11483 5426 806 -31 -248 O
ATOM 2282 CB ALA A 374 -31.887 -24.178 -7.864 1.00 57.65 C
ANISOU 2282 CB ALA A 374 5593 11162 5149 994 50 -273 C
ATOM 2283 N ILE A 375 -29.750 -25.716 -9.819 1.00 56.33 N
ANISOU 2283 N ILE A 375 5799 10464 5139 591 117 -117 N
ATOM 2284 CA ILE A 375 -28.913 -25.656 -11.019 1.00 55.93 C
ANISOU 2284 CA ILE A 375 5918 10226 5106 595 87 -50 C
ATOM 2285 C ILE A 375 -29.248 -26.860 -11.911 1.00 65.09 C
ANISOU 2285 C ILE A 375 7010 11499 6221 377 108 -108 C
ATOM 2286 O ILE A 375 -29.409 -26.714 -13.137 1.00 65.73 O
ANISOU 2286 O ILE A 375 7094 11645 6235 424 41 -115 O
ATOM 2287 CB ILE A 375 -27.415 -25.551 -10.690 1.00 56.20 C
ANISOU 2287 CB ILE A 375 6169 9934 5249 560 144 51 C
ATOM 2288 CG1 ILE A 375 -27.140 -24.227 -10.011 1.00 56.05 C
ANISOU 2288 CG1 ILE A 375 6245 9810 5241 759 109 99 C
ATOM 2289 CG2 ILE A 375 -26.593 -25.638 -11.969 1.00 57.51 C
ANISOU 2289 CG2 ILE A 375 6472 9972 5407 526 127 100 C
ATOM 2290 CD1 ILE A 375 -26.034 -24.227 -9.047 1.00 62.44 C
ANISOU 2290 CD1 ILE A 375 7168 10415 6142 691 183 158 C
ATOM 2291 N LEU A 376 -29.416 -28.028 -11.275 1.00 63.31 N
ANISOU 2291 N LEU A 376 6743 11298 6013 132 198 -151 N
ATOM 2292 CA LEU A 376 -29.812 -29.253 -11.950 1.00 64.41 C
ANISOU 2292 CA LEU A 376 6857 11526 6089 -120 229 -220 C
ATOM 2293 C LEU A 376 -31.214 -29.082 -12.513 1.00 71.77 C
ANISOU 2293 C LEU A 376 7542 12852 6877 -116 157 -327 C
ATOM 2294 O LEU A 376 -31.495 -29.595 -13.597 1.00 73.35 O
ANISOU 2294 O LEU A 376 7723 13146 7002 -227 131 -375 O
ATOM 2295 CB LEU A 376 -29.752 -30.438 -10.987 1.00 64.45 C
ANISOU 2295 CB LEU A 376 6923 11453 6114 -380 339 -239 C
ATOM 2296 CG LEU A 376 -28.418 -30.699 -10.291 1.00 66.75 C
ANISOU 2296 CG LEU A 376 7439 11400 6521 -361 406 -145 C
ATOM 2297 CD1 LEU A 376 -28.587 -31.747 -9.218 1.00 66.94 C
ANISOU 2297 CD1 LEU A 376 7530 11373 6530 -587 500 -163 C
ATOM 2298 CD2 LEU A 376 -27.334 -31.103 -11.289 1.00 67.73 C
ANISOU 2298 CD2 LEU A 376 7753 11303 6678 -342 406 -101 C
ATOM 2299 N ALA A 377 -32.077 -28.311 -11.811 1.00 69.23 N
ANISOU 2299 N ALA A 377 7020 12783 6500 41 118 -371 N
ATOM 2300 CA ALA A 377 -33.432 -28.022 -12.289 1.00 71.59 C
ANISOU 2300 CA ALA A 377 7039 13529 6632 112 37 -485 C
ATOM 2301 C ALA A 377 -33.377 -27.212 -13.603 1.00 76.58 C
ANISOU 2301 C ALA A 377 7713 14171 7213 367 -85 -456 C
ATOM 2302 O ALA A 377 -33.848 -27.714 -14.619 1.00 77.71 O
ANISOU 2302 O ALA A 377 7770 14501 7257 253 -119 -518 O
ATOM 2303 CB ALA A 377 -34.236 -27.287 -11.225 1.00 73.29 C
ANISOU 2303 CB ALA A 377 7049 14006 6791 292 19 -539 C
ATOM 2304 N VAL A 378 -32.698 -26.032 -13.607 1.00 72.29 N
ANISOU 2304 N VAL A 378 7346 13389 6731 672 -142 -354 N
ATOM 2305 CA VAL A 378 -32.537 -25.158 -14.778 1.00 71.64 C
ANISOU 2305 CA VAL A 378 7378 13254 6588 918 -256 -302 C
ATOM 2306 C VAL A 378 -31.639 -25.819 -15.822 1.00 77.46 C
ANISOU 2306 C VAL A 378 8286 13773 7374 727 -225 -247 C
ATOM 2307 O VAL A 378 -31.656 -25.375 -16.975 1.00 80.10 O
ANISOU 2307 O VAL A 378 8676 14133 7626 851 -312 -225 O
ATOM 2308 CB VAL A 378 -32.063 -23.706 -14.465 1.00 73.92 C
ANISOU 2308 CB VAL A 378 7875 13312 6899 1250 -317 -206 C
ATOM 2309 CG1 VAL A 378 -33.084 -22.956 -13.625 1.00 75.54 C
ANISOU 2309 CG1 VAL A 378 7919 13769 7015 1518 -373 -279 C
ATOM 2310 CG2 VAL A 378 -30.701 -23.668 -13.802 1.00 71.09 C
ANISOU 2310 CG2 VAL A 378 7756 12551 6703 1138 -225 -100 C
ATOM 2311 N ALA A 379 -30.886 -26.895 -15.442 1.00 71.69 N
ANISOU 2311 N ALA A 379 7644 12838 6755 444 -106 -232 N
ATOM 2312 CA ALA A 379 -29.968 -27.648 -16.318 1.00 69.53 C
ANISOU 2312 CA ALA A 379 7538 12358 6522 275 -63 -197 C
ATOM 2313 C ALA A 379 -28.984 -26.690 -17.005 1.00 72.48 C
ANISOU 2313 C ALA A 379 8115 12505 6918 457 -110 -84 C
ATOM 2314 O ALA A 379 -29.089 -26.442 -18.204 1.00 73.37 O
ANISOU 2314 O ALA A 379 8256 12680 6944 518 -181 -79 O
ATOM 2315 CB ALA A 379 -30.742 -28.469 -17.344 1.00 71.25 C
ANISOU 2315 CB ALA A 379 7637 12814 6622 112 -89 -296 C
ATOM 2316 N GLN A 380 -28.082 -26.092 -16.205 1.00 66.35 N
ANISOU 2316 N GLN A 380 7481 11492 6238 531 -72 1 N
ATOM 2317 CA GLN A 380 -27.092 -25.119 -16.659 1.00 64.51 C
ANISOU 2317 CA GLN A 380 7458 11046 6006 647 -101 107 C
ATOM 2318 C GLN A 380 -25.684 -25.551 -16.286 1.00 64.80 C
ANISOU 2318 C GLN A 380 7624 10853 6145 510 0 162 C
ATOM 2319 O GLN A 380 -24.815 -24.727 -15.970 1.00 62.57 O
ANISOU 2319 O GLN A 380 7483 10405 5884 563 9 241 O
ATOM 2320 CB GLN A 380 -27.403 -23.738 -16.082 1.00 66.61 C
ANISOU 2320 CB GLN A 380 7788 11283 6240 889 -170 149 C
ATOM 2321 CG GLN A 380 -28.656 -23.109 -16.671 1.00 83.00 C
ANISOU 2321 CG GLN A 380 9775 13590 8173 1113 -296 104 C
ATOM 2322 CD GLN A 380 -28.563 -22.787 -18.136 1.00 95.39 C
ANISOU 2322 CD GLN A 380 11453 15159 9631 1168 -373 143 C
ATOM 2323 OE1 GLN A 380 -27.490 -22.519 -18.695 1.00 94.64 O
ANISOU 2323 OE1 GLN A 380 11572 14842 9545 1099 -352 231 O
ATOM 2324 NE2 GLN A 380 -29.712 -22.759 -18.768 1.00 82.34 N
ANISOU 2324 NE2 GLN A 380 9644 13790 7851 1296 -467 72 N
ATOM 2325 N VAL A 381 -25.461 -26.860 -16.338 1.00 61.14 N
ANISOU 2325 N VAL A 381 7123 10389 5718 333 73 113 N
ATOM 2326 CA VAL A 381 -24.154 -27.429 -16.076 1.00 60.12 C
ANISOU 2326 CA VAL A 381 7100 10086 5655 243 162 146 C
ATOM 2327 C VAL A 381 -23.518 -27.638 -17.430 1.00 67.49 C
ANISOU 2327 C VAL A 381 8112 11004 6526 208 155 153 C
ATOM 2328 O VAL A 381 -24.084 -28.310 -18.306 1.00 68.75 O
ANISOU 2328 O VAL A 381 8232 11261 6628 142 134 90 O
ATOM 2329 CB VAL A 381 -24.183 -28.705 -15.209 1.00 62.98 C
ANISOU 2329 CB VAL A 381 7439 10417 6075 113 245 93 C
ATOM 2330 CG1 VAL A 381 -22.796 -29.308 -15.089 1.00 61.70 C
ANISOU 2330 CG1 VAL A 381 7397 10098 5948 85 320 119 C
ATOM 2331 CG2 VAL A 381 -24.757 -28.409 -13.830 1.00 62.56 C
ANISOU 2331 CG2 VAL A 381 7306 10394 6072 140 257 91 C
ATOM 2332 N ASP A 382 -22.381 -26.974 -17.630 1.00 63.49 N
ANISOU 2332 N ASP A 382 7711 10401 6011 237 169 226 N
ATOM 2333 CA ASP A 382 -21.616 -27.061 -18.863 1.00 62.28 C
ANISOU 2333 CA ASP A 382 7629 10252 5782 197 173 238 C
ATOM 2334 C ASP A 382 -20.187 -27.497 -18.486 1.00 62.92 C
ANISOU 2334 C ASP A 382 7750 10268 5889 153 263 250 C
ATOM 2335 O ASP A 382 -19.751 -27.286 -17.350 1.00 62.24 O
ANISOU 2335 O ASP A 382 7660 10124 5865 170 299 278 O
ATOM 2336 CB ASP A 382 -21.663 -25.713 -19.617 1.00 64.79 C
ANISOU 2336 CB ASP A 382 8040 10572 6006 262 95 313 C
ATOM 2337 CG ASP A 382 -22.963 -24.915 -19.469 1.00 78.19 C
ANISOU 2337 CG ASP A 382 9715 12320 7674 396 -3 319 C
ATOM 2338 OD1 ASP A 382 -23.971 -25.274 -20.139 1.00 80.09 O
ANISOU 2338 OD1 ASP A 382 9864 12704 7864 424 -60 261 O
ATOM 2339 OD2 ASP A 382 -22.965 -23.917 -18.714 1.00 84.98 O
ANISOU 2339 OD2 ASP A 382 10650 13096 8543 484 -27 372 O
ATOM 2340 N GLY A 383 -19.511 -28.180 -19.396 1.00 57.41 N
ANISOU 2340 N GLY A 383 7075 9607 5134 115 297 214 N
ATOM 2341 CA GLY A 383 -18.142 -28.625 -19.169 1.00 56.02 C
ANISOU 2341 CA GLY A 383 6908 9432 4945 115 375 206 C
ATOM 2342 C GLY A 383 -17.117 -27.733 -19.842 1.00 58.92 C
ANISOU 2342 C GLY A 383 7300 9875 5210 72 383 258 C
ATOM 2343 O GLY A 383 -17.466 -26.951 -20.741 1.00 59.49 O
ANISOU 2343 O GLY A 383 7426 9967 5209 36 328 300 O
ATOM 2344 N ASP A 384 -15.846 -27.821 -19.386 1.00 54.64 N
ANISOU 2344 N ASP A 384 6723 9395 4641 68 450 255 N
ATOM 2345 CA ASP A 384 -14.717 -27.083 -19.958 1.00 56.55 C
ANISOU 2345 CA ASP A 384 6963 9767 4754 -23 478 288 C
ATOM 2346 C ASP A 384 -13.461 -27.963 -19.953 1.00 64.71 C
ANISOU 2346 C ASP A 384 7902 10964 5723 27 555 215 C
ATOM 2347 O ASP A 384 -13.131 -28.557 -18.924 1.00 65.14 O
ANISOU 2347 O ASP A 384 7907 11008 5836 123 588 185 O
ATOM 2348 CB ASP A 384 -14.449 -25.734 -19.262 1.00 58.18 C
ANISOU 2348 CB ASP A 384 7221 9937 4949 -116 469 372 C
ATOM 2349 CG ASP A 384 -13.654 -24.707 -20.079 1.00 67.15 C
ANISOU 2349 CG ASP A 384 8426 11171 5918 -287 481 424 C
ATOM 2350 OD1 ASP A 384 -13.348 -23.630 -19.538 1.00 71.18 O
ANISOU 2350 OD1 ASP A 384 9018 11637 6389 -398 481 485 O
ATOM 2351 OD2 ASP A 384 -13.338 -24.985 -21.253 1.00 66.60 O
ANISOU 2351 OD2 ASP A 384 8345 11217 5740 -327 493 400 O
ATOM 2352 N SER A 385 -12.783 -28.058 -21.120 1.00 62.42 N
ANISOU 2352 N SER A 385 7587 10837 5292 -15 580 182 N
ATOM 2353 CA SER A 385 -11.580 -28.861 -21.298 1.00 63.60 C
ANISOU 2353 CA SER A 385 7630 11197 5339 69 648 95 C
ATOM 2354 C SER A 385 -10.367 -28.212 -20.627 1.00 69.95 C
ANISOU 2354 C SER A 385 8316 12206 6057 -4 699 111 C
ATOM 2355 O SER A 385 -9.499 -28.928 -20.127 1.00 70.67 O
ANISOU 2355 O SER A 385 8294 12454 6105 135 744 39 O
ATOM 2356 CB SER A 385 -11.306 -29.079 -22.783 1.00 68.08 C
ANISOU 2356 CB SER A 385 8194 11906 5767 38 659 48 C
ATOM 2357 OG SER A 385 -11.230 -27.842 -23.472 1.00 73.78 O
ANISOU 2357 OG SER A 385 8953 12690 6389 -168 644 127 O
ATOM 2358 N VAL A 386 -10.306 -26.870 -20.607 1.00 67.62 N
ANISOU 2358 N VAL A 386 8064 11913 5715 -218 688 198 N
ATOM 2359 CA VAL A 386 -9.184 -26.159 -20.001 1.00 69.20 C
ANISOU 2359 CA VAL A 386 8167 12319 5808 -356 739 209 C
ATOM 2360 C VAL A 386 -9.328 -26.267 -18.451 1.00 74.55 C
ANISOU 2360 C VAL A 386 8819 12886 6621 -259 732 219 C
ATOM 2361 O VAL A 386 -8.378 -26.708 -17.799 1.00 75.09 O
ANISOU 2361 O VAL A 386 8731 13167 6634 -185 778 161 O
ATOM 2362 CB VAL A 386 -8.988 -24.715 -20.579 1.00 74.69 C
ANISOU 2362 CB VAL A 386 8975 13039 6363 -659 737 293 C
ATOM 2363 CG1 VAL A 386 -10.256 -23.878 -20.540 1.00 74.53 C
ANISOU 2363 CG1 VAL A 386 9192 12679 6447 -697 656 396 C
ATOM 2364 CG2 VAL A 386 -7.820 -23.978 -19.949 1.00 75.28 C
ANISOU 2364 CG2 VAL A 386 8956 13349 6298 -864 797 291 C
ATOM 2365 N SER A 387 -10.540 -26.033 -17.894 1.00 71.13 N
ANISOU 2365 N SER A 387 8519 12153 6356 -219 673 278 N
ATOM 2366 CA SER A 387 -10.779 -26.193 -16.457 1.00 69.67 C
ANISOU 2366 CA SER A 387 8315 11860 6296 -126 668 286 C
ATOM 2367 C SER A 387 -10.754 -27.674 -16.044 1.00 74.48 C
ANISOU 2367 C SER A 387 8861 12470 6970 110 686 212 C
ATOM 2368 O SER A 387 -10.244 -27.997 -14.973 1.00 75.86 O
ANISOU 2368 O SER A 387 8963 12702 7159 199 709 193 O
ATOM 2369 CB SER A 387 -12.096 -25.550 -16.046 1.00 70.80 C
ANISOU 2369 CB SER A 387 8603 11728 6571 -142 605 355 C
ATOM 2370 OG SER A 387 -13.186 -26.431 -16.222 1.00 79.16 O
ANISOU 2370 OG SER A 387 9694 12644 7739 -6 570 331 O
ATOM 2371 N GLY A 388 -11.303 -28.550 -16.878 1.00 69.71 N
ANISOU 2371 N GLY A 388 8311 11792 6384 204 672 171 N
ATOM 2372 CA GLY A 388 -11.346 -29.981 -16.587 1.00 69.25 C
ANISOU 2372 CA GLY A 388 8275 11677 6359 413 686 100 C
ATOM 2373 C GLY A 388 -12.520 -30.423 -15.730 1.00 69.88 C
ANISOU 2373 C GLY A 388 8462 11497 6591 454 657 123 C
ATOM 2374 O GLY A 388 -12.723 -31.621 -15.515 1.00 69.46 O
ANISOU 2374 O GLY A 388 8494 11342 6556 586 666 73 O
ATOM 2375 N ILE A 389 -13.309 -29.472 -15.243 1.00 64.69 N
ANISOU 2375 N ILE A 389 7820 10736 6024 338 622 193 N
ATOM 2376 CA ILE A 389 -14.497 -29.778 -14.441 1.00 63.31 C
ANISOU 2376 CA ILE A 389 7711 10370 5974 351 598 209 C
ATOM 2377 C ILE A 389 -15.786 -29.314 -15.189 1.00 67.19 C
ANISOU 2377 C ILE A 389 8244 10783 6503 261 541 227 C
ATOM 2378 O ILE A 389 -15.728 -28.698 -16.257 1.00 63.40 O
ANISOU 2378 O ILE A 389 7767 10366 5957 201 516 243 O
ATOM 2379 CB ILE A 389 -14.421 -29.183 -12.983 1.00 64.33 C
ANISOU 2379 CB ILE A 389 7803 10472 6166 345 604 256 C
ATOM 2380 CG1 ILE A 389 -14.241 -27.653 -12.991 1.00 64.53 C
ANISOU 2380 CG1 ILE A 389 7804 10545 6168 224 583 315 C
ATOM 2381 CG2 ILE A 389 -13.364 -29.884 -12.110 1.00 62.82 C
ANISOU 2381 CG2 ILE A 389 7574 10358 5937 469 649 231 C
ATOM 2382 CD1 ILE A 389 -15.252 -26.906 -12.178 1.00 70.74 C
ANISOU 2382 CD1 ILE A 389 8629 11205 7046 198 546 358 C
ATOM 2383 N CYS A 390 -16.948 -29.650 -14.598 1.00 66.66 N
ANISOU 2383 N CYS A 390 8203 10605 6521 256 521 221 N
ATOM 2384 CA CYS A 390 -18.269 -29.208 -15.039 1.00 66.29 C
ANISOU 2384 CA CYS A 390 8151 10537 6498 202 462 226 C
ATOM 2385 C CYS A 390 -18.724 -28.164 -14.029 1.00 62.42 C
ANISOU 2385 C CYS A 390 7629 10021 6066 209 436 277 C
ATOM 2386 O CYS A 390 -18.459 -28.317 -12.831 1.00 59.33 O
ANISOU 2386 O CYS A 390 7224 9594 5724 231 472 287 O
ATOM 2387 CB CYS A 390 -19.250 -30.373 -15.160 1.00 68.14 C
ANISOU 2387 CB CYS A 390 8415 10728 6748 164 463 159 C
ATOM 2388 SG CYS A 390 -19.215 -31.209 -16.772 1.00 73.85 S
ANISOU 2388 SG CYS A 390 9196 11486 7379 130 455 91 S
ATOM 2389 N PHE A 391 -19.304 -27.066 -14.512 1.00 56.14 N
ANISOU 2389 N PHE A 391 6844 9242 5246 211 372 311 N
ATOM 2390 CA PHE A 391 -19.737 -26.006 -13.625 1.00 54.58 C
ANISOU 2390 CA PHE A 391 6652 9006 5079 253 340 350 C
ATOM 2391 C PHE A 391 -20.980 -25.303 -14.140 1.00 58.85 C
ANISOU 2391 C PHE A 391 7198 9577 5587 319 254 350 C
ATOM 2392 O PHE A 391 -21.464 -25.589 -15.236 1.00 58.11 O
ANISOU 2392 O PHE A 391 7091 9546 5441 315 216 325 O
ATOM 2393 CB PHE A 391 -18.598 -25.000 -13.386 1.00 55.82 C
ANISOU 2393 CB PHE A 391 6884 9130 5195 219 356 410 C
ATOM 2394 CG PHE A 391 -18.566 -24.485 -11.965 1.00 57.23 C
ANISOU 2394 CG PHE A 391 7062 9256 5427 241 371 427 C
ATOM 2395 CD1 PHE A 391 -18.269 -25.337 -10.901 1.00 59.33 C
ANISOU 2395 CD1 PHE A 391 7250 9533 5758 247 428 402 C
ATOM 2396 CD2 PHE A 391 -18.870 -23.159 -11.680 1.00 59.78 C
ANISOU 2396 CD2 PHE A 391 7491 9505 5718 269 322 466 C
ATOM 2397 CE1 PHE A 391 -18.274 -24.868 -9.588 1.00 59.22 C
ANISOU 2397 CE1 PHE A 391 7231 9484 5786 265 440 415 C
ATOM 2398 CE2 PHE A 391 -18.843 -22.685 -10.365 1.00 61.41 C
ANISOU 2398 CE2 PHE A 391 7706 9662 5965 290 337 471 C
ATOM 2399 CZ PHE A 391 -18.558 -23.546 -9.331 1.00 58.64 C
ANISOU 2399 CZ PHE A 391 7242 9350 5687 282 397 445 C
ATOM 2400 N VAL A 392 -21.508 -24.398 -13.317 1.00 57.53 N
ANISOU 2400 N VAL A 392 7045 9379 5435 401 219 368 N
ATOM 2401 CA VAL A 392 -22.683 -23.577 -13.595 1.00 59.41 C
ANISOU 2401 CA VAL A 392 7292 9661 5619 535 126 363 C
ATOM 2402 C VAL A 392 -22.242 -22.248 -14.278 1.00 65.93 C
ANISOU 2402 C VAL A 392 8327 10378 6345 584 69 438 C
ATOM 2403 O VAL A 392 -21.297 -21.576 -13.840 1.00 66.10 O
ANISOU 2403 O VAL A 392 8480 10279 6355 523 100 489 O
ATOM 2404 CB VAL A 392 -23.575 -23.346 -12.325 1.00 62.72 C
ANISOU 2404 CB VAL A 392 7624 10126 6082 633 117 326 C
ATOM 2405 CG1 VAL A 392 -22.787 -22.753 -11.155 1.00 61.90 C
ANISOU 2405 CG1 VAL A 392 7603 9894 6023 623 161 365 C
ATOM 2406 CG2 VAL A 392 -24.794 -22.492 -12.639 1.00 63.80 C
ANISOU 2406 CG2 VAL A 392 7755 10353 6133 830 12 304 C
ATOM 2407 N GLY A 393 -22.926 -21.918 -15.363 1.00 63.00 N
ANISOU 2407 N GLY A 393 7998 10058 5882 674 -14 441 N
ATOM 2408 CA GLY A 393 -22.703 -20.675 -16.082 1.00 63.95 C
ANISOU 2408 CA GLY A 393 8364 10057 5876 734 -82 517 C
ATOM 2409 C GLY A 393 -21.460 -20.604 -16.933 1.00 67.22 C
ANISOU 2409 C GLY A 393 8906 10407 6227 552 -39 576 C
ATOM 2410 O GLY A 393 -20.877 -19.526 -17.095 1.00 68.85 O
ANISOU 2410 O GLY A 393 9357 10469 6333 510 -56 650 O
ATOM 2411 N TYR A 394 -21.062 -21.734 -17.504 1.00 60.65 N
ANISOU 2411 N TYR A 394 7928 9685 5429 436 17 538 N
ATOM 2412 CA TYR A 394 -19.922 -21.743 -18.394 1.00 59.39 C
ANISOU 2412 CA TYR A 394 7849 9526 5189 278 61 575 C
ATOM 2413 C TYR A 394 -20.371 -21.143 -19.734 1.00 66.60 C
ANISOU 2413 C TYR A 394 8906 10437 5961 327 -26 618 C
ATOM 2414 O TYR A 394 -19.690 -20.239 -20.233 1.00 67.61 O
ANISOU 2414 O TYR A 394 9250 10477 5964 235 -31 694 O
ATOM 2415 CB TYR A 394 -19.326 -23.154 -18.538 1.00 57.67 C
ANISOU 2415 CB TYR A 394 7451 9426 5036 185 145 508 C
ATOM 2416 CG TYR A 394 -18.231 -23.496 -17.544 1.00 55.40 C
ANISOU 2416 CG TYR A 394 7102 9140 4808 101 239 498 C
ATOM 2417 CD1 TYR A 394 -17.619 -22.507 -16.777 1.00 56.78 C
ANISOU 2417 CD1 TYR A 394 7375 9239 4960 44 255 549 C
ATOM 2418 CD2 TYR A 394 -17.765 -24.799 -17.415 1.00 54.39 C
ANISOU 2418 CD2 TYR A 394 6839 9093 4734 85 307 432 C
ATOM 2419 CE1 TYR A 394 -16.583 -22.814 -15.890 1.00 55.11 C
ANISOU 2419 CE1 TYR A 394 7082 9076 4781 -30 335 533 C
ATOM 2420 CE2 TYR A 394 -16.739 -25.119 -16.524 1.00 54.05 C
ANISOU 2420 CE2 TYR A 394 6736 9078 4720 53 381 420 C
ATOM 2421 CZ TYR A 394 -16.128 -24.118 -15.786 1.00 56.48 C
ANISOU 2421 CZ TYR A 394 7098 9357 5003 -10 395 470 C
ATOM 2422 OH TYR A 394 -15.087 -24.429 -14.937 1.00 51.27 O
ANISOU 2422 OH TYR A 394 6355 8775 4351 -41 462 451 O
ATOM 2423 N LYS A 395 -21.558 -21.578 -20.265 1.00 63.75 N
ANISOU 2423 N LYS A 395 8439 10183 5598 462 -97 569 N
ATOM 2424 CA LYS A 395 -22.157 -21.078 -21.519 1.00 64.70 C
ANISOU 2424 CA LYS A 395 8671 10338 5575 553 -196 601 C
ATOM 2425 C LYS A 395 -23.106 -19.872 -21.250 1.00 72.39 C
ANISOU 2425 C LYS A 395 9806 11231 6469 792 -312 642 C
ATOM 2426 O LYS A 395 -23.154 -18.952 -22.068 1.00 72.56 O
ANISOU 2426 O LYS A 395 10071 11168 6332 864 -390 717 O
ATOM 2427 CB LYS A 395 -22.898 -22.200 -22.274 1.00 66.63 C
ANISOU 2427 CB LYS A 395 8706 10781 5830 564 -214 513 C
ATOM 2428 CG LYS A 395 -22.821 -22.118 -23.826 1.00 91.31 C
ANISOU 2428 CG LYS A 395 11919 13967 8808 535 -261 540 C
ATOM 2429 CD LYS A 395 -23.785 -21.085 -24.495 1.00102.43 C
ANISOU 2429 CD LYS A 395 13473 15386 10060 747 -405 591 C
ATOM 2430 CE LYS A 395 -24.196 -21.406 -25.915 1.00112.68 C
ANISOU 2430 CE LYS A 395 14729 16847 11238 763 -468 567 C
ATOM 2431 NZ LYS A 395 -23.125 -21.123 -26.909 1.00120.89 N
ANISOU 2431 NZ LYS A 395 15957 17815 12162 611 -437 642 N
ATOM 2432 N ASN A 396 -23.825 -19.852 -20.103 1.00 71.52 N
ANISOU 2432 N ASN A 396 9585 11144 6447 929 -325 593 N
ATOM 2433 CA ASN A 396 -24.711 -18.732 -19.783 1.00 74.17 C
ANISOU 2433 CA ASN A 396 10068 11421 6693 1203 -435 613 C
ATOM 2434 C ASN A 396 -24.192 -17.918 -18.608 1.00 80.86 C
ANISOU 2434 C ASN A 396 11092 12056 7576 1200 -400 652 C
ATOM 2435 O ASN A 396 -24.447 -18.262 -17.449 1.00 80.25 O
ANISOU 2435 O ASN A 396 10841 12030 7620 1219 -355 592 O
ATOM 2436 CB ASN A 396 -26.121 -19.214 -19.516 1.00 77.43 C
ANISOU 2436 CB ASN A 396 10205 12089 7125 1401 -496 509 C
ATOM 2437 CG ASN A 396 -26.878 -19.525 -20.776 1.00108.73 C
ANISOU 2437 CG ASN A 396 14076 16261 10976 1482 -580 478 C
ATOM 2438 OD1 ASN A 396 -26.494 -20.404 -21.574 1.00 91.20 O
ANISOU 2438 OD1 ASN A 396 11762 14113 8775 1284 -532 461 O
ATOM 2439 ND2 ASN A 396 -27.975 -18.794 -20.981 1.00109.13 N
ANISOU 2439 ND2 ASN A 396 14151 16425 10888 1798 -713 461 N
ATOM 2440 N TYR A 397 -23.496 -16.806 -18.912 1.00 80.18 N
ANISOU 2440 N TYR A 397 11374 11728 7361 1162 -422 752 N
ATOM 2441 CA TYR A 397 -22.926 -15.901 -17.904 1.00 81.08 C
ANISOU 2441 CA TYR A 397 11724 11613 7470 1120 -392 791 C
ATOM 2442 C TYR A 397 -23.997 -15.385 -16.919 1.00 86.83 C
ANISOU 2442 C TYR A 397 12453 12331 8209 1432 -464 739 C
ATOM 2443 O TYR A 397 -23.656 -15.015 -15.793 1.00 87.13 O
ANISOU 2443 O TYR A 397 12562 12245 8298 1396 -419 732 O
ATOM 2444 CB TYR A 397 -22.192 -14.723 -18.572 1.00 84.54 C
ANISOU 2444 CB TYR A 397 12616 11791 7715 1012 -419 905 C
ATOM 2445 CG TYR A 397 -23.069 -13.769 -19.359 1.00 89.69 C
ANISOU 2445 CG TYR A 397 13576 12329 8171 1304 -567 957 C
ATOM 2446 CD1 TYR A 397 -23.249 -13.926 -20.731 1.00 92.44 C
ANISOU 2446 CD1 TYR A 397 13953 12761 8409 1323 -623 994 C
ATOM 2447 CD2 TYR A 397 -23.660 -12.666 -18.744 1.00 92.67 C
ANISOU 2447 CD2 TYR A 397 14252 12507 8453 1577 -655 968 C
ATOM 2448 CE1 TYR A 397 -24.027 -13.026 -21.465 1.00 96.65 C
ANISOU 2448 CE1 TYR A 397 14791 13193 8737 1620 -769 1047 C
ATOM 2449 CE2 TYR A 397 -24.453 -11.773 -19.462 1.00 96.62 C
ANISOU 2449 CE2 TYR A 397 15069 12897 8746 1902 -803 1014 C
ATOM 2450 CZ TYR A 397 -24.629 -11.951 -20.823 1.00106.48 C
ANISOU 2450 CZ TYR A 397 16337 14239 9883 1924 -863 1058 C
ATOM 2451 OH TYR A 397 -25.410 -11.053 -21.513 1.00111.84 O
ANISOU 2451 OH TYR A 397 17346 14812 10336 2277 -1019 1108 O
ATOM 2452 N ARG A 398 -25.280 -15.350 -17.362 1.00 84.01 N
ANISOU 2452 N ARG A 398 12004 12133 7783 1742 -576 694 N
ATOM 2453 CA ARG A 398 -26.436 -14.927 -16.570 1.00 84.14 C
ANISOU 2453 CA ARG A 398 11962 12234 7774 2088 -655 621 C
ATOM 2454 C ARG A 398 -26.581 -15.844 -15.354 1.00 84.73 C
ANISOU 2454 C ARG A 398 11669 12487 8038 1993 -558 527 C
ATOM 2455 O ARG A 398 -26.620 -15.350 -14.222 1.00 85.22 O
ANISOU 2455 O ARG A 398 11792 12462 8126 2083 -545 503 O
ATOM 2456 CB ARG A 398 -27.728 -14.934 -17.420 1.00 85.63 C
ANISOU 2456 CB ARG A 398 12031 12669 7834 2407 -788 573 C
ATOM 2457 CG ARG A 398 -27.810 -13.844 -18.488 1.00102.33 C
ANISOU 2457 CG ARG A 398 14561 14600 9721 2613 -915 666 C
ATOM 2458 CD ARG A 398 -28.645 -12.646 -18.054 1.00121.28 C
ANISOU 2458 CD ARG A 398 17216 16911 11955 3068 -1046 651 C
ATOM 2459 NE ARG A 398 -29.033 -11.803 -19.191 1.00134.82 N
ANISOU 2459 NE ARG A 398 19279 18523 13424 3345 -1194 723 N
ATOM 2460 CZ ARG A 398 -29.685 -10.646 -19.086 1.00149.45 C
ANISOU 2460 CZ ARG A 398 21474 20238 15073 3787 -1332 731 C
ATOM 2461 NH1 ARG A 398 -30.021 -10.170 -17.892 1.00138.28 N
ANISOU 2461 NH1 ARG A 398 20087 18776 13676 3999 -1336 663 N
ATOM 2462 NH2 ARG A 398 -29.999 -9.954 -20.173 1.00134.19 N
ANISOU 2462 NH2 ARG A 398 19879 18205 12902 4040 -1469 807 N
ATOM 2463 N TYR A 399 -26.597 -17.177 -15.584 1.00 77.31 N
ANISOU 2463 N TYR A 399 10387 11772 7216 1795 -487 476 N
ATOM 2464 CA TYR A 399 -26.732 -18.163 -14.516 1.00 75.01 C
ANISOU 2464 CA TYR A 399 9782 11636 7081 1673 -393 396 C
ATOM 2465 C TYR A 399 -25.492 -18.172 -13.604 1.00 77.61 C
ANISOU 2465 C TYR A 399 10209 11759 7521 1447 -282 441 C
ATOM 2466 O TYR A 399 -25.604 -18.488 -12.415 1.00 75.72 O
ANISOU 2466 O TYR A 399 9823 11569 7378 1422 -224 393 O
ATOM 2467 CB TYR A 399 -27.014 -19.558 -15.086 1.00 75.08 C
ANISOU 2467 CB TYR A 399 9491 11885 7149 1508 -352 337 C
ATOM 2468 CG TYR A 399 -28.416 -19.713 -15.635 1.00 79.03 C
ANISOU 2468 CG TYR A 399 9791 12691 7547 1704 -448 253 C
ATOM 2469 CD1 TYR A 399 -28.690 -19.480 -16.982 1.00 82.80 C
ANISOU 2469 CD1 TYR A 399 10341 13226 7894 1797 -539 276 C
ATOM 2470 CD2 TYR A 399 -29.469 -20.097 -14.812 1.00 80.35 C
ANISOU 2470 CD2 TYR A 399 9679 13128 7724 1784 -446 144 C
ATOM 2471 CE1 TYR A 399 -29.979 -19.628 -17.495 1.00 86.06 C
ANISOU 2471 CE1 TYR A 399 10538 13972 8189 1981 -634 188 C
ATOM 2472 CE2 TYR A 399 -30.764 -20.235 -15.309 1.00 83.41 C
ANISOU 2472 CE2 TYR A 399 9838 13869 7986 1948 -533 50 C
ATOM 2473 CZ TYR A 399 -31.016 -20.002 -16.652 1.00 94.42 C
ANISOU 2473 CZ TYR A 399 11295 15330 9251 2055 -631 70 C
ATOM 2474 OH TYR A 399 -32.292 -20.156 -17.143 1.00 99.27 O
ANISOU 2474 OH TYR A 399 11653 16342 9722 2218 -722 -33 O
ATOM 2475 N ARG A 400 -24.330 -17.771 -14.144 1.00 74.89 N
ANISOU 2475 N ARG A 400 10106 11211 7139 1280 -256 530 N
ATOM 2476 CA ARG A 400 -23.082 -17.688 -13.386 1.00 73.48 C
ANISOU 2476 CA ARG A 400 10012 10884 7024 1057 -159 567 C
ATOM 2477 C ARG A 400 -23.174 -16.568 -12.356 1.00 77.17 C
ANISOU 2477 C ARG A 400 10687 11183 7452 1180 -185 573 C
ATOM 2478 O ARG A 400 -22.720 -16.758 -11.230 1.00 76.50 O
ANISOU 2478 O ARG A 400 10520 11088 7459 1085 -112 550 O
ATOM 2479 CB ARG A 400 -21.888 -17.477 -14.319 1.00 75.28 C
ANISOU 2479 CB ARG A 400 10424 11003 7176 835 -127 646 C
ATOM 2480 CG ARG A 400 -20.574 -17.990 -13.757 1.00 86.11 C
ANISOU 2480 CG ARG A 400 11714 12382 8624 568 -8 651 C
ATOM 2481 CD ARG A 400 -19.581 -16.845 -13.668 1.00 96.09 C
ANISOU 2481 CD ARG A 400 13284 13459 9766 407 7 719 C
ATOM 2482 NE ARG A 400 -18.195 -17.315 -13.691 1.00 93.06 N
ANISOU 2482 NE ARG A 400 12812 13161 9386 127 110 726 N
ATOM 2483 CZ ARG A 400 -17.471 -17.476 -14.793 1.00 91.82 C
ANISOU 2483 CZ ARG A 400 12684 13067 9136 -41 135 758 C
ATOM 2484 NH1 ARG A 400 -18.000 -17.221 -15.989 1.00 64.42 N
ANISOU 2484 NH1 ARG A 400 9349 9556 5570 28 65 797 N
ATOM 2485 NH2 ARG A 400 -16.218 -17.906 -14.711 1.00 73.21 N
ANISOU 2485 NH2 ARG A 400 10208 10845 6764 -265 229 746 N
ATOM 2486 N ALA A 401 -23.810 -15.429 -12.708 1.00 74.15 N
ANISOU 2486 N ALA A 401 10580 10672 6922 1416 -295 598 N
ATOM 2487 CA ALA A 401 -24.003 -14.312 -11.773 1.00 74.62 C
ANISOU 2487 CA ALA A 401 10890 10546 6916 1579 -332 591 C
ATOM 2488 C ALA A 401 -24.975 -14.685 -10.645 1.00 75.65 C
ANISOU 2488 C ALA A 401 10741 10867 7134 1779 -331 488 C
ATOM 2489 O ALA A 401 -24.699 -14.408 -9.485 1.00 74.64 O
ANISOU 2489 O ALA A 401 10654 10658 7050 1753 -286 465 O
ATOM 2490 CB ALA A 401 -24.524 -13.099 -12.512 1.00 78.27 C
ANISOU 2490 CB ALA A 401 11739 10825 7175 1838 -462 636 C
ATOM 2491 N GLY A 402 -26.082 -15.333 -11.003 1.00 70.35 N
ANISOU 2491 N GLY A 402 9781 10474 6474 1948 -374 421 N
ATOM 2492 CA GLY A 402 -27.108 -15.743 -10.060 1.00 69.04 C
ANISOU 2492 CA GLY A 402 9317 10559 6358 2111 -371 313 C
ATOM 2493 C GLY A 402 -26.727 -16.849 -9.108 1.00 69.35 C
ANISOU 2493 C GLY A 402 9076 10707 6565 1855 -244 279 C
ATOM 2494 O GLY A 402 -27.251 -16.877 -8.005 1.00 68.69 O
ANISOU 2494 O GLY A 402 8859 10728 6511 1943 -222 211 O
ATOM 2495 N PHE A 403 -25.831 -17.776 -9.520 1.00 65.00 N
ANISOU 2495 N PHE A 403 8447 10140 6109 1558 -163 324 N
ATOM 2496 CA PHE A 403 -25.430 -18.953 -8.725 1.00 62.88 C
ANISOU 2496 CA PHE A 403 7949 9962 5981 1335 -50 299 C
ATOM 2497 C PHE A 403 -23.962 -18.950 -8.252 1.00 65.01 C
ANISOU 2497 C PHE A 403 8348 10042 6313 1114 33 363 C
ATOM 2498 O PHE A 403 -23.570 -19.866 -7.513 1.00 61.92 O
ANISOU 2498 O PHE A 403 7799 9709 6019 970 118 347 O
ATOM 2499 CB PHE A 403 -25.689 -20.258 -9.512 1.00 64.16 C
ANISOU 2499 CB PHE A 403 7892 10303 6182 1202 -24 273 C
ATOM 2500 CG PHE A 403 -27.147 -20.618 -9.730 1.00 66.68 C
ANISOU 2500 CG PHE A 403 7983 10907 6447 1335 -77 182 C
ATOM 2501 CD1 PHE A 403 -27.936 -21.072 -8.675 1.00 68.83 C
ANISOU 2501 CD1 PHE A 403 8036 11373 6743 1344 -40 101 C
ATOM 2502 CD2 PHE A 403 -27.722 -20.530 -10.997 1.00 68.98 C
ANISOU 2502 CD2 PHE A 403 8262 11306 6641 1431 -160 172 C
ATOM 2503 CE1 PHE A 403 -29.277 -21.423 -8.886 1.00 71.09 C
ANISOU 2503 CE1 PHE A 403 8076 11988 6948 1427 -81 3 C
ATOM 2504 CE2 PHE A 403 -29.065 -20.867 -11.202 1.00 72.80 C
ANISOU 2504 CE2 PHE A 403 8499 12114 7048 1541 -211 74 C
ATOM 2505 CZ PHE A 403 -29.831 -21.316 -10.147 1.00 71.34 C
ANISOU 2505 CZ PHE A 403 8078 12149 6879 1527 -169 -14 C
ATOM 2506 N VAL A 404 -23.143 -17.957 -8.682 1.00 63.20 N
ANISOU 2506 N VAL A 404 8405 9604 6005 1074 9 432 N
ATOM 2507 CA VAL A 404 -21.744 -17.890 -8.232 1.00 62.14 C
ANISOU 2507 CA VAL A 404 8361 9355 5893 843 87 477 C
ATOM 2508 C VAL A 404 -21.480 -16.481 -7.681 1.00 66.09 C
ANISOU 2508 C VAL A 404 9168 9645 6300 880 55 499 C
ATOM 2509 O VAL A 404 -21.218 -16.353 -6.489 1.00 65.20 O
ANISOU 2509 O VAL A 404 9036 9511 6227 846 99 474 O
ATOM 2510 CB VAL A 404 -20.638 -18.363 -9.237 1.00 65.36 C
ANISOU 2510 CB VAL A 404 8778 9770 6284 626 130 527 C
ATOM 2511 CG1 VAL A 404 -19.374 -18.760 -8.480 1.00 64.18 C
ANISOU 2511 CG1 VAL A 404 8562 9644 6179 421 224 533 C
ATOM 2512 CG2 VAL A 404 -21.102 -19.540 -10.105 1.00 64.34 C
ANISOU 2512 CG2 VAL A 404 8442 9801 6204 637 131 501 C
ATOM 2513 N LEU A 405 -21.601 -15.438 -8.507 1.00 64.49 N
ANISOU 2513 N LEU A 405 9269 9276 5959 957 -22 543 N
ATOM 2514 CA LEU A 405 -21.396 -14.049 -8.062 1.00 66.10 C
ANISOU 2514 CA LEU A 405 9851 9227 6039 991 -59 563 C
ATOM 2515 C LEU A 405 -22.343 -13.641 -6.915 1.00 70.49 C
ANISOU 2515 C LEU A 405 10394 9781 6610 1257 -94 489 C
ATOM 2516 O LEU A 405 -21.884 -13.030 -5.951 1.00 71.46 O
ANISOU 2516 O LEU A 405 10666 9774 6712 1187 -63 476 O
ATOM 2517 CB LEU A 405 -21.564 -13.049 -9.225 1.00 68.01 C
ANISOU 2517 CB LEU A 405 10470 9268 6102 1078 -153 626 C
ATOM 2518 CG LEU A 405 -20.359 -12.714 -10.078 1.00 72.03 C
ANISOU 2518 CG LEU A 405 11213 9652 6504 759 -118 711 C
ATOM 2519 CD1 LEU A 405 -20.746 -11.705 -11.117 1.00 74.67 C
ANISOU 2519 CD1 LEU A 405 11956 9770 6647 891 -222 775 C
ATOM 2520 CD2 LEU A 405 -19.225 -12.150 -9.251 1.00 72.77 C
ANISOU 2520 CD2 LEU A 405 11482 9616 6550 471 -45 721 C
ATOM 2521 N ALA A 406 -23.647 -13.965 -7.025 1.00 66.80 N
ANISOU 2521 N ALA A 406 9739 9485 6157 1551 -156 430 N
ATOM 2522 CA ALA A 406 -24.644 -13.646 -5.996 1.00 67.88 C
ANISOU 2522 CA ALA A 406 9809 9696 6287 1827 -188 342 C
ATOM 2523 C ALA A 406 -24.314 -14.342 -4.634 1.00 68.73 C
ANISOU 2523 C ALA A 406 9665 9920 6531 1669 -82 298 C
ATOM 2524 O ALA A 406 -24.148 -13.608 -3.657 1.00 68.05 O
ANISOU 2524 O ALA A 406 9742 9704 6409 1710 -75 271 O
ATOM 2525 CB ALA A 406 -26.047 -14.006 -6.469 1.00 69.74 C
ANISOU 2525 CB ALA A 406 9811 10193 6494 2123 -263 275 C
ATOM 2526 N PRO A 407 -24.115 -15.692 -4.530 1.00 63.33 N
ANISOU 2526 N PRO A 407 8640 9441 5983 1481 -1 294 N
ATOM 2527 CA PRO A 407 -23.757 -16.272 -3.216 1.00 61.72 C
ANISOU 2527 CA PRO A 407 8259 9313 5879 1348 91 265 C
ATOM 2528 C PRO A 407 -22.428 -15.743 -2.671 1.00 67.76 C
ANISOU 2528 C PRO A 407 9228 9887 6632 1140 139 310 C
ATOM 2529 O PRO A 407 -22.387 -15.320 -1.512 1.00 67.87 O
ANISOU 2529 O PRO A 407 9282 9863 6641 1164 161 272 O
ATOM 2530 CB PRO A 407 -23.678 -17.776 -3.486 1.00 61.55 C
ANISOU 2530 CB PRO A 407 7940 9480 5966 1184 155 271 C
ATOM 2531 CG PRO A 407 -24.450 -17.986 -4.750 1.00 66.70 C
ANISOU 2531 CG PRO A 407 8541 10224 6578 1285 91 267 C
ATOM 2532 CD PRO A 407 -24.252 -16.749 -5.557 1.00 63.48 C
ANISOU 2532 CD PRO A 407 8453 9616 6052 1394 8 311 C
ATOM 2533 N ILE A 408 -21.355 -15.709 -3.509 1.00 65.48 N
ANISOU 2533 N ILE A 408 9062 9501 6314 928 155 380 N
ATOM 2534 CA ILE A 408 -20.028 -15.208 -3.094 1.00 65.21 C
ANISOU 2534 CA ILE A 408 9195 9348 6234 682 205 413 C
ATOM 2535 C ILE A 408 -20.169 -13.728 -2.658 1.00 68.72 C
ANISOU 2535 C ILE A 408 10007 9553 6549 764 153 398 C
ATOM 2536 O ILE A 408 -19.578 -13.341 -1.650 1.00 67.42 O
ANISOU 2536 O ILE A 408 9915 9337 6366 645 193 376 O
ATOM 2537 CB ILE A 408 -18.929 -15.433 -4.183 1.00 68.36 C
ANISOU 2537 CB ILE A 408 9631 9751 6593 441 232 478 C
ATOM 2538 CG1 ILE A 408 -18.644 -16.928 -4.386 1.00 66.83 C
ANISOU 2538 CG1 ILE A 408 9099 9778 6515 374 292 477 C
ATOM 2539 CG2 ILE A 408 -17.623 -14.706 -3.851 1.00 70.75 C
ANISOU 2539 CG2 ILE A 408 10124 9967 6792 166 275 499 C
ATOM 2540 CD1 ILE A 408 -17.895 -17.220 -5.679 1.00 74.63 C
ANISOU 2540 CD1 ILE A 408 10096 10805 7457 226 303 522 C
ATOM 2541 N GLY A 409 -21.004 -12.960 -3.367 1.00 66.29 N
ANISOU 2541 N GLY A 409 9932 9110 6146 991 60 402 N
ATOM 2542 CA GLY A 409 -21.268 -11.566 -3.031 1.00 68.67 C
ANISOU 2542 CA GLY A 409 10643 9148 6300 1135 -5 383 C
ATOM 2543 C GLY A 409 -21.905 -11.424 -1.664 1.00 73.71 C
ANISOU 2543 C GLY A 409 11193 9840 6974 1326 2 293 C
ATOM 2544 O GLY A 409 -21.417 -10.673 -0.811 1.00 73.68 O
ANISOU 2544 O GLY A 409 11415 9675 6904 1241 21 270 O
ATOM 2545 N LEU A 410 -22.978 -12.197 -1.445 1.00 70.96 N
ANISOU 2545 N LEU A 410 10495 9747 6718 1550 -6 237 N
ATOM 2546 CA LEU A 410 -23.726 -12.230 -0.199 1.00 71.59 C
ANISOU 2546 CA LEU A 410 10418 9955 6827 1737 7 143 C
ATOM 2547 C LEU A 410 -22.848 -12.761 0.969 1.00 74.13 C
ANISOU 2547 C LEU A 410 10585 10338 7244 1468 112 139 C
ATOM 2548 O LEU A 410 -22.937 -12.193 2.061 1.00 73.68 O
ANISOU 2548 O LEU A 410 10620 10227 7146 1539 120 79 O
ATOM 2549 CB LEU A 410 -24.995 -13.071 -0.372 1.00 71.43 C
ANISOU 2549 CB LEU A 410 10027 10250 6863 1955 -12 86 C
ATOM 2550 CG LEU A 410 -26.108 -12.750 0.612 1.00 77.90 C
ANISOU 2550 CG LEU A 410 10752 11215 7632 2260 -36 -29 C
ATOM 2551 CD1 LEU A 410 -27.033 -11.668 0.050 1.00 80.71 C
ANISOU 2551 CD1 LEU A 410 11359 11490 7818 2666 -163 -74 C
ATOM 2552 CD2 LEU A 410 -26.884 -14.015 0.995 1.00 79.11 C
ANISOU 2552 CD2 LEU A 410 10429 11751 7879 2243 19 -83 C
ATOM 2553 N VAL A 411 -21.961 -13.785 0.724 1.00 68.77 N
ANISOU 2553 N VAL A 411 9698 9766 6667 1183 185 199 N
ATOM 2554 CA VAL A 411 -21.068 -14.301 1.773 1.00 68.02 C
ANISOU 2554 CA VAL A 411 9463 9746 6635 960 273 199 C
ATOM 2555 C VAL A 411 -20.056 -13.197 2.177 1.00 72.50 C
ANISOU 2555 C VAL A 411 10352 10102 7092 785 278 205 C
ATOM 2556 O VAL A 411 -19.602 -13.186 3.319 1.00 72.98 O
ANISOU 2556 O VAL A 411 10367 10203 7160 685 327 174 O
ATOM 2557 CB VAL A 411 -20.348 -15.676 1.514 1.00 70.83 C
ANISOU 2557 CB VAL A 411 9537 10279 7099 756 342 250 C
ATOM 2558 CG1 VAL A 411 -21.271 -16.739 0.934 1.00 70.00 C
ANISOU 2558 CG1 VAL A 411 9183 10340 7073 870 336 246 C
ATOM 2559 CG2 VAL A 411 -19.065 -15.546 0.713 1.00 70.77 C
ANISOU 2559 CG2 VAL A 411 9644 10203 7043 514 357 314 C
ATOM 2560 N LEU A 412 -19.731 -12.267 1.256 1.00 68.56 N
ANISOU 2560 N LEU A 412 10194 9383 6473 730 229 244 N
ATOM 2561 CA LEU A 412 -18.829 -11.154 1.553 1.00 68.43 C
ANISOU 2561 CA LEU A 412 10541 9145 6313 518 234 246 C
ATOM 2562 C LEU A 412 -19.544 -10.085 2.397 1.00 71.53 C
ANISOU 2562 C LEU A 412 11221 9343 6613 742 185 170 C
ATOM 2563 O LEU A 412 -18.904 -9.528 3.282 1.00 71.56 O
ANISOU 2563 O LEU A 412 11382 9260 6547 571 218 136 O
ATOM 2564 CB LEU A 412 -18.240 -10.522 0.270 1.00 69.17 C
ANISOU 2564 CB LEU A 412 10947 9056 6280 345 203 317 C
ATOM 2565 CG LEU A 412 -17.170 -11.332 -0.467 1.00 71.53 C
ANISOU 2565 CG LEU A 412 11029 9538 6613 45 265 378 C
ATOM 2566 CD1 LEU A 412 -17.170 -11.012 -1.914 1.00 72.05 C
ANISOU 2566 CD1 LEU A 412 11303 9483 6589 11 220 445 C
ATOM 2567 CD2 LEU A 412 -15.778 -11.111 0.112 1.00 73.89 C
ANISOU 2567 CD2 LEU A 412 11347 9897 6829 -333 337 369 C
ATOM 2568 N ILE A 413 -20.854 -9.809 2.152 1.00 67.23 N
ANISOU 2568 N ILE A 413 10736 8758 6051 1132 107 133 N
ATOM 2569 CA ILE A 413 -21.568 -8.784 2.929 1.00 68.77 C
ANISOU 2569 CA ILE A 413 11210 8784 6134 1406 54 46 C
ATOM 2570 C ILE A 413 -21.770 -9.286 4.383 1.00 70.92 C
ANISOU 2570 C ILE A 413 11177 9272 6500 1439 117 -34 C
ATOM 2571 O ILE A 413 -21.394 -8.570 5.317 1.00 70.72 O
ANISOU 2571 O ILE A 413 11371 9107 6393 1374 133 -86 O
ATOM 2572 CB ILE A 413 -22.894 -8.203 2.288 1.00 73.94 C
ANISOU 2572 CB ILE A 413 12042 9357 6694 1869 -61 13 C
ATOM 2573 CG1 ILE A 413 -24.215 -8.858 2.806 1.00 73.90 C
ANISOU 2573 CG1 ILE A 413 11625 9683 6771 2221 -72 -77 C
ATOM 2574 CG2 ILE A 413 -22.847 -8.060 0.737 1.00 74.05 C
ANISOU 2574 CG2 ILE A 413 12235 9253 6649 1863 -123 105 C
ATOM 2575 CD1 ILE A 413 -25.443 -7.865 3.009 1.00 77.47 C
ANISOU 2575 CD1 ILE A 413 12311 10062 7063 2729 -176 -181 C
ATOM 2576 N VAL A 414 -22.290 -10.524 4.564 1.00 66.53 N
ANISOU 2576 N VAL A 414 10141 9042 6095 1498 158 -40 N
ATOM 2577 CA VAL A 414 -22.551 -11.145 5.882 1.00 65.62 C
ANISOU 2577 CA VAL A 414 9720 9154 6059 1515 222 -103 C
ATOM 2578 C VAL A 414 -21.220 -11.427 6.633 1.00 70.25 C
ANISOU 2578 C VAL A 414 10261 9750 6680 1152 304 -70 C
ATOM 2579 O VAL A 414 -21.085 -11.005 7.783 1.00 70.87 O
ANISOU 2579 O VAL A 414 10406 9808 6714 1138 328 -132 O
ATOM 2580 CB VAL A 414 -23.432 -12.417 5.795 1.00 67.34 C
ANISOU 2580 CB VAL A 414 9489 9701 6396 1622 247 -111 C
ATOM 2581 CG1 VAL A 414 -23.800 -12.912 7.184 1.00 66.77 C
ANISOU 2581 CG1 VAL A 414 9166 9840 6365 1643 311 -178 C
ATOM 2582 CG2 VAL A 414 -24.694 -12.157 4.984 1.00 68.23 C
ANISOU 2582 CG2 VAL A 414 9602 9871 6451 1961 163 -152 C
ATOM 2583 N GLY A 415 -20.265 -12.098 5.973 1.00 65.77 N
ANISOU 2583 N GLY A 415 9583 9237 6171 886 340 16 N
ATOM 2584 CA GLY A 415 -18.938 -12.373 6.524 1.00 65.04 C
ANISOU 2584 CA GLY A 415 9427 9205 6079 565 407 42 C
ATOM 2585 C GLY A 415 -18.171 -11.097 6.834 1.00 72.10 C
ANISOU 2585 C GLY A 415 10701 9877 6819 389 396 13 C
ATOM 2586 O GLY A 415 -17.467 -11.013 7.844 1.00 71.08 O
ANISOU 2586 O GLY A 415 10544 9807 6655 224 440 -22 O
ATOM 2587 N GLY A 416 -18.344 -10.093 5.973 1.00 71.83 N
ANISOU 2587 N GLY A 416 11045 9576 6670 426 335 25 N
ATOM 2588 CA GLY A 416 -17.741 -8.775 6.126 1.00 73.81 C
ANISOU 2588 CA GLY A 416 11761 9547 6736 249 317 -1 C
ATOM 2589 C GLY A 416 -18.355 -8.028 7.285 1.00 79.00 C
ANISOU 2589 C GLY A 416 12610 10079 7327 447 297 -103 C
ATOM 2590 O GLY A 416 -17.640 -7.322 7.997 1.00 81.34 O
ANISOU 2590 O GLY A 416 13154 10250 7500 223 318 -146 O
ATOM 2591 N TYR A 417 -19.684 -8.213 7.509 1.00 73.45 N
ANISOU 2591 N TYR A 417 11773 9444 6689 857 259 -152 N
ATOM 2592 CA TYR A 417 -20.418 -7.584 8.616 1.00 73.56 C
ANISOU 2592 CA TYR A 417 11918 9395 6638 1111 241 -265 C
ATOM 2593 C TYR A 417 -19.882 -8.083 9.963 1.00 75.17 C
ANISOU 2593 C TYR A 417 11858 9806 6896 925 322 -305 C
ATOM 2594 O TYR A 417 -19.601 -7.270 10.845 1.00 76.63 O
ANISOU 2594 O TYR A 417 12296 9854 6967 865 328 -380 O
ATOM 2595 CB TYR A 417 -21.935 -7.842 8.500 1.00 74.51 C
ANISOU 2595 CB TYR A 417 11858 9650 6801 1579 190 -317 C
ATOM 2596 CG TYR A 417 -22.729 -7.429 9.720 1.00 77.33 C
ANISOU 2596 CG TYR A 417 12222 10058 7102 1857 186 -446 C
ATOM 2597 CD1 TYR A 417 -23.171 -6.119 9.878 1.00 82.01 C
ANISOU 2597 CD1 TYR A 417 13287 10360 7512 2120 113 -532 C
ATOM 2598 CD2 TYR A 417 -23.030 -8.348 10.726 1.00 76.73 C
ANISOU 2598 CD2 TYR A 417 11704 10315 7135 1862 256 -485 C
ATOM 2599 CE1 TYR A 417 -23.888 -5.727 11.012 1.00 83.62 C
ANISOU 2599 CE1 TYR A 417 13496 10628 7648 2398 111 -666 C
ATOM 2600 CE2 TYR A 417 -23.730 -7.964 11.871 1.00 78.94 C
ANISOU 2600 CE2 TYR A 417 11977 10669 7347 2100 260 -609 C
ATOM 2601 CZ TYR A 417 -24.169 -6.654 12.003 1.00 87.65 C
ANISOU 2601 CZ TYR A 417 13523 11506 8273 2380 188 -706 C
ATOM 2602 OH TYR A 417 -24.867 -6.264 13.122 1.00 87.97 O
ANISOU 2602 OH TYR A 417 13556 11636 8232 2642 192 -843 O
ATOM 2603 N PHE A 418 -19.728 -9.409 10.114 1.00 67.65 N
ANISOU 2603 N PHE A 418 10433 9169 6101 837 381 -255 N
ATOM 2604 CA PHE A 418 -19.250 -10.005 11.349 1.00 65.44 C
ANISOU 2604 CA PHE A 418 9892 9104 5867 692 452 -278 C
ATOM 2605 C PHE A 418 -17.798 -9.695 11.616 1.00 68.98 C
ANISOU 2605 C PHE A 418 10457 9519 6234 305 486 -261 C
ATOM 2606 O PHE A 418 -17.421 -9.659 12.781 1.00 70.36 O
ANISOU 2606 O PHE A 418 10574 9788 6374 208 524 -313 O
ATOM 2607 CB PHE A 418 -19.485 -11.509 11.360 1.00 65.16 C
ANISOU 2607 CB PHE A 418 9392 9374 5993 718 497 -221 C
ATOM 2608 CG PHE A 418 -20.948 -11.846 11.520 1.00 67.23 C
ANISOU 2608 CG PHE A 418 9483 9758 6305 1048 483 -271 C
ATOM 2609 CD1 PHE A 418 -21.634 -11.504 12.681 1.00 70.98 C
ANISOU 2609 CD1 PHE A 418 9949 10293 6727 1221 493 -372 C
ATOM 2610 CD2 PHE A 418 -21.648 -12.483 10.500 1.00 68.79 C
ANISOU 2610 CD2 PHE A 418 9519 10041 6578 1175 460 -229 C
ATOM 2611 CE1 PHE A 418 -22.995 -11.777 12.810 1.00 72.37 C
ANISOU 2611 CE1 PHE A 418 9939 10643 6916 1515 484 -434 C
ATOM 2612 CE2 PHE A 418 -23.009 -12.766 10.634 1.00 71.65 C
ANISOU 2612 CE2 PHE A 418 9697 10573 6953 1451 449 -290 C
ATOM 2613 CZ PHE A 418 -23.673 -12.410 11.785 1.00 71.12 C
ANISOU 2613 CZ PHE A 418 9604 10596 6824 1618 462 -394 C
ATOM 2614 N LEU A 419 -16.983 -9.429 10.581 1.00 64.64 N
ANISOU 2614 N LEU A 419 10070 8862 5628 70 475 -199 N
ATOM 2615 CA LEU A 419 -15.576 -9.090 10.826 1.00 64.56 C
ANISOU 2615 CA LEU A 419 10148 8881 5502 -336 513 -200 C
ATOM 2616 C LEU A 419 -15.484 -7.662 11.324 1.00 70.47 C
ANISOU 2616 C LEU A 419 11376 9338 6062 -427 489 -285 C
ATOM 2617 O LEU A 419 -14.737 -7.393 12.271 1.00 70.25 O
ANISOU 2617 O LEU A 419 11363 9385 5943 -665 526 -341 O
ATOM 2618 CB LEU A 419 -14.678 -9.322 9.605 1.00 64.24 C
ANISOU 2618 CB LEU A 419 10085 8885 5437 -594 521 -117 C
ATOM 2619 CG LEU A 419 -14.403 -10.802 9.232 1.00 65.69 C
ANISOU 2619 CG LEU A 419 9798 9389 5773 -575 556 -45 C
ATOM 2620 CD1 LEU A 419 -13.863 -10.921 7.804 1.00 65.20 C
ANISOU 2620 CD1 LEU A 419 9763 9326 5686 -732 551 27 C
ATOM 2621 CD2 LEU A 419 -13.486 -11.505 10.252 1.00 64.59 C
ANISOU 2621 CD2 LEU A 419 9350 9560 5632 -734 611 -62 C
ATOM 2622 N ILE A 420 -16.314 -6.765 10.754 1.00 68.97 N
ANISOU 2622 N ILE A 420 11585 8818 5802 -204 423 -303 N
ATOM 2623 CA ILE A 420 -16.392 -5.370 11.200 1.00 71.75 C
ANISOU 2623 CA ILE A 420 12480 8825 5957 -219 390 -390 C
ATOM 2624 C ILE A 420 -17.003 -5.360 12.633 1.00 75.59 C
ANISOU 2624 C ILE A 420 12859 9395 6465 8 402 -499 C
ATOM 2625 O ILE A 420 -16.508 -4.629 13.499 1.00 76.90 O
ANISOU 2625 O ILE A 420 13276 9452 6490 -176 418 -580 O
ATOM 2626 CB ILE A 420 -17.130 -4.458 10.172 1.00 76.51 C
ANISOU 2626 CB ILE A 420 13567 9046 6459 18 304 -375 C
ATOM 2627 CG1 ILE A 420 -16.221 -4.239 8.927 1.00 77.19 C
ANISOU 2627 CG1 ILE A 420 13850 9020 6457 -339 306 -277 C
ATOM 2628 CG2 ILE A 420 -17.533 -3.104 10.780 1.00 80.07 C
ANISOU 2628 CG2 ILE A 420 14599 9118 6709 153 256 -482 C
ATOM 2629 CD1 ILE A 420 -16.923 -3.803 7.647 1.00 81.93 C
ANISOU 2629 CD1 ILE A 420 14742 9368 7020 -86 226 -215 C
ATOM 2630 N ARG A 421 -17.993 -6.240 12.905 1.00 69.48 N
ANISOU 2630 N ARG A 421 11690 8852 5857 355 405 -501 N
ATOM 2631 CA ARG A 421 -18.582 -6.339 14.239 1.00 68.96 C
ANISOU 2631 CA ARG A 421 11473 8921 5807 555 427 -599 C
ATOM 2632 C ARG A 421 -17.574 -6.908 15.237 1.00 73.28 C
ANISOU 2632 C ARG A 421 11746 9722 6375 234 501 -599 C
ATOM 2633 O ARG A 421 -17.629 -6.549 16.417 1.00 73.95 O
ANISOU 2633 O ARG A 421 11877 9828 6392 257 520 -694 O
ATOM 2634 CB ARG A 421 -19.876 -7.160 14.239 1.00 65.79 C
ANISOU 2634 CB ARG A 421 10710 8741 5546 949 420 -602 C
ATOM 2635 CG ARG A 421 -21.081 -6.362 13.756 1.00 80.18 C
ANISOU 2635 CG ARG A 421 12811 10364 7289 1374 339 -666 C
ATOM 2636 CD ARG A 421 -21.788 -5.596 14.865 1.00 93.97 C
ANISOU 2636 CD ARG A 421 14731 12055 8918 1651 325 -814 C
ATOM 2637 NE ARG A 421 -23.040 -6.252 15.247 1.00105.02 N
ANISOU 2637 NE ARG A 421 15743 13769 10391 2013 332 -870 N
ATOM 2638 CZ ARG A 421 -23.333 -6.666 16.475 1.00119.75 C
ANISOU 2638 CZ ARG A 421 17330 15892 12278 2053 391 -942 C
ATOM 2639 NH1 ARG A 421 -22.469 -6.487 17.468 1.00101.58 N
ANISOU 2639 NH1 ARG A 421 15094 13564 9938 1784 441 -967 N
ATOM 2640 NH2 ARG A 421 -24.495 -7.256 16.723 1.00111.40 N
ANISOU 2640 NH2 ARG A 421 15921 15145 11260 2346 401 -994 N
ATOM 2641 N GLY A 422 -16.650 -7.739 14.746 1.00 68.16 N
ANISOU 2641 N GLY A 422 10833 9268 5797 -41 536 -502 N
ATOM 2642 CA GLY A 422 -15.595 -8.332 15.553 1.00 67.48 C
ANISOU 2642 CA GLY A 422 10474 9458 5708 -323 593 -494 C
ATOM 2643 C GLY A 422 -14.539 -7.326 15.976 1.00 75.77 C
ANISOU 2643 C GLY A 422 11829 10402 6558 -687 602 -560 C
ATOM 2644 O GLY A 422 -14.191 -7.260 17.157 1.00 75.56 O
ANISOU 2644 O GLY A 422 11739 10501 6468 -783 630 -630 O
ATOM 2645 N VAL A 423 -14.018 -6.525 15.018 1.00 76.18 N
ANISOU 2645 N VAL A 423 12227 10228 6489 -919 580 -541 N
ATOM 2646 CA VAL A 423 -13.004 -5.488 15.293 1.00 78.94 C
ANISOU 2646 CA VAL A 423 12929 10456 6610 -1340 592 -606 C
ATOM 2647 C VAL A 423 -13.619 -4.397 16.180 1.00 86.16 C
ANISOU 2647 C VAL A 423 14269 11070 7399 -1212 567 -729 C
ATOM 2648 O VAL A 423 -12.959 -3.973 17.125 1.00 86.89 O
ANISOU 2648 O VAL A 423 14446 11216 7352 -1478 595 -814 O
ATOM 2649 CB VAL A 423 -12.294 -4.889 14.034 1.00 84.41 C
ANISOU 2649 CB VAL A 423 13925 10973 7174 -1657 581 -552 C
ATOM 2650 CG1 VAL A 423 -11.284 -5.869 13.438 1.00 82.49 C
ANISOU 2650 CG1 VAL A 423 13243 11112 6989 -1891 621 -467 C
ATOM 2651 CG2 VAL A 423 -13.283 -4.418 12.971 1.00 84.70 C
ANISOU 2651 CG2 VAL A 423 14304 10641 7238 -1356 518 -509 C
ATOM 2652 N MET A 424 -14.895 -3.998 15.927 1.00 84.99 N
ANISOU 2652 N MET A 424 14356 10647 7290 -779 513 -749 N
ATOM 2653 CA MET A 424 -15.623 -3.014 16.747 1.00 88.10 C
ANISOU 2653 CA MET A 424 15143 10766 7564 -548 482 -877 C
ATOM 2654 C MET A 424 -15.624 -3.440 18.218 1.00 90.52 C
ANISOU 2654 C MET A 424 15137 11352 7905 -518 528 -957 C
ATOM 2655 O MET A 424 -15.348 -2.621 19.089 1.00 92.45 O
ANISOU 2655 O MET A 424 15679 11463 7984 -649 534 -1070 O
ATOM 2656 CB MET A 424 -17.073 -2.839 16.260 1.00 91.42 C
ANISOU 2656 CB MET A 424 15685 11005 8047 3 416 -885 C
ATOM 2657 CG MET A 424 -17.246 -1.799 15.168 1.00 98.50 C
ANISOU 2657 CG MET A 424 17163 11461 8801 53 346 -864 C
ATOM 2658 SD MET A 424 -18.775 -2.030 14.195 1.00102.92 S
ANISOU 2658 SD MET A 424 17653 11979 9474 678 265 -825 S
ATOM 2659 CE MET A 424 -20.010 -1.407 15.363 1.00101.82 C
ANISOU 2659 CE MET A 424 17704 11745 9239 1198 226 -1002 C
ATOM 2660 N THR A 425 -15.896 -4.731 18.481 1.00 84.31 N
ANISOU 2660 N THR A 425 13775 10943 7318 -366 561 -896 N
ATOM 2661 CA THR A 425 -15.914 -5.316 19.823 1.00 83.45 C
ANISOU 2661 CA THR A 425 13323 11134 7251 -329 607 -945 C
ATOM 2662 C THR A 425 -14.506 -5.277 20.447 1.00 89.11 C
ANISOU 2662 C THR A 425 13981 12024 7852 -793 647 -962 C
ATOM 2663 O THR A 425 -14.384 -4.875 21.600 1.00 91.43 O
ANISOU 2663 O THR A 425 14348 12350 8040 -853 664 -1066 O
ATOM 2664 CB THR A 425 -16.469 -6.758 19.816 1.00 87.30 C
ANISOU 2664 CB THR A 425 13265 11950 7953 -105 634 -854 C
ATOM 2665 OG1 THR A 425 -17.478 -6.901 18.819 1.00 90.41 O
ANISOU 2665 OG1 THR A 425 13680 12229 8443 213 595 -815 O
ATOM 2666 CG2 THR A 425 -17.041 -7.159 21.150 1.00 84.44 C
ANISOU 2666 CG2 THR A 425 12655 11811 7617 64 670 -916 C
ATOM 2667 N LEU A 426 -13.456 -5.676 19.688 1.00 83.54 N
ANISOU 2667 N LEU A 426 13134 11459 7148 -1113 660 -874 N
ATOM 2668 CA LEU A 426 -12.061 -5.719 20.132 1.00 83.35 C
ANISOU 2668 CA LEU A 426 12986 11688 6994 -1557 694 -892 C
ATOM 2669 C LEU A 426 -11.598 -4.366 20.675 1.00 89.91 C
ANISOU 2669 C LEU A 426 14294 12292 7576 -1859 691 -1022 C
ATOM 2670 O LEU A 426 -11.019 -4.326 21.760 1.00 91.19 O
ANISOU 2670 O LEU A 426 14349 12664 7634 -2050 717 -1098 O
ATOM 2671 CB LEU A 426 -11.177 -6.178 18.966 1.00 82.84 C
ANISOU 2671 CB LEU A 426 12764 11769 6942 -1803 701 -790 C
ATOM 2672 CG LEU A 426 -9.658 -6.080 19.087 1.00 88.70 C
ANISOU 2672 CG LEU A 426 13402 12798 7503 -2296 731 -816 C
ATOM 2673 CD1 LEU A 426 -9.115 -7.044 20.126 1.00 87.16 C
ANISOU 2673 CD1 LEU A 426 12721 13063 7334 -2286 756 -819 C
ATOM 2674 CD2 LEU A 426 -9.016 -6.358 17.735 1.00 91.32 C
ANISOU 2674 CD2 LEU A 426 13656 13209 7832 -2487 734 -729 C
ATOM 2675 N PHE A 427 -11.907 -3.267 19.965 1.00 87.70 N
ANISOU 2675 N PHE A 427 14565 11570 7186 -1885 657 -1051 N
ATOM 2676 CA PHE A 427 -11.540 -1.916 20.402 1.00 90.79 C
ANISOU 2676 CA PHE A 427 15519 11662 7316 -2175 651 -1177 C
ATOM 2677 C PHE A 427 -12.498 -1.421 21.501 1.00 93.69 C
ANISOU 2677 C PHE A 427 16092 11845 7660 -1833 635 -1299 C
ATOM 2678 O PHE A 427 -12.145 -0.496 22.249 1.00 96.87 O
ANISOU 2678 O PHE A 427 16868 12089 7851 -2064 640 -1426 O
ATOM 2679 CB PHE A 427 -11.470 -0.937 19.215 1.00 95.11 C
ANISOU 2679 CB PHE A 427 16641 11775 7722 -2343 619 -1153 C
ATOM 2680 CG PHE A 427 -10.290 -1.197 18.300 1.00 97.00 C
ANISOU 2680 CG PHE A 427 16736 12222 7899 -2815 650 -1070 C
ATOM 2681 CD1 PHE A 427 -9.067 -0.573 18.518 1.00103.23 C
ANISOU 2681 CD1 PHE A 427 17699 13093 8428 -3418 687 -1139 C
ATOM 2682 CD2 PHE A 427 -10.396 -2.084 17.231 1.00 96.56 C
ANISOU 2682 CD2 PHE A 427 16349 12313 8024 -2667 645 -935 C
ATOM 2683 CE1 PHE A 427 -7.976 -0.816 17.669 1.00104.57 C
ANISOU 2683 CE1 PHE A 427 17699 13520 8515 -3859 720 -1076 C
ATOM 2684 CE2 PHE A 427 -9.302 -2.335 16.391 1.00 99.49 C
ANISOU 2684 CE2 PHE A 427 16568 12911 8323 -3084 676 -871 C
ATOM 2685 CZ PHE A 427 -8.104 -1.694 16.609 1.00100.54 C
ANISOU 2685 CZ PHE A 427 16858 13151 8190 -3672 715 -943 C
ATOM 2686 N SER A 428 -13.686 -2.059 21.627 1.00 85.21 N
ANISOU 2686 N SER A 428 14760 10830 6786 -1307 620 -1272 N
ATOM 2687 CA SER A 428 -14.633 -1.740 22.696 1.00 84.71 C
ANISOU 2687 CA SER A 428 14788 10692 6704 -951 612 -1391 C
ATOM 2688 C SER A 428 -14.143 -2.394 23.988 1.00 85.73 C
ANISOU 2688 C SER A 428 14500 11227 6844 -1094 665 -1429 C
ATOM 2689 O SER A 428 -14.173 -1.748 25.031 1.00 86.16 O
ANISOU 2689 O SER A 428 14773 11211 6751 -1133 672 -1563 O
ATOM 2690 CB SER A 428 -16.041 -2.195 22.341 1.00 86.06 C
ANISOU 2690 CB SER A 428 14790 10857 7051 -387 584 -1357 C
ATOM 2691 OG SER A 428 -17.000 -1.342 22.940 1.00 97.76 O
ANISOU 2691 OG SER A 428 16623 12093 8429 -27 552 -1496 O
ATOM 2692 N ILE A 429 -13.620 -3.651 23.897 1.00 79.63 N
ANISOU 2692 N ILE A 429 13162 10870 6222 -1185 697 -1310 N
ATOM 2693 CA ILE A 429 -13.027 -4.407 25.013 1.00 78.87 C
ANISOU 2693 CA ILE A 429 12644 11193 6130 -1318 739 -1315 C
ATOM 2694 C ILE A 429 -11.725 -3.704 25.421 1.00 86.22 C
ANISOU 2694 C ILE A 429 13755 12176 6827 -1831 750 -1396 C
ATOM 2695 O ILE A 429 -11.386 -3.678 26.597 1.00 86.25 O
ANISOU 2695 O ILE A 429 13658 12380 6734 -1939 770 -1478 O
ATOM 2696 CB ILE A 429 -12.761 -5.925 24.684 1.00 78.96 C
ANISOU 2696 CB ILE A 429 12082 11589 6331 -1265 759 -1161 C
ATOM 2697 CG1 ILE A 429 -13.938 -6.681 23.991 1.00 77.31 C
ANISOU 2697 CG1 ILE A 429 11699 11334 6340 -848 750 -1068 C
ATOM 2698 CG2 ILE A 429 -12.182 -6.701 25.881 1.00 78.22 C
ANISOU 2698 CG2 ILE A 429 11597 11909 6213 -1354 790 -1162 C
ATOM 2699 CD1 ILE A 429 -15.083 -7.180 24.844 1.00 89.37 C
ANISOU 2699 CD1 ILE A 429 13034 12968 7955 -485 770 -1096 C
ATOM 2700 N LYS A 430 -10.987 -3.160 24.440 1.00 85.42 N
ANISOU 2700 N LYS A 430 13908 11926 6622 -2169 739 -1374 N
ATOM 2701 CA LYS A 430 -9.719 -2.462 24.662 1.00 88.17 C
ANISOU 2701 CA LYS A 430 14439 12345 6716 -2728 755 -1455 C
ATOM 2702 C LYS A 430 -9.931 -1.195 25.473 1.00 95.23 C
ANISOU 2702 C LYS A 430 15873 12909 7401 -2822 748 -1622 C
ATOM 2703 O LYS A 430 -9.091 -0.868 26.309 1.00 96.45 O
ANISOU 2703 O LYS A 430 16035 13249 7364 -3191 770 -1722 O
ATOM 2704 CB LYS A 430 -9.034 -2.135 23.321 1.00 91.83 C
ANISOU 2704 CB LYS A 430 15090 12698 7104 -3063 751 -1391 C
ATOM 2705 N SER A 431 -11.057 -0.499 25.244 1.00 94.04 N
ANISOU 2705 N SER A 431 16168 12291 7270 -2468 715 -1661 N
ATOM 2706 CA SER A 431 -11.395 0.731 25.957 1.00 98.24 C
ANISOU 2706 CA SER A 431 17280 12448 7597 -2468 700 -1827 C
ATOM 2707 C SER A 431 -12.005 0.419 27.329 1.00103.58 C
ANISOU 2707 C SER A 431 17719 13314 8321 -2158 716 -1916 C
ATOM 2708 O SER A 431 -11.484 0.911 28.329 1.00105.17 O
ANISOU 2708 O SER A 431 18055 13568 8335 -2423 734 -2045 O
ATOM 2709 CB SER A 431 -12.340 1.600 25.130 1.00103.74 C
ANISOU 2709 CB SER A 431 18570 12581 8266 -2162 648 -1838 C
ATOM 2710 OG SER A 431 -11.825 2.909 24.935 1.00114.97 O
ANISOU 2710 OG SER A 431 20702 13582 9399 -2547 635 -1930 O
ATOM 2711 N ASN A 432 -13.081 -0.418 27.375 1.00 99.11 N
ANISOU 2711 N ASN A 432 16791 12877 7988 -1635 712 -1851 N
ATOM 2712 CA ASN A 432 -13.823 -0.814 28.589 1.00 98.72 C
ANISOU 2712 CA ASN A 432 16486 13032 7993 -1306 733 -1922 C
ATOM 2713 C ASN A 432 -12.992 -1.649 29.570 1.00103.13 C
ANISOU 2713 C ASN A 432 16549 14085 8553 -1553 776 -1903 C
ATOM 2714 O ASN A 432 -13.215 -1.573 30.783 1.00102.35 O
ANISOU 2714 O ASN A 432 16402 14107 8381 -1475 796 -2007 O
ATOM 2715 CB ASN A 432 -15.085 -1.615 28.222 1.00 95.38 C
ANISOU 2715 CB ASN A 432 15759 12680 7800 -769 727 -1840 C
ATOM 2716 CG ASN A 432 -16.135 -0.859 27.440 1.00118.55 C
ANISOU 2716 CG ASN A 432 19122 15198 10725 -396 675 -1878 C
ATOM 2717 OD1 ASN A 432 -16.394 0.330 27.658 1.00116.48 O
ANISOU 2717 OD1 ASN A 432 19419 14564 10273 -326 645 -2018 O
ATOM 2718 ND2 ASN A 432 -16.811 -1.557 26.544 1.00108.59 N
ANISOU 2718 ND2 ASN A 432 17609 13998 9653 -115 660 -1760 N
ATOM 2719 N HIS A 433 -12.090 -2.491 29.039 1.00100.34 N
ANISOU 2719 N HIS A 433 15815 14033 8275 -1803 787 -1770 N
ATOM 2720 CA HIS A 433 -11.250 -3.392 29.826 1.00 99.97 C
ANISOU 2720 CA HIS A 433 15278 14485 8223 -1990 813 -1732 C
ATOM 2721 C HIS A 433 -9.777 -3.352 29.361 1.00108.00 C
ANISOU 2721 C HIS A 433 16222 15705 9107 -2503 813 -1706 C
ATOM 2722 O HIS A 433 -9.291 -4.376 28.861 1.00105.41 O
ANISOU 2722 O HIS A 433 15472 15687 8891 -2513 815 -1575 O
ATOM 2723 CB HIS A 433 -11.794 -4.829 29.718 1.00 97.12 C
ANISOU 2723 CB HIS A 433 14397 14399 8105 -1646 826 -1581 C
ATOM 2724 CG HIS A 433 -13.255 -4.940 29.992 1.00 99.75 C
ANISOU 2724 CG HIS A 433 14751 14590 8559 -1176 833 -1599 C
ATOM 2725 ND1 HIS A 433 -13.756 -4.848 31.280 1.00102.29 N
ANISOU 2725 ND1 HIS A 433 15034 15013 8817 -1026 857 -1699 N
ATOM 2726 CD2 HIS A 433 -14.283 -5.099 29.132 1.00100.09 C
ANISOU 2726 CD2 HIS A 433 14834 14438 8755 -846 820 -1543 C
ATOM 2727 CE1 HIS A 433 -15.064 -4.977 31.162 1.00100.84 C
ANISOU 2727 CE1 HIS A 433 14850 14719 8747 -614 862 -1703 C
ATOM 2728 NE2 HIS A 433 -15.424 -5.146 29.891 1.00 99.96 N
ANISOU 2728 NE2 HIS A 433 14773 14440 8766 -491 838 -1611 N
ATOM 2729 N PRO A 434 -9.034 -2.216 29.510 1.00110.24 N
ANISOU 2729 N PRO A 434 16905 15847 9134 -2941 812 -1836 N
ATOM 2730 CA PRO A 434 -7.623 -2.217 29.078 1.00111.73 C
ANISOU 2730 CA PRO A 434 16966 16318 9169 -3462 819 -1823 C
ATOM 2731 C PRO A 434 -6.817 -3.245 29.872 1.00116.17 C
ANISOU 2731 C PRO A 434 16928 17493 9718 -3527 828 -1791 C
ATOM 2732 O PRO A 434 -6.911 -3.307 31.103 1.00116.07 O
ANISOU 2732 O PRO A 434 16811 17640 9648 -3451 833 -1865 O
ATOM 2733 CB PRO A 434 -7.157 -0.775 29.330 1.00117.46 C
ANISOU 2733 CB PRO A 434 18267 16767 9594 -3915 822 -1991 C
ATOM 2734 CG PRO A 434 -8.103 -0.224 30.333 1.00122.70 C
ANISOU 2734 CG PRO A 434 19229 17152 10238 -3627 818 -2110 C
ATOM 2735 CD PRO A 434 -9.417 -0.910 30.092 1.00115.24 C
ANISOU 2735 CD PRO A 434 18119 16086 9580 -2999 807 -2008 C
ATOM 2736 N GLY A 435 -6.122 -4.104 29.143 1.00112.94 N
ANISOU 2736 N GLY A 435 16129 17415 9368 -3600 825 -1675 N
ATOM 2737 CA GLY A 435 -5.323 -5.168 29.726 1.00112.99 C
ANISOU 2737 CA GLY A 435 15570 18010 9352 -3602 820 -1630 C
ATOM 2738 C GLY A 435 -6.021 -6.507 29.843 1.00117.01 C
ANISOU 2738 C GLY A 435 15703 18639 10117 -3090 814 -1484 C
ATOM 2739 O GLY A 435 -5.465 -7.419 30.455 1.00116.17 O
ANISOU 2739 O GLY A 435 15180 18979 9981 -3024 803 -1443 O
ATOM 2740 N LEU A 436 -7.236 -6.656 29.260 1.00114.51 N
ANISOU 2740 N LEU A 436 15536 17942 10030 -2728 818 -1406 N
ATOM 2741 CA LEU A 436 -7.957 -7.934 29.292 1.00112.52 C
ANISOU 2741 CA LEU A 436 14959 17788 10008 -2290 819 -1268 C
ATOM 2742 C LEU A 436 -7.288 -8.959 28.342 1.00119.50 C
ANISOU 2742 C LEU A 436 15506 18928 10969 -2278 807 -1133 C
ATOM 2743 O LEU A 436 -7.407 -10.162 28.581 1.00117.07 O
ANISOU 2743 O LEU A 436 14873 18838 10770 -2010 803 -1026 O
ATOM 2744 CB LEU A 436 -9.458 -7.783 28.991 1.00110.87 C
ANISOU 2744 CB LEU A 436 14975 17162 9986 -1930 828 -1246 C
ATOM 2745 CG LEU A 436 -10.336 -9.012 29.304 1.00112.01 C
ANISOU 2745 CG LEU A 436 14819 17416 10324 -1527 842 -1134 C
ATOM 2746 CD1 LEU A 436 -10.357 -9.335 30.785 1.00111.73 C
ANISOU 2746 CD1 LEU A 436 14622 17624 10205 -1464 858 -1176 C
ATOM 2747 CD2 LEU A 436 -11.729 -8.824 28.798 1.00113.09 C
ANISOU 2747 CD2 LEU A 436 15142 17209 10618 -1221 849 -1124 C
ATOM 2748 N LEU A 437 -6.545 -8.485 27.310 1.00121.10 N
ANISOU 2748 N LEU A 437 15804 19118 11090 -2580 802 -1145 N
ATOM 2749 CA LEU A 437 -5.766 -9.343 26.409 1.00121.73 C
ANISOU 2749 CA LEU A 437 15567 19489 11198 -2605 791 -1046 C
ATOM 2750 C LEU A 437 -4.326 -9.471 26.989 1.00131.20 C
ANISOU 2750 C LEU A 437 16469 21235 12147 -2900 780 -1112 C
ATOM 2751 O LEU A 437 -3.337 -9.068 26.361 1.00132.08 O
ANISOU 2751 O LEU A 437 16550 21542 12093 -3258 783 -1158 O
ATOM 2752 CB LEU A 437 -5.778 -8.807 24.965 1.00122.12 C
ANISOU 2752 CB LEU A 437 15854 19266 11281 -2757 796 -1021 C
ATOM 2753 CG LEU A 437 -5.416 -9.817 23.862 1.00126.22 C
ANISOU 2753 CG LEU A 437 16078 19971 11906 -2641 789 -898 C
ATOM 2754 CD1 LEU A 437 -6.576 -10.781 23.576 1.00124.07 C
ANISOU 2754 CD1 LEU A 437 15728 19501 11910 -2169 785 -773 C
ATOM 2755 CD2 LEU A 437 -5.010 -9.105 22.573 1.00129.82 C
ANISOU 2755 CD2 LEU A 437 16748 20284 12294 -2944 798 -907 C
ATOM 2756 N SER A 438 -4.250 -10.000 28.241 1.00130.31 N
ANISOU 2756 N SER A 438 16137 21388 11985 -2752 768 -1123 N
ATOM 2757 CA SER A 438 -3.034 -10.227 29.028 1.00132.77 C
ANISOU 2757 CA SER A 438 16134 22258 12055 -2936 745 -1187 C
ATOM 2758 C SER A 438 -2.676 -11.715 29.069 1.00136.87 C
ANISOU 2758 C SER A 438 16225 23152 12628 -2590 713 -1062 C
ATOM 2759 O SER A 438 -3.502 -12.541 29.486 1.00134.76 O
ANISOU 2759 O SER A 438 15921 22753 12529 -2205 711 -961 O
ATOM 2760 CB SER A 438 -3.204 -9.698 30.453 1.00137.57 C
ANISOU 2760 CB SER A 438 16845 22885 12540 -3005 747 -1295 C
ATOM 2761 OG SER A 438 -4.220 -10.386 31.168 1.00142.91 O
ANISOU 2761 OG SER A 438 17492 23420 13387 -2589 750 -1215 O
ATOM 2762 N GLU A 439 -1.432 -12.046 28.653 1.00135.03 N
ANISOU 2762 N GLU A 439 15683 23399 12224 -2734 689 -1078 N
ATOM 2763 CA GLU A 439 -0.909 -13.414 28.636 1.00159.70 C
ANISOU 2763 CA GLU A 439 18418 26918 15341 -2397 647 -978 C
ATOM 2764 C GLU A 439 -0.571 -13.890 30.060 1.00168.68 C
ANISOU 2764 C GLU A 439 19349 28413 16330 -2246 607 -995 C
ATOM 2765 O GLU A 439 -1.433 -14.407 30.776 1.00112.62 O
ANISOU 2765 O GLU A 439 12331 21096 9363 -1944 608 -915 O
ATOM 2766 CB GLU A 439 0.332 -13.504 27.729 1.00162.59 C
ANISOU 2766 CB GLU A 439 18516 27728 15533 -2594 632 -1017 C
ATOM 2767 N SER A 443 -3.715 -16.036 25.284 1.00119.68 N
ANISOU 2767 N SER A 443 13585 20730 11159 -1353 683 -507 N
ATOM 2768 CA SER A 443 -3.331 -17.270 25.961 1.00119.64 C
ANISOU 2768 CA SER A 443 13339 21030 11089 -1043 645 -436 C
ATOM 2769 C SER A 443 -4.541 -18.171 26.181 1.00122.13 C
ANISOU 2769 C SER A 443 13778 21015 11611 -703 658 -308 C
ATOM 2770 O SER A 443 -5.553 -17.712 26.723 1.00121.24 O
ANISOU 2770 O SER A 443 13860 20609 11597 -722 691 -319 O
ATOM 2771 CB SER A 443 -2.650 -16.967 27.294 1.00124.30 C
ANISOU 2771 CB SER A 443 13801 21978 11450 -1153 620 -523 C
ATOM 2772 OG SER A 443 -1.363 -16.405 27.102 1.00132.74 O
ANISOU 2772 OG SER A 443 14681 23476 12280 -1457 602 -639 O
ATOM 2773 N LYS A 444 -4.420 -19.459 25.752 1.00118.32 N
ANISOU 2773 N LYS A 444 13190 20594 11171 -400 634 -195 N
ATOM 2774 CA LYS A 444 -5.408 -20.555 25.839 1.00116.86 C
ANISOU 2774 CA LYS A 444 13118 20139 11142 -93 646 -63 C
ATOM 2775 C LYS A 444 -6.658 -20.252 25.004 1.00118.50 C
ANISOU 2775 C LYS A 444 13538 19895 11590 -135 696 -37 C
ATOM 2776 O LYS A 444 -6.878 -20.881 23.972 1.00116.63 O
ANISOU 2776 O LYS A 444 13323 19526 11467 -18 698 32 O
ATOM 2777 CB LYS A 444 -5.802 -20.854 27.310 1.00120.57 C
ANISOU 2777 CB LYS A 444 13625 20637 11548 13 647 -36 C
ATOM 2778 CG LYS A 444 -5.893 -22.339 27.681 1.00138.92 C
ANISOU 2778 CG LYS A 444 15956 22982 13846 352 622 101 C
ATOM 2779 CD LYS A 444 -4.568 -22.928 28.212 1.00151.47 C
ANISOU 2779 CD LYS A 444 17342 25027 15183 521 548 103 C
ATOM 2780 CE LYS A 444 -4.263 -22.593 29.659 1.00163.12 C
ANISOU 2780 CE LYS A 444 18756 26742 16481 476 528 58 C
ATOM 2781 NZ LYS A 444 -3.558 -21.288 29.803 1.00171.65 N
ANISOU 2781 NZ LYS A 444 19696 28075 17449 145 526 -103 N
ATOM 2782 N ILE A 445 -7.472 -19.294 25.474 1.00115.06 N
ANISOU 2782 N ILE A 445 13256 19248 11213 -282 731 -100 N
ATOM 2783 CA ILE A 445 -8.727 -18.830 24.885 1.00113.32 C
ANISOU 2783 CA ILE A 445 13231 18643 11183 -299 771 -101 C
ATOM 2784 C ILE A 445 -8.480 -17.545 24.068 1.00115.63 C
ANISOU 2784 C ILE A 445 13631 18832 11473 -552 771 -196 C
ATOM 2785 O ILE A 445 -9.000 -17.425 22.957 1.00114.19 O
ANISOU 2785 O ILE A 445 13545 18420 11420 -539 780 -171 O
ATOM 2786 CB ILE A 445 -9.795 -18.637 26.011 1.00116.72 C
ANISOU 2786 CB ILE A 445 13767 18940 11643 -248 806 -120 C
ATOM 2787 CG1 ILE A 445 -11.163 -18.152 25.459 1.00116.36 C
ANISOU 2787 CG1 ILE A 445 13892 18555 11766 -222 842 -138 C
ATOM 2788 CG2 ILE A 445 -9.273 -17.760 27.178 1.00119.47 C
ANISOU 2788 CG2 ILE A 445 14111 19461 11823 -410 799 -230 C
ATOM 2789 CD1 ILE A 445 -12.404 -18.387 26.400 1.00124.70 C
ANISOU 2789 CD1 ILE A 445 14995 19525 12859 -105 885 -136 C
ATOM 2790 N ASN A 446 -7.683 -16.603 24.618 1.00112.02 N
ANISOU 2790 N ASN A 446 13175 18542 10846 -795 761 -305 N
ATOM 2791 CA ASN A 446 -7.351 -15.332 23.982 1.00111.84 C
ANISOU 2791 CA ASN A 446 13311 18418 10766 -1092 764 -401 C
ATOM 2792 C ASN A 446 -6.398 -15.532 22.786 1.00114.03 C
ANISOU 2792 C ASN A 446 13463 18866 10996 -1204 749 -380 C
ATOM 2793 O ASN A 446 -6.371 -14.680 21.898 1.00114.72 O
ANISOU 2793 O ASN A 446 13720 18787 11082 -1413 758 -420 O
ATOM 2794 CB ASN A 446 -6.751 -14.361 25.004 1.00113.23 C
ANISOU 2794 CB ASN A 446 13536 18745 10742 -1353 762 -527 C
ATOM 2795 N GLU A 447 -5.652 -16.659 22.748 1.00108.07 N
ANISOU 2795 N GLU A 447 12433 18439 10190 -1044 726 -318 N
ATOM 2796 CA GLU A 447 -4.689 -17.001 21.692 1.00107.08 C
ANISOU 2796 CA GLU A 447 12133 18557 9994 -1094 711 -307 C
ATOM 2797 C GLU A 447 -5.385 -17.526 20.418 1.00105.63 C
ANISOU 2797 C GLU A 447 12032 18090 10012 -928 721 -215 C
ATOM 2798 O GLU A 447 -5.002 -17.136 19.303 1.00105.60 O
ANISOU 2798 O GLU A 447 12046 18084 9991 -1092 727 -233 O
ATOM 2799 CB GLU A 447 -3.709 -18.054 22.219 1.00109.58 C
ANISOU 2799 CB GLU A 447 12142 19331 10162 -903 672 -284 C
ATOM 2800 CG GLU A 447 -2.289 -17.916 21.705 1.00124.63 C
ANISOU 2800 CG GLU A 447 13799 21705 11850 -1079 653 -357 C
ATOM 2801 CD GLU A 447 -1.307 -18.891 22.334 1.00150.98 C
ANISOU 2801 CD GLU A 447 16822 25545 15000 -843 602 -354 C
ATOM 2802 OE1 GLU A 447 -1.049 -18.780 23.556 1.00145.62 O
ANISOU 2802 OE1 GLU A 447 16072 25068 14188 -853 581 -395 O
ATOM 2803 OE2 GLU A 447 -0.787 -19.763 21.599 1.00143.80 O
ANISOU 2803 OE2 GLU A 447 15742 24838 14056 -631 579 -316 O
ATOM 2804 N THR A 448 -6.403 -18.413 20.585 1.00 97.09 N
ANISOU 2804 N THR A 448 11005 16785 9102 -630 726 -121 N
ATOM 2805 CA THR A 448 -7.166 -18.997 19.467 1.00 93.19 C
ANISOU 2805 CA THR A 448 10587 16028 8792 -472 735 -38 C
ATOM 2806 C THR A 448 -8.141 -17.972 18.891 1.00 92.82 C
ANISOU 2806 C THR A 448 10786 15615 8865 -598 756 -67 C
ATOM 2807 O THR A 448 -8.632 -18.150 17.780 1.00 91.36 O
ANISOU 2807 O THR A 448 10669 15243 8802 -541 759 -23 O
ATOM 2808 CB THR A 448 -7.919 -20.296 19.856 1.00 93.85 C
ANISOU 2808 CB THR A 448 10664 16015 8980 -163 738 64 C
ATOM 2809 OG1 THR A 448 -9.191 -19.991 20.411 1.00 88.47 O
ANISOU 2809 OG1 THR A 448 10139 15067 8409 -141 766 65 O
ATOM 2810 CG2 THR A 448 -7.118 -21.224 20.762 1.00 93.21 C
ANISOU 2810 CG2 THR A 448 10418 16244 8753 3 709 95 C
ATOM 2811 N MET A 449 -8.434 -16.923 19.668 1.00 87.75 N
ANISOU 2811 N MET A 449 10291 14874 8177 -742 765 -146 N
ATOM 2812 CA MET A 449 -9.325 -15.832 19.302 1.00 86.31 C
ANISOU 2812 CA MET A 449 10384 14348 8064 -823 774 -191 C
ATOM 2813 C MET A 449 -8.742 -14.976 18.179 1.00 89.51 C
ANISOU 2813 C MET A 449 10916 14692 8401 -1072 767 -225 C
ATOM 2814 O MET A 449 -9.447 -14.694 17.210 1.00 88.51 O
ANISOU 2814 O MET A 449 10960 14291 8378 -1028 763 -200 O
ATOM 2815 CB MET A 449 -9.616 -14.960 20.525 1.00 89.53 C
ANISOU 2815 CB MET A 449 10927 14699 8393 -900 782 -281 C
ATOM 2816 CG MET A 449 -11.027 -15.051 20.990 1.00 92.47 C
ANISOU 2816 CG MET A 449 11397 14844 8892 -674 797 -274 C
ATOM 2817 SD MET A 449 -12.112 -13.940 20.087 1.00 96.99 S
ANISOU 2817 SD MET A 449 12292 15015 9544 -645 788 -317 S
ATOM 2818 CE MET A 449 -12.943 -15.084 19.098 1.00 91.81 C
ANISOU 2818 CE MET A 449 11503 14302 9076 -403 790 -206 C
ATOM 2819 N ALEU A 450 -7.464 -14.564 18.311 0.50 87.20 N
ANISOU 2819 N ALEU A 450 10540 14676 7916 -1348 766 -285 N
ATOM 2820 N BLEU A 450 -7.478 -14.560 18.294 0.50 87.08 N
ANISOU 2820 N BLEU A 450 10528 14655 7902 -1347 766 -285 N
ATOM 2821 CA ALEU A 450 -6.799 -13.741 17.308 0.50 88.18 C
ANISOU 2821 CA ALEU A 450 10786 14787 7930 -1655 769 -322 C
ATOM 2822 CA BLEU A 450 -6.904 -13.727 17.251 0.50 87.91 C
ANISOU 2822 CA BLEU A 450 10773 14717 7911 -1640 769 -318 C
ATOM 2823 C ALEU A 450 -6.390 -14.597 16.099 0.50 90.35 C
ANISOU 2823 C ALEU A 450 10875 15202 8254 -1577 767 -249 C
ATOM 2824 C BLEU A 450 -6.375 -14.590 16.089 0.50 90.31 C
ANISOU 2824 C BLEU A 450 10870 15198 8246 -1582 767 -250 C
ATOM 2825 O ALEU A 450 -6.358 -14.082 14.979 0.50 90.49 O
ANISOU 2825 O ALEU A 450 11044 15073 8264 -1727 771 -242 O
ATOM 2826 O BLEU A 450 -6.303 -14.084 14.968 0.50 90.47 O
ANISOU 2826 O BLEU A 450 11034 15088 8254 -1738 772 -244 O
ATOM 2827 CB ALEU A 450 -5.594 -12.970 17.898 0.50 90.73 C
ANISOU 2827 CB ALEU A 450 11080 15398 7994 -2034 777 -429 C
ATOM 2828 CB BLEU A 450 -5.858 -12.749 17.804 0.50 90.46 C
ANISOU 2828 CB BLEU A 450 11143 15241 7985 -2036 777 -430 C
ATOM 2829 CG ALEU A 450 -4.255 -13.695 18.043 0.50 96.08 C
ANISOU 2829 CG ALEU A 450 11367 16629 8512 -2105 773 -446 C
ATOM 2830 CG BLEU A 450 -6.475 -11.451 18.371 0.50 95.82 C
ANISOU 2830 CG BLEU A 450 12214 15573 8618 -2178 780 -510 C
ATOM 2831 CD1ALEU A 450 -3.164 -12.952 17.309 0.50 98.18 C
ANISOU 2831 CD1ALEU A 450 11639 17107 8557 -2540 791 -518 C
ATOM 2832 CD1BLEU A 450 -6.745 -11.556 19.860 0.50 95.53 C
ANISOU 2832 CD1BLEU A 450 12112 15617 8568 -2061 779 -556 C
ATOM 2833 CD2ALEU A 450 -3.891 -13.883 19.499 0.50 99.47 C
ANISOU 2833 CD2ALEU A 450 11628 17332 8835 -2068 761 -496 C
ATOM 2834 CD2BLEU A 450 -5.598 -10.257 18.087 0.50101.33 C
ANISOU 2834 CD2BLEU A 450 13136 16284 9082 -2656 793 -600 C
ATOM 2835 N ARG A 451 -6.118 -15.905 16.321 1.00 84.35 N
ANISOU 2835 N ARG A 451 9819 14697 7532 -1325 758 -194 N
ATOM 2836 CA ARG A 451 -5.720 -16.845 15.257 1.00 81.48 C
ANISOU 2836 CA ARG A 451 9276 14479 7203 -1197 754 -133 C
ATOM 2837 C ARG A 451 -6.923 -17.000 14.317 1.00 81.51 C
ANISOU 2837 C ARG A 451 9464 14087 7420 -1035 755 -61 C
ATOM 2838 O ARG A 451 -6.759 -16.974 13.102 1.00 81.22 O
ANISOU 2838 O ARG A 451 9447 14019 7396 -1092 757 -39 O
ATOM 2839 CB ARG A 451 -5.255 -18.196 15.846 1.00 78.97 C
ANISOU 2839 CB ARG A 451 8679 14467 6859 -916 735 -94 C
ATOM 2840 CG ARG A 451 -4.674 -19.176 14.809 1.00 81.91 C
ANISOU 2840 CG ARG A 451 8869 15033 7220 -763 726 -54 C
ATOM 2841 CD ARG A 451 -3.800 -20.267 15.426 1.00 79.21 C
ANISOU 2841 CD ARG A 451 8261 15084 6752 -523 697 -48 C
ATOM 2842 NE ARG A 451 -3.179 -21.148 14.425 1.00 84.46 N
ANISOU 2842 NE ARG A 451 8765 15953 7373 -352 685 -29 N
ATOM 2843 CZ ARG A 451 -2.015 -20.914 13.812 1.00100.47 C
ANISOU 2843 CZ ARG A 451 10583 18380 9212 -504 686 -103 C
ATOM 2844 NH1 ARG A 451 -1.329 -19.805 14.067 1.00 95.95 N
ANISOU 2844 NH1 ARG A 451 9949 18039 8468 -879 701 -198 N
ATOM 2845 NH2 ARG A 451 -1.536 -21.783 12.931 1.00 81.49 N
ANISOU 2845 NH2 ARG A 451 8037 16155 6770 -297 675 -91 N
ATOM 2846 N LEU A 452 -8.139 -17.012 14.909 1.00 75.09 N
ANISOU 2846 N LEU A 452 8789 12994 6747 -863 755 -37 N
ATOM 2847 CA LEU A 452 -9.449 -17.102 14.262 1.00 72.35 C
ANISOU 2847 CA LEU A 452 8598 12308 6583 -697 753 13 C
ATOM 2848 C LEU A 452 -9.755 -15.837 13.456 1.00 76.40 C
ANISOU 2848 C LEU A 452 9384 12566 7080 -874 746 -22 C
ATOM 2849 O LEU A 452 -10.218 -15.945 12.321 1.00 76.45 O
ANISOU 2849 O LEU A 452 9460 12418 7171 -814 737 21 O
ATOM 2850 CB LEU A 452 -10.518 -17.328 15.342 1.00 71.37 C
ANISOU 2850 CB LEU A 452 8509 12059 6548 -511 761 17 C
ATOM 2851 CG LEU A 452 -11.829 -17.962 14.931 1.00 74.53 C
ANISOU 2851 CG LEU A 452 8945 12253 7119 -289 765 73 C
ATOM 2852 CD1 LEU A 452 -11.662 -19.417 14.572 1.00 73.42 C
ANISOU 2852 CD1 LEU A 452 8639 12225 7033 -137 770 154 C
ATOM 2853 CD2 LEU A 452 -12.810 -17.871 16.053 1.00 77.24 C
ANISOU 2853 CD2 LEU A 452 9331 12520 7497 -181 779 47 C
ATOM 2854 N GLY A 453 -9.480 -14.663 14.036 1.00 72.48 N
ANISOU 2854 N GLY A 453 9064 12020 6456 -1091 747 -100 N
ATOM 2855 CA GLY A 453 -9.678 -13.366 13.391 1.00 72.20 C
ANISOU 2855 CA GLY A 453 9367 11710 6355 -1278 736 -137 C
ATOM 2856 C GLY A 453 -8.707 -13.128 12.253 1.00 74.97 C
ANISOU 2856 C GLY A 453 9727 12164 6593 -1542 742 -127 C
ATOM 2857 O GLY A 453 -8.991 -12.361 11.331 1.00 74.27 O
ANISOU 2857 O GLY A 453 9920 11819 6481 -1642 730 -118 O
ATOM 2858 N ILE A 454 -7.545 -13.780 12.312 1.00 71.97 N
ANISOU 2858 N ILE A 454 9043 12183 6121 -1649 760 -131 N
ATOM 2859 CA ILE A 454 -6.553 -13.675 11.245 1.00 72.63 C
ANISOU 2859 CA ILE A 454 9067 12456 6076 -1898 774 -132 C
ATOM 2860 C ILE A 454 -7.045 -14.549 10.102 1.00 75.41 C
ANISOU 2860 C ILE A 454 9337 12728 6585 -1655 765 -47 C
ATOM 2861 O ILE A 454 -6.999 -14.122 8.949 1.00 76.44 O
ANISOU 2861 O ILE A 454 9615 12745 6684 -1792 766 -26 O
ATOM 2862 CB ILE A 454 -5.130 -14.048 11.743 1.00 76.46 C
ANISOU 2862 CB ILE A 454 9219 13461 6370 -2070 793 -189 C
ATOM 2863 CG1 ILE A 454 -4.535 -12.898 12.597 1.00 77.91 C
ANISOU 2863 CG1 ILE A 454 9542 13716 6343 -2442 806 -290 C
ATOM 2864 CG2 ILE A 454 -4.192 -14.439 10.566 1.00 77.65 C
ANISOU 2864 CG2 ILE A 454 9174 13912 6420 -2193 810 -181 C
ATOM 2865 CD1 ILE A 454 -3.386 -13.299 13.509 1.00 81.21 C
ANISOU 2865 CD1 ILE A 454 9612 14654 6591 -2526 812 -358 C
ATOM 2866 N PHE A 455 -7.580 -15.741 10.438 1.00 69.31 N
ANISOU 2866 N PHE A 455 8372 11990 5974 -1310 756 3 N
ATOM 2867 CA PHE A 455 -8.099 -16.705 9.467 1.00 66.88 C
ANISOU 2867 CA PHE A 455 7988 11610 5815 -1071 748 76 C
ATOM 2868 C PHE A 455 -9.311 -16.149 8.748 1.00 66.88 C
ANISOU 2868 C PHE A 455 8261 11216 5933 -1005 729 108 C
ATOM 2869 O PHE A 455 -9.355 -16.250 7.529 1.00 66.20 O
ANISOU 2869 O PHE A 455 8210 11073 5871 -1014 723 143 O
ATOM 2870 CB PHE A 455 -8.394 -18.051 10.139 1.00 67.86 C
ANISOU 2870 CB PHE A 455 7906 11836 6044 -764 746 115 C
ATOM 2871 CG PHE A 455 -7.181 -18.960 10.156 1.00 71.06 C
ANISOU 2871 CG PHE A 455 8030 12634 6336 -722 751 109 C
ATOM 2872 CD1 PHE A 455 -7.192 -20.171 9.480 1.00 74.23 C
ANISOU 2872 CD1 PHE A 455 8315 13086 6802 -495 746 159 C
ATOM 2873 CD2 PHE A 455 -6.008 -18.578 10.805 1.00 75.21 C
ANISOU 2873 CD2 PHE A 455 8413 13497 6666 -903 756 41 C
ATOM 2874 CE1 PHE A 455 -6.063 -20.992 9.471 1.00 76.01 C
ANISOU 2874 CE1 PHE A 455 8300 13681 6898 -401 743 142 C
ATOM 2875 CE2 PHE A 455 -4.883 -19.403 10.797 1.00 79.05 C
ANISOU 2875 CE2 PHE A 455 8616 14399 7019 -819 752 22 C
ATOM 2876 CZ PHE A 455 -4.910 -20.592 10.109 1.00 76.34 C
ANISOU 2876 CZ PHE A 455 8175 14090 6740 -551 743 72 C
ATOM 2877 N GLY A 456 -10.221 -15.501 9.489 1.00 61.87 N
ANISOU 2877 N GLY A 456 7817 10344 5345 -940 716 84 N
ATOM 2878 CA GLY A 456 -11.419 -14.841 8.972 1.00 60.60 C
ANISOU 2878 CA GLY A 456 7925 9839 5263 -833 686 95 C
ATOM 2879 C GLY A 456 -11.091 -13.749 7.973 1.00 65.60 C
ANISOU 2879 C GLY A 456 8835 10312 5777 -1061 672 91 C
ATOM 2880 O GLY A 456 -11.663 -13.722 6.878 1.00 65.25 O
ANISOU 2880 O GLY A 456 8895 10108 5788 -973 647 136 O
ATOM 2881 N PHE A 457 -10.110 -12.882 8.312 1.00 63.13 N
ANISOU 2881 N PHE A 457 8645 10062 5278 -1384 689 38 N
ATOM 2882 CA PHE A 457 -9.654 -11.813 7.425 1.00 64.47 C
ANISOU 2882 CA PHE A 457 9120 10088 5288 -1681 685 35 C
ATOM 2883 C PHE A 457 -8.865 -12.377 6.237 1.00 71.31 C
ANISOU 2883 C PHE A 457 9800 11178 6116 -1809 707 79 C
ATOM 2884 O PHE A 457 -9.086 -11.934 5.097 1.00 72.80 O
ANISOU 2884 O PHE A 457 10205 11177 6278 -1864 690 121 O
ATOM 2885 CB PHE A 457 -8.830 -10.780 8.186 1.00 67.98 C
ANISOU 2885 CB PHE A 457 9749 10560 5519 -2040 707 -43 C
ATOM 2886 CG PHE A 457 -9.678 -9.710 8.838 1.00 70.82 C
ANISOU 2886 CG PHE A 457 10514 10541 5854 -1974 675 -88 C
ATOM 2887 CD1 PHE A 457 -10.067 -8.575 8.128 1.00 75.32 C
ANISOU 2887 CD1 PHE A 457 11570 10726 6321 -2059 643 -80 C
ATOM 2888 CD2 PHE A 457 -10.089 -9.831 10.166 1.00 71.93 C
ANISOU 2888 CD2 PHE A 457 10573 10705 6051 -1809 675 -142 C
ATOM 2889 CE1 PHE A 457 -10.842 -7.575 8.739 1.00 77.24 C
ANISOU 2889 CE1 PHE A 457 12220 10610 6515 -1950 607 -133 C
ATOM 2890 CE2 PHE A 457 -10.854 -8.830 10.777 1.00 75.48 C
ANISOU 2890 CE2 PHE A 457 11398 10823 6457 -1726 647 -199 C
ATOM 2891 CZ PHE A 457 -11.225 -7.710 10.060 1.00 75.50 C
ANISOU 2891 CZ PHE A 457 11889 10441 6354 -1781 611 -199 C
ATOM 2892 N LEU A 458 -7.974 -13.373 6.487 1.00 67.55 N
ANISOU 2892 N LEU A 458 8929 11111 5627 -1822 739 67 N
ATOM 2893 CA LEU A 458 -7.167 -14.025 5.444 1.00 67.24 C
ANISOU 2893 CA LEU A 458 8666 11346 5537 -1898 761 91 C
ATOM 2894 C LEU A 458 -8.081 -14.722 4.416 1.00 69.05 C
ANISOU 2894 C LEU A 458 8890 11398 5947 -1608 736 165 C
ATOM 2895 O LEU A 458 -7.893 -14.493 3.226 1.00 69.18 O
ANISOU 2895 O LEU A 458 8992 11388 5906 -1730 739 193 O
ATOM 2896 CB LEU A 458 -6.158 -15.003 6.080 1.00 67.56 C
ANISOU 2896 CB LEU A 458 8293 11855 5520 -1865 787 52 C
ATOM 2897 CG LEU A 458 -5.063 -15.690 5.225 1.00 73.57 C
ANISOU 2897 CG LEU A 458 8765 13018 6170 -1934 813 42 C
ATOM 2898 CD1 LEU A 458 -4.392 -14.733 4.216 1.00 75.72 C
ANISOU 2898 CD1 LEU A 458 9192 13333 6247 -2341 841 24 C
ATOM 2899 CD2 LEU A 458 -3.999 -16.325 6.133 1.00 76.28 C
ANISOU 2899 CD2 LEU A 458 8751 13844 6389 -1920 827 -22 C
ATOM 2900 N ALA A 459 -9.133 -15.464 4.869 1.00 64.26 N
ANISOU 2900 N ALA A 459 8218 10659 5538 -1262 713 193 N
ATOM 2901 CA ALA A 459 -10.114 -16.133 3.990 1.00 62.49 C
ANISOU 2901 CA ALA A 459 7991 10277 5477 -1005 688 250 C
ATOM 2902 C ALA A 459 -11.051 -15.135 3.286 1.00 66.99 C
ANISOU 2902 C ALA A 459 8900 10497 6055 -1001 647 273 C
ATOM 2903 O ALA A 459 -11.488 -15.416 2.181 1.00 65.61 O
ANISOU 2903 O ALA A 459 8749 10247 5931 -916 628 315 O
ATOM 2904 CB ALA A 459 -10.940 -17.135 4.774 1.00 61.54 C
ANISOU 2904 CB ALA A 459 7718 10143 5520 -707 683 262 C
ATOM 2905 N PHE A 460 -11.388 -13.996 3.930 1.00 64.68 N
ANISOU 2905 N PHE A 460 8883 9990 5701 -1064 629 240 N
ATOM 2906 CA PHE A 460 -12.235 -12.962 3.324 1.00 64.90 C
ANISOU 2906 CA PHE A 460 9288 9672 5699 -1019 578 255 C
ATOM 2907 C PHE A 460 -11.521 -12.374 2.136 1.00 72.38 C
ANISOU 2907 C PHE A 460 10422 10583 6495 -1290 582 288 C
ATOM 2908 O PHE A 460 -12.150 -12.123 1.104 1.00 73.83 O
ANISOU 2908 O PHE A 460 10789 10572 6690 -1190 540 334 O
ATOM 2909 CB PHE A 460 -12.565 -11.859 4.345 1.00 67.51 C
ANISOU 2909 CB PHE A 460 9907 9792 5952 -1042 561 199 C
ATOM 2910 CG PHE A 460 -13.307 -10.654 3.810 1.00 69.45 C
ANISOU 2910 CG PHE A 460 10613 9659 6114 -980 501 205 C
ATOM 2911 CD1 PHE A 460 -12.616 -9.558 3.308 1.00 74.04 C
ANISOU 2911 CD1 PHE A 460 11572 10072 6489 -1297 500 211 C
ATOM 2912 CD2 PHE A 460 -14.693 -10.595 3.856 1.00 69.63 C
ANISOU 2912 CD2 PHE A 460 10710 9508 6236 -602 445 199 C
ATOM 2913 CE1 PHE A 460 -13.301 -8.451 2.809 1.00 76.33 C
ANISOU 2913 CE1 PHE A 460 12350 9973 6677 -1208 436 224 C
ATOM 2914 CE2 PHE A 460 -15.373 -9.479 3.380 1.00 73.88 C
ANISOU 2914 CE2 PHE A 460 11689 9710 6673 -483 377 199 C
ATOM 2915 CZ PHE A 460 -14.674 -8.417 2.856 1.00 74.40 C
ANISOU 2915 CZ PHE A 460 12172 9559 6537 -772 370 217 C
ATOM 2916 N GLY A 461 -10.216 -12.146 2.299 1.00 70.32 N
ANISOU 2916 N GLY A 461 10108 10536 6075 -1641 632 260 N
ATOM 2917 CA GLY A 461 -9.361 -11.606 1.247 1.00 72.11 C
ANISOU 2917 CA GLY A 461 10481 10801 6116 -1980 653 281 C
ATOM 2918 C GLY A 461 -9.368 -12.450 -0.012 1.00 74.30 C
ANISOU 2918 C GLY A 461 10567 11203 6460 -1882 655 334 C
ATOM 2919 O GLY A 461 -9.441 -11.912 -1.125 1.00 75.51 O
ANISOU 2919 O GLY A 461 10963 11205 6523 -1997 639 380 O
ATOM 2920 N PHE A 462 -9.321 -13.786 0.164 1.00 67.55 N
ANISOU 2920 N PHE A 462 9307 10607 5752 -1659 671 329 N
ATOM 2921 CA PHE A 462 -9.324 -14.736 -0.943 1.00 66.13 C
ANISOU 2921 CA PHE A 462 8932 10555 5639 -1538 675 365 C
ATOM 2922 C PHE A 462 -10.703 -14.782 -1.666 1.00 70.22 C
ANISOU 2922 C PHE A 462 9616 10770 6295 -1268 615 419 C
ATOM 2923 O PHE A 462 -10.739 -14.796 -2.907 1.00 71.55 O
ANISOU 2923 O PHE A 462 9850 10908 6426 -1303 604 459 O
ATOM 2924 CB PHE A 462 -8.891 -16.126 -0.458 1.00 66.06 C
ANISOU 2924 CB PHE A 462 8514 10864 5721 -1361 704 339 C
ATOM 2925 CG PHE A 462 -7.407 -16.246 -0.176 1.00 68.42 C
ANISOU 2925 CG PHE A 462 8586 11566 5845 -1596 756 284 C
ATOM 2926 CD1 PHE A 462 -6.464 -15.962 -1.167 1.00 72.38 C
ANISOU 2926 CD1 PHE A 462 9065 12273 6163 -1873 790 272 C
ATOM 2927 CD2 PHE A 462 -6.951 -16.675 1.064 1.00 69.01 C
ANISOU 2927 CD2 PHE A 462 8449 11855 5918 -1537 771 237 C
ATOM 2928 CE1 PHE A 462 -5.095 -16.067 -0.904 1.00 74.29 C
ANISOU 2928 CE1 PHE A 462 9053 12961 6211 -2093 839 203 C
ATOM 2929 CE2 PHE A 462 -5.582 -16.779 1.324 1.00 72.99 C
ANISOU 2929 CE2 PHE A 462 8713 12788 6233 -1732 811 174 C
ATOM 2930 CZ PHE A 462 -4.663 -16.484 0.336 1.00 72.69 C
ANISOU 2930 CZ PHE A 462 8627 12987 6006 -2007 845 151 C
ATOM 2931 N VAL A 463 -11.814 -14.745 -0.896 1.00 63.96 N
ANISOU 2931 N VAL A 463 8885 9785 5633 -1015 576 413 N
ATOM 2932 CA VAL A 463 -13.194 -14.717 -1.392 1.00 63.02 C
ANISOU 2932 CA VAL A 463 8891 9435 5621 -741 514 442 C
ATOM 2933 C VAL A 463 -13.354 -13.438 -2.218 1.00 69.12 C
ANISOU 2933 C VAL A 463 10073 9941 6247 -849 469 475 C
ATOM 2934 O VAL A 463 -13.989 -13.462 -3.287 1.00 68.22 O
ANISOU 2934 O VAL A 463 10045 9726 6148 -723 424 517 O
ATOM 2935 CB VAL A 463 -14.218 -14.818 -0.214 1.00 66.28 C
ANISOU 2935 CB VAL A 463 9264 9766 6153 -489 493 406 C
ATOM 2936 CG1 VAL A 463 -15.662 -14.746 -0.697 1.00 65.22 C
ANISOU 2936 CG1 VAL A 463 9220 9466 6095 -202 427 416 C
ATOM 2937 CG2 VAL A 463 -14.006 -16.102 0.590 1.00 64.94 C
ANISOU 2937 CG2 VAL A 463 8739 9836 6097 -411 539 386 C
ATOM 2938 N LEU A 464 -12.712 -12.337 -1.745 1.00 67.53 N
ANISOU 2938 N LEU A 464 10144 9632 5883 -1104 482 457 N
ATOM 2939 CA LEU A 464 -12.703 -11.049 -2.443 1.00 69.70 C
ANISOU 2939 CA LEU A 464 10893 9619 5972 -1264 445 492 C
ATOM 2940 C LEU A 464 -11.983 -11.147 -3.823 1.00 72.59 C
ANISOU 2940 C LEU A 464 11268 10087 6228 -1499 468 545 C
ATOM 2941 O LEU A 464 -12.449 -10.530 -4.787 1.00 72.72 O
ANISOU 2941 O LEU A 464 11604 9866 6161 -1464 416 601 O
ATOM 2942 CB LEU A 464 -12.067 -9.957 -1.579 1.00 71.85 C
ANISOU 2942 CB LEU A 464 11456 9772 6072 -1549 468 450 C
ATOM 2943 CG LEU A 464 -12.277 -8.531 -2.077 1.00 79.46 C
ANISOU 2943 CG LEU A 464 13024 10336 6830 -1667 418 482 C
ATOM 2944 CD1 LEU A 464 -13.726 -8.084 -1.885 1.00 80.22 C
ANISOU 2944 CD1 LEU A 464 13372 10111 6995 -1223 324 479 C
ATOM 2945 CD2 LEU A 464 -11.338 -7.577 -1.390 1.00 83.40 C
ANISOU 2945 CD2 LEU A 464 13794 10774 7121 -2077 463 437 C
ATOM 2946 N ILE A 465 -10.888 -11.939 -3.922 1.00 67.22 N
ANISOU 2946 N ILE A 465 10234 9773 5534 -1702 542 525 N
ATOM 2947 CA ILE A 465 -10.191 -12.125 -5.203 1.00 66.97 C
ANISOU 2947 CA ILE A 465 10155 9898 5390 -1910 573 560 C
ATOM 2948 C ILE A 465 -11.062 -12.969 -6.152 1.00 68.68 C
ANISOU 2948 C ILE A 465 10239 10096 5762 -1590 530 601 C
ATOM 2949 O ILE A 465 -11.203 -12.570 -7.312 1.00 68.88 O
ANISOU 2949 O ILE A 465 10485 9992 5693 -1645 501 656 O
ATOM 2950 CB ILE A 465 -8.760 -12.709 -5.074 1.00 69.36 C
ANISOU 2950 CB ILE A 465 10101 10650 5602 -2182 660 508 C
ATOM 2951 CG1 ILE A 465 -7.870 -11.816 -4.178 1.00 71.00 C
ANISOU 2951 CG1 ILE A 465 10437 10918 5620 -2553 703 458 C
ATOM 2952 CG2 ILE A 465 -8.130 -12.933 -6.462 1.00 68.72 C
ANISOU 2952 CG2 ILE A 465 9952 10759 5401 -2361 693 535 C
ATOM 2953 CD1 ILE A 465 -6.572 -12.451 -3.749 1.00 72.41 C
ANISOU 2953 CD1 ILE A 465 10199 11598 5716 -2745 777 384 C
ATOM 2954 N THR A 466 -11.655 -14.109 -5.670 1.00 62.43 N
ANISOU 2954 N THR A 466 9115 9421 5185 -1280 524 573 N
ATOM 2955 CA THR A 466 -12.513 -14.962 -6.521 1.00 60.48 C
ANISOU 2955 CA THR A 466 8739 9169 5073 -1008 487 598 C
ATOM 2956 C THR A 466 -13.717 -14.181 -7.020 1.00 64.94 C
ANISOU 2956 C THR A 466 9624 9419 5632 -826 399 639 C
ATOM 2957 O THR A 466 -13.996 -14.224 -8.210 1.00 64.83 O
ANISOU 2957 O THR A 466 9677 9369 5587 -784 366 680 O
ATOM 2958 CB THR A 466 -12.973 -16.251 -5.855 1.00 63.76 C
ANISOU 2958 CB THR A 466 8815 9725 5685 -755 498 560 C
ATOM 2959 OG1 THR A 466 -13.797 -15.947 -4.735 1.00 67.70 O
ANISOU 2959 OG1 THR A 466 9375 10080 6267 -594 470 538 O
ATOM 2960 CG2 THR A 466 -11.834 -17.165 -5.487 1.00 62.23 C
ANISOU 2960 CG2 THR A 466 8315 9846 5485 -852 570 522 C
ATOM 2961 N PHE A 467 -14.378 -13.418 -6.135 1.00 62.59 N
ANISOU 2961 N PHE A 467 9538 8907 5337 -710 358 624 N
ATOM 2962 CA PHE A 467 -15.508 -12.574 -6.505 1.00 63.91 C
ANISOU 2962 CA PHE A 467 10033 8787 5463 -484 264 650 C
ATOM 2963 C PHE A 467 -15.141 -11.655 -7.695 1.00 70.90 C
ANISOU 2963 C PHE A 467 11300 9495 6144 -670 235 720 C
ATOM 2964 O PHE A 467 -15.908 -11.567 -8.654 1.00 71.17 O
ANISOU 2964 O PHE A 467 11452 9429 6161 -476 164 761 O
ATOM 2965 CB PHE A 467 -15.986 -11.738 -5.291 1.00 66.45 C
ANISOU 2965 CB PHE A 467 10567 8914 5768 -369 234 609 C
ATOM 2966 CG PHE A 467 -17.203 -10.891 -5.588 1.00 69.30 C
ANISOU 2966 CG PHE A 467 11256 9007 6070 -54 128 619 C
ATOM 2967 CD1 PHE A 467 -18.473 -11.460 -5.639 1.00 71.37 C
ANISOU 2967 CD1 PHE A 467 11307 9356 6457 319 72 590 C
ATOM 2968 CD2 PHE A 467 -17.073 -9.542 -5.887 1.00 73.85 C
ANISOU 2968 CD2 PHE A 467 12365 9259 6436 -131 80 654 C
ATOM 2969 CE1 PHE A 467 -19.587 -10.690 -5.984 1.00 73.80 C
ANISOU 2969 CE1 PHE A 467 11884 9477 6680 648 -36 589 C
ATOM 2970 CE2 PHE A 467 -18.188 -8.776 -6.229 1.00 78.48 C
ANISOU 2970 CE2 PHE A 467 13278 9601 6942 219 -32 663 C
ATOM 2971 CZ PHE A 467 -19.438 -9.354 -6.272 1.00 75.56 C
ANISOU 2971 CZ PHE A 467 12645 9367 6697 627 -92 627 C
ATOM 2972 N SER A 468 -13.958 -11.004 -7.629 1.00 69.59 N
ANISOU 2972 N SER A 468 11318 9316 5806 -1063 293 732 N
ATOM 2973 CA SER A 468 -13.432 -10.073 -8.631 1.00 71.55 C
ANISOU 2973 CA SER A 468 11968 9400 5819 -1339 286 800 C
ATOM 2974 C SER A 468 -13.168 -10.778 -9.954 1.00 75.77 C
ANISOU 2974 C SER A 468 12313 10129 6349 -1395 302 840 C
ATOM 2975 O SER A 468 -13.561 -10.265 -11.005 1.00 77.20 O
ANISOU 2975 O SER A 468 12790 10125 6418 -1351 242 908 O
ATOM 2976 CB SER A 468 -12.157 -9.417 -8.117 1.00 75.77 C
ANISOU 2976 CB SER A 468 12650 9971 6169 -1806 364 780 C
ATOM 2977 OG SER A 468 -12.382 -8.807 -6.856 1.00 82.54 O
ANISOU 2977 OG SER A 468 13676 10655 7030 -1759 351 732 O
ATOM 2978 N CYS A 469 -12.539 -11.974 -9.892 1.00 70.11 N
ANISOU 2978 N CYS A 469 11113 9779 5744 -1455 377 796 N
ATOM 2979 CA CYS A 469 -12.232 -12.821 -11.041 1.00 68.38 C
ANISOU 2979 CA CYS A 469 10657 9790 5534 -1484 403 811 C
ATOM 2980 C CYS A 469 -13.520 -13.275 -11.716 1.00 74.85 C
ANISOU 2980 C CYS A 469 11452 10508 6481 -1112 319 835 C
ATOM 2981 O CYS A 469 -13.625 -13.158 -12.935 1.00 77.61 O
ANISOU 2981 O CYS A 469 11932 10821 6736 -1137 289 887 O
ATOM 2982 CB CYS A 469 -11.387 -14.012 -10.615 1.00 66.01 C
ANISOU 2982 CB CYS A 469 9878 9874 5329 -1536 488 741 C
ATOM 2983 SG CYS A 469 -9.714 -13.589 -10.075 1.00 70.96 S
ANISOU 2983 SG CYS A 469 10445 10763 5754 -1999 589 697 S
ATOM 2984 N HIS A 470 -14.509 -13.749 -10.931 1.00 70.49 N
ANISOU 2984 N HIS A 470 10737 9927 6118 -788 279 794 N
ATOM 2985 CA HIS A 470 -15.814 -14.180 -11.431 1.00 70.55 C
ANISOU 2985 CA HIS A 470 10683 9890 6232 -445 199 796 C
ATOM 2986 C HIS A 470 -16.557 -13.022 -12.083 1.00 79.07 C
ANISOU 2986 C HIS A 470 12191 10686 7168 -322 98 857 C
ATOM 2987 O HIS A 470 -17.179 -13.212 -13.137 1.00 77.39 O
ANISOU 2987 O HIS A 470 11992 10479 6936 -175 39 886 O
ATOM 2988 CB HIS A 470 -16.655 -14.797 -10.308 1.00 69.87 C
ANISOU 2988 CB HIS A 470 10356 9856 6335 -185 189 732 C
ATOM 2989 CG HIS A 470 -16.362 -16.252 -10.145 1.00 71.73 C
ANISOU 2989 CG HIS A 470 10181 10354 6717 -188 256 686 C
ATOM 2990 ND1 HIS A 470 -17.157 -17.217 -10.733 1.00 72.82 N
ANISOU 2990 ND1 HIS A 470 10121 10593 6955 -10 231 666 N
ATOM 2991 CD2 HIS A 470 -15.310 -16.858 -9.552 1.00 73.01 C
ANISOU 2991 CD2 HIS A 470 10139 10693 6910 -352 342 656 C
ATOM 2992 CE1 HIS A 470 -16.582 -18.375 -10.454 1.00 71.02 C
ANISOU 2992 CE1 HIS A 470 9617 10552 6816 -69 303 628 C
ATOM 2993 NE2 HIS A 470 -15.470 -18.206 -9.746 1.00 71.43 N
ANISOU 2993 NE2 HIS A 470 9648 10663 6829 -247 367 623 N
ATOM 2994 N PHE A 471 -16.445 -11.812 -11.480 1.00 80.38 N
ANISOU 2994 N PHE A 471 12735 10596 7210 -382 76 874 N
ATOM 2995 CA PHE A 471 -17.071 -10.598 -11.998 1.00 83.89 C
ANISOU 2995 CA PHE A 471 13679 10716 7478 -245 -26 933 C
ATOM 2996 C PHE A 471 -16.461 -10.217 -13.348 1.00 90.02 C
ANISOU 2996 C PHE A 471 14710 11433 8060 -492 -25 1020 C
ATOM 2997 O PHE A 471 -17.219 -9.934 -14.285 1.00 91.50 O
ANISOU 2997 O PHE A 471 15103 11499 8166 -277 -119 1071 O
ATOM 2998 CB PHE A 471 -16.967 -9.428 -11.007 1.00 88.07 C
ANISOU 2998 CB PHE A 471 14602 10964 7899 -286 -40 924 C
ATOM 2999 CG PHE A 471 -18.109 -8.449 -11.162 1.00 92.79 C
ANISOU 2999 CG PHE A 471 15623 11251 8384 87 -171 946 C
ATOM 3000 CD1 PHE A 471 -19.171 -8.449 -10.264 1.00 96.07 C
ANISOU 3000 CD1 PHE A 471 15940 11660 8903 483 -229 872 C
ATOM 3001 CD2 PHE A 471 -18.144 -7.555 -12.235 1.00 98.52 C
ANISOU 3001 CD2 PHE A 471 16841 11714 8879 67 -242 1037 C
ATOM 3002 CE1 PHE A 471 -20.237 -7.561 -10.418 1.00 99.71 C
ANISOU 3002 CE1 PHE A 471 16767 11881 9236 887 -359 877 C
ATOM 3003 CE2 PHE A 471 -19.217 -6.681 -12.401 1.00104.22 C
ANISOU 3003 CE2 PHE A 471 17964 12159 9475 478 -377 1054 C
ATOM 3004 CZ PHE A 471 -20.252 -6.681 -11.484 1.00102.40 C
ANISOU 3004 CZ PHE A 471 17611 11949 9346 902 -437 968 C
ATOM 3005 N TYR A 472 -15.101 -10.234 -13.457 1.00 85.75 N
ANISOU 3005 N TYR A 472 14135 11018 7430 -939 81 1031 N
ATOM 3006 CA TYR A 472 -14.391 -9.938 -14.704 1.00 86.75 C
ANISOU 3006 CA TYR A 472 14457 11149 7354 -1239 105 1104 C
ATOM 3007 C TYR A 472 -14.956 -10.823 -15.812 1.00 87.31 C
ANISOU 3007 C TYR A 472 14276 11389 7509 -1027 68 1116 C
ATOM 3008 O TYR A 472 -15.337 -10.307 -16.858 1.00 87.37 O
ANISOU 3008 O TYR A 472 14586 11244 7366 -982 0 1192 O
ATOM 3009 CB TYR A 472 -12.862 -10.127 -14.543 1.00 88.48 C
ANISOU 3009 CB TYR A 472 14508 11624 7487 -1727 239 1077 C
ATOM 3010 CG TYR A 472 -12.060 -9.979 -15.825 1.00 92.53 C
ANISOU 3010 CG TYR A 472 15132 12240 7787 -2066 284 1135 C
ATOM 3011 CD1 TYR A 472 -11.611 -11.098 -16.526 1.00 93.14 C
ANISOU 3011 CD1 TYR A 472 14772 12684 7931 -2100 342 1103 C
ATOM 3012 CD2 TYR A 472 -11.745 -8.719 -16.336 1.00 96.54 C
ANISOU 3012 CD2 TYR A 472 16206 12472 8004 -2361 271 1219 C
ATOM 3013 CE1 TYR A 472 -10.876 -10.968 -17.707 1.00 94.80 C
ANISOU 3013 CE1 TYR A 472 15064 13024 7932 -2409 388 1147 C
ATOM 3014 CE2 TYR A 472 -11.016 -8.577 -17.519 1.00 98.77 C
ANISOU 3014 CE2 TYR A 472 16594 12866 8068 -2703 319 1275 C
ATOM 3015 CZ TYR A 472 -10.582 -9.705 -18.199 1.00103.14 C
ANISOU 3015 CZ TYR A 472 16663 13827 8701 -2722 379 1235 C
ATOM 3016 OH TYR A 472 -9.846 -9.576 -19.350 1.00105.19 O
ANISOU 3016 OH TYR A 472 17001 14233 8733 -3061 434 1279 O
ATOM 3017 N ASP A 473 -15.090 -12.140 -15.535 1.00 81.22 N
ANISOU 3017 N ASP A 473 12983 10909 6967 -881 105 1040 N
ATOM 3018 CA ASP A 473 -15.636 -13.135 -16.461 1.00 79.40 C
ANISOU 3018 CA ASP A 473 12475 10861 6833 -694 80 1028 C
ATOM 3019 C ASP A 473 -17.068 -12.801 -16.846 1.00 83.57 C
ANISOU 3019 C ASP A 473 13167 11220 7364 -311 -53 1053 C
ATOM 3020 O ASP A 473 -17.371 -12.735 -18.032 1.00 84.16 O
ANISOU 3020 O ASP A 473 13342 11291 7342 -259 -107 1100 O
ATOM 3021 CB ASP A 473 -15.563 -14.547 -15.854 1.00 77.88 C
ANISOU 3021 CB ASP A 473 11770 10951 6869 -613 144 936 C
ATOM 3022 CG ASP A 473 -14.157 -15.084 -15.686 1.00 77.88 C
ANISOU 3022 CG ASP A 473 11546 11197 6849 -920 265 900 C
ATOM 3023 OD1 ASP A 473 -13.421 -15.142 -16.694 1.00 75.34 O
ANISOU 3023 OD1 ASP A 473 11230 11004 6392 -1132 305 922 O
ATOM 3024 OD2 ASP A 473 -13.814 -15.504 -14.557 1.00 83.88 O
ANISOU 3024 OD2 ASP A 473 12097 12055 7717 -924 316 843 O
ATOM 3025 N PHE A 474 -17.920 -12.534 -15.850 1.00 80.25 N
ANISOU 3025 N PHE A 474 12780 10684 7029 -43 -109 1016 N
ATOM 3026 CA PHE A 474 -19.323 -12.203 -16.035 1.00 81.34 C
ANISOU 3026 CA PHE A 474 13026 10723 7155 367 -239 1014 C
ATOM 3027 C PHE A 474 -19.520 -11.009 -16.953 1.00 91.65 C
ANISOU 3027 C PHE A 474 14856 11756 8212 425 -336 1111 C
ATOM 3028 O PHE A 474 -20.248 -11.134 -17.940 1.00 93.31 O
ANISOU 3028 O PHE A 474 15069 12015 8368 640 -423 1133 O
ATOM 3029 CB PHE A 474 -20.012 -11.923 -14.679 1.00 82.53 C
ANISOU 3029 CB PHE A 474 13156 10804 7397 609 -267 950 C
ATOM 3030 CG PHE A 474 -21.323 -11.162 -14.787 1.00 85.49 C
ANISOU 3030 CG PHE A 474 13768 11038 7675 1038 -410 949 C
ATOM 3031 CD1 PHE A 474 -22.486 -11.799 -15.214 1.00 87.07 C
ANISOU 3031 CD1 PHE A 474 13687 11460 7937 1353 -484 899 C
ATOM 3032 CD2 PHE A 474 -21.383 -9.801 -14.500 1.00 89.32 C
ANISOU 3032 CD2 PHE A 474 14772 11183 7980 1131 -474 989 C
ATOM 3033 CE1 PHE A 474 -23.683 -11.092 -15.338 1.00 89.34 C
ANISOU 3033 CE1 PHE A 474 14159 11681 8104 1782 -623 885 C
ATOM 3034 CE2 PHE A 474 -22.581 -9.097 -14.635 1.00 93.51 C
ANISOU 3034 CE2 PHE A 474 15537 11597 8394 1588 -616 981 C
ATOM 3035 CZ PHE A 474 -23.724 -9.750 -15.038 1.00 90.73 C
ANISOU 3035 CZ PHE A 474 14850 11520 8103 1925 -691 925 C
ATOM 3036 N PHE A 475 -18.912 -9.847 -16.623 1.00 91.30 N
ANISOU 3036 N PHE A 475 15278 11416 7997 240 -327 1167 N
ATOM 3037 CA PHE A 475 -19.147 -8.625 -17.385 1.00 94.53 C
ANISOU 3037 CA PHE A 475 16285 11492 8139 311 -427 1265 C
ATOM 3038 C PHE A 475 -18.476 -8.647 -18.776 1.00 96.36 C
ANISOU 3038 C PHE A 475 16645 11756 8212 24 -402 1355 C
ATOM 3039 O PHE A 475 -18.862 -7.832 -19.614 1.00 98.71 O
ANISOU 3039 O PHE A 475 17396 11818 8291 146 -502 1443 O
ATOM 3040 CB PHE A 475 -18.811 -7.354 -16.559 1.00 99.37 C
ANISOU 3040 CB PHE A 475 17424 11736 8597 208 -430 1289 C
ATOM 3041 CG PHE A 475 -17.465 -6.676 -16.665 1.00104.02 C
ANISOU 3041 CG PHE A 475 18372 12160 8991 -337 -337 1354 C
ATOM 3042 CD1 PHE A 475 -16.502 -6.849 -15.675 1.00107.21 C
ANISOU 3042 CD1 PHE A 475 18594 12673 9467 -690 -214 1296 C
ATOM 3043 CD2 PHE A 475 -17.214 -5.740 -17.669 1.00111.07 C
ANISOU 3043 CD2 PHE A 475 19841 12769 9589 -492 -382 1469 C
ATOM 3044 CE1 PHE A 475 -15.275 -6.164 -15.735 1.00110.67 C
ANISOU 3044 CE1 PHE A 475 19357 13002 9690 -1224 -128 1340 C
ATOM 3045 CE2 PHE A 475 -15.983 -5.066 -17.738 1.00116.44 C
ANISOU 3045 CE2 PHE A 475 20877 13311 10053 -1051 -289 1523 C
ATOM 3046 CZ PHE A 475 -15.024 -5.278 -16.765 1.00113.33 C
ANISOU 3046 CZ PHE A 475 20249 13077 9734 -1422 -161 1451 C
ATOM 3047 N ASN A 476 -17.585 -9.632 -19.057 1.00 88.56 N
ANISOU 3047 N ASN A 476 15249 11076 7323 -298 -282 1326 N
ATOM 3048 CA ASN A 476 -16.887 -9.739 -20.337 1.00 88.28 C
ANISOU 3048 CA ASN A 476 15276 11131 7137 -586 -242 1393 C
ATOM 3049 C ASN A 476 -17.251 -10.962 -21.172 1.00 89.84 C
ANISOU 3049 C ASN A 476 15021 11648 7465 -447 -246 1352 C
ATOM 3050 O ASN A 476 -16.839 -11.012 -22.335 1.00 90.81 O
ANISOU 3050 O ASN A 476 15222 11835 7446 -620 -233 1408 O
ATOM 3051 CB ASN A 476 -15.377 -9.754 -20.117 1.00 86.95 C
ANISOU 3051 CB ASN A 476 15054 11083 6899 -1116 -93 1387 C
ATOM 3052 CG ASN A 476 -14.779 -8.423 -19.756 1.00117.03 C
ANISOU 3052 CG ASN A 476 19420 14577 10471 -1415 -77 1450 C
ATOM 3053 OD1 ASN A 476 -14.128 -8.281 -18.719 1.00114.39 O
ANISOU 3053 OD1 ASN A 476 19029 14265 10167 -1635 1 1399 O
ATOM 3054 ND2 ASN A 476 -14.931 -7.428 -20.624 1.00114.16 N
ANISOU 3054 ND2 ASN A 476 19622 13914 9839 -1464 -148 1563 N
ATOM 3055 N GLN A 477 -17.982 -11.946 -20.613 1.00 83.34 N
ANISOU 3055 N GLN A 477 13750 11023 6890 -172 -256 1254 N
ATOM 3056 CA GLN A 477 -18.302 -13.198 -21.326 1.00 81.49 C
ANISOU 3056 CA GLN A 477 13094 11087 6780 -78 -249 1199 C
ATOM 3057 C GLN A 477 -19.118 -13.016 -22.628 1.00 86.06 C
ANISOU 3057 C GLN A 477 13828 11648 7224 125 -365 1252 C
ATOM 3058 O GLN A 477 -18.902 -13.793 -23.556 1.00 84.98 O
ANISOU 3058 O GLN A 477 13485 11717 7087 28 -334 1238 O
ATOM 3059 CB GLN A 477 -19.024 -14.195 -20.416 1.00 80.56 C
ANISOU 3059 CB GLN A 477 12550 11141 6916 159 -246 1088 C
ATOM 3060 CG GLN A 477 -18.575 -15.640 -20.618 1.00 91.30 C
ANISOU 3060 CG GLN A 477 13464 12798 8427 35 -151 1011 C
ATOM 3061 CD GLN A 477 -19.571 -16.625 -20.047 1.00109.51 C
ANISOU 3061 CD GLN A 477 15423 15254 10932 279 -172 915 C
ATOM 3062 OE1 GLN A 477 -19.512 -17.013 -18.871 1.00101.76 O
ANISOU 3062 OE1 GLN A 477 14266 14303 10097 287 -120 859 O
ATOM 3063 NE2 GLN A 477 -20.535 -17.022 -20.862 1.00106.26 N
ANISOU 3063 NE2 GLN A 477 14914 14950 10510 465 -250 892 N
ATOM 3064 N ALA A 478 -20.018 -12.004 -22.702 1.00 84.16 N
ANISOU 3064 N ALA A 478 13953 11173 6852 420 -500 1307 N
ATOM 3065 CA ALA A 478 -20.867 -11.710 -23.872 1.00 85.54 C
ANISOU 3065 CA ALA A 478 14307 11327 6866 674 -633 1360 C
ATOM 3066 C ALA A 478 -20.059 -11.460 -25.154 1.00 90.82 C
ANISOU 3066 C ALA A 478 15214 11965 7331 378 -604 1457 C
ATOM 3067 O ALA A 478 -20.456 -11.946 -26.223 1.00 90.14 O
ANISOU 3067 O ALA A 478 14994 12050 7204 466 -650 1458 O
ATOM 3068 CB ALA A 478 -21.760 -10.511 -23.595 1.00 88.76 C
ANISOU 3068 CB ALA A 478 15155 11448 7120 1034 -776 1409 C
ATOM 3069 N GLU A 479 -18.934 -10.709 -25.053 1.00 88.84 N
ANISOU 3069 N GLU A 479 15305 11518 6934 4 -523 1533 N
ATOM 3070 CA GLU A 479 -18.087 -10.411 -26.212 1.00 90.37 C
ANISOU 3070 CA GLU A 479 15739 11698 6899 -340 -479 1625 C
ATOM 3071 C GLU A 479 -17.256 -11.638 -26.599 1.00 93.15 C
ANISOU 3071 C GLU A 479 15593 12429 7372 -614 -345 1548 C
ATOM 3072 O GLU A 479 -17.138 -11.948 -27.793 1.00 93.66 O
ANISOU 3072 O GLU A 479 15619 12634 7333 -684 -347 1574 O
ATOM 3073 CB GLU A 479 -17.193 -9.176 -25.995 1.00 93.83 C
ANISOU 3073 CB GLU A 479 16725 11825 7102 -694 -433 1723 C
ATOM 3074 CG GLU A 479 -17.745 -7.905 -26.627 1.00106.08 C
ANISOU 3074 CG GLU A 479 18960 12986 8358 -537 -570 1859 C
ATOM 3075 CD GLU A 479 -18.386 -8.035 -28.002 1.00138.43 C
ANISOU 3075 CD GLU A 479 23127 17145 12323 -326 -675 1921 C
ATOM 3076 OE1 GLU A 479 -19.598 -7.740 -28.104 1.00140.21 O
ANISOU 3076 OE1 GLU A 479 23491 17261 12523 170 -836 1932 O
ATOM 3077 OE2 GLU A 479 -17.697 -8.444 -28.968 1.00134.39 O
ANISOU 3077 OE2 GLU A 479 22513 16826 11724 -637 -600 1947 O
ATOM 3078 N TRP A 480 -16.724 -12.359 -25.588 1.00 86.46 N
ANISOU 3078 N TRP A 480 14369 11748 6733 -730 -236 1449 N
ATOM 3079 CA TRP A 480 -15.956 -13.593 -25.765 1.00 83.66 C
ANISOU 3079 CA TRP A 480 13537 11749 6501 -915 -114 1356 C
ATOM 3080 C TRP A 480 -16.796 -14.650 -26.520 1.00 85.29 C
ANISOU 3080 C TRP A 480 13432 12154 6820 -652 -168 1296 C
ATOM 3081 O TRP A 480 -16.239 -15.434 -27.293 1.00 82.84 O
ANISOU 3081 O TRP A 480 12895 12085 6495 -798 -100 1254 O
ATOM 3082 CB TRP A 480 -15.514 -14.136 -24.382 1.00 80.03 C
ANISOU 3082 CB TRP A 480 12766 11388 6253 -954 -26 1262 C
ATOM 3083 CG TRP A 480 -14.468 -13.317 -23.680 1.00 81.53 C
ANISOU 3083 CG TRP A 480 13164 11486 6328 -1291 55 1293 C
ATOM 3084 CD1 TRP A 480 -13.507 -12.537 -24.256 1.00 86.49 C
ANISOU 3084 CD1 TRP A 480 14086 12083 6693 -1680 111 1365 C
ATOM 3085 CD2 TRP A 480 -14.227 -13.272 -22.270 1.00 80.29 C
ANISOU 3085 CD2 TRP A 480 12907 11299 6300 -1309 100 1240 C
ATOM 3086 NE1 TRP A 480 -12.706 -11.982 -23.289 1.00 86.14 N
ANISOU 3086 NE1 TRP A 480 14136 11993 6599 -1952 185 1356 N
ATOM 3087 CE2 TRP A 480 -13.120 -12.423 -22.060 1.00 85.33 C
ANISOU 3087 CE2 TRP A 480 13790 11891 6740 -1717 177 1279 C
ATOM 3088 CE3 TRP A 480 -14.825 -13.894 -21.157 1.00 79.25 C
ANISOU 3088 CE3 TRP A 480 12498 11196 6419 -1044 87 1160 C
ATOM 3089 CZ2 TRP A 480 -12.617 -12.159 -20.786 1.00 84.02 C
ANISOU 3089 CZ2 TRP A 480 13598 11705 6623 -1848 233 1238 C
ATOM 3090 CZ3 TRP A 480 -14.330 -13.622 -19.895 1.00 79.65 C
ANISOU 3090 CZ3 TRP A 480 12532 11210 6520 -1157 142 1128 C
ATOM 3091 CH2 TRP A 480 -13.241 -12.763 -19.718 1.00 81.94 C
ANISOU 3091 CH2 TRP A 480 13063 11455 6615 -1546 211 1165 C
ATOM 3092 N GLU A 481 -18.136 -14.652 -26.276 1.00 82.51 N
ANISOU 3092 N GLU A 481 13069 11721 6561 -268 -291 1279 N
ATOM 3093 CA GLU A 481 -19.119 -15.549 -26.888 1.00 82.18 C
ANISOU 3093 CA GLU A 481 12752 11867 6605 -16 -359 1213 C
ATOM 3094 C GLU A 481 -19.442 -15.103 -28.287 1.00 89.15 C
ANISOU 3094 C GLU A 481 13881 12727 7266 31 -449 1294 C
ATOM 3095 O GLU A 481 -19.736 -15.946 -29.142 1.00 88.50 O
ANISOU 3095 O GLU A 481 13566 12861 7199 71 -459 1241 O
ATOM 3096 CB GLU A 481 -20.400 -15.633 -26.052 1.00 83.18 C
ANISOU 3096 CB GLU A 481 12755 11976 6875 343 -451 1155 C
ATOM 3097 CG GLU A 481 -20.253 -16.545 -24.845 1.00 94.38 C
ANISOU 3097 CG GLU A 481 13808 13512 8541 312 -359 1047 C
ATOM 3098 CD GLU A 481 -21.532 -17.233 -24.418 1.00121.67 C
ANISOU 3098 CD GLU A 481 16982 17107 12142 596 -423 952 C
ATOM 3099 OE1 GLU A 481 -21.799 -18.356 -24.908 1.00110.11 O
ANISOU 3099 OE1 GLU A 481 15228 15859 10748 588 -405 872 O
ATOM 3100 OE2 GLU A 481 -22.270 -16.645 -23.594 1.00124.97 O
ANISOU 3100 OE2 GLU A 481 17474 17427 12582 814 -488 949 O
ATOM 3101 N ARG A 482 -19.393 -13.775 -28.529 1.00 88.71 N
ANISOU 3101 N ARG A 482 14325 12396 6986 22 -515 1422 N
ATOM 3102 CA ARG A 482 -19.622 -13.210 -29.864 1.00 90.89 C
ANISOU 3102 CA ARG A 482 14914 12611 7008 55 -604 1522 C
ATOM 3103 C ARG A 482 -18.381 -13.480 -30.726 1.00 94.07 C
ANISOU 3103 C ARG A 482 15299 13149 7294 -366 -480 1547 C
ATOM 3104 O ARG A 482 -18.527 -13.767 -31.902 1.00 93.60 O
ANISOU 3104 O ARG A 482 15212 13226 7126 -360 -512 1560 O
ATOM 3105 CB ARG A 482 -19.975 -11.702 -29.811 1.00 93.63 C
ANISOU 3105 CB ARG A 482 15869 12582 7126 196 -719 1655 C
ATOM 3106 CG ARG A 482 -21.482 -11.423 -29.707 1.00100.58 C
ANISOU 3106 CG ARG A 482 16796 13418 8003 731 -899 1640 C
ATOM 3107 CD ARG A 482 -21.797 -10.014 -29.226 1.00111.05 C
ANISOU 3107 CD ARG A 482 18693 14349 9152 931 -1000 1736 C
ATOM 3108 NE ARG A 482 -22.697 -10.020 -28.066 1.00119.47 N
ANISOU 3108 NE ARG A 482 19590 15423 10381 1299 -1061 1645 N
ATOM 3109 CZ ARG A 482 -22.859 -9.005 -27.216 1.00132.28 C
ANISOU 3109 CZ ARG A 482 21596 16730 11933 1453 -1109 1679 C
ATOM 3110 NH1 ARG A 482 -22.179 -7.876 -27.382 1.00118.44 N
ANISOU 3110 NH1 ARG A 482 20462 14595 9944 1251 -1105 1807 N
ATOM 3111 NH2 ARG A 482 -23.696 -9.114 -26.192 1.00115.56 N
ANISOU 3111 NH2 ARG A 482 19263 14680 9964 1791 -1157 1579 N
ATOM 3112 N SER A 483 -17.172 -13.454 -30.120 1.00 90.65 N
ANISOU 3112 N SER A 483 14830 12731 6881 -722 -337 1534 N
ATOM 3113 CA SER A 483 -15.897 -13.724 -30.798 1.00 91.13 C
ANISOU 3113 CA SER A 483 14816 12992 6819 -1135 -203 1533 C
ATOM 3114 C SER A 483 -15.795 -15.200 -31.203 1.00 93.86 C
ANISOU 3114 C SER A 483 14639 13697 7326 -1095 -141 1400 C
ATOM 3115 O SER A 483 -15.226 -15.521 -32.255 1.00 94.73 O
ANISOU 3115 O SER A 483 14692 14001 7300 -1282 -86 1396 O
ATOM 3116 CB SER A 483 -14.718 -13.344 -29.905 1.00 93.78 C
ANISOU 3116 CB SER A 483 15190 13310 7132 -1488 -75 1529 C
ATOM 3117 OG SER A 483 -14.580 -11.938 -29.781 1.00103.66 O
ANISOU 3117 OG SER A 483 17001 14230 8156 -1647 -109 1658 O
ATOM 3118 N PHE A 484 -16.360 -16.082 -30.364 1.00 87.77 N
ANISOU 3118 N PHE A 484 13521 13003 6827 -855 -148 1290 N
ATOM 3119 CA PHE A 484 -16.417 -17.521 -30.558 1.00 85.88 C
ANISOU 3119 CA PHE A 484 12840 13037 6752 -780 -100 1155 C
ATOM 3120 C PHE A 484 -17.372 -17.838 -31.705 1.00 89.34 C
ANISOU 3120 C PHE A 484 13269 13544 7130 -588 -204 1152 C
ATOM 3121 O PHE A 484 -16.988 -18.601 -32.580 1.00 89.41 O
ANISOU 3121 O PHE A 484 13106 13767 7097 -684 -152 1093 O
ATOM 3122 CB PHE A 484 -16.833 -18.203 -29.252 1.00 86.22 C
ANISOU 3122 CB PHE A 484 12607 13084 7066 -605 -86 1059 C
ATOM 3123 CG PHE A 484 -17.255 -19.645 -29.367 1.00 87.32 C
ANISOU 3123 CG PHE A 484 12380 13426 7373 -470 -70 926 C
ATOM 3124 CD1 PHE A 484 -16.314 -20.648 -29.564 1.00 90.85 C
ANISOU 3124 CD1 PHE A 484 12588 14084 7848 -611 46 835 C
ATOM 3125 CD2 PHE A 484 -18.593 -20.006 -29.244 1.00 89.64 C
ANISOU 3125 CD2 PHE A 484 12576 13707 7775 -204 -171 883 C
ATOM 3126 CE1 PHE A 484 -16.708 -21.988 -29.646 1.00 90.89 C
ANISOU 3126 CE1 PHE A 484 12323 14223 7987 -488 59 711 C
ATOM 3127 CE2 PHE A 484 -18.985 -21.344 -29.329 1.00 91.42 C
ANISOU 3127 CE2 PHE A 484 12504 14101 8131 -134 -150 757 C
ATOM 3128 CZ PHE A 484 -18.042 -22.325 -29.531 1.00 89.03 C
ANISOU 3128 CZ PHE A 484 12027 13944 7856 -277 -36 676 C
ATOM 3129 N ARG A 485 -18.575 -17.213 -31.748 1.00 85.98 N
ANISOU 3129 N ARG A 485 13036 12962 6671 -314 -352 1209 N
ATOM 3130 CA ARG A 485 -19.518 -17.383 -32.864 1.00 86.57 C
ANISOU 3130 CA ARG A 485 13114 13131 6648 -121 -467 1210 C
ATOM 3131 C ARG A 485 -18.829 -16.941 -34.175 1.00 92.37 C
ANISOU 3131 C ARG A 485 14089 13888 7118 -341 -449 1300 C
ATOM 3132 O ARG A 485 -18.724 -17.757 -35.085 1.00 92.26 O
ANISOU 3132 O ARG A 485 13880 14097 7078 -398 -422 1235 O
ATOM 3133 CB ARG A 485 -20.849 -16.622 -32.609 1.00 87.73 C
ANISOU 3133 CB ARG A 485 13440 13134 6761 242 -636 1258 C
ATOM 3134 CG ARG A 485 -21.286 -15.626 -33.701 1.00100.24 C
ANISOU 3134 CG ARG A 485 15438 14591 8058 360 -768 1391 C
ATOM 3135 CD ARG A 485 -22.538 -14.850 -33.346 1.00111.76 C
ANISOU 3135 CD ARG A 485 17067 15930 9467 778 -939 1423 C
ATOM 3136 NE ARG A 485 -23.677 -15.276 -34.159 1.00120.81 N
ANISOU 3136 NE ARG A 485 18028 17318 10556 1048 -1064 1368 N
ATOM 3137 CZ ARG A 485 -24.471 -16.304 -33.870 1.00132.37 C
ANISOU 3137 CZ ARG A 485 19045 19055 12197 1183 -1077 1219 C
ATOM 3138 NH1 ARG A 485 -24.264 -17.026 -32.774 1.00112.34 N
ANISOU 3138 NH1 ARG A 485 16221 16555 9910 1093 -974 1121 N
ATOM 3139 NH2 ARG A 485 -25.473 -16.623 -34.677 1.00122.08 N
ANISOU 3139 NH2 ARG A 485 17587 17996 10800 1390 -1192 1167 N
ATOM 3140 N ASP A 486 -18.273 -15.695 -34.220 1.00 90.94 N
ANISOU 3140 N ASP A 486 14340 13478 6735 -505 -449 1442 N
ATOM 3141 CA ASP A 486 -17.582 -15.076 -35.366 1.00 93.08 C
ANISOU 3141 CA ASP A 486 14924 13730 6712 -768 -427 1552 C
ATOM 3142 C ASP A 486 -16.412 -15.926 -35.883 1.00 98.69 C
ANISOU 3142 C ASP A 486 15350 14739 7408 -1095 -267 1471 C
ATOM 3143 O ASP A 486 -16.109 -15.851 -37.077 1.00 99.99 O
ANISOU 3143 O ASP A 486 15625 15009 7357 -1246 -257 1515 O
ATOM 3144 CB ASP A 486 -17.072 -13.662 -35.014 1.00 96.38 C
ANISOU 3144 CB ASP A 486 15855 13829 6936 -957 -423 1698 C
ATOM 3145 CG ASP A 486 -18.125 -12.628 -34.633 1.00105.59 C
ANISOU 3145 CG ASP A 486 17427 14656 8037 -624 -588 1795 C
ATOM 3146 OD1 ASP A 486 -19.334 -12.983 -34.595 1.00104.99 O
ANISOU 3146 OD1 ASP A 486 17187 14633 8070 -213 -713 1744 O
ATOM 3147 OD2 ASP A 486 -17.738 -11.483 -34.298 1.00112.11 O
ANISOU 3147 OD2 ASP A 486 18725 15177 8694 -772 -589 1909 O
ATOM 3148 N TYR A 487 -15.754 -16.726 -34.994 1.00 94.28 N
ANISOU 3148 N TYR A 487 14437 14329 7057 -1186 -145 1351 N
ATOM 3149 CA TYR A 487 -14.651 -17.618 -35.381 1.00 93.70 C
ANISOU 3149 CA TYR A 487 14062 14572 6969 -1423 1 1249 C
ATOM 3150 C TYR A 487 -15.216 -18.925 -35.942 1.00 94.85 C
ANISOU 3150 C TYR A 487 13873 14925 7241 -1215 -20 1118 C
ATOM 3151 O TYR A 487 -14.806 -19.343 -37.038 1.00 94.51 O
ANISOU 3151 O TYR A 487 13764 15089 7056 -1328 21 1085 O
ATOM 3152 CB TYR A 487 -13.675 -17.892 -34.214 1.00 93.78 C
ANISOU 3152 CB TYR A 487 13861 14667 7104 -1580 131 1176 C
ATOM 3153 CG TYR A 487 -12.756 -19.081 -34.440 1.00 94.82 C
ANISOU 3153 CG TYR A 487 13599 15157 7271 -1671 259 1029 C
ATOM 3154 CD1 TYR A 487 -11.720 -19.021 -35.369 1.00 98.22 C
ANISOU 3154 CD1 TYR A 487 14021 15839 7458 -1958 354 1025 C
ATOM 3155 CD2 TYR A 487 -12.919 -20.262 -33.719 1.00 93.59 C
ANISOU 3155 CD2 TYR A 487 13100 15092 7368 -1459 284 890 C
ATOM 3156 CE1 TYR A 487 -10.877 -20.111 -35.582 1.00 98.78 C
ANISOU 3156 CE1 TYR A 487 13730 16263 7539 -1988 466 874 C
ATOM 3157 CE2 TYR A 487 -12.088 -21.362 -33.931 1.00 94.38 C
ANISOU 3157 CE2 TYR A 487 12887 15495 7477 -1487 390 750 C
ATOM 3158 CZ TYR A 487 -11.074 -21.286 -34.872 1.00105.05 C
ANISOU 3158 CZ TYR A 487 14215 17112 8586 -1728 478 737 C
ATOM 3159 OH TYR A 487 -10.246 -22.368 -35.076 1.00107.45 O
ANISOU 3159 OH TYR A 487 14210 17737 8879 -1706 578 585 O
ATOM 3160 N VAL A 488 -16.142 -19.565 -35.177 1.00 88.87 N
ANISOU 3160 N VAL A 488 12920 14116 6732 -935 -79 1038 N
ATOM 3161 CA VAL A 488 -16.813 -20.809 -35.563 1.00 88.62 C
ANISOU 3161 CA VAL A 488 12606 14244 6821 -756 -105 907 C
ATOM 3162 C VAL A 488 -17.386 -20.618 -36.962 1.00 97.10 C
ANISOU 3162 C VAL A 488 13815 15378 7699 -714 -198 951 C
ATOM 3163 O VAL A 488 -17.014 -21.351 -37.879 1.00 97.69 O
ANISOU 3163 O VAL A 488 13755 15660 7701 -796 -147 873 O
ATOM 3164 CB VAL A 488 -17.921 -21.266 -34.554 1.00 91.13 C
ANISOU 3164 CB VAL A 488 12770 14474 7380 -497 -175 843 C
ATOM 3165 CG1 VAL A 488 -18.778 -22.383 -35.136 1.00 90.81 C
ANISOU 3165 CG1 VAL A 488 12517 14588 7399 -358 -223 723 C
ATOM 3166 CG2 VAL A 488 -17.339 -21.700 -33.214 1.00 88.94 C
ANISOU 3166 CG2 VAL A 488 12320 14172 7300 -533 -75 778 C
ATOM 3167 N LEU A 489 -18.225 -19.581 -37.130 1.00 96.66 N
ANISOU 3167 N LEU A 489 14049 15143 7534 -577 -333 1077 N
ATOM 3168 CA LEU A 489 -18.884 -19.277 -38.391 1.00 99.48 C
ANISOU 3168 CA LEU A 489 14565 15545 7687 -487 -447 1134 C
ATOM 3169 C LEU A 489 -17.879 -18.958 -39.510 1.00105.55 C
ANISOU 3169 C LEU A 489 15505 16400 8198 -769 -377 1201 C
ATOM 3170 O LEU A 489 -18.105 -19.426 -40.621 1.00105.98 O
ANISOU 3170 O LEU A 489 15500 16627 8140 -752 -408 1165 O
ATOM 3171 CB LEU A 489 -19.937 -18.162 -38.237 1.00101.33 C
ANISOU 3171 CB LEU A 489 15104 15563 7834 -227 -615 1257 C
ATOM 3172 CG LEU A 489 -21.121 -18.416 -37.246 1.00105.19 C
ANISOU 3172 CG LEU A 489 15406 16029 8530 90 -706 1184 C
ATOM 3173 CD1 LEU A 489 -22.257 -17.470 -37.515 1.00107.67 C
ANISOU 3173 CD1 LEU A 489 15972 16249 8688 409 -894 1275 C
ATOM 3174 CD2 LEU A 489 -21.661 -19.864 -37.294 1.00105.66 C
ANISOU 3174 CD2 LEU A 489 15026 16351 8769 146 -685 1002 C
ATOM 3175 N CYS A 490 -16.757 -18.256 -39.227 1.00103.76 N
ANISOU 3175 N CYS A 490 15461 16094 7869 -1051 -274 1281 N
ATOM 3176 CA CYS A 490 -15.738 -17.977 -40.256 1.00106.39 C
ANISOU 3176 CA CYS A 490 15929 16559 7935 -1373 -187 1333 C
ATOM 3177 C CYS A 490 -15.058 -19.283 -40.722 1.00111.09 C
ANISOU 3177 C CYS A 490 16124 17501 8585 -1468 -63 1162 C
ATOM 3178 O CYS A 490 -14.872 -19.477 -41.928 1.00112.15 O
ANISOU 3178 O CYS A 490 16263 17814 8534 -1556 -53 1152 O
ATOM 3179 CB CYS A 490 -14.705 -16.965 -39.767 1.00108.05 C
ANISOU 3179 CB CYS A 490 16405 16640 8008 -1692 -98 1439 C
ATOM 3180 SG CYS A 490 -13.162 -16.949 -40.724 1.00113.98 S
ANISOU 3180 SG CYS A 490 17148 17693 8466 -2172 72 1438 S
ATOM 3181 N GLN A 491 -14.697 -20.170 -39.762 1.00106.55 N
ANISOU 3181 N GLN A 491 15222 17012 8251 -1425 24 1026 N
ATOM 3182 CA GLN A 491 -14.044 -21.460 -40.013 1.00105.16 C
ANISOU 3182 CA GLN A 491 14693 17129 8136 -1453 137 850 C
ATOM 3183 C GLN A 491 -15.035 -22.421 -40.692 1.00108.43 C
ANISOU 3183 C GLN A 491 14963 17616 8621 -1228 59 746 C
ATOM 3184 O GLN A 491 -15.510 -23.374 -40.072 1.00107.01 O
ANISOU 3184 O GLN A 491 14563 17433 8665 -1051 55 621 O
ATOM 3185 CB GLN A 491 -13.494 -22.037 -38.689 1.00104.19 C
ANISOU 3185 CB GLN A 491 14330 17025 8233 -1424 228 753 C
ATOM 3186 CG GLN A 491 -12.049 -21.651 -38.389 1.00108.03 C
ANISOU 3186 CG GLN A 491 14788 17673 8585 -1714 368 762 C
ATOM 3187 CD GLN A 491 -11.043 -22.127 -39.421 1.00112.58 C
ANISOU 3187 CD GLN A 491 15216 18610 8950 -1887 478 676 C
ATOM 3188 OE1 GLN A 491 -11.076 -23.260 -39.909 1.00101.54 O
ANISOU 3188 OE1 GLN A 491 13594 17383 7603 -1734 501 530 O
ATOM 3189 NE2 GLN A 491 -10.108 -21.267 -39.766 1.00105.84 N
ANISOU 3189 NE2 GLN A 491 14494 17886 7835 -2223 554 756 N
ATOM 3190 N ALA A 492 -15.373 -22.121 -41.961 1.00106.13 N
ANISOU 3190 N ALA A 492 14829 17377 8118 -1253 -11 806 N
ATOM 3191 CA ALA A 492 -16.331 -22.830 -42.812 1.00131.06 C
ANISOU 3191 CA ALA A 492 17898 20632 11268 -1089 -97 725 C
ATOM 3192 C ALA A 492 -16.637 -21.997 -44.049 1.00161.80 C
ANISOU 3192 C ALA A 492 22066 24528 14882 -1136 -189 858 C
ATOM 3193 O ALA A 492 -16.404 -22.443 -45.171 1.00127.20 O
ANISOU 3193 O ALA A 492 17624 20343 10364 -1170 -186 795 O
ATOM 3194 CB ALA A 492 -17.617 -23.113 -42.045 1.00130.26 C
ANISOU 3194 CB ALA A 492 17701 20400 11392 -825 -208 679 C
ATOM 3195 N ASP A 506 -6.545 -16.409 -44.052 1.00128.77 N
ANISOU 3195 N ASP A 506 18702 21377 8848 -4380 868 1315 N
ATOM 3196 CA ASP A 506 -6.478 -16.402 -42.590 1.00126.59 C
ANISOU 3196 CA ASP A 506 18309 20963 8824 -4286 874 1277 C
ATOM 3197 C ASP A 506 -7.898 -16.321 -41.977 1.00125.57 C
ANISOU 3197 C ASP A 506 18381 20326 9003 -3846 693 1354 C
ATOM 3198 O ASP A 506 -8.836 -15.901 -42.668 1.00126.53 O
ANISOU 3198 O ASP A 506 18843 20170 9063 -3707 563 1478 O
ATOM 3199 CB ASP A 506 -5.597 -15.234 -42.110 1.00131.68 C
ANISOU 3199 CB ASP A 506 19219 21596 9218 -4803 964 1375 C
ATOM 3200 CG ASP A 506 -5.092 -15.360 -40.680 1.00145.50 C
ANISOU 3200 CG ASP A 506 20720 23408 11155 -4813 1026 1285 C
ATOM 3201 OD1 ASP A 506 -3.860 -15.502 -40.497 1.00148.19 O
ANISOU 3201 OD1 ASP A 506 20758 24213 11333 -5132 1180 1175 O
ATOM 3202 OD2 ASP A 506 -5.922 -15.270 -39.743 1.00149.58 O
ANISOU 3202 OD2 ASP A 506 21343 23533 11956 -4510 918 1324 O
ATOM 3203 N CYS A 507 -8.049 -16.755 -40.696 1.00115.94 N
ANISOU 3203 N CYS A 507 16929 19026 8096 -3616 686 1270 N
ATOM 3204 CA CYS A 507 -9.313 -16.788 -39.938 1.00112.41 C
ANISOU 3204 CA CYS A 507 16579 18178 7953 -3206 537 1307 C
ATOM 3205 C CYS A 507 -8.983 -16.962 -38.437 1.00112.27 C
ANISOU 3205 C CYS A 507 16352 18142 8165 -3162 586 1233 C
ATOM 3206 O CYS A 507 -8.746 -18.081 -37.968 1.00109.30 O
ANISOU 3206 O CYS A 507 15543 17999 7988 -2981 642 1070 O
ATOM 3207 CB CYS A 507 -10.236 -17.893 -40.463 1.00110.74 C
ANISOU 3207 CB CYS A 507 16136 18008 7931 -2799 453 1212 C
ATOM 3208 SG CYS A 507 -11.835 -18.018 -39.608 1.00112.03 S
ANISOU 3208 SG CYS A 507 16359 17776 8431 -2320 276 1235 S
ATOM 3209 N GLU A 508 -8.939 -15.837 -37.701 1.00108.38 N
ANISOU 3209 N GLU A 508 16199 17365 7617 -3336 567 1353 N
ATOM 3210 CA GLU A 508 -8.520 -15.803 -36.302 1.00106.82 C
ANISOU 3210 CA GLU A 508 15858 17150 7579 -3369 619 1300 C
ATOM 3211 C GLU A 508 -9.603 -15.284 -35.325 1.00108.57 C
ANISOU 3211 C GLU A 508 16331 16906 8013 -3088 488 1380 C
ATOM 3212 O GLU A 508 -10.642 -14.775 -35.759 1.00109.20 O
ANISOU 3212 O GLU A 508 16745 16672 8073 -2890 352 1491 O
ATOM 3213 CB GLU A 508 -7.237 -14.956 -36.167 1.00111.08 C
ANISOU 3213 CB GLU A 508 16525 17858 7823 -3914 750 1335 C
ATOM 3214 CG GLU A 508 -7.362 -13.513 -36.638 1.00125.08 C
ANISOU 3214 CG GLU A 508 18927 19299 9297 -4229 707 1531 C
ATOM 3215 CD GLU A 508 -6.552 -12.508 -35.845 1.00149.23 C
ANISOU 3215 CD GLU A 508 22229 22290 12182 -4674 785 1580 C
ATOM 3216 OE1 GLU A 508 -5.646 -11.883 -36.442 1.00142.33 O
ANISOU 3216 OE1 GLU A 508 21541 21589 10949 -5190 885 1628 O
ATOM 3217 OE2 GLU A 508 -6.823 -12.338 -34.632 1.00144.09 O
ANISOU 3217 OE2 GLU A 508 21590 21424 11736 -4532 750 1568 O
ATOM 3218 N ILE A 509 -9.324 -15.419 -34.001 1.00101.87 N
ANISOU 3218 N ILE A 509 15305 16051 7349 -3060 529 1316 N
ATOM 3219 CA ILE A 509 -10.191 -15.034 -32.874 1.00 99.51 C
ANISOU 3219 CA ILE A 509 15162 15384 7264 -2807 431 1357 C
ATOM 3220 C ILE A 509 -9.792 -13.650 -32.355 1.00106.57 C
ANISOU 3220 C ILE A 509 16500 16025 7966 -3131 444 1473 C
ATOM 3221 O ILE A 509 -8.613 -13.438 -32.068 1.00108.69 O
ANISOU 3221 O ILE A 509 16687 16518 8092 -3522 571 1438 O
ATOM 3222 CB ILE A 509 -10.118 -16.099 -31.737 1.00 98.85 C
ANISOU 3222 CB ILE A 509 14614 15454 7490 -2581 472 1209 C
ATOM 3223 CG1 ILE A 509 -10.566 -17.488 -32.231 1.00 96.45 C
ANISOU 3223 CG1 ILE A 509 13942 15344 7361 -2269 455 1092 C
ATOM 3224 CG2 ILE A 509 -10.952 -15.664 -30.529 1.00 98.98 C
ANISOU 3224 CG2 ILE A 509 14780 15123 7704 -2358 385 1248 C
ATOM 3225 CD1 ILE A 509 -9.977 -18.694 -31.525 1.00 96.11 C
ANISOU 3225 CD1 ILE A 509 13438 15581 7498 -2163 544 931 C
ATOM 3226 N LYS A 510 -10.773 -12.725 -32.204 1.00102.88 N
ANISOU 3226 N LYS A 510 16501 15108 7482 -2959 310 1599 N
ATOM 3227 CA LYS A 510 -10.534 -11.358 -31.721 1.00104.54 C
ANISOU 3227 CA LYS A 510 17234 14989 7496 -3226 303 1715 C
ATOM 3228 C LYS A 510 -10.051 -11.375 -30.263 1.00108.16 C
ANISOU 3228 C LYS A 510 17508 15475 8111 -3304 371 1634 C
ATOM 3229 O LYS A 510 -8.873 -11.107 -30.015 1.00110.02 O
ANISOU 3229 O LYS A 510 17695 15919 8187 -3750 500 1604 O
ATOM 3230 CB LYS A 510 -11.784 -10.475 -31.880 1.00107.19 C
ANISOU 3230 CB LYS A 510 18100 14839 7788 -2908 127 1848 C
ATOM 3231 CG LYS A 510 -11.734 -9.593 -33.119 1.00127.14 C
ANISOU 3231 CG LYS A 510 21150 17201 9956 -3113 88 1998 C
ATOM 3232 CD LYS A 510 -12.676 -10.061 -34.235 1.00132.06 C
ANISOU 3232 CD LYS A 510 21736 17839 10602 -2727 -36 2025 C
ATOM 3233 CE LYS A 510 -12.645 -9.122 -35.416 1.00137.20 C
ANISOU 3233 CE LYS A 510 22953 18302 10874 -2924 -82 2188 C
ATOM 3234 NZ LYS A 510 -13.903 -9.188 -36.203 1.00145.94 N
ANISOU 3234 NZ LYS A 510 24198 19273 11980 -2446 -259 2246 N
ATOM 3235 N ASN A 511 -10.946 -11.725 -29.315 1.00100.87 N
ANISOU 3235 N ASN A 511 16450 14390 7485 -2882 288 1589 N
ATOM 3236 CA ASN A 511 -10.666 -11.807 -27.884 1.00 97.81 C
ANISOU 3236 CA ASN A 511 15884 14007 7271 -2883 334 1514 C
ATOM 3237 C ASN A 511 -11.155 -13.137 -27.337 1.00 97.33 C
ANISOU 3237 C ASN A 511 15285 14142 7553 -2497 325 1387 C
ATOM 3238 O ASN A 511 -12.026 -13.762 -27.943 1.00 96.97 O
ANISOU 3238 O ASN A 511 15119 14103 7621 -2175 248 1374 O
ATOM 3239 CB ASN A 511 -11.312 -10.639 -27.128 1.00 96.38 C
ANISOU 3239 CB ASN A 511 16207 13354 7060 -2790 239 1604 C
ATOM 3240 CG ASN A 511 -12.759 -10.338 -27.458 1.00106.78 C
ANISOU 3240 CG ASN A 511 17797 14343 8430 -2323 68 1676 C
ATOM 3241 OD1 ASN A 511 -13.102 -9.211 -27.822 1.00100.17 O
ANISOU 3241 OD1 ASN A 511 17541 13150 7370 -2338 -15 1800 O
ATOM 3242 ND2 ASN A 511 -13.656 -11.296 -27.263 1.00 95.71 N
ANISOU 3242 ND2 ASN A 511 16009 13052 7305 -1894 8 1595 N
ATOM 3243 N ARG A 512 -10.607 -13.573 -26.194 1.00 90.15 N
ANISOU 3243 N ARG A 512 14072 13389 6791 -2540 402 1292 N
ATOM 3244 CA ARG A 512 -10.985 -14.842 -25.560 1.00 85.49 C
ANISOU 3244 CA ARG A 512 13016 12961 6505 -2206 402 1175 C
ATOM 3245 C ARG A 512 -10.839 -14.710 -24.018 1.00 86.61 C
ANISOU 3245 C ARG A 512 13085 13035 6789 -2186 425 1133 C
ATOM 3246 O ARG A 512 -10.260 -13.711 -23.585 1.00 89.14 O
ANISOU 3246 O ARG A 512 13671 13251 6948 -2482 458 1179 O
ATOM 3247 CB ARG A 512 -10.117 -15.985 -26.147 1.00 82.35 C
ANISOU 3247 CB ARG A 512 12191 13002 6097 -2286 504 1070 C
ATOM 3248 CG ARG A 512 -8.852 -16.278 -25.366 1.00 85.96 C
ANISOU 3248 CG ARG A 512 12362 13773 6527 -2509 627 978 C
ATOM 3249 CD ARG A 512 -7.594 -16.088 -26.149 1.00 83.28 C
ANISOU 3249 CD ARG A 512 11966 13777 5899 -2907 736 960 C
ATOM 3250 NE ARG A 512 -6.896 -17.361 -26.275 1.00 77.38 N
ANISOU 3250 NE ARG A 512 10736 13464 5203 -2801 815 819 N
ATOM 3251 CZ ARG A 512 -5.628 -17.569 -25.941 1.00 83.63 C
ANISOU 3251 CZ ARG A 512 11243 14668 5863 -3017 927 725 C
ATOM 3252 NH1 ARG A 512 -4.886 -16.572 -25.464 1.00 53.33 N
ANISOU 3252 NH1 ARG A 512 7542 10889 1832 -3414 983 755 N
ATOM 3253 NH2 ARG A 512 -5.079 -18.760 -26.118 1.00 73.94 N
ANISOU 3253 NH2 ARG A 512 9607 13818 4671 -2839 982 592 N
ATOM 3254 N PRO A 513 -11.284 -15.660 -23.154 1.00 78.75 N
ANISOU 3254 N PRO A 513 11759 12097 6064 -1885 415 1047 N
ATOM 3255 CA PRO A 513 -11.078 -15.458 -21.701 1.00 77.41 C
ANISOU 3255 CA PRO A 513 11543 11871 5999 -1895 440 1014 C
ATOM 3256 C PRO A 513 -9.586 -15.408 -21.294 1.00 80.61 C
ANISOU 3256 C PRO A 513 11786 12573 6268 -2257 565 961 C
ATOM 3257 O PRO A 513 -8.708 -15.837 -22.056 1.00 79.11 O
ANISOU 3257 O PRO A 513 11407 12707 5944 -2441 642 920 O
ATOM 3258 CB PRO A 513 -11.810 -16.650 -21.060 1.00 76.03 C
ANISOU 3258 CB PRO A 513 11030 11747 6111 -1524 414 931 C
ATOM 3259 CG PRO A 513 -12.764 -17.120 -22.119 1.00 80.21 C
ANISOU 3259 CG PRO A 513 11558 12237 6682 -1300 340 944 C
ATOM 3260 CD PRO A 513 -12.039 -16.904 -23.408 1.00 77.60 C
ANISOU 3260 CD PRO A 513 11315 12045 6123 -1548 379 978 C
ATOM 3261 N SER A 514 -9.313 -14.840 -20.089 1.00 77.52 N
ANISOU 3261 N SER A 514 11468 12094 5890 -2360 582 954 N
ATOM 3262 CA SER A 514 -7.970 -14.711 -19.518 1.00 77.75 C
ANISOU 3262 CA SER A 514 11336 12422 5783 -2702 691 894 C
ATOM 3263 C SER A 514 -7.664 -15.863 -18.603 1.00 79.16 C
ANISOU 3263 C SER A 514 11055 12870 6152 -2491 731 782 C
ATOM 3264 O SER A 514 -8.330 -16.048 -17.576 1.00 77.97 O
ANISOU 3264 O SER A 514 10876 12540 6208 -2238 684 772 O
ATOM 3265 CB SER A 514 -7.797 -13.404 -18.751 1.00 81.87 C
ANISOU 3265 CB SER A 514 12229 12702 6176 -2971 688 943 C
ATOM 3266 OG SER A 514 -6.539 -13.399 -18.092 1.00 88.52 O
ANISOU 3266 OG SER A 514 12848 13890 6896 -3292 791 865 O
ATOM 3267 N LEU A 515 -6.619 -16.610 -18.960 1.00 74.58 N
ANISOU 3267 N LEU A 515 10128 12732 5476 -2593 817 697 N
ATOM 3268 CA LEU A 515 -6.154 -17.735 -18.173 1.00 72.28 C
ANISOU 3268 CA LEU A 515 9419 12733 5312 -2385 857 587 C
ATOM 3269 C LEU A 515 -5.421 -17.229 -16.951 1.00 74.15 C
ANISOU 3269 C LEU A 515 9599 13092 5483 -2585 900 552 C
ATOM 3270 O LEU A 515 -5.402 -17.935 -15.945 1.00 72.89 O
ANISOU 3270 O LEU A 515 9203 13019 5475 -2355 900 492 O
ATOM 3271 CB LEU A 515 -5.275 -18.689 -18.993 1.00 73.03 C
ANISOU 3271 CB LEU A 515 9176 13274 5297 -2368 925 495 C
ATOM 3272 CG LEU A 515 -5.987 -19.516 -20.073 1.00 76.23 C
ANISOU 3272 CG LEU A 515 9561 13601 5800 -2101 886 496 C
ATOM 3273 CD1 LEU A 515 -5.035 -20.528 -20.694 1.00 77.02 C
ANISOU 3273 CD1 LEU A 515 9314 14162 5788 -2040 958 380 C
ATOM 3274 CD2 LEU A 515 -7.255 -20.221 -19.534 1.00 74.86 C
ANISOU 3274 CD2 LEU A 515 9411 13105 5927 -1700 803 508 C
ATOM 3275 N LEU A 516 -4.859 -15.999 -17.011 1.00 70.13 N
ANISOU 3275 N LEU A 516 9337 12570 4738 -3022 934 593 N
ATOM 3276 CA LEU A 516 -4.196 -15.394 -15.859 1.00 70.22 C
ANISOU 3276 CA LEU A 516 9339 12682 4660 -3268 973 557 C
ATOM 3277 C LEU A 516 -5.250 -15.143 -14.767 1.00 72.16 C
ANISOU 3277 C LEU A 516 9781 12498 5138 -3018 894 599 C
ATOM 3278 O LEU A 516 -5.085 -15.614 -13.631 1.00 69.78 O
ANISOU 3278 O LEU A 516 9247 12314 4950 -2876 902 537 O
ATOM 3279 CB LEU A 516 -3.472 -14.102 -16.258 1.00 73.38 C
ANISOU 3279 CB LEU A 516 10034 13114 4732 -3835 1027 594 C
ATOM 3280 CG LEU A 516 -2.799 -13.311 -15.136 1.00 79.60 C
ANISOU 3280 CG LEU A 516 10883 13978 5383 -4175 1068 556 C
ATOM 3281 CD1 LEU A 516 -1.566 -14.026 -14.596 1.00 80.26 C
ANISOU 3281 CD1 LEU A 516 10429 14695 5372 -4247 1151 417 C
ATOM 3282 CD2 LEU A 516 -2.474 -11.910 -15.587 1.00 84.40 C
ANISOU 3282 CD2 LEU A 516 11960 14424 5685 -4722 1099 623 C
ATOM 3283 N VAL A 517 -6.378 -14.493 -15.156 1.00 68.21 N
ANISOU 3283 N VAL A 517 9687 11525 4703 -2918 812 700 N
ATOM 3284 CA VAL A 517 -7.523 -14.211 -14.284 1.00 66.05 C
ANISOU 3284 CA VAL A 517 9618 10849 4630 -2643 728 738 C
ATOM 3285 C VAL A 517 -8.052 -15.539 -13.690 1.00 69.09 C
ANISOU 3285 C VAL A 517 9636 11322 5295 -2215 707 680 C
ATOM 3286 O VAL A 517 -8.213 -15.603 -12.461 1.00 69.32 O
ANISOU 3286 O VAL A 517 9596 11305 5438 -2109 701 649 O
ATOM 3287 CB VAL A 517 -8.621 -13.381 -15.003 1.00 69.05 C
ANISOU 3287 CB VAL A 517 10458 10783 4993 -2552 636 843 C
ATOM 3288 CG1 VAL A 517 -9.942 -13.392 -14.234 1.00 66.42 C
ANISOU 3288 CG1 VAL A 517 10223 10126 4887 -2154 544 858 C
ATOM 3289 CG2 VAL A 517 -8.146 -11.944 -15.232 1.00 71.58 C
ANISOU 3289 CG2 VAL A 517 11250 10920 5027 -2977 650 906 C
ATOM 3290 N GLU A 518 -8.230 -16.613 -14.518 1.00 63.11 N
ANISOU 3290 N GLU A 518 8654 10703 4621 -2003 705 661 N
ATOM 3291 CA GLU A 518 -8.694 -17.907 -13.980 1.00 59.92 C
ANISOU 3291 CA GLU A 518 7956 10362 4448 -1638 692 606 C
ATOM 3292 C GLU A 518 -7.657 -18.547 -13.009 1.00 65.37 C
ANISOU 3292 C GLU A 518 8321 11389 5127 -1652 758 520 C
ATOM 3293 O GLU A 518 -8.079 -19.073 -11.978 1.00 64.66 O
ANISOU 3293 O GLU A 518 8131 11232 5204 -1427 739 498 O
ATOM 3294 CB GLU A 518 -9.101 -18.904 -15.072 1.00 59.80 C
ANISOU 3294 CB GLU A 518 7819 10407 4497 -1439 677 594 C
ATOM 3295 CG GLU A 518 -10.097 -18.385 -16.104 1.00 65.23 C
ANISOU 3295 CG GLU A 518 8780 10825 5179 -1396 605 671 C
ATOM 3296 CD GLU A 518 -11.470 -17.864 -15.715 1.00 85.88 C
ANISOU 3296 CD GLU A 518 11627 13082 7923 -1198 511 725 C
ATOM 3297 OE1 GLU A 518 -12.264 -17.594 -16.646 1.00 78.60 O
ANISOU 3297 OE1 GLU A 518 10878 12005 6980 -1113 446 775 O
ATOM 3298 OE2 GLU A 518 -11.756 -17.702 -14.506 1.00 88.63 O
ANISOU 3298 OE2 GLU A 518 11978 13327 8370 -1119 501 713 O
ATOM 3299 N LYS A 519 -6.325 -18.445 -13.295 1.00 62.47 N
ANISOU 3299 N LYS A 519 7795 11400 4541 -1918 833 469 N
ATOM 3300 CA LYS A 519 -5.239 -18.944 -12.434 1.00 61.97 C
ANISOU 3300 CA LYS A 519 7408 11727 4411 -1935 891 377 C
ATOM 3301 C LYS A 519 -5.145 -18.127 -11.144 1.00 68.42 C
ANISOU 3301 C LYS A 519 8324 12454 5218 -2087 888 383 C
ATOM 3302 O LYS A 519 -4.796 -18.675 -10.091 1.00 67.44 O
ANISOU 3302 O LYS A 519 7976 12502 5147 -1949 899 326 O
ATOM 3303 CB LYS A 519 -3.891 -18.880 -13.161 1.00 65.98 C
ANISOU 3303 CB LYS A 519 7719 12710 4642 -2214 970 313 C
ATOM 3304 CG LYS A 519 -3.626 -20.050 -14.092 1.00 67.50 C
ANISOU 3304 CG LYS A 519 7662 13157 4826 -1983 989 253 C
ATOM 3305 CD LYS A 519 -2.275 -19.958 -14.710 1.00 66.33 C
ANISOU 3305 CD LYS A 519 7283 13537 4382 -2250 1071 173 C
ATOM 3306 CE LYS A 519 -2.291 -20.456 -16.112 1.00 84.65 C
ANISOU 3306 CE LYS A 519 9575 15945 6645 -2190 1084 163 C
ATOM 3307 NZ LYS A 519 -1.082 -20.020 -16.852 1.00104.16 N
ANISOU 3307 NZ LYS A 519 11887 18904 8786 -2557 1170 101 N
ATOM 3308 N ILE A 520 -5.422 -16.803 -11.232 1.00 67.03 N
ANISOU 3308 N ILE A 520 8513 12004 4953 -2369 872 449 N
ATOM 3309 CA ILE A 520 -5.428 -15.907 -10.074 1.00 67.63 C
ANISOU 3309 CA ILE A 520 8763 11928 5006 -2528 865 453 C
ATOM 3310 C ILE A 520 -6.584 -16.345 -9.178 1.00 70.00 C
ANISOU 3310 C ILE A 520 9086 11930 5581 -2138 800 472 C
ATOM 3311 O ILE A 520 -6.408 -16.508 -7.965 1.00 69.76 O
ANISOU 3311 O ILE A 520 8930 11972 5605 -2081 807 431 O
ATOM 3312 CB ILE A 520 -5.521 -14.416 -10.512 1.00 72.94 C
ANISOU 3312 CB ILE A 520 9900 12319 5496 -2895 857 522 C
ATOM 3313 CG1 ILE A 520 -4.146 -13.920 -11.013 1.00 75.38 C
ANISOU 3313 CG1 ILE A 520 10151 13008 5483 -3391 945 481 C
ATOM 3314 CG2 ILE A 520 -6.028 -13.532 -9.351 1.00 75.41 C
ANISOU 3314 CG2 ILE A 520 10504 12297 5852 -2918 818 539 C
ATOM 3315 CD1 ILE A 520 -4.126 -12.556 -11.609 1.00 80.63 C
ANISOU 3315 CD1 ILE A 520 11300 13414 5923 -3799 948 551 C
ATOM 3316 N ASN A 521 -7.752 -16.585 -9.813 1.00 65.16 N
ANISOU 3316 N ASN A 521 8608 11028 5123 -1880 739 529 N
ATOM 3317 CA ASN A 521 -8.994 -17.089 -9.229 1.00 63.05 C
ANISOU 3317 CA ASN A 521 8345 10512 5098 -1518 679 544 C
ATOM 3318 C ASN A 521 -8.759 -18.446 -8.542 1.00 64.16 C
ANISOU 3318 C ASN A 521 8128 10884 5365 -1285 705 484 C
ATOM 3319 O ASN A 521 -9.119 -18.609 -7.372 1.00 61.89 O
ANISOU 3319 O ASN A 521 7802 10524 5191 -1150 693 470 O
ATOM 3320 CB ASN A 521 -10.043 -17.227 -10.347 1.00 64.91 C
ANISOU 3320 CB ASN A 521 8719 10535 5410 -1343 621 597 C
ATOM 3321 CG ASN A 521 -11.477 -17.456 -9.927 1.00 80.27 C
ANISOU 3321 CG ASN A 521 10724 12223 7553 -1026 551 613 C
ATOM 3322 OD1 ASN A 521 -12.402 -17.206 -10.707 1.00 82.51 O
ANISOU 3322 OD1 ASN A 521 11175 12317 7857 -912 490 655 O
ATOM 3323 ND2 ASN A 521 -11.705 -17.995 -8.742 1.00 58.92 N
ANISOU 3323 ND2 ASN A 521 7863 9542 4980 -875 559 576 N
ATOM 3324 N LEU A 522 -8.166 -19.416 -9.289 1.00 60.46 N
ANISOU 3324 N LEU A 522 7430 10681 4862 -1224 738 447 N
ATOM 3325 CA LEU A 522 -7.843 -20.759 -8.808 1.00 59.07 C
ANISOU 3325 CA LEU A 522 6968 10714 4762 -980 759 390 C
ATOM 3326 C LEU A 522 -6.915 -20.675 -7.595 1.00 64.35 C
ANISOU 3326 C LEU A 522 7473 11624 5351 -1051 794 340 C
ATOM 3327 O LEU A 522 -7.186 -21.325 -6.587 1.00 61.65 O
ANISOU 3327 O LEU A 522 7042 11258 5126 -833 782 327 O
ATOM 3328 CB LEU A 522 -7.231 -21.647 -9.922 1.00 59.06 C
ANISOU 3328 CB LEU A 522 6794 10964 4681 -914 789 347 C
ATOM 3329 CG LEU A 522 -8.220 -22.263 -10.933 1.00 62.61 C
ANISOU 3329 CG LEU A 522 7332 11208 5249 -734 752 374 C
ATOM 3330 CD1 LEU A 522 -7.508 -22.678 -12.229 1.00 64.42 C
ANISOU 3330 CD1 LEU A 522 7454 11682 5340 -774 786 335 C
ATOM 3331 CD2 LEU A 522 -9.007 -23.445 -10.346 1.00 60.72 C
ANISOU 3331 CD2 LEU A 522 7044 10831 5197 -423 727 361 C
ATOM 3332 N PHE A 523 -5.860 -19.834 -7.675 1.00 65.25 N
ANISOU 3332 N PHE A 523 7566 11975 5252 -1379 835 314 N
ATOM 3333 CA PHE A 523 -4.923 -19.614 -6.578 1.00 67.32 C
ANISOU 3333 CA PHE A 523 7665 12518 5397 -1505 867 256 C
ATOM 3334 C PHE A 523 -5.699 -19.210 -5.305 1.00 69.02 C
ANISOU 3334 C PHE A 523 8030 12444 5752 -1439 832 285 C
ATOM 3335 O PHE A 523 -5.478 -19.825 -4.274 1.00 67.15 O
ANISOU 3335 O PHE A 523 7615 12346 5554 -1279 833 250 O
ATOM 3336 CB PHE A 523 -3.845 -18.568 -6.966 1.00 72.72 C
ANISOU 3336 CB PHE A 523 8360 13466 5805 -1957 919 224 C
ATOM 3337 CG PHE A 523 -3.391 -17.647 -5.855 1.00 76.95 C
ANISOU 3337 CG PHE A 523 8947 14061 6230 -2228 935 198 C
ATOM 3338 CD1 PHE A 523 -2.383 -18.032 -4.979 1.00 82.58 C
ANISOU 3338 CD1 PHE A 523 9339 15208 6830 -2230 964 110 C
ATOM 3339 CD2 PHE A 523 -3.991 -16.406 -5.668 1.00 80.22 C
ANISOU 3339 CD2 PHE A 523 9748 14093 6640 -2457 914 253 C
ATOM 3340 CE1 PHE A 523 -1.999 -17.199 -3.923 1.00 85.03 C
ANISOU 3340 CE1 PHE A 523 9695 15578 7034 -2490 976 78 C
ATOM 3341 CE2 PHE A 523 -3.608 -15.576 -4.616 1.00 84.68 C
ANISOU 3341 CE2 PHE A 523 10392 14684 7099 -2707 927 220 C
ATOM 3342 CZ PHE A 523 -2.610 -15.975 -3.754 1.00 84.17 C
ANISOU 3342 CZ PHE A 523 9987 15065 6929 -2743 961 131 C
ATOM 3343 N ALA A 524 -6.623 -18.224 -5.391 1.00 66.01 N
ANISOU 3343 N ALA A 524 7979 11669 5432 -1530 796 347 N
ATOM 3344 CA ALA A 524 -7.402 -17.754 -4.246 1.00 65.64 C
ANISOU 3344 CA ALA A 524 8091 11352 5498 -1459 763 365 C
ATOM 3345 C ALA A 524 -8.313 -18.850 -3.690 1.00 72.80 C
ANISOU 3345 C ALA A 524 8887 12146 6627 -1081 733 374 C
ATOM 3346 O ALA A 524 -8.338 -19.029 -2.477 1.00 73.99 O
ANISOU 3346 O ALA A 524 8960 12327 6826 -997 735 353 O
ATOM 3347 CB ALA A 524 -8.216 -16.529 -4.618 1.00 66.49 C
ANISOU 3347 CB ALA A 524 8590 11079 5594 -1577 723 420 C
ATOM 3348 N MET A 525 -9.016 -19.610 -4.562 1.00 70.08 N
ANISOU 3348 N MET A 525 8538 11695 6397 -880 711 403 N
ATOM 3349 CA MET A 525 -9.920 -20.717 -4.192 1.00 68.26 C
ANISOU 3349 CA MET A 525 8228 11357 6349 -574 690 410 C
ATOM 3350 C MET A 525 -9.140 -21.909 -3.588 1.00 73.09 C
ANISOU 3350 C MET A 525 8592 12231 6949 -429 721 368 C
ATOM 3351 O MET A 525 -9.646 -22.546 -2.671 1.00 73.82 O
ANISOU 3351 O MET A 525 8655 12248 7147 -252 714 372 O
ATOM 3352 CB MET A 525 -10.744 -21.142 -5.416 1.00 69.76 C
ANISOU 3352 CB MET A 525 8483 11410 6612 -466 663 437 C
ATOM 3353 CG MET A 525 -11.590 -22.387 -5.242 1.00 72.03 C
ANISOU 3353 CG MET A 525 8694 11625 7049 -213 651 434 C
ATOM 3354 SD MET A 525 -11.123 -23.617 -6.490 1.00 77.17 S
ANISOU 3354 SD MET A 525 9229 12428 7666 -119 671 408 S
ATOM 3355 CE MET A 525 -11.525 -22.753 -7.982 1.00 74.56 C
ANISOU 3355 CE MET A 525 9050 11991 7289 -253 640 441 C
ATOM 3356 N PHE A 526 -7.921 -22.189 -4.068 1.00 70.10 N
ANISOU 3356 N PHE A 526 8047 12170 6420 -493 755 326 N
ATOM 3357 CA PHE A 526 -7.101 -23.259 -3.509 1.00 70.22 C
ANISOU 3357 CA PHE A 526 7838 12460 6381 -308 773 278 C
ATOM 3358 C PHE A 526 -6.410 -22.742 -2.257 1.00 76.53 C
ANISOU 3358 C PHE A 526 8545 13444 7089 -413 785 249 C
ATOM 3359 O PHE A 526 -6.361 -23.454 -1.251 1.00 77.22 O
ANISOU 3359 O PHE A 526 8545 13589 7207 -214 778 240 O
ATOM 3360 CB PHE A 526 -6.088 -23.819 -4.534 1.00 72.93 C
ANISOU 3360 CB PHE A 526 8012 13121 6578 -280 800 226 C
ATOM 3361 CG PHE A 526 -6.674 -24.801 -5.528 1.00 73.05 C
ANISOU 3361 CG PHE A 526 8083 12993 6681 -78 787 236 C
ATOM 3362 CD1 PHE A 526 -7.322 -25.954 -5.097 1.00 74.75 C
ANISOU 3362 CD1 PHE A 526 8344 13037 7020 204 768 247 C
ATOM 3363 CD2 PHE A 526 -6.584 -24.571 -6.890 1.00 74.95 C
ANISOU 3363 CD2 PHE A 526 8350 13265 6862 -194 797 232 C
ATOM 3364 CE1 PHE A 526 -7.893 -26.842 -6.012 1.00 74.74 C
ANISOU 3364 CE1 PHE A 526 8424 12890 7083 350 759 247 C
ATOM 3365 CE2 PHE A 526 -7.135 -25.473 -7.803 1.00 77.30 C
ANISOU 3365 CE2 PHE A 526 8703 13435 7231 -19 785 233 C
ATOM 3366 CZ PHE A 526 -7.791 -26.599 -7.356 1.00 74.18 C
ANISOU 3366 CZ PHE A 526 8360 12864 6960 245 766 236 C
ATOM 3367 N GLY A 527 -5.959 -21.487 -2.315 1.00 74.05 N
ANISOU 3367 N GLY A 527 8287 13195 6655 -737 801 238 N
ATOM 3368 CA GLY A 527 -5.294 -20.774 -1.226 1.00 74.94 C
ANISOU 3368 CA GLY A 527 8341 13480 6651 -922 815 201 C
ATOM 3369 C GLY A 527 -6.136 -20.616 0.022 1.00 78.57 C
ANISOU 3369 C GLY A 527 8921 13682 7250 -826 789 229 C
ATOM 3370 O GLY A 527 -5.584 -20.603 1.120 1.00 79.83 O
ANISOU 3370 O GLY A 527 8964 14030 7339 -842 795 192 O
ATOM 3371 N THR A 528 -7.484 -20.530 -0.120 1.00 72.85 N
ANISOU 3371 N THR A 528 8407 12564 6708 -715 760 286 N
ATOM 3372 CA THR A 528 -8.376 -20.437 1.038 1.00 70.91 C
ANISOU 3372 CA THR A 528 8254 12101 6587 -604 740 304 C
ATOM 3373 C THR A 528 -8.227 -21.723 1.852 1.00 74.02 C
ANISOU 3373 C THR A 528 8470 12626 7027 -347 743 300 C
ATOM 3374 O THR A 528 -8.110 -21.643 3.068 1.00 73.91 O
ANISOU 3374 O THR A 528 8421 12659 7002 -328 743 287 O
ATOM 3375 CB THR A 528 -9.835 -20.141 0.649 1.00 72.97 C
ANISOU 3375 CB THR A 528 8732 11993 7001 -521 707 349 C
ATOM 3376 OG1 THR A 528 -9.879 -19.079 -0.294 1.00 69.91 O
ANISOU 3376 OG1 THR A 528 8534 11486 6542 -716 696 362 O
ATOM 3377 CG2 THR A 528 -10.691 -19.750 1.848 1.00 70.67 C
ANISOU 3377 CG2 THR A 528 8537 11523 6792 -453 692 349 C
ATOM 3378 N GLY A 529 -8.153 -22.870 1.174 1.00 70.10 N
ANISOU 3378 N GLY A 529 7889 12189 6556 -157 744 308 N
ATOM 3379 CA GLY A 529 -7.963 -24.168 1.816 1.00 70.00 C
ANISOU 3379 CA GLY A 529 7774 12268 6555 107 742 308 C
ATOM 3380 C GLY A 529 -6.563 -24.372 2.377 1.00 75.10 C
ANISOU 3380 C GLY A 529 8207 13308 7018 138 750 256 C
ATOM 3381 O GLY A 529 -6.409 -24.927 3.471 1.00 74.15 O
ANISOU 3381 O GLY A 529 8039 13254 6882 302 740 259 O
ATOM 3382 N ILE A 530 -5.523 -23.933 1.625 1.00 72.66 N
ANISOU 3382 N ILE A 530 7762 13297 6549 -22 767 203 N
ATOM 3383 CA ILE A 530 -4.125 -24.051 2.056 1.00 73.86 C
ANISOU 3383 CA ILE A 530 7658 13921 6485 -14 774 131 C
ATOM 3384 C ILE A 530 -3.950 -23.222 3.336 1.00 77.02 C
ANISOU 3384 C ILE A 530 8042 14388 6836 -187 774 115 C
ATOM 3385 O ILE A 530 -3.540 -23.775 4.353 1.00 77.62 O
ANISOU 3385 O ILE A 530 7997 14644 6850 -6 757 99 O
ATOM 3386 CB ILE A 530 -3.112 -23.647 0.946 1.00 78.59 C
ANISOU 3386 CB ILE A 530 8099 14864 6899 -206 803 67 C
ATOM 3387 CG1 ILE A 530 -3.271 -24.517 -0.320 1.00 78.42 C
ANISOU 3387 CG1 ILE A 530 8092 14787 6918 -12 804 74 C
ATOM 3388 CG2 ILE A 530 -1.667 -23.687 1.477 1.00 81.99 C
ANISOU 3388 CG2 ILE A 530 8216 15863 7073 -218 811 -26 C
ATOM 3389 CD1 ILE A 530 -2.429 -24.046 -1.540 1.00 82.37 C
ANISOU 3389 CD1 ILE A 530 8468 15583 7247 -238 839 19 C
ATOM 3390 N ALA A 531 -4.325 -21.925 3.296 1.00 71.82 N
ANISOU 3390 N ALA A 531 7541 13551 6198 -513 787 122 N
ATOM 3391 CA ALA A 531 -4.246 -21.016 4.434 1.00 71.54 C
ANISOU 3391 CA ALA A 531 7546 13524 6113 -709 788 99 C
ATOM 3392 C ALA A 531 -5.078 -21.534 5.617 1.00 74.17 C
ANISOU 3392 C ALA A 531 7949 13641 6593 -467 764 141 C
ATOM 3393 O ALA A 531 -4.584 -21.497 6.742 1.00 74.53 O
ANISOU 3393 O ALA A 531 7882 13887 6547 -458 759 109 O
ATOM 3394 CB ALA A 531 -4.705 -19.626 4.032 1.00 72.11 C
ANISOU 3394 CB ALA A 531 7871 13332 6193 -1043 799 108 C
ATOM 3395 N MET A 532 -6.303 -22.071 5.352 1.00 68.68 N
ANISOU 3395 N MET A 532 7418 12579 6100 -280 753 209 N
ATOM 3396 CA MET A 532 -7.223 -22.617 6.358 1.00 66.79 C
ANISOU 3396 CA MET A 532 7258 12127 5993 -81 741 252 C
ATOM 3397 C MET A 532 -6.716 -23.874 7.005 1.00 71.15 C
ANISOU 3397 C MET A 532 7678 12866 6490 190 730 261 C
ATOM 3398 O MET A 532 -7.029 -24.100 8.164 1.00 71.40 O
ANISOU 3398 O MET A 532 7738 12845 6546 281 724 281 O
ATOM 3399 CB MET A 532 -8.597 -22.896 5.762 1.00 67.41 C
ANISOU 3399 CB MET A 532 7510 11843 6258 12 737 307 C
ATOM 3400 CG MET A 532 -9.610 -21.892 6.171 1.00 70.62 C
ANISOU 3400 CG MET A 532 8085 11995 6754 -97 733 311 C
ATOM 3401 SD MET A 532 -8.961 -20.208 6.210 1.00 76.79 S
ANISOU 3401 SD MET A 532 8946 12830 7402 -425 736 257 S
ATOM 3402 CE MET A 532 -10.127 -19.502 7.228 1.00 73.02 C
ANISOU 3402 CE MET A 532 8643 12087 7012 -405 726 252 C
ATOM 3403 N SER A 533 -5.947 -24.695 6.272 1.00 67.43 N
ANISOU 3403 N SER A 533 7085 12607 5930 339 725 245 N
ATOM 3404 CA SER A 533 -5.374 -25.924 6.804 1.00 66.98 C
ANISOU 3404 CA SER A 533 6938 12730 5783 652 703 248 C
ATOM 3405 C SER A 533 -4.289 -25.624 7.831 1.00 69.96 C
ANISOU 3405 C SER A 533 7117 13493 5973 634 690 194 C
ATOM 3406 O SER A 533 -4.148 -26.396 8.775 1.00 69.67 O
ANISOU 3406 O SER A 533 7073 13510 5887 872 665 216 O
ATOM 3407 CB SER A 533 -4.813 -26.789 5.678 1.00 71.48 C
ANISOU 3407 CB SER A 533 7440 13436 6281 836 698 226 C
ATOM 3408 OG SER A 533 -3.700 -26.192 5.036 1.00 80.56 O
ANISOU 3408 OG SER A 533 8371 14976 7264 685 709 147 O
ATOM 3409 N THR A 534 -3.551 -24.486 7.670 1.00 66.70 N
ANISOU 3409 N THR A 534 6561 13343 5438 328 706 123 N
ATOM 3410 CA THR A 534 -2.443 -24.069 8.552 1.00 67.54 C
ANISOU 3410 CA THR A 534 6445 13886 5332 233 697 49 C
ATOM 3411 C THR A 534 -2.954 -23.652 9.942 1.00 72.60 C
ANISOU 3411 C THR A 534 7182 14380 6024 175 690 71 C
ATOM 3412 O THR A 534 -2.177 -23.140 10.753 1.00 74.65 O
ANISOU 3412 O THR A 534 7288 14958 6118 39 684 7 O
ATOM 3413 CB THR A 534 -1.541 -22.972 7.936 1.00 66.31 C
ANISOU 3413 CB THR A 534 6142 14046 5009 -148 726 -38 C
ATOM 3414 OG1 THR A 534 -2.161 -21.697 8.048 1.00 64.48 O
ANISOU 3414 OG1 THR A 534 6117 13524 4859 -502 750 -29 O
ATOM 3415 CG2 THR A 534 -1.113 -23.263 6.497 1.00 61.30 C
ANISOU 3415 CG2 THR A 534 5418 13556 4318 -135 742 -62 C
ATOM 3416 N TRP A 535 -4.240 -23.920 10.235 1.00 67.13 N
ANISOU 3416 N TRP A 535 6723 13244 5538 278 692 151 N
ATOM 3417 CA TRP A 535 -4.842 -23.676 11.545 1.00 66.13 C
ANISOU 3417 CA TRP A 535 6692 12970 5465 267 690 175 C
ATOM 3418 C TRP A 535 -4.240 -24.651 12.561 1.00 72.40 C
ANISOU 3418 C TRP A 535 7371 14006 6130 549 656 186 C
ATOM 3419 O TRP A 535 -4.134 -24.352 13.758 1.00 73.50 O
ANISOU 3419 O TRP A 535 7481 14243 6205 512 647 172 O
ATOM 3420 CB TRP A 535 -6.380 -23.843 11.475 1.00 61.86 C
ANISOU 3420 CB TRP A 535 6397 11954 5153 317 705 249 C
ATOM 3421 CG TRP A 535 -7.010 -23.831 12.832 1.00 61.97 C
ANISOU 3421 CG TRP A 535 6489 11852 5203 355 707 273 C
ATOM 3422 CD1 TRP A 535 -7.183 -24.898 13.665 1.00 64.81 C
ANISOU 3422 CD1 TRP A 535 6877 12198 5548 594 696 329 C
ATOM 3423 CD2 TRP A 535 -7.424 -22.673 13.570 1.00 61.53 C
ANISOU 3423 CD2 TRP A 535 6500 11714 5165 143 721 234 C
ATOM 3424 NE1 TRP A 535 -7.728 -24.484 14.855 1.00 64.22 N
ANISOU 3424 NE1 TRP A 535 6860 12049 5492 530 706 330 N
ATOM 3425 CE2 TRP A 535 -7.897 -23.122 14.821 1.00 65.26 C
ANISOU 3425 CE2 TRP A 535 7010 12138 5647 267 721 266 C
ATOM 3426 CE3 TRP A 535 -7.499 -21.301 13.271 1.00 62.45 C
ANISOU 3426 CE3 TRP A 535 6691 11759 5280 -136 733 175 C
ATOM 3427 CZ2 TRP A 535 -8.391 -22.244 15.793 1.00 64.00 C
ANISOU 3427 CZ2 TRP A 535 6918 11901 5497 133 735 230 C
ATOM 3428 CZ3 TRP A 535 -8.032 -20.444 14.213 1.00 63.52 C
ANISOU 3428 CZ3 TRP A 535 6934 11773 5426 -250 741 142 C
ATOM 3429 CH2 TRP A 535 -8.445 -20.910 15.467 1.00 63.89 C
ANISOU 3429 CH2 TRP A 535 6976 11815 5486 -112 743 163 C
ATOM 3430 N VAL A 536 -3.896 -25.833 12.050 1.00 68.16 N
ANISOU 3430 N VAL A 536 6804 13541 5551 850 633 213 N
ATOM 3431 CA VAL A 536 -3.389 -26.986 12.753 1.00 68.76 C
ANISOU 3431 CA VAL A 536 6844 13785 5496 1208 590 239 C
ATOM 3432 C VAL A 536 -1.830 -26.984 12.746 1.00 76.19 C
ANISOU 3432 C VAL A 536 7467 15314 6167 1294 555 144 C
ATOM 3433 O VAL A 536 -1.235 -27.768 13.476 1.00 77.42 O
ANISOU 3433 O VAL A 536 7556 15696 6163 1604 506 148 O
ATOM 3434 CB VAL A 536 -4.059 -28.212 12.068 1.00 71.22 C
ANISOU 3434 CB VAL A 536 7375 13771 5915 1472 588 316 C
ATOM 3435 CG1 VAL A 536 -3.092 -29.120 11.305 1.00 72.49 C
ANISOU 3435 CG1 VAL A 536 7436 14188 5919 1775 554 282 C
ATOM 3436 CG2 VAL A 536 -4.979 -28.972 13.018 1.00 69.97 C
ANISOU 3436 CG2 VAL A 536 7465 13292 5829 1617 586 411 C
ATOM 3437 N TRP A 537 -1.174 -26.049 12.013 1.00 73.34 N
ANISOU 3437 N TRP A 537 6911 15225 5728 1003 579 54 N
ATOM 3438 CA TRP A 537 0.296 -25.947 12.000 1.00 75.74 C
ANISOU 3438 CA TRP A 537 6867 16162 5747 1021 555 -56 C
ATOM 3439 C TRP A 537 0.800 -25.304 13.304 1.00 82.38 C
ANISOU 3439 C TRP A 537 7558 17307 6437 872 538 -109 C
ATOM 3440 O TRP A 537 1.488 -24.283 13.282 1.00 83.12 O
ANISOU 3440 O TRP A 537 7452 17746 6382 520 558 -208 O
ATOM 3441 CB TRP A 537 0.797 -25.162 10.777 1.00 74.43 C
ANISOU 3441 CB TRP A 537 6561 16192 5526 701 598 -134 C
ATOM 3442 CG TRP A 537 0.563 -25.836 9.465 1.00 74.65 C
ANISOU 3442 CG TRP A 537 6667 16057 5641 872 608 -106 C
ATOM 3443 CD1 TRP A 537 -0.337 -26.828 9.194 1.00 76.18 C
ANISOU 3443 CD1 TRP A 537 7116 15814 6014 1169 597 -12 C
ATOM 3444 CD2 TRP A 537 1.154 -25.480 8.217 1.00 75.31 C
ANISOU 3444 CD2 TRP A 537 6598 16384 5632 694 640 -176 C
ATOM 3445 NE1 TRP A 537 -0.342 -27.108 7.849 1.00 75.56 N
ANISOU 3445 NE1 TRP A 537 7053 15688 5970 1200 616 -23 N
ATOM 3446 CE2 TRP A 537 0.585 -26.314 7.228 1.00 78.14 C
ANISOU 3446 CE2 TRP A 537 7123 16436 6130 930 642 -121 C
ATOM 3447 CE3 TRP A 537 2.115 -24.533 7.833 1.00 78.48 C
ANISOU 3447 CE3 TRP A 537 6747 17246 5828 328 673 -283 C
ATOM 3448 CZ2 TRP A 537 0.977 -26.260 5.891 1.00 77.82 C
ANISOU 3448 CZ2 TRP A 537 6986 16549 6031 854 670 -169 C
ATOM 3449 CZ3 TRP A 537 2.487 -24.466 6.501 1.00 80.55 C
ANISOU 3449 CZ3 TRP A 537 6919 17659 6026 228 706 -326 C
ATOM 3450 CH2 TRP A 537 1.934 -25.334 5.552 1.00 79.98 C
ANISOU 3450 CH2 TRP A 537 6999 17289 6100 508 703 -270 C
ATOM 3451 N THR A 538 0.449 -25.931 14.436 1.00 79.71 N
ANISOU 3451 N THR A 538 7332 16837 6118 1126 501 -44 N
ATOM 3452 CA THR A 538 0.768 -25.510 15.797 1.00 80.88 C
ANISOU 3452 CA THR A 538 7382 17209 6139 1051 478 -75 C
ATOM 3453 C THR A 538 1.735 -26.536 16.475 1.00 87.95 C
ANISOU 3453 C THR A 538 8088 18551 6779 1499 400 -92 C
ATOM 3454 O THR A 538 1.883 -27.664 15.986 1.00 88.88 O
ANISOU 3454 O THR A 538 8247 18662 6861 1903 365 -56 O
ATOM 3455 CB THR A 538 -0.552 -25.297 16.578 1.00 85.78 C
ANISOU 3455 CB THR A 538 8311 17296 6987 961 504 17 C
ATOM 3456 OG1 THR A 538 -0.266 -24.779 17.871 1.00 95.06 O
ANISOU 3456 OG1 THR A 538 9401 18676 8042 850 487 -23 O
ATOM 3457 CG2 THR A 538 -1.405 -26.563 16.701 1.00 81.69 C
ANISOU 3457 CG2 THR A 538 8057 16377 6603 1328 489 144 C
ATOM 3458 N LYS A 539 2.409 -26.121 17.578 1.00 85.09 N
ANISOU 3458 N LYS A 539 7526 18586 6218 1434 367 -155 N
ATOM 3459 CA LYS A 539 3.310 -26.970 18.371 1.00 86.92 C
ANISOU 3459 CA LYS A 539 7572 19274 6179 1860 281 -176 C
ATOM 3460 C LYS A 539 2.517 -28.154 18.954 1.00 89.06 C
ANISOU 3460 C LYS A 539 8185 19104 6549 2290 245 -27 C
ATOM 3461 O LYS A 539 3.031 -29.268 19.025 1.00 90.50 O
ANISOU 3461 O LYS A 539 8362 19461 6563 2779 174 -5 O
ATOM 3462 CB LYS A 539 3.971 -26.146 19.491 1.00 90.87 C
ANISOU 3462 CB LYS A 539 7828 20223 6476 1624 262 -269 C
ATOM 3463 CG LYS A 539 5.276 -26.732 20.000 1.00104.24 C
ANISOU 3463 CG LYS A 539 9173 22629 7806 1979 172 -352 C
ATOM 3464 N ALA A 540 1.244 -27.897 19.327 1.00 82.44 N
ANISOU 3464 N ALA A 540 7661 17695 5968 2095 295 70 N
ATOM 3465 CA ALA A 540 0.262 -28.850 19.846 1.00 80.60 C
ANISOU 3465 CA ALA A 540 7795 16971 5859 2351 288 215 C
ATOM 3466 C ALA A 540 0.017 -30.026 18.874 1.00 85.72 C
ANISOU 3466 C ALA A 540 8659 17344 6566 2682 278 285 C
ATOM 3467 O ALA A 540 -0.149 -31.154 19.336 1.00 86.36 O
ANISOU 3467 O ALA A 540 8987 17241 6585 3048 236 380 O
ATOM 3468 CB ALA A 540 -1.049 -28.127 20.116 1.00 78.13 C
ANISOU 3468 CB ALA A 540 7699 16177 5809 1986 363 265 C
ATOM 3469 N THR A 541 -0.005 -29.763 17.536 1.00 81.57 N
ANISOU 3469 N THR A 541 8075 16770 6148 2540 318 240 N
ATOM 3470 CA THR A 541 -0.209 -30.777 16.493 1.00 81.70 C
ANISOU 3470 CA THR A 541 8280 16543 6220 2811 314 285 C
ATOM 3471 C THR A 541 0.900 -31.830 16.543 1.00 90.27 C
ANISOU 3471 C THR A 541 9277 18003 7017 3337 227 255 C
ATOM 3472 O THR A 541 0.615 -33.017 16.365 1.00 90.98 O
ANISOU 3472 O THR A 541 9671 17803 7094 3701 198 333 O
ATOM 3473 CB THR A 541 -0.324 -30.091 15.145 1.00 89.66 C
ANISOU 3473 CB THR A 541 9188 17506 7370 2508 373 225 C
ATOM 3474 OG1 THR A 541 -1.627 -29.518 15.093 1.00 90.05 O
ANISOU 3474 OG1 THR A 541 9461 17061 7693 2182 437 290 O
ATOM 3475 CG2 THR A 541 -0.144 -31.026 13.954 1.00 87.71 C
ANISOU 3475 CG2 THR A 541 9013 17208 7104 2792 360 222 C
ATOM 3476 N LEU A 542 2.141 -31.405 16.847 1.00 89.60 N
ANISOU 3476 N LEU A 542 8797 18568 6680 3382 182 139 N
ATOM 3477 CA LEU A 542 3.293 -32.300 16.991 1.00 93.10 C
ANISOU 3477 CA LEU A 542 9092 19479 6803 3918 87 88 C
ATOM 3478 C LEU A 542 3.041 -33.279 18.153 1.00 96.62 C
ANISOU 3478 C LEU A 542 9849 19709 7153 4313 19 205 C
ATOM 3479 O LEU A 542 3.318 -34.472 18.016 1.00 97.28 O
ANISOU 3479 O LEU A 542 10133 19745 7085 4838 -48 241 O
ATOM 3480 CB LEU A 542 4.586 -31.478 17.203 1.00 95.77 C
ANISOU 3480 CB LEU A 542 8897 20611 6879 3797 61 -73 C
ATOM 3481 CG LEU A 542 5.517 -31.137 15.979 1.00101.99 C
ANISOU 3481 CG LEU A 542 9312 21893 7545 3709 82 -221 C
ATOM 3482 CD1 LEU A 542 4.757 -30.873 14.645 1.00 98.32 C
ANISOU 3482 CD1 LEU A 542 9024 20971 7361 3422 169 -191 C
ATOM 3483 CD2 LEU A 542 6.404 -29.948 16.306 1.00107.25 C
ANISOU 3483 CD2 LEU A 542 9517 23201 8033 3301 98 -364 C
ATOM 3484 N LEU A 543 2.425 -32.777 19.249 1.00 92.23 N
ANISOU 3484 N LEU A 543 9387 18964 6694 4048 43 269 N
ATOM 3485 CA LEU A 543 2.025 -33.541 20.438 1.00 92.87 C
ANISOU 3485 CA LEU A 543 9789 18793 6706 4310 -3 393 C
ATOM 3486 C LEU A 543 0.987 -34.607 20.048 1.00 94.65 C
ANISOU 3486 C LEU A 543 10541 18339 7083 4468 21 533 C
ATOM 3487 O LEU A 543 1.190 -35.784 20.354 1.00 97.24 O
ANISOU 3487 O LEU A 543 11153 18567 7229 4947 -52 604 O
ATOM 3488 CB LEU A 543 1.436 -32.575 21.497 1.00 91.45 C
ANISOU 3488 CB LEU A 543 9572 18536 6639 3884 44 414 C
ATOM 3489 CG LEU A 543 2.054 -32.445 22.902 1.00 98.25 C
ANISOU 3489 CG LEU A 543 10291 19783 7256 4019 -26 403 C
ATOM 3490 CD1 LEU A 543 1.361 -33.358 23.929 1.00 98.44 C
ANISOU 3490 CD1 LEU A 543 10754 19394 7256 4260 -52 565 C
ATOM 3491 CD2 LEU A 543 3.583 -32.507 22.883 1.00104.93 C
ANISOU 3491 CD2 LEU A 543 10734 21374 7762 4341 -121 275 C
ATOM 3492 N ILE A 544 -0.096 -34.192 19.334 1.00 85.92 N
ANISOU 3492 N ILE A 544 9573 16788 6286 4068 118 563 N
ATOM 3493 CA ILE A 544 -1.192 -35.047 18.853 1.00 83.74 C
ANISOU 3493 CA ILE A 544 9759 15886 6174 4094 158 676 C
ATOM 3494 C ILE A 544 -0.643 -36.242 18.065 1.00 91.75 C
ANISOU 3494 C ILE A 544 10958 16872 7031 4578 99 676 C
ATOM 3495 O ILE A 544 -1.014 -37.388 18.329 1.00 91.32 O
ANISOU 3495 O ILE A 544 11356 16439 6903 4857 72 782 O
ATOM 3496 CB ILE A 544 -2.182 -34.221 17.983 1.00 82.42 C
ANISOU 3496 CB ILE A 544 9565 15428 6325 3600 260 660 C
ATOM 3497 CG1 ILE A 544 -2.895 -33.138 18.816 1.00 80.14 C
ANISOU 3497 CG1 ILE A 544 9188 15078 6183 3173 317 667 C
ATOM 3498 CG2 ILE A 544 -3.193 -35.132 17.260 1.00 81.61 C
ANISOU 3498 CG2 ILE A 544 9880 14766 6362 3623 299 747 C
ATOM 3499 CD1 ILE A 544 -3.524 -32.005 18.029 1.00 81.82 C
ANISOU 3499 CD1 ILE A 544 9256 15193 6640 2727 394 609 C
ATOM 3500 N TRP A 545 0.243 -35.960 17.105 1.00 92.18 N
ANISOU 3500 N TRP A 545 10680 17327 7016 4666 82 550 N
ATOM 3501 CA TRP A 545 0.830 -36.969 16.237 1.00 95.47 C
ANISOU 3501 CA TRP A 545 11216 17778 7279 5127 29 518 C
ATOM 3502 C TRP A 545 1.898 -37.787 16.941 1.00105.74 C
ANISOU 3502 C TRP A 545 12532 19424 8221 5732 -90 507 C
ATOM 3503 O TRP A 545 2.148 -38.918 16.521 1.00107.19 O
ANISOU 3503 O TRP A 545 13018 19455 8255 6208 -145 524 O
ATOM 3504 CB TRP A 545 1.369 -36.330 14.970 1.00 93.69 C
ANISOU 3504 CB TRP A 545 10612 17889 7096 4981 61 383 C
ATOM 3505 CG TRP A 545 0.266 -35.853 14.082 1.00 91.54 C
ANISOU 3505 CG TRP A 545 10454 17179 7147 4521 161 411 C
ATOM 3506 CD1 TRP A 545 -0.152 -34.568 13.915 1.00 91.88 C
ANISOU 3506 CD1 TRP A 545 10265 17249 7395 3988 234 381 C
ATOM 3507 CD2 TRP A 545 -0.628 -36.670 13.312 1.00 90.81 C
ANISOU 3507 CD2 TRP A 545 10774 16534 7194 4560 192 481 C
ATOM 3508 NE1 TRP A 545 -1.225 -34.526 13.054 1.00 89.28 N
ANISOU 3508 NE1 TRP A 545 10150 16453 7321 3727 302 425 N
ATOM 3509 CE2 TRP A 545 -1.535 -35.803 12.663 1.00 91.82 C
ANISOU 3509 CE2 TRP A 545 10847 16431 7609 4050 281 482 C
ATOM 3510 CE3 TRP A 545 -0.733 -38.054 13.081 1.00 94.07 C
ANISOU 3510 CE3 TRP A 545 11619 16627 7496 4979 150 534 C
ATOM 3511 CZ2 TRP A 545 -2.525 -36.274 11.789 1.00 89.74 C
ANISOU 3511 CZ2 TRP A 545 10892 15681 7524 3940 328 530 C
ATOM 3512 CZ3 TRP A 545 -1.718 -38.519 12.222 1.00 94.19 C
ANISOU 3512 CZ3 TRP A 545 11969 16129 7690 4834 205 580 C
ATOM 3513 CH2 TRP A 545 -2.613 -37.636 11.603 1.00 91.68 C
ANISOU 3513 CH2 TRP A 545 11540 15636 7658 4313 293 577 C
ATOM 3514 N ARG A 546 2.498 -37.250 18.023 1.00105.94 N
ANISOU 3514 N ARG A 546 12264 19896 8093 5736 -134 476 N
ATOM 3515 CA ARG A 546 3.473 -38.007 18.815 1.00111.41 C
ANISOU 3515 CA ARG A 546 12964 20945 8421 6331 -259 470 C
ATOM 3516 C ARG A 546 2.721 -39.096 19.594 1.00118.96 C
ANISOU 3516 C ARG A 546 14554 21303 9342 6577 -290 647 C
ATOM 3517 O ARG A 546 3.131 -40.259 19.561 1.00122.13 O
ANISOU 3517 O ARG A 546 15276 21626 9503 7161 -379 680 O
ATOM 3518 CB ARG A 546 4.282 -37.100 19.762 1.00113.04 C
ANISOU 3518 CB ARG A 546 12676 21806 8468 6219 -295 384 C
ATOM 3519 N ARG A 547 1.577 -38.717 20.227 1.00113.65 N
ANISOU 3519 N ARG A 547 14088 20191 8902 6117 -210 759 N
ATOM 3520 CA ARG A 547 0.694 -39.608 20.985 1.00114.02 C
ANISOU 3520 CA ARG A 547 14732 19652 8938 6195 -211 932 C
ATOM 3521 C ARG A 547 -0.032 -40.592 20.048 1.00119.79 C
ANISOU 3521 C ARG A 547 15977 19776 9762 6264 -175 1000 C
ATOM 3522 O ARG A 547 -0.347 -41.702 20.480 1.00122.04 O
ANISOU 3522 O ARG A 547 16823 19645 9902 6539 -213 1123 O
ATOM 3523 CB ARG A 547 -0.320 -38.807 21.824 1.00109.04 C
ANISOU 3523 CB ARG A 547 14091 18812 8525 5638 -122 1000 C
ATOM 3524 N THR A 548 -0.284 -40.199 18.774 1.00115.05 N
ANISOU 3524 N THR A 548 15213 19120 9381 6007 -105 921 N
ATOM 3525 CA THR A 548 -0.963 -41.053 17.792 1.00115.04 C
ANISOU 3525 CA THR A 548 15653 18585 9471 6029 -68 964 C
ATOM 3526 C THR A 548 -0.053 -42.228 17.392 1.00124.58 C
ANISOU 3526 C THR A 548 17113 19843 10377 6710 -174 937 C
ATOM 3527 O THR A 548 -0.532 -43.361 17.346 1.00125.95 O
ANISOU 3527 O THR A 548 17898 19485 10473 6907 -186 1032 O
ATOM 3528 CB THR A 548 -1.428 -40.242 16.570 1.00116.75 C
ANISOU 3528 CB THR A 548 15586 18792 9983 5586 26 880 C
ATOM 3529 N TRP A 549 1.251 -41.965 17.133 1.00124.24 N
ANISOU 3529 N TRP A 549 16615 20449 10141 7069 -250 800 N
ATOM 3530 CA TRP A 549 2.232 -42.991 16.753 1.00128.60 C
ANISOU 3530 CA TRP A 549 17323 21168 10370 7784 -361 743 C
ATOM 3531 C TRP A 549 2.558 -43.909 17.931 1.00136.88 C
ANISOU 3531 C TRP A 549 18776 22132 11101 8306 -473 845 C
ATOM 3532 O TRP A 549 2.789 -45.100 17.717 1.00139.55 O
ANISOU 3532 O TRP A 549 19604 22210 11207 8854 -550 873 O
ATOM 3533 CB TRP A 549 3.518 -42.359 16.205 1.00128.49 C
ANISOU 3533 CB TRP A 549 16633 21967 10221 7973 -402 551 C
ATOM 3534 CG TRP A 549 4.394 -43.323 15.454 1.00133.20 C
ANISOU 3534 CG TRP A 549 17339 22735 10534 8652 -491 459 C
ATOM 3535 CD1 TRP A 549 5.456 -44.021 15.947 1.00140.60 C
ANISOU 3535 CD1 TRP A 549 18297 24050 11073 9377 -629 416 C
ATOM 3536 CD2 TRP A 549 4.275 -43.694 14.074 1.00132.85 C
ANISOU 3536 CD2 TRP A 549 17411 22497 10567 8701 -452 391 C
ATOM 3537 NE1 TRP A 549 6.008 -44.804 14.960 1.00142.54 N
ANISOU 3537 NE1 TRP A 549 18668 24350 11139 9893 -679 319 N
ATOM 3538 CE2 TRP A 549 5.302 -44.625 13.801 1.00141.10 C
ANISOU 3538 CE2 TRP A 549 18550 23815 11248 9477 -569 302 C
ATOM 3539 CE3 TRP A 549 3.401 -43.324 13.035 1.00130.69 C
ANISOU 3539 CE3 TRP A 549 17167 21866 10624 8179 -334 390 C
ATOM 3540 CZ2 TRP A 549 5.480 -45.193 12.533 1.00141.72 C
ANISOU 3540 CZ2 TRP A 549 18755 23806 11286 9734 -564 209 C
ATOM 3541 CZ3 TRP A 549 3.579 -43.888 11.779 1.00133.13 C
ANISOU 3541 CZ3 TRP A 549 17595 22092 10895 8414 -332 305 C
ATOM 3542 CH2 TRP A 549 4.609 -44.809 11.536 1.00138.20 C
ANISOU 3542 CH2 TRP A 549 18333 22999 11178 9175 -442 214 C
ATOM 3543 N CYS A 550 2.573 -43.359 19.167 1.00134.30 N
ANISOU 3543 N CYS A 550 18276 22003 10748 8143 -485 899 N
ATOM 3544 CA CYS A 550 2.815 -44.110 20.409 1.00138.07 C
ANISOU 3544 CA CYS A 550 19122 22410 10929 8575 -589 1012 C
ATOM 3545 C CYS A 550 1.716 -45.160 20.586 1.00143.67 C
ANISOU 3545 C CYS A 550 20666 22259 11664 8535 -557 1193 C
ATOM 3546 O CYS A 550 2.008 -46.293 20.975 1.00147.95 O
ANISOU 3546 O CYS A 550 21743 22574 11896 9092 -659 1274 O
ATOM 3547 CB CYS A 550 2.894 -43.176 21.616 1.00137.18 C
ANISOU 3547 CB CYS A 550 18625 22664 10834 8286 -584 1026 C
ATOM 3548 N ARG A 551 0.459 -44.785 20.244 1.00136.28 N
ANISOU 3548 N ARG A 551 19847 20858 11075 7875 -418 1249 N
ATOM 3549 CA ARG A 551 -0.721 -45.650 20.303 1.00135.89 C
ANISOU 3549 CA ARG A 551 20528 20024 11081 7673 -358 1403 C
ATOM 3550 C ARG A 551 -0.817 -46.552 19.053 1.00140.18 C
ANISOU 3550 C ARG A 551 21472 20188 11604 7883 -357 1371 C
ATOM 3551 O ARG A 551 -1.748 -47.353 18.951 1.00140.16 O
ANISOU 3551 O ARG A 551 22105 19530 11621 7711 -307 1480 O
ATOM 3552 CB ARG A 551 -2.004 -44.820 20.480 1.00131.82 C
ANISOU 3552 CB ARG A 551 19889 19278 10918 6883 -212 1453 C
ATOM 3553 CG ARG A 551 -2.200 -44.303 21.899 1.00142.71 C
ANISOU 3553 CG ARG A 551 21152 20799 12272 6684 -207 1531 C
ATOM 3554 CD ARG A 551 -3.627 -44.510 22.364 1.00153.81 C
ANISOU 3554 CD ARG A 551 22978 21644 13817 6167 -97 1667 C
ATOM 3555 NE ARG A 551 -4.212 -43.293 22.930 1.00159.08 N
ANISOU 3555 NE ARG A 551 23201 22519 14724 5624 -9 1647 N
ATOM 3556 CZ ARG A 551 -4.891 -42.387 22.230 1.00168.26 C
ANISOU 3556 CZ ARG A 551 24017 23705 16210 5130 94 1568 C
ATOM 3557 NH1 ARG A 551 -5.066 -42.541 20.922 1.00150.71 N
ANISOU 3557 NH1 ARG A 551 21808 21332 14120 5084 124 1505 N
ATOM 3558 NH2 ARG A 551 -5.395 -41.317 22.832 1.00153.77 N
ANISOU 3558 NH2 ARG A 551 21833 22042 14551 4702 162 1549 N
ATOM 3559 N LEU A 552 0.156 -46.439 18.125 1.00137.20 N
ANISOU 3559 N LEU A 552 20730 20240 11161 8244 -411 1215 N
ATOM 3560 CA LEU A 552 0.231 -47.249 16.906 1.00138.35 C
ANISOU 3560 CA LEU A 552 21190 20120 11258 8513 -421 1155 C
ATOM 3561 C LEU A 552 1.503 -48.133 16.927 1.00147.21 C
ANISOU 3561 C LEU A 552 22476 21497 11961 9407 -578 1096 C
ATOM 3562 O LEU A 552 1.858 -48.724 15.904 1.00149.06 O
ANISOU 3562 O LEU A 552 22865 21666 12104 9751 -606 1006 O
ATOM 3563 CB LEU A 552 0.195 -46.349 15.656 1.00134.84 C
ANISOU 3563 CB LEU A 552 20173 19961 11099 8146 -337 1011 C
ATOM 3564 N THR A 553 2.166 -48.235 18.101 1.00145.31 N
ANISOU 3564 N THR A 553 22207 21554 11451 9799 -683 1140 N
ATOM 3565 CA THR A 553 3.378 -49.038 18.294 1.00179.45 C
ANISOU 3565 CA THR A 553 26547 26073 15564 10359 -852 1084 C
ATOM 3566 C THR A 553 3.023 -50.520 18.377 1.00201.14 C
ANISOU 3566 C THR A 553 29377 27604 19443 8719 -929 1195 C
ATOM 3567 O THR A 553 2.660 -51.128 17.372 1.00170.11 O
ANISOU 3567 O THR A 553 26840 23790 14002 11061 -873 1187 O
ATOM 3568 CB THR A 553 4.159 -48.594 19.549 1.00184.87 C
ANISOU 3568 CB THR A 553 26696 27152 16395 10072 -951 1085 C
ATOM 3569 OG1 THR A 553 3.306 -48.605 20.696 1.00181.73 O
ANISOU 3569 OG1 THR A 553 26755 26484 15810 10085 -916 1270 O
ATOM 3570 CG2 THR A 553 4.829 -47.233 19.382 1.00181.68 C
ANISOU 3570 CG2 THR A 553 25442 27649 15938 10084 -917 922 C
TER 3571 THR A 553
HETATM 3572 C1 NAG B 1 -22.866 -21.504 -46.772 1.00120.76 C
ANISOU 3572 C1 NAG B 1 15060 15707 15117 -403 614 636 C
HETATM 3573 C2 NAG B 1 -22.936 -21.829 -45.282 1.00120.50 C
ANISOU 3573 C2 NAG B 1 15024 15683 15078 -433 623 629 C
HETATM 3574 C3 NAG B 1 -24.333 -22.384 -45.011 1.00120.55 C
ANISOU 3574 C3 NAG B 1 15029 15690 15084 -439 633 575 C
HETATM 3575 C4 NAG B 1 -25.430 -21.425 -45.479 1.00121.96 C
ANISOU 3575 C4 NAG B 1 15205 15864 15269 -433 613 537 C
HETATM 3576 C5 NAG B 1 -25.153 -20.779 -46.841 1.00121.41 C
ANISOU 3576 C5 NAG B 1 15134 15789 15206 -411 601 547 C
HETATM 3577 C6 NAG B 1 -25.948 -19.504 -47.040 1.00120.81 C
ANISOU 3577 C6 NAG B 1 15047 15716 15139 -411 585 519 C
HETATM 3578 C7 NAG B 1 -20.724 -22.612 -44.492 1.00120.34 C
ANISOU 3578 C7 NAG B 1 15003 15674 15048 -450 650 732 C
HETATM 3579 C8 NAG B 1 -19.788 -23.782 -44.488 1.00120.59 C
ANISOU 3579 C8 NAG B 1 15036 15712 15069 -453 690 786 C
HETATM 3580 N2 NAG B 1 -21.935 -22.848 -45.017 1.00120.39 N
ANISOU 3580 N2 NAG B 1 15012 15674 15056 -438 651 676 N
HETATM 3581 O3 NAG B 1 -24.468 -22.599 -43.610 1.00119.12 O
ANISOU 3581 O3 NAG B 1 14840 15519 14902 -460 638 567 O
HETATM 3582 O4 NAG B 1 -26.617 -22.199 -45.602 1.00122.50 O
ANISOU 3582 O4 NAG B 1 15276 15931 15337 -434 624 505 O
HETATM 3583 O5 NAG B 1 -23.768 -20.421 -46.964 1.00121.22 O
ANISOU 3583 O5 NAG B 1 15108 15765 15184 -402 592 595 O
HETATM 3584 O6 NAG B 1 -25.350 -18.609 -47.970 1.00120.55 O
ANISOU 3584 O6 NAG B 1 15001 15684 15118 -391 570 536 O
HETATM 3585 O7 NAG B 1 -20.397 -21.513 -44.047 1.00119.68 O
ANISOU 3585 O7 NAG B 1 14915 15589 14967 -460 619 743 O
HETATM 3586 C1 NAG B 2 -27.937 -22.013 -45.221 1.00121.70 C
ANISOU 3586 C1 NAG B 2 15172 15831 15238 -440 620 474 C
HETATM 3587 C2 NAG B 2 -29.028 -22.891 -45.832 1.00119.09 C
ANISOU 3587 C2 NAG B 2 14845 15496 14907 -437 626 456 C
HETATM 3588 C3 NAG B 2 -30.311 -22.063 -45.808 1.00120.30 C
ANISOU 3588 C3 NAG B 2 14995 15650 15065 -440 616 440 C
HETATM 3589 C4 NAG B 2 -30.640 -21.638 -44.379 1.00122.77 C
ANISOU 3589 C4 NAG B 2 15303 15964 15379 -444 614 436 C
HETATM 3590 C5 NAG B 2 -29.478 -20.847 -43.779 1.00123.78 C
ANISOU 3590 C5 NAG B 2 15432 16093 15504 -448 610 446 C
HETATM 3591 C6 NAG B 2 -29.655 -20.538 -42.310 1.00124.60 C
ANISOU 3591 C6 NAG B 2 15540 16197 15606 -452 608 443 C
HETATM 3592 C7 NAG B 2 -28.178 -24.495 -47.504 1.00113.70 C
ANISOU 3592 C7 NAG B 2 14188 14801 14211 -422 644 476 C
HETATM 3593 C8 NAG B 2 -27.926 -24.735 -48.961 1.00113.04 C
ANISOU 3593 C8 NAG B 2 14124 14706 14120 -407 646 484 C
HETATM 3594 N2 NAG B 2 -28.703 -23.299 -47.190 1.00115.91 N
ANISOU 3594 N2 NAG B 2 14454 15087 14500 -427 628 464 N
HETATM 3595 O3 NAG B 2 -31.376 -22.837 -46.343 1.00120.05 O
ANISOU 3595 O3 NAG B 2 14966 15615 15033 -442 616 432 O
HETATM 3596 O4 NAG B 2 -31.826 -20.851 -44.359 1.00123.23 O
ANISOU 3596 O4 NAG B 2 15363 16021 15440 -443 612 431 O
HETATM 3597 O5 NAG B 2 -28.267 -21.613 -43.889 1.00124.06 O
ANISOU 3597 O5 NAG B 2 15466 16132 15537 -449 617 465 O
HETATM 3598 O6 NAG B 2 -28.561 -19.780 -41.813 1.00125.62 O
ANISOU 3598 O6 NAG B 2 15676 16326 15730 -462 599 455 O
HETATM 3599 O7 NAG B 2 -27.917 -25.341 -46.654 1.00113.10 O
ANISOU 3599 O7 NAG B 2 14109 14730 14134 -429 660 482 O
HETATM 3600 C1 BMA B 3 -33.071 -21.263 -43.697 1.00122.25 C
ANISOU 3600 C1 BMA B 3 15237 15894 15317 -439 613 433 C
HETATM 3601 C2 BMA B 3 -33.963 -20.042 -43.947 1.00121.16 C
ANISOU 3601 C2 BMA B 3 15103 15755 15178 -439 617 439 C
HETATM 3602 C3 BMA B 3 -35.417 -20.278 -43.515 1.00121.56 C
ANISOU 3602 C3 BMA B 3 15155 15802 15231 -433 619 456 C
HETATM 3603 C4 BMA B 3 -35.977 -21.639 -43.970 1.00123.09 C
ANISOU 3603 C4 BMA B 3 15342 15996 15431 -435 611 462 C
HETATM 3604 C5 BMA B 3 -35.005 -22.820 -43.756 1.00124.76 C
ANISOU 3604 C5 BMA B 3 15548 16209 15645 -434 608 446 C
HETATM 3605 C6 BMA B 3 -35.488 -24.065 -44.518 1.00125.99 C
ANISOU 3605 C6 BMA B 3 15704 16363 15803 -440 601 449 C
HETATM 3606 O2 BMA B 3 -33.882 -19.631 -45.322 1.00120.13 O
ANISOU 3606 O2 BMA B 3 14966 15629 15049 -446 617 437 O
HETATM 3607 O3 BMA B 3 -36.249 -19.226 -44.030 1.00120.54 O
ANISOU 3607 O3 BMA B 3 15028 15674 15099 -437 630 472 O
HETATM 3608 O4 BMA B 3 -37.250 -21.891 -43.353 1.00121.86 O
ANISOU 3608 O4 BMA B 3 15185 15837 15281 -424 609 488 O
HETATM 3609 O5 BMA B 3 -33.658 -22.495 -44.164 1.00123.54 O
ANISOU 3609 O5 BMA B 3 15397 16058 15485 -440 612 434 O
HETATM 3610 O6 BMA B 3 -34.462 -25.064 -44.637 1.00126.14 O
ANISOU 3610 O6 BMA B 3 15724 16384 15821 -441 607 436 O
HETATM 3611 C1 MAN B 4 -36.652 -17.970 -43.380 1.00115.70 C
ANISOU 3611 C1 MAN B 4 14427 15056 14479 -430 645 484 C
HETATM 3612 C2 MAN B 4 -37.786 -17.144 -44.009 1.00115.59 C
ANISOU 3612 C2 MAN B 4 14409 15046 14462 -435 665 513 C
HETATM 3613 C3 MAN B 4 -37.249 -16.042 -44.937 1.00115.25 C
ANISOU 3613 C3 MAN B 4 14354 15015 14420 -447 677 499 C
HETATM 3614 C4 MAN B 4 -36.034 -15.282 -44.380 1.00114.86 C
ANISOU 3614 C4 MAN B 4 14314 14959 14366 -442 671 475 C
HETATM 3615 C5 MAN B 4 -34.997 -16.222 -43.739 1.00115.06 C
ANISOU 3615 C5 MAN B 4 14347 14978 14392 -439 647 456 C
HETATM 3616 C6 MAN B 4 -33.938 -15.449 -42.955 1.00115.09 C
ANISOU 3616 C6 MAN B 4 14366 14973 14388 -439 639 445 C
HETATM 3617 O2 MAN B 4 -38.648 -16.607 -42.990 1.00115.70 O
ANISOU 3617 O2 MAN B 4 14444 15050 14469 -419 681 542 O
HETATM 3618 O3 MAN B 4 -38.295 -15.126 -45.288 1.00115.18 O
ANISOU 3618 O3 MAN B 4 14341 15013 14409 -451 706 530 O
HETATM 3619 O4 MAN B 4 -35.444 -14.492 -45.421 1.00113.77 O
ANISOU 3619 O4 MAN B 4 14156 14836 14237 -449 674 464 O
HETATM 3620 O5 MAN B 4 -35.636 -17.127 -42.822 1.00115.04 O
ANISOU 3620 O5 MAN B 4 14354 14967 14387 -429 644 467 O
HETATM 3621 O6 MAN B 4 -33.134 -16.352 -42.180 1.00114.95 O
ANISOU 3621 O6 MAN B 4 14354 14953 14370 -439 623 437 O
HETATM 3622 C4 SNT A 605 -11.712 -22.106 -14.587 1.00 75.79 C
HETATM 3623 C3 SNT A 605 -12.142 -21.633 -15.840 1.00 73.54 C
HETATM 3624 C2 SNT A 605 -11.325 -21.794 -16.961 1.00 72.63 C
HETATM 3625 C1 SNT A 605 -10.080 -22.416 -16.825 1.00 73.39 C
HETATM 3626 N1 SNT A 605 -12.519 -21.990 -13.522 1.00 76.62 N
HETATM 3627 N2 SNT A 605 -14.682 -21.250 -9.674 1.00 78.62 N
HETATM 3628 N3 SNT A 605 -15.046 -20.662 -8.523 1.00 78.25 N
HETATM 3629 N4 SNT A 605 -15.470 -20.471 -5.728 1.00 75.99 N
HETATM 3630 N5 SNT A 605 -13.547 -22.716 -13.374 1.00 77.07 N
HETATM 3631 C5 SNT A 605 -12.401 -21.199 -12.439 1.00 74.27 C
HETATM 3632 C6 SNT A 605 -13.421 -21.458 -11.606 1.00 76.80 C
HETATM 3633 C7 SNT A 605 -13.640 -20.836 -10.423 1.00 77.82 C
HETATM 3634 C8 SNT A 605 -13.986 -20.129 -7.625 1.00 77.81 C
HETATM 3635 C9 SNT A 605 -14.633 -19.464 -6.428 1.00 76.07 C
HETATM 3636 C10 SNT A 605 -15.972 -20.071 -4.395 1.00 72.40 C
HETATM 3637 C11 SNT A 605 -14.950 -19.940 -3.461 1.00 68.66 C
HETATM 3638 C12 SNT A 605 -14.308 -21.082 -2.978 1.00 67.01 C
HETATM 3639 C13 SNT A 605 -13.280 -20.922 -2.043 1.00 67.50 C
HETATM 3640 C14 SNT A 605 -12.907 -19.651 -1.582 1.00 67.22 C
HETATM 3641 C15 SNT A 605 -9.654 -22.900 -15.580 1.00 74.68 C
HETATM 3642 C16 SNT A 605 -10.477 -22.771 -14.461 1.00 74.94 C
HETATM 3643 C17 SNT A 605 -14.134 -22.416 -12.225 1.00 75.96 C
HETATM 3644 C18 SNT A 605 -15.391 -23.151 -11.784 1.00 73.53 C
HETATM 3645 C19 SNT A 605 -16.567 -20.952 -6.586 1.00 75.31 C
HETATM 3646 C20 SNT A 605 -15.965 -21.591 -7.820 1.00 76.30 C
HETATM 3647 C21 SNT A 605 -13.556 -18.514 -2.070 1.00 66.34 C
HETATM 3648 C22 SNT A 605 -14.573 -18.662 -3.012 1.00 66.93 C
HETATM 3649 C23 SNT A 605 -11.258 -20.199 -12.194 1.00 69.79 C
HETATM 3650 ZN ZN A 606 0.000 -46.810 -36.300 0.50 64.11 ZN2+
HETATM 3651 ZN ZN A 607 -17.095 -4.608 29.138 1.00 78.82 ZN2+
HETATM 3652 C8 OLC A 608 -2.329 -11.885 -5.818 1.00 86.67 C
HETATM 3653 C24 OLC A 608 0.017 -16.490 -16.904 1.00 95.62 C
HETATM 3654 C7 OLC A 608 -1.813 -12.436 -7.144 1.00 88.44 C
HETATM 3655 C6 OLC A 608 -1.286 -13.863 -7.005 1.00 90.14 C
HETATM 3656 C5 OLC A 608 -1.787 -14.730 -8.150 1.00 92.90 C
HETATM 3657 C4 OLC A 608 -0.658 -15.479 -8.844 1.00 96.77 C
HETATM 3658 C3 OLC A 608 -1.198 -16.406 -9.936 1.00 99.80 C
HETATM 3659 C2 OLC A 608 -0.828 -15.923 -11.341 1.00101.33 C
HETATM 3660 C21 OLC A 608 0.165 -17.467 -14.569 1.00 99.81 C
HETATM 3661 C1 OLC A 608 0.092 -16.864 -12.104 1.00102.78 C
HETATM 3662 C22 OLC A 608 0.933 -17.122 -15.847 1.00 98.81 C
HETATM 3663 O19 OLC A 608 0.584 -17.861 -11.583 1.00104.08 O
HETATM 3664 O25 OLC A 608 -0.432 -17.452 -17.877 1.00 92.13 O
HETATM 3665 O23 OLC A 608 2.062 -16.279 -15.562 1.00 99.59 O
HETATM 3666 O20 OLC A 608 0.423 -16.554 -13.497 1.00101.60 O
HETATM 3667 C24 OLC A 609 -26.280 -31.996 14.683 1.00 95.39 C
HETATM 3668 C7 OLC A 609 -23.058 -33.033 3.310 1.00 87.74 C
HETATM 3669 C6 OLC A 609 -23.570 -33.484 4.675 1.00 89.70 C
HETATM 3670 C5 OLC A 609 -22.616 -33.136 5.814 1.00 91.59 C
HETATM 3671 C4 OLC A 609 -22.999 -33.891 7.088 1.00 94.38 C
HETATM 3672 C3 OLC A 609 -22.676 -33.116 8.370 1.00 96.19 C
HETATM 3673 C2 OLC A 609 -23.291 -33.790 9.600 1.00 97.33 C
HETATM 3674 C21 OLC A 609 -24.649 -32.091 12.773 1.00101.62 C
HETATM 3675 C1 OLC A 609 -23.197 -32.926 10.846 1.00 99.64 C
HETATM 3676 C22 OLC A 609 -26.141 -32.060 13.162 1.00 99.47 C
HETATM 3677 O19 OLC A 609 -22.127 -32.814 11.435 1.00100.07 O
HETATM 3678 O25 OLC A 609 -26.012 -30.671 15.170 1.00 93.28 O
HETATM 3679 O23 OLC A 609 -26.848 -30.952 12.573 1.00100.72 O
HETATM 3680 O20 OLC A 609 -24.387 -32.237 11.363 1.00101.33 O
HETATM 3681 C1 PEG A 610 -21.784 -43.964 -36.552 1.00 93.04 C
HETATM 3682 O1 PEG A 610 -22.948 -44.794 -36.587 1.00 90.34 O
HETATM 3683 C2 PEG A 610 -21.993 -42.624 -37.228 1.00 94.45 C
HETATM 3684 O2 PEG A 610 -20.911 -41.743 -36.924 1.00 94.96 O
HETATM 3685 C3 PEG A 610 -21.268 -40.365 -36.835 1.00 94.22 C
HETATM 3686 C4 PEG A 610 -21.191 -39.872 -35.403 1.00 93.81 C
HETATM 3687 O4 PEG A 610 -19.851 -39.717 -34.932 1.00 91.65 O
HETATM 3688 O1 PG4 A 611 4.126 -27.595 13.284 1.00112.29 O
HETATM 3689 C1 PG4 A 611 4.529 -26.237 13.310 1.00113.98 C
HETATM 3690 C2 PG4 A 611 4.834 -25.776 14.706 1.00116.51 C
HETATM 3691 O2 PG4 A 611 5.094 -24.377 14.727 1.00119.08 O
HETATM 3692 C3 PG4 A 611 4.088 -23.624 15.400 1.00121.51 C
HETATM 3693 C4 PG4 A 611 4.212 -22.170 15.047 1.00123.52 C
HETATM 3694 O3 PG4 A 611 2.966 -21.470 15.116 1.00124.21 O
HETATM 3695 C5 PG4 A 611 2.334 -21.190 13.859 1.00124.74 C
HETATM 3696 C6 PG4 A 611 3.281 -20.705 12.778 1.00124.72 C
HETATM 3697 O4 PG4 A 611 3.099 -21.396 11.539 1.00124.56 O
HETATM 3698 C7 PG4 A 611 3.793 -22.640 11.436 1.00123.33 C
HETATM 3699 C8 PG4 A 611 5.118 -22.466 10.760 1.00122.47 C
HETATM 3700 O5 PG4 A 611 5.913 -23.635 10.866 1.00121.84 O
HETATM 3701 O HOH A 701 0.232 -20.710 -21.541 1.00 67.54 O
HETATM 3702 O HOH A 702 2.503 -19.706 -13.384 1.00 81.55 O
HETATM 3703 O HOH A 703 -17.442 -24.058 -22.320 1.00 47.06 O
HETATM 3704 O HOH A 704 -21.154 -42.479 -14.829 1.00 62.72 O
HETATM 3705 O HOH A 705 -1.874 -20.492 -19.855 1.00 78.18 O
HETATM 3706 O HOH A 706 -16.672 -4.451 26.675 1.00 55.21 O
HETATM 3707 O HOH A 707 -16.256 0.179 31.606 1.00 63.21 O
HETATM 3708 O HOH A 708 -19.366 -42.402 -42.458 1.00 41.45 O
CONECT 501 3650
CONECT 526 3650
CONECT 862 1032
CONECT 1032 862
CONECT 1059 1660
CONECT 1660 1059
CONECT 1799 2388
CONECT 2388 1799
CONECT 2728 3651
CONECT 3180 3208
CONECT 3208 3180
CONECT 3572 3573 3583
CONECT 3573 3572 3574 3580
CONECT 3574 3573 3575 3581
CONECT 3575 3574 3576 3582
CONECT 3576 3575 3577 3583
CONECT 3577 3576 3584
CONECT 3578 3579 3580 3585
CONECT 3579 3578
CONECT 3580 3573 3578
CONECT 3581 3574
CONECT 3582 3575 3586
CONECT 3583 3572 3576
CONECT 3584 3577
CONECT 3585 3578
CONECT 3586 3582 3587 3597
CONECT 3587 3586 3588 3594
CONECT 3588 3587 3589 3595
CONECT 3589 3588 3590 3596
CONECT 3590 3589 3591 3597
CONECT 3591 3590 3598
CONECT 3592 3593 3594 3599
CONECT 3593 3592
CONECT 3594 3587 3592
CONECT 3595 3588
CONECT 3596 3589 3600
CONECT 3597 3586 3590
CONECT 3598 3591
CONECT 3599 3592
CONECT 3600 3596 3601 3609
CONECT 3601 3600 3602 3606
CONECT 3602 3601 3603 3607
CONECT 3603 3602 3604 3608
CONECT 3604 3603 3605 3609
CONECT 3605 3604 3610
CONECT 3606 3601
CONECT 3607 3602 3611
CONECT 3608 3603
CONECT 3609 3600 3604
CONECT 3610 3605
CONECT 3611 3607 3612 3620
CONECT 3612 3611 3613 3617
CONECT 3613 3612 3614 3618
CONECT 3614 3613 3615 3619
CONECT 3615 3614 3616 3620
CONECT 3616 3615 3621
CONECT 3617 3612
CONECT 3618 3613
CONECT 3619 3614
CONECT 3620 3611 3615
CONECT 3621 3616
CONECT 3622 3623 3626 3642
CONECT 3623 3622 3624
CONECT 3624 3623 3625
CONECT 3625 3624 3641
CONECT 3626 3622 3630 3631
CONECT 3627 3628 3633
CONECT 3628 3627 3634 3646
CONECT 3629 3635 3636 3645
CONECT 3630 3626 3643
CONECT 3631 3626 3632 3649
CONECT 3632 3631 3633 3643
CONECT 3633 3627 3632
CONECT 3634 3628 3635
CONECT 3635 3629 3634
CONECT 3636 3629 3637
CONECT 3637 3636 3638 3648
CONECT 3638 3637 3639
CONECT 3639 3638 3640
CONECT 3640 3639 3647
CONECT 3641 3625 3642
CONECT 3642 3622 3641
CONECT 3643 3630 3632 3644
CONECT 3644 3643
CONECT 3645 3629 3646
CONECT 3646 3628 3645
CONECT 3647 3640 3648
CONECT 3648 3637 3647
CONECT 3649 3631
CONECT 3650 501 526
CONECT 3651 2728 3706
CONECT 3652 3654
CONECT 3653 3662 3664
CONECT 3654 3652 3655
CONECT 3655 3654 3656
CONECT 3656 3655 3657
CONECT 3657 3656 3658
CONECT 3658 3657 3659
CONECT 3659 3658 3661
CONECT 3660 3662 3666
CONECT 3661 3659 3663 3666
CONECT 3662 3653 3660 3665
CONECT 3663 3661
CONECT 3664 3653
CONECT 3665 3662
CONECT 3666 3660 3661
CONECT 3667 3676 3678
CONECT 3668 3669
CONECT 3669 3668 3670
CONECT 3670 3669 3671
CONECT 3671 3670 3672
CONECT 3672 3671 3673
CONECT 3673 3672 3675
CONECT 3674 3676 3680
CONECT 3675 3673 3677 3680
CONECT 3676 3667 3674 3679
CONECT 3677 3675
CONECT 3678 3667
CONECT 3679 3676
CONECT 3680 3674 3675
CONECT 3681 3682 3683
CONECT 3682 3681
CONECT 3683 3681 3684
CONECT 3684 3683 3685
CONECT 3685 3684 3686
CONECT 3686 3685 3687
CONECT 3687 3686
CONECT 3688 3689
CONECT 3689 3688 3690
CONECT 3690 3689 3691
CONECT 3691 3690 3692
CONECT 3692 3691 3693
CONECT 3693 3692 3694
CONECT 3694 3693 3695
CONECT 3695 3694 3696
CONECT 3696 3695 3697
CONECT 3697 3696 3698
CONECT 3698 3697 3699
CONECT 3699 3698 3700
CONECT 3700 3699
CONECT 3706 3651
MASTER 398 0 11 18 4 0 0 6 3688 1 141 37
END